diff --git a/.gitignore b/.gitignore index cd320ec..0d8ee4e 100644 --- a/.gitignore +++ b/.gitignore @@ -5,7 +5,6 @@ env ._* .DS_Store __pycache__ -config.txt .ipynb_checkpoints .tox/ *.egg-info @@ -14,3 +13,4 @@ docs/_static/ docs/_templates/ notebooks/ proteofav/analysis/ +tests/*.sqlite diff --git a/__main__.py b/__main__.py index 7e335ab..918ed01 100644 --- a/__main__.py +++ b/__main__.py @@ -1,12 +1,18 @@ -#!/usr/bin/env python # -*- coding: utf-8 + """ -Created on 14:18 17/02/2017 2017 +ProteoFAV: Protein Feature Aggregation and Variants +--------------------------------------------------- + +Open-source framework for simple and fast integration +of protein structure data with sequence annotations +and genetic variation +:copyright: (c) 2015-2017. +:license: TBD, see LICENSE for more details. """ -from __future__ import absolute_import from proteofav.main import main if __name__ == '__main__': - main() \ No newline at end of file + main() diff --git a/analysis/__init__.py b/analysis/__init__.py deleted file mode 100644 index e69de29..0000000 diff --git a/analysis/clustering.py b/analysis/clustering.py deleted file mode 100644 index d70c61d..0000000 --- a/analysis/clustering.py +++ /dev/null @@ -1,946 +0,0 @@ -#!/usr/bin/env python -# -*- coding: utf-8 - -""" -"Starting out with the example from -http://stackoverflow.com/questions/21638130/tutorial-for-scipy-cluster-hierarchy -""" - -import csv -import os -import sys -from operator import itemgetter -from subprocess import call -from time import strftime - -import matplotlib.pyplot as plt -import numpy as np -import pandas as pd -import scipy.cluster.hierarchy as hac -from proteofav.main import merge_tables -from mcl.mcl_clustering import mcl -from mpl_toolkits.mplot3d.art3d import Poly3DCollection -from scipy.spatial import ConvexHull -from scipy.spatial.distance import pdist, squareform, euclidean -from scipy.spatial.qhull import QhullError - -from analysis.random_annotations import add_random_disease_variants -from analysis.utils import delete_file, _get_colors, _fractional_to_cartesian, \ - _autoscale_axes - -__author__ = 'smacgowan' - - -############################################################################## -# Distance Matrix Helpers -############################################################################## -def atom_dist(table, mask, cartesian=False): - """ - Find the intervariant distances for a given PDB chain. - - :param table: - :param cartesian: - :return: The reduced distance matrix produced by `pdist` and the XYZ - coordinates of the mapped variants. - """ - included = table[mask] - excluded = table[~mask] - - # Build array distance matrix - included, included_xyz = select_valid_coordinates(included) - excluded, excluded_xyz = select_valid_coordinates(excluded) - - # Convert to fractional coordinates - if cartesian: - pdb_id = table.PDB_dbAccessionId.unique()[0] - included_xyz = _fractional_to_cartesian(included_xyz, pdb_id) - excluded_xyz = _fractional_to_cartesian(excluded_xyz, pdb_id) - - d = pdist(included_xyz) - - return d, included_xyz, included[['UniProt_dbResNum', 'chain_id']], excluded_xyz - - -def select_valid_coordinates(table): - """ - - :param table: - :return: - """ - real_cartn_mask = np.isfinite(table['Cartn_x']) - table = table[real_cartn_mask] - coord_array = np.array([table.Cartn_x, table.Cartn_y, table.Cartn_z]) - coord_array = np.transpose(coord_array) - return table, coord_array - - -def dist_to_sim(d, method='max_minus_d', threshold=float('inf'), gamma=1./3, **kwargs): - """ - - :param d: A reduced distance matrix, such as produced by `pdist` or the - expanded, squarematrix form. - :param method: The distance-to-similarity conversion to employ before MCL analysis. - Choose from: 'max_minus_d' or 'reciprocal' - :param threshold: The threshold to discard distances (i.e. remove edges) - before conversion to similarities - :param gamma: The gamma coefficient in the exponential decay transform (s = e^(-d * gamma) - :return: - - NB. **kwargs is just so that this can be called with extraneous arguments. - """ - if method == 'max_minus_d': - d[d > threshold] = d.max() - s = d.max() - d - - if method == 'reciprocal': - d = d + 1 - s = 1. / d - - if method == 'exp_decay': - if gamma <= 0: - raise ValueError('Invalid gamma: must be >= 0') - s = np.exp(-d * gamma) - - if method == 'alt_reciprocal': - ##d[d > threshold] = float('inf') #TODO: Any threshold here hides cluster structure. Why? - s = 1. / (d / d.max()) - - return s - - -############################################################################## -# MCL Program Interface -############################################################################## -def write_mcl_input(s): - """ - Re-format a similarity matrix into a list of edge weights and write to a file. - - :param s: A similarity matrix - :return: Writes a CSV file in the current directory - """ - with open('mcl_interactions.csv', 'wb') as file: - writer = csv.writer(file, delimiter=' ') - length = len(s) - for i in xrange(length): - for j in xrange(length): - if s[i, j] != 0.: - writer.writerow([i, j, s[i, j]]) - - -def read_mcl_clusters(file='mcl_results.txt'): - """ - Parse a results file produced by the MCL program. - - :param file: The name of an MCL results file - :return: A list containing the nodes found in each cluster - """ - with open(file, 'rb') as csvfile: - reader = csv.reader(csvfile, delimiter='\t') - clusters = [row for row in reader] - - return clusters - - -def launch_mcl(s, format='partition', inflate=None, silent=True, **kwargs): - """ - Perform MCL analysis using an external MCL implementation. - - :param s: A similarity matrix - :param format: 'partition' returns the clusters in the same format produced - by `fcluster` on a linkage object; - any other value leaves the clusters in the format provided by the MCL program - :return: The clusters found by the MCL program - - NB. **kwargs is just so that this can be called with extraneous arguments. - """ - # Write the MCL input graph to a file - write_mcl_input(s) - - # Build and submit the call - mcl_call = ['mcl', 'mcl_interactions.csv', '--abc', '-o', 'mcl_results.txt'] - if inflate: - mcl_call.append('-I') - mcl_call.append(str(inflate)) - if silent: - call(mcl_call, stdout=open(os.devnull, 'wb'), stderr=open(os.devnull, 'wb')) - else: - call(mcl_call) - - # Read results - clusters = read_mcl_clusters('mcl_results.txt') - - # Cleanup - delete_file('mcl_results.txt') - delete_file('mcl_interactions.csv') - - if format == 'partition': - part = ['unassigned'] * len(s) - cluster_id = 0 - for i in clusters: - for j in i: - part[int(j)] = cluster_id - cluster_id += 1 - return part - else: - return clusters - - -############################################################################## -# Cluster results formatting -############################################################################## -def cluster_dict_to_partitions(cluster_dict): - """ - Convert the cluster output format from the MCL function to a partition list; - like that produced by `fcluster` - - :param cluster_dict: A dictionary where the keys indicate cluster_dict and the - list elements indicate node membership - :return: A list where the positioning indexes correspond to node numbers and the - values correspond to its cluster - """ - new_dict = {e: k for k, v in cluster_dict.items() for e in v} - part = [new_dict[k] + 1 for k in sorted(new_dict.keys())] - part = np.array(part) - return part - - -def merge_clusters_to_table(residue_ids, partition, target_table, multichain=False): - df = pd.DataFrame(residue_ids) - df['Cluster'] = pd.Series(partition) - target_table.UniProt_dbResNum = target_table.UniProt_dbResNum.astype('float') - if multichain: - merge_columns = ['UniProt_dbResNum', 'chain_id'] - else: - merge_columns = 'UniProt_dbResNum' - merged = pd.merge(target_table, df, on=merge_columns) - return merged - - -############################################################################## -# Comparing clustering routines -############################################################################## -def linkage_cluster(d, methods=['single', 'complete'], similarity='max_minus_d', - **kwargs): - """ - - :param d: A reduced distance matrix, such as produced by `pdist` - :param methods: A list of strings indicating the cluster methods to employ. - Choose from: 'single', 'complete', 'average' and 'mcl' - :param invert_method: See `dist_to_sim` - :param threshold: See `dist_to_sim` - :return: - """ - linkages = [] - for method in methods: - if not method.startswith('mcl'): - z = hac.linkage(d, method=method) - linkages.append([z, method]) - else: - sq = squareform(d) - s = dist_to_sim(sq, method=similarity, **kwargs) - if method.startswith('mcl_program'): - clusters = launch_mcl(s, **kwargs) - linkages.append([clusters, method]) - else: - if not 'inflate' in kwargs: - inflate_factor = 2 - else: - inflate_factor = kwargs['inflate'] - M, clusters = mcl(s, max_loop=50, inflate_factor=inflate_factor) - linkages.append([[M, clusters], method]) - - return linkages - - -def compare_clustering(linkages, xyz, title=None, addn_points=None): - """ - Generate a plots comparing the cluster analyses provided. - - :param linkages: A list of cluster analyses as produced by `linkage_cluster` - :param xyz: The coordinates of the original clustered points - :return: - """ - nrows = len(linkages) - fig, axes23 = plt.subplots(nrows, 3) - links, methods = zip(*linkages) - offsets = [0, 3, 6, 9][:nrows] - - for z, method, axes, offset in zip(links, methods, axes23, offsets): - - # Plotting - if not method.startswith('mcl'): - axes[0].plot(range(1, len(z) + 1), z[::-1, 2]) - knee = np.diff(z[::-1, 2], 2) - axes[0].plot(range(2, len(z)), knee) - - num_clust1 = knee.argmax() + 2 - knee[knee.argmax()] = 0 - num_clust2 = knee.argmax() + 2 - - axes[0].text(num_clust1, z[::-1, 2][num_clust1 - 1], 'possible\n<- knee point') - - part1 = hac.fcluster(z, num_clust1, 'maxclust') - part2 = hac.fcluster(z, num_clust2, 'maxclust') - - elif method.startswith('mcl_program'): - part1 = np.array(z) - num_clust1 = max(part1) + 1 - part2 = part1 - num_clust2 = num_clust1 - - else: - # Convert the MCL clusters into a partition vector - part1 = cluster_dict_to_partitions(z[1]) - num_clust1 = max(part1) - part2 = part1 - num_clust2 = num_clust1 - - clr = _get_colors(max([num_clust1, num_clust2])) - - for part, i in zip([part1, part2], [2, 3]): - ax = fig.add_subplot(nrows, 3, i + offset, projection='3d') - for cluster in set(part): - ax.scatter(xyz[part == cluster, 0], xyz[part == cluster, 1], - xyz[part == cluster, 2], c=clr[cluster - 1]) - # Compute and plot the Point Cloud Complex Hull - points = xyz[part == cluster] - if len(points) >= 4: - try: - hull = ConvexHull(points) - for simplex in hull.simplices: - simplex = np.append(simplex, simplex[0]) # Closes facet - ax.plot(points[simplex, 0], points[simplex, 1], - points[simplex, 2], color=clr[cluster - 1]) - tri = Poly3DCollection([zip(points[simplex, 0], points[simplex, 1], - points[simplex, 2])], - alpha=0.2) - tri.set_color(clr[cluster - 1]) - tri.set_edgecolor('k') - ax.add_collection3d(tri) - except QhullError: - pass - else: - points = np.vstack([points, points[0]]) # Gives triangle for 3-points - ax.plot(points[:, 0], points[:, 1], points[:, 2], color=clr[cluster - 1]) - if addn_points is not None: - ax.scatter(addn_points[:, 0], addn_points[:, 1], addn_points[:, 2], c='grey', s=5, - alpha=0.3) - x = np.append(xyz[:, 0], addn_points[:, 0]) - y = np.append(xyz[:, 1], addn_points[:, 1]) - z = np.append(xyz[:, 2], addn_points[:, 2]) - all_points = np.array([x, y, z]).T - x, y, z = _autoscale_axes(all_points) - ax.auto_scale_xyz(x, y, z) - else: - x, y, z = _autoscale_axes(xyz) - ax.auto_scale_xyz(x, y, z) - - m = '\n(method: {})'.format(method) - plt.setp(axes[0], title='Screeplot{}'.format(m), xlabel='partition', - ylabel='{}\ncluster distance'.format(m)) - plt.setp(axes[1], title='{} Clusters'.format(num_clust1)) - plt.setp(axes[2], title='{} Clusters'.format(num_clust2)) - axes[1].axis('off') - axes[2].axis('off') - - plt.tight_layout() - plt.suptitle(title) - file = 'cluster_figs/cluster_fig_' + strftime("%Y%m%d_%H%M%S") + '.png' - plt.savefig(file, format='png') - # plt.show() - - -############################################################################## -# Cluster statistic functions -############################################################################## -def n_clusters(partition): - """ - Determine the number of clusters from a partition list. - - :param part: A partition list - :type part: List - :return: The number of clusters in the partition list - """ - part = list(partition) # Copy to avoid sorting outside scope - part.sort() - - if part[0] == 0: - return part[-1] + 1 - else: - return part[-1] - - -def partition_to_sizes(part): - """ - Determine the number of elements in each cluster from a partition list. - - :param part: A partition list - :type part: List - :return: - """ - offset = 1 # Need this if 1-indexed - if 0 in part: - offset = 0 - - sizes = [part.count(i + offset) for i in xrange(n_clusters(part))] - - return sizes - - -def top_k_clusters(sizes, k=2): - """ - - :param part: - :return: - """ - sizes.sort(reverse=True) - n_members = sum(sizes[:k]) - - return n_members - - -def n_isolated(sizes): - """ - - :param sizes: - :return: - """ - return sizes.count(1) - - -def n_50_clusters(sizes): - return n_x_clusters(sizes, 50) - - -def n_x_clusters(sizes, percent): - """ - - :param sizes: - :return: Minimum number of clusters that contains half the observations. - """ - n_required = sum(sizes) / (100. / percent) ## TODO: Not perfect for odd numbers - sizes = list(sizes) - sizes.sort() - n_obs = 0 - n_clusters = 0 - while n_obs < n_required: - n_obs += sizes.pop() - n_clusters += 1 - return n_clusters - - -def cluster_size_stats(part, statistics=(np.mean, np.median, np.std, min, max, len, - top_k_clusters, n_isolated, n_50_clusters), - names=False): - """ - - :param part: - :param statistics: - :return: - """ - sizes = partition_to_sizes(part) - results = [stat(sizes) for stat in statistics] - if not names: - return results - else: - stat_functions = [stat.__name__ for stat in statistics] - results = {k: v for k, v in zip(stat_functions, results)} - return results - - -def centroids(partition, observations): - """ - Return cluster centroids. - - :param part: Partition vector - :type part: List - :param obs: Observation array - :type obs: NumPy array - :return: A dictionary containing the cluster centroids. - """ - cluster_ids = list(set(partition)) - cluster_ids.sort() - cluster_centroids = {} - for cid in cluster_ids: - members = member_indexes(partition, cid) - member_observations = observations[members, :] - cluster_centroids[cid] = np.mean(member_observations, axis=0) - return cluster_centroids - - -def member_indexes(partition, cluster_id): - return [i for i, x in enumerate(partition) if x == cluster_id] - - -def davies_bouldin(partition, observations): - """ - Return the Davies-Bouldin index for the given clustering. - - :param part: Partition vector - :type part: List - :param obs: Observation array - :type obs: NumPy array - :return: The Davies-Bouldin index - """ - - n = n_clusters(partition) - cluster_ids = list(set(partition)) - cluster_ids.sort() - cluster_centroids = centroids(partition, observations) - terms = [] - for i in cluster_ids: - ci = cluster_centroids[i] - i_indexes = member_indexes(partition, i) - sigma_i = np.mean([euclidean(u, ci) for u in observations[i_indexes, :]]) - Sij = [] - for j in cluster_ids: - if i != j: - cj = cluster_centroids[j] - d = euclidean(ci, cj) - j_indexes = member_indexes(partition, j) - sigma_j = np.mean([euclidean(u, cj) for u in observations[j_indexes, :]]) - Sij.append((sigma_i + sigma_j) / d) - if len(Sij) > 0: - terms.append(max(Sij)) - return sum(terms) / n - - -def dunn(partition, observations): - """ - Return the Dunn index for a clustering. - - :param part: Partition vector - :type part: List - :param obs: Observation array - :type obs: NumPy array - :return: The Dunn index - """ - cluster_ids = list(set(partition)) - - # NA if only one cluster - if len(cluster_ids) == 1: - return np.nan - - cluster_ids.sort() - min_inter = min(pdist(centroids(partition, observations).values())) - intras = [] - for cid in cluster_ids: - member_ids = member_indexes(partition, cid) - d = pdist(observations[member_ids, :]) - if len(d) != 0: ## Handles singleton clusters - intras.append(max(d)) - - if len(intras) == 0: - return np.nan - else: - max_intra = max(intras) - - return(min_inter / max_intra) - - -############################################################################## -# Cluster geometry -############################################################################## -def cluster_hull_volumes(partition, points): - """ - - :param partition: - :param points: - :return: - - See http://stackoverflow.com/questions/24733185/volume-of-convex-hull-with-qhull-from-scipy - for some discussion (and some of the code used here). - """ - def tetrahedron_volume(a, b, c, d): - return np.abs(np.einsum('ij,ij->i', a-d, np.cross(b-d, c-d))) / 6 - - def convex_hull_volume_bis(pts): - ch = ConvexHull(pts) - - simplices = np.column_stack((np.repeat(ch.vertices[0], ch.nsimplex), - ch.simplices)) - tets = ch.points[simplices] - return np.sum(tetrahedron_volume(tets[:, 0], tets[:, 1], - tets[:, 2], tets[:, 3])) - - cluster_ids = list(set(partition)) - cluster_ids.sort() - volumes = {} - for cid in cluster_ids: - member_ids = member_indexes(partition, cid) - member_pts = points[member_ids, :] - if len(member_pts) >= 4: ## Ignore 'plane' clusters, TODO: handle duplicates - volume = convex_hull_volume_bis(member_pts) - else: - volume = 0 - volumes[cid] = 0 if volume is None else volume - return volumes - - -############################################################################## -# Cluster bootstrapping -############################################################################## -def bootstrap(table, methods, n_residues, n_phenotypes, - samples=10, **kwargs): - """ - - :param table: - :param methods: - :param statistics: - :return: - """ - partitions = [] - for i in xrange(samples): - # Build random data - test_table = add_random_disease_variants(table, n_residues, n_phenotypes) - - # Compute the clustering - d, points, resids, unmapped_points = atom_dist(test_table) - links = linkage_cluster(d, methods, **kwargs) - partitions.append(links[0][0]) - - return partitions - - -def bootstrap_stats(partitions, **kwargs): - """ - - :param partitions: - :param statistics: - :return: - """ - stats = [cluster_size_stats(part, **kwargs) for part in partitions] - - return stats - - -def boot_pvalue(sample_stats, test): - """ - - :param sample_stats: - :param test: - :return: - """ - n_samples = len(sample_stats) - p_value = sum(map(test, sample_stats)) / float(n_samples) - p_value = round(p_value * n_samples) / n_samples - if p_value == 0.: - p_value = '< ' + str(1. / n_samples) - - return p_value - - -def tail_thresholds(alpha, samples, stats): - """ - - :param alpha: - :param samples: - :param stats: - :return: - """ - thresholds = [] - for i in zip(*stats): - i = np.sort(i) - thresholds.append((i[int((alpha / 2.0) * samples)], i[int((1 - alpha / 2.0) * samples)])) - - return thresholds - - -def plot_sample_distributions(results, names): - for i in xrange(len(names)): - plt.subplot(3, 4, i + 1) - plt.title(names[i]) - data = zip(*results['sample_stats'])[i] - if np.nan in data: - data = [x for x in data if not np.isnan(x)] - if all(isinstance(x, int) for x in data): - plt.hist(data, color='c', bins=range(min(data), max(data) + 1, 1)) - else: - plt.hist(data, color='c') - plt.axvline(results['obs_stats'][names[i]], color='b', linestyle='dashed', linewidth=2) - plt.xticks(rotation=45) - - -############################################################################## -# Convenience wrappers -############################################################################## -def cluster_table(table, mask, method, sites_only=True, similarity='max_minus_d', - **kwargs): - """ - - :param table: - :param mask: - :param test_significance: - :param kwargs: - :return: - """ - - # Create string describing clustering for metadata - cluster_parameters_whitelist = ['method', 'threshold', 'similarity'] - cluster_parameters = [] - for k, v in locals().iteritems(): - if k in cluster_parameters_whitelist: - cluster_parameters.append(str(k)) - cluster_parameters.append(str(v)) - cluster_meta_tag = '_'.join(cluster_parameters) - - # # Apply mask - # table = table[mask] - # mask = np.array([True] * len(table)) #TODO: Remove the need for this hack needed for `atom_dist` - - # Dedupe table by UniProt and chain if only clustering sites - if sites_only: - table = table.drop_duplicates(subset=['UniProt_dbResNum', 'chain_id']) - # mask = np.array([True] * len(table)) #TODO: See above - - # Perform clustering - d, points, resids, unmapped_points = atom_dist(table, table.resn.notnull()) - links = linkage_cluster(d, methods=method, similarity=similarity, **kwargs) - part = links[0][0] - - # Format the results - labelled_points = add_clusters_to_points(part, points) - annotated_table = add_clusters_to_table(labelled_points, table) - annotated_table.loc[annotated_table.cluster_id.notnull(), 'cluster_info'] = cluster_meta_tag ## New column until pandas reliably stores metadata - - return annotated_table - - -def test_cluster_significance(test_table, method, similarity, table, show_progress, n_samples, return_samples, - **kwargs): - n_variants = sum(table.resn.notnull() & np.isfinite(table['Cartn_x'])) - n_phenotypes = len(table.disease.dropna().unique()) - clean_table = table.drop_duplicates(subset=['UniProt_dbResNum', 'chain_id']).drop(['resn', 'mut', 'disease'], - axis=1) - clean_table = clean_table[np.isfinite(clean_table['Cartn_x'])] - # Bootstrap samples - annotated_tables = bootstrap_residue_clusters(clean_table, method, - n_phenotypes, - n_samples, - n_variants, - show_progress, - similarity, - **kwargs) - # Drop unneccesary data - column_whitelist = ['Cartn_x', 'Cartn_y', 'Cartn_z', 'cluster_id'] - annotated_tables[:] = [i.loc[i.cluster_id.notnull(), column_whitelist] for i in annotated_tables] - - part, points = clustered_table_to_partition_and_points(test_table) - bs_stats, p_values, sample_cluster_sizes, stats = collect_cluster_sample_statistics(part, points, - annotated_tables) - - results = {'p': p_values, 'obs_stats': stats, 'sample_stats': bs_stats} - if return_samples: - results.update({'sample_size_dist': sample_cluster_sizes, 'random_samples': annotated_tables}) - - return results - - -def collect_cluster_sample_statistics(test_part, test_points, sample_tables): - - # Parse the random sample cluster tables - parsed_samples = [clustered_table_to_partition_and_points(i) for i in sample_tables] - - # Gather the random sample cluster statistics - sample_davies_bouldins = [davies_bouldin(part, points) for part, points in parsed_samples] - sample_dunns = [dunn(part, points) for part, points in parsed_samples] - sample_largest_cluster_volume = [max(cluster_hull_volumes(part, points)) for part, points in parsed_samples] - random_sample_cluster_statistics = bootstrap_stats(zip(*parsed_samples)[0], names=True) # Partition metrics - - # Combine the random sample cluster statistics - for i in xrange(len(sample_tables)): - random_sample_cluster_statistics[i].update({'Davies-Bouldin': sample_davies_bouldins[i]}) - random_sample_cluster_statistics[i].update({'Dunn_index': sample_dunns[i]}) - random_sample_cluster_statistics[i].update({'largest_cluster_volume': sample_largest_cluster_volume[i]}) - - # Collect the observed cluster statistics - observed_stats = {} - observed_stats.update(cluster_size_stats(test_part, names=True)) - observed_stats.update(cluster_spatial_statistics(test_part, test_points)) - - # Calculate p for randomly seeing a value smaller, equal to or larger than observed statistic - p_values = {} - for stat_key in observed_stats: - sampled = map(itemgetter(stat_key), random_sample_cluster_statistics) - obs = observed_stats[stat_key] - left = boot_pvalue(sampled, lambda x: x < obs) - mid = boot_pvalue(sampled, lambda x: x == obs) - right = boot_pvalue(sampled, lambda x: x > obs) - p_values.update({stat_key: (left, mid, right)}) - - ## For complete cluster size distribution - sample_cluster_sizes = [] - for i in zip(*parsed_samples)[0]: - sample_cluster_sizes.append(partition_to_sizes(i)) - sample_cluster_sizes = [e for sublist in sample_cluster_sizes for e in sublist] # Flatten - - return random_sample_cluster_statistics, p_values, sample_cluster_sizes, observed_stats - - -def cluster_spatial_statistics(test_part, test_points): - obs_stats = [] - obs_stats.append(davies_bouldin(test_part, test_points)) - obs_stats.append(dunn(test_part, test_points)) - obs_stats.append(max(cluster_hull_volumes(test_part, test_points).values())) - names = [] - names.append('Davies-Bouldin') - names.append('Dunn_index') - names.append('largest_cluster_volume') - results = {k: v for k, v in zip(names, obs_stats)} - return results - - -############################################################################## -# Bootstrapping -############################################################################## -def bootstrap_residue_clusters(clean_table, method, n_phenotypes, n_samples, n_variants, show_progress, similarity, - **kwargs): - """ - - :param clean_table: A structure table - :param method: Method to use for clustering. - :param n_phenotypes: Number of phenotypes for `add_random_disease_variants`. - :param n_samples: Number of random samples to produce and assess. - :param n_variants: Number of variants for `add_random_disease_variants`. - :param show_progress: Show a progress bar. - :param kwargs: Arguments passed to `cluster_table`. - :return: - """ - annotated_tables = [] - for i in xrange(n_samples): - sample_table = add_random_disease_variants(clean_table, n_variants, n_phenotypes) - sample_mask = sample_table.resn.notnull() - annotated_table = cluster_table(sample_table, sample_mask, method, n_samples=0, - similarity=similarity, **kwargs) - annotated_tables.append(annotated_table) - if show_progress: - pc_complete = (i + 1) / float(n_samples) * 100 - if pc_complete % 10 == 0: - sys.stdout.write("\r%d%%" % (pc_complete)) - sys.stdout.flush() - - return annotated_tables - - -############################################################################## -# Data handling -############################################################################## -def add_clusters_to_points(cluster_partition, clustered_points): - """ - - :param cluster_partition: - :param clustered_points: - :return: - """ - points = pd.DataFrame(clustered_points) - points.loc[:, 'cluster_id'] = pd.Series(cluster_partition, index=points.index) - points = points.rename(columns={0: 'Cartn_x', 1: 'Cartn_y', 2: 'Cartn_z'}) - return points - - -def add_clusters_to_table(labelled_points, clustered_table): - """ - - :param cluster_partition: - :param clustered_table: - :return: - """ - index_name = clustered_table.index.name - if index_name is not None: - merged_table = clustered_table.reset_index().merge(labelled_points, how='left').set_index(index_name) - else: - merged_table = clustered_table.merge(labelled_points, how='left') - return merged_table - - -def clustered_table_to_partition_and_points(table): - """ - - :param table: A structure table with clustered sites. - :return: A 2-tuple with the partition vector (list) and point positions (np.array). - """ - partition = list(pd.Series(table.cluster_id.dropna(), dtype=int)) - points = np.array(table.loc[table.cluster_id.notnull(), ['Cartn_x', 'Cartn_y', 'Cartn_z']]) - return partition, points - - -if __name__ == '__main__': - # Porphobilinogen deaminase example - table = merge_tables(pdb_id='3ecr', chain='A', uniprot_variants=True) - mask = table.resn.notnull() - d, points, resids, unmapped_points = atom_dist(table, mask) - links = linkage_cluster(d, methods=['single', 'complete']) - compare_clustering(links, points, '3ecr(a) P08397') - links = linkage_cluster(d, methods=['average', 'mcl_program'], threshold=10) - compare_clustering(links, points, '3ecr(a) P08397') - links = linkage_cluster(d, methods=['mcl_program', 'mcl'], threshold=10) - compare_clustering(links, points, '3ecr(a) P08397', addn_points=unmapped_points) - - # Comparing MCL inflation factors and distance to similarity conversion - sq = squareform(d) - links = [] - for inf_fact in [2., 6.]: - s = dist_to_sim(sq, method='max_minus_d', threshold=10) - links.append([mcl(s, max_loop=50, inflate_factor=inf_fact), - 'mcl_IF=' + str(inf_fact) + '\nmax_minus_d(t=10)']) - compare_clustering(links, points, '3ecr(a) P08397') - - # No min. distance for connected threshold (saturated network) - links = [] - for inf_fact in [2., 6.]: - s = dist_to_sim(sq, method='max_minus_d') - links.append([mcl(s, max_loop=50, inflate_factor=inf_fact), - 'mcl_IF=' + str(inf_fact) + '\nmax_minus_d(t=inf)']) - compare_clustering(links, points, '3ecr(a) P08397') - - # Using reciprocal distance for similarity - links = [] - for inf_fact in [2., 6.]: - s = dist_to_sim(sq, method='reciprocal') - links.append([mcl(s, max_loop=50, inflate_factor=inf_fact), - 'mcl_IF=' + str(inf_fact) + '\nreciprocal']) - compare_clustering(links, points, '3ecr(a) P08397') - - # KRT14 from K5/14 dimer example (multichain) - table = merge_tables(pdb_id='3tnu', chain='all', uniprot_variants=True) - mask = table.resn.notnull() - d, points, resids, unmapped_points = atom_dist(table, mask) - links = linkage_cluster(d, methods=['average', 'mcl_program'], threshold=15) - compare_clustering(links, points, '3tnu(a/b) P02533/P13647', addn_points=unmapped_points) - - # Now look at the same structure with random variants added - n_variants = sum(table.resn.notnull()) - table = merge_tables(pdb_id='3tnu', chain='all') - table = add_random_disease_variants(table, n_variants, 1) - mask = table.resn.notnull() - d, points, resids, unmapped_points = atom_dist(table, mask) - links = linkage_cluster(d, methods=['average', 'mcl_program'], threshold=15) - compare_clustering(links, points, '3tnu(a/b) P02533/P13647', addn_points=unmapped_points) - - # Serine/threonine-protein kinase receptor R3, Telangiectasia example - table = merge_tables(pdb_id='3my0', chain='A', uniprot_variants=True) - mask = table.resn.notnull() - d, points, resids, unmapped_points = atom_dist(table, mask) - links = linkage_cluster(d, methods=['average', 'mcl_program'], threshold=10) - compare_clustering(links, points, '3my0(a) P37023', addn_points=unmapped_points) - - # Alpha-galactosidase A, Fabry disease example - table = merge_tables(pdb_id='3s5z', chain='A', uniprot_variants=True) - mask = table.resn.notnull() - d, points, resids, unmapped_points = atom_dist(table, mask) - links = linkage_cluster(d, methods=['average', 'mcl_program'], threshold=10) - compare_clustering(links, points, '3s5z(a) P06280', addn_points=unmapped_points) - - # Cholinesterase, BChE deficiency example - table = merge_tables(pdb_id='4tpk', chain='A', uniprot_variants=True) - mask = table.resn.notnull() - d, points, resids, unmapped_points = atom_dist(table, mask) - links = linkage_cluster(d, methods=['average', 'mcl_program'], threshold=10) - compare_clustering(links, points, '4tpk(a) P06276', addn_points=unmapped_points) - - # UDP-glucose 4-epimerase, EDG example - table = merge_tables(pdb_id='1ek6', chain='A', uniprot_variants=True) - mask = table.resn.notnull() - d, points, resids, unmapped_points = atom_dist(table, mask) - links = linkage_cluster(d, methods=['average', 'mcl_program'], threshold=10) - compare_clustering(links, points, '1ek6(a) Q14376', addn_points=unmapped_points) diff --git a/analysis/pipeline.py b/analysis/pipeline.py deleted file mode 100755 index 73a0530..0000000 --- a/analysis/pipeline.py +++ /dev/null @@ -1,216 +0,0 @@ -import logging - -logging.basicConfig(filename='variant_clustering.log', level=logging.DEBUG) -logger = logging.getLogger(__name__) - -import sys - -sys.path.extend(['/Users/smacgowan/PycharmProjects/ProteoFAV']) - -from analysis import query_uniprot -import argparse -import cPickle as pickle -import logging -from proteofav import main -import os -import time -from analysis import clustering -from analysis.utils import is_valid_file, create_directory - -if __name__ == '__main__': - - # Parameters - parser = argparse.ArgumentParser(description='Execute disease variant structure clustering pipeline') - parser.add_argument('RESULTS_DIR', type=str, help='Directory to save results') - parser.add_argument('--proteins', type=lambda x: is_valid_file(parser, x), help='File containing UniProt IDs') - parser.add_argument('--IF', dest='inflate', type=float, help='MCL inflation factor. Will use default if ommitted') - parser.add_argument('--threshold', dest='threshold', type=float, default=7.5, - help='Distance threshold to break edges of positional similarity graph') - parser.add_argument('--similarity', dest='similarity', type=str, default='max_minus_d', - help='Method to transform interatomic distances into a graph') - parser.add_argument('--retry_failed', dest='retry_failed', action='store_true') - - # Setup results dir - args = parser.parse_args() - if not os.path.isdir(args.RESULTS_DIR): - os.makedirs(args.RESULTS_DIR) - - # Logging setup and log pipeline configuration - - # define a Handler which writes INFO messages or higher to the sys.stderr - console = logging.StreamHandler() - console.setLevel(logging.INFO) - logger.addHandler(console) - - logging.getLogger("requests").setLevel(logging.WARNING) - logger.info('Starting disease variant clustering pipeline.') - for arg, value in sorted(vars(args).items()): - logger.info("Pipeline argument %s: %r", arg, value) - - # Setup directory structure ---------------------------------------------------------------------------------------- - # Cluster analyses are stored according to the parameter sets used - cluster_parameters_whitelist = ['inflate', 'threshold', 'similarity'] - cluster_parameters = [] - for k, v in vars(args).iteritems(): - if k in cluster_parameters_whitelist: - cluster_parameters.append(str(k)) - cluster_parameters.append(str(v)) - cluster_dir = os.path.join('pickled', 'clusters_' + '_'.join(cluster_parameters)) - - # Create required folders - if not os.path.isdir('pickled'): - create_directory('pickled') - - structure_table_dir = os.path.join('pickled', 'structure_tables') - for datadir in [structure_table_dir, cluster_dir]: - if not os.path.isdir(datadir): - create_directory(datadir) - - # Get UniProt IDs -------------------------------------------------------------------------------------------------- - - # Get suitable list of proteins - if not args.proteins: - protein_set = query_uniprot()[:10] # Results from default query terms - else: - protein_set = [x.strip() for x in args.proteins] - - logger.info('Processing {} UniProt IDs'.format(len(protein_set))) - - # Get structure and variant data ----------------------------------------------------------------------------------- - - # Get structure and uniprot variant table. Will be reloaded if previously pickled, - # skipped if a previous attempt failed and 'retry_failed' is not set and retrieved - # in any other case - structure_tables = [] - for prot in protein_set: - table_failed_placeholder = os.path.join(structure_table_dir, 'structure_table_' + prot + '.failed') - table_pickle_name = 'structure_table_' + prot + '.pkl' - table_file_name = os.path.join(structure_table_dir, table_pickle_name) - if not os.path.isfile(table_file_name): - if not os.path.isfile(table_failed_placeholder) or args.retry_failed: - # TODO: Figure a way to complete analysis for as many proteins as possible - logger.info('Processing UniProt ID {} out of {}...'.format(protein_set.index(prot) + 1, - len(protein_set))) - try: - structure_table = main.merge_tables(uniprot_id=prot, chain='all', - add_uniprot_variants=True) - structure_tables.append((prot, structure_table)) - with open(table_file_name, 'wb') as output: - pickle.dump(structure_table, output, -1) - if os.path.isfile(table_failed_placeholder): - os.remove(table_failed_placeholder) - except: - logger.warning('Cannot get structure table for {}... skipping.'.format(prot)) - with open(table_failed_placeholder, 'w') as output: - output.write('Last attempted at {}\n'.format(time.strftime('%a %d %b - %H:%M:%S'))) - else: - logger.info('Structure table for {} recorded as unavailable... skipping.'.format(prot)) - else: - structure_table = pickle.load(open(table_file_name, 'rb')) - structure_tables.append((prot, structure_table)) - logger.info('Reloaded structure table for {}.'.format(prot)) - - # Cluster analysis ------------------------------------------------------------------------------------------------- - results = [] - for prot, table in structure_tables: - - # Basic processing - deduped = table.drop_duplicates(subset=['UniProt_dbResNum', 'chain_id']) - mask = deduped.resn.notnull() - n_variants = sum(mask) - - # File names - cluster_failed_placeholder = os.path.join(cluster_dir, 'cluster_results_' + prot + '.failed') - cluster_pickle_name = 'cluster_results_' + prot + '.pkl' - cluster_file_name = os.path.join(cluster_dir, cluster_pickle_name) - - # Check if the results are already available or marked as failed - if not os.path.isfile(cluster_file_name): - if not os.path.isfile(cluster_failed_placeholder) or args.retry_failed: - - # Try to complete the cluster analysis and store the results. Otherwise, record the failure and move on. - try: - logger.info('Running cluster analysis for {}.'.format(prot)) - annotated_table = clustering.cluster_table(deduped, mask=mask, method=['mcl_program'], - **vars(args)) - cluster_table = clustering.test_cluster_significance(annotated_table, method=['mcl_program'], - table=deduped, show_progress=False, - n_samples=50, return_samples=True, - **vars(args)) - with open(cluster_file_name, 'wb') as output: - pickle.dump(cluster_table, output, -1) - results.append((prot, n_variants, cluster_table)) - except: - logger.warning('Cannot complete cluster analysis for {}... skipping.'.format(prot)) - with open(cluster_failed_placeholder, 'w') as output: - output.write('Last attempted at {}\n'.format(time.strftime('%a %d %b - %H:%M:%S'))) - - else: - # Log and skip - logger.info('Clustering for {} recorded as failed... skipping.'.format(prot)) - - else: - # Reload the clustering - cluster_table = pickle.load(open(cluster_file_name, 'rb')) - results.append((prot, n_variants, cluster_table)) - logger.info('Reloaded clustering results for {}.'.format(prot)) - - # Create results plots - names = ['mean', 'median', 'std', 'min', 'max', 'len', 'top_k_clusters', 'n_isolated', 'n_50_clusters'] - names.append('Davies-Bouldin') - names.append('Dunn_index') - names.append('largest_cluster_volume') - # for prot, n_variants, stats in results: - # plot_failed_placeholder = os.path.join(args.RESULTS_DIR, 'plot_file_' + prot + '.failed') - # plot_file_name = 'cluster_metrics_' + prot + '.png' - # plot_file = os.path.join(args.RESULTS_DIR, plot_file_name) - # if not os.path.isfile(plot_file): - # if not os.path.isfile(plot_failed_placeholder) or args.retry_failed: - # try: - # logger.info('Plotting results for {}.'.format(prot)) - # analysis.clustering.plot_sample_distributions(stats, names) - # plt.suptitle(prot) - # plt.tight_layout() - # plt.savefig(plot_file, format='png') - # plt.close() - # except: - # logger.warning('Cannot provide plot for {}... skipping.'.format(prot)) - # with open(plot_failed_placeholder, 'w') as output: - # output.write('Last attempted at {}\n'.format(time.strftime('%a %d %b - %H:%M:%S'))) - # else: - # logger.info('Results already plotted for {}... skipping.'.format(prot)) - - # Write some summary stats - results_file = os.path.join(args.RESULTS_DIR, 'results_summary.txt') - with open(results_file, 'w+') as summary: - # Results Header - names_pvalues = [] - names_psmall = [] - names_plarge = [] - for var in names: - names_pvalues.append('p(s/e/l)_' + var) - names_psmall.append('p_small_' + var) - names_plarge.append('p_large_' + var) - summary.write('# p-values indicate the proportion of random samples are smaller/equal/larger than observed.\n') - summary.write('UniProtID\tN_variants\t' + '\t'.join(names) + '\t' + '\t'.join(names_psmall) + '\t' + - '\t'.join(names_plarge) + '\t' + '\t'.join(names_pvalues) + '\n') - - for i in results: - uniprot_id = i[0] - n_variants = str(i[1]) - - p_values = [] - p_small = [] - p_large = [] - observed_stats = [] - for var in names: - observed_stats.append(str(i[2]['obs_stats'][var])) - p_tuple = i[2]['p'][var] - p_values.append(str(p_tuple)) - - p_num = [0 if isinstance(x, str) else x for x in p_tuple] - p_small.append(str(sum(p_num[:2]))) - p_large.append(str(sum(p_num[1:]))) - - - summary.write('\t'.join([uniprot_id, n_variants] + observed_stats + p_small + p_large + p_values) + '\n') diff --git a/analysis/pymol_scripts/__init__.py b/analysis/pymol_scripts/__init__.py deleted file mode 100644 index e69de29..0000000 diff --git a/analysis/pymol_scripts/drawBoundingBox.py b/analysis/pymol_scripts/drawBoundingBox.py deleted file mode 100644 index dad09d3..0000000 --- a/analysis/pymol_scripts/drawBoundingBox.py +++ /dev/null @@ -1,118 +0,0 @@ -# -*- coding: utf-8 -*- -from pymol.cgo import * -from pymol import cmd -from random import randint - -############################################################################# -# -# drawBoundingBox.py -- Draws a box surrounding a selection -# -# -# AUTHOR: Jason Vertrees -# DATE : 2/20/2009 -# NOTES : See comments below. -# -############################################################################# -def drawBoundingBox(selection="(all)", padding=0.0, linewidth=2.0, r=1.0, g=1.0, b=1.0): - """ - DESCRIPTION - Given selection, draw the bounding box around it. - - USAGE: - drawBoundingBox [selection, [padding, [linewidth, [r, [g, b]]]]] - - PARAMETERS: - selection, the selection to enboxen. :-) - defaults to (all) - - padding, defaults to 0 - - linewidth, width of box lines - defaults to 2.0 - - r, red color component, valid range is [0.0, 1.0] - defaults to 1.0 - - g, green color component, valid range is [0.0, 1.0] - defaults to 1.0 - - b, blue color component, valid range is [0.0, 1.0] - defaults to 1.0 - - RETURNS - string, the name of the CGO box - - NOTES - * This function creates a randomly named CGO box that minimally spans the protein. The - user can specify the width of the lines, the padding and also the color. - """ - - ([minX, minY, minZ],[maxX, maxY, maxZ]) = cmd.get_extent(selection) - - print "Box dimensions (%.2f, %.2f, %.2f)" % (maxX-minX, maxY-minY, maxZ-minZ) - - minX = minX - float(padding) - minY = minY - float(padding) - minZ = minZ - float(padding) - maxX = maxX + float(padding) - maxY = maxY + float(padding) - maxZ = maxZ + float(padding) - - if padding != 0: - print "Box dimensions + padding (%.2f, %.2f, %.2f)" % (maxX-minX, maxY-minY, maxZ-minZ) - - boundingBox = [ - LINEWIDTH, float(linewidth), - - BEGIN, LINES, - COLOR, float(r), float(g), float(b), - - VERTEX, minX, minY, minZ, #1 - VERTEX, minX, minY, maxZ, #2 - - VERTEX, minX, maxY, minZ, #3 - VERTEX, minX, maxY, maxZ, #4 - - VERTEX, maxX, minY, minZ, #5 - VERTEX, maxX, minY, maxZ, #6 - - VERTEX, maxX, maxY, minZ, #7 - VERTEX, maxX, maxY, maxZ, #8 - - - VERTEX, minX, minY, minZ, #1 - VERTEX, maxX, minY, minZ, #5 - - VERTEX, minX, maxY, minZ, #3 - VERTEX, maxX, maxY, minZ, #7 - - VERTEX, minX, maxY, maxZ, #4 - VERTEX, maxX, maxY, maxZ, #8 - - VERTEX, minX, minY, maxZ, #2 - VERTEX, maxX, minY, maxZ, #6 - - - VERTEX, minX, minY, minZ, #1 - VERTEX, minX, maxY, minZ, #3 - - VERTEX, maxX, minY, minZ, #5 - VERTEX, maxX, maxY, minZ, #7 - - VERTEX, minX, minY, maxZ, #2 - VERTEX, minX, maxY, maxZ, #4 - - VERTEX, maxX, minY, maxZ, #6 - VERTEX, maxX, maxY, maxZ, #8 - - END - ] - - boxName = "box_" + selection - # while boxName in cmd.get_names(): - # boxName = "box_" + str(randint(0,10000)) - - cmd.load_cgo(boundingBox, boxName) - return boxName - -cmd.extend("drawBoundingBox", drawBoundingBox) \ No newline at end of file diff --git a/analysis/query_uniprot.py b/analysis/query_uniprot.py deleted file mode 100644 index 9635eb7..0000000 --- a/analysis/query_uniprot.py +++ /dev/null @@ -1,33 +0,0 @@ -#!/usr/bin/env python -# -*- coding: utf-8 -*- - -import requests -import logging - - -logger = logging.getLogger(__name__) - - -# TODO: move this to variants.py? -def query_uniprot(search_terms=('keyword:Disease', 'reviewed:yes', 'organism:human', 'database:(type:pdb)')): - """ - Query the UniProt API for proteins that have particualar characteristics. - - :param search_terms: A tuple of UniProt Query search terms. - :return: A list of UniProt IDs - """ - url = 'http://www.uniprot.org/uniprot' - params = {'query': ' AND '.join(search_terms), - 'format': 'tab', 'columns': 'id'} - logger.info('Querying UniProt DB...') - r = requests.get(url, params=params) - uniprots = r.content.split('\n')[1:] - logger.info('Retreived {} UniProt IDs matching query.'.format(len(uniprots))) - - return uniprots - - -if __name__ == '__main__': - uniprot_ids = query_uniprot() - for i in uniprot_ids: - print i \ No newline at end of file diff --git a/analysis/random_annotations.py b/analysis/random_annotations.py deleted file mode 100644 index 20c2217..0000000 --- a/analysis/random_annotations.py +++ /dev/null @@ -1,232 +0,0 @@ -#!/usr/bin/env python -# -*- coding: utf-8 - -""" -Created on 25/11/2015 -Functions to help with random selection of PDB atoms/residues and significance -testing via bootstrapping. -""" - -import logging -from numpy.random import choice, random_integers, permutation -from numpy import array, isfinite -from pandas import Series, DataFrame, crosstab -from string import letters -from random import shuffle - -__author__ = 'smacgowan' - - -def random_uniprot_patho_table(merge_table, n_residues, n_phenotypes=1, - proportions=None, repeats_allowed=False, force=False): - """ - - :param merge_table: - :param n_residues: - :param n_phenotypes: - :param proportions: A Pandas Series denoting the number of each residue classification required - as produced by Series.value_counts on an amino acid column OR a Pandas DataFrame containing - a cross tabulation of two attributes giving the proportion of each residue class required as - produced by `pandas.crosstab`. - :return: - """ - - # TODO: if I read a variant table, I can get the actual AA composition and dssp and - # keep these constant - # TODO: currently different chains are handled by the `add_random_disease_variants` - # wrapper, is this ideal? - - # We are going to pick residues from the supplied merge_table, so first get rid of - # unobserved residues - merge_table = merge_table[merge_table.aa.notnull()].reset_index() - - # Create a random selection - ## TODO: Were rand indexes better as allowed repeats - shuffled_table = merge_table.reindex(permutation(merge_table.index)) - - if repeats_allowed: - # Copy all rows 21 times so that we have p > 0 of all possible variants on the same residue - row_replicator = range(len(shuffled_table)) * 21 - shuffled_table = shuffled_table.iloc[row_replicator, :].reset_index() - shuffled_table = shuffled_table.reindex(permutation(shuffled_table.index)) - - # By now index has been reset as neccessary so can pick columns - columns = [] - for col in ['UniProt_dbResNum', 'aa']: - columns.append(shuffled_table.columns.get_loc(col)) - - if proportions is None: - table = shuffled_table.iloc[:n_residues, columns] - - elif type(proportions) == Series: - table = DataFrame() - n_residues = sum(proportions) ## TODO: Fix this! - column_name = proportions.name - for value, count in proportions.iteritems(): - mask = shuffled_table[[column_name]] == value - rows = range(count) - try: - table = table.append(shuffled_table[mask].iloc[rows, columns]) - except IndexError: - msg = 'Fewer residues with {}: {} available than requested including repeats!' - logging.error(msg.format(column_name, value)) - if force: - msg = 'Falling back to giving all variants on this residue type.' - logging.warning(msg) - table = table.append(shuffled_table[mask].iloc[:, columns]) - n_residues = n_residues - count + sum(mask) - else: - msg = 'Could not generate variants with requested proportions. Try changing ' \ - 'proportions or use force=True.' - logging.error(msg) - raise - - - # If number drawn forces replicates, report it - n_choices = sum(merge_table[column_name] == value) - ratio = count / float(n_choices) - if count > n_choices: - msg = 'FORCED REPEATS: Fewer residues with {}: {} available than requested.' - logging.warning(msg.format(column_name, value)) - elif ratio > 0.8: - msg = 'RESTRICTED SELECTION: {}% of available residues with {}: {} requested.' - logging.warning(msg.format(round(ratio * 100), column_name, value)) - - elif type(proportions) == DataFrame: - # TODO: need to handle NaNs in `ss` - # In this case it is a cross tab and we want the proportions fixed for each pair - table = DataFrame() - n_residues = proportions.sum().sum() ## TODO: Fix this! - column_name = proportions.columns.name - row_name = proportions.index.name - for column, series in proportions.iteritems(): - for row, count in series.iteritems(): - mask = (shuffled_table[column_name] == column) & (shuffled_table[row_name] == row) - rows = range(count) - try: - table = table.append(shuffled_table[mask].iloc[rows, columns]) - except IndexError: - msg = 'Fewer residues with {}: {} and {}: {} available than requested ' \ - 'including repeats!' - logging.error(msg.format(column_name, column, row_name, row)) - if force: - msg = 'Falling back to giving all variants on this residue type.' - logging.warning(msg) - table = table.append(shuffled_table[mask].iloc[:, columns]) - n_residues = n_residues - count + sum(mask) - else: - msg = 'Could not generate variants with requested proportions. ' \ - 'Try changing proportions or use force=True.' - logging.error(msg) - raise - - # If number drawn forces replicates, report it - orig_mask = (merge_table[column_name] == column) & (merge_table[row_name] == row) - n_choices = sum(orig_mask) - ratio = count / float(n_choices) - if count > n_choices: - msg = 'FORCED REPEATS: Fewer residues with {}: {} and {}: {} available ' \ - 'than requested.' - logging.warning(msg.format(column_name, column, row_name, row)) - elif ratio > 0.8: - msg = 'RESTRICTED SELECTION: {}% of available residues with {}: {} ' \ - 'and {}: {} requested.' - logging.warning(msg.format(round(ratio * 100), column_name, column, row_name, row)) - - # Now generate random variant residues and phenotypes - selection = random_integers(0, n_phenotypes - 1, n_residues) - disease = [letters[i] for i in selection] - aa1 = array(list('ACDEFGHIKLMNPQRSTVWY')) - # TODO: set p to match a variant distribution - mut = choice(aa1, n_residues, replace=True) - - # And add them to table and make it exactly like a real uniprot_variant table - table['mut'] = mut - table['disease'] = disease - table = table.rename(columns={'aa': 'resn'}) - - # TODO: Fix any entries where resn == mut - # eq = table.resn == table.mut - # vars.mut[eq] = 'K' ## has warning but works - - return table - - -def add_random_disease_variants(merge_table, n_residues, n_phenotypes): - """ - Add phenotype annotations to random entries on a PDB merged table. - :param merge_table: - :param n_residues: - :param n_phenotypes: - :return: - """ - # If there are already variants on the table, we need to drop them and remove duplicate atoms - if 'resn' in merge_table.columns: - n_residues = sum(merge_table.resn.notnull() & isfinite(merge_table['Cartn_x'])) - n_phenotypes = len(merge_table.disease.dropna().unique()) - merge_table = merge_table.drop_duplicates(subset='UniProt_dbResNum').drop(['resn', 'mut', 'disease'], axis=1) - merge_table = merge_table[isfinite(merge_table['Cartn_x'])] - - # If we have more than one chain then we need to use split/apply/combine - n_prots = len(merge_table.UniProt_dbAccessionId.dropna().unique()) - n_chains = len(merge_table.chain_id.dropna().unique()) - if n_prots == 1 and n_chains == 1: - variants = random_uniprot_patho_table(merge_table, n_residues, n_phenotypes) - table = merge_table.merge(variants, how='left') - return table - - elif n_chains == 1: - # This means we have one chain that maps to multiple UniProts so we can - # randomly distribute the number of variants to each unique protein - n_vars_per_prot = [] - remaining = n_residues - for _ in xrange(n_prots - 1): - n_vars_per_prot.append(random_integers(0, remaining, 1)) - remaining = remaining - n_vars_per_prot[-1] - n_vars_per_prot.append(remaining) - shuffle(n_vars_per_prot) - - # Now split, apply, combine by iteration so we can vary the number of residues - # TODO: This drops any where uniprot is NaN, fix or log - grouped = merge_table.groupby('UniProt_dbAccessionId') - table = DataFrame() - for i, (name, group) in enumerate(grouped): - table = table.append(add_random_disease_variants(group, n_vars_per_prot[i], - n_phenotypes)) - return table - - elif n_prots == 1: - # This means there is one protein represented by multiple chains. Depending - # on the degree of overlaping UniProt coverage we have to avoid doubling the - # total number of variants. - - mask = merge_table.chain_id.notnull() - n_dupe = sum(merge_table[mask].duplicated(subset='UniProt_dbResNum', keep=False)) / n_chains - pc_duplicated = float(n_dupe) / len(merge_table[mask].UniProt_dbResNum.dropna().unique()) - adjustment = (1. / n_chains) * pc_duplicated - adj_n_residues = int(round(n_residues * adjustment)) - - # Now fetch variants and merge as usual - discrepancy = 2 - while abs(discrepancy) > 1: - variants = random_uniprot_patho_table(merge_table, adj_n_residues, n_phenotypes) - table = merge_table.merge(variants, how='left') - discrepancy = sum(table.resn.notnull()) - n_residues - adj_n_residues = adj_n_residues - (discrepancy / 2) - - return table - - else: - grouped = merge_table.groupby(['UniProt_dbAccessionId', 'chain_id']) - - # Work out the divisor for even distribution - cross = crosstab(merge_table.UniProt_dbAccessionId, merge_table.chain_id) - num = cross._get_numeric_data() - num[num > 0] = 1 - divisor = cross.sum().sum() - - n_residues = int(round(n_residues / divisor)) - table = DataFrame() - for name, group in grouped: - table = table.append(add_random_disease_variants(group, n_residues, n_phenotypes)) - return table diff --git a/analysis/utils.py b/analysis/utils.py deleted file mode 100644 index 0a7e31a..0000000 --- a/analysis/utils.py +++ /dev/null @@ -1,159 +0,0 @@ -#!/usr/bin/env python -# -*- coding: utf-8 -*- - - -import colorsys -import os -import numpy as np -from os import path - -from proteofav.config import defaults - - -def is_valid_file(parser, arg): - """ - Check if arg is a valid file and throw a parsing error if not. - - :param parser: argparse.ArgumentParser - :param arg: argument - :return: Open file handle - !FIXME argparse support file as an type - https://docs.python.org/2/library/argparse.html#type - """ - try: - return open(arg, 'r') - except: - parser.error("Not a valid file: %s" % arg) - - -def delete_file(filename): - """ - - :param filename: File to delete - :return: None - """ - os.remove(filename) - - -def create_directory(directory): - """ - Creates a directory structure if it does not exist. - - :param directory: directory name (expects full path) - :return: creates a directory if it does not exist yet - """ - return os.makedirs(directory) - - -def _get_colors(num_colors): - """ - See - http://stackoverflow.com/questions/470690/how-to-automatically-generate-n-distinct-colors - - :param num_colors: number of color - :return: a list of colors - :rtype: list - """ - colors = [] - for i in np.arange(0., 360., 360. / num_colors): - hue = i / 360. - lightness = (50 + np.random.rand() * 10) / 100. - saturation = (90 + np.random.rand() * 10) / 100. - colors.append(colorsys.hls_to_rgb(hue, lightness, saturation)) - return colors - - -def _fractional_to_cartesian(coords, pdb_id, matrix_only=False): - """ - Converts fractional unit cell coords to cartesian. - - :param coords: Atom coordinates - :param pdb_id: PDB id - :param matrix_only: boolean - :return: cartesian coordinates - :rtype: np.array - """ - - # retrieve and parse unit cell parameters - d = _mmcif_unit_cell(pdb_id) - a2r = np.pi / 180. - alpha = a2r * float(d['angle_alpha']) - beta = a2r * float(d['angle_beta']) - gamma = a2r * float(d['angle_gamma']) - a = float(d['length_a']) - b = float(d['length_b']) - c = float(d['length_c']) - - # unit cell volume - v = np.sqrt(1 - np.cos(alpha) * np.cos(alpha) - np.cos(beta) * np.cos(beta) - - np.cos(gamma) * np.cos(gamma) + 2 * np.cos(alpha) * np.cos(beta) * np.cos(gamma)) - - # build the transformation matrix - tr = np.matrix([ - [a, b * np.cos(gamma), c * np.cos(beta)], - [0, b * np.sin(gamma), - c * ((np.cos(alpha) - np.cos(beta) * np.cos(gamma)) / np.sin(gamma))], - [0, 0, c * (v / np.sin(gamma))] - ]) - - if matrix_only: - return tr - - # now apply the transformation to the coordinates - # TODO: type check this? - coords = np.matrix(coords) - coords = coords * tr - - # return the Nx3 results - return np.array(coords) - - -def _autoscale_axes(xyz, margin=5): - """ - Auto scales the xyz axes by a margin. - - :param xyz: Atom coordinates - :param margin: spacial margin size/length - :return: array - """ - - x = xyz[:, 0] - y = xyz[:, 1] - z = xyz[:, 2] - - rx = max(x) - min(x) - ry = max(y) - min(y) - rz = max(z) - min(z) - - max_range = max([rx, ry, rz]) + margin - - pad = [] - for i in [rx, ry, rz]: - pad.append((max_range - i) / 2) - - return [[max(x) + pad[0], min(x) - pad[0]], - [max(y) + pad[1], min(y) - pad[1]], - [max(z) + pad[2], min(z) - pad[2]]] - - -def _mmcif_unit_cell(pdb_id): - """ - Loader of mmCIF unit cell parameters. - - :param pdb_id: PDB id - :return: pandas table dataframe - :rtype: dict - """ - - cif_path = path.join(defaults.db_mmcif, pdb_id + '.cif') - - lines = [] - with open(cif_path) as inlines: - for line in inlines: - if line.startswith("_cell."): - lines.append(line.split('.')[1].rstrip()) - - l = [i.split() for i in lines] - d = {k: v for k, v in l} - - return d \ No newline at end of file diff --git a/analysis/visualise.py b/analysis/visualise.py deleted file mode 100644 index 8d67ad8..0000000 --- a/analysis/visualise.py +++ /dev/null @@ -1,198 +0,0 @@ -#!/usr/bin/env python -# -*- coding: utf-8 - - -import logging -import re - -import pandas as pd -import requests - -from proteofav.config import defaults -from proteofav.main import log -from proteofav.main import merge_tables -from proteofav.utils import get_url_or_retry - -try: - import pymol -except ImportError: - log.error('pymol not installed') - -__author__ = 'smacgowan' - - -def _fetch_variant_characteristics_from_identifiers(variant_ids, use_vep=False): - """ - Retrieves variant annotation from ENSEMBL. - - :param variant_ids: Ensembl Variant identifier - :param use_vep: whether to use predicted variants from VEP - :return: - """ - - # POST if given a list of ids - if isinstance(variant_ids, (list, pd.Series)): - # Remove any nans from the list - variant_ids = [i for i in variant_ids if not str(i) == 'nan'] - - ensembl_endpoint = "variation/homo_sapiens" - if use_vep: - ensembl_endpoint = "vep/human/id" - url = defaults.api_ensembl + ensembl_endpoint - headers = {"Content-Type": "application/json", - "Accept": "application/json"} - data = '{ "ids" : ' + str(variant_ids).replace("u'", "'") \ - + ', "phenotypes" : 1 }' # FIXME - data = data.replace("'", "\"") - result = requests.post(url, headers=headers, data=data) - return result - # GET if given single id - if isinstance(variant_ids, str): - ensembl_endpoint = "variation/homo_sapiens/" + variant_ids - if use_vep: - ensembl_endpoint = "vep/human/id/" + variant_ids - headers = {"Content-Type": "application/json"} - params = {"phenotypes": 1} - url = defaults.api_ensembl + ensembl_endpoint - result = get_url_or_retry(url, json=True, header=headers, **params) - return result - - -def visualise(pdb_id, assembly=False, use_ensembl=False, use_uniprot=False): - """ - - :param pdb_id: - :param group_by_trait: - :param use_ensembl: - :param use_uniprot: - :return: - """ - - def build_selection(chain, select_name, in_group, mapped_variants): - """ - - :param chain: - :param group: - :param in_group: - :param mapped_variants: - :return: - """ - - # Find the residues we want to highlight - in_chain = mapped_variants.chain_id == chain - start = mapped_variants.PDB_dbResNum[in_group & in_chain] - variant_residues = list(start.dropna().astype(int).astype(str).unique()) - - # Construct PyMol select command - # Sanitisation of the selection name for pymol is important - # or the name existence test will always fail and we'll over write - # entries from previous chains! - select_name = re.sub("[\W\d]+", "_", select_name.strip()) - if select_name not in pymol.cmd.get_names('selections'): - pymol.cmd.select(select_name, 'none') - selection = 'chain ' + chain + ' and resi ' + '+'.join( - variant_residues) + ' or ' + select_name - - # Make the selection - message = "Creating PyMol selection {} from '{}'".format(select_name, - selection) - logging.debug(message) - pymol.cmd.select(select_name, selection) - - # Apply some styles - pymol.cmd.show("lines", select_name) - pymol.util.cnc(select_name) - - # Open the PDB as requested with PyMol and apply a few styles - pymol.finish_launching() - if assembly: - pymol.cmd.fetch(pdb_id, type='pdb1') - pymol.cmd.set('all_states', 'on') - else: - pymol.cmd.fetch(pdb_id) - - pymol.cmd.hide("everything", "all") - pymol.cmd.show("ribbon", "all") - pymol.util.cbc() - - # Get variants for all chains - residue_mappings = merge_tables(pdb_id=pdb_id, chain='all', - add_ensembl_variants=True) - has_variant = residue_mappings.start.notnull() - - # If we're going to make selections from ensembl traits get that data now - if use_ensembl: - variant_ids = residue_mappings.id_y[has_variant] - traits = ensembl_traits(variant_ids) - - # Now create a PyMol selection for the variants on each chain - chains = pymol.cmd.get_chains(pdb_id) - for chain in chains: - group = 'chain_' + chain - in_chain = residue_mappings.chain_id == chain - build_selection(chain, select_name=group, in_group=in_chain & has_variant, - mapped_variants=residue_mappings) - - if use_ensembl: - groups = set(zip(*traits)[1]) - for group in groups: - variants_in_group = [] - for id, trait in traits: - if trait == group: - variants_in_group.append(id) - - # Get the relevant residues and create - # selection for current group - in_group = [True if x in variants_in_group else False for x in - residue_mappings.id_y] - - build_selection(chain, group, in_group, residue_mappings) - - if use_uniprot: - - # Extract first uniprot (REFACTOR THIS, also `merge_tables`) - structure_uniprots = residue_mappings.UniProt_dbAccessionId[in_chain] - structure_uniprots = structure_uniprots[ - structure_uniprots.notnull()] - structure_uniprot = structure_uniprots.unique()[0] - - # Get the variants and merge onto residue_mappings - uniprot_vars = _fetch_uniprot_variants(structure_uniprot) - # Not ideal as UniProt_dbResNum is not unique but is fit for - # purpose - - mapped = pd.merge(residue_mappings, uniprot_vars, - on='UniProt_dbResNum') - - # Create a selection for each trait - groups = mapped.disease.unique() - for group in groups: - in_group = mapped.disease == group - - build_selection(chain, group, in_group, mapped) - - -def ensembl_traits(variant_ids): - """ - - :param variant_ids: - :return: - """ - # For now, need to iterate with GET requests - # until POST can retrieve phenotypes - traits = [] - for variant in variant_ids: - phenos = \ - _fetch_variant_characteristics_from_identifiers(str(variant))[ - 'phenotypes'] - if phenos == []: - traits.append([variant, 'No_Available_Phenotype']) - else: - for entry in phenos: - trait = entry['trait'] - traits.append([variant, trait]) - return traits - - -if __name__ == '__main__': - visualise('3tnu', assembly=True, use_ensembl=True, use_uniprot=True) diff --git a/analysis/visualise2.py b/analysis/visualise2.py deleted file mode 100644 index 061683a..0000000 --- a/analysis/visualise2.py +++ /dev/null @@ -1,218 +0,0 @@ -#!/usr/bin/env python -# -*- coding: utf-8 - -import logging -import re - -import pandas as pd -import pymol ##TODO: This import kicks of pymol, consider it for in function. -from analysis.clustering import clustered_table_to_partition_and_points, add_clusters_to_points -from pymol.cgo import * -from scipy.spatial import ConvexHull - -from analysis.pymol_scripts import drawBoundingBox - - -def view_table(table, show=None, show_group_by=None, biological_assembly=True): - """ - View the PDB entry associated with the provided structure table in PyMol and optionally create residue selections - based on annotation columns. - - :param table: A structure table from `main.merge_tables` - :param show: List of annotation columns to produce a selection passed on a boolean test (e.g., 'has_variant`) - :param show_group_by: List of annotation columns to produce a selection based on the annotations value - :param biological_assembly: Show the biological assembly. - :return: - """ - - # First figure out what PDB and chains are in the table - pdb_id = table.PDB_dbAccessionId.unique()[0] - - # Open the PDB as requested with PyMol and apply a few styles - pymol.finish_launching() - if biological_assembly: - pymol.cmd.fetch(pdb_id, type='pdb1') - pymol.cmd.set('all_states', 'on') - else: - pymol.cmd.fetch(pdb_id) - - pymol.cmd.hide("everything", "all") - pymol.cmd.show("ribbon", "all") - pymol.util.cbc() - - # Create a pymol selection for any column names in `show` ---------- - - # First find PDB_dbResNum (as could be column or index) and chain IDs - if table.index.name == 'PDB_dbResNum': - residueIds = pd.Series(table.index, index=table.index) - else: - residueIds = table.PDB_dbResNum - - # Get residue IDs in suitable format and drop residues with no PDB reference - ##TODO: this may be useful elsewhere - dropped = residueIds.isnull() - residueIds = residueIds.dropna() - residueIds = residueIds.astype('object').astype('int').astype('string') - table = table[dropped == False] - - chain_ids = table.chain_id - unique_chains = chain_ids.dropna().unique() - - # Now create labelled boolean selections - selections = [] - if show: - for column in show: - ## TODO: either parametrise test (e.g. allow .isnull() or create inverse selection too. - select_atom = table[column].notnull() - select_name = 'has_' + column - - # Selection must be built per chain to avoid ambiguous selections - for chain in unique_chains: - select_ResNums = residueIds[select_atom & (chain_ids == chain)] # Get correct residues - selections.append(make_selection(chain, select_ResNums, select_name)) - - # Create level selections - if show_group_by: - for column in show_group_by: - unique_values = table[column].dropna().unique() - for value in unique_values: - select_atom = (table[column] == value) - select_name = column + '_{}'.format(value) - for chain in unique_chains: - select_ResNums = residueIds[select_atom & (chain_ids == chain)] # Get correct residues - selections.append(make_selection(chain, select_ResNums, select_name)) - - selections = set(selections) - - # Now style them - if len(selections) > 0: - for select_name in selections: - style_selection(select_name) - - -def make_selection(chain, select_ResNums, select_name): - """ - Create a new selection or add residues to an existing selection in PyMol. - - :param chain: A Chain ID - :param select_ResNums: PDB residue numbers - :param select_name: The name for the selection - :return: - """ - # Sanitise select_name - select_name = re.sub("[!@#$%^&*()'\"[\]{}\|~`<>.?/ ]+", "_", select_name.strip()) - - # Create or append to the selection - if select_name not in pymol.cmd.get_names('selections'): - pymol.cmd.select('"{0}"'.format(select_name), 'none') - logging.debug('Created selection "{0}" in PyMol'.format(select_name)) - selection = 'chain ' + chain + ' and resi ' + '+'.join( - select_ResNums) + ' or ' + select_name - pymol.cmd.select(select_name, selection) - message = 'Added residues "{0}" to PyMol selection "{1}"'.format(selection, select_name) - logging.debug(message) - - return select_name - - -def style_selection(select_name): - # Apply some styles - pymol.cmd.show("lines", select_name) - pymol.util.cnc(select_name) - - # # Show bounding surface - # pymol.cmd.flag('ignore', 'not ' + select_name, 'set') - # pymol.cmd.delete('indicate') - # pymol.cmd.show('surface') - # pymol.cmd.rebuild() - # pymol.cmd.flag('ignore', 'all', 'reset') - - drawBoundingBox(select_name) - - -def int_to_chain(x): - if x <= 25: - return chr(x + ord('A')) - else: - y = (x / 26) - return chr((y - 1) + ord('A')) + int_to_chain(x - (26 * y)) - - -def plot_convex_hulls(clustered_table): - # Extract points for convex hull calculation - part, points = clustered_table_to_partition_and_points(clustered_table) - point_table = add_clusters_to_points(part, points) - - # Don't bother with clusters of less than four points - counts = point_table.cluster_id.value_counts() - clusters_to_drop = list(counts[counts < 4].index) - for cluster_id in clusters_to_drop: - point_table = point_table[point_table['cluster_id'] != cluster_id] - - grouped_point_tables = point_table.groupby('cluster_id') - - # Calculate convex hulls - cluster_hulls = [] - for _, cluster_point_table in grouped_point_tables: - _, cluster_points = clustered_table_to_partition_and_points(cluster_point_table) - cluster_hulls.append(ConvexHull(cluster_points)) - - # Prepare hull CGO lists - hull_cgo_lists = [] - for hull, (_, cluster_point_table) in zip(cluster_hulls, grouped_point_tables): - # Calculate facets - cgo_facets = [] - for simplex in hull.simplices: - _, cluster_points = clustered_table_to_partition_and_points(cluster_point_table) - cgo = build_cgo(cluster_points[simplex, ]) - cgo_facets.append(cgo) - hull_cgo_lists.append(concat_cgo_lists(cgo_facets)) - - # Plot them all - for i, cgo in enumerate(hull_cgo_lists): - pymol.cmd.load_cgo(cgo, 'hull_' + str(i)) - - -def build_cgo(array): - cgo = [ - BEGIN, LINES, - COLOR, 1., 1., 1. - ] - - # Draw lines between points - for start, finish in zip(array[:-1], array[1:]): - cgo.append(VERTEX) - for component in start: - cgo.append(component) - cgo.append(VERTEX) - for component in finish: - cgo.append(component) - - # Once more to join ends - start, finish = array[-1], array[0] - cgo.append(VERTEX) - for component in start: - cgo.append(component) - cgo.append(VERTEX) - for component in finish: - cgo.append(component) - - cgo.append(END) - - return cgo - - -def concat_cgo_lists(list_of_cgo_lists): - concat_cgo = [] - for i, cgo in enumerate(list_of_cgo_lists): - i += 1 - if i == 1: - mod_cgo = cgo[:-1] # Remove END element - elif i < len(list_of_cgo_lists): - mod_cgo = cgo[6:-1] # Remove BEGIN, LINES, COLOR and rgb elements and END - else: - mod_cgo = cgo[6:] # Remove BEGIN, LINES, COLOR and rgb elements - concat_cgo.append(mod_cgo) - concat_cgo[:] = [e for cgo in concat_cgo for e in cgo] - return concat_cgo - diff --git a/proteofav/__init__.py b/proteofav/__init__.py index ad5751a..c3add08 100644 --- a/proteofav/__init__.py +++ b/proteofav/__init__.py @@ -1,11 +1,12 @@ -#!/usr/bin/env python # -*- coding: utf-8 + """ -ProteoFAV: protein feature aggregation and variants --------------------------------------------------- +ProteoFAV: Protein Feature Aggregation and Variants +--------------------------------------------------- -Exploring the power of Pandas to work with protein structures, -sequences and genetic variants. +Open-source framework for simple and fast integration +of protein structure data with sequence annotations +and genetic variation :copyright: (c) 2015-2017. :license: TBD, see LICENSE for more details. diff --git a/proteofav/annotation.py b/proteofav/annotation.py new file mode 100644 index 0000000..3aec821 --- /dev/null +++ b/proteofav/annotation.py @@ -0,0 +1,189 @@ +# -*- coding: utf-8 + +""" +Created on 17:26 19/02/2016 2016 +Define auxiliary functions for interacting with Uniprot. +""" + +import os +import logging +import pandas as pd + +try: + # python 2.7 + from StringIO import StringIO +except ImportError: + from io import StringIO, BytesIO +try: + # python 2.7 + from urlparse import parse_qs +except ImportError: + from urllib.parse import parse_qs + +from proteofav.config import defaults +from proteofav.utils import (exclude_columns, constrain_column_types, + Downloader, GenericInputs) +from proteofav.library import annotation_types + +log = logging.getLogger('proteofav.config') + +__all__ = ["_fetch_uniprot_gff", "parse_gff_features", "filter_annotation", + "select_annotation", "download_annotation", "Annotation"] + + +def parse_gff_features(filename, excluded_cols=None): + """ + Map Uniprot GFF features to the protein sequence. + + :param filename: path to the Annotation file + :param excluded_cols: option to exclude Validation columns + :return: returns a pandas DataFrame + """ + + header = ('NAME', 'SOURCE', 'TYPE', 'START', 'END', + 'SCORE', 'STRAND', 'FRAME', 'GROUP', 'empty') + data = pd.read_table(filename, skiprows=2, names=header) + groups = data.GROUP.apply(parse_qs) + groups = pd.DataFrame.from_records(groups) + + table = data.merge(groups, left_index=True, right_index=True) + + # excluding columns + if excluded_cols is None: + excluded_cols = ('empty',) + table = exclude_columns(table, excluded=excluded_cols) + + # enforce some specific column types + table = constrain_column_types(table, col_type_dict=annotation_types) + + if table.empty: + raise ValueError("The filters resulted in an empty DataFrame...") + return table + + +def annotation_aggregation(table, identifier=None, query_type='', group_residues=True, + drop_types=('Helix', 'Beta strand', 'Turn', 'Chain')): + """ + Filtering and making the final Annotation Table. + + :param table: pandas DataFrame object + :param identifier: to add a new column with 'accession' ID + :param str query_type: Select type of feature + :param bool group_residues: by default each row in the resulting table, + maps to a residue. When set to False, each row represent a feature + per residue. + :param tuple drop_types: Filter out some of the features, important to + remove fetures that spam. + :return pd.DataFrame: table. Columns will depend on parameters. + """ + if query_type: + table = table[table.TYPE == query_type] + elif drop_types: + table = table[~table.TYPE.isin(drop_types)] + + lines = [] + for i, row in table.iterrows(): + lines.extend({'idx': i, 'annotation': _annotation_writer(row)} + for i in range(row.START, row.END + 1)) + table = pd.DataFrame(lines) + + if group_residues: + table = table.groupby('idx').agg({'annotation': lambda x: ', '.join(x)}) + + table['site'] = table.index.astype(str) + table['accession'] = [identifier] * len(table) + if table.empty: + raise ValueError("The filters resulted in an empty DataFrame...") + return table + + +def _annotation_writer(gff_row): + """ + Establish a set of rules to annotate Uniprot GFF. + + :param pd.Series gff_row: each line in the GFF file. + :return str: template filled with type-specific fields. + """ + if not gff_row.ID and not gff_row.Note: + return gff_row.TYPE + elif not gff_row.ID: + return '{0.TYPE}: {0.Note}'.format(gff_row) + elif not gff_row.Note: + return '{0.TYPE} ({0.ID})'.format(gff_row) + else: + return '{0.TYPE}: {0.Note} ({0.ID})'.format(gff_row) + + +def filter_annotation(table, identifier=None, annotation_agg=False, **kwargs): + """ + Filtering and making the final Annotation Table. + + :param table: pandas DataFrame object + :param identifier: to add a new column with 'accession' ID + :param annotation_agg: boolean + :return: returns a pandas DataFrame + """ + + if annotation_agg: + table = annotation_aggregation(table, identifier=identifier, **kwargs) + + if table.empty: + raise ValueError("The filters resulted in an empty DataFrame...") + return table + + +def select_annotation(identifier, excluded_cols=None, overwrite=False, **kwargs): + """ + Produces table from PDB validation XML file. + + :param identifier: UniProt accession ID + :param excluded_cols: option to exclude columns + :param overwrite: boolean + :return: returns a pandas DataFrame + """ + filename = os.path.join(defaults.db_annotation, "{}.gff".format(identifier)) + + download_annotation(identifier=identifier, filename=filename, + overwrite=overwrite) + + table = parse_gff_features(filename=filename, excluded_cols=excluded_cols) + table = filter_annotation(table, identifier, **kwargs) + table = constrain_column_types(table, col_type_dict=annotation_types) + return table + + +def download_annotation(identifier=None, filename=None, overwrite=False): + """ + Downloads a Annotation GFF from the UniProt. + + :param identifier: (str) UniProt accession ID + :param filename: path to the Validation file + :param overwrite: (boolean) + :return: (side effects) output file path + """ + + url_root = defaults.api_uniprot + url_endpoint = "{}.gff".format(identifier) + url = url_root + url_endpoint + Downloader(url=url, filename=filename, + decompress=False, overwrite=overwrite) + + +class Annotation(GenericInputs): + def read(self, filename=None, **kwargs): + filename = self._get_filename(filename) + self.table = parse_gff_features(filename=filename, **kwargs) + return self.table + + def download(self, identifier=None, filename=None, **kwargs): + identifier = self._get_identifier(identifier) + filename = self._get_filename(filename) + return download_annotation(identifier=identifier, filename=filename, **kwargs) + + def select(self, identifier=None, **kwargs): + identifier = self._get_identifier(identifier) + self.table = select_annotation(identifier=identifier, **kwargs) + return self.table + + +Annotation = Annotation() diff --git a/proteofav/config.txt b/proteofav/config.ini similarity index 69% rename from proteofav/config.txt rename to proteofav/config.ini index 216e36e..61daf97 100644 --- a/proteofav/config.txt +++ b/proteofav/config.ini @@ -1,9 +1,11 @@ -# proteofav config file +# ProteoFAV main configuration file. [Global] db_pdb = ... db_mmcif = ... db_sifts = ... db_dssp = ... +db_validation = ... +db_annotation = ... db_germline_variants = ... db_somatic_variants = ... @@ -13,9 +15,9 @@ api_rcsb = http://www.rcsb.org/pdb/rest/ api_uniprot = http://www.uniprot.org/uniprot/ api_ensembl = http://rest.ensembl.org/ api_icgc = https://dcc.icgc.org/api/v1/ -api_ebi_uniprot = http://www.ebi.ac.uk/proteins/api/ +api_proteins = http://www.ebi.ac.uk/proteins/api/ -cif_fetch = http://www.ebi.ac.uk/pdbe/entry-files/ +pdbe_fetch = http://www.ebi.ac.uk/pdbe/entry-files/ bio_fetch = http://www.ebi.ac.uk/pdbe/static/entry/download/ dssp_fetch = ftp://ftp.cmbi.ru.nl//pub/molbio/data/dssp/ sifts_fetch = ftp://ftp.ebi.ac.uk/pub/databases/msd/sifts/xml/ @@ -23,8 +25,3 @@ validation_fetch = http://www.ebi.ac.uk/pdbe/entry-files/download/ [Variables] contact_email = ... -cif_extension = _updated.cif -bio_extension = .cif.gz -dssp_extension = .dssp -sifts_extension = .xml.gz -validation_extension = _validation.xml diff --git a/proteofav/config.py b/proteofav/config.py index 774ed83..f0d8bdf 100644 --- a/proteofav/config.py +++ b/proteofav/config.py @@ -1,5 +1,5 @@ -#!/usr/bin/env python # -*- coding: utf-8 -*- + """ Defines the methods that load and validate user configuration parameters, such as data resources web address or local and remote file paths. @@ -8,11 +8,9 @@ >>> print(defaults.api_pdbe) http://www.ebi.ac.uk/pdbe/api/ >>> from proteofav.config import Defaults ->>> local_defaults = Defaults("config.txt") +>>> local_defaults = Defaults('config.ini') >>> print(local_defaults.api_uniprot) http://www.uniprot.org/uniprot/ ->>> print(local_defaults.sifts_extension) -.xml.gz >>> print(local_defaults.email) Traceback (most recent call last): ... @@ -20,27 +18,25 @@ """ -from __future__ import absolute_import - -import tempfile -import logging import os -from os import path import sys +import click +import logging +import tempfile + try: # python 2.7 from ConfigParser import ConfigParser except ImportError: from configparser import ConfigParser -import click - -__all__ = ["defaults", "Defaults"] log = logging.getLogger(__name__) logging.captureWarnings(True) logging.basicConfig(stream=sys.stderr, level=logging.INFO, format='%(asctime)s - %(levelname)s - %(message)s ') +__all__ = ["defaults", "Defaults"] + class Defaults(object): """ @@ -53,25 +49,25 @@ class Defaults(object): >>> defaults.api_pdbe = 'test' >>> print(defaults.api_pdbe) test - """ + def __init__(self, config_file=None): if config_file: # user provided config pass - elif path.isfile(path.join(click.get_app_dir('proteofav'), 'config.txt')): + elif os.path.isfile(os.path.join(click.get_app_dir('proteofav'), 'config.ini')): # os config - config_file = path.join(click.get_app_dir('proteofav'), 'config.txt') + config_file = os.path.join(click.get_app_dir('proteofav'), 'config.ini') else: # proteofav default config - config_file = path.join(path.dirname(__file__), 'config.txt') + config_file = os.path.join(os.path.dirname(__file__), 'config.ini') config = ConfigParser() - if path.isfile(config_file): + if os.path.isfile(config_file): config.read(config_file) self.__config = config self.populate_attributes() self.config_file = config_file - else: # pragma: no cover + else: # pragma: no cover raise IOError('Config file {} not available.'.format(config_file)) def populate_attributes(self): @@ -91,14 +87,14 @@ def update(self, config_file): def commit_configuration(self): pass - def write(self, file_path=None): - file_path = file_path or path.join(click.get_app_dir('proteofav'), 'config.txt') + file_path = file_path or os.path.join(click.get_app_dir('proteofav'), 'config.ini') - if not path.exists(path.dirname(file_path)): - os.makedirs(path.dirname(file_path)) + if not os.path.exists(os.path.dirname(file_path)): + os.makedirs(os.path.dirname(file_path)) # self.reverse_attributes() # TODO reverse populate from __dict__ to self.config with open(file_path, 'w') as f: self.__config.write(f) + defaults = Defaults() diff --git a/proteofav/dssp.py b/proteofav/dssp.py new file mode 100644 index 0000000..d69cf8a --- /dev/null +++ b/proteofav/dssp.py @@ -0,0 +1,444 @@ +# -*- coding: utf-8 -*- + +import os +import logging +import pandas as pd +from string import digits +from string import ascii_uppercase + +try: + # python 2.7 + from StringIO import StringIO +except ImportError: + from io import StringIO + +from proteofav.structures import select_structures +from proteofav.utils import (row_selector, InputFileHandler, + constrain_column_types, exclude_columns, + GenericInputs, Downloader) +from proteofav.library import (scop_3to1, dssp_types, aa_codes_1to3_extended) +from proteofav.library import (ASA_Miller, ASA_Wilke, ASA_Sander) + +from proteofav.config import defaults + +log = logging.getLogger('proteofav.config') + +__all__ = ['parse_dssp_residues', '_import_dssp_chains_ids', 'select_dssp', + 'filter_dssp', 'get_rsa', 'get_rsa_class', 'download_dssp', 'DSSP'] + + +def parse_dssp_residues(filename, excluded_cols=None): + """ + Parse lines of the DSSP file to get entries for every Residue + in each CHAIN. The hierarchy is maintained. CHAIN->RESIDUE->[...]. + + :param filename: path to the DSSP file + :param excluded_cols: list of columns to be excluded + :return: returns a pandas DataFrame + """ + + log.info("Parsing DSSP from lines...") + + # example lines with some problems + """ + # RESIDUE AA STRUCTURE BP1 BP2 ACC N-H-->O O-->H-N N-H-->O O-->H-N TCO KAPPA ALPHA PHI PSI X-CA Y-CA Z-CA + 1 1 A M 0 0 127 0, 0.0 345,-0.1 0, 0.0 3,-0.1 0.000 360.0 360.0 360.0 162.0 -18.7 21.6 -55.4 + 2 2 A R + 0 0 117 1,-0.1 28,-0.4 343,-0.1 2,-0.3 0.455 360.0 81.5-136.8 -28.7 -17.0 22.3 -52.1 + + 381 394 A K 0 0 125 -2,-0.4 -21,-0.1 -21,-0.2 -2,-0.0 -0.421 360.0 360.0 64.1 360.0 -22.5 44.2 -25.4 + 382 !* 0 0 0 0, 0.0 0, 0.0 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 360.0 0.0 0.0 0.0 + 383 1 A M 0 0 127 0, 0.0 345,-0.1 0, 0.0 3,-0.1 0.000 360.0 360.0 360.0 162.0 -10.0 71.4 -55.4 + + 10278 103 H H E -XZ1023010269W 69 -9,-2.3 -9,-2.2 -2,-0.3 2,-1.0 -0.884 22.6-128.4-108.1 141.6 -97.0 28.7 112.2 + 10279 104 H I E +XZ1022910268W 0 -50,-2.2 -50,-0.6 -2,-0.4 -11,-0.3 -0.801 30.6 175.4 -90.4 95.6 -98.5 32.0 111.3 + 10280 105 H L E + 0 0 21 -13,-1.7 -55,-2.5 -2,-1.0 2,-0.3 0.812 62.6 4.9 -70.5 -35.5 -96.3 34.5 113.1 + + # missing segment break + 145 ! 0 0 0 0, 0.0 0, 0.0 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 360.0 0.0 0.0 0.0 + + # chain break + 382 !* 0 0 0 0, 0.0 0, 0.0 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 360.0 0.0 0.0 0.0 + """ + + InputFileHandler(filename) + + lines = [] + parse = False + with open(filename) as inlines: + for line in inlines: + line = line.rstrip() + if parse: + lines.append(line) + if line.startswith(" #"): + parse = True + lines = "\n".join(lines) + + # column width descriptors + header = ("LINE", "RES", "RES_FULL", "INSCODE", "CHAIN", "AA", "SS", "STRUCTURE", + "BP1", "BP2", "BP2_CHAIN", "ACC", + "NH_O_1", "NH_O_1_nrg", "O_HN_1", "O_HN_1_nrg", + "NH_O_2", "NH_O_2_nrg", "O_HN_2", "O_HN_2_nrg", + "TCO", "KAPPA", "ALPHA", "PHI", "PSI", + "X-CA", "Y-CA", "Z-CA") + + widths = ((0, 5), (5, 10), (5, 11), (10, 11), (11, 12), (12, 15), (16, 17), (17, 25), + (25, 29), (29, 33), (33, 34), (34, 38), + (38, 45), (46, 50), (50, 56), (57, 61), + (61, 67), (68, 72), (72, 78), (79, 84), + (85, 91), (91, 97), (97, 103), (103, 109), (109, 115), + (115, 123), (123, 130), (130, 137)) + + all_str = {key: str for key in header} + table = pd.read_fwf(StringIO(lines), names=header, colspecs=widths, + compression=None, converters=all_str, keep_default_na=False) + + # excluding columns + if excluded_cols is None: + excluded_cols = ("LINE", "STRUCTURE", "BP1", "BP2", "BP2_CHAIN", + "NH_O_1", "NH_O_1_nrg", "O_HN_1", "O_HN_1_nrg", + "NH_O_2", "NH_O_2_nrg", "O_HN_2", "O_HN_2_nrg", + "X-CA", "Y-CA", "Z-CA") + + table = exclude_columns(table, excluded=excluded_cols) + + # enforce some specific column types + table = constrain_column_types(table, col_type_dict=dssp_types) + + if table.empty: + log.error('DSSP file {} resulted in a empty Dataframe'.format(filename)) + raise ValueError('DSSP file {} resulted in a empty Dataframe'.format( + filename)) + return table + + +def _import_dssp_chains_ids(pdb_id): + """Imports mmCIF chain identifier to DSSP. + + :param pdb_id: + :return: DSSP table with corrected chain ids. + """ + dssp_table = select_dssp(pdb_id) + cif_table = select_structures(pdb_id) + cif_seq = cif_table.auth_comp_id.apply(scop_3to1.get) + dssp_has_seq = dssp_table.aa.isin(scop_3to1.values()) + dssp_seq = dssp_table.aa[dssp_has_seq] + # Import only if the sequences are identical + if not (cif_seq == dssp_seq).all(): + err = ('Inconsitent DSSP / mmCIF sequence for {} protein structure cannot be fixed' + 'by import_dssp_chains_ids') + raise ValueError(err.format(pdb_id)) + dssp_table.loc[dssp_has_seq, 'CHAIN'] = cif_table.auth_asym_id + return dssp_table + + +def _add_dssp_rsa(data, method="Sander"): + """ + Utility that adds a new column to the table. + Adds a new column with Relative Solvent Accessibility (RSA). + + :param data: pandas DataFrame object + :param method: name of the method + :return: returns a modified pandas DataFrame + """ + + table = data + rsas = [] + for i in table.index: + rsas.append(get_rsa(table.loc[i, "ACC"], table.loc[i, "AA"], + method=method)) + table["RSA"] = rsas + return table + + +def _add_dssp_full_chain(data): + """ + Utility that adds a new column to the table. + Specific to DSSP outputs that are generated from mmCIF files containing + multiple char chain IDs (e.g. 'AA' and 'BA'). These are found in the + Biological Unit mmCIF structures. + + :param data: pandas DataFrame object + :return: returns a modified pandas DataFrame + """ + + # BioUnits chain naming seems to follow the pattern: + # chain A becomes AA then + # AA->AZ then A0->A9 [A-Z then 0-9] and then AAA->AAZ and AA0->AA9 + # then ABA->ABZ and AB0->AB9 + alpha1 = [k for k in ascii_uppercase + digits] + alpha2 = ['A' + k for k in alpha1] + alpha3 = ['B' + k for k in alpha1] + new_alphabet = alpha1 + alpha2 + alpha3 + + table = data + chains_full = [] + c = -1 + for ix in table.index: + chain_id = table.loc[ix, "CHAIN"] + aa_id = table.loc[ix, "AA"] + if aa_id == "!*": + if table.loc[ix - 1, "CHAIN"] == table.loc[ix + 1, "CHAIN"]: + c += 1 + else: + c = -1 + if c != -1 and aa_id != "!*" and aa_id != "!": + if c >= len(new_alphabet): + raise IndexError('Alphabet needs update to accommodate ' + 'such high number of chains...') + chain_id += new_alphabet[c] + chains_full.append(chain_id) + if not chains_full: + table["CHAIN_FULL"] = table["CHAIN"] + else: + table["CHAIN_FULL"] = chains_full + return table + + +def _add_dssp_rsa_class(data, rsa_col='RSA'): + """ + Utility that adds a new column to the table. + Adds a new column with Relative Solvent Accessibility (RSA) classes. + + :param data: pandas DataFrame object + :param rsa_col: column name + :return: returns a modified pandas DataFrame + """ + + table = data + rsas_class = [] + for i in table.index: + rsas_class.append(get_rsa_class(table.loc[i, "{}".format(rsa_col)])) + table["{}_CLASS".format(rsa_col)] = rsas_class + return table + + +def _add_dssp_ss_reduced(data): + """ + Utility that adds a new column to the table. + Adds a reduced-stated Secondary Structure (SS). + + :param data: pandas DataFrame object + :return: returns a modified pandas DataFrame + """ + + table = data + alphas = ['H'] + betas = ['E'] + coils = ['G', 'I', 'B', 'C', 'T', 'S', '', ' '] + + # replace some NaN with custom strings + # table['SS'] = table.SS.fillnan('-') + sss = [] + for ix in table.index: + ss = table.loc[ix, "SS"] + if ss in alphas: + ss = 'H' + elif ss in betas: + ss = 'E' + elif ss in coils: + ss = 'C' + else: + ss = '-' + sss.append(ss) + + table["SS_CLASS"] = sss + + return table + + +def get_rsa(acc, resname, method="Sander"): + """ + Computes Relative Solvent Accessibility (RSA) from an input + DSSP ACC value, and according to ASA standard values. + + :param acc: (int) DSSP ACC + :param resname: single letter residue name + :param method: name of the method + :return: (float) RSA value + """ + + rsa = "" + try: + acc = float(acc) + except ValueError: + return rsa + + try: + assert len(resname) == 1 + except AssertionError: + return rsa + + if method == "Miller": + sasa = ASA_Miller + elif method == "Wilke": + sasa = ASA_Wilke + elif method == "Sander": + sasa = ASA_Sander + else: + raise ValueError("Method {} is not implemented...".format(method)) + + try: + rsa = round((acc / sasa[aa_codes_1to3_extended[resname]] * 100), 3) + except KeyError: + return rsa + + return rsa + + +def get_rsa_class(rsa): + """ + Gets a class based on the RSA value + + :param rsa: (float) RSA score or string + :return: RSA class + """ + rsa_class = '-' + try: + rsa = float(rsa) + # surface is rsa >= 25% (value = 2) + # exposed is rsa >= 5% and rsa < 25% (value = 1) + # core is rsa < 5% (value = 0) + if rsa >= 25.0: + rsa_class = 'Surface' + elif 5.0 <= rsa < 25.0: + rsa_class = 'Part. Exposed' + else: + rsa_class = 'Core' + except ValueError: + # returns a string + pass + return rsa_class + + +def select_dssp(identifier, excluded_cols=None, overwrite=False, **kwargs): + """ + Produce table from DSSP file output. + + :param identifier: PDB/mmCIF accession ID + :param excluded_cols: option to exclude DSSP columns + :param overwrite: boolean + :return: returns a pandas DataFrame + """ + + filename = os.path.join(defaults.db_dssp, "{}.dssp".format(identifier)) + + download_dssp(identifier=identifier, filename=filename, overwrite=overwrite) + + table = parse_dssp_residues(filename=filename, excluded_cols=excluded_cols) + + table = filter_dssp(table=table, excluded_cols=excluded_cols, **kwargs) + table = constrain_column_types(table, col_type_dict=dssp_types) + + if table.duplicated(['RES_FULL', 'CHAIN']).any(): + log.info('DSSP file for {} has not unique index'.format(identifier)) + return table + + +def filter_dssp(table, excluded_cols=None, + chains=None, chains_full=None, res=None, + add_full_chain=True, add_ss_reduced=False, + add_rsa=True, rsa_method="Sander", add_rsa_class=False, + reset_res_id=False): + """ + Filter for DSSP Pandas Dataframes. + + :param table: pandas DataFrame object + :param excluded_cols: option to exclude DSSP columns + :param chains: (tuple) chain IDs or None + :param chains_full: (tuple) alternative chain IDs or None + :param res: (tuple) res IDs or None + :param add_full_chain: boolean + :param add_ss_reduced: boolean + :param add_rsa: boolean + :param rsa_method: "Sander", "Miller" or "Wilke" + :param add_rsa_class: boolean + :param reset_res_id: boolean + :return: returns a pandas DataFrame + """ + + # selections / filtering + # excluding columns + table = exclude_columns(table, excluded=excluded_cols) + + # table modular extensions + if add_full_chain: + table = _add_dssp_full_chain(table) + log.info("DSSP added full chain...") + + table['SS'] = table.SS.fillna('-') + if add_ss_reduced: + table = _add_dssp_ss_reduced(table) + log.info("DSSP added reduced SS...") + + if add_rsa: + table = _add_dssp_rsa(table, method=rsa_method) + log.info("DSSP added RSA...") + + if add_rsa_class: + table = _add_dssp_rsa_class(table) + log.info("DSSP added RSA class...") + + # drop missing residues ("!") and chain breaks ("!*") + table = table[table['AA'] != '!'] + table = table[table['AA'] != '!*'] + + # excluding rows + if chains is not None: + table = row_selector(table, 'CHAIN', chains) + log.info("DSSP table filtered by CHAIN...") + + if chains_full is not None: + table = row_selector(table, 'CHAIN_FULL', chains_full) + log.info("DSSP table filtered by CHAIN_FULL...") + + if res is not None: + table = row_selector(table, 'RES', res) + log.info("DSSP table filtered by RES...") + + if reset_res_id: + table.reset_index(inplace=True) + table = table.drop(['index'], axis=1) + table['LINE'] = table.index + 1 + log.info("DSSP reset residue number...") + + if table.empty: + raise ValueError("The filters resulted in an empty DataFrame...") + return table + + +def download_dssp(identifier=None, filename=None, overwrite=False): + """ + Downloads a pre-computed DSSP from the CMBI Netherlands FTP + to the filesystem. + + :param identifier: (str) PDB accession ID + :param filename: path to the DSSP file + :param overwrite: (boolean) + :return: (side effects) output file path + """ + + url_root = defaults.dssp_fetch + url_endpoint = "{}.dssp".format(identifier) + url = url_root + url_endpoint + Downloader(url=url, filename=filename, + decompress=False, overwrite=overwrite) + + +class DSSP(GenericInputs): + def read(self, filename=None, **kwargs): + filename = self._get_filename(filename) + self.table = parse_dssp_residues(filename=filename, **kwargs) + return self.table + + def download(self, identifier=None, filename=None, **kwargs): + identifier = self._get_identifier(identifier) + filename = self._get_filename(filename) + return download_dssp(identifier=identifier, filename=filename, **kwargs) + + def select(self, identifier=None, **kwargs): + identifier = self._get_identifier(identifier) + self.table = select_dssp(identifier=identifier, **kwargs) + return self.table + + +DSSP = DSSP() diff --git a/proteofav/library.py b/proteofav/library.py index be1806e..56dc549 100644 --- a/proteofav/library.py +++ b/proteofav/library.py @@ -1,4 +1,3 @@ -#!/usr/bin/env python # -*- coding: utf-8 -*- __all__ = ["single_letter_aa", "three_letter_aa", "scop_3to1", "to_single_aa", @@ -202,6 +201,75 @@ to_single_aa = dict(zip(three_letter_aa, single_letter_aa)) +# Asx B Aspartic acid or Asparagine +# Glx Z Glutamic acid or Glutamine +# Xaa X Any amino acid +# Xle J Leucine or Isoleucine +aa_codes_1to3_extended = { + 'A': 'ALA', 'C': 'CYS', 'D': 'ASP', + 'E': 'GLU', 'F': 'PHE', 'G': 'GLY', + 'H': 'HIS', 'K': 'LYS', 'I': 'ILE', + 'L': 'LEU', 'M': 'MET', 'N': 'ASN', + 'P': 'PRO', 'Q': 'GLN', 'R': 'ARG', + 'S': 'SER', 'T': 'THR', 'V': 'VAL', + 'Y': 'TYR', 'W': 'TRP', + 'X': 'LNT', 'B': 'ASX', 'Z': 'GLX', + 'J': 'XLE', 'U': 'SEC', 'O': 'PYL', + '-': '---', +} + +aa_default_atoms = { + 'ALA': ['N', 'O', 'CA', 'C', 'CB'], + 'CYS': ['N', 'O', 'CA', 'C', 'SG', 'CB'], + 'ASP': ['N', 'O', 'CA', 'C', 'CG', 'OD2', 'OD1', 'CB'], + 'GLU': ['N', 'O', 'CA', 'C', 'CD', 'CG', 'OE1', 'CB', 'OE2'], + 'PHE': ['N', 'O', 'CA', 'C', 'CE1', 'CD1', 'CZ', 'CG', 'CB', 'CE2', 'CD2'], + 'GLY': ['N', 'O', 'CA', 'C'], + 'HIS': ['N', 'O', 'CA', 'C', 'CB', 'CG', 'ND1', 'CD2', 'CE1', 'NE2'], + 'LYS': ['N', 'O', 'CA', 'C', 'NZ', 'CD', 'CE', 'CG', 'CB'], + 'ILE': ['N', 'O', 'CA', 'C', 'CG2', 'CD1', 'CB', 'CG1'], + 'LEU': ['N', 'O', 'CA', 'C', 'CD2', 'CD1', 'CG', 'CB'], + 'MET': ['N', 'O', 'CA', 'C', 'SD', 'CG', 'CB', 'CE'], + 'ASN': ['N', 'O', 'CA', 'C', 'ND2', 'OD1', 'CB', 'CG'], + 'PRO': ['N', 'O', 'CA', 'C', 'CD', 'CG', 'CB'], + 'GLN': ['N', 'O', 'CA', 'C', 'CD', 'NE2', 'OE1', 'CB', 'CG'], + 'ARG': ['N', 'O', 'CA', 'C', 'CZ', 'CD', 'NE', 'CG', 'CB'], + 'SER': ['N', 'O', 'CA', 'C', 'CB', 'OG'], + 'THR': ['N', 'O', 'CA', 'C', 'OG1', 'CG2', 'CB'], + 'VAL': ['N', 'O', 'CA', 'C', 'CB', 'CG2', 'CG1'], + 'TYR': ['N', 'O', 'CA', 'C', 'CE1', 'CD1', 'CZ', 'CG', 'CB', 'CE2', 'CD2'], + 'TRP': ['N', 'O', 'CA', 'C', 'NE1', 'CZ3', 'CD1', 'CE3', 'CG', 'CB', 'CZ2', 'CE2', 'CD2'], +} + +# obtained from biopython at +# https://github.com/biopython/biopython/blob/master/Bio/PDB/DSSP.py +# Miller max acc: Miller et al. 1987 http://dx.doi.org/10.1016/0022-2836(87)90038-6 +# Wilke: Tien et al. 2013 http://dx.doi.org/10.1371/journal.pone.0080635 +# Sander: Sander & Rost 1994 http://dx.doi.org/10.1002/prot.340200303 +ASA_Miller = { + 'ALA': 113.0, 'ARG': 241.0, 'ASN': 158.0, 'ASP': 151.0, + 'CYS': 140.0, 'GLN': 189.0, 'GLU': 183.0, 'GLY': 85.0, + 'HIS': 194.0, 'ILE': 182.0, 'LEU': 180.0, 'LYS': 211.0, + 'MET': 204.0, 'PHE': 218.0, 'PRO': 143.0, 'SER': 122.0, + 'THR': 146.0, 'TRP': 259.0, 'TYR': 229.0, 'VAL': 160.0 +} + +ASA_Wilke = { + 'ALA': 129.0, 'ARG': 274.0, 'ASN': 195.0, 'ASP': 193.0, + 'CYS': 167.0, 'GLN': 225.0, 'GLU': 223.0, 'GLY': 104.0, + 'HIS': 224.0, 'ILE': 197.0, 'LEU': 201.0, 'LYS': 236.0, + 'MET': 224.0, 'PHE': 240.0, 'PRO': 159.0, 'SER': 155.0, + 'THR': 172.0, 'TRP': 285.0, 'TYR': 263.0, 'VAL': 174.0 +} + +ASA_Sander = { + 'ALA': 106.0, 'ARG': 248.0, 'ASN': 157.0, 'ASP': 163.0, + 'CYS': 135.0, 'GLN': 198.0, 'GLU': 194.0, 'GLY': 84.0, + 'HIS': 184.0, 'ILE': 169.0, 'LEU': 164.0, 'LYS': 205.0, + 'MET': 188.0, 'PHE': 197.0, 'PRO': 136.0, 'SER': 130.0, + 'THR': 142.0, 'TRP': 227.0, 'TYR': 222.0, 'VAL': 142.0 +} + # taken from http://www.ensembl.org/info/about/species.html # on 10.08.2015 valid_ensembl_species = ['orycteropus_afer_afer', @@ -314,3 +382,197 @@ 'rattus_norvegicus', 'saccharomyces_cerevisiae', 'tetraodon_nigroviridis'] + +_convert_dtypes = { + int: 'int64', + float: 'float64', + str: 'object' +} + +_pdbx_types = { + 'group_PDB': str, + 'id': int, + 'type_symbol': str, + 'label_atom_id': str, + 'label_alt_id': str, + 'label_comp_id': str, + 'label_asym_id': str, + 'label_entity_id': str, + 'label_seq_id': str, + 'new_asym_id': str, + 'new_seq_id': str, + 'pdbx_PDB_ins_code': str, + 'Cartn_x': float, + 'Cartn_y': float, + 'Cartn_z': float, + 'occupancy': float, + 'B_iso_or_equiv': float, + 'Cartn_x_esd': float, + 'Cartn_y_esd': float, + 'Cartn_z_esd': float, + 'occupancy_esd': float, + 'B_iso_or_equiv_esd': float, + 'pdbx_formal_charge': int, + 'auth_seq_id': str, + 'auth_comp_id': str, + 'auth_asym_id': str, + 'auth_atom_id': str, + 'pdbx_PDB_model_num': str, + 'pdbe_label_seq_id': str, + 'orig_label_asym_id': str, + 'orig_auth_asym_id': str, + 'auth_seq_id_full': str, + 'label_seq_id_full': str, + 'contact_indexes': str, +} + +_dssp_types = { + 'LINE': int, + 'RES': str, + 'RES_FULL': str, + 'CHAIN': str, + 'CHAIN_FULL': str, + 'INSCODE': str, + 'AA': str, + 'SS': str, + 'SS_CLASS': str, + 'STRUCTURE': str, + 'BP1': str, + 'BP2': str, + 'BP2_CHAIN': str, + 'ACC': int, + 'RSA': float, + 'RSA_CLASS': str, + 'NH_O_1': int, + 'NH_O_1_nrg': float, + 'O_HN_1': int, + 'O_HN_1_nrg': float, + 'NH_O_2': int, + 'NH_O_2_nrg': float, + 'O_HN_2': int, + 'O_HN_2_nrg': float, + 'TCO': float, + 'KAPPA': float, + 'ALPHA': float, + 'PHI': float, + 'PSI': float, + 'X-CA': float, + 'Y-CA': float, + 'Z-CA': float +} + +_sifts_types = { + 'PDB_regionId': int, + 'PDB_regionStart': int, + 'PDB_regionEnd': int, + 'PDB_regionResNum': str, + 'PDB_dbVersion': str, + 'PDB_dbAccessionId': str, + 'PDB_dbResNum': str, + 'PDB_dbResName': str, + 'PDB_dbChainId': str, + 'PDB_Annotation': str, + 'PDB_entityId': str, + 'PDB_codeSecondaryStructure': str, + 'PDB_nameSecondaryStructure': str, + 'UniProt_regionId': int, + 'UniProt_regionStart': int, + 'UniProt_regionEnd': int, + 'UniProt_regionResNum': str, + 'UniProt_dbVersion': str, + 'UniProt_dbAccessionId': str, + 'UniProt_dbResNum': str, + 'UniProt_dbResName': str, + 'CATH_regionId': int, + 'CATH_regionStart': int, + 'CATH_regionEnd': int, + 'CATH_regionResNum': str, + 'CATH_dbVersion': str, + 'CATH_dbAccessionId': str, + 'SCOP_regionId': int, + 'SCOP_regionStart': int, + 'SCOP_regionEnd': int, + 'SCOP_regionResNum': str, + 'SCOP_dbVersion': str, + 'SCOP_dbAccessionId': str, + 'Pfam_regionId': int, + 'Pfam_regionStart': int, + 'Pfam_regionEnd': int, + 'Pfam_regionResNum': str, + 'Pfam_dbVersion': str, + 'Pfam_dbAccessionId': str +} + +_validation_types = { + 'validation_model': int, + 'validation_ent': str, + 'validation_chain': str, + 'validation_resname': str, + 'validation_resnum': str, + 'validation_resnum_full': str, + 'validation_seq': str, + 'validation_altcode': str, + 'validation_icode': str, + 'validation_ligRSRZ': str, + 'validation_ligRSRnbrMean': str, + 'validation_ligRSRnbrStdev': str, + 'validation_ligRSRnumnbrs': str, + 'validation_avgoccu': float, + 'validation_rota': str, + 'validation_rsr': float, + 'validation_owab': float, + 'validation_rsrz': str, + 'validation_num-H-reduce': str, + 'validation_rama': str, + 'validation_said': str, + 'validation_NatomsEDS': int, + 'validation_flippable-sidechain': str, + 'validation_rscc': float, + 'validation_phi': float, + 'validation_psi': float, + 'validation_mogul-ignore': str +} + +_annotation_types = { + 'empty': str, + 'END': str, + 'FRAME': str, + 'GROUP': str, + 'ID': str, + 'NAME': str, + 'NOTE': str, + 'SCORE': str, + 'SOURCE': str, + 'START': str, + 'STRAND': str, + 'TYPE': str, + 'site': str, + 'accession': str +} + +_uni_ens_var_types = { + 'begin': int, + 'end': int, + 'polyphenScore': float, + 'siftScore': float, +} + +pdbx_types = {k: _convert_dtypes[v] for k, v in _pdbx_types.items()} +dssp_types = {k: _convert_dtypes[v] for k, v in _dssp_types.items()} +sifts_types = {k: _convert_dtypes[v] for k, v in _sifts_types.items()} +validation_types = {k: _convert_dtypes[v] for k, v in _validation_types.items()} +annotation_types = {k: _convert_dtypes[v] for k, v in _annotation_types.items()} +uni_ens_var_types = {k: _convert_dtypes[v] for k, v in _uni_ens_var_types.items()} + +# updating terms in ensembl output so that they match +# UniProt Proteins API counterparts +update_ensembl_to_uniprot = { + 'minor_allele_frequency': 'frequency', + 'start': 'begin', + 'end': 'end', + 'sift': 'siftScore', + 'polyphen': 'polyphenScore', + 'type': 'consequenceType', + 'id': 'xrefs_id' +} + diff --git a/proteofav/main.py b/proteofav/main.py index 0bf5fb0..0653567 100644 --- a/proteofav/main.py +++ b/proteofav/main.py @@ -1,195 +1,18 @@ -#!/usr/bin/env python # -*- coding: utf-8 -from __future__ import absolute_import -import logging -import sys +import sys import click +import logging -from proteofav.library import to_single_aa -from proteofav.structures import (select_cif, - select_dssp, - select_sifts, - select_validation, - sifts_best) - -from proteofav.variants import (map_gff_features_to_sequence, - select_variants) +from proteofav.mergers import Tables -__all__ = ['merge_tables', - 'parse_args', +__all__ = ['parse_args', 'main'] -log = logging.getLogger('proteofav.config') - - -def merge_tables(uniprot_id=None, - pdb_id=None, - chain=None, - atoms='CA', - model='first', - sequence_check='raise', - drop_empty_cols=False, - add_validation=False, - add_annotation=False, - add_ensembl_variants=False, - add_uniprot_variants=False): - """ - Automatically merge data tables from various resources. If no pdb_id set - sifts_best_structure, which is sorted by sequence coverage. - If no chain is set, uses the first one. - - :param bool add_ensembl_variants: Whether to add variant table from Ensembl - :param bool add_validation: whether to merge PDB validation information - :param bool add_annotation: whether to merge UniProt GFF information - :param bool drop_empty_cols: whether to drop columns without useful information - :param str sequence_check: how to handle sequence inconsistencies. Choose from raise, - warn or ignore - :param pdb_id: Entry to be loaded - :type pdb_id: str or None - :param uniprot_id: Select PDB entry with highest sequence - coverage for the selected UniProt protein sequence - :type uniprot_id: str or None - :param chain: Protein chain to loaded - :type chain: str or None - :param atoms: Atom to be selected in the - :type atoms: str or None - :param model: Select the PDB entity, like in structures determined by NMR - :type model: str or None - """ - if not any((uniprot_id, pdb_id)): - raise TypeError('One of the following arguments is expected:' - 'uniprot_id or pdb_id') - - if model != 'first': - raise NotImplementedError('Proteofav current implementation ignore alternative models.') - - if sequence_check not in ['raise', 'warn ' or 'ignore']: - sequence_check = 'raise' - - if not pdb_id: - best_pdb = sifts_best(uniprot_id, first=True) - if best_pdb is None: - logging.error('Could not process {}'.format(uniprot_id)) - return None - pdb_id = best_pdb['pdb_id'] - chain = best_pdb['chain_id'] - log.info('Best structure, chain: {}|{} for {} '.format(pdb_id, chain, uniprot_id)) - - cif_table = select_cif(pdb_id, chains=chain, models=model, atoms=atoms) - - dssp_table = select_dssp(pdb_id, chains=chain) - cif_table.loc[:, 'label_seq_id'] = cif_table.loc[:, 'label_seq_id'].astype(int) - table = cif_table.merge(dssp_table, how='left', - left_on=['auth_seq_id', 'auth_asym_id'], - right_on=['icode', 'chain_id']) - - if sequence_check == 'ignore' or atoms is None: - # sequence check not support for multiple atoms - pass - else: - # exchange lower cased aa's for for cysteines - lower_cased_aa = table['aa'].str.islower() - if lower_cased_aa.any(): - table.loc[lower_cased_aa, 'aa'] = 'C' - - mask = table['label_comp_id'].isnull() | table['aa'].isnull() - mask |= table['aa'] == 'X' - cif_seq = table['label_comp_id'].apply(to_single_aa.get, args='X') - dssp_seq = table['aa'] - - # Check if the sequences are the same - if not (dssp_seq[~mask] == cif_seq[~mask]).all(): - log_msg = '{}|{} Cif and DSSP files have different sequences.'.format(pdb_id, chain) - if sequence_check == 'raise': - raise ValueError(log_msg) - else: - log.warning(log_msg) - - sifts_table = select_sifts(pdb_id, chains=chain) - try: - sifts_table.loc[:, 'PDB_dbResNum'] = sifts_table.loc[:, 'PDB_dbResNum'].astype(int) - table = sifts_table.merge(table, how='left', - left_on=['PDB_dbResNum', 'PDB_dbChainId'], - right_on=['auth_seq_id', 'auth_asym_id']) - - except ValueError: - # PDB resnumber has a insertion code - table.pdbx_PDB_ins_code = table.pdbx_PDB_ins_code.replace('?', '') - table['index'] = table.auth_seq_id.astype(str) + table.pdbx_PDB_ins_code - table = table.merge(sifts_table, how='left', - left_on=['index', 'auth_asym_id'], - right_on=['PDB_dbResNum', 'PDB_dbChainId']) - - if sequence_check == 'ignore' or atoms is None: - pass - else: - # Update reference sequence with the new table - mask = table['auth_comp_id'].isnull() | table['PDB_dbResName'].isnull() - cif_seq = table['auth_comp_id'].apply(to_single_aa.get, args='X') - sifts_seq = table['PDB_dbResName'].apply(to_single_aa.get, args='X') - - # Check if the sequences are the same - if not (sifts_seq[~mask] == cif_seq[~mask]).all(): - log_msg = '{}|{} Cif and Sifts files have different sequences.'.format(pdb_id, chain) - if sequence_check == 'raise': - raise ValueError(log_msg) - else: - log.warning(log_msg) - - if add_validation: - validation_table = select_validation(pdb_id, chains=chain) - validation_table.loc[:, 'validation_resnum'] = validation_table.loc[:, - 'validation_resnum'].astype(int) - table = table.merge(table, how='left', - left_on=['PDB_dbResNum', 'PDB_dbChainId'], - right_on=['validation_resnum', 'validation_chain']) - - variant_features = [] - if add_ensembl_variants: - variant_features.extend(['ensembl_somatic', 'ensembl_germline']) - if add_uniprot_variants: - variant_features.append(['uniprot']) - if variant_features: - for identifier in table['UniProt_dbAccessionId'].dropna().unique(): - variants_table = select_variants(identifier, features=variant_features) - variants_table.reset_index(inplace=True) - variants_table['UniProt_dbAccessionId'] = identifier - variants_table.rename(columns={'start': 'UniProt_dbResNum'}, inplace=True) - table = table.merge(variants_table, - how='left', - on=['UniProt_dbResNum', 'UniProt_dbAccessionId']) - - if add_annotation: - for identifier in table['UniProt_dbAccessionId'].dropna().unique(): - uniprot_annotation = map_gff_features_to_sequence(identifier) - uniprot_annotation.reset_index(inplace=True) - uniprot_annotation['UniProt_dbAccessionId'] = identifier - uniprot_annotation.rename(columns={'index': 'UniProt_dbResNum'}, inplace=True) - table = table.merge(uniprot_annotation, - how='left', - on=['UniProt_dbAccessionId', 'UniProt_dbResNum']) - - # non-positional information goes to an attribute - if drop_empty_cols: - for col in table: - try: - value = table[col].dropna().unique() - except TypeError: - # break for list-like columns - continue - - if value.shape[0] == 1: - if value[0] == '?': - # if the only value is a `?` we don't need to keep - continue - del table[col] - setattr(table, col, value) - log.info('Column {} is now an attribute.'.format(col)) - return table +log = logging.getLogger('proteofav.config') -@click.command() +@click.command(context_settings={'help_option_names': ['-h', '--help']}) @click.option('--pdb', type=str, default=None, help='Protein data bank identifier.') @click.option('--chain', type=str, default=None, help='Protein structure chain identifier.') @click.option('--uniprot', type=str, default=None, help='UniProt KnowledgeBase accession.') @@ -199,17 +22,19 @@ def merge_tables(uniprot_id=None, @click.option('-v', '--verbose', is_flag=True, help="Show more verbose logging.") @click.option('-l', '--log', default=sys.stderr, help="Path to the logfile.", type=click.File('wb')) -@click.option('--add_annotation', is_flag=True, - help="Whether to merge annotation information to the output.") +@click.option('--add_dssp', is_flag=True, + help="Whether to merge DSSP information to the output.") +@click.option('--add_annotations', is_flag=True, + help="Whether to merge annotations information to the output.") @click.option('--add_validation', is_flag=True, help="Whether to merge protein structure validation information to the output.") @click.option('--add_variants', is_flag=True, help="Whether to merge genetic variant information to the output.") -@click.option('--remove_redundant', is_flag=True, - help="Whether to remove columns with redundant information from the output.") +# @click.option('--remove_redundant', is_flag=True, +# help="Whether to remove columns with redundant information from the output.") @click.argument('output', type=click.File('wb')) -def main(pdb, chain, uniprot, output_type, verbose, log, add_annotation, add_validation, - add_variants, remove_redundant, output): +def main(pdb, chain, uniprot, output_type, verbose, log, add_dssp, + add_annotations, add_validation, add_variants, output): """ ProteFAV: a Python framework to process and integrate protein structure and features to genetic variants. @@ -220,13 +45,16 @@ def main(pdb, chain, uniprot, output_type, verbose, log, add_annotation, add_val logging.basicConfig(stream=log, level=level, format='%(asctime)s - %(levelname)s - %(message)s ') - table = merge_tables(pdb_id=pdb, - chain=chain, - uniprot_id=uniprot, - add_annotation=add_annotation, - add_validation=add_validation, - add_ensembl_variants=add_variants, - drop_empty_cols=remove_redundant) + table = Tables.generate(pdb_id=pdb, + uniprot_id=uniprot, + chains=chain, + sifts=True, + dssp=add_dssp, + validation=add_validation, + annotations=add_annotations, + variants=add_variants, + merge_tables=True, + sequence_check='ignore') if output_type == 'csv': table.to_csv(output) @@ -243,10 +71,10 @@ def main(pdb, chain, uniprot, output_type, verbose, log, add_annotation, add_val @click.confirmation_option() def setup(): from proteofav.config import Defaults - from os import path + import os - defaults = Defaults(path.join(path.dirname(__file__), 'config.txt')) - default_db = path.expanduser("~/Downloads/") + defaults = Defaults(os.path.join(os.path.dirname(__file__), 'config.ini')) + default_db = os.path.expanduser("~/Downloads/") items = {k: v for k, v in defaults.__dict__.items() if k.startswith('db')} for attr, value in items.items(): diff --git a/proteofav/mergers.py b/proteofav/mergers.py new file mode 100644 index 0000000..ef7d681 --- /dev/null +++ b/proteofav/mergers.py @@ -0,0 +1,629 @@ +# -*- coding: utf-8 + +import logging +import numpy as np +import pandas as pd + +from proteofav.structures import select_structures, mmCIF +from proteofav.sifts import select_sifts, sifts_best, SIFTS +from proteofav.dssp import select_dssp, DSSP +from proteofav.variants import select_variants, Variants, fetch_pdb_uniprot_mapping +from proteofav.annotation import select_annotation, Annotation +from proteofav.validation import select_validation, Validation +from proteofav.utils import merging_down_by_key +from proteofav.library import to_single_aa + +__all__ = ['mmcif_sifts_table_merger', 'mmcif_dssp_table_merger', + 'mmcif_validation_table_merger', 'sifts_annotation_table_merger', + 'sifts_variants_table_merger', 'uniprot_vars_ensembl_vars_merger', + 'merge_tables', 'table_merger', 'table_generator', 'Tables'] + +log = logging.getLogger('proteofav.config') + + +class TableMergerError(Exception): + pass + + +def mmcif_sifts_table_merger(mmcif_table, sifts_table, category='auth'): + """ + Merge the mmCIF and SIFTS Tables. + + :param mmcif_table: mmCIF pandas DataFrame + :param sifts_table: SIFTS pandas DataFrame + :param category: data category to be used as precedence in _atom_site.*_* + asym_id, seq_id and atom_id + :return: merged pandas DataFrame + """ + + # bare minimal columns needed + if ('{}_seq_id_full'.format(category) in mmcif_table and + '{}_asym_id'.format(category) in mmcif_table and + 'PDB_dbResNum' in sifts_table and 'PDB_dbChainId' in sifts_table): + + # workaround for BioUnits + if 'orig_{}_asym_id'.format(category) in mmcif_table: + table = mmcif_table.merge(sifts_table, how='left', + left_on=['{}_seq_id_full'.format(category), + 'orig_{}_asym_id'.format(category)], + right_on=['PDB_dbResNum', 'PDB_dbChainId']) + else: + table = mmcif_table.merge(sifts_table, how='left', + left_on=['{}_seq_id_full'.format(category), + '{}_asym_id'.format(category)], + right_on=['PDB_dbResNum', 'PDB_dbChainId']) + + else: + raise TableMergerError('Not possible to merge mmCIF and SIFTS table! ' + 'Some of the necessary columns are missing...') + + log.info("Merged mmCIF and SIFTS Tables...") + return table + + +def mmcif_dssp_table_merger(mmcif_table, dssp_table, category='auth'): + """ + Merge the mmCIF and DSSP Tables. + + :param mmcif_table: mmCIF pandas DataFrame + :param dssp_table: DSSP pandas DataFrame + :param category: data category to be used as precedence in _atom_site.*_* + asym_id, seq_id and atom_id + :return: merged pandas DataFrame + """ + + # bare minimal columns needed + if ('{}_seq_id_full'.format(category) in mmcif_table and + '{}_asym_id'.format(category) in mmcif_table and + 'RES_FULL' in dssp_table and 'CHAIN_FULL' in dssp_table): + + # workaround for BioUnits + if ('orig_{}_asym_id'.format(category) in mmcif_table and not + (set(mmcif_table['{}_asym_id'.format(category)].unique()) == + set(dssp_table['CHAIN_FULL'].unique()))): + table = mmcif_table.merge(dssp_table, how='left', + left_on=['{}_seq_id_full'.format(category), + 'orig_{}_asym_id'.format(category)], + right_on=['RES_FULL', 'CHAIN_FULL']) + else: + table = mmcif_table.merge(dssp_table, how='left', + left_on=['{}_seq_id_full'.format(category), + '{}_asym_id'.format(category)], + right_on=['RES_FULL', 'CHAIN_FULL']) + + else: + raise TableMergerError('Not possible to merge mmCIF and DSSP table! ' + 'Some of the necessary columns are missing...') + + log.info("Merged mmCIF and DSSP Tables...") + return table + + +def mmcif_validation_table_merger(mmcif_table, validation_table, category='auth'): + """ + Merge the mmCIF/PDB and Validation Tables. + + :param mmcif_table: mmCIF pandas DataFrame + :param validation_table: Validation pandas DataFrame + :param category: data category to be used as precedence in _atom_site.*_* + asym_id, seq_id and atom_id + :return: merged pandas DataFrame + """ + + # bare minimal columns needed + if ('{}_seq_id_full'.format(category) in mmcif_table and + '{}_asym_id'.format(category) in mmcif_table and + 'validation_resnum_full' in validation_table and + 'validation_chain' in validation_table): + + # workaround for BioUnits + if 'orig_{}_asym_id'.format(category) in mmcif_table: + table = mmcif_table.merge(validation_table, how='left', + left_on=['{}_seq_id_full'.format(category), + 'orig_{}_asym_id'.format(category)], + right_on=['validation_resnum_full', + 'validation_chain']) + else: + table = mmcif_table.merge(validation_table, how='left', + left_on=['{}_seq_id_full'.format(category), + '{}_asym_id'.format(category)], + right_on=['validation_resnum_full', + 'validation_chain']) + else: + raise TableMergerError('Not possible to merge mmCIF and Validation table! ' + 'Some of the necessary columns are missing...') + + log.info("Merged mmCIF and Validation Tables...") + return table + + +def sifts_annotation_table_merger(sifts_table, annotation_table): + """ + Merge the SIFTS and Annotation Tables (annotation needs to be aggregated + by residue - via `filter_annotation`). + + :param sifts_table: SIFTS pandas DataFrame + :param annotation_table: Annotation pandas DataFrame + :return: merged pandas DataFrame + """ + + # bare minimal columns needed + if ('UniProt_dbAccessionId' in sifts_table and 'UniProt_dbResNum' in sifts_table and + 'accession' in annotation_table and 'site' in annotation_table): + + table = sifts_table.merge(annotation_table, how='left', + left_on=['UniProt_dbAccessionId', 'UniProt_dbResNum'], + right_on=['accession', 'site']) + + else: + raise TableMergerError('Not possible to merge SIFTS and Annotation table! ' + 'Some of the necessary columns are missing...') + + log.info("Merged SIFTS and Annotation Tables...") + return table + + +def sifts_variants_table_merger(sifts_table, variants_table): + """ + Merge the mmCIF/PDB and Variants Tables. + + :param sifts_table: SIFTS pandas DataFrame + :param variants_table: Variants pandas DataFrame + :return: merged pandas DataFrame + """ + + # bare minimal columns needed + if ('UniProt_dbAccessionId' in sifts_table and 'UniProt_dbResNum' in sifts_table and + 'accession' in variants_table and 'begin' in variants_table): + variants_table['begin'] = variants_table['begin'].astype(str) + + table = sifts_table.merge(variants_table, how='left', + left_on=['UniProt_dbAccessionId', 'UniProt_dbResNum'], + right_on=['accession', 'begin']) + + else: + raise TableMergerError('Not possible to merge SIFTS and Variants table! ' + 'Some of the necessary columns are missing...') + + log.info("Merged SIFTS and Variants Tables...") + return table + + +def uniprot_vars_ensembl_vars_merger(uniprot_vars_table, ensembl_vars_table): + """ + Merges the tables provided using appropriate columns. + + :param uniprot_vars_table: UniProt Variants pandas DataFrame + :param ensembl_vars_table: Ensembl Variants pandas DataFrame + :return: merged pandas DataFrame + """ + + # bare minimal columns needed + merge_on = ['begin', 'end', 'xrefs_id', 'frequency', + 'consequenceType', 'siftScore', 'polyphenScore'] + + if (set(merge_on).issubset(uniprot_vars_table.columns) and + set(merge_on).issubset(ensembl_vars_table.columns)): + + table = uniprot_vars_table.merge(ensembl_vars_table, how='outer', + on=merge_on).reset_index(drop=True) + + table = merging_down_by_key(table, key='xrefs_id') + table.fillna(np.nan, inplace=True) + else: + raise TableMergerError('Not possible to merge UniProt and Ensembl Vars table! ' + 'Some of the necessary columns are missing...') + + log.info("Merged UniProt and Ensembl Vars tables...") + return table + + +# TODO replace by mew table_generator +def merge_tables(uniprot_id=None, + pdb_id=None, + chain=None, + atoms='CA', + model='first', + sequence_check='raise', + drop_empty_cols=False, + add_validation=False, + add_annotation=False, + add_ensembl_variants=False, + add_uniprot_variants=False): + """ + Automatically merge data Tables from various resources. If no pdb_id set + sifts_best_structure, which is sorted by sequence coverage. + If no chain is set, uses the first one. + + :param bool add_ensembl_variants: Whether to add variant table from Ensembl + :param bool add_validation: whether to merge PDB validation information + :param bool add_annotation: whether to merge UniProt GFF information + :param bool drop_empty_cols: whether to drop columns without useful information + :param str sequence_check: how to handle sequence inconsistencies. Choose from raise, + warn or ignore + :param pdb_id: Entry to be loaded + :type pdb_id: str or None + :param uniprot_id: Select PDB entry with highest sequence + coverage for the selected UniProt protein sequence + :type uniprot_id: str or None + :param chain: Protein chain to loaded + :type chain: str or None + :param atoms: Atom to be selected in the + :type atoms: str or None + :param model: Select the PDB entity, like in structures determined by NMR + :type model: str or None + """ + if not any((uniprot_id, pdb_id)): + raise TypeError('One of the following arguments is expected:' + 'uniprot_id or pdb_id') + + if model != 'first': + raise NotImplementedError('Proteofav current implementation ignore alternative models.') + + if sequence_check not in ['raise', 'warn', 'ignore']: + sequence_check = 'raise' + + if not pdb_id: + best_pdb = sifts_best(uniprot_id, first=True) + if best_pdb is None: + logging.error('Could not process {}'.format(uniprot_id)) + return None + pdb_id = best_pdb['pdb_id'] + chain = best_pdb['chain_id'] + log.info('Best structure, chain: {}|{} for {} '.format(pdb_id, chain, uniprot_id)) + + cif_table = select_structures(pdb_id, chains=chain, models=model, atoms=atoms) + + dssp_table = select_dssp(pdb_id, chains=chain) + + cif_table.loc[:, 'auth_seq_id'] = cif_table.loc[:, 'auth_seq_id'].astype(str) + dssp_table.loc[:, 'RES_FULL'] = dssp_table.loc[:, 'RES_FULL'].astype(str) + table = cif_table.merge(dssp_table, how='left', + left_on=['auth_seq_id', 'auth_asym_id'], + right_on=['RES_FULL', 'CHAIN']) + + if sequence_check == 'ignore' or atoms is None: + # sequence check not support for multiple atoms + pass + else: + # exchange lower cased aa's for for cysteines + lower_cased_aa = table['AA'].str.islower() + if lower_cased_aa.any(): + table.loc[lower_cased_aa, 'AA'] = 'C' + + mask = table['label_comp_id'].isnull() | table['AA'].isnull() + mask |= table['AA'] == 'X' + cif_seq = table['label_comp_id'].apply(to_single_aa.get, args='X') + dssp_seq = table['AA'] + + # Check if the sequences are the same + if not (dssp_seq[~mask] == cif_seq[~mask]).all(): + log_msg = '{}|{} Cif and DSSP files have different sequences.'.format(pdb_id, chain) + if sequence_check == 'raise': + raise ValueError(log_msg) + else: + log.warning(log_msg) + + sifts_table = select_sifts(pdb_id, chains=chain) + try: + sifts_table.loc[:, 'PDB_dbResNum'] = sifts_table.loc[:, 'PDB_dbResNum'].astype(str) + table = sifts_table.merge(table, how='left', + left_on=['PDB_dbResNum', 'PDB_dbChainId'], + right_on=['auth_seq_id', 'auth_asym_id']) + + except ValueError: + # PDB resnumber has a insertion code + table.pdbx_PDB_ins_code = table.pdbx_PDB_ins_code.replace('?', '') + table['index'] = table.auth_seq_id.astype(str) + table.pdbx_PDB_ins_code + table = table.merge(sifts_table, how='left', + left_on=['index', 'auth_asym_id'], + right_on=['PDB_dbResNum', 'PDB_dbChainId']) + + if sequence_check == 'ignore' or atoms is None: + pass + else: + # Update reference sequence with the new table + mask = table['auth_comp_id'].isnull() | table['PDB_dbResName'].isnull() + cif_seq = table['auth_comp_id'].apply(to_single_aa.get, args='X') + sifts_seq = table['PDB_dbResName'].apply(to_single_aa.get, args='X') + + # Check if the sequences are the same + if not (sifts_seq[~mask] == cif_seq[~mask]).all(): + log_msg = '{}|{} Cif and Sifts files have different sequences.'.format(pdb_id, chain) + if sequence_check == 'raise': + raise ValueError(log_msg) + else: + log.warning(log_msg) + + if add_validation: + validation_table = select_validation(pdb_id, chains=chain) + validation_table.loc[:, 'validation_resnum'] = validation_table.loc[:, + 'validation_resnum'].astype(int) + table = table.merge(table, how='left', + left_on=['PDB_dbResNum', 'PDB_dbChainId'], + right_on=['validation_resnum', 'validation_chain']) + + if add_uniprot_variants or add_ensembl_variants: + for identifier in table['UniProt_dbAccessionId'].dropna().unique(): + uniprot_vars, ensembl_vars = select_variants(identifier, + uniprot_vars=add_uniprot_variants, + ensembl_germline_vars=add_ensembl_variants, + ensembl_somatic_vars=add_ensembl_variants) + + if isinstance(uniprot_vars, pd.DataFrame) and isinstance(ensembl_vars, pd.DataFrame): + variants_table = uniprot_vars_ensembl_vars_merger(uniprot_vars, ensembl_vars) + elif isinstance(uniprot_vars, pd.DataFrame): + variants_table = uniprot_vars + elif isinstance(ensembl_vars, pd.DataFrame): + variants_table = ensembl_vars + else: + log.info('No variants found...') + variants_table = pd.DataFrame() + + if not variants_table.empty: + variants_table.reset_index(inplace=True) + variants_table['UniProt_dbAccessionId'] = identifier + variants_table.rename(columns={'begin': 'UniProt_dbResNum'}, inplace=True) + table = table.merge(variants_table, + how='left', + on=['UniProt_dbResNum', 'UniProt_dbAccessionId']) + + if add_annotation: + for identifier in table['UniProt_dbAccessionId'].dropna().unique(): + uniprot_annotation = select_annotation(identifier, annotation_agg=True) + uniprot_annotation.reset_index(inplace=True) + uniprot_annotation['UniProt_dbAccessionId'] = identifier + uniprot_annotation.rename(columns={'index': 'UniProt_dbResNum'}, inplace=True) + table = table.merge(uniprot_annotation, + how='left', + on=['UniProt_dbAccessionId', 'UniProt_dbResNum']) + + # non-positional information goes to an attribute + if drop_empty_cols: + for col in table: + try: + value = table[col].dropna().unique() + except TypeError: + # break for list-like columns + continue + + if value.shape[0] == 1: + if value[0] == '?': + # if the only value is a `?` we don't need to keep + continue + del table[col] + setattr(table, col, value) + log.info('Column {} is now an attribute.'.format(col)) + return table + + +def table_merger(mmcif_table=None, dssp_table=None, sifts_table=None, + validation_table=None, annotation_table=None, + variants_table=None): + """ + Merges the Tables provided using appropriate columns. + + :param mmcif_table: (optional) mmCIF pandas DataFrame + :param dssp_table: (optional) DSSP pandas DataFrame + :param sifts_table: (optional) SIFTS pandas DataFrame + :param validation_table: (optional) Validation pandas DataFrame + :param annotation_table: (optional) Annotation pandas DataFrame + :param variants_table: (optional) Variants pandas DataFrame + :return: merged pandas DataFrame + """ + + available = [mmcif_table, dssp_table, sifts_table, + validation_table, annotation_table, variants_table] + available = [k for k in available if k is not None] + if len(available) < 2 and (mmcif_table or sifts_table): + raise TableMergerError( + "At least two Tables are needed in order to merge...") + + table = None + if mmcif_table is not None: + if dssp_table is not None: + mmcif_table = mmcif_dssp_table_merger(mmcif_table, dssp_table) + if validation_table is not None: + mmcif_table = mmcif_validation_table_merger(mmcif_table, + validation_table) + table = mmcif_table + + if sifts_table is not None: + if annotation_table is not None: + sifts_table = sifts_annotation_table_merger(sifts_table, + annotation_table) + if variants_table is not None: + sifts_table = sifts_variants_table_merger(sifts_table, + variants_table) + table = sifts_table + + if mmcif_table is not None and sifts_table is not None: + table = mmcif_sifts_table_merger(mmcif_table, sifts_table) + + return table + + +def table_generator(uniprot_id=None, pdb_id=None, bio_unit=False, + sifts=True, dssp=False, validation=False, annotations=False, variants=False, + chains=None, res=None, sites=None, atoms=None, lines=None, + residue_agg=False, overwrite=False): + """ + Simplifies the process of generating Tables and merging them. + + Automatically merge data Tables from various resources. If no pdb_id set + `sifts_best`, which is sorted by sequence coverage. If no chain is set, uses all. + + :param uniprot_id: (str) UniProt ID + :param pdb_id: (str) PDB ID + :param bio_unit: boolean for using AsymUnits or BioUnits + :param sifts: boolean + :param dssp: boolean + :param validation: boolean + :param annotations: boolean + :param variants: boolean + :param chains: (tuple) Chain ID ('*_asym_id') + :param res: (tuple) PDB ResNum ('*_seq_id_full') + :param sites: (tuple) UniProt ResNum (positional index) + :param atoms: (tuple) atom IDs or None + :param lines: 'ATOM' or 'HETATM' or None (both) + :param residue_agg: boolean + :param overwrite: boolean + :returns: mmcif, sifts, dssp, variants and annotations Tables + """ + + # generates the Tables for the uniprot_id, pdb_id + # chains, res, sites are only processed after + if uniprot_id or pdb_id: + # get pdb_id if only uniprot_id is provided + if uniprot_id and not pdb_id: + # fetch the best structures from the PDBe API + data = sifts_best(uniprot_id)[uniprot_id] + if data is not None: + # uses the first structure + pdb_id = data[0]['pdb_id'] + chains = (data[0]['chain_id'],) + else: + log.info("Best structures not available from the PDBe API for %s", + uniprot_id) + raise TableMergerError('Nothing to merge...') + + # mmCIF table + mmcif_table = mmCIF.select(identifier=pdb_id, bio_unit=bio_unit, + bio_unit_preferred=True, overwrite=overwrite, + add_atom_altloc=True, add_res_full=True, + category='auth', residue_agg=residue_agg, + chains=chains, res_full=res, atoms=atoms, lines=lines) + + # SIFTS table + if sifts: + sifts_table = SIFTS.select(identifier=pdb_id, add_regions=True, add_dbs=False, + chains=chains, res=res, uniprot=uniprot_id, site=sites) + else: + sifts_table = None + + # DSSP table + if dssp: + dssp_table = DSSP.select(identifier=pdb_id, + add_ss_reduced=True, add_rsa_class=True, + chains_full=chains, res=res) + else: + dssp_table = None + + # Validation table + if validation: + validation_table = Validation.select(identifier=pdb_id) + else: + validation_table = None + + # Annotations table + if annotations: + if uniprot_id: + annotations_table = Annotation.select(identifier=uniprot_id, + annotation_agg=True) + else: + annotations_table = None + annot_tables = [] + data = fetch_pdb_uniprot_mapping(identifier=pdb_id).json()[pdb_id]['UniProt'] + for uniprot_id in data: + annot_tables.append(Annotation.select(identifier=uniprot_id, + annotation_agg=True)) + if len(annot_tables) > 1: + annotations_table = pd.concat(annot_tables).reset_index(drop=True) + elif len(annot_tables): + annotations_table = annot_tables[0] + else: + annotations_table = None + + # Variants table + if variants: + if uniprot_id: + uni_vars, ens_vars = Variants.select(identifier=uniprot_id, + id_source='uniprot', + synonymous=True, + uniprot_vars=True, + ensembl_germline_vars=True, + ensembl_somatic_vars=True) + variants_table = uniprot_vars_ensembl_vars_merger(uni_vars, ens_vars) + else: + variants_table = None + vars_tables = [] + data = fetch_pdb_uniprot_mapping(identifier=pdb_id).json()[pdb_id]['UniProt'] + for uniprot_id in data: + uni_vars, ens_vars = Variants.select(identifier=uniprot_id, + id_source='uniprot', + synonymous=True, + uniprot_vars=True, + ensembl_germline_vars=True, + ensembl_somatic_vars=True) + vars_tables.append(uniprot_vars_ensembl_vars_merger(uni_vars, ens_vars)) + if len(vars_tables) > 1: + variants_table = pd.concat(vars_tables).reset_index(drop=True) + elif len(vars_tables): + variants_table = vars_tables[0] + else: + variants_table = None + + return (mmcif_table, dssp_table, sifts_table, + validation_table, annotations_table, variants_table) + + else: + raise ValueError('No UniProt ID or PDB ID provided...') + + +class Tables(object): + def __init__(self): + self.mmcif = None + self.sifts = None + self.dssp = None + self.validation = None + self.annotation = None + self.variants = None + self.table = None + + def merge(self, mmcif=None, dssp=None, sifts=None, + validation=None, annotation=None, variants=None): + """Merges the provided Tables and stores""" + + if mmcif is not None: + self.mmcif = mmcif + if dssp is not None: + self.dssp = dssp + if sifts is not None: + self.sifts = sifts + if validation is not None: + self.validation = validation + if annotation is not None: + self.annotation = annotation + if variants is not None: + self.variants = variants + self.table = table_merger(self.mmcif, self.dssp, self.sifts, + self.validation, self.annotation, self.variants) + return self.table + + def generate(self, merge_tables=False, sequence_check='ignore', **kwargs): + """Generates the Tables, merges and stores + + :param merge_tables: (bool) merge the Tables after generating them + :param str sequence_check: how to handle sequence inconsistencies. + Choose from 'raise', 'warn' or 'ignore' + """ + self.mmcif, self.dssp, self.sifts, self.validation, self.annotation, self.variants = \ + table_generator(**kwargs) + if not merge_tables: + return (self.mmcif, self.dssp, self.sifts, + self.validation, self.annotation, self.variants) + else: + table = table_merger(self.mmcif, self.dssp, self.sifts, + self.validation, self.annotation, self.variants) + + if sequence_check == 'raise' or sequence_check == 'warn': + # TODO + pass + elif sequence_check != 'ignore': + raise ValueError("Sequence check method '{}' not implemented." + "".format(sequence_check)) + + return table + + +Tables = Tables() diff --git a/proteofav/sifts.py b/proteofav/sifts.py new file mode 100644 index 0000000..6f4d6eb --- /dev/null +++ b/proteofav/sifts.py @@ -0,0 +1,475 @@ +# -*- coding: utf-8 -*- + +import os +import logging +import pandas as pd +from lxml import etree +from collections import OrderedDict + +from proteofav.variants import fetch_uniprot_pdb_mapping +from proteofav.utils import (row_selector, InputFileHandler, Downloader, + GenericInputs, constrain_column_types, exclude_columns) +from proteofav.library import sifts_types + +from proteofav.config import defaults + +log = logging.getLogger('proteofav.config') + +__all__ = ['parse_sifts_residues', 'select_sifts', 'sifts_best', + 'download_sifts', 'SIFTS'] + + +def _parse_sifts_dbs_from_file(filename, excluded_cols=None): + """ + Parses the residue fields of a SIFTS XML file. + + :param filename: path to the SIFTS file + :param excluded_cols: option to exclude SIFTS dbSources + :return: returns a nested dictionary + """ + + log.info("Parsing SIFTS dbs from lines...") + + InputFileHandler(filename) + + # excluding columns + if excluded_cols is None: + excluded_cols = ("InterPro", "GO", "EC", "NCBI") + + # parsing sifts segments + try: + tree = etree.parse(filename) + except etree.XMLSyntaxError: + raise IOError("{} not available or could not be read...".format(filename)) + root = tree.getroot() + namespace = root.nsmap[None] + namespace_map = {'ns': namespace} + + # DB entries and versions + sifts_object = OrderedDict() + for db_list in root.iterfind('.//ns:listDB', namespaces=namespace_map): + for db in db_list: + source = '' + db_entries = OrderedDict() + for k, v in db.attrib.items(): + db_entries[k] = v + if k == 'dbSource' and v not in excluded_cols: + source = v + if source not in excluded_cols and source != '': + sifts_object[source] = db_entries + + return sifts_object + + +def _parse_sifts_regions_from_file(filename, excluded_cols=None): + """ + Parses the residue fields of a SIFTS XML file. + + :param filename: path to the SIFTS file + :param excluded_cols: option to exclude SIFTS dbSources + :return: returns a nested dictionary + """ + + log.info("Parsing SIFTS regions from lines...") + + InputFileHandler(filename) + + # excluding columns + if excluded_cols is None: + excluded_cols = ("InterPro", "GO", "EC", "NCBI") + + # parsing sifts segments + try: + tree = etree.parse(filename) + except etree.XMLSyntaxError: + raise IOError("{} not available or could not be read...".format(filename)) + root = tree.getroot() + namespace = root.nsmap[None] + namespace_map = {'ns': namespace} + db_reference = "{{{}}}db".format(namespace) + + sifts_object = OrderedDict() + + # Entities + for entity_list in root.iterfind('.//ns:entity[@type="protein"]', + namespaces=namespace_map): + entity_id = entity_list.attrib['entityId'] + regions_full = OrderedDict() + # Entities : Segments + for segment in entity_list: + + # parse the regions found for this segment + # Entities : Segments : Regions + for region_list in segment.iterfind('.//ns:listMapRegion', + namespaces=namespace_map): + for region in region_list: + # get region annotations + # parse extra annotations for each region + for annotation in region: + for k, v in annotation.attrib.items(): + # db entries + if annotation.tag == db_reference: + if k == 'dbSource' and v not in excluded_cols: + source = v + else: + continue + if source not in regions_full: + counter = 1 + region_object = OrderedDict() + else: + region_object = regions_full[source] + keys = regions_full[source] + last_counter = [int(k) for k in keys][-1] + counter = last_counter + 1 + try: + coord = annotation.attrib['dbCoordSys'] + except KeyError: + coord = '-' + region_annotation = OrderedDict() + region_annotation['dbAccessionId'] = annotation.attrib['dbAccessionId'] + region_annotation['start'] = int(region.attrib['start']) + region_annotation['end'] = int(region.attrib['end']) + region_annotation['dbCoordSys'] = coord + region_object["{}".format(counter)] = region_annotation + regions_full[source] = region_object + + sifts_object[entity_id] = regions_full + + return sifts_object + + +def parse_sifts_residues(filename, add_regions=True, add_dbs=False, + excluded_cols=None): + """ + Parses the residue fields of a SIFTS XML file. + + :param filename: path to the SIFTS file + :param add_regions: boolean + :param add_dbs: boolean + :param excluded_cols: list of columns to be excluded + :return: returns a pandas DataFrame + """ + + log.info("Parsing SIFTS residues from lines...") + + # example lines with some problems + """ + + + + + + Copyright notice: (c) 2004-2013, EMBL-EBI, PDBe-UniProt + Jose M. Dana, Paul Gane, Jie Luo, Glen van Ginkel, Claire O'Donovan, Maria J. Martin, Sameer Velankar. + The information included is supplied as-is, under the terms and conditions of the licence agreement. + + + + + + + + + + + + + + + + + + + + + + + + + + + + + T + loop + + (...) + """ + + InputFileHandler(filename) + + # excluding columns + if excluded_cols is None: + excluded_cols = ("InterPro", "GO", "EC", "NCBI") + + # parse regions first + if add_regions: + regions = _parse_sifts_regions_from_file(filename=filename, + excluded_cols=excluded_cols) + if add_dbs: + dbs = _parse_sifts_dbs_from_file(filename=filename, + excluded_cols=excluded_cols) + + # parsing sifts segments + try: + tree = etree.parse(filename) + except etree.XMLSyntaxError: + raise IOError("{} not available or could not be read...".format(filename)) + root = tree.getroot() + namespace = root.nsmap[None] + namespace_map = {'ns': namespace} + cross_reference = "{{{}}}crossRefDb".format(namespace) + residue_detail = "{{{}}}residueDetail".format(namespace) + + rows = [] + # Entities + for entity_list in root.iterfind('.//ns:entity[@type="protein"]', + namespaces=namespace_map): + + entity_id = entity_list.attrib['entityId'] + # Entities : Segments + for segment in entity_list: + + # Entities : Segments : Residues + for list_residue in segment.iterfind('.//ns:listResidue', + namespaces=namespace_map): + for residue in list_residue: + # get residue annotations + residue_annotation = OrderedDict() + # key, value pairs + for k, v in residue.attrib.items(): + # skipping dbSource + if k == 'dbResNum': + # adding to the dictionary + # residue_annotation[k] = v + resnum = int(v) + else: + continue + + # parse extra annotations for each residue + for annotation in residue: + for k, v in annotation.attrib.items(): + # crossRefDb entries + if annotation.tag == cross_reference: + if annotation.attrib["dbSource"] not in excluded_cols: + # skipping various fields + if k == 'dbSource' or k == 'dbCoordSys': + continue + elif (annotation.attrib["dbSource"] != "PDB" and + annotation.attrib["dbSource"] != "UniProt"): + if k == 'dbResName' or k == 'dbResNum' or k == 'dbChainId': + continue + # elif annotation.attrib["dbSource"] == "PDB" and k == "dbAccessionId": + # continue + + # adding a new column with the regionId from the 'regions' + if add_regions: + if k == "dbAccessionId": + source = annotation.attrib["dbSource"] + if source in regions[entity_id]: + keys = regions[entity_id][source] + for key in [k for k in keys]: + entry = regions[entity_id][source][key] + if v == entry["dbAccessionId"]: + start = int(entry["start"]) + end = int(entry["end"]) + if resnum in range(start, end + 1, 1): + nk = "{}_regionId".format(source) + residue_annotation[nk] = key + nk = "{}_regionStart".format(source) + residue_annotation[nk] = start + nk = "{}_regionEnd".format(source) + residue_annotation[nk] = end + nk = "{}_regionResNum".format(source) + residue_annotation[nk] = resnum + + if add_dbs: + source = annotation.attrib["dbSource"] + if source in dbs: + nk = "{}_dbVersion".format(source) + residue_annotation[nk] = dbs[source]['dbVersion'] + + # renaming all keys with dbSource prefix + k = "{}_{}".format( + annotation.attrib["dbSource"], k) + if k == "{}_1".format(annotation.attrib["dbSource"]): + continue + + if annotation.tag == residue_detail: + if 'PDB' not in excluded_cols: + k = "PDB_{}".format(annotation.attrib["property"]) + # value is the text field in the XML + v = annotation.text + + # adding to the dictionary + if "_" in k: + try: + if v in residue_annotation[k]: + continue + if k != "PDB_Annotation": + residue_annotation[k].append(v) + else: + residue_annotation[k] = v + except KeyError: + residue_annotation[k] = v + except AttributeError: + residue_annotation[k] = [residue_annotation[k]] + residue_annotation[k].append(v) + except TypeError: + # bool column for annotation + residue_annotation[k] = v + if 'PDB' not in excluded_cols and "PDB_Annotation" not in residue_annotation: + residue_annotation["PDB_Annotation"] = "Observed" + + # adding the entity_id + if 'PDB_entityId' not in residue_annotation: + residue_annotation['PDB_entityId'] = entity_id + + rows.append(residue_annotation) + + table = pd.DataFrame(rows) + + # # enforce some specific column types + # table = constrain_column_types(table, sifts_types) + + for c in list(table): + if '_regionId' in c: + table[c] = table[c].fillna('-').astype(str) + elif '_regionStart' in c or '_regionEnd' in c: + table[c] = table[c].fillna(0).astype(int) + + # excluding columns + table = exclude_columns(table, excluded=excluded_cols) + + # enforce some specific column types + table = constrain_column_types(table, col_type_dict=sifts_types) + + if table.empty: + log.error('SIFTS file {} resulted in a empty Dataframe'.format(filename)) + raise ValueError('SIFTS file {} resulted in a empty Dataframe'.format( + filename)) + return table + + +def select_sifts(identifier, excluded_cols=None, add_regions=True, add_dbs=False, + overwrite=False, **kwargs): + """ + Produce table ready from SIFTS XML file. + + :param identifier: PDB/mmCIF accession ID + :param excluded_cols: option to exclude mmCIF columns + :param add_regions: boolean + :param add_dbs: boolean + :param overwrite: boolean + :return: returns a pandas DataFrame + """ + + filename = os.path.join(defaults.db_sifts, "{}.xml".format(identifier)) + + download_sifts(identifier=identifier, filename=filename, overwrite=overwrite) + + table = parse_sifts_residues(filename=filename, excluded_cols=excluded_cols, + add_regions=add_regions, add_dbs=add_dbs) + + table = filter_sifts(table, **kwargs) + table = constrain_column_types(table, col_type_dict=sifts_types) + return table + + +def filter_sifts(table, excluded_cols=None, chains=None, + chain_auth=None, res=None, uniprot=None, site=None): + """ + Parses the residue fields of a SIFTS XML file. + + :param table: pandas DataFrame object + :param excluded_cols: option to exclude SIFTS dbSources + :param chains: (tuple) chain IDs or None + :param chain_auth: (tuple) chain IDs or None + :param res: (tuple) res IDs or None + :param uniprot: (tuple) UniProt IDs or None + :param site: (tuple) UniProt (positional) sites or None + :return: returns a pandas DataFrame + """ + + # selections / filtering + # excluding columns + table = exclude_columns(table, excluded=excluded_cols) + + # excluding rows + if chains is not None: + table = row_selector(table, 'PDB_entityId', chains) + log.info("SIFTS table filtered by PDB_entityId...") + + if chain_auth is not None: + table = row_selector(table, 'PDB_dbChainId', chain_auth) + log.info("SIFTS table filtered by PDB_dbChainId...") + + if res is not None: + table = row_selector(table, 'PDB_dbResNum', res) + log.info("SIFTS table filtered by PDB_dbResNum...") + + if uniprot is not None: + table = row_selector(table, 'UniProt_dbAccessionId', uniprot) + log.info("SIFTS table filtered by UniProt_dbAccessionId...") + + if site is not None: + table = row_selector(table, 'UniProt_dbResNum', site) + log.info("SIFTS table filtered by UniProt_dbResNum...") + log.info("DSSP reset residue number...") + + if table.empty: + raise ValueError("The filters resulted in an empty DataFrame...") + return table + + +def download_sifts(identifier=None, filename=None, overwrite=False): + """ + Downloads a SIFTS xml from the EBI FTP to the filesystem. + + :param identifier: (str) PDB accession ID + :param filename: path to the SIFTS file + :param overwrite: (boolean) + :return: (side effects) output file path + """ + + url_root = defaults.sifts_fetch + url_endpoint = "{}.xml.gz".format(identifier) + url = url_root + url_endpoint + Downloader(url=url, filename=filename, + decompress=True, overwrite=overwrite) + + +def sifts_best(identifier, first=False): + """ + Retrieves the best structures from the SIFTS endpoint in the PDBe API. + + :param identifier: UniProt accession ID + :param first: gets the first entry + :return: url content or url content in JSON data structure. + """ + response = fetch_uniprot_pdb_mapping(identifier=identifier) + if not response.ok or response is None: + log.error('No SIFTS mapping found for {}'.format(identifier)) + return None + return response.json() if not first else response.json()[identifier][0] + + +class SIFTS(GenericInputs): + def read(self, filename=None, **kwargs): + filename = self._get_filename(filename) + self.table = parse_sifts_residues(filename=filename, **kwargs) + return self.table + + def download(self, identifier=None, filename=None, **kwargs): + identifier = self._get_identifier(identifier) + filename = self._get_filename(filename) + return download_sifts(identifier=identifier, filename=filename, **kwargs) + + def select(self, identifier=None, add_regions=True, add_dbs=False, **kwargs): + identifier = self._get_identifier(identifier) + self.table = select_sifts(identifier=identifier, add_regions=add_regions, + add_dbs=add_dbs, **kwargs) + return self.table + + +SIFTS = SIFTS() diff --git a/proteofav/structures.py b/proteofav/structures.py index 4250818..5e0a8df 100644 --- a/proteofav/structures.py +++ b/proteofav/structures.py @@ -1,4 +1,3 @@ -#!/usr/bin/env python # -*- coding: utf-8 -*- """ @@ -7,61 +6,39 @@ the information. Prefers the use o the wrapper instead the private functions for better error handling. Both levels are covered by test cases. """ -from __future__ import absolute_import + +import os import logging +import pandas as pd +from string import ascii_uppercase + try: # python 2.7 from StringIO import StringIO except ImportError: from io import StringIO -from os import path - -import pandas as pd -from lxml import etree -from requests import HTTPError -from scipy.spatial import cKDTree from proteofav.config import defaults -from proteofav.library import scop_3to1 -from proteofav.utils import fetch_files, get_url_or_retry, get_preferred_assembly_id +from proteofav.utils import (fetch_from_url_or_retry, row_selector, + InputFileHandler, OutputFileHandler, GenericInputs, + constrain_column_types, exclude_columns, Downloader) +from proteofav.library import pdbx_types, aa_default_atoms log = logging.getLogger('proteofav.config') -__all__ = ['_dssp', '_mmcif_atom', '_sifts_residues_regions', '_pdb_validation_to_table', - '_rcsb_description', '_get_contacts_from_table', '_table_selector', - # '_residues_as_centroid', '_import_dssp_chains_ids', - 'select_cif', 'select_dssp', 'select_sifts', 'select_validation', 'sifts_best'] + +__all__ = ['parse_mmcif_atoms', 'residues_aggregation', + 'fetch_summary_properties_pdbe', 'get_preferred_assembly_id', + 'filter_structures', 'select_structures', 'write_mmcif_from_table', 'write_pdb_from_table', + 'read_structures', 'download_structures', 'write_structures', 'PDB', 'mmCIF'] UNIFIED_COL = ['pdbx_PDB_model_num', 'auth_asym_id', 'auth_seq_id'] +PDB_FORMAT = "%s%5i %-4s%c%3s %c%4s%c %8.3f%8.3f%8.3f%s%6.2f %4s%2s%2s\n" + ############################################################################## # Private methods ############################################################################## -def _dssp(filename): - """ - Parses DSSP file output to a pandas DataFrame. - - :param filename: input SIFTS xml file - :return: pandas table dataframe - """ - # column width descriptors - cols_widths = ((0, 5), (6, 11), (11, 12), (13, 14), (16, 17), (35, 38), - (103, 109), (109, 115)) - # simplified headers for the table - dssp_header = ("dssp_index", "icode", "chain_id", "aa", "ss", "acc", "phi", "psi") - dssp_table = pd.read_fwf(filename, - skiprows=28, - names=dssp_header, - colspecs=cols_widths, - index_col=0, - compression=None) - if dssp_table.empty: - log.error('DSSP file {} resulted in a empty Dataframe'.format(filename)) - raise ValueError('DSSP file {} resulted in a empty Dataframe'.format( - filename)) - return dssp_table - - def yield_lines(filename): """ Custom function for iterating over line from filename. @@ -73,41 +50,199 @@ def yield_lines(filename): yield line -def _mmcif_atom(filename, delimiter=None): +def parse_mmcif_atoms(filename, excluded_cols=None): """ - Parse mmCIF ATOM and HETEROATOM lines to a pandas DataFrame. + Parse mmCIF ATOM and HETATM lines. - :param filename: input CIF file path - :return: pandas table dataframe + :param filename: path to the mmCIF file + :param excluded_cols: list of columns to be excluded + :return: returns a pandas DataFrame """ + + log.info("Parsing mmCIF atoms from lines...") + + # example lines with some problems + """ + _atom_site.pdbx_PDB_model_num + _atom_site.pdbe_label_seq_id + _atom_site.orig_label_asym_id + _atom_site.orig_auth_asym_id + ATOM 1 N N . VAL A 1 1 ? -7.069 21.943 18.770 1.0 56.51 ? ? ? ? ? ? 118 VAL A N 1 1 A A + ATOM 2 C CA . VAL A 1 1 ? -7.077 21.688 20.244 1.0 59.09 ? ? ? ? ? ? 118 VAL A CA 1 1 A A + ATOM 3 C C . VAL A 1 1 ? -5.756 21.077 20.700 1.0 44.63 ? ? ? ? ? ? 118 VAL A C 1 1 A A + ATOM 4 O O . VAL A 1 1 ? -5.346 20.029 20.204 1.0 59.84 ? ? ? ? ? ? 118 VAL A O 1 1 A A + """ + + InputFileHandler(filename) + # parsing atom lines - _header_mmcif = [] + header = [] lines = [] - for line in yield_lines(filename): - if line.startswith("_atom_site."): - _header_mmcif.append(line.split('.')[1].rstrip()) - elif line.startswith("ATOM") or "ATOM" in line[0:6]: - lines.append(line) - elif line.startswith("HETATM"): - lines.append(line) + with open(filename) as inlines: + for line in inlines: + if line.startswith("_atom_site."): + header.append(line.split('.')[1].rstrip()) + elif line.startswith("ATOM") or "ATOM" in line[0:6]: + lines.append(line) + elif line.startswith("HETATM"): + lines.append(line) lines = "".join(lines) - if delimiter is None: - table = pd.read_table(StringIO(lines), - delim_whitespace=True, - low_memory=False, - names=_header_mmcif, - compression=None) - else: - table = pd.read_table(StringIO(lines), - sep=str(delimiter), - low_memory=False, - names=_header_mmcif, - compression=None) - - # drop the 'esd' entries - excluded = [x for x in table.columns.values if x.endswith('_esd')] - table = table.drop(excluded, axis=1) + all_str = {key: str for key in header} + table = pd.read_table(StringIO(lines), delim_whitespace=True, low_memory=False, + names=header, compression=None, converters=all_str, + keep_default_na=False) + # excluding columns + if excluded_cols is None: + excluded_cols = ('Cartn_x_esd', 'Cartn_y_esd', 'Cartn_z_esd', + 'occupancy_esd', 'B_iso_or_equiv_esd', + 'pdbx_formal_charge') + + table = exclude_columns(table, excluded=excluded_cols) + + # enforce some specific column types + table = constrain_column_types(table, col_type_dict=pdbx_types) + + if table.empty: + log.error('mmCIF file {} resulted in a empty Dataframe'.format(filename)) + raise ValueError('mmCIF file {} resulted in a empty Dataframe'.format( + filename)) + return table + + +def parse_pdb_atoms(filename, excluded_cols=None, + fix_label_alt_id=True, fix_ins_code=True, fix_type_symbol=True): + """ + Parse PDB ATOM and HETATM lines. The ATOM lines are imported + to the dictionary names used in the mmCIF format. + + :param filename: path to the PDB file + :param excluded_cols: list of columns to be excluded + :param fix_label_alt_id: boolean + :param fix_ins_code: boolean + :param fix_type_symbol: boolean + :return: returns a pandas DataFrame + """ + + log.info("Parsing PDB atoms from lines...") + + # example lines + """ + MODEL 1 + ATOM 0 N SER A -1 104.083 78.916 -1.349 1.00 61.47 N + ATOM 1 N VAL A 118 -7.069 21.943 18.770 1.00 56.51 N + ATOM 2 CA VAL A 118 -7.077 21.688 20.244 1.00 59.09 C + ATOM 3 C VAL A 118 -5.756 21.077 20.700 1.00 44.63 C + ATOM 4 O VAL A 118 -5.346 20.029 20.204 1.00 59.84 O + """ + + InputFileHandler(filename) + + # parsing atom lines, converting it to mmcif-style headers + lines = [] + modelnumb = '1' + with open(filename) as inlines: + for line in inlines: + line = line.rstrip() + line = line[0:78] + if line.startswith("MODEL"): + modelnumb = line.split()[1] + elif line.startswith("ATOM"): + lines.append(line + "%s" % modelnumb) + elif line.startswith("HETATM"): + lines.append(line + "%s" % modelnumb) + lines = "\n".join(lines) + + header = ('group_PDB', 'id', 'label_atom_id', 'label_alt_id', 'label_comp_id', + 'label_asym_id', 'label_seq_id_full', 'label_seq_id', + 'pdbx_PDB_ins_code', 'Cartn_x', 'Cartn_y', 'Cartn_z', + 'occupancy', 'B_iso_or_equiv', 'type_symbol', 'auth_atom_id', 'auth_comp_id', + 'auth_asym_id', 'auth_seq_id_full', 'auth_seq_id', 'pdbx_PDB_model_num') + + # https://www.cgl.ucsf.edu/chimera/docs/UsersGuide/tutorials/pdbintro.html + widths = ((0, 6), (6, 11), (12, 16), (16, 17), (17, 20), (21, 22), (22, 27), (22, 26), (26, 27), + (30, 38), (38, 46), (46, 54), (54, 60), (60, 66), (76, 78), # (72, 76), ('seg_id') + (12, 16), (17, 20), (21, 22), (22, 27), (22, 26), (78, 79)) + + all_str = {key: str for key in header} + table = pd.read_fwf(StringIO(lines), names=header, colspecs=widths, + compression=None, converters=all_str, keep_default_na=False) + + # fixes the 'pdbx_PDB_ins_code' + if fix_ins_code: + table = _fix_pdb_ins_code(table) + # fixes the 'label_alt_id + if fix_label_alt_id: + table = _fix_label_alt_id(table) + # fixes 'type_symbol' if missing + if fix_type_symbol: + table = _fix_type_symbol(table) + + # excluding columns + if excluded_cols is None: + excluded_cols = ('Cartn_x_esd', 'Cartn_y_esd', 'Cartn_z_esd', + 'occupancy_esd', 'B_iso_or_equiv_esd', + 'pdbx_formal_charge') + + table = exclude_columns(table, excluded=excluded_cols) + + # enforce some specific column types + table = constrain_column_types(table, col_type_dict=pdbx_types) + + if table.empty: + log.error('PDB file {} resulted in a empty Dataframe'.format(filename)) + raise ValueError('PDB file {} resulted in a empty Dataframe'.format( + filename)) + return table + + +def _fix_pdb_ins_code(table): + """ + Utility that fixes the 'pdbx_PDB_ins_code' column to match what is expected + in the mmCIF format. + + :param table: pandas DataFrame object + :return: returns a modified pandas DataFrame + """ + + table['pdbx_PDB_ins_code'] = table['pdbx_PDB_ins_code'].str.replace('\ |', '?') + table['pdbx_PDB_ins_code'] = table['pdbx_PDB_ins_code'].fillna('?').astype(str) + return table + + +def _fix_label_alt_id(table): + """ + Utility that fixes the 'label_alt_id' column to match what is + expected in the mmCIF format. + + :param table: pandas DataFrame object + :return: returns a modified pandas DataFrame + """ + + table['label_alt_id'] = table['label_alt_id'].str.replace('\ |\?', '.') + table['label_alt_id'] = table['label_alt_id'].fillna('.').astype(str) + return table + + +def _fix_type_symbol(table): + """ + Utility that fixes the 'type_symbol' column to match what is + expected in the mmCIF format - when missing in the Structure. + + :param table: pandas DataFrame object + :return: returns a modified pandas DataFrame + """ + + def get_type_symbol(table, key, key_fix): + # this maybe a bit crude way of assigning this value + if table[key] != " " and table[key] != "" and len(table[key]): + return table[key] + else: + return ''.join([x for x in table[key_fix] if x in ascii_uppercase])[0] + + table.is_copy = False + table['type_symbol'] = table.apply(get_type_symbol, axis=1, + args=('type_symbol', 'label_atom_id')) return table @@ -176,476 +311,653 @@ def _mmcif_fields(filename, field_name='exptl.', return table -def _sifts_residues_regions(filename, cols=None, - sources=('CATH', 'SCOP', 'Pfam', 'InterPro')): - """ - Parses the residue fields of a SIFTS XML file to a pandas DataFrame. - - :param filename: input SIFTS xml file - :param cols: option to select a columns (post-parsing) - :param sources: option to select SIFTS dbSources - :return: pandas table dataframe - """ - - # parsing sifts segments - tree = etree.parse(filename) - root = tree.getroot() - namespace = root.nsmap[None] - namespace_map = {'ns': namespace} - cross_reference = "{{{}}}crossRefDb".format(namespace) - residue_detail = "{{{}}}residueDetail".format(namespace) - db_reference = "{{{}}}db".format(namespace) - # db_detail = "{{{}}}dbDetail".format(namespace) - rows = [] - - sources += ('PDB', 'UniProt') - - for segment_list in root.iterfind('.//ns:entity[@type="protein"]', - namespaces=namespace_map): - - entity_id = segment_list.attrib['entityId'] - for segment in segment_list: - # 1st parse the regions found for this segment - regions_full = {} - for region_list in segment.iterfind('.//ns:listMapRegion', - namespaces=namespace_map): - region_source = {} - for region in region_list: - # get region annotations - # parse extra annotations for each region - for annotation in region: - for k, v in annotation.attrib.items(): - # db entries - if annotation.tag == db_reference: - if k == 'dbSource' and v in sources: - source = v - else: - continue - - if source not in region_source: - region_source[source] = [] - try: - coord = annotation.attrib['dbCoordSys'] - except KeyError: - coord = '-' - region_source[source].append([annotation.attrib['dbAccessionId'], - region.attrib['start'], - region.attrib['end'], - coord]) - regions_full[entity_id] = region_source - - # 2nd parse each residue and - for list_residue in segment.iterfind('.//ns:listResidue', - namespaces=namespace_map): - for residue in list_residue: - # get residue annotations - residue_annotation = {} - # key, value pairs - for k, v in residue.attrib.items(): - # skipping dbSource - if k == 'dbSource' or k == 'dbCoordSys' or k == 'dbResName': - continue - - k = "PDB_index" - # adding to the dictionary - residue_annotation[k] = v - resnum = int(v) - - # parse extra annotations for each residue - for annotation in residue: - for k, v in annotation.attrib.items(): - # crossRefDb entries - if annotation.tag == cross_reference: - if annotation.attrib["dbSource"] in sources: - # skipping dbSource - if k == 'dbSource' or k == 'dbCoordSys': - continue - if (annotation.attrib["dbSource"] != "PDB" and - annotation.attrib["dbSource"] != "UniProt"): - if k == 'dbResName' or k == 'dbResNum' or k == 'dbChainId': - continue - if annotation.attrib["dbSource"] == "PDB" and k == "dbAccessionId": - continue - - # adding a new column with the regionId from the 'regions' - if k == "dbAccessionId": - if annotation.attrib["dbSource"] in regions_full[entity_id]: - for c, entry in enumerate(regions_full[entity_id][annotation.attrib["dbSource"]]): - if v == entry[0]: - start = int(entry[1]) - end = int(entry[2]) - if resnum in range(start, end + 1, 1): - nk = "{}_regionId".format(annotation.attrib["dbSource"]) - nv = str(c + 1) - residue_annotation[nk] = nv - - # renaming all keys with dbSource prefix - k = "{}_{}".format( - annotation.attrib["dbSource"], k) - - if annotation.tag == residue_detail: - k = "PDB_{}".format(annotation.attrib["property"]) - # value is the text field in the XML - v = annotation.text - - # adding to the dictionary - if "_" in k: - try: - if v in residue_annotation[k]: - continue - residue_annotation[k].append(v) - except KeyError: - residue_annotation[k] = v - except AttributeError: - residue_annotation[k] = [residue_annotation[k]] - residue_annotation[k].append(v) - except TypeError: - # bool column for annotation - residue_annotation[k] = v - - rows.append(residue_annotation) - if cols: - data = pd.DataFrame(rows, columns=cols) - else: - data = pd.DataFrame(rows) - return data - - -def _pdb_validation_to_table(filename, global_parameters=False): - """ - Parse the PDB's validation validation file to a pandas DataFrame. - Private method, prefer its higher level wrapper. +def _add_mmcif_res_full(table): + """ + Utility that adds a new column to the table. + Adds a new column with the 'full res' (i.e. seq_id + ins_code). - :type global_parameters: bool - :param filename: path to file - :return: table with validation information - :rtype: pandas.DataFrame + :param table: pandas DataFrame object + :return: returns a modified pandas DataFrame """ - tree = etree.parse(filename) - root = tree.getroot() - if global_parameters: - global_parameters = root.find('Entry').attrib - log.info(global_parameters) - rows = [] - header = set() - for i, elem in enumerate(root.iterfind('ModelledSubgroup')): - rows.append(dict(elem.attrib)) - header.update(rows[-1].keys()) - for row in rows: - not_in = {k: None for k in header.difference(row.keys())} - row.update(not_in) - df = pd.DataFrame(rows, columns=header) - return df + # adds both 'label' and 'auth' entries + if 'label_seq_id' in table: + table['label_seq_id_full'] = (table['label_seq_id'] + + table['pdbx_PDB_ins_code'].str.replace('?', '')) + if 'auth_seq_id' in table: + table['auth_seq_id_full'] = (table['auth_seq_id'] + + table['pdbx_PDB_ins_code'].str.replace('?', '')) + return table + + +def _add_mmcif_atom_altloc(table): + """ + Utility that adds new columns to the table. + adds: 'label_atom_altloc_id', and 'auth_atom_altloc_id' which is a + string join between '*_atom_id' + 'label_alt_id' -def _rcsb_description(pdb_id, tag, key): + :param table: pandas DataFrame object + :return: returns a modified pandas DataFrame """ - Gets description from RCSB PDB api. - :param pdb_id: PDB id - :param tag: name tag as defined in the api - :param key: key name as defined in the api - :return: list of values + def join_atom_altloc(table, category='label'): + atom = table['{}_atom_id'.format(category)] + altloc = table['label_alt_id'] + + new_column = (atom + '.' + altloc) + has_no_alt = altloc.isin(['.', '', ' ']) + new_column[has_no_alt] = atom.loc[has_no_alt] + + return new_column + + # NB. Use of assign prevents inplace modification + table = table.assign(label_atom_altloc_id=join_atom_altloc(table, 'label')) + table = table.assign(auth_atom_altloc_id=join_atom_altloc(table, 'auth')) + return table + + +def _remove_multiple_altlocs(table): """ - api = defaults.api_rcsb - endpoint = 'describeMol' - query = '?structureId=' + pdb_id + Removes alternative locations (i.e. 'rows') leaving only the first. + Needs to find rows with alt_id != '.' and then find following rows until + '.' appears again (expects atoms to be consequent). - url = api + endpoint + query + :param table: pandas DataFrame object + :return: returns a modified pandas DataFrame + """ - tree = etree.fromstring(get_url_or_retry(url)) - values = [] - for i in tree.iter(tag): - values.append(i.attrib[key]) - return values + drop_ixs = [] + for ix in table.index: + altloc = table.loc[ix, 'label_alt_id'] + if altloc != '.': + # table.loc[ix, 'label_alt_id'] = '.' + table.set_value(ix, 'label_alt_id', '.') + atomid = table.loc[ix, 'label_atom_id'] + try: + for nx in range(1, 100, 1): + altnx = table.loc[ix + nx, 'label_alt_id'] + atomnx = table.loc[ix + nx, 'label_atom_id'] + if altnx != '.' and atomnx == atomid: + # store indexes of the rows to be dropped + drop_ixs.append(ix + nx) + else: + break + except KeyError: + break + return table.drop(table.index[drop_ixs]) -def _get_contacts_from_table(df, distance=5, ignore_consecutive=3): +def _remove_partial_residues(table, category='label'): + """ + Removes residues that contain missing atoms. Needs to check + which atoms are available for each residue. Also removes residues with + same '*_seq_id' as the previous residue. + + :param table: pandas DataFrame object + :param category: data category to be used as precedence in _atom_site.*_* + asym_id, seq_id and atom_id + :return: returns a modified pandas DataFrame """ - Just a simple testing distance measure. - :param df: pd.Dataframe - :param distance: distance threshold in Angstrom - :param ignore_consecutive: number of consecutive residues that will be ignored - (in both directions) - :return: new pd.Dataframe + drop_ixs = [] + curr_ixs = [] + curr_atoms = [] + prev_res = '' + prev_seq = '' + next_res_for_rm = False + table.reset_index(inplace=True) + table = table.drop(['index'], axis=1) + for ix in table.index: + group = table.loc[ix, 'group_PDB'] + if group == 'ATOM': + curr_res = table.loc[ix, '{}_comp_id'.format(category)] + curr_seq = table.loc[ix, '{}_seq_id'.format(category)] + if curr_res in aa_default_atoms: + curr_atom = table.loc[ix, '{}_atom_id'.format(category)] + if prev_res == curr_res and prev_seq == curr_seq: + curr_ixs.append(ix) + curr_atoms.append(curr_atom) + else: + if curr_ixs: + # check available atoms + default_atoms = aa_default_atoms[prev_res] + intersection = list(set(default_atoms) - set(curr_atoms)) + if intersection != [] or next_res_for_rm: + # missing atoms: means that there are atoms in the 'default' list + # that are not observed in the structure + drop_ixs += curr_ixs + next_res_for_rm = False + elif prev_seq == curr_seq: + # duplicated *_seq_id: means that the next residue has got the same + # *_seq_id as the previous res (could come from removing altlocs) + next_res_for_rm = True + # resetting variables + prev_res = curr_res + prev_seq = curr_seq + curr_ixs = [ix] + curr_atoms = [curr_atom] + + return table.drop(table.index[drop_ixs]) + + +def residues_aggregation(table, agg_method='centroid', category='label'): """ - ig = ignore_consecutive + Gets the residues' atoms and their centroids (mean). - # using KDTree - tree = cKDTree(df[['Cartn_y', 'Cartn_y', 'Cartn_z']]) - nearby = [] - for i in df.index: - query_point = df.loc[i, ['Cartn_y', 'Cartn_y', 'Cartn_z']] - idx = tree.query_ball_point(query_point, r=distance, p=2) - idx = df.index[idx] - # ignoring nearby residues (not likely to be true contacts) - # TODO: need to assess this - idx = [j for j in idx if (j <= i - ig or j >= i + ig)] - nearby.append(idx) - # for j in idx: - # chain_i = str(df.loc[i, 'auth_asym_id']) - # chain_j = str(df.loc[j, 'auth_asym_id']) - # if chain_i != chain_j: - # - # cont = [df.loc[i, ['auth_asym_id', 'auth_seq_id', - # 'pdbx_PDB_ins_code', 'auth_comp_id' ]], - # df.loc[j, ['auth_asym_id', 'auth_seq_id', - # 'pdbx_PDB_ins_code', 'auth_comp_id' ]]] - # contacts.append(cont) + :param table: pandas DataFrame object + :param agg_method: current values: 'centroid', 'backbone_centroid'', + first', 'mean' and 'unique' + :param category: data category to be used as precedence in _atom_site.*_* + asym_id, seq_id and atom_id + :return: returns a modified pandas DataFrame + """ - df['contacts'] = nearby - return df + agg_generic = agg_method + agg_cols = ['pdbx_PDB_model_num', '{}_asym_id'.format(category), + '{}_seq_id'.format(category)] + if agg_method not in ['centroid', 'first', 'unique', 'mean', 'backbone_centroid']: + raise ValueError('Method {} is not currently implemented...' + ''.format(agg_method)) + if agg_method == 'backbone_centroid': + table = row_selector(table, '{}_atom_id'.format(category), ('CA', 'N', 'C', 'O')) + agg_method = 'centroid' + if agg_method == 'centroid' or agg_method == 'mean': + agg_generic = 'first' + agg_method = 'mean' + columns_to_agg = {col: agg_generic if table[col].dtype == 'object' else agg_method + for col in table.columns if col not in agg_cols} + columns_to_agg['id'] = 'first' + table = table.groupby(by=agg_cols, as_index=False).agg(columns_to_agg) + table = table.sort_values(by='id').reset_index() + return table -def _table_selector(table, column, value): +def write_mmcif_from_table(table, filename, overwrite=False): """ - Generic table selector. + Generic method that writes 'atom' lines in mmCIF format. - :param table: a pandas DataFrame - :param column: a column in the DataFrame - :param value: the query - :return: the DataFrame filtered for + :param table: pandas DataFrame object + :param filename: path to the mmCIF file + :param overwrite: boolean + :return: (side effects) writes to file """ - if value == 'first': - value = table[column].iloc[0] - table = table[table[column] == value] - - elif not hasattr(value, '__iter__') or isinstance(value, str): - table = table[table[column] == value] + atom_lines = ['data_mmCIF_generated_by_ProteoFAV', 'loop_'] + atom_lines += ["_atom_site.{}".format(v) for v in list(table)] + for i in table.index: + line = ' '.join([str(v) for v in list(table.loc[i, :])]) + atom_lines.append(line) + + # write the final output + if not os.path.exists(filename) or overwrite: + with open(filename, 'w') as outlines: + outlines.write("\n".join(atom_lines)) else: - table = table[table[column].isin(value)] + log.info("mmCIF for %s already available...", filename) + return - if table.empty: - raise ValueError('Column {} does not contain {} value(s)'.format( - column, value)) - return table + +def write_pdb_from_table(table, filename, overwrite=False, category='auth'): + """ + Generic method that writes 'atom' lines in PDB format. + + :param table: pandas DataFrame object + :param filename: path to the PDB file + :param overwrite: boolean + :param category: data category to be used as precedence in _atom_site.*_* + asym_id, seq_id and atom_id + :return: (side effects) writes to file + """ + + atom_lines = ['REMARK 100 PDB generated by ProteoFAV\n'] + atom_number = 0 + for i in table.index: + atom_number += 1 + atom_lines.append(_get_atom_line(table=table, index=i, + atom_number=atom_number, + category=category)) + + # write the final output + if not os.path.exists(filename) or overwrite: + with open(filename, 'w') as outlines: + outlines.write("".join(atom_lines)) + else: + log.info("PDB for %s already available...", filename) + return -def _residues_as_centroid(table): +def _get_atom_line(table, index, atom_number, category='auth'): """ - Gets the residues' atoms and their centroids (mean). + Returns an ATOM PDB-formatted string. + (Based on code from the PDB module in Biopython.) + + :param table: pandas DataFrame object + :param index: atom index + :param atom_number: incremental number + :param category: data category to be used as precedence in _atom_site.*_* + asym_id, seq_id and atom_id + :return: returns a PDB-formatted ATOM/HETATM line + """ + + ix = index + record_type = table.loc[ix, 'group_PDB'] + if record_type == "ATOM": + record_type = "ATOM " - :param table: main dataframe - :return: compressed dataframe """ - columns_to_agg = {col: "first" if table[col].dtype == 'object' else 'mean' - for col in table.columns - if col not in UNIFIED_COL} - columns_to_agg['auth_atom_id'] = 'unique' - return table.groupby(by=UNIFIED_COL, as_index=False).agg(columns_to_agg) + ATOM 16 CB ASN A 2 22.780 31.612 8.039 1.00 97.98 C + ATOM 17 CG ASN A 2 23.735 31.870 9.167 1.00100.56 C + ATOM 18 OD1 ASN A 2 23.345 32.366 10.218 1.00 97.84 O + ATOM 19 ND2 ASN A 2 25.014 31.606 8.922 1.00106.62 N + ATOM 20 H ASN A 2 24.256 34.106 6.858 1.00 0.00 H + ATOM 21 HD21 ASN A 2 25.654 31.751 9.644 1.00 0.00 H + ATOM 22 HD22 ASN A 2 25.276 31.270 8.035 1.00 0.00 H + """ + + name = table.loc[ix, '{}_atom_id'.format(category)] + if len(name) == 1: + name = " {} ".format(name.strip()) + elif len(name) == 2: + name = " {} ".format(name.strip()) + elif len(name) == 3: + name = " {}".format(name.strip()) + elif len(name) == 4: + name = name.strip() + + altloc = table.loc[ix, 'label_alt_id'] + if altloc == ".": + altloc = " " + + resname = table.loc[ix, '{}_comp_id'.format(category)] + + chain_id = table.loc[ix, '{}_asym_id'.format(category)] + chain_id = chain_id[0] + + resseq = str(table.loc[ix, '{}_seq_id'.format(category)]) + + icode = table.loc[ix, 'pdbx_PDB_ins_code'] + if icode == "?": + icode = " " + + x = float(table.loc[ix, 'Cartn_x']) + y = float(table.loc[ix, 'Cartn_y']) + z = float(table.loc[ix, 'Cartn_z']) + + occupancy_str = "%6.2f" % float(table.loc[ix, 'occupancy']) + + bfactor = float(table.loc[ix, 'B_iso_or_equiv']) + + segid = "" + + element = table.loc[ix, 'type_symbol'] + element = element.strip().upper() -def _import_dssp_chains_ids(pdb_id): - """Imports mmCIF chain identifier to DSSP. + charge = " " - :param pdb_id: - :return: DSSP table with corrected chain ids. + values = (record_type, atom_number, name, altloc, resname, chain_id, + resseq, icode, x, y, z, occupancy_str, bfactor, segid, + element, charge) + + return PDB_FORMAT % values + + +def fetch_summary_properties_pdbe(identifier, retry_in=(429,)): + """ + Queries the PDBe api to get summary validation report. + + :param identifier: PDB ID + :param retry_in: http code for retrying connections + :return: Requests object + """ + pdbe_endpoint = "pdb/entry/summary/{}".format(identifier) + url = defaults.api_pdbe + pdbe_endpoint + response = fetch_from_url_or_retry(url, json=True, retry_in=retry_in) + return response + + +def get_preferred_assembly_id(identifier, verbose=False): + """ + Gets the preferred assembly id for the given PDB ID, from the PDBe API. + + :param identifier: PDB ID + :param verbose: boolean + :return: str """ - dssp_table = select_dssp(pdb_id) - cif_table = select_cif(pdb_id) - cif_seq = cif_table.auth_comp_id.apply(scop_3to1.get) - dssp_has_seq = dssp_table.aa.isin(scop_3to1.values()) - dssp_seq = dssp_table.aa[dssp_has_seq] - # Import only if the sequences are identical - if not (cif_seq == dssp_seq).all(): - err = ('Inconsitent DSSP / mmCIF sequence for {} protein structure cannot be fixed' - 'by import_dssp_chains_ids') - raise ValueError(err.format(pdb_id)) - dssp_table.loc[dssp_has_seq, 'chain_id'] = cif_table.auth_asym_id - return dssp_table + + # getting the preferred biological assembly from the PDBe API + try: + data = fetch_summary_properties_pdbe(identifier).json() + except Exception as e: + message = "Something went wrong for {}... {}".format(identifier, e) + if verbose: + log.error(message) + try: + nassemblies = data[identifier][0]["assemblies"] + if len(nassemblies) > 1: + for entry in nassemblies: + if entry["preferred"]: + pref_assembly = entry["assembly_id"] + break + else: + pref_assembly = data[identifier][0]["assemblies"][0]["assembly_id"] + except Exception: + pref_assembly = "1" + + bio_best = str(pref_assembly) + return bio_best ############################################################################## # Public methods ############################################################################## -def select_cif(pdb_id, models='first', chains=None, lines='ATOM', atoms='CA', - biounit=False, assembly_id=None): +def select_structures(identifier=None, excluded_cols=None, + bio_unit=False, bio_unit_preferred=False, bio_unit_id="1", + overwrite=False, **kwargs): """ Produce table read from mmCIF file. - :param atoms: Which atom should represent the structure - :param pdb_id: PDB identifier - :param models: protein structure entity - :param chains: protein structure chain - :param lines: choice of ATOM, HETATMS or both (list). - :param biounit: boolean to use the preferred biounit available - :param assembly_id: only applies when biounit is True - :return: Table read to be joined - """ - - # asymmetric unit or biological unit? - if biounit: - if assembly_id is None: - # get the preferred bio assembly id from the PDBe API - assembly_id = get_preferred_assembly_id(pdb_id) - - # load the table - cif_path = path.join(defaults.db_mmcif, - pdb_id + '-assembly-' + assembly_id + '.cif') - - try: - cif_table = _mmcif_atom(cif_path) - except IOError: - cif_path = fetch_files(pdb_id + '-assembly-' + assembly_id, - sources='bio', directory=defaults.db_mmcif)[0] - cif_table = _mmcif_atom(cif_path) + :param identifier: PDB/mmCIF accession ID + :param excluded_cols: option to exclude mmCIF columns + :param bio_unit: (boolean) whether to get BioUnit instead of AsymUnit + :param bio_unit_preferred: (boolean) if True fetches the 'preferred' + biological assembly instead + :param bio_unit_id: biological unit identifier + :param overwrite: boolean + :return: returns a pandas DataFrame + """ + + if bio_unit: + filename = os.path.join(defaults.db_mmcif, "{}_bio.cif".format(identifier)) else: - # load the table - cif_path = path.join(defaults.db_mmcif, pdb_id + '.cif') - try: - cif_table = _mmcif_atom(cif_path) - except IOError: - cif_path = fetch_files(pdb_id, sources='cif', directory=defaults.db_mmcif)[0] - cif_table = _mmcif_atom(cif_path) + filename = os.path.join(defaults.db_mmcif, "{}.cif".format(identifier)) + + download_structures(identifier=identifier, filename=filename, + bio_unit=bio_unit, bio_unit_preferred=bio_unit_preferred, + bio_unit_id=bio_unit_id, overwrite=overwrite) + + table = read_structures(filename=filename, excluded_cols=excluded_cols) + + table = filter_structures(table=table, excluded_cols=excluded_cols, **kwargs) + table = constrain_column_types(table, col_type_dict=pdbx_types) + + # id is the atom identifier and it is need for all atoms tables. + if table[UNIFIED_COL + ['id']].duplicated().any(): + log.error('Failed to find unique index for {}'.format(filename)) + + return table + + +def filter_structures(table, excluded_cols=None, + models='first', chains=None, res=None, res_full=None, + comps=None, atoms=None, lines=None, category='label', + residue_agg=False, agg_method='centroid', + add_res_full=True, add_atom_altloc=False, reset_atom_id=True, + remove_altloc=False, remove_hydrogens=True, remove_partial_res=False): + """ + Filter and residue aggregation for mmCIF and PDB Pandas Dataframes. + Improves consistency ATOM and HETATM lines from mmCIF or PDB files. + + :param table: pandas DataFrame object + :param excluded_cols: option to exclude mmCIF columns + :param models: (tuple) model IDs or 'first' or None + :param chains: (tuple) chain IDs or None + :param res: (tuple) res IDs or None + :param res_full: (tuple) full res IDs ('*_seq_id' + 'pdbx_PDB_ins_code') or None + :param comps: (tuple) comp IDs or None + :param atoms: (tuple) atom IDs or None + :param lines: (tuple) 'ATOM' or 'HETATM' or None (both) + :param category: data category to be used as precedence in _atom_site.*_* + asym_id, seq_id and atom_id + :param residue_agg: (boolean) whether to do residue aggregation + :param agg_method: current values: 'centroid', 'first', 'mean' and 'unique' + :param add_res_full: option to extend the table with 'res_full' + i.e. res_number + insertion_code (e.g. '12A') + :param add_atom_altloc: boolean (new string join) + :param reset_atom_id: boolean + :param remove_altloc: boolean + :param remove_hydrogens: boolean + :param remove_partial_res: (boolean) removes amino acids with missing atoms + :return: returns a pandas DataFrame + """ + + # selections / filtering + # excluding columns + table = exclude_columns(table, excluded=excluded_cols) + + # excluding rows # select the models + # if only first model (>1 in NMR structures) if models: - try: - cif_table = _table_selector(cif_table, 'pdbx_PDB_model_num', models) - except AttributeError: - err = 'Structure {} has only one model, which was kept'.format - log.info(err(pdb_id)) + table = row_selector(table, 'pdbx_PDB_model_num', models) + log.info("mmCIF/PDB table filtered by pdbx_PDB_model_num...") # select chains if chains: - cif_table = _table_selector(cif_table, 'auth_asym_id', chains) + table = row_selector(table, '{}_asym_id'.format(category), chains) + log.info("mmCIF/PDB table filtered by %s_asym_id...", category) # select lines if lines: - cif_table = _table_selector(cif_table, 'group_PDB', lines) - - # select which atom line will represent - if atoms == 'centroid': - cif_table = _residues_as_centroid(cif_table) - elif atoms == 'backbone_centroid': - cif_table = _table_selector( - cif_table, 'label_atom_id', ('CA', 'N', 'C', 'O')) - cif_table = _residues_as_centroid(cif_table) + table = row_selector(table, 'group_PDB', lines) + log.info("mmCIF/PDB table filtered by group_PDB...") + + # table modular extensions or selections + if add_res_full: + table = _add_mmcif_res_full(table) + log.info("mmCIF/PDB added full res (res + ins_code)...") + + if add_atom_altloc: + table = _add_mmcif_atom_altloc(table) + log.info("mmCIF/PDB added full atom (atom + altloc)...") + + if remove_hydrogens: + table = row_selector(table, key='type_symbol', value='H', reverse=True) + log.info("mmCIF/PDB removed existing hydrogens...") + + if remove_altloc: + table = _remove_multiple_altlocs(table) + reset_atom_id = True + log.info("mmCIF/PDB removed altlocs...") + + if remove_partial_res: + table = _remove_partial_residues(table) + log.info("mmCIF/PDB removed incomplete residues...") + + if reset_atom_id: + table.reset_index(inplace=True) + table = table.drop(['index'], axis=1) + table['id'] = table.index + 1 + log.info("mmCIF/PDB reset atom numbers...") + + # excluding rows + # select residues + if res: + table = row_selector(table, '{}_seq_id'.format(category), res) + log.info("mmCIF/PDB table filtered by %s_seq_id...", category) + + if res_full: + table = row_selector(table, '{}_seq_id_full'.format(category), res_full) + log.info("mmCIF/PDB table filtered by %s_seq_id_full...", category) + + # select amino acids/molecules + if comps: + table = row_selector(table, '{}_comp_id'.format(category), comps) + log.info("mmCIF/PDB table filtered by %s_comp_id...", category) + + # select atoms + if atoms == 'centroid' or atoms == 'backbone_centroid': + table = residues_aggregation(table, agg_method=atoms) elif atoms: - cif_table = _table_selector(cif_table, 'label_atom_id', atoms) + table = row_selector(table, '{}_atom_id'.format(category), atoms) + log.info("mmCIF/PDB table filtered by %s_atom_id...", category) - # id is the atom identifier and it is need for all atoms tables. - if cif_table[UNIFIED_COL + ['id']].duplicated().any(): - log.error('Failed to find unique index for {}'.format(cif_path)) + if residue_agg: + table = residues_aggregation(table, agg_method=agg_method, + category=category) - return cif_table + if table.empty: + raise ValueError("The filters resulted in an empty DataFrame...") + return table -def select_dssp(pdb_id, chains=None): +def read_structures(filename=None, input_format=None, excluded_cols=None, + pdb_fix_ins_code=True, pdb_fix_label_alt_id=True, pdb_fix_type_symbol=True): """ - Produce table from DSSP file output. - - :param pdb_id: PDB identifier - :param chains: PDB protein chain - :return: pandas dataframe + Parse ATOM and HETATM lines from mmCIF or PDB files. + + :param filename: path to the mmCIF/PDB file + :param input_format: either 'mmcif', 'cif', 'pdb' or 'ent' + :param excluded_cols: option to exclude mmCIF columns + :param pdb_fix_ins_code: boolean + :param pdb_fix_label_alt_id: boolean + :param pdb_fix_type_symbol: boolean + :return: returns a pandas DataFrame """ - dssp_path = path.join(defaults.db_dssp, pdb_id + '.dssp') - try: - dssp_table = _dssp(dssp_path) - except IOError: - dssp_path = fetch_files(pdb_id, sources='dssp', directory=defaults.db_dssp)[0] - dssp_table = _dssp(dssp_path) - except StopIteration: - raise IOError('{} is unreadable.'.format(dssp_path)) - if chains: - try: - dssp_table = _table_selector(dssp_table, 'chain_id', chains) - except ValueError: - # TODO: - # Could not find the correct PDB chain. It happens for protein structures with complex - # chain identifier, as 4v9d. - # dssp_table = _import_dssp_chains_ids(pdb_id) - # dssp_table = _table_selector(dssp_table, 'chain_id', chains) - log.error('Error loading DSSP file: Chain {} not in {}'.format(chains, pdb_id)) - return None - # remove dssp line of transition between chains - dssp_table = dssp_table[dssp_table.aa != '!'] - - dssp_table.reset_index(inplace=True) - if dssp_table.duplicated(['icode', 'chain_id']).any(): - log.info('DSSP file for {} has not unique index'.format(pdb_id)) - try: - dssp_table.loc[:, 'icode'] = dssp_table.loc[:, 'icode'].astype(int) - except ValueError: - log.warning("{} insertion code detected in the DSSP file.".format(pdb_id)) - dssp_table.loc[:, 'icode'] = dssp_table.loc[:, 'icode'].astype(str) + InputFileHandler(filename) - return dssp_table + # try to guess the correct format + if input_format is None: + if filename.endswith('.pdb') or filename.endswith('.ent'): + input_format = "pdb" + elif filename.endswith('.cif') or filename.endswith('.mmcif'): + input_format = "mmcif" + else: + message = ("Could not guess the format of the input file... " + "Please define it by passing 'input_format'=''") + raise ValueError(message) + + if input_format == 'mmcif': + table = parse_mmcif_atoms(filename, excluded_cols=excluded_cols) + elif input_format == 'pdb': + table = parse_pdb_atoms(filename, excluded_cols=excluded_cols, + fix_ins_code=pdb_fix_ins_code, + fix_label_alt_id=pdb_fix_label_alt_id, + fix_type_symbol=pdb_fix_type_symbol) + if table.empty: + raise ValueError('{} resulted in an empty DataFrame...'.format(filename)) + return table -def select_sifts(pdb_id, chains=None): +def write_structures(table=None, filename=None, overwrite=False, + output_format=None, category='label'): """ - Produce table ready from SIFTS XML file. - - :param pdb_id: PDB identifier - :param chains: Protein structure chain - :return: table read to be merged + Writes 'ATOM' lines in PDB or mmCIF format. + + :param table: pandas DataFrame object + :param filename: path to the mmCIF/PDB file + :param overwrite: boolean + :param category: data category to be used as precedence in _atom_site.*_* + asym_id, seq_id and atom_id (generally either 'label' or 'auth') + :param output_format: either 'mmcif', 'cif', 'pdb' or 'ent' + :return: (side effects) writes to a file """ - sifts_path = path.join(defaults.db_sifts, pdb_id + '.xml') - try: - sift_table = _sifts_residues_regions(sifts_path, - sources=('CATH', 'SCOP', 'Pfam')) - except IOError: - sifts_path = fetch_files(pdb_id, sources='sifts', - directory=defaults.db_sifts)[0] - sift_table = _sifts_residues_regions(sifts_path) - # standardise column types - for col in sift_table: - # bool columns - if col.startswith('is'): - sift_table[col].fillna(False) - if chains is None: - return sift_table - else: - return _table_selector(sift_table, 'PDB_dbChainId', chains) + OutputFileHandler(filename, overwrite=overwrite) + if output_format is None: + if filename.endswith('.pdb') or filename.endswith('.ent'): + output_format = "pdb" + elif filename.endswith('.cif') or filename.endswith('.mmcif'): + output_format = "mmcif" + else: + message = ("Could not guess the format of the input file... " + "Please define it by passing 'input_format'=''") + raise ValueError(message) + + if output_format == 'mmcif' or output_format == 'cif': + write_mmcif_from_table(filename=filename, table=table, + overwrite=overwrite) + elif output_format == 'pdb' or output_format == 'ent': + write_pdb_from_table(filename=filename, table=table, + overwrite=overwrite, category=category) -def select_validation(pdb_id, chains=None): - """ - Produces table from PDB validation XML file. - :param pdb_id: PDB identifier - :param chains: PDB protein chain - :return: pandas dataframe +def download_structures(identifier=None, filename=None, output_format='mmcif', + bio_unit=False, bio_unit_preferred=False, bio_unit_id="1", + overwrite=False): + """ + Downloads a structure from the PDBe to the filesystem. + BioUnits only work for mmCIF. If `pdb=True` the bio_unit arguments + are ignored. + + :param identifier: (str) PDB accession ID + :param filename: path to the mmCIF/PDB file + :param output_format: either 'mmcif', 'cif', 'pdb' or 'ent' + :param bio_unit: (boolean) whether to get BioUnit instead of AsymUnit + :param bio_unit_preferred: (boolean) if True fetches the 'preferred' + biological assembly instead + :param bio_unit_id: biological unit identifier + :param overwrite: boolean + :return: (side effects) writes to a file """ - val_path = path.join(defaults.db_validation, pdb_id + defaults.validation_extension) - try: - val_table = _pdb_validation_to_table(val_path) - except IOError: - val_path = fetch_files(pdb_id, sources='validation', directory=defaults.db_pdb)[0] - val_table = _pdb_validation_to_table(val_path) - if chains: - val_table = _table_selector(val_table, 'chain', chains) - if not val_table.empty: - val_table.columns = ["validation_" + name for name in val_table.columns] - return val_table - raise ValueError('Parsing {} resulted in a empty table'.format(val_path)) + if output_format is None: + if filename.endswith('.pdb') or filename.endswith('.ent'): + output_format = "pdb" + elif filename.endswith('.cif') or filename.endswith('.mmcif'): + output_format = "mmcif" + else: + message = ("Could not guess the format of the input file... " + "Please define it by passing 'input_format'=''") + raise ValueError(message) + + decompress = False + if output_format == 'mmcif' or output_format == 'cif': + if bio_unit: + # atom lines only? + # url_endpoint = ("{}-assembly-{}_atom_site.cif.gz".format(identifier, pref)) + if bio_unit_preferred: + pref = get_preferred_assembly_id(identifier=identifier) + else: + pref = bio_unit_id + url_endpoint = ("{}-assembly-{}.cif.gz".format(identifier, pref)) + decompress = True + url_root = defaults.bio_fetch + url = url_root + url_endpoint + else: + # original mmCIF? + # url_endpoint = "download/{}.cif".format(pdbid) + url_endpoint = "download/{}_updated.cif".format(identifier) + url_root = defaults.pdbe_fetch + url = url_root + url_endpoint + elif output_format == 'pdb' or output_format == 'ent': + url_endpoint = "download/pdb{}.ent".format(identifier) + url_root = defaults.pdbe_fetch + url = url_root + url_endpoint -def sifts_best(uniprot_id, first=False): - """ - Retrieves the best structures from the SIFTS endpoint in the PDBe api. + else: + message = ("Could not guess the format of the output file... " + "Please define it by passing 'output_format'=''") + raise ValueError(message) - :param uniprot_id: Uniprot ID - :param first: gets the first entry - :return: url content or url content in json data structure. - """ - sifts_endpoint = "mappings/best_structures/" - url = defaults.api_pdbe + sifts_endpoint + str(uniprot_id) - try: - response = get_url_or_retry(url, json=True) - except HTTPError as e: - if e.response.status_code == 404: - logging.error('No SIFTS mapping found for {}'.format(uniprot_id)) - return None - else: - raise - return response if not first else response[uniprot_id][0] + Downloader(url=url, filename=filename, + decompress=decompress, overwrite=overwrite) + + +class Structure(GenericInputs): + def read(self, filename=None, **kwargs): + filename = self._get_filename(filename) + self.table = read_structures(filename=filename, **kwargs) + return self.table + + def write(self, table=None, filename=None, **kwargs): + table = self._get_table(table) + filename = self._get_filename(filename) + return write_structures(table=table, filename=filename, **kwargs) + + def download(self, identifier=None, filename=None, **kwargs): + identifier = self._get_identifier(identifier) + filename = self._get_filename(filename) + return download_structures(identifier=identifier, filename=filename, **kwargs) + + def select(self, identifier=None, **kwargs): + identifier = self._get_identifier(identifier) + self.table = select_structures(identifier=identifier, **kwargs) + return self.table -if __name__ == '__main__': - pass +PDB = Structure() +mmCIF = Structure() diff --git a/proteofav/uniprot.py b/proteofav/uniprot.py deleted file mode 100644 index dbc9369..0000000 --- a/proteofav/uniprot.py +++ /dev/null @@ -1,210 +0,0 @@ -#!/usr/bin/env python -# -*- coding: utf-8 -""" -Created on 17:26 19/02/2016 2016 -Define auxiliary functions for interacting with Uniprot. -""" -from __future__ import absolute_import -import logging - -try: - # python 2.7 - from StringIO import StringIO -except ImportError: - from io import StringIO, BytesIO -try: - # python 2.7 - from urlparse import parse_qs -except ImportError: - from urllib.parse import parse_qs - -import pandas as pd - -from proteofav.config import defaults -from proteofav.utils import get_url_or_retry -from proteofav.structures import _table_selector - -__all__ = ["fetch_uniprot_sequence", - "fetch_uniprot_formal_specie", - "_uniprot_info", - "_fetch_uniprot_gff", - "map_gff_features_to_sequence", - "_uniprot_to_ensembl_xref"] -log = logging.getLogger('proteofav.config') - - -def fetch_uniprot_sequence(uniprot_id): - """ - Gets current sequence of a Uniprot entry. - - :param str uniprot_id: Uniprot accession - :return str: the sequence - - >>> print(fetch_uniprot_formal_specie('P17612')) - Homo sapiens - - """ - - return _uniprot_info(uniprot_id, cols='sequence').iloc[0, 1] - - -def fetch_uniprot_formal_specie(uniprot_id, remove_isoform=True): - """ - Gets the species name of an organism expressing a protein. - - :param Bool remove_isoform: whether to remove the isoform identifier. - :param str uniprot_id: Uniprot accession - :return: the species name (two words) - :rtype: str or None - - >>> print(fetch_uniprot_sequence('P17612'))[:20] - MGNAAAAKKGSEQESVKEFL - - """ - if remove_isoform: - uniprot_id = uniprot_id.split('-')[0] - - full_specie = _uniprot_info(uniprot_id, cols='organism').iloc[0, 1] - - try: - return " ".join(full_specie.split()[0:2]) - except AttributeError: - log.error('Could not retrieve {} information. Maybe obsolete UniProt accession?'.format( - uniprot_id)) - return None - - -def _uniprot_info(uniprot_id, retry_in=(503, 500), cols=None): - """ - Retrieve Uniprot information from the database. - - :param str uniprot_id: Uniprot accession identifier - :param retry_in: iterable of status_code to be retried upon error. - :type retry_in: list of [int] - :return pandas.DataFrame: table from Uniprot. - Default table columns: - :raises requests.HTTPError: when hits a bad status_code - """ - - if not cols: - cols = ('id', 'entry name', 'reviewed', 'protein names', 'genes', 'organism', - 'sequence', 'length') - elif isinstance(cols, str): - cols = ('id', cols) - - params = {'query': 'accession:' + str(uniprot_id), - 'columns': ",".join(cols), - 'format': 'tab', - 'contact': ""} - url = defaults.api_uniprot - response = get_url_or_retry(url=url, retry_in=retry_in, **params) - try: - data = pd.read_table(StringIO(response)) - except TypeError: - # python 3.5 - data = pd.read_table(BytesIO(response)) - except ValueError as e: - log.error(e) - return None - # id column is called Entry in the table - return _table_selector(data, 'Entry', uniprot_id) - - -def _fetch_uniprot_gff(uniprot_id): - """ - Retrieve Uniprot data from the GFF file. - - :param str uniprot_id: Uniprot accession - :return pandas.DataFrame: table - :raises requests.HTTPError: when hits a bad status_code - """ - url = defaults.api_uniprot + uniprot_id + ".gff" - cols = "NAME SOURCE TYPE START END SCORE STRAND FRAME GROUP empty".split() - - data = pd.read_table(url, skiprows=2, names=cols) - groups = data.GROUP.apply(parse_qs) - groups = pd.DataFrame.from_records(groups) - - return data.merge(groups, left_index=True, right_index=True) - - -def map_gff_features_to_sequence(uniprot_id, - query_type='', - group_residues=True, - drop_types=('Helix', 'Beta strand', 'Turn', 'Chain')): - """ - Map Uniprot GFF features to the protein sequence. - - :param str uniprot_id: Uniprot accession - :param str query_type: Select type of feature - :param bool group_residues: by default each row in the resulting table, - maps to a residue. When set to False, each row represent a feature - per residue. - - :param tuple drop_types: Filter out some of the features, important to - remove fetures that spam. - - :return pd.DataFrame: table. Columns will depend on paramenters. - """ - - def annotation_writer(gff_row): - """ - Establish a set of rules to annotate Uniprot GFF. - - :param pd.Series gff_row: each line in the GFF file. - :return str: template filled with type-specific fields. - """ - if not gff_row.ID and not gff_row.Note: - return gff_row.TYPE - elif not gff_row.ID: - - return '{0.TYPE}: {0.Note}'.format(gff_row) - elif not gff_row.Note: - - return '{0.TYPE} ({0.ID})'.format(gff_row) - else: - - return '{0.TYPE}: {0.Note} ({0.ID})'.format(gff_row) - - table = _fetch_uniprot_gff(uniprot_id) - if query_type: - table = table[table.TYPE == query_type] - elif drop_types: - table = table[~table.TYPE.isin(drop_types)] - - lines = [] - for i, row in table.iterrows(): - lines.extend({'idx': i, 'annotation': annotation_writer(row)} - for i in range(row.START, row.END + 1)) - table = pd.DataFrame(lines) - - if table.empty: - return table - - if group_residues: - - return table.groupby('idx').agg({'annotation': lambda x: ', '.join(x)}) - else: - - return table - - -def _uniprot_to_ensembl_xref(uniprot_id, species='homo_sapiens'): - """ - Return Gene, transcripts and translational ids from Ensembl to Uniprot. - Ensembl -> Uniprot reference is ideal because Ensembl database change more - often the Uniprot'smove quicker than Uniprot. - - :param str uniprot_id: Uniprot accession - :param str species: species name - :return pandas.DataFrame: table with columns - """ - - url = "{}xrefs/symbol/{}/{}?content-type=application/json".format( - defaults.api_ensembl, species, uniprot_id) - - return pd.read_json(url) - - -if __name__ == '__main__': - pass diff --git a/proteofav/utils.py b/proteofav/utils.py index 1b8d4bf..038de87 100644 --- a/proteofav/utils.py +++ b/proteofav/utils.py @@ -1,13 +1,18 @@ -#!/usr/bin/env python # -*- coding: utf-8 -*- -from __future__ import absolute_import -import gzip -import json -import logging + import os +import gzip +import time +import copy import shutil import socket -import time +import logging +import tempfile +import requests +import numpy as np +import pandas as pd +import requests_cache + try: from urllib import quote as urllib_quote from urllib import urlretrieve @@ -15,516 +20,444 @@ from urllib.parse import quote as urllib_quote from urllib.request import urlretrieve -import numpy as np -import pandas as pd -import requests - -from proteofav.config import defaults -from proteofav.library import valid_ensembl_species_variation - -__all__ = ["get_url_or_retry", "check_local_or_fetch", "fetch_files", "get_preferred_assembly_id", - "IDNotValidError", "raise_if_not_ok", "_pdb_uniprot_sifts_mapping", - "_uniprot_pdb_sifts_mapping", "icgc_missense_variant", "is_valid", - "is_valid_ensembl_id", "confirm_column_types"] log = logging.getLogger('proteofav.config') socket.setdefaulttimeout(15) # avoid infinite hanging +requests_cache.install_cache('proteofav') + +__all__ = ["fetch_from_url_or_retry", "row_selector", "constrain_column_types", "exclude_columns", + "splitting_up_by_key", "merging_down_by_key", + "flatten_nested_structure", "refactor_key_val_singletons", + "InputFileHandler", "OutputFileHandler", "Downloader", "GenericInputs"] -def get_url_or_retry(url, retry_in=None, wait=1, n_retries=10, json=False, header=None, **params): + +def fetch_from_url_or_retry(url, json=True, header=None, post=False, data=None, + retry_in=None, wait=1, n_retries=10, stream=False, **params): """ Fetch an url using Requests or retry fetching it if the server is - complaining with retry_in error. + complaining with retry_in error. There is a limit to the number of retries. + + Retry code examples: 429, 500 and 503 - :param retry_in: list or array of http status codes - :param json: boolean - :param header: dictionary with head params :param url: url to be fetched as a string + :param json: json output + :param header: dictionary + :param post: boolean + :param data: dictionary: only if post is True + :param retry_in: http codes for retrying :param wait: sleeping between tries in seconds :param n_retries: number of retry attempts + :param stream: boolean :param params: request.get kwargs. - :return: url content or url content in json data structure. + :return: url content """ - if not header: + + if retry_in is None: + retry_in = () + else: + assert type(retry_in) is tuple or type(retry_in) is list + + if header is None: header = {} - if not retry_in: - retry_in = [] + else: + assert type(header) is dict + if json: header.update({"Content-Type": "application/json"}) - response = requests.get(url, headers=header, params=params) + else: + if "Content-Type" not in header: + header.update({"Content-Type": "text/plain"}) - if response.ok and json: - return response.json() - elif response.ok: - return response.content + if post: + if data is not None: + assert type(data) is dict or type(data) is str + response = requests.post(url, headers=header, data=data) + else: + return None + else: + response = requests.get(url, headers=header, params=params, stream=stream) + + if response.ok: + return response elif response.status_code in retry_in and n_retries >= 0: time.sleep(wait) - return get_url_or_retry(url, retry_in, (n_retries - 1), wait, json, header, **params) + return fetch_from_url_or_retry(url, json, header, post, data, retry_in, wait, + (n_retries - 1), stream, **params) else: - log.error(response.status_code) - response.raise_for_status() + try: + response.raise_for_status() + except requests.exceptions.HTTPError as e: + log.debug("%s: Unable to retrieve %s for %s", + response.status_code, url, e) -def fetch_files(identifier, directory=None, sources=("cif", "dssp", "sifts")): +def row_selector(table, key=None, value=None, reverse=False): """ - Small routine to fetch data files from their respective repositories. - Use defaults to fetch files from servers. Defaults server are defined - in the default config.txt. Returns None since it has side effects. - - :param identifier: protein identifier as PDB identifier - :param directory: path to download. The default downloads all files to - default.temp folder. If is a string and valid path downloads all files - to that folder. If its a iterable and all valid path downloads to the - respective folders - - :param sources: where to fetch the data. Must be in the config file. - :return list: list of paths - :raise: TypeError + Generic method to filter columns + :param table: pandas DataFrame + :param key: pandas DataFrame column name + :param value: value(s) to be looked for + :param reverse: opposite behavior (e.g. 'isin' becomes 'isnotin' + and 'equals' becomes 'differs') + :return: returns a modified pandas DataFrame """ - if isinstance(sources, str): - sources = [sources] - if not directory: - directory = defaults.tmp - elif isinstance(directory, str): - if not os.path.isdir(directory): - raise IOError(directory + " is not a valid path.") - directory = [directory] * len(sources) - elif hasattr(directory, "__iter__"): - if len(directory) != len(sources): - raise IOError(directory + " you need one directory for each source," - "or a path for all.") - for d in directory: - if not os.path.isdir(d): - raise IOError(d + " is not a valid path.") - else: - raise TypeError('Unidentified source|directory combination.') - result = [] - for source, destination in zip(sources, directory): - filename = identifier + getattr(defaults, source + '_extension') - url = getattr(defaults, source + '_fetch') + filename - try: - urlretrieve(url, destination + filename) - except IOError as e: - log.error('Unable to retrieve {} for {}'.format(url, str(e))) - raise - if filename.endswith('.gz'): - with gzip.open(destination + filename, 'rb') as input_f, \ - open(destination + filename.replace('.gz', ''), - 'wb') as output_f: - shutil.copyfileobj(input_f, output_f) - filename = filename.replace('.gz', '') - result.append(destination + filename) - return result - - -def _fetch_summary_properties_pdbe(pdbid, retry_in=(429,)): - """ - Queries the PDBe api to get summary validation report. + assert type(table) is pd.core.frame.DataFrame + if key is not None and value is not None: + assert type(key) is str + if key in table: + if value == 'first': + value = table[key].iloc[0] + table = table.loc[table[key] == value] + elif (hasattr(value, '__iter__') and + (type(value) is tuple or type(value) is list)): + if not reverse: + table = table.loc[table[key].isin(value)] + else: + table = table.loc[~table[key].isin(value)] + else: + if not reverse: + table = table.loc[table[key] == value] + else: + table = table.loc[table[key] != value] + else: + log.debug("%s not in the DataFrame...", key) - :param pdbid: PDB ID - :param retry_in: http code for retrying connections - :return: dictionary - """ - pdbe_endpoint = "pdb/entry/summary/" - url = defaults.api_pdbe + pdbe_endpoint + pdbid - rows = get_url_or_retry(url, retry_in=retry_in, json=True) - return rows + if table.empty: + message = 'Column {} does not contain {} value(s)...'.format(key, value) + log.debug(message) + raise ValueError(message) + return table -def get_preferred_assembly_id(pdbid, verbose=False): - """ - Gets the preferred assembly id for the given PDB ID, from the PDBe API. - :param pdbid: PDB ID - :param verbose: boolean - :return: str +def constrain_column_types(table, col_type_dict=None, nan_value_dict=None, + replace_value_dict=None): """ + Helper method that helps in constraining data types for the + various DataFrame columns. - # getting the preferred biological assembly from the PDBe API - try: - data = _fetch_summary_properties_pdbe(pdbid) - except Exception as e: - message = "Something went wrong for {}... {}".format(pdbid, e) - if verbose: - log.error(message) - try: - nassemblies = data[pdbid][0]["assemblies"] - if len(nassemblies) > 1: - for entry in nassemblies: - if entry["preferred"]: - pref_assembly = entry["assembly_id"] - break - else: - pref_assembly = data[pdbid][0]["assemblies"][0]["assembly_id"] - except Exception as e: - pref_assembly = "1" + This function checks a table's column types against a defined + column name/type dictionary and correct them if necessary. - bio_best = str(pref_assembly) - return bio_best + .. notes:: + There are fewer pandas `dtypes` than the corresponding numpy + type, but all numpy types can be accommodated. -############################################################################## -# Some other utils not currently in use -############################################################################## -class IDNotValidError(Exception): - """ - Base class for database related exceptions. - Databases: UniProt, PDB, Ensembl, etc. - """ - pass + NaNs and Upcasting: + The upcasting of dtypes on columns that contain NaNs has been an issue and + can lead to inconsistencies between the column types of different + tables that contain equivalent data. E.g., a `merged_table` from a PDB + entry may have NaNs in UniProt_dbResNum and so is cast to float64 + whilst a UniProt variants table will have no NaNs in this field and + so remains int64 by default. The main issue here is that it creates + additional work for merging these tables as the keys must be of the + same type. It's also a problem if you want to test elements say for + example you expect to be testing integer equality but the values have + been coerced to floats. + Ideally then we need to ensure that all equivalent column types are by + default the least generic dtype that can contain all possible values + that can be seen in the column, i.e. if NaNs are possible then even + when not present, a column of integers that can contain NaNs should + always be at least float. -def raise_if_not_ok(response): - """ + dtypes and element types: + It seems that coercion to certain dtypes alters the element types too. + For instance, int64 -> float64 will make an equivalent change to + individual value types. However, the original element types can be + preserved with the generic `object` dtype, so this will be used in + preference for integer columns that can contain NaNs. - :param response: + :param table: pandas DataFrame + :param col_type_dict: (dict) optional defines common types + :param nan_value_dict: (dict) optional new value passed to replace NaNs + :param replace_value_dict: (dict) optional new value passed to replace + specific values + :return: modified pandas DataFrame + (the table with the same data, but normalised column types) """ - if not response.ok: - response.raise_for_status() + for col in table: + if col_type_dict is not None and col in col_type_dict: + try: + table[col] = table[col].astype(col_type_dict[col]) + except (ValueError, KeyError, TypeError): + # probably there are some NaNs in there + # and it is impossible to coerce the column to the + # pre-defined dtype + pass + if nan_value_dict is not None and col in nan_value_dict: + if table[col].isnull().any().any(): + table[col] = table[col].fillna(nan_value_dict[col]) + if replace_value_dict is not None and col in replace_value_dict: + table[col] = table[col].replace(replace_value_dict[col][0], + replace_value_dict[col][1]) -def _pdb_uniprot_sifts_mapping(identifier): - """ - Queries the PDBe API for SIFTS mapping between PDB - UniProt. - One to many relationship expected. + return table - :param identifier: PDB id - :return: pandas table dataframe + +def exclude_columns(table, excluded=()): """ + Helper method that helps in filtering out columns based + on the column name. - sifts_endpoint = 'mappings/uniprot/' - url = defaults.api_pdbe + sifts_endpoint + identifier - information = get_url_or_retry(url, json=True) + :param table: pandas DataFrame + :param excluded: (tuple) optional columns to be excluded + :return: modified pandas DataFrame + """ - rows = [] - for uniprot in information[identifier]['UniProt']: - uniprots = {'uniprot_id': uniprot} - rows.append(uniprots) - return pd.DataFrame(rows) + if excluded is not None: + assert hasattr(excluded, '__iter__') + try: + table = table.drop(list(excluded), axis=1) + except ValueError: + # most likely theses are not in there + pass + return table -def _uniprot_pdb_sifts_mapping(identifier): +def splitting_up_by_key(table, key="xrefs_id"): """ - Queries the PDBe API for SIFTS mapping between UniProt - PDB entries. - One to many relationship expected. + Helper method that splits the rows containing + multi-value entries (e.g. [ID_1, ID_2]), according + to the 'key' passed to the function. - :param identifier: UniProt ID - :return: pandas table dataframe + :param table: pandas DataFrame + :param key: key to base the 'split up' upon + :return: modified pandas DataFrame """ - sifts_endpoint = 'mappings/best_structures/' - url = defaults.api_pdbe + sifts_endpoint + str(identifier) - information = get_url_or_retry(url, json=True) - rows = [] - for entry in information[identifier]: - rows.append(entry) - return pd.DataFrame(rows) - + for ix in table.index: + entries = {k: table.loc[ix, k] for k in list(table)} + val = table.loc[ix, key] + if type(val) is tuple or type(val) is list: + for v in val: + nentries = copy.deepcopy(entries) + nentries[key] = v + rows.append(nentries) + else: + rows.append(entries) -def icgc_missense_variant(ensembl_gene_id): - """Fetch a gene missense variants from ICGC data portal. + new_table = pd.DataFrame(rows) - :param str ensembl_gene_id: ensembl gene accession - :return pd.DataFrame: DataFrame with one mutation per row. - :example: + return new_table.reset_index(drop=True) - >>> table = icgc_missense_variant('ENSG00000012048') - >>> table.loc[0, ['id', 'mutation', 'type', 'start']] - id MU601299 - mutation G>A - type single base substitution - start 41245683 - Name: 0, dtype: object - .. note:: ICGC doc https://dcc.icgc.org/docs/#!/genes/findMutations_get_8 +def merging_down_by_key(table, key="xrefs_id"): """ - base_url = defaults.api_icgc + ensembl_gene_id + "/mutations/" - headers = {'content-type': 'application/json'} - filt = json.dumps({"mutation": {"consequenceType": {"is": ['missense_variant']}}}) - params = {"filters": filt} - - # First counts the number of mutation entries - counts_resp = requests.get(base_url + "counts/", headers=headers, params=params) - raise_if_not_ok(counts_resp) - total = counts_resp.json()['Total'] - - # then iterate the pages of entries, max 100 entries per page - hits = [] - params['size'] = 100 - for i in range(total // 100 + 1): - params['from'] = i * 100 + 1 - mutation_resp = requests.get(base_url, headers=headers, params=params) - raise_if_not_ok(mutation_resp) - hits.extend(mutation_resp.json()['hits']) - - return pd.DataFrame(hits) - - -def is_valid(identifier, database=None, url=None): + Helper method that mergers the rows containing data + that have the same value (e.g. ID), according + to the 'key' passed to function. + This works as a collapse down (from many-to-one rows). + Aggregation is possible since multi-value cells are stored as + tuples which are hashable. + + :param table: pandas DataFrame + :param key: key to base the 'merge down' upon + :return: modified pandas DataFrame """ - Generic method to check if a given id is valid. - :param url: if given use this instead - :param identifier: accession id - :param database: database to test against - :return: simply a true or false - :rtype: boolean + new_table = table.copy() + duplicated = {} + drop_indexes = [] + for ix in table.index: + pid = table.loc[ix, key] + dup = table[table[key] == pid].index.tolist() + duplicated[pid] = dup + if len(dup) > 1: + drop_indexes.append(ix) + + new_table = new_table.drop(new_table.index[drop_indexes]) + for key, val in duplicated.items(): + if type(val) is list and len(val) > 1: + rows = [] + d = {} + for i in range(len(list(table))): + values = [] + for j in range(len(val)): + v = table.loc[val[j], list(table)[i]] + if v not in values: + if type(v) is tuple or type(v) is list: + for g in v: + values.append(g) + else: + values.append(v) + if not values: + values = np.nan + elif len(values) == 1: + values = values[0] + else: + values = [v for v in values if not pd.isnull(v)] + if not values: + values = np.nan + elif len(values) == 1: + values = values[0] + else: + values = tuple(set(values)) + + d[list(table)[i]] = values + rows.append(d) + combined = pd.DataFrame(rows) + new_table = new_table.append(combined) + + return new_table.reset_index(drop=True) + + +def flatten_nested_structure(data, dictionary, keys=None, values=None): """ - - try: - identifier = str(identifier) - except ValueError: - # raise IDNotValidError - return False - - if len(str(identifier)) < 1: - # raise IDNotValidError - return False - if not url: - url = getattr(defaults, 'api_' + database) + identifier - r = requests.get(url) - if not r.ok: - # not the best approach - try: - raise IDNotValidError('{} not found at {}: (url check:{}'.format( - identifier, database, r.url)) - except IDNotValidError: - return False + Flattens a deeply nested json structure to unique columns (keys), + where columns with multiple values are aggregated to the same column, + and the items grouped by order in a list. Also copes with + + :param data: json.load() content + :param dictionary: mutable dictionary + :param keys: dict keys (used during recursion) + :param values: dict values (used during recursion) + :return: (side-effects) updates an input dictionary + """ + if type(data) is tuple or type(data) is list: + for e in data: + flatten_nested_structure(e, dictionary, keys, values) + elif type(data) is dict: + for k, v in data.items(): + if keys is not None: + k = '_'.join([keys, k]) + flatten_nested_structure(v, dictionary, k, v) else: - return True + if keys is not None and values is not None: + if keys not in dictionary: + dictionary[keys] = [values] + else: + if values not in dictionary[keys]: + dictionary[keys].append(values) -def is_valid_ensembl_id(identifier, species='human', variant=False): +def refactor_key_val_singletons(dictionary): """ - Checks if an Ensembl id is valid. + Simply updates a dictionary values that are singletons + i.e. len(val) == 1: - :param identifier: testing ID - :param species: Ensembl species - :param variant: boolean if True uses the variant endpoint - :return: simply a true or false - :rtype: boolean + :param dictionary: mutable dictionary + :return: updated dictionary """ + new_dictionary = {} + for k, v in dictionary.items(): + if (type(v) is list or type(v) is tuple) and len(v) == 1: + new_dictionary[k] = v[0] + else: + new_dictionary[k] = v + return new_dictionary - try: - identifier = str(identifier) - except ValueError: - # raise IDNotValidError - return False - if len(str(identifier)) < 1: - # raise IDNotValidError - return False +class InputFileHandler(object): + """Validates input file paths.""" - if variant: - if species not in valid_ensembl_species_variation: - raise ValueError('Provided species {} is not valid'.format(species)) - ensembl_endpoint = "variation/{}/".format(species) - else: - ensembl_endpoint = "lookup/id/" - try: - if identifier != '': - url = defaults.api_ensembl + ensembl_endpoint + urllib_quote(identifier, safe='') - data = get_url_or_retry(url, json=True) - if 'error' in data: - return False - return True - else: - raise IDNotValidError - except IDNotValidError: - return False - except requests.HTTPError: - return False + def __init__(self, filename): + self.__filename = filename + self.__validate() + def __validate(self): + if not os.path.isfile(self.__filename): + raise IOError("File '%s' not available..." % self.__filename) -def confirm_column_types(table): - """ - Check a table's column types against a defined column name/type dictionary - and correct them if necessary. - :param pd.DataFrame table: A table produced by ProteoFAV - :return pd.DataFrame: the table with the same data, but normalised column types +class OutputFileHandler(object): + """Validates output file paths.""" - .. note:: There are fewer pandas `dtypes` than the corresponding numpy - type, but all numpy types can be accommodated. + def __init__(self, filename, overwrite=False): + self.__filename = filename + self.__overwrite = overwrite + self.__validate() - NaNs and Upcasting: - The upcasting of dtypes on columns that contain NaNs has been an issue and - can lead to inconsistencies between the column types of different - tables that contain equivalent data. E.g., a `merged_table` from a PDB - entry may have NaNs in UniProt_dbResNum and so is cast to float64 - whilst a UniProt variants table will have no NaNs in this field and - so remains int64 by default. The main issue here is that it creates - additional work for merging these tables as the keys must be of the - same type. It's also a problem if you want to test elements say for - example you expect to be testing integer equality but the values have - been coerced to floats. + def __validate(self): + if os.path.exists(self.__filename) and not self.__overwrite: + raise OSError("File '%s' already exists..." % self.__filename) + elif not os.access(os.path.dirname(self.__filename), os.W_OK): + raise OSError("File '%s' cannot be written..." % self.__filename) - Ideally then we need to ensure that all equivalent column types are by - default the least generic dtype that can contain all possible values - that can be seen in the column, i.e. if NaNs are possible then even - when not present, a column of integers that can contain NaNs should - always be at least float. - dtypes and element types: - It seems that coercion to certain dtypes alters the element types too. - For instance, int64 -> float64 will make an equivalent change to - individual value types. However, the original element types can be - preserved with the generic `object` dtype, so this will be used in - preference for integer columns that can contain NaNs. +class Downloader(object): + def __init__(self, url, filename, decompress=False, overwrite=False): + """ + :param filename: (str) Output filename + :param decompress: (boolean) Decompresses the file + :param overwrite: (boolean) Overrides any existing file, if available + """ - """ + self._url = url + self._filename = filename + self._decompress = decompress + self._overwrite = overwrite - # TODO: update this to accomodate the new sifts table headers - column_types_long = { - # SIFTs mappings - 'CATH_dbAccessionId': 'string', - 'CATH_dbChainId': 'string', - 'CATH_dbCoordSys': 'string', - 'CATH_dbResName': 'string', - 'CATH_dbResNum': 'string', - 'InterPro_dbAccessionId': 'string', - 'InterPro_dbCoordSys': 'string', - 'InterPro_dbEvidence': 'string', - 'InterPro_dbResName': 'string', - 'InterPro_dbResNum': 'string', - 'NCBI_dbAccessionId': 'string', - 'NCBI_dbCoordSys': 'string', - 'NCBI_dbResName': 'string', - 'NCBI_dbResNum': 'string', - 'PDB_dbAccessionId': 'string', - 'PDB_dbChainId': 'string', - 'PDB_dbCoordSys': 'string', - 'PDB_dbResName': 'string', - 'PDB_dbResNum': 'string', - 'Pfam_dbAccessionId': 'string', - 'Pfam_dbCoordSys': 'string', - 'Pfam_dbResName': 'string', - 'Pfam_dbResNum': 'string', - 'REF_codeSecondaryStructure': 'string', - 'REF_dbCoordSys': 'string', - 'REF_dbResName': 'string', - 'REF_dbResNum': 'string', - 'REF_nameSecondaryStructure': 'string', - 'UniProt_dbAccessionId': 'string', - 'UniProt_dbCoordSys': 'string', - 'UniProt_dbResName': 'string', - 'UniProt_dbResNum': 'string', - # mmCIF fields - 'auth_asym_id': 'string', - 'auth_atom_id': 'string', - 'auth_comp_id': 'string', - 'auth_seq_id': 'string', - 'B_iso_or_equiv': 'float', - 'B_iso_or_equiv_esd': 'float', - 'Cartn_x': 'float', - 'Cartn_x_esd': 'float', - 'Cartn_y': 'float', - 'Cartn_y_esd': 'float', - 'Cartn_z': 'float', - 'Cartn_z_esd': 'float', - 'label_alt_id': 'string', - 'label_asym_id': 'string', - 'label_atom_id': 'string', - 'label_comp_id': 'string', - 'label_entity_id': 'string', - 'label_seq_id': 'integer', - 'occupancy': 'float', - 'occupancy_esd': 'float', - 'pdbe_label_seq_id': 'integer', - 'pdbx_formal_charge': 'integer', - 'pdbx_PDB_ins_code': 'string', - 'pdbx_PDB_model_num': 'integer', - 'type_symbol': 'string', - 'group_PDB': 'string', - 'id': 'string', - # DSSP - 'chain_id': 'string', - 'aa': 'string', - 'ss': 'string', - 'acc': 'float', - 'phi': 'float', - 'psi': 'float', - # Merged table - 'dssp_aa': 'string', - 'cif_aa': 'string', - 'sifts_aa': 'string', - # UniProt variant table - 'resn': 'string', - 'mut': 'string', - 'disease': 'string', - # UniProt variants table 2 - 'translation': 'string', - 'id': 'string', - 'start': 'string', - 'residues': 'string', - # Derived boolean columns - 'is_expression_tag': 'bool', - 'is_not_observed': 'bool' - } - - type_to_dtype = { - 'string': 'object', - 'float': 'float64', - 'integer': 'int64', - 'bool': 'bool', - 'O': 'object' - } - - type_to_dtype_if_contains_nan = { - 'string': 'object', - 'float': 'float64', - 'integer': 'object', - 'bool': 'object', - 'O': 'object' - } - - # Columns in this dictionary will undergo `.replace(value[0], value[1])` - column_replacements = { - 'Cartn_x_esd': ['?', np.nan], - 'Cartn_y_esd': ['?', np.nan], - 'Cartn_z_esd': ['?', np.nan], - 'occupancy_esd': ['?', np.nan], - 'B_iso_or_equiv_esd': ['?', np.nan] - } - - for column in table: - type_should_be = column_types_long.get(column) - - # Get dtype from column type depending on whether can contain NaN - can_be_nan = True # TODO: Either this should be a test or just get rid of the if block - if can_be_nan: - dtype_should_be = type_to_dtype_if_contains_nan.get(type_should_be) - else: - dtype_should_be = type_to_dtype.get(type_should_be) - - if dtype_should_be is None: - logging.warning('Column `{}` not recognised'.format(column)) - continue - - # Element replacements as required - if column in column_replacements: - to_replace, replacement = column_replacements.get(column) - logging.debug( - 'Replacing {} with {} in column {}'.format(to_replace, replacement, column)) - table[column] = table[column].replace(to_replace, replacement) - - # Coerce column if neccessary - current_dtype = table[column].dtype - if current_dtype != dtype_should_be: - logging.debug('Coercing `{}` to `{}`'.format(column, dtype_should_be)) - table[column] = table[column].astype(dtype_should_be) - - # Now check that the index is the correct type - column = table.index.name - type_should_be = column_types_long.get(column) - dtype_should_be = type_to_dtype_if_contains_nan.get(type_should_be) - if dtype_should_be is None: - logging.warning('Index column `{}` not recognised'.format(column)) - current_dtype = table.index.dtype - if current_dtype != dtype_should_be: - logging.debug('Coercing index `{}` to `{}`'.format(column, dtype_should_be)) - table.index = table.index.astype(dtype_should_be) - return table + if not os.path.exists(self._filename) or self._overwrite: + OutputFileHandler(self._filename, overwrite=self._overwrite) + self._tempfile = tempfile.NamedTemporaryFile().name + OutputFileHandler(self._tempfile, overwrite=self._overwrite) + + self._download() + if self._decompress: + self._uncompress() + + def _download(self): + try: + try: + import urllib.request + from urllib.error import URLError, HTTPError + with urllib.request.urlopen(self._url) as response, \ + open(self._tempfile, 'wb') as outfile: + shutil.copyfileobj(response, outfile) + except (AttributeError, ImportError): + import urllib + urllib.urlretrieve(self._url, self._tempfile) + InputFileHandler(self._tempfile) + with open(self._tempfile, 'rb') as infile, \ + open(self._filename, 'wb') as outfile: + shutil.copyfileobj(infile, outfile) + os.remove(self._tempfile) + except (URLError, HTTPError, IOError, Exception) as e: + log.debug("Unable to retrieve %s for %s", self._url, e) + + def _uncompress(self): + InputFileHandler(self._filename) + with open(self._filename, 'rb') as infile, \ + open(self._tempfile, 'wb') as outfile: + shutil.copyfileobj(infile, outfile) + InputFileHandler(self._tempfile) + with gzip.open(self._tempfile, 'rb') as infile, \ + open(self._filename, 'wb') as outfile: + shutil.copyfileobj(infile, outfile) + os.remove(self._tempfile) + log.info("Decompressed %s", self._filename) + + +class GenericInputs(object): + def __init__(self, identifier=None, filename=None, table=None): + self._identifier = identifier + self._filename = filename + self._table = table + + def _get_identifier(self, identifier=None): + if identifier is None and self._identifier is None: + raise ValueError("An Identifier is needed!") + elif identifier is not None: + self._identifier = identifier + return self._identifier + + def _get_filename(self, filename=None): + if filename is None and self._filename is None: + raise ValueError("A filename is needed!") + elif filename is not None: + self._filename = filename + return self._filename + + def _get_table(self, table=None): + if table is None and self._table is None: + raise ValueError("A Pandas DataFrame is needed!") + elif table is not None: + self._table = table + return self._table if __name__ == '__main__': diff --git a/proteofav/validation.py b/proteofav/validation.py new file mode 100644 index 0000000..84a4c39 --- /dev/null +++ b/proteofav/validation.py @@ -0,0 +1,210 @@ +# -*- coding: utf-8 -*- + +import os +import logging +import numpy as np +import pandas as pd +from lxml import etree + +from proteofav.config import defaults +from proteofav.utils import (row_selector, constrain_column_types, + exclude_columns, Downloader, GenericInputs) +from proteofav.library import validation_types + +log = logging.getLogger('proteofav.config') + +__all__ = ['parse_validation_residues', 'select_validation', + 'filter_validation', 'download_validation', 'Validation'] + + +def parse_validation_residues(filename, excluded_cols=None, global_parameters=False, + fix_label_alt_id=True, fix_ins_code=True): + """ + Parse the PDB's validation file to a pandas DataFrame. + + :param filename: path to the Validation file + :param excluded_cols: list of columns to be excluded + :param global_parameters: bool + :param fix_label_alt_id: boolean + :param fix_ins_code: boolean + :return: returns a pandas DataFrame + """ + + tree = etree.parse(filename) + root = tree.getroot() + if global_parameters: + global_parameters = root.find('Entry').attrib + log.info(global_parameters) + rows = [] + header = set() + for i, elem in enumerate(root.iterfind('ModelledSubgroup')): + rows.append(dict(elem.attrib)) + header.update(rows[-1].keys()) + for row in rows: + not_in = {k: None for k in header.difference(row.keys())} + row.update(not_in) + + table = pd.DataFrame(rows, columns=header) + + # column renaming + table.columns = ["validation_" + name for name in table.columns] + + # fixes the 'icode' + if fix_ins_code: + table = _fix_pdb_ins_code(table) + # fixes the 'altcode + if fix_label_alt_id: + table = _fix_label_alt_id(table) + + # exclude columns + table = exclude_columns(table, excluded=excluded_cols) + + # enforce some specific column types + table = constrain_column_types(table, col_type_dict=validation_types) + # replace 'NoneTypes' by NaNs + table.fillna(value=np.nan, inplace=True) + + if table.empty: + log.error('Validation file {} resulted in a empty Dataframe'.format(filename)) + raise ValueError('Validation file {} resulted in a empty Dataframe'.format( + filename)) + return table + + +def _fix_pdb_ins_code(table): + """ + Utility that fixes the 'pdbx_PDB_ins_code' column to match what is expected + in the mmCIF format. + + :param table: pandas DataFrame object + :return: returns a modified pandas DataFrame + """ + + table['validation_icode'] = table['validation_icode'].str.replace('\ |', '?') + table['validation_icode'] = table['validation_icode'].fillna('?').astype(str) + return table + + +def _fix_label_alt_id(table): + """ + Utility that fixes the 'label_alt_id' column to match what is + expected in the mmCIF format. + + :param table: pandas DataFrame object + :return: returns a modified pandas DataFrame + """ + + table['validation_altcode'] = table['validation_altcode'].str.replace('\ |\?', '.') + table['validation_altcode'] = table['validation_altcode'].fillna('.').astype(str) + return table + + +def _add_validation_res_full(table): + """ + Utility that adds a new column to the table. + Adds a new column with the 'full res' (i.e. seq_id + ins_code). + + :param table: pandas DataFrame object + :return: returns a modified pandas DataFrame + """ + + # adds both 'label' and 'auth' entries + if 'validation_resnum' in table and 'validation_icode' in table: + table['validation_resnum_full'] = (table['validation_resnum'] + + table['validation_icode'].str.replace('?', '')) + return table + + +def select_validation(identifier, excluded_cols=None, overwrite=False, **kwargs): + """ + Produces table from PDB validation XML file. + + :param identifier: PDB/mmCIF accession ID + :param excluded_cols: option to exclude mmCIF columns + :param overwrite: boolean + :return: returns a pandas DataFrame + """ + filename = os.path.join(defaults.db_validation, + "{}_validation.xml".format(identifier)) + + download_validation(identifier=identifier, filename=filename, + overwrite=overwrite) + + table = parse_validation_residues(filename=filename, excluded_cols=excluded_cols) + + table = filter_validation(table, excluded_cols=excluded_cols, **kwargs) + table = constrain_column_types(table, col_type_dict=validation_types) + return table + + +def filter_validation(table, excluded_cols=None, chains=None, res=None, + add_res_full=True): + """ + Filter for Validation Pandas Dataframes. + + :param table: pandas DataFrame object + :param excluded_cols: option to exclude Validation columns + :param chains: (tuple) chain IDs or None + :param res: (tuple) res IDs or None + :param add_res_full: option to extend the table with 'res_full' + :return: returns a pandas DataFrame + """ + + # selections / filtering + # excluding columns + table = exclude_columns(table, excluded=excluded_cols) + + # table modular extensions or selections + if add_res_full: + table = _add_validation_res_full(table) + log.info("Validation added full res (res + ins_code)...") + + # excluding rows + if chains is not None: + table = row_selector(table, 'validation_chain', chains) + log.info("Validation table filtered by CHAIN...") + + if res is not None: + table = row_selector(table, 'validation_resnum', res) + log.info("Validation table filtered by RES...") + + if table.empty: + raise ValueError("The filters resulted in an empty DataFrame...") + return table + + +def download_validation(identifier=None, filename=None, overwrite=False): + """ + Downloads a Validation Data XML from the PDBe. + + :param identifier: (str) PDB accession ID + :param filename: path to the Validation file + :param overwrite: (boolean) + :return: (side effects) output file path + """ + + url_root = defaults.validation_fetch + url_endpoint = "{}_validation.xml".format(identifier) + url = url_root + url_endpoint + Downloader(url=url, filename=filename, + decompress=False, overwrite=overwrite) + + +class Validation(GenericInputs): + def read(self, filename=None, **kwargs): + filename = self._get_filename(filename) + self.table = parse_validation_residues(filename=filename, **kwargs) + return self.table + + def download(self, identifier=None, filename=None, **kwargs): + identifier = self._get_identifier(identifier) + filename = self._get_filename(filename) + return download_validation(identifier=identifier, filename=filename, **kwargs) + + def select(self, identifier=None, **kwargs): + identifier = self._get_identifier(identifier) + self.table = select_validation(identifier=identifier, **kwargs) + return self.table + + +Validation = Validation() diff --git a/proteofav/variants.py b/proteofav/variants.py index 667fb84..66bb5e0 100644 --- a/proteofav/variants.py +++ b/proteofav/variants.py @@ -1,191 +1,342 @@ -#!/usr/bin/env python # -*- coding: utf-8 -*- -from __future__ import absolute_import -import logging +import json +import logging +import requests import pandas as pd +from io import BytesIO +from io import StringIO from pandas.io.json import json_normalize +from proteofav.annotation import select_annotation +from proteofav.utils import (fetch_from_url_or_retry, row_selector, + constrain_column_types, exclude_columns, GenericInputs, + flatten_nested_structure, refactor_key_val_singletons, + splitting_up_by_key, merging_down_by_key) +from proteofav.library import (valid_ensembl_species, uni_ens_var_types, + update_ensembl_to_uniprot) + from proteofav.config import defaults -from proteofav.uniprot import (map_gff_features_to_sequence, - _uniprot_to_ensembl_xref, - fetch_uniprot_formal_specie, - fetch_uniprot_sequence, - _uniprot_info) -from proteofav.utils import get_url_or_retry -from proteofav.library import valid_ensembl_species - -__all__ = ["_fetch_icgc_variants", - "_fetch_ebi_variants", - "_fetch_ensembl_variants", - "_sequence_from_ensembl_protein", - "_uniprot_ensembl_mapping", + +log = logging.getLogger('proteofav.config') + +__all__ = ["fetch_uniprot_variants", + "fetch_ensembl_variants", + "fetch_ensembl_sequence_from_id", + "fetch_uniprot_ensembl_mapping", + "fetch_ensembl_uniprot_mapping", + "fetch_uniprot_species_from_id", + "fetch_pdb_uniprot_mapping", + "fetch_uniprot_pdb_mapping", + "get_ensembl_species_from_uniprot", + "get_uniprot_id_from_mapping", + "get_ensembl_protein_id_from_mapping", + "get_preferred_uniprot_id_from_mapping", + "get_preferred_ensembl_id_from_mapping", "_match_uniprot_ensembl_seq", "_apply_sequence_index_map", "_compare_sequences", "_count_mismatches", + "fetch_uniprot_sequence", + "fetch_uniprot_formal_specie", "select_variants", + "flatten_uniprot_variants_ebi", + "flatten_ensembl_variants", + "Variants", "parse_uniprot_variants", - "select_uniprot_variants"] -log = logging.getLogger('proteofav.config') + "select_uniprot_variants", + "icgc_missense_variant", + "_fetch_icgc_variants"] -############################################################################## -# Private methods -############################################################################## - -def _fetch_icgc_variants(identifier): - """ - Queries the ICGC data portal for the PanCancer variants based on Ensembl - transcript identifier. - :param str identifier: Ensembl transcript - :return pandas.DataFrame: pandas table dataframe +def fetch_uniprot_variants(identifier, retry_in=(429,)): """ - transition_regex = '(?P[A-Z])(?P[0-9]+)(?P[A-Z\*])?' - variation_endpoint = "protein/" - url = defaults.api_icgc + variation_endpoint + identifier - # fetches a nested json - # normalise the data, making it flat - data = get_url_or_retry(url, json=True) - data = pd.io.json.json_normalize( - data['hits'], - ['transcripts'], - ['affectedDonorCountTotal', 'id', 'mutation'], meta_prefix='_') - data = data[data['id'] == identifier] - data.drop(['id'], axis=1, inplace=True) - data.rename(columns={'_id': 'id'}, inplace=True) - - consequence = data.pop('consequence') - if consequence.index.duplicated().any(): # pragma: no cover - log.warning('Joining ICGC variant data with its consequences data aborted:' - ' Duplicated index for {}.'.format(identifier)) - else: - data = data.join(consequence.apply(pd.Series), rsuffix='_protein') - transition = data.aaMutation.str.extract(transition_regex) - data = data.join(transition) - - return data + Queries the EBI Proteins API for variants based on + UniProt identifiers (e.g. O15294). + JSON structure flattening is sorted out in another helper + function. -def _fetch_ebi_variants(uniprot_idd, flat_xrefs=True): - """ - Fetchs the variant data from EBI. This datasource is also used in the UniProt feature viewer - :param bool flat_xrefs: whether to parse or not the cross-reference field that indicates - data provenance. - :param uniprot_idd: UniProt accession - :return pd.DataFrame: the table where each row is associated with a variation entry - .. note:: - if flat_xrefs is true multiple rows are produced with the same index to + :param identifier: UniProt ID + :param retry_in: http code for retrying connections + :return: Requests response object """ - endpoint = "variation/" - url = defaults.api_ebi_uniprot + endpoint + uniprot_idd - data = get_url_or_retry(url, json=True) - data = json_normalize(data, ['features'], meta=['accession', 'entryName']) - - # flatten the xref field, which has the id column. - # ideally this could be normalised with: - # table = json_normalize(data, ['features', 'xref'] ... - # but this field is not present in all entries, - if flat_xrefs: - flat_xref = data['xrefs'].apply(pd.Series).stack().apply(pd.Series) - flat_xref.reset_index(level=1, drop=True, inplace=True) - data = data.join(flat_xref) - return data + url_root = defaults.api_proteins + url_endpoint = "variation/{}".format(identifier) + url = url_root + url_endpoint + response = fetch_from_url_or_retry(url=url, json=True, retry_in=retry_in) + return response -def _fetch_ensembl_variants(ensembl_ptn_id, feature=None): - """Queries the Ensembl API for germline variants (mostly dbSNP) and somatic +def fetch_ensembl_variants(identifier, feature=None, retry_in=(429,)): + """ + Queries the Ensembl API for germline variants (mostly dbSNP) and somatic (mostly COSMIC) based on Ensembl Protein identifiers (e.g. ENSP00000326864). - :param ensembl_ptn_id: Ensembl accession to a protein: ENSP00000XXXXXX - :return: table[Parent: str, - allele§: str, - clinical_significance: list, - codons: str, - end: int, - feature_type: str, - id: str, - minor_allele_frequency: float , - polyphen: float, - residues: str, - seq_region_name: str, - sift: float, - start: int, - translation: str, - type: str ] - :rtype: pandas.DataFrame + :param identifier: Ensembl Protein ID + :param feature: variation type + :param retry_in: http code for retrying connections + :return: Requests response object """ - ensembl_endpoint = "overlap/translation/" + + url_root = defaults.api_ensembl + url_endpoint = "overlap/translation/{}".format(identifier) supported_feats = ['transcript_variation', 'somatic_transcript_variation'] if feature is None: raise NotImplementedError('Use two functions call to get both somatic' ' and germline variants.') - # params = {'feature': supported_feats, - # 'type': 'missense_variant'} elif feature not in supported_feats: - raise NotImplementedError('feature argument should be one of {} '.format(', '''.join( - supported_feats))) + raise NotImplementedError("Feature argument should be one of '{}'" + "".format("', '".join(supported_feats))) else: params = {'feature': feature} - url = defaults.api_ensembl + ensembl_endpoint + ensembl_ptn_id - - rows = get_url_or_retry(url, json=True, **params) - return pd.DataFrame(rows) + # params = {'feature': feature, + # 'type': 'missense_variant'} + url = url_root + url_endpoint + response = fetch_from_url_or_retry(url, json=True, retry_in=retry_in, **params) + return response -def _sequence_from_ensembl_protein(identifier, protein=True): +def fetch_ensembl_sequence_from_id(identifier, protein=True, retry_in=(429,)): """ - Gets the sequence for an Ensembl identifier. + Queries the Ensembl REST API for the sequence of a Ensembl Protein ID. - :param identifier: Ensembl ID - :return: sequence + :param identifier: Ensembl Protein ID + :param protein: boolean + :param retry_in: http code for retrying connections + :return: Requests response object """ - ensembl_endpoint = "sequence/id/" - url = defaults.api_ensembl + ensembl_endpoint + str(identifier) - header = {'content-type': 'text/plain'} + url_root = defaults.api_ensembl + url_endpoint = "sequence/id/{}".format(identifier) + url = url_root + url_endpoint if protein: params = {'type': 'protein'} else: params = {} + response = fetch_from_url_or_retry(url=url, json=True, + retry_in=retry_in, **params) + return response - return get_url_or_retry(url, header=header, **params) - -def _uniprot_ensembl_mapping(identifier, species=None): +def fetch_uniprot_ensembl_mapping(identifier, species='homo_sapiens', retry_in=(429,)): """ - Uses the UniProt mapping service to try and get Ensembl IDs for the - UniProt accession identifier provided + Uses the Ensembl REST mapping service to try and get Ensembl IDs for + the UniProt accession identifier provided. :param identifier: UniProt accession identifier + :param retry_in: http code for retrying connections :param species: Ensembl species - :return: pandas table dataframe + :return: Requests response object """ if species not in valid_ensembl_species: raise ValueError('Provided species {} is not valid'.format(species)) - information = {} - rows = [] + url_root = defaults.api_ensembl + url_endpoint = "xrefs/symbol/{}/{}".format(species, identifier) + url = url_root + url_endpoint + + response = fetch_from_url_or_retry(url=url, json=True, retry_in=retry_in) + return response + - ensembl_endpoint = "xrefs/symbol/{}/".format(species) - url = defaults.api_ensembl + ensembl_endpoint + str(identifier) - data = get_url_or_retry(url, json=True) +def fetch_ensembl_uniprot_mapping(identifier, retry_in=(429,)): + """ + Uses the Ensembl REST mapping service to try and get UniProt IDs for + the Ensembl Protein accession identifier provided. + + :param identifier: Ensembl Protein accession identifier + :param retry_in: http code for retrying connections + :return: Requests response object + """ + + url_root = defaults.api_ensembl + url_endpoint = "xrefs/id/{}".format(identifier) + url = url_root + url_endpoint + # params = {'external_db': "Uniprot/SWISSPROT"} + # params = {'external_db': "Uniprot/SPTREMBL"} + + response = fetch_from_url_or_retry(url=url, json=True, retry_in=retry_in) + return response + + +def fetch_uniprot_species_from_id(identifier, retry_in=(429,)): + """ + Retrieve Species from UniProt ID. + + :param identifier: UniProt accession identifier + :param retry_in: http code for retrying connections + :return: Requests response object + """ + + url_root = defaults.api_uniprot + url_endpoint = "?query={}&columns=organism&format=tab".format(identifier) + url = url_root + url_endpoint + response = fetch_from_url_or_retry(url=url, json=False, retry_in=retry_in) + return response + + +def fetch_pdb_uniprot_mapping(identifier, retry_in=(429,)): + """ + Queries the PDBe API for SIFTS mapping between PDB - UniProt. + One to many relationship expected. + + :param identifier: PDB accession identifier + :param retry_in: http code for retrying connections + :return: Requests response object + """ + + sifts_endpoint = 'mappings/uniprot/{}'.format(identifier) + url = defaults.api_pdbe + sifts_endpoint + response = fetch_from_url_or_retry(url, json=True, retry_in=retry_in) + return response + + +def fetch_uniprot_pdb_mapping(identifier, retry_in=(429,)): + """ + Queries the PDBe API for SIFTS mapping between UniProt - PDB entries. + One to many relationship expected. + + :param identifier: UniProt accession identifier + :param retry_in: http code for retrying connections + :return: Requests response object + """ + sifts_endpoint = 'mappings/best_structures/{}'.format(identifier) + url = defaults.api_pdbe + sifts_endpoint + response = fetch_from_url_or_retry(url, json=True, retry_in=retry_in) + return response + + +def get_ensembl_species_from_uniprot(data): + """ + Gets a Species Name from a UniProt organism lookup. + + :param data: Request object from the UniProt Query endpoint. + :return: (str) formatted species name + """ + organism = str(data.content, encoding='utf-8').split('\n')[1] + species = '_'.join(organism.split()[0:2]).lower() + return species + + +def get_ensembl_protein_id_from_mapping(data): + """ + Gets a list of Ensembl IDs from a 'xrefs/symbol/' mapping. + + :param data: Requests object from the Ensembl-UniProt Mapping + :return: list of Ensembl Protein IDs + """ + ensps = [] for entry in data: - typ = entry['type'].upper() - eid = entry['id'] - try: - if eid in information[typ]: - continue - information[typ].append(eid) - except KeyError: - information[typ] = eid - except AttributeError: - information[typ] = [information[typ]] - information[typ].append(eid) + if 'type' in entry and 'id' in entry: + if entry['type'] == 'translation': + if entry['id'] not in ensps: + ensps.append(entry['id']) + return ensps - rows.append(information) - return pd.DataFrame(rows) + +def get_uniprot_id_from_mapping(data, full_entry=False, uniprot_id=None): + """ + Gets a list of UniProt IDs from a '"xrefs/id/"' mapping. + + :param data: Requests object from the Ensembl-UniProt Mapping + :param full_entry: (boolean) if True gets dictionary instead of just + the UniProt IDs + :param uniprot_id: if not None means that we want the data for a specific + UniProt ID + :return: list of UniProt IDs + """ + uniprots = [] + for entry in data: + if 'dbname' in entry and 'primary_id' in entry: + if uniprot_id is not None and entry['primary_id'] == uniprot_id: + if full_entry: + uniprots = [entry] + else: + uniprots = [entry['primary_id']] + break + elif entry['dbname'] == 'Uniprot/SWISSPROT': + if entry['primary_id'] not in uniprots: + if full_entry: + uniprots.append(entry) + else: + uniprots.append(entry['primary_id']) + elif entry['dbname'] == 'Uniprot/SPTREMBL': + if entry['primary_id'] not in uniprots: + if full_entry: + uniprots.append(entry) + else: + uniprots.append(entry['primary_id']) + return uniprots + + +def get_preferred_uniprot_id_from_mapping(data): + """ + Takes a list of Ensembl xrefs/ids mapped from a UniProt ID + and gets the preferred entry (Many-to-one), based on seq + identity and coverage. + + :param data: list of dictionaries + :return: (str) preferred UniProt ID + """ + + best_match = None + curr_ix = -1 + prev_identity = 0 + prev_coverage = 0 + prev_id = "-" * 100 + for ix, entry in enumerate(data): + if ('ensembl_identity' in entry and 'xref_identity' in entry and + 'xref_start' in entry and 'xref_end' in entry): + identity = entry['ensembl_identity'] + entry['xref_identity'] + coverage = entry['xref_end'] - entry['xref_start'] + if identity + coverage >= prev_identity + prev_coverage: + prev_identity = identity + prev_coverage = coverage + # preferring the smallest UniProt ID (for getting variants) + if len(entry['primary_id']) < len(prev_id): + prev_id = entry['primary_id'] + curr_ix = ix + if curr_ix != -1 and 'primary_id' in data[curr_ix]: + best_match = data[curr_ix]['primary_id'] + return best_match + + +def get_preferred_ensembl_id_from_mapping(identifiers, uniprot_id=None): + """ + Takes a list of Ensembl xrefs/ids mapped from a UniProt ID + and gets the preferred entry (Many-to-one), based on seq + identity and coverage. + + :param identifiers: list of Ensembl IDs + :param uniprot_id: if not None means that we want the data for a specific + UniProt ID + :return: (str) preferred Ensembl ID + """ + + best_match = None + curr_ix = -1 + prev_identity = 0 + prev_coverage = 0 + for ix, ensp in enumerate(identifiers): + info = fetch_ensembl_uniprot_mapping(ensp).json() + # gets the mapping for a specific uniprot + data = get_uniprot_id_from_mapping(info, full_entry=True, + uniprot_id=uniprot_id) + for entry in data: + if ('ensembl_identity' in entry and 'xref_identity' in entry and + 'xref_start' in entry and 'xref_end' in entry): + + identity = entry['ensembl_identity'] + entry['xref_identity'] + coverage = entry['xref_end'] - entry['xref_start'] + if identity + coverage > prev_identity + prev_coverage: + prev_identity = identity + prev_coverage = coverage + curr_ix = ix + if curr_ix != -1: + best_match = identifiers[curr_ix] + return best_match def _match_uniprot_ensembl_seq(uniprot_id): @@ -206,8 +357,8 @@ def _match_uniprot_ensembl_seq(uniprot_id): raise ValueError('{} is not a valid Ensembl specie ({}).'.format( species, uniprot_id)) # we remove the isoform identifier to xref to ensembl, but keep it while checking the seq - ensembl_xref = _uniprot_to_ensembl_xref(uniprot_id.split('-')[0], - species=species) + ensembl_xref = pd.DataFrame(fetch_uniprot_ensembl_mapping(uniprot_id.split('-')[0], + species=species).json()) if ensembl_xref.empty: raise ValueError('No cross-reference found for {} Ensembl mapping.'.format( @@ -217,7 +368,7 @@ def _match_uniprot_ensembl_seq(uniprot_id): uniprot_sequence = fetch_uniprot_sequence(uniprot_id) for ensembl_ptn_id in ensembl_ptn_ids: - ensembl_ptn_seq = _sequence_from_ensembl_protein(ensembl_ptn_id) + ensembl_ptn_seq = fetch_ensembl_sequence_from_id(ensembl_ptn_id) if _compare_sequences(uniprot_sequence, ensembl_ptn_seq, permissive=False): return ensembl_ptn_id raise ValueError('No protein with the same sequence was retrieved from Ensembl {}'.format( @@ -272,62 +423,280 @@ def _count_mismatches(sequence1, sequence2): return sum(i != j for i, j in zip(sequence1, sequence2)) +def fetch_uniprot_sequence(uniprot_id): + """ + Gets current sequence of a Uniprot entry. + + :param str uniprot_id: Uniprot accession + :return str: the sequence + + >>> print(fetch_uniprot_formal_specie('P17612')) + Homo sapiens + """ + + return _uniprot_info(uniprot_id, cols='sequence').iloc[0, 1] + + +def fetch_uniprot_formal_specie(uniprot_id, remove_isoform=True): + """ + Gets the species name of an organism expressing a protein. + + :param Bool remove_isoform: whether to remove the isoform identifier. + :param str uniprot_id: Uniprot accession + :return: the species name (two words) + :rtype: str or None + + >>> print(fetch_uniprot_sequence('P17612'))[:20] + MGNAAAAKKGSEQESVKEFL + """ + if remove_isoform: + uniprot_id = uniprot_id.split('-')[0] + + full_specie = _uniprot_info(uniprot_id, cols='organism').iloc[0, 1] + + try: + return " ".join(full_specie.split()[0:2]) + except AttributeError: + log.error('Could not retrieve {} information. Maybe obsolete ' + 'UniProt accession?'.format(uniprot_id)) + return None + + +def _uniprot_info(uniprot_id, retry_in=(503, 500), cols=None): + """ + Retrieve Uniprot information from the database. + + :param str uniprot_id: Uniprot accession identifier + :param retry_in: iterable of status_code to be retried upon error. + :type retry_in: list of [int] + :return pandas.DataFrame: table from Uniprot. + Default table columns: + :raises requests.HTTPError: when hits a bad status_code + """ + + if not cols: + cols = ('id', 'entry name', 'reviewed', 'protein names', 'genes', 'organism', + 'sequence', 'length') + elif isinstance(cols, str): + cols = ('id', cols) + + params = {'query': 'accession:' + str(uniprot_id), + 'columns': ",".join(cols), + 'format': 'tab', + 'contact': ""} + url = defaults.api_uniprot + response = fetch_from_url_or_retry(url=url, retry_in=retry_in, **params).content + try: + data = pd.read_table(StringIO(response)) + except TypeError: + # python 3.5 + data = pd.read_table(BytesIO(response)) + except ValueError as e: + log.error(e) + return None + # id column is called Entry in the table + return row_selector(data, 'Entry', uniprot_id) + + ############################################################################## # Public methods ############################################################################## -def select_variants(uniprot_id, features=('uniprot', 'ensembl_somatic', 'ensembl_germline')): +def select_variants(identifier, id_source=None, synonymous=True, uniprot_vars=True, + ensembl_germline_vars=True, ensembl_somatic_vars=True): + """ + Aggregates Variants from UniProt Proteins API and Ensembl REST API. + + :param identifier: UniProt or Ensembl Protein ID + :param id_source: either 'uniprot' or 'ensembl' + :param synonymous: boolean + :param uniprot_vars: boolean + :param ensembl_germline_vars: boolean + :param ensembl_somatic_vars: boolean + :return: Pandas DataFrame """ + uni_vars, germ_vars, som_vars = fetch_variants(identifier, id_source, + synonymous, uniprot_vars, + ensembl_germline_vars, + ensembl_somatic_vars) + + if isinstance(germ_vars, pd.DataFrame) and isinstance(som_vars, pd.DataFrame): + ens_vars = pd.concat([germ_vars, som_vars]).reset_index(drop=True) + elif isinstance(germ_vars, pd.DataFrame): + ens_vars = germ_vars + elif isinstance(som_vars, pd.DataFrame): + ens_vars = som_vars + else: + ens_vars = None - :param features: - :param uniprot_id: + return uni_vars, ens_vars + + +def fetch_variants(identifier, id_source=None, synonymous=True, uniprot_vars=True, + ensembl_germline_vars=False, ensembl_somatic_vars=False): """ - ensembl_ptn_id = None - tables = [] - # use the uniprot natural variants as our reference (left) table - if 'uniprot' in features: - table_uni = parse_uniprot_variants(uniprot_id) - if not table_uni.empty: - table_uni = table_uni['ids'] - table_uni.name = 'uniprot_variants' - else: - table_uni['uniprot_variants'] = None + Fetches Variants from UniProt Proteins API and Ensembl REST API. + + :param identifier: UniProt or Ensembl Protein ID + :param id_source: either 'uniprot' or 'ensembl' + :param synonymous: boolean + :param uniprot_vars: boolean + :param ensembl_germline_vars: boolean + :param ensembl_somatic_vars: boolean + :return: Pandas DataFrame + """ + + supported_sources = ['uniprot', 'ensembl'] + if id_source is None or id_source not in supported_sources: + raise ValueError("The ID source needs to be provided.\n Pass one of " + "'{}'".format("', '".join(supported_sources))) + if id_source == 'uniprot': + uniprot_id = identifier - tables.append(table_uni) + # get best match Ensembl ID + info = fetch_uniprot_species_from_id(identifier) + species = get_ensembl_species_from_uniprot(info) + try: + info = fetch_uniprot_ensembl_mapping(identifier, + species=species).json() + except ValueError: + log.info('Provided species {} is not valid'.format(species)) + return None + ensps = get_ensembl_protein_id_from_mapping(info) + best_match = get_preferred_ensembl_id_from_mapping(ensps, + uniprot_id=identifier) + ensembl_id = best_match + + elif id_source == 'ensembl': + ensembl_id = identifier + + # get best match UniProt ID + info = fetch_ensembl_uniprot_mapping(identifier).json() + data = get_uniprot_id_from_mapping(info, full_entry=True) + best_match = get_preferred_uniprot_id_from_mapping(data) + uniprot_id = best_match + + # return variants + uni_vars = None + germ_vars = None + som_vars = None + + if uniprot_id is not None and uniprot_vars: + r = fetch_uniprot_variants(uniprot_id) + if r is not None: + uni_vars = flatten_uniprot_variants_ebi(r) + + if (ensembl_id is not None and + (ensembl_germline_vars or ensembl_somatic_vars)): + + if ensembl_germline_vars: + r = fetch_ensembl_variants(ensembl_id, + feature='transcript_variation') + if r is not None: + germ_vars = flatten_ensembl_variants(r, synonymous=synonymous) + + if ensembl_somatic_vars: + r = fetch_ensembl_variants(ensembl_id, + feature='somatic_transcript_variation') + if r is not None: + som_vars = flatten_ensembl_variants(r, synonymous=synonymous) + + return uni_vars, germ_vars, som_vars + + +def flatten_uniprot_variants_ebi(data, excluded=()): + """ + Flattens the json output obtained from the Proteins API variants + endpoint. + + :param data: original response (json output) + :param excluded: option to exclude VAR columns + :return: returns a pandas DataFrame + """ try: - ensembl_ptn_id = _match_uniprot_ensembl_seq(uniprot_id) + data = data.json() + except AttributeError: + assert type(data) is dict - except ValueError as e: - # No Ensembl mapping - log.error(e) - return pd.concat(tables, axis=1) + var_rows = [] + for entry in data["features"]: + entries = {key: val for key, val in data.items() if key != 'features'} - if 'ensembl_somatic' in features: - table_som = _fetch_ensembl_variants( - ensembl_ptn_id, feature='somatic_transcript_variation') + flatten_nested_structure(entry, entries) + var_rows.append(refactor_key_val_singletons(entries)) - if not table_som.empty: - table_som = table_som[table_som['type'] == 'coding_sequence_variant'] - table_som = table_som.groupby('start')['id'].apply(list) - table_som.name = 'somatic_variants' - else: - table_som['somatic_variants'] = None + table = pd.DataFrame(var_rows) - tables.append(table_som) + # excluding columns + table = exclude_columns(table, excluded=excluded) - if 'ensembl_germline' in features: - table_ger = _fetch_ensembl_variants(ensembl_ptn_id, feature='transcript_variation') + # enforce some specific column types + table = constrain_column_types(table, uni_ens_var_types) - if not table_ger.empty: - table_ger = table_ger[table_ger['type'] == 'missense_variant'] - table_ger = table_ger.groupby('start')['id'].apply(list) - table_ger.name = 'germline_variants' - else: - table_ger['germline_variants'] = None + # split multi id rows + table = splitting_up_by_key(table, key='xrefs_id') + + # merge down multi rows with same id + table = merging_down_by_key(table, key='xrefs_id') + + if table.empty: + raise ValueError('Variants collapsing resulted in an empty DataFrame...') - tables.append(table_ger) + return table + + +def flatten_ensembl_variants(data, excluded=(), synonymous=True): + """ + Flattens the json output obtained from the Proteins API variants + endpoint. - return pd.concat(tables, axis=1) + :param data: original response (json output) + :param excluded: option to exclude VAR columns + :param synonymous: (boolean) + :return: returns a pandas DataFrame + """ + + try: + data = data.json() + except AttributeError: + assert type(data) is dict + + table = pd.DataFrame(data) + # rename columns + table.rename(columns=update_ensembl_to_uniprot, inplace=True) + + # excluding columns + table = exclude_columns(table, excluded=excluded) + + # enforce some specific column types + table = constrain_column_types(table, uni_ens_var_types) + + # split multi id rows + table = splitting_up_by_key(table, key='xrefs_id') + + # merge down multi rows with same id + table = merging_down_by_key(table, key='xrefs_id') + + # filter synonymous + if not synonymous: + table = row_selector(table, key='consequenceType', + value='synonymous_variant', reverse=True) + return table + + +class Variants(GenericInputs): + def fetch(self, identifier=None, **kwargs): + identifier = self._get_identifier(identifier) + uni, germ, som = fetch_variants(identifier=identifier, **kwargs) + return uni, germ, som + + def select(self, identifier=None, **kwargs): + identifier = self._get_identifier(identifier) + uni, ens = select_variants(identifier=identifier, **kwargs) + return uni, ens + + +Variants = Variants() def parse_uniprot_variants(uniprot_id): @@ -344,7 +713,8 @@ def parse_uniprot_variants(uniprot_id): res_transition_group = '(?P[A-Z]+)->(?P[A-Z]+)' ids_group = "\(\[\'([a-zA-Z0-9_]+)\'\]\)" - table = map_gff_features_to_sequence(uniprot_id, query_type='Natural variant') + table = select_annotation(uniprot_id, annotation_agg=True, + query_type='Natural variant') if table.empty: return table @@ -378,7 +748,7 @@ def select_uniprot_variants(identifier, align_transcripts=False): # get the ensembl ids: this also validate this species as available # through ensembl - ens = _uniprot_ensembl_mapping(identifier, species=org) + ens = fetch_uniprot_ensembl_mapping(identifier, species=org) # get the ensembl protein ids ens_pros = ens.loc[0, 'TRANSLATION'] @@ -391,7 +761,7 @@ def select_uniprot_variants(identifier, align_transcripts=False): seq_maps = [] for i, enspro in enumerate(ens_pros): - seq_pro = _sequence_from_ensembl_protein(enspro, protein=True) + seq_pro = fetch_ensembl_sequence_from_id(enspro, protein=True) # validate if the sequence of uniprot and ensembl protein matches if _compare_sequences(seq, seq_pro, permissive=False): @@ -417,8 +787,8 @@ def select_uniprot_variants(identifier, align_transcripts=False): # get the variants for the ensembl proteins that match the uniprot tables = [] for i in usable_indexes: - vars = _fetch_ensembl_variants(ens_pros[i], feature='transcript_variation') - muts = _fetch_ensembl_variants(ens_pros[i], feature='somatic_transcript_variation') + vars = fetch_ensembl_variants(ens_pros[i], feature='transcript_variation') + muts = fetch_ensembl_variants(ens_pros[i], feature='somatic_transcript_variation') # TODO: From... TO... mutated residues as different columns in the table # TODO: Shouldn't the default behaviour return all the columns? @@ -430,8 +800,8 @@ def select_uniprot_variants(identifier, align_transcripts=False): # Get variants from aligned sequences if align_transcripts: for i in aligned_indexes: - vars = _fetch_ensembl_variants(ens_pros[i], feature='transcript_variation') - muts = _fetch_ensembl_variants(ens_pros[i], feature='somatic_transcript_variation') + vars = fetch_ensembl_variants(ens_pros[i], feature='transcript_variation') + muts = fetch_ensembl_variants(ens_pros[i], feature='somatic_transcript_variation') var_table = vars[['translation', 'id', 'start', 'residues']] mut_table = muts[['translation', 'id', 'start', 'residues']] @@ -450,5 +820,83 @@ def select_uniprot_variants(identifier, align_transcripts=False): return table -if __name__ == '__main__': - pass +def raise_if_not_ok(response): + """ + + :param response: + """ + if not response.ok: + response.raise_for_status() + + +def icgc_missense_variant(ensembl_gene_id): + """Fetch a gene missense variants from ICGC data portal. + + :param str ensembl_gene_id: ensembl gene accession + :return pd.DataFrame: DataFrame with one mutation per row. + :example: + + >>> table = icgc_missense_variant('ENSG00000012048') + >>> table.loc[0, ['id', 'mutation', 'type', 'start']] + id MU601299 + mutation G>A + type single base substitution + start 41245683 + Name: 0, dtype: object + + .. note:: ICGC doc https://dcc.icgc.org/docs/#!/genes/findMutations_get_8 + """ + base_url = defaults.api_icgc + ensembl_gene_id + "/mutations/" + headers = {'content-type': 'application/json'} + filt = json.dumps({"mutation": {"consequenceType": {"is": ['missense_variant']}}}) + params = {"filters": filt} + + # First counts the number of mutation entries + counts_resp = requests.get(base_url + "counts/", headers=headers, params=params) + raise_if_not_ok(counts_resp) + total = counts_resp.json()['Total'] + + # then iterate the pages of entries, max 100 entries per page + hits = [] + params['size'] = 100 + for i in range(total // 100 + 1): + params['from'] = i * 100 + 1 + mutation_resp = requests.get(base_url, headers=headers, params=params) + raise_if_not_ok(mutation_resp) + hits.extend(mutation_resp.json()['hits']) + + return pd.DataFrame(hits) + + +def _fetch_icgc_variants(identifier): + """ + Queries the ICGC data portal for the PanCancer variants based on Ensembl + transcript identifier. + :param str identifier: Ensembl transcript + :return pandas.DataFrame: pandas table dataframe + """ + transition_regex = '(?P[A-Z])(?P[0-9]+)(?P[A-Z\*])?' + variation_endpoint = "protein/" + url = defaults.api_icgc + variation_endpoint + identifier + # fetches a nested json + # normalise the data, making it flat + data = fetch_from_url_or_retry(url, json=True).json() + data = pd.io.json.json_normalize( + data['hits'], + ['transcripts'], + ['affectedDonorCountTotal', 'id', 'mutation'], meta_prefix='_') + data = data[data['id'] == identifier] + data.drop(['id'], axis=1, inplace=True) + data.rename(columns={'_id': 'id'}, inplace=True) + + consequence = data.pop('consequence') + if consequence.index.duplicated().any(): # pragma: no cover + log.warning('Joining ICGC variant data with its consequences data aborted:' + ' Duplicated index for {}.'.format(identifier)) + else: + data = data.join(consequence.apply(pd.Series), rsuffix='_protein') + transition = data.aaMutation.str.extract(transition_regex) + data = data.join(transition) + + return data + diff --git a/proteofav/visualise.py b/proteofav/visualise.py index 0da2c5a..35e9598 100644 --- a/proteofav/visualise.py +++ b/proteofav/visualise.py @@ -1,14 +1,12 @@ -#!/usr/bin/env python # -*- coding: utf-8 + """ Created on 18:07 28/02/2017 2017 Methods aiming to integrate ProteoFAV table to viewers such as UFSC Chimera and Jalview. """ -from __future__ import absolute_import -import logging -import os -from proteofav.config import defaults +import os +import logging log = logging.getLogger('proteofav.config') @@ -109,4 +107,4 @@ def write_file(content, filename): # pragma: no cover :param str filename: path to the file """ with open(filename, 'w') as open_file: - open_file.write(content) \ No newline at end of file + open_file.write(content) diff --git a/requirements.txt b/requirements.txt index 2e16f0e..a9542fc 100644 --- a/requirements.txt +++ b/requirements.txt @@ -1,10 +1,11 @@ # This requirements file lists all third-party dependencies for this project. # # Run 'pip install -r requirements.txt' to install these dependencies -# TODO add six -python>=3 -pandas>=0.17 -requests>=2.12 -lxml>=3.6 -click>=6 -scipy + +numpy>=1.13.3 +pandas>=0.20.3 +requests>=2.18.2 +requests_cache>=0.4.13 +responses>=0.8.1 +lxml>=3.7.3 +click>=6.7 diff --git a/setup.py b/setup.py index eed0d51..3d9a8ee 100644 --- a/setup.py +++ b/setup.py @@ -1,24 +1,30 @@ -#!/usr/bin/env python # -*- coding: utf-8 -*- """ -ProteFAV: protein feature aggregation and variants --------------------------------------------------- +ProteoFAV: Protein Feature Aggregation and Variants +--------------------------------------------------- -Exploring the power of Pandas to work with protein structures, -sequences and genetic variants. +Open-source framework for simple and fast integration +of protein structure data with sequence annotations +and genetic variation :copyright: (c) 2015-2017. :license: TBD, see LICENSE for more details. """ - -from setuptools import setup -from setuptools import find_packages +import os +from setuptools import setup, find_packages from proteofav import __version__, __authors__ +def gather_dependencies(): + with open('requirements.txt', 'r') as f_in: + return [l for l in f_in.read().rsplit(os.linesep) + if l and not l.startswith("#")] +DEPENDENCIES = gather_dependencies() + + setup( # Basic package information. name='proteofav', @@ -31,13 +37,8 @@ py_modules=['proteofav.main'], # Package dependencies. - install_requires=['pandas>=0.17', - 'requests>=2.12', - 'lxml>=3.6', - 'click>=6', - 'scipy' - ], - test_requires=['mock', 'python_version>"3.4"'], # + install_requires=DEPENDENCIES, + test_requires=['mock', 'python_version>"3.5"'], # Tests. test_suite='tests', diff --git a/tests/SIFTS/2pm7.xml.gz b/tests/SIFTS/2pm7.xml.gz deleted file mode 100644 index 960aa7d..0000000 Binary files a/tests/SIFTS/2pm7.xml.gz and /dev/null differ diff --git a/tests/SIFTS/3ehk.xml.gz b/tests/SIFTS/3ehk.xml.gz deleted file mode 100644 index 7cb71e6..0000000 Binary files a/tests/SIFTS/3ehk.xml.gz and /dev/null differ diff --git a/tests/SIFTS/3fqd.xml.gz b/tests/SIFTS/3fqd.xml.gz deleted file mode 100644 index f5cdec2..0000000 Binary files a/tests/SIFTS/3fqd.xml.gz and /dev/null differ diff --git a/tests/SIFTS/4abo.xml.gz b/tests/SIFTS/4abo.xml.gz deleted file mode 100644 index 4731686..0000000 Binary files a/tests/SIFTS/4abo.xml.gz and /dev/null differ diff --git a/tests/SIFTS/4v9d.xml.gz b/tests/SIFTS/4v9d.xml.gz deleted file mode 100644 index d7e6dea..0000000 Binary files a/tests/SIFTS/4v9d.xml.gz and /dev/null differ diff --git a/tests/SIFTS/4why.xml.gz b/tests/SIFTS/4why.xml.gz deleted file mode 100644 index 0c55bce..0000000 Binary files a/tests/SIFTS/4why.xml.gz and /dev/null differ diff --git a/tests/__init__.py b/tests/__init__.py index 98f72d7..8b13789 100644 --- a/tests/__init__.py +++ b/tests/__init__.py @@ -1,3 +1 @@ -#!/usr/bin/env python -# -*- coding: utf-8 diff --git a/tests/config.txt b/tests/config.txt deleted file mode 100644 index d7fb5a7..0000000 --- a/tests/config.txt +++ /dev/null @@ -1,6 +0,0 @@ -[Global] -db_mmcif = ... -db_sifts = ... -db_dssp = ... - -[Addresses] diff --git a/tests/test_annotation.py b/tests/test_annotation.py new file mode 100644 index 0000000..532881d --- /dev/null +++ b/tests/test_annotation.py @@ -0,0 +1,125 @@ +# -*- coding: utf-8 -*- + +import os +import sys +import logging +import unittest + +try: + import mock +except ImportError: + import unittest.mock as mock + +from proteofav.annotation import (parse_gff_features, select_annotation, + annotation_aggregation, filter_annotation, + download_annotation, Annotation) + + +class TestUNIPROTParser(unittest.TestCase): + """Test UniProt fetcher/parser methods.""" + + def setUp(self): + """Initialize the framework for testing.""" + + self.uniprotid = "P38995" + self.example_annotation = os.path.join(os.path.dirname(__file__), "testdata", + "annotation", "P38995.gff") + self.output_annotation = os.path.join(os.path.dirname(__file__), "testdata", + "P38995.gff") + self.parse_gff_features = parse_gff_features + self.ccc2_sequence = ("MREVILAVHGMTCSACTNTINTQLRALKGVTKCDISLVTNECQVTYDNEVTADSIKEIIE" + "DCGFDCEILRDSEITAISTKEGLLSVQGMTCGSCVSTVTKQVEGIEGVESVVVSLVTEEC" + "HVIYEPSKTTLETAREMIEDCGFDSNIIMDGNGNADMTEKTVILKVTKAFEDESPLILSS" + "VSERFQFLLDLGVKSIEISDDMHTLTIKYCCNELGIRDLLRHLERTGYKFTVFSNLDNTT" + "QLRLLSKEDEIRFWKKNSIKSTLLAIICMLLYMIVPMMWPTIVQDRIFPYKETSFVRGLF" + "YRDILGVILASYIQFSVGFYFYKAAWASLKHGSGTMDTLVCVSTTCAYTFSVFSLVHNMF" + "HPSSTGKLPRIVFDTSIMIISYISIGKYLETLAKSQTSTALSKLIQLTPSVCSIISDVER" + "NETKEIPIELLQVNDIVEIKPGMKIPADGIITRGESEIDESLMTGESILVPKKTGFPVIA" + "GSVNGPGHFYFRTTTVGEETKLANIIKVMKEAQLSKAPIQGYADYLASIFVPGILILAVL" + "TFFIWCFILNISANPPVAFTANTKADNFFICLQTATSVVIVACPCALGLATPTAIMVGTG" + "VGAQNGVLIKGGEVLEKFNSITTFVFDKTGTLTTGFMVVKKFLKDSNWVGNVDEDEVLAC" + "IKATESISDHPVSKAIIRYCDGLNCNKALNAVVLESEYVLGKGIVSKCQVNGNTYDICIG" + "NEALILEDALKKSGFINSNVDQGNTVSYVSVNGHVFGLFEINDEVKHDSYATVQYLQRNG" + "YETYMITGDNNSAAKRVAREVGISFENVYSDVSPTGKCDLVKKIQDKEGNNKVAVVGDGI" + "NDAPALALSDLGIAISTGTEIAIEAADIVILCGNDLNTNSLRGLANAIDISLKTFKRIKL" + "NLFWALCYNIFMIPIAMGVLIPWGITLPPMLAGLAMAFSSVSVVLSSLMLKKWTPPDIES" + "HGISDFKSKFSIGNFWSRLFSTRAIAGEQDIESQAGLMSNEEVL") + self.annotation_aggregation = annotation_aggregation + self.filter_annotation = filter_annotation + self.download_annotation = download_annotation + self.Annotation = Annotation + + def tearDown(self): + """Remove testing framework.""" + + self.uniprotid = None + self.example_annotation = None + self.output_annotation = None + self.map_gff_features_to_sequence = None + self.ccc2_sequence = None + self.annotation_aggregation = None + self.filter_annotation = None + self.download_annotation = None + self.Annotation = None + + def test_parse_uniprot_gff(self): + """ + Test whether Uniprot GFF logic still valid. + """ + table = self.parse_gff_features(self.example_annotation) + self.assertTrue(set("NAME SOURCE TYPE START END SCORE STRAND FRAME GROUP".split()) + .issubset(table.columns)) + self.assertNotIn('empty', table) + self.assertTrue(table['END'].max() <= len(self.ccc2_sequence)) + + def test_filter_annotation_uniprot_gff(self): + table = self.parse_gff_features(self.example_annotation) + table = self.annotation_aggregation(table) + self.assertEqual(set(table.columns), {'annotation', 'site', 'accession'}) + self.assertTrue((~table.annotation.str.contains('Chain')).all()) + self.assertEqual(table.shape[0], len(self.ccc2_sequence)) + + table = self.parse_gff_features(self.example_annotation) + table = self.filter_annotation(table, annotation_agg=True) + self.assertEqual(set(table.columns), {'annotation', 'site', 'accession'}) + self.assertTrue((~table.annotation.str.contains('Chain')).all()) + self.assertEqual(table.shape[0], len(self.ccc2_sequence)) + + def test_parse_uniprot_gff_un_grouped(self): + table = self.parse_gff_features(self.example_annotation) + table = self.annotation_aggregation(table, group_residues=False) + self.assertEqual(set(table.columns), {'annotation', 'idx', 'site', 'accession'}) + self.assertTrue(table.idx.max() >= len(self.ccc2_sequence)) + + table = self.parse_gff_features(self.example_annotation) + table = self.filter_annotation(table, annotation_agg=True, group_residues=False) + self.assertEqual(set(table.columns), {'annotation', 'idx', 'site', 'accession'}) + self.assertTrue(table.idx.max() >= len(self.ccc2_sequence)) + + def test_download_uniprot_gff(self): + self.download_annotation(self.uniprotid, filename=self.output_annotation, + overwrite=True) + if os.path.exists(self.output_annotation): + os.remove(self.output_annotation) + + def test_main_Annotation(self): + # read + table = self.Annotation.read(self.example_annotation) + self.assertTrue(set("NAME SOURCE TYPE START END SCORE STRAND FRAME GROUP".split()) + .issubset(table.columns)) + self.assertNotIn('empty', table) + self.assertTrue(table['END'].max() <= len(self.ccc2_sequence)) + # download + self.Annotation.download(self.uniprotid, filename=self.output_annotation, + overwrite=True) + if os.path.exists(self.output_annotation): + os.remove(self.output_annotation) + # select + self.Annotation.select(self.uniprotid) + + +if __name__ == '__main__': + logging.basicConfig(stream=sys.stderr) + logging.getLogger("proteofav.config").setLevel(logging.CRITICAL) + suite = unittest.TestLoader().loadTestsFromTestCase(TestUNIPROTParser) + unittest.TextTestRunner(verbosity=2).run(suite) diff --git a/tests/test_config.py b/tests/test_config.py index 91dce8c..798819e 100644 --- a/tests/test_config.py +++ b/tests/test_config.py @@ -1,7 +1,5 @@ -#!/local/bin/python # -*- coding: utf-8 -*- - import os import sys import logging @@ -35,16 +33,12 @@ def setUp(self): self.config = config self.defaults = Defaults - logging.disable(logging.DEBUG) - def tearDown(self): """Remove testing framework.""" self.config = None self.defaults = None - logging.disable(logging.NOTSET) - def test_loading_config_defaults(self): config = self.config self.assertTrue(hasattr(config, 'db_pdb')) @@ -114,6 +108,6 @@ def test_write_default_config(self): if __name__ == '__main__': logging.basicConfig(stream=sys.stderr) - logging.getLogger("proteofav").setLevel(logging.DEBUG) + logging.getLogger("proteofav.config").setLevel(logging.CRITICAL) suite = unittest.TestLoader().loadTestsFromTestCase(TestConfig) unittest.TextTestRunner(verbosity=2).run(suite) diff --git a/tests/test_dssp.py b/tests/test_dssp.py new file mode 100644 index 0000000..97ee285 --- /dev/null +++ b/tests/test_dssp.py @@ -0,0 +1,276 @@ +# -*- coding: utf-8 -*- + +import os +import sys +import logging +import unittest + +try: + from mock import patch +except ImportError: + # python 3.5 + from unittest.mock import patch + +from proteofav.library import scop_3to1 +from proteofav.config import defaults +from proteofav.dssp import (parse_dssp_residues, _import_dssp_chains_ids, + select_dssp, filter_dssp, get_rsa, get_rsa_class, + _add_dssp_rsa, _add_dssp_rsa_class, + _add_dssp_ss_reduced, _add_dssp_full_chain, + download_dssp, DSSP) + +root = os.path.abspath(os.path.dirname(__file__)) +defaults.db_dssp = os.path.join(root, "testdata", "dssp") + + +@patch("proteofav.dssp.defaults", defaults) +class TestDSSPParser(unittest.TestCase): + """Test the DSSP parser methods.""" + + def setUp(self): + """Initialize the framework for testing.""" + self.example_dssp = os.path.join(os.path.dirname(__file__), "testdata", + "dssp", "1iej.dssp") + self.example_dssp2 = os.path.join(os.path.dirname(__file__), "testdata", + "dssp", "2pah.dssp") + self.example_dssp_bio = os.path.join(os.path.dirname(__file__), "testdata", + "dssp", "2pah_bio.dssp") + self.dssp_ins_code = os.path.join(os.path.dirname(__file__), "testdata", + "dssp", "3mg7.dssp") + self.output_dssp = os.path.join(os.path.dirname(__file__), "testdata", + "2pah.dssp") + self.residues_parser = parse_dssp_residues + self.fix_dssp_ignoring_chains_ids = _import_dssp_chains_ids + self.pdbid = '2pah' + self.filter_dssp = filter_dssp + self.add_full_chain = _add_dssp_full_chain + self.add_rsa = _add_dssp_rsa + self.add_rsa_class = _add_dssp_rsa_class + self.add_ss_reduced = _add_dssp_ss_reduced + self.get_rsa = get_rsa + self.get_rsa_class = get_rsa_class + self.download_dssp = download_dssp + self.DSSP = DSSP + + def tearDown(self): + """Remove testing framework.""" + + self.example_dssp = None + self.example_dssp2 = None + self.example_dssp_bio = None + self.dssp_ins_code = None + self.output_dssp = None + self.residues_parser = None + self.fix_dssp_ignoring_chains_ids = None + self.filter_dssp = None + self.add_full_chain = None + self.add_rsa = None + self.add_rsa_class = None + self.add_ss_reduced = None + self.get_rsa = None + self.get_rsa_class = None + self.download_dssp = None + self.DSSP = None + + def test_to_table_dssp_residues(self): + """ + Tests the parsing real DSSP files.‰ + + Some checks are made to whether the parsed keys and values + are the ones we are expecting. + """ + + data = self.residues_parser(self.example_dssp) + # number of values per column (or rows) + self.assertEqual(len(data), 329) + # number of keys (or columns) + self.assertEqual(len(data.columns.values), 12) + # check whether there are particular keys + self.assertIn('CHAIN', data.columns.values) + # check the values for particular entries + self.assertTrue(data.loc[0, 'CHAIN'] == 'A') + self.assertEqual(data.loc[7, 'SS'], 'E') + self.assertEqual(data.loc[0, 'ACC'], 179) + + @unittest.expectedFailure # FIXME + def test_fix_dssp_ignoring_chains_ids_has_as_many_chains(self): + fix = self.fix_dssp_ignoring_chains_ids + chains_4v9d = ( + 'AB', 'AC', 'AD', 'AE', 'AF', 'AG', 'AH', 'AI', 'AJ', 'AK', 'AL', 'AM', 'AN', 'AO', + 'AP', 'AQ', 'AR', 'AS', 'AT', 'AU', 'AY', 'BB', 'BC', 'BD', 'BE', 'BF', 'BG', 'BH', + 'BI', 'BJ', 'BK', 'BL', 'BM', 'BN', 'BO', 'BP', 'BQ', 'BR', 'BS', 'BT', 'BU', 'CC', + 'CD', 'CE', 'CF', 'CG', 'CH', 'CI', 'CJ', 'CK', 'CL', 'CM', 'CN', 'CO', 'CP', 'CQ', + 'CR', 'CS', 'CT', 'CU', 'CV', 'CW', 'CX', 'CY', 'CZ', 'C0', 'C1', 'C2', 'C3', 'C4', + 'DC', 'DD', 'DE', 'DF', 'DG', 'DH', 'DI', 'DJ', 'DK', 'DL', 'DM', 'DN', 'DO', 'DP', + 'DQ', 'DR', 'DS', 'DT', 'DU', 'DV', 'DW', 'DX', 'DY', 'DZ', 'D0', 'D1', 'D2', 'D3', + 'D4') + table = fix('4v9d') + dssp_has_seq = table.aa.isin(scop_3to1.values()) + try: + self.assertItemsEqual(table.loc[dssp_has_seq, 'CHAIN'].unique(), chains_4v9d) + except NameError: + # python 3.5 + self.assertCountEqual(table.loc[dssp_has_seq, 'CHAIN'].unique(), chains_4v9d) + + def test_to_table_dssp_3mg7(self): + """ + Getting some letters in the accession column. + """ + self.data = self.residues_parser(self.dssp_ins_code) + self.assertFalse(self.data.empty, 'Empty DataFrame for example with ' + 'insertion code.') + + self.assertEqual(self.data.loc[3302, 'RES_FULL'], '102A') + self.assertEqual(self.data.loc[3302, 'AA'], 'I') + self.assertEqual(self.data.loc[3302, 'SS'], 'H') + self.assertEqual(self.data.loc[3302, 'ACC'], 55) + self.assertEqual(self.data.loc[3302, 'PHI'], -92.9) + self.assertEqual(self.data.loc[3302, 'PSI'], -50.1) + self.assertNotEqual(self.data.loc[3302, 'RES'], 102) + self.assertEqual(self.data.loc[3302, 'RES'], '102') + self.assertEqual(self.data.loc[3302, 'INSCODE'], 'A') + + self.assertEqual(self.data.loc[6401, 'RES_FULL'], '187J') + self.assertEqual(self.data.loc[6401, 'AA'], 'L') + self.assertEqual(self.data.loc[6401, 'SS'], '') + self.assertEqual(self.data.loc[6401, 'ACC'], 92) + self.assertEqual(self.data.loc[6401, 'PHI'], -57.8) + self.assertEqual(self.data.loc[6401, 'PSI'], 360) + self.assertNotEqual(self.data.loc[6401, 'PSI'], 800) + + def test_empty(self): + with self.assertRaises(ValueError): + self.residues_parser(os.path.join(os.path.dirname(__file__), + "testdata", "dssp", "empty.dssp")) + + def test_parser_dssp(self): + data = self.residues_parser(self.example_dssp2) + self.assertEqual(data.loc[0, 'CHAIN'], 'A') + self.assertEqual(data.loc[0, 'RES'], '118') + self.assertEqual(data.loc[331, 'CHAIN'], 'B') + self.assertEqual(data.loc[331, 'RES'], '118') + + def test_parser_dssp_bio(self): + data = self.residues_parser(self.example_dssp_bio) + self.assertEqual(data.loc[0, 'CHAIN'], 'A') + self.assertEqual(data.loc[0, 'RES'], '118') + self.assertEqual(data.loc[662, 'CHAIN'], 'B') + self.assertEqual(data.loc[662, 'RES'], '118') + + def test_filter_dssp_excluded_cols(self): + data = self.residues_parser(self.example_dssp2, excluded_cols=()) + keys = [k for k in data] + self.assertIn("LINE", keys) + self.assertIn("STRUCTURE", keys) + self.assertIn("BP1", keys) + self.assertIn("BP2", keys) + self.assertIn("BP2_CHAIN", keys) + self.assertIn("X-CA", keys) + self.assertIn("Y-CA", keys) + self.assertIn("Z-CA", keys) + exc_cols = ("LINE", "STRUCTURE", "BP1", "BP2", "BP2_CHAIN", "X-CA", "Y-CA", "Z-CA") + data = self.filter_dssp(data, excluded_cols=exc_cols) + keys = [k for k in data] + self.assertNotIn("LINE", keys) + self.assertNotIn("STRUCTURE", keys) + self.assertNotIn("BP1", keys) + self.assertNotIn("BP2", keys) + self.assertNotIn("BP2_CHAIN", keys) + self.assertNotIn("X-CA", keys) + self.assertNotIn("Y-CA", keys) + self.assertNotIn("Z-CA", keys) + + def test_filter_dssp_add_chain_full(self): + data = self.residues_parser(self.example_dssp_bio) + data = self.add_full_chain(data) + self.assertIn("AA", data.CHAIN_FULL.unique()) + self.assertIn("BA", data.CHAIN_FULL.unique()) + data = self.residues_parser(self.example_dssp_bio) + data = self.filter_dssp(data, add_full_chain=True) + self.assertIn("AA", data.CHAIN_FULL.unique()) + self.assertIn("BA", data.CHAIN_FULL.unique()) + + def test_filter_dssp_add_rsa(self): + data = self.residues_parser(self.example_dssp_bio) + data = self.add_rsa(data) + self.assertEqual(52.863, data.loc[2, 'RSA']) + data = self.residues_parser(self.example_dssp_bio) + data = self.filter_dssp(data, add_rsa=True) + self.assertEqual(52.863, data.loc[2, 'RSA']) + + def test_filter_dssp_add_ss_reduced(self): + data = self.residues_parser(self.example_dssp_bio) + data = self.add_ss_reduced(data) + self.assertEqual('H', data.loc[29, 'SS_CLASS']) + data = self.residues_parser(self.example_dssp_bio) + data = self.filter_dssp(data, add_ss_reduced=True) + self.assertEqual('H', data.loc[29, 'SS_CLASS']) + + def test_filter_dssp_add_rsa_class(self): + data = self.residues_parser(self.example_dssp_bio) + data = self.add_rsa(data) + data = self.add_rsa_class(data) + self.assertEqual('Surface', data.loc[2, 'RSA_CLASS']) + data = self.residues_parser(self.example_dssp_bio) + data = self.filter_dssp(data, add_rsa=True, add_rsa_class=True) + self.assertEqual('Surface', data.loc[2, 'RSA_CLASS']) + + def test_filter_dssp_chain(self): + data = self.residues_parser(self.example_dssp2) + data = self.filter_dssp(data, chains=('A',)) + self.assertNotIn("B", data.CHAIN.unique()) + + def test_filter_dssp_chain_full(self): + data = self.residues_parser(self.example_dssp_bio) + data = self.filter_dssp(data, chains_full=('BA',)) + self.assertIn("B", data.CHAIN.unique()) + self.assertNotIn("B", data.CHAIN_FULL.unique()) + + def test_filter_dssp_res(self): + data = self.residues_parser(self.example_dssp2) + data = self.filter_dssp(data, res=('118',)) + self.assertNotIn('119', data.RES.unique()) + + def test_get_rsa(self): + rsa = self.get_rsa(10.0, "A", method="Sander") + self.assertEqual(9.434, rsa) + rsa = self.get_rsa(20.0, "A", method="Miller") + self.assertEqual(17.699, rsa) + rsa = self.get_rsa(30.0, "A", method="Wilke") + self.assertEqual(23.256, rsa) + + def test_get_rsa_class(self): + rsa_class = self.get_rsa_class(25.5) + self.assertEqual('Surface', rsa_class) + rsa_class = self.get_rsa_class(7.5) + self.assertEqual('Part. Exposed', rsa_class) + rsa_class = self.get_rsa_class(1.5) + self.assertEqual('Core', rsa_class) + + def test_download_dssp(self): + self.download_dssp(self.pdbid, filename=self.output_dssp, + overwrite=True) + if os.path.exists(self.output_dssp): + os.remove(self.output_dssp) + + def test_main_DSSP(self): + # read + data = self.DSSP.read(self.example_dssp2) + self.assertEqual(data.loc[0, 'CHAIN'], 'A') + self.assertEqual(data.loc[0, 'RES'], '118') + self.assertEqual(data.loc[331, 'CHAIN'], 'B') + self.assertEqual(data.loc[331, 'RES'], '118') + # download + self.DSSP.download(self.pdbid, filename=self.output_dssp, + overwrite=True) + if os.path.exists(self.output_dssp): + os.remove(self.output_dssp) + # select + self.DSSP.select(self.pdbid) + + +if __name__ == '__main__': + logging.basicConfig(stream=sys.stderr) + logging.getLogger("proteofav.config").setLevel(logging.CRITICAL) + suite = unittest.TestLoader().loadTestsFromTestCase(TestDSSPParser) + unittest.TextTestRunner(verbosity=2).run(suite) diff --git a/tests/test_mergers.py b/tests/test_mergers.py new file mode 100644 index 0000000..fcc0858 --- /dev/null +++ b/tests/test_mergers.py @@ -0,0 +1,585 @@ +# -*- coding: utf-8 -*- + +import os +import sys +import logging +import unittest + +try: + from mock import patch +except ImportError: + # python 3.5 + from unittest.mock import patch + +from proteofav.config import defaults +from proteofav.structures import parse_mmcif_atoms, mmCIF +from proteofav.dssp import parse_dssp_residues, DSSP, filter_dssp +from proteofav.sifts import parse_sifts_residues, SIFTS +from proteofav.variants import Variants +from proteofav.validation import Validation +from proteofav.annotation import Annotation + +from proteofav.mergers import (mmcif_dssp_table_merger, + mmcif_sifts_table_merger, + mmcif_validation_table_merger, + sifts_annotation_table_merger, + sifts_variants_table_merger, + uniprot_vars_ensembl_vars_merger, + table_merger, table_generator, + Tables) + +root = os.path.dirname(__file__) +defaults.db_cif = os.path.join(root, "testdata", "mmcif") +defaults.db_sifts = os.path.join(root, "testdata", "sifts") +defaults.db_dssp = os.path.join(root, "testdata", "dssp") +defaults.db_validation = os.path.join(root, "testdata", "validation") +defaults.db_annotation = os.path.join(root, "testdata", "annotation") + + +@patch("proteofav.structures.defaults", defaults) +@patch("proteofav.dssp.defaults", defaults) +@patch("proteofav.sifts.defaults", defaults) +@patch("proteofav.validation.defaults", defaults) +@patch("proteofav.annotation.defaults", defaults) +class TestMerger(unittest.TestCase): + """Test table merging methods.""" + + def setUp(self): + """Initialize the framework for testing.""" + + self.cif_to_table = parse_mmcif_atoms + self.sifts_to_table = parse_sifts_residues + self.dssp_to_table = parse_dssp_residues + + self.pdbid = TestMerger.pdbid + self.uniprotid = TestMerger.uniprotid + self.inputbiodssp = TestMerger.inputbiodssp + + self.mmcif = TestMerger.mmcif + self.mmcif_bio = TestMerger.mmcif_bio + self.dssp = TestMerger.dssp + self.dssp_bio = TestMerger.dssp_bio + self.sifts = TestMerger.sifts + self.validation = TestMerger.validation + self.annotation = TestMerger.annotation + self.uni_vars = TestMerger.uni_vars + self.ens_vars = TestMerger.ens_vars + self.variants = TestMerger.variants + + self.mmcif_sifts = mmcif_sifts_table_merger + self.mmcif_dssp = mmcif_dssp_table_merger + self.mmcif_validation = mmcif_validation_table_merger + self.sifts_annotation = sifts_annotation_table_merger + self.sifts_variants = sifts_variants_table_merger + self.uni_ens_vars = uniprot_vars_ensembl_vars_merger + + self.table_merger = table_merger + self.table_generator = table_generator + self.Tables = Tables + + def tearDown(self): + """Remove testing framework by cleaning the namespace.""" + + self.cif_to_table = None + self.sifts_to_table = None + self.dssp_to_table = None + + self.pdbid = None + self.uniprotid = None + self.inputbiodssp = None + + self.mmcif = None + self.mmcif_bio = None + self.dssp = None + self.dssp_bio = None + self.sifts = None + self.validation = None + self.annotation = None + self.uni_vars = None + self.ens_vars = None + self.variants = None + + self.mmcif_sifts = None + self.mmcif_dssp = None + self.mmcif_validation = None + self.sifts_annotation = None + self.sifts_variants = None + self.uni_ens_vars = None + + self.table_merger = None + self.table_generator = None + self.Tables = None + + @classmethod + def setUpClass(cls): + # to be run only once + super(TestMerger, cls).setUpClass() + + cls.pdbid = '2pah' + cls.uniprotid = 'P00439' + + cls.inputbiodssp = os.path.join(root, "testdata", defaults.db_dssp, + "{}_bio.dssp".format(cls.pdbid)) + + cls.mmcif = mmCIF.select(identifier=cls.pdbid, + add_res_full=True, atoms=('CA',)) + + cls.mmcif_bio = mmCIF.select(identifier=cls.pdbid, bio_unit=True, + bio_unit_preferred=True, + add_res_full=True, atoms=('CA',)) + + cls.dssp = DSSP.select(identifier=cls.pdbid, + add_rsa_class=True, add_ss_reduced=True) + + dssp_bio = DSSP.read(filename=cls.inputbiodssp) + cls.dssp_bio = filter_dssp(dssp_bio, add_rsa_class=True, add_ss_reduced=True) + + cls.sifts = SIFTS.select(identifier=cls.pdbid, add_regions=True, add_dbs=False) + + cls.validation = Validation.select(identifier=cls.pdbid, add_res_full=True) + + cls.annotation = Annotation.select(identifier=cls.uniprotid, annotation_agg=True) + + cls.uni_vars, cls.ens_vars = Variants.select(cls.uniprotid, + id_source='uniprot', + synonymous=True, + uniprot_vars=True, + ensembl_germline_vars=True, + ensembl_somatic_vars=True) + cls.variants = uniprot_vars_ensembl_vars_merger(cls.uni_vars, cls.ens_vars) + + @classmethod + def tearDownClass(cls): + cls.pdbid = None + cls.uniprotid = None + cls.inputbiodssp = None + + cls.mmcif = None + cls.mmcif_bio = None + cls.dssp = None + cls.dssp_bio = None + cls.sifts = None + cls.validation = None + cls.annotation = None + cls.uni_vars = None + cls.ens_vars = None + cls.variants = None + + def test_empty(self): + """Test no argument cases.""" + with self.assertRaises(ValueError): + self.Tables.generate(pdb_id=None) + self.Tables.generate(uniprot_id=None) + + def test_camKIV_ca_atom(self): + """Test table merger for a simple protein example.""" + data = self.Tables.generate(pdb_id="2w4o", chains="A", dssp=True, atoms='CA', + merge_tables=True) + self.assertIsNotNone(data) + self.assertFalse(data.empty) + + self.assertEqual(data.label_atom_id.dropna().unique()[0], 'CA', 'Other atoms than CA') + + self.assertEqual(data.PDB_dbChainId.unique()[0], 'A', 'Other chain') + self.assertEqual(data.CHAIN.dropna().unique()[0], 'A', 'Other chain') + self.assertEqual(data.label_asym_id.dropna().unique()[0], 'A', 'Other chain') + + self.assertEqual(data.shape[0], 278, 'wrong number of rows') + self.assertEqual(data.AA[~data.AA.isnull()].shape[0], 278, 'wrong number of residues') + self.assertEqual(data.UniProt_dbResName[~data.UniProt_dbResName.isnull()].shape[0], + 278, 'wrong number of residues') + + def test_merge_4ibw_A_with_alt_loc(self): + """ + Test case in a structure with alt locations.""" + data = self.Tables.generate(pdb_id="4ibw", chains="A", + merge_tables=True) + self.assertFalse(data.empty) + + def test_merge_3mn5_with_insertion_code(self): + """ + Test case with insertion code + """ + self.cif_path = os.path.join(os.path.dirname(__file__), "testdata", + "mmcif", "3mn5.cif") + self.sifts_path = os.path.join(os.path.dirname(__file__), "testdata", + "sifts", "3mn5.xml") + self.dssp_path = os.path.join(os.path.dirname(__file__), "testdata", + "dssp", "3mn5.dssp") + + self.cif = self.cif_to_table(self.cif_path) + self.sifts = self.sifts_to_table(self.sifts_path) + self.dssp = self.dssp_to_table(self.dssp_path) + + self.assertFalse(self.cif.empty) + self.assertFalse(self.sifts.empty) + self.assertFalse(self.dssp.empty) + + data = self.Tables.generate(pdb_id="3mn5", chains="A", + merge_tables=True) + self.assertFalse(data.empty) + + def test_merge_3fqd_A_no_pdbe_label_seq_id(self): + self.data = self.Tables.generate(pdb_id='3fqd', chains='A', + merge_tables=True) + self.assertFalse(self.data.empty) + + def test_merge_3ehk_D_lowercased_dssp(self): + self.data = self.Tables.generate(pdb_id='3ehk', chains='D', + merge_tables=True) + self.assertFalse(self.data.empty) + + # @unittest.expectedFailure + def test_merge_4v9d_BD_excessive_chains(self): + """ + DSSP files does not have BD chain, since its chain naming only support one character. + Although its possible to map and reference the BD chain into the mmCIF table, + it is currently unsupported by merge_tables. + """ + data = self.Tables.generate(pdb_id='4v9d', chains='BD', + merge_tables=True) + self.assertFalse(data.empty) + + def test_merge_4abo_A_DSSP_missing_first_residue(self): + data = self.Tables.generate(pdb_id='4abo', chains='A', + merge_tables=True) + self.assertFalse(data.empty) + + def test_merge_4why_K_DSSP_index_as_object(self): + data = self.Tables.generate(pdb_id='4why', chains='K', + merge_tables=True) + self.assertFalse(data.empty) + + def test_merge_2pm7_D_missing_residue_DSSP(self): + data = self.Tables.generate(pdb_id='2pm7', chains='D', + merge_tables=True) + self.assertFalse(data.empty) + + def test_merge_4myi_A_fail(self): + data = self.Tables.generate(pdb_id='2pm7', chains='D', + merge_tables=True) + self.assertFalse(data.empty) + + def test_camKIV_wrong_chain(self): + with self.assertRaises(ValueError): + self.Tables.generate(pdb_id='2w4o', chains='D', + merge_tables=True) + + def test_camKIV_wrong_atom(self): + with self.assertRaises(ValueError): + self.Tables.generate(pdb_id='2w4o', chains='A', atoms=['CC'], + merge_tables=True) + + def test_camKIV_atom_list(self): + # TODO test_camIV_list_mode(self): + data = self.Tables.generate(pdb_id='2w4o', chains='A', atoms=['CA', 'CB'], + merge_tables=True) + self.assertFalse(data.empty) + + def test_camKIV_atom_centroid(self): + # TODO test_camIV_centroid_mode(self): + data = self.Tables.generate(pdb_id='2w4o', chains='A', atoms='centroid', + merge_tables=True) + self.assertFalse(data.empty) + + def test_3edv_string_index(self): + # TODO def test_sift_3edv(self): Example dbResNum is a string, therefore was not merging. + pass + + def test_camKIV_from_uniprot_id(self): + data = self.Tables.generate(uniprot_id='Q16566', merge_tables=True) + self.assertFalse(data.empty) + + def test_sequence_check_raise(self): + # The first and the second residues in the cif file were swapped to GLY + # so they can't be checked with dssp and sifts sequences + badcif_path = os.path.join(os.path.dirname(__file__), "testdata", + "mmcif", "2w4o_with_error.cif") + baddata = self.cif_to_table(badcif_path) + + with patch("proteofav.structures.parse_mmcif_atoms", return_value=baddata): + # with self.assertRaises(ValueError): + data = self.Tables.generate(pdb_id='2w4o', merge_tables=True) + self.assertFalse(data.empty) + + def test_mmcif_dssp_merger(self): + table = self.mmcif_dssp(self.mmcif, self.dssp) + # Chain level + self.assertIn('label_asym_id', table) + self.assertIn('CHAIN_FULL', table) + self.assertNotIn('PDB_entityId', table) + # Res level + self.assertIn('label_seq_id_full', table) + self.assertIn('RES', table) + self.assertNotIn('PDB_dbResNum', table) + # values + self.assertEqual('CA', table.loc[0, 'label_atom_id']) + self.assertEqual('A', table.loc[0, 'label_asym_id']) + self.assertEqual('118', table.loc[0, 'RES']) + self.assertEqual('V', table.loc[0, 'AA']) + + def test_mmcif_dssp_bio_merger(self): + table = self.mmcif_dssp(self.mmcif_bio, self.dssp_bio) + # Chain level + self.assertIn('label_asym_id', table) + self.assertIn('CHAIN_FULL', table) + self.assertNotIn('PDB_entityId', table) + # Res level + self.assertIn('label_seq_id_full', table) + self.assertIn('RES', table) + self.assertNotIn('PDB_dbResNum', table) + # values + self.assertEqual('CA', table.loc[329, 'label_atom_id']) + self.assertEqual('AA', table.loc[329, 'label_asym_id']) + self.assertEqual('118', table.loc[329, 'RES']) + self.assertEqual('V', table.loc[329, 'AA']) + + def test_mmcif_sifts_merger(self): + table = self.mmcif_sifts(self.mmcif, self.sifts) + # Chain level + self.assertIn('label_asym_id', table) + self.assertNotIn('CHAIN_FULL', table) + self.assertIn('PDB_entityId', table) + # Res level + self.assertIn('label_seq_id_full', table) + self.assertNotIn('RES', table) + self.assertIn('PDB_dbResNum', table) + # values + self.assertEqual('CA', table.loc[0, 'label_atom_id']) + self.assertEqual('A', table.loc[0, 'label_asym_id']) + self.assertEqual('118', table.loc[0, 'PDB_dbResNum']) + self.assertEqual('VAL', table.loc[0, 'PDB_dbResName']) + + def test_mmcif_sifts_bio_merger(self): + table = self.mmcif_sifts(self.mmcif_bio, self.sifts) + # Chain level + self.assertIn('label_asym_id', table) + self.assertNotIn('CHAIN_FULL', table) + self.assertIn('PDB_entityId', table) + # Res level + self.assertIn('label_seq_id_full', table) + self.assertNotIn('RES', table) + self.assertIn('PDB_dbResNum', table) + # values + self.assertEqual('CA', table.loc[329, 'label_atom_id']) + self.assertEqual('AA', table.loc[329, 'label_asym_id']) + self.assertEqual('118', table.loc[329, 'PDB_dbResNum']) + self.assertEqual('VAL', table.loc[329, 'PDB_dbResName']) + + def test_mmcif_validation_merger(self): + table = self.mmcif_validation(self.mmcif, self.validation) + self.assertIn('auth_asym_id', table) + self.assertIn('validation_rsr', table) + self.assertEqual(table.loc[0, 'auth_asym_id'], 'A') + self.assertEqual(table.loc[0, 'validation_rsr'], 0.242) + self.assertEqual(table.loc[0, 'auth_seq_id_full'], '118') + self.assertEqual(table.loc[0, 'validation_resnum_full'], '118') + + def test_sifts_annotation_merger(self): + table = self.sifts_annotation(self.sifts, self.annotation) + self.assertIn('UniProt_dbResNum', table) + self.assertIn('site', table) + self.assertEqual(table.loc[0, 'UniProt_dbResNum'], '118') + self.assertEqual(table.loc[3, 'UniProt_dbResNum'], '121') + self.assertEqual(table.loc[3, 'site'], '121') + self.assertIn('Natural variant:', table.loc[3, 'annotation']) + + def test_sifts_variants_merger(self): + table = self.sifts_variants(self.sifts, self.variants) + self.assertIn('UniProt_dbAccessionId', table) + self.assertIn('UniProt_dbResNum', table) + self.assertIn('xrefs_id', table) + self.assertIn('accession', table) + self.assertIn('begin', table) + self.assertEqual(table.loc[0, 'UniProt_dbResNum'], '118') + self.assertEqual(table.loc[0, 'UniProt_dbAccessionId'], 'P00439') + self.assertEqual(table.loc[0, 'accession'], 'P00439') + self.assertEqual(table.loc[0, 'xrefs_id'], 'rs776442422') + self.assertEqual(table.loc[0, 'siftScore'], 0.14) + + def test_uni_ens_vars_merger(self): + table = self.uni_ens_vars(self.uni_vars, self.ens_vars) + # UniProt + self.assertNotIn('translation', list(self.uni_vars)) + self.assertNotIn('allele', list(self.uni_vars)) + self.assertIn('taxid', list(self.uni_vars)) + self.assertIn('description', list(self.uni_vars)) + # Ensembl + self.assertIn('translation', list(self.ens_vars)) + self.assertIn('allele', list(self.ens_vars)) + self.assertNotIn('taxid', list(self.ens_vars)) + self.assertNotIn('description', list(self.ens_vars)) + # Merged Table + self.assertIn('translation', list(table)) + self.assertIn('allele', list(table)) + self.assertIn('taxid', list(table)) + self.assertIn('description', list(table)) + self.assertIn('begin', list(table)) + self.assertIn('end', list(table)) + + def test_table_merger(self): + table = self.Tables.merge(self.mmcif, self.dssp, self.sifts, + self.validation, self.annotation, self.variants) + # Chain level + self.assertIn('label_asym_id', table) + self.assertIn('CHAIN_FULL', table) + self.assertIn('PDB_entityId', table) + # Res level + self.assertIn('label_seq_id_full', table) + self.assertIn('RES', table) + self.assertIn('PDB_dbResNum', table) + # values + self.assertEqual('CA', table.loc[0, 'label_atom_id']) + self.assertEqual('A', table.loc[0, 'label_asym_id']) + self.assertEqual('118', table.loc[0, 'RES']) + self.assertEqual('VAL', table.loc[0, 'PDB_dbResName']) + + def test_table_merger_method(self): + table = self.table_merger(self.mmcif, self.dssp, self.sifts, + self.validation, self.annotation, self.variants) + # Chain level + self.assertIn('label_asym_id', table) + self.assertIn('CHAIN_FULL', table) + self.assertIn('PDB_entityId', table) + # Res level + self.assertIn('label_seq_id_full', table) + self.assertIn('RES', table) + self.assertIn('PDB_dbResNum', table) + # values + self.assertEqual('CA', table.loc[0, 'label_atom_id']) + self.assertEqual('A', table.loc[0, 'label_asym_id']) + self.assertEqual('118', table.loc[0, 'RES']) + self.assertEqual('VAL', table.loc[0, 'PDB_dbResName']) + self.assertEqual('V', table.loc[0, 'UniProt_dbResName']) + + def test_table_merger_method_bio(self): + table = self.table_merger(self.mmcif_bio, self.dssp_bio, self.sifts, + self.validation, self.annotation, self.variants) + # Chain level + self.assertIn('label_asym_id', table) + self.assertIn('CHAIN_FULL', table) + self.assertIn('PDB_entityId', table) + # Res level + self.assertIn('label_seq_id_full', table) + self.assertIn('RES', table) + self.assertIn('PDB_dbResNum', table) + # values + self.assertEqual('CA', table.loc[407, 'label_atom_id']) + self.assertEqual('AA', table.loc[407, 'label_asym_id']) + self.assertEqual('118', table.loc[407, 'RES']) + self.assertEqual('VAL', table.loc[407, 'PDB_dbResName']) + self.assertEqual('V', table.loc[407, 'UniProt_dbResName']) + + def test_table_generator(self): + mmcif_table, dssp_table, sifts_table, valid_table, annot_table, vars_table = \ + self.table_generator(uniprot_id=None, pdb_id=self.pdbid, bio_unit=True, + sifts=True, dssp=True, validation=False, annotations=False, variants=False, + chains=None, res=None, sites=None, atoms=('CA',), lines=None, + residue_agg=False, overwrite=False) + + table = self.table_merger(mmcif_table, dssp_table, sifts_table, + valid_table, annot_table, vars_table) + # Chain level + self.assertIn('label_asym_id', table) + self.assertIn('CHAIN_FULL', table) + self.assertIn('PDB_entityId', table) + # Res level + self.assertIn('label_seq_id_full', table) + self.assertIn('RES', table) + self.assertIn('PDB_dbResNum', table) + # values + self.assertEqual('CA', table.loc[0, 'label_atom_id']) + self.assertEqual('A', table.loc[0, 'label_asym_id']) + self.assertEqual('118', table.loc[0, 'RES']) + self.assertEqual('VAL', table.loc[0, 'PDB_dbResName']) + self.assertEqual('V', table.loc[0, 'UniProt_dbResName']) + + def test_table_generator_bio(self): + mmcif_table, dssp_table, sifts_table, valid_table, annot_table, vars_table = \ + self.table_generator(uniprot_id=None, pdb_id=self.pdbid, bio_unit=True, + sifts=True, dssp=True, variants=False, annotations=False, + chains=None, res=None, sites=None, atoms=('CA',), lines=None, + residue_agg=False, overwrite=False) + + table = self.table_merger(mmcif_table, dssp_table, sifts_table, + valid_table, annot_table, vars_table) + # Chain level + self.assertIn('label_asym_id', table) + self.assertIn('CHAIN_FULL', table) + self.assertIn('PDB_entityId', table) + # Res level + self.assertIn('label_seq_id_full', table) + self.assertIn('RES', table) + self.assertIn('PDB_dbResNum', table) + # values + self.assertEqual('CA', table.loc[329, 'label_atom_id']) + self.assertEqual('AA', table.loc[329, 'label_asym_id']) + # self.assertEqual('118', table.loc[329, 'RES']) + self.assertEqual('VAL', table.loc[329, 'PDB_dbResName']) + self.assertEqual('V', table.loc[329, 'UniProt_dbResName']) + + def test_table_merger_bio(self): + self.Tables.generate(pdb_id=self.pdbid, atoms=('CA',), bio_unit=True, + dssp=True, sifts=True) + table = self.Tables.merge() + # Chain level + self.assertIn('label_asym_id', table) + self.assertIn('CHAIN_FULL', table) + self.assertIn('PDB_entityId', table) + # Res level + self.assertIn('label_seq_id_full', table) + self.assertIn('RES', table) + self.assertIn('PDB_dbResNum', table) + # values + self.assertEqual('CA', table.loc[329, 'label_atom_id']) + self.assertEqual('AA', table.loc[329, 'label_asym_id']) + # self.assertEqual('118', table.loc[329, 'RES']) + self.assertEqual('VAL', table.loc[329, 'PDB_dbResName']) + self.assertEqual('V', table.loc[329, 'UniProt_dbResName']) + + def test_table_generator_full(self): + mmcif_table, dssp_table, sifts_table, valid_table, annot_table, vars_table = \ + self.table_generator(uniprot_id=None, pdb_id=self.pdbid, bio_unit=True, + sifts=True, dssp=True, validation=True, annotations=True, variants=True, + chains=None, res=None, sites=None, atoms=('CA',), lines=None, + residue_agg=False, overwrite=False) + + table = self.table_merger(mmcif_table, dssp_table, sifts_table, + valid_table, annot_table, vars_table) + + # Chain level + self.assertIn('label_asym_id', table) + self.assertIn('CHAIN_FULL', table) + self.assertIn('PDB_entityId', table) + # Res level + self.assertIn('label_seq_id_full', table) + self.assertIn('RES', table) + self.assertIn('PDB_dbResNum', table) + # values + self.assertEqual('CA', table.loc[0, 'label_atom_id']) + self.assertEqual('A', table.loc[0, 'label_asym_id']) + self.assertEqual('AA', table.loc[407, 'label_asym_id']) + self.assertEqual('118', table.loc[0, 'RES']) + self.assertEqual('118', table.loc[407, 'RES']) + self.assertEqual('VAL', table.loc[0, 'PDB_dbResName']) + self.assertEqual('V', table.loc[0, 'UniProt_dbResName']) + # validation + self.assertEqual('118', table.loc[0, 'validation_resnum_full']) + self.assertEqual('118', table.loc[407, 'validation_resnum_full']) + self.assertEqual('A', table.loc[0, 'validation_chain']) + self.assertEqual('A', table.loc[407, 'validation_chain']) + # annotations + self.assertIn('Natural variant:', table.loc[4, 'annotation']) + # variants + self.assertEqual('large_scale_study', table.loc[0, 'sourceType']) + self.assertEqual('ENSP00000448059', table.loc[0, 'translation']) + self.assertEqual('rs776442422', table.loc[0, 'xrefs_id']) + self.assertEqual('ExAC', table.loc[0, 'xrefs_name']) + self.assertEqual(0.14, table.loc[0, 'siftScore']) + + +if __name__ == '__main__': + logging.basicConfig(stream=sys.stderr) + logging.getLogger("proteofav.config").setLevel(logging.CRITICAL) + suite = unittest.TestLoader().loadTestsFromTestCase(TestMerger) + unittest.TextTestRunner(verbosity=2).run(suite) diff --git a/tests/test_sifts.py b/tests/test_sifts.py new file mode 100644 index 0000000..036a312 --- /dev/null +++ b/tests/test_sifts.py @@ -0,0 +1,193 @@ +# -*- coding: utf-8 -*- + +import os +import sys +import logging +import unittest + +try: + from mock import patch +except ImportError: + # python 3.5 + from unittest.mock import patch + +from proteofav.sifts import (parse_sifts_residues, sifts_best, + _parse_sifts_regions_from_file, + _parse_sifts_dbs_from_file, select_sifts, + filter_sifts, download_sifts, SIFTS) + +from proteofav.config import defaults + +root = os.path.abspath(os.path.dirname(__file__)) +defaults.db_sifts = os.path.join(root, "testdata", "sifts") + + +@patch("proteofav.sifts.defaults", defaults) +class TestSIFTSParser(unittest.TestCase): + """Test the SIFTS parser methods.""" + + def setUp(self): + """Initialize the framework for testing.""" + self.example_xml = os.path.join(os.path.dirname(__file__), + "testdata", "sifts", "2pah.xml") + self.residues_parser = parse_sifts_residues + self.output_sifts = os.path.join(os.path.dirname(__file__), + "testdata", "2pah.xml") + self.pdbid = '2pah' + self.uniprot_id = 'P00439' + self.pdb_best = sifts_best + self.parser_sifts_regions = _parse_sifts_regions_from_file + self.parser_sifts_dbs = _parse_sifts_dbs_from_file + self.filter_sifts = filter_sifts + self.download_sifts = download_sifts + self.SIFTS = SIFTS + + def tearDown(self): + """Remove testing framework.""" + + self.example_xml = None + self.residue_parser = None + self.output_sifts = None + self.pdbid = None + self.uniprot_id = None + self.pdb_best = None + self.parser_sifts_regions = None + self.parser_sifts_dbs = None + self.filter_sifts = None + self.download_sifts = None + self.SIFTS = None + + def test_to_table_sifts_residues_and_regions(self): + """ + Tests the parsing real SIFTS xml files. + This test focuses on the method that parses the residue entries + and the region entries. + + Some checks are made to whether the parsed keys and values + are the ones we are expecting. + """ + + data = self.residues_parser(self.example_xml) + + # number of values per column (or rows) + self.assertEqual(len(data), 670) + + # number of keys (or columns) + self.assertEqual(len(data.columns.values), 34) + + # state of the residue + self.assertEqual(data.loc[0, 'PDB_Annotation'], 'Observed') + + # check whether there are particular keys + self.assertIn('CATH_dbAccessionId', data.columns.values) + + # check the values for particular entries + self.assertTrue(data['CATH_dbAccessionId'][0] == '1.10.800.10') + self.assertEqual(data['PDB_dbChainId'][0], 'A') + self.assertEqual(data['PDB_dbResName'][0], 'VAL') + + # check whether there are particular keys + self.assertIn('UniProt_regionId', data.columns.values) + self.assertIn('CATH_regionId', data.columns.values) + + # check the values of particular entries + self.assertTrue(data['CATH_regionId'][0] == 1) + + def test_to_table_uniprot_pdb_sifts_best(self): + """ + Testing the PDBe API for mapping between UniProt and PDB + accession identifiers. + """ + + data = self.pdb_best(self.uniprot_id, first=True) + + # number of values + self.assertEqual(len(data), 10) + + # number of keys (or columns) + self.assertIn('coverage', data) + self.assertIn('pdb_id', data) + self.assertIn('chain_id', data) + + def test_parser_sifts_regions(self): + data = self.parser_sifts_regions(self.example_xml) + self.assertEqual(data['B']['PDB']['1']['dbAccessionId'], self.pdbid) + self.assertEqual(data['B']['PDB']['1']['start'], 1) + self.assertEqual(data['B']['PDB']['1']['end'], 335) + self.assertEqual(data['B']['PDB']['1']['dbCoordSys'], 'PDBresnum') + + def test_parser_sifts_dbs(self): + data = self.parser_sifts_dbs(self.example_xml) + self.assertEqual(data['UniProt']['dbSource'], 'UniProt') + self.assertEqual(data['UniProt']['dbCoordSys'], 'UniProt') + self.assertEqual(data['UniProt']['dbVersion'], '2017.03') + + def test_sifts_filter_default_excluded(self): + data = self.residues_parser(self.example_xml, excluded_cols=()) + keys = [k for k in data] + self.assertIn("InterPro_dbAccessionId", keys) + self.assertIn("NCBI_dbAccessionId", keys) + + exc_cols = ("InterPro", "GO", "EC", "NCBI") + data = self.residues_parser(self.example_xml, excluded_cols=exc_cols) + keys = [k for k in data] + self.assertNotIn("InterPro_dbAccessionId", keys) + self.assertNotIn("NCBI_dbAccessionId", keys) + + def test_sifts_filter_uniprot_id(self): + data = self.residues_parser(self.example_xml) + data = self.filter_sifts(data, uniprot=('P00439',)) + self.assertEqual("P00439", data.loc[0, 'UniProt_dbAccessionId']) + + def test_sifts_filter_chain(self): + data = self.residues_parser(self.example_xml) + data = self.filter_sifts(data, chains=('A',)) + self.assertIn("A", data.PDB_entityId.unique()) + self.assertNotIn("B", data.PDB_entityId.unique()) + + def test_sifts_filter_chain_auth(self): + data = self.residues_parser(self.example_xml) + data = self.filter_sifts(data, chain_auth=('A',)) + self.assertIn("A", data.PDB_dbChainId.unique()) + self.assertNotIn("B", data.PDB_dbChainId.unique()) + + def test_sifts_filter_res(self): + data = self.residues_parser(self.example_xml) + data = self.filter_sifts(data, res=('285',)) + self.assertIn("285", data.PDB_dbResNum.unique()) + self.assertNotIn("286", data.PDB_dbResNum.unique()) + + def test_sifts_filter_site(self): + data = self.residues_parser(self.example_xml) + data = self.filter_sifts(data, site=('118',)) + self.assertIn("118", data.UniProt_dbResNum.unique()) + self.assertNotIn("119", data.UniProt_dbResNum.unique()) + + def test_download_sifts(self): + self.download_sifts(self.pdbid, filename=self.output_sifts, + overwrite=True) + if os.path.exists(self.output_sifts): + os.remove(self.output_sifts) + + def test_main_SIFTS(self): + # read + data = self.SIFTS.read(self.example_xml) + self.assertTrue(data['CATH_dbAccessionId'][0] == '1.10.800.10') + self.assertEqual(data['PDB_dbChainId'][0], 'A') + self.assertEqual(data['PDB_dbResName'][0], 'VAL') + self.assertIn('UniProt_regionId', data.columns.values) + self.assertIn('CATH_regionId', data.columns.values) + # download + self.SIFTS.download(self.pdbid, filename=self.output_sifts, + overwrite=True) + if os.path.exists(self.output_sifts): + os.remove(self.output_sifts) + # select + self.SIFTS.select(self.pdbid) + + +if __name__ == '__main__': + logging.basicConfig(stream=sys.stderr) + logging.getLogger("proteofav.config").setLevel(logging.CRITICAL) + suite = unittest.TestLoader().loadTestsFromTestCase(TestSIFTSParser) + unittest.TextTestRunner(verbosity=2).run(suite) diff --git a/tests/test_structures.py b/tests/test_structures.py new file mode 100644 index 0000000..e03d11b --- /dev/null +++ b/tests/test_structures.py @@ -0,0 +1,606 @@ +# -*- coding: utf-8 -*- + +import os +import sys +import logging +import unittest + +try: + from mock import patch +except ImportError: + # python 3.5 + from unittest.mock import patch + +from proteofav.config import defaults +from proteofav.structures import (parse_mmcif_atoms, _mmcif_fields, select_structures, + parse_pdb_atoms, _fix_type_symbol, + _fix_pdb_ins_code, _fix_label_alt_id, + write_mmcif_from_table, write_pdb_from_table, + _get_atom_line, residues_aggregation, + filter_structures, + _add_mmcif_res_full, _add_mmcif_atom_altloc, + _remove_multiple_altlocs, _remove_partial_residues, + read_structures, write_structures, download_structures, + PDB, mmCIF, get_preferred_assembly_id, + fetch_summary_properties_pdbe) + + +@patch("proteofav.structures.defaults", defaults) +class TestMMCIFParser(unittest.TestCase): + """Test the mmCIF parser methods.""" + + def setUp(self): + """Initialize the framework for testing.""" + self.example_mmcif = os.path.join(os.path.dirname(__file__), "testdata", + "mmcif", "2pah.cif") + self.example_mmcif_bio = os.path.join(os.path.dirname(__file__), "testdata", + "mmcif", "2pah_bio.cif") + self.example_pdb = os.path.join(os.path.dirname(__file__), "testdata", + "pdb", "2pah.pdb") + self.example_pdb2 = os.path.join(os.path.dirname(__file__), "testdata", + "pdb", "1ejg.pdb") + self.output_mmcif = os.path.join(os.path.dirname(__file__), "testdata", + "2pah.cif") + self.output_pdb = os.path.join(os.path.dirname(__file__), "testdata", + "2pah.pdb") + self.mmcif_atom_parser = parse_mmcif_atoms + self.mmcif_info_parser = _mmcif_fields + self.example_tsv_out = os.path.join(os.path.dirname(__file__), "testdata", + "mmcif", "2pah-bio.tsv") + self.select_structures = select_structures + self.fetch_summary_properties_pdbe = fetch_summary_properties_pdbe + self.get_preferred_assembly_id = get_preferred_assembly_id + self.pdbid = '2pah' + self.pdb_atom_parser = parse_pdb_atoms + self.fix_label_alt_id = _fix_label_alt_id + self.fix_pdb_ins_code = _fix_pdb_ins_code + self.fix_type_symbol = _fix_type_symbol + self.write_mmcif_from_table = write_mmcif_from_table + self.write_pdb_from_table = write_pdb_from_table + self.get_atom_line = _get_atom_line + self.residues_aggregation = residues_aggregation + self.filter_structures = filter_structures + self.add_mmcif_res_full = _add_mmcif_res_full + self.add_mmcif_atom_altloc = _add_mmcif_atom_altloc + self.remove_multiple_altlocs = _remove_multiple_altlocs + self.remove_partial_residues = _remove_partial_residues + self.read_structures = read_structures + self.write_structures = write_structures + self.download_structures = download_structures + self.PDB = PDB + self.mmCIF = mmCIF + + def tearDown(self): + """Remove testing framework.""" + + self.example_mmcif = None + self.example_mmcif_bio = None + self.example_pdb = None + self.example_pdb2 = None + self.output_mmcif = None + self.output_pdb = None + self.mmcif_atom_parser = None + self.mmcif_info_parser = None + self.example_tsv_out = None + self.select_structures = None + self.fetch_summary_properties_pdbe = None + self.get_preferred_assembly_id = None + self.pdbid = None + self.pdb_atom_parser = None + self.fix_label_alt_id = None + self.fix_pdb_ins_code = None + self.fix_type_symbol = None + self.write_mmcif_from_table = None + self.write_pdb_from_table = None + self.get_atom_line = None + self.residues_aggregation = None + self.filter_structures = None + self.add_mmcif_res_full = None + self.add_mmcif_atom_altloc = None + self.remove_multiple_altlocs = None + self.remove_partial_residues = None + self.read_structures = None + self.write_structures = None + self.download_structures = None + self.PDB = None + self.mmCIF = None + + def test_atom_to_table_mmcif(self): + """ + Tests the parsing real mmCIF files. + + Some checks are made to whether the parsed keys and values + are the ones we are expecting. + + Parsing of ATOM and HETATOM lines. + """ + + data = self.mmcif_atom_parser(self.example_mmcif) + + # number of values per column (or rows) + self.assertEqual(len(data), 5317) + + # number of keys (or columns) + self.assertEqual(len(data.columns.values), 20) + + # check whether there are particular keys + self.assertIn('label_asym_id', data.columns.values) + + # check the values for particular entries + self.assertTrue(data.loc[1, 'label_asym_id'] == 'A') + self.assertEqual(data.loc[1, 'pdbx_PDB_model_num'], '1') + self.assertEqual(data['group_PDB'][0], 'ATOM') + + def test_info_to_table_mmcif(self): + """ + Tests the parsing real mmCIF files. + + Some checks are made to whether the parsed keys and values + are the ones we are expecting. + + Parsing all lines other than ATOM/HETATOM lines. + """ + + # describes possible macromolecular assemblies + assembly = self.mmcif_info_parser(self.example_mmcif, + field_name='_pdbx_struct_assembly.') + # check some data values + self.assertEqual(assembly.loc[0, 'details'], 'author_and_software_defined_assembly') + self.assertEqual(assembly.loc[0, 'oligomeric_details'], 'tetrameric') + self.assertEqual(assembly.loc[0, 'oligomeric_count'], 4) + + # details the generation of each macromolecular assembly + assembly_gen = self.mmcif_info_parser(self.example_mmcif, + field_name='_pdbx_struct_assembly_gen.') + # check some data values + self.assertEqual(assembly_gen.loc[0, 'asym_id_list'], 'A,C,B,D') + + # details translation and rotation operations required to generate/transform + # assembly coordinates + oper_list = self.mmcif_info_parser(self.example_mmcif, + field_name='_pdbx_struct_oper_list.', + require_index=True) + # check some data values + self.assertEqual(oper_list.loc[0, 'type'], 'identity operation') + + def test_bio_unit_to_table_mmcif(self): + """ + Tests the parsing real mmCIF files. + + Some checks are made to whether the parsed keys and values + are the ones we are expecting. + + Parses the atom lines and the info lines and looks for + biological assemblies. Finds the most likely and generates + a new pandas Dataframe with the new atoms. + """ + + # new approach that looks up the biological assemblies and + # gets the preferred one from the PDBe server instead of + # generating it locally + + # test loading the atom lines with biological assemblies + best_assembly = self.get_preferred_assembly_id(self.pdbid) + data = self.select_structures(self.pdbid, bio_unit=True, + bio_unit_id=best_assembly) + + # check some values + # Biological assemblies from the PDBe come with updated chains + # (auth_aym_id and label_aym_id) and two extra columns with the + # original chain identifiers + self.assertIn('orig_label_asym_id', data) + self.assertIn('orig_auth_asym_id', data) + + def test_parser_cif(self): + data = self.mmcif_atom_parser(self.example_mmcif) + self.assertEqual(data.loc[0, 'label_asym_id'], 'A') + self.assertEqual(data.loc[2686, 'label_asym_id'], 'B') + self.assertEqual(data.loc[5315, 'label_asym_id'], 'C') + self.assertEqual(data.loc[5316, 'label_asym_id'], 'D') + self.assertEqual(data.loc[1, 'label_atom_id'], 'CA') + self.assertEqual(data.loc[2687, 'label_atom_id'], 'CA') + self.assertEqual(data.loc[5315, 'label_atom_id'], 'FE') + self.assertEqual(data.loc[5316, 'label_atom_id'], 'FE') + + def test_parser_mmcif_bio(self): + data = self.mmcif_atom_parser(self.example_mmcif_bio) + self.assertEqual(data.loc[0, 'label_asym_id'], 'A') + self.assertEqual(data.loc[5372, 'label_asym_id'], 'B') + self.assertEqual(data.loc[10630, 'label_asym_id'], 'C') + self.assertEqual(data.loc[10632, 'label_asym_id'], 'D') + self.assertEqual(data.loc[2686, 'label_asym_id'], 'AA') + self.assertEqual(data.loc[8001, 'label_asym_id'], 'BA') + self.assertEqual(data.loc[10631, 'label_asym_id'], 'CA') + self.assertEqual(data.loc[10633, 'label_asym_id'], 'DA') + + def test_parser_pdb(self): + data = self.pdb_atom_parser(self.example_pdb) + self.assertEqual(data.loc[0, 'label_asym_id'], 'A') + self.assertEqual(data.loc[2686, 'label_asym_id'], 'B') + self.assertEqual(data.loc[5315, 'label_asym_id'], 'A') + self.assertEqual(data.loc[5316, 'label_asym_id'], 'B') + self.assertEqual(data.loc[1, 'label_atom_id'], 'CA') + + def test_fix_pdb_ins_code(self): + data = self.pdb_atom_parser(self.example_pdb2, fix_ins_code=False) + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('', data.loc[0, 'pdbx_PDB_ins_code']) + data = self.fix_pdb_ins_code(data) + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('?', data.loc[0, 'pdbx_PDB_ins_code']) + + def test_fix_label_alt_id(self): + data = self.pdb_atom_parser(self.example_pdb2, fix_label_alt_id=False) + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('N', data.loc[0, 'label_atom_id']) + self.assertEqual('A', data.loc[0, 'label_alt_id']) + data = self.fix_label_alt_id(data) + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('N', data.loc[0, 'label_atom_id']) + self.assertEqual('A', data.loc[0, 'label_alt_id']) + + def test_fix_type_symbol(self): + data = self.pdb_atom_parser(self.example_pdb2, fix_type_symbol=False) + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('', data.loc[0, 'type_symbol']) + data = self.fix_type_symbol(data) + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('N', data.loc[0, 'type_symbol']) + + def test_writer_cif(self): + data = self.mmcif_atom_parser(self.example_mmcif) + self.write_mmcif_from_table(table=data, filename=self.output_mmcif, + overwrite=True) + self.assertTrue(os.path.isfile(self.output_mmcif)) + data = self.mmcif_atom_parser(self.output_mmcif) + self.assertIn('label_asym_id', list(data)) + os.remove(self.output_mmcif) + + def test_writer_biocif(self): + data = self.mmcif_atom_parser(self.example_mmcif_bio) + self.write_mmcif_from_table(table=data, filename=self.output_mmcif, + overwrite=True) + self.assertTrue(os.path.isfile(self.output_mmcif)) + data = self.mmcif_atom_parser(self.output_mmcif) + self.assertIn('label_asym_id', list(data)) + os.remove(self.output_mmcif) + + def test_writer_mmcif2pdb(self): + data = self.mmcif_atom_parser(self.example_mmcif) + self.write_pdb_from_table(table=data, filename=self.output_pdb, + overwrite=True) + self.assertTrue(os.path.isfile(self.output_pdb)) + data = self.pdb_atom_parser(self.output_pdb) + self.assertIn('label_asym_id', list(data)) + os.remove(self.output_pdb) + + def test_writer_pdb2mmcif(self): + data = self.pdb_atom_parser(self.example_pdb) + self.write_mmcif_from_table(table=data, filename=self.output_mmcif, + overwrite=True) + self.assertTrue(os.path.isfile(self.output_mmcif)) + data = self.mmcif_atom_parser(self.output_mmcif) + self.assertIn('label_asym_id', list(data)) + os.remove(self.output_mmcif) + + def test_get_atom_line(self): + data = self.mmcif_atom_parser(self.example_mmcif) + line = self.get_atom_line(data, index=0, atom_number=1) + r = 'ATOM 1 N VAL A 118 -7.069 21.943 18.770 1.00 56.51 N \n' + self.assertEqual(str(line), r) + line = self.get_atom_line(data, index=1000, atom_number=1000) + r = 'ATOM 1000 CD ARG A 241 1.614 7.798 40.365 1.00 23.29 C \n' + self.assertEqual(str(line), r) + + def test_residues_aggregation_first(self): + data = self.mmcif_atom_parser(self.example_mmcif) + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('N', data.loc[0, 'type_symbol']) + self.assertEqual('N', data.loc[0, 'label_atom_id']) + self.assertEqual('VAL', data.loc[0, 'label_comp_id']) + self.assertEqual('118', data.loc[0, 'auth_seq_id']) + self.assertEqual(-7.069, data.loc[0, 'Cartn_x']) + data = self.residues_aggregation(data, agg_method='first', category='label') + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('N', data.loc[0, 'type_symbol']) + self.assertEqual('N', data.loc[0, 'label_atom_id']) + self.assertEqual('VAL', data.loc[0, 'label_comp_id']) + self.assertEqual('118', data.loc[0, 'auth_seq_id']) + self.assertEqual(-7.069, data.loc[0, 'Cartn_x']) + + def test_residues_aggregation_centroid(self): + data = self.mmcif_atom_parser(self.example_mmcif) + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('N', data.loc[0, 'type_symbol']) + self.assertEqual('N', data.loc[0, 'label_atom_id']) + self.assertEqual('VAL', data.loc[0, 'label_comp_id']) + self.assertEqual('118', data.loc[0, 'auth_seq_id']) + self.assertEqual(-7.069, data.loc[0, 'Cartn_x']) + data = self.residues_aggregation(data, agg_method='centroid', category='label') + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('N', data.loc[0, 'type_symbol']) + self.assertEqual('N', data.loc[0, 'label_atom_id']) + self.assertEqual('VAL', data.loc[0, 'label_comp_id']) + self.assertEqual('118', data.loc[0, 'auth_seq_id']) + self.assertAlmostEqual(-7.310, data.loc[0, 'Cartn_x'], places=2) + + def test_residues_aggregation_backbone_centroid(self): + data = self.mmcif_atom_parser(self.example_mmcif) + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('N', data.loc[0, 'type_symbol']) + self.assertEqual('N', data.loc[0, 'label_atom_id']) + self.assertEqual('VAL', data.loc[0, 'label_comp_id']) + self.assertEqual('118', data.loc[0, 'auth_seq_id']) + self.assertEqual(-7.069, data.loc[0, 'Cartn_x']) + data = self.residues_aggregation(data, agg_method='backbone_centroid', category='label') + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('N', data.loc[0, 'type_symbol']) + self.assertEqual('N', data.loc[0, 'label_atom_id']) + self.assertEqual('VAL', data.loc[0, 'label_comp_id']) + self.assertEqual('118', data.loc[0, 'auth_seq_id']) + self.assertAlmostEqual(-6.312, data.loc[0, 'Cartn_x'], places=2) + + def test_residues_aggregation_mean(self): + data = self.mmcif_atom_parser(self.example_mmcif) + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('N', data.loc[0, 'type_symbol']) + self.assertEqual('N', data.loc[0, 'label_atom_id']) + self.assertEqual('VAL', data.loc[0, 'label_comp_id']) + self.assertEqual('118', data.loc[0, 'auth_seq_id']) + self.assertEqual(-7.069, data.loc[0, 'Cartn_x']) + data = self.residues_aggregation(data, agg_method='backbone_centroid', category='label') + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('N', data.loc[0, 'type_symbol']) + self.assertEqual('N', data.loc[0, 'label_atom_id']) + self.assertEqual('VAL', data.loc[0, 'label_comp_id']) + self.assertEqual('118', data.loc[0, 'auth_seq_id']) + self.assertAlmostEqual(-6.312, data.loc[0, 'Cartn_x'], places=2) + + def test_filter_structures_residues_aggregation_centroid(self): + data = self.mmcif_atom_parser(self.example_mmcif) + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('N', data.loc[0, 'type_symbol']) + self.assertEqual('N', data.loc[0, 'label_atom_id']) + self.assertEqual('VAL', data.loc[0, 'label_comp_id']) + self.assertEqual('118', data.loc[0, 'auth_seq_id']) + self.assertEqual(-7.069, data.loc[0, 'Cartn_x']) + data = self.filter_structures(data, residue_agg=True, agg_method='centroid') + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('N', data.loc[0, 'type_symbol']) + self.assertEqual('N', data.loc[0, 'label_atom_id']) + self.assertEqual('VAL', data.loc[0, 'label_comp_id']) + self.assertEqual('118', data.loc[0, 'auth_seq_id']) + self.assertAlmostEqual(-7.310, data.loc[0, 'Cartn_x'], places=2) + + def test_filter_structures_excluded_cols(self): + data = self.mmcif_atom_parser(self.example_mmcif, excluded_cols=()) + keys = [k for k in data] + self.assertIn("Cartn_x_esd", keys) + self.assertIn("Cartn_y_esd", keys) + self.assertIn("Cartn_z_esd", keys) + self.assertIn("occupancy_esd", keys) + self.assertIn("B_iso_or_equiv_esd", keys) + exc_cols = ('Cartn_x_esd', 'Cartn_y_esd', 'Cartn_z_esd', + 'occupancy_esd', 'B_iso_or_equiv_esd') + data = self.filter_structures(data, excluded_cols=exc_cols) + keys = [k for k in data] + self.assertNotIn("Cartn_x_esd", keys) + self.assertNotIn("Cartn_y_esd", keys) + self.assertNotIn("Cartn_z_esd", keys) + self.assertNotIn("occupancy_esd", keys) + self.assertNotIn("B_iso_or_equiv_esd", keys) + + def test_filter_structures_chain_id(self): + data = self.mmcif_atom_parser(self.example_mmcif) + data = self.filter_structures(data, chains=('A',)) + self.assertIn("A", data.label_asym_id.unique()) + self.assertNotIn("B", data.label_asym_id.unique()) + + def test_filter_structures_atom_lines(self): + data = self.mmcif_atom_parser(self.example_mmcif) + data = self.filter_structures(data, lines=('ATOM',)) + self.assertIn("ATOM", data.group_PDB.unique()) + self.assertNotIn("HETATM", data.group_PDB.unique()) + + def test_filter_structures_comps(self): + data = self.mmcif_atom_parser(self.example_mmcif) + data = self.filter_structures(data, comps=('PHE',)) + self.assertIn("PHE", data.label_comp_id.unique()) + self.assertNotIn("TYR", data.label_comp_id.unique()) + + def test_filter_structures_res(self): + data = self.mmcif_atom_parser(self.example_mmcif) + data = self.filter_structures(data, res=('285',)) + self.assertIn("285", data.label_seq_id.unique()) + self.assertNotIn("289", data.label_seq_id.unique()) + + def test_filter_structures_atoms(self): + data = self.mmcif_atom_parser(self.example_mmcif) + data = self.filter_structures(data, atoms=('CA',)) + self.assertIn("CA", data.label_atom_id.unique()) + self.assertNotIn("N", data.label_atom_id.unique()) + + def test_filter_structures_remove_hydrogen(self): + data = self.pdb_atom_parser(self.example_pdb2) + self.assertIn("H", data.label_atom_id.unique()) + data = self.filter_structures(data, remove_hydrogens=True) + self.assertNotIn("H", data.label_atom_id.unique()) + + def test_filter_structures_add_res_full(self): + data = self.pdb_atom_parser(self.example_pdb2) + data = self.add_mmcif_res_full(data) + self.assertIn('label_seq_id_full', data) + self.assertIn('auth_seq_id_full', data) + self.assertEqual(data.loc[0, 'auth_seq_id_full'], '1') + data = self.pdb_atom_parser(self.example_pdb2) + data = self.filter_structures(data, add_res_full=True) + self.assertEqual(data.loc[0, 'auth_seq_id_full'], '1') + + def test_filter_structures_add_pdb_altloc(self): + data = self.pdb_atom_parser(self.example_pdb2) + data = self.add_mmcif_atom_altloc(data) + self.assertIn('label_atom_altloc_id', [k for k in data]) + self.assertIn('auth_atom_altloc_id', [k for k in data]) + self.assertEqual('N.A', data.loc[0, 'label_atom_altloc_id']) + self.assertEqual('N.B', data.loc[1, 'label_atom_altloc_id']) + self.assertEqual('CA.A', data.loc[2, 'label_atom_altloc_id']) + self.assertEqual('CA.B', data.loc[3, 'label_atom_altloc_id']) + self.assertEqual('C', data.loc[4, 'label_atom_altloc_id']) + self.assertEqual('O', data.loc[5, 'label_atom_altloc_id']) + data = self.pdb_atom_parser(self.example_pdb2) + data = self.filter_structures(data, remove_altloc=False, add_atom_altloc=True) + self.assertIn('label_atom_altloc_id', [k for k in data]) + self.assertIn('auth_atom_altloc_id', [k for k in data]) + self.assertEqual('N.A', data.loc[0, 'label_atom_altloc_id']) + self.assertEqual('N.B', data.loc[1, 'label_atom_altloc_id']) + self.assertEqual('CA.A', data.loc[2, 'label_atom_altloc_id']) + self.assertEqual('CA.B', data.loc[3, 'label_atom_altloc_id']) + self.assertEqual('C', data.loc[4, 'label_atom_altloc_id']) + self.assertEqual('O', data.loc[5, 'label_atom_altloc_id']) + + def test_filter_structures_remove_altloc(self): + data = self.pdb_atom_parser(self.example_pdb2) + data = self.remove_multiple_altlocs(data) + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('N', data.loc[0, 'type_symbol']) + self.assertEqual('N', data.loc[0, 'label_atom_id']) + self.assertEqual('.', data.loc[0, 'label_alt_id']) + data = self.pdb_atom_parser(self.example_pdb2) + data = self.filter_structures(data, remove_altloc=True) + self.assertEqual(1, data.loc[0, 'id']) + self.assertEqual('N', data.loc[0, 'type_symbol']) + self.assertEqual('N', data.loc[0, 'label_atom_id']) + self.assertEqual('.', data.loc[0, 'label_alt_id']) + + def test_filter_structures_remove_partial_res(self): + data = self.pdb_atom_parser(self.example_pdb2) + # counting the number of atoms in res with label_seq_id = '25' + self.assertEqual(54, list(data.label_seq_id.tolist()).count('25')) + data = self.remove_partial_residues(data) + self.assertEqual(19, list(data.label_seq_id.tolist()).count('25')) + data = self.pdb_atom_parser(self.example_pdb2) + self.assertEqual(54, list(data.label_seq_id.tolist()).count('25')) + data = filter_structures(data, models=None, remove_partial_res=True, + remove_altloc=False, remove_hydrogens=False, + reset_atom_id=False, add_res_full=False) + self.assertEqual(19, list(data.label_seq_id.tolist()).count('25')) + + def test_read_structures(self): + data = self.read_structures(self.example_mmcif) + self.assertEqual(data.loc[0, 'label_asym_id'], 'A') + self.assertEqual(data.loc[2686, 'label_asym_id'], 'B') + self.assertEqual(data.loc[5315, 'label_asym_id'], 'C') + self.assertEqual(data.loc[5316, 'label_asym_id'], 'D') + self.assertEqual(data.loc[1, 'label_atom_id'], 'CA') + self.assertEqual(data.loc[2687, 'label_atom_id'], 'CA') + self.assertEqual(data.loc[5315, 'label_atom_id'], 'FE') + self.assertEqual(data.loc[5316, 'label_atom_id'], 'FE') + + data = self.read_structures(self.example_pdb) + self.assertEqual(data.loc[0, 'label_asym_id'], 'A') + self.assertEqual(data.loc[2686, 'label_asym_id'], 'B') + self.assertEqual(data.loc[5315, 'label_asym_id'], 'A') + self.assertEqual(data.loc[5316, 'label_asym_id'], 'B') + self.assertEqual(data.loc[1, 'label_atom_id'], 'CA') + + example_dssp = os.path.join(os.path.dirname(__file__), "testdata", + "dssp", "2pah.dssp") + with self.assertRaises(ValueError, msg='DSSP format is not recognised'): + self.read_structures(example_dssp) + + def test_write_structures(self): + # read mmcif and write pdb + data = self.mmcif_atom_parser(self.example_mmcif) + self.write_structures(data, filename=self.output_pdb, overwrite=True) + self.assertTrue(os.path.isfile(self.output_pdb)) + data = self.pdb_atom_parser(self.output_pdb) + self.assertIn('label_asym_id', list(data)) + os.remove(self.output_pdb) + + # read pdb and write mmcif + data = self.pdb_atom_parser(self.example_pdb) + self.write_structures(data, filename=self.output_mmcif, overwrite=True) + self.assertTrue(os.path.isfile(self.output_mmcif)) + data = self.mmcif_atom_parser(self.output_mmcif) + self.assertIn('label_asym_id', list(data)) + os.remove(self.output_mmcif) + + def test_download_structures(self): + self.download_structures(self.pdbid, self.output_mmcif, + overwrite=True) + self.assertTrue(os.path.isfile(self.output_mmcif)) + os.remove(self.output_mmcif) + + self.download_structures(self.pdbid, self.output_mmcif, bio_unit=True, + overwrite=True) + self.assertTrue(os.path.isfile(self.output_mmcif)) + os.remove(self.output_mmcif) + + self.download_structures(self.pdbid, self.output_pdb, + overwrite=True) + self.assertTrue(os.path.isfile(self.output_pdb)) + os.remove(self.output_pdb) + + def test_main_mmCIF(self): + # read + data = self.mmCIF.read(self.example_mmcif) + self.assertEqual(data.loc[0, 'label_asym_id'], 'A') + self.assertEqual(data.loc[2686, 'label_asym_id'], 'B') + self.assertEqual(data.loc[5315, 'label_asym_id'], 'C') + self.assertEqual(data.loc[5316, 'label_asym_id'], 'D') + self.assertEqual(data.loc[1, 'label_atom_id'], 'CA') + self.assertEqual(data.loc[2687, 'label_atom_id'], 'CA') + self.assertEqual(data.loc[5315, 'label_atom_id'], 'FE') + self.assertEqual(data.loc[5316, 'label_atom_id'], 'FE') + # read mmcif and write pdb + data = self.mmCIF.read(self.example_mmcif) + self.mmCIF.write(data, filename=self.output_pdb, overwrite=True) + self.assertTrue(os.path.isfile(self.output_pdb)) + data = self.pdb_atom_parser(self.output_pdb) + self.assertIn('label_asym_id', list(data)) + os.remove(self.output_pdb) + # download + self.mmCIF.download(self.pdbid, self.output_mmcif, + overwrite=True) + self.assertTrue(os.path.isfile(self.output_mmcif)) + os.remove(self.output_mmcif) + # select + self.mmCIF.select(self.pdbid) + + def test_main_PDB(self): + # read + data = self.PDB.read(self.example_pdb) + self.assertEqual(data.loc[0, 'label_asym_id'], 'A') + self.assertEqual(data.loc[2686, 'label_asym_id'], 'B') + self.assertEqual(data.loc[5315, 'label_asym_id'], 'A') + self.assertEqual(data.loc[5316, 'label_asym_id'], 'B') + self.assertEqual(data.loc[1, 'label_atom_id'], 'CA') + # read pdb and write mmcif + data = self.PDB.read(self.example_pdb) + self.PDB.write(data, filename=self.output_mmcif, overwrite=True) + self.assertTrue(os.path.isfile(self.output_mmcif)) + data = self.mmcif_atom_parser(self.output_mmcif) + self.assertIn('label_asym_id', list(data)) + os.remove(self.output_mmcif) + # download + self.PDB.download(self.pdbid, self.output_pdb, + overwrite=True) + self.assertTrue(os.path.isfile(self.output_pdb)) + os.remove(self.output_pdb) + # select + self.PDB.select(self.pdbid) + + def test_summary_properties_pdbe(self): + r = self.fetch_summary_properties_pdbe(self.pdbid) + self.assertTrue(r.ok) + + def test_preferred_assembly_pdbe(self): + r = self.get_preferred_assembly_id(self.pdbid) + self.assertEqual("1", r) + + +if __name__ == '__main__': + logging.basicConfig(stream=sys.stderr) + logging.getLogger("proteofav.config").setLevel(logging.CRITICAL) + suite = unittest.TestLoader().loadTestsFromTestCase(TestMMCIFParser) + unittest.TextTestRunner(verbosity=2).run(suite) diff --git a/tests/test_table_merge.py b/tests/test_table_merge.py deleted file mode 100644 index e575dff..0000000 --- a/tests/test_table_merge.py +++ /dev/null @@ -1,175 +0,0 @@ -#!/local/bin/python -# -*- coding: utf-8 -*- -import logging -import unittest -from os import path - -try: - from mock import patch -except ImportError: - # python 3.5 - from unittest.mock import patch - -from proteofav.config import Defaults -from proteofav.main import merge_tables -from proteofav.structures import _dssp, _sifts_residues_regions, _mmcif_atom - -logging.getLogger('proteofav').setLevel(logging.CRITICAL) # turn off logging -defaults = Defaults(path.join(path.dirname(__file__), "config.txt")) -defaults.db_cif = path.join(path.dirname(__file__), "CIF/") -defaults.db_sifts = path.join(path.dirname(__file__), "SIFTS/") -defaults.db_dssp = path.join(path.dirname(__file__), "DSSP/") - - -@patch("proteofav.structures.defaults", defaults) -class TestTableMerger(unittest.TestCase): - """Test table merging methods.""" - - def setUp(self): - """Initialize the framework for testing.""" - - self.cif_to_table = _mmcif_atom - self.sifts_to_table = _sifts_residues_regions - self.dssp_to_table = _dssp - - self.merge_table = merge_tables - - def tearDown(self): - """Remove testing framework by cleaning the namespace.""" - self.defaults = None - self.merge_table = None - - self.cif_to_table = None - self.sifts_to_table = None - self.dssp_to_table = None - - self.merge_table = None - - def test_empty(self): - """Test no argument cases.""" - with self.assertRaises(TypeError): - self.merge_table(pdb_id=None) - self.merge_table(uniprot_id=None) - - def test_camKIV_ca_atom(self): - """Test table merger for a simple protein example.""" - data = self.merge_table(pdb_id="2w4o", chain="A") - self.assertIsNotNone(data) - self.assertFalse(data.empty) - - self.assertEqual(data.label_atom_id.dropna().unique()[0], 'CA', 'Other atoms than CA') - - self.assertEqual(data.PDB_dbChainId.unique()[0], 'A', 'Other chain') - self.assertEqual(data.chain_id.dropna().unique()[0], 'A', 'Other chain') - self.assertEqual(data.label_asym_id.dropna().unique()[0], 'A', 'Other chain') - - self.assertEqual(data.shape[0], 349, 'wrong number of rows') - self.assertEqual(data.aa[~data.aa.isnull()].shape[0], 278, 'wrong number of residues') - self.assertEqual( - data.UniProt_dbResName[~data.UniProt_dbResName.isnull()].shape[0], - 326, - 'wrong number of residues') - - def test_merge_4ibw_A_with_alt_loc(self): - """ - Test case in a structure with alt locations.""" - data = self.merge_table(pdb_id="4ibw", chain="A") - self.assertFalse(data.empty) - - def test_merge_3mn5_with_insertion_code(self): - """ - Test case with insertion code - """ - self.cif_path = path.join(path.dirname(__file__), "CIF/3mn5.cif") - self.sifts_path = path.join(path.dirname(__file__), "SIFTS/3mn5.xml") - self.dssp_path = path.join(path.dirname(__file__), "DSSP/3mn5.dssp") - - self.cif = self.cif_to_table(self.cif_path) - self.sifts = self.sifts_to_table(self.sifts_path) - self.dssp = self.dssp_to_table(self.dssp_path) - - self.assertFalse(self.cif.empty) - self.assertFalse(self.sifts.empty) - self.assertFalse(self.dssp.empty) - - data = self.merge_table(pdb_id="3mn5", chain="A") - self.assertFalse(data.empty) - - def test_merge_3fqd_A_no_pdbe_label_seq_id(self): - self.data = self.merge_table(pdb_id='3fqd', chain='A') - self.assertFalse(self.data.empty) - - def test_merge_3ehk_D_lowercased_dssp(self): - self.data = self.merge_table(pdb_id='3ehk', chain='D') - self.assertFalse(self.data.empty) - - @unittest.expectedFailure - def test_merge_4v9d_BD_excessive_chains(self): - """ - DSSP files does not have BD chain, since its chain naming only support one character. - Although its possible to map and reference the BD chain into the mmCIF table, - it is currently unsupported by merge_tables. - """ - data = self.merge_table(pdb_id='4v9d', chain='BD') - self.assertFalse(data.empty) - - def test_merge_4abo_A_DSSP_missing_first_residue(self): - data = self.merge_table(pdb_id='4abo', chain='A') - self.assertFalse(data.empty) - - def test_merge_4why_K_DSSP_index_as_object(self): - data = self.merge_table(pdb_id='4why', chain='K') - self.assertFalse(data.empty) - - def test_merge_2pm7_D_missing_residue_DSSP(self): - data = self.merge_table(pdb_id='2pm7', chain='D') - self.assertFalse(data.empty) - - def test_merge_4myi_A_fail(self): - data = self.merge_table(pdb_id='2pm7', chain='D') - self.assertFalse(data.empty) - - def test_camKIV_wrong_chain(self): - with self.assertRaises(ValueError): - self.merge_table(pdb_id='2w4o', chain='D') - - def test_camKIV_wrong_atom(self): - with self.assertRaises(ValueError): - self.merge_table(pdb_id='2w4o', chain='A', atoms=['CC']) - - def test_camKIV_atom_list(self): - # TODO test_camIV_list_mode(self): - data = self.merge_table(pdb_id='2w4o', chain='A', atoms=['CA', 'CB']) - self.assertFalse(data.empty) - - def test_camKIV_atom_centroid(self): - # TODO test_camIV_centroid_mode(self): - data = self.merge_table(pdb_id='2w4o', chain='A', atoms='centroid') - self.assertFalse(data.empty) - - def test_3edv_string_index(self): - # TODO def test_sift_3edv(self): Example dbResNum is a string, therefore was not merging. - pass - - def test_camKIV_from_uniprot_id(self): - defaults.api_pdbe = 'http://www.ebi.ac.uk/pdbe/api/' - with patch('proteofav.structures.defaults', defaults): - data = self.merge_table(uniprot_id='Q16566') - self.assertFalse(data.empty) - - def test_sequence_check_raise(self): - # The first and the second residues in the cif file were swaped to GLY - # so they can't be checked with dssp and sift sequences - badcif_path = path.join(path.dirname(__file__), "CIF/2w4o_with_error.cif") - baddata = self.cif_to_table(badcif_path) - - with patch("proteofav.structures._mmcif_atom", return_value=baddata): - with self.assertRaises(ValueError): - self.merge_table(pdb_id='2w4o') - # data = self.merge_table(pdb_id='2w4o', sequence_check='warn') # todo try capture warn - # self.assertFalse(data.empty) - - -if __name__ == '__main__': - suite = unittest.TestLoader().loadTestsFromTestCase(TestTableMerger) - unittest.TextTestRunner(verbosity=1).run(suite) diff --git a/tests/test_to_table_dssp.py b/tests/test_to_table_dssp.py deleted file mode 100644 index 69057a5..0000000 --- a/tests/test_to_table_dssp.py +++ /dev/null @@ -1,106 +0,0 @@ -#!/local/bin/python -# -*- coding: utf-8 -*- - - -import unittest -from os import path - -import logging -import numpy - -from proteofav.library import scop_3to1 -from proteofav.structures import _dssp, _import_dssp_chains_ids - -logging.getLogger('proteofav').setLevel(logging.CRITICAL) # turn off logging - - -class TestDSSPParser(unittest.TestCase): - """Test the DSSP parser methods.""" - - def setUp(self): - """Initialize the framework for testing.""" - self.example_dssp = path.join(path.dirname(__file__), "DSSP/1iej.dssp") - self.dssp_ins_code = path.join(path.dirname(__file__), "DSSP/3mg7.dssp") - self.residues_parser = _dssp - self.fix_dssp_ignoring_chains_ids = _import_dssp_chains_ids - - def tearDown(self): - """Remove testing framework.""" - - self.example_dssp = None - self.dssp_ins_code = None - self.residues_parser = None - self.fix_dssp_ignoring_chains_ids = None - - def test_to_table_dssp_residues(self): - """ - Tests the parsing real DSSP files.‰ - - Some checks are made to whether the parsed keys and values - are the ones we are expecting. - """ - - data = self.residues_parser(self.example_dssp) - # number of values per column (or rows) - self.assertEqual(len(data), 329) - # number of keys (or columns) - self.assertEqual(len(data.columns.values), 7) - # check whether there are particular keys - self.assertIn('chain_id', data.columns.values) - # check the values for particular entries - self.assertTrue(data.loc[1, 'chain_id'] == 'A') - self.assertEqual(data.loc[8, 'ss'], 'E') - self.assertEqual(data.loc[1, 'acc'], 179) - - @unittest.expectedFailure # FIXME - def test_fix_dssp_ignoring_chains_ids_has_as_many_chains(self): - fix = self.fix_dssp_ignoring_chains_ids - chains_4v9d = ( - 'AB', 'AC', 'AD', 'AE', 'AF', 'AG', 'AH', 'AI', 'AJ', 'AK', 'AL', 'AM', 'AN', 'AO', - 'AP', 'AQ', 'AR', 'AS', 'AT', 'AU', 'AY', 'BB', 'BC', 'BD', 'BE', 'BF', 'BG', 'BH', - 'BI', 'BJ', 'BK', 'BL', 'BM', 'BN', 'BO', 'BP', 'BQ', 'BR', 'BS', 'BT', 'BU', 'CC', - 'CD', 'CE', 'CF', 'CG', 'CH', 'CI', 'CJ', 'CK', 'CL', 'CM', 'CN', 'CO', 'CP', 'CQ', - 'CR', 'CS', 'CT', 'CU', 'CV', 'CW', 'CX', 'CY', 'CZ', 'C0', 'C1', 'C2', 'C3', 'C4', - 'DC', 'DD', 'DE', 'DF', 'DG', 'DH', 'DI', 'DJ', 'DK', 'DL', 'DM', 'DN', 'DO', 'DP', - 'DQ', 'DR', 'DS', 'DT', 'DU', 'DV', 'DW', 'DX', 'DY', 'DZ', 'D0', 'D1', 'D2', 'D3', - 'D4') - table = fix('4v9d') - dssp_has_seq = table.aa.isin(scop_3to1.values()) - try: - self.assertItemsEqual(table.loc[dssp_has_seq, 'chain_id'].unique(), chains_4v9d) - except NameError: - # python 3.5 - self.assertCountEqual(table.loc[dssp_has_seq, 'chain_id'].unique(), chains_4v9d) - - def test_to_table_dssp_3mg7(self): - """ - Getting some letters in the accession column. - """ - self.data = self.residues_parser(self.dssp_ins_code) - self.assertFalse(self.data.empty, 'Empty DataFrame for example with ' - 'insertion code.') - - self.assertEqual(self.data.loc[3303, 'icode'], '102A') - self.assertEqual(self.data.loc[3303, 'aa'], 'I') - self.assertEqual(self.data.loc[3303, 'ss'], 'H') - self.assertEqual(self.data.loc[3303, 'acc'], 55) - self.assertEqual(self.data.loc[3303, 'phi'], -92.9) - self.assertEqual(self.data.loc[3303, 'psi'], -50.1) - self.assertNotEqual(self.data.loc[3303, 'icode'], 102) - - self.assertEqual(self.data.loc[6402, 'icode'], '187J') - self.assertEqual(self.data.loc[6402, 'aa'], 'L') - self.assertTrue(numpy.isnan(self.data.loc[6402, 'ss'])) - self.assertEqual(self.data.loc[6402, 'acc'], 92) - self.assertEqual(self.data.loc[6402, 'phi'], -57.8) - self.assertEqual(self.data.loc[6402, 'psi'], 360) - self.assertNotEqual(self.data.loc[6402, 'psi'], 800) - - def test_empty(self): - with self.assertRaises(ValueError): - self.residues_parser(path.join(path.dirname(__file__), "DSSP/empty.dssp")) - - -if __name__ == '__main__': - suite = unittest.TestLoader().loadTestsFromTestCase(TestDSSPParser) - unittest.TextTestRunner(verbosity=2).run(suite) diff --git a/tests/test_to_table_ensembl.py b/tests/test_to_table_ensembl.py deleted file mode 100644 index e007e75..0000000 --- a/tests/test_to_table_ensembl.py +++ /dev/null @@ -1,200 +0,0 @@ -#!/local/bin/python -# -*- coding: utf-8 -*- - - -import unittest -from os import path - -import pandas as pd - -from proteofav.variants import _fetch_ensembl_variants - - -class TestENSEMBLParser(unittest.TestCase): - """Test Ensembl fetcher/parser methods.""" - - def setUp(self): - """Initialize the framework for testing.""" - self.uniprot_id = 'O96013' - self.ensembl_id = 'ENSP00000326864' - self.ensembl_id_error1 = '' - self.ensembl_id_error2 = '1234 ads' - self.ensembl_id_error3 = 1234567890102340 - self.ensembl_id_error4 = () - self.ensembl_id_error5 = [] - self.variant_id = 'rs557625940' - self.variant_id_error1 = '' - self.variant_id_error2 = 123456 - self.variant_id_error3 = [] - self.ensembl_trascript = _fetch_ensembl_variants - self.fetch_variant = _fetch_ensembl_variants - - def tearDown(self): - """Remove testing framework.""" - - self.uniprot_id = None - self.ensembl_id = None - self.ensembl_id_error1 = None - self.ensembl_id_error2 = None - self.ensembl_id_error3 = None - self.ensembl_id_error4 = None - self.ensembl_id_error5 = None - self.variant_id = None - self.variant_id_error1 = None - self.variant_id_error2 = None - self.variant_id_error3 = None - self.ensembl_trascript = None - self.fetch_variant = None - self.uniprot_variants = None - - def test_querying_ensembl_transcript_variants(self): - data = self.fetch_variant(self.ensembl_id, feature='transcript_variation') - - # doesn't check anything about the output - self.assertIsInstance(data, pd.DataFrame) - - def test_querying_ensembl_somatic_variants(self): - data = self.fetch_variant( - self.ensembl_id, feature='somatic_transcript_variation') - - # doesn't check anything about the output - self.assertIsInstance(data, pd.DataFrame) - - def test_to_table_transcript_variants_ensembl(self): - """ - Tests the fetching and parsing real Ensembl Protein ids. - - Some checks are made to whether the parsed keys and values - are the ones we are expecting. - - Using mocking because variant data varies over time. - For simplicity here loading the resulting pandas table from a - dumped csv file. - """ - - # data = self.ensembl_trascript(self.ensembl_id, species='human') - # mocking the resulting pandas dataframe - variants = path.join(path.dirname(__file__), - "VARIATION/transcript_variation_{}.csv".format(self.ensembl_id)) - data = pd.read_csv(variants) - - # number of values per column (or rows) - self.assertEqual(len(data), 206) - - # number of keys (or columns) - self.assertEqual(len(data.columns.values), 16) - - # check whether there are particular keys - self.assertIn('Parent', data.columns.values) - - # check the values for particular entries - self.assertTrue(data['Parent'][0] == 'ENST00000321944') - self.assertTrue(data['feature_type'][0] == "transcript_variation") - self.assertEqual(data['codons'][0], 'Cat/Tat') - self.assertEqual(data['start'][0], 135) - - def test_to_table_somatic_variants_ensembl(self): - """ - Tests the fetching and parsing real Ensembl Protein ids. - - Some checks are made to whether the parsed keys and values - are the ones we are expecting. - - Using mocking because variant data varies over time. - For simplicity here loading the resulting pandas table from a - dumped csv file. - """ - - # data = self.ensembl_somatic(self.ensembl_id, species='human') - # mocking the resulting pandas dataframe - variants = path.join(path.dirname(__file__), - "VARIATION/somatic_variation_{}.csv".format(self.ensembl_id)) - data = pd.read_csv(variants) - - # number of values per column (or rows) - self.assertEqual(len(data), 40) - - # number of keys (or columns) - self.assertEqual(len(data.columns.values), 16) - - # check whether there are particular keys - self.assertIn('Parent', data.columns.values) - - # check the values for particular entries - self.assertTrue(data['Parent'][0] == 'ENST00000321944') - self.assertTrue(data['feature_type'][0] == "somatic_transcript_variation") - self.assertEqual(data['codons'][0], 'Gag/Cag') - self.assertEqual(data['start'][0], 119) - - def test_to_table_ensembl_variant(self): - """ - Tests the fetching and parsing real Ensembl Variant ids. - - Some checks are made to whether the parsed keys and values - are the ones we are expecting. - - Using mocking because variant data varies over time. - For simplicity here loading the resulting pandas table from a - dumped csv file. - """ - - # data = self.ensembl_variant(self.variant_id, species='human') - # mocking the resulting pandas dataframe - variants = path.join(path.dirname(__file__), - "VARIATION/ensembl_variation_{}.csv".format(self.variant_id)) - data = pd.read_csv(variants) - - # number of values per column (or rows) - self.assertEqual(len(data), 1) - - # number of keys (or columns) - self.assertEqual(len(data.columns.values), 19) - - # check whether there are particular keys - self.assertIn('location', data.columns.values) - - # check the values for particular entries - self.assertEqual(data['location'][0], '19:39175331-39175331') - self.assertTrue(data['name'][0] == "rs557625940") - self.assertEqual(data['seq_region_name'][0], 19) - self.assertEqual(data['most_severe_consequence'][0], 'missense_variant') - - def test_to_table_uniprot_ensembl_variants(self): - """ - Tests the wrapper method that goes from a uniprot to a list - of ensembl protein transcripts and to variants. - - Using mocking because variant data varies over time. - For simplicity here loading the resulting pandas table from a - dumped csv file. - """ - - # querying the various ensembl endpoints - # data = self.uniprot_variants(self.uniprot_id) - # mocking the resulting pandas dataframe - variants = path.join(path.dirname(__file__), - "VARIATION/uniprot_variants_{}.csv".format(self.uniprot_id)) - data = pd.read_csv(variants) - - # number of values per column (or rows) - self.assertEqual(len(data), 903) - - # number of keys (or columns) - self.assertEqual(len(data.columns.values), 5) - - # check whether there are particular keys - self.assertIn('translation', data.columns.values) - self.assertIn('id', data.columns.values) - self.assertIn('start', data.columns.values) - self.assertIn('residues', data.columns.values) - - # check the values for particular entries - self.assertEqual(data['translation'][0], 'ENSP00000351049') - self.assertTrue(data['id'][0] == "rs769098772") - self.assertTrue(data['start'][0] == 295) - self.assertTrue(data['residues'][0] == "E/A") - - -if __name__ == '__main__': - suite = unittest.TestLoader().loadTestsFromTestCase(TestENSEMBLParser) - unittest.TextTestRunner(verbosity=2).run(suite) diff --git a/tests/test_to_table_mmcif.py b/tests/test_to_table_mmcif.py deleted file mode 100644 index b99958a..0000000 --- a/tests/test_to_table_mmcif.py +++ /dev/null @@ -1,140 +0,0 @@ -#!/local/bin/python -# -*- coding: utf-8 -*- - - -import logging -import sys -import unittest -try: - from mock import patch -except ImportError: - # python 3.5 - from unittest.mock import patch -from os import path - -from proteofav.config import Defaults -from proteofav.structures import _mmcif_atom, _mmcif_fields, select_cif -from proteofav.utils import get_preferred_assembly_id - -log = logging.getLogger(__name__) - -defaults = Defaults("config.txt") - - -@patch("proteofav.structures.defaults", defaults) -class TestMMCIFParser(unittest.TestCase): - """Test the mmCIF parser methods.""" - - def setUp(self): - """Initialize the framework for testing.""" - self.example_mmcif = path.join(path.dirname(__file__), "CIF/2pah.cif") - self.mmcif_atom_parser = _mmcif_atom - self.mmcif_info_parser = _mmcif_fields - self.example_tsv_out = path.join(path.dirname(__file__), "CIF/2pah-bio.tsv") - self.select_cif = select_cif - self.best_assembly = get_preferred_assembly_id - self.pdbid = '2pah' - - def tearDown(self): - """Remove testing framework.""" - - self.example_mmcif = None - self.mmcif_atom_parser = None - self.mmcif_info_parser = None - self.example_tsv_out = None - self.select_cif = None - self.best_assembly = None - self.pdbid = None - - def test_atom_to_table_mmcif(self): - """ - Tests the parsing real mmCIF files. - - Some checks are made to whether the parsed keys and values - are the ones we are expecting. - - Parsing of ATOM and HETATOM lines. - """ - - data = self.mmcif_atom_parser(self.example_mmcif) - - # number of values per column (or rows) - self.assertEqual(len(data), 5317) - - # number of keys (or columns) - self.assertEqual(len(data.columns.values), 21) - - # check whether there are particular keys - self.assertIn('label_asym_id', data.columns.values) - - # check the values for particular entries - self.assertTrue(data.loc[1, 'label_asym_id'] == 'A') - self.assertEqual(data.loc[1, 'pdbx_PDB_model_num'], 1) - self.assertEqual(data['group_PDB'][0], 'ATOM') - - def test_info_to_table_mmcif(self): - """ - Tests the parsing real mmCIF files. - - Some checks are made to whether the parsed keys and values - are the ones we are expecting. - - Parsing all lines other than ATOM/HETATOM lines. - """ - - # describes possible macromolecular assemblies - assembly = self.mmcif_info_parser(self.example_mmcif, - field_name='_pdbx_struct_assembly.') - # check some data values - self.assertEqual(assembly.loc[0, 'details'], 'author_and_software_defined_assembly') - self.assertEqual(assembly.loc[0, 'oligomeric_details'], 'tetrameric') - self.assertEqual(assembly.loc[0, 'oligomeric_count'], 4) - - # details the generation of each macromolecular assembly - assembly_gen = self.mmcif_info_parser(self.example_mmcif, - field_name='_pdbx_struct_assembly_gen.') - # check some data values - self.assertEqual(assembly_gen.loc[0, 'asym_id_list'], 'A,C,B,D') - - # details translation and rotation operations required to generate/transform - # assembly coordinates - oper_list = self.mmcif_info_parser(self.example_mmcif, - field_name='_pdbx_struct_oper_list.', - require_index=True) - # check some data values - self.assertEqual(oper_list.loc[0, 'type'], 'identity operation') - - def test_bio_unit_to_table_mmcif(self): - """ - Tests the parsing real mmCIF files. - - Some checks are made to whether the parsed keys and values - are the ones we are expecting. - - Parses the atom lines and the info lines and looks for - biological assemblies. Finds the most likely and generates - a new pandas Dataframe with the new atoms. - """ - - # new approach that looks up the biological assemblies and - # gets the preferred one from the PDBe server instead of - # generating it locally - - # test loading the atom lines with biological assemblies - best_assembly = self.best_assembly(self.pdbid) - data = self.select_cif(self.pdbid, biounit=True, - assembly_id=best_assembly) - - # check some values - # Biological assemblies from the PDBe come with updated chains - # (auth_aym_id and label_aym_id) and two extra columns with the - # original chain identifiers - self.assertIn('orig_label_asym_id', data) - self.assertIn('orig_auth_asym_id', data) - - -if __name__ == '__main__': - logging.basicConfig(stream=sys.stderr) - logging.getLogger("mmCIF related methods").setLevel(logging.DEBUG) - suite = unittest.TestLoader().loadTestsFromTestCase(TestMMCIFParser) - unittest.TextTestRunner(verbosity=2).run(suite) diff --git a/tests/test_to_table_sifts.py b/tests/test_to_table_sifts.py deleted file mode 100644 index 65edfa2..0000000 --- a/tests/test_to_table_sifts.py +++ /dev/null @@ -1,131 +0,0 @@ -#!/local/bin/python -# -*- coding: utf-8 -*- - - -import unittest -from os import path - -from proteofav.structures import _sifts_residues_regions, sifts_best -from proteofav.utils import (_pdb_uniprot_sifts_mapping, - _uniprot_pdb_sifts_mapping) - - -class TestSIFTSParser(unittest.TestCase): - """Test the SIFTS parser methods.""" - - def setUp(self): - """Initialize the framework for testing.""" - self.example_xml = path.join(path.dirname(__file__), "SIFTS/2pah.xml") - self.residues_parser = _sifts_residues_regions - - self.pdb_id = '2pah' - self.uniprot_id = 'P00439' - self.pdb_uniprot = _pdb_uniprot_sifts_mapping - self.uniprot_pdb = _uniprot_pdb_sifts_mapping - self.pdb_best = sifts_best - - def tearDown(self): - """Remove testing framework.""" - - self.example_xml = None - self.residue_parser = None - - self.pdb_id = None - self.uniprot_id = None - self.pdb_uniprot = None - self.uniprot_uniprot = None - self.pdb_best = None - - def test_to_table_sifts_residues_and_regions(self): - """ - Tests the parsing real SIFTS xml files. - This test focuses on the method that parses the residue entries - and the region entries. - - Some checks are made to whether the parsed keys and values - are the ones we are expecting. - """ - - data = self.residues_parser(self.example_xml, - sources=('CATH', 'SCOP', 'Pfam')) - - # number of values per column (or rows) - self.assertEqual(len(data), 670) - - # number of keys (or columns) - self.assertEqual(len(data.columns.values), 17) - - # check whether there are particular keys - self.assertIn('CATH_dbAccessionId', data.columns.values) - - # check the values for particular entries - self.assertTrue(data['CATH_dbAccessionId'][0] == '1.10.800.10') - self.assertEqual(data['PDB_dbChainId'][0], 'A') - self.assertEqual(data['PDB_dbResName'][0], 'VAL') - - # check whether there are particular keys - self.assertIn('UniProt_regionId', data.columns.values) - self.assertIn('CATH_regionId', data.columns.values) - - # check the values of particular entries - self.assertTrue(data['CATH_regionId'][0] == '1') - - def test_to_table_pdb_uniprot_sifts_mapping(self): - """ - Testing the PDBe API for mapping between PDB and UniProt - accession identifiers. - """ - - data = self.pdb_uniprot(self.pdb_id) - - # number of values per column (or rows) - self.assertEqual(len(data), 1) - - # number of keys (or columns) - self.assertEqual(len(data.columns.values), 1) - - # check whether there are particular keys - self.assertIn('uniprot_id', data.columns.values) - - # check the values of particular entries - self.assertTrue(data['uniprot_id'][0] == 'P00439') - - def test_to_table_uniprot_pdb_sifts_mapping(self): - """ - Testing the PDBe API for mapping between UniProt and PDB - accession identifiers. - """ - - data = self.uniprot_pdb(self.uniprot_id) - - # check whether there are particular keys - self.assertIn('pdb_id', data.columns.values) - - # check the values of particular entries - self.assertEqual(data['pdb_id'].unique()[0], '2pah') - self.assertIn('A', data['chain_id'].unique()) - self.assertIn('X-ray diffraction', data['experimental_method'].unique()) - self.assertTrue(type(data['coverage'][0]), float) - self.assertTrue(type(data['resolution'][0]), float) - self.assertTrue(type(data['tax_id'][0]), int) - - def test_to_table_uniprot_pdb_sifts_best(self): - """ - Testing the PDBe API for mapping between UniProt and PDB - accession identifiers. - """ - - data = self.pdb_best(self.uniprot_id, first=True) - - # number of values - self.assertEqual(len(data), 10) - - # number of keys (or columns) - self.assertIn('coverage', data) - self.assertIn('pdb_id', data) - self.assertIn('chain_id', data) - - -if __name__ == '__main__': - suite = unittest.TestLoader().loadTestsFromTestCase(TestSIFTSParser) - unittest.TextTestRunner(verbosity=2).run(suite) diff --git a/tests/test_to_table_uniprot.py b/tests/test_to_table_uniprot.py deleted file mode 100644 index 909224c..0000000 --- a/tests/test_to_table_uniprot.py +++ /dev/null @@ -1,101 +0,0 @@ -#!/local/bin/python -# -*- coding: utf-8 -*- -import numpy as np -import unittest -import logging - -from proteofav.uniprot import _uniprot_info -from proteofav.variants import _uniprot_ensembl_mapping - -logging.getLogger('proteofav').setLevel(logging.CRITICAL) # turn off logging - - -class TestUNIPROTParser(unittest.TestCase): - """Test UniProt fetcher/parser methods.""" - - def setUp(self): - """Initialize the framework for testing.""" - self.uniprot_id = 'O96013' - self.uniprot_id_error1 = '' - self.uniprot_id_error2 = '1234 ads' - self.uniprot_id_error3 = 1234 - self.uniprot_id_error4 = () - self.uniprot_id_error5 = [] - self.uniprot_info = _uniprot_info - self.uniprot_ensembl = _uniprot_ensembl_mapping - - def tearDown(self): - """Remove testing framework.""" - - self.uniprot_id = None - self.uniprot_id_error1 = None - self.uniprot_id_error2 = None - self.uniprot_id_error3 = None - self.uniprot_id_error4 = None - self.uniprot_id_error5 = None - self.uniprot_info = None - self.uniprot_ensembl = None - - def test_to_table_uniprot_info(self): - """ - Tests the fetching and parsing real UniProt ids. - This test focuses on the method that parses the residue entries. - - Some checks are made to whether the parsed keys and values - are the ones we are expecting. - """ - - data = self.uniprot_info(self.uniprot_id) - - # number of values per column (or rows) - self.assertEqual(len(data), 1) - - # number of keys (or columns) - self.assertEqual(len(data.columns.values), 8) - - # check whether there are particular keys - self.assertIn('Sequence', data.columns.values) - - # check the values for particular entries - self.assertTrue(data['Length'][0] == 591) - self.assertTrue(data['Status'][0] == "reviewed") - self.assertEqual(data['Entry name'][0], 'PAK4_HUMAN') - - def test_to_table_uniprot_ensembl_mapping(self): - """ - Tests the fetching and parsing real UniProt ids. - This test focuses on the method that parses the residue entries. - - Some checks are made to whether the parsed keys and values - are the ones we are expecting. - """ - - data = self.uniprot_ensembl(self.uniprot_id, 'homo_sapiens') - - # number of values per column (or rows) - self.assertEqual(len(data), 1) - - # number of keys (or columns) - self.assertEqual(len(data.columns.values), 3) - - # check whether there are particular keys - self.assertIn('TRANSCRIPT', data.columns.values) - - # check the values for particular entries - self.assertEqual(data['GENE'][0], 'ENSG00000130669') - - def test_obsolete_uniprot_accession(self): - data = self.uniprot_info('Q91887') - self.assertEqual(len(data), 1) - - # number of keys (or columns) - self.assertEqual(len(data.columns.values), 8) - - # check the values for particular entries - self.assertTrue(np.isnan(data.iloc[0, -1])) # 'Length' - self.assertTrue(np.isnan(data.iloc[0, -1])) # 'Status' - - -if __name__ == '__main__': - suite = unittest.TestLoader().loadTestsFromTestCase(TestUNIPROTParser) - unittest.TextTestRunner(verbosity=2).run(suite) diff --git a/tests/test_to_table_validation.py b/tests/test_to_table_validation.py deleted file mode 100644 index c3084d3..0000000 --- a/tests/test_to_table_validation.py +++ /dev/null @@ -1,38 +0,0 @@ -#!/local/bin/python -# -*- coding: utf-8 -*- - - -import unittest -from os import path - -from proteofav.structures import _pdb_validation_to_table - - -class TestValidationParser(unittest.TestCase): - """Initial testing for parsing PDB validation xml files.""" - - def setUp(self): - """Initialize the framework for testing.""" - self.path_2pah = path.join(path.dirname(__file__), - "VALIDATION/2pah_validation.xml") - self.parser = _pdb_validation_to_table - - def tearDown(self): - """Remove testing framework.""" - self.path_2pah = None - self.parser = None - - def test_to_2pah(self): - """ - """ - data = self.parser(self.path_2pah) - self.assertFalse(data.empty, 'Parser returned an empty DataFrame') - self.assertEqual(data.shape, (653, 26), 'Parser returned a DataFrame ' - 'with unexpected shape') - self.assertEqual(data.chain.unique().tolist(), ['A', 'B']) - self.assertEqual(data.loc[626, 'resname'], 'THR') - - -if __name__ == '__main__': - suite = unittest.TestLoader().loadTestsFromTestCase(TestValidationParser) - unittest.TextTestRunner(verbosity=2).run(suite) diff --git a/tests/test_uniprot.py b/tests/test_uniprot.py deleted file mode 100644 index e6a8ed5..0000000 --- a/tests/test_uniprot.py +++ /dev/null @@ -1,161 +0,0 @@ -# coding=utf-8 -import unittest - -try: - import mock -except ImportError: - import unittest.mock as mock -from requests.exceptions import HTTPError - -from proteofav.uniprot import (fetch_uniprot_sequence, fetch_uniprot_formal_specie, _uniprot_info, - _fetch_uniprot_gff, map_gff_features_to_sequence, - _uniprot_to_ensembl_xref) -from proteofav.utils import get_url_or_retry - - -class UniprotTestCase(unittest.TestCase): - """Test for the Uniprot.py""" - - def setUp(self): - """Initialize the framework for testing.""" - self.get_url_or_retry = get_url_or_retry - self.get_uniprot_sequence = fetch_uniprot_sequence - self.get_uniprot_organism = fetch_uniprot_formal_specie - self.fetch_uniprot_gff = _fetch_uniprot_gff - self.uniprot_info = _uniprot_info - self.map_gff_features_to_sequence = map_gff_features_to_sequence - self.uniprot_to_ensembl_xref = _uniprot_to_ensembl_xref - self.mock_url = 'www.mockurl.com' - self.ccc2_sequence = ("MREVILAVHGMTCSACTNTINTQLRALKGVTKCDISLVTNECQVTYDNEVTADSIKEIIE" - "DCGFDCEILRDSEITAISTKEGLLSVQGMTCGSCVSTVTKQVEGIEGVESVVVSLVTEEC" - "HVIYEPSKTTLETAREMIEDCGFDSNIIMDGNGNADMTEKTVILKVTKAFEDESPLILSS" - "VSERFQFLLDLGVKSIEISDDMHTLTIKYCCNELGIRDLLRHLERTGYKFTVFSNLDNTT" - "QLRLLSKEDEIRFWKKNSIKSTLLAIICMLLYMIVPMMWPTIVQDRIFPYKETSFVRGLF" - "YRDILGVILASYIQFSVGFYFYKAAWASLKHGSGTMDTLVCVSTTCAYTFSVFSLVHNMF" - "HPSSTGKLPRIVFDTSIMIISYISIGKYLETLAKSQTSTALSKLIQLTPSVCSIISDVER" - "NETKEIPIELLQVNDIVEIKPGMKIPADGIITRGESEIDESLMTGESILVPKKTGFPVIA" - "GSVNGPGHFYFRTTTVGEETKLANIIKVMKEAQLSKAPIQGYADYLASIFVPGILILAVL" - "TFFIWCFILNISANPPVAFTANTKADNFFICLQTATSVVIVACPCALGLATPTAIMVGTG" - "VGAQNGVLIKGGEVLEKFNSITTFVFDKTGTLTTGFMVVKKFLKDSNWVGNVDEDEVLAC" - "IKATESISDHPVSKAIIRYCDGLNCNKALNAVVLESEYVLGKGIVSKCQVNGNTYDICIG" - "NEALILEDALKKSGFINSNVDQGNTVSYVSVNGHVFGLFEINDEVKHDSYATVQYLQRNG" - "YETYMITGDNNSAAKRVAREVGISFENVYSDVSPTGKCDLVKKIQDKEGNNKVAVVGDGI" - "NDAPALALSDLGIAISTGTEIAIEAADIVILCGNDLNTNSLRGLANAIDISLKTFKRIKL" - "NLFWALCYNIFMIPIAMGVLIPWGITLPPMLAGLAMAFSSVSVVLSSLMLKKWTPPDIES" - "HGISDFKSKFSIGNFWSRLFSTRAIAGEQDIESQAGLMSNEEVL") - - def tearDown(self): - """Remove testing framework by cleaning the namespace.""" - self.get_uniprot_sequence = None - self.get_url_or_retry = None - self.silly_url = None - - def test_get(self): - with mock.patch('proteofav.utils.requests') as mock_get: - mock_get.get.return_value.ok = True - mock_get.get.return_value.status = 200 - self.get_url_or_retry(self.mock_url) - mock_get.get.assert_called_once_with(mock.ANY, headers=mock.ANY, params=mock.ANY) - - @unittest.expectedFailure - def test_raise_for_not_found(self): - with mock.patch('proteofav.utils.requests.get') as mock_get: - with self.assertRaises(HTTPError) as context: - mock_get.get.return_value.ok = False - mock_get.get.return_value.status = 404 - response = self.get_url_or_retry(self.mock_url) - mock_get.side_effect = HTTPError(mock.Mock(status=404), 'not found') - - # self.assertTrue('not found' in context.exception) - self.assertIsNone(response) - mock_get.get.assert_called_once_with(mock.ANY, headers=mock.ANY, params=mock.ANY) - - def test_mock_a_ptn_sequence(self): - """ - Test _uniprot_info table parsing with a Mock request. - - ..note: - query=accession%3AP38995&contact=%20"&columns=id%2Csequence%2C&format=tab - """ - - table = """Entry Sequence\nP38995 """ + self.ccc2_sequence - - - with mock.patch('proteofav.utils.requests') as mock_get: - mock_get.get.return_value.ok = True - mock_get.get.return_value.status = 200 - mock_get.get.return_value.content = table - self.assertEqual(self.get_uniprot_sequence('P38995'), self.ccc2_sequence) - - mock_get.get.assert_called_once_with('http://www.uniprot.org/uniprot/', - headers=mock.ANY, params=mock.ANY) - - def test_mock_a_ptn_organism_name(self): - """ - Test whether the UniProt info table is parsed correctly by mocking the request. - - ..note:: query=accession%3AP38995&contact=%20"&columns=id%2Corganism%2C&format=tab - """ - ccc2_organism = 'Saccharomyces cerevisiae' - table = """Entry Organism\nP38995 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)""" - - with mock.patch('proteofav.utils.requests') as mock_get: - mock_get.get.return_value.ok = True - mock_get.get.return_value.status = 200 - mock_get.get.return_value.content = table - self.assertEqual(self.get_uniprot_organism('P38995'), ccc2_organism) - - mock_get.get.assert_called_once_with('http://www.uniprot.org/uniprot/', - headers=mock.ANY, - params=mock.ANY) - - def test_uniprot_info_with_defaults(self): - """ - Test whether Uniprot query logic still valid. - - ..note: - Intentionally get info from Uniprot. An Uniprot update may break this. - """ - - cols = ("Entry", "Entry name", "Status", "Protein names", "Gene names", "Organism", - "Sequence", "Length") - - first_field = "P38995" - last_field = 1004 - - table = self.uniprot_info('P38995') - self.assertEqual(set(table.columns), set(cols)) - self.assertEqual(table.iloc[0, 0], first_field) - self.assertEqual(table.iloc[0, -1], last_field) - - def test_fetch_uniprot_gff(self): - """ - Test whether Uniprot GFF logic still valid. - """ - table = self.fetch_uniprot_gff('P38995') - - self.assertTrue(set("NAME SOURCE TYPE START END SCORE STRAND FRAME GROUP".split()) - .issubset(table.columns)) - self.assertTrue(table['empty'].isnull().all()) - self.assertTrue(table['END'].max() <= len(self.ccc2_sequence)) - - def test_map_uniprot_gff(self): - table = self.map_gff_features_to_sequence('P38995') - - self.assertEqual(list(table.columns), ['annotation']) - self.assertTrue((~table.annotation.str.contains('Chain')).all()) - self.assertEqual(table.shape[0], len(self.ccc2_sequence)) - - def test_map_uniprot_gff_un_grouped(self): - table = map_gff_features_to_sequence('P38995', group_residues=False) - self.assertEqual(set(table.columns), {'annotation', 'idx'}) - self.assertTrue(table.idx.max() >= len(self.ccc2_sequence)) - - def test_uniprot_to_ensembl_xref(self): - self.assertTrue(self.uniprot_to_ensembl_xref('P38995').empty) - table = self.uniprot_to_ensembl_xref('P38995', 'saccharomyces_cerevisiae') - self.assertEqual(set(table.columns), {'id', 'type'}) - - -if __name__ == '__main__': - unittest.main() diff --git a/tests/test_utils.py b/tests/test_utils.py new file mode 100644 index 0000000..39c054d --- /dev/null +++ b/tests/test_utils.py @@ -0,0 +1,438 @@ +# -*- coding: utf-8 -*- + +import os +import re +import sys +import json +import logging +import requests +import responses +import unittest +import numpy as np +import pandas as pd +import requests_cache + +try: + import mock +except ImportError: + import unittest.mock as mock + +from proteofav.utils import (fetch_from_url_or_retry, + InputFileHandler, OutputFileHandler, + row_selector, constrain_column_types, + exclude_columns, Downloader, GenericInputs, + flatten_nested_structure, + refactor_key_val_singletons, + splitting_up_by_key, + merging_down_by_key) + +from proteofav.config import defaults as config + + +def response_mocker(kwargs, base_url, endpoint_url, status=200, + content_type='application/json', post=False, data=None): + """ + Generates a mocked requests response for a given set of + kwargs, base url and endpoint url + """ + + url = re.sub('\{\{(?P[a-zA-Z_]+)\}\}', lambda m: "%s" % kwargs.get(m.group(1)), + base_url + endpoint_url) + with responses.RequestsMock() as rsps: + if post: + rsps.add(responses.POST, url, + body=b'{"data": "some json formatted output"}', + status=status, content_type='application/json') + response = requests.post(url, data=data) + + elif content_type == 'application/json': + rsps.add(responses.GET, url, + body=b'{"data": "some json formatted output"}', + status=status, content_type='application/json') + response = requests.get(url) + elif content_type == 'text/plain': + rsps.add(responses.GET, url, + body="Some text-based content\n spanning multiple lines", + status=status, content_type='text/plain') + response = requests.get(url) + else: + rsps.add(responses.GET, url, + body=b"Some other binary stuff...", + status=status, content_type='application/octet-stream') + response = requests.get(url) + return response + + +class TestUTILS(unittest.TestCase): + """Test the utility methods.""" + + def setUp(self): + """Initialize the framework for testing.""" + + requests_cache.uninstall_cache() + + self.fetch_from_url_or_retry = fetch_from_url_or_retry + self.row_selector = row_selector + self.mock_df = pd.DataFrame( + [{'label': '1', 'value': 1, 'type': 23.4}, + {'label': '2', 'value': 1, 'type': 1}, + {'label': '3', 'value': 2, 'type': np.nan}, + {'label': '4', 'value': 3, 'type': 123.1}, + {'label': '5', 'value': 5, 'type': 0.32}]) + + self.InputFileHandler = InputFileHandler + self.OutputFileHandler = OutputFileHandler + self.constrain_column_types = constrain_column_types + self.exclude_columns = exclude_columns + + self.pdbid = "2pah" + root = os.path.abspath(os.path.dirname(__file__)) + self.outputcif = os.path.join(os.path.join(root, "testdata", + "{}.cif".format(self.pdbid))) + self.outputsifts = os.path.join(os.path.join(root, "testdata", + "{}.xml".format(self.pdbid))) + self.Downloader = Downloader + self.GenericInputs = GenericInputs + self.mock_url = 'www.mockurl.com' + + self.splitting_up_by_key = splitting_up_by_key + self.merging_down_by_key = merging_down_by_key + self.flatten_nested_structure = flatten_nested_structure + self.refactor_key_val_singletons = refactor_key_val_singletons + + self.vars_mock = pd.DataFrame([{'xrefs_id': ['id1', 'id2'], 'other_key': 123}, + {'xrefs_id': ['id1', 'id2', 'id3'], 'other_key': 456}]) + + self.vars_mock2 = pd.DataFrame([{'xrefs_id': 'id1', 'other_key': []}, + {'xrefs_id': 'id2', 'other_key': 123}, + {'xrefs_id': 'id1', 'other_key': []}, + {'xrefs_id': 'id3', 'other_key': 'string'}, + {'xrefs_id': 'id2', 'other_key': 245}, + {'xrefs_id': 'id3', 'other_key': np.nan}]) + + self.json_mock = { + 'M1': [{'d1': 1}, + {'d1': 2}, + {'d2': 3}, + {'d3': {'dd3': 'dd3'}}], + 'M2': 'value', + 'M3': {'x1': + {'x2': 1, 'x3': 2} + }, + 'M4': 'four', + 'M5': [1, 2, 3], + 'M6': {'z1': 'z1'} + } + + def tearDown(self): + """Remove testing framework.""" + + self.fetch_from_url_or_retry = None + self.row_selector = None + self.mock_df = None + + self.InputFileHandler = None + self.OutputFileHandler = None + self.constrain_column_types = None + self.exclude_columns = None + self.pdbid = None + self.outputcif = None + self.outputsifts = None + self.Downloader = None + self.GenericInputs = None + self.mock_url = None + self.splitting_up_by_key = None + self.merging_down_by_key = None + self.flatten_nested_structure = None + self.refactor_key_val_singletons = None + self.vars_mock = None + self.vars_mock2 = None + self.json_mock = None + + def test_fetch_from_url_or_retry_get_json(self): + # mocked requests + identifier = "2pah" + base_url = config.api_pdbe + endpoint_url = "pdb/entry/summary/" + response = response_mocker(kwargs={identifier}, base_url=base_url, + endpoint_url=endpoint_url, + content_type='application/json') + self.fetch_from_url_or_retry = mock.MagicMock(return_value=response) + url = base_url + endpoint_url + identifier + r = self.fetch_from_url_or_retry(url, json=True, + header={'application/json'}).json() + self.assertEqual(r, json.loads('{"data": "some json formatted output"}')) + + def test_fetch_from_url_or_retry_get_binary(self): + # mocked requests + identifier = "P00439" + base_url = config.api_uniprot + endpoint_url = "{}.fasta".format(identifier) + response = response_mocker(kwargs={"P00439.fasta"}, base_url=base_url, + endpoint_url="", + content_type='application/octet-stream') + self.fetch_from_url_or_retry = mock.MagicMock(return_value=response) + url = base_url + endpoint_url + r = self.fetch_from_url_or_retry(url, json=True, + header={'application/octet-stream'}, + retry_in=None, wait=0, + n_retries=10, stream=False).content + self.assertEqual(r, b"Some other binary stuff...") + + def test_fetch_from_url_or_retry_post_json(self): + # mocked requests + identifier = "1csb, 2pah" + base_url = config.api_pdbe + endpoint_url = "pdb/entry/summary/" + response = response_mocker(kwargs={}, base_url=base_url, + endpoint_url=endpoint_url, + content_type='application/octet-stream', + post=True, data=identifier) + self.fetch_from_url_or_retry = mock.MagicMock(return_value=response) + url = base_url + endpoint_url + identifier + r = self.fetch_from_url_or_retry(url, json=True, post=True, data=identifier, + header={'application/octet-stream'}, + retry_in=None, wait=0, + n_retries=10, stream=False).json() + self.assertEqual(r, json.loads('{"data": "some json formatted output"}')) + + def test_fetch_from_url_or_retry_get_404(self): + # mocked requests + identifier = "P00439" + base_url = config.api_uniprot + endpoint_url = "{}.fasta".format(identifier) + response = response_mocker(kwargs={"P00439.fasta"}, base_url=base_url, + endpoint_url="", + content_type='text/plain', status=404) + self.fetch_from_url_or_retry = mock.MagicMock(return_value=response) + url = base_url + endpoint_url + r = self.fetch_from_url_or_retry(url, json=True, header={'text/plain'}, + retry_in=None, wait=0, + n_retries=10, stream=False) + self.assertEqual(r.status_code, 404) + self.assertFalse(r.ok) + + def test_fetch_from_url_or_retry_get_500(self): + # mocked requests + identifier = "P00439" + base_url = config.api_uniprot + endpoint_url = "{}.fasta".format(identifier) + response = response_mocker(kwargs={"P00439.fasta"}, base_url=base_url, + endpoint_url="", + content_type='text/plain', status=500) + self.fetch_from_url_or_retry = mock.MagicMock(return_value=response) + url = base_url + endpoint_url + r = self.fetch_from_url_or_retry(url, json=True, header={'text/plain'}, + retry_in=(500,), wait=1, + n_retries=10, stream=False) + self.assertEqual(r.status_code, 500) + self.assertFalse(r.ok) + + def test_get(self): + with mock.patch('proteofav.utils.requests') as mock_get: + mock_get.get.return_value.ok = True + mock_get.get.return_value.status = 200 + self.fetch_from_url_or_retry(self.mock_url) + mock_get.get.assert_called_once_with(mock.ANY, headers=mock.ANY, + params=mock.ANY, stream=mock.ANY) + + @unittest.expectedFailure + def test_raise_for_not_found(self): + with mock.patch('proteofav.utils.requests.get') as mock_get: + with self.assertRaises(mock.HTTPError) as context: + mock_get.get.return_value.ok = False + mock_get.get.return_value.status = 404 + response = self.fetch_from_url_or_retry(self.mock_url) + mock_get.side_effect = mock.HTTPError(mock.Mock(status=404), 'not found') + + # self.assertTrue('not found' in context.exception) + self.assertIsNone(response) + mock_get.get.assert_called_once_with(mock.ANY, headers=mock.ANY, params=mock.ANY) + + def test_row_selector(self): + d = self.row_selector(self.mock_df, key='value', value=3) + self.assertEqual(len(d.index), 1) + d = self.row_selector(self.mock_df, key='value', value=3, reverse=True) + self.assertEqual(len(d.index), 4) + d = self.row_selector(self.mock_df, key='value', value='first') + self.assertEqual(len(d.index), 2) + d = self.row_selector(self.mock_df, key='value', value=(2, 3)) + self.assertEqual(len(d.index), 2) + + def test_inputfilehandler(self): + config.db_mmcif = "mmcif" + valid = os.path.join(os.path.dirname(__file__), "testdata", + config.db_mmcif, "2pah.cif") + self.InputFileHandler(valid) + + invalid = os.path.join(os.path.dirname(__file__), "testdata", + config.db_mmcif, "null.cif") + with self.assertRaises(IOError) or self.assertRaises(OSError): + self.InputFileHandler(invalid) + + def test_outputfilehandler(self): + config.db_mmcif = "mmcif" + valid = os.path.join(os.path.dirname(__file__), "testdata", + config.db_mmcif, "2pah.cif") + self.OutputFileHandler(valid, overwrite=True) + + with self.assertRaises(OSError): + self.OutputFileHandler(valid, overwrite=False) + + invalid = os.path.join(os.path.dirname(__file__), "testdata", + "NEW_DIR", "null.cif") + with self.assertRaises(OSError): + self.InputFileHandler(invalid) + + def test_download(self): + url = config.pdbe_fetch + "download/{}_updated.cif".format(self.pdbid) + self.Downloader(url=url, filename=self.outputcif, + decompress=False, overwrite=True) + os.remove(self.outputcif) + + def test_download_decompress(self): + url = config.sifts_fetch + "{}.xml.gz".format(self.pdbid) + self.Downloader(url=url, filename=self.outputsifts, + decompress=True, overwrite=True) + os.remove(self.outputsifts) + + def test_constrain_column_types(self): + dtypes = {'type': 'float64', + 'value': 'int64', + 'label': 'object'} + dnans = {'type': 0.0} + dreplaces = {'label': ['1', 'i']} + + self.mock_df = self.constrain_column_types(self.mock_df, dtypes) + self.assertEqual(self.mock_df["type"].dtype, np.float64) + self.assertEqual(self.mock_df["value"].dtype, np.int64) + self.assertEqual(self.mock_df["label"].dtype, np.object) + + self.mock_df = self.constrain_column_types(self.mock_df, dtypes, + nan_value_dict=dnans) + self.assertEqual(self.mock_df["type"].dtype, np.float64) + self.assertEqual(self.mock_df.loc[2, "type"], 0.0) + + self.mock_df = self.constrain_column_types(self.mock_df, dtypes, dnans, + replace_value_dict=dreplaces) + self.assertEqual(self.mock_df["label"].dtype, np.object) + self.assertEqual(self.mock_df.loc[0, "label"], "i") + + def test_exclude_columns(self): + self.assertEqual(len(self.mock_df.columns), 3) + self.mock_df = self.exclude_columns(self.mock_df, excluded=("type",)) + self.assertEqual(len(self.mock_df.columns), 2) + self.assertNotIn("type", self.mock_df) + + def test_generic_inputs(self): + # identifier + t = self.GenericInputs(identifier="test1") + v = t._get_identifier() + self.assertEqual(v, "test1") + v = t._get_identifier(identifier="test2") + self.assertEqual(v, "test2") + t = self.GenericInputs() + v = t._get_identifier(identifier="test2") + self.assertEqual(v, "test2") + v = self.GenericInputs(identifier="test1")._get_identifier() + self.assertEqual(v, "test1") + v = self.GenericInputs()._get_identifier(identifier="test2") + self.assertEqual(v, "test2") + v = self.GenericInputs(identifier="test1")._get_identifier(identifier="test2") + self.assertEqual(v, "test2") + + # filename + v = self.GenericInputs(filename="test1")._get_filename() + self.assertEqual(v, "test1") + v = self.GenericInputs()._get_filename(filename="test2") + self.assertEqual(v, "test2") + + # table + t = self.GenericInputs(table="test1") + v = t._get_table(table=None) + self.assertEqual(v, "test1") + v = t._get_table(table="test2") + self.assertEqual(v, "test2") + + def test_splitting_up_by_key(self): + table = self.splitting_up_by_key(self.vars_mock, key='xrefs_id') + self.assertEqual(len(self.vars_mock), 2) + self.assertEqual(len(table), 5) + self.assertEqual(table.loc[0, 'xrefs_id'], 'id1') + self.assertEqual(table.loc[1, 'xrefs_id'], 'id2') + self.assertEqual(table.loc[0, 'other_key'], 123) + self.assertEqual(table.loc[1, 'other_key'], 123) + self.assertEqual(table.loc[2, 'xrefs_id'], 'id1') + self.assertEqual(table.loc[3, 'xrefs_id'], 'id2') + self.assertEqual(table.loc[4, 'xrefs_id'], 'id3') + self.assertEqual(table.loc[2, 'other_key'], 456) + self.assertEqual(table.loc[3, 'other_key'], 456) + self.assertEqual(table.loc[4, 'other_key'], 456) + + def test_merging_down_by_key(self): + table = self.merging_down_by_key(self.vars_mock2, key='xrefs_id') + self.assertEqual(len(self.vars_mock2), 6) + self.assertEqual(len(table), 3) + self.assertEqual(table.loc[0, 'xrefs_id'], 'id1') + self.assertEqual(table.loc[1, 'other_key'], (123, 245)) + self.assertEqual(table.loc[2, 'other_key'], 'string') + + def test_flatten_nested_structure(self): + data = {} + self.flatten_nested_structure(self.json_mock, data) + # keys + self.assertIn('M1_d1', data) + self.assertIn('M1_d2', data) + self.assertIn('M1_d3_dd3', data) + self.assertNotIn('M1', data) + self.assertIn('M2', data) + self.assertIn('M3_x1_x2', data) + self.assertIn('M3_x1_x3', data) + self.assertNotIn('M3', data) + self.assertIn('M4', data) + self.assertIn('M5', data) + self.assertIn('M6_z1', data) + # values + self.assertEqual(data['M1_d1'], [1, 2]) + self.assertEqual(data['M1_d2'], [3]) + self.assertEqual(data['M1_d3_dd3'], ['dd3']) + self.assertEqual(data['M2'], ['value']) + self.assertEqual(data['M3_x1_x2'], [1]) + self.assertEqual(data['M3_x1_x3'], [2]) + self.assertEqual(data['M4'], ['four']) + self.assertEqual(data['M5'], [[1, 2, 3]]) + self.assertEqual(data['M6_z1'], ['z1']) + + def test_refactor_key_val_singletons(self): + data = {} + self.flatten_nested_structure(self.json_mock, data) + data = self.refactor_key_val_singletons(data) + # keys + self.assertIn('M1_d1', data) + self.assertIn('M1_d2', data) + self.assertIn('M1_d3_dd3', data) + self.assertNotIn('M1', data) + self.assertIn('M2', data) + self.assertIn('M3_x1_x2', data) + self.assertIn('M3_x1_x3', data) + self.assertNotIn('M3', data) + self.assertIn('M4', data) + self.assertIn('M5', data) + self.assertIn('M6_z1', data) + # values + self.assertEqual(data['M1_d1'], [1, 2]) + self.assertEqual(data['M1_d2'], 3) + self.assertEqual(data['M1_d3_dd3'], 'dd3') + self.assertEqual(data['M2'], 'value') + self.assertEqual(data['M3_x1_x2'], 1) + self.assertEqual(data['M3_x1_x3'], 2) + self.assertEqual(data['M4'], 'four') + self.assertEqual(data['M5'], [1, 2, 3]) + self.assertEqual(data['M6_z1'], 'z1') + + +if __name__ == '__main__': + logging.basicConfig(stream=sys.stderr) + logging.getLogger("proteofav.config").setLevel(logging.CRITICAL) + suite = unittest.TestLoader().loadTestsFromTestCase(TestUTILS) + unittest.TextTestRunner(verbosity=2).run(suite) diff --git a/tests/test_validation.py b/tests/test_validation.py new file mode 100644 index 0000000..2f7e5da --- /dev/null +++ b/tests/test_validation.py @@ -0,0 +1,118 @@ +# -*- coding: utf-8 -*- + +import os +import sys +import logging +import unittest + +from proteofav.validation import (parse_validation_residues, select_validation, + _fix_label_alt_id, _fix_pdb_ins_code, + _add_validation_res_full, + filter_validation, download_validation, + Validation) + + +class TestValidationParser(unittest.TestCase): + """Initial testing for parsing PDB validation xml files.""" + + def setUp(self): + """Initialize the framework for testing.""" + self.pdbid = "2pah" + self.example_validation = os.path.join(os.path.dirname(__file__), "testdata", + "validation", "2pah_validation.xml") + self.output_validation = os.path.join(os.path.dirname(__file__), "testdata", + "2pah_validation.xml") + self.parser = parse_validation_residues + self.fix_label_alt_id = _fix_label_alt_id + self.fix_pdb_ins_code = _fix_pdb_ins_code + self.filter_validation = filter_validation + self.download_validation = download_validation + self.Validation = Validation + self.add_validation_res_full = _add_validation_res_full + + def tearDown(self): + """Remove testing framework.""" + self.pdbid = None + self.example_validation = None + self.output_validation = None + self.parser = None + self.fix_label_alt_id = None + self.fix_pdb_ins_code = None + self.filter_validation = None + self.download_validation = None + self.Validation = None + self.add_validation_res_full = None + + def test_to_2pah(self): + data = self.parser(self.example_validation) + self.assertFalse(data.empty, 'Parser returned an empty DataFrame') + self.assertEqual(data.shape, (653, 26), 'Parser returned a DataFrame ' + 'with unexpected shape') + self.assertEqual(data.validation_chain.unique().tolist(), ['A', 'B']) + self.assertEqual(data.loc[626, 'validation_resname'], 'THR') + + def test_fix_label_alt_id(self): + data = self.parser(self.example_validation, fix_label_alt_id=False) + self.assertEqual('118', data.loc[0, 'validation_resnum']) + self.assertEqual(' ', data.loc[0, 'validation_altcode']) + data = self.fix_label_alt_id(data) + self.assertEqual('118', data.loc[0, 'validation_resnum']) + self.assertEqual('.', data.loc[0, 'validation_altcode']) + + def test_fix_type_symbol(self): + data = self.parser(self.example_validation, fix_ins_code=False) + self.assertEqual('118', data.loc[0, 'validation_resnum']) + self.assertEqual(' ', data.loc[0, 'validation_icode']) + data = self.fix_pdb_ins_code(data) + self.assertEqual('118', data.loc[0, 'validation_resnum']) + self.assertEqual('?', data.loc[0, 'validation_icode']) + + def test_filter_validation_chain(self): + data = self.parser(self.example_validation) + data = self.filter_validation(data, chains=('A',)) + self.assertNotIn("B", data.validation_chain.unique()) + + def test_filter_validation_res(self): + data = self.parser(self.example_validation) + data = self.filter_validation(data, res=('118',)) + self.assertNotIn('119', data.validation_resnum.unique()) + + def test_filter_validation_add_res_full(self): + data = self.parser(self.example_validation) + self.assertIn('validation_resnum', data) + self.assertIn('validation_icode', data) + self.assertNotIn('validation_resnum_full', data) + data = self.add_validation_res_full(data) + self.assertIn('validation_resnum_full', data) + self.assertEqual(data.loc[0, 'validation_resnum_full'], '118') + data = self.parser(self.example_validation) + data = self.filter_validation(data, add_res_full=True) + self.assertEqual(data.loc[0, 'validation_resnum_full'], '118') + + def test_download_validation(self): + self.download_validation(self.pdbid, filename=self.output_validation, + overwrite=True) + if os.path.exists(self.output_validation): + os.remove(self.output_validation) + + def test_main_Validation(self): + # read + data = self.Validation.read(self.example_validation) + self.assertEqual(data.shape, (653, 26), 'Parser returned a DataFrame ' + 'with unexpected shape') + self.assertEqual(data.validation_chain.unique().tolist(), ['A', 'B']) + self.assertEqual(data.loc[626, 'validation_resname'], 'THR') + # download + self.Validation.download(self.pdbid, filename=self.output_validation, + overwrite=True) + if os.path.exists(self.output_validation): + os.remove(self.output_validation) + # select + self.Validation.select(self.pdbid) + + +if __name__ == '__main__': + logging.basicConfig(stream=sys.stderr) + logging.getLogger("proteofav.config").setLevel(logging.CRITICAL) + suite = unittest.TestLoader().loadTestsFromTestCase(TestValidationParser) + unittest.TextTestRunner(verbosity=2).run(suite) diff --git a/tests/test_variants.py b/tests/test_variants.py index 207fd9b..e0258db 100644 --- a/tests/test_variants.py +++ b/tests/test_variants.py @@ -1,18 +1,110 @@ +# -*- coding: utf-8 -*- + +import os +import sys import json +import logging import unittest -from os import path +import numpy as np +import pandas as pd try: import mock except ImportError: import unittest.mock as mock -from proteofav.config import Defaults -from proteofav.variants import (_fetch_icgc_variants, _fetch_ebi_variants, _fetch_ensembl_variants, - _sequence_from_ensembl_protein, _match_uniprot_ensembl_seq, - _compare_sequences, _count_mismatches, parse_uniprot_variants) - -defaults = Defaults(path.join(path.dirname(__file__), "config.txt")) +from proteofav.config import defaults +from proteofav.variants import (_fetch_icgc_variants, fetch_uniprot_variants, fetch_ensembl_variants, + fetch_ensembl_sequence_from_id, _match_uniprot_ensembl_seq, + _compare_sequences, _count_mismatches, parse_uniprot_variants, + fetch_uniprot_sequence, + fetch_uniprot_ensembl_mapping, fetch_ensembl_uniprot_mapping, + get_uniprot_id_from_mapping, get_ensembl_protein_id_from_mapping, + fetch_uniprot_pdb_mapping, fetch_pdb_uniprot_mapping, + get_preferred_uniprot_id_from_mapping, + get_preferred_ensembl_id_from_mapping, + fetch_uniprot_species_from_id, get_ensembl_species_from_uniprot, + fetch_uniprot_formal_specie, _uniprot_info, + flatten_uniprot_variants_ebi, flatten_ensembl_variants, + select_variants, fetch_variants, Variants) + +example_uniprot_variants = { + 'accession': 'P40227', + 'entryName': 'TCPZ_HUMAN', + 'sequence': 'MAAVKTLNPKAEVARAQAAMKATNILLVDEIMRAGMSSLKG', + 'sequenceChecksum': '4876218983604824961', + 'taxid': 9606, + 'features': [ + {'type': 'VARIANT', + 'alternativeSequence': 'F', + 'begin': '231', + 'end': '231', + 'xrefs': [{'name': '1000Genomes', + 'id': 'rs148616984', + 'url': 'http://www.ensembl.org/Homo_sapiens/Variation/Explore?v=rs148616984;vdb=variation'}, + {'name': 'ESP', + 'id': 'rs148616984', + 'url': 'http://evs.gs.washington.edu/EVS/PopStatsServlet?searchBy=rsID&target=rs148616984&x=0&y=0'}, + {'name': 'ExAC', + 'id': 'rs148616984', + 'url': 'http://exac.broadinstitute.org/awesome?query=rs148616984'} + ], + 'wildType': 'L', + 'frequency': 0.000399361, + 'polyphenPrediction': 'benign', + 'polyphenScore': 0.41, + 'siftPrediction': 'deleterious', + 'siftScore': 0.01, + 'somaticStatus': 0, + 'cytogeneticBand': '7p11.2', + 'consequenceType': 'missense', + 'genomicLocation': 'NC_000007.14:g.56058069C>T', + 'sourceType': 'large_scale_study'}, + {'type': 'VARIANT', + 'alternativeSequence': 'S', + 'begin': '83', + 'end': '83', + 'xrefs': [{'name': 'ExAC', + 'id': 'rs779741978', + 'url': 'http://exac.broadinstitute.org/awesome?query=rs779741978'} + ], + 'wildType': 'A', + 'frequency': 0.0, + 'polyphenPrediction': 'benign', + 'polyphenScore': 0.305, + 'siftPrediction': 'tolerated', + 'siftScore': 0.06, + 'somaticStatus': 0, + 'cytogeneticBand': '7p11.2', + 'consequenceType': 'missense', + 'genomicLocation': 'NC_000007.14:g.56054414G>T', + 'sourceType': 'large_scale_study'}, + {'type': 'VARIANT', + 'description': '[LSS_COSMIC]: primary tissue(s): lung', + 'alternativeSequence': 'V', + 'begin': '292', + 'end': '292', + 'xrefs': [{'name': 'cosmic curated', + 'id': 'COSM1549991', + 'url': 'http://cancer.sanger.ac.uk/cosmic/mutation/overview?id=1549991'} + ], + 'evidences': [{'code': 'ECO:0000313', + 'source': {'name': 'cosmic_study', + 'id': 'COSU:417', + 'url': 'http://cancer.sanger.ac.uk/cosmic/study/overview?study_id=417'} + } + ], + 'wildType': 'I', + 'polyphenPrediction': 'benign', + 'polyphenScore': 0.021, + 'siftPrediction': 'tolerated', + 'siftScore': 0.1, 'somaticStatus': 0, + 'cytogeneticBand': '7p11.2', + 'consequenceType': 'missense', + 'genomicLocation': '7:g.56058510A>G', + 'sourceType': 'large_scale_study'} + ] +} @mock.patch("proteofav.structures.defaults", defaults) @@ -21,31 +113,101 @@ class VariantsTestCase(unittest.TestCase): def setUp(self): """Initialize the framework for testing.""" + self.uniprot_id = 'O96013' + self.pdbid = '2pah' + self.uniprot_id2 = 'P00439' + self.ensembl_id = 'ENSP00000326864' + self.ensembl_id2 = "ENSP00000448059" + self.variant_id = 'rs557625940' self.fetch_icgc_variants = _fetch_icgc_variants - self.fetch_ebi_variants = _fetch_ebi_variants - self.fetch_ensembl_variants = _fetch_ensembl_variants - self.sequence_from_ensembl_protein = _sequence_from_ensembl_protein + self.fetch_uniprot_variants = fetch_uniprot_variants + self.fetch_ensembl_variants = fetch_ensembl_variants + self.fetch_ensembl_sequence_from_id = fetch_ensembl_sequence_from_id self.match_uniprot_ensembl_seq = _match_uniprot_ensembl_seq self.compare_sequences = _compare_sequences self.count_mismatches = _count_mismatches self.parse_uniprot_variants = parse_uniprot_variants + self.uniprot_info = _uniprot_info + self.fetch_uniprot_ensembl_mapping = fetch_uniprot_ensembl_mapping + self.fetch_ensembl_uniprot_mapping = fetch_ensembl_uniprot_mapping + self.get_preferred_uniprot_id_from_mapping = get_preferred_uniprot_id_from_mapping + self.get_preferred_ensembl_id_from_mapping = get_preferred_ensembl_id_from_mapping + self.get_uniprot_id_from_mapping = get_uniprot_id_from_mapping + self.get_ensembl_protein_id_from_mapping = get_ensembl_protein_id_from_mapping + self.fetch_uniprot_species_from_id = fetch_uniprot_species_from_id + self.get_ensembl_species_from_uniprot = get_ensembl_species_from_uniprot + self.get_uniprot_sequence = fetch_uniprot_sequence + self.get_uniprot_organism = fetch_uniprot_formal_specie + self.uniprot_info = _uniprot_info + self.ccc2_sequence = ("MREVILAVHGMTCSACTNTINTQLRALKGVTKCDISLVTNECQVTYDNEVTADSIKEIIE" + "DCGFDCEILRDSEITAISTKEGLLSVQGMTCGSCVSTVTKQVEGIEGVESVVVSLVTEEC" + "HVIYEPSKTTLETAREMIEDCGFDSNIIMDGNGNADMTEKTVILKVTKAFEDESPLILSS" + "VSERFQFLLDLGVKSIEISDDMHTLTIKYCCNELGIRDLLRHLERTGYKFTVFSNLDNTT" + "QLRLLSKEDEIRFWKKNSIKSTLLAIICMLLYMIVPMMWPTIVQDRIFPYKETSFVRGLF" + "YRDILGVILASYIQFSVGFYFYKAAWASLKHGSGTMDTLVCVSTTCAYTFSVFSLVHNMF" + "HPSSTGKLPRIVFDTSIMIISYISIGKYLETLAKSQTSTALSKLIQLTPSVCSIISDVER" + "NETKEIPIELLQVNDIVEIKPGMKIPADGIITRGESEIDESLMTGESILVPKKTGFPVIA" + "GSVNGPGHFYFRTTTVGEETKLANIIKVMKEAQLSKAPIQGYADYLASIFVPGILILAVL" + "TFFIWCFILNISANPPVAFTANTKADNFFICLQTATSVVIVACPCALGLATPTAIMVGTG" + "VGAQNGVLIKGGEVLEKFNSITTFVFDKTGTLTTGFMVVKKFLKDSNWVGNVDEDEVLAC" + "IKATESISDHPVSKAIIRYCDGLNCNKALNAVVLESEYVLGKGIVSKCQVNGNTYDICIG" + "NEALILEDALKKSGFINSNVDQGNTVSYVSVNGHVFGLFEINDEVKHDSYATVQYLQRNG" + "YETYMITGDNNSAAKRVAREVGISFENVYSDVSPTGKCDLVKKIQDKEGNNKVAVVGDGI" + "NDAPALALSDLGIAISTGTEIAIEAADIVILCGNDLNTNSLRGLANAIDISLKTFKRIKL" + "NLFWALCYNIFMIPIAMGVLIPWGITLPPMLAGLAMAFSSVSVVLSSLMLKKWTPPDIES" + "HGISDFKSKFSIGNFWSRLFSTRAIAGEQDIESQAGLMSNEEVL") + self.fetch_pdb_uniprot_mapping = fetch_pdb_uniprot_mapping + self.fetch_uniprot_pdb_mapping = fetch_uniprot_pdb_mapping + self.flatten_uniprot_variants_ebi = flatten_uniprot_variants_ebi + self.flatten_ensembl_variants = flatten_ensembl_variants + self.fetch_variants = fetch_variants + self.select_variants = select_variants + self.Variants = Variants def tearDown(self): """Remove testing framework by cleaning the namespace.""" + + self.uniprot_id = None + self.pdbid = None + self.uniprot_id2 = None + self.ensembl_id = None + self.ensembl_id2 = None + self.variant_id = None self.fetch_icgc_variants = None - self.fetch_ebi_variants = None + self.fetch_uniprot_variants = None self.fetch_ensembl_variants = None - self.sequence_from_ensembl_protein = None + self.fetch_ensembl_sequence_from_id = None self.match_uniprot_ensembl_seq = None self.compare_sequences = None self.parse_uniprot_variants = None + self.uniprot_info = None + self.fetch_uniprot_ensembl_mapping = None + self.fetch_ensembl_uniprot_mapping = None + self.get_uniprot_id_from_mapping = None + self.get_ensembl_protein_id_from_mapping = None + self.get_preferred_uniprot_id_from_mapping = None + self.get_preferred_ensembl_id_from_mapping = None + self.fetch_uniprot_species_from_id = None + self.get_ensembl_species_from_uniprot = None + self.get_uniprot_sequence = None + self.get_uniprot_organism = None + self.uniprot_info = None + self.ccc2_sequence = None + self.fetch_pdb_uniprot_mapping = None + self.fetch_uniprot_pdb_mapping = None + self.flatten_uniprot_variants_ebi = None + self.flatten_ensembl_variants = None + self.fetch_variants = None + self.select_variants = None + self.Variants = None def test_icgc_parsing(self): mock_response = mock.Mock() mock_response.return_value.ok = True mock_response.return_value.status = 200 - with open('VARIATION/icgc_ENST00000308677.json') as open_f: + with open(os.path.join(os.path.dirname(__file__), "testdata", + "variation", "icgc_ENST00000308677.json")) as open_f: response = json.load(open_f) mock_response.json.return_value = response @@ -70,7 +232,19 @@ def test_ebi_variants_parsing(self): with mock.patch('proteofav.utils.requests.get') as mock_get: mock_get.return_value = mock_response - data = self.fetch_ebi_variants('P17612') + data = self.fetch_uniprot_variants('P17612') + + from pandas.io.json import json_normalize + data = json_normalize(data.json(), ['features'], + meta=['accession', 'entryName']) + + # flatten the xref field, which has the id column. + # ideally this could be normalised with: + # table = json_normalize(data, ['features', 'xref'] ... + # but this field is not present in all entries, + flat_xref = data['xrefs'].apply(pd.Series).stack().apply(pd.Series) + flat_xref.reset_index(level=1, drop=True, inplace=True) + data = data.join(flat_xref) self.assertEqual(data.shape, (3, 21)) # deal with duplicated index - two data sources for the first variant @@ -102,6 +276,7 @@ def test_fetch_ensembl_variants_transcript_variation_parsing(self): mock_get.return_value = mock_response data = self.fetch_ensembl_variants('XXXXX', # ENSP00000309591 feature='transcript_variation') + data = pd.DataFrame(data.json()) self.assertEqual(data.shape, (2, 15)) self.assertEqual(data.loc[0, 'Parent'], 'ENST00000288602') @@ -131,6 +306,7 @@ def test_fetch_ensembl_variants_somatic_transcript_variation_parsing(self): mock_get.return_value = mock_response data = self.fetch_ensembl_variants('XXXXX', # ENSP00000309591 feature='somatic_transcript_variation') + data = pd.DataFrame(data.json()) self.assertEqual(data.shape, (2, 15)) self.assertEqual(data.loc[0, 'Parent'], 'ENST00000288602') @@ -143,25 +319,28 @@ def test_fetch_ensembl_variants_somatic_transcript_variation_parsing(self): def test_sequence_from_ensembl_protein(self): response = 'MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFER' - with mock.patch('proteofav.variants.get_url_or_retry') as mock_get: + with mock.patch('proteofav.variants.fetch_from_url_or_retry') as mock_get: mock_get.return_value = response - sequence = self.sequence_from_ensembl_protein('XXXXXX') # ENSP00000309591 + sequence = self.fetch_ensembl_sequence_from_id('XXXXXX') # ENSP00000309591 self.assertEqual(sequence, response) @mock.patch('proteofav.variants.fetch_uniprot_formal_specie', return_value='homo_sapiens') @mock.patch('proteofav.variants.fetch_uniprot_sequence', return_value='ABC') - @mock.patch('proteofav.variants._sequence_from_ensembl_protein', return_value='ABC') + @mock.patch('proteofav.variants.fetch_ensembl_sequence_from_id', return_value='ABC') def test_match_uniprot_ensembl_seq(self, mock_fun, mock_fun1, mock_fun2): import pandas as pd - ensembl_response = [{"type": "gene", "id": "ENSG00000072062"}, {"type": "transcript", - "id": "ENST00000308677"}, - {"type": "transcript", "id": "ENST00000589994"}, - {"type": "translation", "id": "XXXX"}, {"type": "translation", - "id": "ENSP00000466651"}] - - with mock.patch('proteofav.variants._uniprot_to_ensembl_xref') as mock_fun3: - mock_fun3.return_value = pd.DataFrame(ensembl_response) + ensembl_response = """[{"type": "gene", "id": "ENSG00000072062"}, {"type": "transcript", + "id": "ENST00000308677"}, + {"type": "transcript", "id": "ENST00000589994"}, + {"type": "translation", "id": "XXXX"}, {"type": "translation", + "id": "ENSP00000466651"}]""" + mock_response = mock.Mock() + mock_response.return_value.ok = True + mock_response.return_value.status = 200 + mock_response.json.return_value = json.loads(ensembl_response) + with mock.patch('proteofav.variants.fetch_uniprot_ensembl_mapping') as mock_fun3: + mock_fun3.return_value = mock_response self.match_uniprot_ensembl_seq('XXXX') @mock.patch('proteofav.variants.fetch_uniprot_formal_specie', return_value='alien') @@ -191,16 +370,566 @@ def test_parse_uniprot_variants(self): 206: "Natural variant: ['In PPNAD4; somatic mutation; the mutation results in cAMP-independent basal protein kinase activity and constitutive activation of protein kinase A. L->R'] (['VAR_071707'])", 264: "Natural variant: ['S->C'] (['VAR_040593'])"}) - with mock.patch('proteofav.variants.map_gff_features_to_sequence') as mock_fun: + with mock.patch('proteofav.variants.select_annotation') as mock_fun: mock_fun.return_value = pd.DataFrame(mock_data) data = self.parse_uniprot_variants('XXXX') - self.assertEqual(data.shape, (4,3)) + self.assertEqual(data.shape, (4, 3)) self.assertFalse('annotation' in data) self.assertIn('PPNAD4', data.loc[206, 'disease']) - + def test_mock_a_ptn_sequence(self): + """ + Test _uniprot_info table parsing with a Mock request. + + ..note: + query=accession%3AP38995&contact=%20"&columns=id%2Csequence%2C&format=tab + """ + + table = """Entry Sequence\nP38995 """ + self.ccc2_sequence + + with mock.patch('proteofav.utils.requests') as mock_get: + mock_get.get.return_value.ok = True + mock_get.get.return_value.status = 200 + mock_get.get.return_value.content = table + self.assertEqual(self.get_uniprot_sequence('P38995'), self.ccc2_sequence) + + mock_get.get.assert_called_once_with('http://www.uniprot.org/uniprot/', + headers=mock.ANY, + params=mock.ANY, + stream=mock.ANY) + + def test_mock_a_ptn_organism_name(self): + """ + Test whether the UniProt info table is parsed correctly by mocking the request. + + ..note:: query=accession%3AP38995&contact=%20"&columns=id%2Corganism%2C&format=tab + """ + ccc2_organism = 'Saccharomyces cerevisiae' + table = """Entry Organism\nP38995 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)""" + + with mock.patch('proteofav.utils.requests') as mock_get: + mock_get.get.return_value.ok = True + mock_get.get.return_value.status = 200 + mock_get.get.return_value.content = table + self.assertEqual(self.get_uniprot_organism('P38995'), ccc2_organism) + + mock_get.get.assert_called_once_with('http://www.uniprot.org/uniprot/', + headers=mock.ANY, + params=mock.ANY, + stream=mock.ANY) + + def test_obsolete_uniprot_accession(self): + data = self.uniprot_info('Q91887') + self.assertEqual(len(data), 1) + + # number of keys (or columns) + self.assertEqual(len(data.columns.values), 8) + + # check the values for particular entries + self.assertTrue(np.isnan(data.iloc[0, -1])) # 'Length' + self.assertTrue(np.isnan(data.iloc[0, -1])) # 'Status' + + def test_uniprot_variants_ebi(self): + r = self.fetch_uniprot_variants(self.uniprot_id) + self.assertTrue(r.ok) + + def test_fetch_ensembl_transcript_variants(self): + r = self.fetch_ensembl_variants(self.ensembl_id, + feature="transcript_variation") + self.assertTrue(r.ok) + + def test_fetch_ensembl_somatic_variants(self): + r = self.fetch_ensembl_variants(self.ensembl_id, + feature="somatic_transcript_variation") + self.assertTrue(r.ok) + + def fetch_fetch_ensembl_sequence_from_id(self): + r = self.fetch_ensembl_sequence_from_id(self.ensembl_id) + self.assertTrue(r.ok) + + def test_fetch_uniprot_species_from_id(self): + r = self.fetch_uniprot_species_from_id(self.uniprot_id2) + self.assertTrue(r.ok) + organism = str(r.content, encoding='utf-8').split('\n')[1] + species = '_'.join(organism.split()[0:2]).lower() + self.assertEqual(species, "homo_sapiens") + + def test_fetch_fetch_uniprot_pdb_mapping(self): + r = self.fetch_uniprot_pdb_mapping(self.uniprot_id) + self.assertTrue(r.ok) + + def test_fetch_fetch_pdb_uniprot_mapping(self): + r = self.fetch_pdb_uniprot_mapping(self.pdbid) + self.assertTrue(r.ok) + + def test_get_ensembl_species_from_uniprot(self): + data = self.fetch_uniprot_species_from_id(self.uniprot_id2) + species = self.get_ensembl_species_from_uniprot(data) + self.assertEqual(species, 'homo_sapiens') + + def test_fetch_uniprot_ensembl_mapping(self): + r = self.fetch_uniprot_ensembl_mapping(self.uniprot_id2) + self.assertTrue(r.ok) + ensps = self.get_ensembl_protein_id_from_mapping(r.json()) + self.assertEqual(ensps, [self.ensembl_id2]) + + def test_fetch_ensembl_uniprot_mapping(self): + r = self.fetch_ensembl_uniprot_mapping(self.ensembl_id2) + self.assertTrue(r.ok) + uniprots = self.get_uniprot_id_from_mapping(r.json()) + self.assertEqual(uniprots, ['A0A024RBG4', self.uniprot_id2]) + + def test_to_table_uniprot_ensembl_mapping_full(self): + """ + Tests the fetching and parsing real UniProt ids. + This test focuses on the method that parses the residue entries. + + Some checks are made to whether the parsed keys and values + are the ones we are expecting. + """ + + data = self.fetch_uniprot_ensembl_mapping(self.uniprot_id, + species='homo_sapiens') + + information = {} + rows = [] + for entry in data.json(): + typ = entry['type'].upper() + eid = entry['id'] + try: + if eid in information[typ]: + continue + information[typ].append(eid) + except KeyError: + information[typ] = eid + except AttributeError: + information[typ] = [information[typ]] + information[typ].append(eid) + + rows.append(information) + data = pd.DataFrame(rows) + + # number of values per column (or rows) + self.assertEqual(len(data), 1) + + # number of keys (or columns) + self.assertEqual(len(data.columns.values), 3) + + # check whether there are particular keys + self.assertIn('TRANSCRIPT', data.columns.values) + + # check the values for particular entries + self.assertEqual(data['GENE'][0], 'ENSG00000130669') + + def test_get_uniprot_id_from_mapping(self): + data = self.fetch_ensembl_uniprot_mapping(self.ensembl_id2) + + r = self.get_uniprot_id_from_mapping(data.json(), full_entry=False, + uniprot_id=None) + self.assertEqual(r, ['A0A024RBG4', self.uniprot_id2]) + + r = self.get_uniprot_id_from_mapping(data.json(), full_entry=True, + uniprot_id=None) + self.assertIn('dbname', r[0]) + self.assertIn('xref_start', r[0]) + self.assertIn('ensembl_start', r[0]) + + r = self.get_uniprot_id_from_mapping(data.json(), full_entry=False, + uniprot_id=self.uniprot_id2) + self.assertEqual(r, [self.uniprot_id2]) + + def test_get_ensembl_protein_id_from_mapping(self): + data = self.fetch_uniprot_ensembl_mapping(self.uniprot_id2) + r = self.get_ensembl_protein_id_from_mapping(data.json()) + self.assertEqual(r, [self.ensembl_id2]) + + def test_preferred_uniprot_id_from_mapping(self): + info = self.fetch_ensembl_uniprot_mapping(self.ensembl_id2) + data = self.get_uniprot_id_from_mapping(info.json(), full_entry=True) + best_match = self.get_preferred_uniprot_id_from_mapping(data) + self.assertEqual(best_match, 'P00439') + + def test_preferred_ensembl_id_from_mapping(self): + data = self.fetch_uniprot_species_from_id(self.uniprot_id2) + species = self.get_ensembl_species_from_uniprot(data) + info = self.fetch_uniprot_ensembl_mapping(self.uniprot_id2, + species=species) + r = self.get_ensembl_protein_id_from_mapping(info.json()) + best_match = self.get_preferred_ensembl_id_from_mapping(r) + self.assertEqual(best_match, 'ENSP00000448059') + + def test_to_table_uniprot_info(self): + """ + Tests the fetching and parsing real UniProt ids. + This test focuses on the method that parses the residue entries. + + Some checks are made to whether the parsed keys and values + are the ones we are expecting. + """ + + data = self.uniprot_info(self.uniprot_id) + + # number of values per column (or rows) + self.assertEqual(len(data), 1) + + # number of keys (or columns) + self.assertEqual(len(data.columns.values), 8) + + # check whether there are particular keys + self.assertIn('Sequence', data.columns.values) + + # check the values for particular entries + self.assertTrue(data['Length'][0] == 591) + self.assertTrue(data['Status'][0] == "reviewed") + self.assertEqual(data['Entry name'][0], 'PAK4_HUMAN') + + def test_uniprot_info_with_defaults(self): + """ + Test whether Uniprot query logic still valid. + + ..note: + Intentionally get info from Uniprot. An Uniprot update may break this. + """ + + cols = ("Entry", "Entry name", "Status", "Protein names", "Gene names", "Organism", + "Sequence", "Length") + + first_field = "P38995" + last_field = 1004 + + table = self.uniprot_info('P38995') + self.assertEqual(set(table.columns), set(cols)) + self.assertEqual(table.iloc[0, 0], first_field) + self.assertEqual(table.iloc[0, -1], last_field) + + def test_uniprot_to_ensembl_xref(self): + self.assertEqual(self.fetch_uniprot_ensembl_mapping('P38995').json(), []) + table = self.fetch_uniprot_ensembl_mapping('P38995', 'saccharomyces_cerevisiae') + table = pd.DataFrame(table.json()) + self.assertEqual(set(table.columns), {'id', 'type'}) + + def test_to_table_pdb_uniprot_sifts_mapping(self): + """ + Testing the PDBe API for mapping between PDB and UniProt + accession identifiers. + """ + + information = self.fetch_pdb_uniprot_mapping(self.pdbid) + rows = [] + for uniprot in information.json()[self.pdbid]['UniProt']: + uniprots = {'uniprot_id': uniprot} + rows.append(uniprots) + data = pd.DataFrame(rows) + + # number of values per column (or rows) + self.assertEqual(len(data), 1) + + # number of keys (or columns) + self.assertEqual(len(data.columns.values), 1) + + # check whether there are particular keys + self.assertIn('uniprot_id', data.columns.values) + + # check the values of particular entries + self.assertTrue(data['uniprot_id'][0] == 'P00439') + + def test_to_table_uniprot_pdb_sifts_mapping(self): + """ + Testing the PDBe API for mapping between UniProt and PDB + accession identifiers. + """ + + information = self.fetch_uniprot_pdb_mapping(self.uniprot_id2) + rows = [] + for entry in information.json()[self.uniprot_id2]: + rows.append(entry) + data = pd.DataFrame(rows) + + # check whether there are particular keys + self.assertIn('pdb_id', data.columns.values) + + # check the values of particular entries + self.assertEqual(data['pdb_id'].unique()[0], '2pah') + self.assertIn('A', data['chain_id'].unique()) + self.assertIn('X-ray diffraction', data['experimental_method'].unique()) + self.assertTrue(type(data['coverage'][0]), float) + self.assertTrue(type(data['resolution'][0]), float) + self.assertTrue(type(data['tax_id'][0]), int) + + def test_to_table_transcript_variants_ensembl(self): + """ + Tests the fetching and parsing real Ensembl Protein ids. + + Some checks are made to whether the parsed keys and values + are the ones we are expecting. + + Using mocking because variant data varies over time. + For simplicity here loading the resulting pandas table from a + dumped csv file. + """ + + # data = self.ensembl_trascript(self.ensembl_id, species='human') + # mocking the resulting pandas dataframe + variants = os.path.join(os.path.dirname(__file__), "testdata", + "variation", "transcript_variation_{}.csv".format(self.ensembl_id)) + data = pd.read_csv(variants) + + # number of values per column (or rows) + self.assertEqual(len(data), 206) + + # number of keys (or columns) + self.assertEqual(len(data.columns.values), 16) + + # check whether there are particular keys + self.assertIn('Parent', data.columns.values) + + # check the values for particular entries + self.assertTrue(data['Parent'][0] == 'ENST00000321944') + self.assertTrue(data['feature_type'][0] == "transcript_variation") + self.assertEqual(data['codons'][0], 'Cat/Tat') + self.assertEqual(data['start'][0], 135) + + def test_to_table_somatic_variants_ensembl(self): + """ + Tests the fetching and parsing real Ensembl Protein ids. + + Some checks are made to whether the parsed keys and values + are the ones we are expecting. + + Using mocking because variant data varies over time. + For simplicity here loading the resulting pandas table from a + dumped csv file. + """ + + # data = self.ensembl_somatic(self.ensembl_id, species='human') + # mocking the resulting pandas dataframe + variants = os.path.join(os.path.dirname(__file__), "testdata", "variation", + "somatic_variation_{}.csv".format(self.ensembl_id)) + data = pd.read_csv(variants) + + # number of values per column (or rows) + self.assertEqual(len(data), 40) + + # number of keys (or columns) + self.assertEqual(len(data.columns.values), 16) + + # check whether there are particular keys + self.assertIn('Parent', data.columns.values) + + # check the values for particular entries + self.assertTrue(data['Parent'][0] == 'ENST00000321944') + self.assertTrue(data['feature_type'][0] == "somatic_transcript_variation") + self.assertEqual(data['codons'][0], 'Gag/Cag') + self.assertEqual(data['start'][0], 119) + + def test_to_table_ensembl_variant(self): + """ + Tests the fetching and parsing real Ensembl Variant ids. + + Some checks are made to whether the parsed keys and values + are the ones we are expecting. + + Using mocking because variant data varies over time. + For simplicity here loading the resulting pandas table from a + dumped csv file. + """ + + # data = self.ensembl_variant(self.variant_id, species='human') + # mocking the resulting pandas dataframe + variants = os.path.join(os.path.dirname(__file__), "testdata", "variation", + "ensembl_variation_{}.csv".format(self.variant_id)) + data = pd.read_csv(variants) + + # number of values per column (or rows) + self.assertEqual(len(data), 1) + + # number of keys (or columns) + self.assertEqual(len(data.columns.values), 19) + + # check whether there are particular keys + self.assertIn('location', data.columns.values) + + # check the values for particular entries + self.assertEqual(data['location'][0], '19:39175331-39175331') + self.assertTrue(data['name'][0] == "rs557625940") + self.assertEqual(data['seq_region_name'][0], 19) + self.assertEqual(data['most_severe_consequence'][0], 'missense_variant') + + def test_to_table_uniprot_ensembl_variants(self): + """ + Tests the wrapper method that goes from a uniprot to a list + of ensembl protein transcripts and to variants. + + Using mocking because variant data varies over time. + For simplicity here loading the resulting pandas table from a + dumped csv file. + """ + + # querying the various ensembl endpoints + # data = self.uniprot_variants(self.uniprot_id) + # mocking the resulting pandas dataframe + variants = os.path.join(os.path.dirname(__file__), "testdata", "variation", + "uniprot_variants_{}.csv".format(self.uniprot_id)) + data = pd.read_csv(variants) + + # number of values per column (or rows) + self.assertEqual(len(data), 903) + + # number of keys (or columns) + self.assertEqual(len(data.columns.values), 5) + + # check whether there are particular keys + self.assertIn('translation', data.columns.values) + self.assertIn('id', data.columns.values) + self.assertIn('start', data.columns.values) + self.assertIn('residues', data.columns.values) + + # check the values for particular entries + self.assertEqual(data['translation'][0], 'ENSP00000351049') + self.assertTrue(data['id'][0] == "rs769098772") + self.assertTrue(data['start'][0] == 295) + self.assertTrue(data['residues'][0] == "E/A") + + def test_flatten_uniprot_variants_ebi(self): + r = self.fetch_uniprot_variants(self.uniprot_id2) + if r.ok: + table = self.flatten_uniprot_variants_ebi(r) + self.assertIn('accession', list(table)) + self.assertIn('sequence', list(table)) + self.assertIn('polyphenScore', list(table)) + self.assertIn('siftScore', list(table)) + self.assertIn('begin', list(table)) + self.assertIn('end', list(table)) + + def test_flatten_uniprot_variants_ebi_mock(self): + data = example_uniprot_variants + r = self.flatten_uniprot_variants_ebi(data) + + # flattening the accession + self.assertEqual('P40227', data['accession']) + self.assertEqual('P40227', r.loc[0, 'accession']) + + # flattening the 'xrefs' + self.assertEqual('1000Genomes', data['features'][0]['xrefs'][0]['name']) + self.assertEqual('1000Genomes', r.loc[0, 'xrefs_name'][0]) + self.assertEqual(['1000Genomes', 'ESP', 'ExAC'], r.loc[0, 'xrefs_name']) + self.assertTrue(np.isnan(r.loc[1, 'evidences_source_name'])) + + # flattening the 'evidences' + self.assertEqual('cosmic_study', data['features'][2]['evidences'][0]['source']['name']) + self.assertEqual('cosmic_study', r.loc[2, 'evidences_source_name']) + + def test_flatten_ensembl_variants(self): + r = self.fetch_ensembl_variants(self.ensembl_id2, feature='transcript_variation') + if r.ok: + table = self.flatten_ensembl_variants(r, synonymous=True) + self.assertIn('polyphenScore', list(table)) + self.assertIn('siftScore', list(table)) + self.assertIn('begin', list(table)) + self.assertIn('end', list(table)) + + def test_fetch_variants_all(self): + uniprot, germline, somatic = self.fetch_variants(self.uniprot_id2, + id_source='uniprot', + synonymous=True, + uniprot_vars=True, + ensembl_germline_vars=True, + ensembl_somatic_vars=True) + + self.assertEqual(uniprot.loc[0, 'accession'], self.uniprot_id2) + self.assertEqual(germline.loc[0, 'translation'], self.ensembl_id2) + self.assertEqual(somatic.loc[0, 'translation'], self.ensembl_id2) + self.assertIn('polyphenScore', list(uniprot)) + self.assertIn('siftScore', list(uniprot)) + self.assertIn('begin', list(germline)) + self.assertIn('begin', list(somatic)) + self.assertIn('end', list(germline)) + self.assertIn('end', list(somatic)) + + def test_variants_fetch_from_uniprot_id(self): + uniprot, germline, somatic = self.Variants.fetch(self.uniprot_id2, + id_source='uniprot', + synonymous=True, + uniprot_vars=True, + ensembl_germline_vars=True, + ensembl_somatic_vars=True) + self.assertEqual(uniprot.loc[0, 'accession'], self.uniprot_id2) + self.assertEqual(germline.loc[0, 'translation'], self.ensembl_id2) + self.assertEqual(somatic.loc[0, 'translation'], self.ensembl_id2) + self.assertIn('polyphenScore', list(uniprot)) + self.assertIn('siftScore', list(uniprot)) + self.assertIn('begin', list(germline)) + self.assertIn('begin', list(somatic)) + self.assertIn('end', list(germline)) + self.assertIn('end', list(somatic)) + + def test_variants_fetch_from_ensembl_id(self): + uniprot, germline, somatic = self.Variants.fetch(self.ensembl_id2, + id_source='ensembl', + synonymous=True, + uniprot_vars=True, + ensembl_germline_vars=True, + ensembl_somatic_vars=True) + self.assertEqual(uniprot.loc[0, 'accession'], self.uniprot_id2) + self.assertEqual(germline.loc[0, 'translation'], self.ensembl_id2) + self.assertEqual(somatic.loc[0, 'translation'], self.ensembl_id2) + self.assertIn('polyphenScore', list(uniprot)) + self.assertIn('siftScore', list(uniprot)) + self.assertIn('begin', list(germline)) + self.assertIn('begin', list(somatic)) + self.assertIn('end', list(germline)) + self.assertIn('end', list(somatic)) + + def test_variants_select(self): + uniprot, ensembl = self.select_variants(self.uniprot_id2, + id_source='uniprot', + synonymous=True, + uniprot_vars=True, + ensembl_germline_vars=True, + ensembl_somatic_vars=True) + self.assertIn('polyphenScore', list(uniprot)) + self.assertIn('siftScore', list(uniprot)) + self.assertIn('begin', list(uniprot)) + self.assertIn('end', list(uniprot)) + self.assertIn('accession', list(uniprot)) + self.assertIn('translation', list(ensembl)) + self.assertIn('begin', list(ensembl)) + self.assertIn('end', list(ensembl)) + + def test_variants_select_from_uniprot_id(self): + uniprot, ensembl = self.Variants.select(self.uniprot_id2, + id_source='uniprot', + synonymous=True, + uniprot_vars=False, + ensembl_germline_vars=True, + ensembl_somatic_vars=True) + self.assertIn('polyphenScore', list(ensembl)) + self.assertIn('siftScore', list(ensembl)) + self.assertIn('begin', list(ensembl)) + self.assertIn('end', list(ensembl)) + self.assertNotIn('accession', list(ensembl)) + self.assertIn('translation', list(ensembl)) + self.assertIsNone(uniprot) + + def test_variants_select_from_ensembl_id(self): + uniprot, ensembl = self.Variants.select(self.ensembl_id2, + id_source='ensembl', + synonymous=True, + uniprot_vars=True, + ensembl_germline_vars=False, + ensembl_somatic_vars=False) + self.assertIn('polyphenScore', list(uniprot)) + self.assertIn('siftScore', list(uniprot)) + self.assertIn('begin', list(uniprot)) + self.assertIn('end', list(uniprot)) + self.assertIn('accession', list(uniprot)) + self.assertNotIn('translation', list(uniprot)) + self.assertIsNone(ensembl) if __name__ == '__main__': - unittest.main() + logging.basicConfig(stream=sys.stderr) + logging.getLogger("proteofav.config").setLevel(logging.CRITICAL) + suite = unittest.TestLoader().loadTestsFromTestCase(VariantsTestCase) + unittest.TextTestRunner(verbosity=2).run(suite) diff --git a/tests/test_visualise.py b/tests/test_visualise.py index 26481f1..03a87a1 100644 --- a/tests/test_visualise.py +++ b/tests/test_visualise.py @@ -1,16 +1,18 @@ -# coding=utf-8 -import unittest +# -*- coding: utf-8 -*- +import sys +import logging +import unittest import pandas as pd from proteofav.visualise import make_chimera_attribute_file, make_chimera_command_file - class TestVisualiser(unittest.TestCase): def setUp(self): """Initialize the framework for testing.""" - # self.example_dssp = path.join(path.dirname(__file__), "DSSP/1iej.dssp") + # self.example_dssp = path.join(path.dirname(__file__), "testdata", + # "dssp", "1iej.dssp") self.chimera_attribute = make_chimera_attribute_file self.chimera_command = make_chimera_command_file @@ -48,9 +50,13 @@ def test_make_chimera_command_file(self): lines = self.chimera_command('here', content='test\n') self.assertEqual(lines, result) + # TODO def test_visualise_chimera(self): - pass # TODO + pass if __name__ == '__main__': - unittest.main() + logging.basicConfig(stream=sys.stderr) + logging.getLogger("proteofav.config").setLevel(logging.CRITICAL) + suite = unittest.TestLoader().loadTestsFromTestCase(TestVisualiser) + unittest.TextTestRunner(verbosity=2).run(suite) diff --git a/tests/testdata/annotation/P00439.gff b/tests/testdata/annotation/P00439.gff new file mode 100644 index 0000000..20af6c1 --- /dev/null +++ b/tests/testdata/annotation/P00439.gff @@ -0,0 +1,263 @@ +##gff-version 3 +##sequence-region P00439 1 452 +P00439 UniProtKB Chain 1 452 . . . ID=PRO_0000205548;Note=Phenylalanine-4-hydroxylase +P00439 UniProtKB Domain 36 114 . . . Note=ACT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01007 +P00439 UniProtKB Metal binding 285 285 . . . Note=Iron%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04176 +P00439 UniProtKB Metal binding 290 290 . . . Note=Iron%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04176 +P00439 UniProtKB Metal binding 330 330 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04176 +P00439 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:24275569,ECO:0000269|PubMed:12185072;Dbxref=PMID:24275569,PMID:12185072 +P00439 UniProtKB Natural variant 16 16 . . . ID=VAR_000869;Note=In PKU. S->P;Dbxref=dbSNP:rs62642946 +P00439 UniProtKB Natural variant 20 20 . . . ID=VAR_009239;Note=In HPA. Q->L;Dbxref=dbSNP:rs199475662 +P00439 UniProtKB Natural variant 39 39 . . . ID=VAR_000870;Note=In HPA and PKU%3B haplotype 1. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12501224;Dbxref=dbSNP:rs62642926,PMID:12501224 +P00439 UniProtKB Natural variant 39 39 . . . ID=VAR_000871;Note=In PKU%3B haplotypes 9%2C21. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23792259,ECO:0000269|PubMed:9452062;Dbxref=PMID:23792259,PMID:9452062 +P00439 UniProtKB Natural variant 40 40 . . . ID=VAR_000872;Note=In PKU. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8889590;Dbxref=dbSNP:rs62642938,PMID:8889590 +P00439 UniProtKB Natural variant 41 41 . . . ID=VAR_000873;Note=In PKU. L->F;Dbxref=dbSNP:rs62642928 +P00439 UniProtKB Natural variant 41 41 . . . ID=VAR_009240;Note=In PKU%3B mild. L->P;Dbxref=dbSNP:rs62642916 +P00439 UniProtKB Natural variant 42 42 . . . ID=VAR_000874;Note=In PKU%3B haplotype 21. K->I;Dbxref=dbSNP:rs62635346 +P00439 UniProtKB Natural variant 45 45 . . . ID=VAR_067994;Note=In PKU. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22513348;Dbxref=PMID:22513348 +P00439 UniProtKB Natural variant 46 46 . . . ID=VAR_000875;Note=In PKU%3B haplotype 5%3B significantly reduces phenylalanine binding. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8889590;Dbxref=dbSNP:rs74603784,PMID:8889590 +P00439 UniProtKB Natural variant 47 47 . . . ID=VAR_000876;Note=In non-PKU HPA%3B haplotype 4%3B significantly reduces phenylalanine binding. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8088845;Dbxref=dbSNP:rs118203925,PMID:8088845 +P00439 UniProtKB Natural variant 48 48 . . . ID=VAR_000877;Note=In PKU%3B mild%3B haplotypes 3%2C4. L->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:1679030,ECO:0000269|PubMed:22513348,ECO:0000269|PubMed:8889590,ECO:0000269|PubMed:9521426;Dbxref=dbSNP:rs5030841,PMID:12501224,PMID:1679030,PMID:22513348,PMID:8889590,PMID:9521426 +P00439 UniProtKB Natural variant 53 53 . . . ID=VAR_000878;Note=In PKU. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452061;Dbxref=dbSNP:rs118092776,PMID:9452061 +P00439 UniProtKB Natural variant 55 55 . . . ID=VAR_000879;Note=In HPA and PKU%3B does not affect oligomerization%3B results in loss of substrate activation. F->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:18538294,ECO:0000269|PubMed:9521426;Dbxref=dbSNP:rs199475598,PMID:12501224,PMID:18538294,PMID:9521426 +P00439 UniProtKB Natural variant 56 56 . . . ID=VAR_000880;Note=In PKU%3B haplotype 10. E->D;Dbxref=dbSNP:rs199475567 +P00439 UniProtKB Natural variant 61 61 . . . ID=VAR_067995;Note=In PKU. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12501224;Dbxref=dbSNP:rs199475651,PMID:12501224 +P00439 UniProtKB Natural variant 62 62 . . . ID=VAR_067996;Note=In PKU. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22513348;Dbxref=PMID:22513348 +P00439 UniProtKB Natural variant 63 64 . . . ID=VAR_000881;Note=In PKU%3B haplotype 1%3B abolishes phenylalanine binding. TH->PN +P00439 UniProtKB Natural variant 65 65 . . . ID=VAR_000882;Note=In PKU. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9521426;Dbxref=dbSNP:rs75193786,PMID:9521426 +P00439 UniProtKB Natural variant 65 65 . . . ID=VAR_067997;Note=In PKU%3B results in disturbed oligomerization%3B results in loss of substrate activation. I->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:18538294;Dbxref=dbSNP:rs75193786,PMID:12501224,PMID:18538294 +P00439 UniProtKB Natural variant 65 65 . . . ID=VAR_000883;Note=In PKU%3B haplotypes 1%2C5%2C9%2C21%2CB%3B abolishes phenylalanine binding. I->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:8889590,ECO:0000269|PubMed:9452062;Dbxref=dbSNP:rs75193786,PMID:12501224,PMID:8889590,PMID:9452062 +P00439 UniProtKB Natural variant 65 65 . . . ID=VAR_067998;Note=In HPA and PKU. I->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:23792259;Dbxref=dbSNP:rs199475643,PMID:12501224,PMID:23792259 +P00439 UniProtKB Natural variant 67 67 . . . ID=VAR_000884;Note=In PKU%3B haplotype 4. S->P;Dbxref=dbSNP:rs5030842 +P00439 UniProtKB Natural variant 68 68 . . . ID=VAR_000885;Note=In PKU%3B haplotype 1. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8889590;Dbxref=dbSNP:rs76394784,PMID:8889590 +P00439 UniProtKB Natural variant 76 76 . . . ID=VAR_000886;Note=In PKU. E->A;Dbxref=dbSNP:rs62507347 +P00439 UniProtKB Natural variant 76 76 . . . ID=VAR_067999;Note=In non-PKU HPA. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11935335;Dbxref=dbSNP:rs62507347,PMID:11935335 +P00439 UniProtKB Natural variant 84 84 . . . ID=VAR_000887;Note=In PKU%3B haplotype 4. D->Y;Dbxref=dbSNP:rs62514902 +P00439 UniProtKB Natural variant 87 87 . . . ID=VAR_000888;Note=In non-PKU HPA%3B haplotype 1. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8088845;Dbxref=dbSNP:rs62516151,PMID:8088845 +P00439 UniProtKB Natural variant 92 92 . . . ID=VAR_000889;Note=In PKU. T->I;Dbxref=dbSNP:rs62514903 +P00439 UniProtKB Natural variant 94 94 . . . ID=VAR_000890;Note=In PKU%3B mild%3B haplotype 2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1709636;Dbxref=PMID:1709636 +P00439 UniProtKB Natural variant 98 98 . . . ID=VAR_000891;Note=In non-PKU HPA. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8364546;Dbxref=dbSNP:rs62517167,PMID:8364546 +P00439 UniProtKB Natural variant 104 104 . . . ID=VAR_000892;Note=In PKU%3B mild%3B haplotype 1. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9792411;Dbxref=dbSNP:rs62642929,PMID:9792411 +P00439 UniProtKB Natural variant 110 110 . . . ID=VAR_009241;Note=In HPA. S->C +P00439 UniProtKB Natural variant 121 121 . . . ID=VAR_069776;Note=In HPA. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23792259;Dbxref=PMID:23792259 +P00439 UniProtKB Natural variant 124 124 . . . ID=VAR_000893;Note=In PKU%3B haplotype 28. T->I;Dbxref=dbSNP:rs199475571 +P00439 UniProtKB Natural variant 129 129 . . . ID=VAR_000894;Note=In PKU. D->Y;Dbxref=dbSNP:rs199475606 +P00439 UniProtKB Natural variant 143 143 . . . ID=VAR_000895;Note=In PKU%3B haplotype 11. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8889583;Dbxref=dbSNP:rs199475572,PMID:8889583 +P00439 UniProtKB Natural variant 145 145 . . . ID=VAR_011566;Note=In PKU. D->V;Dbxref=dbSNP:rs140175796 +P00439 UniProtKB Natural variant 146 146 . . . ID=VAR_000896;Note=In PKU. H->Y;Dbxref=dbSNP:rs199475599 +P00439 UniProtKB Natural variant 148 148 . . . ID=VAR_000897;Note=In PKU%3B haplotypes 1%2C2%2C7. G->S;Dbxref=dbSNP:rs80297647 +P00439 UniProtKB Natural variant 151 151 . . . ID=VAR_000898;Note=In PKU%3B haplotypes 1%2C8. D->H;Dbxref=dbSNP:rs199475597 +P00439 UniProtKB Natural variant 154 154 . . . ID=VAR_000899;Note=In PKU. Y->N;Dbxref=dbSNP:rs199475587 +P00439 UniProtKB Natural variant 155 155 . . . ID=VAR_009242;Note=In PKU. R->P;Dbxref=dbSNP:rs199475663 +P00439 UniProtKB Natural variant 157 157 . . . ID=VAR_000900;Note=In PKU%3B severe%3B 5%25 activity%3B requires 2 nucleotide substitutions. R->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9792411;Dbxref=PMID:9792411 +P00439 UniProtKB Natural variant 157 157 . . . ID=VAR_068000;Note=In PKU. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22513348;Dbxref=dbSNP:rs199475612,PMID:22513348 +P00439 UniProtKB Natural variant 158 158 . . . ID=VAR_000901;Note=In PKU%3B haplotypes 1%2C2%2C4%2C7%2C16%2C 28. R->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:22513348,ECO:0000269|PubMed:9452062;Dbxref=dbSNP:rs5030843,PMID:12501224,PMID:22513348,PMID:9452062 +P00439 UniProtKB Natural variant 158 158 . . . ID=VAR_000902;Note=In PKU. R->W;Dbxref=dbSNP:rs75166491 +P00439 UniProtKB Natural variant 160 160 . . . ID=VAR_000903;Note=In PKU. Q->P;Dbxref=dbSNP:rs199475601 +P00439 UniProtKB Natural variant 161 161 . . . ID=VAR_000904;Note=In PKU%3B haplotype 4. F->S;Dbxref=dbSNP:rs79635844 +P00439 UniProtKB Natural variant 164 164 . . . ID=VAR_000905;Note=In PKU%3B haplotype 1. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7833954;Dbxref=dbSNP:rs199475595,PMID:7833954 +P00439 UniProtKB Natural variant 167 167 . . . ID=VAR_000906;Note=In PKU. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452062;Dbxref=dbSNP:rs77554925,PMID:9452062 +P00439 UniProtKB Natural variant 167 167 . . . ID=VAR_011567;Note=In HPA. N->S;Dbxref=dbSNP:rs77554925 +P00439 UniProtKB Natural variant 169 169 . . . ID=VAR_011568;Note=In PKU. R->H;Dbxref=dbSNP:rs199475679 +P00439 UniProtKB Natural variant 170 170 . . . ID=VAR_011569;Note=In HPA. H->D;Dbxref=dbSNP:rs199475655 +P00439 UniProtKB Natural variant 170 170 . . . ID=VAR_068001;Note=In PKU%3B does not affect oligomerization. H->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:18538294;Dbxref=dbSNP:rs199475652,PMID:12501224,PMID:18538294 +P00439 UniProtKB Natural variant 170 170 . . . ID=VAR_000907;Note=In PKU. H->R;Dbxref=dbSNP:rs199475573 +P00439 UniProtKB Natural variant 171 171 . . . ID=VAR_000908;Note=In PKU%3B haplotype 1. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7833954;Dbxref=dbSNP:rs199475596,PMID:7833954 +P00439 UniProtKB Natural variant 171 171 . . . ID=VAR_000909;Note=In PKU. G->R;Dbxref=dbSNP:rs199475613 +P00439 UniProtKB Natural variant 173 173 . . . ID=VAR_000910;Note=In PKU%3B haplotype 4. P->T;Dbxref=dbSNP:rs199475574 +P00439 UniProtKB Natural variant 174 174 . . . ID=VAR_000911;Note=In PKU%3B haplotype 1. I->T;Dbxref=dbSNP:rs138809906 +P00439 UniProtKB Natural variant 174 174 . . . ID=VAR_011570;Note=In PKU. I->V;Dbxref=dbSNP:rs199475632 +P00439 UniProtKB Natural variant 175 175 . . . ID=VAR_000912;Note=In PKU. P->A;Dbxref=dbSNP:rs199475604 +P00439 UniProtKB Natural variant 176 176 . . . ID=VAR_000913;Note=In non-PKU HPA. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8088845;Dbxref=dbSNP:rs74486803,PMID:8088845 +P00439 UniProtKB Natural variant 176 176 . . . ID=VAR_000914;Note=In PKU. R->P;Dbxref=dbSNP:rs74486803 +P00439 UniProtKB Natural variant 177 177 . . . ID=VAR_000915;Note=In PKU%3B haplotype 6. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22513348;Dbxref=dbSNP:rs199475602,PMID:22513348 +P00439 UniProtKB Natural variant 177 177 . . . ID=VAR_068002;Note=In HPA. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12501224;Dbxref=dbSNP:rs199475602,PMID:12501224 +P00439 UniProtKB Natural variant 178 178 . . . ID=VAR_000916;Note=In non-PKU HPA. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22513348;Dbxref=dbSNP:rs77958223,PMID:22513348 +P00439 UniProtKB Natural variant 183 183 . . . ID=VAR_009243;Note=In PKU. E->Q;Dbxref=dbSNP:rs199475664 +P00439 UniProtKB Natural variant 190 190 . . . ID=VAR_000917;Note=In PKU%3B haplotype 3. V->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22513348,ECO:0000269|PubMed:9452062;Dbxref=dbSNP:rs62514919,PMID:22513348,PMID:9452062 +P00439 UniProtKB Natural variant 194 194 . . . ID=VAR_000918;Note=In PKU. L->P;Dbxref=dbSNP:rs5030844 +P00439 UniProtKB Natural variant 194 194 . . . ID=VAR_000919;Note=In PKU. Missing +P00439 UniProtKB Natural variant 196 196 . . . ID=VAR_069777;Note=In HPA. S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23792259;Dbxref=PMID:23792259 +P00439 UniProtKB Natural variant 197 197 . . . ID=VAR_000920;Note=In PKU. Missing +P00439 UniProtKB Natural variant 198 198 . . . ID=VAR_000921;Note=In PKU%3B haplotype 2. Missing +P00439 UniProtKB Natural variant 201 201 . . . ID=VAR_000922;Note=In PKU. H->R;Dbxref=dbSNP:rs62517180 +P00439 UniProtKB Natural variant 201 201 . . . ID=VAR_000923;Note=In non-PKU HPA%3B haplotype 1. H->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23792259,ECO:0000269|PubMed:9521426;Dbxref=dbSNP:rs62517205,PMID:23792259,PMID:9521426 +P00439 UniProtKB Natural variant 204 204 . . . ID=VAR_000924;Note=In PKU%3B mild%3B haplotypes 3%2C4. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9048935;Dbxref=dbSNP:rs62514927,PMID:9048935 +P00439 UniProtKB Natural variant 205 205 . . . ID=VAR_011571;Note=In PKU. E->A;Dbxref=dbSNP:rs62508593 +P00439 UniProtKB Natural variant 206 206 . . . ID=VAR_000925;Note=In PKU. Y->D;Dbxref=dbSNP:rs62517170 +P00439 UniProtKB Natural variant 207 207 . . . ID=VAR_000926;Note=In PKU. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452061;Dbxref=dbSNP:rs62508572,PMID:9452061 +P00439 UniProtKB Natural variant 207 207 . . . ID=VAR_000927;Note=In PKU%3B severe%3B haplotype 4. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9048935;Dbxref=dbSNP:rs62508721,PMID:9048935 +P00439 UniProtKB Natural variant 211 211 . . . ID=VAR_000928;Note=In PKU%3B haplotype 4. P->T;Dbxref=dbSNP:rs62514931 +P00439 UniProtKB Natural variant 212 212 . . . ID=VAR_000929;Note=In PKU. L->P;Dbxref=dbSNP:rs62517198 +P00439 UniProtKB Natural variant 213 213 . . . ID=VAR_000930;Note=In PKU%3B severe. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9521426;Dbxref=dbSNP:rs62516109,PMID:9521426 +P00439 UniProtKB Natural variant 217 217 . . . ID=VAR_000931;Note=In PKU. C->G;Dbxref=dbSNP:rs62508718 +P00439 UniProtKB Natural variant 218 218 . . . ID=VAR_000932;Note=In PKU%3B haplotypes 1%2C2. G->V;Dbxref=dbSNP:rs62514933 +P00439 UniProtKB Natural variant 221 221 . . . ID=VAR_000933;Note=In PKU%3B haplotype 4. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1679030;Dbxref=dbSNP:rs62514934,PMID:1679030 +P00439 UniProtKB Natural variant 222 222 . . . ID=VAR_000934;Note=In PKU%3B haplotypes 3%2C4. D->V;Dbxref=dbSNP:rs62507319 +P00439 UniProtKB Natural variant 224 224 . . . ID=VAR_000935;Note=In PKU%3B haplotype 4. I->M;Dbxref=dbSNP:rs199475576 +P00439 UniProtKB Natural variant 225 225 . . . ID=VAR_000936;Note=In PKU. P->R;Dbxref=dbSNP:rs62517204 +P00439 UniProtKB Natural variant 225 225 . . . ID=VAR_000937;Note=In PKU%3B haplotype 1. P->T;Dbxref=dbSNP:rs199475589 +P00439 UniProtKB Natural variant 226 226 . . . ID=VAR_068003;Note=In PKU. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22513348;Dbxref=dbSNP:rs62508615,PMID:22513348 +P00439 UniProtKB Natural variant 230 230 . . . ID=VAR_000938;Note=In non-PKU HPA%3B haplotype 4. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23792259;Dbxref=dbSNP:rs62516152,PMID:23792259 +P00439 UniProtKB Natural variant 231 231 . . . ID=VAR_009244;Note=In PKU. S->F;Dbxref=dbSNP:rs62508577 +P00439 UniProtKB Natural variant 231 231 . . . ID=VAR_000939;Note=In PKU. S->P;Dbxref=dbSNP:rs5030845 +P00439 UniProtKB Natural variant 233 233 . . . ID=VAR_000940;Note=In PKU%3B haplotypes 2%2C3. F->L;Dbxref=dbSNP:rs62517208 +P00439 UniProtKB Natural variant 238 238 . . . ID=VAR_000941;Note=In PKU%3B haplotype 4. T->P;Dbxref=dbSNP:rs199475577 +P00439 UniProtKB Natural variant 239 239 . . . ID=VAR_000942;Note=In PKU. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7833954;Dbxref=dbSNP:rs62517178,PMID:7833954 +P00439 UniProtKB Natural variant 240 240 . . . ID=VAR_011572;Note=In PKU. F->S;Dbxref=dbSNP:rs62508594 +P00439 UniProtKB Natural variant 241 241 . . . ID=VAR_000943;Note=In non-PKU HPA and PKU%3B haplotype 34. R->C;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8889590,ECO:0000269|PubMed:9452062,ECO:0000269|PubMed:9852673;Dbxref=dbSNP:rs76687508,PMID:8889590,PMID:9452062,PMID:9852673 +P00439 UniProtKB Natural variant 241 241 . . . ID=VAR_000944;Note=In PKU%3B haplotypes 1%2C5. R->H;Dbxref=dbSNP:rs62508730 +P00439 UniProtKB Natural variant 241 241 . . . ID=VAR_000945;Note=In PKU. R->L;Dbxref=dbSNP:rs62508730 +P00439 UniProtKB Natural variant 242 242 . . . ID=VAR_000946;Note=In PKU. L->F;Dbxref=dbSNP:rs199475578 +P00439 UniProtKB Natural variant 243 243 . . . ID=VAR_000947;Note=In non-PKU HPA and PKU%3B haplotypes 4%2C7%2C9. R->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9600453,ECO:0000269|PubMed:9852673;Dbxref=dbSNP:rs62508588,PMID:9600453,PMID:9852673 +P00439 UniProtKB Natural variant 244 244 . . . ID=VAR_000948;Note=In PKU%3B haplotype 12. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1363838;Dbxref=dbSNP:rs118203923,PMID:1363838 +P00439 UniProtKB Natural variant 245 245 . . . ID=VAR_000949;Note=In PKU%2C HPA and non-PKU HPA%3B haplotypes 3%2C7. V->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:22513348,ECO:0000269|PubMed:8088845,ECO:0000269|PubMed:8889590;Dbxref=dbSNP:rs796052017,PMID:12501224,PMID:22513348,PMID:8088845,PMID:8889590 +P00439 UniProtKB Natural variant 245 245 . . . ID=VAR_000950;Note=In PKU%3B haplotype 11. V->E;Dbxref=dbSNP:rs76212747 +P00439 UniProtKB Natural variant 245 245 . . . ID=VAR_000951;Note=In PKU. V->L;Dbxref=dbSNP:rs62508694 +P00439 UniProtKB Natural variant 246 246 . . . ID=VAR_000952;Note=In PKU. A->D;Dbxref=dbSNP:rs199475610 +P00439 UniProtKB Natural variant 247 247 . . . ID=VAR_000953;Note=In PKU%3B haplotype 4. G->V;Dbxref=dbSNP:rs199475579 +P00439 UniProtKB Natural variant 248 248 . . . ID=VAR_000954;Note=In PKU. L->P;Dbxref=dbSNP:rs62507340 +P00439 UniProtKB Natural variant 249 249 . . . ID=VAR_000955;Note=In PKU%3B haplotype 1. L->F;Dbxref=dbSNP:rs74503222 +P00439 UniProtKB Natural variant 252 252 . . . ID=VAR_000956;Note=In PKU%3B haplotype 7. R->G;Dbxref=dbSNP:rs5030847 +P00439 UniProtKB Natural variant 252 252 . . . ID=VAR_000957;Note=In PKU%3B haplotype 1. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7833954;Dbxref=dbSNP:rs62644503,PMID:7833954 +P00439 UniProtKB Natural variant 252 252 . . . ID=VAR_000958;Note=In PKU%3B haplotypes 1%2C6%2C7%2C8%2C42%2C 69%3B complete loss of activity. R->W;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11461196,ECO:0000269|PubMed:1672294,ECO:0000269|PubMed:22513348,ECO:0000269|PubMed:23792259;Dbxref=dbSNP:rs5030847,PMID:11461196,PMID:1672294,PMID:22513348,PMID:23792259 +P00439 UniProtKB Natural variant 255 255 . . . ID=VAR_000960;Note=In PKU%3B haplotype 36. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2014802;Dbxref=dbSNP:rs62642930,PMID:2014802 +P00439 UniProtKB Natural variant 255 255 . . . ID=VAR_000959;Note=In PKU%3B haplotypes 18%2C21. L->V;Dbxref=dbSNP:rs62642931 +P00439 UniProtKB Natural variant 257 257 . . . ID=VAR_000961;Note=In PKU. G->C;Dbxref=dbSNP:rs5030848 +P00439 UniProtKB Natural variant 259 259 . . . ID=VAR_000962;Note=In PKU%3B haplotype 3. A->T;Dbxref=dbSNP:rs62642932 +P00439 UniProtKB Natural variant 259 259 . . . ID=VAR_000963;Note=In PKU%3B haplotypes 7%2C42. A->V;Dbxref=dbSNP:rs118203921 +P00439 UniProtKB Natural variant 261 261 . . . ID=VAR_000964;Note=In PKU. R->P;Dbxref=dbSNP:rs5030849 +P00439 UniProtKB Natural variant 261 261 . . . ID=VAR_000965;Note=In HPA and PKU%3B mild%3B haplotypes 1%2C2%2C4%2C22%2C 24%2C28. R->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:1671810,ECO:0000269|PubMed:22513348,ECO:0000269|PubMed:23792259,ECO:0000269|PubMed:8889590;Dbxref=dbSNP:rs5030849,PMID:12501224,PMID:1671810,PMID:22513348,PMID:23792259,PMID:8889590 +P00439 UniProtKB Natural variant 263 263 . . . ID=VAR_000966;Note=In PKU. F->L;Dbxref=dbSNP:rs62642944 +P00439 UniProtKB Natural variant 264 264 . . . ID=VAR_000967;Note=In PKU. H->L;Dbxref=dbSNP:rs199475580 +P00439 UniProtKB Natural variant 265 265 . . . ID=VAR_000968;Note=In PKU. C->G;Dbxref=dbSNP:rs62517181 +P00439 UniProtKB Natural variant 269 269 . . . ID=VAR_000969;Note=In non-PKU HPA. I->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9521426;Dbxref=dbSNP:rs62508692,PMID:9521426 +P00439 UniProtKB Natural variant 270 270 . . . ID=VAR_000970;Note=In PKU. R->K;Dbxref=dbSNP:rs62514950 +P00439 UniProtKB Natural variant 270 270 . . . ID=VAR_000971;Note=In PKU%3B haplotype 1. R->S;Dbxref=dbSNP:rs62514951 +P00439 UniProtKB Natural variant 271 271 . . . ID=VAR_000972;Note=In PKU. H->Y;Dbxref=dbSNP:rs62517164 +P00439 UniProtKB Natural variant 273 273 . . . ID=VAR_000973;Note=In PKU%3B haplotype 7. S->F;Dbxref=dbSNP:rs62514953 +P00439 UniProtKB Natural variant 274 274 . . . ID=VAR_011573;Note=K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11461196;Dbxref=dbSNP:rs142934616,PMID:11461196 +P00439 UniProtKB Natural variant 275 275 . . . ID=VAR_068004;Note=In PKU%3B reduced activity%3B increased affinity for the substrate%3B mildly reduced substrate activation%3B decreased cofactor affinity. P->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:18538294;Dbxref=dbSNP:rs62508715,PMID:12501224,PMID:18538294 +P00439 UniProtKB Natural variant 276 276 . . . ID=VAR_000974;Note=In PKU. M->I;Dbxref=dbSNP:rs62514954 +P00439 UniProtKB Natural variant 276 276 . . . ID=VAR_000975;Note=In PKU%3B haplotype 4. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8068076;Dbxref=dbSNP:rs62516149,PMID:8068076 +P00439 UniProtKB Natural variant 277 277 . . . ID=VAR_000976;Note=In PKU. Y->C;Dbxref=dbSNP:rs62516155 +P00439 UniProtKB Natural variant 277 277 . . . ID=VAR_000977;Note=In PKU%3B haplotype 2. Y->D;Dbxref=dbSNP:rs78655458 +P00439 UniProtKB Natural variant 278 278 . . . ID=VAR_000978;Note=In PKU. T->A;Dbxref=dbSNP:rs62516156 +P00439 UniProtKB Natural variant 278 278 . . . ID=VAR_000979;Note=In PKU. T->N;Dbxref=dbSNP:rs62507262 +P00439 UniProtKB Natural variant 280 280 . . . ID=VAR_000980;Note=In PKU%3B haplotypes 1%2C2%2C4%2C16%2C38%3B partial residual activity. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22513348,ECO:0000269|PubMed:2564729,ECO:0000269|PubMed:8889590;Dbxref=dbSNP:rs62508698,PMID:22513348,PMID:2564729,PMID:8889590 +P00439 UniProtKB Natural variant 281 281 . . . ID=VAR_000981;Note=In PKU%3B haplotypes 1%2C4. P->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:1672290,ECO:0000269|PubMed:1672294,ECO:0000269|PubMed:22513348,ECO:0000269|PubMed:8889590;Dbxref=dbSNP:rs5030851,PMID:12501224,PMID:1672290,PMID:1672294,PMID:22513348,PMID:8889590 +P00439 UniProtKB Natural variant 282 282 . . . ID=VAR_000982;Note=In PKU%3B haplotype 1. D->N;Dbxref=dbSNP:rs199475582 +P00439 UniProtKB Natural variant 283 283 . . . ID=VAR_000983;Note=In PKU%3B haplotype 21. I->F;Dbxref=dbSNP:rs62517168 +P00439 UniProtKB Natural variant 283 283 . . . ID=VAR_000984;Note=In PKU%3B severe. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9521426;Dbxref=dbSNP:rs62508693,PMID:9521426 +P00439 UniProtKB Natural variant 290 290 . . . ID=VAR_067758;Note=In PKU. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22526846;Dbxref=PMID:22526846 +P00439 UniProtKB Natural variant 297 297 . . . ID=VAR_000985;Note=In PKU%3B haplotype 4. R->C;Dbxref=dbSNP:rs62642945 +P00439 UniProtKB Natural variant 297 297 . . . ID=VAR_000986;Note=In PKU. R->H;Dbxref=dbSNP:rs62642939 +P00439 UniProtKB Natural variant 299 299 . . . ID=VAR_000987;Note=In PKU%3B haplotype 8. F->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8889590;Dbxref=dbSNP:rs62642933,PMID:8889590 +P00439 UniProtKB Natural variant 300 300 . . . ID=VAR_000988;Note=In PKU and HPA%3B haplotype 1%3B does not affect oligomerization%3B reduction in activity is probably due to a global conformational change in the protein that reduces allostery. A->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:18538294,ECO:0000269|PubMed:22513348,ECO:0000269|PubMed:23792259;Dbxref=dbSNP:rs5030853,PMID:12501224,PMID:18538294,PMID:22513348,PMID:23792259 +P00439 UniProtKB Natural variant 300 300 . . . ID=VAR_000989;Note=In PKU. A->V;Dbxref=dbSNP:rs199475609 +P00439 UniProtKB Natural variant 303 303 . . . ID=VAR_000990;Note=In PKU%3B haplotype 5. S->P;Dbxref=dbSNP:rs199475608 +P00439 UniProtKB Natural variant 304 304 . . . ID=VAR_000991;Note=In PKU. Q->R;Dbxref=dbSNP:rs199475592 +P00439 UniProtKB Natural variant 306 306 . . . ID=VAR_000992;Note=In non-PKU HPA%3B haplotype 4. I->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1358789,ECO:0000269|PubMed:23792259;Dbxref=dbSNP:rs62642934,PMID:1358789,PMID:23792259 +P00439 UniProtKB Natural variant 309 309 . . . ID=VAR_000993;Note=In PKU%3B haplotype 7. A->D;Dbxref=dbSNP:rs62642935 +P00439 UniProtKB Natural variant 309 309 . . . ID=VAR_000994;Note=In PKU. A->V;Dbxref=dbSNP:rs62642935 +P00439 UniProtKB Natural variant 310 310 . . . ID=VAR_000995;Note=In PKU%3B haplotype 7. S->F;Dbxref=dbSNP:rs62642913 +P00439 UniProtKB Natural variant 310 310 . . . ID=VAR_068005;Note=In HPA%3B reduction in activity is probably due to a global conformational change in the protein that reduces allostery. S->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:18538294;Dbxref=dbSNP:rs62642913,PMID:12501224,PMID:18538294 +P00439 UniProtKB Natural variant 311 311 . . . ID=VAR_000996;Note=In PKU%3B haplotypes 1%2C7%2C10. L->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2615649,ECO:0000269|PubMed:2840952;Dbxref=dbSNP:rs62642936,PMID:2615649,PMID:2840952 +P00439 UniProtKB Natural variant 314 314 . . . ID=VAR_000997;Note=In PKU. P->H;Dbxref=dbSNP:rs62642940 +P00439 UniProtKB Natural variant 314 314 . . . ID=VAR_068006;Note=In HPA%3B does not affect oligomerization%3B reduction in activity is probably due to a global conformational change in the protein that reduces allostery. P->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:18538294;Dbxref=dbSNP:rs199475650,PMID:12501224,PMID:18538294 +P00439 UniProtKB Natural variant 318 318 . . . ID=VAR_011574;Note=In PKU%3B partial loss of activity. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11461196;Dbxref=dbSNP:rs62642918,PMID:11461196 +P00439 UniProtKB Natural variant 322 322 . . . ID=VAR_000998;Note=In PKU%3B haplotype 12. A->G;Dbxref=dbSNP:rs62514958 +P00439 UniProtKB Natural variant 322 322 . . . ID=VAR_000999;Note=In PKU%3B haplotype 1. A->T;Dbxref=dbSNP:rs62514957 +P00439 UniProtKB Natural variant 322 322 . . . ID=VAR_067759;Note=In PKU. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22526846;Dbxref=PMID:22526846 +P00439 UniProtKB Natural variant 325 325 . . . ID=VAR_009245;Note=In PKU. Y->C;Dbxref=dbSNP:rs62508578 +P00439 UniProtKB Natural variant 330 330 . . . ID=VAR_009246;Note=In PKU. E->D;Dbxref=dbSNP:rs62508580 +P00439 UniProtKB Natural variant 331 331 . . . ID=VAR_001000;Note=In PKU%3B haplotype 1. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7833954;Dbxref=dbSNP:rs62517179,PMID:7833954 +P00439 UniProtKB Natural variant 333 333 . . . ID=VAR_001001;Note=In PKU. L->F;Dbxref=dbSNP:rs62516060 +P00439 UniProtKB Natural variant 334 334 . . . ID=VAR_001002;Note=In PKU. C->S;Dbxref=dbSNP:rs62517174 +P00439 UniProtKB Natural variant 337 337 . . . ID=VAR_001003;Note=In PKU. G->V;Dbxref=dbSNP:rs62517206 +P00439 UniProtKB Natural variant 338 338 . . . ID=VAR_001004;Note=In PKU%3B haplotype 4. D->Y;Dbxref=dbSNP:rs62516150 +P00439 UniProtKB Natural variant 341 341 . . . ID=VAR_001005;Note=In PKU. K->R;Dbxref=dbSNP:rs62516153 +P00439 UniProtKB Natural variant 341 341 . . . ID=VAR_001006;Note=In PKU. K->T;Dbxref=dbSNP:rs62516153 +P00439 UniProtKB Natural variant 342 342 . . . ID=VAR_001007;Note=In PKU%3B haplotype 5. A->T;Dbxref=dbSNP:rs62507282 +P00439 UniProtKB Natural variant 343 343 . . . ID=VAR_001008;Note=In PKU. Y->C;Dbxref=dbSNP:rs62507265 +P00439 UniProtKB Natural variant 344 344 . . . ID=VAR_009247;Note=In PKU. G->R;Dbxref=dbSNP:rs62508679 +P00439 UniProtKB Natural variant 344 344 . . . ID=VAR_009248;Note=In PKU. G->V;Dbxref=dbSNP:rs62508582 +P00439 UniProtKB Natural variant 345 345 . . . ID=VAR_001009;Note=In PKU. A->S;Dbxref=dbSNP:rs62516062 +P00439 UniProtKB Natural variant 345 345 . . . ID=VAR_001010;Note=In PKU%3B haplotype 7. A->T;Dbxref=dbSNP:rs62516062 +P00439 UniProtKB Natural variant 347 347 . . . ID=VAR_001011;Note=In PKU. L->F;Dbxref=dbSNP:rs62516154 +P00439 UniProtKB Natural variant 348 348 . . . ID=VAR_001012;Note=In PKU%3B mild haplotype 9. L->V;Dbxref=dbSNP:rs62516092 +P00439 UniProtKB Natural variant 349 349 . . . ID=VAR_001013;Note=In PKU%3B severe. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9600453;Dbxref=dbSNP:rs62507279,PMID:9600453 +P00439 UniProtKB Natural variant 349 349 . . . ID=VAR_001014;Note=In PKU%3B haplotypes 1%2C4. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22513348;Dbxref=dbSNP:rs62508646,PMID:22513348 +P00439 UniProtKB Natural variant 350 350 . . . ID=VAR_001015;Note=In PKU%3B haplotype 2. S->T;Dbxref=dbSNP:rs62517183 +P00439 UniProtKB Natural variant 357 357 . . . ID=VAR_011575;Note=In PKU. C->G;Dbxref=dbSNP:rs62508595 +P00439 UniProtKB Natural variant 362 362 . . . ID=VAR_001016;Note=In PKU. P->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10200057;Dbxref=dbSNP:rs62507329,PMID:10200057 +P00439 UniProtKB Natural variant 364 368 . . . ID=VAR_001018;Note=In PKU. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1363837;Dbxref=PMID:1363837 +P00439 UniProtKB Natural variant 364 364 . . . ID=VAR_001017;Note=In PKU%3B haplotype 5. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1975559;Dbxref=PMID:1975559 +P00439 UniProtKB Natural variant 366 366 . . . ID=VAR_001019;Note=In PKU. P->H;Dbxref=dbSNP:rs62516098 +P00439 UniProtKB Natural variant 372 372 . . . ID=VAR_001020;Note=In PKU. T->S;Dbxref=dbSNP:rs62517163 +P00439 UniProtKB Natural variant 377 377 . . . ID=VAR_001021;Note=In PKU%3B haplotype 4. Y->C;Dbxref=dbSNP:rs62642942 +P00439 UniProtKB Natural variant 380 380 . . . ID=VAR_001022;Note=In non-PKU HPA%3B haplotype 4. T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23792259;Dbxref=dbSNP:rs62642937,PMID:23792259 +P00439 UniProtKB Natural variant 386 386 . . . ID=VAR_001023;Note=In PKU%3B common mutation. Y->C;Dbxref=dbSNP:rs62516141 +P00439 UniProtKB Natural variant 387 387 . . . ID=VAR_001024;Note=In PKU%3B haplotype 1. Y->H;Dbxref=dbSNP:rs62517194 +P00439 UniProtKB Natural variant 388 388 . . . ID=VAR_001025;Note=In PKU. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452061;Dbxref=dbSNP:rs62516101,PMID:9452061 +P00439 UniProtKB Natural variant 388 388 . . . ID=VAR_001026;Note=In PKU%3B haplotypes 1%2C4. V->M;Dbxref=dbSNP:rs62516101 +P00439 UniProtKB Natural variant 390 390 . . . ID=VAR_001027;Note=In PKU and non-PKU HPA%3B haplotype 4. E->G;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:22513348,ECO:0000269|PubMed:23792259,ECO:0000269|PubMed:8098245,ECO:0000269|PubMed:8889590;Dbxref=dbSNP:rs5030856,PMID:12501224,PMID:22513348,PMID:23792259,PMID:8098245,PMID:8889590 +P00439 UniProtKB Natural variant 394 394 . . . ID=VAR_001028;Note=In PKU. D->A;Dbxref=dbSNP:rs62516102 +P00439 UniProtKB Natural variant 394 394 . . . ID=VAR_001029;Note=In PKU. D->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8889590;Dbxref=dbSNP:rs62516142,PMID:8889590 +P00439 UniProtKB Natural variant 395 395 . . . ID=VAR_001030;Note=In PKU. A->G;Dbxref=dbSNP:rs62508736 +P00439 UniProtKB Natural variant 395 395 . . . ID=VAR_001031;Note=In PKU%3B haplotype 1. A->P;Dbxref=dbSNP:rs62516103 +P00439 UniProtKB Natural variant 399 400 . . . ID=VAR_001032;Note=In PKU%3B haplotype 7. Missing +P00439 UniProtKB Natural variant 403 403 . . . ID=VAR_001033;Note=In non-PKU HPA and PKU%3B haplotype 43. A->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:22513348,ECO:0000269|PubMed:23792259,ECO:0000269|PubMed:8889590;Dbxref=dbSNP:rs5030857,PMID:12501224,PMID:22513348,PMID:23792259,PMID:8889590 +P00439 UniProtKB Natural variant 407 407 . . . ID=VAR_068007;Note=In PKU. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9950317;Dbxref=dbSNP:rs62644473,PMID:9950317 +P00439 UniProtKB Natural variant 407 407 . . . ID=VAR_011576;Note=In PKU. P->S;Dbxref=dbSNP:rs62644465 +P00439 UniProtKB Natural variant 408 408 . . . ID=VAR_001034;Note=In PKU%3B haplotypes 4%2C12. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1355066;Dbxref=dbSNP:rs5030859,PMID:1355066 +P00439 UniProtKB Natural variant 408 408 . . . ID=VAR_001035;Note=In HPA and PKU%3B haplotypes 1%2C2%2C4%2C5%2C13%2C34%2C 41%2C44%3B most common mutation%3B reduction in activity is probably due to a global conformational change in the protein that reduces allostery. R->W;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:1355066,ECO:0000269|PubMed:18538294,ECO:0000269|PubMed:22513348,ECO:0000269|PubMed:23792259,ECO:0000269|PubMed:8889590,ECO:0000269|PubMed:9452062,ECO:0000269|PubMed:9600453;Dbxref=dbSNP:rs5030858,PMID:12501224,PMID:1355066,PMID:18538294,PMID:22513348,PMID:23792259,PMID:8889590,PMID:9452062,PMID:9600453 +P00439 UniProtKB Natural variant 410 410 . . . ID=VAR_009249;Note=In PKU%3B mild. F->S;Dbxref=dbSNP:rs62644475 +P00439 UniProtKB Natural variant 413 413 . . . ID=VAR_001036;Note=In non-PKU HPA and PKU%3B haplotype 4. R->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:9852673;Dbxref=dbSNP:rs79931499,PMID:12501224,PMID:9852673 +P00439 UniProtKB Natural variant 413 413 . . . ID=VAR_001037;Note=In PKU%3B haplotype 1. R->S;Dbxref=dbSNP:rs62644467 +P00439 UniProtKB Natural variant 414 414 . . . ID=VAR_001038;Note=In HPA and PKU%3B haplotype 4%3B does not affect oligomerization%3B reduction in activity is probably due to a global conformational change in the protein that reduces allostery. Y->C;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:18538294,ECO:0000269|PubMed:8889590;Dbxref=dbSNP:rs5030860,PMID:12501224,PMID:18538294,PMID:8889590 +P00439 UniProtKB Natural variant 415 415 . . . ID=VAR_001039;Note=In PKU%2C HPA and non-PKU HPA%3B haplotype 1. D->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:1358789,ECO:0000269|PubMed:22513348;Dbxref=dbSNP:rs62644499,PMID:12501224,PMID:1358789,PMID:22513348 +P00439 UniProtKB Natural variant 417 417 . . . ID=VAR_068008;Note=In PKU%3B reduction in activity is probably due to a global conformational change in the protein that reduces allostery. Y->H;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12501224,ECO:0000269|PubMed:18538294;Dbxref=dbSNP:rs62644471,PMID:12501224,PMID:18538294 +P00439 UniProtKB Natural variant 418 418 . . . ID=VAR_001040;Note=In PKU%3B haplotype 4. T->P;Dbxref=dbSNP:rs62644501 +P00439 UniProtKB Natural variant 421 421 . . . ID=VAR_067760;Note=In PKU. I->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22526846;Dbxref=PMID:22526846 +P00439 UniProtKB Natural variant 430 430 . . . ID=VAR_001041;Note=In PKU. L->P;Dbxref=dbSNP:rs199475607 +P00439 UniProtKB Natural variant 447 447 . . . ID=VAR_001042;Note=In PKU. A->D;Dbxref=dbSNP:rs76542238 +P00439 UniProtKB Mutagenesis 283 283 . . . Note=Loss of positive cooperativity and reduction of fold-activation by L-Phe preincubation. I->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18835579;Dbxref=PMID:18835579 +P00439 UniProtKB Sequence conflict 183 183 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00439 UniProtKB Beta strand 35 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FII +P00439 UniProtKB Helix 47 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FII +P00439 UniProtKB Beta strand 62 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FII +P00439 UniProtKB Beta strand 76 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FII +P00439 UniProtKB Helix 85 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FII +P00439 UniProtKB Helix 91 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FII +P00439 UniProtKB Beta strand 105 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FII +P00439 UniProtKB Helix 125 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Beta strand 135 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAH +P00439 UniProtKB Helix 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Turn 147 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Helix 152 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Helix 181 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Helix 204 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Helix 227 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Beta strand 241 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Beta strand 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MMT +P00439 UniProtKB Helix 251 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Beta strand 262 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Helix 283 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Helix 291 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Helix 297 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Helix 315 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Turn 328 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Beta strand 333 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Beta strand 339 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Helix 345 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Helix 351 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Beta strand 359 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Helix 369 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Beta strand 379 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Beta strand 384 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Helix 392 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Beta strand 409 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Turn 416 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Beta strand 420 424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J8U +P00439 UniProtKB Helix 426 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PAH \ No newline at end of file diff --git a/tests/testdata/annotation/P38995.gff b/tests/testdata/annotation/P38995.gff new file mode 100644 index 0000000..b0af337 --- /dev/null +++ b/tests/testdata/annotation/P38995.gff @@ -0,0 +1,37 @@ +##gff-version 3 +##sequence-region P38995 1 1004 +P38995 UniProtKB Chain 1 1004 . . . ID=PRO_0000046318;Note=Copper-transporting ATPase +P38995 UniProtKB Topological domain 1 262 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Transmembrane 263 283 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Topological domain 284 303 . . . Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Transmembrane 304 324 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Topological domain 325 335 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Transmembrane 336 356 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Topological domain 357 370 . . . Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Transmembrane 371 391 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Topological domain 392 528 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Transmembrane 529 549 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Topological domain 550 577 . . . Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Transmembrane 578 598 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Topological domain 599 901 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Transmembrane 902 924 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Topological domain 925 927 . . . Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Transmembrane 928 950 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Topological domain 951 1004 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Domain 3 68 . . . Note=HMA 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38995 UniProtKB Domain 81 147 . . . Note=HMA 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38995 UniProtKB Active site 627 627 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38995 UniProtKB Metal binding 13 13 . . . Note=Copper +P38995 UniProtKB Metal binding 16 16 . . . Note=Copper +P38995 UniProtKB Metal binding 91 91 . . . Note=Copper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38995 UniProtKB Metal binding 94 94 . . . Note=Copper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38995 UniProtKB Metal binding 838 838 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38995 UniProtKB Metal binding 842 842 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38995 UniProtKB Beta strand 2 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ +P38995 UniProtKB Helix 14 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ +P38995 UniProtKB Beta strand 27 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ +P38995 UniProtKB Turn 37 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ +P38995 UniProtKB Beta strand 41 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ +P38995 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVS +P38995 UniProtKB Helix 52 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ +P38995 UniProtKB Beta strand 66 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ diff --git a/tests/DSSP/1iej.dssp b/tests/testdata/dssp/1iej.dssp similarity index 100% rename from tests/DSSP/1iej.dssp rename to tests/testdata/dssp/1iej.dssp diff --git a/tests/testdata/dssp/2pah.dssp b/tests/testdata/dssp/2pah.dssp new file mode 100644 index 0000000..77e0c15 --- /dev/null +++ b/tests/testdata/dssp/2pah.dssp @@ -0,0 +1,682 @@ +==== Secondary Structure Definition by the program DSSP, CMBI version by M.L. Hekkelman/2010-10-21 ==== DATE=2017-03-23 . +REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . +HEADER HYDROXYLASE, PHENYLKETONURIA 2PAH . +COMPND PROTEIN (PHENYLALANINE HYDROXYLASE) . +SOURCE Homo sapiens . +AUTHOR . + 651 4 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . + 31806.6 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . + 448 68.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . + 26 4.0 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . + 30 4.6 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . + 2 0.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES . + 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . + 4 0.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-3), SAME NUMBER PER 100 RESIDUES . + 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-2), SAME NUMBER PER 100 RESIDUES . + 1 0.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-1), SAME NUMBER PER 100 RESIDUES . + 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+0), SAME NUMBER PER 100 RESIDUES . + 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+1), SAME NUMBER PER 100 RESIDUES . + 34 5.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . + 78 12.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . + 253 38.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . + 16 2.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+5), SAME NUMBER PER 100 RESIDUES . + 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 *** HISTOGRAMS OF *** . + 0 0 2 4 0 2 0 2 0 0 4 0 3 3 0 2 0 0 0 0 2 0 1 0 1 0 0 0 0 0 RESIDUES PER ALPHA HELIX . + 2 4 0 2 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 PARALLEL BRIDGES PER LADDER . + 4 0 0 2 2 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 ANTIPARALLEL BRIDGES PER LADDER . + 2 2 0 2 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 LADDERS PER SHEET . + # RESIDUE AA STRUCTURE BP1 BP2 ACC N-H-->O O-->H-N N-H-->O O-->H-N TCO KAPPA ALPHA PHI PSI X-CA Y-CA Z-CA + 1 118 A V 0 0 127 0, 0.0 190,-0.1 0, 0.0 285,-0.0 0.000 360.0 360.0 360.0 124.7 -7.1 21.7 20.2 + 2 119 A P - 0 0 42 0, 0.0 2,-0.3 0, 0.0 0, 0.0 -0.071 360.0-105.4 -51.6 149.9 -3.8 21.2 22.2 + 3 120 A W - 0 0 120 186,-0.0 187,-0.2 187,-0.0 0, 0.0 -0.593 41.9-178.8 -81.0 139.2 -2.6 17.7 22.8 + 4 121 A F - 0 0 17 -2,-0.3 2,-0.2 185,-0.1 127,-0.1 -0.980 33.0 -92.9-138.9 150.9 -3.1 16.3 26.3 + 5 122 A P - 0 0 4 0, 0.0 3,-0.1 0, 0.0 6,-0.1 -0.405 27.9-176.6 -65.3 130.9 -2.2 13.0 28.1 + 6 123 A R S S+ 0 0 121 -2,-0.2 293,-3.9 1,-0.1 2,-0.3 0.766 72.8 42.2 -94.3 -34.0 -5.0 10.4 28.1 + 7 124 A T B > S-A 298 0A 23 291,-0.2 3,-1.0 1,-0.1 291,-0.2 -0.796 81.4-122.8-114.6 157.2 -3.1 7.9 30.2 + 8 125 A I G > S+ 0 0 2 289,-1.5 3,-0.9 -2,-0.3 290,-0.1 0.785 114.7 55.4 -65.5 -30.0 -0.8 8.3 33.3 + 9 126 A Q G > S+ 0 0 87 288,-0.3 3,-1.2 1,-0.2 -1,-0.3 0.594 89.5 77.1 -79.3 -11.7 2.0 6.7 31.4 + 10 127 A E G X S+ 0 0 55 -3,-1.0 3,-1.1 1,-0.3 -1,-0.2 0.490 71.6 81.8 -76.5 -3.3 1.6 9.2 28.6 + 11 128 A L G X> + 0 0 0 -3,-0.9 3,-1.3 1,-0.3 4,-0.8 0.472 66.9 88.0 -78.6 -2.0 3.4 11.8 30.8 + 12 129 A D G <4 S+ 0 0 36 -3,-1.2 -1,-0.3 1,-0.3 -2,-0.1 0.536 77.0 66.8 -71.6 -7.5 6.6 10.1 29.5 + 13 130 A R G X4 S+ 0 0 146 -3,-1.1 3,-0.8 1,-0.1 -1,-0.3 0.687 90.0 61.7 -85.5 -22.6 6.4 12.6 26.7 + 14 131 A F T <4 S+ 0 0 38 -3,-1.3 2,-0.4 1,-0.3 3,-0.2 0.916 113.4 34.7 -68.7 -44.7 7.0 15.5 29.1 + 15 132 A A T 3< S+ 0 0 4 -4,-0.8 -1,-0.3 1,-0.2 -2,-0.1 -0.484 79.4 141.0-107.2 57.7 10.5 14.1 30.0 + 16 133 A N < - 0 0 49 -3,-0.8 -1,-0.2 -2,-0.4 3,-0.1 0.994 58.7-129.6 -60.0 -65.6 11.2 12.7 26.5 + 17 134 A Q S S+ 0 0 93 1,-1.2 -1,-0.1 -3,-0.2 2,-0.1 -0.524 89.4 61.4 141.1 -54.7 14.9 13.6 26.4 + 18 135 A I 0 0 121 1,-0.2 -1,-1.2 26,-0.1 -2,-0.2 -0.370 360.0 360.0 -86.4 172.3 14.7 15.2 23.0 + 19 136 A L 0 0 187 -3,-0.1 -1,-0.2 -2,-0.1 -3,-0.1 0.893 360.0 360.0 74.5 360.0 12.4 18.3 22.5 + 20 ! 0 0 0 0, 0.0 0, 0.0 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 360.0 0.0 0.0 0.0 + 21 143 A D > 0 0 153 3,-0.1 3,-4.4 2,-0.1 6,-0.1 0.000 360.0 360.0 360.0 100.9 21.8 31.8 32.4 + 22 144 A A T 3 + 0 0 66 1,-0.3 5,-0.3 5,-0.1 6,-0.2 0.628 360.0 63.8 -21.6 -47.3 24.8 33.7 33.8 + 23 145 A D T 3 S+ 0 0 111 2,-0.1 -1,-0.3 4,-0.1 -2,-0.1 0.689 82.0 104.5 -60.7 -16.3 22.8 35.4 36.5 + 24 146 A H S X S- 0 0 27 -3,-4.4 3,-1.9 1,-0.1 2,-0.3 -0.516 82.7-117.8 -71.0 123.7 22.2 32.0 38.0 + 25 147 A P T 3 S+ 0 0 27 0, 0.0 124,-0.3 0, 0.0 -1,-0.1 -0.460 102.3 27.8 -65.0 121.5 24.4 31.3 41.0 + 26 148 A G T > S+ 0 0 14 -2,-0.3 3,-0.8 -4,-0.1 7,-0.2 0.449 79.6 122.6 105.7 3.2 26.7 28.4 40.2 + 27 149 A F T < S+ 0 0 74 -3,-1.9 -5,-0.1 -5,-0.3 -6,-0.1 0.822 78.9 48.0 -64.5 -31.3 26.8 29.1 36.5 + 28 150 A K T 3 S+ 0 0 188 -4,-0.2 -1,-0.3 -6,-0.2 -6,-0.0 0.518 89.5 100.4 -87.2 -6.4 30.5 29.4 36.8 + 29 151 A D <> - 0 0 48 -3,-0.8 4,-2.0 1,-0.2 5,-0.2 -0.719 53.8-167.9 -87.1 107.0 30.8 26.1 38.8 + 30 152 A P H > S+ 0 0 102 0, 0.0 4,-1.8 0, 0.0 -1,-0.2 0.783 86.4 46.0 -62.1 -30.3 31.9 23.3 36.5 + 31 153 A V H > S+ 0 0 93 2,-0.2 4,-2.4 3,-0.1 5,-0.2 0.984 114.1 42.1 -75.8 -69.7 31.0 20.7 39.1 + 32 154 A Y H > S+ 0 0 20 1,-0.2 4,-2.7 2,-0.2 5,-0.2 0.843 115.4 57.0 -44.4 -38.3 27.6 21.8 40.3 + 33 155 A R H X S+ 0 0 135 -4,-2.0 4,-1.0 1,-0.2 3,-0.3 0.986 110.9 38.0 -57.5 -63.8 26.9 22.4 36.7 + 34 156 A A H X S+ 0 0 60 -4,-1.8 4,-0.6 1,-0.2 -1,-0.2 0.687 114.3 59.6 -62.6 -19.3 27.6 18.8 35.6 + 35 157 A R H >X S+ 0 0 25 -4,-2.4 4,-1.8 2,-0.2 3,-0.6 0.928 104.6 46.9 -73.9 -45.8 26.0 17.7 38.8 + 36 158 A R H 3X S+ 0 0 50 -4,-2.7 4,-1.5 -3,-0.3 -2,-0.2 0.655 110.6 53.2 -69.2 -17.2 22.7 19.4 37.8 + 37 159 A K H 3X S+ 0 0 141 -4,-1.0 4,-1.7 2,-0.2 -1,-0.3 0.673 104.6 57.0 -87.0 -21.8 23.0 17.8 34.4 + 38 160 A Q H X S+ 0 0 8 -4,-1.8 4,-1.5 2,-0.2 3,-0.5 0.949 111.1 52.2 -63.8 -50.4 20.1 15.0 37.9 + 40 162 A A H 3X S+ 0 0 15 -4,-1.5 4,-2.4 1,-0.3 3,-0.2 0.891 105.0 55.4 -53.5 -45.0 18.4 16.1 34.7 + 41 163 A D H 3X S+ 0 0 62 -4,-1.7 4,-1.8 1,-0.3 -1,-0.3 0.864 101.4 58.6 -57.9 -37.1 19.6 13.0 32.8 + 42 164 A I H < S+ 0 0 2 -4,-1.5 3,-1.2 1,-0.2 -2,-0.2 0.944 108.3 52.2 -59.7 -53.6 14.7 12.6 34.6 + 44 166 A Y H 3< S+ 0 0 73 -4,-2.4 -1,-0.2 1,-0.3 -2,-0.2 0.778 114.3 45.0 -56.0 -28.5 15.1 12.1 30.9 + 45 167 A N H 3< S+ 0 0 106 -4,-1.8 2,-0.4 -3,-0.2 -1,-0.3 0.579 90.2 105.8 -92.5 -12.1 15.7 8.4 31.6 + 46 168 A Y << - 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0 0 0 -2,-0.5 -21,-0.9 -23,-0.3 2,-0.3 -0.866 30.7-137.8-141.7 100.3 -23.7 51.7 39.9 + 589 387 B Y E - n 0 567F 12 -2,-0.3 -54,-1.4 -56,-0.2 2,-0.8 -0.461 15.3-138.7 -66.5 120.9 -22.8 48.0 40.4 + 590 388 B V E -mn 535 568F 20 -23,-3.5 -21,-1.7 -2,-0.3 2,-0.3 -0.716 17.1-161.2 -86.6 107.6 -22.7 46.2 37.0 + 591 389 B A E -m 536 0F 0 -56,-2.3 -54,-0.8 -2,-0.8 3,-0.1 -0.659 18.0-140.9 -88.3 141.2 -24.3 42.7 37.2 + 592 390 B E S S- 0 0 98 -2,-0.3 -55,-0.8 1,-0.3 2,-0.3 0.973 78.3 -30.7 -62.2 -53.5 -23.5 40.1 34.5 + 593 391 B S > - 0 0 46 -57,-0.1 4,-4.1 1,-0.1 -1,-0.3 -0.959 53.1-110.1-158.1 168.1 -27.1 39.0 34.5 + 594 392 B F H > S+ 0 0 4 -2,-0.3 4,-1.9 2,-0.2 -1,-0.1 0.836 123.8 52.2 -73.2 -33.0 -30.2 38.6 36.7 + 595 393 B N H 4 S+ 0 0 84 2,-0.2 4,-0.4 1,-0.2 -1,-0.2 0.834 117.7 40.5 -67.2 -32.8 -29.7 34.8 36.5 + 596 394 B D H >> S+ 0 0 39 2,-0.2 3,-1.1 1,-0.1 4,-1.1 0.885 111.4 51.3 -82.1 -48.2 -26.2 35.6 37.6 + 597 395 B A H >X S+ 0 0 0 -4,-4.1 4,-2.2 1,-0.3 3,-0.6 0.902 102.2 68.2 -56.6 -37.2 -26.9 38.3 40.2 + 598 396 B K H 3X S+ 0 0 27 -4,-1.9 4,-2.7 1,-0.3 -1,-0.3 0.829 97.3 50.2 -48.9 -40.8 -29.3 35.7 41.5 + 599 397 B E H <> S+ 0 0 90 -3,-1.1 4,-1.8 -4,-0.4 -1,-0.3 0.817 110.0 46.3 -73.3 -33.9 -26.4 33.5 42.6 + 600 398 B K H > -J 622 0E 32 5,-2.3 4,-1.3 -2,-0.4 5,-1.0 -0.884 4.5-168.2-108.6 101.1 -45.2 26.4 47.9 + 618 416 B P T 45S+ 0 0 84 0, 0.0 -1,-0.1 0, 0.0 5,-0.0 0.660 85.4 55.6 -61.3 -18.3 -46.9 27.9 44.9 + 619 417 B Y T 45S+ 0 0 217 1,-0.1 -2,-0.0 3,-0.1 0, 0.0 0.914 121.6 24.8 -81.8 -46.8 -49.8 25.3 45.1 + 620 418 B T T 45S- 0 0 68 -3,-0.2 -1,-0.1 2,-0.1 3,-0.1 0.408 97.9-138.0 -95.2 -0.6 -50.8 26.0 48.7 + 621 419 B Q T <5 + 0 0 55 -4,-1.3 -282,-1.4 1,-0.2 2,-0.2 0.848 61.3 129.6 41.9 42.5 -49.4 29.6 48.4 + 622 420 B R E < -IJ 338 617E 143 -5,-1.0 -5,-2.3 -284,-0.2 2,-0.6 -0.696 64.5-116.1-115.0 167.6 -48.0 29.0 51.9 + 623 421 B I E - J 0 616E 5 -286,-2.0 2,-0.5 -2,-0.2 -7,-0.2 -0.955 29.5-144.9-110.6 119.3 -44.5 29.6 53.2 + 624 422 B E E - J 0 615E 42 -9,-3.7 -9,-3.0 -2,-0.6 2,-0.7 -0.750 1.1-148.7 -91.7 122.8 -42.9 26.3 54.4 + 625 423 B V E - J 0 614E 16 -2,-0.5 2,-1.0 -11,-0.2 3,-0.5 -0.788 11.2-151.0 -89.8 114.4 -40.5 26.4 57.4 + 626 424 B L E + J 0 613E 21 -13,-3.2 -13,-1.2 -2,-0.7 3,-0.1 -0.771 57.9 110.2 -90.8 102.4 -37.9 23.7 56.9 + 627 425 B D + 0 0 120 -2,-1.0 2,-0.2 -15,-0.1 -1,-0.2 0.405 58.8 77.7-141.8 -24.6 -36.9 22.6 60.4 + 628 426 B N S > S- 0 0 85 -3,-0.5 4,-0.9 1,-0.1 3,-0.3 -0.628 78.9-125.1 -95.2 154.4 -38.4 19.1 60.6 + 629 427 B T H > S+ 0 0 63 1,-0.2 4,-0.6 -2,-0.2 -1,-0.1 0.736 113.6 50.7 -67.7 -23.8 -37.0 15.9 59.1 + 630 428 B Q H > S+ 0 0 94 2,-0.2 4,-1.2 1,-0.2 -1,-0.2 0.715 98.7 66.1 -85.2 -21.7 -40.3 15.2 57.4 + 631 429 B Q H > S+ 0 0 37 -3,-0.3 4,-0.9 1,-0.2 -2,-0.2 0.828 104.9 45.1 -65.4 -31.7 -40.3 18.7 56.0 + 632 430 B L H X S+ 0 0 71 -4,-0.9 4,-2.4 2,-0.2 -1,-0.2 0.729 99.0 69.4 -83.9 -24.8 -37.2 17.8 53.9 + 633 431 B K H X S+ 0 0 21 -4,-0.6 4,-1.4 1,-0.2 -2,-0.2 0.895 106.1 41.8 -58.7 -40.0 -38.7 14.4 52.8 + 634 432 B I H X S+ 0 0 70 -4,-1.2 4,-2.1 2,-0.2 -1,-0.2 0.808 111.2 51.1 -79.4 -35.1 -41.2 16.4 50.7 + 635 433 B L H X S+ 0 0 47 -4,-0.9 4,-2.5 2,-0.2 5,-0.2 0.918 110.1 53.7 -67.9 -39.8 -38.8 19.0 49.3 + 636 434 B A H X S+ 0 0 4 -4,-2.4 4,-3.2 1,-0.2 -2,-0.2 0.926 108.4 49.5 -56.3 -46.6 -36.6 16.1 48.3 + 637 435 B D H X S+ 0 0 80 -4,-1.4 4,-2.1 2,-0.2 -1,-0.2 0.886 107.1 54.7 -60.9 -41.3 -39.6 14.6 46.5 + 638 436 B S H X S+ 0 0 51 -4,-2.1 4,-1.8 2,-0.2 -2,-0.2 0.958 114.6 40.1 -58.0 -51.6 -40.3 17.8 44.7 + 639 437 B I H X S+ 0 0 71 -4,-2.5 4,-2.5 1,-0.2 5,-0.4 0.968 109.2 59.5 -61.7 -54.9 -36.8 18.0 43.4 + 640 438 B N H X S+ 0 0 50 -4,-3.2 4,-1.8 1,-0.3 -1,-0.2 0.851 110.7 42.3 -41.1 -48.0 -36.5 14.2 42.6 + 641 439 B S H X S+ 0 0 69 -4,-2.1 4,-1.0 1,-0.2 -1,-0.3 0.874 111.9 54.5 -70.5 -38.7 -39.5 14.4 40.3 + 642 440 B E H X S+ 0 0 137 -4,-1.8 4,-2.0 -3,-0.3 -2,-0.2 0.848 110.7 44.7 -65.6 -36.3 -38.4 17.7 38.7 + 643 441 B I H X S+ 0 0 16 -4,-2.5 4,-3.4 2,-0.2 5,-0.2 0.912 104.3 63.2 -72.8 -42.0 -34.9 16.3 37.7 + 644 442 B G H X S+ 0 0 20 -4,-1.8 4,-1.8 -5,-0.4 -1,-0.2 0.812 108.2 44.4 -50.0 -29.6 -36.6 13.2 36.5 + 645 443 B I H X S+ 0 0 113 -4,-1.0 4,-2.8 2,-0.2 -1,-0.3 0.929 110.3 52.7 -78.1 -49.6 -38.2 15.5 34.0 + 646 444 B L H X S+ 0 0 97 -4,-2.0 4,-1.9 1,-0.2 -2,-0.2 0.811 113.6 45.9 -54.2 -34.9 -34.9 17.3 33.3 + 647 445 B C H X S+ 0 0 7 -4,-3.4 4,-3.8 2,-0.2 5,-0.3 0.970 111.1 48.1 -73.6 -58.9 -33.3 13.9 32.6 + 648 446 B S H X S+ 0 0 63 -4,-1.8 4,-0.9 -5,-0.2 -2,-0.2 0.881 115.0 48.9 -49.1 -43.0 -36.0 12.5 30.4 + 649 447 B A H >< S+ 0 0 57 -4,-2.8 3,-1.5 2,-0.2 -1,-0.2 0.978 113.5 44.9 -60.9 -57.2 -36.0 15.8 28.5 + 650 448 B L H >< S+ 0 0 31 -4,-1.9 3,-2.2 1,-0.3 -2,-0.2 0.881 106.9 60.1 -54.3 -43.2 -32.2 15.7 28.2 + 651 449 B Q H 3< S+ 0 0 70 -4,-3.8 -1,-0.3 1,-0.3 -2,-0.2 0.754 104.1 52.4 -58.4 -24.2 -32.2 12.1 27.2 + 652 450 B K T << S+ 0 0 165 -3,-1.5 2,-0.3 -4,-0.9 -1,-0.3 0.315 91.2 80.9 -96.2 8.9 -34.4 13.0 24.2 + 653 451 B I < 0 0 107 -3,-2.2 -1,-0.2 1,-0.1 -344,-0.1 -0.453 360.0 360.0-114.6 60.9 -32.0 15.7 23.0 + 654 452 B K 0 0 219 -2,-0.3 -1,-0.1 -3,-0.2 -2,-0.1 0.919 360.0 360.0 -92.6 360.0 -29.3 13.9 21.0 diff --git a/tests/testdata/dssp/2pah_bio.dssp b/tests/testdata/dssp/2pah_bio.dssp new file mode 100644 index 0000000..3554642 --- /dev/null +++ b/tests/testdata/dssp/2pah_bio.dssp @@ -0,0 +1,1337 @@ +==== Secondary Structure Definition by the program DSSP, CMBI version by M.L. Hekkelman/2010-10-21 ==== DATE=2017-03-23 . +REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . +HEADER 2PAH . +COMPND PROTEIN (PHENYLALANINE HYDROXYLASE) . +SOURCE Homo sapiens . +AUTHOR . + 1302 8 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . + 56276.2 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . + 896 68.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . + 52 4.0 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . + 60 4.6 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . + 4 0.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES . + 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . + 8 0.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-3), SAME NUMBER PER 100 RESIDUES . + 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-2), SAME NUMBER PER 100 RESIDUES . + 2 0.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-1), SAME NUMBER PER 100 RESIDUES . + 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+0), SAME NUMBER PER 100 RESIDUES . + 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+1), SAME NUMBER PER 100 RESIDUES . + 68 5.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . + 156 12.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . + 506 38.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . + 32 2.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+5), SAME NUMBER PER 100 RESIDUES . + 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 *** HISTOGRAMS OF *** . + 0 0 4 8 0 4 0 4 0 0 8 0 6 6 0 4 0 0 0 0 4 0 2 0 2 0 0 0 0 0 RESIDUES PER ALPHA HELIX . + 4 8 0 4 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 PARALLEL BRIDGES PER LADDER . + 8 0 0 4 4 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 ANTIPARALLEL BRIDGES PER LADDER . + 4 4 0 4 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 LADDERS PER SHEET . + # RESIDUE AA STRUCTURE BP1 BP2 ACC N-H-->O O-->H-N N-H-->O O-->H-N TCO KAPPA ALPHA PHI PSI X-CA Y-CA Z-CA + 1 118 A V 0 0 127 0, 0.0 190,-0.1 0, 0.0 285,-0.0 0.000 360.0 360.0 360.0 124.7 -7.1 21.7 20.2 + 2 119 A P - 0 0 42 0, 0.0 2,-0.3 0, 0.0 0, 0.0 -0.071 360.0-105.4 -51.6 149.9 -3.8 21.2 22.2 + 3 120 A W - 0 0 120 186,-0.0 187,-0.2 187,-0.0 0, 0.0 -0.593 41.9-178.8 -81.0 139.2 -2.6 17.7 22.8 + 4 121 A F - 0 0 17 -2,-0.3 2,-0.2 185,-0.1 127,-0.1 -0.980 33.0 -92.9-138.9 150.9 -3.1 16.3 26.3 + 5 122 A P - 0 0 4 0, 0.0 3,-0.1 0, 0.0 6,-0.1 -0.405 27.9-176.6 -65.3 130.9 -2.2 13.0 28.1 + 6 123 A R S S+ 0 0 121 -2,-0.2 293,-3.9 1,-0.1 2,-0.3 0.766 72.8 42.2 -94.3 -34.0 -5.0 10.4 28.1 + 7 124 A T B > S-A 298 0A 23 291,-0.2 3,-1.0 1,-0.1 291,-0.2 -0.796 81.4-122.8-114.6 157.2 -3.1 7.9 30.2 + 8 125 A I G > S+ 0 0 2 289,-1.5 3,-0.9 -2,-0.3 290,-0.1 0.785 114.7 55.4 -65.5 -30.0 -0.8 8.3 33.3 + 9 126 A Q G > S+ 0 0 87 288,-0.3 3,-1.2 1,-0.2 -1,-0.3 0.594 89.5 77.1 -79.3 -11.7 2.0 6.7 31.4 + 10 127 A E G X S+ 0 0 55 -3,-1.0 3,-1.1 1,-0.3 -1,-0.2 0.490 71.6 81.8 -76.5 -3.3 1.6 9.2 28.6 + 11 128 A L G X> + 0 0 0 -3,-0.9 3,-1.3 1,-0.3 4,-0.8 0.472 66.9 88.0 -78.6 -2.0 3.4 11.8 30.8 + 12 129 A D G <4 S+ 0 0 36 -3,-1.2 -1,-0.3 1,-0.3 -2,-0.1 0.536 77.0 66.8 -71.6 -7.5 6.6 10.1 29.5 + 13 130 A R G X4 S+ 0 0 146 -3,-1.1 3,-0.8 1,-0.1 -1,-0.3 0.687 90.0 61.7 -85.5 -22.6 6.4 12.6 26.7 + 14 131 A F T <4 S+ 0 0 38 -3,-1.3 2,-0.4 1,-0.3 3,-0.2 0.916 113.4 34.7 -68.7 -44.7 7.0 15.5 29.1 + 15 132 A A T 3< S+ 0 0 4 -4,-0.8 -1,-0.3 1,-0.2 -2,-0.1 -0.484 79.4 141.0-107.2 57.7 10.5 14.1 30.0 + 16 133 A N < - 0 0 49 -3,-0.8 -1,-0.2 -2,-0.4 3,-0.1 0.994 58.7-129.6 -60.0 -65.6 11.2 12.7 26.5 + 17 134 A Q S S+ 0 0 93 1,-1.2 -1,-0.1 -3,-0.2 2,-0.1 -0.524 89.4 61.4 141.1 -54.7 14.9 13.6 26.4 + 18 135 A I 0 0 121 1,-0.2 -1,-1.2 26,-0.1 -2,-0.2 -0.370 360.0 360.0 -86.4 172.3 14.7 15.2 23.0 + 19 136 A L 0 0 187 -3,-0.1 -1,-0.2 -2,-0.1 -3,-0.1 0.893 360.0 360.0 74.5 360.0 12.4 18.3 22.5 + 20 ! 0 0 0 0, 0.0 0, 0.0 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 360.0 0.0 0.0 0.0 + 21 143 A D > 0 0 153 3,-0.1 3,-4.4 2,-0.1 6,-0.1 0.000 360.0 360.0 360.0 100.9 21.8 31.8 32.4 + 22 144 A A T 3 + 0 0 66 1,-0.3 5,-0.3 5,-0.1 6,-0.2 0.628 360.0 63.8 -21.6 -47.3 24.8 33.7 33.8 + 23 145 A D T 3 S+ 0 0 111 2,-0.1 -1,-0.3 4,-0.1 -2,-0.1 0.689 82.0 104.5 -60.7 -16.3 22.8 35.4 36.5 + 24 146 A H S X S- 0 0 27 -3,-4.4 3,-1.9 1,-0.1 2,-0.3 -0.516 82.7-117.8 -71.0 123.7 22.2 32.0 38.0 + 25 147 A P T 3 S+ 0 0 27 0, 0.0 124,-0.3 0, 0.0 -1,-0.1 -0.460 102.3 27.8 -65.0 121.5 24.4 31.3 41.0 + 26 148 A G T > S+ 0 0 14 -2,-0.3 3,-0.8 -4,-0.1 7,-0.2 0.449 79.6 122.6 105.7 3.2 26.7 28.4 40.2 + 27 149 A F T < S+ 0 0 74 -3,-1.9 -5,-0.1 -5,-0.3 -6,-0.1 0.822 78.9 48.0 -64.5 -31.3 26.8 29.1 36.5 + 28 150 A K T 3 S+ 0 0 188 -4,-0.2 -1,-0.3 -6,-0.2 -6,-0.0 0.518 89.5 100.4 -87.2 -6.4 30.5 29.4 36.8 + 29 151 A D <> - 0 0 48 -3,-0.8 4,-2.0 1,-0.2 5,-0.2 -0.719 53.8-167.9 -87.1 107.0 30.8 26.1 38.8 + 30 152 A P H > S+ 0 0 102 0, 0.0 4,-1.8 0, 0.0 -1,-0.2 0.783 86.4 46.0 -62.1 -30.3 31.9 23.3 36.5 + 31 153 A V H > S+ 0 0 93 2,-0.2 4,-2.4 3,-0.1 5,-0.2 0.984 114.1 42.1 -75.8 -69.7 31.0 20.7 39.1 + 32 154 A Y H > S+ 0 0 20 1,-0.2 4,-2.7 2,-0.2 5,-0.2 0.843 115.4 57.0 -44.4 -38.3 27.6 21.8 40.3 + 33 155 A R H X S+ 0 0 135 -4,-2.0 4,-1.0 1,-0.2 3,-0.3 0.986 110.9 38.0 -57.5 -63.8 26.9 22.4 36.7 + 34 156 A A H X S+ 0 0 60 -4,-1.8 4,-0.6 1,-0.2 -1,-0.2 0.687 114.3 59.6 -62.6 -19.3 27.6 18.8 35.6 + 35 157 A R H >X S+ 0 0 25 -4,-2.4 4,-1.8 2,-0.2 3,-0.6 0.928 104.6 46.9 -73.9 -45.8 26.0 17.7 38.8 + 36 158 A R H 3X S+ 0 0 50 -4,-2.7 4,-1.5 -3,-0.3 -2,-0.2 0.655 110.6 53.2 -69.2 -17.2 22.7 19.4 37.8 + 37 159 A K H 3X S+ 0 0 141 -4,-1.0 4,-1.7 2,-0.2 -1,-0.3 0.673 104.6 57.0 -87.0 -21.8 23.0 17.8 34.4 + 38 160 A Q H X S+ 0 0 8 -4,-1.8 4,-1.5 2,-0.2 3,-0.5 0.949 111.1 52.2 -63.8 -50.4 20.1 15.0 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0, 0.0 3,-0.1 0, 0.0 6,-0.1 -0.392 28.0-176.3 -64.9 130.4 -54.3 21.6 27.4 + 992 123 B R S S+ 0 0 121 -2,-0.2 286,-2.0 1,-0.1 2,-0.3 0.776 72.9 42.4 -93.5 -34.5 -51.3 24.0 27.8 + 993 124 B T B > S-Y 1277 0M 25 284,-0.2 3,-1.0 1,-0.1 284,-0.2 -0.787 81.6-122.8-113.6 157.8 -53.1 26.3 30.1 + 994 125 B I G > S+ 0 0 0 282,-1.4 3,-1.0 -2,-0.3 33,-0.1 0.799 114.7 55.6 -65.9 -30.4 -55.4 25.7 33.1 + 995 126 B Q G > S+ 0 0 86 1,-0.2 3,-1.2 281,-0.2 -1,-0.3 0.601 89.4 77.1 -78.4 -12.2 -58.1 27.7 31.4 + 996 127 B E G X S+ 0 0 61 -3,-1.0 3,-0.8 1,-0.3 -1,-0.2 0.477 71.5 82.2 -76.4 -2.5 -57.9 25.5 28.3 + 997 128 B L G < + 0 0 18 -3,-1.0 -1,-0.3 1,-0.2 -2,-0.1 0.464 63.2 95.7 -79.3 -1.1 -59.9 22.8 30.2 + 998 129 B D G < 0 0 50 -3,-1.2 -1,-0.2 29,-0.0 -2,-0.1 0.443 360.0 360.0 -69.6 3.4 -62.9 24.8 29.1 + 999 130 B R < 0 0 215 -3,-0.8 -3,-0.0 0, 0.0 0, 0.0 -0.345 360.0 360.0 -91.5 360.0 -63.2 22.4 26.2 + 1000 ! 0 0 0 0, 0.0 0, 0.0 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 360.0 0.0 0.0 0.0 + 1001 144 B A 0 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389 B A E -c 1191 0N 1 -56,-2.3 -54,-0.8 -2,-0.8 3,-0.1 -0.660 18.0-140.9 -88.3 141.2 -49.2 -0.3 46.8 + 1247 390 B E S S- 0 0 100 -2,-0.3 -55,-0.8 1,-0.3 2,-0.3 0.973 78.3 -30.7 -62.2 -53.5 -46.5 0.3 49.5 + 1248 391 B S > - 0 0 47 -57,-0.1 4,-4.1 1,-0.1 -1,-0.3 -0.959 53.1-110.1-158.1 168.1 -47.3 4.0 49.5 + 1249 392 B F H > S+ 0 0 4 -2,-0.3 4,-1.9 2,-0.2 -1,-0.1 0.836 123.8 52.2 -73.2 -33.0 -48.5 6.9 47.3 + 1250 393 B N H 4 S+ 0 0 36 2,-0.2 4,-0.4 1,-0.2 -1,-0.2 0.835 117.7 40.5 -67.3 -32.7 -45.0 8.3 47.5 + 1251 394 B D H >> S+ 0 0 37 2,-0.2 3,-1.1 1,-0.1 4,-1.1 0.885 111.4 51.4 -82.2 -48.2 -43.9 4.8 46.4 + 1252 395 B A H >X S+ 0 0 0 -4,-4.1 4,-2.2 1,-0.3 3,-0.6 0.902 102.2 68.2 -56.6 -37.2 -46.6 4.1 43.8 + 1253 396 B K H 3X S+ 0 0 0 -4,-1.9 4,-2.7 1,-0.3 -1,-0.3 0.828 97.3 50.2 -48.9 -40.8 -45.6 7.5 42.5 + 1254 397 B E H <> S+ 0 0 63 -3,-1.1 4,-1.8 -4,-0.4 -1,-0.3 0.817 110.0 46.3 -73.4 -34.0 -42.2 6.1 41.4 + 1255 398 B K H > -Z 1277 0M 13 5,-2.3 4,-1.3 -2,-0.4 5,-1.0 -0.884 4.5-168.2-108.5 101.1 -45.4 25.9 36.1 + 1273 416 B P T 45S+ 0 0 28 0, 0.0 -1,-0.1 0, 0.0 5,-0.0 0.660 85.4 55.6 -61.3 -18.4 -47.6 26.7 39.1 + 1274 417 B Y T 45S+ 0 0 51 1,-0.1 -503,-0.1 3,-0.1 -504,-0.1 0.914 121.6 24.8 -81.8 -46.8 -46.8 30.4 38.9 + 1275 418 B T T 45S- 0 0 14 -3,-0.2 -1,-0.1 2,-0.1 -503,-0.1 0.407 97.9-138.0 -95.2 -0.6 -48.0 31.0 35.3 + 1276 419 B Q T <5 + 0 0 49 -4,-1.3 -282,-1.4 1,-0.2 2,-0.2 0.848 61.3 129.6 41.9 42.5 -50.3 28.0 35.6 + 1277 420 B R E < -YZ 9931272M 113 -5,-1.0 -5,-2.3 -284,-0.2 2,-0.6 -0.697 64.5-116.1-115.0 167.6 -49.1 27.0 32.1 + 1278 421 B I E - Z 01271M 4 -286,-2.0 2,-0.5 -2,-0.2 -7,-0.2 -0.955 29.5-144.9-110.6 119.3 -47.8 23.7 30.8 + 1279 422 B E E - Z 01270M 39 -9,-3.7 -9,-3.0 -2,-0.6 2,-0.7 -0.750 1.1-148.7 -91.7 122.8 -44.2 24.0 29.6 + 1280 423 B V E - Z 01269M 18 -2,-0.5 2,-1.0 -11,-0.2 3,-0.5 -0.788 11.2-151.0 -89.8 114.4 -43.1 21.9 26.6 + 1281 424 B L E + Z 01268M 5 -13,-3.2 -13,-1.2 -2,-0.7 3,-0.1 -0.771 57.9 110.2 -90.8 102.5 -39.5 21.0 27.1 + 1282 425 B D + 0 0 107 -2,-1.0 2,-0.2 -15,-0.1 -1,-0.2 0.406 58.8 77.7-141.8 -24.6 -38.0 20.7 23.6 + 1283 426 B N S > S- 0 0 85 -3,-0.5 4,-0.9 1,-0.1 3,-0.3 -0.628 78.9-125.0 -95.2 154.5 -35.7 23.7 23.4 + 1284 427 B T H > S+ 0 0 46 1,-0.2 4,-0.6 -2,-0.2 -1,-0.1 0.735 113.6 50.7 -67.8 -23.8 -32.3 24.1 24.9 + 1285 428 B Q H > S+ 0 0 91 2,-0.2 4,-1.2 1,-0.2 -1,-0.2 0.715 98.7 66.1 -85.2 -21.8 -33.3 27.3 26.6 + 1286 429 B Q H > S+ 0 0 39 -3,-0.3 4,-0.9 1,-0.2 -2,-0.2 0.828 104.9 45.1 -65.3 -31.6 -36.4 25.5 28.0 + 1287 430 B L H X S+ 0 0 7 -4,-0.9 4,-2.4 2,-0.2 -1,-0.2 0.729 99.0 69.4 -83.9 -24.8 -34.0 23.4 30.1 + 1288 431 B K H X S+ 0 0 21 -4,-0.6 4,-1.4 1,-0.2 -2,-0.2 0.895 106.1 41.8 -58.6 -40.0 -31.8 26.3 31.2 + 1289 432 B I H X S+ 0 0 18 -4,-1.2 4,-2.1 2,-0.2 -1,-0.2 0.808 111.2 51.1 -79.4 -35.0 -34.8 27.5 33.3 + 1290 433 B L H X S+ 0 0 0 -4,-0.9 4,-2.5 2,-0.2 5,-0.2 0.918 110.1 53.7 -67.9 -39.8 -35.9 24.1 34.7 + 1291 434 B A H X S+ 0 0 0 -4,-2.4 4,-3.2 1,-0.2 -2,-0.2 0.926 108.4 49.5 -56.2 -46.6 -32.3 23.6 35.7 + 1292 435 B D H X S+ 0 0 4 -4,-1.4 4,-2.1 2,-0.2 -1,-0.2 0.886 107.1 54.7 -60.9 -41.3 -32.4 27.0 37.5 + 1293 436 B S H X S+ 0 0 19 -4,-2.1 4,-1.8 2,-0.2 -2,-0.2 0.958 114.6 40.1 -57.9 -51.6 -35.6 26.0 39.3 + 1294 437 B I H X S+ 0 0 0 -4,-2.5 4,-2.5 1,-0.2 5,-0.4 0.968 109.2 59.5 -61.7 -54.9 -34.0 22.9 40.6 + 1295 438 B N H X S+ 0 0 16 -4,-3.2 4,-1.8 1,-0.3 -1,-0.2 0.851 110.7 42.3 -41.1 -48.0 -30.6 24.5 41.4 + 1296 439 B S H X S+ 0 0 15 -4,-2.1 4,-1.0 1,-0.2 -1,-0.3 0.874 111.8 54.5 -70.4 -38.7 -32.2 27.0 43.7 + 1297 440 B E H X S+ 0 0 35 -4,-1.8 4,-2.0 -3,-0.3 -2,-0.2 0.848 110.7 44.7 -65.6 -36.4 -34.5 24.4 45.3 + 1298 441 B I H X S+ 0 0 0 -4,-2.5 4,-3.4 2,-0.2 5,-0.2 0.912 104.3 63.2 -72.8 -42.0 -31.6 22.1 46.3 + 1299 442 B G H X S+ 0 0 5 -4,-1.8 4,-1.8 -5,-0.4 -1,-0.2 0.812 108.2 44.4 -49.9 -29.6 -29.7 25.1 47.5 + 1300 443 B I H X S+ 0 0 24 -4,-1.0 4,-2.8 2,-0.2 -1,-0.3 0.929 110.3 52.7 -78.1 -49.6 -32.5 25.3 50.0 + 1301 444 B L H X S+ 0 0 2 -4,-2.0 4,-1.9 1,-0.2 -2,-0.2 0.810 113.6 45.9 -54.2 -35.0 -32.4 21.5 50.7 + 1302 445 B C H X S+ 0 0 8 -4,-3.4 4,-3.8 2,-0.2 5,-0.3 0.970 111.1 48.1 -73.5 -58.9 -28.7 21.9 51.4 + 1303 446 B S H X S+ 0 0 31 -4,-1.8 4,-0.9 -5,-0.2 -2,-0.2 0.881 115.0 48.9 -49.1 -43.0 -28.8 24.9 53.6 + 1304 447 B A H >< S+ 0 0 7 -4,-2.8 3,-1.5 2,-0.2 -1,-0.2 0.978 113.5 44.9 -60.9 -57.1 -31.6 23.3 55.5 + 1305 448 B L H >< S+ 0 0 2 -4,-1.9 3,-2.2 1,-0.3 -2,-0.2 0.881 106.9 60.1 -54.4 -43.2 -29.7 20.0 55.8 + 1306 449 B Q H 3< S+ 0 0 70 -4,-3.8 -1,-0.3 1,-0.3 -2,-0.2 0.754 104.1 52.4 -58.4 -24.2 -26.6 21.9 56.8 + 1307 450 B K T << S+ 0 0 101 -3,-1.5 2,-0.3 -4,-0.9 -1,-0.3 0.315 91.2 80.9 -96.2 8.9 -28.5 23.2 59.8 + 1308 451 B I < 0 0 66 -3,-2.2 -1,-0.2 1,-0.1 -668,-0.1 -0.452 360.0 360.0-114.6 60.8 -29.6 19.9 61.0 + 1309 452 B K 0 0 221 -2,-0.3 -1,-0.1 -3,-0.2 -2,-0.1 0.919 360.0 360.0 -92.6 360.0 -26.7 18.5 63.0 diff --git a/tests/DSSP/2pm7.dssp b/tests/testdata/dssp/2pm7.dssp similarity index 100% rename from tests/DSSP/2pm7.dssp rename to tests/testdata/dssp/2pm7.dssp diff --git a/tests/DSSP/2w4o.dssp b/tests/testdata/dssp/2w4o.dssp similarity index 100% rename from tests/DSSP/2w4o.dssp rename to tests/testdata/dssp/2w4o.dssp diff --git a/tests/DSSP/3ehk.dssp b/tests/testdata/dssp/3ehk.dssp similarity index 100% rename from tests/DSSP/3ehk.dssp rename to tests/testdata/dssp/3ehk.dssp diff --git a/tests/DSSP/3fqd.dssp b/tests/testdata/dssp/3fqd.dssp similarity index 100% rename from tests/DSSP/3fqd.dssp rename to tests/testdata/dssp/3fqd.dssp diff --git a/tests/DSSP/3mg7.dssp b/tests/testdata/dssp/3mg7.dssp similarity index 100% rename from tests/DSSP/3mg7.dssp rename to tests/testdata/dssp/3mg7.dssp diff --git a/tests/DSSP/3mn5.dssp b/tests/testdata/dssp/3mn5.dssp similarity index 100% rename from tests/DSSP/3mn5.dssp rename to tests/testdata/dssp/3mn5.dssp diff --git a/tests/DSSP/4abo.dssp b/tests/testdata/dssp/4abo.dssp similarity index 100% rename from tests/DSSP/4abo.dssp rename to tests/testdata/dssp/4abo.dssp diff --git a/tests/DSSP/4ibw.dssp b/tests/testdata/dssp/4ibw.dssp similarity index 100% rename from tests/DSSP/4ibw.dssp rename to tests/testdata/dssp/4ibw.dssp diff --git a/tests/DSSP/4v9d.dssp b/tests/testdata/dssp/4v9d.dssp similarity index 100% rename from tests/DSSP/4v9d.dssp rename to tests/testdata/dssp/4v9d.dssp diff --git a/tests/DSSP/4why.dssp b/tests/testdata/dssp/4why.dssp similarity index 100% rename from tests/DSSP/4why.dssp rename to tests/testdata/dssp/4why.dssp diff --git a/tests/DSSP/empty.dssp b/tests/testdata/dssp/empty.dssp similarity index 100% rename from tests/DSSP/empty.dssp rename to tests/testdata/dssp/empty.dssp diff --git a/tests/CIF/2pah-assembly-1.cif b/tests/testdata/mmcif/2pah-assembly-1.cif similarity index 100% rename from tests/CIF/2pah-assembly-1.cif rename to tests/testdata/mmcif/2pah-assembly-1.cif diff --git a/tests/CIF/2pah.cif b/tests/testdata/mmcif/2pah.cif similarity index 100% rename from tests/CIF/2pah.cif rename to tests/testdata/mmcif/2pah.cif diff --git a/tests/testdata/mmcif/2pah_bio.cif b/tests/testdata/mmcif/2pah_bio.cif new file mode 100644 index 0000000..bcffa5c --- /dev/null +++ b/tests/testdata/mmcif/2pah_bio.cif @@ -0,0 +1,11664 @@ +data_2PAH-assembly-1 +# +_entry.id 2PAH +# +# +_cell.entry_id 2PAH +_cell.length_a 125.434658325 +_cell.length_b 122.320173977 +_cell.length_c 66.929 +_cell.angle_alpha 90.00 +_cell.angle_beta 90.00 +_cell.angle_gamma 90.00 +_cell.Z_PDB 1 +_cell.pdbx_unique_axis ? +# +_pdbe_orig_cell.entry_id 2PAH +_pdbe_orig_cell.length_a 119.500 +_pdbe_orig_cell.length_b 119.500 +_pdbe_orig_cell.length_c 126.000 +_pdbe_orig_cell.angle_alpha 90.00 +_pdbe_orig_cell.angle_beta 90.00 +_pdbe_orig_cell.angle_gamma 120.00 +_pdbe_orig_cell.Z_PDB 12 +_pdbe_orig_cell.pdbx_unique_axis ? +# +_symmetry.entry_id 2PAH +_symmetry.space_group_name_H-M "P 1" +_symmetry.pdbx_full_space_group_name_H-M ? +_symmetry.cell_setting ? +_symmetry.Int_Tables_number ? +# +_pdbe_orig_symmetry.entry_id 2PAH +_pdbe_orig_symmetry.space_group_name_H-M "P 31 1 2" +_pdbe_orig_symmetry.pdbx_full_space_group_name_H-M ? +_pdbe_orig_symmetry.cell_setting ? +_pdbe_orig_symmetry.Int_Tables_number ? +# +loop_ +_entity_name_com.entity_id +_entity_name_com.name +1 PAH +2 ? +# +# +_entity_src_gen.entity_id 1 +_entity_src_gen.gene_src_common_name human +_entity_src_gen.gene_src_genus Homo +_entity_src_gen.pdbx_gene_src_gene ? +_entity_src_gen.gene_src_species ? +_entity_src_gen.gene_src_strain ? +_entity_src_gen.gene_src_tissue ? +_entity_src_gen.gene_src_tissue_fraction ? +_entity_src_gen.gene_src_details ? +_entity_src_gen.pdbx_gene_src_fragment ? +_entity_src_gen.pdbx_gene_src_scientific_name "Homo sapiens" +_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 +_entity_src_gen.pdbx_gene_src_variant ? +_entity_src_gen.pdbx_gene_src_cell_line ? +_entity_src_gen.pdbx_gene_src_atcc ? +_entity_src_gen.pdbx_gene_src_organ ? +_entity_src_gen.pdbx_gene_src_organelle ? +_entity_src_gen.pdbx_gene_src_cell ? +_entity_src_gen.pdbx_gene_src_cellular_location ? +_entity_src_gen.host_org_common_name ? +_entity_src_gen.pdbx_host_org_scientific_name "Escherichia coli BL21" +_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 511693 +_entity_src_gen.host_org_genus Escherichia +_entity_src_gen.pdbx_host_org_gene ? +_entity_src_gen.pdbx_host_org_organ ? +_entity_src_gen.host_org_species "Escherichia coli" +_entity_src_gen.pdbx_host_org_tissue ? +_entity_src_gen.pdbx_host_org_tissue_fraction ? +_entity_src_gen.pdbx_host_org_strain BL21 +_entity_src_gen.pdbx_host_org_variant ? +_entity_src_gen.pdbx_host_org_cell_line ? +_entity_src_gen.pdbx_host_org_atcc ? +_entity_src_gen.pdbx_host_org_culture_collection ? +_entity_src_gen.pdbx_host_org_cell ? +_entity_src_gen.pdbx_host_org_organelle ? +_entity_src_gen.pdbx_host_org_cellular_location ? +_entity_src_gen.pdbx_host_org_vector_type ? +_entity_src_gen.pdbx_host_org_vector ? +_entity_src_gen.plasmid_name PET-3A-D +_entity_src_gen.plasmid_details ? +_entity_src_gen.pdbx_description ? +# +_exptl.entry_id 2PAH +_exptl.method "X-ray diffraction" +_exptl.crystals_number 1 +# +_reflns.entry_id 2PAH +_reflns.observed_criterion_sigma_I 0.0 +_reflns.observed_criterion_sigma_F ? +_reflns.d_resolution_low 20.0 +_reflns.d_resolution_high 3.1 +_reflns.number_obs 120922 +_reflns.number_all ? +_reflns.percent_possible_obs 99.0 +_reflns.pdbx_Rmerge_I_obs 0.075 +_reflns.pdbx_Rsym_value 0.075 +_reflns.pdbx_netI_over_sigmaI 10.0 +_reflns.B_iso_Wilson_estimate 33.0 +_reflns.pdbx_redundancy 6.5 +_reflns.R_free_details ? +_reflns.pdbx_ordinal 1 +_reflns.pdbx_diffrn_id 1 +# +_refine.entry_id 2PAH +_refine.ls_number_reflns_obs 18446 +_refine.ls_number_reflns_all ? +_refine.pdbx_ls_sigma_I ? +_refine.pdbx_ls_sigma_F 0.0 +_refine.pdbx_data_cutoff_high_absF 100000000.0 +_refine.pdbx_data_cutoff_low_absF 0.001 +_refine.pdbx_data_cutoff_high_rms_absF ? +_refine.ls_d_res_low 20.0 +_refine.ls_d_res_high 3.1 +_refine.ls_percent_reflns_obs 99.9 +_refine.ls_R_factor_obs 0.2510000 +_refine.ls_R_factor_all ? +_refine.ls_R_factor_R_work 0.2510000 +_refine.ls_R_factor_R_free 0.3260000 +_refine.ls_R_factor_R_free_error ? +_refine.ls_R_factor_R_free_error_details ? +_refine.ls_percent_reflns_R_free 10.0 +_refine.ls_number_reflns_R_free 1800 +_refine.ls_number_parameters ? +_refine.ls_number_restraints ? +_refine.occupancy_min ? +_refine.occupancy_max ? +_refine.B_iso_mean 33.0 +_refine.aniso_B[1][1] 0.0 +_refine.aniso_B[2][2] 0.0 +_refine.aniso_B[3][3] 0.0 +_refine.aniso_B[1][2] 0.0 +_refine.aniso_B[1][3] 0.0 +_refine.aniso_B[2][3] 0.0 +_refine.solvent_model_details ? +_refine.solvent_model_param_ksol ? +_refine.solvent_model_param_bsol ? +_refine.pdbx_ls_cross_valid_method THROUGHOUT +_refine.details ? +_refine.pdbx_starting_model 1TOH +_refine.pdbx_method_to_determine_struct "MOLECULAR REPLACEMENT" +_refine.pdbx_isotropic_thermal_model ? +_refine.pdbx_stereochemistry_target_values ? +_refine.pdbx_stereochem_target_val_spec_case ? +_refine.pdbx_R_Free_selection_details RANDOM +_refine.pdbx_overall_ESU_R ? +_refine.pdbx_overall_ESU_R_Free ? +_refine.overall_SU_ML ? +_refine.overall_SU_B ? +_refine.ls_redundancy_reflns_obs ? +_refine.pdbx_refine_id "X-ray diffraction" +_refine.pdbx_diffrn_id 1 +# +_refine_hist.pdbx_refine_id "X-ray diffraction" +_refine_hist.cycle_id LAST +_refine_hist.pdbx_number_atoms_protein 5315 +_refine_hist.pdbx_number_atoms_nucleic_acid 0 +_refine_hist.pdbx_number_atoms_ligand 2 +_refine_hist.number_atoms_solvent 0 +_refine_hist.number_atoms_total 5317 +_refine_hist.d_res_high 3.1 +_refine_hist.d_res_low 20.0 +# +# +_pdbx_struct_assembly.id 1 +_pdbx_struct_assembly.details author_and_software_defined_assembly +_pdbx_struct_assembly.method_details PISA,PQS +_pdbx_struct_assembly.oligomeric_details tetrameric +_pdbx_struct_assembly.oligomeric_count 4 +# +_pdbx_struct_assembly_gen.assembly_id 1 +_pdbx_struct_assembly_gen.oper_expression 1,2 +_pdbx_struct_assembly_gen.asym_id_list A,C,B,D +# +loop_ +_pdbx_struct_oper_list.id +_pdbx_struct_oper_list.type +_pdbx_struct_oper_list.name +_pdbx_struct_oper_list.symmetry_operation +_pdbx_struct_oper_list.matrix[1][1] +_pdbx_struct_oper_list.matrix[1][2] +_pdbx_struct_oper_list.matrix[1][3] +_pdbx_struct_oper_list.vector[1] +_pdbx_struct_oper_list.matrix[2][1] +_pdbx_struct_oper_list.matrix[2][2] +_pdbx_struct_oper_list.matrix[2][3] +_pdbx_struct_oper_list.vector[2] +_pdbx_struct_oper_list.matrix[3][1] +_pdbx_struct_oper_list.matrix[3][2] +_pdbx_struct_oper_list.matrix[3][3] +_pdbx_struct_oper_list.vector[3] +1 "identity operation" 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 +2 "crystal symmetry operation" 4_555 -y,-x,-z+2/3 0.5000000000 -0.8660254038 0.0000000000 0.0000000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 84.0000000000 +# +loop_ +_struct_asym.id +_struct_asym.pdbx_blank_PDB_chainid_flag +_struct_asym.pdbx_modified +_struct_asym.entity_id +_struct_asym.details +A N N 1 ? +B N N 1 ? +C N N 2 ? +D N N 2 ? +# +_struct.entry_id 2PAH +_struct.title "TETRAMERIC HUMAN PHENYLALANINE HYDROXYLASE" +_struct.pdbx_descriptor "PROTEIN (PHENYLALANINE HYDROXYLASE) (1.14.16.1)" +_struct.pdbx_model_details ? +_struct.pdbx_CASP_flag ? +_struct.pdbx_model_type_details ? +# +_atom_sites.entry_id 2PAH +_atom_sites.Cartn_transform_axes ? +_atom_sites.fract_transf_matrix[1][1] 1.000000 +_atom_sites.fract_transf_matrix[1][2] 0.000000 +_atom_sites.fract_transf_matrix[1][3] 0.000000 +_atom_sites.fract_transf_matrix[2][1] 0.000000 +_atom_sites.fract_transf_matrix[2][2] 1.000000 +_atom_sites.fract_transf_matrix[2][3] 0.000000 +_atom_sites.fract_transf_matrix[3][1] 0.000000 +_atom_sites.fract_transf_matrix[3][2] 0.000000 +_atom_sites.fract_transf_matrix[3][3] 1.000000 +_atom_sites.fract_transf_vector[1] 0.00000 +_atom_sites.fract_transf_vector[2] 0.00000 +_atom_sites.fract_transf_vector[3] 0.00000 +# +loop_ +_pdbe_orig_poly_seq_scheme.asym_id +_pdbe_orig_poly_seq_scheme.entity_id +_pdbe_orig_poly_seq_scheme.seq_id +_pdbe_orig_poly_seq_scheme.mon_id +_pdbe_orig_poly_seq_scheme.ndb_seq_num +_pdbe_orig_poly_seq_scheme.pdb_seq_num +_pdbe_orig_poly_seq_scheme.auth_seq_num +_pdbe_orig_poly_seq_scheme.pdb_mon_id +_pdbe_orig_poly_seq_scheme.auth_mon_id +_pdbe_orig_poly_seq_scheme.pdb_strand_id +_pdbe_orig_poly_seq_scheme.pdb_ins_code +_pdbe_orig_poly_seq_scheme.hetero +A 1 1 VAL 1 118 118 VAL VAL A . n +A 1 2 PRO 2 119 119 PRO PRO A . n +A 1 3 TRP 3 120 120 TRP TRP A . n +A 1 4 PHE 4 121 121 PHE PHE A . n +A 1 5 PRO 5 122 122 PRO PRO A . n +A 1 6 ARG 6 123 123 ARG ARG A . n +A 1 7 THR 7 124 124 THR THR A . n +A 1 8 ILE 8 125 125 ILE ILE A . n +A 1 9 GLN 9 126 126 GLN GLN A . n +A 1 10 GLU 10 127 127 GLU GLU A . n +A 1 11 LEU 11 128 128 LEU LEU A . n +A 1 12 ASP 12 129 129 ASP ASP A . n +A 1 13 ARG 13 130 130 ARG ARG A . n +A 1 14 PHE 14 131 131 PHE PHE A . n +A 1 15 ALA 15 132 132 ALA ALA A . n +A 1 16 ASN 16 133 133 ASN ASN A . n +A 1 17 GLN 17 134 134 GLN GLN A . n +A 1 18 ILE 18 135 135 ILE ILE A . n +A 1 19 LEU 19 136 136 LEU LEU A . n +A 1 20 SER 20 137 ? ? ? A . n +A 1 21 TYR 21 138 ? ? ? A . n +A 1 22 GLY 22 139 ? ? ? A . n +A 1 23 ALA 23 140 ? ? ? A . n +A 1 24 GLU 24 141 ? ? ? A . n +A 1 25 LEU 25 142 ? ? ? A . n +A 1 26 ASP 26 143 143 ASP ASP A . n +A 1 27 ALA 27 144 144 ALA ALA A . n +A 1 28 ASP 28 145 145 ASP ASP A . n +A 1 29 HIS 29 146 146 HIS HIS A . n +A 1 30 PRO 30 147 147 PRO PRO A . n +A 1 31 GLY 31 148 148 GLY GLY A . n +A 1 32 PHE 32 149 149 PHE PHE A . n +A 1 33 LYS 33 150 150 LYS LYS A . n +A 1 34 ASP 34 151 151 ASP ASP A . n +A 1 35 PRO 35 152 152 PRO PRO A . n +A 1 36 VAL 36 153 153 VAL VAL A . n +A 1 37 TYR 37 154 154 TYR TYR A . n +A 1 38 ARG 38 155 155 ARG ARG A . n +A 1 39 ALA 39 156 156 ALA ALA A . n +A 1 40 ARG 40 157 157 ARG ARG A . n +A 1 41 ARG 41 158 158 ARG ARG A . n +A 1 42 LYS 42 159 159 LYS LYS A . n +A 1 43 GLN 43 160 160 GLN GLN A . n +A 1 44 PHE 44 161 161 PHE PHE A . n +A 1 45 ALA 45 162 162 ALA ALA A . n +A 1 46 ASP 46 163 163 ASP ASP A . n +A 1 47 ILE 47 164 164 ILE ILE A . n +A 1 48 ALA 48 165 165 ALA ALA A . n +A 1 49 TYR 49 166 166 TYR TYR A . n +A 1 50 ASN 50 167 167 ASN ASN A . n +A 1 51 TYR 51 168 168 TYR TYR A . n +A 1 52 ARG 52 169 169 ARG ARG A . n +A 1 53 HIS 53 170 170 HIS HIS A . n +A 1 54 GLY 54 171 171 GLY GLY A . n +A 1 55 GLN 55 172 172 GLN GLN A . n +A 1 56 PRO 56 173 173 PRO PRO A . n +A 1 57 ILE 57 174 174 ILE ILE A . n +A 1 58 PRO 58 175 175 PRO PRO A . n +A 1 59 ARG 59 176 176 ARG ARG A . n +A 1 60 VAL 60 177 177 VAL VAL A . n +A 1 61 GLU 61 178 178 GLU GLU A . n +A 1 62 TYR 62 179 179 TYR TYR A . n +A 1 63 MET 63 180 180 MET MET A . n +A 1 64 GLU 64 181 181 GLU GLU A . n +A 1 65 GLU 65 182 182 GLU GLU A . n +A 1 66 GLU 66 183 183 GLU GLU A . n +A 1 67 LYS 67 184 184 LYS LYS A . n +A 1 68 LYS 68 185 185 LYS LYS A . n +A 1 69 THR 69 186 186 THR THR A . n +A 1 70 TRP 70 187 187 TRP TRP A . n +A 1 71 GLY 71 188 188 GLY GLY A . n +A 1 72 THR 72 189 189 THR THR A . n +A 1 73 VAL 73 190 190 VAL VAL A . n +A 1 74 PHE 74 191 191 PHE PHE A . n +A 1 75 LYS 75 192 192 LYS LYS A . n +A 1 76 THR 76 193 193 THR THR A . n +A 1 77 LEU 77 194 194 LEU LEU A . n +A 1 78 LYS 78 195 195 LYS LYS A . n +A 1 79 SER 79 196 196 SER SER A . n +A 1 80 LEU 80 197 197 LEU LEU A . n +A 1 81 TYR 81 198 198 TYR TYR A . n +A 1 82 LYS 82 199 199 LYS LYS A . n +A 1 83 THR 83 200 200 THR THR A . n +A 1 84 HIS 84 201 201 HIS HIS A . n +A 1 85 ALA 85 202 202 ALA ALA A . n +A 1 86 CYS 86 203 203 CYS CYS A . n +A 1 87 TYR 87 204 204 TYR TYR A . n +A 1 88 GLU 88 205 205 GLU GLU A . n +A 1 89 TYR 89 206 206 TYR TYR A . n +A 1 90 ASN 90 207 207 ASN ASN A . n +A 1 91 HIS 91 208 208 HIS HIS A . n +A 1 92 ILE 92 209 209 ILE ILE A . n +A 1 93 PHE 93 210 210 PHE PHE A . n +A 1 94 PRO 94 211 211 PRO PRO A . n +A 1 95 LEU 95 212 212 LEU LEU A . n +A 1 96 LEU 96 213 213 LEU LEU A . n +A 1 97 GLU 97 214 214 GLU GLU A . n +A 1 98 LYS 98 215 215 LYS LYS A . n +A 1 99 TYR 99 216 216 TYR TYR A . n +A 1 100 CYS 100 217 217 CYS CYS A . n +A 1 101 GLY 101 218 218 GLY GLY A . n +A 1 102 PHE 102 219 219 PHE PHE A . n +A 1 103 HIS 103 220 220 HIS HIS A . n +A 1 104 GLU 104 221 221 GLU GLU A . n +A 1 105 ASP 105 222 222 ASP ASP A . n +A 1 106 ASN 106 223 223 ASN ASN A . n +A 1 107 ILE 107 224 224 ILE ILE A . n +A 1 108 PRO 108 225 225 PRO PRO A . n +A 1 109 GLN 109 226 226 GLN GLN A . n +A 1 110 LEU 110 227 227 LEU LEU A . n +A 1 111 GLU 111 228 228 GLU GLU A . n +A 1 112 ASP 112 229 229 ASP ASP A . n +A 1 113 VAL 113 230 230 VAL VAL A . n +A 1 114 SER 114 231 231 SER SER A . n +A 1 115 GLN 115 232 232 GLN GLN A . n +A 1 116 PHE 116 233 233 PHE PHE A . n +A 1 117 LEU 117 234 234 LEU LEU A . n +A 1 118 GLN 118 235 235 GLN GLN A . n +A 1 119 THR 119 236 236 THR THR A . n +A 1 120 CYS 120 237 237 CYS CYS A . n +A 1 121 THR 121 238 238 THR THR A . n +A 1 122 GLY 122 239 239 GLY GLY A . n +A 1 123 PHE 123 240 240 PHE PHE A . n +A 1 124 ARG 124 241 241 ARG ARG A . n +A 1 125 LEU 125 242 242 LEU LEU A . n +A 1 126 ARG 126 243 243 ARG ARG A . n +A 1 127 PRO 127 244 244 PRO PRO A . n +A 1 128 VAL 128 245 245 VAL VAL A . n +A 1 129 ALA 129 246 246 ALA ALA A . n +A 1 130 GLY 130 247 247 GLY GLY A . n +A 1 131 LEU 131 248 248 LEU LEU A . n +A 1 132 LEU 132 249 249 LEU LEU A . n +A 1 133 SER 133 250 250 SER SER A . n +A 1 134 SER 134 251 251 SER SER A . n +A 1 135 ARG 135 252 252 ARG ARG A . n +A 1 136 ASP 136 253 253 ASP ASP A . n +A 1 137 PHE 137 254 254 PHE PHE A . n +A 1 138 LEU 138 255 255 LEU LEU A . n +A 1 139 GLY 139 256 256 GLY GLY A . n +A 1 140 GLY 140 257 257 GLY GLY A . n +A 1 141 LEU 141 258 258 LEU LEU A . n +A 1 142 ALA 142 259 259 ALA ALA A . n +A 1 143 PHE 143 260 260 PHE PHE A . n +A 1 144 ARG 144 261 261 ARG ARG A . n +A 1 145 VAL 145 262 262 VAL VAL A . n +A 1 146 PHE 146 263 263 PHE PHE A . n +A 1 147 HIS 147 264 264 HIS HIS A . n +A 1 148 CYS 148 265 265 CYS CYS A . n +A 1 149 THR 149 266 266 THR THR A . n +A 1 150 GLN 150 267 267 GLN GLN A . n +A 1 151 TYR 151 268 268 TYR TYR A . n +A 1 152 ILE 152 269 269 ILE ILE A . n +A 1 153 ARG 153 270 270 ARG ARG A . n +A 1 154 HIS 154 271 271 HIS HIS A . n +A 1 155 GLY 155 272 272 GLY GLY A . n +A 1 156 SER 156 273 273 SER SER A . n +A 1 157 LYS 157 274 274 LYS LYS A . n +A 1 158 PRO 158 275 275 PRO PRO A . n +A 1 159 MET 159 276 276 MET MET A . n +A 1 160 TYR 160 277 277 TYR TYR A . n +A 1 161 THR 161 278 278 THR THR A . n +A 1 162 PRO 162 279 279 PRO PRO A . n +A 1 163 GLU 163 280 280 GLU GLU A . n +A 1 164 PRO 164 281 281 PRO PRO A . n +A 1 165 ASP 165 282 282 ASP ASP A . n +A 1 166 ILE 166 283 283 ILE ILE A . n +A 1 167 CYS 167 284 284 CYS CYS A . n +A 1 168 HIS 168 285 285 HIS HIS A . n +A 1 169 GLU 169 286 286 GLU GLU A . n +A 1 170 LEU 170 287 287 LEU LEU A . n +A 1 171 LEU 171 288 288 LEU LEU A . n +A 1 172 GLY 172 289 289 GLY GLY A . n +A 1 173 HIS 173 290 290 HIS HIS A . n +A 1 174 VAL 174 291 291 VAL VAL A . n +A 1 175 PRO 175 292 292 PRO PRO A . n +A 1 176 LEU 176 293 293 LEU LEU A . n +A 1 177 PHE 177 294 294 PHE PHE A . n +A 1 178 SER 178 295 295 SER SER A . n +A 1 179 ASP 179 296 296 ASP ASP A . n +A 1 180 ARG 180 297 297 ARG ARG A . n +A 1 181 SER 181 298 298 SER SER A . n +A 1 182 PHE 182 299 299 PHE PHE A . n +A 1 183 ALA 183 300 300 ALA ALA A . n +A 1 184 GLN 184 301 301 GLN GLN A . n +A 1 185 PHE 185 302 302 PHE PHE A . n +A 1 186 SER 186 303 303 SER SER A . n +A 1 187 GLN 187 304 304 GLN GLN A . n +A 1 188 GLU 188 305 305 GLU GLU A . n +A 1 189 ILE 189 306 306 ILE ILE A . n +A 1 190 GLY 190 307 307 GLY GLY A . n +A 1 191 LEU 191 308 308 LEU LEU A . n +A 1 192 ALA 192 309 309 ALA ALA A . n +A 1 193 SER 193 310 310 SER SER A . n +A 1 194 LEU 194 311 311 LEU LEU A . n +A 1 195 GLY 195 312 312 GLY GLY A . n +A 1 196 ALA 196 313 313 ALA ALA A . n +A 1 197 PRO 197 314 314 PRO PRO A . n +A 1 198 ASP 198 315 315 ASP ASP A . n +A 1 199 GLU 199 316 316 GLU GLU A . n +A 1 200 TYR 200 317 317 TYR TYR A . n +A 1 201 ILE 201 318 318 ILE ILE A . n +A 1 202 GLU 202 319 319 GLU GLU A . n +A 1 203 LYS 203 320 320 LYS LYS A . n +A 1 204 LEU 204 321 321 LEU LEU A . n +A 1 205 ALA 205 322 322 ALA ALA A . n +A 1 206 THR 206 323 323 THR THR A . n +A 1 207 ILE 207 324 324 ILE ILE A . n +A 1 208 TYR 208 325 325 TYR TYR A . n +A 1 209 TRP 209 326 326 TRP TRP A . n +A 1 210 PHE 210 327 327 PHE PHE A . n +A 1 211 THR 211 328 328 THR THR A . n +A 1 212 VAL 212 329 329 VAL VAL A . n +A 1 213 GLU 213 330 330 GLU GLU A . n +A 1 214 PHE 214 331 331 PHE PHE A . n +A 1 215 GLY 215 332 332 GLY GLY A . n +A 1 216 LEU 216 333 333 LEU LEU A . n +A 1 217 CYS 217 334 334 CYS CYS A . n +A 1 218 LYS 218 335 335 LYS LYS A . n +A 1 219 GLN 219 336 336 GLN GLN A . n +A 1 220 GLY 220 337 337 GLY GLY A . n +A 1 221 ASP 221 338 338 ASP ASP A . n +A 1 222 SER 222 339 339 SER SER A . n +A 1 223 ILE 223 340 340 ILE ILE A . n +A 1 224 LYS 224 341 341 LYS LYS A . n +A 1 225 ALA 225 342 342 ALA ALA A . n +A 1 226 TYR 226 343 343 TYR TYR A . n +A 1 227 GLY 227 344 344 GLY GLY A . n +A 1 228 ALA 228 345 345 ALA ALA A . n +A 1 229 GLY 229 346 346 GLY GLY A . n +A 1 230 LEU 230 347 347 LEU LEU A . n +A 1 231 LEU 231 348 348 LEU LEU A . n +A 1 232 SER 232 349 349 SER SER A . n +A 1 233 SER 233 350 350 SER SER A . n +A 1 234 PHE 234 351 351 PHE PHE A . n +A 1 235 GLY 235 352 352 GLY GLY A . n +A 1 236 GLU 236 353 353 GLU GLU A . n +A 1 237 LEU 237 354 354 LEU LEU A . n +A 1 238 GLN 238 355 355 GLN GLN A . n +A 1 239 TYR 239 356 356 TYR TYR A . n +A 1 240 CYS 240 357 357 CYS CYS A . n +A 1 241 LEU 241 358 358 LEU LEU A . n +A 1 242 SER 242 359 359 SER SER A . n +A 1 243 GLU 243 360 360 GLU GLU A . n +A 1 244 LYS 244 361 361 LYS LYS A . n +A 1 245 PRO 245 362 362 PRO PRO A . n +A 1 246 LYS 246 363 363 LYS LYS A . n +A 1 247 LEU 247 364 364 LEU LEU A . n +A 1 248 LEU 248 365 365 LEU LEU A . n +A 1 249 PRO 249 366 366 PRO PRO A . n +A 1 250 LEU 250 367 367 LEU LEU A . n +A 1 251 GLU 251 368 368 GLU GLU A . n +A 1 252 LEU 252 369 369 LEU LEU A . n +A 1 253 GLU 253 370 370 GLU GLU A . n +A 1 254 LYS 254 371 371 LYS LYS A . n +A 1 255 THR 255 372 372 THR THR A . n +A 1 256 ALA 256 373 373 ALA ALA A . n +A 1 257 ILE 257 374 374 ILE ILE A . n +A 1 258 GLN 258 375 375 GLN GLN A . n +A 1 259 ASN 259 376 376 ASN ASN A . n +A 1 260 TYR 260 377 377 TYR TYR A . n +A 1 261 THR 261 378 378 THR THR A . n +A 1 262 VAL 262 379 379 VAL VAL A . n +A 1 263 THR 263 380 380 THR THR A . n +A 1 264 GLU 264 381 381 GLU GLU A . n +A 1 265 PHE 265 382 382 PHE PHE A . n +A 1 266 GLN 266 383 383 GLN GLN A . n +A 1 267 PRO 267 384 384 PRO PRO A . n +A 1 268 LEU 268 385 385 LEU LEU A . n +A 1 269 TYR 269 386 386 TYR TYR A . n +A 1 270 TYR 270 387 387 TYR TYR A . n +A 1 271 VAL 271 388 388 VAL VAL A . n +A 1 272 ALA 272 389 389 ALA ALA A . n +A 1 273 GLU 273 390 390 GLU GLU A . n +A 1 274 SER 274 391 391 SER SER A . n +A 1 275 PHE 275 392 392 PHE PHE A . n +A 1 276 ASN 276 393 393 ASN ASN A . n +A 1 277 ASP 277 394 394 ASP ASP A . n +A 1 278 ALA 278 395 395 ALA ALA A . n +A 1 279 LYS 279 396 396 LYS LYS A . n +A 1 280 GLU 280 397 397 GLU GLU A . n +A 1 281 LYS 281 398 398 LYS LYS A . n +A 1 282 VAL 282 399 399 VAL VAL A . n +A 1 283 ARG 283 400 400 ARG ARG A . n +A 1 284 ASN 284 401 401 ASN ASN A . n +A 1 285 PHE 285 402 402 PHE PHE A . n +A 1 286 ALA 286 403 403 ALA ALA A . n +A 1 287 ALA 287 404 404 ALA ALA A . n +A 1 288 THR 288 405 405 THR THR A . n +A 1 289 ILE 289 406 406 ILE ILE A . n +A 1 290 PRO 290 407 407 PRO PRO A . n +A 1 291 ARG 291 408 408 ARG ARG A . n +A 1 292 PRO 292 409 409 PRO PRO A . n +A 1 293 PHE 293 410 410 PHE PHE A . n +A 1 294 SER 294 411 411 SER SER A . n +A 1 295 VAL 295 412 412 VAL VAL A . n +A 1 296 ARG 296 413 413 ARG ARG A . n +A 1 297 TYR 297 414 414 TYR TYR A . n +A 1 298 ASP 298 415 415 ASP ASP A . n +A 1 299 PRO 299 416 416 PRO PRO A . n +A 1 300 TYR 300 417 417 TYR TYR A . n +A 1 301 THR 301 418 418 THR THR A . n +A 1 302 GLN 302 419 419 GLN GLN A . n +A 1 303 ARG 303 420 420 ARG ARG A . n +A 1 304 ILE 304 421 421 ILE ILE A . n +A 1 305 GLU 305 422 422 GLU GLU A . n +A 1 306 VAL 306 423 423 VAL VAL A . n +A 1 307 LEU 307 424 424 LEU LEU A . n +A 1 308 ASP 308 425 425 ASP ASP A . n +A 1 309 ASN 309 426 426 ASN ASN A . n +A 1 310 THR 310 427 427 THR THR A . n +A 1 311 GLN 311 428 428 GLN GLN A . n +A 1 312 GLN 312 429 429 GLN GLN A . n +A 1 313 LEU 313 430 430 LEU LEU A . n +A 1 314 LYS 314 431 431 LYS LYS A . n +A 1 315 ILE 315 432 432 ILE ILE A . n +A 1 316 LEU 316 433 433 LEU LEU A . n +A 1 317 ALA 317 434 434 ALA ALA A . n +A 1 318 ASP 318 435 435 ASP ASP A . n +A 1 319 SER 319 436 436 SER SER A . n +A 1 320 ILE 320 437 437 ILE ILE A . n +A 1 321 ASN 321 438 438 ASN ASN A . n +A 1 322 SER 322 439 439 SER SER A . n +A 1 323 GLU 323 440 440 GLU GLU A . n +A 1 324 ILE 324 441 441 ILE ILE A . n +A 1 325 GLY 325 442 442 GLY GLY A . n +A 1 326 ILE 326 443 443 ILE ILE A . n +A 1 327 LEU 327 444 444 LEU LEU A . n +A 1 328 CYS 328 445 445 CYS CYS A . n +A 1 329 SER 329 446 446 SER SER A . n +A 1 330 ALA 330 447 447 ALA ALA A . n +A 1 331 LEU 331 448 448 LEU LEU A . n +A 1 332 GLN 332 449 449 GLN GLN A . n +A 1 333 LYS 333 450 450 LYS LYS A . n +A 1 334 ILE 334 451 451 ILE ILE A . n +A 1 335 LYS 335 452 452 LYS LYS A . n +B 1 1 VAL 1 118 118 VAL VAL B . n +B 1 2 PRO 2 119 119 PRO PRO B . n +B 1 3 TRP 3 120 120 TRP TRP B . n +B 1 4 PHE 4 121 121 PHE PHE B . n +B 1 5 PRO 5 122 122 PRO PRO B . n +B 1 6 ARG 6 123 123 ARG ARG B . n +B 1 7 THR 7 124 124 THR THR B . n +B 1 8 ILE 8 125 125 ILE ILE B . n +B 1 9 GLN 9 126 126 GLN GLN B . n +B 1 10 GLU 10 127 127 GLU GLU B . n +B 1 11 LEU 11 128 128 LEU LEU B . n +B 1 12 ASP 12 129 129 ASP ASP B . n +B 1 13 ARG 13 130 130 ARG ARG B . n +B 1 14 PHE 14 131 ? ? ? B . n +B 1 15 ALA 15 132 ? ? ? B . n +B 1 16 ASN 16 133 ? ? ? B . n +B 1 17 GLN 17 134 ? ? ? B . n +B 1 18 ILE 18 135 ? ? ? B . n +B 1 19 LEU 19 136 ? ? ? B . n +B 1 20 SER 20 137 ? ? ? B . n +B 1 21 TYR 21 138 ? ? ? B . n +B 1 22 GLY 22 139 ? ? ? B . n +B 1 23 ALA 23 140 ? ? ? B . n +B 1 24 GLU 24 141 ? ? ? B . n +B 1 25 LEU 25 142 ? ? ? B . n +B 1 26 ASP 26 143 ? ? ? B . n +B 1 27 ALA 27 144 144 ALA ALA B . n +B 1 28 ASP 28 145 145 ASP ASP B . n +B 1 29 HIS 29 146 146 HIS HIS B . n +B 1 30 PRO 30 147 147 PRO PRO B . n +B 1 31 GLY 31 148 148 GLY GLY B . n +B 1 32 PHE 32 149 149 PHE PHE B . n +B 1 33 LYS 33 150 150 LYS LYS B . n +B 1 34 ASP 34 151 151 ASP ASP B . n +B 1 35 PRO 35 152 152 PRO PRO B . n +B 1 36 VAL 36 153 153 VAL VAL B . n +B 1 37 TYR 37 154 154 TYR TYR B . n +B 1 38 ARG 38 155 155 ARG ARG B . n +B 1 39 ALA 39 156 156 ALA ALA B . n +B 1 40 ARG 40 157 157 ARG ARG B . n +B 1 41 ARG 41 158 158 ARG ARG B . n +B 1 42 LYS 42 159 159 LYS LYS B . n +B 1 43 GLN 43 160 160 GLN GLN B . n +B 1 44 PHE 44 161 161 PHE PHE B . n +B 1 45 ALA 45 162 162 ALA ALA B . n +B 1 46 ASP 46 163 163 ASP ASP B . n +B 1 47 ILE 47 164 164 ILE ILE B . n +B 1 48 ALA 48 165 165 ALA ALA B . n +B 1 49 TYR 49 166 166 TYR TYR B . n +B 1 50 ASN 50 167 167 ASN ASN B . n +B 1 51 TYR 51 168 168 TYR TYR B . n +B 1 52 ARG 52 169 169 ARG ARG B . n +B 1 53 HIS 53 170 170 HIS HIS B . n +B 1 54 GLY 54 171 171 GLY GLY B . n +B 1 55 GLN 55 172 172 GLN GLN B . n +B 1 56 PRO 56 173 173 PRO PRO B . n +B 1 57 ILE 57 174 174 ILE ILE B . n +B 1 58 PRO 58 175 175 PRO PRO B . n +B 1 59 ARG 59 176 176 ARG ARG B . n +B 1 60 VAL 60 177 177 VAL VAL B . n +B 1 61 GLU 61 178 178 GLU GLU B . n +B 1 62 TYR 62 179 179 TYR TYR B . n +B 1 63 MET 63 180 180 MET MET B . n +B 1 64 GLU 64 181 181 GLU GLU B . n +B 1 65 GLU 65 182 182 GLU GLU B . n +B 1 66 GLU 66 183 183 GLU GLU B . n +B 1 67 LYS 67 184 184 LYS LYS B . n +B 1 68 LYS 68 185 185 LYS LYS B . n +B 1 69 THR 69 186 186 THR THR B . n +B 1 70 TRP 70 187 187 TRP TRP B . n +B 1 71 GLY 71 188 188 GLY GLY B . n +B 1 72 THR 72 189 189 THR THR B . n +B 1 73 VAL 73 190 190 VAL VAL B . n +B 1 74 PHE 74 191 191 PHE PHE B . n +B 1 75 LYS 75 192 192 LYS LYS B . n +B 1 76 THR 76 193 193 THR THR B . n +B 1 77 LEU 77 194 194 LEU LEU B . n +B 1 78 LYS 78 195 195 LYS LYS B . n +B 1 79 SER 79 196 196 SER SER B . n +B 1 80 LEU 80 197 197 LEU LEU B . n +B 1 81 TYR 81 198 198 TYR TYR B . n +B 1 82 LYS 82 199 199 LYS LYS B . n +B 1 83 THR 83 200 200 THR THR B . n +B 1 84 HIS 84 201 201 HIS HIS B . n +B 1 85 ALA 85 202 202 ALA ALA B . n +B 1 86 CYS 86 203 203 CYS CYS B . n +B 1 87 TYR 87 204 204 TYR TYR B . n +B 1 88 GLU 88 205 205 GLU GLU B . n +B 1 89 TYR 89 206 206 TYR TYR B . n +B 1 90 ASN 90 207 207 ASN ASN B . n +B 1 91 HIS 91 208 208 HIS HIS B . n +B 1 92 ILE 92 209 209 ILE ILE B . n +B 1 93 PHE 93 210 210 PHE PHE B . n +B 1 94 PRO 94 211 211 PRO PRO B . n +B 1 95 LEU 95 212 212 LEU LEU B . n +B 1 96 LEU 96 213 213 LEU LEU B . n +B 1 97 GLU 97 214 214 GLU GLU B . n +B 1 98 LYS 98 215 215 LYS LYS B . n +B 1 99 TYR 99 216 216 TYR TYR B . n +B 1 100 CYS 100 217 217 CYS CYS B . n +B 1 101 GLY 101 218 218 GLY GLY B . n +B 1 102 PHE 102 219 219 PHE PHE B . n +B 1 103 HIS 103 220 220 HIS HIS B . n +B 1 104 GLU 104 221 221 GLU GLU B . n +B 1 105 ASP 105 222 222 ASP ASP B . n +B 1 106 ASN 106 223 223 ASN ASN B . n +B 1 107 ILE 107 224 224 ILE ILE B . n +B 1 108 PRO 108 225 225 PRO PRO B . n +B 1 109 GLN 109 226 226 GLN GLN B . n +B 1 110 LEU 110 227 227 LEU LEU B . n +B 1 111 GLU 111 228 228 GLU GLU B . n +B 1 112 ASP 112 229 229 ASP ASP B . n +B 1 113 VAL 113 230 230 VAL VAL B . n +B 1 114 SER 114 231 231 SER SER B . n +B 1 115 GLN 115 232 232 GLN GLN B . n +B 1 116 PHE 116 233 233 PHE PHE B . n +B 1 117 LEU 117 234 234 LEU LEU B . n +B 1 118 GLN 118 235 235 GLN GLN B . n +B 1 119 THR 119 236 236 THR THR B . n +B 1 120 CYS 120 237 237 CYS CYS B . n +B 1 121 THR 121 238 238 THR THR B . n +B 1 122 GLY 122 239 239 GLY GLY B . n +B 1 123 PHE 123 240 240 PHE PHE B . n +B 1 124 ARG 124 241 241 ARG ARG B . n +B 1 125 LEU 125 242 242 LEU LEU B . n +B 1 126 ARG 126 243 243 ARG ARG B . n +B 1 127 PRO 127 244 244 PRO PRO B . n +B 1 128 VAL 128 245 245 VAL VAL B . n +B 1 129 ALA 129 246 246 ALA ALA B . n +B 1 130 GLY 130 247 247 GLY GLY B . n +B 1 131 LEU 131 248 248 LEU LEU B . n +B 1 132 LEU 132 249 249 LEU LEU B . n +B 1 133 SER 133 250 250 SER SER B . n +B 1 134 SER 134 251 251 SER SER B . n +B 1 135 ARG 135 252 252 ARG ARG B . n +B 1 136 ASP 136 253 253 ASP ASP B . n +B 1 137 PHE 137 254 254 PHE PHE B . n +B 1 138 LEU 138 255 255 LEU LEU B . n +B 1 139 GLY 139 256 256 GLY GLY B . n +B 1 140 GLY 140 257 257 GLY GLY B . n +B 1 141 LEU 141 258 258 LEU LEU B . n +B 1 142 ALA 142 259 259 ALA ALA B . n +B 1 143 PHE 143 260 260 PHE PHE B . n +B 1 144 ARG 144 261 261 ARG ARG B . n +B 1 145 VAL 145 262 262 VAL VAL B . n +B 1 146 PHE 146 263 263 PHE PHE B . n +B 1 147 HIS 147 264 264 HIS HIS B . n +B 1 148 CYS 148 265 265 CYS CYS B . n +B 1 149 THR 149 266 266 THR THR B . n +B 1 150 GLN 150 267 267 GLN GLN B . n +B 1 151 TYR 151 268 268 TYR TYR B . n +B 1 152 ILE 152 269 269 ILE ILE B . n +B 1 153 ARG 153 270 270 ARG ARG B . n +B 1 154 HIS 154 271 271 HIS HIS B . n +B 1 155 GLY 155 272 272 GLY GLY B . n +B 1 156 SER 156 273 273 SER SER B . n +B 1 157 LYS 157 274 274 LYS LYS B . n +B 1 158 PRO 158 275 275 PRO PRO B . n +B 1 159 MET 159 276 276 MET MET B . n +B 1 160 TYR 160 277 277 TYR TYR B . n +B 1 161 THR 161 278 278 THR THR B . n +B 1 162 PRO 162 279 279 PRO PRO B . n +B 1 163 GLU 163 280 280 GLU GLU B . n +B 1 164 PRO 164 281 281 PRO PRO B . n +B 1 165 ASP 165 282 282 ASP ASP B . n +B 1 166 ILE 166 283 283 ILE ILE B . n +B 1 167 CYS 167 284 284 CYS CYS B . n +B 1 168 HIS 168 285 285 HIS HIS B . n +B 1 169 GLU 169 286 286 GLU GLU B . n +B 1 170 LEU 170 287 287 LEU LEU B . n +B 1 171 LEU 171 288 288 LEU LEU B . n +B 1 172 GLY 172 289 289 GLY GLY B . n +B 1 173 HIS 173 290 290 HIS HIS B . n +B 1 174 VAL 174 291 291 VAL VAL B . n +B 1 175 PRO 175 292 292 PRO PRO B . n +B 1 176 LEU 176 293 293 LEU LEU B . n +B 1 177 PHE 177 294 294 PHE PHE B . n +B 1 178 SER 178 295 295 SER SER B . n +B 1 179 ASP 179 296 296 ASP ASP B . n +B 1 180 ARG 180 297 297 ARG ARG B . n +B 1 181 SER 181 298 298 SER SER B . n +B 1 182 PHE 182 299 299 PHE PHE B . n +B 1 183 ALA 183 300 300 ALA ALA B . n +B 1 184 GLN 184 301 301 GLN GLN B . n +B 1 185 PHE 185 302 302 PHE PHE B . n +B 1 186 SER 186 303 303 SER SER B . n +B 1 187 GLN 187 304 304 GLN GLN B . n +B 1 188 GLU 188 305 305 GLU GLU B . n +B 1 189 ILE 189 306 306 ILE ILE B . n +B 1 190 GLY 190 307 307 GLY GLY B . n +B 1 191 LEU 191 308 308 LEU LEU B . n +B 1 192 ALA 192 309 309 ALA ALA B . n +B 1 193 SER 193 310 310 SER SER B . n +B 1 194 LEU 194 311 311 LEU LEU B . n +B 1 195 GLY 195 312 312 GLY GLY B . n +B 1 196 ALA 196 313 313 ALA ALA B . n +B 1 197 PRO 197 314 314 PRO PRO B . n +B 1 198 ASP 198 315 315 ASP ASP B . n +B 1 199 GLU 199 316 316 GLU GLU B . n +B 1 200 TYR 200 317 317 TYR TYR B . n +B 1 201 ILE 201 318 318 ILE ILE B . n +B 1 202 GLU 202 319 319 GLU GLU B . n +B 1 203 LYS 203 320 320 LYS LYS B . n +B 1 204 LEU 204 321 321 LEU LEU B . n +B 1 205 ALA 205 322 322 ALA ALA B . n +B 1 206 THR 206 323 323 THR THR B . n +B 1 207 ILE 207 324 324 ILE ILE B . n +B 1 208 TYR 208 325 325 TYR TYR B . n +B 1 209 TRP 209 326 326 TRP TRP B . n +B 1 210 PHE 210 327 327 PHE PHE B . n +B 1 211 THR 211 328 328 THR THR B . n +B 1 212 VAL 212 329 329 VAL VAL B . n +B 1 213 GLU 213 330 330 GLU GLU B . n +B 1 214 PHE 214 331 331 PHE PHE B . n +B 1 215 GLY 215 332 332 GLY GLY B . n +B 1 216 LEU 216 333 333 LEU LEU B . n +B 1 217 CYS 217 334 334 CYS CYS B . n +B 1 218 LYS 218 335 335 LYS LYS B . n +B 1 219 GLN 219 336 336 GLN GLN B . n +B 1 220 GLY 220 337 337 GLY GLY B . n +B 1 221 ASP 221 338 338 ASP ASP B . n +B 1 222 SER 222 339 339 SER SER B . n +B 1 223 ILE 223 340 340 ILE ILE B . n +B 1 224 LYS 224 341 341 LYS LYS B . n +B 1 225 ALA 225 342 342 ALA ALA B . n +B 1 226 TYR 226 343 343 TYR TYR B . n +B 1 227 GLY 227 344 344 GLY GLY B . n +B 1 228 ALA 228 345 345 ALA ALA B . n +B 1 229 GLY 229 346 346 GLY GLY B . n +B 1 230 LEU 230 347 347 LEU LEU B . n +B 1 231 LEU 231 348 348 LEU LEU B . n +B 1 232 SER 232 349 349 SER SER B . n +B 1 233 SER 233 350 350 SER SER B . n +B 1 234 PHE 234 351 351 PHE PHE B . n +B 1 235 GLY 235 352 352 GLY GLY B . n +B 1 236 GLU 236 353 353 GLU GLU B . n +B 1 237 LEU 237 354 354 LEU LEU B . n +B 1 238 GLN 238 355 355 GLN GLN B . n +B 1 239 TYR 239 356 356 TYR TYR B . n +B 1 240 CYS 240 357 357 CYS CYS B . n +B 1 241 LEU 241 358 358 LEU LEU B . n +B 1 242 SER 242 359 359 SER SER B . n +B 1 243 GLU 243 360 360 GLU GLU B . n +B 1 244 LYS 244 361 361 LYS LYS B . n +B 1 245 PRO 245 362 362 PRO PRO B . n +B 1 246 LYS 246 363 363 LYS LYS B . n +B 1 247 LEU 247 364 364 LEU LEU B . n +B 1 248 LEU 248 365 365 LEU LEU B . n +B 1 249 PRO 249 366 366 PRO PRO B . n +B 1 250 LEU 250 367 367 LEU LEU B . n +B 1 251 GLU 251 368 368 GLU GLU B . n +B 1 252 LEU 252 369 369 LEU LEU B . n +B 1 253 GLU 253 370 370 GLU GLU B . n +B 1 254 LYS 254 371 371 LYS LYS B . n +B 1 255 THR 255 372 372 THR THR B . n +B 1 256 ALA 256 373 373 ALA ALA B . n +B 1 257 ILE 257 374 374 ILE ILE B . n +B 1 258 GLN 258 375 375 GLN GLN B . n +B 1 259 ASN 259 376 376 ASN ASN B . n +B 1 260 TYR 260 377 377 TYR TYR B . n +B 1 261 THR 261 378 378 THR THR B . n +B 1 262 VAL 262 379 379 VAL VAL B . n +B 1 263 THR 263 380 380 THR THR B . n +B 1 264 GLU 264 381 381 GLU GLU B . n +B 1 265 PHE 265 382 382 PHE PHE B . n +B 1 266 GLN 266 383 383 GLN GLN B . n +B 1 267 PRO 267 384 384 PRO PRO B . n +B 1 268 LEU 268 385 385 LEU LEU B . n +B 1 269 TYR 269 386 386 TYR TYR B . n +B 1 270 TYR 270 387 387 TYR TYR B . n +B 1 271 VAL 271 388 388 VAL VAL B . n +B 1 272 ALA 272 389 389 ALA ALA B . n +B 1 273 GLU 273 390 390 GLU GLU B . n +B 1 274 SER 274 391 391 SER SER B . n +B 1 275 PHE 275 392 392 PHE PHE B . n +B 1 276 ASN 276 393 393 ASN ASN B . n +B 1 277 ASP 277 394 394 ASP ASP B . n +B 1 278 ALA 278 395 395 ALA ALA B . n +B 1 279 LYS 279 396 396 LYS LYS B . n +B 1 280 GLU 280 397 397 GLU GLU B . n +B 1 281 LYS 281 398 398 LYS LYS B . n +B 1 282 VAL 282 399 399 VAL VAL B . n +B 1 283 ARG 283 400 400 ARG ARG B . n +B 1 284 ASN 284 401 401 ASN ASN B . n +B 1 285 PHE 285 402 402 PHE PHE B . n +B 1 286 ALA 286 403 403 ALA ALA B . n +B 1 287 ALA 287 404 404 ALA ALA B . n +B 1 288 THR 288 405 405 THR THR B . n +B 1 289 ILE 289 406 406 ILE ILE B . n +B 1 290 PRO 290 407 407 PRO PRO B . n +B 1 291 ARG 291 408 408 ARG ARG B . n +B 1 292 PRO 292 409 409 PRO PRO B . n +B 1 293 PHE 293 410 410 PHE PHE B . n +B 1 294 SER 294 411 411 SER SER B . n +B 1 295 VAL 295 412 412 VAL VAL B . n +B 1 296 ARG 296 413 413 ARG ARG B . n +B 1 297 TYR 297 414 414 TYR TYR B . n +B 1 298 ASP 298 415 415 ASP ASP B . n +B 1 299 PRO 299 416 416 PRO PRO B . n +B 1 300 TYR 300 417 417 TYR TYR B . n +B 1 301 THR 301 418 418 THR THR B . n +B 1 302 GLN 302 419 419 GLN GLN B . n +B 1 303 ARG 303 420 420 ARG ARG B . n +B 1 304 ILE 304 421 421 ILE ILE B . n +B 1 305 GLU 305 422 422 GLU GLU B . n +B 1 306 VAL 306 423 423 VAL VAL B . n +B 1 307 LEU 307 424 424 LEU LEU B . n +B 1 308 ASP 308 425 425 ASP ASP B . n +B 1 309 ASN 309 426 426 ASN ASN B . n +B 1 310 THR 310 427 427 THR THR B . n +B 1 311 GLN 311 428 428 GLN GLN B . n +B 1 312 GLN 312 429 429 GLN GLN B . n +B 1 313 LEU 313 430 430 LEU LEU B . n +B 1 314 LYS 314 431 431 LYS LYS B . n +B 1 315 ILE 315 432 432 ILE ILE B . n +B 1 316 LEU 316 433 433 LEU LEU B . n +B 1 317 ALA 317 434 434 ALA ALA B . n +B 1 318 ASP 318 435 435 ASP ASP B . n +B 1 319 SER 319 436 436 SER SER B . n +B 1 320 ILE 320 437 437 ILE ILE B . n +B 1 321 ASN 321 438 438 ASN ASN B . n +B 1 322 SER 322 439 439 SER SER B . n +B 1 323 GLU 323 440 440 GLU GLU B . n +B 1 324 ILE 324 441 441 ILE ILE B . n +B 1 325 GLY 325 442 442 GLY GLY B . n +B 1 326 ILE 326 443 443 ILE ILE B . n +B 1 327 LEU 327 444 444 LEU LEU B . n +B 1 328 CYS 328 445 445 CYS CYS B . n +B 1 329 SER 329 446 446 SER SER B . n +B 1 330 ALA 330 447 447 ALA ALA B . n +B 1 331 LEU 331 448 448 LEU LEU B . n +B 1 332 GLN 332 449 449 GLN GLN B . n +B 1 333 LYS 333 450 450 LYS LYS B . n +B 1 334 ILE 334 451 451 ILE ILE B . n +B 1 335 LYS 335 452 452 LYS LYS B . n +# +loop_ +_pdbe_orig_nonpoly_scheme.asym_id +_pdbe_orig_nonpoly_scheme.entity_id +_pdbe_orig_nonpoly_scheme.mon_id +_pdbe_orig_nonpoly_scheme.ndb_seq_num +_pdbe_orig_nonpoly_scheme.pdb_seq_num +_pdbe_orig_nonpoly_scheme.auth_seq_num +_pdbe_orig_nonpoly_scheme.pdb_mon_id +_pdbe_orig_nonpoly_scheme.auth_mon_id +_pdbe_orig_nonpoly_scheme.pdb_strand_id +_pdbe_orig_nonpoly_scheme.pdb_ins_code +C 2 FE 1 453 453 FE FE A . +D 2 FE 1 454 454 FE FE B . +# +loop_ +_entity.id +_entity.type +_entity.src_method +_entity.pdbx_description +_entity.formula_weight +_entity.pdbx_number_of_molecules +_entity.details +_entity.pdbx_mutation +_entity.pdbx_fragment +_entity.pdbx_ec +_entity.assembly_id +1 polymer man "PROTEIN (PHENYLALANINE HYDROXYLASE)" 38642.312 4 "ACTIVE SITE IRON ATOM FE" ? "RESIDUES 118-452" 1.14.16.1 2PAH-assembly-1 +2 non-polymer syn "FE (III) ION" 55.847 4 ? ? ? ? 2PAH-assembly-1 +# +_entity_poly.entity_id 1 +_entity_poly.nstd_monomer no +_entity_poly.pdbx_seq_one_letter_code_can +;VPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSL +YKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMY +TPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYC +LSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVLDNTQQLKILADSI +NSEIGILCSALQKIK +; + +_entity_poly.nstd_linkage no +_entity_poly.pdbx_seq_one_letter_code +;VPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSL +YKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMY +TPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYC +LSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVLDNTQQLKILADSI +NSEIGILCSALQKIK +; + +_entity_poly.assembly_id 2PAH-assembly-1 +_entity_poly.type polypeptide(L) +_entity_poly.pdbx_strand_id A,AA,B,BA +# +_pdbx_entity_nonpoly.assembly_id 2PAH-assembly-1 +_pdbx_entity_nonpoly.entity_id 2 +_pdbx_entity_nonpoly.name "FE (III) ION" +_pdbx_entity_nonpoly.comp_id FE +# +loop_ +_pdbe_entity_remapping.source_coordinates +_pdbe_entity_remapping.assembly_id +_pdbe_entity_remapping.entity_id +_pdbe_entity_remapping.type +_pdbe_entity_remapping.description +2PAH 2PAH-assembly-1 1 polypeptide(L) "PROTEIN (PHENYLALANINE HYDROXYLASE)" +2PAH 2PAH-assembly-1 2 ligand "FE (III) ION" +# +loop_ +_pdbe_chain_remapping.source_coordinates +_pdbe_chain_remapping.assembly_id +_pdbe_chain_remapping.model_num +_pdbe_chain_remapping.entity_id +_pdbe_chain_remapping.orig_auth_asym_id +_pdbe_chain_remapping.new_auth_asym_id +_pdbe_chain_remapping.orig_label_asym_id +_pdbe_chain_remapping.new_label_asym_id +_pdbe_chain_remapping.applied_operations +2PAH 2PAH-assembly-1 1 1 A A A A "_1" +2PAH 2PAH-assembly-1 1 1 A AA A AA "_2" +2PAH 2PAH-assembly-1 1 1 B B B B "_1" +2PAH 2PAH-assembly-1 1 1 B BA B BA "_2" +2PAH 2PAH-assembly-1 1 2 A C C C "_1" +2PAH 2PAH-assembly-1 1 2 A CA C CA "_2" +2PAH 2PAH-assembly-1 1 2 B D D D "_1" +2PAH 2PAH-assembly-1 1 2 B DA D DA "_2" +# +loop_ +_atom_site.group_PDB +_atom_site.id +_atom_site.type_symbol +_atom_site.label_atom_id +_atom_site.label_alt_id +_atom_site.label_comp_id +_atom_site.label_asym_id +_atom_site.label_entity_id +_atom_site.label_seq_id +_atom_site.pdbx_PDB_ins_code +_atom_site.Cartn_x +_atom_site.Cartn_y +_atom_site.Cartn_z +_atom_site.occupancy +_atom_site.B_iso_or_equiv +_atom_site.Cartn_x_esd +_atom_site.Cartn_y_esd +_atom_site.Cartn_z_esd +_atom_site.occupancy_esd +_atom_site.B_iso_or_equiv_esd +_atom_site.pdbx_formal_charge +_atom_site.auth_seq_id +_atom_site.auth_comp_id +_atom_site.auth_asym_id +_atom_site.auth_atom_id +_atom_site.pdbx_PDB_model_num +_atom_site.pdbe_label_seq_id +_atom_site.orig_label_asym_id +_atom_site.orig_auth_asym_id +ATOM 1 N N . VAL A 1 1 ? -7.069 21.943 18.770 1.0 56.51 ? ? ? ? ? ? 118 VAL A N 1 1 A A +ATOM 2 C CA . VAL A 1 1 ? -7.077 21.688 20.244 1.0 59.09 ? ? ? ? ? ? 118 VAL A CA 1 1 A A +ATOM 3 C C . VAL A 1 1 ? -5.756 21.077 20.700 1.0 44.63 ? ? ? ? ? ? 118 VAL A C 1 1 A A +ATOM 4 O O . VAL A 1 1 ? -5.346 20.029 20.204 1.0 59.84 ? ? ? ? ? ? 118 VAL A O 1 1 A A +ATOM 5 C CB . VAL A 1 1 ? -8.218 20.724 20.638 1.0 53.9 ? ? ? ? ? ? 118 VAL A CB 1 1 A A +ATOM 6 C CG1 . VAL A 1 1 ? -8.154 20.417 22.126 1.0 24.03 ? ? ? ? ? ? 118 VAL A CG1 1 1 A A +ATOM 7 C CG2 . VAL A 1 1 ? -9.555 21.344 20.287 1.0 72.82 ? ? ? ? ? ? 118 VAL A CG2 1 1 A A +ATOM 8 N N . PRO A 1 2 ? -5.090 21.711 21.683 1.0 27.43 ? ? ? ? ? ? 119 PRO A N 1 2 A A +ATOM 9 C CA . PRO A 1 2 ? -3.808 21.216 22.195 1.0 20.13 ? ? ? ? ? ? 119 PRO A CA 1 2 A A +ATOM 10 C C . PRO A 1 2 ? -3.864 19.750 22.588 1.0 30.85 ? ? ? ? ? ? 119 PRO A C 1 2 A A +ATOM 11 O O . PRO A 1 2 ? -4.908 19.250 22.999 1.0 42.83 ? ? ? ? ? ? 119 PRO A O 1 2 A A +ATOM 12 C CB . PRO A 1 2 ? -3.520 22.117 23.394 1.0 7.28 ? ? ? ? ? ? 119 PRO A CB 1 2 A A +ATOM 13 C CG . PRO A 1 2 ? -4.316 23.335 23.159 1.0 31.66 ? ? ? ? ? ? 119 PRO A CG 1 2 A A +ATOM 14 C CD . PRO A 1 2 ? -5.536 22.916 22.397 1.0 41.73 ? ? ? ? ? ? 119 PRO A CD 1 2 A A +ATOM 15 N N . TRP A 1 3 ? -2.731 19.068 22.464 1.0 36.51 ? ? ? ? ? ? 120 TRP A N 1 3 A A +ATOM 16 C CA . TRP A 1 3 ? -2.647 17.659 22.821 1.0 33.96 ? ? ? ? ? ? 120 TRP A CA 1 3 A A +ATOM 17 C C . TRP A 1 3 ? -2.475 17.514 24.327 1.0 42.42 ? ? ? ? ? ? 120 TRP A C 1 3 A A +ATOM 18 O O . TRP A 1 3 ? -1.735 18.278 24.950 1.0 43.61 ? ? ? ? ? ? 120 TRP A O 1 3 A A +ATOM 19 C CB . TRP A 1 3 ? -1.460 16.995 22.109 1.0 27.89 ? ? ? ? ? ? 120 TRP A CB 1 3 A A +ATOM 20 C CG . TRP A 1 3 ? -1.200 15.578 22.560 1.0 23.25 ? ? ? ? ? ? 120 TRP A CG 1 3 A A +ATOM 21 C CD1 . TRP A 1 3 ? -1.645 14.433 21.962 1.0 45.51 ? ? ? ? ? ? 120 TRP A CD1 1 3 A A +ATOM 22 C CD2 . TRP A 1 3 ? -0.460 15.161 23.718 1.0 22.82 ? ? ? ? ? ? 120 TRP A CD2 1 3 A A +ATOM 23 N NE1 . TRP A 1 3 ? -1.234 13.330 22.677 1.0 46.58 ? ? ? ? ? ? 120 TRP A NE1 1 3 A A +ATOM 24 C CE2 . TRP A 1 3 ? -0.504 13.751 23.759 1.0 27.53 ? ? ? ? ? ? 120 TRP A CE2 1 3 A A +ATOM 25 C CE3 . TRP A 1 3 ? 0.229 15.844 24.731 1.0 15.24 ? ? ? ? ? ? 120 TRP A CE3 1 3 A A +ATOM 26 C CZ2 . TRP A 1 3 ? 0.120 13.009 24.767 1.0 36.09 ? ? ? ? ? ? 120 TRP A CZ2 1 3 A A +ATOM 27 C CZ3 . TRP A 1 3 ? 0.854 15.105 25.731 1.0 30.46 ? ? ? ? ? ? 120 TRP A CZ3 1 3 A A +ATOM 28 C CH2 . TRP A 1 3 ? 0.790 13.703 25.743 1.0 36.66 ? ? ? ? ? ? 120 TRP A CH2 1 3 A A +ATOM 29 N N . PHE A 1 4 ? -3.165 16.535 24.906 1.0 36.52 ? ? ? ? ? ? 121 PHE A N 1 4 A A +ATOM 30 C CA . PHE A 1 4 ? -3.068 16.272 26.337 1.0 34.42 ? ? ? ? ? ? 121 PHE A CA 1 4 A A +ATOM 31 C C . PHE A 1 4 ? -3.023 14.773 26.610 1.0 36.94 ? ? ? ? ? ? 121 PHE A C 1 4 A A +ATOM 32 O O . PHE A 1 4 ? -3.565 13.973 25.839 1.0 28.54 ? ? ? ? ? ? 121 PHE A O 1 4 A A +ATOM 33 C CB . PHE A 1 4 ? -4.241 16.911 27.091 1.0 43.63 ? ? ? ? ? ? 121 PHE A CB 1 4 A A +ATOM 34 C CG . PHE A 1 4 ? -5.582 16.364 26.709 1.0 43.79 ? ? ? ? ? ? 121 PHE A CG 1 4 A A +ATOM 35 C CD1 . PHE A 1 4 ? -6.071 15.206 27.305 1.0 49.28 ? ? ? ? ? ? 121 PHE A CD1 1 4 A A +ATOM 36 C CD2 . PHE A 1 4 ? -6.365 17.013 25.762 1.0 41.43 ? ? ? ? ? ? 121 PHE A CD2 1 4 A A +ATOM 37 C CE1 . PHE A 1 4 ? -7.320 14.702 26.965 1.0 37.53 ? ? ? ? ? ? 121 PHE A CE1 1 4 A A +ATOM 38 C CE2 . PHE A 1 4 ? -7.614 16.518 25.416 1.0 43.57 ? ? ? ? ? ? 121 PHE A CE2 1 4 A A +ATOM 39 C CZ . PHE A 1 4 ? -8.093 15.357 26.020 1.0 44.15 ? ? ? ? ? ? 121 PHE A CZ 1 4 A A +ATOM 40 N N . PRO A 1 5 ? -2.359 14.374 27.711 1.0 30.16 ? ? ? ? ? ? 122 PRO A N 1 5 A A +ATOM 41 C CA . PRO A 1 5 ? -2.238 12.962 28.089 1.0 28.65 ? ? ? ? ? ? 122 PRO A CA 1 5 A A +ATOM 42 C C . PRO A 1 5 ? -3.555 12.293 28.458 1.0 26.18 ? ? ? ? ? ? 122 PRO A C 1 5 A A +ATOM 43 O O . PRO A 1 5 ? -4.329 12.824 29.246 1.0 40.25 ? ? ? ? ? ? 122 PRO A O 1 5 A A +ATOM 44 C CB . PRO A 1 5 ? -1.255 12.984 29.258 1.0 24.5 ? ? ? ? ? ? 122 PRO A CB 1 5 A A +ATOM 45 C CG . PRO A 1 5 ? -1.356 14.355 29.802 1.0 21.8 ? ? ? ? ? ? 122 PRO A CG 1 5 A A +ATOM 46 C CD . PRO A 1 5 ? -1.656 15.256 28.656 1.0 11.45 ? ? ? ? ? ? 122 PRO A CD 1 5 A A +ATOM 47 N N . ARG A 1 6 ? -3.801 11.124 27.872 1.0 42.98 ? ? ? ? ? ? 123 ARG A N 1 6 A A +ATOM 48 C CA . ARG A 1 6 ? -5.016 10.367 28.145 1.0 51.56 ? ? ? ? ? ? 123 ARG A CA 1 6 A A +ATOM 49 C C . ARG A 1 6 ? -4.721 9.356 29.246 1.0 49.43 ? ? ? ? ? ? 123 ARG A C 1 6 A A +ATOM 50 O O . ARG A 1 6 ? -5.581 9.053 30.070 1.0 52.64 ? ? ? ? ? ? 123 ARG A O 1 6 A A +ATOM 51 C CB . ARG A 1 6 ? -5.482 9.631 26.885 1.0 79.49 ? ? ? ? ? ? 123 ARG A CB 1 6 A A +ATOM 52 C CG . ARG A 1 6 ? -5.655 10.524 25.665 1.0 80.86 ? ? ? ? ? ? 123 ARG A CG 1 6 A A +ATOM 53 C CD . ARG A 1 6 ? -6.878 11.411 25.805 1.0 89.46 ? ? ? ? ? ? 123 ARG A CD 1 6 A A +ATOM 54 N NE . ARG A 1 6 ? -7.375 11.859 24.508 1.0 100.0 ? ? ? ? ? ? 123 ARG A NE 1 6 A A +ATOM 55 C CZ . ARG A 1 6 ? -8.308 11.226 23.804 1.0 100.0 ? ? ? ? ? ? 123 ARG A CZ 1 6 A A +ATOM 56 N NH1 . ARG A 1 6 ? -8.850 10.109 24.271 1.0 100.0 ? ? ? ? ? ? 123 ARG A NH1 1 6 A A +ATOM 57 N NH2 . ARG A 1 6 ? -8.698 11.710 22.632 1.0 100.0 ? ? ? ? ? ? 123 ARG A NH2 1 6 A A +ATOM 58 N N . THR A 1 7 ? -3.494 8.844 29.247 1.0 38.4 ? ? ? ? ? ? 124 THR A N 1 7 A A +ATOM 59 C CA . THR A 1 7 ? -3.057 7.868 30.237 1.0 39.91 ? ? ? ? ? ? 124 THR A CA 1 7 A A +ATOM 60 C C . THR A 1 7 ? -1.964 8.454 31.112 1.0 31.37 ? ? ? ? ? ? 124 THR A C 1 7 A A +ATOM 61 O O . THR A 1 7 ? -1.270 9.395 30.716 1.0 40.84 ? ? ? ? ? ? 124 THR A O 1 7 A A +ATOM 62 C CB . THR A 1 7 ? -2.486 6.592 29.589 1.0 49.36 ? ? ? ? ? ? 124 THR A CB 1 7 A A +ATOM 63 O OG1 . THR A 1 7 ? -3.354 6.151 28.541 1.0 66.48 ? ? ? ? ? ? 124 THR A OG1 1 7 A A +ATOM 64 C CG2 . THR A 1 7 ? -2.354 5.486 30.631 1.0 58.27 ? ? ? ? ? ? 124 THR A CG2 1 7 A A +ATOM 65 N N . ILE A 1 8 ? -1.823 7.877 32.303 1.0 31.21 ? ? ? ? ? ? 125 ILE A N 1 8 A A +ATOM 66 C CA . ILE A 1 8 ? -0.827 8.303 33.279 1.0 32.65 ? ? ? ? ? ? 125 ILE A CA 1 8 A A +ATOM 67 C C . ILE A 1 8 ? 0.589 8.044 32.765 1.0 38.63 ? ? ? ? ? ? 125 ILE A C 1 8 A A +ATOM 68 O O . ILE A 1 8 ? 1.529 8.769 33.109 1.0 41.02 ? ? ? ? ? ? 125 ILE A O 1 8 A A +ATOM 69 C CB . ILE A 1 8 ? -1.015 7.556 34.616 1.0 22.18 ? ? ? ? ? ? 125 ILE A CB 1 8 A A +ATOM 70 C CG1 . ILE A 1 8 ? -0.129 8.177 35.694 1.0 31.62 ? ? ? ? ? ? 125 ILE A CG1 1 8 A A +ATOM 71 C CG2 . ILE A 1 8 ? -0.692 6.085 34.435 1.0 23.1 ? ? ? ? ? ? 125 ILE A CG2 1 8 A A +ATOM 72 C CD1 . ILE A 1 8 ? -0.645 7.967 37.107 1.0 42.67 ? ? ? ? ? ? 125 ILE A CD1 1 8 A A +ATOM 73 N N . GLN A 1 9 ? 0.734 7.010 31.939 1.0 26.14 ? ? ? ? ? ? 126 GLN A N 1 9 A A +ATOM 74 C CA . GLN A 1 9 ? 2.032 6.653 31.380 1.0 31.21 ? ? ? ? ? ? 126 GLN A CA 1 9 A A +ATOM 75 C C . GLN A 1 9 ? 2.403 7.554 30.206 1.0 26.0 ? ? ? ? ? ? 126 GLN A C 1 9 A A +ATOM 76 O O . GLN A 1 9 ? 3.541 7.545 29.740 1.0 35.26 ? ? ? ? ? ? 126 GLN A O 1 9 A A +ATOM 77 C CB . GLN A 1 9 ? 2.023 5.193 30.921 1.0 52.92 ? ? ? ? ? ? 126 GLN A CB 1 9 A A +ATOM 78 C CG . GLN A 1 9 ? 1.589 4.205 31.987 1.0 74.24 ? ? ? ? ? ? 126 GLN A CG 1 9 A A +ATOM 79 C CD . GLN A 1 9 ? 0.175 3.707 31.775 1.0 86.27 ? ? ? ? ? ? 126 GLN A CD 1 9 A A +ATOM 80 O OE1 . GLN A 1 9 ? -0.231 3.420 30.648 1.0 100.0 ? ? ? ? ? ? 126 GLN A OE1 1 9 A A +ATOM 81 N NE2 . GLN A 1 9 ? -0.583 3.598 32.859 1.0 91.63 ? ? ? ? ? ? 126 GLN A NE2 1 9 A A +ATOM 82 N N . GLU A 1 10 ? 1.429 8.324 29.733 1.0 24.99 ? ? ? ? ? ? 127 GLU A N 1 10 A A +ATOM 83 C CA . GLU A 1 10 ? 1.639 9.225 28.608 1.0 29.2 ? ? ? ? ? ? 127 GLU A CA 1 10 A A +ATOM 84 C C . GLU A 1 10 ? 2.400 10.479 29.004 1.0 26.32 ? ? ? ? ? ? 127 GLU A C 1 10 A A +ATOM 85 O O . GLU A 1 10 ? 2.711 11.316 28.160 1.0 34.58 ? ? ? ? ? ? 127 GLU A O 1 10 A A +ATOM 86 C CB . GLU A 1 10 ? 0.299 9.615 27.995 1.0 29.55 ? ? ? ? ? ? 127 GLU A CB 1 10 A A +ATOM 87 C CG . GLU A 1 10 ? -0.444 8.454 27.368 1.0 48.32 ? ? ? ? ? ? 127 GLU A CG 1 10 A A +ATOM 88 C CD . GLU A 1 10 ? -1.363 8.892 26.246 1.0 52.9 ? ? ? ? ? ? 127 GLU A CD 1 10 A A +ATOM 89 O OE1 . GLU A 1 10 ? -1.628 10.109 26.136 1.0 51.84 ? ? ? ? ? ? 127 GLU A OE1 1 10 A A +ATOM 90 O OE2 . GLU A 1 10 ? -1.817 8.021 25.472 1.0 41.2 ? ? ? ? ? ? 127 GLU A OE2 1 10 A A +ATOM 91 N N . LEU A 1 11 ? 2.692 10.601 30.292 1.0 25.59 ? ? ? ? ? ? 128 LEU A N 1 11 A A +ATOM 92 C CA . LEU A 1 11 ? 3.427 11.750 30.806 1.0 40.76 ? ? ? ? ? ? 128 LEU A CA 1 11 A A +ATOM 93 C C . LEU A 1 11 ? 4.913 11.562 30.504 1.0 42.92 ? ? ? ? ? ? 128 LEU A C 1 11 A A +ATOM 94 O O . LEU A 1 11 ? 5.744 12.418 30.813 1.0 43.06 ? ? ? ? ? ? 128 LEU A O 1 11 A A +ATOM 95 C CB . LEU A 1 11 ? 3.215 11.877 32.321 1.0 57.74 ? ? ? ? ? ? 128 LEU A CB 1 11 A A +ATOM 96 C CG . LEU A 1 11 ? 1.780 12.086 32.826 1.0 61.98 ? ? ? ? ? ? 128 LEU A CG 1 11 A A +ATOM 97 C CD1 . LEU A 1 11 ? 1.774 12.145 34.339 1.0 55.34 ? ? ? ? ? ? 128 LEU A CD1 1 11 A A +ATOM 98 C CD2 . LEU A 1 11 ? 1.204 13.361 32.244 1.0 61.21 ? ? ? ? ? ? 128 LEU A CD2 1 11 A A +ATOM 99 N N . ASP A 1 12 ? 5.233 10.421 29.900 1.0 30.8 ? ? ? ? ? ? 129 ASP A N 1 12 A A +ATOM 100 C CA . ASP A 1 12 ? 6.604 10.086 29.546 1.0 26.65 ? ? ? ? ? ? 129 ASP A CA 1 12 A A +ATOM 101 C C . ASP A 1 12 ? 7.058 10.948 28.391 1.0 34.53 ? ? ? ? ? ? 129 ASP A C 1 12 A A +ATOM 102 O O . ASP A 1 12 ? 8.226 10.912 27.990 1.0 55.86 ? ? ? ? ? ? 129 ASP A O 1 12 A A +ATOM 103 C CB . ASP A 1 12 ? 6.695 8.623 29.131 1.0 32.05 ? ? ? ? ? ? 129 ASP A CB 1 12 A A +ATOM 104 C CG . ASP A 1 12 ? 6.496 7.674 30.285 1.0 37.31 ? ? ? ? ? ? 129 ASP A CG 1 12 A A +ATOM 105 O OD1 . ASP A 1 12 ? 6.596 8.115 31.447 1.0 22.36 ? ? ? ? ? ? 129 ASP A OD1 1 12 A A +ATOM 106 O OD2 . ASP A 1 12 ? 6.245 6.480 30.028 1.0 43.85 ? ? ? ? ? ? 129 ASP A OD2 1 12 A A +ATOM 107 N N . ARG A 1 13 ? 6.105 11.696 27.844 1.0 26.69 ? ? ? ? ? ? 130 ARG A N 1 13 A A +ATOM 108 C CA . ARG A 1 13 ? 6.359 12.576 26.715 1.0 43.72 ? ? ? ? ? ? 130 ARG A CA 1 13 A A +ATOM 109 C C . ARG A 1 13 ? 6.875 13.921 27.205 1.0 42.68 ? ? ? ? ? ? 130 ARG A C 1 13 A A +ATOM 110 O O . ARG A 1 13 ? 7.537 14.647 26.464 1.0 51.14 ? ? ? ? ? ? 130 ARG A O 1 13 A A +ATOM 111 C CB . ARG A 1 13 ? 5.076 12.757 25.892 1.0 48.35 ? ? ? ? ? ? 130 ARG A CB 1 13 A A +ATOM 112 C CG . ARG A 1 13 ? 4.785 11.589 24.935 1.0 88.58 ? ? ? ? ? ? 130 ARG A CG 1 13 A A +ATOM 113 C CD . ARG A 1 13 ? 3.644 11.888 23.953 1.0 100.0 ? ? ? ? ? ? 130 ARG A CD 1 13 A A +ATOM 114 N NE . ARG A 1 13 ? 3.410 10.773 23.031 1.0 100.0 ? ? ? ? ? ? 130 ARG A NE 1 13 A A +ATOM 115 C CZ . ARG A 1 13 ? 2.274 10.557 22.369 1.0 90.45 ? ? ? ? ? ? 130 ARG A CZ 1 13 A A +ATOM 116 N NH1 . ARG A 1 13 ? 1.246 11.377 22.516 1.0 86.66 ? ? ? ? ? ? 130 ARG A NH1 1 13 A A +ATOM 117 N NH2 . ARG A 1 13 ? 2.163 9.515 21.555 1.0 74.81 ? ? ? ? ? ? 130 ARG A NH2 1 13 A A +ATOM 118 N N . PHE A 1 14 ? 6.575 14.243 28.459 1.0 47.82 ? ? ? ? ? ? 131 PHE A N 1 14 A A +ATOM 119 C CA . PHE A 1 14 ? 7.023 15.494 29.059 1.0 49.03 ? ? ? ? ? ? 131 PHE A CA 1 14 A A +ATOM 120 C C . PHE A 1 14 ? 8.537 15.450 29.242 1.0 48.51 ? ? ? ? ? ? 131 PHE A C 1 14 A A +ATOM 121 O O . PHE A 1 14 ? 9.243 16.411 28.945 1.0 53.68 ? ? ? ? ? ? 131 PHE A O 1 14 A A +ATOM 122 C CB . PHE A 1 14 ? 6.352 15.700 30.422 1.0 56.74 ? ? ? ? ? ? 131 PHE A CB 1 14 A A +ATOM 123 C CG . PHE A 1 14 ? 4.881 15.992 30.342 1.0 54.59 ? ? ? ? ? ? 131 PHE A CG 1 14 A A +ATOM 124 C CD1 . PHE A 1 14 ? 4.077 15.849 31.467 1.0 67.99 ? ? ? ? ? ? 131 PHE A CD1 1 14 A A +ATOM 125 C CD2 . PHE A 1 14 ? 4.299 16.418 29.154 1.0 28.7 ? ? ? ? ? ? 131 PHE A CD2 1 14 A A +ATOM 126 C CE1 . PHE A 1 14 ? 2.716 16.123 31.409 1.0 47.89 ? ? ? ? ? ? 131 PHE A CE1 1 14 A A +ATOM 127 C CE2 . PHE A 1 14 ? 2.938 16.694 29.089 1.0 49.87 ? ? ? ? ? ? 131 PHE A CE2 1 14 A A +ATOM 128 C CZ . PHE A 1 14 ? 2.147 16.547 30.220 1.0 43.98 ? ? ? ? ? ? 131 PHE A CZ 1 14 A A +ATOM 129 N N . ALA A 1 15 ? 9.030 14.321 29.744 1.0 48.67 ? ? ? ? ? ? 132 ALA A N 1 15 A A +ATOM 130 C CA . ALA A 1 15 ? 10.458 14.127 29.961 1.0 62.55 ? ? ? ? ? ? 132 ALA A CA 1 15 A A +ATOM 131 C C . ALA A 1 15 ? 10.961 13.163 28.909 1.0 67.09 ? ? ? ? ? ? 132 ALA A C 1 15 A A +ATOM 132 O O . ALA A 1 15 ? 11.498 12.106 29.222 1.0 80.85 ? ? ? ? ? ? 132 ALA A O 1 15 A A +ATOM 133 C CB . ALA A 1 15 ? 10.705 13.564 31.348 1.0 75.74 ? ? ? ? ? ? 132 ALA A CB 1 15 A A +ATOM 134 N N . ASN A 1 16 ? 10.766 13.523 27.648 1.0 70.09 ? ? ? ? ? ? 133 ASN A N 1 16 A A +ATOM 135 C CA . ASN A 1 16 ? 11.192 12.692 26.532 1.0 77.55 ? ? ? ? ? ? 133 ASN A CA 1 16 A A +ATOM 136 C C . ASN A 1 16 ? 12.697 12.475 26.577 1.0 84.87 ? ? ? ? ? ? 133 ASN A C 1 16 A A +ATOM 137 O O . ASN A 1 16 ? 13.163 11.351 26.791 1.0 84.52 ? ? ? ? ? ? 133 ASN A O 1 16 A A +ATOM 138 C CB . ASN A 1 16 ? 10.793 13.360 25.215 1.0 77.32 ? ? ? ? ? ? 133 ASN A CB 1 16 A A +ATOM 139 C CG . ASN A 1 16 ? 10.979 12.455 24.020 1.0 93.97 ? ? ? ? ? ? 133 ASN A CG 1 16 A A +ATOM 140 O OD1 . ASN A 1 16 ? 10.554 11.310 24.017 1.0 100.0 ? ? ? ? ? ? 133 ASN A OD1 1 16 A A +ATOM 141 N ND2 . ASN A 1 16 ? 11.619 12.985 22.988 1.0 99.59 ? ? ? ? ? ? 133 ASN A ND2 1 16 A A +ATOM 142 N N . GLN A 1 17 ? 13.436 13.567 26.394 1.0 82.31 ? ? ? ? ? ? 134 GLN A N 1 17 A A +ATOM 143 C CA . GLN A 1 17 ? 14.897 13.608 26.369 1.0 87.1 ? ? ? ? ? ? 134 GLN A CA 1 17 A A +ATOM 144 C C . GLN A 1 17 ? 15.133 14.618 25.254 1.0 82.51 ? ? ? ? ? ? 134 GLN A C 1 17 A A +ATOM 145 O O . GLN A 1 17 ? 15.796 15.639 25.444 1.0 86.33 ? ? ? ? ? ? 134 GLN A O 1 17 A A +ATOM 146 C CB . GLN A 1 17 ? 15.499 12.251 25.985 1.0 96.7 ? ? ? ? ? ? 134 GLN A CB 1 17 A A +ATOM 147 C CG . GLN A 1 17 ? 16.954 12.291 25.518 1.0 100.0 ? ? ? ? ? ? 134 GLN A CG 1 17 A A +ATOM 148 C CD . GLN A 1 17 ? 17.800 13.261 26.319 1.0 100.0 ? ? ? ? ? ? 134 GLN A CD 1 17 A A +ATOM 149 O OE1 . GLN A 1 17 ? 17.982 14.408 25.922 1.0 100.0 ? ? ? ? ? ? 134 GLN A OE1 1 17 A A +ATOM 150 N NE2 . GLN A 1 17 ? 18.321 12.806 27.446 1.0 100.0 ? ? ? ? ? ? 134 GLN A NE2 1 17 A A +ATOM 151 N N . ILE A 1 18 ? 14.547 14.339 24.094 1.0 75.59 ? ? ? ? ? ? 135 ILE A N 1 18 A A +ATOM 152 C CA . ILE A 1 18 ? 14.653 15.234 22.957 1.0 68.45 ? ? ? ? ? ? 135 ILE A CA 1 18 A A +ATOM 153 C C . ILE A 1 18 ? 13.510 16.208 23.190 1.0 75.79 ? ? ? ? ? ? 135 ILE A C 1 18 A A +ATOM 154 O O . ILE A 1 18 ? 12.703 16.006 24.112 1.0 75.72 ? ? ? ? ? ? 135 ILE A O 1 18 A A +ATOM 155 C CB . ILE A 1 18 ? 14.427 14.500 21.634 1.0 65.37 ? ? ? ? ? ? 135 ILE A CB 1 18 A A +ATOM 156 C CG1 . ILE A 1 18 ? 15.303 13.246 21.571 1.0 63.4 ? ? ? ? ? ? 135 ILE A CG1 1 18 A A +ATOM 157 C CG2 . ILE A 1 18 ? 14.738 15.424 20.468 1.0 58.73 ? ? ? ? ? ? 135 ILE A CG2 1 18 A A +ATOM 158 C CD1 . ILE A 1 18 ? 15.063 12.393 20.366 1.0 63.25 ? ? ? ? ? ? 135 ILE A CD1 1 18 A A +ATOM 159 N N . LEU A 1 19 ? 13.450 17.256 22.377 1.0 79.56 ? ? ? ? ? ? 136 LEU A N 1 19 A A +ATOM 160 C CA . LEU A 1 19 ? 12.402 18.270 22.496 1.0 82.0 ? ? ? ? ? ? 136 LEU A CA 1 19 A A +ATOM 161 C C . LEU A 1 19 ? 12.634 19.188 23.697 1.0 78.51 ? ? ? ? ? ? 136 LEU A C 1 19 A A +ATOM 162 O O . LEU A 1 19 ? 11.651 19.482 24.393 1.0 77.87 ? ? ? ? ? ? 136 LEU A O 1 19 A A +ATOM 163 C CB . LEU A 1 19 ? 11.024 17.598 22.610 1.0 62.69 ? ? ? ? ? ? 136 LEU A CB 1 19 A A +ATOM 164 C CG . LEU A 1 19 ? 10.392 16.880 21.402 1.0 64.59 ? ? ? ? ? ? 136 LEU A CG 1 19 A A +ATOM 165 C CD1 . LEU A 1 19 ? 11.402 16.030 20.685 1.0 57.81 ? ? ? ? ? ? 136 LEU A CD1 1 19 A A +ATOM 166 C CD2 . LEU A 1 19 ? 9.257 16.021 21.897 1.0 49.28 ? ? ? ? ? ? 136 LEU A CD2 1 19 A A +ATOM 167 N N . ASP A 1 26 ? 21.929 30.291 32.414 1.0 84.31 ? ? ? ? ? ? 143 ASP A N 1 26 A A +ATOM 168 C CA . ASP A 1 26 ? 21.764 31.776 32.435 1.0 99.88 ? ? ? ? ? ? 143 ASP A CA 1 26 A A +ATOM 169 C C . ASP A 1 26 ? 22.677 32.437 33.459 1.0 98.47 ? ? ? ? ? ? 143 ASP A C 1 26 A A +ATOM 170 O O . ASP A 1 26 ? 22.379 32.454 34.651 1.0 96.96 ? ? ? ? ? ? 143 ASP A O 1 26 A A +ATOM 171 C CB . ASP A 1 26 ? 20.312 32.148 32.738 1.0 100.0 ? ? ? ? ? ? 143 ASP A CB 1 26 A A +ATOM 172 C CG . ASP A 1 26 ? 19.880 33.427 32.037 1.0 100.0 ? ? ? ? ? ? 143 ASP A CG 1 26 A A +ATOM 173 O OD1 . ASP A 1 26 ? 20.746 34.102 31.435 1.0 100.0 ? ? ? ? ? ? 143 ASP A OD1 1 26 A A +ATOM 174 O OD2 . ASP A 1 26 ? 18.675 33.756 32.084 1.0 100.0 ? ? ? ? ? ? 143 ASP A OD2 1 26 A A +ATOM 175 N N . ALA A 1 27 ? 23.779 32.993 32.963 1.0 92.92 ? ? ? ? ? ? 144 ALA A N 1 27 A A +ATOM 176 C CA . ALA A 1 27 ? 24.795 33.667 33.771 1.0 94.63 ? ? ? ? ? ? 144 ALA A CA 1 27 A A +ATOM 177 C C . ALA A 1 27 ? 24.384 34.188 35.153 1.0 98.79 ? ? ? ? ? ? 144 ALA A C 1 27 A A +ATOM 178 O O . ALA A 1 27 ? 25.097 33.966 36.132 1.0 100.0 ? ? ? ? ? ? 144 ALA A O 1 27 A A +ATOM 179 C CB . ALA A 1 27 ? 25.413 34.800 32.958 1.0 94.11 ? ? ? ? ? ? 144 ALA A CB 1 27 A A +ATOM 180 N N . ASP A 1 28 ? 23.253 34.884 35.238 1.0 92.37 ? ? ? ? ? ? 145 ASP A N 1 28 A A +ATOM 181 C CA . ASP A 1 28 ? 22.790 35.439 36.517 1.0 86.15 ? ? ? ? ? ? 145 ASP A CA 1 28 A A +ATOM 182 C C . ASP A 1 28 ? 22.543 34.345 37.554 1.0 77.55 ? ? ? ? ? ? 145 ASP A C 1 28 A A +ATOM 183 O O . ASP A 1 28 ? 22.449 34.617 38.752 1.0 75.84 ? ? ? ? ? ? 145 ASP A O 1 28 A A +ATOM 184 C CB . ASP A 1 28 ? 21.504 36.243 36.309 1.0 94.52 ? ? ? ? ? ? 145 ASP A CB 1 28 A A +ATOM 185 C CG . ASP A 1 28 ? 20.351 35.380 35.837 1.0 100.0 ? ? ? ? ? ? 145 ASP A CG 1 28 A A +ATOM 186 O OD1 . ASP A 1 28 ? 20.462 34.782 34.746 1.0 100.0 ? ? ? ? ? ? 145 ASP A OD1 1 28 A A +ATOM 187 O OD2 . ASP A 1 28 ? 19.333 35.297 36.556 1.0 100.0 ? ? ? ? ? ? 145 ASP A OD2 1 28 A A +ATOM 188 N N . HIS A 1 29 ? 22.446 33.106 37.084 1.0 70.06 ? ? ? ? ? ? 146 HIS A N 1 29 A A +ATOM 189 C CA . HIS A 1 29 ? 22.203 31.960 37.951 1.0 70.17 ? ? ? ? ? ? 146 HIS A CA 1 29 A A +ATOM 190 C C . HIS A 1 29 ? 23.421 31.637 38.805 1.0 66.1 ? ? ? ? ? ? 146 HIS A C 1 29 A A +ATOM 191 O O . HIS A 1 29 ? 24.515 31.413 38.289 1.0 69.28 ? ? ? ? ? ? 146 HIS A O 1 29 A A +ATOM 192 C CB . HIS A 1 29 ? 21.826 30.738 37.107 1.0 88.83 ? ? ? ? ? ? 146 HIS A CB 1 29 A A +ATOM 193 C CG . HIS A 1 29 ? 21.565 29.500 37.908 1.0 92.84 ? ? ? ? ? ? 146 HIS A CG 1 29 A A +ATOM 194 N ND1 . HIS A 1 29 ? 22.552 28.842 38.610 1.0 78.79 ? ? ? ? ? ? 146 HIS A ND1 1 29 A A +ATOM 195 C CD2 . HIS A 1 29 ? 20.429 28.786 38.101 1.0 92.7 ? ? ? ? ? ? 146 HIS A CD2 1 29 A A +ATOM 196 C CE1 . HIS A 1 29 ? 22.037 27.778 39.200 1.0 79.37 ? ? ? ? ? ? 146 HIS A CE1 1 29 A A +ATOM 197 N NE2 . HIS A 1 29 ? 20.750 27.722 38.907 1.0 85.27 ? ? ? ? ? ? 146 HIS A NE2 1 29 A A +ATOM 198 N N . PRO A 1 30 ? 23.241 31.612 40.135 1.0 72.24 ? ? ? ? ? ? 147 PRO A N 1 30 A A +ATOM 199 C CA . PRO A 1 30 ? 24.356 31.309 41.039 1.0 76.33 ? ? ? ? ? ? 147 PRO A CA 1 30 A A +ATOM 200 C C . PRO A 1 30 ? 24.838 29.877 40.830 1.0 83.68 ? ? ? ? ? ? 147 PRO A C 1 30 A A +ATOM 201 O O . PRO A 1 30 ? 24.071 28.925 40.966 1.0 100.0 ? ? ? ? ? ? 147 PRO A O 1 30 A A +ATOM 202 C CB . PRO A 1 30 ? 23.767 31.536 42.433 1.0 80.01 ? ? ? ? ? ? 147 PRO A CB 1 30 A A +ATOM 203 C CG . PRO A 1 30 ? 22.295 31.400 42.251 1.0 83.34 ? ? ? ? ? ? 147 PRO A CG 1 30 A A +ATOM 204 C CD . PRO A 1 30 ? 21.984 31.855 40.860 1.0 79.41 ? ? ? ? ? ? 147 PRO A CD 1 30 A A +ATOM 205 N N . GLY A 1 31 ? 26.113 29.732 40.487 1.0 76.43 ? ? ? ? ? ? 148 GLY A N 1 31 A A +ATOM 206 C CA . GLY A 1 31 ? 26.666 28.412 40.249 1.0 74.5 ? ? ? ? ? ? 148 GLY A CA 1 31 A A +ATOM 207 C C . GLY A 1 31 ? 26.874 28.156 38.769 1.0 68.35 ? ? ? ? ? ? 148 GLY A C 1 31 A A +ATOM 208 O O . GLY A 1 31 ? 27.273 27.063 38.367 1.0 69.42 ? ? ? ? ? ? 148 GLY A O 1 31 A A +ATOM 209 N N . PHE A 1 32 ? 26.591 29.171 37.957 1.0 66.68 ? ? ? ? ? ? 149 PHE A N 1 32 A A +ATOM 210 C CA . PHE A 1 32 ? 26.751 29.075 36.511 1.0 79.1 ? ? ? ? ? ? 149 PHE A CA 1 32 A A +ATOM 211 C C . PHE A 1 32 ? 28.222 28.884 36.159 1.0 85.64 ? ? ? ? ? ? 149 PHE A C 1 32 A A +ATOM 212 O O . PHE A 1 32 ? 28.557 28.230 35.173 1.0 87.84 ? ? ? ? ? ? 149 PHE A O 1 32 A A +ATOM 213 C CB . PHE A 1 32 ? 26.213 30.350 35.845 1.0 86.78 ? ? ? ? ? ? 149 PHE A CB 1 32 A A +ATOM 214 C CG . PHE A 1 32 ? 26.459 30.425 34.359 1.0 93.25 ? ? ? ? ? ? 149 PHE A CG 1 32 A A +ATOM 215 C CD1 . PHE A 1 32 ? 25.712 29.654 33.473 1.0 94.59 ? ? ? ? ? ? 149 PHE A CD1 1 32 A A +ATOM 216 C CD2 . PHE A 1 32 ? 27.421 31.288 33.844 1.0 96.74 ? ? ? ? ? ? 149 PHE A CD2 1 32 A A +ATOM 217 C CE1 . PHE A 1 32 ? 25.916 29.745 32.095 1.0 84.73 ? ? ? ? ? ? 149 PHE A CE1 1 32 A A +ATOM 218 C CE2 . PHE A 1 32 ? 27.631 31.385 32.467 1.0 92.82 ? ? ? ? ? ? 149 PHE A CE2 1 32 A A +ATOM 219 C CZ . PHE A 1 32 ? 26.878 30.611 31.594 1.0 85.29 ? ? ? ? ? ? 149 PHE A CZ 1 32 A A +ATOM 220 N N . LYS A 1 33 ? 29.096 29.452 36.983 1.0 87.59 ? ? ? ? ? ? 150 LYS A N 1 33 A A +ATOM 221 C CA . LYS A 1 33 ? 30.534 29.364 36.764 1.0 76.77 ? ? ? ? ? ? 150 LYS A CA 1 33 A A +ATOM 222 C C . LYS A 1 33 ? 31.131 28.107 37.392 1.0 78.87 ? ? ? ? ? ? 150 LYS A C 1 33 A A +ATOM 223 O O . LYS A 1 33 ? 32.307 27.808 37.195 1.0 83.74 ? ? ? ? ? ? 150 LYS A O 1 33 A A +ATOM 224 C CB . LYS A 1 33 ? 31.209 30.611 37.336 1.0 86.37 ? ? ? ? ? ? 150 LYS A CB 1 33 A A +ATOM 225 C CG . LYS A 1 33 ? 30.447 31.895 37.020 1.0 90.4 ? ? ? ? ? ? 150 LYS A CG 1 33 A A +ATOM 226 C CD . LYS A 1 33 ? 31.179 33.139 37.496 1.0 100.0 ? ? ? ? ? ? 150 LYS A CD 1 33 A A +ATOM 227 C CE . LYS A 1 33 ? 30.593 34.392 36.852 1.0 100.0 ? ? ? ? ? ? 150 LYS A CE 1 33 A A +ATOM 228 N NZ . LYS A 1 33 ? 31.333 35.632 37.228 1.0 100.0 ? ? ? ? ? ? 150 LYS A NZ 1 33 A A +ATOM 229 N N . ASP A 1 34 ? 30.315 27.366 38.138 1.0 82.59 ? ? ? ? ? ? 151 ASP A N 1 34 A A +ATOM 230 C CA . ASP A 1 34 ? 30.782 26.148 38.788 1.0 81.68 ? ? ? ? ? ? 151 ASP A CA 1 34 A A +ATOM 231 C C . ASP A 1 34 ? 30.669 24.932 37.877 1.0 75.99 ? ? ? ? ? ? 151 ASP A C 1 34 A A +ATOM 232 O O . ASP A 1 34 ? 29.576 24.423 37.638 1.0 80.97 ? ? ? ? ? ? 151 ASP A O 1 34 A A +ATOM 233 C CB . ASP A 1 34 ? 30.000 25.888 40.076 1.0 81.66 ? ? ? ? ? ? 151 ASP A CB 1 34 A A +ATOM 234 C CG . ASP A 1 34 ? 30.622 24.794 40.917 1.0 87.43 ? ? ? ? ? ? 151 ASP A CG 1 34 A A +ATOM 235 O OD1 . ASP A 1 34 ? 31.089 23.787 40.339 1.0 84.99 ? ? ? ? ? ? 151 ASP A OD1 1 34 A A +ATOM 236 O OD2 . ASP A 1 34 ? 30.645 24.935 42.156 1.0 100.0 ? ? ? ? ? ? 151 ASP A OD2 1 34 A A +ATOM 237 N N . PRO A 1 35 ? 31.812 24.440 37.374 1.0 70.56 ? ? ? ? ? ? 152 PRO A N 1 35 A A +ATOM 238 C CA . PRO A 1 35 ? 31.856 23.277 36.482 1.0 76.86 ? ? ? ? ? ? 152 PRO A CA 1 35 A A +ATOM 239 C C . PRO A 1 35 ? 31.335 21.987 37.109 1.0 79.85 ? ? ? ? ? ? 152 PRO A C 1 35 A A +ATOM 240 O O . PRO A 1 35 ? 30.806 21.123 36.409 1.0 82.69 ? ? ? ? ? ? 152 PRO A O 1 35 A A +ATOM 241 C CB . PRO A 1 35 ? 33.332 23.164 36.094 1.0 87.13 ? ? ? ? ? ? 152 PRO A CB 1 35 A A +ATOM 242 C CG . PRO A 1 35 ? 33.958 24.456 36.513 1.0 88.74 ? ? ? ? ? ? 152 PRO A CG 1 35 A A +ATOM 243 C CD . PRO A 1 35 ? 33.154 24.964 37.659 1.0 82.23 ? ? ? ? ? ? 152 PRO A CD 1 35 A A +ATOM 244 N N . VAL A 1 36 ? 31.490 21.852 38.424 1.0 81.47 ? ? ? ? ? ? 153 VAL A N 1 36 A A +ATOM 245 C CA . VAL A 1 36 ? 31.024 20.654 39.117 1.0 88.21 ? ? ? ? ? ? 153 VAL A CA 1 36 A A +ATOM 246 C C . VAL A 1 36 ? 29.507 20.706 39.261 1.0 90.32 ? ? ? ? ? ? 153 VAL A C 1 36 A A +ATOM 247 O O . VAL A 1 36 ? 28.788 19.938 38.623 1.0 87.73 ? ? ? ? ? ? 153 VAL A O 1 36 A A +ATOM 248 C CB . VAL A 1 36 ? 31.665 20.520 40.525 1.0 82.85 ? ? ? ? ? ? 153 VAL A CB 1 36 A A +ATOM 249 C CG1 . VAL A 1 36 ? 30.909 19.483 41.355 1.0 91.99 ? ? ? ? ? ? 153 VAL A CG1 1 36 A A +ATOM 250 C CG2 . VAL A 1 36 ? 33.122 20.114 40.395 1.0 86.49 ? ? ? ? ? ? 153 VAL A CG2 1 36 A A +ATOM 251 N N . TYR A 1 37 ? 29.033 21.618 40.104 1.0 95.5 ? ? ? ? ? ? 154 TYR A N 1 37 A A +ATOM 252 C CA . TYR A 1 37 ? 27.605 21.797 40.348 1.0 92.74 ? ? ? ? ? ? 154 TYR A CA 1 37 A A +ATOM 253 C C . TYR A 1 37 ? 26.863 21.772 39.021 1.0 80.78 ? ? ? ? ? ? 154 TYR A C 1 37 A A +ATOM 254 O O . TYR A 1 37 ? 25.765 21.228 38.913 1.0 79.24 ? ? ? ? ? ? 154 TYR A O 1 37 A A +ATOM 255 C CB . TYR A 1 37 ? 27.373 23.131 41.067 1.0 100.0 ? ? ? ? ? ? 154 TYR A CB 1 37 A A +ATOM 256 C CG . TYR A 1 37 ? 25.934 23.595 41.119 1.0 100.0 ? ? ? ? ? ? 154 TYR A CG 1 37 A A +ATOM 257 C CD1 . TYR A 1 37 ? 24.968 22.869 41.816 1.0 98.95 ? ? ? ? ? ? 154 TYR A CD1 1 37 A A +ATOM 258 C CD2 . TYR A 1 37 ? 25.544 24.779 40.492 1.0 92.2 ? ? ? ? ? ? 154 TYR A CD2 1 37 A A +ATOM 259 C CE1 . TYR A 1 37 ? 23.648 23.312 41.889 1.0 94.85 ? ? ? ? ? ? 154 TYR A CE1 1 37 A A +ATOM 260 C CE2 . TYR A 1 37 ? 24.227 25.229 40.558 1.0 95.72 ? ? ? ? ? ? 154 TYR A CE2 1 37 A A +ATOM 261 C CZ . TYR A 1 37 ? 23.287 24.494 41.259 1.0 95.18 ? ? ? ? ? ? 154 TYR A CZ 1 37 A A +ATOM 262 O OH . TYR A 1 37 ? 21.993 24.949 41.335 1.0 100.0 ? ? ? ? ? ? 154 TYR A OH 1 37 A A +ATOM 263 N N . ARG A 1 38 ? 27.481 22.370 38.013 1.0 62.91 ? ? ? ? ? ? 155 ARG A N 1 38 A A +ATOM 264 C CA . ARG A 1 38 ? 26.907 22.414 36.679 1.0 59.41 ? ? ? ? ? ? 155 ARG A CA 1 38 A A +ATOM 265 C C . ARG A 1 38 ? 26.650 20.991 36.184 1.0 55.79 ? ? ? ? ? ? 155 ARG A C 1 38 A A +ATOM 266 O O . ARG A 1 38 ? 25.505 20.599 35.949 1.0 65.02 ? ? ? ? ? ? 155 ARG A O 1 38 A A +ATOM 267 C CB . ARG A 1 38 ? 27.872 23.121 35.732 1.0 59.75 ? ? ? ? ? ? 155 ARG A CB 1 38 A A +ATOM 268 C CG . ARG A 1 38 ? 27.245 23.666 34.473 1.0 68.07 ? ? ? ? ? ? 155 ARG A CG 1 38 A A +ATOM 269 C CD . ARG A 1 38 ? 28.304 24.336 33.625 1.0 79.8 ? ? ? ? ? ? 155 ARG A CD 1 38 A A +ATOM 270 N NE . ARG A 1 38 ? 27.785 24.801 32.344 1.0 93.15 ? ? ? ? ? ? 155 ARG A NE 1 38 A A +ATOM 271 C CZ . ARG A 1 38 ? 27.704 26.081 31.996 1.0 98.65 ? ? ? ? ? ? 155 ARG A CZ 1 38 A A +ATOM 272 N NH1 . ARG A 1 38 ? 28.107 27.023 32.836 1.0 99.79 ? ? ? ? ? ? 155 ARG A NH1 1 38 A A +ATOM 273 N NH2 . ARG A 1 38 ? 27.230 26.421 30.804 1.0 100.0 ? ? ? ? ? ? 155 ARG A NH2 1 38 A A +ATOM 274 N N . ALA A 1 39 ? 27.727 20.226 36.024 1.0 47.55 ? ? ? ? ? ? 156 ALA A N 1 39 A A +ATOM 275 C CA . ALA A 1 39 ? 27.642 18.848 35.552 1.0 43.67 ? ? ? ? ? ? 156 ALA A CA 1 39 A A +ATOM 276 C C . ALA A 1 39 ? 26.852 17.981 36.524 1.0 48.1 ? ? ? ? ? ? 156 ALA A C 1 39 A A +ATOM 277 O O . ALA A 1 39 ? 26.384 16.897 36.172 1.0 40.44 ? ? ? ? ? ? 156 ALA A O 1 39 A A +ATOM 278 C CB . ALA A 1 39 ? 29.038 18.280 35.364 1.0 58.64 ? ? ? ? ? ? 156 ALA A CB 1 39 A A +ATOM 279 N N . ARG A 1 40 ? 26.725 18.451 37.759 1.0 52.11 ? ? ? ? ? ? 157 ARG A N 1 40 A A +ATOM 280 C CA . ARG A 1 40 ? 25.975 17.717 38.764 1.0 51.03 ? ? ? ? ? ? 157 ARG A CA 1 40 A A +ATOM 281 C C . ARG A 1 40 ? 24.493 17.868 38.439 1.0 53.36 ? ? ? ? ? ? 157 ARG A C 1 40 A A +ATOM 282 O O . ARG A 1 40 ? 23.746 16.890 38.447 1.0 43.4 ? ? ? ? ? ? 157 ARG A O 1 40 A A +ATOM 283 C CB . ARG A 1 40 ? 26.265 18.278 40.160 1.0 38.02 ? ? ? ? ? ? 157 ARG A CB 1 40 A A +ATOM 284 C CG . ARG A 1 40 ? 25.354 17.749 41.247 1.0 41.41 ? ? ? ? ? ? 157 ARG A CG 1 40 A A +ATOM 285 C CD . ARG A 1 40 ? 25.845 16.412 41.749 1.0 44.18 ? ? ? ? ? ? 157 ARG A CD 1 40 A A +ATOM 286 N NE . ARG A 1 40 ? 25.289 16.082 43.058 1.0 39.11 ? ? ? ? ? ? 157 ARG A NE 1 40 A A +ATOM 287 C CZ . ARG A 1 40 ? 25.229 14.849 43.553 1.0 47.49 ? ? ? ? ? ? 157 ARG A CZ 1 40 A A +ATOM 288 N NH1 . ARG A 1 40 ? 25.692 13.824 42.847 1.0 44.14 ? ? ? ? ? ? 157 ARG A NH1 1 40 A A +ATOM 289 N NH2 . ARG A 1 40 ? 24.706 14.639 44.753 1.0 31.56 ? ? ? ? ? ? 157 ARG A NH2 1 40 A A +ATOM 290 N N . ARG A 1 41 ? 24.084 19.101 38.139 1.0 46.66 ? ? ? ? ? ? 158 ARG A N 1 41 A A +ATOM 291 C CA . ARG A 1 41 ? 22.692 19.401 37.816 1.0 53.07 ? ? ? ? ? ? 158 ARG A CA 1 41 A A +ATOM 292 C C . ARG A 1 41 ? 22.279 18.807 36.477 1.0 50.94 ? ? ? ? ? ? 158 ARG A C 1 41 A A +ATOM 293 O O . ARG A 1 41 ? 21.092 18.699 36.178 1.0 77.16 ? ? ? ? ? ? 158 ARG A O 1 41 A A +ATOM 294 C CB . ARG A 1 41 ? 22.465 20.915 37.807 1.0 58.71 ? ? ? ? ? ? 158 ARG A CB 1 41 A A +ATOM 295 C CG . ARG A 1 41 ? 20.996 21.313 37.798 1.0 73.28 ? ? ? ? ? ? 158 ARG A CG 1 41 A A +ATOM 296 C CD . ARG A 1 41 ? 20.800 22.746 38.262 1.0 52.26 ? ? ? ? ? ? 158 ARG A CD 1 41 A A +ATOM 297 N NE . ARG A 1 41 ? 19.541 23.305 37.772 1.0 66.0 ? ? ? ? ? ? 158 ARG A NE 1 41 A A +ATOM 298 C CZ . ARG A 1 41 ? 18.999 24.434 38.216 1.0 73.11 ? ? ? ? ? ? 158 ARG A CZ 1 41 A A +ATOM 299 N NH1 . ARG A 1 41 ? 19.600 25.134 39.167 1.0 77.08 ? ? ? ? ? ? 158 ARG A NH1 1 41 A A +ATOM 300 N NH2 . ARG A 1 41 ? 17.848 24.863 37.715 1.0 79.76 ? ? ? ? ? ? 158 ARG A NH2 1 41 A A +ATOM 301 N N . LYS A 1 42 ? 23.267 18.443 35.668 1.0 46.7 ? ? ? ? ? ? 159 LYS A N 1 42 A A +ATOM 302 C CA . LYS A 1 42 ? 23.013 17.837 34.366 1.0 49.83 ? ? ? ? ? ? 159 LYS A CA 1 42 A A +ATOM 303 C C . LYS A 1 42 ? 22.877 16.342 34.612 1.0 46.38 ? ? ? ? ? ? 159 LYS A C 1 42 A A +ATOM 304 O O . LYS A 1 42 ? 22.287 15.609 33.822 1.0 52.99 ? ? ? ? ? ? 159 LYS A O 1 42 A A +ATOM 305 C CB . LYS A 1 42 ? 24.184 18.105 33.422 1.0 70.21 ? ? ? ? ? ? 159 LYS A CB 1 42 A A +ATOM 306 C CG . LYS A 1 42 ? 24.115 17.340 32.116 1.0 82.3 ? ? ? ? ? ? 159 LYS A CG 1 42 A A +ATOM 307 C CD . LYS A 1 42 ? 25.243 17.756 31.189 1.0 91.14 ? ? ? ? ? ? 159 LYS A CD 1 42 A A +ATOM 308 C CE . LYS A 1 42 ? 25.069 17.172 29.795 1.0 92.35 ? ? ? ? ? ? 159 LYS A CE 1 42 A A +ATOM 309 N NZ . LYS A 1 42 ? 26.072 17.722 28.838 1.0 100.0 ? ? ? ? ? ? 159 LYS A NZ 1 42 A A +ATOM 310 N N . GLN A 1 43 ? 23.442 15.910 35.732 1.0 40.78 ? ? ? ? ? ? 160 GLN A N 1 43 A A +ATOM 311 C CA . GLN A 1 43 ? 23.414 14.521 36.160 1.0 42.9 ? ? ? ? ? ? 160 GLN A CA 1 43 A A +ATOM 312 C C . GLN A 1 43 ? 21.995 14.224 36.609 1.0 45.11 ? ? ? ? ? ? 160 GLN A C 1 43 A A +ATOM 313 O O . GLN A 1 43 ? 21.417 13.187 36.281 1.0 54.18 ? ? ? ? ? ? 160 GLN A O 1 43 A A +ATOM 314 C CB . GLN A 1 43 ? 24.373 14.348 37.333 1.0 52.45 ? ? ? ? ? ? 160 GLN A CB 1 43 A A +ATOM 315 C CG . GLN A 1 43 ? 24.724 12.933 37.672 1.0 46.55 ? ? ? ? ? ? 160 GLN A CG 1 43 A A +ATOM 316 C CD . GLN A 1 43 ? 25.879 12.875 38.639 1.0 56.61 ? ? ? ? ? ? 160 GLN A CD 1 43 A A +ATOM 317 O OE1 . GLN A 1 43 ? 26.249 13.885 39.237 1.0 57.95 ? ? ? ? ? ? 160 GLN A OE1 1 43 A A +ATOM 318 N NE2 . GLN A 1 43 ? 26.463 11.696 38.795 1.0 56.32 ? ? ? ? ? ? 160 GLN A NE2 1 43 A A +ATOM 319 N N . PHE A 1 44 ? 21.444 15.156 37.376 1.0 45.78 ? ? ? ? ? ? 161 PHE A N 1 44 A A +ATOM 320 C CA . PHE A 1 44 ? 20.092 15.029 37.885 1.0 51.09 ? ? ? ? ? ? 161 PHE A CA 1 44 A A +ATOM 321 C C . PHE A 1 44 ? 19.106 15.022 36.715 1.0 55.48 ? ? ? ? ? ? 161 PHE A C 1 44 A A +ATOM 322 O O . PHE A 1 44 ? 18.252 14.139 36.621 1.0 55.24 ? ? ? ? ? ? 161 PHE A O 1 44 A A +ATOM 323 C CB . PHE A 1 44 ? 19.778 16.192 38.832 1.0 49.99 ? ? ? ? ? ? 161 PHE A CB 1 44 A A +ATOM 324 C CG . PHE A 1 44 ? 20.428 16.073 40.185 1.0 43.25 ? ? ? ? ? ? 161 PHE A CG 1 44 A A +ATOM 325 C CD1 . PHE A 1 44 ? 21.244 17.090 40.666 1.0 52.12 ? ? ? ? ? ? 161 PHE A CD1 1 44 A A +ATOM 326 C CD2 . PHE A 1 44 ? 20.215 14.952 40.983 1.0 46.64 ? ? ? ? ? ? 161 PHE A CD2 1 44 A A +ATOM 327 C CE1 . PHE A 1 44 ? 21.841 16.997 41.919 1.0 64.08 ? ? ? ? ? ? 161 PHE A CE1 1 44 A A +ATOM 328 C CE2 . PHE A 1 44 ? 20.808 14.845 42.242 1.0 59.01 ? ? ? ? ? ? 161 PHE A CE2 1 44 A A +ATOM 329 C CZ . PHE A 1 44 ? 21.622 15.872 42.710 1.0 72.77 ? ? ? ? ? ? 161 PHE A CZ 1 44 A A +ATOM 330 N N . ALA A 1 45 ? 19.236 16.003 35.824 1.0 53.32 ? ? ? ? ? ? 162 ALA A N 1 45 A A +ATOM 331 C CA . ALA A 1 45 ? 18.357 16.113 34.661 1.0 50.06 ? ? ? ? ? ? 162 ALA A CA 1 45 A A +ATOM 332 C C . ALA A 1 45 ? 18.314 14.825 33.846 1.0 43.46 ? ? ? ? ? ? 162 ALA A C 1 45 A A +ATOM 333 O O . ALA A 1 45 ? 17.244 14.374 33.438 1.0 46.93 ? ? ? ? ? ? 162 ALA A O 1 45 A A +ATOM 334 C CB . ALA A 1 45 ? 18.806 17.269 33.777 1.0 22.2 ? ? ? ? ? ? 162 ALA A CB 1 45 A A +ATOM 335 N N . ASP A 1 46 ? 19.482 14.239 33.607 1.0 37.62 ? ? ? ? ? ? 163 ASP A N 1 46 A A +ATOM 336 C CA . ASP A 1 46 ? 19.575 13.006 32.837 1.0 55.82 ? ? ? ? ? ? 163 ASP A CA 1 46 A A +ATOM 337 C C . ASP A 1 46 ? 18.737 11.924 33.499 1.0 55.29 ? ? ? ? ? ? 163 ASP A C 1 46 A A +ATOM 338 O O . ASP A 1 46 ? 18.116 11.104 32.820 1.0 55.64 ? ? ? ? ? ? 163 ASP A O 1 46 A A +ATOM 339 C CB . ASP A 1 46 ? 21.033 12.546 32.742 1.0 73.47 ? ? ? ? ? ? 163 ASP A CB 1 46 A A +ATOM 340 C CG . ASP A 1 46 ? 21.755 13.130 31.541 1.0 88.52 ? ? ? ? ? ? 163 ASP A CG 1 46 A A +ATOM 341 O OD1 . ASP A 1 46 ? 21.558 12.618 30.418 1.0 86.66 ? ? ? ? ? ? 163 ASP A OD1 1 46 A A +ATOM 342 O OD2 . ASP A 1 46 ? 22.525 14.098 31.724 1.0 100.0 ? ? ? ? ? ? 163 ASP A OD2 1 46 A A +ATOM 343 N N . ILE A 1 47 ? 18.730 11.918 34.829 1.0 54.93 ? ? ? ? ? ? 164 ILE A N 1 47 A A +ATOM 344 C CA . ILE A 1 47 ? 17.948 10.931 35.569 1.0 54.88 ? ? ? ? ? ? 164 ILE A CA 1 47 A A +ATOM 345 C C . ILE A 1 47 ? 16.504 11.062 35.104 1.0 49.54 ? ? ? ? ? ? 164 ILE A C 1 47 A A +ATOM 346 O O . ILE A 1 47 ? 15.835 10.066 34.823 1.0 36.54 ? ? ? ? ? ? 164 ILE A O 1 47 A A +ATOM 347 C CB . ILE A 1 47 ? 17.994 11.183 37.099 1.0 59.6 ? ? ? ? ? ? 164 ILE A CB 1 47 A A +ATOM 348 C CG1 . ILE A 1 47 ? 19.398 10.914 37.648 1.0 68.7 ? ? ? ? ? ? 164 ILE A CG1 1 47 A A +ATOM 349 C CG2 . ILE A 1 47 ? 17.004 10.274 37.801 1.0 56.46 ? ? ? ? ? ? 164 ILE A CG2 1 47 A A +ATOM 350 C CD1 . ILE A 1 47 ? 19.594 11.372 39.084 1.0 53.83 ? ? ? ? ? ? 164 ILE A CD1 1 47 A A +ATOM 351 N N . ALA A 1 48 ? 16.046 12.310 35.022 1.0 43.8 ? ? ? ? ? ? 165 ALA A N 1 48 A A +ATOM 352 C CA . ALA A 1 48 ? 14.686 12.633 34.598 1.0 42.24 ? ? ? ? ? ? 165 ALA A CA 1 48 A A +ATOM 353 C C . ALA A 1 48 ? 14.406 12.121 33.193 1.0 44.69 ? ? ? ? ? ? 165 ALA A C 1 48 A A +ATOM 354 O O . ALA A 1 48 ? 13.435 11.402 32.965 1.0 61.71 ? ? ? ? ? ? 165 ALA A O 1 48 A A +ATOM 355 C CB . ALA A 1 48 ? 14.467 14.148 34.654 1.0 26.07 ? ? ? ? ? ? 165 ALA A CB 1 48 A A +ATOM 356 N N . TYR A 1 49 ? 15.265 12.493 32.253 1.0 43.01 ? ? ? ? ? ? 166 TYR A N 1 49 A A +ATOM 357 C CA . TYR A 1 49 ? 15.113 12.080 30.866 1.0 31.65 ? ? ? ? ? ? 166 TYR A CA 1 49 A A +ATOM 358 C C . TYR A 1 49 ? 15.043 10.564 30.707 1.0 45.23 ? ? ? ? ? ? 166 TYR A C 1 49 A A +ATOM 359 O O . TYR A 1 49 ? 14.423 10.061 29.770 1.0 46.7 ? ? ? ? ? ? 166 TYR A O 1 49 A A +ATOM 360 C CB . TYR A 1 49 ? 16.273 12.626 30.037 1.0 40.4 ? ? ? ? ? ? 166 TYR A CB 1 49 A A +ATOM 361 C CG . TYR A 1 49 ? 16.327 14.131 29.984 1.0 45.05 ? ? ? ? ? ? 166 TYR A CG 1 49 A A +ATOM 362 C CD1 . TYR A 1 49 ? 17.503 14.817 30.274 1.0 46.24 ? ? ? ? ? ? 166 TYR A CD1 1 49 A A +ATOM 363 C CD2 . TYR A 1 49 ? 15.205 14.871 29.628 1.0 48.86 ? ? ? ? ? ? 166 TYR A CD2 1 49 A A +ATOM 364 C CE1 . TYR A 1 49 ? 17.561 16.205 30.205 1.0 53.79 ? ? ? ? ? ? 166 TYR A CE1 1 49 A A +ATOM 365 C CE2 . TYR A 1 49 ? 15.250 16.257 29.556 1.0 47.99 ? ? ? ? ? ? 166 TYR A CE2 1 49 A A +ATOM 366 C CZ . TYR A 1 49 ? 16.430 16.919 29.845 1.0 51.43 ? ? ? ? ? ? 166 TYR A CZ 1 49 A A +ATOM 367 O OH . TYR A 1 49 ? 16.480 18.293 29.753 1.0 60.63 ? ? ? ? ? ? 166 TYR A OH 1 49 A A +ATOM 368 N N . ASN A 1 50 ? 15.679 9.840 31.623 1.0 54.06 ? ? ? ? ? ? 167 ASN A N 1 50 A A +ATOM 369 C CA . ASN A 1 50 ? 15.696 8.382 31.566 1.0 65.84 ? ? ? ? ? ? 167 ASN A CA 1 50 A A +ATOM 370 C C . ASN A 1 50 ? 14.576 7.741 32.365 1.0 62.84 ? ? ? ? ? ? 167 ASN A C 1 50 A A +ATOM 371 O O . ASN A 1 50 ? 14.321 6.543 32.241 1.0 73.35 ? ? ? ? ? ? 167 ASN A O 1 50 A A +ATOM 372 C CB . ASN A 1 50 ? 17.032 7.854 32.081 1.0 72.59 ? ? ? ? ? ? 167 ASN A CB 1 50 A A +ATOM 373 C CG . ASN A 1 50 ? 18.197 8.315 31.244 1.0 72.14 ? ? ? ? ? ? 167 ASN A CG 1 50 A A +ATOM 374 O OD1 . ASN A 1 50 ? 18.230 8.095 30.033 1.0 80.82 ? ? ? ? ? ? 167 ASN A OD1 1 50 A A +ATOM 375 N ND2 . ASN A 1 50 ? 19.165 8.963 31.882 1.0 83.09 ? ? ? ? ? ? 167 ASN A ND2 1 50 A A +ATOM 376 N N . TYR A 1 51 ? 13.906 8.536 33.187 1.0 49.39 ? ? ? ? ? ? 168 TYR A N 1 51 A A +ATOM 377 C CA . TYR A 1 51 ? 12.830 8.010 34.011 1.0 39.76 ? ? ? ? ? ? 168 TYR A CA 1 51 A A +ATOM 378 C C . TYR A 1 51 ? 11.525 7.769 33.266 1.0 42.3 ? ? ? ? ? ? 168 TYR A C 1 51 A A +ATOM 379 O O . TYR A 1 51 ? 10.976 8.668 32.626 1.0 58.64 ? ? ? ? ? ? 168 TYR A O 1 51 A A +ATOM 380 C CB . TYR A 1 51 ? 12.553 8.939 35.194 1.0 46.65 ? ? ? ? ? ? 168 TYR A CB 1 51 A A +ATOM 381 C CG . TYR A 1 51 ? 11.500 8.389 36.120 1.0 39.97 ? ? ? ? ? ? 168 TYR A CG 1 51 A A +ATOM 382 C CD1 . TYR A 1 51 ? 11.800 7.353 36.998 1.0 66.54 ? ? ? ? ? ? 168 TYR A CD1 1 51 A A +ATOM 383 C CD2 . TYR A 1 51 ? 10.191 8.858 36.074 1.0 54.93 ? ? ? ? ? ? 168 TYR A CD2 1 51 A A +ATOM 384 C CE1 . TYR A 1 51 ? 10.828 6.796 37.808 1.0 67.76 ? ? ? ? ? ? 168 TYR A CE1 1 51 A A +ATOM 385 C CE2 . TYR A 1 51 ? 9.207 8.309 36.881 1.0 61.72 ? ? ? ? ? ? 168 TYR A CE2 1 51 A A +ATOM 386 C CZ . TYR A 1 51 ? 9.533 7.274 37.741 1.0 65.89 ? ? ? ? ? ? 168 TYR A CZ 1 51 A A +ATOM 387 O OH . TYR A 1 51 ? 8.566 6.712 38.537 1.0 88.35 ? ? ? ? ? ? 168 TYR A OH 1 51 A A +ATOM 388 N N . ARG A 1 52 ? 11.034 6.540 33.358 1.0 32.96 ? ? ? ? ? ? 169 ARG A N 1 52 A A +ATOM 389 C CA . ARG A 1 52 ? 9.777 6.170 32.732 1.0 40.34 ? ? ? ? ? ? 169 ARG A CA 1 52 A A +ATOM 390 C C . ARG A 1 52 ? 8.838 5.723 33.849 1.0 47.72 ? ? ? ? ? ? 169 ARG A C 1 52 A A +ATOM 391 O O . ARG A 1 52 ? 9.260 5.068 34.803 1.0 59.03 ? ? ? ? ? ? 169 ARG A O 1 52 A A +ATOM 392 C CB . ARG A 1 52 ? 9.992 5.039 31.729 1.0 41.42 ? ? ? ? ? ? 169 ARG A CB 1 52 A A +ATOM 393 C CG . ARG A 1 52 ? 10.123 5.510 30.292 1.0 58.13 ? ? ? ? ? ? 169 ARG A CG 1 52 A A +ATOM 394 C CD . ARG A 1 52 ? 11.442 6.225 30.063 1.0 63.85 ? ? ? ? ? ? 169 ARG A CD 1 52 A A +ATOM 395 N NE . ARG A 1 52 ? 11.604 6.646 28.674 1.0 72.67 ? ? ? ? ? ? 169 ARG A NE 1 52 A A +ATOM 396 C CZ . ARG A 1 52 ? 11.664 7.914 28.280 1.0 77.19 ? ? ? ? ? ? 169 ARG A CZ 1 52 A A +ATOM 397 N NH1 . ARG A 1 52 ? 11.575 8.888 29.173 1.0 77.86 ? ? ? ? ? ? 169 ARG A NH1 1 52 A A +ATOM 398 N NH2 . ARG A 1 52 ? 11.808 8.210 26.995 1.0 77.36 ? ? ? ? ? ? 169 ARG A NH2 1 52 A A +ATOM 399 N N . HIS A 1 53 ? 7.569 6.092 33.731 1.0 42.46 ? ? ? ? ? ? 170 HIS A N 1 53 A A +ATOM 400 C CA . HIS A 1 53 ? 6.571 5.746 34.733 1.0 40.05 ? ? ? ? ? ? 170 HIS A CA 1 53 A A +ATOM 401 C C . HIS A 1 53 ? 6.577 4.261 35.060 1.0 45.75 ? ? ? ? ? ? 170 HIS A C 1 53 A A +ATOM 402 O O . HIS A 1 53 ? 6.906 3.426 34.217 1.0 46.56 ? ? ? ? ? ? 170 HIS A O 1 53 A A +ATOM 403 C CB . HIS A 1 53 ? 5.178 6.164 34.245 1.0 51.11 ? ? ? ? ? ? 170 HIS A CB 1 53 A A +ATOM 404 C CG . HIS A 1 53 ? 4.058 5.693 35.120 1.0 53.11 ? ? ? ? ? ? 170 HIS A CG 1 53 A A +ATOM 405 N ND1 . HIS A 1 53 ? 3.605 6.414 36.205 1.0 37.55 ? ? ? ? ? ? 170 HIS A ND1 1 53 A A +ATOM 406 C CD2 . HIS A 1 53 ? 3.295 4.576 35.067 1.0 48.78 ? ? ? ? ? ? 170 HIS A CD2 1 53 A A +ATOM 407 C CE1 . HIS A 1 53 ? 2.612 5.760 36.780 1.0 46.68 ? ? ? ? ? ? 170 HIS A CE1 1 53 A A +ATOM 408 N NE2 . HIS A 1 53 ? 2.404 4.642 36.110 1.0 39.31 ? ? ? ? ? ? 170 HIS A NE2 1 53 A A +ATOM 409 N N . GLY A 1 54 ? 6.217 3.944 36.300 1.0 41.41 ? ? ? ? ? ? 171 GLY A N 1 54 A A +ATOM 410 C CA . GLY A 1 54 ? 6.166 2.558 36.725 1.0 62.11 ? ? ? ? ? ? 171 GLY A CA 1 54 A A +ATOM 411 C C . GLY A 1 54 ? 7.376 2.091 37.504 1.0 65.87 ? ? ? ? ? ? 171 GLY A C 1 54 A A +ATOM 412 O O . GLY A 1 54 ? 7.246 1.311 38.448 1.0 78.15 ? ? ? ? ? ? 171 GLY A O 1 54 A A +ATOM 413 N N . GLN A 1 55 ? 8.555 2.558 37.107 1.0 71.98 ? ? ? ? ? ? 172 GLN A N 1 55 A A +ATOM 414 C CA . GLN A 1 55 ? 9.789 2.172 37.777 1.0 75.85 ? ? ? ? ? ? 172 GLN A CA 1 55 A A +ATOM 415 C C . GLN A 1 55 ? 10.080 3.109 38.937 1.0 69.09 ? ? ? ? ? ? 172 GLN A C 1 55 A A +ATOM 416 O O . GLN A 1 55 ? 9.745 4.292 38.887 1.0 64.34 ? ? ? ? ? ? 172 GLN A O 1 55 A A +ATOM 417 C CB . GLN A 1 55 ? 10.956 2.201 36.793 1.0 77.26 ? ? ? ? ? ? 172 GLN A CB 1 55 A A +ATOM 418 C CG . GLN A 1 55 ? 11.248 3.578 36.238 1.0 59.13 ? ? ? ? ? ? 172 GLN A CG 1 55 A A +ATOM 419 C CD . GLN A 1 55 ? 11.848 3.517 34.856 1.0 53.97 ? ? ? ? ? ? 172 GLN A CD 1 55 A A +ATOM 420 O OE1 . GLN A 1 55 ? 12.781 4.251 34.538 1.0 56.19 ? ? ? ? ? ? 172 GLN A OE1 1 55 A A +ATOM 421 N NE2 . GLN A 1 55 ? 11.312 2.637 34.019 1.0 58.99 ? ? ? ? ? ? 172 GLN A NE2 1 55 A A +ATOM 422 N N . PRO A 1 56 ? 10.721 2.591 39.996 1.0 60.1 ? ? ? ? ? ? 173 PRO A N 1 56 A A +ATOM 423 C CA . PRO A 1 56 ? 11.038 3.425 41.161 1.0 51.4 ? ? ? ? ? ? 173 PRO A CA 1 56 A A +ATOM 424 C C . PRO A 1 56 ? 12.004 4.565 40.838 1.0 46.66 ? ? ? ? ? ? 173 PRO A C 1 56 A A +ATOM 425 O O . PRO A 1 56 ? 12.923 4.410 40.032 1.0 48.13 ? ? ? ? ? ? 173 PRO A O 1 56 A A +ATOM 426 C CB . PRO A 1 56 ? 11.611 2.430 42.172 1.0 56.78 ? ? ? ? ? ? 173 PRO A CB 1 56 A A +ATOM 427 C CG . PRO A 1 56 ? 12.072 1.269 41.354 1.0 66.08 ? ? ? ? ? ? 173 PRO A CG 1 56 A A +ATOM 428 C CD . PRO A 1 56 ? 11.186 1.201 40.155 1.0 57.41 ? ? ? ? ? ? 173 PRO A CD 1 56 A A +ATOM 429 N N . ILE A 1 57 ? 11.780 5.717 41.463 1.0 46.86 ? ? ? ? ? ? 174 ILE A N 1 57 A A +ATOM 430 C CA . ILE A 1 57 ? 12.637 6.870 41.246 1.0 58.88 ? ? ? ? ? ? 174 ILE A CA 1 57 A A +ATOM 431 C C . ILE A 1 57 ? 14.035 6.548 41.758 1.0 66.24 ? ? ? ? ? ? 174 ILE A C 1 57 A A +ATOM 432 O O . ILE A 1 57 ? 14.212 6.191 42.920 1.0 67.03 ? ? ? ? ? ? 174 ILE A O 1 57 A A +ATOM 433 C CB . ILE A 1 57 ? 12.102 8.109 41.994 1.0 53.24 ? ? ? ? ? ? 174 ILE A CB 1 57 A A +ATOM 434 C CG1 . ILE A 1 57 ? 10.598 8.242 41.775 1.0 38.78 ? ? ? ? ? ? 174 ILE A CG1 1 57 A A +ATOM 435 C CG2 . ILE A 1 57 ? 12.822 9.361 41.515 1.0 41.47 ? ? ? ? ? ? 174 ILE A CG2 1 57 A A +ATOM 436 C CD1 . ILE A 1 57 ? 9.949 9.287 42.655 1.0 52.33 ? ? ? ? ? ? 174 ILE A CD1 1 57 A A +ATOM 437 N N . PRO A 1 58 ? 15.048 6.650 40.883 1.0 69.49 ? ? ? ? ? ? 175 PRO A N 1 58 A A +ATOM 438 C CA . PRO A 1 58 ? 16.428 6.357 41.294 1.0 70.55 ? ? ? ? ? ? 175 PRO A CA 1 58 A A +ATOM 439 C C . PRO A 1 58 ? 16.886 7.184 42.493 1.0 70.56 ? ? ? ? ? ? 175 PRO A C 1 58 A A +ATOM 440 O O . PRO A 1 58 ? 16.562 8.367 42.602 1.0 61.0 ? ? ? ? ? ? 175 PRO A O 1 58 A A +ATOM 441 C CB . PRO A 1 58 ? 17.258 6.655 40.039 1.0 61.75 ? ? ? ? ? ? 175 PRO A CB 1 58 A A +ATOM 442 C CG . PRO A 1 58 ? 16.354 7.459 39.151 1.0 44.44 ? ? ? ? ? ? 175 PRO A CG 1 58 A A +ATOM 443 C CD . PRO A 1 58 ? 14.962 7.035 39.465 1.0 50.89 ? ? ? ? ? ? 175 PRO A CD 1 58 A A +ATOM 444 N N . ARG A 1 59 ? 17.643 6.555 43.390 1.0 68.23 ? ? ? ? ? ? 176 ARG A N 1 59 A A +ATOM 445 C CA . ARG A 1 59 ? 18.141 7.246 44.572 1.0 66.01 ? ? ? ? ? ? 176 ARG A CA 1 59 A A +ATOM 446 C C . ARG A 1 59 ? 19.476 7.902 44.255 1.0 55.42 ? ? ? ? ? ? 176 ARG A C 1 59 A A +ATOM 447 O O . ARG A 1 59 ? 20.184 7.475 43.344 1.0 55.67 ? ? ? ? ? ? 176 ARG A O 1 59 A A +ATOM 448 C CB . ARG A 1 59 ? 18.301 6.267 45.741 1.0 71.12 ? ? ? ? ? ? 176 ARG A CB 1 59 A A +ATOM 449 C CG . ARG A 1 59 ? 17.013 5.555 46.130 1.0 70.25 ? ? ? ? ? ? 176 ARG A CG 1 59 A A +ATOM 450 C CD . ARG A 1 59 ? 17.253 4.516 47.208 1.0 58.5 ? ? ? ? ? ? 176 ARG A CD 1 59 A A +ATOM 451 N NE . ARG A 1 59 ? 16.128 4.439 48.130 1.0 69.14 ? ? ? ? ? ? 176 ARG A NE 1 59 A A +ATOM 452 C CZ . ARG A 1 59 ? 16.062 5.092 49.284 1.0 65.87 ? ? ? ? ? ? 176 ARG A CZ 1 59 A A +ATOM 453 N NH1 . ARG A 1 59 ? 17.060 5.878 49.664 1.0 64.13 ? ? ? ? ? ? 176 ARG A NH1 1 59 A A +ATOM 454 N NH2 . ARG A 1 59 ? 14.995 4.961 50.057 1.0 57.7 ? ? ? ? ? ? 176 ARG A NH2 1 59 A A +ATOM 455 N N . VAL A 1 60 ? 19.811 8.943 45.009 1.0 40.96 ? ? ? ? ? ? 177 VAL A N 1 60 A A +ATOM 456 C CA . VAL A 1 60 ? 21.058 9.663 44.794 1.0 58.52 ? ? ? ? ? ? 177 VAL A CA 1 60 A A +ATOM 457 C C . VAL A 1 60 ? 21.813 9.916 46.099 1.0 60.43 ? ? ? ? ? ? 177 VAL A C 1 60 A A +ATOM 458 O O . VAL A 1 60 ? 21.211 10.135 47.151 1.0 62.67 ? ? ? ? ? ? 177 VAL A O 1 60 A A +ATOM 459 C CB . VAL A 1 60 ? 20.798 11.020 44.091 1.0 61.33 ? ? ? ? ? ? 177 VAL A CB 1 60 A A +ATOM 460 C CG1 . VAL A 1 60 ? 22.079 11.829 44.017 1.0 83.94 ? ? ? ? ? ? 177 VAL A CG1 1 60 A A +ATOM 461 C CG2 . VAL A 1 60 ? 20.247 10.788 42.698 1.0 53.69 ? ? ? ? ? ? 177 VAL A CG2 1 60 A A +ATOM 462 N N . GLU A 1 61 ? 23.139 9.880 46.013 1.0 45.91 ? ? ? ? ? ? 178 GLU A N 1 61 A A +ATOM 463 C CA . GLU A 1 61 ? 24.004 10.112 47.158 1.0 49.76 ? ? ? ? ? ? 178 GLU A CA 1 61 A A +ATOM 464 C C . GLU A 1 61 ? 24.393 11.590 47.191 1.0 52.05 ? ? ? ? ? ? 178 GLU A C 1 61 A A +ATOM 465 O O . GLU A 1 61 ? 25.411 11.986 46.626 1.0 55.89 ? ? ? ? ? ? 178 GLU A O 1 61 A A +ATOM 466 C CB . GLU A 1 61 ? 25.258 9.241 47.040 1.0 52.19 ? ? ? ? ? ? 178 GLU A CB 1 61 A A +ATOM 467 C CG . GLU A 1 61 ? 25.816 8.754 48.368 1.0 71.52 ? ? ? ? ? ? 178 GLU A CG 1 61 A A +ATOM 468 C CD . GLU A 1 61 ? 26.864 7.659 48.199 1.0 84.05 ? ? ? ? ? ? 178 GLU A CD 1 61 A A +ATOM 469 O OE1 . GLU A 1 61 ? 28.008 7.976 47.796 1.0 85.57 ? ? ? ? ? ? 178 GLU A OE1 1 61 A A +ATOM 470 O OE2 . GLU A 1 61 ? 26.544 6.479 48.467 1.0 80.92 ? ? ? ? ? ? 178 GLU A OE2 1 61 A A +ATOM 471 N N . TYR A 1 62 ? 23.577 12.404 47.851 1.0 48.56 ? ? ? ? ? ? 179 TYR A N 1 62 A A +ATOM 472 C CA . TYR A 1 62 ? 23.836 13.839 47.939 1.0 63.62 ? ? ? ? ? ? 179 TYR A CA 1 62 A A +ATOM 473 C C . TYR A 1 62 ? 25.145 14.150 48.653 1.0 66.92 ? ? ? ? ? ? 179 TYR A C 1 62 A A +ATOM 474 O O . TYR A 1 62 ? 25.563 13.410 49.539 1.0 79.31 ? ? ? ? ? ? 179 TYR A O 1 62 A A +ATOM 475 C CB . TYR A 1 62 ? 22.672 14.535 48.644 1.0 66.47 ? ? ? ? ? ? 179 TYR A CB 1 62 A A +ATOM 476 C CG . TYR A 1 62 ? 21.398 14.493 47.840 1.0 64.67 ? ? ? ? ? ? 179 TYR A CG 1 62 A A +ATOM 477 C CD1 . TYR A 1 62 ? 20.953 15.614 47.143 1.0 62.18 ? ? ? ? ? ? 179 TYR A CD1 1 62 A A +ATOM 478 C CD2 . TYR A 1 62 ? 20.647 13.322 47.753 1.0 72.84 ? ? ? ? ? ? 179 TYR A CD2 1 62 A A +ATOM 479 C CE1 . TYR A 1 62 ? 19.793 15.572 46.380 1.0 79.47 ? ? ? ? ? ? 179 TYR A CE1 1 62 A A +ATOM 480 C CE2 . TYR A 1 62 ? 19.483 13.268 46.992 1.0 77.72 ? ? ? ? ? ? 179 TYR A CE2 1 62 A A +ATOM 481 C CZ . TYR A 1 62 ? 19.061 14.399 46.308 1.0 80.12 ? ? ? ? ? ? 179 TYR A CZ 1 62 A A +ATOM 482 O OH . TYR A 1 62 ? 17.903 14.365 45.564 1.0 71.22 ? ? ? ? ? ? 179 TYR A OH 1 62 A A +ATOM 483 N N . MET A 1 63 ? 25.784 15.250 48.262 1.0 61.45 ? ? ? ? ? ? 180 MET A N 1 63 A A +ATOM 484 C CA . MET A 1 63 ? 27.057 15.657 48.853 1.0 62.82 ? ? ? ? ? ? 180 MET A CA 1 63 A A +ATOM 485 C C . MET A 1 63 ? 26.878 16.617 50.020 1.0 65.47 ? ? ? ? ? ? 180 MET A C 1 63 A A +ATOM 486 O O . MET A 1 63 ? 25.852 17.287 50.132 1.0 73.13 ? ? ? ? ? ? 180 MET A O 1 63 A A +ATOM 487 C CB . MET A 1 63 ? 27.947 16.303 47.788 1.0 67.13 ? ? ? ? ? ? 180 MET A CB 1 63 A A +ATOM 488 C CG . MET A 1 63 ? 28.112 15.466 46.528 1.0 66.76 ? ? ? ? ? ? 180 MET A CG 1 63 A A +ATOM 489 S SD . MET A 1 63 ? 29.117 16.259 45.245 1.0 65.33 ? ? ? ? ? ? 180 MET A SD 1 63 A A +ATOM 490 C CE . MET A 1 63 ? 28.525 17.956 45.302 1.0 31.44 ? ? ? ? ? ? 180 MET A CE 1 63 A A +ATOM 491 N N . GLU A 1 64 ? 27.892 16.681 50.880 1.0 60.02 ? ? ? ? ? ? 181 GLU A N 1 64 A A +ATOM 492 C CA . GLU A 1 64 ? 27.857 17.547 52.055 1.0 60.6 ? ? ? ? ? ? 181 GLU A CA 1 64 A A +ATOM 493 C C . GLU A 1 64 ? 27.665 19.017 51.718 1.0 62.39 ? ? ? ? ? ? 181 GLU A C 1 64 A A +ATOM 494 O O . GLU A 1 64 ? 26.931 19.726 52.406 1.0 55.85 ? ? ? ? ? ? 181 GLU A O 1 64 A A +ATOM 495 C CB . GLU A 1 64 ? 29.136 17.387 52.872 1.0 64.53 ? ? ? ? ? ? 181 GLU A CB 1 64 A A +ATOM 496 C CG . GLU A 1 64 ? 28.990 16.445 54.046 1.0 73.52 ? ? ? ? ? ? 181 GLU A CG 1 64 A A +ATOM 497 C CD . GLU A 1 64 ? 28.839 15.008 53.599 1.0 79.03 ? ? ? ? ? ? 181 GLU A CD 1 64 A A +ATOM 498 O OE1 . GLU A 1 64 ? 29.212 14.713 52.441 1.0 79.95 ? ? ? ? ? ? 181 GLU A OE1 1 64 A A +ATOM 499 O OE2 . GLU A 1 64 ? 28.354 14.178 54.400 1.0 75.62 ? ? ? ? ? ? 181 GLU A OE2 1 64 A A +ATOM 500 N N . GLU A 1 65 ? 28.342 19.482 50.675 1.0 65.1 ? ? ? ? ? ? 182 GLU A N 1 65 A A +ATOM 501 C CA . GLU A 1 65 ? 28.213 20.875 50.275 1.0 69.61 ? ? ? ? ? ? 182 GLU A CA 1 65 A A +ATOM 502 C C . GLU A 1 65 ? 26.736 21.128 49.989 1.0 76.9 ? ? ? ? ? ? 182 GLU A C 1 65 A A +ATOM 503 O O . GLU A 1 65 ? 26.253 22.259 50.073 1.0 82.04 ? ? ? ? ? ? 182 GLU A O 1 65 A A +ATOM 504 C CB . GLU A 1 65 ? 29.051 21.149 49.026 1.0 74.6 ? ? ? ? ? ? 182 GLU A CB 1 65 A A +ATOM 505 C CG . GLU A 1 65 ? 30.553 21.011 49.239 1.0 87.81 ? ? ? ? ? ? 182 GLU A CG 1 65 A A +ATOM 506 C CD . GLU A 1 65 ? 30.999 19.562 49.374 1.0 97.73 ? ? ? ? ? ? 182 GLU A CD 1 65 A A +ATOM 507 O OE1 . GLU A 1 65 ? 32.013 19.311 50.057 1.0 100.0 ? ? ? ? ? ? 182 GLU A OE1 1 65 A A +ATOM 508 O OE2 . GLU A 1 65 ? 30.337 18.674 48.797 1.0 92.34 ? ? ? ? ? ? 182 GLU A OE2 1 65 A A +ATOM 509 N N . GLU A 1 66 ? 26.026 20.052 49.657 1.0 71.44 ? ? ? ? ? ? 183 GLU A N 1 66 A A +ATOM 510 C CA . GLU A 1 66 ? 24.601 20.115 49.361 1.0 56.58 ? ? ? ? ? ? 183 GLU A CA 1 66 A A +ATOM 511 C C . GLU A 1 66 ? 23.824 19.910 50.656 1.0 59.61 ? ? ? ? ? ? 183 GLU A C 1 66 A A +ATOM 512 O O . GLU A 1 66 ? 22.942 20.697 50.997 1.0 61.56 ? ? ? ? ? ? 183 GLU A O 1 66 A A +ATOM 513 C CB . GLU A 1 66 ? 24.226 19.031 48.339 1.0 41.0 ? ? ? ? ? ? 183 GLU A CB 1 66 A A +ATOM 514 C CG . GLU A 1 66 ? 25.021 19.121 47.040 1.0 52.5 ? ? ? ? ? ? 183 GLU A CG 1 66 A A +ATOM 515 C CD . GLU A 1 66 ? 24.696 18.010 46.054 1.0 58.87 ? ? ? ? ? ? 183 GLU A CD 1 66 A A +ATOM 516 O OE1 . GLU A 1 66 ? 24.670 16.831 46.469 1.0 43.01 ? ? ? ? ? ? 183 GLU A OE1 1 66 A A +ATOM 517 O OE2 . GLU A 1 66 ? 24.470 18.321 44.861 1.0 52.0 ? ? ? ? ? ? 183 GLU A OE2 1 66 A A +ATOM 518 N N . LYS A 1 67 ? 24.167 18.850 51.380 1.0 53.06 ? ? ? ? ? ? 184 LYS A N 1 67 A A +ATOM 519 C CA . LYS A 1 67 ? 23.506 18.536 52.638 1.0 57.91 ? ? ? ? ? ? 184 LYS A CA 1 67 A A +ATOM 520 C C . LYS A 1 67 ? 23.575 19.713 53.603 1.0 64.25 ? ? ? ? ? ? 184 LYS A C 1 67 A A +ATOM 521 O O . LYS A 1 67 ? 22.739 19.839 54.499 1.0 65.13 ? ? ? ? ? ? 184 LYS A O 1 67 A A +ATOM 522 C CB . LYS A 1 67 ? 24.148 17.306 53.279 1.0 52.43 ? ? ? ? ? ? 184 LYS A CB 1 67 A A +ATOM 523 C CG . LYS A 1 67 ? 23.777 15.996 52.613 1.0 46.38 ? ? ? ? ? ? 184 LYS A CG 1 67 A A +ATOM 524 C CD . LYS A 1 67 ? 24.360 14.816 53.368 1.0 42.06 ? ? ? ? ? ? 184 LYS A CD 1 67 A A +ATOM 525 C CE . LYS A 1 67 ? 23.957 13.503 52.730 1.0 45.51 ? ? ? ? ? ? 184 LYS A CE 1 67 A A +ATOM 526 N NZ . LYS A 1 67 ? 24.537 12.335 53.447 1.0 53.49 ? ? ? ? ? ? 184 LYS A NZ 1 67 A A +ATOM 527 N N . LYS A 1 68 ? 24.576 20.571 53.424 1.0 58.11 ? ? ? ? ? ? 185 LYS A N 1 68 A A +ATOM 528 C CA . LYS A 1 68 ? 24.724 21.736 54.286 1.0 67.71 ? ? ? ? ? ? 185 LYS A CA 1 68 A A +ATOM 529 C C . LYS A 1 68 ? 23.656 22.745 53.905 1.0 61.16 ? ? ? ? ? ? 185 LYS A C 1 68 A A +ATOM 530 O O . LYS A 1 68 ? 22.981 23.316 54.764 1.0 73.17 ? ? ? ? ? ? 185 LYS A O 1 68 A A +ATOM 531 C CB . LYS A 1 68 ? 26.104 22.372 54.115 1.0 71.53 ? ? ? ? ? ? 185 LYS A CB 1 68 A A +ATOM 532 C CG . LYS A 1 68 ? 26.301 23.624 54.954 1.0 84.28 ? ? ? ? ? ? 185 LYS A CG 1 68 A A +ATOM 533 C CD . LYS A 1 68 ? 27.557 24.373 54.552 1.0 85.26 ? ? ? ? ? ? 185 LYS A CD 1 68 A A +ATOM 534 C CE . LYS A 1 68 ? 27.913 25.437 55.576 1.0 87.16 ? ? ? ? ? ? 185 LYS A CE 1 68 A A +ATOM 535 N NZ . LYS A 1 68 ? 27.000 26.613 55.508 1.0 87.22 ? ? ? ? ? ? 185 LYS A NZ 1 68 A A +ATOM 536 N N . THR A 1 69 ? 23.507 22.958 52.604 1.0 42.82 ? ? ? ? ? ? 186 THR A N 1 69 A A +ATOM 537 C CA . THR A 1 69 ? 22.516 23.896 52.101 1.0 62.42 ? ? ? ? ? ? 186 THR A CA 1 69 A A +ATOM 538 C C . THR A 1 69 ? 21.113 23.426 52.468 1.0 60.37 ? ? ? ? ? ? 186 THR A C 1 69 A A +ATOM 539 O O . THR A 1 69 ? 20.218 24.234 52.712 1.0 60.5 ? ? ? ? ? ? 186 THR A O 1 69 A A +ATOM 540 C CB . THR A 1 69 ? 22.616 24.034 50.574 1.0 66.13 ? ? ? ? ? ? 186 THR A CB 1 69 A A +ATOM 541 O OG1 . THR A 1 69 ? 23.993 24.143 50.194 1.0 53.16 ? ? ? ? ? ? 186 THR A OG1 1 69 A A +ATOM 542 C CG2 . THR A 1 69 ? 21.865 25.270 50.104 1.0 51.28 ? ? ? ? ? ? 186 THR A CG2 1 69 A A +ATOM 543 N N . TRP A 1 70 ? 20.925 22.112 52.499 1.0 58.38 ? ? ? ? ? ? 187 TRP A N 1 70 A A +ATOM 544 C CA . TRP A 1 70 ? 19.632 21.545 52.847 1.0 71.46 ? ? ? ? ? ? 187 TRP A CA 1 70 A A +ATOM 545 C C . TRP A 1 70 ? 19.310 21.898 54.297 1.0 76.26 ? ? ? ? ? ? 187 TRP A C 1 70 A A +ATOM 546 O O . TRP A 1 70 ? 18.235 22.417 54.598 1.0 74.65 ? ? ? ? ? ? 187 TRP A O 1 70 A A +ATOM 547 C CB . TRP A 1 70 ? 19.661 20.025 52.664 1.0 73.41 ? ? ? ? ? ? 187 TRP A CB 1 70 A A +ATOM 548 C CG . TRP A 1 70 ? 18.535 19.303 53.345 1.0 82.27 ? ? ? ? ? ? 187 TRP A CG 1 70 A A +ATOM 549 C CD1 . TRP A 1 70 ? 18.608 18.585 54.502 1.0 81.34 ? ? ? ? ? ? 187 TRP A CD1 1 70 A A +ATOM 550 C CD2 . TRP A 1 70 ? 17.170 19.214 52.903 1.0 85.83 ? ? ? ? ? ? 187 TRP A CD2 1 70 A A +ATOM 551 N NE1 . TRP A 1 70 ? 17.379 18.051 54.808 1.0 91.72 ? ? ? ? ? ? 187 TRP A NE1 1 70 A A +ATOM 552 C CE2 . TRP A 1 70 ? 16.482 18.417 53.843 1.0 88.31 ? ? ? ? ? ? 187 TRP A CE2 1 70 A A +ATOM 553 C CE3 . TRP A 1 70 ? 16.469 19.722 51.800 1.0 84.92 ? ? ? ? ? ? 187 TRP A CE3 1 70 A A +ATOM 554 C CZ2 . TRP A 1 70 ? 15.117 18.121 53.717 1.0 89.08 ? ? ? ? ? ? 187 TRP A CZ2 1 70 A A +ATOM 555 C CZ3 . TRP A 1 70 ? 15.111 19.424 51.676 1.0 82.88 ? ? ? ? ? ? 187 TRP A CZ3 1 70 A A +ATOM 556 C CH2 . TRP A 1 70 ? 14.451 18.634 52.633 1.0 80.38 ? ? ? ? ? ? 187 TRP A CH2 1 70 A A +ATOM 557 N N . GLY A 1 71 ? 20.259 21.617 55.186 1.0 79.18 ? ? ? ? ? ? 188 GLY A N 1 71 A A +ATOM 558 C CA . GLY A 1 71 ? 20.075 21.902 56.596 1.0 71.95 ? ? ? ? ? ? 188 GLY A CA 1 71 A A +ATOM 559 C C . GLY A 1 71 ? 20.007 23.382 56.917 1.0 74.01 ? ? ? ? ? ? 188 GLY A C 1 71 A A +ATOM 560 O O . GLY A 1 71 ? 19.427 23.773 57.930 1.0 90.17 ? ? ? ? ? ? 188 GLY A O 1 71 A A +ATOM 561 N N . THR A 1 72 ? 20.602 24.209 56.063 1.0 61.43 ? ? ? ? ? ? 189 THR A N 1 72 A A +ATOM 562 C CA . THR A 1 72 ? 20.582 25.651 56.278 1.0 79.14 ? ? ? ? ? ? 189 THR A CA 1 72 A A +ATOM 563 C C . THR A 1 72 ? 19.171 26.180 56.027 1.0 83.53 ? ? ? ? ? ? 189 THR A C 1 72 A A +ATOM 564 O O . THR A 1 72 ? 18.755 27.185 56.608 1.0 86.76 ? ? ? ? ? ? 189 THR A O 1 72 A A +ATOM 565 C CB . THR A 1 72 ? 21.572 26.374 55.341 1.0 77.79 ? ? ? ? ? ? 189 THR A CB 1 72 A A +ATOM 566 O OG1 . THR A 1 72 ? 22.911 25.988 55.675 1.0 73.16 ? ? ? ? ? ? 189 THR A OG1 1 72 A A +ATOM 567 C CG2 . THR A 1 72 ? 21.442 27.888 55.481 1.0 81.44 ? ? ? ? ? ? 189 THR A CG2 1 72 A A +ATOM 568 N N . VAL A 1 73 ? 18.442 25.487 55.158 1.0 86.25 ? ? ? ? ? ? 190 VAL A N 1 73 A A +ATOM 569 C CA . VAL A 1 73 ? 17.074 25.867 54.826 1.0 85.35 ? ? ? ? ? ? 190 VAL A CA 1 73 A A +ATOM 570 C C . VAL A 1 73 ? 16.101 25.118 55.734 1.0 83.6 ? ? ? ? ? ? 190 VAL A C 1 73 A A +ATOM 571 O O . VAL A 1 73 ? 15.051 25.641 56.112 1.0 75.22 ? ? ? ? ? ? 190 VAL A O 1 73 A A +ATOM 572 C CB . VAL A 1 73 ? 16.741 25.533 53.357 1.0 79.63 ? ? ? ? ? ? 190 VAL A CB 1 73 A A +ATOM 573 C CG1 . VAL A 1 73 ? 15.429 26.193 52.961 1.0 75.13 ? ? ? ? ? ? 190 VAL A CG1 1 73 A A +ATOM 574 C CG2 . VAL A 1 73 ? 17.864 25.993 52.452 1.0 75.09 ? ? ? ? ? ? 190 VAL A CG2 1 73 A A +ATOM 575 N N . PHE A 1 74 ? 16.467 23.885 56.076 1.0 79.24 ? ? ? ? ? ? 191 PHE A N 1 74 A A +ATOM 576 C CA . PHE A 1 74 ? 15.655 23.039 56.945 1.0 76.08 ? ? ? ? ? ? 191 PHE A CA 1 74 A A +ATOM 577 C C . PHE A 1 74 ? 15.634 23.589 58.369 1.0 85.23 ? ? ? ? ? ? 191 PHE A C 1 74 A A +ATOM 578 O O . PHE A 1 74 ? 14.741 23.276 59.152 1.0 99.86 ? ? ? ? ? ? 191 PHE A O 1 74 A A +ATOM 579 C CB . PHE A 1 74 ? 16.213 21.616 56.958 1.0 67.59 ? ? ? ? ? ? 191 PHE A CB 1 74 A A +ATOM 580 C CG . PHE A 1 74 ? 15.343 20.628 57.676 1.0 73.28 ? ? ? ? ? ? 191 PHE A CG 1 74 A A +ATOM 581 C CD1 . PHE A 1 74 ? 14.405 19.876 56.979 1.0 80.98 ? ? ? ? ? ? 191 PHE A CD1 1 74 A A +ATOM 582 C CD2 . PHE A 1 74 ? 15.469 20.437 59.048 1.0 79.62 ? ? ? ? ? ? 191 PHE A CD2 1 74 A A +ATOM 583 C CE1 . PHE A 1 74 ? 13.605 18.945 57.638 1.0 81.2 ? ? ? ? ? ? 191 PHE A CE1 1 74 A A +ATOM 584 C CE2 . PHE A 1 74 ? 14.674 19.508 59.717 1.0 79.7 ? ? ? ? ? ? 191 PHE A CE2 1 74 A A +ATOM 585 C CZ . PHE A 1 74 ? 13.740 18.761 59.010 1.0 80.86 ? ? ? ? ? ? 191 PHE A CZ 1 74 A A +ATOM 586 N N . LYS A 1 75 ? 16.627 24.405 58.703 1.0 89.68 ? ? ? ? ? ? 192 LYS A N 1 75 A A +ATOM 587 C CA . LYS A 1 75 ? 16.706 24.994 60.034 1.0 86.96 ? ? ? ? ? ? 192 LYS A CA 1 75 A A +ATOM 588 C C . LYS A 1 75 ? 16.018 26.350 60.046 1.0 83.34 ? ? ? ? ? ? 192 LYS A C 1 75 A A +ATOM 589 O O . LYS A 1 75 ? 15.218 26.647 60.932 1.0 91.7 ? ? ? ? ? ? 192 LYS A O 1 75 A A +ATOM 590 C CB . LYS A 1 75 ? 18.165 25.167 60.454 1.0 91.2 ? ? ? ? ? ? 192 LYS A CB 1 75 A A +ATOM 591 C CG . LYS A 1 75 ? 18.335 25.741 61.849 1.0 100.0 ? ? ? ? ? ? 192 LYS A CG 1 75 A A +ATOM 592 C CD . LYS A 1 75 ? 19.800 25.914 62.209 1.0 100.0 ? ? ? ? ? ? 192 LYS A CD 1 75 A A +ATOM 593 C CE . LYS A 1 75 ? 20.408 24.597 62.664 1.0 100.0 ? ? ? ? ? ? 192 LYS A CE 1 75 A A +ATOM 594 N NZ . LYS A 1 75 ? 19.996 24.235 64.051 1.0 100.0 ? ? ? ? ? ? 192 LYS A NZ 1 75 A A +ATOM 595 N N . THR A 1 76 ? 16.341 27.166 59.050 1.0 76.1 ? ? ? ? ? ? 193 THR A N 1 76 A A +ATOM 596 C CA . THR A 1 76 ? 15.770 28.499 58.931 1.0 90.5 ? ? ? ? ? ? 193 THR A CA 1 76 A A +ATOM 597 C C . THR A 1 76 ? 14.247 28.499 58.830 1.0 96.09 ? ? ? ? ? ? 193 THR A C 1 76 A A +ATOM 598 O O . THR A 1 76 ? 13.590 29.409 59.337 1.0 100.0 ? ? ? ? ? ? 193 THR A O 1 76 A A +ATOM 599 C CB . THR A 1 76 ? 16.322 29.226 57.694 1.0 100.0 ? ? ? ? ? ? 193 THR A CB 1 76 A A +ATOM 600 O OG1 . THR A 1 76 ? 15.665 30.493 57.550 1.0 100.0 ? ? ? ? ? ? 193 THR A OG1 1 76 A A +ATOM 601 C CG2 . THR A 1 76 ? 16.081 28.399 56.448 1.0 100.0 ? ? ? ? ? ? 193 THR A CG2 1 76 A A +ATOM 602 N N . LEU A 1 77 ? 13.689 27.484 58.177 1.0 90.36 ? ? ? ? ? ? 194 LEU A N 1 77 A A +ATOM 603 C CA . LEU A 1 77 ? 12.243 27.402 57.999 1.0 85.08 ? ? ? ? ? ? 194 LEU A CA 1 77 A A +ATOM 604 C C . LEU A 1 77 ? 11.500 26.599 59.068 1.0 82.86 ? ? ? ? ? ? 194 LEU A C 1 77 A A +ATOM 605 O O . LEU A 1 77 ? 10.344 26.890 59.375 1.0 85.6 ? ? ? ? ? ? 194 LEU A O 1 77 A A +ATOM 606 C CB . LEU A 1 77 ? 11.924 26.829 56.615 1.0 74.24 ? ? ? ? ? ? 194 LEU A CB 1 77 A A +ATOM 607 C CG . LEU A 1 77 ? 12.348 27.686 55.418 1.0 72.3 ? ? ? ? ? ? 194 LEU A CG 1 77 A A +ATOM 608 C CD1 . LEU A 1 77 ? 12.093 26.924 54.131 1.0 73.94 ? ? ? ? ? ? 194 LEU A CD1 1 77 A A +ATOM 609 C CD2 . LEU A 1 77 ? 11.579 28.995 55.417 1.0 77.3 ? ? ? ? ? ? 194 LEU A CD2 1 77 A A +ATOM 610 N N . LYS A 1 78 ? 12.159 25.591 59.631 1.0 79.81 ? ? ? ? ? ? 195 LYS A N 1 78 A A +ATOM 611 C CA . LYS A 1 78 ? 11.533 24.752 60.652 1.0 80.42 ? ? ? ? ? ? 195 LYS A CA 1 78 A A +ATOM 612 C C . LYS A 1 78 ? 11.021 25.556 61.839 1.0 86.3 ? ? ? ? ? ? 195 LYS A C 1 78 A A +ATOM 613 O O . LYS A 1 78 ? 10.099 25.133 62.540 1.0 84.76 ? ? ? ? ? ? 195 LYS A O 1 78 A A +ATOM 614 C CB . LYS A 1 78 ? 12.519 23.700 61.152 1.0 86.69 ? ? ? ? ? ? 195 LYS A CB 1 78 A A +ATOM 615 C CG . LYS A 1 78 ? 11.904 22.696 62.112 1.0 88.67 ? ? ? ? ? ? 195 LYS A CG 1 78 A A +ATOM 616 C CD . LYS A 1 78 ? 12.800 21.481 62.296 1.0 93.28 ? ? ? ? ? ? 195 LYS A CD 1 78 A A +ATOM 617 C CE . LYS A 1 78 ? 12.347 20.642 63.479 1.0 92.2 ? ? ? ? ? ? 195 LYS A CE 1 78 A A +ATOM 618 N NZ . LYS A 1 78 ? 10.955 20.144 63.309 1.0 88.53 ? ? ? ? ? ? 195 LYS A NZ 1 78 A A +ATOM 619 N N . SER A 1 79 ? 11.630 26.713 62.065 1.0 94.23 ? ? ? ? ? ? 196 SER A N 1 79 A A +ATOM 620 C CA . SER A 1 79 ? 11.241 27.574 63.173 1.0 100.0 ? ? ? ? ? ? 196 SER A CA 1 79 A A +ATOM 621 C C . SER A 1 79 ? 9.950 28.343 62.894 1.0 100.0 ? ? ? ? ? ? 196 SER A C 1 79 A A +ATOM 622 O O . SER A 1 79 ? 9.106 28.497 63.780 1.0 100.0 ? ? ? ? ? ? 196 SER A O 1 79 A A +ATOM 623 C CB . SER A 1 79 ? 12.365 28.566 63.480 1.0 100.0 ? ? ? ? ? ? 196 SER A CB 1 79 A A +ATOM 624 O OG . SER A 1 79 ? 12.518 29.504 62.426 1.0 85.8 ? ? ? ? ? ? 196 SER A OG 1 79 A A +ATOM 625 N N . LEU A 1 80 ? 9.795 28.812 61.659 1.0 96.32 ? ? ? ? ? ? 197 LEU A N 1 80 A A +ATOM 626 C CA . LEU A 1 80 ? 8.618 29.589 61.278 1.0 93.99 ? ? ? ? ? ? 197 LEU A CA 1 80 A A +ATOM 627 C C . LEU A 1 80 ? 7.403 28.799 60.809 1.0 88.37 ? ? ? ? ? ? 197 LEU A C 1 80 A A +ATOM 628 O O . LEU A 1 80 ? 6.415 29.392 60.382 1.0 81.94 ? ? ? ? ? ? 197 LEU A O 1 80 A A +ATOM 629 C CB . LEU A 1 80 ? 8.984 30.590 60.182 1.0 95.3 ? ? ? ? ? ? 197 LEU A CB 1 80 A A +ATOM 630 C CG . LEU A 1 80 ? 10.268 31.406 60.330 1.0 93.83 ? ? ? ? ? ? 197 LEU A CG 1 80 A A +ATOM 631 C CD1 . LEU A 1 80 ? 10.387 32.346 59.144 1.0 100.0 ? ? ? ? ? ? 197 LEU A CD1 1 80 A A +ATOM 632 C CD2 . LEU A 1 80 ? 10.250 32.192 61.633 1.0 100.0 ? ? ? ? ? ? 197 LEU A CD2 1 80 A A +ATOM 633 N N . TYR A 1 81 ? 7.454 27.474 60.886 1.0 87.34 ? ? ? ? ? ? 198 TYR A N 1 81 A A +ATOM 634 C CA . TYR A 1 81 ? 6.320 26.679 60.426 1.0 89.12 ? ? ? ? ? ? 198 TYR A CA 1 81 A A +ATOM 635 C C . TYR A 1 81 ? 5.164 26.608 61.413 1.0 85.78 ? ? ? ? ? ? 198 TYR A C 1 81 A A +ATOM 636 O O . TYR A 1 81 ? 4.016 26.851 61.046 1.0 80.49 ? ? ? ? ? ? 198 TYR A O 1 81 A A +ATOM 637 C CB . TYR A 1 81 ? 6.774 25.270 60.043 1.0 84.46 ? ? ? ? ? ? 198 TYR A CB 1 81 A A +ATOM 638 C CG . TYR A 1 81 ? 7.357 25.191 58.649 1.0 83.63 ? ? ? ? ? ? 198 TYR A CG 1 81 A A +ATOM 639 C CD1 . TYR A 1 81 ? 6.947 26.077 57.649 1.0 72.73 ? ? ? ? ? ? 198 TYR A CD1 1 81 A A +ATOM 640 C CD2 . TYR A 1 81 ? 8.342 24.257 58.336 1.0 78.08 ? ? ? ? ? ? 198 TYR A CD2 1 81 A A +ATOM 641 C CE1 . TYR A 1 81 ? 7.507 26.035 56.376 1.0 67.94 ? ? ? ? ? ? 198 TYR A CE1 1 81 A A +ATOM 642 C CE2 . TYR A 1 81 ? 8.909 24.206 57.066 1.0 72.97 ? ? ? ? ? ? 198 TYR A CE2 1 81 A A +ATOM 643 C CZ . TYR A 1 81 ? 8.486 25.098 56.093 1.0 71.06 ? ? ? ? ? ? 198 TYR A CZ 1 81 A A +ATOM 644 O OH . TYR A 1 81 ? 9.042 25.048 54.837 1.0 81.83 ? ? ? ? ? ? 198 TYR A OH 1 81 A A +ATOM 645 N N . LYS A 1 82 ? 5.454 26.263 62.661 1.0 92.31 ? ? ? ? ? ? 199 LYS A N 1 82 A A +ATOM 646 C CA . LYS A 1 82 ? 4.397 26.190 63.667 1.0 100.0 ? ? ? ? ? ? 199 LYS A CA 1 82 A A +ATOM 647 C C . LYS A 1 82 ? 3.805 27.583 63.837 1.0 100.0 ? ? ? ? ? ? 199 LYS A C 1 82 A A +ATOM 648 O O . LYS A 1 82 ? 2.677 27.751 64.310 1.0 100.0 ? ? ? ? ? ? 199 LYS A O 1 82 A A +ATOM 649 C CB . LYS A 1 82 ? 4.958 25.706 65.004 1.0 99.73 ? ? ? ? ? ? 199 LYS A CB 1 82 A A +ATOM 650 C CG . LYS A 1 82 ? 6.227 26.418 65.433 1.0 96.19 ? ? ? ? ? ? 199 LYS A CG 1 82 A A +ATOM 651 C CD . LYS A 1 82 ? 6.942 25.631 66.515 1.0 100.0 ? ? ? ? ? ? 199 LYS A CD 1 82 A A +ATOM 652 C CE . LYS A 1 82 ? 7.390 24.272 65.995 1.0 100.0 ? ? ? ? ? ? 199 LYS A CE 1 82 A A +ATOM 653 N NZ . LYS A 1 82 ? 8.257 24.390 64.784 1.0 100.0 ? ? ? ? ? ? 199 LYS A NZ 1 82 A A +ATOM 654 N N . THR A 1 83 ? 4.580 28.582 63.437 1.0 100.0 ? ? ? ? ? ? 200 THR A N 1 83 A A +ATOM 655 C CA . THR A 1 83 ? 4.153 29.964 63.544 1.0 98.21 ? ? ? ? ? ? 200 THR A CA 1 83 A A +ATOM 656 C C . THR A 1 83 ? 3.325 30.419 62.351 1.0 92.84 ? ? ? ? ? ? 200 THR A C 1 83 A A +ATOM 657 O O . THR A 1 83 ? 2.122 30.649 62.467 1.0 85.72 ? ? ? ? ? ? 200 THR A O 1 83 A A +ATOM 658 C CB . THR A 1 83 ? 5.365 30.900 63.675 1.0 100.0 ? ? ? ? ? ? 200 THR A CB 1 83 A A +ATOM 659 O OG1 . THR A 1 83 ? 6.272 30.370 64.648 1.0 100.0 ? ? ? ? ? ? 200 THR A OG1 1 83 A A +ATOM 660 C CG2 . THR A 1 83 ? 4.919 32.295 64.100 1.0 92.31 ? ? ? ? ? ? 200 THR A CG2 1 83 A A +ATOM 661 N N . HIS A 1 84 ? 3.982 30.538 61.202 1.0 91.59 ? ? ? ? ? ? 201 HIS A N 1 84 A A +ATOM 662 C CA . HIS A 1 84 ? 3.334 31.007 59.983 1.0 96.97 ? ? ? ? ? ? 201 HIS A CA 1 84 A A +ATOM 663 C C . HIS A 1 84 ? 2.666 29.956 59.087 1.0 98.81 ? ? ? ? ? ? 201 HIS A C 1 84 A A +ATOM 664 O O . HIS A 1 84 ? 1.668 30.251 58.425 1.0 100.0 ? ? ? ? ? ? 201 HIS A O 1 84 A A +ATOM 665 C CB . HIS A 1 84 ? 4.344 31.809 59.154 1.0 97.39 ? ? ? ? ? ? 201 HIS A CB 1 84 A A +ATOM 666 C CG . HIS A 1 84 ? 4.989 32.931 59.909 1.0 100.0 ? ? ? ? ? ? 201 HIS A CG 1 84 A A +ATOM 667 N ND1 . HIS A 1 84 ? 4.270 33.811 60.689 1.0 100.0 ? ? ? ? ? ? 201 HIS A ND1 1 84 A A +ATOM 668 C CD2 . HIS A 1 84 ? 6.283 33.318 59.999 1.0 100.0 ? ? ? ? ? ? 201 HIS A CD2 1 84 A A +ATOM 669 C CE1 . HIS A 1 84 ? 5.094 34.695 61.226 1.0 100.0 ? ? ? ? ? ? 201 HIS A CE1 1 84 A A +ATOM 670 N NE2 . HIS A 1 84 ? 6.321 34.417 60.822 1.0 100.0 ? ? ? ? ? ? 201 HIS A NE2 1 84 A A +ATOM 671 N N . ALA A 1 85 ? 3.205 28.740 59.057 1.0 99.97 ? ? ? ? ? ? 202 ALA A N 1 85 A A +ATOM 672 C CA . ALA A 1 85 ? 2.641 27.684 58.216 1.0 95.61 ? ? ? ? ? ? 202 ALA A CA 1 85 A A +ATOM 673 C C . ALA A 1 85 ? 1.244 27.257 58.658 1.0 92.19 ? ? ? ? ? ? 202 ALA A C 1 85 A A +ATOM 674 O O . ALA A 1 85 ? 0.884 27.385 59.828 1.0 83.66 ? ? ? ? ? ? 202 ALA A O 1 85 A A +ATOM 675 C CB . ALA A 1 85 ? 3.570 26.478 58.192 1.0 100.0 ? ? ? ? ? ? 202 ALA A CB 1 85 A A +ATOM 676 N N . CYS A 1 86 ? 0.464 26.750 57.706 1.0 88.73 ? ? ? ? ? ? 203 CYS A N 1 86 A A +ATOM 677 C CA . CYS A 1 86 ? -0.900 26.303 57.974 1.0 91.74 ? ? ? ? ? ? 203 CYS A CA 1 86 A A +ATOM 678 C C . CYS A 1 86 ? -0.947 24.967 58.715 1.0 89.57 ? ? ? ? ? ? 203 CYS A C 1 86 A A +ATOM 679 O O . CYS A 1 86 ? 0.016 24.198 58.708 1.0 90.42 ? ? ? ? ? ? 203 CYS A O 1 86 A A +ATOM 680 C CB . CYS A 1 86 ? -1.693 26.202 56.667 1.0 93.32 ? ? ? ? ? ? 203 CYS A CB 1 86 A A +ATOM 681 S SG . CYS A 1 86 ? -1.253 24.804 55.613 1.0 100.0 ? ? ? ? ? ? 203 CYS A SG 1 86 A A +ATOM 682 N N . TYR A 1 87 ? -2.085 24.706 59.349 1.0 89.75 ? ? ? ? ? ? 204 TYR A N 1 87 A A +ATOM 683 C CA . TYR A 1 87 ? -2.294 23.494 60.127 1.0 89.68 ? ? ? ? ? ? 204 TYR A CA 1 87 A A +ATOM 684 C C . TYR A 1 87 ? -1.942 22.199 59.404 1.0 92.54 ? ? ? ? ? ? 204 TYR A C 1 87 A A +ATOM 685 O O . TYR A 1 87 ? -1.113 21.427 59.880 1.0 100.0 ? ? ? ? ? ? 204 TYR A O 1 87 A A +ATOM 686 C CB . TYR A 1 87 ? -3.747 23.438 60.611 1.0 90.65 ? ? ? ? ? ? 204 TYR A CB 1 87 A A +ATOM 687 C CG . TYR A 1 87 ? -4.223 22.054 60.997 1.0 95.13 ? ? ? ? ? ? 204 TYR A CG 1 87 A A +ATOM 688 C CD1 . TYR A 1 87 ? -3.540 21.300 61.953 1.0 100.0 ? ? ? ? ? ? 204 TYR A CD1 1 87 A A +ATOM 689 C CD2 . TYR A 1 87 ? -5.355 21.496 60.405 1.0 100.0 ? ? ? ? ? ? 204 TYR A CD2 1 87 A A +ATOM 690 C CE1 . TYR A 1 87 ? -3.972 20.024 62.311 1.0 100.0 ? ? ? ? ? ? 204 TYR A CE1 1 87 A A +ATOM 691 C CE2 . TYR A 1 87 ? -5.797 20.219 60.755 1.0 100.0 ? ? ? ? ? ? 204 TYR A CE2 1 87 A A +ATOM 692 C CZ . TYR A 1 87 ? -5.100 19.491 61.709 1.0 100.0 ? ? ? ? ? ? 204 TYR A CZ 1 87 A A +ATOM 693 O OH . TYR A 1 87 ? -5.531 18.234 62.068 1.0 86.78 ? ? ? ? ? ? 204 TYR A OH 1 87 A A +ATOM 694 N N . GLU A 1 88 ? -2.581 21.959 58.263 1.0 96.85 ? ? ? ? ? ? 205 GLU A N 1 88 A A +ATOM 695 C CA . GLU A 1 88 ? -2.339 20.739 57.494 1.0 94.12 ? ? ? ? ? ? 205 GLU A CA 1 88 A A +ATOM 696 C C . GLU A 1 88 ? -0.848 20.475 57.321 1.0 92.18 ? ? ? ? ? ? 205 GLU A C 1 88 A A +ATOM 697 O O . GLU A 1 88 ? -0.421 19.329 57.161 1.0 76.01 ? ? ? ? ? ? 205 GLU A O 1 88 A A +ATOM 698 C CB . GLU A 1 88 ? -3.014 20.832 56.123 1.0 91.15 ? ? ? ? ? ? 205 GLU A CB 1 88 A A +ATOM 699 C CG . GLU A 1 88 ? -4.511 21.094 56.182 1.0 80.29 ? ? ? ? ? ? 205 GLU A CG 1 88 A A +ATOM 700 C CD . GLU A 1 88 ? -4.833 22.514 56.604 1.0 94.15 ? ? ? ? ? ? 205 GLU A CD 1 88 A A +ATOM 701 O OE1 . GLU A 1 88 ? -5.964 22.753 57.075 1.0 98.51 ? ? ? ? ? ? 205 GLU A OE1 1 88 A A +ATOM 702 O OE2 . GLU A 1 88 ? -3.952 23.390 56.463 1.0 100.0 ? ? ? ? ? ? 205 GLU A OE2 1 88 A A +ATOM 703 N N . TYR A 1 89 ? -0.061 21.547 57.360 1.0 90.46 ? ? ? ? ? ? 206 TYR A N 1 89 A A +ATOM 704 C CA . TYR A 1 89 ? 1.388 21.454 57.215 1.0 87.27 ? ? ? ? ? ? 206 TYR A CA 1 89 A A +ATOM 705 C C . TYR A 1 89 ? 1.998 20.994 58.529 1.0 87.37 ? ? ? ? ? ? 206 TYR A C 1 89 A A +ATOM 706 O O . TYR A 1 89 ? 2.735 20.008 58.574 1.0 90.91 ? ? ? ? ? ? 206 TYR A O 1 89 A A +ATOM 707 C CB . TYR A 1 89 ? 1.965 22.821 56.837 1.0 84.49 ? ? ? ? ? ? 206 TYR A CB 1 89 A A +ATOM 708 C CG . TYR A 1 89 ? 3.382 22.782 56.308 1.0 83.47 ? ? ? ? ? ? 206 TYR A CG 1 89 A A +ATOM 709 C CD1 . TYR A 1 89 ? 3.669 23.194 55.009 1.0 84.19 ? ? ? ? ? ? 206 TYR A CD1 1 89 A A +ATOM 710 C CD2 . TYR A 1 89 ? 4.438 22.354 57.112 1.0 81.07 ? ? ? ? ? ? 206 TYR A CD2 1 89 A A +ATOM 711 C CE1 . TYR A 1 89 ? 4.971 23.182 54.520 1.0 81.36 ? ? ? ? ? ? 206 TYR A CE1 1 89 A A +ATOM 712 C CE2 . TYR A 1 89 ? 5.746 22.339 56.632 1.0 88.23 ? ? ? ? ? ? 206 TYR A CE2 1 89 A A +ATOM 713 C CZ . TYR A 1 89 ? 6.005 22.756 55.335 1.0 88.88 ? ? ? ? ? ? 206 TYR A CZ 1 89 A A +ATOM 714 O OH . TYR A 1 89 ? 7.294 22.747 54.852 1.0 86.93 ? ? ? ? ? ? 206 TYR A OH 1 89 A A +ATOM 715 N N . ASN A 1 90 ? 1.681 21.724 59.596 1.0 83.68 ? ? ? ? ? ? 207 ASN A N 1 90 A A +ATOM 716 C CA . ASN A 1 90 ? 2.188 21.423 60.930 1.0 85.33 ? ? ? ? ? ? 207 ASN A CA 1 90 A A +ATOM 717 C C . ASN A 1 90 ? 1.759 20.042 61.413 1.0 87.45 ? ? ? ? ? ? 207 ASN A C 1 90 A A +ATOM 718 O O . ASN A 1 90 ? 2.390 19.465 62.299 1.0 84.26 ? ? ? ? ? ? 207 ASN A O 1 90 A A +ATOM 719 C CB . ASN A 1 90 ? 1.710 22.484 61.921 1.0 86.6 ? ? ? ? ? ? 207 ASN A CB 1 90 A A +ATOM 720 C CG . ASN A 1 90 ? 2.235 23.869 61.590 1.0 100.0 ? ? ? ? ? ? 207 ASN A CG 1 90 A A +ATOM 721 O OD1 . ASN A 1 90 ? 3.446 24.096 61.563 1.0 100.0 ? ? ? ? ? ? 207 ASN A OD1 1 90 A A +ATOM 722 N ND2 . ASN A 1 90 ? 1.326 24.802 61.333 1.0 100.0 ? ? ? ? ? ? 207 ASN A ND2 1 90 A A +ATOM 723 N N . HIS A 1 91 ? 0.688 19.518 60.823 1.0 89.56 ? ? ? ? ? ? 208 HIS A N 1 91 A A +ATOM 724 C CA . HIS A 1 91 ? 0.178 18.203 61.199 1.0 85.85 ? ? ? ? ? ? 208 HIS A CA 1 91 A A +ATOM 725 C C . HIS A 1 91 ? 0.982 17.079 60.556 1.0 76.51 ? ? ? ? ? ? 208 HIS A C 1 91 A A +ATOM 726 O O . HIS A 1 91 ? 1.413 16.139 61.227 1.0 63.62 ? ? ? ? ? ? 208 HIS A O 1 91 A A +ATOM 727 C CB . HIS A 1 91 ? -1.295 18.063 60.792 1.0 73.65 ? ? ? ? ? ? 208 HIS A CB 1 91 A A +ATOM 728 C CG . HIS A 1 91 ? -1.783 16.646 60.783 1.0 75.73 ? ? ? ? ? ? 208 HIS A CG 1 91 A A +ATOM 729 N ND1 . HIS A 1 91 ? -2.327 16.052 59.662 1.0 67.92 ? ? ? ? ? ? 208 HIS A ND1 1 91 A A +ATOM 730 C CD2 . HIS A 1 91 ? -1.783 15.694 61.745 1.0 87.75 ? ? ? ? ? ? 208 HIS A CD2 1 91 A A +ATOM 731 C CE1 . HIS A 1 91 ? -2.639 14.798 59.937 1.0 66.17 ? ? ? ? ? ? 208 HIS A CE1 1 91 A A +ATOM 732 N NE2 . HIS A 1 91 ? -2.319 14.555 61.196 1.0 74.7 ? ? ? ? ? ? 208 HIS A NE2 1 91 A A +ATOM 733 N N . ILE A 1 92 ? 1.182 17.184 59.250 1.0 70.01 ? ? ? ? ? ? 209 ILE A N 1 92 A A +ATOM 734 C CA . ILE A 1 92 ? 1.905 16.164 58.504 1.0 76.07 ? ? ? ? ? ? 209 ILE A CA 1 92 A A +ATOM 735 C C . ILE A 1 92 ? 3.421 16.146 58.694 1.0 81.86 ? ? ? ? ? ? 209 ILE A C 1 92 A A +ATOM 736 O O . ILE A 1 92 ? 4.054 15.095 58.565 1.0 81.22 ? ? ? ? ? ? 209 ILE A O 1 92 A A +ATOM 737 C CB . ILE A 1 92 ? 1.614 16.291 56.993 1.0 73.26 ? ? ? ? ? ? 209 ILE A CB 1 92 A A +ATOM 738 C CG1 . ILE A 1 92 ? 2.157 15.063 56.257 1.0 57.57 ? ? ? ? ? ? 209 ILE A CG1 1 92 A A +ATOM 739 C CG2 . ILE A 1 92 ? 2.233 17.576 56.451 1.0 70.08 ? ? ? ? ? ? 209 ILE A CG2 1 92 A A +ATOM 740 C CD1 . ILE A 1 92 ? 1.523 13.767 56.698 1.0 52.0 ? ? ? ? ? ? 209 ILE A CD1 1 92 A A +ATOM 741 N N . PHE A 1 93 ? 4.005 17.303 59.001 1.0 85.71 ? ? ? ? ? ? 210 PHE A N 1 93 A A +ATOM 742 C CA . PHE A 1 93 ? 5.453 17.394 59.174 1.0 75.69 ? ? ? ? ? ? 210 PHE A CA 1 93 A A +ATOM 743 C C . PHE A 1 93 ? 6.055 16.324 60.071 1.0 76.41 ? ? ? ? ? ? 210 PHE A C 1 93 A A +ATOM 744 O O . PHE A 1 93 ? 6.895 15.542 59.628 1.0 73.65 ? ? ? ? ? ? 210 PHE A O 1 93 A A +ATOM 745 C CB . PHE A 1 93 ? 5.854 18.773 59.695 1.0 72.53 ? ? ? ? ? ? 210 PHE A CB 1 93 A A +ATOM 746 C CG . PHE A 1 93 ? 7.067 19.343 59.015 1.0 89.37 ? ? ? ? ? ? 210 PHE A CG 1 93 A A +ATOM 747 C CD1 . PHE A 1 93 ? 8.163 19.780 59.754 1.0 100.0 ? ? ? ? ? ? 210 PHE A CD1 1 93 A A +ATOM 748 C CD2 . PHE A 1 93 ? 7.114 19.444 57.629 1.0 100.0 ? ? ? ? ? ? 210 PHE A CD2 1 93 A A +ATOM 749 C CE1 . PHE A 1 93 ? 9.290 20.310 59.119 1.0 100.0 ? ? ? ? ? ? 210 PHE A CE1 1 93 A A +ATOM 750 C CE2 . PHE A 1 93 ? 8.236 19.973 56.985 1.0 100.0 ? ? ? ? ? ? 210 PHE A CE2 1 93 A A +ATOM 751 C CZ . PHE A 1 93 ? 9.325 20.408 57.735 1.0 98.73 ? ? ? ? ? ? 210 PHE A CZ 1 93 A A +ATOM 752 N N . PRO A 1 94 ? 5.628 16.263 61.345 1.0 78.71 ? ? ? ? ? ? 211 PRO A N 1 94 A A +ATOM 753 C CA . PRO A 1 94 ? 6.210 15.238 62.218 1.0 72.51 ? ? ? ? ? ? 211 PRO A CA 1 94 A A +ATOM 754 C C . PRO A 1 94 ? 6.125 13.831 61.636 1.0 66.57 ? ? ? ? ? ? 211 PRO A C 1 94 A A +ATOM 755 O O . PRO A 1 94 ? 6.876 12.942 62.039 1.0 66.09 ? ? ? ? ? ? 211 PRO A O 1 94 A A +ATOM 756 C CB . PRO A 1 94 ? 5.421 15.382 63.518 1.0 88.21 ? ? ? ? ? ? 211 PRO A CB 1 94 A A +ATOM 757 C CG . PRO A 1 94 ? 4.849 16.760 63.476 1.0 89.51 ? ? ? ? ? ? 211 PRO A CG 1 94 A A +ATOM 758 C CD . PRO A 1 94 ? 4.609 17.071 62.034 1.0 79.55 ? ? ? ? ? ? 211 PRO A CD 1 94 A A +ATOM 759 N N . LEU A 1 95 ? 5.213 13.632 60.687 1.0 67.37 ? ? ? ? ? ? 212 LEU A N 1 95 A A +ATOM 760 C CA . LEU A 1 95 ? 5.048 12.329 60.046 1.0 76.53 ? ? ? ? ? ? 212 LEU A CA 1 95 A A +ATOM 761 C C . LEU A 1 95 ? 6.048 12.215 58.902 1.0 80.7 ? ? ? ? ? ? 212 LEU A C 1 95 A A +ATOM 762 O O . LEU A 1 95 ? 6.529 11.127 58.589 1.0 72.08 ? ? ? ? ? ? 212 LEU A O 1 95 A A +ATOM 763 C CB . LEU A 1 95 ? 3.625 12.174 59.500 1.0 72.65 ? ? ? ? ? ? 212 LEU A CB 1 95 A A +ATOM 764 C CG . LEU A 1 95 ? 2.487 12.057 60.517 1.0 53.72 ? ? ? ? ? ? 212 LEU A CG 1 95 A A +ATOM 765 C CD1 . LEU A 1 95 ? 1.180 12.453 59.853 1.0 47.91 ? ? ? ? ? ? 212 LEU A CD1 1 95 A A +ATOM 766 C CD2 . LEU A 1 95 ? 2.422 10.635 61.058 1.0 26.98 ? ? ? ? ? ? 212 LEU A CD2 1 95 A A +ATOM 767 N N . LEU A 1 96 ? 6.345 13.351 58.275 1.0 79.57 ? ? ? ? ? ? 213 LEU A N 1 96 A A +ATOM 768 C CA . LEU A 1 96 ? 7.304 13.400 57.176 1.0 73.46 ? ? ? ? ? ? 213 LEU A CA 1 96 A A +ATOM 769 C C . LEU A 1 96 ? 8.691 13.214 57.780 1.0 75.68 ? ? ? ? ? ? 213 LEU A C 1 96 A A +ATOM 770 O O . LEU A 1 96 ? 9.534 12.500 57.238 1.0 73.21 ? ? ? ? ? ? 213 LEU A O 1 96 A A +ATOM 771 C CB . LEU A 1 96 ? 7.235 14.755 56.474 1.0 60.67 ? ? ? ? ? ? 213 LEU A CB 1 96 A A +ATOM 772 C CG . LEU A 1 96 ? 6.085 14.981 55.492 1.0 68.02 ? ? ? ? ? ? 213 LEU A CG 1 96 A A +ATOM 773 C CD1 . LEU A 1 96 ? 5.965 16.472 55.189 1.0 61.82 ? ? ? ? ? ? 213 LEU A CD1 1 96 A A +ATOM 774 C CD2 . LEU A 1 96 ? 6.332 14.182 54.221 1.0 51.97 ? ? ? ? ? ? 213 LEU A CD2 1 96 A A +ATOM 775 N N . GLU A 1 97 ? 8.914 13.875 58.911 1.0 80.67 ? ? ? ? ? ? 214 GLU A N 1 97 A A +ATOM 776 C CA . GLU A 1 97 ? 10.185 13.792 59.610 1.0 78.9 ? ? ? ? ? ? 214 GLU A CA 1 97 A A +ATOM 777 C C . GLU A 1 97 ? 10.397 12.375 60.129 1.0 76.25 ? ? ? ? ? ? 214 GLU A C 1 97 A A +ATOM 778 O O . GLU A 1 97 ? 11.459 11.787 59.942 1.0 82.01 ? ? ? ? ? ? 214 GLU A O 1 97 A A +ATOM 779 C CB . GLU A 1 97 ? 10.208 14.785 60.776 1.0 84.27 ? ? ? ? ? ? 214 GLU A CB 1 97 A A +ATOM 780 C CG . GLU A 1 97 ? 9.896 16.217 60.372 1.0 97.39 ? ? ? ? ? ? 214 GLU A CG 1 97 A A +ATOM 781 C CD . GLU A 1 97 ? 9.835 17.160 61.561 1.0 100.0 ? ? ? ? ? ? 214 GLU A CD 1 97 A A +ATOM 782 O OE1 . GLU A 1 97 ? 8.720 17.605 61.914 1.0 100.0 ? ? ? ? ? ? 214 GLU A OE1 1 97 A A +ATOM 783 O OE2 . GLU A 1 97 ? 10.903 17.457 62.143 1.0 100.0 ? ? ? ? ? ? 214 GLU A OE2 1 97 A A +ATOM 784 N N . LYS A 1 98 ? 9.372 11.831 60.776 1.0 70.39 ? ? ? ? ? ? 215 LYS A N 1 98 A A +ATOM 785 C CA . LYS A 1 98 ? 9.448 10.489 61.335 1.0 70.4 ? ? ? ? ? ? 215 LYS A CA 1 98 A A +ATOM 786 C C . LYS A 1 98 ? 9.396 9.375 60.291 1.0 79.87 ? ? ? ? ? ? 215 LYS A C 1 98 A A +ATOM 787 O O . LYS A 1 98 ? 9.718 8.225 60.595 1.0 91.68 ? ? ? ? ? ? 215 LYS A O 1 98 A A +ATOM 788 C CB . LYS A 1 98 ? 8.313 10.276 62.339 1.0 72.12 ? ? ? ? ? ? 215 LYS A CB 1 98 A A +ATOM 789 C CG . LYS A 1 98 ? 8.403 8.954 63.085 1.0 92.07 ? ? ? ? ? ? 215 LYS A CG 1 98 A A +ATOM 790 C CD . LYS A 1 98 ? 7.267 8.788 64.081 1.0 96.37 ? ? ? ? ? ? 215 LYS A CD 1 98 A A +ATOM 791 C CE . LYS A 1 98 ? 7.487 9.652 65.314 1.0 100.0 ? ? ? ? ? ? 215 LYS A CE 1 98 A A +ATOM 792 N NZ . LYS A 1 98 ? 8.719 9.273 66.065 1.0 100.0 ? ? ? ? ? ? 215 LYS A NZ 1 98 A A +ATOM 793 N N . TYR A 1 99 ? 9.003 9.704 59.064 1.0 84.91 ? ? ? ? ? ? 216 TYR A N 1 99 A A +ATOM 794 C CA . TYR A 1 99 ? 8.896 8.676 58.034 1.0 91.21 ? ? ? ? ? ? 216 TYR A CA 1 99 A A +ATOM 795 C C . TYR A 1 99 ? 9.778 8.803 56.796 1.0 87.96 ? ? ? ? ? ? 216 TYR A C 1 99 A A +ATOM 796 O O . TYR A 1 99 ? 10.553 7.897 56.491 1.0 84.66 ? ? ? ? ? ? 216 TYR A O 1 99 A A +ATOM 797 C CB . TYR A 1 99 ? 7.430 8.539 57.618 1.0 94.0 ? ? ? ? ? ? 216 TYR A CB 1 99 A A +ATOM 798 C CG . TYR A 1 99 ? 6.583 7.898 58.689 1.0 100.0 ? ? ? ? ? ? 216 TYR A CG 1 99 A A +ATOM 799 C CD1 . TYR A 1 99 ? 5.745 8.664 59.501 1.0 96.76 ? ? ? ? ? ? 216 TYR A CD1 1 99 A A +ATOM 800 C CD2 . TYR A 1 99 ? 6.644 6.524 58.915 1.0 100.0 ? ? ? ? ? ? 216 TYR A CD2 1 99 A A +ATOM 801 C CE1 . TYR A 1 99 ? 4.992 8.076 60.514 1.0 96.2 ? ? ? ? ? ? 216 TYR A CE1 1 99 A A +ATOM 802 C CE2 . TYR A 1 99 ? 5.897 5.926 59.923 1.0 100.0 ? ? ? ? ? ? 216 TYR A CE2 1 99 A A +ATOM 803 C CZ . TYR A 1 99 ? 5.073 6.705 60.720 1.0 100.0 ? ? ? ? ? ? 216 TYR A CZ 1 99 A A +ATOM 804 O OH . TYR A 1 99 ? 4.337 6.111 61.723 1.0 100.0 ? ? ? ? ? ? 216 TYR A OH 1 99 A A +ATOM 805 N N . CYS A 1 100 ? 9.669 9.916 56.083 1.0 77.03 ? ? ? ? ? ? 217 CYS A N 1 100 A A +ATOM 806 C CA . CYS A 1 100 ? 10.459 10.100 54.872 1.0 82.44 ? ? ? ? ? ? 217 CYS A CA 1 100 A A +ATOM 807 C C . CYS A 1 100 ? 11.850 10.689 55.094 1.0 87.08 ? ? ? ? ? ? 217 CYS A C 1 100 A A +ATOM 808 O O . CYS A 1 100 ? 12.455 11.246 54.175 1.0 93.26 ? ? ? ? ? ? 217 CYS A O 1 100 A A +ATOM 809 C CB . CYS A 1 100 ? 9.684 10.965 53.880 1.0 89.04 ? ? ? ? ? ? 217 CYS A CB 1 100 A A +ATOM 810 S SG . CYS A 1 100 ? 8.256 10.130 53.168 1.0 100.0 ? ? ? ? ? ? 217 CYS A SG 1 100 A A +ATOM 811 N N . GLY A 1 101 ? 12.357 10.557 56.313 1.0 85.81 ? ? ? ? ? ? 218 GLY A N 1 101 A A +ATOM 812 C CA . GLY A 1 101 ? 13.676 11.071 56.622 1.0 87.04 ? ? ? ? ? ? 218 GLY A CA 1 101 A A +ATOM 813 C C . GLY A 1 101 ? 13.826 12.575 56.501 1.0 86.37 ? ? ? ? ? ? 218 GLY A C 1 101 A A +ATOM 814 O O . GLY A 1 101 ? 14.829 13.064 55.980 1.0 90.0 ? ? ? ? ? ? 218 GLY A O 1 101 A A +ATOM 815 N N . PHE A 1 102 ? 12.833 13.313 56.984 1.0 79.48 ? ? ? ? ? ? 219 PHE A N 1 102 A A +ATOM 816 C CA . PHE A 1 102 ? 12.885 14.768 56.930 1.0 73.33 ? ? ? ? ? ? 219 PHE A CA 1 102 A A +ATOM 817 C C . PHE A 1 102 ? 13.665 15.298 58.126 1.0 79.58 ? ? ? ? ? ? 219 PHE A C 1 102 A A +ATOM 818 O O . PHE A 1 102 ? 13.096 15.572 59.177 1.0 87.13 ? ? ? ? ? ? 219 PHE A O 1 102 A A +ATOM 819 C CB . PHE A 1 102 ? 11.469 15.351 56.916 1.0 54.87 ? ? ? ? ? ? 219 PHE A CB 1 102 A A +ATOM 820 C CG . PHE A 1 102 ? 10.931 15.602 55.531 1.0 54.38 ? ? ? ? ? ? 219 PHE A CG 1 102 A A +ATOM 821 C CD1 . PHE A 1 102 ? 10.736 14.542 54.645 1.0 47.42 ? ? ? ? ? ? 219 PHE A CD1 1 102 A A +ATOM 822 C CD2 . PHE A 1 102 ? 10.634 16.896 55.102 1.0 38.98 ? ? ? ? ? ? 219 PHE A CD2 1 102 A A +ATOM 823 C CE1 . PHE A 1 102 ? 10.245 14.764 53.355 1.0 33.19 ? ? ? ? ? ? 219 PHE A CE1 1 102 A A +ATOM 824 C CE2 . PHE A 1 102 ? 10.143 17.128 53.814 1.0 31.12 ? ? ? ? ? ? 219 PHE A CE2 1 102 A A +ATOM 825 C CZ . PHE A 1 102 ? 9.951 16.062 52.939 1.0 35.16 ? ? ? ? ? ? 219 PHE A CZ 1 102 A A +ATOM 826 N N . HIS A 1 103 ? 14.978 15.424 57.953 1.0 83.06 ? ? ? ? ? ? 220 HIS A N 1 103 A A +ATOM 827 C CA . HIS A 1 103 ? 15.870 15.917 58.999 1.0 90.4 ? ? ? ? ? ? 220 HIS A CA 1 103 A A +ATOM 828 C C . HIS A 1 103 ? 16.946 16.781 58.346 1.0 93.84 ? ? ? ? ? ? 220 HIS A C 1 103 A A +ATOM 829 O O . HIS A 1 103 ? 17.367 16.504 57.222 1.0 100.0 ? ? ? ? ? ? 220 HIS A O 1 103 A A +ATOM 830 C CB . HIS A 1 103 ? 16.521 14.744 59.733 1.0 90.54 ? ? ? ? ? ? 220 HIS A CB 1 103 A A +ATOM 831 C CG . HIS A 1 103 ? 17.269 15.139 60.967 1.0 100.0 ? ? ? ? ? ? 220 HIS A CG 1 103 A A +ATOM 832 N ND1 . HIS A 1 103 ? 18.320 14.402 61.469 1.0 100.0 ? ? ? ? ? ? 220 HIS A ND1 1 103 A A +ATOM 833 C CD2 . HIS A 1 103 ? 17.114 16.191 61.810 1.0 97.71 ? ? ? ? ? ? 220 HIS A CD2 1 103 A A +ATOM 834 C CE1 . HIS A 1 103 ? 18.778 14.978 62.564 1.0 100.0 ? ? ? ? ? ? 220 HIS A CE1 1 103 A A +ATOM 835 N NE2 . HIS A 1 103 ? 18.063 16.066 62.793 1.0 99.67 ? ? ? ? ? ? 220 HIS A NE2 1 103 A A +ATOM 836 N N . GLU A 1 104 ? 17.395 17.819 59.045 1.0 81.93 ? ? ? ? ? ? 221 GLU A N 1 104 A A +ATOM 837 C CA . GLU A 1 104 ? 18.410 18.710 58.492 1.0 73.21 ? ? ? ? ? ? 221 GLU A CA 1 104 A A +ATOM 838 C C . GLU A 1 104 ? 19.723 18.021 58.151 1.0 66.02 ? ? ? ? ? ? 221 GLU A C 1 104 A A +ATOM 839 O O . GLU A 1 104 ? 20.549 18.583 57.431 1.0 76.25 ? ? ? ? ? ? 221 GLU A O 1 104 A A +ATOM 840 C CB . GLU A 1 104 ? 18.684 19.862 59.456 1.0 74.49 ? ? ? ? ? ? 221 GLU A CB 1 104 A A +ATOM 841 C CG . GLU A 1 104 ? 19.037 19.422 60.860 1.0 91.38 ? ? ? ? ? ? 221 GLU A CG 1 104 A A +ATOM 842 C CD . GLU A 1 104 ? 19.376 20.594 61.757 1.0 100.0 ? ? ? ? ? ? 221 GLU A CD 1 104 A A +ATOM 843 O OE1 . GLU A 1 104 ? 19.907 20.365 62.866 1.0 100.0 ? ? ? ? ? ? 221 GLU A OE1 1 104 A A +ATOM 844 O OE2 . GLU A 1 104 ? 19.111 21.747 61.351 1.0 92.36 ? ? ? ? ? ? 221 GLU A OE2 1 104 A A +ATOM 845 N N . ASP A 1 105 ? 19.915 16.805 58.655 1.0 58.15 ? ? ? ? ? ? 222 ASP A N 1 105 A A +ATOM 846 C CA . ASP A 1 105 ? 21.153 16.077 58.397 1.0 64.41 ? ? ? ? ? ? 222 ASP A CA 1 105 A A +ATOM 847 C C . ASP A 1 105 ? 21.111 15.138 57.201 1.0 60.43 ? ? ? ? ? ? 222 ASP A C 1 105 A A +ATOM 848 O O . ASP A 1 105 ? 22.145 14.610 56.784 1.0 53.79 ? ? ? ? ? ? 222 ASP A O 1 105 A A +ATOM 849 C CB . ASP A 1 105 ? 21.568 15.304 59.645 1.0 82.99 ? ? ? ? ? ? 222 ASP A CB 1 105 A A +ATOM 850 C CG . ASP A 1 105 ? 22.047 16.216 60.754 1.0 97.61 ? ? ? ? ? ? 222 ASP A CG 1 105 A A +ATOM 851 O OD1 . ASP A 1 105 ? 21.192 16.888 61.369 1.0 100.0 ? ? ? ? ? ? 222 ASP A OD1 1 105 A A +ATOM 852 O OD2 . ASP A 1 105 ? 23.272 16.268 61.005 1.0 91.26 ? ? ? ? ? ? 222 ASP A OD2 1 105 A A +ATOM 853 N N . ASN A 1 106 ? 19.925 14.929 56.643 1.0 56.54 ? ? ? ? ? ? 223 ASN A N 1 106 A A +ATOM 854 C CA . ASN A 1 106 ? 19.793 14.049 55.490 1.0 56.77 ? ? ? ? ? ? 223 ASN A CA 1 106 A A +ATOM 855 C C . ASN A 1 106 ? 18.732 14.524 54.509 1.0 53.96 ? ? ? ? ? ? 223 ASN A C 1 106 A A +ATOM 856 O O . ASN A 1 106 ? 17.620 14.870 54.906 1.0 51.52 ? ? ? ? ? ? 223 ASN A O 1 106 A A +ATOM 857 C CB . ASN A 1 106 ? 19.463 12.625 55.937 1.0 72.23 ? ? ? ? ? ? 223 ASN A CB 1 106 A A +ATOM 858 C CG . ASN A 1 106 ? 19.111 11.717 54.767 1.0 93.67 ? ? ? ? ? ? 223 ASN A CG 1 106 A A +ATOM 859 O OD1 . ASN A 1 106 ? 17.964 11.291 54.622 1.0 100.0 ? ? ? ? ? ? 223 ASN A OD1 1 106 A A +ATOM 860 N ND2 . ASN A 1 106 ? 20.098 11.422 53.923 1.0 88.6 ? ? ? ? ? ? 223 ASN A ND2 1 106 A A +ATOM 861 N N . ILE A 1 107 ? 19.083 14.537 53.224 1.0 60.64 ? ? ? ? ? ? 224 ILE A N 1 107 A A +ATOM 862 C CA . ILE A 1 107 ? 18.154 14.955 52.179 1.0 57.31 ? ? ? ? ? ? 224 ILE A CA 1 107 A A +ATOM 863 C C . ILE A 1 107 ? 17.238 13.783 51.832 1.0 50.66 ? ? ? ? ? ? 224 ILE A C 1 107 A A +ATOM 864 O O . ILE A 1 107 ? 17.705 12.709 51.455 1.0 49.35 ? ? ? ? ? ? 224 ILE A O 1 107 A A +ATOM 865 C CB . ILE A 1 107 ? 18.904 15.407 50.913 1.0 49.19 ? ? ? ? ? ? 224 ILE A CB 1 107 A A +ATOM 866 C CG1 . ILE A 1 107 ? 19.634 16.724 51.191 1.0 46.06 ? ? ? ? ? ? 224 ILE A CG1 1 107 A A +ATOM 867 C CG2 . ILE A 1 107 ? 17.921 15.582 49.770 1.0 48.55 ? ? ? ? ? ? 224 ILE A CG2 1 107 A A +ATOM 868 C CD1 . ILE A 1 107 ? 20.371 17.287 49.992 1.0 49.6 ? ? ? ? ? ? 224 ILE A CD1 1 107 A A +ATOM 869 N N . PRO A 1 108 ? 15.915 13.984 51.943 1.0 38.91 ? ? ? ? ? ? 225 PRO A N 1 108 A A +ATOM 870 C CA . PRO A 1 108 ? 14.928 12.939 51.651 1.0 39.74 ? ? ? ? ? ? 225 PRO A CA 1 108 A A +ATOM 871 C C . PRO A 1 108 ? 14.946 12.415 50.220 1.0 43.17 ? ? ? ? ? ? 225 PRO A C 1 108 A A +ATOM 872 O O . PRO A 1 108 ? 15.039 13.187 49.266 1.0 45.06 ? ? ? ? ? ? 225 PRO A O 1 108 A A +ATOM 873 C CB . PRO A 1 108 ? 13.588 13.588 52.000 1.0 48.74 ? ? ? ? ? ? 225 PRO A CB 1 108 A A +ATOM 874 C CG . PRO A 1 108 ? 13.927 14.810 52.780 1.0 63.06 ? ? ? ? ? ? 225 PRO A CG 1 108 A A +ATOM 875 C CD . PRO A 1 108 ? 15.273 15.248 52.329 1.0 51.19 ? ? ? ? ? ? 225 PRO A CD 1 108 A A +ATOM 876 N N . GLN A 1 109 ? 14.837 11.095 50.086 1.0 38.21 ? ? ? ? ? ? 226 GLN A N 1 109 A A +ATOM 877 C CA . GLN A 1 109 ? 14.833 10.448 48.781 1.0 50.78 ? ? ? ? ? ? 226 GLN A CA 1 109 A A +ATOM 878 C C . GLN A 1 109 ? 13.430 10.430 48.178 1.0 50.49 ? ? ? ? ? ? 226 GLN A C 1 109 A A +ATOM 879 O O . GLN A 1 109 ? 12.476 9.981 48.813 1.0 46.1 ? ? ? ? ? ? 226 GLN A O 1 109 A A +ATOM 880 C CB . GLN A 1 109 ? 15.372 9.017 48.893 1.0 59.66 ? ? ? ? ? ? 226 GLN A CB 1 109 A A +ATOM 881 C CG . GLN A 1 109 ? 16.875 8.931 49.149 1.0 64.83 ? ? ? ? ? ? 226 GLN A CG 1 109 A A +ATOM 882 C CD . GLN A 1 109 ? 17.720 9.352 47.949 1.0 72.4 ? ? ? ? ? ? 226 GLN A CD 1 109 A A +ATOM 883 O OE1 . GLN A 1 109 ? 18.805 8.814 47.724 1.0 78.96 ? ? ? ? ? ? 226 GLN A OE1 1 109 A A +ATOM 884 N NE2 . GLN A 1 109 ? 17.226 10.315 47.176 1.0 81.37 ? ? ? ? ? ? 226 GLN A NE2 1 109 A A +ATOM 885 N N . LEU A 1 110 ? 13.329 10.911 46.940 1.0 53.52 ? ? ? ? ? ? 227 LEU A N 1 110 A A +ATOM 886 C CA . LEU A 1 110 ? 12.063 10.988 46.218 1.0 51.51 ? ? ? ? ? ? 227 LEU A CA 1 110 A A +ATOM 887 C C . LEU A 1 110 ? 11.239 9.705 46.204 1.0 54.39 ? ? ? ? ? ? 227 LEU A C 1 110 A A +ATOM 888 O O . LEU A 1 110 ? 10.021 9.748 46.380 1.0 47.39 ? ? ? ? ? ? 227 LEU A O 1 110 A A +ATOM 889 C CB . LEU A 1 110 ? 12.313 11.449 44.779 1.0 32.21 ? ? ? ? ? ? 227 LEU A CB 1 110 A A +ATOM 890 C CG . LEU A 1 110 ? 12.952 12.830 44.585 1.0 50.79 ? ? ? ? ? ? 227 LEU A CG 1 110 A A +ATOM 891 C CD1 . LEU A 1 110 ? 12.504 13.409 43.247 1.0 37.22 ? ? ? ? ? ? 227 LEU A CD1 1 110 A A +ATOM 892 C CD2 . LEU A 1 110 ? 12.560 13.766 45.720 1.0 43.31 ? ? ? ? ? ? 227 LEU A CD2 1 110 A A +ATOM 893 N N . GLU A 1 111 ? 11.889 8.567 45.988 1.0 52.15 ? ? ? ? ? ? 228 GLU A N 1 111 A A +ATOM 894 C CA . GLU A 1 111 ? 11.168 7.300 45.960 1.0 45.45 ? ? ? ? ? ? 228 GLU A CA 1 111 A A +ATOM 895 C C . GLU A 1 111 ? 10.405 7.101 47.261 1.0 46.15 ? ? ? ? ? ? 228 GLU A C 1 111 A A +ATOM 896 O O . GLU A 1 111 ? 9.326 6.510 47.275 1.0 43.58 ? ? ? ? ? ? 228 GLU A O 1 111 A A +ATOM 897 C CB . GLU A 1 111 ? 12.136 6.139 45.753 1.0 42.63 ? ? ? ? ? ? 228 GLU A CB 1 111 A A +ATOM 898 C CG . GLU A 1 111 ? 11.718 5.181 44.652 1.0 58.54 ? ? ? ? ? ? 228 GLU A CG 1 111 A A +ATOM 899 C CD . GLU A 1 111 ? 10.228 4.891 44.649 1.0 53.14 ? ? ? ? ? ? 228 GLU A CD 1 111 A A +ATOM 900 O OE1 . GLU A 1 111 ? 9.470 5.692 44.069 1.0 60.98 ? ? ? ? ? ? 228 GLU A OE1 1 111 A A +ATOM 901 O OE2 . GLU A 1 111 ? 9.814 3.861 45.220 1.0 59.24 ? ? ? ? ? ? 228 GLU A OE2 1 111 A A +ATOM 902 N N . ASP A 1 112 ? 10.975 7.604 48.350 1.0 39.29 ? ? ? ? ? ? 229 ASP A N 1 112 A A +ATOM 903 C CA . ASP A 1 112 ? 10.364 7.492 49.669 1.0 45.38 ? ? ? ? ? ? 229 ASP A CA 1 112 A A +ATOM 904 C C . ASP A 1 112 ? 9.177 8.435 49.772 1.0 42.03 ? ? ? ? ? ? 229 ASP A C 1 112 A A +ATOM 905 O O . ASP A 1 112 ? 8.062 8.022 50.097 1.0 43.4 ? ? ? ? ? ? 229 ASP A O 1 112 A A +ATOM 906 C CB . ASP A 1 112 ? 11.388 7.834 50.752 1.0 53.25 ? ? ? ? ? ? 229 ASP A CB 1 112 A A +ATOM 907 C CG . ASP A 1 112 ? 12.540 6.849 50.799 1.0 48.93 ? ? ? ? ? ? 229 ASP A CG 1 112 A A +ATOM 908 O OD1 . ASP A 1 112 ? 12.332 5.676 50.421 1.0 41.9 ? ? ? ? ? ? 229 ASP A OD1 1 112 A A +ATOM 909 O OD2 . ASP A 1 112 ? 13.649 7.249 51.213 1.0 50.62 ? ? ? ? ? ? 229 ASP A OD2 1 112 A A +ATOM 910 N N . VAL A 1 113 ? 9.425 9.708 49.490 1.0 27.1 ? ? ? ? ? ? 230 VAL A N 1 113 A A +ATOM 911 C CA . VAL A 1 113 ? 8.378 10.720 49.537 1.0 37.17 ? ? ? ? ? ? 230 VAL A CA 1 113 A A +ATOM 912 C C . VAL A 1 113 ? 7.219 10.330 48.623 1.0 36.33 ? ? ? ? ? ? 230 VAL A C 1 113 A A +ATOM 913 O O . VAL A 1 113 ? 6.056 10.369 49.025 1.0 24.34 ? ? ? ? ? ? 230 VAL A O 1 113 A A +ATOM 914 C CB . VAL A 1 113 ? 8.916 12.092 49.093 1.0 41.74 ? ? ? ? ? ? 230 VAL A CB 1 113 A A +ATOM 915 C CG1 . VAL A 1 113 ? 7.898 13.184 49.400 1.0 43.64 ? ? ? ? ? ? 230 VAL A CG1 1 113 A A +ATOM 916 C CG2 . VAL A 1 113 ? 10.228 12.376 49.784 1.0 49.93 ? ? ? ? ? ? 230 VAL A CG2 1 113 A A +ATOM 917 N N . SER A 1 114 ? 7.545 9.960 47.389 1.0 31.56 ? ? ? ? ? ? 231 SER A N 1 114 A A +ATOM 918 C CA . SER A 1 114 ? 6.527 9.556 46.430 1.0 45.89 ? ? ? ? ? ? 231 SER A CA 1 114 A A +ATOM 919 C C . SER A 1 114 ? 5.759 8.372 47.007 1.0 46.44 ? ? ? ? ? ? 231 SER A C 1 114 A A +ATOM 920 O O . SER A 1 114 ? 4.538 8.422 47.148 1.0 41.88 ? ? ? ? ? ? 231 SER A O 1 114 A A +ATOM 921 C CB . SER A 1 114 ? 7.176 9.163 45.099 1.0 50.12 ? ? ? ? ? ? 231 SER A CB 1 114 A A +ATOM 922 O OG . SER A 1 114 ? 6.233 8.561 44.228 1.0 48.07 ? ? ? ? ? ? 231 SER A OG 1 114 A A +ATOM 923 N N . GLN A 1 115 ? 6.489 7.310 47.344 1.0 43.04 ? ? ? ? ? ? 232 GLN A N 1 115 A A +ATOM 924 C CA . GLN A 1 115 ? 5.871 6.121 47.916 1.0 50.18 ? ? ? ? ? ? 232 GLN A CA 1 115 A A +ATOM 925 C C . GLN A 1 115 ? 4.974 6.481 49.095 1.0 60.01 ? ? ? ? ? ? 232 GLN A C 1 115 A A +ATOM 926 O O . GLN A 1 115 ? 3.939 5.863 49.316 1.0 67.03 ? ? ? ? ? ? 232 GLN A O 1 115 A A +ATOM 927 C CB . GLN A 1 115 ? 6.941 5.116 48.348 1.0 51.33 ? ? ? ? ? ? 232 GLN A CB 1 115 A A +ATOM 928 C CG . GLN A 1 115 ? 6.535 3.662 48.169 1.0 68.14 ? ? ? ? ? ? 232 GLN A CG 1 115 A A +ATOM 929 C CD . GLN A 1 115 ? 6.212 3.322 46.728 1.0 81.94 ? ? ? ? ? ? 232 GLN A CD 1 115 A A +ATOM 930 O OE1 . GLN A 1 115 ? 5.227 2.641 46.446 1.0 97.08 ? ? ? ? ? ? 232 GLN A OE1 1 115 A A +ATOM 931 N NE2 . GLN A 1 115 ? 6.905 3.692 45.656 1.0 20.0 ? ? ? ? ? ? 232 GLN A NE2 1 115 A A +ATOM 932 N N . PHE A 1 116 ? 5.393 7.503 49.838 1.0 57.14 ? ? ? ? ? ? 233 PHE A N 1 116 A A +ATOM 933 C CA . PHE A 1 116 ? 4.657 7.961 51.008 1.0 59.22 ? ? ? ? ? ? 233 PHE A CA 1 116 A A +ATOM 934 C C . PHE A 1 116 ? 3.381 8.676 50.588 1.0 56.05 ? ? ? ? ? ? 233 PHE A C 1 116 A A +ATOM 935 O O . PHE A 1 116 ? 2.274 8.229 50.888 1.0 68.44 ? ? ? ? ? ? 233 PHE A O 1 116 A A +ATOM 936 C CB . PHE A 1 116 ? 5.519 8.912 51.841 1.0 57.15 ? ? ? ? ? ? 233 PHE A CB 1 116 A A +ATOM 937 C CG . PHE A 1 116 ? 4.819 9.468 53.053 1.0 45.21 ? ? ? ? ? ? 233 PHE A CG 1 116 A A +ATOM 938 C CD1 . PHE A 1 116 ? 4.000 8.661 53.837 1.0 49.78 ? ? ? ? ? ? 233 PHE A CD1 1 116 A A +ATOM 939 C CD2 . PHE A 1 116 ? 4.984 10.800 53.416 1.0 49.92 ? ? ? ? ? ? 233 PHE A CD2 1 116 A A +ATOM 940 C CE1 . PHE A 1 116 ? 3.356 9.172 54.961 1.0 58.4 ? ? ? ? ? ? 233 PHE A CE1 1 116 A A +ATOM 941 C CE2 . PHE A 1 116 ? 4.345 11.321 54.538 1.0 48.9 ? ? ? ? ? ? 233 PHE A CE2 1 116 A A +ATOM 942 C CZ . PHE A 1 116 ? 3.530 10.506 55.312 1.0 48.87 ? ? ? ? ? ? 233 PHE A CZ 1 116 A A +ATOM 943 N N . LEU A 1 117 ? 3.555 9.796 49.899 1.0 40.06 ? ? ? ? ? ? 234 LEU A N 1 117 A A +ATOM 944 C CA . LEU A 1 117 ? 2.437 10.603 49.424 1.0 38.99 ? ? ? ? ? ? 234 LEU A CA 1 117 A A +ATOM 945 C C . LEU A 1 117 ? 1.347 9.745 48.793 1.0 50.84 ? ? ? ? ? ? 234 LEU A C 1 117 A A +ATOM 946 O O . LEU A 1 117 ? 0.158 10.050 48.905 1.0 56.22 ? ? ? ? ? ? 234 LEU A O 1 117 A A +ATOM 947 C CB . LEU A 1 117 ? 2.932 11.626 48.396 1.0 50.49 ? ? ? ? ? ? 234 LEU A CB 1 117 A A +ATOM 948 C CG . LEU A 1 117 ? 3.551 12.912 48.949 1.0 43.22 ? ? ? ? ? ? 234 LEU A CG 1 117 A A +ATOM 949 C CD1 . LEU A 1 117 ? 4.255 13.666 47.837 1.0 51.1 ? ? ? ? ? ? 234 LEU A CD1 1 117 A A +ATOM 950 C CD2 . LEU A 1 117 ? 2.466 13.772 49.564 1.0 30.63 ? ? ? ? ? ? 234 LEU A CD2 1 117 A A +ATOM 951 N N . GLN A 1 118 ? 1.755 8.672 48.125 1.0 41.81 ? ? ? ? ? ? 235 GLN A N 1 118 A A +ATOM 952 C CA . GLN A 1 118 ? 0.803 7.796 47.463 1.0 32.74 ? ? ? ? ? ? 235 GLN A CA 1 118 A A +ATOM 953 C C . GLN A 1 118 ? -0.194 7.165 48.424 1.0 30.32 ? ? ? ? ? ? 235 GLN A C 1 118 A A +ATOM 954 O O . GLN A 1 118 ? -1.376 7.046 48.103 1.0 43.72 ? ? ? ? ? ? 235 GLN A O 1 118 A A +ATOM 955 C CB . GLN A 1 118 ? 1.553 6.717 46.686 1.0 36.87 ? ? ? ? ? ? 235 GLN A CB 1 118 A A +ATOM 956 C CG . GLN A 1 118 ? 2.316 7.262 45.495 1.0 51.02 ? ? ? ? ? ? 235 GLN A CG 1 118 A A +ATOM 957 C CD . GLN A 1 118 ? 3.042 6.180 44.716 1.0 68.21 ? ? ? ? ? ? 235 GLN A CD 1 118 A A +ATOM 958 O OE1 . GLN A 1 118 ? 2.441 5.184 44.306 1.0 60.38 ? ? ? ? ? ? 235 GLN A OE1 1 118 A A +ATOM 959 N NE2 . GLN A 1 118 ? 4.342 6.370 44.506 1.0 66.98 ? ? ? ? ? ? 235 GLN A NE2 1 118 A A +ATOM 960 N N . THR A 1 119 ? 0.276 6.766 49.600 1.0 33.61 ? ? ? ? ? ? 236 THR A N 1 119 A A +ATOM 961 C CA . THR A 1 119 ? -0.599 6.142 50.590 1.0 38.05 ? ? ? ? ? ? 236 THR A CA 1 119 A A +ATOM 962 C C . THR A 1 119 ? -1.495 7.159 51.287 1.0 30.93 ? ? ? ? ? ? 236 THR A C 1 119 A A +ATOM 963 O O . THR A 1 119 ? -2.517 6.798 51.868 1.0 46.11 ? ? ? ? ? ? 236 THR A O 1 119 A A +ATOM 964 C CB . THR A 1 119 ? 0.213 5.399 51.661 1.0 34.8 ? ? ? ? ? ? 236 THR A CB 1 119 A A +ATOM 965 O OG1 . THR A 1 119 ? 1.301 6.227 52.085 1.0 51.78 ? ? ? ? ? ? 236 THR A OG1 1 119 A A +ATOM 966 C CG2 . THR A 1 119 ? 0.752 4.091 51.106 1.0 49.05 ? ? ? ? ? ? 236 THR A CG2 1 119 A A +ATOM 967 N N . CYS A 1 120 ? -1.109 8.431 51.228 1.0 16.22 ? ? ? ? ? ? 237 CYS A N 1 120 A A +ATOM 968 C CA . CYS A 1 120 ? -1.889 9.501 51.855 1.0 28.35 ? ? ? ? ? ? 237 CYS A CA 1 120 A A +ATOM 969 C C . CYS A 1 120 ? -3.040 9.949 50.963 1.0 31.88 ? ? ? ? ? ? 237 CYS A C 1 120 A A +ATOM 970 O O . CYS A 1 120 ? -4.200 9.941 51.373 1.0 16.59 ? ? ? ? ? ? 237 CYS A O 1 120 A A +ATOM 971 C CB . CYS A 1 120 ? -1.009 10.720 52.155 1.0 9.51 ? ? ? ? ? ? 237 CYS A CB 1 120 A A +ATOM 972 S SG . CYS A 1 120 ? 0.505 10.363 53.027 1.0 33.72 ? ? ? ? ? ? 237 CYS A SG 1 120 A A +ATOM 973 N N . THR A 1 121 ? -2.710 10.330 49.732 1.0 33.98 ? ? ? ? ? ? 238 THR A N 1 121 A A +ATOM 974 C CA . THR A 1 121 ? -3.710 10.807 48.788 1.0 28.31 ? ? ? ? ? ? 238 THR A CA 1 121 A A +ATOM 975 C C . THR A 1 121 ? -3.668 10.079 47.447 1.0 20.4 ? ? ? ? ? ? 238 THR A C 1 121 A A +ATOM 976 O O . THR A 1 121 ? -4.664 10.017 46.729 1.0 25.9 ? ? ? ? ? ? 238 THR A O 1 121 A A +ATOM 977 C CB . THR A 1 121 ? -3.529 12.314 48.545 1.0 22.53 ? ? ? ? ? ? 238 THR A CB 1 121 A A +ATOM 978 O OG1 . THR A 1 121 ? -2.226 12.550 48.008 1.0 28.52 ? ? ? ? ? ? 238 THR A OG1 1 121 A A +ATOM 979 C CG2 . THR A 1 121 ? -3.665 13.082 49.849 1.0 11.53 ? ? ? ? ? ? 238 THR A CG2 1 121 A A +ATOM 980 N N . GLY A 1 122 ? -2.514 9.518 47.119 1.0 18.84 ? ? ? ? ? ? 239 GLY A N 1 122 A A +ATOM 981 C CA . GLY A 1 122 ? -2.384 8.814 45.860 1.0 24.31 ? ? ? ? ? ? 239 GLY A CA 1 122 A A +ATOM 982 C C . GLY A 1 122 ? -1.453 9.554 44.922 1.0 34.75 ? ? ? ? ? ? 239 GLY A C 1 122 A A +ATOM 983 O O . GLY A 1 122 ? -1.175 9.101 43.807 1.0 30.25 ? ? ? ? ? ? 239 GLY A O 1 122 A A +ATOM 984 N N . PHE A 1 123 ? -0.967 10.701 45.386 1.0 33.76 ? ? ? ? ? ? 240 PHE A N 1 123 A A +ATOM 985 C CA . PHE A 1 123 ? -0.054 11.532 44.610 1.0 35.25 ? ? ? ? ? ? 240 PHE A CA 1 123 A A +ATOM 986 C C . PHE A 1 123 ? 1.319 10.889 44.523 1.0 34.59 ? ? ? ? ? ? 240 PHE A C 1 123 A A +ATOM 987 O O . PHE A 1 123 ? 1.946 10.592 45.540 1.0 41.61 ? ? ? ? ? ? 240 PHE A O 1 123 A A +ATOM 988 C CB . PHE A 1 123 ? 0.082 12.914 45.250 1.0 34.81 ? ? ? ? ? ? 240 PHE A CB 1 123 A A +ATOM 989 C CG . PHE A 1 123 ? -0.551 14.010 44.455 1.0 34.21 ? ? ? ? ? ? 240 PHE A CG 1 123 A A +ATOM 990 C CD1 . PHE A 1 123 ? -1.915 14.256 44.554 1.0 30.04 ? ? ? ? ? ? 240 PHE A CD1 1 123 A A +ATOM 991 C CD2 . PHE A 1 123 ? 0.212 14.791 43.598 1.0 16.01 ? ? ? ? ? ? 240 PHE A CD2 1 123 A A +ATOM 992 C CE1 . PHE A 1 123 ? -2.510 15.266 43.810 1.0 33.78 ? ? ? ? ? ? 240 PHE A CE1 1 123 A A +ATOM 993 C CE2 . PHE A 1 123 ? -0.370 15.802 42.850 1.0 32.94 ? ? ? ? ? ? 240 PHE A CE2 1 123 A A +ATOM 994 C CZ . PHE A 1 123 ? -1.735 16.041 42.956 1.0 20.13 ? ? ? ? ? ? 240 PHE A CZ 1 123 A A +ATOM 995 N N . ARG A 1 124 ? 1.784 10.673 43.300 1.0 42.92 ? ? ? ? ? ? 241 ARG A N 1 124 A A +ATOM 996 C CA . ARG A 1 124 ? 3.089 10.078 43.090 1.0 32.18 ? ? ? ? ? ? 241 ARG A CA 1 124 A A +ATOM 997 C C . ARG A 1 124 ? 3.994 11.164 42.559 1.0 27.59 ? ? ? ? ? ? 241 ARG A C 1 124 A A +ATOM 998 O O . ARG A 1 124 ? 3.537 12.083 41.890 1.0 28.12 ? ? ? ? ? ? 241 ARG A O 1 124 A A +ATOM 999 C CB . ARG A 1 124 ? 2.999 8.943 42.075 1.0 27.04 ? ? ? ? ? ? 241 ARG A CB 1 124 A A +ATOM 1000 C CG . ARG A 1 124 ? 1.868 9.099 41.077 1.0 26.05 ? ? ? ? ? ? 241 ARG A CG 1 124 A A +ATOM 1001 C CD . ARG A 1 124 ? 1.614 7.798 40.365 1.0 23.29 ? ? ? ? ? ? 241 ARG A CD 1 124 A A +ATOM 1002 N NE . ARG A 1 124 ? 1.126 6.779 41.283 1.0 32.91 ? ? ? ? ? ? 241 ARG A NE 1 124 A A +ATOM 1003 C CZ . ARG A 1 124 ? 0.761 5.560 40.904 1.0 44.01 ? ? ? ? ? ? 241 ARG A CZ 1 124 A A +ATOM 1004 N NH1 . ARG A 1 124 ? 0.834 5.219 39.625 1.0 52.31 ? ? ? ? ? ? 241 ARG A NH1 1 124 A A +ATOM 1005 N NH2 . ARG A 1 124 ? 0.318 4.684 41.797 1.0 54.45 ? ? ? ? ? ? 241 ARG A NH2 1 124 A A +ATOM 1006 N N . LEU A 1 125 ? 5.279 11.064 42.862 1.0 34.78 ? ? ? ? ? ? 242 LEU A N 1 125 A A +ATOM 1007 C CA . LEU A 1 125 ? 6.224 12.057 42.387 1.0 34.24 ? ? ? ? ? ? 242 LEU A CA 1 125 A A +ATOM 1008 C C . LEU A 1 125 ? 6.834 11.599 41.071 1.0 35.4 ? ? ? ? ? ? 242 LEU A C 1 125 A A +ATOM 1009 O O . LEU A 1 125 ? 6.844 10.411 40.761 1.0 28.24 ? ? ? ? ? ? 242 LEU A O 1 125 A A +ATOM 1010 C CB . LEU A 1 125 ? 7.324 12.272 43.428 1.0 39.08 ? ? ? ? ? ? 242 LEU A CB 1 125 A A +ATOM 1011 C CG . LEU A 1 125 ? 6.945 13.105 44.658 1.0 50.27 ? ? ? ? ? ? 242 LEU A CG 1 125 A A +ATOM 1012 C CD1 . LEU A 1 125 ? 8.149 13.235 45.577 1.0 40.92 ? ? ? ? ? ? 242 LEU A CD1 1 125 A A +ATOM 1013 C CD2 . LEU A 1 125 ? 6.468 14.483 44.227 1.0 54.53 ? ? ? ? ? ? 242 LEU A CD2 1 125 A A +ATOM 1014 N N . ARG A 1 126 ? 7.318 12.558 40.290 1.0 36.98 ? ? ? ? ? ? 243 ARG A N 1 126 A A +ATOM 1015 C CA . ARG A 1 126 ? 7.960 12.268 39.016 1.0 38.32 ? ? ? ? ? ? 243 ARG A CA 1 126 A A +ATOM 1016 C C . ARG A 1 126 ? 9.085 13.270 38.820 1.0 46.23 ? ? ? ? ? ? 243 ARG A C 1 126 A A +ATOM 1017 O O . ARG A 1 126 ? 8.855 14.478 38.802 1.0 58.57 ? ? ? ? ? ? 243 ARG A O 1 126 A A +ATOM 1018 C CB . ARG A 1 126 ? 6.970 12.374 37.852 1.0 38.91 ? ? ? ? ? ? 243 ARG A CB 1 126 A A +ATOM 1019 C CG . ARG A 1 126 ? 7.475 11.684 36.597 1.0 36.65 ? ? ? ? ? ? 243 ARG A CG 1 126 A A +ATOM 1020 C CD . ARG A 1 126 ? 6.650 12.017 35.373 1.0 50.44 ? ? ? ? ? ? 243 ARG A CD 1 126 A A +ATOM 1021 N NE . ARG A 1 126 ? 7.325 11.565 34.159 1.0 47.02 ? ? ? ? ? ? 243 ARG A NE 1 126 A A +ATOM 1022 C CZ . ARG A 1 126 ? 6.990 10.476 33.478 1.0 42.93 ? ? ? ? ? ? 243 ARG A CZ 1 126 A A +ATOM 1023 N NH1 . ARG A 1 126 ? 5.985 9.715 33.884 1.0 24.97 ? ? ? ? ? ? 243 ARG A NH1 1 126 A A +ATOM 1024 N NH2 . ARG A 1 126 ? 7.669 10.142 32.393 1.0 57.01 ? ? ? ? ? ? 243 ARG A NH2 1 126 A A +ATOM 1025 N N . PRO A 1 127 ? 10.327 12.776 38.680 1.0 42.99 ? ? ? ? ? ? 244 PRO A N 1 127 A A +ATOM 1026 C CA . PRO A 1 127 ? 11.482 13.660 38.487 1.0 38.6 ? ? ? ? ? ? 244 PRO A CA 1 127 A A +ATOM 1027 C C . PRO A 1 127 ? 11.475 14.384 37.140 1.0 46.2 ? ? ? ? ? ? 244 PRO A C 1 127 A A +ATOM 1028 O O . PRO A 1 127 ? 11.559 13.760 36.084 1.0 54.57 ? ? ? ? ? ? 244 PRO A O 1 127 A A +ATOM 1029 C CB . PRO A 1 127 ? 12.679 12.722 38.637 1.0 26.93 ? ? ? ? ? ? 244 PRO A CB 1 127 A A +ATOM 1030 C CG . PRO A 1 127 ? 12.152 11.381 38.275 1.0 26.61 ? ? ? ? ? ? 244 PRO A CG 1 127 A A +ATOM 1031 C CD . PRO A 1 127 ? 10.714 11.355 38.699 1.0 43.68 ? ? ? ? ? ? 244 PRO A CD 1 127 A A +ATOM 1032 N N . VAL A 1 128 ? 11.374 15.709 37.188 1.0 40.08 ? ? ? ? ? ? 245 VAL A N 1 128 A A +ATOM 1033 C CA . VAL A 1 128 ? 11.360 16.524 35.978 1.0 38.82 ? ? ? ? ? ? 245 VAL A CA 1 128 A A +ATOM 1034 C C . VAL A 1 128 ? 12.760 17.073 35.719 1.0 44.01 ? ? ? ? ? ? 245 VAL A C 1 128 A A +ATOM 1035 O O . VAL A 1 128 ? 13.454 17.481 36.651 1.0 36.98 ? ? ? ? ? ? 245 VAL A O 1 128 A A +ATOM 1036 C CB . VAL A 1 128 ? 10.364 17.708 36.115 1.0 37.07 ? ? ? ? ? ? 245 VAL A CB 1 128 A A +ATOM 1037 C CG1 . VAL A 1 128 ? 10.943 18.784 37.020 1.0 38.19 ? ? ? ? ? ? 245 VAL A CG1 1 128 A A +ATOM 1038 C CG2 . VAL A 1 128 ? 10.041 18.279 34.752 1.0 39.24 ? ? ? ? ? ? 245 VAL A CG2 1 128 A A +ATOM 1039 N N . ALA A 1 129 ? 13.173 17.080 34.456 1.0 54.02 ? ? ? ? ? ? 246 ALA A N 1 129 A A +ATOM 1040 C CA . ALA A 1 129 ? 14.489 17.589 34.088 1.0 57.88 ? ? ? ? ? ? 246 ALA A CA 1 129 A A +ATOM 1041 C C . ALA A 1 129 ? 14.769 18.920 34.787 1.0 60.78 ? ? ? ? ? ? 246 ALA A C 1 129 A A +ATOM 1042 O O . ALA A 1 129 ? 15.664 19.015 35.627 1.0 67.19 ? ? ? ? ? ? 246 ALA A O 1 129 A A +ATOM 1043 C CB . ALA A 1 129 ? 14.571 17.763 32.579 1.0 77.71 ? ? ? ? ? ? 246 ALA A CB 1 129 A A +ATOM 1044 N N . GLY A 1 130 ? 13.992 19.940 34.437 1.0 52.89 ? ? ? ? ? ? 247 GLY A N 1 130 A A +ATOM 1045 C CA . GLY A 1 130 ? 14.163 21.251 35.037 1.0 62.98 ? ? ? ? ? ? 247 GLY A CA 1 130 A A +ATOM 1046 C C . GLY A 1 130 ? 12.835 21.965 35.205 1.0 67.72 ? ? ? ? ? ? 247 GLY A C 1 130 A A +ATOM 1047 O O . GLY A 1 130 ? 12.324 22.099 36.318 1.0 80.51 ? ? ? ? ? ? 247 GLY A O 1 130 A A +ATOM 1048 N N . LEU A 1 131 ? 12.274 22.421 34.091 1.0 65.11 ? ? ? ? ? ? 248 LEU A N 1 131 A A +ATOM 1049 C CA . LEU A 1 131 ? 10.998 23.126 34.098 1.0 56.05 ? ? ? ? ? ? 248 LEU A CA 1 131 A A +ATOM 1050 C C . LEU A 1 131 ? 10.159 22.668 32.911 1.0 61.16 ? ? ? ? ? ? 248 LEU A C 1 131 A A +ATOM 1051 O O . LEU A 1 131 ? 10.671 22.027 31.992 1.0 74.12 ? ? ? ? ? ? 248 LEU A O 1 131 A A +ATOM 1052 C CB . LEU A 1 131 ? 11.234 24.637 34.012 1.0 59.12 ? ? ? ? ? ? 248 LEU A CB 1 131 A A +ATOM 1053 C CG . LEU A 1 131 ? 11.497 25.237 32.626 1.0 79.7 ? ? ? ? ? ? 248 LEU A CG 1 131 A A +ATOM 1054 C CD1 . LEU A 1 131 ? 11.429 26.749 32.712 1.0 87.18 ? ? ? ? ? ? 248 LEU A CD1 1 131 A A +ATOM 1055 C CD2 . LEU A 1 131 ? 12.850 24.785 32.111 1.0 72.88 ? ? ? ? ? ? 248 LEU A CD2 1 131 A A +ATOM 1056 N N . LEU A 1 132 ? 8.871 22.989 32.934 1.0 46.27 ? ? ? ? ? ? 249 LEU A N 1 132 A A +ATOM 1057 C CA . LEU A 1 132 ? 7.977 22.623 31.842 1.0 45.65 ? ? ? ? ? ? 249 LEU A CA 1 132 A A +ATOM 1058 C C . LEU A 1 132 ? 6.771 23.550 31.775 1.0 47.53 ? ? ? ? ? ? 249 LEU A C 1 132 A A +ATOM 1059 O O . LEU A 1 132 ? 6.452 24.240 32.739 1.0 50.63 ? ? ? ? ? ? 249 LEU A O 1 132 A A +ATOM 1060 C CB . LEU A 1 132 ? 7.506 21.172 31.976 1.0 32.93 ? ? ? ? ? ? 249 LEU A CB 1 132 A A +ATOM 1061 C CG . LEU A 1 132 ? 7.514 20.481 33.336 1.0 37.61 ? ? ? ? ? ? 249 LEU A CG 1 132 A A +ATOM 1062 C CD1 . LEU A 1 132 ? 6.701 21.274 34.337 1.0 47.51 ? ? ? ? ? ? 249 LEU A CD1 1 132 A A +ATOM 1063 C CD2 . LEU A 1 132 ? 6.950 19.084 33.169 1.0 20.77 ? ? ? ? ? ? 249 LEU A CD2 1 132 A A +ATOM 1064 N N . SER A 1 133 ? 6.114 23.569 30.621 1.0 49.94 ? ? ? ? ? ? 250 SER A N 1 133 A A +ATOM 1065 C CA . SER A 1 133 ? 4.951 24.417 30.398 1.0 58.56 ? ? ? ? ? ? 250 SER A CA 1 133 A A +ATOM 1066 C C . SER A 1 133 ? 3.888 24.248 31.481 1.0 61.47 ? ? ? ? ? ? 250 SER A C 1 133 A A +ATOM 1067 O O . SER A 1 133 ? 3.831 23.215 32.148 1.0 66.63 ? ? ? ? ? ? 250 SER A O 1 133 A A +ATOM 1068 C CB . SER A 1 133 ? 4.348 24.105 29.025 1.0 56.4 ? ? ? ? ? ? 250 SER A CB 1 133 A A +ATOM 1069 O OG . SER A 1 133 ? 3.095 24.739 28.854 1.0 80.26 ? ? ? ? ? ? 250 SER A OG 1 133 A A +ATOM 1070 N N . SER A 1 134 ? 3.052 25.269 31.657 1.0 57.53 ? ? ? ? ? ? 251 SER A N 1 134 A A +ATOM 1071 C CA . SER A 1 134 ? 1.987 25.218 32.650 1.0 45.91 ? ? ? ? ? ? 251 SER A CA 1 134 A A +ATOM 1072 C C . SER A 1 134 ? 1.015 24.131 32.239 1.0 41.98 ? ? ? ? ? ? 251 SER A C 1 134 A A +ATOM 1073 O O . SER A 1 134 ? 0.457 23.428 33.080 1.0 47.44 ? ? ? ? ? ? 251 SER A O 1 134 A A +ATOM 1074 C CB . SER A 1 134 ? 1.252 26.554 32.717 1.0 59.78 ? ? ? ? ? ? 251 SER A CB 1 134 A A +ATOM 1075 O OG . SER A 1 134 ? 2.157 27.639 32.622 1.0 81.13 ? ? ? ? ? ? 251 SER A OG 1 134 A A +ATOM 1076 N N . ARG A 1 135 ? 0.818 24.004 30.932 1.0 30.74 ? ? ? ? ? ? 252 ARG A N 1 135 A A +ATOM 1077 C CA . ARG A 1 135 ? -0.081 23.000 30.384 1.0 31.41 ? ? ? ? ? ? 252 ARG A CA 1 135 A A +ATOM 1078 C C . ARG A 1 135 ? 0.420 21.607 30.739 1.0 23.75 ? ? ? ? ? ? 252 ARG A C 1 135 A A +ATOM 1079 O O . ARG A 1 135 ? -0.362 20.725 31.087 1.0 34.67 ? ? ? ? ? ? 252 ARG A O 1 135 A A +ATOM 1080 C CB . ARG A 1 135 ? -0.170 23.143 28.865 1.0 35.53 ? ? ? ? ? ? 252 ARG A CB 1 135 A A +ATOM 1081 C CG . ARG A 1 135 ? -1.028 22.085 28.192 1.0 53.82 ? ? ? ? ? ? 252 ARG A CG 1 135 A A +ATOM 1082 C CD . ARG A 1 135 ? -1.061 22.280 26.687 1.0 46.69 ? ? ? ? ? ? 252 ARG A CD 1 135 A A +ATOM 1083 N NE . ARG A 1 135 ? -1.599 23.586 26.319 1.0 40.65 ? ? ? ? ? ? 252 ARG A NE 1 135 A A +ATOM 1084 C CZ . ARG A 1 135 ? -2.881 23.922 26.419 1.0 48.03 ? ? ? ? ? ? 252 ARG A CZ 1 135 A A +ATOM 1085 N NH1 . ARG A 1 135 ? -3.765 23.048 26.879 1.0 44.01 ? ? ? ? ? ? 252 ARG A NH1 1 135 A A +ATOM 1086 N NH2 . ARG A 1 135 ? -3.281 25.132 26.058 1.0 50.32 ? ? ? ? ? ? 252 ARG A NH2 1 135 A A +ATOM 1087 N N . ASP A 1 136 ? 1.732 21.418 30.648 1.0 16.34 ? ? ? ? ? ? 253 ASP A N 1 136 A A +ATOM 1088 C CA . ASP A 1 136 ? 2.348 20.128 30.958 1.0 28.42 ? ? ? ? ? ? 253 ASP A CA 1 136 A A +ATOM 1089 C C . ASP A 1 136 ? 2.353 19.853 32.453 1.0 29.16 ? ? ? ? ? ? 253 ASP A C 1 136 A A +ATOM 1090 O O . ASP A 1 136 ? 2.029 18.752 32.895 1.0 33.43 ? ? ? ? ? ? 253 ASP A O 1 136 A A +ATOM 1091 C CB . ASP A 1 136 ? 3.778 20.091 30.425 1.0 46.51 ? ? ? ? ? ? 253 ASP A CB 1 136 A A +ATOM 1092 C CG . ASP A 1 136 ? 3.839 20.249 28.923 1.0 73.75 ? ? ? ? ? ? 253 ASP A CG 1 136 A A +ATOM 1093 O OD1 . ASP A 1 136 ? 3.678 21.386 28.432 1.0 70.2 ? ? ? ? ? ? 253 ASP A OD1 1 136 A A +ATOM 1094 O OD2 . ASP A 1 136 ? 4.045 19.232 28.232 1.0 82.65 ? ? ? ? ? ? 253 ASP A OD2 1 136 A A +ATOM 1095 N N . PHE A 1 137 ? 2.736 20.860 33.225 1.0 36.9 ? ? ? ? ? ? 254 PHE A N 1 137 A A +ATOM 1096 C CA . PHE A 1 137 ? 2.772 20.741 34.672 1.0 47.73 ? ? ? ? ? ? 254 PHE A CA 1 137 A A +ATOM 1097 C C . PHE A 1 137 ? 1.372 20.375 35.161 1.0 53.7 ? ? ? ? ? ? 254 PHE A C 1 137 A A +ATOM 1098 O O . PHE A 1 137 ? 1.170 19.324 35.772 1.0 62.08 ? ? ? ? ? ? 254 PHE A O 1 137 A A +ATOM 1099 C CB . PHE A 1 137 ? 3.210 22.070 35.291 1.0 58.44 ? ? ? ? ? ? 254 PHE A CB 1 137 A A +ATOM 1100 C CG . PHE A 1 137 ? 3.632 21.970 36.730 1.0 64.83 ? ? ? ? ? ? 254 PHE A CG 1 137 A A +ATOM 1101 C CD1 . PHE A 1 137 ? 3.566 20.759 37.415 1.0 76.33 ? ? ? ? ? ? 254 PHE A CD1 1 137 A A +ATOM 1102 C CD2 . PHE A 1 137 ? 4.099 23.096 37.403 1.0 86.07 ? ? ? ? ? ? 254 PHE A CD2 1 137 A A +ATOM 1103 C CE1 . PHE A 1 137 ? 3.954 20.673 38.750 1.0 86.3 ? ? ? ? ? ? 254 PHE A CE1 1 137 A A +ATOM 1104 C CE2 . PHE A 1 137 ? 4.491 23.020 38.741 1.0 100.0 ? ? ? ? ? ? 254 PHE A CE2 1 137 A A +ATOM 1105 C CZ . PHE A 1 137 ? 4.419 21.807 39.414 1.0 95.87 ? ? ? ? ? ? 254 PHE A CZ 1 137 A A +ATOM 1106 N N . LEU A 1 138 ? 0.411 21.249 34.880 1.0 40.62 ? ? ? ? ? ? 255 LEU A N 1 138 A A +ATOM 1107 C CA . LEU A 1 138 ? -0.969 21.037 35.283 1.0 29.53 ? ? ? ? ? ? 255 LEU A CA 1 138 A A +ATOM 1108 C C . LEU A 1 138 ? -1.497 19.693 34.803 1.0 35.98 ? ? ? ? ? ? 255 LEU A C 1 138 A A +ATOM 1109 O O . LEU A 1 138 ? -2.260 19.033 35.508 1.0 44.56 ? ? ? ? ? ? 255 LEU A O 1 138 A A +ATOM 1110 C CB . LEU A 1 138 ? -1.841 22.166 34.739 1.0 37.3 ? ? ? ? ? ? 255 LEU A CB 1 138 A A +ATOM 1111 C CG . LEU A 1 138 ? -1.898 23.438 35.595 1.0 31.39 ? ? ? ? ? ? 255 LEU A CG 1 138 A A +ATOM 1112 C CD1 . LEU A 1 138 ? -0.602 23.622 36.351 1.0 20.93 ? ? ? ? ? ? 255 LEU A CD1 1 138 A A +ATOM 1113 C CD2 . LEU A 1 138 ? -2.174 24.633 34.707 1.0 19.28 ? ? ? ? ? ? 255 LEU A CD2 1 138 A A +ATOM 1114 N N . GLY A 1 139 ? -1.089 19.288 33.605 1.0 23.82 ? ? ? ? ? ? 256 GLY A N 1 139 A A +ATOM 1115 C CA . GLY A 1 139 ? -1.541 18.019 33.064 1.0 22.93 ? ? ? ? ? ? 256 GLY A CA 1 139 A A +ATOM 1116 C C . GLY A 1 139 ? -1.191 16.845 33.961 1.0 27.16 ? ? ? ? ? ? 256 GLY A C 1 139 A A +ATOM 1117 O O . GLY A 1 139 ? -1.919 15.853 34.022 1.0 13.49 ? ? ? ? ? ? 256 GLY A O 1 139 A A +ATOM 1118 N N . GLY A 1 140 ? -0.071 16.951 34.665 1.0 21.45 ? ? ? ? ? ? 257 GLY A N 1 140 A A +ATOM 1119 C CA . GLY A 1 140 ? 0.334 15.878 35.549 1.0 40.44 ? ? ? ? ? ? 257 GLY A CA 1 140 A A +ATOM 1120 C C . GLY A 1 140 ? -0.604 15.773 36.733 1.0 40.36 ? ? ? ? ? ? 257 GLY A C 1 140 A A +ATOM 1121 O O . GLY A 1 140 ? -0.908 14.684 37.208 1.0 47.8 ? ? ? ? ? ? 257 GLY A O 1 140 A A +ATOM 1122 N N . LEU A 1 141 ? -1.067 16.922 37.207 1.0 40.24 ? ? ? ? ? ? 258 LEU A N 1 141 A A +ATOM 1123 C CA . LEU A 1 141 ? -1.972 16.979 38.346 1.0 34.55 ? ? ? ? ? ? 258 LEU A CA 1 141 A A +ATOM 1124 C C . LEU A 1 141 ? -3.256 16.189 38.107 1.0 24.3 ? ? ? ? ? ? 258 LEU A C 1 141 A A +ATOM 1125 O O . LEU A 1 141 ? -3.851 15.670 39.047 1.0 33.84 ? ? ? ? ? ? 258 LEU A O 1 141 A A +ATOM 1126 C CB . LEU A 1 141 ? -2.298 18.445 38.678 1.0 35.0 ? ? ? ? ? ? 258 LEU A CB 1 141 A A +ATOM 1127 C CG . LEU A 1 141 ? -1.083 19.362 38.906 1.0 41.25 ? ? ? ? ? ? 258 LEU A CG 1 141 A A +ATOM 1128 C CD1 . LEU A 1 141 ? -1.519 20.823 38.867 1.0 31.39 ? ? ? ? ? ? 258 LEU A CD1 1 141 A A +ATOM 1129 C CD2 . LEU A 1 141 ? -0.422 19.025 40.234 1.0 28.27 ? ? ? ? ? ? 258 LEU A CD2 1 141 A A +ATOM 1130 N N . ALA A 1 142 ? -3.678 16.100 36.851 1.0 13.11 ? ? ? ? ? ? 259 ALA A N 1 142 A A +ATOM 1131 C CA . ALA A 1 142 ? -4.896 15.379 36.502 1.0 16.98 ? ? ? ? ? ? 259 ALA A CA 1 142 A A +ATOM 1132 C C . ALA A 1 142 ? -4.786 13.910 36.865 1.0 19.95 ? ? ? ? ? ? 259 ALA A C 1 142 A A +ATOM 1133 O O . ALA A 1 142 ? -5.793 13.209 36.948 1.0 33.25 ? ? ? ? ? ? 259 ALA A O 1 142 A A +ATOM 1134 C CB . ALA A 1 142 ? -5.181 15.523 35.022 1.0 17.11 ? ? ? ? ? ? 259 ALA A CB 1 142 A A +ATOM 1135 N N . PHE A 1 143 ? -3.558 13.445 37.076 1.0 17.1 ? ? ? ? ? ? 260 PHE A N 1 143 A A +ATOM 1136 C CA . PHE A 1 143 ? -3.315 12.047 37.423 1.0 29.31 ? ? ? ? ? ? 260 PHE A CA 1 143 A A +ATOM 1137 C C . PHE A 1 143 ? -2.744 11.957 38.823 1.0 25.66 ? ? ? ? ? ? 260 PHE A C 1 143 A A +ATOM 1138 O O . PHE A 1 143 ? -2.286 10.894 39.246 1.0 36.3 ? ? ? ? ? ? 260 PHE A O 1 143 A A +ATOM 1139 C CB . PHE A 1 143 ? -2.328 11.412 36.441 1.0 17.78 ? ? ? ? ? ? 260 PHE A CB 1 143 A A +ATOM 1140 C CG . PHE A 1 143 ? -2.717 11.573 35.010 1.0 15.54 ? ? ? ? ? ? 260 PHE A CG 1 143 A A +ATOM 1141 C CD1 . PHE A 1 143 ? -2.506 12.781 34.353 1.0 23.61 ? ? ? ? ? ? 260 PHE A CD1 1 143 A A +ATOM 1142 C CD2 . PHE A 1 143 ? -3.310 10.528 34.322 1.0 9.2 ? ? ? ? ? ? 260 PHE A CD2 1 143 A A +ATOM 1143 C CE1 . PHE A 1 143 ? -2.883 12.949 33.028 1.0 19.04 ? ? ? ? ? ? 260 PHE A CE1 1 143 A A +ATOM 1144 C CE2 . PHE A 1 143 ? -3.690 10.684 32.996 1.0 28.72 ? ? ? ? ? ? 260 PHE A CE2 1 143 A A +ATOM 1145 C CZ . PHE A 1 143 ? -3.475 11.898 32.346 1.0 32.54 ? ? ? ? ? ? 260 PHE A CZ 1 143 A A +ATOM 1146 N N . ARG A 1 144 ? -2.775 13.080 39.534 1.0 30.74 ? ? ? ? ? ? 261 ARG A N 1 144 A A +ATOM 1147 C CA . ARG A 1 144 ? -2.246 13.150 40.890 1.0 30.16 ? ? ? ? ? ? 261 ARG A CA 1 144 A A +ATOM 1148 C C . ARG A 1 144 ? -0.763 12.820 40.842 1.0 28.65 ? ? ? ? ? ? 261 ARG A C 1 144 A A +ATOM 1149 O O . ARG A 1 144 ? -0.241 12.094 41.689 1.0 34.8 ? ? ? ? ? ? 261 ARG A O 1 144 A A +ATOM 1150 C CB . ARG A 1 144 ? -2.985 12.172 41.805 1.0 30.66 ? ? ? ? ? ? 261 ARG A CB 1 144 A A +ATOM 1151 C CG . ARG A 1 144 ? -4.447 12.519 41.996 1.0 32.76 ? ? ? ? ? ? 261 ARG A CG 1 144 A A +ATOM 1152 C CD . ARG A 1 144 ? -4.968 12.096 43.353 1.0 39.38 ? ? ? ? ? ? 261 ARG A CD 1 144 A A +ATOM 1153 N NE . ARG A 1 144 ? -6.403 12.351 43.458 1.0 47.15 ? ? ? ? ? ? 261 ARG A NE 1 144 A A +ATOM 1154 C CZ . ARG A 1 144 ? -7.078 12.453 44.598 1.0 30.86 ? ? ? ? ? ? 261 ARG A CZ 1 144 A A +ATOM 1155 N NH1 . ARG A 1 144 ? -6.463 12.307 45.762 1.0 48.34 ? ? ? ? ? ? 261 ARG A NH1 1 144 A A +ATOM 1156 N NH2 . ARG A 1 144 ? -8.379 12.697 44.570 1.0 31.94 ? ? ? ? ? ? 261 ARG A NH2 1 144 A A +ATOM 1157 N N . VAL A 1 145 ? -0.106 13.363 39.819 1.0 21.99 ? ? ? ? ? ? 262 VAL A N 1 145 A A +ATOM 1158 C CA . VAL A 1 145 ? 1.323 13.176 39.599 1.0 24.05 ? ? ? ? ? ? 262 VAL A CA 1 145 A A +ATOM 1159 C C . VAL A 1 145 ? 2.006 14.537 39.676 1.0 29.44 ? ? ? ? ? ? 262 VAL A C 1 145 A A +ATOM 1160 O O . VAL A 1 145 ? 1.625 15.475 38.968 1.0 27.93 ? ? ? ? ? ? 262 VAL A O 1 145 A A +ATOM 1161 C CB . VAL A 1 145 ? 1.608 12.557 38.210 1.0 11.44 ? ? ? ? ? ? 262 VAL A CB 1 145 A A +ATOM 1162 C CG1 . VAL A 1 145 ? 3.078 12.659 37.883 1.0 21.4 ? ? ? ? ? ? 262 VAL A CG1 1 145 A A +ATOM 1163 C CG2 . VAL A 1 145 ? 1.163 11.099 38.184 1.0 29.17 ? ? ? ? ? ? 262 VAL A CG2 1 145 A A +ATOM 1164 N N . PHE A 1 146 ? 3.011 14.643 40.542 1.0 40.09 ? ? ? ? ? ? 263 PHE A N 1 146 A A +ATOM 1165 C CA . PHE A 1 146 ? 3.742 15.892 40.717 1.0 42.03 ? ? ? ? ? ? 263 PHE A CA 1 146 A A +ATOM 1166 C C . PHE A 1 146 ? 5.134 15.815 40.094 1.0 47.79 ? ? ? ? ? ? 263 PHE A C 1 146 A A +ATOM 1167 O O . PHE A 1 146 ? 5.911 14.907 40.393 1.0 49.0 ? ? ? ? ? ? 263 PHE A O 1 146 A A +ATOM 1168 C CB . PHE A 1 146 ? 3.860 16.228 42.206 1.0 28.47 ? ? ? ? ? ? 263 PHE A CB 1 146 A A +ATOM 1169 C CG . PHE A 1 146 ? 4.388 17.607 42.476 1.0 32.77 ? ? ? ? ? ? 263 PHE A CG 1 146 A A +ATOM 1170 C CD1 . PHE A 1 146 ? 3.850 18.715 41.824 1.0 52.86 ? ? ? ? ? ? 263 PHE A CD1 1 146 A A +ATOM 1171 C CD2 . PHE A 1 146 ? 5.426 17.800 43.381 1.0 25.5 ? ? ? ? ? ? 263 PHE A CD2 1 146 A A +ATOM 1172 C CE1 . PHE A 1 146 ? 4.339 19.994 42.070 1.0 46.81 ? ? ? ? ? ? 263 PHE A CE1 1 146 A A +ATOM 1173 C CE2 . PHE A 1 146 ? 5.923 19.074 43.635 1.0 42.05 ? ? ? ? ? ? 263 PHE A CE2 1 146 A A +ATOM 1174 C CZ . PHE A 1 146 ? 5.378 20.174 42.977 1.0 54.09 ? ? ? ? ? ? 263 PHE A CZ 1 146 A A +ATOM 1175 N N . HIS A 1 147 ? 5.444 16.766 39.219 1.0 50.29 ? ? ? ? ? ? 264 HIS A N 1 147 A A +ATOM 1176 C CA . HIS A 1 147 ? 6.747 16.796 38.570 1.0 55.68 ? ? ? ? ? ? 264 HIS A CA 1 147 A A +ATOM 1177 C C . HIS A 1 147 ? 7.709 17.534 39.486 1.0 54.21 ? ? ? ? ? ? 264 HIS A C 1 147 A A +ATOM 1178 O O . HIS A 1 147 ? 7.685 18.759 39.591 1.0 66.04 ? ? ? ? ? ? 264 HIS A O 1 147 A A +ATOM 1179 C CB . HIS A 1 147 ? 6.632 17.476 37.203 1.0 60.8 ? ? ? ? ? ? 264 HIS A CB 1 147 A A +ATOM 1180 C CG . HIS A 1 147 ? 5.915 16.646 36.186 1.0 53.37 ? ? ? ? ? ? 264 HIS A CG 1 147 A A +ATOM 1181 N ND1 . HIS A 1 147 ? 6.573 15.898 35.236 1.0 58.65 ? ? ? ? ? ? 264 HIS A ND1 1 147 A A +ATOM 1182 C CD2 . HIS A 1 147 ? 4.593 16.402 36.005 1.0 56.24 ? ? ? ? ? ? 264 HIS A CD2 1 147 A A +ATOM 1183 C CE1 . HIS A 1 147 ? 5.689 15.229 34.513 1.0 37.58 ? ? ? ? ? ? 264 HIS A CE1 1 147 A A +ATOM 1184 N NE2 . HIS A 1 147 ? 4.485 15.519 34.961 1.0 49.84 ? ? ? ? ? ? 264 HIS A NE2 1 147 A A +ATOM 1185 N N . CYS A 1 148 ? 8.555 16.762 40.158 1.0 52.29 ? ? ? ? ? ? 265 CYS A N 1 148 A A +ATOM 1186 C CA . CYS A 1 148 ? 9.513 17.303 41.114 1.0 59.81 ? ? ? ? ? ? 265 CYS A CA 1 148 A A +ATOM 1187 C C . CYS A 1 148 ? 10.958 17.343 40.620 1.0 60.63 ? ? ? ? ? ? 265 CYS A C 1 148 A A +ATOM 1188 O O . CYS A 1 148 ? 11.368 16.548 39.770 1.0 62.02 ? ? ? ? ? ? 265 CYS A O 1 148 A A +ATOM 1189 C CB . CYS A 1 148 ? 9.431 16.487 42.408 1.0 56.39 ? ? ? ? ? ? 265 CYS A CB 1 148 A A +ATOM 1190 S SG . CYS A 1 148 ? 10.530 17.011 43.732 1.0 81.8 ? ? ? ? ? ? 265 CYS A SG 1 148 A A +ATOM 1191 N N . THR A 1 149 ? 11.717 18.290 41.168 1.0 57.33 ? ? ? ? ? ? 266 THR A N 1 149 A A +ATOM 1192 C CA . THR A 1 149 ? 13.128 18.470 40.836 1.0 54.19 ? ? ? ? ? ? 266 THR A CA 1 149 A A +ATOM 1193 C C . THR A 1 149 ? 13.977 17.704 41.852 1.0 45.74 ? ? ? ? ? ? 266 THR A C 1 149 A A +ATOM 1194 O O . THR A 1 149 ? 13.806 17.862 43.060 1.0 43.17 ? ? ? ? ? ? 266 THR A O 1 149 A A +ATOM 1195 C CB . THR A 1 149 ? 13.531 19.962 40.886 1.0 60.72 ? ? ? ? ? ? 266 THR A CB 1 149 A A +ATOM 1196 O OG1 . THR A 1 149 ? 13.574 20.404 42.249 1.0 48.14 ? ? ? ? ? ? 266 THR A OG1 1 149 A A +ATOM 1197 C CG2 . THR A 1 149 ? 12.531 20.809 40.116 1.0 67.4 ? ? ? ? ? ? 266 THR A CG2 1 149 A A +ATOM 1198 N N . GLN A 1 150 ? 14.889 16.875 41.357 1.0 52.16 ? ? ? ? ? ? 267 GLN A N 1 150 A A +ATOM 1199 C CA . GLN A 1 150 ? 15.749 16.087 42.227 1.0 44.22 ? ? ? ? ? ? 267 GLN A CA 1 150 A A +ATOM 1200 C C . GLN A 1 150 ? 16.982 16.864 42.671 1.0 45.27 ? ? ? ? ? ? 267 GLN A C 1 150 A A +ATOM 1201 O O . GLN A 1 150 ? 17.602 16.526 43.676 1.0 34.83 ? ? ? ? ? ? 267 GLN A O 1 150 A A +ATOM 1202 C CB . GLN A 1 150 ? 16.182 14.810 41.509 1.0 36.86 ? ? ? ? ? ? 267 GLN A CB 1 150 A A +ATOM 1203 C CG . GLN A 1 150 ? 17.054 13.902 42.347 1.0 27.09 ? ? ? ? ? ? 267 GLN A CG 1 150 A A +ATOM 1204 C CD . GLN A 1 150 ? 16.531 12.475 42.397 1.0 50.69 ? ? ? ? ? ? 267 GLN A CD 1 150 A A +ATOM 1205 O OE1 . GLN A 1 150 ? 16.316 11.843 41.359 1.0 43.07 ? ? ? ? ? ? 267 GLN A OE1 1 150 A A +ATOM 1206 N NE2 . GLN A 1 150 ? 16.329 11.958 43.609 1.0 54.57 ? ? ? ? ? ? 267 GLN A NE2 1 150 A A +ATOM 1207 N N . TYR A 1 151 ? 17.328 17.910 41.924 1.0 39.74 ? ? ? ? ? ? 268 TYR A N 1 151 A A +ATOM 1208 C CA . TYR A 1 151 ? 18.501 18.720 42.234 1.0 41.65 ? ? ? ? ? ? 268 TYR A CA 1 151 A A +ATOM 1209 C C . TYR A 1 151 ? 18.311 19.730 43.365 1.0 44.54 ? ? ? ? ? ? 268 TYR A C 1 151 A A +ATOM 1210 O O . TYR A 1 151 ? 17.262 19.773 44.009 1.0 42.77 ? ? ? ? ? ? 268 TYR A O 1 151 A A +ATOM 1211 C CB . TYR A 1 151 ? 19.003 19.430 40.967 1.0 47.36 ? ? ? ? ? ? 268 TYR A CB 1 151 A A +ATOM 1212 C CG . TYR A 1 151 ? 18.031 20.406 40.339 1.0 47.68 ? ? ? ? ? ? 268 TYR A CG 1 151 A A +ATOM 1213 C CD1 . TYR A 1 151 ? 17.924 21.714 40.812 1.0 41.55 ? ? ? ? ? ? 268 TYR A CD1 1 151 A A +ATOM 1214 C CD2 . TYR A 1 151 ? 17.255 20.037 39.241 1.0 64.94 ? ? ? ? ? ? 268 TYR A CD2 1 151 A A +ATOM 1215 C CE1 . TYR A 1 151 ? 17.071 22.633 40.206 1.0 32.05 ? ? ? ? ? ? 268 TYR A CE1 1 151 A A +ATOM 1216 C CE2 . TYR A 1 151 ? 16.398 20.949 38.629 1.0 62.63 ? ? ? ? ? ? 268 TYR A CE2 1 151 A A +ATOM 1217 C CZ . TYR A 1 151 ? 16.314 22.245 39.115 1.0 42.2 ? ? ? ? ? ? 268 TYR A CZ 1 151 A A +ATOM 1218 O OH . TYR A 1 151 ? 15.480 23.154 38.501 1.0 37.44 ? ? ? ? ? ? 268 TYR A OH 1 151 A A +ATOM 1219 N N . ILE A 1 152 ? 19.341 20.544 43.592 1.0 56.45 ? ? ? ? ? ? 269 ILE A N 1 152 A A +ATOM 1220 C CA . ILE A 1 152 ? 19.323 21.549 44.654 1.0 60.67 ? ? ? ? ? ? 269 ILE A CA 1 152 A A +ATOM 1221 C C . ILE A 1 152 ? 20.065 22.829 44.277 1.0 61.55 ? ? ? ? ? ? 269 ILE A C 1 152 A A +ATOM 1222 O O . ILE A 1 152 ? 21.015 22.799 43.499 1.0 65.11 ? ? ? ? ? ? 269 ILE A O 1 152 A A +ATOM 1223 C CB . ILE A 1 152 ? 19.975 21.007 45.933 1.0 50.21 ? ? ? ? ? ? 269 ILE A CB 1 152 A A +ATOM 1224 C CG1 . ILE A 1 152 ? 19.954 22.079 47.022 1.0 55.34 ? ? ? ? ? ? 269 ILE A CG1 1 152 A A +ATOM 1225 C CG2 . ILE A 1 152 ? 21.406 20.589 45.640 1.0 43.33 ? ? ? ? ? ? 269 ILE A CG2 1 152 A A +ATOM 1226 C CD1 . ILE A 1 152 ? 20.348 21.573 48.384 1.0 70.88 ? ? ? ? ? ? 269 ILE A CD1 1 152 A A +ATOM 1227 N N . ARG A 1 153 ? 19.633 23.947 44.851 1.0 70.19 ? ? ? ? ? ? 270 ARG A N 1 153 A A +ATOM 1228 C CA . ARG A 1 153 ? 20.251 25.242 44.591 1.0 76.56 ? ? ? ? ? ? 270 ARG A CA 1 153 A A +ATOM 1229 C C . ARG A 1 153 ? 21.742 25.175 44.899 1.0 74.71 ? ? ? ? ? ? 270 ARG A C 1 153 A A +ATOM 1230 O O . ARG A 1 153 ? 22.213 24.222 45.520 1.0 68.44 ? ? ? ? ? ? 270 ARG A O 1 153 A A +ATOM 1231 C CB . ARG A 1 153 ? 19.601 26.312 45.467 1.0 84.04 ? ? ? ? ? ? 270 ARG A CB 1 153 A A +ATOM 1232 C CG . ARG A 1 153 ? 19.686 26.015 46.956 1.0 85.5 ? ? ? ? ? ? 270 ARG A CG 1 153 A A +ATOM 1233 C CD . ARG A 1 153 ? 18.927 27.042 47.769 1.0 88.12 ? ? ? ? ? ? 270 ARG A CD 1 153 A A +ATOM 1234 N NE . ARG A 1 153 ? 17.550 26.626 48.010 1.0 82.86 ? ? ? ? ? ? 270 ARG A NE 1 153 A A +ATOM 1235 C CZ . ARG A 1 153 ? 16.795 27.089 48.999 1.0 79.01 ? ? ? ? ? ? 270 ARG A CZ 1 153 A A +ATOM 1236 N NH1 . ARG A 1 153 ? 17.286 27.985 49.842 1.0 74.83 ? ? ? ? ? ? 270 ARG A NH1 1 153 A A +ATOM 1237 N NH2 . ARG A 1 153 ? 15.550 26.659 49.145 1.0 64.13 ? ? ? ? ? ? 270 ARG A NH2 1 153 A A +ATOM 1238 N N . HIS A 1 154 ? 22.483 26.188 44.462 1.0 73.45 ? ? ? ? ? ? 271 HIS A N 1 154 A A +ATOM 1239 C CA . HIS A 1 154 ? 23.916 26.225 44.717 1.0 76.37 ? ? ? ? ? ? 271 HIS A CA 1 154 A A +ATOM 1240 C C . HIS A 1 154 ? 24.175 26.776 46.110 1.0 80.1 ? ? ? ? ? ? 271 HIS A C 1 154 A A +ATOM 1241 O O . HIS A 1 154 ? 23.508 27.711 46.553 1.0 90.33 ? ? ? ? ? ? 271 HIS A O 1 154 A A +ATOM 1242 C CB . HIS A 1 154 ? 24.639 27.092 43.688 1.0 85.46 ? ? ? ? ? ? 271 HIS A CB 1 154 A A +ATOM 1243 C CG . HIS A 1 154 ? 26.130 26.961 43.742 1.0 90.77 ? ? ? ? ? ? 271 HIS A CG 1 154 A A +ATOM 1244 N ND1 . HIS A 1 154 ? 26.960 28.016 44.053 1.0 95.04 ? ? ? ? ? ? 271 HIS A ND1 1 154 A A +ATOM 1245 C CD2 . HIS A 1 154 ? 26.937 25.889 43.558 1.0 89.61 ? ? ? ? ? ? 271 HIS A CD2 1 154 A A +ATOM 1246 C CE1 . HIS A 1 154 ? 28.215 27.599 44.058 1.0 100.0 ? ? ? ? ? ? 271 HIS A CE1 1 154 A A +ATOM 1247 N NE2 . HIS A 1 154 ? 28.227 26.312 43.760 1.0 89.7 ? ? ? ? ? ? 271 HIS A NE2 1 154 A A +ATOM 1248 N N . GLY A 1 155 ? 25.156 26.195 46.790 1.0 78.16 ? ? ? ? ? ? 272 GLY A N 1 155 A A +ATOM 1249 C CA . GLY A 1 155 ? 25.487 26.625 48.136 1.0 82.41 ? ? ? ? ? ? 272 GLY A CA 1 155 A A +ATOM 1250 C C . GLY A 1 155 ? 25.908 28.074 48.311 1.0 76.8 ? ? ? ? ? ? 272 GLY A C 1 155 A A +ATOM 1251 O O . GLY A 1 155 ? 25.953 28.562 49.440 1.0 83.1 ? ? ? ? ? ? 272 GLY A O 1 155 A A +ATOM 1252 N N . SER A 1 156 ? 26.222 28.769 47.221 1.0 69.09 ? ? ? ? ? ? 273 SER A N 1 156 A A +ATOM 1253 C CA . SER A 1 156 ? 26.639 30.169 47.324 1.0 68.79 ? ? ? ? ? ? 273 SER A CA 1 156 A A +ATOM 1254 C C . SER A 1 156 ? 25.621 30.981 48.120 1.0 68.32 ? ? ? ? ? ? 273 SER A C 1 156 A A +ATOM 1255 O O . SER A 1 156 ? 25.972 31.644 49.096 1.0 75.05 ? ? ? ? ? ? 273 SER A O 1 156 A A +ATOM 1256 C CB . SER A 1 156 ? 26.828 30.783 45.929 1.0 77.85 ? ? ? ? ? ? 273 SER A CB 1 156 A A +ATOM 1257 O OG . SER A 1 156 ? 25.628 30.770 45.176 1.0 83.43 ? ? ? ? ? ? 273 SER A OG 1 156 A A +ATOM 1258 N N . LYS A 1 157 ? 24.363 30.922 47.696 1.0 66.77 ? ? ? ? ? ? 274 LYS A N 1 157 A A +ATOM 1259 C CA . LYS A 1 157 ? 23.287 31.631 48.375 1.0 64.76 ? ? ? ? ? ? 274 LYS A CA 1 157 A A +ATOM 1260 C C . LYS A 1 157 ? 22.198 30.632 48.763 1.0 67.12 ? ? ? ? ? ? 274 LYS A C 1 157 A A +ATOM 1261 O O . LYS A 1 157 ? 21.233 30.423 48.028 1.0 66.67 ? ? ? ? ? ? 274 LYS A O 1 157 A A +ATOM 1262 C CB . LYS A 1 157 ? 22.728 32.727 47.465 1.0 68.16 ? ? ? ? ? ? 274 LYS A CB 1 157 A A +ATOM 1263 C CG . LYS A 1 157 ? 23.604 33.971 47.414 1.0 79.05 ? ? ? ? ? ? 274 LYS A CG 1 157 A A +ATOM 1264 C CD . LYS A 1 157 ? 23.785 34.574 48.803 1.0 94.09 ? ? ? ? ? ? 274 LYS A CD 1 157 A A +ATOM 1265 C CE . LYS A 1 157 ? 24.769 35.738 48.788 1.0 96.98 ? ? ? ? ? ? 274 LYS A CE 1 157 A A +ATOM 1266 N NZ . LYS A 1 157 ? 25.076 36.232 50.160 1.0 100.0 ? ? ? ? ? ? 274 LYS A NZ 1 157 A A +ATOM 1267 N N . PRO A 1 158 ? 22.353 29.998 49.938 1.0 61.91 ? ? ? ? ? ? 275 PRO A N 1 158 A A +ATOM 1268 C CA . PRO A 1 158 ? 21.414 29.004 50.468 1.0 65.03 ? ? ? ? ? ? 275 PRO A CA 1 158 A A +ATOM 1269 C C . PRO A 1 158 ? 20.085 29.589 50.937 1.0 72.4 ? ? ? ? ? ? 275 PRO A C 1 158 A A +ATOM 1270 O O . PRO A 1 158 ? 19.269 28.888 51.537 1.0 89.09 ? ? ? ? ? ? 275 PRO A O 1 158 A A +ATOM 1271 C CB . PRO A 1 158 ? 22.191 28.352 51.610 1.0 60.82 ? ? ? ? ? ? 275 PRO A CB 1 158 A A +ATOM 1272 C CG . PRO A 1 158 ? 23.131 29.411 52.064 1.0 76.64 ? ? ? ? ? ? 275 PRO A CG 1 158 A A +ATOM 1273 C CD . PRO A 1 158 ? 23.482 30.229 50.854 1.0 72.44 ? ? ? ? ? ? 275 PRO A CD 1 158 A A +ATOM 1274 N N . MET A 1 159 ? 19.868 30.871 50.661 1.0 57.47 ? ? ? ? ? ? 276 MET A N 1 159 A A +ATOM 1275 C CA . MET A 1 159 ? 18.629 31.531 51.056 1.0 67.57 ? ? ? ? ? ? 276 MET A CA 1 159 A A +ATOM 1276 C C . MET A 1 159 ? 17.898 32.077 49.834 1.0 74.14 ? ? ? ? ? ? 276 MET A C 1 159 A A +ATOM 1277 O O . MET A 1 159 ? 16.976 32.882 49.955 1.0 84.59 ? ? ? ? ? ? 276 MET A O 1 159 A A +ATOM 1278 C CB . MET A 1 159 ? 18.928 32.669 52.035 1.0 79.9 ? ? ? ? ? ? 276 MET A CB 1 159 A A +ATOM 1279 C CG . MET A 1 159 ? 18.162 32.587 53.349 1.0 82.99 ? ? ? ? ? ? 276 MET A CG 1 159 A A +ATOM 1280 S SD . MET A 1 159 ? 18.343 31.004 54.201 1.0 94.71 ? ? ? ? ? ? 276 MET A SD 1 159 A A +ATOM 1281 C CE . MET A 1 159 ? 16.776 30.240 53.829 1.0 100.0 ? ? ? ? ? ? 276 MET A CE 1 159 A A +ATOM 1282 N N . TYR A 1 160 ? 18.309 31.625 48.655 1.0 81.71 ? ? ? ? ? ? 277 TYR A N 1 160 A A +ATOM 1283 C CA . TYR A 1 160 ? 17.688 32.074 47.421 1.0 95.68 ? ? ? ? ? ? 277 TYR A CA 1 160 A A +ATOM 1284 C C . TYR A 1 160 ? 17.840 31.066 46.284 1.0 96.34 ? ? ? ? ? ? 277 TYR A C 1 160 A A +ATOM 1285 O O . TYR A 1 160 ? 18.906 30.474 46.096 1.0 94.33 ? ? ? ? ? ? 277 TYR A O 1 160 A A +ATOM 1286 C CB . TYR A 1 160 ? 18.281 33.418 47.000 1.0 92.57 ? ? ? ? ? ? 277 TYR A CB 1 160 A A +ATOM 1287 C CG . TYR A 1 160 ? 18.183 33.685 45.518 1.0 98.35 ? ? ? ? ? ? 277 TYR A CG 1 160 A A +ATOM 1288 C CD1 . TYR A 1 160 ? 16.971 34.051 44.939 1.0 100.0 ? ? ? ? ? ? 277 TYR A CD1 1 160 A A +ATOM 1289 C CD2 . TYR A 1 160 ? 19.300 33.562 44.691 1.0 93.13 ? ? ? ? ? ? 277 TYR A CD2 1 160 A A +ATOM 1290 C CE1 . TYR A 1 160 ? 16.872 34.289 43.572 1.0 95.63 ? ? ? ? ? ? 277 TYR A CE1 1 160 A A +ATOM 1291 C CE2 . TYR A 1 160 ? 19.213 33.797 43.324 1.0 94.92 ? ? ? ? ? ? 277 TYR A CE2 1 160 A A +ATOM 1292 C CZ . TYR A 1 160 ? 17.996 34.161 42.771 1.0 95.01 ? ? ? ? ? ? 277 TYR A CZ 1 160 A A +ATOM 1293 O OH . TYR A 1 160 ? 17.908 34.406 41.419 1.0 91.12 ? ? ? ? ? ? 277 TYR A OH 1 160 A A +ATOM 1294 N N . THR A 1 161 ? 16.759 30.882 45.532 1.0 86.12 ? ? ? ? ? ? 278 THR A N 1 161 A A +ATOM 1295 C CA . THR A 1 161 ? 16.743 29.970 44.393 1.0 75.54 ? ? ? ? ? ? 278 THR A CA 1 161 A A +ATOM 1296 C C . THR A 1 161 ? 15.967 30.632 43.262 1.0 72.73 ? ? ? ? ? ? 278 THR A C 1 161 A A +ATOM 1297 O O . THR A 1 161 ? 14.854 31.113 43.458 1.0 73.03 ? ? ? ? ? ? 278 THR A O 1 161 A A +ATOM 1298 C CB . THR A 1 161 ? 16.074 28.630 44.745 1.0 82.17 ? ? ? ? ? ? 278 THR A CB 1 161 A A +ATOM 1299 O OG1 . THR A 1 161 ? 16.356 28.303 46.112 1.0 98.31 ? ? ? ? ? ? 278 THR A OG1 1 161 A A +ATOM 1300 C CG2 . THR A 1 161 ? 16.609 27.533 43.847 1.0 85.64 ? ? ? ? ? ? 278 THR A CG2 1 161 A A +ATOM 1301 N N . PRO A 1 162 ? 16.544 30.655 42.054 1.0 78.92 ? ? ? ? ? ? 279 PRO A N 1 162 A A +ATOM 1302 C CA . PRO A 1 162 ? 15.875 31.277 40.908 1.0 76.69 ? ? ? ? ? ? 279 PRO A CA 1 162 A A +ATOM 1303 C C . PRO A 1 162 ? 14.781 30.400 40.318 1.0 70.76 ? ? ? ? ? ? 279 PRO A C 1 162 A A +ATOM 1304 O O . PRO A 1 162 ? 14.047 30.815 39.425 1.0 64.88 ? ? ? ? ? ? 279 PRO A O 1 162 A A +ATOM 1305 C CB . PRO A 1 162 ? 17.010 31.516 39.923 1.0 69.92 ? ? ? ? ? ? 279 PRO A CB 1 162 A A +ATOM 1306 C CG . PRO A 1 162 ? 18.006 30.444 40.236 1.0 82.58 ? ? ? ? ? ? 279 PRO A CG 1 162 A A +ATOM 1307 C CD . PRO A 1 162 ? 17.841 30.065 41.686 1.0 84.25 ? ? ? ? ? ? 279 PRO A CD 1 162 A A +ATOM 1308 N N . GLU A 1 163 ? 14.674 29.181 40.838 1.0 68.53 ? ? ? ? ? ? 280 GLU A N 1 163 A A +ATOM 1309 C CA . GLU A 1 163 ? 13.677 28.234 40.368 1.0 69.05 ? ? ? ? ? ? 280 GLU A CA 1 163 A A +ATOM 1310 C C . GLU A 1 163 ? 13.519 27.087 41.361 1.0 63.34 ? ? ? ? ? ? 280 GLU A C 1 163 A A +ATOM 1311 O O . GLU A 1 163 ? 14.321 26.935 42.275 1.0 60.75 ? ? ? ? ? ? 280 GLU A O 1 163 A A +ATOM 1312 C CB . GLU A 1 163 ? 14.088 27.702 38.993 1.0 74.71 ? ? ? ? ? ? 280 GLU A CB 1 163 A A +ATOM 1313 C CG . GLU A 1 163 ? 15.044 26.532 39.064 1.0 78.89 ? ? ? ? ? ? 280 GLU A CG 1 163 A A +ATOM 1314 C CD . GLU A 1 163 ? 16.491 26.970 39.085 1.0 76.97 ? ? ? ? ? ? 280 GLU A CD 1 163 A A +ATOM 1315 O OE1 . GLU A 1 163 ? 16.984 27.439 38.041 1.0 74.45 ? ? ? ? ? ? 280 GLU A OE1 1 163 A A +ATOM 1316 O OE2 . GLU A 1 163 ? 17.139 26.845 40.142 1.0 77.77 ? ? ? ? ? ? 280 GLU A OE2 1 163 A A +ATOM 1317 N N . PRO A 1 164 ? 12.493 26.239 41.164 1.0 59.44 ? ? ? ? ? ? 281 PRO A N 1 164 A A +ATOM 1318 C CA . PRO A 1 164 ? 12.254 25.109 42.072 1.0 57.6 ? ? ? ? ? ? 281 PRO A CA 1 164 A A +ATOM 1319 C C . PRO A 1 164 ? 13.405 24.126 42.245 1.0 49.97 ? ? ? ? ? ? 281 PRO A C 1 164 A A +ATOM 1320 O O . PRO A 1 164 ? 13.968 23.634 41.272 1.0 53.11 ? ? ? ? ? ? 281 PRO A O 1 164 A A +ATOM 1321 C CB . PRO A 1 164 ? 11.017 24.427 41.488 1.0 51.17 ? ? ? ? ? ? 281 PRO A CB 1 164 A A +ATOM 1322 C CG . PRO A 1 164 ? 10.425 25.410 40.544 1.0 70.63 ? ? ? ? ? ? 281 PRO A CG 1 164 A A +ATOM 1323 C CD . PRO A 1 164 ? 11.533 26.268 40.049 1.0 59.4 ? ? ? ? ? ? 281 PRO A CD 1 164 A A +ATOM 1324 N N . ASP A 1 165 ? 13.735 23.843 43.503 1.0 45.57 ? ? ? ? ? ? 282 ASP A N 1 165 A A +ATOM 1325 C CA . ASP A 1 165 ? 14.792 22.898 43.868 1.0 43.57 ? ? ? ? ? ? 282 ASP A CA 1 165 A A +ATOM 1326 C C . ASP A 1 165 ? 14.183 21.916 44.861 1.0 36.46 ? ? ? ? ? ? 282 ASP A C 1 165 A A +ATOM 1327 O O . ASP A 1 165 ? 13.079 22.144 45.351 1.0 47.96 ? ? ? ? ? ? 282 ASP A O 1 165 A A +ATOM 1328 C CB . ASP A 1 165 ? 15.966 23.628 44.518 1.0 55.07 ? ? ? ? ? ? 282 ASP A CB 1 165 A A +ATOM 1329 C CG . ASP A 1 165 ? 15.648 24.114 45.920 1.0 67.89 ? ? ? ? ? ? 282 ASP A CG 1 165 A A +ATOM 1330 O OD1 . ASP A 1 165 ? 16.529 24.003 46.800 1.0 65.08 ? ? ? ? ? ? 282 ASP A OD1 1 165 A A +ATOM 1331 O OD2 . ASP A 1 165 ? 14.521 24.605 46.141 1.0 75.95 ? ? ? ? ? ? 282 ASP A OD2 1 165 A A +ATOM 1332 N N . ILE A 1 166 ? 14.895 20.837 45.170 1.0 33.07 ? ? ? ? ? ? 283 ILE A N 1 166 A A +ATOM 1333 C CA . ILE A 1 166 ? 14.373 19.831 46.097 1.0 45.55 ? ? ? ? ? ? 283 ILE A CA 1 166 A A +ATOM 1334 C C . ILE A 1 166 ? 13.895 20.380 47.449 1.0 52.96 ? ? ? ? ? ? 283 ILE A C 1 166 A A +ATOM 1335 O O . ILE A 1 166 ? 13.236 19.675 48.219 1.0 56.77 ? ? ? ? ? ? 283 ILE A O 1 166 A A +ATOM 1336 C CB . ILE A 1 166 ? 15.407 18.719 46.369 1.0 42.94 ? ? ? ? ? ? 283 ILE A CB 1 166 A A +ATOM 1337 C CG1 . ILE A 1 166 ? 14.702 17.509 46.999 1.0 52.36 ? ? ? ? ? ? 283 ILE A CG1 1 166 A A +ATOM 1338 C CG2 . ILE A 1 166 ? 16.511 19.244 47.278 1.0 38.58 ? ? ? ? ? ? 283 ILE A CG2 1 166 A A +ATOM 1339 C CD1 . ILE A 1 166 ? 15.455 16.199 46.851 1.0 55.61 ? ? ? ? ? ? 283 ILE A CD1 1 166 A A +ATOM 1340 N N . CYS A 1 167 ? 14.226 21.633 47.741 1.0 51.82 ? ? ? ? ? ? 284 CYS A N 1 167 A A +ATOM 1341 C CA . CYS A 1 167 ? 13.803 22.250 48.991 1.0 56.36 ? ? ? ? ? ? 284 CYS A CA 1 167 A A +ATOM 1342 C C . CYS A 1 167 ? 12.407 22.824 48.804 1.0 54.65 ? ? ? ? ? ? 284 CYS A C 1 167 A A +ATOM 1343 O O . CYS A 1 167 ? 11.514 22.594 49.618 1.0 67.24 ? ? ? ? ? ? 284 CYS A O 1 167 A A +ATOM 1344 C CB . CYS A 1 167 ? 14.774 23.364 49.388 1.0 74.89 ? ? ? ? ? ? 284 CYS A CB 1 167 A A +ATOM 1345 S SG . CYS A 1 167 ? 16.518 22.892 49.344 1.0 99.53 ? ? ? ? ? ? 284 CYS A SG 1 167 A A +ATOM 1346 N N . HIS A 1 168 ? 12.226 23.571 47.721 1.0 62.12 ? ? ? ? ? ? 285 HIS A N 1 168 A A +ATOM 1347 C CA . HIS A 1 168 ? 10.936 24.176 47.418 1.0 64.94 ? ? ? ? ? ? 285 HIS A CA 1 168 A A +ATOM 1348 C C . HIS A 1 168 ? 9.874 23.095 47.251 1.0 59.74 ? ? ? ? ? ? 285 HIS A C 1 168 A A +ATOM 1349 O O . HIS A 1 168 ? 8.764 23.213 47.769 1.0 64.62 ? ? ? ? ? ? 285 HIS A O 1 168 A A +ATOM 1350 C CB . HIS A 1 168 ? 11.047 25.016 46.142 1.0 61.21 ? ? ? ? ? ? 285 HIS A CB 1 168 A A +ATOM 1351 C CG . HIS A 1 168 ? 9.730 25.349 45.513 1.0 76.62 ? ? ? ? ? ? 285 HIS A CG 1 168 A A +ATOM 1352 N ND1 . HIS A 1 168 ? 8.955 26.411 45.925 1.0 93.0 ? ? ? ? ? ? 285 HIS A ND1 1 168 A A +ATOM 1353 C CD2 . HIS A 1 168 ? 9.068 24.773 44.484 1.0 87.22 ? ? ? ? ? ? 285 HIS A CD2 1 168 A A +ATOM 1354 C CE1 . HIS A 1 168 ? 7.870 26.476 45.175 1.0 100.0 ? ? ? ? ? ? 285 HIS A CE1 1 168 A A +ATOM 1355 N NE2 . HIS A 1 168 ? 7.913 25.494 44.293 1.0 99.45 ? ? ? ? ? ? 285 HIS A NE2 1 168 A A +ATOM 1356 N N . GLU A 1 169 ? 10.232 22.033 46.541 1.0 52.73 ? ? ? ? ? ? 286 GLU A N 1 169 A A +ATOM 1357 C CA . GLU A 1 169 ? 9.312 20.934 46.286 1.0 57.66 ? ? ? ? ? ? 286 GLU A CA 1 169 A A +ATOM 1358 C C . GLU A 1 169 ? 8.987 20.109 47.525 1.0 60.34 ? ? ? ? ? ? 286 GLU A C 1 169 A A +ATOM 1359 O O . GLU A 1 169 ? 7.834 19.728 47.732 1.0 77.83 ? ? ? ? ? ? 286 GLU A O 1 169 A A +ATOM 1360 C CB . GLU A 1 169 ? 9.882 20.012 45.205 1.0 61.13 ? ? ? ? ? ? 286 GLU A CB 1 169 A A +ATOM 1361 C CG . GLU A 1 169 ? 10.533 20.741 44.046 1.0 76.3 ? ? ? ? ? ? 286 GLU A CG 1 169 A A +ATOM 1362 C CD . GLU A 1 169 ? 9.545 21.127 42.964 1.0 85.35 ? ? ? ? ? ? 286 GLU A CD 1 169 A A +ATOM 1363 O OE1 . GLU A 1 169 ? 9.383 20.351 42.000 1.0 72.35 ? ? ? ? ? ? 286 GLU A OE1 1 169 A A +ATOM 1364 O OE2 . GLU A 1 169 ? 8.934 22.209 43.070 1.0 88.17 ? ? ? ? ? ? 286 GLU A OE2 1 169 A A +ATOM 1365 N N . LEU A 1 170 ? 10.000 19.838 48.346 1.0 48.09 ? ? ? ? ? ? 287 LEU A N 1 170 A A +ATOM 1366 C CA . LEU A 1 170 ? 9.815 19.033 49.557 1.0 60.37 ? ? ? ? ? ? 287 LEU A CA 1 170 A A +ATOM 1367 C C . LEU A 1 170 ? 9.349 19.809 50.794 1.0 62.26 ? ? ? ? ? ? 287 LEU A C 1 170 A A +ATOM 1368 O O . LEU A 1 170 ? 8.495 19.335 51.545 1.0 60.64 ? ? ? ? ? ? 287 LEU A O 1 170 A A +ATOM 1369 C CB . LEU A 1 170 ? 11.107 18.287 49.893 1.0 55.75 ? ? ? ? ? ? 287 LEU A CB 1 170 A A +ATOM 1370 C CG . LEU A 1 170 ? 11.452 17.036 49.077 1.0 61.06 ? ? ? ? ? ? 287 LEU A CG 1 170 A A +ATOM 1371 C CD1 . LEU A 1 170 ? 12.622 16.323 49.734 1.0 59.23 ? ? ? ? ? ? 287 LEU A CD1 1 170 A A +ATOM 1372 C CD2 . LEU A 1 170 ? 10.250 16.110 48.989 1.0 40.81 ? ? ? ? ? ? 287 LEU A CD2 1 170 A A +ATOM 1373 N N . LEU A 1 171 ? 9.913 20.993 51.007 1.0 60.18 ? ? ? ? ? ? 288 LEU A N 1 171 A A +ATOM 1374 C CA . LEU A 1 171 ? 9.544 21.819 52.153 1.0 54.52 ? ? ? ? ? ? 288 LEU A CA 1 171 A A +ATOM 1375 C C . LEU A 1 171 ? 8.560 22.911 51.736 1.0 63.82 ? ? ? ? ? ? 288 LEU A C 1 171 A A +ATOM 1376 O O . LEU A 1 171 ? 8.535 23.994 52.323 1.0 73.18 ? ? ? ? ? ? 288 LEU A O 1 171 A A +ATOM 1377 C CB . LEU A 1 171 ? 10.794 22.464 52.769 1.0 56.91 ? ? ? ? ? ? 288 LEU A CB 1 171 A A +ATOM 1378 C CG . LEU A 1 171 ? 11.972 21.546 53.108 1.0 46.12 ? ? ? ? ? ? 288 LEU A CG 1 171 A A +ATOM 1379 C CD1 . LEU A 1 171 ? 13.191 22.381 53.463 1.0 35.1 ? ? ? ? ? ? 288 LEU A CD1 1 171 A A +ATOM 1380 C CD2 . LEU A 1 171 ? 11.588 20.630 54.250 1.0 36.21 ? ? ? ? ? ? 288 LEU A CD2 1 171 A A +ATOM 1381 N N . GLY A 1 172 ? 7.752 22.624 50.721 1.0 69.02 ? ? ? ? ? ? 289 GLY A N 1 172 A A +ATOM 1382 C CA . GLY A 1 172 ? 6.789 23.604 50.259 1.0 74.13 ? ? ? ? ? ? 289 GLY A CA 1 172 A A +ATOM 1383 C C . GLY A 1 172 ? 5.558 22.990 49.631 1.0 66.63 ? ? ? ? ? ? 289 GLY A C 1 172 A A +ATOM 1384 O O . GLY A 1 172 ? 4.439 23.246 50.072 1.0 81.62 ? ? ? ? ? ? 289 GLY A O 1 172 A A +ATOM 1385 N N . HIS A 1 173 ? 5.764 22.178 48.599 1.0 50.97 ? ? ? ? ? ? 290 HIS A N 1 173 A A +ATOM 1386 C CA . HIS A 1 173 ? 4.663 21.530 47.896 1.0 46.5 ? ? ? ? ? ? 290 HIS A CA 1 173 A A +ATOM 1387 C C . HIS A 1 173 ? 4.200 20.229 48.556 1.0 50.67 ? ? ? ? ? ? 290 HIS A C 1 173 A A +ATOM 1388 O O . HIS A 1 173 ? 3.036 20.095 48.937 1.0 50.37 ? ? ? ? ? ? 290 HIS A O 1 173 A A +ATOM 1389 C CB . HIS A 1 173 ? 5.069 21.240 46.449 1.0 52.24 ? ? ? ? ? ? 290 HIS A CB 1 173 A A +ATOM 1390 C CG . HIS A 1 173 ? 4.970 22.428 45.541 1.0 62.48 ? ? ? ? ? ? 290 HIS A CG 1 173 A A +ATOM 1391 N ND1 . HIS A 1 173 ? 3.813 22.762 44.873 1.0 64.94 ? ? ? ? ? ? 290 HIS A ND1 1 173 A A +ATOM 1392 C CD2 . HIS A 1 173 ? 5.892 23.356 45.188 1.0 49.65 ? ? ? ? ? ? 290 HIS A CD2 1 173 A A +ATOM 1393 C CE1 . HIS A 1 173 ? 4.023 23.845 44.146 1.0 64.48 ? ? ? ? ? ? 290 HIS A CE1 1 173 A A +ATOM 1394 N NE2 . HIS A 1 173 ? 5.276 24.226 44.320 1.0 54.47 ? ? ? ? ? ? 290 HIS A NE2 1 173 A A +ATOM 1395 N N . VAL A 1 174 ? 5.121 19.275 48.683 1.0 51.67 ? ? ? ? ? ? 291 VAL A N 1 174 A A +ATOM 1396 C CA . VAL A 1 174 ? 4.838 17.962 49.265 1.0 60.23 ? ? ? ? ? ? 291 VAL A CA 1 174 A A +ATOM 1397 C C . VAL A 1 174 ? 3.882 17.916 50.462 1.0 63.65 ? ? ? ? ? ? 291 VAL A C 1 174 A A +ATOM 1398 O O . VAL A 1 174 ? 2.890 17.187 50.436 1.0 66.68 ? ? ? ? ? ? 291 VAL A O 1 174 A A +ATOM 1399 C CB . VAL A 1 174 ? 6.155 17.248 49.658 1.0 68.66 ? ? ? ? ? ? 291 VAL A CB 1 174 A A +ATOM 1400 C CG1 . VAL A 1 174 ? 5.861 15.938 50.377 1.0 51.75 ? ? ? ? ? ? 291 VAL A CG1 1 174 A A +ATOM 1401 C CG2 . VAL A 1 174 ? 6.982 16.984 48.417 1.0 59.3 ? ? ? ? ? ? 291 VAL A CG2 1 174 A A +ATOM 1402 N N . PRO A 1 175 ? 4.164 18.696 51.525 1.0 56.06 ? ? ? ? ? ? 292 PRO A N 1 175 A A +ATOM 1403 C CA . PRO A 1 175 ? 3.269 18.662 52.691 1.0 52.02 ? ? ? ? ? ? 292 PRO A CA 1 175 A A +ATOM 1404 C C . PRO A 1 175 ? 1.803 18.953 52.383 1.0 48.25 ? ? ? ? ? ? 292 PRO A C 1 175 A A +ATOM 1405 O O . PRO A 1 175 ? 0.916 18.467 53.075 1.0 55.38 ? ? ? ? ? ? 292 PRO A O 1 175 A A +ATOM 1406 C CB . PRO A 1 175 ? 3.867 19.696 53.649 1.0 50.93 ? ? ? ? ? ? 292 PRO A CB 1 175 A A +ATOM 1407 C CG . PRO A 1 175 ? 5.256 19.914 53.177 1.0 66.89 ? ? ? ? ? ? 292 PRO A CG 1 175 A A +ATOM 1408 C CD . PRO A 1 175 ? 5.273 19.645 51.705 1.0 48.46 ? ? ? ? ? ? 292 PRO A CD 1 175 A A +ATOM 1409 N N . LEU A 1 176 ? 1.550 19.746 51.348 1.0 45.32 ? ? ? ? ? ? 293 LEU A N 1 176 A A +ATOM 1410 C CA . LEU A 1 176 ? 0.181 20.079 50.982 1.0 40.66 ? ? ? ? ? ? 293 LEU A CA 1 176 A A +ATOM 1411 C C . LEU A 1 176 ? -0.445 18.946 50.188 1.0 44.9 ? ? ? ? ? ? 293 LEU A C 1 176 A A +ATOM 1412 O O . LEU A 1 176 ? -1.643 18.695 50.297 1.0 48.65 ? ? ? ? ? ? 293 LEU A O 1 176 A A +ATOM 1413 C CB . LEU A 1 176 ? 0.150 21.367 50.155 1.0 39.05 ? ? ? ? ? ? 293 LEU A CB 1 176 A A +ATOM 1414 C CG . LEU A 1 176 ? 0.119 22.680 50.944 1.0 46.07 ? ? ? ? ? ? 293 LEU A CG 1 176 A A +ATOM 1415 C CD1 . LEU A 1 176 ? -0.999 22.650 51.973 1.0 37.81 ? ? ? ? ? ? 293 LEU A CD1 1 176 A A +ATOM 1416 C CD2 . LEU A 1 176 ? 1.452 22.890 51.622 1.0 56.64 ? ? ? ? ? ? 293 LEU A CD2 1 176 A A +ATOM 1417 N N . PHE A 1 177 ? 0.375 18.263 49.393 1.0 40.73 ? ? ? ? ? ? 294 PHE A N 1 177 A A +ATOM 1418 C CA . PHE A 1 177 ? -0.102 17.153 48.577 1.0 34.87 ? ? ? ? ? ? 294 PHE A CA 1 177 A A +ATOM 1419 C C . PHE A 1 177 ? -0.369 15.915 49.424 1.0 35.06 ? ? ? ? ? ? 294 PHE A C 1 177 A A +ATOM 1420 O O . PHE A 1 177 ? -0.740 14.867 48.900 1.0 41.72 ? ? ? ? ? ? 294 PHE A O 1 177 A A +ATOM 1421 C CB . PHE A 1 177 ? 0.915 16.817 47.485 1.0 47.1 ? ? ? ? ? ? 294 PHE A CB 1 177 A A +ATOM 1422 C CG . PHE A 1 177 ? 0.971 17.827 46.376 1.0 41.71 ? ? ? ? ? ? 294 PHE A CG 1 177 A A +ATOM 1423 C CD1 . PHE A 1 177 ? -0.003 17.853 45.387 1.0 40.38 ? ? ? ? ? ? 294 PHE A CD1 1 177 A A +ATOM 1424 C CD2 . PHE A 1 177 ? 2.002 18.755 46.322 1.0 34.31 ? ? ? ? ? ? 294 PHE A CD2 1 177 A A +ATOM 1425 C CE1 . PHE A 1 177 ? 0.049 18.790 44.359 1.0 44.21 ? ? ? ? ? ? 294 PHE A CE1 1 177 A A +ATOM 1426 C CE2 . PHE A 1 177 ? 2.062 19.696 45.299 1.0 46.58 ? ? ? ? ? ? 294 PHE A CE2 1 177 A A +ATOM 1427 C CZ . PHE A 1 177 ? 1.083 19.712 44.314 1.0 53.93 ? ? ? ? ? ? 294 PHE A CZ 1 177 A A +ATOM 1428 N N . SER A 1 178 ? -0.176 16.039 50.734 1.0 31.86 ? ? ? ? ? ? 295 SER A N 1 178 A A +ATOM 1429 C CA . SER A 1 178 ? -0.425 14.925 51.640 1.0 50.78 ? ? ? ? ? ? 295 SER A CA 1 178 A A +ATOM 1430 C C . SER A 1 178 ? -1.829 15.070 52.214 1.0 49.82 ? ? ? ? ? ? 295 SER A C 1 178 A A +ATOM 1431 O O . SER A 1 178 ? -2.368 14.136 52.806 1.0 58.5 ? ? ? ? ? ? 295 SER A O 1 178 A A +ATOM 1432 C CB . SER A 1 178 ? 0.599 14.916 52.772 1.0 43.11 ? ? ? ? ? ? 295 SER A CB 1 178 A A +ATOM 1433 O OG . SER A 1 178 ? 0.553 16.123 53.509 1.0 79.46 ? ? ? ? ? ? 295 SER A OG 1 178 A A +ATOM 1434 N N . ASP A 1 179 ? -2.423 16.244 52.005 1.0 41.9 ? ? ? ? ? ? 296 ASP A N 1 179 A A +ATOM 1435 C CA . ASP A 1 179 ? -3.763 16.535 52.500 1.0 35.45 ? ? ? ? ? ? 296 ASP A CA 1 179 A A +ATOM 1436 C C . ASP A 1 179 ? -4.847 16.144 51.503 1.0 37.03 ? ? ? ? ? ? 296 ASP A C 1 179 A A +ATOM 1437 O O . ASP A 1 179 ? -4.854 16.590 50.359 1.0 48.53 ? ? ? ? ? ? 296 ASP A O 1 179 A A +ATOM 1438 C CB . ASP A 1 179 ? -3.891 18.020 52.840 1.0 61.62 ? ? ? ? ? ? 296 ASP A CB 1 179 A A +ATOM 1439 C CG . ASP A 1 179 ? -5.318 18.423 53.168 1.0 66.1 ? ? ? ? ? ? 296 ASP A CG 1 179 A A +ATOM 1440 O OD1 . ASP A 1 179 ? -5.852 17.949 54.194 1.0 74.5 ? ? ? ? ? ? 296 ASP A OD1 1 179 A A +ATOM 1441 O OD2 . ASP A 1 179 ? -5.904 19.215 52.397 1.0 62.35 ? ? ? ? ? ? 296 ASP A OD2 1 179 A A +ATOM 1442 N N . ARG A 1 180 ? -5.770 15.312 51.971 1.0 36.5 ? ? ? ? ? ? 297 ARG A N 1 180 A A +ATOM 1443 C CA . ARG A 1 180 ? -6.882 14.811 51.174 1.0 37.44 ? ? ? ? ? ? 297 ARG A CA 1 180 A A +ATOM 1444 C C . ARG A 1 180 ? -7.606 15.857 50.334 1.0 30.3 ? ? ? ? ? ? 297 ARG A C 1 180 A A +ATOM 1445 O O . ARG A 1 180 ? -7.783 15.681 49.130 1.0 29.1 ? ? ? ? ? ? 297 ARG A O 1 180 A A +ATOM 1446 C CB . ARG A 1 180 ? -7.893 14.128 52.097 1.0 67.03 ? ? ? ? ? ? 297 ARG A CB 1 180 A A +ATOM 1447 C CG . ARG A 1 180 ? -9.177 13.715 51.413 1.0 76.26 ? ? ? ? ? ? 297 ARG A CG 1 180 A A +ATOM 1448 C CD . ARG A 1 180 ? -8.982 12.421 50.658 1.0 87.04 ? ? ? ? ? ? 297 ARG A CD 1 180 A A +ATOM 1449 N NE . ARG A 1 180 ? -10.199 12.002 49.973 1.0 100.0 ? ? ? ? ? ? 297 ARG A NE 1 180 A A +ATOM 1450 C CZ . ARG A 1 180 ? -11.256 11.473 50.580 1.0 100.0 ? ? ? ? ? ? 297 ARG A CZ 1 180 A A +ATOM 1451 N NH1 . ARG A 1 180 ? -11.252 11.296 51.895 1.0 94.55 ? ? ? ? ? ? 297 ARG A NH1 1 180 A A +ATOM 1452 N NH2 . ARG A 1 180 ? -12.319 11.118 49.868 1.0 87.1 ? ? ? ? ? ? 297 ARG A NH2 1 180 A A +ATOM 1453 N N . SER A 1 181 ? -8.043 16.931 50.979 1.0 33.65 ? ? ? ? ? ? 298 SER A N 1 181 A A +ATOM 1454 C CA . SER A 1 181 ? -8.775 17.989 50.294 1.0 48.8 ? ? ? ? ? ? 298 SER A CA 1 181 A A +ATOM 1455 C C . SER A 1 181 ? -7.939 18.725 49.255 1.0 55.8 ? ? ? ? ? ? 298 SER A C 1 181 A A +ATOM 1456 O O . SER A 1 181 ? -8.447 19.105 48.199 1.0 69.35 ? ? ? ? ? ? 298 SER A O 1 181 A A +ATOM 1457 C CB . SER A 1 181 ? -9.329 18.991 51.312 1.0 70.22 ? ? ? ? ? ? 298 SER A CB 1 181 A A +ATOM 1458 O OG . SER A 1 181 ? -10.117 18.341 52.295 1.0 90.58 ? ? ? ? ? ? 298 SER A OG 1 181 A A +ATOM 1459 N N . PHE A 1 182 ? -6.658 18.921 49.551 1.0 51.08 ? ? ? ? ? ? 299 PHE A N 1 182 A A +ATOM 1460 C CA . PHE A 1 182 ? -5.770 19.624 48.629 1.0 47.74 ? ? ? ? ? ? 299 PHE A CA 1 182 A A +ATOM 1461 C C . PHE A 1 182 ? -5.536 18.857 47.326 1.0 45.77 ? ? ? ? ? ? 299 PHE A C 1 182 A A +ATOM 1462 O O . PHE A 1 182 ? -5.510 19.446 46.244 1.0 48.51 ? ? ? ? ? ? 299 PHE A O 1 182 A A +ATOM 1463 C CB . PHE A 1 182 ? -4.425 19.914 49.304 1.0 40.1 ? ? ? ? ? ? 299 PHE A CB 1 182 A A +ATOM 1464 C CG . PHE A 1 182 ? -3.520 20.798 48.490 1.0 44.36 ? ? ? ? ? ? 299 PHE A CG 1 182 A A +ATOM 1465 C CD1 . PHE A 1 182 ? -3.424 22.158 48.760 1.0 48.96 ? ? ? ? ? ? 299 PHE A CD1 1 182 A A +ATOM 1466 C CD2 . PHE A 1 182 ? -2.776 20.271 47.437 1.0 54.77 ? ? ? ? ? ? 299 PHE A CD2 1 182 A A +ATOM 1467 C CE1 . PHE A 1 182 ? -2.602 22.984 47.989 1.0 47.65 ? ? ? ? ? ? 299 PHE A CE1 1 182 A A +ATOM 1468 C CE2 . PHE A 1 182 ? -1.952 21.086 46.662 1.0 44.92 ? ? ? ? ? ? 299 PHE A CE2 1 182 A A +ATOM 1469 C CZ . PHE A 1 182 ? -1.865 22.445 46.939 1.0 50.64 ? ? ? ? ? ? 299 PHE A CZ 1 182 A A +ATOM 1470 N N . ALA A 1 183 ? -5.361 17.544 47.434 1.0 44.41 ? ? ? ? ? ? 300 ALA A N 1 183 A A +ATOM 1471 C CA . ALA A 1 183 ? -5.125 16.704 46.266 1.0 21.58 ? ? ? ? ? ? 300 ALA A CA 1 183 A A +ATOM 1472 C C . ALA A 1 183 ? -6.244 16.825 45.232 1.0 27.76 ? ? ? ? ? ? 300 ALA A C 1 183 A A +ATOM 1473 O O . ALA A 1 183 ? -5.984 17.149 44.072 1.0 30.56 ? ? ? ? ? ? 300 ALA A O 1 183 A A +ATOM 1474 C CB . ALA A 1 183 ? -4.960 15.255 46.696 1.0 28.65 ? ? ? ? ? ? 300 ALA A CB 1 183 A A +ATOM 1475 N N . GLN A 1 184 ? -7.484 16.566 45.648 1.0 19.15 ? ? ? ? ? ? 301 GLN A N 1 184 A A +ATOM 1476 C CA . GLN A 1 184 ? -8.624 16.655 44.738 1.0 29.43 ? ? ? ? ? ? 301 GLN A CA 1 184 A A +ATOM 1477 C C . GLN A 1 184 ? -8.628 18.031 44.099 1.0 27.53 ? ? ? ? ? ? 301 GLN A C 1 184 A A +ATOM 1478 O O . GLN A 1 184 ? -8.853 18.172 42.898 1.0 31.56 ? ? ? ? ? ? 301 GLN A O 1 184 A A +ATOM 1479 C CB . GLN A 1 184 ? -9.933 16.440 45.493 1.0 35.17 ? ? ? ? ? ? 301 GLN A CB 1 184 A A +ATOM 1480 C CG . GLN A 1 184 ? -10.015 15.124 46.232 1.0 61.01 ? ? ? ? ? ? 301 GLN A CG 1 184 A A +ATOM 1481 C CD . GLN A 1 184 ? -11.220 15.066 47.149 1.0 66.46 ? ? ? ? ? ? 301 GLN A CD 1 184 A A +ATOM 1482 O OE1 . GLN A 1 184 ? -11.674 16.091 47.657 1.0 69.57 ? ? ? ? ? ? 301 GLN A OE1 1 184 A A +ATOM 1483 N NE2 . GLN A 1 184 ? -11.747 13.868 47.363 1.0 80.16 ? ? ? ? ? ? 301 GLN A NE2 1 184 A A +ATOM 1484 N N . PHE A 1 185 ? -8.369 19.041 44.920 1.0 25.62 ? ? ? ? ? ? 302 PHE A N 1 185 A A +ATOM 1485 C CA . PHE A 1 185 ? -8.319 20.427 44.468 1.0 40.62 ? ? ? ? ? ? 302 PHE A CA 1 185 A A +ATOM 1486 C C . PHE A 1 185 ? -7.313 20.567 43.325 1.0 40.18 ? ? ? ? ? ? 302 PHE A C 1 185 A A +ATOM 1487 O O . PHE A 1 185 ? -7.646 21.047 42.242 1.0 50.94 ? ? ? ? ? ? 302 PHE A O 1 185 A A +ATOM 1488 C CB . PHE A 1 185 ? -7.934 21.330 45.648 1.0 46.62 ? ? ? ? ? ? 302 PHE A CB 1 185 A A +ATOM 1489 C CG . PHE A 1 185 ? -7.403 22.682 45.250 1.0 43.28 ? ? ? ? ? ? 302 PHE A CG 1 185 A A +ATOM 1490 C CD1 . PHE A 1 185 ? -7.956 23.391 44.188 1.0 39.76 ? ? ? ? ? ? 302 PHE A CD1 1 185 A A +ATOM 1491 C CD2 . PHE A 1 185 ? -6.352 23.255 45.959 1.0 59.26 ? ? ? ? ? ? 302 PHE A CD2 1 185 A A +ATOM 1492 C CE1 . PHE A 1 185 ? -7.469 24.646 43.838 1.0 30.38 ? ? ? ? ? ? 302 PHE A CE1 1 185 A A +ATOM 1493 C CE2 . PHE A 1 185 ? -5.858 24.509 45.618 1.0 52.72 ? ? ? ? ? ? 302 PHE A CE2 1 185 A A +ATOM 1494 C CZ . PHE A 1 185 ? -6.418 25.206 44.556 1.0 53.46 ? ? ? ? ? ? 302 PHE A CZ 1 185 A A +ATOM 1495 N N . SER A 1 186 ? -6.079 20.146 43.579 1.0 41.42 ? ? ? ? ? ? 303 SER A N 1 186 A A +ATOM 1496 C CA . SER A 1 186 ? -5.027 20.209 42.575 1.0 35.49 ? ? ? ? ? ? 303 SER A CA 1 186 A A +ATOM 1497 C C . SER A 1 186 ? -5.484 19.483 41.316 1.0 30.28 ? ? ? ? ? ? 303 SER A C 1 186 A A +ATOM 1498 O O . SER A 1 186 ? -5.446 20.030 40.216 1.0 40.36 ? ? ? ? ? ? 303 SER A O 1 186 A A +ATOM 1499 C CB . SER A 1 186 ? -3.754 19.550 43.111 1.0 41.52 ? ? ? ? ? ? 303 SER A CB 1 186 A A +ATOM 1500 O OG . SER A 1 186 ? -3.298 20.201 44.284 1.0 55.45 ? ? ? ? ? ? 303 SER A OG 1 186 A A +ATOM 1501 N N . GLN A 1 187 ? -5.922 18.243 41.494 1.0 2.0 ? ? ? ? ? ? 304 GLN A N 1 187 A A +ATOM 1502 C CA . GLN A 1 187 ? -6.384 17.421 40.390 1.0 2.0 ? ? ? ? ? ? 304 GLN A CA 1 187 A A +ATOM 1503 C C . GLN A 1 187 ? -7.422 18.124 39.531 1.0 13.01 ? ? ? ? ? ? 304 GLN A C 1 187 A A +ATOM 1504 O O . GLN A 1 187 ? -7.443 17.954 38.314 1.0 21.06 ? ? ? ? ? ? 304 GLN A O 1 187 A A +ATOM 1505 C CB . GLN A 1 187 ? -6.971 16.119 40.924 1.0 10.14 ? ? ? ? ? ? 304 GLN A CB 1 187 A A +ATOM 1506 C CG . GLN A 1 187 ? -7.281 15.097 39.845 1.0 17.3 ? ? ? ? ? ? 304 GLN A CG 1 187 A A +ATOM 1507 C CD . GLN A 1 187 ? -7.561 13.725 40.417 1.0 17.68 ? ? ? ? ? ? 304 GLN A CD 1 187 A A +ATOM 1508 O OE1 . GLN A 1 187 ? -7.734 13.572 41.624 1.0 44.51 ? ? ? ? ? ? 304 GLN A OE1 1 187 A A +ATOM 1509 N NE2 . GLN A 1 187 ? -7.609 12.715 39.552 1.0 27.72 ? ? ? ? ? ? 304 GLN A NE2 1 187 A A +ATOM 1510 N N . GLU A 1 188 ? -8.295 18.897 40.169 1.0 30.55 ? ? ? ? ? ? 305 GLU A N 1 188 A A +ATOM 1511 C CA . GLU A 1 188 ? -9.335 19.625 39.448 1.0 57.3 ? ? ? ? ? ? 305 GLU A CA 1 188 A A +ATOM 1512 C C . GLU A 1 188 ? -8.684 20.495 38.383 1.0 52.89 ? ? ? ? ? ? 305 GLU A C 1 188 A A +ATOM 1513 O O . GLU A 1 188 ? -9.063 20.455 37.217 1.0 69.22 ? ? ? ? ? ? 305 GLU A O 1 188 A A +ATOM 1514 C CB . GLU A 1 188 ? -10.143 20.499 40.412 1.0 68.9 ? ? ? ? ? ? 305 GLU A CB 1 188 A A +ATOM 1515 C CG . GLU A 1 188 ? -11.053 19.723 41.354 1.0 71.26 ? ? ? ? ? ? 305 GLU A CG 1 188 A A +ATOM 1516 C CD . GLU A 1 188 ? -11.967 18.751 40.628 1.0 68.34 ? ? ? ? ? ? 305 GLU A CD 1 188 A A +ATOM 1517 O OE1 . GLU A 1 188 ? -12.053 17.579 41.054 1.0 64.13 ? ? ? ? ? ? 305 GLU A OE1 1 188 A A +ATOM 1518 O OE2 . GLU A 1 188 ? -12.600 19.159 39.632 1.0 41.57 ? ? ? ? ? ? 305 GLU A OE2 1 188 A A +ATOM 1519 N N . ILE A 1 189 ? -7.701 21.283 38.797 1.0 22.83 ? ? ? ? ? ? 306 ILE A N 1 189 A A +ATOM 1520 C CA . ILE A 1 189 ? -6.986 22.151 37.875 1.0 23.03 ? ? ? ? ? ? 306 ILE A CA 1 189 A A +ATOM 1521 C C . ILE A 1 189 ? -6.399 21.324 36.732 1.0 35.89 ? ? ? ? ? ? 306 ILE A C 1 189 A A +ATOM 1522 O O . ILE A 1 189 ? -6.455 21.725 35.568 1.0 35.29 ? ? ? ? ? ? 306 ILE A O 1 189 A A +ATOM 1523 C CB . ILE A 1 189 ? -5.834 22.889 38.587 1.0 21.44 ? ? ? ? ? ? 306 ILE A CB 1 189 A A +ATOM 1524 C CG1 . ILE A 1 189 ? -6.293 23.367 39.965 1.0 21.06 ? ? ? ? ? ? 306 ILE A CG1 1 189 A A +ATOM 1525 C CG2 . ILE A 1 189 ? -5.367 24.055 37.742 1.0 25.83 ? ? ? ? ? ? 306 ILE A CG2 1 189 A A +ATOM 1526 C CD1 . ILE A 1 189 ? -5.204 24.028 40.782 1.0 23.91 ? ? ? ? ? ? 306 ILE A CD1 1 189 A A +ATOM 1527 N N . GLY A 1 190 ? -5.833 20.169 37.075 1.0 44.29 ? ? ? ? ? ? 307 GLY A N 1 190 A A +ATOM 1528 C CA . GLY A 1 190 ? -5.251 19.300 36.067 1.0 47.84 ? ? ? ? ? ? 307 GLY A CA 1 190 A A +ATOM 1529 C C . GLY A 1 190 ? -6.288 18.876 35.046 1.0 42.72 ? ? ? ? ? ? 307 GLY A C 1 190 A A +ATOM 1530 O O . GLY A 1 190 ? -6.061 18.956 33.840 1.0 52.99 ? ? ? ? ? ? 307 GLY A O 1 190 A A +ATOM 1531 N N . LEU A 1 191 ? -7.440 18.439 35.539 1.0 26.68 ? ? ? ? ? ? 308 LEU A N 1 191 A A +ATOM 1532 C CA . LEU A 1 191 ? -8.520 18.005 34.675 1.0 24.4 ? ? ? ? ? ? 308 LEU A CA 1 191 A A +ATOM 1533 C C . LEU A 1 191 ? -9.053 19.191 33.879 1.0 20.6 ? ? ? ? ? ? 308 LEU A C 1 191 A A +ATOM 1534 O O . LEU A 1 191 ? -9.550 19.030 32.768 1.0 32.31 ? ? ? ? ? ? 308 LEU A O 1 191 A A +ATOM 1535 C CB . LEU A 1 191 ? -9.620 17.378 35.525 1.0 18.68 ? ? ? ? ? ? 308 LEU A CB 1 191 A A +ATOM 1536 C CG . LEU A 1 191 ? -9.160 16.086 36.196 1.0 22.99 ? ? ? ? ? ? 308 LEU A CG 1 191 A A +ATOM 1537 C CD1 . LEU A 1 191 ? -9.675 16.018 37.614 1.0 29.02 ? ? ? ? ? ? 308 LEU A CD1 1 191 A A +ATOM 1538 C CD2 . LEU A 1 191 ? -9.655 14.908 35.377 1.0 42.41 ? ? ? ? ? ? 308 LEU A CD2 1 191 A A +ATOM 1539 N N . ALA A 1 192 ? -8.935 20.382 34.457 1.0 20.27 ? ? ? ? ? ? 309 ALA A N 1 192 A A +ATOM 1540 C CA . ALA A 1 192 ? -9.398 21.604 33.807 1.0 32.97 ? ? ? ? ? ? 309 ALA A CA 1 192 A A +ATOM 1541 C C . ALA A 1 192 ? -8.505 21.933 32.619 1.0 38.35 ? ? ? ? ? ? 309 ALA A C 1 192 A A +ATOM 1542 O O . ALA A 1 192 ? -8.974 22.091 31.491 1.0 61.64 ? ? ? ? ? ? 309 ALA A O 1 192 A A +ATOM 1543 C CB . ALA A 1 192 ? -9.383 22.759 34.798 1.0 44.37 ? ? ? ? ? ? 309 ALA A CB 1 192 A A +ATOM 1544 N N . SER A 1 193 ? -7.209 22.020 32.889 1.0 45.34 ? ? ? ? ? ? 310 SER A N 1 193 A A +ATOM 1545 C CA . SER A 1 193 ? -6.215 22.340 31.873 1.0 43.85 ? ? ? ? ? ? 310 SER A CA 1 193 A A +ATOM 1546 C C . SER A 1 193 ? -6.170 21.373 30.692 1.0 44.66 ? ? ? ? ? ? 310 SER A C 1 193 A A +ATOM 1547 O O . SER A 1 193 ? -5.660 21.718 29.630 1.0 43.51 ? ? ? ? ? ? 310 SER A O 1 193 A A +ATOM 1548 C CB . SER A 1 193 ? -4.828 22.406 32.517 1.0 20.23 ? ? ? ? ? ? 310 SER A CB 1 193 A A +ATOM 1549 O OG . SER A 1 193 ? -4.440 21.135 33.009 1.0 31.77 ? ? ? ? ? ? 310 SER A OG 1 193 A A +ATOM 1550 N N . LEU A 1 194 ? -6.704 20.168 30.869 1.0 35.5 ? ? ? ? ? ? 311 LEU A N 1 194 A A +ATOM 1551 C CA . LEU A 1 194 ? -6.674 19.177 29.794 1.0 34.72 ? ? ? ? ? ? 311 LEU A CA 1 194 A A +ATOM 1552 C C . LEU A 1 194 ? -7.368 19.652 28.517 1.0 29.11 ? ? ? ? ? ? 311 LEU A C 1 194 A A +ATOM 1553 O O . LEU A 1 194 ? -8.599 19.667 28.430 1.0 33.8 ? ? ? ? ? ? 311 LEU A O 1 194 A A +ATOM 1554 C CB . LEU A 1 194 ? -7.294 17.855 30.269 1.0 34.25 ? ? ? ? ? ? 311 LEU A CB 1 194 A A +ATOM 1555 C CG . LEU A 1 194 ? -6.514 17.088 31.344 1.0 28.71 ? ? ? ? ? ? 311 LEU A CG 1 194 A A +ATOM 1556 C CD1 . LEU A 1 194 ? -7.256 15.820 31.720 1.0 38.96 ? ? ? ? ? ? 311 LEU A CD1 1 194 A A +ATOM 1557 C CD2 . LEU A 1 194 ? -5.131 16.754 30.828 1.0 34.55 ? ? ? ? ? ? 311 LEU A CD2 1 194 A A +ATOM 1558 N N . GLY A 1 195 ? -6.564 20.042 27.529 1.0 27.51 ? ? ? ? ? ? 312 GLY A N 1 195 A A +ATOM 1559 C CA . GLY A 1 195 ? -7.101 20.497 26.261 1.0 27.15 ? ? ? ? ? ? 312 GLY A CA 1 195 A A +ATOM 1560 C C . GLY A 1 195 ? -7.631 21.913 26.293 1.0 33.5 ? ? ? ? ? ? 312 GLY A C 1 195 A A +ATOM 1561 O O . GLY A 1 195 ? -8.263 22.359 25.341 1.0 47.74 ? ? ? ? ? ? 312 GLY A O 1 195 A A +ATOM 1562 N N . ALA A 1 196 ? -7.370 22.620 27.386 1.0 35.93 ? ? ? ? ? ? 313 ALA A N 1 196 A A +ATOM 1563 C CA . ALA A 1 196 ? -7.838 23.995 27.534 1.0 42.84 ? ? ? ? ? ? 313 ALA A CA 1 196 A A +ATOM 1564 C C . ALA A 1 196 ? -7.041 24.958 26.661 1.0 49.69 ? ? ? ? ? ? 313 ALA A C 1 196 A A +ATOM 1565 O O . ALA A 1 196 ? -5.841 24.776 26.456 1.0 39.03 ? ? ? ? ? ? 313 ALA A O 1 196 A A +ATOM 1566 C CB . ALA A 1 196 ? -7.748 24.419 28.992 1.0 58.23 ? ? ? ? ? ? 313 ALA A CB 1 196 A A +ATOM 1567 N N . PRO A 1 197 ? -7.700 26.009 26.140 1.0 50.08 ? ? ? ? ? ? 314 PRO A N 1 197 A A +ATOM 1568 C CA . PRO A 1 197 ? -6.990 26.972 25.292 1.0 41.23 ? ? ? ? ? ? 314 PRO A CA 1 197 A A +ATOM 1569 C C . PRO A 1 197 ? -5.987 27.797 26.094 1.0 42.9 ? ? ? ? ? ? 314 PRO A C 1 197 A A +ATOM 1570 O O . PRO A 1 197 ? -6.208 28.102 27.269 1.0 37.65 ? ? ? ? ? ? 314 PRO A O 1 197 A A +ATOM 1571 C CB . PRO A 1 197 ? -8.107 27.821 24.687 1.0 37.63 ? ? ? ? ? ? 314 PRO A CB 1 197 A A +ATOM 1572 C CG . PRO A 1 197 ? -9.234 27.708 25.647 1.0 50.98 ? ? ? ? ? ? 314 PRO A CG 1 197 A A +ATOM 1573 C CD . PRO A 1 197 ? -9.120 26.364 26.320 1.0 52.52 ? ? ? ? ? ? 314 PRO A CD 1 197 A A +ATOM 1574 N N . ASP A 1 198 ? -4.885 28.145 25.439 1.0 34.49 ? ? ? ? ? ? 315 ASP A N 1 198 A A +ATOM 1575 C CA . ASP A 1 198 ? -3.808 28.915 26.055 1.0 49.06 ? ? ? ? ? ? 315 ASP A CA 1 198 A A +ATOM 1576 C C . ASP A 1 198 ? -4.252 29.977 27.061 1.0 51.21 ? ? ? ? ? ? 315 ASP A C 1 198 A A +ATOM 1577 O O . ASP A 1 198 ? -3.794 29.985 28.202 1.0 56.95 ? ? ? ? ? ? 315 ASP A O 1 198 A A +ATOM 1578 C CB . ASP A 1 198 ? -2.948 29.563 24.966 1.0 48.54 ? ? ? ? ? ? 315 ASP A CB 1 198 A A +ATOM 1579 C CG . ASP A 1 198 ? -2.394 28.552 23.983 1.0 70.86 ? ? ? ? ? ? 315 ASP A CG 1 198 A A +ATOM 1580 O OD1 . ASP A 1 198 ? -3.128 28.160 23.053 1.0 86.04 ? ? ? ? ? ? 315 ASP A OD1 1 198 A A +ATOM 1581 O OD2 . ASP A 1 198 ? -1.226 28.148 24.142 1.0 74.96 ? ? ? ? ? ? 315 ASP A OD2 1 198 A A +ATOM 1582 N N . GLU A 1 199 ? -5.136 30.873 26.639 1.0 57.76 ? ? ? ? ? ? 316 GLU A N 1 199 A A +ATOM 1583 C CA . GLU A 1 199 ? -5.610 31.938 27.520 1.0 63.9 ? ? ? ? ? ? 316 GLU A CA 1 199 A A +ATOM 1584 C C . GLU A 1 199 ? -6.022 31.416 28.883 1.0 54.58 ? ? ? ? ? ? 316 GLU A C 1 199 A A +ATOM 1585 O O . GLU A 1 199 ? -5.680 32.004 29.905 1.0 63.62 ? ? ? ? ? ? 316 GLU A O 1 199 A A +ATOM 1586 C CB . GLU A 1 199 ? -6.799 32.674 26.901 1.0 76.14 ? ? ? ? ? ? 316 GLU A CB 1 199 A A +ATOM 1587 C CG . GLU A 1 199 ? -7.902 31.760 26.431 1.0 99.2 ? ? ? ? ? ? 316 GLU A CG 1 199 A A +ATOM 1588 C CD . GLU A 1 199 ? -7.782 31.433 24.959 1.0 100.0 ? ? ? ? ? ? 316 GLU A CD 1 199 A A +ATOM 1589 O OE1 . GLU A 1 199 ? -8.819 31.128 24.335 1.0 100.0 ? ? ? ? ? ? 316 GLU A OE1 1 199 A A +ATOM 1590 O OE2 . GLU A 1 199 ? -6.651 31.483 24.426 1.0 99.33 ? ? ? ? ? ? 316 GLU A OE2 1 199 A A +ATOM 1591 N N . TYR A 1 200 ? -6.766 30.317 28.894 1.0 55.07 ? ? ? ? ? ? 317 TYR A N 1 200 A A +ATOM 1592 C CA . TYR A 1 200 ? -7.227 29.740 30.147 1.0 62.74 ? ? ? ? ? ? 317 TYR A CA 1 200 A A +ATOM 1593 C C . TYR A 1 200 ? -6.131 28.961 30.848 1.0 63.68 ? ? ? ? ? ? 317 TYR A C 1 200 A A +ATOM 1594 O O . TYR A 1 200 ? -6.111 28.865 32.075 1.0 62.23 ? ? ? ? ? ? 317 TYR A O 1 200 A A +ATOM 1595 C CB . TYR A 1 200 ? -8.436 28.843 29.895 1.0 62.04 ? ? ? ? ? ? 317 TYR A CB 1 200 A A +ATOM 1596 C CG . TYR A 1 200 ? -9.707 29.630 29.729 1.0 73.8 ? ? ? ? ? ? 317 TYR A CG 1 200 A A +ATOM 1597 C CD1 . TYR A 1 200 ? -10.133 30.035 28.467 1.0 72.45 ? ? ? ? ? ? 317 TYR A CD1 1 200 A A +ATOM 1598 C CD2 . TYR A 1 200 ? -10.461 30.012 30.837 1.0 77.85 ? ? ? ? ? ? 317 TYR A CD2 1 200 A A +ATOM 1599 C CE1 . TYR A 1 200 ? -11.276 30.808 28.311 1.0 84.03 ? ? ? ? ? ? 317 TYR A CE1 1 200 A A +ATOM 1600 C CE2 . TYR A 1 200 ? -11.608 30.785 30.693 1.0 92.79 ? ? ? ? ? ? 317 TYR A CE2 1 200 A A +ATOM 1601 C CZ . TYR A 1 200 ? -12.011 31.178 29.428 1.0 92.66 ? ? ? ? ? ? 317 TYR A CZ 1 200 A A +ATOM 1602 O OH . TYR A 1 200 ? -13.149 31.938 29.284 1.0 96.95 ? ? ? ? ? ? 317 TYR A OH 1 200 A A +ATOM 1603 N N . ILE A 1 201 ? -5.226 28.390 30.063 1.0 60.35 ? ? ? ? ? ? 318 ILE A N 1 201 A A +ATOM 1604 C CA . ILE A 1 201 ? -4.113 27.639 30.625 1.0 54.44 ? ? ? ? ? ? 318 ILE A CA 1 201 A A +ATOM 1605 C C . ILE A 1 201 ? -3.306 28.613 31.482 1.0 58.97 ? ? ? ? ? ? 318 ILE A C 1 201 A A +ATOM 1606 O O . ILE A 1 201 ? -2.974 28.336 32.637 1.0 45.23 ? ? ? ? ? ? 318 ILE A O 1 201 A A +ATOM 1607 C CB . ILE A 1 201 ? -3.203 27.072 29.509 1.0 35.8 ? ? ? ? ? ? 318 ILE A CB 1 201 A A +ATOM 1608 C CG1 . ILE A 1 201 ? -3.844 25.829 28.889 1.0 44.13 ? ? ? ? ? ? 318 ILE A CG1 1 201 A A +ATOM 1609 C CG2 . ILE A 1 201 ? -1.831 26.732 30.069 1.0 50.68 ? ? ? ? ? ? 318 ILE A CG2 1 201 A A +ATOM 1610 C CD1 . ILE A 1 201 ? -3.905 24.628 29.814 1.0 43.38 ? ? ? ? ? ? 318 ILE A CD1 1 201 A A +ATOM 1611 N N . GLU A 1 202 ? -3.002 29.765 30.893 1.0 63.96 ? ? ? ? ? ? 319 GLU A N 1 202 A A +ATOM 1612 C CA . GLU A 1 202 ? -2.243 30.807 31.567 1.0 69.66 ? ? ? ? ? ? 319 GLU A CA 1 202 A A +ATOM 1613 C C . GLU A 1 202 ? -3.010 31.317 32.785 1.0 71.97 ? ? ? ? ? ? 319 GLU A C 1 202 A A +ATOM 1614 O O . GLU A 1 202 ? -2.420 31.611 33.825 1.0 78.92 ? ? ? ? ? ? 319 GLU A O 1 202 A A +ATOM 1615 C CB . GLU A 1 202 ? -1.970 31.955 30.592 1.0 70.55 ? ? ? ? ? ? 319 GLU A CB 1 202 A A +ATOM 1616 C CG . GLU A 1 202 ? -1.114 33.067 31.162 1.0 87.11 ? ? ? ? ? ? 319 GLU A CG 1 202 A A +ATOM 1617 C CD . GLU A 1 202 ? -1.795 34.418 31.072 1.0 90.13 ? ? ? ? ? ? 319 GLU A CD 1 202 A A +ATOM 1618 O OE1 . GLU A 1 202 ? -1.378 35.238 30.224 1.0 88.14 ? ? ? ? ? ? 319 GLU A OE1 1 202 A A +ATOM 1619 O OE2 . GLU A 1 202 ? -2.749 34.656 31.846 1.0 100.0 ? ? ? ? ? ? 319 GLU A OE2 1 202 A A +ATOM 1620 N N . LYS A 1 203 ? -4.328 31.423 32.642 1.0 71.83 ? ? ? ? ? ? 320 LYS A N 1 203 A A +ATOM 1621 C CA . LYS A 1 203 ? -5.195 31.880 33.722 1.0 65.51 ? ? ? ? ? ? 320 LYS A CA 1 203 A A +ATOM 1622 C C . LYS A 1 203 ? -5.112 30.914 34.901 1.0 64.01 ? ? ? ? ? ? 320 LYS A C 1 203 A A +ATOM 1623 O O . LYS A 1 203 ? -5.010 31.335 36.052 1.0 72.7 ? ? ? ? ? ? 320 LYS A O 1 203 A A +ATOM 1624 C CB . LYS A 1 203 ? -6.645 31.966 33.238 1.0 77.04 ? ? ? ? ? ? 320 LYS A CB 1 203 A A +ATOM 1625 C CG . LYS A 1 203 ? -6.965 33.201 32.415 1.0 87.96 ? ? ? ? ? ? 320 LYS A CG 1 203 A A +ATOM 1626 C CD . LYS A 1 203 ? -8.428 33.214 32.008 1.0 84.41 ? ? ? ? ? ? 320 LYS A CD 1 203 A A +ATOM 1627 C CE . LYS A 1 203 ? -8.781 34.470 31.235 1.0 80.24 ? ? ? ? ? ? 320 LYS A CE 1 203 A A +ATOM 1628 N NZ . LYS A 1 203 ? -10.191 34.441 30.762 1.0 68.82 ? ? ? ? ? ? 320 LYS A NZ 1 203 A A +ATOM 1629 N N . LEU A 1 204 ? -5.156 29.614 34.608 1.0 61.92 ? ? ? ? ? ? 321 LEU A N 1 204 A A +ATOM 1630 C CA . LEU A 1 204 ? -5.075 28.586 35.643 1.0 41.48 ? ? ? ? ? ? 321 LEU A CA 1 204 A A +ATOM 1631 C C . LEU A 1 204 ? -3.718 28.668 36.334 1.0 49.38 ? ? ? ? ? ? 321 LEU A C 1 204 A A +ATOM 1632 O O . LEU A 1 204 ? -3.631 28.618 37.560 1.0 40.94 ? ? ? ? ? ? 321 LEU A O 1 204 A A +ATOM 1633 C CB . LEU A 1 204 ? -5.260 27.198 35.031 1.0 28.77 ? ? ? ? ? ? 321 LEU A CB 1 204 A A +ATOM 1634 C CG . LEU A 1 204 ? -6.682 26.829 34.594 1.0 53.73 ? ? ? ? ? ? 321 LEU A CG 1 204 A A +ATOM 1635 C CD1 . LEU A 1 204 ? -6.621 25.756 33.516 1.0 63.28 ? ? ? ? ? ? 321 LEU A CD1 1 204 A A +ATOM 1636 C CD2 . LEU A 1 204 ? -7.485 26.343 35.795 1.0 45.22 ? ? ? ? ? ? 321 LEU A CD2 1 204 A A +ATOM 1637 N N . ALA A 1 205 ? -2.660 28.789 35.539 1.0 50.27 ? ? ? ? ? ? 322 ALA A N 1 205 A A +ATOM 1638 C CA . ALA A 1 205 ? -1.317 28.902 36.090 1.0 55.07 ? ? ? ? ? ? 322 ALA A CA 1 205 A A +ATOM 1639 C C . ALA A 1 205 ? -1.321 30.041 37.099 1.0 53.68 ? ? ? ? ? ? 322 ALA A C 1 205 A A +ATOM 1640 O O . ALA A 1 205 ? -0.887 29.880 38.237 1.0 62.64 ? ? ? ? ? ? 322 ALA A O 1 205 A A +ATOM 1641 C CB . ALA A 1 205 ? -0.315 29.192 34.983 1.0 71.28 ? ? ? ? ? ? 322 ALA A CB 1 205 A A +ATOM 1642 N N . THR A 1 206 ? -1.829 31.190 36.671 1.0 62.35 ? ? ? ? ? ? 323 THR A N 1 206 A A +ATOM 1643 C CA . THR A 1 206 ? -1.903 32.363 37.531 1.0 72.61 ? ? ? ? ? ? 323 THR A CA 1 206 A A +ATOM 1644 C C . THR A 1 206 ? -2.660 32.043 38.819 1.0 70.34 ? ? ? ? ? ? 323 THR A C 1 206 A A +ATOM 1645 O O . THR A 1 206 ? -2.296 32.525 39.894 1.0 85.31 ? ? ? ? ? ? 323 THR A O 1 206 A A +ATOM 1646 C CB . THR A 1 206 ? -2.604 33.534 36.815 1.0 77.67 ? ? ? ? ? ? 323 THR A CB 1 206 A A +ATOM 1647 O OG1 . THR A 1 206 ? -2.084 33.662 35.485 1.0 80.21 ? ? ? ? ? ? 323 THR A OG1 1 206 A A +ATOM 1648 C CG2 . THR A 1 206 ? -2.374 34.834 37.571 1.0 80.45 ? ? ? ? ? ? 323 THR A CG2 1 206 A A +ATOM 1649 N N . ILE A 1 207 ? -3.716 31.239 38.707 1.0 51.98 ? ? ? ? ? ? 324 ILE A N 1 207 A A +ATOM 1650 C CA . ILE A 1 207 ? -4.503 30.848 39.876 1.0 58.05 ? ? ? ? ? ? 324 ILE A CA 1 207 A A +ATOM 1651 C C . ILE A 1 207 ? -3.628 29.937 40.729 1.0 66.0 ? ? ? ? ? ? 324 ILE A C 1 207 A A +ATOM 1652 O O . ILE A 1 207 ? -3.511 30.117 41.940 1.0 82.1 ? ? ? ? ? ? 324 ILE A O 1 207 A A +ATOM 1653 C CB . ILE A 1 207 ? -5.772 30.065 39.477 1.0 63.37 ? ? ? ? ? ? 324 ILE A CB 1 207 A A +ATOM 1654 C CG1 . ILE A 1 207 ? -6.651 30.913 38.557 1.0 66.11 ? ? ? ? ? ? 324 ILE A CG1 1 207 A A +ATOM 1655 C CG2 . ILE A 1 207 ? -6.541 29.654 40.726 1.0 49.75 ? ? ? ? ? ? 324 ILE A CG2 1 207 A A +ATOM 1656 C CD1 . ILE A 1 207 ? -7.137 32.198 39.190 1.0 76.62 ? ? ? ? ? ? 324 ILE A CD1 1 207 A A +ATOM 1657 N N . TYR A 1 208 ? -3.011 28.960 40.073 1.0 63.58 ? ? ? ? ? ? 325 TYR A N 1 208 A A +ATOM 1658 C CA . TYR A 1 208 ? -2.119 28.003 40.721 1.0 74.13 ? ? ? ? ? ? 325 TYR A CA 1 208 A A +ATOM 1659 C C . TYR A 1 208 ? -1.112 28.755 41.589 1.0 73.28 ? ? ? ? ? ? 325 TYR A C 1 208 A A +ATOM 1660 O O . TYR A 1 208 ? -0.704 28.284 42.651 1.0 57.45 ? ? ? ? ? ? 325 TYR A O 1 208 A A +ATOM 1661 C CB . TYR A 1 208 ? -1.394 27.191 39.640 1.0 87.95 ? ? ? ? ? ? 325 TYR A CB 1 208 A A +ATOM 1662 C CG . TYR A 1 208 ? -0.381 26.187 40.142 1.0 94.17 ? ? ? ? ? ? 325 TYR A CG 1 208 A A +ATOM 1663 C CD1 . TYR A 1 208 ? 0.966 26.529 40.267 1.0 86.2 ? ? ? ? ? ? 325 TYR A CD1 1 208 A A +ATOM 1664 C CD2 . TYR A 1 208 ? -0.760 24.877 40.442 1.0 92.24 ? ? ? ? ? ? 325 TYR A CD2 1 208 A A +ATOM 1665 C CE1 . TYR A 1 208 ? 1.913 25.590 40.677 1.0 86.39 ? ? ? ? ? ? 325 TYR A CE1 1 208 A A +ATOM 1666 C CE2 . TYR A 1 208 ? 0.178 23.930 40.852 1.0 87.95 ? ? ? ? ? ? 325 TYR A CE2 1 208 A A +ATOM 1667 C CZ . TYR A 1 208 ? 1.511 24.293 40.965 1.0 92.56 ? ? ? ? ? ? 325 TYR A CZ 1 208 A A +ATOM 1668 O OH . TYR A 1 208 ? 2.439 23.354 41.355 1.0 100.0 ? ? ? ? ? ? 325 TYR A OH 1 208 A A +ATOM 1669 N N . TRP A 1 209 ? -0.716 29.932 41.121 1.0 71.2 ? ? ? ? ? ? 326 TRP A N 1 209 A A +ATOM 1670 C CA . TRP A 1 209 ? 0.233 30.776 41.827 1.0 76.56 ? ? ? ? ? ? 326 TRP A CA 1 209 A A +ATOM 1671 C C . TRP A 1 209 ? -0.376 31.305 43.118 1.0 79.27 ? ? ? ? ? ? 326 TRP A C 1 209 A A +ATOM 1672 O O . TRP A 1 209 ? 0.061 30.946 44.210 1.0 76.38 ? ? ? ? ? ? 326 TRP A O 1 209 A A +ATOM 1673 C CB . TRP A 1 209 ? 0.638 31.955 40.940 1.0 79.57 ? ? ? ? ? ? 326 TRP A CB 1 209 A A +ATOM 1674 C CG . TRP A 1 209 ? 1.838 32.707 41.434 1.0 95.51 ? ? ? ? ? ? 326 TRP A CG 1 209 A A +ATOM 1675 C CD1 . TRP A 1 209 ? 1.845 33.802 42.253 1.0 90.06 ? ? ? ? ? ? 326 TRP A CD1 1 209 A A +ATOM 1676 C CD2 . TRP A 1 209 ? 3.208 32.449 41.102 1.0 97.95 ? ? ? ? ? ? 326 TRP A CD2 1 209 A A +ATOM 1677 N NE1 . TRP A 1 209 ? 3.132 34.240 42.449 1.0 85.64 ? ? ? ? ? ? 326 TRP A NE1 1 209 A A +ATOM 1678 C CE2 . TRP A 1 209 ? 3.987 33.427 41.755 1.0 95.89 ? ? ? ? ? ? 326 TRP A CE2 1 209 A A +ATOM 1679 C CE3 . TRP A 1 209 ? 3.850 31.479 40.317 1.0 100.0 ? ? ? ? ? ? 326 TRP A CE3 1 209 A A +ATOM 1680 C CZ2 . TRP A 1 209 ? 5.383 33.469 41.646 1.0 99.19 ? ? ? ? ? ? 326 TRP A CZ2 1 209 A A +ATOM 1681 C CZ3 . TRP A 1 209 ? 5.240 31.521 40.209 1.0 100.0 ? ? ? ? ? ? 326 TRP A CZ3 1 209 A A +ATOM 1682 C CH2 . TRP A 1 209 ? 5.989 32.514 40.869 1.0 100.0 ? ? ? ? ? ? 326 TRP A CH2 1 209 A A +ATOM 1683 N N . PHE A 1 210 ? -1.387 32.159 42.985 1.0 85.13 ? ? ? ? ? ? 327 PHE A N 1 210 A A +ATOM 1684 C CA . PHE A 1 210 ? -2.057 32.762 44.136 1.0 88.36 ? ? ? ? ? ? 327 PHE A CA 1 210 A A +ATOM 1685 C C . PHE A 1 210 ? -2.804 31.754 45.006 1.0 85.94 ? ? ? ? ? ? 327 PHE A C 1 210 A A +ATOM 1686 O O . PHE A 1 210 ? -3.663 32.129 45.805 1.0 91.3 ? ? ? ? ? ? 327 PHE A O 1 210 A A +ATOM 1687 C CB . PHE A 1 210 ? -3.037 33.842 43.663 1.0 95.87 ? ? ? ? ? ? 327 PHE A CB 1 210 A A +ATOM 1688 C CG . PHE A 1 210 ? -2.369 35.045 43.057 1.0 100.0 ? ? ? ? ? ? 327 PHE A CG 1 210 A A +ATOM 1689 C CD1 . PHE A 1 210 ? -1.628 35.921 43.847 1.0 95.08 ? ? ? ? ? ? 327 PHE A CD1 1 210 A A +ATOM 1690 C CD2 . PHE A 1 210 ? -2.479 35.309 41.691 1.0 96.1 ? ? ? ? ? ? 327 PHE A CD2 1 210 A A +ATOM 1691 C CE1 . PHE A 1 210 ? -1.004 37.033 43.289 1.0 100.0 ? ? ? ? ? ? 327 PHE A CE1 1 210 A A +ATOM 1692 C CE2 . PHE A 1 210 ? -1.860 36.416 41.122 1.0 83.49 ? ? ? ? ? ? 327 PHE A CE2 1 210 A A +ATOM 1693 C CZ . PHE A 1 210 ? -1.119 37.280 41.921 1.0 97.35 ? ? ? ? ? ? 327 PHE A CZ 1 210 A A +ATOM 1694 N N . THR A 1 211 ? -2.475 30.477 44.839 1.0 76.73 ? ? ? ? ? ? 328 THR A N 1 211 A A +ATOM 1695 C CA . THR A 1 211 ? -3.104 29.414 45.613 1.0 66.8 ? ? ? ? ? ? 328 THR A CA 1 211 A A +ATOM 1696 C C . THR A 1 211 ? -2.051 28.443 46.107 1.0 62.01 ? ? ? ? ? ? 328 THR A C 1 211 A A +ATOM 1697 O O . THR A 1 211 ? -1.643 28.483 47.263 1.0 53.07 ? ? ? ? ? ? 328 THR A O 1 211 A A +ATOM 1698 C CB . THR A 1 211 ? -4.143 28.642 44.774 1.0 59.57 ? ? ? ? ? ? 328 THR A CB 1 211 A A +ATOM 1699 O OG1 . THR A 1 211 ? -3.535 28.160 43.572 1.0 66.06 ? ? ? ? ? ? 328 THR A OG1 1 211 A A +ATOM 1700 C CG2 . THR A 1 211 ? -5.316 29.544 44.422 1.0 61.12 ? ? ? ? ? ? 328 THR A CG2 1 211 A A +ATOM 1701 N N . VAL A 1 212 ? -1.602 27.581 45.204 1.0 68.93 ? ? ? ? ? ? 329 VAL A N 1 212 A A +ATOM 1702 C CA . VAL A 1 212 ? -0.597 26.571 45.520 1.0 72.84 ? ? ? ? ? ? 329 VAL A CA 1 212 A A +ATOM 1703 C C . VAL A 1 212 ? 0.774 27.159 45.821 1.0 71.72 ? ? ? ? ? ? 329 VAL A C 1 212 A A +ATOM 1704 O O . VAL A 1 212 ? 1.427 26.769 46.781 1.0 62.53 ? ? ? ? ? ? 329 VAL A O 1 212 A A +ATOM 1705 C CB . VAL A 1 212 ? -0.462 25.552 44.355 1.0 74.58 ? ? ? ? ? ? 329 VAL A CB 1 212 A A +ATOM 1706 C CG1 . VAL A 1 212 ? 0.551 24.463 44.718 1.0 74.82 ? ? ? ? ? ? 329 VAL A CG1 1 212 A A +ATOM 1707 C CG2 . VAL A 1 212 ? -1.822 24.933 44.035 1.0 84.73 ? ? ? ? ? ? 329 VAL A CG2 1 212 A A +ATOM 1708 N N . GLU A 1 213 ? 1.199 28.101 44.991 1.0 80.14 ? ? ? ? ? ? 330 GLU A N 1 213 A A +ATOM 1709 C CA . GLU A 1 213 ? 2.497 28.736 45.156 1.0 92.46 ? ? ? ? ? ? 330 GLU A CA 1 213 A A +ATOM 1710 C C . GLU A 1 213 ? 2.550 29.803 46.245 1.0 96.63 ? ? ? ? ? ? 330 GLU A C 1 213 A A +ATOM 1711 O O . GLU A 1 213 ? 3.339 29.705 47.181 1.0 86.36 ? ? ? ? ? ? 330 GLU A O 1 213 A A +ATOM 1712 C CB . GLU A 1 213 ? 2.949 29.330 43.823 1.0 92.3 ? ? ? ? ? ? 330 GLU A CB 1 213 A A +ATOM 1713 C CG . GLU A 1 213 ? 3.317 28.282 42.794 1.0 97.63 ? ? ? ? ? ? 330 GLU A CG 1 213 A A +ATOM 1714 C CD . GLU A 1 213 ? 4.639 27.608 43.108 1.0 99.92 ? ? ? ? ? ? 330 GLU A CD 1 213 A A +ATOM 1715 O OE1 . GLU A 1 213 ? 5.122 26.825 42.260 1.0 100.0 ? ? ? ? ? ? 330 GLU A OE1 1 213 A A +ATOM 1716 O OE2 . GLU A 1 213 ? 5.196 27.864 44.199 1.0 80.99 ? ? ? ? ? ? 330 GLU A OE2 1 213 A A +ATOM 1717 N N . PHE A 1 214 ? 1.704 30.821 46.122 1.0 100.0 ? ? ? ? ? ? 331 PHE A N 1 214 A A +ATOM 1718 C CA . PHE A 1 214 ? 1.668 31.912 47.093 1.0 100.0 ? ? ? ? ? ? 331 PHE A CA 1 214 A A +ATOM 1719 C C . PHE A 1 214 ? 0.267 32.206 47.615 1.0 100.0 ? ? ? ? ? ? 331 PHE A C 1 214 A A +ATOM 1720 O O . PHE A 1 214 ? -0.227 33.332 47.512 1.0 100.0 ? ? ? ? ? ? 331 PHE A O 1 214 A A +ATOM 1721 C CB . PHE A 1 214 ? 2.253 33.183 46.473 1.0 100.0 ? ? ? ? ? ? 331 PHE A CB 1 214 A A +ATOM 1722 C CG . PHE A 1 214 ? 3.718 33.087 46.171 1.0 100.0 ? ? ? ? ? ? 331 PHE A CG 1 214 A A +ATOM 1723 C CD1 . PHE A 1 214 ? 4.163 32.463 45.009 1.0 99.45 ? ? ? ? ? ? 331 PHE A CD1 1 214 A A +ATOM 1724 C CD2 . PHE A 1 214 ? 4.658 33.609 47.054 1.0 100.0 ? ? ? ? ? ? 331 PHE A CD2 1 214 A A +ATOM 1725 C CE1 . PHE A 1 214 ? 5.524 32.360 44.732 1.0 100.0 ? ? ? ? ? ? 331 PHE A CE1 1 214 A A +ATOM 1726 C CE2 . PHE A 1 214 ? 6.022 33.512 46.786 1.0 100.0 ? ? ? ? ? ? 331 PHE A CE2 1 214 A A +ATOM 1727 C CZ . PHE A 1 214 ? 6.454 32.886 45.622 1.0 100.0 ? ? ? ? ? ? 331 PHE A CZ 1 214 A A +ATOM 1728 N N . GLY A 1 215 ? -0.376 31.191 48.175 1.0 89.37 ? ? ? ? ? ? 332 GLY A N 1 215 A A +ATOM 1729 C CA . GLY A 1 215 ? -1.715 31.381 48.693 1.0 80.87 ? ? ? ? ? ? 332 GLY A CA 1 215 A A +ATOM 1730 C C . GLY A 1 215 ? -1.739 31.390 50.205 1.0 82.14 ? ? ? ? ? ? 332 GLY A C 1 215 A A +ATOM 1731 O O . GLY A 1 215 ? -0.827 30.869 50.850 1.0 75.18 ? ? ? ? ? ? 332 GLY A O 1 215 A A +ATOM 1732 N N . LEU A 1 216 ? -2.785 31.991 50.766 1.0 90.21 ? ? ? ? ? ? 333 LEU A N 1 216 A A +ATOM 1733 C CA . LEU A 1 216 ? -2.963 32.064 52.212 1.0 96.85 ? ? ? ? ? ? 333 LEU A CA 1 216 A A +ATOM 1734 C C . LEU A 1 216 ? -4.344 31.513 52.544 1.0 99.83 ? ? ? ? ? ? 333 LEU A C 1 216 A A +ATOM 1735 O O . LEU A 1 216 ? -5.331 31.865 51.898 1.0 96.81 ? ? ? ? ? ? 333 LEU A O 1 216 A A +ATOM 1736 C CB . LEU A 1 216 ? -2.849 33.511 52.693 1.0 99.98 ? ? ? ? ? ? 333 LEU A CB 1 216 A A +ATOM 1737 C CG . LEU A 1 216 ? -1.451 34.128 52.604 1.0 100.0 ? ? ? ? ? ? 333 LEU A CG 1 216 A A +ATOM 1738 C CD1 . LEU A 1 216 ? -1.514 35.582 53.034 1.0 93.61 ? ? ? ? ? ? 333 LEU A CD1 1 216 A A +ATOM 1739 C CD2 . LEU A 1 216 ? -0.484 33.353 53.481 1.0 96.96 ? ? ? ? ? ? 333 LEU A CD2 1 216 A A +ATOM 1740 N N . CYS A 1 217 ? -4.417 30.653 53.554 1.0 100.0 ? ? ? ? ? ? 334 CYS A N 1 217 A A +ATOM 1741 C CA . CYS A 1 217 ? -5.691 30.051 53.935 1.0 96.68 ? ? ? ? ? ? 334 CYS A CA 1 217 A A +ATOM 1742 C C . CYS A 1 217 ? -6.319 30.639 55.194 1.0 96.69 ? ? ? ? ? ? 334 CYS A C 1 217 A A +ATOM 1743 O O . CYS A 1 217 ? -5.752 31.518 55.847 1.0 93.2 ? ? ? ? ? ? 334 CYS A O 1 217 A A +ATOM 1744 C CB . CYS A 1 217 ? -5.523 28.541 54.118 1.0 89.59 ? ? ? ? ? ? 334 CYS A CB 1 217 A A +ATOM 1745 S SG . CYS A 1 217 ? -4.503 28.069 55.544 1.0 98.82 ? ? ? ? ? ? 334 CYS A SG 1 217 A A +ATOM 1746 N N . LYS A 1 218 ? -7.499 30.125 55.524 1.0 93.07 ? ? ? ? ? ? 335 LYS A N 1 218 A A +ATOM 1747 C CA . LYS A 1 218 ? -8.252 30.567 56.689 1.0 92.31 ? ? ? ? ? ? 335 LYS A CA 1 218 A A +ATOM 1748 C C . LYS A 1 218 ? -8.249 29.525 57.802 1.0 93.47 ? ? ? ? ? ? 335 LYS A C 1 218 A A +ATOM 1749 O O . LYS A 1 218 ? -8.699 28.395 57.608 1.0 84.68 ? ? ? ? ? ? 335 LYS A O 1 218 A A +ATOM 1750 C CB . LYS A 1 218 ? -9.692 30.865 56.283 1.0 92.51 ? ? ? ? ? ? 335 LYS A CB 1 218 A A +ATOM 1751 C CG . LYS A 1 218 ? -9.838 32.102 55.428 1.0 94.2 ? ? ? ? ? ? 335 LYS A CG 1 218 A A +ATOM 1752 C CD . LYS A 1 218 ? -10.683 33.144 56.135 1.0 100.0 ? ? ? ? ? ? 335 LYS A CD 1 218 A A +ATOM 1753 C CE . LYS A 1 218 ? -9.825 34.061 56.993 1.0 100.0 ? ? ? ? ? ? 335 LYS A CE 1 218 A A +ATOM 1754 N NZ . LYS A 1 218 ? -9.241 33.369 58.179 1.0 100.0 ? ? ? ? ? ? 335 LYS A NZ 1 218 A A +ATOM 1755 N N . GLN A 1 219 ? -7.751 29.916 58.972 1.0 98.07 ? ? ? ? ? ? 336 GLN A N 1 219 A A +ATOM 1756 C CA . GLN A 1 219 ? -7.697 29.015 60.119 1.0 100.0 ? ? ? ? ? ? 336 GLN A CA 1 219 A A +ATOM 1757 C C . GLN A 1 219 ? -8.427 29.611 61.321 1.0 100.0 ? ? ? ? ? ? 336 GLN A C 1 219 A A +ATOM 1758 O O . GLN A 1 219 ? -7.814 29.929 62.341 1.0 100.0 ? ? ? ? ? ? 336 GLN A O 1 219 A A +ATOM 1759 C CB . GLN A 1 219 ? -6.240 28.719 60.486 1.0 100.0 ? ? ? ? ? ? 336 GLN A CB 1 219 A A +ATOM 1760 C CG . GLN A 1 219 ? -5.462 28.008 59.386 1.0 97.01 ? ? ? ? ? ? 336 GLN A CG 1 219 A A +ATOM 1761 C CD . GLN A 1 219 ? -5.703 26.510 59.370 1.0 92.6 ? ? ? ? ? ? 336 GLN A CD 1 219 A A +ATOM 1762 O OE1 . GLN A 1 219 ? -6.254 25.945 60.316 1.0 92.65 ? ? ? ? ? ? 336 GLN A OE1 1 219 A A +ATOM 1763 N NE2 . GLN A 1 219 ? -5.285 25.857 58.291 1.0 100.0 ? ? ? ? ? ? 336 GLN A NE2 1 219 A A +ATOM 1764 N N . GLY A 1 220 ? -9.743 29.748 61.191 1.0 100.0 ? ? ? ? ? ? 337 GLY A N 1 220 A A +ATOM 1765 C CA . GLY A 1 220 ? -10.548 30.311 62.259 1.0 97.11 ? ? ? ? ? ? 337 GLY A CA 1 220 A A +ATOM 1766 C C . GLY A 1 220 ? -10.766 31.795 62.039 1.0 91.62 ? ? ? ? ? ? 337 GLY A C 1 220 A A +ATOM 1767 O O . GLY A 1 220 ? -11.723 32.203 61.383 1.0 80.53 ? ? ? ? ? ? 337 GLY A O 1 220 A A +ATOM 1768 N N . ASP A 1 221 ? -9.870 32.607 62.588 1.0 93.19 ? ? ? ? ? ? 338 ASP A N 1 221 A A +ATOM 1769 C CA . ASP A 1 221 ? -9.958 34.054 62.438 1.0 97.91 ? ? ? ? ? ? 338 ASP A CA 1 221 A A +ATOM 1770 C C . ASP A 1 221 ? -8.681 34.522 61.764 1.0 98.74 ? ? ? ? ? ? 338 ASP A C 1 221 A A +ATOM 1771 O O . ASP A 1 221 ? -8.690 35.394 60.890 1.0 100.0 ? ? ? ? ? ? 338 ASP A O 1 221 A A +ATOM 1772 C CB . ASP A 1 221 ? -10.079 34.727 63.807 1.0 100.0 ? ? ? ? ? ? 338 ASP A CB 1 221 A A +ATOM 1773 C CG . ASP A 1 221 ? -11.382 34.399 64.504 1.0 100.0 ? ? ? ? ? ? 338 ASP A CG 1 221 A A +ATOM 1774 O OD1 . ASP A 1 221 ? -12.450 34.673 63.917 1.0 100.0 ? ? ? ? ? ? 338 ASP A OD1 1 221 A A +ATOM 1775 O OD2 . ASP A 1 221 ? -11.339 33.870 65.635 1.0 88.6 ? ? ? ? ? ? 338 ASP A OD2 1 221 A A +ATOM 1776 N N . SER A 1 222 ? -7.582 33.912 62.188 1.0 100.0 ? ? ? ? ? ? 339 SER A N 1 222 A A +ATOM 1777 C CA . SER A 1 222 ? -6.263 34.233 61.673 1.0 100.0 ? ? ? ? ? ? 339 SER A CA 1 222 A A +ATOM 1778 C C . SER A 1 222 ? -6.014 33.665 60.282 1.0 100.0 ? ? ? ? ? ? 339 SER A C 1 222 A A +ATOM 1779 O O . SER A 1 222 ? -6.785 32.844 59.779 1.0 81.59 ? ? ? ? ? ? 339 SER A O 1 222 A A +ATOM 1780 C CB . SER A 1 222 ? -5.194 33.710 62.635 1.0 100.0 ? ? ? ? ? ? 339 SER A CB 1 222 A A +ATOM 1781 O OG . SER A 1 222 ? -5.404 32.337 62.928 1.0 100.0 ? ? ? ? ? ? 339 SER A OG 1 222 A A +ATOM 1782 N N . ILE A 1 223 ? -4.920 34.115 59.677 1.0 100.0 ? ? ? ? ? ? 340 ILE A N 1 223 A A +ATOM 1783 C CA . ILE A 1 223 ? -4.522 33.675 58.350 1.0 100.0 ? ? ? ? ? ? 340 ILE A CA 1 223 A A +ATOM 1784 C C . ILE A 1 223 ? -3.171 32.970 58.410 1.0 100.0 ? ? ? ? ? ? 340 ILE A C 1 223 A A +ATOM 1785 O O . ILE A 1 223 ? -2.237 33.440 59.068 1.0 100.0 ? ? ? ? ? ? 340 ILE A O 1 223 A A +ATOM 1786 C CB . ILE A 1 223 ? -4.426 34.872 57.370 1.0 89.23 ? ? ? ? ? ? 340 ILE A CB 1 223 A A +ATOM 1787 C CG1 . ILE A 1 223 ? -5.706 34.952 56.539 1.0 72.49 ? ? ? ? ? ? 340 ILE A CG1 1 223 A A +ATOM 1788 C CG2 . ILE A 1 223 ? -3.207 34.729 56.463 1.0 94.22 ? ? ? ? ? ? 340 ILE A CG2 1 223 A A +ATOM 1789 C CD1 . ILE A 1 223 ? -6.901 35.449 57.316 1.0 58.91 ? ? ? ? ? ? 340 ILE A CD1 1 223 A A +ATOM 1790 N N . LYS A 1 224 ? -3.079 31.844 57.713 1.0 98.6 ? ? ? ? ? ? 341 LYS A N 1 224 A A +ATOM 1791 C CA . LYS A 1 224 ? -1.848 31.069 57.663 1.0 96.02 ? ? ? ? ? ? 341 LYS A CA 1 224 A A +ATOM 1792 C C . LYS A 1 224 ? -1.344 30.972 56.226 1.0 99.82 ? ? ? ? ? ? 341 LYS A C 1 224 A A +ATOM 1793 O O . LYS A 1 224 ? -2.078 31.258 55.274 1.0 96.22 ? ? ? ? ? ? 341 LYS A O 1 224 A A +ATOM 1794 C CB . LYS A 1 224 ? -2.081 29.666 58.226 1.0 85.54 ? ? ? ? ? ? 341 LYS A CB 1 224 A A +ATOM 1795 C CG . LYS A 1 224 ? -2.294 29.634 59.730 1.0 80.54 ? ? ? ? ? ? 341 LYS A CG 1 224 A A +ATOM 1796 C CD . LYS A 1 224 ? -1.011 29.953 60.473 1.0 85.94 ? ? ? ? ? ? 341 LYS A CD 1 224 A A +ATOM 1797 C CE . LYS A 1 224 ? -1.154 29.699 61.962 1.0 80.46 ? ? ? ? ? ? 341 LYS A CE 1 224 A A +ATOM 1798 N NZ . LYS A 1 224 ? -2.326 30.418 62.527 1.0 92.52 ? ? ? ? ? ? 341 LYS A NZ 1 224 A A +ATOM 1799 N N . ALA A 1 225 ? -0.084 30.578 56.074 1.0 100.0 ? ? ? ? ? ? 342 ALA A N 1 225 A A +ATOM 1800 C CA . ALA A 1 225 ? 0.513 30.440 54.753 1.0 97.67 ? ? ? ? ? ? 342 ALA A CA 1 225 A A +ATOM 1801 C C . ALA A 1 225 ? 0.511 28.977 54.331 1.0 100.0 ? ? ? ? ? ? 342 ALA A C 1 225 A A +ATOM 1802 O O . ALA A 1 225 ? 0.977 28.106 55.066 1.0 96.17 ? ? ? ? ? ? 342 ALA A O 1 225 A A +ATOM 1803 C CB . ALA A 1 225 ? 1.940 30.984 54.758 1.0 87.48 ? ? ? ? ? ? 342 ALA A CB 1 225 A A +ATOM 1804 N N . TYR A 1 226 ? -0.029 28.708 53.149 1.0 100.0 ? ? ? ? ? ? 343 TYR A N 1 226 A A +ATOM 1805 C CA . TYR A 1 226 ? -0.082 27.347 52.627 1.0 97.03 ? ? ? ? ? ? 343 TYR A CA 1 226 A A +ATOM 1806 C C . TYR A 1 226 ? 0.575 27.294 51.252 1.0 96.93 ? ? ? ? ? ? 343 TYR A C 1 226 A A +ATOM 1807 O O . TYR A 1 226 ? 0.706 26.227 50.653 1.0 90.8 ? ? ? ? ? ? 343 TYR A O 1 226 A A +ATOM 1808 C CB . TYR A 1 226 ? -1.536 26.860 52.548 1.0 97.91 ? ? ? ? ? ? 343 TYR A CB 1 226 A A +ATOM 1809 C CG . TYR A 1 226 ? -2.316 27.379 51.361 1.0 100.0 ? ? ? ? ? ? 343 TYR A CG 1 226 A A +ATOM 1810 C CD1 . TYR A 1 226 ? -3.010 28.586 51.432 1.0 100.0 ? ? ? ? ? ? 343 TYR A CD1 1 226 A A +ATOM 1811 C CD2 . TYR A 1 226 ? -2.375 26.654 50.172 1.0 95.4 ? ? ? ? ? ? 343 TYR A CD2 1 226 A A +ATOM 1812 C CE1 . TYR A 1 226 ? -3.741 29.057 50.345 1.0 100.0 ? ? ? ? ? ? 343 TYR A CE1 1 226 A A +ATOM 1813 C CE2 . TYR A 1 226 ? -3.102 27.115 49.083 1.0 94.37 ? ? ? ? ? ? 343 TYR A CE2 1 226 A A +ATOM 1814 C CZ . TYR A 1 226 ? -3.781 28.316 49.174 1.0 100.0 ? ? ? ? ? ? 343 TYR A CZ 1 226 A A +ATOM 1815 O OH . TYR A 1 226 ? -4.489 28.779 48.091 1.0 100.0 ? ? ? ? ? ? 343 TYR A OH 1 226 A A +ATOM 1816 N N . GLY A 1 227 ? 0.985 28.461 50.762 1.0 96.05 ? ? ? ? ? ? 344 GLY A N 1 227 A A +ATOM 1817 C CA . GLY A 1 227 ? 1.637 28.539 49.469 1.0 88.25 ? ? ? ? ? ? 344 GLY A CA 1 227 A A +ATOM 1818 C C . GLY A 1 227 ? 2.981 27.837 49.510 1.0 87.24 ? ? ? ? ? ? 344 GLY A C 1 227 A A +ATOM 1819 O O . GLY A 1 227 ? 3.737 27.974 50.478 1.0 70.32 ? ? ? ? ? ? 344 GLY A O 1 227 A A +ATOM 1820 N N . ALA A 1 228 ? 3.279 27.083 48.458 1.0 90.18 ? ? ? ? ? ? 345 ALA A N 1 228 A A +ATOM 1821 C CA . ALA A 1 228 ? 4.533 26.346 48.374 1.0 83.69 ? ? ? ? ? ? 345 ALA A CA 1 228 A A +ATOM 1822 C C . ALA A 1 228 ? 5.715 27.293 48.231 1.0 74.01 ? ? ? ? ? ? 345 ALA A C 1 228 A A +ATOM 1823 O O . ALA A 1 228 ? 6.782 27.053 48.793 1.0 65.65 ? ? ? ? ? ? 345 ALA A O 1 228 A A +ATOM 1824 C CB . ALA A 1 228 ? 4.488 25.386 47.203 1.0 88.07 ? ? ? ? ? ? 345 ALA A CB 1 228 A A +ATOM 1825 N N . GLY A 1 229 ? 5.521 28.367 47.475 1.0 74.04 ? ? ? ? ? ? 346 GLY A N 1 229 A A +ATOM 1826 C CA . GLY A 1 229 ? 6.582 29.336 47.288 1.0 89.94 ? ? ? ? ? ? 346 GLY A CA 1 229 A A +ATOM 1827 C C . GLY A 1 229 ? 6.846 30.099 48.573 1.0 96.5 ? ? ? ? ? ? 346 GLY A C 1 229 A A +ATOM 1828 O O . GLY A 1 229 ? 7.955 30.581 48.804 1.0 100.0 ? ? ? ? ? ? 346 GLY A O 1 229 A A +ATOM 1829 N N . LEU A 1 230 ? 5.820 30.208 49.412 1.0 100.0 ? ? ? ? ? ? 347 LEU A N 1 230 A A +ATOM 1830 C CA . LEU A 1 230 ? 5.935 30.910 50.687 1.0 97.91 ? ? ? ? ? ? 347 LEU A CA 1 230 A A +ATOM 1831 C C . LEU A 1 230 ? 6.681 30.070 51.718 1.0 92.74 ? ? ? ? ? ? 347 LEU A C 1 230 A A +ATOM 1832 O O . LEU A 1 230 ? 7.621 30.536 52.357 1.0 97.68 ? ? ? ? ? ? 347 LEU A O 1 230 A A +ATOM 1833 C CB . LEU A 1 230 ? 4.548 31.239 51.244 1.0 97.57 ? ? ? ? ? ? 347 LEU A CB 1 230 A A +ATOM 1834 C CG . LEU A 1 230 ? 3.641 32.170 50.440 1.0 98.6 ? ? ? ? ? ? 347 LEU A CG 1 230 A A +ATOM 1835 C CD1 . LEU A 1 230 ? 2.228 32.099 51.004 1.0 97.3 ? ? ? ? ? ? 347 LEU A CD1 1 230 A A +ATOM 1836 C CD2 . LEU A 1 230 ? 4.179 33.591 50.497 1.0 86.84 ? ? ? ? ? ? 347 LEU A CD2 1 230 A A +ATOM 1837 N N . LEU A 1 231 ? 6.242 28.827 51.874 1.0 92.32 ? ? ? ? ? ? 348 LEU A N 1 231 A A +ATOM 1838 C CA . LEU A 1 231 ? 6.832 27.905 52.836 1.0 90.82 ? ? ? ? ? ? 348 LEU A CA 1 231 A A +ATOM 1839 C C . LEU A 1 231 ? 8.304 27.585 52.606 1.0 85.36 ? ? ? ? ? ? 348 LEU A C 1 231 A A +ATOM 1840 O O . LEU A 1 231 ? 9.042 27.356 53.560 1.0 82.64 ? ? ? ? ? ? 348 LEU A O 1 231 A A +ATOM 1841 C CB . LEU A 1 231 ? 6.019 26.608 52.863 1.0 100.0 ? ? ? ? ? ? 348 LEU A CB 1 231 A A +ATOM 1842 C CG . LEU A 1 231 ? 4.565 26.809 53.308 1.0 100.0 ? ? ? ? ? ? 348 LEU A CG 1 231 A A +ATOM 1843 C CD1 . LEU A 1 231 ? 3.693 25.698 52.750 1.0 91.11 ? ? ? ? ? ? 348 LEU A CD1 1 231 A A +ATOM 1844 C CD2 . LEU A 1 231 ? 4.497 26.855 54.826 1.0 96.11 ? ? ? ? ? ? 348 LEU A CD2 1 231 A A +ATOM 1845 N N . SER A 1 232 ? 8.728 27.557 51.347 1.0 91.34 ? ? ? ? ? ? 349 SER A N 1 232 A A +ATOM 1846 C CA . SER A 1 232 ? 10.120 27.256 51.031 1.0 95.94 ? ? ? ? ? ? 349 SER A CA 1 232 A A +ATOM 1847 C C . SER A 1 232 ? 10.990 28.508 51.060 1.0 96.35 ? ? ? ? ? ? 349 SER A C 1 232 A A +ATOM 1848 O O . SER A 1 232 ? 12.218 28.419 51.069 1.0 100.0 ? ? ? ? ? ? 349 SER A O 1 232 A A +ATOM 1849 C CB . SER A 1 232 ? 10.217 26.596 49.654 1.0 96.27 ? ? ? ? ? ? 349 SER A CB 1 232 A A +ATOM 1850 O OG . SER A 1 232 ? 9.866 27.500 48.619 1.0 100.0 ? ? ? ? ? ? 349 SER A OG 1 232 A A +ATOM 1851 N N . SER A 1 233 ? 10.350 29.674 51.078 1.0 90.64 ? ? ? ? ? ? 350 SER A N 1 233 A A +ATOM 1852 C CA . SER A 1 233 ? 11.072 30.943 51.101 1.0 87.36 ? ? ? ? ? ? 350 SER A CA 1 233 A A +ATOM 1853 C C . SER A 1 233 ? 10.990 31.605 52.473 1.0 92.09 ? ? ? ? ? ? 350 SER A C 1 233 A A +ATOM 1854 O O . SER A 1 233 ? 9.914 31.992 52.927 1.0 91.76 ? ? ? ? ? ? 350 SER A O 1 233 A A +ATOM 1855 C CB . SER A 1 233 ? 10.511 31.889 50.040 1.0 83.6 ? ? ? ? ? ? 350 SER A CB 1 233 A A +ATOM 1856 O OG . SER A 1 233 ? 10.765 33.239 50.380 1.0 49.23 ? ? ? ? ? ? 350 SER A OG 1 233 A A +ATOM 1857 N N . PHE A 1 234 ? 12.143 31.741 53.121 1.0 100.0 ? ? ? ? ? ? 351 PHE A N 1 234 A A +ATOM 1858 C CA . PHE A 1 234 ? 12.229 32.337 54.451 1.0 100.0 ? ? ? ? ? ? 351 PHE A CA 1 234 A A +ATOM 1859 C C . PHE A 1 234 ? 11.807 33.804 54.532 1.0 97.44 ? ? ? ? ? ? 351 PHE A C 1 234 A A +ATOM 1860 O O . PHE A 1 234 ? 11.081 34.200 55.442 1.0 91.23 ? ? ? ? ? ? 351 PHE A O 1 234 A A +ATOM 1861 C CB . PHE A 1 234 ? 13.657 32.206 54.989 1.0 95.52 ? ? ? ? ? ? 351 PHE A CB 1 234 A A +ATOM 1862 C CG . PHE A 1 234 ? 13.903 32.996 56.243 1.0 100.0 ? ? ? ? ? ? 351 PHE A CG 1 234 A A +ATOM 1863 C CD1 . PHE A 1 234 ? 13.379 32.571 57.458 1.0 100.0 ? ? ? ? ? ? 351 PHE A CD1 1 234 A A +ATOM 1864 C CD2 . PHE A 1 234 ? 14.643 34.174 56.209 1.0 99.81 ? ? ? ? ? ? 351 PHE A CD2 1 234 A A +ATOM 1865 C CE1 . PHE A 1 234 ? 13.586 33.305 58.624 1.0 100.0 ? ? ? ? ? ? 351 PHE A CE1 1 234 A A +ATOM 1866 C CE2 . PHE A 1 234 ? 14.856 34.917 57.369 1.0 100.0 ? ? ? ? ? ? 351 PHE A CE2 1 234 A A +ATOM 1867 C CZ . PHE A 1 234 ? 14.326 34.481 58.580 1.0 100.0 ? ? ? ? ? ? 351 PHE A CZ 1 234 A A +ATOM 1868 N N . GLY A 1 235 ? 12.276 34.606 53.583 1.0 100.0 ? ? ? ? ? ? 352 GLY A N 1 235 A A +ATOM 1869 C CA . GLY A 1 235 ? 11.959 36.023 53.584 1.0 93.05 ? ? ? ? ? ? 352 GLY A CA 1 235 A A +ATOM 1870 C C . GLY A 1 235 ? 10.501 36.382 53.375 1.0 87.07 ? ? ? ? ? ? 352 GLY A C 1 235 A A +ATOM 1871 O O . GLY A 1 235 ? 10.013 37.357 53.942 1.0 85.59 ? ? ? ? ? ? 352 GLY A O 1 235 A A +ATOM 1872 N N . GLU A 1 236 ? 9.799 35.601 52.563 1.0 88.12 ? ? ? ? ? ? 353 GLU A N 1 236 A A +ATOM 1873 C CA . GLU A 1 236 ? 8.394 35.877 52.290 1.0 91.87 ? ? ? ? ? ? 353 GLU A CA 1 236 A A +ATOM 1874 C C . GLU A 1 236 ? 7.450 35.189 53.263 1.0 83.67 ? ? ? ? ? ? 353 GLU A C 1 236 A A +ATOM 1875 O O . GLU A 1 236 ? 6.275 35.541 53.352 1.0 74.09 ? ? ? ? ? ? 353 GLU A O 1 236 A A +ATOM 1876 C CB . GLU A 1 236 ? 8.040 35.461 50.866 1.0 96.37 ? ? ? ? ? ? 353 GLU A CB 1 236 A A +ATOM 1877 C CG . GLU A 1 236 ? 6.970 36.325 50.229 1.0 78.33 ? ? ? ? ? ? 353 GLU A CG 1 236 A A +ATOM 1878 C CD . GLU A 1 236 ? 7.084 36.360 48.722 1.0 91.93 ? ? ? ? ? ? 353 GLU A CD 1 236 A A +ATOM 1879 O OE1 . GLU A 1 236 ? 6.188 36.931 48.067 1.0 95.55 ? ? ? ? ? ? 353 GLU A OE1 1 236 A A +ATOM 1880 O OE2 . GLU A 1 236 ? 8.075 35.818 48.191 1.0 99.96 ? ? ? ? ? ? 353 GLU A OE2 1 236 A A +ATOM 1881 N N . LEU A 1 237 ? 7.965 34.199 53.980 1.0 84.35 ? ? ? ? ? ? 354 LEU A N 1 237 A A +ATOM 1882 C CA . LEU A 1 237 ? 7.160 33.468 54.947 1.0 94.8 ? ? ? ? ? ? 354 LEU A CA 1 237 A A +ATOM 1883 C C . LEU A 1 237 ? 6.716 34.411 56.061 1.0 98.39 ? ? ? ? ? ? 354 LEU A C 1 237 A A +ATOM 1884 O O . LEU A 1 237 ? 5.583 34.341 56.539 1.0 97.83 ? ? ? ? ? ? 354 LEU A O 1 237 A A +ATOM 1885 C CB . LEU A 1 237 ? 7.971 32.309 55.532 1.0 100.0 ? ? ? ? ? ? 354 LEU A CB 1 237 A A +ATOM 1886 C CG . LEU A 1 237 ? 7.287 31.387 56.545 1.0 100.0 ? ? ? ? ? ? 354 LEU A CG 1 237 A A +ATOM 1887 C CD1 . LEU A 1 237 ? 5.972 30.851 55.984 1.0 100.0 ? ? ? ? ? ? 354 LEU A CD1 1 237 A A +ATOM 1888 C CD2 . LEU A 1 237 ? 8.236 30.248 56.881 1.0 96.48 ? ? ? ? ? ? 354 LEU A CD2 1 237 A A +ATOM 1889 N N . GLN A 1 238 ? 7.619 35.297 56.465 1.0 100.0 ? ? ? ? ? ? 355 GLN A N 1 238 A A +ATOM 1890 C CA . GLN A 1 238 ? 7.325 36.259 57.517 1.0 100.0 ? ? ? ? ? ? 355 GLN A CA 1 238 A A +ATOM 1891 C C . GLN A 1 238 ? 6.675 37.520 56.955 1.0 99.16 ? ? ? ? ? ? 355 GLN A C 1 238 A A +ATOM 1892 O O . GLN A 1 238 ? 5.990 38.247 57.675 1.0 100.0 ? ? ? ? ? ? 355 GLN A O 1 238 A A +ATOM 1893 C CB . GLN A 1 238 ? 8.611 36.628 58.253 1.0 100.0 ? ? ? ? ? ? 355 GLN A CB 1 238 A A +ATOM 1894 C CG . GLN A 1 238 ? 9.855 36.610 57.374 1.0 96.38 ? ? ? ? ? ? 355 GLN A CG 1 238 A A +ATOM 1895 C CD . GLN A 1 238 ? 11.134 36.643 58.186 1.0 100.0 ? ? ? ? ? ? 355 GLN A CD 1 238 A A +ATOM 1896 O OE1 . GLN A 1 238 ? 11.983 37.517 58.004 1.0 97.77 ? ? ? ? ? ? 355 GLN A OE1 1 238 A A +ATOM 1897 N NE2 . GLN A 1 238 ? 11.277 35.684 59.094 1.0 100.0 ? ? ? ? ? ? 355 GLN A NE2 1 238 A A +ATOM 1898 N N . TYR A 1 239 ? 6.886 37.772 55.666 1.0 86.51 ? ? ? ? ? ? 356 TYR A N 1 239 A A +ATOM 1899 C CA . TYR A 1 239 ? 6.324 38.953 55.020 1.0 81.28 ? ? ? ? ? ? 356 TYR A CA 1 239 A A +ATOM 1900 C C . TYR A 1 239 ? 4.831 38.835 54.725 1.0 81.58 ? ? ? ? ? ? 356 TYR A C 1 239 A A +ATOM 1901 O O . TYR A 1 239 ? 4.069 39.776 54.943 1.0 79.85 ? ? ? ? ? ? 356 TYR A O 1 239 A A +ATOM 1902 C CB . TYR A 1 239 ? 7.059 39.251 53.715 1.0 92.91 ? ? ? ? ? ? 356 TYR A CB 1 239 A A +ATOM 1903 C CG . TYR A 1 239 ? 6.277 40.155 52.786 1.0 100.0 ? ? ? ? ? ? 356 TYR A CG 1 239 A A +ATOM 1904 C CD1 . TYR A 1 239 ? 5.952 41.456 53.166 1.0 100.0 ? ? ? ? ? ? 356 TYR A CD1 1 239 A A +ATOM 1905 C CD2 . TYR A 1 239 ? 5.851 39.709 51.534 1.0 100.0 ? ? ? ? ? ? 356 TYR A CD2 1 239 A A +ATOM 1906 C CE1 . TYR A 1 239 ? 5.229 42.294 52.324 1.0 99.01 ? ? ? ? ? ? 356 TYR A CE1 1 239 A A +ATOM 1907 C CE2 . TYR A 1 239 ? 5.126 40.541 50.682 1.0 100.0 ? ? ? ? ? ? 356 TYR A CE2 1 239 A A +ATOM 1908 C CZ . TYR A 1 239 ? 4.819 41.830 51.084 1.0 100.0 ? ? ? ? ? ? 356 TYR A CZ 1 239 A A +ATOM 1909 O OH . TYR A 1 239 ? 4.115 42.658 50.238 1.0 100.0 ? ? ? ? ? ? 356 TYR A OH 1 239 A A +ATOM 1910 N N . CYS A 1 240 ? 4.424 37.682 54.209 1.0 90.52 ? ? ? ? ? ? 357 CYS A N 1 240 A A +ATOM 1911 C CA . CYS A 1 240 ? 3.027 37.443 53.867 1.0 97.06 ? ? ? ? ? ? 357 CYS A CA 1 240 A A +ATOM 1912 C C . CYS A 1 240 ? 2.125 37.404 55.097 1.0 100.0 ? ? ? ? ? ? 357 CYS A C 1 240 A A +ATOM 1913 O O . CYS A 1 240 ? 0.915 37.608 54.994 1.0 100.0 ? ? ? ? ? ? 357 CYS A O 1 240 A A +ATOM 1914 C CB . CYS A 1 240 ? 2.895 36.124 53.100 1.0 100.0 ? ? ? ? ? ? 357 CYS A CB 1 240 A A +ATOM 1915 S SG . CYS A 1 240 ? 3.405 34.655 54.038 1.0 100.0 ? ? ? ? ? ? 357 CYS A SG 1 240 A A +ATOM 1916 N N . LEU A 1 241 ? 2.720 37.149 56.259 1.0 98.65 ? ? ? ? ? ? 358 LEU A N 1 241 A A +ATOM 1917 C CA . LEU A 1 241 ? 1.967 37.064 57.506 1.0 98.17 ? ? ? ? ? ? 358 LEU A CA 1 241 A A +ATOM 1918 C C . LEU A 1 241 ? 1.817 38.408 58.216 1.0 100.0 ? ? ? ? ? ? 358 LEU A C 1 241 A A +ATOM 1919 O O . LEU A 1 241 ? 1.040 38.533 59.164 1.0 100.0 ? ? ? ? ? ? 358 LEU A O 1 241 A A +ATOM 1920 C CB . LEU A 1 241 ? 2.640 36.059 58.444 1.0 88.93 ? ? ? ? ? ? 358 LEU A CB 1 241 A A +ATOM 1921 C CG . LEU A 1 241 ? 1.812 34.840 58.871 1.0 80.52 ? ? ? ? ? ? 358 LEU A CG 1 241 A A +ATOM 1922 C CD1 . LEU A 1 241 ? 0.728 35.281 59.837 1.0 71.58 ? ? ? ? ? ? 358 LEU A CD1 1 241 A A +ATOM 1923 C CD2 . LEU A 1 241 ? 1.207 34.159 57.655 1.0 66.0 ? ? ? ? ? ? 358 LEU A CD2 1 241 A A +ATOM 1924 N N . SER A 1 242 ? 2.550 39.414 57.748 1.0 100.0 ? ? ? ? ? ? 359 SER A N 1 242 A A +ATOM 1925 C CA . SER A 1 242 ? 2.492 40.742 58.352 1.0 98.89 ? ? ? ? ? ? 359 SER A CA 1 242 A A +ATOM 1926 C C . SER A 1 242 ? 1.337 41.589 57.816 1.0 100.0 ? ? ? ? ? ? 359 SER A C 1 242 A A +ATOM 1927 O O . SER A 1 242 ? 0.554 41.137 56.978 1.0 100.0 ? ? ? ? ? ? 359 SER A O 1 242 A A +ATOM 1928 C CB . SER A 1 242 ? 3.817 41.480 58.133 1.0 97.9 ? ? ? ? ? ? 359 SER A CB 1 242 A A +ATOM 1929 O OG . SER A 1 242 ? 4.089 41.655 56.753 1.0 98.54 ? ? ? ? ? ? 359 SER A OG 1 242 A A +ATOM 1930 N N . GLU A 1 243 ? 1.246 42.821 58.309 1.0 100.0 ? ? ? ? ? ? 360 GLU A N 1 243 A A +ATOM 1931 C CA . GLU A 1 243 ? 0.195 43.748 57.900 1.0 100.0 ? ? ? ? ? ? 360 GLU A CA 1 243 A A +ATOM 1932 C C . GLU A 1 243 ? 0.696 44.776 56.890 1.0 97.86 ? ? ? ? ? ? 360 GLU A C 1 243 A A +ATOM 1933 O O . GLU A 1 243 ? 0.388 45.964 56.992 1.0 100.0 ? ? ? ? ? ? 360 GLU A O 1 243 A A +ATOM 1934 C CB . GLU A 1 243 ? -0.375 44.462 59.125 1.0 100.0 ? ? ? ? ? ? 360 GLU A CB 1 243 A A +ATOM 1935 C CG . GLU A 1 243 ? -1.314 43.603 59.946 1.0 98.37 ? ? ? ? ? ? 360 GLU A CG 1 243 A A +ATOM 1936 C CD . GLU A 1 243 ? -1.416 44.070 61.381 1.0 100.0 ? ? ? ? ? ? 360 GLU A CD 1 243 A A +ATOM 1937 O OE1 . GLU A 1 243 ? -1.756 45.252 61.591 1.0 100.0 ? ? ? ? ? ? 360 GLU A OE1 1 243 A A +ATOM 1938 O OE2 . GLU A 1 243 ? -1.152 43.259 62.295 1.0 100.0 ? ? ? ? ? ? 360 GLU A OE2 1 243 A A +ATOM 1939 N N . LYS A 1 244 ? 1.470 44.312 55.917 1.0 98.71 ? ? ? ? ? ? 361 LYS A N 1 244 A A +ATOM 1940 C CA . LYS A 1 244 ? 2.004 45.189 54.885 1.0 98.62 ? ? ? ? ? ? 361 LYS A CA 1 244 A A +ATOM 1941 C C . LYS A 1 244 ? 1.287 44.958 53.552 1.0 100.0 ? ? ? ? ? ? 361 LYS A C 1 244 A A +ATOM 1942 O O . LYS A 1 244 ? 0.924 45.913 52.861 1.0 98.32 ? ? ? ? ? ? 361 LYS A O 1 244 A A +ATOM 1943 C CB . LYS A 1 244 ? 3.510 44.960 54.729 1.0 94.02 ? ? ? ? ? ? 361 LYS A CB 1 244 A A +ATOM 1944 C CG . LYS A 1 244 ? 4.298 45.240 56.003 1.0 91.55 ? ? ? ? ? ? 361 LYS A CG 1 244 A A +ATOM 1945 C CD . LYS A 1 244 ? 5.800 45.110 55.795 1.0 95.22 ? ? ? ? ? ? 361 LYS A CD 1 244 A A +ATOM 1946 C CE . LYS A 1 244 ? 6.560 45.495 57.060 1.0 85.93 ? ? ? ? ? ? 361 LYS A CE 1 244 A A +ATOM 1947 N NZ . LYS A 1 244 ? 8.038 45.436 56.883 1.0 81.42 ? ? ? ? ? ? 361 LYS A NZ 1 244 A A +ATOM 1948 N N . PRO A 1 245 ? 1.052 43.681 53.185 1.0 100.0 ? ? ? ? ? ? 362 PRO A N 1 245 A A +ATOM 1949 C CA . PRO A 1 245 ? 0.372 43.358 51.924 1.0 100.0 ? ? ? ? ? ? 362 PRO A CA 1 245 A A +ATOM 1950 C C . PRO A 1 245 ? -1.138 43.570 52.022 1.0 97.24 ? ? ? ? ? ? 362 PRO A C 1 245 A A +ATOM 1951 O O . PRO A 1 245 ? -1.721 43.431 53.097 1.0 98.12 ? ? ? ? ? ? 362 PRO A O 1 245 A A +ATOM 1952 C CB . PRO A 1 245 ? 0.735 41.896 51.695 1.0 100.0 ? ? ? ? ? ? 362 PRO A CB 1 245 A A +ATOM 1953 C CG . PRO A 1 245 ? 0.912 41.344 53.071 1.0 100.0 ? ? ? ? ? ? 362 PRO A CG 1 245 A A +ATOM 1954 C CD . PRO A 1 245 ? 1.385 42.466 53.950 1.0 100.0 ? ? ? ? ? ? 362 PRO A CD 1 245 A A +ATOM 1955 N N . LYS A 1 246 ? -1.767 43.909 50.899 1.0 95.94 ? ? ? ? ? ? 363 LYS A N 1 246 A A +ATOM 1956 C CA . LYS A 1 246 ? -3.210 44.139 50.878 1.0 98.3 ? ? ? ? ? ? 363 LYS A CA 1 246 A A +ATOM 1957 C C . LYS A 1 246 ? -3.943 42.861 50.469 1.0 99.01 ? ? ? ? ? ? 363 LYS A C 1 246 A A +ATOM 1958 O O . LYS A 1 246 ? -4.081 42.555 49.284 1.0 100.0 ? ? ? ? ? ? 363 LYS A O 1 246 A A +ATOM 1959 C CB . LYS A 1 246 ? -3.553 45.286 49.917 1.0 96.33 ? ? ? ? ? ? 363 LYS A CB 1 246 A A +ATOM 1960 C CG . LYS A 1 246 ? -2.891 45.202 48.546 1.0 88.38 ? ? ? ? ? ? 363 LYS A CG 1 246 A A +ATOM 1961 C CD . LYS A 1 246 ? -2.111 46.473 48.218 1.0 87.54 ? ? ? ? ? ? 363 LYS A CD 1 246 A A +ATOM 1962 C CE . LYS A 1 246 ? -2.942 47.729 48.472 1.0 87.32 ? ? ? ? ? ? 363 LYS A CE 1 246 A A +ATOM 1963 N NZ . LYS A 1 246 ? -3.967 47.956 47.418 1.0 93.79 ? ? ? ? ? ? 363 LYS A NZ 1 246 A A +ATOM 1964 N N . LEU A 1 247 ? -4.405 42.121 51.472 1.0 98.43 ? ? ? ? ? ? 364 LEU A N 1 247 A A +ATOM 1965 C CA . LEU A 1 247 ? -5.115 40.864 51.264 1.0 93.8 ? ? ? ? ? ? 364 LEU A CA 1 247 A A +ATOM 1966 C C . LEU A 1 247 ? -6.451 41.026 50.557 1.0 94.63 ? ? ? ? ? ? 364 LEU A C 1 247 A A +ATOM 1967 O O . LEU A 1 247 ? -7.110 42.061 50.666 1.0 97.05 ? ? ? ? ? ? 364 LEU A O 1 247 A A +ATOM 1968 C CB . LEU A 1 247 ? -5.356 40.166 52.607 1.0 92.04 ? ? ? ? ? ? 364 LEU A CB 1 247 A A +ATOM 1969 C CG . LEU A 1 247 ? -4.148 39.760 53.457 1.0 89.85 ? ? ? ? ? ? 364 LEU A CG 1 247 A A +ATOM 1970 C CD1 . LEU A 1 247 ? -3.116 39.084 52.576 1.0 95.33 ? ? ? ? ? ? 364 LEU A CD1 1 247 A A +ATOM 1971 C CD2 . LEU A 1 247 ? -3.562 40.977 54.154 1.0 96.01 ? ? ? ? ? ? 364 LEU A CD2 1 247 A A +ATOM 1972 N N . LEU A 1 248 ? -6.839 39.981 49.835 1.0 93.72 ? ? ? ? ? ? 365 LEU A N 1 248 A A +ATOM 1973 C CA . LEU A 1 248 ? -8.102 39.957 49.108 1.0 96.16 ? ? ? ? ? ? 365 LEU A CA 1 248 A A +ATOM 1974 C C . LEU A 1 248 ? -8.679 38.542 49.151 1.0 99.86 ? ? ? ? ? ? 365 LEU A C 1 248 A A +ATOM 1975 O O . LEU A 1 248 ? -7.969 37.580 49.442 1.0 95.59 ? ? ? ? ? ? 365 LEU A O 1 248 A A +ATOM 1976 C CB . LEU A 1 248 ? -7.894 40.405 47.660 1.0 92.91 ? ? ? ? ? ? 365 LEU A CB 1 248 A A +ATOM 1977 C CG . LEU A 1 248 ? -7.503 41.875 47.472 1.0 98.37 ? ? ? ? ? ? 365 LEU A CG 1 248 A A +ATOM 1978 C CD1 . LEU A 1 248 ? -7.186 42.119 46.009 1.0 100.0 ? ? ? ? ? ? 365 LEU A CD1 1 248 A A +ATOM 1979 C CD2 . LEU A 1 248 ? -8.629 42.789 47.944 1.0 99.54 ? ? ? ? ? ? 365 LEU A CD2 1 248 A A +ATOM 1980 N N . PRO A 1 249 ? -9.981 38.396 48.852 1.0 100.0 ? ? ? ? ? ? 366 PRO A N 1 249 A A +ATOM 1981 C CA . PRO A 1 249 ? -10.612 37.074 48.877 1.0 96.24 ? ? ? ? ? ? 366 PRO A CA 1 249 A A +ATOM 1982 C C . PRO A 1 249 ? -10.316 36.237 47.643 1.0 92.66 ? ? ? ? ? ? 366 PRO A C 1 249 A A +ATOM 1983 O O . PRO A 1 249 ? -10.209 36.757 46.533 1.0 93.04 ? ? ? ? ? ? 366 PRO A O 1 249 A A +ATOM 1984 C CB . PRO A 1 249 ? -12.094 37.394 49.012 1.0 86.09 ? ? ? ? ? ? 366 PRO A CB 1 249 A A +ATOM 1985 C CG . PRO A 1 249 ? -12.243 38.706 48.311 1.0 94.58 ? ? ? ? ? ? 366 PRO A CG 1 249 A A +ATOM 1986 C CD . PRO A 1 249 ? -10.933 39.446 48.447 1.0 100.0 ? ? ? ? ? ? 366 PRO A CD 1 249 A A +ATOM 1987 N N . LEU A 1 250 ? -10.180 34.932 47.842 1.0 90.26 ? ? ? ? ? ? 367 LEU A N 1 250 A A +ATOM 1988 C CA . LEU A 1 250 ? -9.908 34.044 46.727 1.0 100.0 ? ? ? ? ? ? 367 LEU A CA 1 250 A A +ATOM 1989 C C . LEU A 1 250 ? -11.120 34.042 45.799 1.0 100.0 ? ? ? ? ? ? 367 LEU A C 1 250 A A +ATOM 1990 O O . LEU A 1 250 ? -12.099 33.329 46.030 1.0 96.26 ? ? ? ? ? ? 367 LEU A O 1 250 A A +ATOM 1991 C CB . LEU A 1 250 ? -9.615 32.620 47.222 1.0 96.71 ? ? ? ? ? ? 367 LEU A CB 1 250 A A +ATOM 1992 C CG . LEU A 1 250 ? -9.264 31.634 46.097 1.0 90.96 ? ? ? ? ? ? 367 LEU A CG 1 250 A A +ATOM 1993 C CD1 . LEU A 1 250 ? -7.942 32.037 45.448 1.0 90.36 ? ? ? ? ? ? 367 LEU A CD1 1 250 A A +ATOM 1994 C CD2 . LEU A 1 250 ? -9.184 30.224 46.649 1.0 83.71 ? ? ? ? ? ? 367 LEU A CD2 1 250 A A +ATOM 1995 N N . GLU A 1 251 ? -11.047 34.864 44.756 1.0 100.0 ? ? ? ? ? ? 368 GLU A N 1 251 A A +ATOM 1996 C CA . GLU A 1 251 ? -12.118 34.980 43.769 1.0 100.0 ? ? ? ? ? ? 368 GLU A CA 1 251 A A +ATOM 1997 C C . GLU A 1 251 ? -11.530 34.722 42.382 1.0 100.0 ? ? ? ? ? ? 368 GLU A C 1 251 A A +ATOM 1998 O O . GLU A 1 251 ? -11.121 35.652 41.687 1.0 100.0 ? ? ? ? ? ? 368 GLU A O 1 251 A A +ATOM 1999 C CB . GLU A 1 251 ? -12.729 36.381 43.818 1.0 100.0 ? ? ? ? ? ? 368 GLU A CB 1 251 A A +ATOM 2000 C CG . GLU A 1 251 ? -14.144 36.469 43.284 1.0 100.0 ? ? ? ? ? ? 368 GLU A CG 1 251 A A +ATOM 2001 C CD . GLU A 1 251 ? -14.758 37.833 43.517 1.0 99.78 ? ? ? ? ? ? 368 GLU A CD 1 251 A A +ATOM 2002 O OE1 . GLU A 1 251 ? -15.286 38.426 42.551 1.0 100.0 ? ? ? ? ? ? 368 GLU A OE1 1 251 A A +ATOM 2003 O OE2 . GLU A 1 251 ? -14.704 38.313 44.670 1.0 90.93 ? ? ? ? ? ? 368 GLU A OE2 1 251 A A +ATOM 2004 N N . LEU A 1 252 ? -11.494 33.450 41.992 1.0 100.0 ? ? ? ? ? ? 369 LEU A N 1 252 A A +ATOM 2005 C CA . LEU A 1 252 ? -10.933 33.034 40.708 1.0 95.06 ? ? ? ? ? ? 369 LEU A CA 1 252 A A +ATOM 2006 C C . LEU A 1 252 ? -11.316 33.890 39.503 1.0 94.49 ? ? ? ? ? ? 369 LEU A C 1 252 A A +ATOM 2007 O O . LEU A 1 252 ? -10.606 33.899 38.494 1.0 89.42 ? ? ? ? ? ? 369 LEU A O 1 252 A A +ATOM 2008 C CB . LEU A 1 252 ? -11.297 31.572 40.433 1.0 72.92 ? ? ? ? ? ? 369 LEU A CB 1 252 A A +ATOM 2009 C CG . LEU A 1 252 ? -10.466 30.556 41.222 1.0 70.31 ? ? ? ? ? ? 369 LEU A CG 1 252 A A +ATOM 2010 C CD1 . LEU A 1 252 ? -10.813 30.650 42.697 1.0 77.73 ? ? ? ? ? ? 369 LEU A CD1 1 252 A A +ATOM 2011 C CD2 . LEU A 1 252 ? -10.727 29.158 40.690 1.0 56.07 ? ? ? ? ? ? 369 LEU A CD2 1 252 A A +ATOM 2012 N N . GLU A 1 253 ? -12.429 34.607 39.599 1.0 95.61 ? ? ? ? ? ? 370 GLU A N 1 253 A A +ATOM 2013 C CA . GLU A 1 253 ? -12.864 35.446 38.492 1.0 95.94 ? ? ? ? ? ? 370 GLU A CA 1 253 A A +ATOM 2014 C C . GLU A 1 253 ? -11.875 36.579 38.242 1.0 100.0 ? ? ? ? ? ? 370 GLU A C 1 253 A A +ATOM 2015 O O . GLU A 1 253 ? -11.369 36.744 37.130 1.0 92.14 ? ? ? ? ? ? 370 GLU A O 1 253 A A +ATOM 2016 C CB . GLU A 1 253 ? -14.250 36.028 38.772 1.0 94.59 ? ? ? ? ? ? 370 GLU A CB 1 253 A A +ATOM 2017 C CG . GLU A 1 253 ? -15.178 36.006 37.562 1.0 99.49 ? ? ? ? ? ? 370 GLU A CG 1 253 A A +ATOM 2018 C CD . GLU A 1 253 ? -14.585 36.706 36.351 1.0 100.0 ? ? ? ? ? ? 370 GLU A CD 1 253 A A +ATOM 2019 O OE1 . GLU A 1 253 ? -14.769 37.935 36.222 1.0 100.0 ? ? ? ? ? ? 370 GLU A OE1 1 253 A A +ATOM 2020 O OE2 . GLU A 1 253 ? -13.936 36.028 35.527 1.0 98.6 ? ? ? ? ? ? 370 GLU A OE2 1 253 A A +ATOM 2021 N N . LYS A 1 254 ? -11.602 37.356 39.284 1.0 100.0 ? ? ? ? ? ? 371 LYS A N 1 254 A A +ATOM 2022 C CA . LYS A 1 254 ? -10.687 38.485 39.182 1.0 100.0 ? ? ? ? ? ? 371 LYS A CA 1 254 A A +ATOM 2023 C C . LYS A 1 254 ? -9.261 38.131 39.600 1.0 100.0 ? ? ? ? ? ? 371 LYS A C 1 254 A A +ATOM 2024 O O . LYS A 1 254 ? -8.380 38.992 39.628 1.0 100.0 ? ? ? ? ? ? 371 LYS A O 1 254 A A +ATOM 2025 C CB . LYS A 1 254 ? -11.210 39.644 40.035 1.0 100.0 ? ? ? ? ? ? 371 LYS A CB 1 254 A A +ATOM 2026 C CG . LYS A 1 254 ? -12.622 40.076 39.675 1.0 89.3 ? ? ? ? ? ? 371 LYS A CG 1 254 A A +ATOM 2027 C CD . LYS A 1 254 ? -12.694 40.566 38.235 1.0 90.44 ? ? ? ? ? ? 371 LYS A CD 1 254 A A +ATOM 2028 C CE . LYS A 1 254 ? -14.109 40.956 37.849 1.0 86.33 ? ? ? ? ? ? 371 LYS A CE 1 254 A A +ATOM 2029 N NZ . LYS A 1 254 ? -14.188 41.350 36.418 1.0 76.33 ? ? ? ? ? ? 371 LYS A NZ 1 254 A A +ATOM 2030 N N . THR A 1 255 ? -9.035 36.863 39.923 1.0 91.49 ? ? ? ? ? ? 372 THR A N 1 255 A A +ATOM 2031 C CA . THR A 1 255 ? -7.708 36.423 40.335 1.0 86.86 ? ? ? ? ? ? 372 THR A CA 1 255 A A +ATOM 2032 C C . THR A 1 255 ? -6.869 36.026 39.128 1.0 89.34 ? ? ? ? ? ? 372 THR A C 1 255 A A +ATOM 2033 O O . THR A 1 255 ? -5.645 36.162 39.141 1.0 93.02 ? ? ? ? ? ? 372 THR A O 1 255 A A +ATOM 2034 C CB . THR A 1 255 ? -7.778 35.212 41.287 1.0 80.77 ? ? ? ? ? ? 372 THR A CB 1 255 A A +ATOM 2035 O OG1 . THR A 1 255 ? -8.541 35.554 42.450 1.0 73.3 ? ? ? ? ? ? 372 THR A OG1 1 255 A A +ATOM 2036 C CG2 . THR A 1 255 ? -6.380 34.795 41.712 1.0 81.82 ? ? ? ? ? ? 372 THR A CG2 1 255 A A +ATOM 2037 N N . ALA A 1 256 ? -7.536 35.534 38.087 1.0 90.66 ? ? ? ? ? ? 373 ALA A N 1 256 A A +ATOM 2038 C CA . ALA A 1 256 ? -6.860 35.107 36.866 1.0 89.88 ? ? ? ? ? ? 373 ALA A CA 1 256 A A +ATOM 2039 C C . ALA A 1 256 ? -6.355 36.295 36.049 1.0 93.94 ? ? ? ? ? ? 373 ALA A C 1 256 A A +ATOM 2040 O O . ALA A 1 256 ? -5.378 36.182 35.304 1.0 96.1 ? ? ? ? ? ? 373 ALA A O 1 256 A A +ATOM 2041 C CB . ALA A 1 256 ? -7.803 34.258 36.021 1.0 77.92 ? ? ? ? ? ? 373 ALA A CB 1 256 A A +ATOM 2042 N N . ILE A 1 257 ? -7.028 37.431 36.190 1.0 93.44 ? ? ? ? ? ? 374 ILE A N 1 257 A A +ATOM 2043 C CA . ILE A 1 257 ? -6.647 38.638 35.467 1.0 95.05 ? ? ? ? ? ? 374 ILE A CA 1 257 A A +ATOM 2044 C C . ILE A 1 257 ? -5.403 39.259 36.086 1.0 99.9 ? ? ? ? ? ? 374 ILE A C 1 257 A A +ATOM 2045 O O . ILE A 1 257 ? -4.540 39.790 35.386 1.0 99.6 ? ? ? ? ? ? 374 ILE A O 1 257 A A +ATOM 2046 C CB . ILE A 1 257 ? -7.777 39.678 35.502 1.0 95.85 ? ? ? ? ? ? 374 ILE A CB 1 257 A A +ATOM 2047 C CG1 . ILE A 1 257 ? -9.077 39.043 35.000 1.0 100.0 ? ? ? ? ? ? 374 ILE A CG1 1 257 A A +ATOM 2048 C CG2 . ILE A 1 257 ? -7.397 40.889 34.659 1.0 100.0 ? ? ? ? ? ? 374 ILE A CG2 1 257 A A +ATOM 2049 C CD1 . ILE A 1 257 ? -10.331 39.733 35.491 1.0 100.0 ? ? ? ? ? ? 374 ILE A CD1 1 257 A A +ATOM 2050 N N . GLN A 1 258 ? -5.326 39.175 37.409 1.0 97.32 ? ? ? ? ? ? 375 GLN A N 1 258 A A +ATOM 2051 C CA . GLN A 1 258 ? -4.216 39.718 38.182 1.0 100.0 ? ? ? ? ? ? 375 GLN A CA 1 258 A A +ATOM 2052 C C . GLN A 1 258 ? -2.820 39.405 37.639 1.0 100.0 ? ? ? ? ? ? 375 GLN A C 1 258 A A +ATOM 2053 O O . GLN A 1 258 ? -2.465 38.242 37.451 1.0 100.0 ? ? ? ? ? ? 375 GLN A O 1 258 A A +ATOM 2054 C CB . GLN A 1 258 ? -4.313 39.215 39.622 1.0 100.0 ? ? ? ? ? ? 375 GLN A CB 1 258 A A +ATOM 2055 C CG . GLN A 1 258 ? -3.045 39.417 40.422 1.0 100.0 ? ? ? ? ? ? 375 GLN A CG 1 258 A A +ATOM 2056 C CD . GLN A 1 258 ? -2.851 40.856 40.836 1.0 100.0 ? ? ? ? ? ? 375 GLN A CD 1 258 A A +ATOM 2057 O OE1 . GLN A 1 258 ? -3.655 41.724 40.495 1.0 100.0 ? ? ? ? ? ? 375 GLN A OE1 1 258 A A +ATOM 2058 N NE2 . GLN A 1 258 ? -1.781 41.122 41.578 1.0 100.0 ? ? ? ? ? ? 375 GLN A NE2 1 258 A A +ATOM 2059 N N . ASN A 1 259 ? -2.031 40.456 37.421 1.0 100.0 ? ? ? ? ? ? 376 ASN A N 1 259 A A +ATOM 2060 C CA . ASN A 1 259 ? -0.664 40.327 36.917 1.0 100.0 ? ? ? ? ? ? 376 ASN A CA 1 259 A A +ATOM 2061 C C . ASN A 1 259 ? 0.323 40.374 38.087 1.0 100.0 ? ? ? ? ? ? 376 ASN A C 1 259 A A +ATOM 2062 O O . ASN A 1 259 ? 0.185 41.202 38.987 1.0 97.37 ? ? ? ? ? ? 376 ASN A O 1 259 A A +ATOM 2063 C CB . ASN A 1 259 ? -0.360 41.463 35.935 1.0 93.27 ? ? ? ? ? ? 376 ASN A CB 1 259 A A +ATOM 2064 C CG . ASN A 1 259 ? 0.627 41.056 34.859 1.0 91.62 ? ? ? ? ? ? 376 ASN A CG 1 259 A A +ATOM 2065 O OD1 . ASN A 1 259 ? 1.728 41.601 34.775 1.0 86.47 ? ? ? ? ? ? 376 ASN A OD1 1 259 A A +ATOM 2066 N ND2 . ASN A 1 259 ? 0.237 40.096 34.026 1.0 95.27 ? ? ? ? ? ? 376 ASN A ND2 1 259 A A +ATOM 2067 N N . TYR A 1 260 ? 1.319 39.490 38.072 1.0 100.0 ? ? ? ? ? ? 377 TYR A N 1 260 A A +ATOM 2068 C CA . TYR A 1 260 ? 2.305 39.438 39.153 1.0 100.0 ? ? ? ? ? ? 377 TYR A CA 1 260 A A +ATOM 2069 C C . TYR A 1 260 ? 3.765 39.423 38.692 1.0 99.33 ? ? ? ? ? ? 377 TYR A C 1 260 A A +ATOM 2070 O O . TYR A 1 260 ? 4.067 39.138 37.530 1.0 100.0 ? ? ? ? ? ? 377 TYR A O 1 260 A A +ATOM 2071 C CB . TYR A 1 260 ? 2.046 38.210 40.034 1.0 97.62 ? ? ? ? ? ? 377 TYR A CB 1 260 A A +ATOM 2072 C CG . TYR A 1 260 ? 2.193 36.892 39.303 1.0 100.0 ? ? ? ? ? ? 377 TYR A CG 1 260 A A +ATOM 2073 C CD1 . TYR A 1 260 ? 3.419 36.225 39.266 1.0 100.0 ? ? ? ? ? ? 377 TYR A CD1 1 260 A A +ATOM 2074 C CD2 . TYR A 1 260 ? 1.112 36.319 38.635 1.0 97.98 ? ? ? ? ? ? 377 TYR A CD2 1 260 A A +ATOM 2075 C CE1 . TYR A 1 260 ? 3.564 35.017 38.584 1.0 98.13 ? ? ? ? ? ? 377 TYR A CE1 1 260 A A +ATOM 2076 C CE2 . TYR A 1 260 ? 1.246 35.111 37.950 1.0 100.0 ? ? ? ? ? ? 377 TYR A CE2 1 260 A A +ATOM 2077 C CZ . TYR A 1 260 ? 2.476 34.466 37.928 1.0 100.0 ? ? ? ? ? ? 377 TYR A CZ 1 260 A A +ATOM 2078 O OH . TYR A 1 260 ? 2.618 33.269 37.261 1.0 91.5 ? ? ? ? ? ? 377 TYR A OH 1 260 A A +ATOM 2079 N N . THR A 1 261 ? 4.664 39.729 39.626 1.0 91.74 ? ? ? ? ? ? 378 THR A N 1 261 A A +ATOM 2080 C CA . THR A 1 261 ? 6.099 39.746 39.355 1.0 95.1 ? ? ? ? ? ? 378 THR A CA 1 261 A A +ATOM 2081 C C . THR A 1 261 ? 6.667 38.373 39.682 1.0 95.66 ? ? ? ? ? ? 378 THR A C 1 261 A A +ATOM 2082 O O . THR A 1 261 ? 6.136 37.663 40.534 1.0 92.13 ? ? ? ? ? ? 378 THR A O 1 261 A A +ATOM 2083 C CB . THR A 1 261 ? 6.835 40.795 40.223 1.0 100.0 ? ? ? ? ? ? 378 THR A CB 1 261 A A +ATOM 2084 O OG1 . THR A 1 261 ? 8.240 40.750 39.940 1.0 99.09 ? ? ? ? ? ? 378 THR A OG1 1 261 A A +ATOM 2085 C CG2 . THR A 1 261 ? 6.618 40.511 41.707 1.0 98.52 ? ? ? ? ? ? 378 THR A CG2 1 261 A A +ATOM 2086 N N . VAL A 1 262 ? 7.755 38.008 39.018 1.0 100.0 ? ? ? ? ? ? 379 VAL A N 1 262 A A +ATOM 2087 C CA . VAL A 1 262 ? 8.371 36.709 39.240 1.0 99.46 ? ? ? ? ? ? 379 VAL A CA 1 262 A A +ATOM 2088 C C . VAL A 1 262 ? 9.538 36.742 40.228 1.0 100.0 ? ? ? ? ? ? 379 VAL A C 1 262 A A +ATOM 2089 O O . VAL A 1 262 ? 9.660 35.865 41.084 1.0 100.0 ? ? ? ? ? ? 379 VAL A O 1 262 A A +ATOM 2090 C CB . VAL A 1 262 ? 8.880 36.114 37.908 1.0 100.0 ? ? ? ? ? ? 379 VAL A CB 1 262 A A +ATOM 2091 C CG1 . VAL A 1 262 ? 9.858 37.081 37.242 1.0 96.93 ? ? ? ? ? ? 379 VAL A CG1 1 262 A A +ATOM 2092 C CG2 . VAL A 1 262 ? 9.545 34.767 38.162 1.0 87.09 ? ? ? ? ? ? 379 VAL A CG2 1 262 A A +ATOM 2093 N N . THR A 1 263 ? 10.384 37.761 40.112 1.0 100.0 ? ? ? ? ? ? 380 THR A N 1 263 A A +ATOM 2094 C CA . THR A 1 263 ? 11.563 37.881 40.964 1.0 99.35 ? ? ? ? ? ? 380 THR A CA 1 263 A A +ATOM 2095 C C . THR A 1 263 ? 11.352 38.445 42.364 1.0 97.45 ? ? ? ? ? ? 380 THR A C 1 263 A A +ATOM 2096 O O . THR A 1 263 ? 12.230 38.317 43.218 1.0 94.83 ? ? ? ? ? ? 380 THR A O 1 263 A A +ATOM 2097 C CB . THR A 1 263 ? 12.647 38.741 40.283 1.0 100.0 ? ? ? ? ? ? 380 THR A CB 1 263 A A +ATOM 2098 O OG1 . THR A 1 263 ? 12.115 40.040 39.992 1.0 100.0 ? ? ? ? ? ? 380 THR A OG1 1 263 A A +ATOM 2099 C CG2 . THR A 1 263 ? 13.119 38.083 38.995 1.0 100.0 ? ? ? ? ? ? 380 THR A CG2 1 263 A A +ATOM 2100 N N . GLU A 1 264 ? 10.205 39.063 42.614 1.0 96.16 ? ? ? ? ? ? 381 GLU A N 1 264 A A +ATOM 2101 C CA . GLU A 1 264 ? 9.985 39.638 43.930 1.0 94.77 ? ? ? ? ? ? 381 GLU A CA 1 264 A A +ATOM 2102 C C . GLU A 1 264 ? 8.657 39.327 44.608 1.0 100.0 ? ? ? ? ? ? 381 GLU A C 1 264 A A +ATOM 2103 O O . GLU A 1 264 ? 7.833 38.578 44.081 1.0 100.0 ? ? ? ? ? ? 381 GLU A O 1 264 A A +ATOM 2104 C CB . GLU A 1 264 ? 10.197 41.147 43.861 1.0 90.67 ? ? ? ? ? ? 381 GLU A CB 1 264 A A +ATOM 2105 C CG . GLU A 1 264 ? 11.655 41.536 43.704 1.0 96.58 ? ? ? ? ? ? 381 GLU A CG 1 264 A A +ATOM 2106 C CD . GLU A 1 264 ? 11.835 43.025 43.550 1.0 99.52 ? ? ? ? ? ? 381 GLU A CD 1 264 A A +ATOM 2107 O OE1 . GLU A 1 264 ? 12.707 43.439 42.757 1.0 100.0 ? ? ? ? ? ? 381 GLU A OE1 1 264 A A +ATOM 2108 O OE2 . GLU A 1 264 ? 11.102 43.781 44.223 1.0 100.0 ? ? ? ? ? ? 381 GLU A OE2 1 264 A A +ATOM 2109 N N . PHE A 1 265 ? 8.474 39.916 45.789 1.0 100.0 ? ? ? ? ? ? 382 PHE A N 1 265 A A +ATOM 2110 C CA . PHE A 1 265 ? 7.278 39.724 46.613 1.0 99.86 ? ? ? ? ? ? 382 PHE A CA 1 265 A A +ATOM 2111 C C . PHE A 1 265 ? 6.001 40.312 46.019 1.0 98.85 ? ? ? ? ? ? 382 PHE A C 1 265 A A +ATOM 2112 O O . PHE A 1 265 ? 6.020 41.376 45.397 1.0 93.87 ? ? ? ? ? ? 382 PHE A O 1 265 A A +ATOM 2113 C CB . PHE A 1 265 ? 7.497 40.325 48.007 1.0 85.54 ? ? ? ? ? ? 382 PHE A CB 1 265 A A +ATOM 2114 C CG . PHE A 1 265 ? 8.611 39.680 48.794 1.0 91.55 ? ? ? ? ? ? 382 PHE A CG 1 265 A A +ATOM 2115 C CD1 . PHE A 1 265 ? 9.519 38.817 48.186 1.0 88.06 ? ? ? ? ? ? 382 PHE A CD1 1 265 A A +ATOM 2116 C CD2 . PHE A 1 265 ? 8.760 39.951 50.149 1.0 96.89 ? ? ? ? ? ? 382 PHE A CD2 1 265 A A +ATOM 2117 C CE1 . PHE A 1 265 ? 10.557 38.239 48.916 1.0 88.79 ? ? ? ? ? ? 382 PHE A CE1 1 265 A A +ATOM 2118 C CE2 . PHE A 1 265 ? 9.794 39.378 50.888 1.0 93.24 ? ? ? ? ? ? 382 PHE A CE2 1 265 A A +ATOM 2119 C CZ . PHE A 1 265 ? 10.693 38.520 50.269 1.0 87.02 ? ? ? ? ? ? 382 PHE A CZ 1 265 A A +ATOM 2120 N N . GLN A 1 266 ? 4.890 39.615 46.239 1.0 100.0 ? ? ? ? ? ? 383 GLN A N 1 266 A A +ATOM 2121 C CA . GLN A 1 266 ? 3.590 40.043 45.733 1.0 100.0 ? ? ? ? ? ? 383 GLN A CA 1 266 A A +ATOM 2122 C C . GLN A 1 266 ? 2.759 40.725 46.820 1.0 99.33 ? ? ? ? ? ? 383 GLN A C 1 266 A A +ATOM 2123 O O . GLN A 1 266 ? 2.519 40.152 47.881 1.0 97.3 ? ? ? ? ? ? 383 GLN A O 1 266 A A +ATOM 2124 C CB . GLN A 1 266 ? 2.817 38.837 45.181 1.0 97.24 ? ? ? ? ? ? 383 GLN A CB 1 266 A A +ATOM 2125 C CG . GLN A 1 266 ? 3.445 38.202 43.951 1.0 93.63 ? ? ? ? ? ? 383 GLN A CG 1 266 A A +ATOM 2126 C CD . GLN A 1 266 ? 4.613 37.301 44.296 1.0 100.0 ? ? ? ? ? ? 383 GLN A CD 1 266 A A +ATOM 2127 O OE1 . GLN A 1 266 ? 5.564 37.175 43.526 1.0 100.0 ? ? ? ? ? ? 383 GLN A OE1 1 266 A A +ATOM 2128 N NE2 . GLN A 1 266 ? 4.547 36.670 45.463 1.0 80.97 ? ? ? ? ? ? 383 GLN A NE2 1 266 A A +ATOM 2129 N N . PRO A 1 267 ? 2.295 41.961 46.559 1.0 100.0 ? ? ? ? ? ? 384 PRO A N 1 267 A A +ATOM 2130 C CA . PRO A 1 267 ? 1.489 42.681 47.552 1.0 100.0 ? ? ? ? ? ? 384 PRO A CA 1 267 A A +ATOM 2131 C C . PRO A 1 267 ? 0.134 42.009 47.723 1.0 100.0 ? ? ? ? ? ? 384 PRO A C 1 267 A A +ATOM 2132 O O . PRO A 1 267 ? -0.535 42.178 48.744 1.0 100.0 ? ? ? ? ? ? 384 PRO A O 1 267 A A +ATOM 2133 C CB . PRO A 1 267 ? 1.363 44.087 46.968 1.0 100.0 ? ? ? ? ? ? 384 PRO A CB 1 267 A A +ATOM 2134 C CG . PRO A 1 267 ? 1.532 43.894 45.499 1.0 100.0 ? ? ? ? ? ? 384 PRO A CG 1 267 A A +ATOM 2135 C CD . PRO A 1 267 ? 2.470 42.735 45.319 1.0 100.0 ? ? ? ? ? ? 384 PRO A CD 1 267 A A +ATOM 2136 N N . LEU A 1 268 ? -0.249 41.234 46.714 1.0 98.23 ? ? ? ? ? ? 385 LEU A N 1 268 A A +ATOM 2137 C CA . LEU A 1 268 ? -1.518 40.522 46.721 1.0 96.1 ? ? ? ? ? ? 385 LEU A CA 1 268 A A +ATOM 2138 C C . LEU A 1 268 ? -1.350 39.044 47.067 1.0 100.0 ? ? ? ? ? ? 385 LEU A C 1 268 A A +ATOM 2139 O O . LEU A 1 268 ? -0.504 38.351 46.496 1.0 100.0 ? ? ? ? ? ? 385 LEU A O 1 268 A A +ATOM 2140 C CB . LEU A 1 268 ? -2.196 40.645 45.352 1.0 91.24 ? ? ? ? ? ? 385 LEU A CB 1 268 A A +ATOM 2141 C CG . LEU A 1 268 ? -2.987 41.919 45.037 1.0 94.27 ? ? ? ? ? ? 385 LEU A CG 1 268 A A +ATOM 2142 C CD1 . LEU A 1 268 ? -4.006 41.593 43.961 1.0 78.81 ? ? ? ? ? ? 385 LEU A CD1 1 268 A A +ATOM 2143 C CD2 . LEU A 1 268 ? -3.691 42.452 46.281 1.0 100.0 ? ? ? ? ? ? 385 LEU A CD2 1 268 A A +ATOM 2144 N N . TYR A 1 269 ? -2.159 38.581 48.018 1.0 98.42 ? ? ? ? ? ? 386 TYR A N 1 269 A A +ATOM 2145 C CA . TYR A 1 269 ? -2.167 37.189 48.467 1.0 90.07 ? ? ? ? ? ? 386 TYR A CA 1 269 A A +ATOM 2146 C C . TYR A 1 269 ? -3.635 36.846 48.721 1.0 89.16 ? ? ? ? ? ? 386 TYR A C 1 269 A A +ATOM 2147 O O . TYR A 1 269 ? -4.188 37.209 49.759 1.0 100.0 ? ? ? ? ? ? 386 TYR A O 1 269 A A +ATOM 2148 C CB . TYR A 1 269 ? -1.385 37.021 49.777 1.0 82.19 ? ? ? ? ? ? 386 TYR A CB 1 269 A A +ATOM 2149 C CG . TYR A 1 269 ? 0.119 37.190 49.666 1.0 90.41 ? ? ? ? ? ? 386 TYR A CG 1 269 A A +ATOM 2150 C CD1 . TYR A 1 269 ? 0.784 38.140 50.440 1.0 97.78 ? ? ? ? ? ? 386 TYR A CD1 1 269 A A +ATOM 2151 C CD2 . TYR A 1 269 ? 0.882 36.377 48.822 1.0 93.82 ? ? ? ? ? ? 386 TYR A CD2 1 269 A A +ATOM 2152 C CE1 . TYR A 1 269 ? 2.169 38.280 50.383 1.0 100.0 ? ? ? ? ? ? 386 TYR A CE1 1 269 A A +ATOM 2153 C CE2 . TYR A 1 269 ? 2.273 36.509 48.757 1.0 96.67 ? ? ? ? ? ? 386 TYR A CE2 1 269 A A +ATOM 2154 C CZ . TYR A 1 269 ? 2.908 37.461 49.542 1.0 100.0 ? ? ? ? ? ? 386 TYR A CZ 1 269 A A +ATOM 2155 O OH . TYR A 1 269 ? 4.278 37.587 49.492 1.0 100.0 ? ? ? ? ? ? 386 TYR A OH 1 269 A A +ATOM 2156 N N . TYR A 1 270 ? -4.263 36.157 47.774 1.0 85.74 ? ? ? ? ? ? 387 TYR A N 1 270 A A +ATOM 2157 C CA . TYR A 1 270 ? -5.672 35.793 47.905 1.0 92.52 ? ? ? ? ? ? 387 TYR A CA 1 270 A A +ATOM 2158 C C . TYR A 1 270 ? -5.930 34.798 49.030 1.0 100.0 ? ? ? ? ? ? 387 TYR A C 1 270 A A +ATOM 2159 O O . TYR A 1 270 ? -5.386 33.693 49.037 1.0 100.0 ? ? ? ? ? ? 387 TYR A O 1 270 A A +ATOM 2160 C CB . TYR A 1 270 ? -6.197 35.234 46.579 1.0 87.5 ? ? ? ? ? ? 387 TYR A CB 1 270 A A +ATOM 2161 C CG . TYR A 1 270 ? -6.211 36.267 45.483 1.0 78.83 ? ? ? ? ? ? 387 TYR A CG 1 270 A A +ATOM 2162 C CD1 . TYR A 1 270 ? -5.030 36.658 44.860 1.0 77.83 ? ? ? ? ? ? 387 TYR A CD1 1 270 A A +ATOM 2163 C CD2 . TYR A 1 270 ? -7.396 36.895 45.102 1.0 80.82 ? ? ? ? ? ? 387 TYR A CD2 1 270 A A +ATOM 2164 C CE1 . TYR A 1 270 ? -5.024 37.651 43.884 1.0 96.01 ? ? ? ? ? ? 387 TYR A CE1 1 270 A A +ATOM 2165 C CE2 . TYR A 1 270 ? -7.403 37.892 44.126 1.0 89.89 ? ? ? ? ? ? 387 TYR A CE2 1 270 A A +ATOM 2166 C CZ . TYR A 1 270 ? -6.211 38.267 43.522 1.0 95.76 ? ? ? ? ? ? 387 TYR A CZ 1 270 A A +ATOM 2167 O OH . TYR A 1 270 ? -6.196 39.257 42.561 1.0 80.81 ? ? ? ? ? ? 387 TYR A OH 1 270 A A +ATOM 2168 N N . VAL A 1 271 ? -6.777 35.203 49.974 1.0 100.0 ? ? ? ? ? ? 388 VAL A N 1 271 A A +ATOM 2169 C CA . VAL A 1 271 ? -7.118 34.378 51.129 1.0 97.26 ? ? ? ? ? ? 388 VAL A CA 1 271 A A +ATOM 2170 C C . VAL A 1 271 ? -8.277 33.417 50.874 1.0 96.92 ? ? ? ? ? ? 388 VAL A C 1 271 A A +ATOM 2171 O O . VAL A 1 271 ? -9.432 33.834 50.779 1.0 100.0 ? ? ? ? ? ? 388 VAL A O 1 271 A A +ATOM 2172 C CB . VAL A 1 271 ? -7.479 35.264 52.342 1.0 97.4 ? ? ? ? ? ? 388 VAL A CB 1 271 A A +ATOM 2173 C CG1 . VAL A 1 271 ? -7.740 34.397 53.566 1.0 98.41 ? ? ? ? ? ? 388 VAL A CG1 1 271 A A +ATOM 2174 C CG2 . VAL A 1 271 ? -6.357 36.254 52.609 1.0 100.0 ? ? ? ? ? ? 388 VAL A CG2 1 271 A A +ATOM 2175 N N . ALA A 1 272 ? -7.960 32.128 50.769 1.0 92.96 ? ? ? ? ? ? 389 ALA A N 1 272 A A +ATOM 2176 C CA . ALA A 1 272 ? -8.971 31.103 50.539 1.0 87.23 ? ? ? ? ? ? 389 ALA A CA 1 272 A A +ATOM 2177 C C . ALA A 1 272 ? -9.519 30.605 51.870 1.0 88.83 ? ? ? ? ? ? 389 ALA A C 1 272 A A +ATOM 2178 O O . ALA A 1 272 ? -8.779 30.460 52.846 1.0 84.56 ? ? ? ? ? ? 389 ALA A O 1 272 A A +ATOM 2179 C CB . ALA A 1 272 ? -8.375 29.941 49.762 1.0 83.42 ? ? ? ? ? ? 389 ALA A CB 1 272 A A +ATOM 2180 N N . GLU A 1 273 ? -10.823 30.354 51.908 1.0 91.8 ? ? ? ? ? ? 390 GLU A N 1 273 A A +ATOM 2181 C CA . GLU A 1 273 ? -11.456 29.860 53.122 1.0 91.37 ? ? ? ? ? ? 390 GLU A CA 1 273 A A +ATOM 2182 C C . GLU A 1 273 ? -10.844 28.507 53.454 1.0 88.96 ? ? ? ? ? ? 390 GLU A C 1 273 A A +ATOM 2183 O O . GLU A 1 273 ? -10.351 28.288 54.562 1.0 97.4 ? ? ? ? ? ? 390 GLU A O 1 273 A A +ATOM 2184 C CB . GLU A 1 273 ? -12.960 29.711 52.911 1.0 94.09 ? ? ? ? ? ? 390 GLU A CB 1 273 A A +ATOM 2185 C CG . GLU A 1 273 ? -13.667 31.019 52.625 1.0 100.0 ? ? ? ? ? ? 390 GLU A CG 1 273 A A +ATOM 2186 C CD . GLU A 1 273 ? -15.175 30.861 52.548 1.0 100.0 ? ? ? ? ? ? 390 GLU A CD 1 273 A A +ATOM 2187 O OE1 . GLU A 1 273 ? -15.661 29.712 52.665 1.0 100.0 ? ? ? ? ? ? 390 GLU A OE1 1 273 A A +ATOM 2188 O OE2 . GLU A 1 273 ? -15.872 31.887 52.373 1.0 100.0 ? ? ? ? ? ? 390 GLU A OE2 1 273 A A +ATOM 2189 N N . SER A 1 274 ? -10.879 27.606 52.477 1.0 77.84 ? ? ? ? ? ? 391 SER A N 1 274 A A +ATOM 2190 C CA . SER A 1 274 ? -10.326 26.269 52.633 1.0 69.81 ? ? ? ? ? ? 391 SER A CA 1 274 A A +ATOM 2191 C C . SER A 1 274 ? -10.011 25.686 51.263 1.0 65.41 ? ? ? ? ? ? 391 SER A C 1 274 A A +ATOM 2192 O O . SER A 1 274 ? -10.419 26.232 50.238 1.0 67.04 ? ? ? ? ? ? 391 SER A O 1 274 A A +ATOM 2193 C CB . SER A 1 274 ? -11.321 25.362 53.364 1.0 68.26 ? ? ? ? ? ? 391 SER A CB 1 274 A A +ATOM 2194 O OG . SER A 1 274 ? -10.719 24.131 53.733 1.0 78.68 ? ? ? ? ? ? 391 SER A OG 1 274 A A +ATOM 2195 N N . PHE A 1 275 ? -9.272 24.582 51.252 1.0 64.72 ? ? ? ? ? ? 392 PHE A N 1 275 A A +ATOM 2196 C CA . PHE A 1 275 ? -8.913 23.920 50.004 1.0 63.71 ? ? ? ? ? ? 392 PHE A CA 1 275 A A +ATOM 2197 C C . PHE A 1 275 ? -10.162 23.244 49.463 1.0 65.72 ? ? ? ? ? ? 392 PHE A C 1 275 A A +ATOM 2198 O O . PHE A 1 275 ? -10.360 23.148 48.253 1.0 57.64 ? ? ? ? ? ? 392 PHE A O 1 275 A A +ATOM 2199 C CB . PHE A 1 275 ? -7.808 22.894 50.258 1.0 63.72 ? ? ? ? ? ? 392 PHE A CB 1 275 A A +ATOM 2200 C CG . PHE A 1 275 ? -6.774 23.358 51.241 1.0 79.95 ? ? ? ? ? ? 392 PHE A CG 1 275 A A +ATOM 2201 C CD1 . PHE A 1 275 ? -6.639 22.734 52.477 1.0 96.25 ? ? ? ? ? ? 392 PHE A CD1 1 275 A A +ATOM 2202 C CD2 . PHE A 1 275 ? -5.943 24.433 50.939 1.0 77.52 ? ? ? ? ? ? 392 PHE A CD2 1 275 A A +ATOM 2203 C CE1 . PHE A 1 275 ? -5.690 23.173 53.399 1.0 100.0 ? ? ? ? ? ? 392 PHE A CE1 1 275 A A +ATOM 2204 C CE2 . PHE A 1 275 ? -4.990 24.881 51.851 1.0 83.36 ? ? ? ? ? ? 392 PHE A CE2 1 275 A A +ATOM 2205 C CZ . PHE A 1 275 ? -4.864 24.250 53.085 1.0 99.74 ? ? ? ? ? ? 392 PHE A CZ 1 275 A A +ATOM 2206 N N . ASN A 1 276 ? -11.005 22.785 50.381 1.0 69.65 ? ? ? ? ? ? 393 ASN A N 1 276 A A +ATOM 2207 C CA . ASN A 1 276 ? -12.257 22.134 50.030 1.0 67.8 ? ? ? ? ? ? 393 ASN A CA 1 276 A A +ATOM 2208 C C . ASN A 1 276 ? -13.155 23.171 49.367 1.0 64.99 ? ? ? ? ? ? 393 ASN A C 1 276 A A +ATOM 2209 O O . ASN A 1 276 ? -13.945 22.858 48.479 1.0 61.92 ? ? ? ? ? ? 393 ASN A O 1 276 A A +ATOM 2210 C CB . ASN A 1 276 ? -12.935 21.598 51.293 1.0 55.58 ? ? ? ? ? ? 393 ASN A CB 1 276 A A +ATOM 2211 C CG . ASN A 1 276 ? -13.984 20.555 50.991 1.0 63.01 ? ? ? ? ? ? 393 ASN A CG 1 276 A A +ATOM 2212 O OD1 . ASN A 1 276 ? -14.791 20.715 50.076 1.0 73.68 ? ? ? ? ? ? 393 ASN A OD1 1 276 A A +ATOM 2213 N ND2 . ASN A 1 276 ? -13.980 19.474 51.762 1.0 72.87 ? ? ? ? ? ? 393 ASN A ND2 1 276 A A +ATOM 2214 N N . ASP A 1 277 ? -13.021 24.416 49.803 1.0 60.25 ? ? ? ? ? ? 394 ASP A N 1 277 A A +ATOM 2215 C CA . ASP A 1 277 ? -13.824 25.499 49.263 1.0 65.04 ? ? ? ? ? ? 394 ASP A CA 1 277 A A +ATOM 2216 C C . ASP A 1 277 ? -13.403 25.869 47.849 1.0 69.42 ? ? ? ? ? ? 394 ASP A C 1 277 A A +ATOM 2217 O O . ASP A 1 277 ? -14.237 26.003 46.953 1.0 72.92 ? ? ? ? ? ? 394 ASP A O 1 277 A A +ATOM 2218 C CB . ASP A 1 277 ? -13.708 26.728 50.163 1.0 79.78 ? ? ? ? ? ? 394 ASP A CB 1 277 A A +ATOM 2219 C CG . ASP A 1 277 ? -14.821 27.721 49.934 1.0 91.97 ? ? ? ? ? ? 394 ASP A CG 1 277 A A +ATOM 2220 O OD1 . ASP A 1 277 ? -16.001 27.312 49.983 1.0 91.8 ? ? ? ? ? ? 394 ASP A OD1 1 277 A A +ATOM 2221 O OD2 . ASP A 1 277 ? -14.516 28.910 49.703 1.0 92.7 ? ? ? ? ? ? 394 ASP A OD2 1 277 A A +ATOM 2222 N N . ALA A 1 278 ? -12.100 26.037 47.661 1.0 75.65 ? ? ? ? ? ? 395 ALA A N 1 278 A A +ATOM 2223 C CA . ALA A 1 278 ? -11.549 26.414 46.365 1.0 62.68 ? ? ? ? ? ? 395 ALA A CA 1 278 A A +ATOM 2224 C C . ALA A 1 278 ? -11.776 25.367 45.280 1.0 65.12 ? ? ? ? ? ? 395 ALA A C 1 278 A A +ATOM 2225 O O . ALA A 1 278 ? -12.087 25.710 44.140 1.0 66.49 ? ? ? ? ? ? 395 ALA A O 1 278 A A +ATOM 2226 C CB . ALA A 1 278 ? -10.066 26.706 46.506 1.0 43.25 ? ? ? ? ? ? 395 ALA A CB 1 278 A A +ATOM 2227 N N . LYS A 1 279 ? -11.610 24.095 45.635 1.0 59.26 ? ? ? ? ? ? 396 LYS A N 1 279 A A +ATOM 2228 C CA . LYS A 1 279 ? -11.799 22.999 44.685 1.0 46.21 ? ? ? ? ? ? 396 LYS A CA 1 279 A A +ATOM 2229 C C . LYS A 1 279 ? -13.055 23.193 43.846 1.0 40.74 ? ? ? ? ? ? 396 LYS A C 1 279 A A +ATOM 2230 O O . LYS A 1 279 ? -13.068 22.873 42.658 1.0 28.37 ? ? ? ? ? ? 396 LYS A O 1 279 A A +ATOM 2231 C CB . LYS A 1 279 ? -11.893 21.661 45.422 1.0 51.44 ? ? ? ? ? ? 396 LYS A CB 1 279 A A +ATOM 2232 C CG . LYS A 1 279 ? -12.490 20.542 44.588 1.0 22.9 ? ? ? ? ? ? 396 LYS A CG 1 279 A A +ATOM 2233 C CD . LYS A 1 279 ? -12.410 19.224 45.323 1.0 31.36 ? ? ? ? ? ? 396 LYS A CD 1 279 A A +ATOM 2234 C CE . LYS A 1 279 ? -13.665 18.974 46.124 1.0 41.1 ? ? ? ? ? ? 396 LYS A CE 1 279 A A +ATOM 2235 N NZ . LYS A 1 279 ? -13.770 17.556 46.564 1.0 37.34 ? ? ? ? ? ? 396 LYS A NZ 1 279 A A +ATOM 2236 N N . GLU A 1 280 ? -14.110 23.701 44.478 1.0 41.13 ? ? ? ? ? ? 397 GLU A N 1 280 A A +ATOM 2237 C CA . GLU A 1 280 ? -15.373 23.948 43.793 1.0 49.25 ? ? ? ? ? ? 397 GLU A CA 1 280 A A +ATOM 2238 C C . GLU A 1 280 ? -15.213 25.125 42.837 1.0 51.92 ? ? ? ? ? ? 397 GLU A C 1 280 A A +ATOM 2239 O O . GLU A 1 280 ? -15.681 25.080 41.698 1.0 60.13 ? ? ? ? ? ? 397 GLU A O 1 280 A A +ATOM 2240 C CB . GLU A 1 280 ? -16.476 24.260 44.805 1.0 60.2 ? ? ? ? ? ? 397 GLU A CB 1 280 A A +ATOM 2241 C CG . GLU A 1 280 ? -16.578 23.247 45.922 1.0 82.81 ? ? ? ? ? ? 397 GLU A CG 1 280 A A +ATOM 2242 C CD . GLU A 1 280 ? -16.989 21.882 45.422 1.0 100.0 ? ? ? ? ? ? 397 GLU A CD 1 280 A A +ATOM 2243 O OE1 . GLU A 1 280 ? -17.773 21.815 44.450 1.0 100.0 ? ? ? ? ? ? 397 GLU A OE1 1 280 A A +ATOM 2244 O OE2 . GLU A 1 280 ? -16.531 20.876 46.002 1.0 100.0 ? ? ? ? ? ? 397 GLU A OE2 1 280 A A +ATOM 2245 N N . LYS A 1 281 ? -14.549 26.177 43.310 1.0 47.17 ? ? ? ? ? ? 398 LYS A N 1 281 A A +ATOM 2246 C CA . LYS A 1 281 ? -14.321 27.365 42.502 1.0 52.5 ? ? ? ? ? ? 398 LYS A CA 1 281 A A +ATOM 2247 C C . LYS A 1 281 ? -13.622 26.969 41.205 1.0 49.29 ? ? ? ? ? ? 398 LYS A C 1 281 A A +ATOM 2248 O O . LYS A 1 281 ? -13.665 27.697 40.214 1.0 56.88 ? ? ? ? ? ? 398 LYS A O 1 281 A A +ATOM 2249 C CB . LYS A 1 281 ? -13.466 28.362 43.278 1.0 67.3 ? ? ? ? ? ? 398 LYS A CB 1 281 A A +ATOM 2250 C CG . LYS A 1 281 ? -13.822 28.453 44.751 1.0 65.58 ? ? ? ? ? ? 398 LYS A CG 1 281 A A +ATOM 2251 C CD . LYS A 1 281 ? -14.985 29.403 44.983 1.0 76.37 ? ? ? ? ? ? 398 LYS A CD 1 281 A A +ATOM 2252 C CE . LYS A 1 281 ? -15.053 29.844 46.439 1.0 68.23 ? ? ? ? ? ? 398 LYS A CE 1 281 A A +ATOM 2253 N NZ . LYS A 1 281 ? -13.928 30.755 46.787 1.0 72.84 ? ? ? ? ? ? 398 LYS A NZ 1 281 A A +ATOM 2254 N N . VAL A 1 282 ? -12.988 25.801 41.223 1.0 44.34 ? ? ? ? ? ? 399 VAL A N 1 282 A A +ATOM 2255 C CA . VAL A 1 282 ? -12.273 25.284 40.062 1.0 47.58 ? ? ? ? ? ? 399 VAL A CA 1 282 A A +ATOM 2256 C C . VAL A 1 282 ? -13.160 24.352 39.236 1.0 47.85 ? ? ? ? ? ? 399 VAL A C 1 282 A A +ATOM 2257 O O . VAL A 1 282 ? -13.116 24.364 38.004 1.0 49.4 ? ? ? ? ? ? 399 VAL A O 1 282 A A +ATOM 2258 C CB . VAL A 1 282 ? -11.001 24.521 40.498 1.0 41.31 ? ? ? ? ? ? 399 VAL A CB 1 282 A A +ATOM 2259 C CG1 . VAL A 1 282 ? -9.908 24.694 39.458 1.0 42.53 ? ? ? ? ? ? 399 VAL A CG1 1 282 A A +ATOM 2260 C CG2 . VAL A 1 282 ? -10.524 25.024 41.852 1.0 35.0 ? ? ? ? ? ? 399 VAL A CG2 1 282 A A +ATOM 2261 N N . ARG A 1 283 ? -13.972 23.554 39.923 1.0 45.56 ? ? ? ? ? ? 400 ARG A N 1 283 A A +ATOM 2262 C CA . ARG A 1 283 ? -14.876 22.624 39.258 1.0 52.75 ? ? ? ? ? ? 400 ARG A CA 1 283 A A +ATOM 2263 C C . ARG A 1 283 ? -15.722 23.354 38.222 1.0 58.51 ? ? ? ? ? ? 400 ARG A C 1 283 A A +ATOM 2264 O O . ARG A 1 283 ? -15.717 23.009 37.042 1.0 63.72 ? ? ? ? ? ? 400 ARG A O 1 283 A A +ATOM 2265 C CB . ARG A 1 283 ? -15.790 21.953 40.284 1.0 55.93 ? ? ? ? ? ? 400 ARG A CB 1 283 A A +ATOM 2266 C CG . ARG A 1 283 ? -15.236 20.667 40.843 1.0 54.36 ? ? ? ? ? ? 400 ARG A CG 1 283 A A +ATOM 2267 C CD . ARG A 1 283 ? -16.347 19.692 41.166 1.0 58.44 ? ? ? ? ? ? 400 ARG A CD 1 283 A A +ATOM 2268 N NE . ARG A 1 283 ? -15.819 18.457 41.736 1.0 77.88 ? ? ? ? ? ? 400 ARG A NE 1 283 A A +ATOM 2269 C CZ . ARG A 1 283 ? -15.908 17.262 41.159 1.0 86.01 ? ? ? ? ? ? 400 ARG A CZ 1 283 A A +ATOM 2270 N NH1 . ARG A 1 283 ? -16.513 17.127 39.985 1.0 78.05 ? ? ? ? ? ? 400 ARG A NH1 1 283 A A +ATOM 2271 N NH2 . ARG A 1 283 ? -15.389 16.198 41.759 1.0 99.95 ? ? ? ? ? ? 400 ARG A NH2 1 283 A A +ATOM 2272 N N . ASN A 1 284 ? -16.442 24.371 38.682 1.0 75.85 ? ? ? ? ? ? 401 ASN A N 1 284 A A +ATOM 2273 C CA . ASN A 1 284 ? -17.305 25.174 37.823 1.0 77.91 ? ? ? ? ? ? 401 ASN A CA 1 284 A A +ATOM 2274 C C . ASN A 1 284 ? -16.503 25.977 36.805 1.0 68.26 ? ? ? ? ? ? 401 ASN A C 1 284 A A +ATOM 2275 O O . ASN A 1 284 ? -16.860 26.031 35.627 1.0 72.47 ? ? ? ? ? ? 401 ASN A O 1 284 A A +ATOM 2276 C CB . ASN A 1 284 ? -18.137 26.123 38.679 1.0 87.48 ? ? ? ? ? ? 401 ASN A CB 1 284 A A +ATOM 2277 C CG . ASN A 1 284 ? -17.454 26.473 39.983 1.0 93.59 ? ? ? ? ? ? 401 ASN A CG 1 284 A A +ATOM 2278 O OD1 . ASN A 1 284 ? -17.926 26.106 41.062 1.0 92.46 ? ? ? ? ? ? 401 ASN A OD1 1 284 A A +ATOM 2279 N ND2 . ASN A 1 284 ? -16.330 27.181 39.893 1.0 99.85 ? ? ? ? ? ? 401 ASN A ND2 1 284 A A +ATOM 2280 N N . PHE A 1 285 ? -15.428 26.614 37.263 1.0 43.4 ? ? ? ? ? ? 402 PHE A N 1 285 A A +ATOM 2281 C CA . PHE A 1 285 ? -14.575 27.404 36.379 1.0 48.71 ? ? ? ? ? ? 402 PHE A CA 1 285 A A +ATOM 2282 C C . PHE A 1 285 ? -14.218 26.563 35.160 1.0 54.14 ? ? ? ? ? ? 402 PHE A C 1 285 A A +ATOM 2283 O O . PHE A 1 285 ? -13.987 27.089 34.072 1.0 52.45 ? ? ? ? ? ? 402 PHE A O 1 285 A A +ATOM 2284 C CB . PHE A 1 285 ? -13.292 27.831 37.109 1.0 45.77 ? ? ? ? ? ? 402 PHE A CB 1 285 A A +ATOM 2285 C CG . PHE A 1 285 ? -12.417 28.783 36.322 1.0 59.63 ? ? ? ? ? ? 402 PHE A CG 1 285 A A +ATOM 2286 C CD1 . PHE A 1 285 ? -11.166 29.153 36.809 1.0 62.54 ? ? ? ? ? ? 402 PHE A CD1 1 285 A A +ATOM 2287 C CD2 . PHE A 1 285 ? -12.840 29.314 35.107 1.0 48.87 ? ? ? ? ? ? 402 PHE A CD2 1 285 A A +ATOM 2288 C CE1 . PHE A 1 285 ? -10.351 30.033 36.091 1.0 49.67 ? ? ? ? ? ? 402 PHE A CE1 1 285 A A +ATOM 2289 C CE2 . PHE A 1 285 ? -12.033 30.191 34.387 1.0 49.79 ? ? ? ? ? ? 402 PHE A CE2 1 285 A A +ATOM 2290 C CZ . PHE A 1 285 ? -10.788 30.551 34.882 1.0 33.15 ? ? ? ? ? ? 402 PHE A CZ 1 285 A A +ATOM 2291 N N . ALA A 1 286 ? -14.178 25.249 35.349 1.0 68.74 ? ? ? ? ? ? 403 ALA A N 1 286 A A +ATOM 2292 C CA . ALA A 1 286 ? -13.858 24.345 34.256 1.0 84.45 ? ? ? ? ? ? 403 ALA A CA 1 286 A A +ATOM 2293 C C . ALA A 1 286 ? -15.011 24.325 33.254 1.0 85.9 ? ? ? ? ? ? 403 ALA A C 1 286 A A +ATOM 2294 O O . ALA A 1 286 ? -14.795 24.270 32.040 1.0 82.18 ? ? ? ? ? ? 403 ALA A O 1 286 A A +ATOM 2295 C CB . ALA A 1 286 ? -13.596 22.944 34.800 1.0 89.73 ? ? ? ? ? ? 403 ALA A CB 1 286 A A +ATOM 2296 N N . ALA A 1 287 ? -16.236 24.371 33.769 1.0 77.85 ? ? ? ? ? ? 404 ALA A N 1 287 A A +ATOM 2297 C CA . ALA A 1 287 ? -17.422 24.368 32.920 1.0 64.27 ? ? ? ? ? ? 404 ALA A CA 1 287 A A +ATOM 2298 C C . ALA A 1 287 ? -17.478 25.673 32.148 1.0 64.71 ? ? ? ? ? ? 404 ALA A C 1 287 A A +ATOM 2299 O O . ALA A 1 287 ? -17.991 25.731 31.033 1.0 57.92 ? ? ? ? ? ? 404 ALA A O 1 287 A A +ATOM 2300 C CB . ALA A 1 287 ? -18.670 24.215 33.767 1.0 39.11 ? ? ? ? ? ? 404 ALA A CB 1 287 A A +ATOM 2301 N N . THR A 1 288 ? -16.937 26.720 32.759 1.0 63.15 ? ? ? ? ? ? 405 THR A N 1 288 A A +ATOM 2302 C CA . THR A 1 288 ? -16.908 28.039 32.146 1.0 66.29 ? ? ? ? ? ? 405 THR A CA 1 288 A A +ATOM 2303 C C . THR A 1 288 ? -15.749 28.141 31.149 1.0 74.21 ? ? ? ? ? ? 405 THR A C 1 288 A A +ATOM 2304 O O . THR A 1 288 ? -15.511 29.198 30.553 1.0 77.41 ? ? ? ? ? ? 405 THR A O 1 288 A A +ATOM 2305 C CB . THR A 1 288 ? -16.755 29.127 33.218 1.0 66.02 ? ? ? ? ? ? 405 THR A CB 1 288 A A +ATOM 2306 O OG1 . THR A 1 288 ? -15.429 29.081 33.757 1.0 68.61 ? ? ? ? ? ? 405 THR A OG1 1 288 A A +ATOM 2307 C CG2 . THR A 1 288 ? -17.756 28.903 34.346 1.0 50.34 ? ? ? ? ? ? 405 THR A CG2 1 288 A A +ATOM 2308 N N . ILE A 1 289 ? -15.034 27.034 30.969 1.0 69.12 ? ? ? ? ? ? 406 ILE A N 1 289 A A +ATOM 2309 C CA . ILE A 1 289 ? -13.906 26.995 30.042 1.0 63.63 ? ? ? ? ? ? 406 ILE A CA 1 289 A A +ATOM 2310 C C . ILE A 1 289 ? -14.344 26.465 28.683 1.0 58.59 ? ? ? ? ? ? 406 ILE A C 1 289 A A +ATOM 2311 O O . ILE A 1 289 ? -14.956 25.401 28.589 1.0 54.64 ? ? ? ? ? ? 406 ILE A O 1 289 A A +ATOM 2312 C CB . ILE A 1 289 ? -12.766 26.076 30.551 1.0 65.45 ? ? ? ? ? ? 406 ILE A CB 1 289 A A +ATOM 2313 C CG1 . ILE A 1 289 ? -12.211 26.599 31.875 1.0 56.74 ? ? ? ? ? ? 406 ILE A CG1 1 289 A A +ATOM 2314 C CG2 . ILE A 1 289 ? -11.643 26.021 29.520 1.0 52.19 ? ? ? ? ? ? 406 ILE A CG2 1 289 A A +ATOM 2315 C CD1 . ILE A 1 289 ? -11.240 25.644 32.539 1.0 41.69 ? ? ? ? ? ? 406 ILE A CD1 1 289 A A +ATOM 2316 N N . PRO A 1 290 ? -14.029 27.203 27.609 1.0 58.31 ? ? ? ? ? ? 407 PRO A N 1 290 A A +ATOM 2317 C CA . PRO A 1 290 ? -14.389 26.804 26.245 1.0 58.51 ? ? ? ? ? ? 407 PRO A CA 1 290 A A +ATOM 2318 C C . PRO A 1 290 ? -13.641 25.549 25.795 1.0 59.72 ? ? ? ? ? ? 407 PRO A C 1 290 A A +ATOM 2319 O O . PRO A 1 290 ? -12.476 25.608 25.403 1.0 56.66 ? ? ? ? ? ? 407 PRO A O 1 290 A A +ATOM 2320 C CB . PRO A 1 290 ? -14.029 28.028 25.404 1.0 64.77 ? ? ? ? ? ? 407 PRO A CB 1 290 A A +ATOM 2321 C CG . PRO A 1 290 ? -12.993 28.736 26.191 1.0 71.72 ? ? ? ? ? ? 407 PRO A CG 1 290 A A +ATOM 2322 C CD . PRO A 1 290 ? -13.300 28.480 27.635 1.0 63.55 ? ? ? ? ? ? 407 PRO A CD 1 290 A A +ATOM 2323 N N . ARG A 1 291 ? -14.327 24.414 25.861 1.0 57.5 ? ? ? ? ? ? 408 ARG A N 1 291 A A +ATOM 2324 C CA . ARG A 1 291 ? -13.743 23.135 25.467 1.0 54.43 ? ? ? ? ? ? 408 ARG A CA 1 291 A A +ATOM 2325 C C . ARG A 1 291 ? -14.775 22.305 24.715 1.0 45.32 ? ? ? ? ? ? 408 ARG A C 1 291 A A +ATOM 2326 O O . ARG A 1 291 ? -15.815 21.948 25.264 1.0 44.45 ? ? ? ? ? ? 408 ARG A O 1 291 A A +ATOM 2327 C CB . ARG A 1 291 ? -13.274 22.362 26.708 1.0 65.13 ? ? ? ? ? ? 408 ARG A CB 1 291 A A +ATOM 2328 C CG . ARG A 1 291 ? -11.834 22.652 27.135 1.0 50.86 ? ? ? ? ? ? 408 ARG A CG 1 291 A A +ATOM 2329 C CD . ARG A 1 291 ? -11.298 21.600 28.119 1.0 59.04 ? ? ? ? ? ? 408 ARG A CD 1 291 A A +ATOM 2330 N NE . ARG A 1 291 ? -11.957 21.657 29.427 1.0 65.61 ? ? ? ? ? ? 408 ARG A NE 1 291 A A +ATOM 2331 C CZ . ARG A 1 291 ? -11.688 20.845 30.450 1.0 41.74 ? ? ? ? ? ? 408 ARG A CZ 1 291 A A +ATOM 2332 N NH1 . ARG A 1 291 ? -10.768 19.898 30.333 1.0 32.43 ? ? ? ? ? ? 408 ARG A NH1 1 291 A A +ATOM 2333 N NH2 . ARG A 1 291 ? -12.352 20.969 31.592 1.0 44.03 ? ? ? ? ? ? 408 ARG A NH2 1 291 A A +ATOM 2334 N N . PRO A 1 292 ? -14.492 21.977 23.446 1.0 39.23 ? ? ? ? ? ? 409 PRO A N 1 292 A A +ATOM 2335 C CA . PRO A 1 292 ? -15.434 21.180 22.652 1.0 39.23 ? ? ? ? ? ? 409 PRO A CA 1 292 A A +ATOM 2336 C C . PRO A 1 292 ? -15.610 19.771 23.193 1.0 44.36 ? ? ? ? ? ? 409 PRO A C 1 292 A A +ATOM 2337 O O . PRO A 1 292 ? -15.910 18.844 22.443 1.0 55.39 ? ? ? ? ? ? 409 PRO A O 1 292 A A +ATOM 2338 C CB . PRO A 1 292 ? -14.819 21.170 21.250 1.0 41.24 ? ? ? ? ? ? 409 PRO A CB 1 292 A A +ATOM 2339 C CG . PRO A 1 292 ? -13.728 22.183 21.277 1.0 61.62 ? ? ? ? ? ? 409 PRO A CG 1 292 A A +ATOM 2340 C CD . PRO A 1 292 ? -13.276 22.301 22.692 1.0 51.69 ? ? ? ? ? ? 409 PRO A CD 1 292 A A +ATOM 2341 N N . PHE A 1 293 ? -15.418 19.619 24.502 1.0 51.53 ? ? ? ? ? ? 410 PHE A N 1 293 A A +ATOM 2342 C CA . PHE A 1 293 ? -15.534 18.324 25.162 1.0 51.06 ? ? ? ? ? ? 410 PHE A CA 1 293 A A +ATOM 2343 C C . PHE A 1 293 ? -15.413 18.508 26.672 1.0 52.16 ? ? ? ? ? ? 410 PHE A C 1 293 A A +ATOM 2344 O O . PHE A 1 293 ? -15.307 19.632 27.168 1.0 55.17 ? ? ? ? ? ? 410 PHE A O 1 293 A A +ATOM 2345 C CB . PHE A 1 293 ? -14.416 17.394 24.684 1.0 49.76 ? ? ? ? ? ? 410 PHE A CB 1 293 A A +ATOM 2346 C CG . PHE A 1 293 ? -13.038 17.874 25.056 1.0 62.85 ? ? ? ? ? ? 410 PHE A CG 1 293 A A +ATOM 2347 C CD1 . PHE A 1 293 ? -12.392 18.838 24.289 1.0 61.48 ? ? ? ? ? ? 410 PHE A CD1 1 293 A A +ATOM 2348 C CD2 . PHE A 1 293 ? -12.406 17.401 26.202 1.0 73.01 ? ? ? ? ? ? 410 PHE A CD2 1 293 A A +ATOM 2349 C CE1 . PHE A 1 293 ? -11.144 19.329 24.658 1.0 59.87 ? ? ? ? ? ? 410 PHE A CE1 1 293 A A +ATOM 2350 C CE2 . PHE A 1 293 ? -11.154 17.887 26.581 1.0 55.37 ? ? ? ? ? ? 410 PHE A CE2 1 293 A A +ATOM 2351 C CZ . PHE A 1 293 ? -10.523 18.852 25.806 1.0 56.26 ? ? ? ? ? ? 410 PHE A CZ 1 293 A A +ATOM 2352 N N . SER A 1 294 ? -15.426 17.392 27.394 1.0 41.42 ? ? ? ? ? ? 411 SER A N 1 294 A A +ATOM 2353 C CA . SER A 1 294 ? -15.296 17.399 28.847 1.0 44.89 ? ? ? ? ? ? 411 SER A CA 1 294 A A +ATOM 2354 C C . SER A 1 294 ? -14.493 16.157 29.218 1.0 46.8 ? ? ? ? ? ? 411 SER A C 1 294 A A +ATOM 2355 O O . SER A 1 294 ? -14.660 15.106 28.602 1.0 38.91 ? ? ? ? ? ? 411 SER A O 1 294 A A +ATOM 2356 C CB . SER A 1 294 ? -16.679 17.360 29.504 1.0 60.81 ? ? ? ? ? ? 411 SER A CB 1 294 A A +ATOM 2357 O OG . SER A 1 294 ? -17.288 18.640 29.496 1.0 83.94 ? ? ? ? ? ? 411 SER A OG 1 294 A A +ATOM 2358 N N . VAL A 1 295 ? -13.621 16.279 30.212 1.0 47.12 ? ? ? ? ? ? 412 VAL A N 1 295 A A +ATOM 2359 C CA . VAL A 1 295 ? -12.787 15.156 30.630 1.0 41.5 ? ? ? ? ? ? 412 VAL A CA 1 295 A A +ATOM 2360 C C . VAL A 1 295 ? -13.286 14.466 31.896 1.0 40.55 ? ? ? ? ? ? 412 VAL A C 1 295 A A +ATOM 2361 O O . VAL A 1 295 ? -14.032 15.047 32.682 1.0 43.56 ? ? ? ? ? ? 412 VAL A O 1 295 A A +ATOM 2362 C CB . VAL A 1 295 ? -11.340 15.621 30.847 1.0 37.58 ? ? ? ? ? ? 412 VAL A CB 1 295 A A +ATOM 2363 C CG1 . VAL A 1 295 ? -10.751 16.076 29.524 1.0 29.68 ? ? ? ? ? ? 412 VAL A CG1 1 295 A A +ATOM 2364 C CG2 . VAL A 1 295 ? -11.302 16.759 31.851 1.0 32.03 ? ? ? ? ? ? 412 VAL A CG2 1 295 A A +ATOM 2365 N N . ARG A 1 296 ? -12.871 13.216 32.081 1.0 46.03 ? ? ? ? ? ? 413 ARG A N 1 296 A A +ATOM 2366 C CA . ARG A 1 296 ? -13.276 12.425 33.242 1.0 36.71 ? ? ? ? ? ? 413 ARG A CA 1 296 A A +ATOM 2367 C C . ARG A 1 296 ? -12.185 11.422 33.600 1.0 33.03 ? ? ? ? ? ? 413 ARG A C 1 296 A A +ATOM 2368 O O . ARG A 1 296 ? -11.858 10.544 32.805 1.0 37.61 ? ? ? ? ? ? 413 ARG A O 1 296 A A +ATOM 2369 C CB . ARG A 1 296 ? -14.583 11.688 32.933 1.0 43.97 ? ? ? ? ? ? 413 ARG A CB 1 296 A A +ATOM 2370 C CG . ARG A 1 296 ? -14.815 10.425 33.742 1.0 51.36 ? ? ? ? ? ? 413 ARG A CG 1 296 A A +ATOM 2371 C CD . ARG A 1 296 ? -16.295 10.078 33.797 1.0 61.85 ? ? ? ? ? ? 413 ARG A CD 1 296 A A +ATOM 2372 N NE . ARG A 1 296 ? -16.766 9.499 32.539 1.0 59.9 ? ? ? ? ? ? 413 ARG A NE 1 296 A A +ATOM 2373 C CZ . ARG A 1 296 ? -17.907 8.832 32.403 1.0 60.5 ? ? ? ? ? ? 413 ARG A CZ 1 296 A A +ATOM 2374 N NH1 . ARG A 1 296 ? -18.698 8.649 33.452 1.0 52.53 ? ? ? ? ? ? 413 ARG A NH1 1 296 A A +ATOM 2375 N NH2 . ARG A 1 296 ? -18.257 8.344 31.219 1.0 23.98 ? ? ? ? ? ? 413 ARG A NH2 1 296 A A +ATOM 2376 N N . TYR A 1 297 ? -11.623 11.551 34.798 1.0 32.09 ? ? ? ? ? ? 414 TYR A N 1 297 A A +ATOM 2377 C CA . TYR A 1 297 ? -10.562 10.643 35.220 1.0 32.39 ? ? ? ? ? ? 414 TYR A CA 1 297 A A +ATOM 2378 C C . TYR A 1 297 ? -11.057 9.365 35.901 1.0 31.53 ? ? ? ? ? ? 414 TYR A C 1 297 A A +ATOM 2379 O O . TYR A 1 297 ? -12.000 9.386 36.695 1.0 65.12 ? ? ? ? ? ? 414 TYR A O 1 297 A A +ATOM 2380 C CB . TYR A 1 297 ? -9.573 11.359 36.149 1.0 14.01 ? ? ? ? ? ? 414 TYR A CB 1 297 A A +ATOM 2381 C CG . TYR A 1 297 ? -8.312 10.559 36.381 1.0 25.23 ? ? ? ? ? ? 414 TYR A CG 1 297 A A +ATOM 2382 C CD1 . TYR A 1 297 ? -7.456 10.258 35.322 1.0 39.31 ? ? ? ? ? ? 414 TYR A CD1 1 297 A A +ATOM 2383 C CD2 . TYR A 1 297 ? -8.008 10.038 37.637 1.0 19.41 ? ? ? ? ? ? 414 TYR A CD2 1 297 A A +ATOM 2384 C CE1 . TYR A 1 297 ? -6.332 9.454 35.502 1.0 52.9 ? ? ? ? ? ? 414 TYR A CE1 1 297 A A +ATOM 2385 C CE2 . TYR A 1 297 ? -6.884 9.232 37.828 1.0 45.56 ? ? ? ? ? ? 414 TYR A CE2 1 297 A A +ATOM 2386 C CZ . TYR A 1 297 ? -6.052 8.941 36.754 1.0 48.02 ? ? ? ? ? ? 414 TYR A CZ 1 297 A A +ATOM 2387 O OH . TYR A 1 297 ? -4.955 8.123 36.920 1.0 55.29 ? ? ? ? ? ? 414 TYR A OH 1 297 A A +ATOM 2388 N N . ASP A 1 298 ? -10.409 8.251 35.571 1.0 44.74 ? ? ? ? ? ? 415 ASP A N 1 298 A A +ATOM 2389 C CA . ASP A 1 298 ? -10.736 6.943 36.136 1.0 45.65 ? ? ? ? ? ? 415 ASP A CA 1 298 A A +ATOM 2390 C C . ASP A 1 298 ? -9.522 6.431 36.920 1.0 54.5 ? ? ? ? ? ? 415 ASP A C 1 298 A A +ATOM 2391 O O . ASP A 1 298 ? -8.570 5.900 36.342 1.0 62.76 ? ? ? ? ? ? 415 ASP A O 1 298 A A +ATOM 2392 C CB . ASP A 1 298 ? -11.085 5.954 35.021 1.0 52.89 ? ? ? ? ? ? 415 ASP A CB 1 298 A A +ATOM 2393 C CG . ASP A 1 298 ? -11.463 4.582 35.546 1.0 39.17 ? ? ? ? ? ? 415 ASP A CG 1 298 A A +ATOM 2394 O OD1 . ASP A 1 298 ? -11.495 3.622 34.749 1.0 52.8 ? ? ? ? ? ? 415 ASP A OD1 1 298 A A +ATOM 2395 O OD2 . ASP A 1 298 ? -11.735 4.465 36.759 1.0 41.7 ? ? ? ? ? ? 415 ASP A OD2 1 298 A A +ATOM 2396 N N . PRO A 1 299 ? -9.545 6.583 38.254 1.0 40.81 ? ? ? ? ? ? 416 PRO A N 1 299 A A +ATOM 2397 C CA . PRO A 1 299 ? -8.432 6.130 39.093 1.0 19.09 ? ? ? ? ? ? 416 PRO A CA 1 299 A A +ATOM 2398 C C . PRO A 1 299 ? -8.224 4.619 39.064 1.0 20.61 ? ? ? ? ? ? 416 PRO A C 1 299 A A +ATOM 2399 O O . PRO A 1 299 ? -7.143 4.131 39.383 1.0 40.06 ? ? ? ? ? ? 416 PRO A O 1 299 A A +ATOM 2400 C CB . PRO A 1 299 ? -8.801 6.639 40.486 1.0 18.39 ? ? ? ? ? ? 416 PRO A CB 1 299 A A +ATOM 2401 C CG . PRO A 1 299 ? -10.275 6.820 40.450 1.0 36.47 ? ? ? ? ? ? 416 PRO A CG 1 299 A A +ATOM 2402 C CD . PRO A 1 299 ? -10.634 7.179 39.046 1.0 39.25 ? ? ? ? ? ? 416 PRO A CD 1 299 A A +ATOM 2403 N N . TYR A 1 300 ? -9.263 3.884 38.677 1.0 23.31 ? ? ? ? ? ? 417 TYR A N 1 300 A A +ATOM 2404 C CA . TYR A 1 300 ? -9.202 2.428 38.606 1.0 18.04 ? ? ? ? ? ? 417 TYR A CA 1 300 A A +ATOM 2405 C C . TYR A 1 300 ? -8.345 1.944 37.437 1.0 26.33 ? ? ? ? ? ? 417 TYR A C 1 300 A A +ATOM 2406 O O . TYR A 1 300 ? -7.694 0.905 37.531 1.0 42.27 ? ? ? ? ? ? 417 TYR A O 1 300 A A +ATOM 2407 C CB . TYR A 1 300 ? -10.613 1.860 38.496 1.0 34.2 ? ? ? ? ? ? 417 TYR A CB 1 300 A A +ATOM 2408 C CG . TYR A 1 300 ? -11.441 2.080 39.740 1.0 31.39 ? ? ? ? ? ? 417 TYR A CG 1 300 A A +ATOM 2409 C CD1 . TYR A 1 300 ? -12.343 3.137 39.826 1.0 44.97 ? ? ? ? ? ? 417 TYR A CD1 1 300 A A +ATOM 2410 C CD2 . TYR A 1 300 ? -11.321 1.232 40.838 1.0 43.77 ? ? ? ? ? ? 417 TYR A CD2 1 300 A A +ATOM 2411 C CE1 . TYR A 1 300 ? -13.103 3.344 40.979 1.0 60.75 ? ? ? ? ? ? 417 TYR A CE1 1 300 A A +ATOM 2412 C CE2 . TYR A 1 300 ? -12.077 1.431 41.994 1.0 47.93 ? ? ? ? ? ? 417 TYR A CE2 1 300 A A +ATOM 2413 C CZ . TYR A 1 300 ? -12.965 2.487 42.057 1.0 46.98 ? ? ? ? ? ? 417 TYR A CZ 1 300 A A +ATOM 2414 O OH . TYR A 1 300 ? -13.712 2.688 43.193 1.0 34.47 ? ? ? ? ? ? 417 TYR A OH 1 300 A A +ATOM 2415 N N . THR A 1 301 ? -8.350 2.694 36.336 1.0 29.23 ? ? ? ? ? ? 418 THR A N 1 301 A A +ATOM 2416 C CA . THR A 1 301 ? -7.551 2.346 35.158 1.0 22.36 ? ? ? ? ? ? 418 THR A CA 1 301 A A +ATOM 2417 C C . THR A 1 301 ? -6.510 3.419 34.858 1.0 20.46 ? ? ? ? ? ? 418 THR A C 1 301 A A +ATOM 2418 O O . THR A 1 301 ? -5.811 3.341 33.847 1.0 20.8 ? ? ? ? ? ? 418 THR A O 1 301 A A +ATOM 2419 C CB . THR A 1 301 ? -8.420 2.174 33.899 1.0 18.97 ? ? ? ? ? ? 418 THR A CB 1 301 A A +ATOM 2420 O OG1 . THR A 1 301 ? -9.083 3.408 33.603 1.0 50.92 ? ? ? ? ? ? 418 THR A OG1 1 301 A A +ATOM 2421 C CG2 . THR A 1 301 ? -9.448 1.084 34.110 1.0 37.66 ? ? ? ? ? ? 418 THR A CG2 1 301 A A +ATOM 2422 N N . GLN A 1 302 ? -6.409 4.407 35.749 1.0 37.04 ? ? ? ? ? ? 419 GLN A N 1 302 A A +ATOM 2423 C CA . GLN A 1 302 ? -5.459 5.508 35.593 1.0 38.68 ? ? ? ? ? ? 419 GLN A CA 1 302 A A +ATOM 2424 C C . GLN A 1 302 ? -5.572 6.013 34.167 1.0 41.44 ? ? ? ? ? ? 419 GLN A C 1 302 A A +ATOM 2425 O O . GLN A 1 302 ? -4.578 6.120 33.449 1.0 53.88 ? ? ? ? ? ? 419 GLN A O 1 302 A A +ATOM 2426 C CB . GLN A 1 302 ? -4.030 5.028 35.836 1.0 39.99 ? ? ? ? ? ? 419 GLN A CB 1 302 A A +ATOM 2427 C CG . GLN A 1 302 ? -3.746 4.561 37.248 1.0 43.23 ? ? ? ? ? ? 419 GLN A CG 1 302 A A +ATOM 2428 C CD . GLN A 1 302 ? -2.366 3.952 37.373 1.0 55.23 ? ? ? ? ? ? 419 GLN A CD 1 302 A A +ATOM 2429 O OE1 . GLN A 1 302 ? -2.072 2.921 36.766 1.0 66.54 ? ? ? ? ? ? 419 GLN A OE1 1 302 A A +ATOM 2430 N NE2 . GLN A 1 302 ? -1.509 4.587 38.160 1.0 65.41 ? ? ? ? ? ? 419 GLN A NE2 1 302 A A +ATOM 2431 N N . ARG A 1 303 ? -6.794 6.321 33.759 1.0 36.0 ? ? ? ? ? ? 420 ARG A N 1 303 A A +ATOM 2432 C CA . ARG A 1 303 ? -7.035 6.780 32.405 1.0 36.42 ? ? ? ? ? ? 420 ARG A CA 1 303 A A +ATOM 2433 C C . ARG A 1 303 ? -8.029 7.928 32.360 1.0 28.89 ? ? ? ? ? ? 420 ARG A C 1 303 A A +ATOM 2434 O O . ARG A 1 303 ? -8.985 7.966 33.130 1.0 38.54 ? ? ? ? ? ? 420 ARG A O 1 303 A A +ATOM 2435 C CB . ARG A 1 303 ? -7.560 5.615 31.568 1.0 43.32 ? ? ? ? ? ? 420 ARG A CB 1 303 A A +ATOM 2436 C CG . ARG A 1 303 ? -7.004 5.546 30.162 1.0 46.86 ? ? ? ? ? ? 420 ARG A CG 1 303 A A +ATOM 2437 C CD . ARG A 1 303 ? -7.553 4.328 29.428 1.0 65.16 ? ? ? ? ? ? 420 ARG A CD 1 303 A A +ATOM 2438 N NE . ARG A 1 303 ? -7.693 3.176 30.318 1.0 68.48 ? ? ? ? ? ? 420 ARG A NE 1 303 A A +ATOM 2439 C CZ . ARG A 1 303 ? -7.499 1.911 29.951 1.0 71.5 ? ? ? ? ? ? 420 ARG A CZ 1 303 A A +ATOM 2440 N NH1 . ARG A 1 303 ? -7.151 1.621 28.703 1.0 63.28 ? ? ? ? ? ? 420 ARG A NH1 1 303 A A +ATOM 2441 N NH2 . ARG A 1 303 ? -7.647 0.936 30.839 1.0 60.1 ? ? ? ? ? ? 420 ARG A NH2 1 303 A A +ATOM 2442 N N . ILE A 1 304 ? -7.791 8.864 31.451 1.0 5.09 ? ? ? ? ? ? 421 ILE A N 1 304 A A +ATOM 2443 C CA . ILE A 1 304 ? -8.679 10.001 31.288 1.0 22.29 ? ? ? ? ? ? 421 ILE A CA 1 304 A A +ATOM 2444 C C . ILE A 1 304 ? -9.675 9.629 30.191 1.0 35.36 ? ? ? ? ? ? 421 ILE A C 1 304 A A +ATOM 2445 O O . ILE A 1 304 ? -9.301 8.971 29.215 1.0 37.76 ? ? ? ? ? ? 421 ILE A O 1 304 A A +ATOM 2446 C CB . ILE A 1 304 ? -7.899 11.274 30.842 1.0 17.55 ? ? ? ? ? ? 421 ILE A CB 1 304 A A +ATOM 2447 C CG1 . ILE A 1 304 ? -7.312 11.990 32.058 1.0 11.22 ? ? ? ? ? ? 421 ILE A CG1 1 304 A A +ATOM 2448 C CG2 . ILE A 1 304 ? -8.821 12.219 30.077 1.0 27.04 ? ? ? ? ? ? 421 ILE A CG2 1 304 A A +ATOM 2449 C CD1 . ILE A 1 304 ? -8.337 12.695 32.912 1.0 30.57 ? ? ? ? ? ? 421 ILE A CD1 1 304 A A +ATOM 2450 N N . GLU A 1 305 ? -10.938 10.029 30.357 1.0 44.17 ? ? ? ? ? ? 422 GLU A N 1 305 A A +ATOM 2451 C CA . GLU A 1 305 ? -11.960 9.765 29.345 1.0 42.82 ? ? ? ? ? ? 422 GLU A CA 1 305 A A +ATOM 2452 C C . GLU A 1 305 ? -12.428 11.103 28.792 1.0 56.06 ? ? ? ? ? ? 422 GLU A C 1 305 A A +ATOM 2453 O O . GLU A 1 305 ? -12.695 12.035 29.548 1.0 70.09 ? ? ? ? ? ? 422 GLU A O 1 305 A A +ATOM 2454 C CB . GLU A 1 305 ? -13.153 9.002 29.927 1.0 49.23 ? ? ? ? ? ? 422 GLU A CB 1 305 A A +ATOM 2455 C CG . GLU A 1 305 ? -14.105 8.493 28.846 1.0 66.49 ? ? ? ? ? ? 422 GLU A CG 1 305 A A +ATOM 2456 C CD . GLU A 1 305 ? -15.322 7.775 29.402 1.0 83.44 ? ? ? ? ? ? 422 GLU A CD 1 305 A A +ATOM 2457 O OE1 . GLU A 1 305 ? -16.271 7.529 28.626 1.0 61.26 ? ? ? ? ? ? 422 GLU A OE1 1 305 A A +ATOM 2458 O OE2 . GLU A 1 305 ? -15.328 7.455 30.610 1.0 86.85 ? ? ? ? ? ? 422 GLU A OE2 1 305 A A +ATOM 2459 N N . VAL A 1 306 ? -12.510 11.202 27.469 1.0 57.84 ? ? ? ? ? ? 423 VAL A N 1 306 A A +ATOM 2460 C CA . VAL A 1 306 ? -12.938 12.438 26.819 1.0 50.66 ? ? ? ? ? ? 423 VAL A CA 1 306 A A +ATOM 2461 C C . VAL A 1 306 ? -14.405 12.351 26.404 1.0 41.37 ? ? ? ? ? ? 423 VAL A C 1 306 A A +ATOM 2462 O O . VAL A 1 306 ? -14.783 11.512 25.594 1.0 26.86 ? ? ? ? ? ? 423 VAL A O 1 306 A A +ATOM 2463 C CB . VAL A 1 306 ? -12.059 12.736 25.584 1.0 38.04 ? ? ? ? ? ? 423 VAL A CB 1 306 A A +ATOM 2464 C CG1 . VAL A 1 306 ? -12.374 14.119 25.045 1.0 46.38 ? ? ? ? ? ? 423 VAL A CG1 1 306 A A +ATOM 2465 C CG2 . VAL A 1 306 ? -10.589 12.641 25.964 1.0 40.98 ? ? ? ? ? ? 423 VAL A CG2 1 306 A A +ATOM 2466 N N . LEU A 1 307 ? -15.228 13.224 26.971 1.0 46.86 ? ? ? ? ? ? 424 LEU A N 1 307 A A +ATOM 2467 C CA . LEU A 1 307 ? -16.648 13.218 26.673 1.0 44.59 ? ? ? ? ? ? 424 LEU A CA 1 307 A A +ATOM 2468 C C . LEU A 1 307 ? -17.093 14.362 25.773 1.0 54.91 ? ? ? ? ? ? 424 LEU A C 1 307 A A +ATOM 2469 O O . LEU A 1 307 ? -16.446 15.408 25.694 1.0 59.89 ? ? ? ? ? ? 424 LEU A O 1 307 A A +ATOM 2470 C CB . LEU A 1 307 ? -17.454 13.255 27.973 1.0 35.66 ? ? ? ? ? ? 424 LEU A CB 1 307 A A +ATOM 2471 C CG . LEU A 1 307 ? -17.354 12.020 28.864 1.0 33.05 ? ? ? ? ? ? 424 LEU A CG 1 307 A A +ATOM 2472 C CD1 . LEU A 1 307 ? -17.910 12.327 30.240 1.0 38.05 ? ? ? ? ? ? 424 LEU A CD1 1 307 A A +ATOM 2473 C CD2 . LEU A 1 307 ? -18.113 10.882 28.222 1.0 20.8 ? ? ? ? ? ? 424 LEU A CD2 1 307 A A +ATOM 2474 N N . ASP A 1 308 ? -18.217 14.143 25.097 1.0 42.91 ? ? ? ? ? ? 425 ASP A N 1 308 A A +ATOM 2475 C CA . ASP A 1 308 ? -18.808 15.122 24.198 1.0 36.38 ? ? ? ? ? ? 425 ASP A CA 1 308 A A +ATOM 2476 C C . ASP A 1 308 ? -19.887 15.885 24.962 1.0 36.99 ? ? ? ? ? ? 425 ASP A C 1 308 A A +ATOM 2477 O O . ASP A 1 308 ? -20.897 15.312 25.366 1.0 45.17 ? ? ? ? ? ? 425 ASP A O 1 308 A A +ATOM 2478 C CB . ASP A 1 308 ? -19.425 14.403 22.990 1.0 42.98 ? ? ? ? ? ? 425 ASP A CB 1 308 A A +ATOM 2479 C CG . ASP A 1 308 ? -20.631 15.131 22.431 1.0 50.49 ? ? ? ? ? ? 425 ASP A CG 1 308 A A +ATOM 2480 O OD1 . ASP A 1 308 ? -21.714 14.514 22.364 1.0 50.76 ? ? ? ? ? ? 425 ASP A OD1 1 308 A A +ATOM 2481 O OD2 . ASP A 1 308 ? -20.481 16.313 22.063 1.0 60.47 ? ? ? ? ? ? 425 ASP A OD2 1 308 A A +ATOM 2482 N N . ASN A 1 309 ? -19.658 17.180 25.163 1.0 36.35 ? ? ? ? ? ? 426 ASN A N 1 309 A A +ATOM 2483 C CA . ASN A 1 309 ? -20.573 18.059 25.880 1.0 56.38 ? ? ? ? ? ? 426 ASN A CA 1 309 A A +ATOM 2484 C C . ASN A 1 309 ? -22.018 17.551 26.000 1.0 54.47 ? ? ? ? ? ? 426 ASN A C 1 309 A A +ATOM 2485 O O . ASN A 1 309 ? -22.624 17.646 27.062 1.0 64.32 ? ? ? ? ? ? 426 ASN A O 1 309 A A +ATOM 2486 C CB . ASN A 1 309 ? -20.567 19.440 25.223 1.0 67.66 ? ? ? ? ? ? 426 ASN A CB 1 309 A A +ATOM 2487 C CG . ASN A 1 309 ? -19.712 19.477 23.967 1.0 86.65 ? ? ? ? ? ? 426 ASN A CG 1 309 A A +ATOM 2488 O OD1 . ASN A 1 309 ? -18.492 19.607 24.043 1.0 84.18 ? ? ? ? ? ? 426 ASN A OD1 1 309 A A +ATOM 2489 N ND2 . ASN A 1 309 ? -20.349 19.364 22.810 1.0 95.28 ? ? ? ? ? ? 426 ASN A ND2 1 309 A A +ATOM 2490 N N . THR A 1 310 ? -22.564 17.034 24.904 1.0 52.24 ? ? ? ? ? ? 427 THR A N 1 310 A A +ATOM 2491 C CA . THR A 1 310 ? -23.931 16.512 24.875 1.0 49.39 ? ? ? ? ? ? 427 THR A CA 1 310 A A +ATOM 2492 C C . THR A 1 310 ? -24.119 15.287 25.758 1.0 44.74 ? ? ? ? ? ? 427 THR A C 1 310 A A +ATOM 2493 O O . THR A 1 310 ? -25.042 15.229 26.565 1.0 42.41 ? ? ? ? ? ? 427 THR A O 1 310 A A +ATOM 2494 C CB . THR A 1 310 ? -24.331 16.139 23.443 1.0 60.18 ? ? ? ? ? ? 427 THR A CB 1 310 A A +ATOM 2495 O OG1 . THR A 1 310 ? -24.295 17.311 22.617 1.0 80.03 ? ? ? ? ? ? 427 THR A OG1 1 310 A A +ATOM 2496 C CG2 . THR A 1 310 ? -25.726 15.511 23.424 1.0 47.23 ? ? ? ? ? ? 427 THR A CG2 1 310 A A +ATOM 2497 N N . GLN A 1 311 ? -23.243 14.306 25.583 1.0 47.04 ? ? ? ? ? ? 428 GLN A N 1 311 A A +ATOM 2498 C CA . GLN A 1 311 ? -23.288 13.080 26.365 1.0 41.76 ? ? ? ? ? ? 428 GLN A CA 1 311 A A +ATOM 2499 C C . GLN A 1 311 ? -22.836 13.407 27.775 1.0 37.71 ? ? ? ? ? ? 428 GLN A C 1 311 A A +ATOM 2500 O O . GLN A 1 311 ? -23.197 12.723 28.727 1.0 37.38 ? ? ? ? ? ? 428 GLN A O 1 311 A A +ATOM 2501 C CB . GLN A 1 311 ? -22.372 12.021 25.759 1.0 57.95 ? ? ? ? ? ? 428 GLN A CB 1 311 A A +ATOM 2502 C CG . GLN A 1 311 ? -20.903 12.400 25.756 1.0 71.47 ? ? ? ? ? ? 428 GLN A CG 1 311 A A +ATOM 2503 C CD . GLN A 1 311 ? -20.130 11.687 24.663 1.0 77.03 ? ? ? ? ? ? 428 GLN A CD 1 311 A A +ATOM 2504 O OE1 . GLN A 1 311 ? -18.945 11.382 24.817 1.0 80.85 ? ? ? ? ? ? 428 GLN A OE1 1 311 A A +ATOM 2505 N NE2 . GLN A 1 311 ? -20.794 11.426 23.551 1.0 78.75 ? ? ? ? ? ? 428 GLN A NE2 1 311 A A +ATOM 2506 N N . GLN A 1 312 ? -22.031 14.458 27.899 1.0 32.32 ? ? ? ? ? ? 429 GLN A N 1 312 A A +ATOM 2507 C CA . GLN A 1 312 ? -21.548 14.895 29.201 1.0 44.95 ? ? ? ? ? ? 429 GLN A CA 1 312 A A +ATOM 2508 C C . GLN A 1 312 ? -22.763 15.429 29.964 1.0 53.81 ? ? ? ? ? ? 429 GLN A C 1 312 A A +ATOM 2509 O O . GLN A 1 312 ? -22.913 15.210 31.169 1.0 51.75 ? ? ? ? ? ? 429 GLN A O 1 312 A A +ATOM 2510 C CB . GLN A 1 312 ? -20.512 16.008 29.040 1.0 41.33 ? ? ? ? ? ? 429 GLN A CB 1 312 A A +ATOM 2511 C CG . GLN A 1 312 ? -19.548 16.133 30.205 1.0 62.27 ? ? ? ? ? ? 429 GLN A CG 1 312 A A +ATOM 2512 C CD . GLN A 1 312 ? -20.039 17.080 31.279 1.0 54.21 ? ? ? ? ? ? 429 GLN A CD 1 312 A A +ATOM 2513 O OE1 . GLN A 1 312 ? -20.175 16.700 32.442 1.0 48.76 ? ? ? ? ? ? 429 GLN A OE1 1 312 A A +ATOM 2514 N NE2 . GLN A 1 312 ? -20.302 18.323 30.896 1.0 50.57 ? ? ? ? ? ? 429 GLN A NE2 1 312 A A +ATOM 2515 N N . LEU A 1 313 ? -23.621 16.134 29.227 1.0 64.83 ? ? ? ? ? ? 430 LEU A N 1 313 A A +ATOM 2516 C CA . LEU A 1 313 ? -24.860 16.721 29.739 1.0 44.71 ? ? ? ? ? ? 430 LEU A CA 1 313 A A +ATOM 2517 C C . LEU A 1 313 ? -25.696 15.589 30.318 1.0 33.89 ? ? ? ? ? ? 430 LEU A C 1 313 A A +ATOM 2518 O O . LEU A 1 313 ? -26.067 15.607 31.489 1.0 32.98 ? ? ? ? ? ? 430 LEU A O 1 313 A A +ATOM 2519 C CB . LEU A 1 313 ? -25.628 17.384 28.583 1.0 25.78 ? ? ? ? ? ? 430 LEU A CB 1 313 A A +ATOM 2520 C CG . LEU A 1 313 ? -26.466 18.661 28.737 1.0 39.27 ? ? ? ? ? ? 430 LEU A CG 1 313 A A +ATOM 2521 C CD1 . LEU A 1 313 ? -25.905 19.576 29.817 1.0 34.15 ? ? ? ? ? ? 430 LEU A CD1 1 313 A A +ATOM 2522 C CD2 . LEU A 1 313 ? -26.491 19.381 27.394 1.0 18.5 ? ? ? ? ? ? 430 LEU A CD2 1 313 A A +ATOM 2523 N N . LYS A 1 314 ? -25.981 14.609 29.466 1.0 27.52 ? ? ? ? ? ? 431 LYS A N 1 314 A A +ATOM 2524 C CA . LYS A 1 314 ? -26.760 13.440 29.838 1.0 42.32 ? ? ? ? ? ? 431 LYS A CA 1 314 A A +ATOM 2525 C C . LYS A 1 314 ? -26.161 12.743 31.053 1.0 52.75 ? ? ? ? ? ? 431 LYS A C 1 314 A A +ATOM 2526 O O . LYS A 1 314 ? -26.887 12.280 31.932 1.0 62.72 ? ? ? ? ? ? 431 LYS A O 1 314 A A +ATOM 2527 C CB . LYS A 1 314 ? -26.813 12.459 28.669 1.0 52.8 ? ? ? ? ? ? 431 LYS A CB 1 314 A A +ATOM 2528 C CG . LYS A 1 314 ? -27.510 13.000 27.440 1.0 68.93 ? ? ? ? ? ? 431 LYS A CG 1 314 A A +ATOM 2529 C CD . LYS A 1 314 ? -27.812 11.887 26.455 1.0 86.73 ? ? ? ? ? ? 431 LYS A CD 1 314 A A +ATOM 2530 C CE . LYS A 1 314 ? -28.484 12.418 25.201 1.0 89.43 ? ? ? ? ? ? 431 LYS A CE 1 314 A A +ATOM 2531 N NZ . LYS A 1 314 ? -28.905 11.304 24.311 1.0 85.66 ? ? ? ? ? ? 431 LYS A NZ 1 314 A A +ATOM 2532 N N . ILE A 1 315 ? -24.834 12.665 31.095 1.0 54.13 ? ? ? ? ? ? 432 ILE A N 1 315 A A +ATOM 2533 C CA . ILE A 1 315 ? -24.143 12.019 32.206 1.0 49.64 ? ? ? ? ? ? 432 ILE A CA 1 315 A A +ATOM 2534 C C . ILE A 1 315 ? -24.449 12.738 33.516 1.0 50.77 ? ? ? ? ? ? 432 ILE A C 1 315 A A +ATOM 2535 O O . ILE A 1 315 ? -24.717 12.103 34.534 1.0 46.54 ? ? ? ? ? ? 432 ILE A O 1 315 A A +ATOM 2536 C CB . ILE A 1 315 ? -22.615 11.991 31.973 1.0 48.67 ? ? ? ? ? ? 432 ILE A CB 1 315 A A +ATOM 2537 C CG1 . ILE A 1 315 ? -22.277 10.987 30.867 1.0 39.82 ? ? ? ? ? ? 432 ILE A CG1 1 315 A A +ATOM 2538 C CG2 . ILE A 1 315 ? -21.892 11.613 33.254 1.0 52.52 ? ? ? ? ? ? 432 ILE A CG2 1 315 A A +ATOM 2539 C CD1 . ILE A 1 315 ? -23.153 9.746 30.857 1.0 39.19 ? ? ? ? ? ? 432 ILE A CD1 1 315 A A +ATOM 2540 N N . LEU A 1 316 ? -24.409 14.064 33.486 1.0 38.29 ? ? ? ? ? ? 433 LEU A N 1 316 A A +ATOM 2541 C CA . LEU A 1 316 ? -24.706 14.852 34.673 1.0 37.4 ? ? ? ? ? ? 433 LEU A CA 1 316 A A +ATOM 2542 C C . LEU A 1 316 ? -26.137 14.569 35.130 1.0 47.88 ? ? ? ? ? ? 433 LEU A C 1 316 A A +ATOM 2543 O O . LEU A 1 316 ? -26.391 14.315 36.309 1.0 44.2 ? ? ? ? ? ? 433 LEU A O 1 316 A A +ATOM 2544 C CB . LEU A 1 316 ? -24.558 16.340 34.364 1.0 17.6 ? ? ? ? ? ? 433 LEU A CB 1 316 A A +ATOM 2545 C CG . LEU A 1 316 ? -23.146 16.815 34.048 1.0 38.38 ? ? ? ? ? ? 433 LEU A CG 1 316 A A +ATOM 2546 C CD1 . LEU A 1 316 ? -23.193 17.827 32.920 1.0 51.77 ? ? ? ? ? ? 433 LEU A CD1 1 316 A A +ATOM 2547 C CD2 . LEU A 1 316 ? -22.533 17.418 35.297 1.0 44.05 ? ? ? ? ? ? 433 LEU A CD2 1 316 A A +ATOM 2548 N N . ALA A 1 317 ? -27.070 14.622 34.184 1.0 40.82 ? ? ? ? ? ? 434 ALA A N 1 317 A A +ATOM 2549 C CA . ALA A 1 317 ? -28.476 14.376 34.471 1.0 31.1 ? ? ? ? ? ? 434 ALA A CA 1 317 A A +ATOM 2550 C C . ALA A 1 317 ? -28.665 13.096 35.284 1.0 45.92 ? ? ? ? ? ? 434 ALA A C 1 317 A A +ATOM 2551 O O . ALA A 1 317 ? -29.240 13.117 36.374 1.0 57.7 ? ? ? ? ? ? 434 ALA A O 1 317 A A +ATOM 2552 C CB . ALA A 1 317 ? -29.262 14.287 33.165 1.0 50.7 ? ? ? ? ? ? 434 ALA A CB 1 317 A A +ATOM 2553 N N . ASP A 1 318 ? -28.186 11.981 34.740 1.0 39.05 ? ? ? ? ? ? 435 ASP A N 1 318 A A +ATOM 2554 C CA . ASP A 1 318 ? -28.303 10.691 35.407 1.0 44.06 ? ? ? ? ? ? 435 ASP A CA 1 318 A A +ATOM 2555 C C . ASP A 1 318 ? -27.677 10.753 36.792 1.0 51.97 ? ? ? ? ? ? 435 ASP A C 1 318 A A +ATOM 2556 O O . ASP A 1 318 ? -28.266 10.293 37.768 1.0 49.25 ? ? ? ? ? ? 435 ASP A O 1 318 A A +ATOM 2557 C CB . ASP A 1 318 ? -27.609 9.602 34.581 1.0 65.86 ? ? ? ? ? ? 435 ASP A CB 1 318 A A +ATOM 2558 C CG . ASP A 1 318 ? -28.199 9.457 33.191 1.0 82.38 ? ? ? ? ? ? 435 ASP A CG 1 318 A A +ATOM 2559 O OD1 . ASP A 1 318 ? -29.439 9.528 33.062 1.0 85.74 ? ? ? ? ? ? 435 ASP A OD1 1 318 A A +ATOM 2560 O OD2 . ASP A 1 318 ? -27.424 9.273 32.228 1.0 100.0 ? ? ? ? ? ? 435 ASP A OD2 1 318 A A +ATOM 2561 N N . SER A 1 319 ? -26.480 11.328 36.871 1.0 46.23 ? ? ? ? ? ? 436 SER A N 1 319 A A +ATOM 2562 C CA . SER A 1 319 ? -25.772 11.448 38.142 1.0 40.37 ? ? ? ? ? ? 436 SER A CA 1 319 A A +ATOM 2563 C C . SER A 1 319 ? -26.622 12.153 39.184 1.0 35.36 ? ? ? ? ? ? 436 SER A C 1 319 A A +ATOM 2564 O O . SER A 1 319 ? -26.746 11.684 40.313 1.0 27.25 ? ? ? ? ? ? 436 SER A O 1 319 A A +ATOM 2565 C CB . SER A 1 319 ? -24.465 12.220 37.965 1.0 40.94 ? ? ? ? ? ? 436 SER A CB 1 319 A A +ATOM 2566 O OG . SER A 1 319 ? -23.842 12.443 39.220 1.0 18.64 ? ? ? ? ? ? 436 SER A OG 1 319 A A +ATOM 2567 N N . ILE A 1 320 ? -27.192 13.291 38.805 1.0 43.24 ? ? ? ? ? ? 437 ILE A N 1 320 A A +ATOM 2568 C CA . ILE A 1 320 ? -28.036 14.055 39.716 1.0 35.72 ? ? ? ? ? ? 437 ILE A CA 1 320 A A +ATOM 2569 C C . ILE A 1 320 ? -29.258 13.228 40.083 1.0 25.6 ? ? ? ? ? ? 437 ILE A C 1 320 A A +ATOM 2570 O O . ILE A 1 320 ? -29.517 12.957 41.255 1.0 31.76 ? ? ? ? ? ? 437 ILE A O 1 320 A A +ATOM 2571 C CB . ILE A 1 320 ? -28.518 15.378 39.068 1.0 45.25 ? ? ? ? ? ? 437 ILE A CB 1 320 A A +ATOM 2572 C CG1 . ILE A 1 320 ? -27.340 16.100 38.410 1.0 47.42 ? ? ? ? ? ? 437 ILE A CG1 1 320 A A +ATOM 2573 C CG2 . ILE A 1 320 ? -29.160 16.281 40.125 1.0 52.02 ? ? ? ? ? ? 437 ILE A CG2 1 320 A A +ATOM 2574 C CD1 . ILE A 1 320 ? -27.715 17.391 37.730 1.0 59.4 ? ? ? ? ? ? 437 ILE A CD1 1 320 A A +ATOM 2575 N N . ASN A 1 321 ? -30.003 12.831 39.059 1.0 25.65 ? ? ? ? ? ? 438 ASN A N 1 321 A A +ATOM 2576 C CA . ASN A 1 321 ? -31.209 12.036 39.228 1.0 29.75 ? ? ? ? ? ? 438 ASN A CA 1 321 A A +ATOM 2577 C C . ASN A 1 321 ? -31.000 10.878 40.203 1.0 29.52 ? ? ? ? ? ? 438 ASN A C 1 321 A A +ATOM 2578 O O . ASN A 1 321 ? -31.900 10.527 40.965 1.0 40.32 ? ? ? ? ? ? 438 ASN A O 1 321 A A +ATOM 2579 C CB . ASN A 1 321 ? -31.663 11.506 37.866 1.0 22.2 ? ? ? ? ? ? 438 ASN A CB 1 321 A A +ATOM 2580 C CG . ASN A 1 321 ? -33.010 10.821 37.925 1.0 43.18 ? ? ? ? ? ? 438 ASN A CG 1 321 A A +ATOM 2581 O OD1 . ASN A 1 321 ? -34.052 11.474 37.973 1.0 53.6 ? ? ? ? ? ? 438 ASN A OD1 1 321 A A +ATOM 2582 N ND2 . ASN A 1 321 ? -32.996 9.495 37.919 1.0 75.69 ? ? ? ? ? ? 438 ASN A ND2 1 321 A A +ATOM 2583 N N . SER A 1 322 ? -29.807 10.294 40.177 1.0 26.55 ? ? ? ? ? ? 439 SER A N 1 322 A A +ATOM 2584 C CA . SER A 1 322 ? -29.490 9.173 41.052 1.0 30.2 ? ? ? ? ? ? 439 SER A CA 1 322 A A +ATOM 2585 C C . SER A 1 322 ? -29.284 9.615 42.496 1.0 33.18 ? ? ? ? ? ? 439 SER A C 1 322 A A +ATOM 2586 O O . SER A 1 322 ? -29.983 9.167 43.402 1.0 40.71 ? ? ? ? ? ? 439 SER A O 1 322 A A +ATOM 2587 C CB . SER A 1 322 ? -28.228 8.467 40.555 1.0 42.46 ? ? ? ? ? ? 439 SER A CB 1 322 A A +ATOM 2588 O OG . SER A 1 322 ? -28.020 7.241 41.236 1.0 54.88 ? ? ? ? ? ? 439 SER A OG 1 322 A A +ATOM 2589 N N . GLU A 1 323 ? -28.310 10.496 42.693 1.0 44.97 ? ? ? ? ? ? 440 GLU A N 1 323 A A +ATOM 2590 C CA . GLU A 1 323 ? -27.961 11.018 44.008 1.0 53.35 ? ? ? ? ? ? 440 GLU A CA 1 323 A A +ATOM 2591 C C . GLU A 1 323 ? -29.156 11.492 44.827 1.0 58.79 ? ? ? ? ? ? 440 GLU A C 1 323 A A +ATOM 2592 O O . GLU A 1 323 ? -29.221 11.265 46.036 1.0 53.68 ? ? ? ? ? ? 440 GLU A O 1 323 A A +ATOM 2593 C CB . GLU A 1 323 ? -26.962 12.161 43.843 1.0 60.44 ? ? ? ? ? ? 440 GLU A CB 1 323 A A +ATOM 2594 C CG . GLU A 1 323 ? -25.561 11.696 43.508 1.0 64.52 ? ? ? ? ? ? 440 GLU A CG 1 323 A A +ATOM 2595 C CD . GLU A 1 323 ? -24.684 11.613 44.737 1.0 89.45 ? ? ? ? ? ? 440 GLU A CD 1 323 A A +ATOM 2596 O OE1 . GLU A 1 323 ? -25.219 11.779 45.855 1.0 100.0 ? ? ? ? ? ? 440 GLU A OE1 1 323 A A +ATOM 2597 O OE2 . GLU A 1 323 ? -23.462 11.388 44.589 1.0 88.09 ? ? ? ? ? ? 440 GLU A OE2 1 323 A A +ATOM 2598 N N . ILE A 1 324 ? -30.096 12.154 44.163 1.0 59.7 ? ? ? ? ? ? 441 ILE A N 1 324 A A +ATOM 2599 C CA . ILE A 1 324 ? -31.285 12.669 44.829 1.0 60.5 ? ? ? ? ? ? 441 ILE A CA 1 324 A A +ATOM 2600 C C . ILE A 1 324 ? -32.195 11.572 45.377 1.0 64.02 ? ? ? ? ? ? 441 ILE A C 1 324 A A +ATOM 2601 O O . ILE A 1 324 ? -32.649 11.657 46.519 1.0 77.13 ? ? ? ? ? ? 441 ILE A O 1 324 A A +ATOM 2602 C CB . ILE A 1 324 ? -32.113 13.569 43.887 1.0 58.83 ? ? ? ? ? ? 441 ILE A CB 1 324 A A +ATOM 2603 C CG1 . ILE A 1 324 ? -33.235 14.239 44.678 1.0 47.01 ? ? ? ? ? ? 441 ILE A CG1 1 324 A A +ATOM 2604 C CG2 . ILE A 1 324 ? -32.693 12.754 42.742 1.0 65.37 ? ? ? ? ? ? 441 ILE A CG2 1 324 A A +ATOM 2605 C CD1 . ILE A 1 324 ? -32.745 15.244 45.685 1.0 35.89 ? ? ? ? ? ? 441 ILE A CD1 1 324 A A +ATOM 2606 N N . GLY A 1 325 ? -32.466 10.553 44.564 1.0 49.58 ? ? ? ? ? ? 442 GLY A N 1 325 A A +ATOM 2607 C CA . GLY A 1 325 ? -33.320 9.466 45.011 1.0 55.28 ? ? ? ? ? ? 442 GLY A CA 1 325 A A +ATOM 2608 C C . GLY A 1 325 ? -32.771 8.817 46.268 1.0 54.37 ? ? ? ? ? ? 442 GLY A C 1 325 A A +ATOM 2609 O O . GLY A 1 325 ? -33.520 8.425 47.165 1.0 52.7 ? ? ? ? ? ? 442 GLY A O 1 325 A A +ATOM 2610 N N . ILE A 1 326 ? -31.450 8.695 46.323 1.0 54.9 ? ? ? ? ? ? 443 ILE A N 1 326 A A +ATOM 2611 C CA . ILE A 1 326 ? -30.779 8.105 47.470 1.0 51.18 ? ? ? ? ? ? 443 ILE A CA 1 326 A A +ATOM 2612 C C . ILE A 1 326 ? -30.938 9.061 48.644 1.0 53.49 ? ? ? ? ? ? 443 ILE A C 1 326 A A +ATOM 2613 O O . ILE A 1 326 ? -31.126 8.635 49.782 1.0 50.05 ? ? ? ? ? ? 443 ILE A O 1 326 A A +ATOM 2614 C CB . ILE A 1 326 ? -29.280 7.884 47.177 1.0 48.17 ? ? ? ? ? ? 443 ILE A CB 1 326 A A +ATOM 2615 C CG1 . ILE A 1 326 ? -29.097 6.615 46.337 1.0 49.81 ? ? ? ? ? ? 443 ILE A CG1 1 326 A A +ATOM 2616 C CG2 . ILE A 1 326 ? -28.501 7.768 48.476 1.0 55.24 ? ? ? ? ? ? 443 ILE A CG2 1 326 A A +ATOM 2617 C CD1 . ILE A 1 326 ? -29.910 6.589 45.049 1.0 50.65 ? ? ? ? ? ? 443 ILE A CD1 1 326 A A +ATOM 2618 N N . LEU A 1 327 ? -30.855 10.357 48.347 1.0 43.2 ? ? ? ? ? ? 444 LEU A N 1 327 A A +ATOM 2619 C CA . LEU A 1 327 ? -31.015 11.403 49.349 1.0 32.45 ? ? ? ? ? ? 444 LEU A CA 1 327 A A +ATOM 2620 C C . LEU A 1 327 ? -32.441 11.290 49.872 1.0 45.17 ? ? ? ? ? ? 444 LEU A C 1 327 A A +ATOM 2621 O O . LEU A 1 327 ? -32.731 11.657 51.010 1.0 49.34 ? ? ? ? ? ? 444 LEU A O 1 327 A A +ATOM 2622 C CB . LEU A 1 327 ? -30.792 12.780 48.715 1.0 26.2 ? ? ? ? ? ? 444 LEU A CB 1 327 A A +ATOM 2623 C CG . LEU A 1 327 ? -30.720 14.018 49.618 1.0 15.2 ? ? ? ? ? ? 444 LEU A CG 1 327 A A +ATOM 2624 C CD1 . LEU A 1 327 ? -32.111 14.532 49.897 1.0 28.5 ? ? ? ? ? ? 444 LEU A CD1 1 327 A A +ATOM 2625 C CD2 . LEU A 1 327 ? -30.005 13.683 50.906 1.0 24.79 ? ? ? ? ? ? 444 LEU A CD2 1 327 A A +ATOM 2626 N N . CYS A 1 328 ? -33.321 10.763 49.024 1.0 37.67 ? ? ? ? ? ? 445 CYS A N 1 328 A A +ATOM 2627 C CA . CYS A 1 328 ? -34.720 10.563 49.375 1.0 47.14 ? ? ? ? ? ? 445 CYS A CA 1 328 A A +ATOM 2628 C C . CYS A 1 328 ? -34.822 9.374 50.323 1.0 58.91 ? ? ? ? ? ? 445 CYS A C 1 328 A A +ATOM 2629 O O . CYS A 1 328 ? -35.435 9.462 51.388 1.0 68.68 ? ? ? ? ? ? 445 CYS A O 1 328 A A +ATOM 2630 C CB . CYS A 1 328 ? -35.550 10.287 48.121 1.0 36.14 ? ? ? ? ? ? 445 CYS A CB 1 328 A A +ATOM 2631 S SG . CYS A 1 328 ? -36.340 11.745 47.423 1.0 51.83 ? ? ? ? ? ? 445 CYS A SG 1 328 A A +ATOM 2632 N N . SER A 1 329 ? -34.209 8.263 49.931 1.0 55.38 ? ? ? ? ? ? 446 SER A N 1 329 A A +ATOM 2633 C CA . SER A 1 329 ? -34.228 7.054 50.744 1.0 49.49 ? ? ? ? ? ? 446 SER A CA 1 329 A A +ATOM 2634 C C . SER A 1 329 ? -33.547 7.297 52.084 1.0 48.41 ? ? ? ? ? ? 446 SER A C 1 329 A A +ATOM 2635 O O . SER A 1 329 ? -34.015 6.829 53.124 1.0 41.89 ? ? ? ? ? ? 446 SER A O 1 329 A A +ATOM 2636 C CB . SER A 1 329 ? -33.523 5.921 50.005 1.0 31.22 ? ? ? ? ? ? 446 SER A CB 1 329 A A +ATOM 2637 O OG . SER A 1 329 ? -34.113 5.706 48.735 1.0 49.48 ? ? ? ? ? ? 446 SER A OG 1 329 A A +ATOM 2638 N N . ALA A 1 330 ? -32.433 8.022 52.051 1.0 46.09 ? ? ? ? ? ? 447 ALA A N 1 330 A A +ATOM 2639 C CA . ALA A 1 330 ? -31.685 8.342 53.263 1.0 42.91 ? ? ? ? ? ? 447 ALA A CA 1 330 A A +ATOM 2640 C C . ALA A 1 330 ? -32.595 9.023 54.287 1.0 51.1 ? ? ? ? ? ? 447 ALA A C 1 330 A A +ATOM 2641 O O . ALA A 1 330 ? -32.578 8.694 55.473 1.0 44.02 ? ? ? ? ? ? 447 ALA A O 1 330 A A +ATOM 2642 C CB . ALA A 1 330 ? -30.510 9.252 52.923 1.0 48.36 ? ? ? ? ? ? 447 ALA A CB 1 330 A A +ATOM 2643 N N . LEU A 1 331 ? -33.397 9.969 53.814 1.0 57.01 ? ? ? ? ? ? 448 LEU A N 1 331 A A +ATOM 2644 C CA . LEU A 1 331 ? -34.313 10.701 54.678 1.0 52.65 ? ? ? ? ? ? 448 LEU A CA 1 331 A A +ATOM 2645 C C . LEU A 1 331 ? -35.341 9.775 55.316 1.0 52.29 ? ? ? ? ? ? 448 LEU A C 1 331 A A +ATOM 2646 O O . LEU A 1 331 ? -35.625 9.879 56.508 1.0 54.42 ? ? ? ? ? ? 448 LEU A O 1 331 A A +ATOM 2647 C CB . LEU A 1 331 ? -35.036 11.788 53.878 1.0 43.89 ? ? ? ? ? ? 448 LEU A CB 1 331 A A +ATOM 2648 C CG . LEU A 1 331 ? -34.202 12.996 53.440 1.0 37.47 ? ? ? ? ? ? 448 LEU A CG 1 331 A A +ATOM 2649 C CD1 . LEU A 1 331 ? -35.054 13.898 52.578 1.0 28.39 ? ? ? ? ? ? 448 LEU A CD1 1 331 A A +ATOM 2650 C CD2 . LEU A 1 331 ? -33.692 13.753 54.647 1.0 21.1 ? ? ? ? ? ? 448 LEU A CD2 1 331 A A +ATOM 2651 N N . GLN A 1 332 ? -35.893 8.872 54.515 1.0 60.96 ? ? ? ? ? ? 449 GLN A N 1 332 A A +ATOM 2652 C CA . GLN A 1 332 ? -36.909 7.937 54.987 1.0 82.15 ? ? ? ? ? ? 449 GLN A CA 1 332 A A +ATOM 2653 C C . GLN A 1 332 ? -36.542 7.132 56.238 1.0 92.63 ? ? ? ? ? ? 449 GLN A C 1 332 A A +ATOM 2654 O O . GLN A 1 332 ? -37.324 7.056 57.185 1.0 94.93 ? ? ? ? ? ? 449 GLN A O 1 332 A A +ATOM 2655 C CB . GLN A 1 332 ? -37.286 6.979 53.856 1.0 83.67 ? ? ? ? ? ? 449 GLN A CB 1 332 A A +ATOM 2656 C CG . GLN A 1 332 ? -37.907 7.671 52.661 1.0 92.3 ? ? ? ? ? ? 449 GLN A CG 1 332 A A +ATOM 2657 C CD . GLN A 1 332 ? -38.992 8.647 53.067 1.0 100.0 ? ? ? ? ? ? 449 GLN A CD 1 332 A A +ATOM 2658 O OE1 . GLN A 1 332 ? -39.961 8.270 53.724 1.0 100.0 ? ? ? ? ? ? 449 GLN A OE1 1 332 A A +ATOM 2659 N NE2 . GLN A 1 332 ? -38.831 9.910 52.686 1.0 96.42 ? ? ? ? ? ? 449 GLN A NE2 1 332 A A +ATOM 2660 N N . LYS A 1 333 ? -35.359 6.525 56.240 1.0 91.95 ? ? ? ? ? ? 450 LYS A N 1 333 A A +ATOM 2661 C CA . LYS A 1 333 ? -34.929 5.718 57.379 1.0 93.47 ? ? ? ? ? ? 450 LYS A CA 1 333 A A +ATOM 2662 C C . LYS A 1 333 ? -34.544 6.559 58.595 1.0 93.85 ? ? ? ? ? ? 450 LYS A C 1 333 A A +ATOM 2663 O O . LYS A 1 333 ? -34.690 6.114 59.736 1.0 94.86 ? ? ? ? ? ? 450 LYS A O 1 333 A A +ATOM 2664 C CB . LYS A 1 333 ? -33.755 4.823 56.976 1.0 90.11 ? ? ? ? ? ? 450 LYS A CB 1 333 A A +ATOM 2665 C CG . LYS A 1 333 ? -32.663 5.538 56.209 1.0 100.0 ? ? ? ? ? ? 450 LYS A CG 1 333 A A +ATOM 2666 C CD . LYS A 1 333 ? -31.726 4.546 55.539 1.0 100.0 ? ? ? ? ? ? 450 LYS A CD 1 333 A A +ATOM 2667 C CE . LYS A 1 333 ? -30.753 5.266 54.623 1.0 100.0 ? ? ? ? ? ? 450 LYS A CE 1 333 A A +ATOM 2668 N NZ . LYS A 1 333 ? -29.790 4.346 53.968 1.0 93.35 ? ? ? ? ? ? 450 LYS A NZ 1 333 A A +ATOM 2669 N N . ILE A 1 334 ? -34.056 7.771 58.352 1.0 95.0 ? ? ? ? ? ? 451 ILE A N 1 334 A A +ATOM 2670 C CA . ILE A 1 334 ? -33.662 8.662 59.434 1.0 89.19 ? ? ? ? ? ? 451 ILE A CA 1 334 A A +ATOM 2671 C C . ILE A 1 334 ? -34.899 9.342 60.029 1.0 90.74 ? ? ? ? ? ? 451 ILE A C 1 334 A A +ATOM 2672 O O . ILE A 1 334 ? -34.813 10.414 60.629 1.0 83.74 ? ? ? ? ? ? 451 ILE A O 1 334 A A +ATOM 2673 C CB . ILE A 1 334 ? -32.639 9.730 58.937 1.0 86.0 ? ? ? ? ? ? 451 ILE A CB 1 334 A A +ATOM 2674 C CG1 . ILE A 1 334 ? -31.788 10.220 60.111 1.0 82.61 ? ? ? ? ? ? 451 ILE A CG1 1 334 A A +ATOM 2675 C CG2 . ILE A 1 334 ? -33.361 10.887 58.262 1.0 67.45 ? ? ? ? ? ? 451 ILE A CG2 1 334 A A +ATOM 2676 C CD1 . ILE A 1 334 ? -30.458 10.809 59.692 1.0 62.56 ? ? ? ? ? ? 451 ILE A CD1 1 334 A A +ATOM 2677 N N . LYS A 1 335 ? -36.051 8.701 59.852 1.0 92.93 ? ? ? ? ? ? 452 LYS A N 1 335 A A +ATOM 2678 C CA . LYS A 1 335 ? -37.329 9.192 60.367 1.0 99.91 ? ? ? ? ? ? 452 LYS A CA 1 335 A A +ATOM 2679 C C . LYS A 1 335 ? -37.757 10.585 59.890 1.0 100.0 ? ? ? ? ? ? 452 LYS A C 1 335 A A +ATOM 2680 O O . LYS A 1 335 ? -38.932 10.941 60.140 1.0 100.0 ? ? ? ? ? ? 452 LYS A O 1 335 A A +ATOM 2681 C CB . LYS A 1 335 ? -37.311 9.161 61.897 1.0 94.91 ? ? ? ? ? ? 452 LYS A CB 1 335 A A +ATOM 2682 C CG . LYS A 1 335 ? -37.685 7.815 62.482 1.0 87.47 ? ? ? ? ? ? 452 LYS A CG 1 335 A A +ATOM 2683 C CD . LYS A 1 335 ? -39.163 7.524 62.282 1.0 100.0 ? ? ? ? ? ? 452 LYS A CD 1 335 A A +ATOM 2684 C CE . LYS A 1 335 ? -39.509 6.114 62.732 1.0 99.94 ? ? ? ? ? ? 452 LYS A CE 1 335 A A +ATOM 2685 N NZ . LYS A 1 335 ? -39.007 5.096 61.768 1.0 100.0 ? ? ? ? ? ? 452 LYS A NZ 1 335 A A +ATOM 2686 O OXT . LYS A 1 335 ? -36.930 11.299 59.282 1.0 100.0 ? ? ? ? ? ? 452 LYS A OXT 1 335 A A +ATOM 2687 N N . VAL AA 1 1 ? -22.538 -4.850 65.230 1.0 56.51 ? ? ? ? ? ? 118 VAL AA N 1 1 A A +ATOM 2688 C CA . VAL AA 1 1 ? -22.321 -4.715 63.756 1.0 59.09 ? ? ? ? ? ? 118 VAL AA CA 1 1 A A +ATOM 2689 C C . VAL AA 1 1 ? -21.131 -5.554 63.300 1.0 44.63 ? ? ? ? ? ? 118 VAL AA C 1 1 A A +ATOM 2690 O O . VAL AA 1 1 ? -20.019 -5.385 63.796 1.0 59.84 ? ? ? ? ? ? 118 VAL AA O 1 1 A A +ATOM 2691 C CB . VAL AA 1 1 ? -22.057 -3.245 63.362 1.0 53.9 ? ? ? ? ? ? 118 VAL AA CB 1 1 A A +ATOM 2692 C CG1 . VAL AA 1 1 ? -21.759 -3.147 61.874 1.0 24.03 ? ? ? ? ? ? 118 VAL AA CG1 1 1 A A +ATOM 2693 C CG2 . VAL AA 1 1 ? -23.262 -2.397 63.713 1.0 72.82 ? ? ? ? ? ? 118 VAL AA CG2 1 1 A A +ATOM 2694 N N . PRO AA 1 2 ? -21.347 -6.447 62.317 1.0 27.43 ? ? ? ? ? ? 119 PRO AA N 1 2 A A +ATOM 2695 C CA . PRO AA 1 2 ? -20.278 -7.310 61.805 1.0 20.13 ? ? ? ? ? ? 119 PRO AA CA 1 2 A A +ATOM 2696 C C . PRO AA 1 2 ? -19.036 -6.529 61.412 1.0 30.85 ? ? ? ? ? ? 119 PRO AA C 1 2 A A +ATOM 2697 O O . PRO AA 1 2 ? -19.125 -5.375 61.001 1.0 42.83 ? ? ? ? ? ? 119 PRO AA O 1 2 A A +ATOM 2698 C CB . PRO AA 1 2 ? -20.914 -8.010 60.606 1.0 7.28 ? ? ? ? ? ? 119 PRO AA CB 1 2 A A +ATOM 2699 C CG . PRO AA 1 2 ? -22.367 -7.930 60.841 1.0 31.66 ? ? ? ? ? ? 119 PRO AA CG 1 2 A A +ATOM 2700 C CD . PRO AA 1 2 ? -22.614 -6.664 61.603 1.0 41.73 ? ? ? ? ? ? 119 PRO AA CD 1 2 A A +ATOM 2701 N N . TRP AA 1 3 ? -17.879 -7.169 61.536 1.0 36.51 ? ? ? ? ? ? 120 TRP AA N 1 3 A A +ATOM 2702 C CA . TRP AA 1 3 ? -16.617 -6.537 61.179 1.0 33.96 ? ? ? ? ? ? 120 TRP AA CA 1 3 A A +ATOM 2703 C C . TRP AA 1 3 ? -16.405 -6.614 59.673 1.0 42.42 ? ? ? ? ? ? 120 TRP AA C 1 3 A A +ATOM 2704 O O . TRP AA 1 3 ? -16.697 -7.636 59.050 1.0 43.61 ? ? ? ? ? ? 120 TRP AA O 1 3 A A +ATOM 2705 C CB . TRP AA 1 3 ? -15.448 -7.233 61.891 1.0 27.89 ? ? ? ? ? ? 120 TRP AA CB 1 3 A A +ATOM 2706 C CG . TRP AA 1 3 ? -14.091 -6.750 61.440 1.0 23.25 ? ? ? ? ? ? 120 TRP AA CG 1 3 A A +ATOM 2707 C CD1 . TRP AA 1 3 ? -13.322 -5.792 62.038 1.0 45.51 ? ? ? ? ? ? 120 TRP AA CD1 1 3 A A +ATOM 2708 C CD2 . TRP AA 1 3 ? -13.360 -7.182 60.282 1.0 22.82 ? ? ? ? ? ? 120 TRP AA CD2 1 3 A A +ATOM 2709 N NE1 . TRP AA 1 3 ? -12.161 -5.596 61.323 1.0 46.58 ? ? ? ? ? ? 120 TRP AA NE1 1 3 A A +ATOM 2710 C CE2 . TRP AA 1 3 ? -12.161 -6.439 60.241 1.0 27.53 ? ? ? ? ? ? 120 TRP AA CE2 1 3 A A +ATOM 2711 C CE3 . TRP AA 1 3 ? -13.607 -8.120 59.269 1.0 15.24 ? ? ? ? ? ? 120 TRP AA CE3 1 3 A A +ATOM 2712 C CZ2 . TRP AA 1 3 ? -11.206 -6.608 59.233 1.0 36.09 ? ? ? ? ? ? 120 TRP AA CZ2 1 3 A A +ATOM 2713 C CZ3 . TRP AA 1 3 ? -12.654 -8.292 58.269 1.0 30.46 ? ? ? ? ? ? 120 TRP AA CZ3 1 3 A A +ATOM 2714 C CH2 . TRP AA 1 3 ? -11.472 -7.536 58.257 1.0 36.66 ? ? ? ? ? ? 120 TRP AA CH2 1 3 A A +ATOM 2715 N N . PHE AA 1 4 ? -15.902 -5.527 59.094 1.0 36.52 ? ? ? ? ? ? 121 PHE AA N 1 4 A A +ATOM 2716 C CA . PHE AA 1 4 ? -15.626 -5.479 57.663 1.0 34.42 ? ? ? ? ? ? 121 PHE AA CA 1 4 A A +ATOM 2717 C C . PHE AA 1 4 ? -14.305 -4.769 57.390 1.0 36.94 ? ? ? ? ? ? 121 PHE AA C 1 4 A A +ATOM 2718 O O . PHE AA 1 4 ? -13.883 -3.899 58.161 1.0 28.54 ? ? ? ? ? ? 121 PHE AA O 1 4 A A +ATOM 2719 C CB . PHE AA 1 4 ? -16.766 -4.783 56.909 1.0 43.63 ? ? ? ? ? ? 121 PHE AA CB 1 4 A A +ATOM 2720 C CG . PHE AA 1 4 ? -16.963 -3.348 57.291 1.0 43.79 ? ? ? ? ? ? 121 PHE AA CG 1 4 A A +ATOM 2721 C CD1 . PHE AA 1 4 ? -16.204 -2.345 56.695 1.0 49.28 ? ? ? ? ? ? 121 PHE AA CD1 1 4 A A +ATOM 2722 C CD2 . PHE AA 1 4 ? -17.916 -2.994 58.238 1.0 41.43 ? ? ? ? ? ? 121 PHE AA CD2 1 4 A A +ATOM 2723 C CE1 . PHE AA 1 4 ? -16.392 -1.012 57.035 1.0 37.53 ? ? ? ? ? ? 121 PHE AA CE1 1 4 A A +ATOM 2724 C CE2 . PHE AA 1 4 ? -18.112 -1.665 58.584 1.0 43.57 ? ? ? ? ? ? 121 PHE AA CE2 1 4 A A +ATOM 2725 C CZ . PHE AA 1 4 ? -17.346 -0.670 57.980 1.0 44.15 ? ? ? ? ? ? 121 PHE AA CZ 1 4 A A +ATOM 2726 N N . PRO AA 1 5 ? -13.628 -5.144 56.289 1.0 30.16 ? ? ? ? ? ? 122 PRO AA N 1 5 A A +ATOM 2727 C CA . PRO AA 1 5 ? -12.344 -4.543 55.911 1.0 28.65 ? ? ? ? ? ? 122 PRO AA CA 1 5 A A +ATOM 2728 C C . PRO AA 1 5 ? -12.424 -3.068 55.542 1.0 26.18 ? ? ? ? ? ? 122 PRO AA C 1 5 A A +ATOM 2729 O O . PRO AA 1 5 ? -13.270 -2.663 54.754 1.0 40.25 ? ? ? ? ? ? 122 PRO AA O 1 5 A A +ATOM 2730 C CB . PRO AA 1 5 ? -11.872 -5.405 54.742 1.0 24.5 ? ? ? ? ? ? 122 PRO AA CB 1 5 A A +ATOM 2731 C CG . PRO AA 1 5 ? -13.110 -6.003 54.198 1.0 21.8 ? ? ? ? ? ? 122 PRO AA CG 1 5 A A +ATOM 2732 C CD . PRO AA 1 5 ? -14.040 -6.194 55.344 1.0 11.45 ? ? ? ? ? ? 122 PRO AA CD 1 5 A A +ATOM 2733 N N . ARG AA 1 6 ? -11.534 -2.270 56.128 1.0 42.98 ? ? ? ? ? ? 123 ARG AA N 1 6 A A +ATOM 2734 C CA . ARG AA 1 6 ? -11.486 -0.840 55.855 1.0 51.56 ? ? ? ? ? ? 123 ARG AA CA 1 6 A A +ATOM 2735 C C . ARG AA 1 6 ? -10.463 -0.589 54.754 1.0 49.43 ? ? ? ? ? ? 123 ARG AA C 1 6 A A +ATOM 2736 O O . ARG AA 1 6 ? -10.631 0.307 53.930 1.0 52.64 ? ? ? ? ? ? 123 ARG AA O 1 6 A A +ATOM 2737 C CB . ARG AA 1 6 ? -11.082 -0.068 57.115 1.0 79.49 ? ? ? ? ? ? 123 ARG AA CB 1 6 A A +ATOM 2738 C CG . ARG AA 1 6 ? -11.942 -0.365 58.335 1.0 80.86 ? ? ? ? ? ? 123 ARG AA CG 1 6 A A +ATOM 2739 C CD . ARG AA 1 6 ? -13.321 0.251 58.195 1.0 89.46 ? ? ? ? ? ? 123 ARG AA CD 1 6 A A +ATOM 2740 N NE . ARG AA 1 6 ? -13.958 0.457 59.492 1.0 100.0 ? ? ? ? ? ? 123 ARG AA NE 1 6 A A +ATOM 2741 C CZ . ARG AA 1 6 ? -13.876 1.582 60.196 1.0 100.0 ? ? ? ? ? ? 123 ARG AA CZ 1 6 A A +ATOM 2742 N NH1 . ARG AA 1 6 ? -13.180 2.610 59.729 1.0 100.0 ? ? ? ? ? ? 123 ARG AA NH1 1 6 A A +ATOM 2743 N NH2 . ARG AA 1 6 ? -14.490 1.678 61.368 1.0 100.0 ? ? ? ? ? ? 123 ARG AA NH2 1 6 A A +ATOM 2744 N N . THR AA 1 7 ? -9.406 -1.396 54.753 1.0 38.4 ? ? ? ? ? ? 124 THR AA N 1 7 A A +ATOM 2745 C CA . THR AA 1 7 ? -8.342 -1.287 53.763 1.0 39.91 ? ? ? ? ? ? 124 THR AA CA 1 7 A A +ATOM 2746 C C . THR AA 1 7 ? -8.303 -2.526 52.888 1.0 31.37 ? ? ? ? ? ? 124 THR AA C 1 7 A A +ATOM 2747 O O . THR AA 1 7 ? -8.771 -3.598 53.284 1.0 40.84 ? ? ? ? ? ? 124 THR AA O 1 7 A A +ATOM 2748 C CB . THR AA 1 7 ? -6.952 -1.143 54.411 1.0 49.36 ? ? ? ? ? ? 124 THR AA CB 1 7 A A +ATOM 2749 O OG1 . THR AA 1 7 ? -7.004 -0.171 55.459 1.0 66.48 ? ? ? ? ? ? 124 THR AA OG1 1 7 A A +ATOM 2750 C CG2 . THR AA 1 7 ? -5.928 -0.704 53.369 1.0 58.27 ? ? ? ? ? ? 124 THR AA CG2 1 7 A A +ATOM 2751 N N . ILE AA 1 8 ? -7.733 -2.360 51.697 1.0 31.21 ? ? ? ? ? ? 125 ILE AA N 1 8 A A +ATOM 2752 C CA . ILE AA 1 8 ? -7.604 -3.435 50.721 1.0 32.65 ? ? ? ? ? ? 125 ILE AA CA 1 8 A A +ATOM 2753 C C . ILE AA 1 8 ? -6.672 -4.532 51.235 1.0 38.63 ? ? ? ? ? ? 125 ILE AA C 1 8 A A +ATOM 2754 O O . ILE AA 1 8 ? -6.830 -5.709 50.891 1.0 41.02 ? ? ? ? ? ? 125 ILE AA O 1 8 A A +ATOM 2755 C CB . ILE AA 1 8 ? -7.051 -2.899 49.384 1.0 22.18 ? ? ? ? ? ? 125 ILE AA CB 1 8 A A +ATOM 2756 C CG1 . ILE AA 1 8 ? -7.146 -3.977 48.306 1.0 31.62 ? ? ? ? ? ? 125 ILE AA CG1 1 8 A A +ATOM 2757 C CG2 . ILE AA 1 8 ? -5.616 -2.443 49.565 1.0 23.1 ? ? ? ? ? ? 125 ILE AA CG2 1 8 A A +ATOM 2758 C CD1 . ILE AA 1 8 ? -7.222 -3.425 46.893 1.0 42.67 ? ? ? ? ? ? 125 ILE AA CD1 1 8 A A +ATOM 2759 N N . GLN AA 1 9 ? -5.704 -4.141 52.061 1.0 26.14 ? ? ? ? ? ? 126 GLN AA N 1 9 A A +ATOM 2760 C CA . GLN AA 1 9 ? -4.746 -5.086 52.620 1.0 31.21 ? ? ? ? ? ? 126 GLN AA CA 1 9 A A +ATOM 2761 C C . GLN AA 1 9 ? -5.340 -5.858 53.794 1.0 26.0 ? ? ? ? ? ? 126 GLN AA C 1 9 A A +ATOM 2762 O O . GLN AA 1 9 ? -4.764 -6.839 54.260 1.0 35.26 ? ? ? ? ? ? 126 GLN AA O 1 9 A A +ATOM 2763 C CB . GLN AA 1 9 ? -3.486 -4.348 53.079 1.0 52.92 ? ? ? ? ? ? 126 GLN AA CB 1 9 A A +ATOM 2764 C CG . GLN AA 1 9 ? -2.847 -3.479 52.013 1.0 74.24 ? ? ? ? ? ? 126 GLN AA CG 1 9 A A +ATOM 2765 C CD . GLN AA 1 9 ? -3.123 -2.005 52.225 1.0 86.27 ? ? ? ? ? ? 126 GLN AA CD 1 9 A A +ATOM 2766 O OE1 . GLN AA 1 9 ? -3.077 -1.510 53.352 1.0 100.0 ? ? ? ? ? ? 126 GLN AA OE1 1 9 A A +ATOM 2767 N NE2 . GLN AA 1 9 ? -3.407 -1.294 51.141 1.0 91.63 ? ? ? ? ? ? 126 GLN AA NE2 1 9 A A +ATOM 2768 N N . GLU AA 1 10 ? -6.494 -5.400 54.267 1.0 24.99 ? ? ? ? ? ? 127 GLU AA N 1 10 A A +ATOM 2769 C CA . GLU AA 1 10 ? -7.170 -6.032 55.392 1.0 29.2 ? ? ? ? ? ? 127 GLU AA CA 1 10 A A +ATOM 2770 C C . GLU AA 1 10 ? -7.875 -7.318 54.996 1.0 26.32 ? ? ? ? ? ? 127 GLU AA C 1 10 A A +ATOM 2771 O O . GLU AA 1 10 ? -8.444 -8.006 55.840 1.0 34.58 ? ? ? ? ? ? 127 GLU AA O 1 10 A A +ATOM 2772 C CB . GLU AA 1 10 ? -8.177 -5.066 56.005 1.0 29.55 ? ? ? ? ? ? 127 GLU AA CB 1 10 A A +ATOM 2773 C CG . GLU AA 1 10 ? -7.543 -3.842 56.632 1.0 48.32 ? ? ? ? ? ? 127 GLU AA CG 1 10 A A +ATOM 2774 C CD . GLU AA 1 10 ? -8.382 -3.266 57.754 1.0 52.9 ? ? ? ? ? ? 127 GLU AA CD 1 10 A A +ATOM 2775 O OE1 . GLU AA 1 10 ? -9.569 -3.645 57.864 1.0 51.84 ? ? ? ? ? ? 127 GLU AA OE1 1 10 A A +ATOM 2776 O OE2 . GLU AA 1 10 ? -7.855 -2.437 58.528 1.0 41.2 ? ? ? ? ? ? 127 GLU AA OE2 1 10 A A +ATOM 2777 N N . LEU AA 1 11 ? -7.835 -7.632 53.708 1.0 25.59 ? ? ? ? ? ? 128 LEU AA N 1 11 A A +ATOM 2778 C CA . LEU AA 1 11 ? -8.462 -8.843 53.194 1.0 40.76 ? ? ? ? ? ? 128 LEU AA CA 1 11 A A +ATOM 2779 C C . LEU AA 1 11 ? -7.556 -10.036 53.496 1.0 42.92 ? ? ? ? ? ? 128 LEU AA C 1 11 A A +ATOM 2780 O O . LEU AA 1 11 ? -7.882 -11.183 53.187 1.0 43.06 ? ? ? ? ? ? 128 LEU AA O 1 11 A A +ATOM 2781 C CB . LEU AA 1 11 ? -8.678 -8.723 51.679 1.0 57.74 ? ? ? ? ? ? 128 LEU AA CB 1 11 A A +ATOM 2782 C CG . LEU AA 1 11 ? -9.577 -7.585 51.174 1.0 61.98 ? ? ? ? ? ? 128 LEU AA CG 1 11 A A +ATOM 2783 C CD1 . LEU AA 1 11 ? -9.631 -7.609 49.661 1.0 55.34 ? ? ? ? ? ? 128 LEU AA CD1 1 11 A A +ATOM 2784 C CD2 . LEU AA 1 11 ? -10.969 -7.723 51.756 1.0 61.21 ? ? ? ? ? ? 128 LEU AA CD2 1 11 A A +ATOM 2785 N N . ASP AA 1 12 ? -6.408 -9.742 54.100 1.0 30.8 ? ? ? ? ? ? 129 ASP AA N 1 12 A A +ATOM 2786 C CA . ASP AA 1 12 ? -5.433 -10.762 54.454 1.0 26.65 ? ? ? ? ? ? 129 ASP AA CA 1 12 A A +ATOM 2787 C C . ASP AA 1 12 ? -5.952 -11.586 55.609 1.0 34.53 ? ? ? ? ? ? 129 ASP AA C 1 12 A A +ATOM 2788 O O . ASP AA 1 12 ? -5.337 -12.580 56.010 1.0 55.86 ? ? ? ? ? ? 129 ASP AA O 1 12 A A +ATOM 2789 C CB . ASP AA 1 12 ? -4.120 -10.110 54.869 1.0 32.05 ? ? ? ? ? ? 129 ASP AA CB 1 12 A A +ATOM 2790 C CG . ASP AA 1 12 ? -3.398 -9.463 53.715 1.0 37.31 ? ? ? ? ? ? 129 ASP AA CG 1 12 A A +ATOM 2791 O OD1 . ASP AA 1 12 ? -3.730 -9.770 52.553 1.0 22.36 ? ? ? ? ? ? 129 ASP AA OD1 1 12 A A +ATOM 2792 O OD2 . ASP AA 1 12 ? -2.489 -8.648 53.972 1.0 43.85 ? ? ? ? ? ? 129 ASP AA OD2 1 12 A A +ATOM 2793 N N . ARG AA 1 13 ? -7.077 -11.135 56.156 1.0 26.69 ? ? ? ? ? ? 130 ARG AA N 1 13 A A +ATOM 2794 C CA . ARG AA 1 13 ? -7.712 -11.795 57.285 1.0 43.72 ? ? ? ? ? ? 130 ARG AA CA 1 13 A A +ATOM 2795 C C . ARG AA 1 13 ? -8.618 -12.914 56.795 1.0 42.68 ? ? ? ? ? ? 130 ARG AA C 1 13 A A +ATOM 2796 O O . ARG AA 1 13 ? -8.916 -13.851 57.536 1.0 51.14 ? ? ? ? ? ? 130 ARG AA O 1 13 A A +ATOM 2797 C CB . ARG AA 1 13 ? -8.510 -10.774 58.108 1.0 48.35 ? ? ? ? ? ? 130 ARG AA CB 1 13 A A +ATOM 2798 C CG . ARG AA 1 13 ? -7.644 -9.938 59.065 1.0 88.58 ? ? ? ? ? ? 130 ARG AA CG 1 13 A A +ATOM 2799 C CD . ARG AA 1 13 ? -8.473 -9.100 60.047 1.0 100.0 ? ? ? ? ? ? 130 ARG AA CD 1 13 A A +ATOM 2800 N NE . ARG AA 1 13 ? -7.625 -8.340 60.969 1.0 100.0 ? ? ? ? ? ? 130 ARG AA NE 1 13 A A +ATOM 2801 C CZ . ARG AA 1 13 ? -8.006 -7.248 61.631 1.0 90.45 ? ? ? ? ? ? 130 ARG AA CZ 1 13 A A +ATOM 2802 N NH1 . ARG AA 1 13 ? -9.230 -6.768 61.484 1.0 86.66 ? ? ? ? ? ? 130 ARG AA NH1 1 13 A A +ATOM 2803 N NH2 . ARG AA 1 13 ? -7.159 -6.631 62.445 1.0 74.81 ? ? ? ? ? ? 130 ARG AA NH2 1 13 A A +ATOM 2804 N N . PHE AA 1 14 ? -9.047 -12.816 55.541 1.0 47.82 ? ? ? ? ? ? 131 PHE AA N 1 14 A A +ATOM 2805 C CA . PHE AA 1 14 ? -9.907 -13.829 54.941 1.0 49.03 ? ? ? ? ? ? 131 PHE AA CA 1 14 A A +ATOM 2806 C C . PHE AA 1 14 ? -9.112 -15.118 54.758 1.0 48.51 ? ? ? ? ? ? 131 PHE AA C 1 14 A A +ATOM 2807 O O . PHE AA 1 14 ? -9.591 -16.210 55.055 1.0 53.68 ? ? ? ? ? ? 131 PHE AA O 1 14 A A +ATOM 2808 C CB . PHE AA 1 14 ? -10.421 -13.351 53.578 1.0 56.74 ? ? ? ? ? ? 131 PHE AA CB 1 14 A A +ATOM 2809 C CG . PHE AA 1 14 ? -11.409 -12.223 53.658 1.0 54.59 ? ? ? ? ? ? 131 PHE AA CG 1 14 A A +ATOM 2810 C CD1 . PHE AA 1 14 ? -11.687 -11.455 52.533 1.0 67.99 ? ? ? ? ? ? 131 PHE AA CD1 1 14 A A +ATOM 2811 C CD2 . PHE AA 1 14 ? -12.069 -11.932 54.846 1.0 28.7 ? ? ? ? ? ? 131 PHE AA CD2 1 14 A A +ATOM 2812 C CE1 . PHE AA 1 14 ? -12.605 -10.414 52.591 1.0 47.89 ? ? ? ? ? ? 131 PHE AA CE1 1 14 A A +ATOM 2813 C CE2 . PHE AA 1 14 ? -12.988 -10.891 54.911 1.0 49.87 ? ? ? ? ? ? 131 PHE AA CE2 1 14 A A +ATOM 2814 C CZ . PHE AA 1 14 ? -13.257 -10.133 53.780 1.0 43.98 ? ? ? ? ? ? 131 PHE AA CZ 1 14 A A +ATOM 2815 N N . ALA AA 1 15 ? -7.887 -14.981 54.256 1.0 48.67 ? ? ? ? ? ? 132 ALA AA N 1 15 A A +ATOM 2816 C CA . ALA AA 1 15 ? -7.005 -16.120 54.039 1.0 62.55 ? ? ? ? ? ? 132 ALA AA CA 1 15 A A +ATOM 2817 C C . ALA AA 1 15 ? -5.919 -16.074 55.091 1.0 67.09 ? ? ? ? ? ? 132 ALA AA C 1 15 A A +ATOM 2818 O O . ALA AA 1 15 ? -4.735 -16.011 54.778 1.0 80.85 ? ? ? ? ? ? 132 ALA AA O 1 15 A A +ATOM 2819 C CB . ALA AA 1 15 ? -6.394 -16.053 52.652 1.0 75.74 ? ? ? ? ? ? 132 ALA AA CB 1 15 A A +ATOM 2820 N N . ASN AA 1 16 ? -6.328 -16.085 56.352 1.0 70.09 ? ? ? ? ? ? 133 ASN AA N 1 16 A A +ATOM 2821 C CA . ASN AA 1 16 ? -5.396 -16.039 57.468 1.0 77.55 ? ? ? ? ? ? 133 ASN AA CA 1 16 A A +ATOM 2822 C C . ASN AA 1 16 ? -4.455 -17.233 57.423 1.0 84.87 ? ? ? ? ? ? 133 ASN AA C 1 16 A A +ATOM 2823 O O . ASN AA 1 16 ? -3.249 -17.075 57.209 1.0 84.52 ? ? ? ? ? ? 133 ASN AA O 1 16 A A +ATOM 2824 C CB . ASN AA 1 16 ? -6.174 -16.027 58.785 1.0 77.32 ? ? ? ? ? ? 133 ASN AA CB 1 16 A A +ATOM 2825 C CG . ASN AA 1 16 ? -5.297 -15.736 59.980 1.0 93.97 ? ? ? ? ? ? 133 ASN AA CG 1 16 A A +ATOM 2826 O OD1 . ASN AA 1 16 ? -4.518 -14.795 59.983 1.0 100.0 ? ? ? ? ? ? 133 ASN AA OD1 1 16 A A +ATOM 2827 N ND2 . ASN AA 1 16 ? -5.436 -16.555 61.012 1.0 99.59 ? ? ? ? ? ? 133 ASN AA ND2 1 16 A A +ATOM 2828 N N . GLN AA 1 17 ? -5.031 -18.419 57.606 1.0 82.31 ? ? ? ? ? ? 134 GLN AA N 1 17 A A +ATOM 2829 C CA . GLN AA 1 17 ? -4.336 -19.705 57.631 1.0 87.1 ? ? ? ? ? ? 134 GLN AA CA 1 17 A A +ATOM 2830 C C . GLN AA 1 17 ? -5.093 -20.415 58.746 1.0 82.51 ? ? ? ? ? ? 134 GLN AA C 1 17 A A +ATOM 2831 O O . GLN AA 1 17 ? -5.646 -21.499 58.556 1.0 86.33 ? ? ? ? ? ? 134 GLN AA O 1 17 A A +ATOM 2832 C CB . GLN AA 1 17 ? -2.860 -19.548 58.015 1.0 96.7 ? ? ? ? ? ? 134 GLN AA CB 1 17 A A +ATOM 2833 C CG . GLN AA 1 17 ? -2.167 -20.828 58.482 1.0 100.0 ? ? ? ? ? ? 134 GLN AA CG 1 17 A A +ATOM 2834 C CD . GLN AA 1 17 ? -2.584 -22.046 57.681 1.0 100.0 ? ? ? ? ? ? 134 GLN AA CD 1 17 A A +ATOM 2835 O OE1 . GLN AA 1 17 ? -3.487 -22.777 58.078 1.0 100.0 ? ? ? ? ? ? 134 GLN AA OE1 1 17 A A +ATOM 2836 N NE2 . GLN AA 1 17 ? -1.930 -22.269 56.554 1.0 100.0 ? ? ? ? ? ? 134 GLN AA NE2 1 17 A A +ATOM 2837 N N . ILE AA 1 18 ? -5.144 -19.768 59.906 1.0 75.59 ? ? ? ? ? ? 135 ILE AA N 1 18 A A +ATOM 2838 C CA . ILE AA 1 18 ? -5.867 -20.307 61.043 1.0 68.45 ? ? ? ? ? ? 135 ILE AA CA 1 18 A A +ATOM 2839 C C . ILE AA 1 18 ? -7.282 -19.804 60.810 1.0 75.79 ? ? ? ? ? ? 135 ILE AA C 1 18 A A +ATOM 2840 O O . ILE AA 1 18 ? -7.510 -19.004 59.888 1.0 75.72 ? ? ? ? ? ? 135 ILE AA O 1 18 A A +ATOM 2841 C CB . ILE AA 1 18 ? -5.344 -19.744 62.366 1.0 65.37 ? ? ? ? ? ? 135 ILE AA CB 1 18 A A +ATOM 2842 C CG1 . ILE AA 1 18 ? -3.820 -19.876 62.429 1.0 63.4 ? ? ? ? ? ? 135 ILE AA CG1 1 18 A A +ATOM 2843 C CG2 . ILE AA 1 18 ? -5.989 -20.475 63.532 1.0 58.73 ? ? ? ? ? ? 135 ILE AA CG2 1 18 A A +ATOM 2844 C CD1 . ILE AA 1 18 ? -3.201 -19.241 63.634 1.0 63.25 ? ? ? ? ? ? 135 ILE AA CD1 1 18 A A +ATOM 2845 N N . LEU AA 1 19 ? -8.219 -20.276 61.623 1.0 79.56 ? ? ? ? ? ? 136 LEU AA N 1 19 A A +ATOM 2846 C CA . LEU AA 1 19 ? -9.621 -19.875 61.504 1.0 82.0 ? ? ? ? ? ? 136 LEU AA CA 1 19 A A +ATOM 2847 C C . LEU AA 1 19 ? -10.300 -20.535 60.303 1.0 78.51 ? ? ? ? ? ? 136 LEU AA C 1 19 A A +ATOM 2848 O O . LEU AA 1 19 ? -11.046 -19.831 59.607 1.0 77.87 ? ? ? ? ? ? 136 LEU AA O 1 19 A A +ATOM 2849 C CB . LEU AA 1 19 ? -9.728 -18.346 61.390 1.0 62.69 ? ? ? ? ? ? 136 LEU AA CB 1 19 A A +ATOM 2850 C CG . LEU AA 1 19 ? -9.423 -17.440 62.598 1.0 64.59 ? ? ? ? ? ? 136 LEU AA CG 1 19 A A +ATOM 2851 C CD1 . LEU AA 1 19 ? -8.181 -17.889 63.315 1.0 57.81 ? ? ? ? ? ? 136 LEU AA CD1 1 19 A A +ATOM 2852 C CD2 . LEU AA 1 19 ? -9.246 -16.027 62.103 1.0 49.28 ? ? ? ? ? ? 136 LEU AA CD2 1 19 A A +ATOM 2853 N N . ASP AA 1 26 ? -15.268 -34.137 51.586 1.0 84.31 ? ? ? ? ? ? 143 ASP AA N 1 26 A A +ATOM 2854 C CA . ASP AA 1 26 ? -16.637 -34.736 51.565 1.0 99.88 ? ? ? ? ? ? 143 ASP AA CA 1 26 A A +ATOM 2855 C C . ASP AA 1 26 ? -16.753 -35.857 50.541 1.0 98.47 ? ? ? ? ? ? 143 ASP AA C 1 26 A A +ATOM 2856 O O . ASP AA 1 26 ? -16.916 -35.608 49.349 1.0 96.96 ? ? ? ? ? ? 143 ASP AA O 1 26 A A +ATOM 2857 C CB . ASP AA 1 26 ? -17.685 -33.665 51.262 1.0 100.0 ? ? ? ? ? ? 143 ASP AA CB 1 26 A A +ATOM 2858 C CG . ASP AA 1 26 ? -19.009 -33.930 51.963 1.0 100.0 ? ? ? ? ? ? 143 ASP AA CG 1 26 A A +ATOM 2859 O OD1 . ASP AA 1 26 ? -19.160 -35.018 52.565 1.0 100.0 ? ? ? ? ? ? 143 ASP AA OD1 1 26 A A +ATOM 2860 O OD2 . ASP AA 1 26 ? -19.896 -33.051 51.916 1.0 100.0 ? ? ? ? ? ? 143 ASP AA OD2 1 26 A A +ATOM 2861 N N . ALA AA 1 27 ? -16.683 -37.090 51.037 1.0 92.92 ? ? ? ? ? ? 144 ALA AA N 1 27 A A +ATOM 2862 C CA . ALA AA 1 27 ? -16.759 -38.307 50.229 1.0 94.63 ? ? ? ? ? ? 144 ALA AA CA 1 27 A A +ATOM 2863 C C . ALA AA 1 27 ? -17.416 -38.211 48.847 1.0 98.79 ? ? ? ? ? ? 144 ALA AA C 1 27 A A +ATOM 2864 O O . ALA AA 1 27 ? -16.867 -38.718 47.868 1.0 100.0 ? ? ? ? ? ? 144 ALA AA O 1 27 A A +ATOM 2865 C CB . ALA AA 1 27 ? -17.431 -39.408 51.042 1.0 94.11 ? ? ? ? ? ? 144 ALA AA CB 1 27 A A +ATOM 2866 N N . ASP AA 1 28 ? -18.584 -37.580 48.762 1.0 92.37 ? ? ? ? ? ? 145 ASP AA N 1 28 A A +ATOM 2867 C CA . ASP AA 1 28 ? -19.296 -37.456 47.483 1.0 86.15 ? ? ? ? ? ? 145 ASP AA CA 1 28 A A +ATOM 2868 C C . ASP AA 1 28 ? -18.472 -36.695 46.446 1.0 77.55 ? ? ? ? ? ? 145 ASP AA C 1 28 A A +ATOM 2869 O O . ASP AA 1 28 ? -18.755 -36.750 45.248 1.0 75.84 ? ? ? ? ? ? 145 ASP AA O 1 28 A A +ATOM 2870 C CB . ASP AA 1 28 ? -20.635 -36.745 47.691 1.0 94.52 ? ? ? ? ? ? 145 ASP AA CB 1 28 A A +ATOM 2871 C CG . ASP AA 1 28 ? -20.464 -35.314 48.163 1.0 100.0 ? ? ? ? ? ? 145 ASP AA CG 1 28 A A +ATOM 2872 O OD1 . ASP AA 1 28 ? -19.891 -35.112 49.254 1.0 100.0 ? ? ? ? ? ? 145 ASP AA OD1 1 28 A A +ATOM 2873 O OD2 . ASP AA 1 28 ? -20.902 -34.391 47.444 1.0 100.0 ? ? ? ? ? ? 145 ASP AA OD2 1 28 A A +ATOM 2874 N N . HIS AA 1 29 ? -17.448 -35.992 46.916 1.0 70.06 ? ? ? ? ? ? 146 HIS AA N 1 29 A A +ATOM 2875 C CA . HIS AA 1 29 ? -16.577 -35.208 46.049 1.0 70.17 ? ? ? ? ? ? 146 HIS AA CA 1 29 A A +ATOM 2876 C C . HIS AA 1 29 ? -15.688 -36.102 45.195 1.0 66.1 ? ? ? ? ? ? 146 HIS AA C 1 29 A A +ATOM 2877 O O . HIS AA 1 29 ? -14.947 -36.937 45.711 1.0 69.28 ? ? ? ? ? ? 146 HIS AA O 1 29 A A +ATOM 2878 C CB . HIS AA 1 29 ? -15.707 -34.271 46.893 1.0 88.83 ? ? ? ? ? ? 146 HIS AA CB 1 29 A A +ATOM 2879 C CG . HIS AA 1 29 ? -14.765 -33.426 46.092 1.0 92.84 ? ? ? ? ? ? 146 HIS AA CG 1 29 A A +ATOM 2880 N ND1 . HIS AA 1 29 ? -13.702 -33.952 45.390 1.0 78.79 ? ? ? ? ? ? 146 HIS AA ND1 1 29 A A +ATOM 2881 C CD2 . HIS AA 1 29 ? -14.715 -32.085 45.899 1.0 92.7 ? ? ? ? ? ? 146 HIS AA CD2 1 29 A A +ATOM 2882 C CE1 . HIS AA 1 29 ? -13.038 -32.974 44.800 1.0 79.37 ? ? ? ? ? ? 146 HIS AA CE1 1 29 A A +ATOM 2883 N NE2 . HIS AA 1 29 ? -13.633 -31.831 45.093 1.0 85.27 ? ? ? ? ? ? 146 HIS AA NE2 1 29 A A +ATOM 2884 N N . PRO AA 1 30 ? -15.756 -35.933 43.865 1.0 72.24 ? ? ? ? ? ? 147 PRO AA N 1 30 A A +ATOM 2885 C CA . PRO AA 1 30 ? -14.936 -36.747 42.961 1.0 76.33 ? ? ? ? ? ? 147 PRO AA CA 1 30 A A +ATOM 2886 C C . PRO AA 1 30 ? -13.455 -36.449 43.170 1.0 83.68 ? ? ? ? ? ? 147 PRO AA C 1 30 A A +ATOM 2887 O O . PRO AA 1 30 ? -13.014 -35.309 43.034 1.0 100.0 ? ? ? ? ? ? 147 PRO AA O 1 30 A A +ATOM 2888 C CB . PRO AA 1 30 ? -15.427 -36.351 41.567 1.0 80.01 ? ? ? ? ? ? 147 PRO AA CB 1 30 A A +ATOM 2889 C CG . PRO AA 1 30 ? -16.046 -35.008 41.749 1.0 83.34 ? ? ? ? ? ? 147 PRO AA CG 1 30 A A +ATOM 2890 C CD . PRO AA 1 30 ? -16.595 -34.966 43.140 1.0 79.41 ? ? ? ? ? ? 147 PRO AA CD 1 30 A A +ATOM 2891 N N . GLY AA 1 31 ? -12.692 -37.481 43.513 1.0 76.43 ? ? ? ? ? ? 148 GLY AA N 1 31 A A +ATOM 2892 C CA . GLY AA 1 31 ? -11.273 -37.299 43.751 1.0 74.5 ? ? ? ? ? ? 148 GLY AA CA 1 31 A A +ATOM 2893 C C . GLY AA 1 31 ? -10.947 -37.352 45.231 1.0 68.35 ? ? ? ? ? ? 148 GLY AA C 1 31 A A +ATOM 2894 O O . GLY AA 1 31 ? -9.801 -37.151 45.633 1.0 69.42 ? ? ? ? ? ? 148 GLY AA O 1 31 A A +ATOM 2895 N N . PHE AA 1 32 ? -11.967 -37.614 46.043 1.0 66.68 ? ? ? ? ? ? 149 PHE AA N 1 32 A A +ATOM 2896 C CA . PHE AA 1 32 ? -11.804 -37.705 47.489 1.0 79.1 ? ? ? ? ? ? 149 PHE AA CA 1 32 A A +ATOM 2897 C C . PHE AA 1 32 ? -10.903 -38.883 47.841 1.0 85.64 ? ? ? ? ? ? 149 PHE AA C 1 32 A A +ATOM 2898 O O . PHE AA 1 32 ? -10.169 -38.846 48.827 1.0 87.84 ? ? ? ? ? ? 149 PHE AA O 1 32 A A +ATOM 2899 C CB . PHE AA 1 32 ? -13.177 -37.876 48.155 1.0 86.78 ? ? ? ? ? ? 149 PHE AA CB 1 32 A A +ATOM 2900 C CG . PHE AA 1 32 ? -13.119 -38.127 49.641 1.0 93.25 ? ? ? ? ? ? 149 PHE AA CG 1 32 A A +ATOM 2901 C CD1 . PHE AA 1 32 ? -12.825 -37.094 50.527 1.0 94.59 ? ? ? ? ? ? 149 PHE AA CD1 1 32 A A +ATOM 2902 C CD2 . PHE AA 1 32 ? -13.386 -39.391 50.156 1.0 96.74 ? ? ? ? ? ? 149 PHE AA CD2 1 32 A A +ATOM 2903 C CE1 . PHE AA 1 32 ? -12.802 -37.316 51.905 1.0 84.73 ? ? ? ? ? ? 149 PHE AA CE1 1 32 A A +ATOM 2904 C CE2 . PHE AA 1 32 ? -13.365 -39.622 51.533 1.0 92.82 ? ? ? ? ? ? 149 PHE AA CE2 1 32 A A +ATOM 2905 C CZ . PHE AA 1 32 ? -13.071 -38.583 52.406 1.0 85.29 ? ? ? ? ? ? 149 PHE AA CZ 1 32 A A +ATOM 2906 N N . LYS AA 1 33 ? -10.958 -39.924 47.017 1.0 87.59 ? ? ? ? ? ? 150 LYS AA N 1 33 A A +ATOM 2907 C CA . LYS AA 1 33 ? -10.163 -41.125 47.236 1.0 76.77 ? ? ? ? ? ? 150 LYS AA CA 1 33 A A +ATOM 2908 C C . LYS AA 1 33 ? -8.776 -41.014 46.608 1.0 78.87 ? ? ? ? ? ? 150 LYS AA C 1 33 A A +ATOM 2909 O O . LYS AA 1 33 ? -7.929 -41.883 46.805 1.0 83.74 ? ? ? ? ? ? 150 LYS AA O 1 33 A A +ATOM 2910 C CB . LYS AA 1 33 ? -10.905 -42.333 46.664 1.0 86.37 ? ? ? ? ? ? 150 LYS AA CB 1 33 A A +ATOM 2911 C CG . LYS AA 1 33 ? -12.398 -42.315 46.980 1.0 90.4 ? ? ? ? ? ? 150 LYS AA CG 1 33 A A +ATOM 2912 C CD . LYS AA 1 33 ? -13.110 -43.571 46.504 1.0 100.0 ? ? ? ? ? ? 150 LYS AA CD 1 33 A A +ATOM 2913 C CE . LYS AA 1 33 ? -14.488 -43.690 47.148 1.0 100.0 ? ? ? ? ? ? 150 LYS AA CE 1 33 A A +ATOM 2914 N NZ . LYS AA 1 33 ? -15.192 -44.951 46.772 1.0 100.0 ? ? ? ? ? ? 150 LYS AA NZ 1 33 A A +ATOM 2915 N N . ASP AA 1 34 ? -8.542 -39.937 45.862 1.0 82.59 ? ? ? ? ? ? 151 ASP AA N 1 34 A A +ATOM 2916 C CA . ASP AA 1 34 ? -7.254 -39.732 45.212 1.0 81.68 ? ? ? ? ? ? 151 ASP AA CA 1 34 A A +ATOM 2917 C C . ASP AA 1 34 ? -6.257 -39.026 46.123 1.0 75.99 ? ? ? ? ? ? 151 ASP AA C 1 34 A A +ATOM 2918 O O . ASP AA 1 34 ? -6.363 -37.825 46.362 1.0 80.97 ? ? ? ? ? ? 151 ASP AA O 1 34 A A +ATOM 2919 C CB . ASP AA 1 34 ? -7.420 -38.925 43.924 1.0 81.66 ? ? ? ? ? ? 151 ASP AA CB 1 34 A A +ATOM 2920 C CG . ASP AA 1 34 ? -6.161 -38.916 43.083 1.0 87.43 ? ? ? ? ? ? 151 ASP AA CG 1 34 A A +ATOM 2921 O OD1 . ASP AA 1 34 ? -5.056 -38.817 43.661 1.0 84.99 ? ? ? ? ? ? 151 ASP AA OD1 1 34 A A +ATOM 2922 O OD2 . ASP AA 1 34 ? -6.272 -39.007 41.844 1.0 100.0 ? ? ? ? ? ? 151 ASP AA OD2 1 34 A A +ATOM 2923 N N . PRO AA 1 35 ? -5.260 -39.770 46.626 1.0 70.56 ? ? ? ? ? ? 152 PRO AA N 1 35 A A +ATOM 2924 C CA . PRO AA 1 35 ? -4.230 -39.227 47.518 1.0 76.86 ? ? ? ? ? ? 152 PRO AA CA 1 35 A A +ATOM 2925 C C . PRO AA 1 35 ? -3.374 -38.130 46.891 1.0 79.85 ? ? ? ? ? ? 152 PRO AA C 1 35 A A +ATOM 2926 O O . PRO AA 1 35 ? -2.890 -37.240 47.591 1.0 82.69 ? ? ? ? ? ? 152 PRO AA O 1 35 A A +ATOM 2927 C CB . PRO AA 1 35 ? -3.395 -40.448 47.906 1.0 87.13 ? ? ? ? ? ? 152 PRO AA CB 1 35 A A +ATOM 2928 C CG . PRO AA 1 35 ? -4.201 -41.636 47.487 1.0 88.74 ? ? ? ? ? ? 152 PRO AA CG 1 35 A A +ATOM 2929 C CD . PRO AA 1 35 ? -5.042 -41.194 46.341 1.0 82.23 ? ? ? ? ? ? 152 PRO AA CD 1 35 A A +ATOM 2930 N N . VAL AA 1 36 ? -3.179 -38.197 45.576 1.0 81.47 ? ? ? ? ? ? 153 VAL AA N 1 36 A A +ATOM 2931 C CA . VAL AA 1 36 ? -2.375 -37.195 44.883 1.0 88.21 ? ? ? ? ? ? 153 VAL AA CA 1 36 A A +ATOM 2932 C C . VAL AA 1 36 ? -3.178 -35.907 44.739 1.0 90.32 ? ? ? ? ? ? 153 VAL AA C 1 36 A A +ATOM 2933 O O . VAL AA 1 36 ? -2.873 -34.900 45.377 1.0 87.73 ? ? ? ? ? ? 153 VAL AA O 1 36 A A +ATOM 2934 C CB . VAL AA 1 36 ? -1.938 -37.683 43.475 1.0 82.85 ? ? ? ? ? ? 153 VAL AA CB 1 36 A A +ATOM 2935 C CG1 . VAL AA 1 36 ? -1.418 -36.509 42.645 1.0 91.99 ? ? ? ? ? ? 153 VAL AA CG1 1 36 A A +ATOM 2936 C CG2 . VAL AA 1 36 ? -0.858 -38.741 43.605 1.0 86.49 ? ? ? ? ? ? 153 VAL AA CG2 1 36 A A +ATOM 2937 N N . TYR AA 1 37 ? -4.205 -35.952 43.896 1.0 95.5 ? ? ? ? ? ? 154 TYR AA N 1 37 A A +ATOM 2938 C CA . TYR AA 1 37 ? -5.074 -34.805 43.652 1.0 92.74 ? ? ? ? ? ? 154 TYR AA CA 1 37 A A +ATOM 2939 C C . TYR AA 1 37 ? -5.424 -34.150 44.979 1.0 80.78 ? ? ? ? ? ? 154 TYR AA C 1 37 A A +ATOM 2940 O O . TYR AA 1 37 ? -5.501 -32.927 45.087 1.0 79.24 ? ? ? ? ? ? 154 TYR AA O 1 37 A A +ATOM 2941 C CB . TYR AA 1 37 ? -6.346 -35.271 42.933 1.0 100.0 ? ? ? ? ? ? 154 TYR AA CB 1 37 A A +ATOM 2942 C CG . TYR AA 1 37 ? -7.467 -34.257 42.881 1.0 100.0 ? ? ? ? ? ? 154 TYR AA CG 1 37 A A +ATOM 2943 C CD1 . TYR AA 1 37 ? -7.321 -33.057 42.184 1.0 98.95 ? ? ? ? ? ? 154 TYR AA CD1 1 37 A A +ATOM 2944 C CD2 . TYR AA 1 37 ? -8.687 -34.511 43.508 1.0 92.2 ? ? ? ? ? ? 154 TYR AA CD2 1 37 A A +ATOM 2945 C CE1 . TYR AA 1 37 ? -8.365 -32.136 42.111 1.0 94.85 ? ? ? ? ? ? 154 TYR AA CE1 1 37 A A +ATOM 2946 C CE2 . TYR AA 1 37 ? -9.735 -33.596 43.442 1.0 95.72 ? ? ? ? ? ? 154 TYR AA CE2 1 37 A A +ATOM 2947 C CZ . TYR AA 1 37 ? -9.569 -32.414 42.741 1.0 95.18 ? ? ? ? ? ? 154 TYR AA CZ 1 37 A A +ATOM 2948 O OH . TYR AA 1 37 ? -10.610 -31.521 42.665 1.0 100.0 ? ? ? ? ? ? 154 TYR AA OH 1 37 A A +ATOM 2949 N N . ARG AA 1 38 ? -5.632 -34.984 45.987 1.0 62.91 ? ? ? ? ? ? 155 ARG AA N 1 38 A A +ATOM 2950 C CA . ARG AA 1 38 ? -5.958 -34.509 47.321 1.0 59.41 ? ? ? ? ? ? 155 ARG AA CA 1 38 A A +ATOM 2951 C C . ARG AA 1 38 ? -4.854 -33.575 47.816 1.0 55.79 ? ? ? ? ? ? 155 ARG AA C 1 38 A A +ATOM 2952 O O . ARG AA 1 38 ? -5.087 -32.387 48.051 1.0 65.02 ? ? ? ? ? ? 155 ARG AA O 1 38 A A +ATOM 2953 C CB . ARG AA 1 38 ? -6.087 -35.698 48.268 1.0 59.75 ? ? ? ? ? ? 155 ARG AA CB 1 38 A A +ATOM 2954 C CG . ARG AA 1 38 ? -6.873 -35.428 49.527 1.0 68.07 ? ? ? ? ? ? 155 ARG AA CG 1 38 A A +ATOM 2955 C CD . ARG AA 1 38 ? -6.924 -36.680 50.375 1.0 79.8 ? ? ? ? ? ? 155 ARG AA CD 1 38 A A +ATOM 2956 N NE . ARG AA 1 38 ? -7.586 -36.463 51.656 1.0 93.15 ? ? ? ? ? ? 155 ARG AA NE 1 38 A A +ATOM 2957 C CZ . ARG AA 1 38 ? -8.735 -37.033 52.004 1.0 98.65 ? ? ? ? ? ? 155 ARG AA CZ 1 38 A A +ATOM 2958 N NH1 . ARG AA 1 38 ? -9.349 -37.853 51.164 1.0 99.79 ? ? ? ? ? ? 155 ARG AA NH1 1 38 A A +ATOM 2959 N NH2 . ARG AA 1 38 ? -9.266 -36.792 53.196 1.0 100.0 ? ? ? ? ? ? 155 ARG AA NH2 1 38 A A +ATOM 2960 N N . ALA AA 1 39 ? -3.653 -34.125 47.976 1.0 47.55 ? ? ? ? ? ? 156 ALA AA N 1 39 A A +ATOM 2961 C CA . ALA AA 1 39 ? -2.502 -33.363 48.448 1.0 43.67 ? ? ? ? ? ? 156 ALA AA CA 1 39 A A +ATOM 2962 C C . ALA AA 1 39 ? -2.146 -32.245 47.476 1.0 48.1 ? ? ? ? ? ? 156 ALA AA C 1 39 A A +ATOM 2963 O O . ALA AA 1 39 ? -1.441 -31.298 47.828 1.0 40.44 ? ? ? ? ? ? 156 ALA AA O 1 39 A A +ATOM 2964 C CB . ALA AA 1 39 ? -1.312 -34.288 48.636 1.0 58.64 ? ? ? ? ? ? 156 ALA AA CB 1 39 A A +ATOM 2965 N N . ARG AA 1 40 ? -2.617 -32.370 46.241 1.0 52.11 ? ? ? ? ? ? 157 ARG AA N 1 40 A A +ATOM 2966 C CA . ARG AA 1 40 ? -2.356 -31.354 45.236 1.0 51.03 ? ? ? ? ? ? 157 ARG AA CA 1 40 A A +ATOM 2967 C C . ARG AA 1 40 ? -3.228 -30.146 45.561 1.0 53.36 ? ? ? ? ? ? 157 ARG AA C 1 40 A A +ATOM 2968 O O . ARG AA 1 40 ? -2.754 -29.010 45.553 1.0 43.4 ? ? ? ? ? ? 157 ARG AA O 1 40 A A +ATOM 2969 C CB . ARG AA 1 40 ? -2.697 -31.885 43.840 1.0 38.02 ? ? ? ? ? ? 157 ARG AA CB 1 40 A A +ATOM 2970 C CG . ARG AA 1 40 ? -2.694 -30.832 42.753 1.0 41.41 ? ? ? ? ? ? 157 ARG AA CG 1 40 A A +ATOM 2971 C CD . ARG AA 1 40 ? -1.291 -30.588 42.251 1.0 44.18 ? ? ? ? ? ? 157 ARG AA CD 1 40 A A +ATOM 2972 N NE . ARG AA 1 40 ? -1.283 -29.942 40.942 1.0 39.11 ? ? ? ? ? ? 157 ARG AA NE 1 40 A A +ATOM 2973 C CZ . ARG AA 1 40 ? -0.245 -29.273 40.447 1.0 47.49 ? ? ? ? ? ? 157 ARG AA CZ 1 40 A A +ATOM 2974 N NH1 . ARG AA 1 40 ? 0.874 -29.162 41.153 1.0 44.14 ? ? ? ? ? ? 157 ARG AA NH1 1 40 A A +ATOM 2975 N NH2 . ARG AA 1 40 ? -0.325 -28.716 39.247 1.0 31.56 ? ? ? ? ? ? 157 ARG AA NH2 1 40 A A +ATOM 2976 N N . ARG AA 1 41 ? -4.500 -30.408 45.861 1.0 46.66 ? ? ? ? ? ? 158 ARG AA N 1 41 A A +ATOM 2977 C CA . ARG AA 1 41 ? -5.456 -29.352 46.184 1.0 53.07 ? ? ? ? ? ? 158 ARG AA CA 1 41 A A +ATOM 2978 C C . ARG AA 1 41 ? -5.148 -28.698 47.523 1.0 50.94 ? ? ? ? ? ? 158 ARG AA C 1 41 A A +ATOM 2979 O O . ARG AA 1 41 ? -5.648 -27.616 47.822 1.0 77.16 ? ? ? ? ? ? 158 ARG AA O 1 41 A A +ATOM 2980 C CB . ARG AA 1 41 ? -6.880 -29.913 46.193 1.0 58.71 ? ? ? ? ? ? 158 ARG AA CB 1 41 A A +ATOM 2981 C CG . ARG AA 1 41 ? -7.960 -28.840 46.202 1.0 73.28 ? ? ? ? ? ? 158 ARG AA CG 1 41 A A +ATOM 2982 C CD . ARG AA 1 41 ? -9.299 -29.386 45.738 1.0 52.26 ? ? ? ? ? ? 158 ARG AA CD 1 41 A A +ATOM 2983 N NE . ARG AA 1 41 ? -10.412 -28.576 46.228 1.0 66.0 ? ? ? ? ? ? 158 ARG AA NE 1 41 A A +ATOM 2984 C CZ . ARG AA 1 41 ? -11.661 -28.671 45.784 1.0 73.11 ? ? ? ? ? ? 158 ARG AA CZ 1 41 A A +ATOM 2985 N NH1 . ARG AA 1 41 ? -11.967 -29.541 44.833 1.0 77.08 ? ? ? ? ? ? 158 ARG AA NH1 1 41 A A +ATOM 2986 N NH2 . ARG AA 1 41 ? -12.608 -27.888 46.285 1.0 79.76 ? ? ? ? ? ? 158 ARG AA NH2 1 41 A A +ATOM 2987 N N . LYS AA 1 42 ? -4.339 -29.371 48.332 1.0 46.7 ? ? ? ? ? ? 159 LYS AA N 1 42 A A +ATOM 2988 C CA . LYS AA 1 42 ? -3.941 -28.848 49.634 1.0 49.83 ? ? ? ? ? ? 159 LYS AA CA 1 42 A A +ATOM 2989 C C . LYS AA 1 42 ? -2.714 -27.983 49.388 1.0 46.38 ? ? ? ? ? ? 159 LYS AA C 1 42 A A +ATOM 2990 O O . LYS AA 1 42 ? -2.374 -27.106 50.178 1.0 52.99 ? ? ? ? ? ? 159 LYS AA O 1 42 A A +ATOM 2991 C CB . LYS AA 1 42 ? -3.587 -29.996 50.578 1.0 70.21 ? ? ? ? ? ? 159 LYS AA CB 1 42 A A +ATOM 2992 C CG . LYS AA 1 42 ? -2.959 -29.554 51.884 1.0 82.3 ? ? ? ? ? ? 159 LYS AA CG 1 42 A A +ATOM 2993 C CD . LYS AA 1 42 ? -2.756 -30.739 52.811 1.0 91.14 ? ? ? ? ? ? 159 LYS AA CD 1 42 A A +ATOM 2994 C CE . LYS AA 1 42 ? -2.337 -30.296 54.205 1.0 92.35 ? ? ? ? ? ? 159 LYS AA CE 1 42 A A +ATOM 2995 N NZ . LYS AA 1 42 ? -2.312 -31.440 55.162 1.0 100.0 ? ? ? ? ? ? 159 LYS AA NZ 1 42 A A +ATOM 2996 N N . GLN AA 1 43 ? -2.057 -28.256 48.268 1.0 40.78 ? ? ? ? ? ? 160 GLN AA N 1 43 A A +ATOM 2997 C CA . GLN AA 1 43 ? -0.869 -27.538 47.840 1.0 42.9 ? ? ? ? ? ? 160 GLN AA CA 1 43 A A +ATOM 2998 C C . GLN AA 1 43 ? -1.321 -26.160 47.391 1.0 45.11 ? ? ? ? ? ? 160 GLN AA C 1 43 A A +ATOM 2999 O O . GLN AA 1 43 ? -0.712 -25.141 47.719 1.0 54.18 ? ? ? ? ? ? 160 GLN AA O 1 43 A A +ATOM 3000 C CB . GLN AA 1 43 ? -0.239 -28.282 46.667 1.0 52.45 ? ? ? ? ? ? 160 GLN AA CB 1 43 A A +ATOM 3001 C CG . GLN AA 1 43 ? 1.162 -27.878 46.328 1.0 46.55 ? ? ? ? ? ? 160 GLN AA CG 1 43 A A +ATOM 3002 C CD . GLN AA 1 43 ? 1.789 -28.849 45.361 1.0 56.61 ? ? ? ? ? ? 160 GLN AA CD 1 43 A A +ATOM 3003 O OE1 . GLN AA 1 43 ? 1.100 -29.675 44.763 1.0 57.95 ? ? ? ? ? ? 160 GLN AA OE1 1 43 A A +ATOM 3004 N NE2 . GLN AA 1 43 ? 3.102 -28.766 45.205 1.0 56.32 ? ? ? ? ? ? 160 GLN AA NE2 1 43 A A +ATOM 3005 N N . PHE AA 1 44 ? -2.403 -26.149 46.624 1.0 45.78 ? ? ? ? ? ? 161 PHE AA N 1 44 A A +ATOM 3006 C CA . PHE AA 1 44 ? -2.969 -24.915 46.115 1.0 51.09 ? ? ? ? ? ? 161 PHE AA CA 1 44 A A +ATOM 3007 C C . PHE AA 1 44 ? -3.456 -24.057 47.285 1.0 55.48 ? ? ? ? ? ? 161 PHE AA C 1 44 A A +ATOM 3008 O O . PHE AA 1 44 ? -3.119 -22.876 47.379 1.0 55.24 ? ? ? ? ? ? 161 PHE AA O 1 44 A A +ATOM 3009 C CB . PHE AA 1 44 ? -4.134 -25.224 45.168 1.0 49.99 ? ? ? ? ? ? 161 PHE AA CB 1 44 A A +ATOM 3010 C CG . PHE AA 1 44 ? -3.706 -25.728 43.815 1.0 43.25 ? ? ? ? ? ? 161 PHE AA CG 1 44 A A +ATOM 3011 C CD1 . PHE AA 1 44 ? -4.178 -26.943 43.334 1.0 52.12 ? ? ? ? ? ? 161 PHE AA CD1 1 44 A A +ATOM 3012 C CD2 . PHE AA 1 44 ? -2.841 -24.983 43.017 1.0 46.64 ? ? ? ? ? ? 161 PHE AA CD2 1 44 A A +ATOM 3013 C CE1 . PHE AA 1 44 ? -3.799 -27.413 42.081 1.0 64.08 ? ? ? ? ? ? 161 PHE AA CE1 1 44 A A +ATOM 3014 C CE2 . PHE AA 1 44 ? -2.452 -25.443 41.758 1.0 59.01 ? ? ? ? ? ? 161 PHE AA CE2 1 44 A A +ATOM 3015 C CZ . PHE AA 1 44 ? -2.935 -26.661 41.290 1.0 72.77 ? ? ? ? ? ? 161 PHE AA CZ 1 44 A A +ATOM 3016 N N . ALA AA 1 45 ? -4.241 -24.660 48.176 1.0 53.32 ? ? ? ? ? ? 162 ALA AA N 1 45 A A +ATOM 3017 C CA . ALA AA 1 45 ? -4.776 -23.954 49.339 1.0 50.06 ? ? ? ? ? ? 162 ALA AA CA 1 45 A A +ATOM 3018 C C . ALA AA 1 45 ? -3.682 -23.273 50.154 1.0 43.46 ? ? ? ? ? ? 162 ALA AA C 1 45 A A +ATOM 3019 O O . ALA AA 1 45 ? -3.826 -22.121 50.562 1.0 46.93 ? ? ? ? ? ? 162 ALA AA O 1 45 A A +ATOM 3020 C CB . ALA AA 1 45 ? -5.552 -24.921 50.223 1.0 22.2 ? ? ? ? ? ? 162 ALA AA CB 1 45 A A +ATOM 3021 N N . ASP AA 1 46 ? -2.590 -23.991 50.393 1.0 37.62 ? ? ? ? ? ? 163 ASP AA N 1 46 A A +ATOM 3022 C CA . ASP AA 1 46 ? -1.476 -23.455 51.163 1.0 55.82 ? ? ? ? ? ? 163 ASP AA CA 1 46 A A +ATOM 3023 C C . ASP AA 1 46 ? -0.958 -22.189 50.501 1.0 55.29 ? ? ? ? ? ? 163 ASP AA C 1 46 A A +ATOM 3024 O O . ASP AA 1 46 ? -0.558 -21.241 51.180 1.0 55.64 ? ? ? ? ? ? 163 ASP AA O 1 46 A A +ATOM 3025 C CB . ASP AA 1 46 ? -0.349 -24.488 51.258 1.0 73.47 ? ? ? ? ? ? 163 ASP AA CB 1 46 A A +ATOM 3026 C CG . ASP AA 1 46 ? -0.493 -25.405 52.459 1.0 88.52 ? ? ? ? ? ? 163 ASP AA CG 1 46 A A +ATOM 3027 O OD1 . ASP AA 1 46 ? -0.149 -24.979 53.582 1.0 86.66 ? ? ? ? ? ? 163 ASP AA OD1 1 46 A A +ATOM 3028 O OD2 . ASP AA 1 46 ? -0.947 -26.556 52.276 1.0 100.0 ? ? ? ? ? ? 163 ASP AA OD2 1 46 A A +ATOM 3029 N N . ILE AA 1 47 ? -0.956 -22.180 49.171 1.0 54.93 ? ? ? ? ? ? 164 ILE AA N 1 47 A A +ATOM 3030 C CA . ILE AA 1 47 ? -0.493 -21.009 48.431 1.0 54.88 ? ? ? ? ? ? 164 ILE AA CA 1 47 A A +ATOM 3031 C C . ILE AA 1 47 ? -1.328 -19.824 48.896 1.0 49.54 ? ? ? ? ? ? 164 ILE AA C 1 47 A A +ATOM 3032 O O . ILE AA 1 47 ? -0.800 -18.747 49.177 1.0 36.54 ? ? ? ? ? ? 164 ILE AA O 1 47 A A +ATOM 3033 C CB . ILE AA 1 47 ? -0.688 -21.175 46.901 1.0 59.6 ? ? ? ? ? ? 164 ILE AA CB 1 47 A A +ATOM 3034 C CG1 . ILE AA 1 47 ? 0.247 -22.256 46.352 1.0 68.7 ? ? ? ? ? ? 164 ILE AA CG1 1 47 A A +ATOM 3035 C CG2 . ILE AA 1 47 ? -0.396 -19.863 46.199 1.0 56.46 ? ? ? ? ? ? 164 ILE AA CG2 1 47 A A +ATOM 3036 C CD1 . ILE AA 1 47 ? -0.051 -22.655 44.916 1.0 53.83 ? ? ? ? ? ? 164 ILE AA CD1 1 47 A A +ATOM 3037 N N . ALA AA 1 48 ? -2.638 -20.051 48.978 1.0 43.8 ? ? ? ? ? ? 165 ALA AA N 1 48 A A +ATOM 3038 C CA . ALA AA 1 48 ? -3.597 -19.035 49.402 1.0 42.24 ? ? ? ? ? ? 165 ALA AA CA 1 48 A A +ATOM 3039 C C . ALA AA 1 48 ? -3.294 -18.536 50.807 1.0 44.69 ? ? ? ? ? ? 165 ALA AA C 1 48 A A +ATOM 3040 O O . ALA AA 1 48 ? -3.157 -17.336 51.035 1.0 61.71 ? ? ? ? ? ? 165 ALA AA O 1 48 A A +ATOM 3041 C CB . ALA AA 1 48 ? -5.019 -19.603 49.346 1.0 26.07 ? ? ? ? ? ? 165 ALA AA CB 1 48 A A +ATOM 3042 N N . TYR AA 1 49 ? -3.187 -19.466 51.747 1.0 43.01 ? ? ? ? ? ? 166 TYR AA N 1 49 A A +ATOM 3043 C CA . TYR AA 1 49 ? -2.905 -19.128 53.134 1.0 31.65 ? ? ? ? ? ? 166 TYR AA CA 1 49 A A +ATOM 3044 C C . TYR AA 1 49 ? -1.627 -18.310 53.293 1.0 45.23 ? ? ? ? ? ? 166 TYR AA C 1 49 A A +ATOM 3045 O O . TYR AA 1 49 ? -1.502 -17.521 54.230 1.0 46.7 ? ? ? ? ? ? 166 TYR AA O 1 49 A A +ATOM 3046 C CB . TYR AA 1 49 ? -2.798 -20.406 53.963 1.0 40.4 ? ? ? ? ? ? 166 TYR AA CB 1 49 A A +ATOM 3047 C CG . TYR AA 1 49 ? -4.074 -21.205 54.016 1.0 45.05 ? ? ? ? ? ? 166 TYR AA CG 1 49 A A +ATOM 3048 C CD1 . TYR AA 1 49 ? -4.080 -22.567 53.726 1.0 46.24 ? ? ? ? ? ? 166 TYR AA CD1 1 49 A A +ATOM 3049 C CD2 . TYR AA 1 49 ? -5.276 -20.603 54.372 1.0 48.86 ? ? ? ? ? ? 166 TYR AA CD2 1 49 A A +ATOM 3050 C CE1 . TYR AA 1 49 ? -5.253 -23.311 53.795 1.0 53.79 ? ? ? ? ? ? 166 TYR AA CE1 1 49 A A +ATOM 3051 C CE2 . TYR AA 1 49 ? -6.454 -21.335 54.444 1.0 47.99 ? ? ? ? ? ? 166 TYR AA CE2 1 49 A A +ATOM 3052 C CZ . TYR AA 1 49 ? -6.437 -22.688 54.155 1.0 51.43 ? ? ? ? ? ? 166 TYR AA CZ 1 49 A A +ATOM 3053 O OH . TYR AA 1 49 ? -7.602 -23.419 54.247 1.0 60.63 ? ? ? ? ? ? 166 TYR AA OH 1 49 A A +ATOM 3054 N N . ASN AA 1 50 ? -0.682 -18.498 52.377 1.0 54.06 ? ? ? ? ? ? 167 ASN AA N 1 50 A A +ATOM 3055 C CA . ASN AA 1 50 ? 0.589 -17.784 52.434 1.0 65.84 ? ? ? ? ? ? 167 ASN AA CA 1 50 A A +ATOM 3056 C C . ASN AA 1 50 ? 0.584 -16.494 51.635 1.0 62.84 ? ? ? ? ? ? 167 ASN AA C 1 50 A A +ATOM 3057 O O . ASN AA 1 50 ? 1.494 -15.674 51.759 1.0 73.35 ? ? ? ? ? ? 167 ASN AA O 1 50 A A +ATOM 3058 C CB . ASN AA 1 50 ? 1.714 -18.677 51.919 1.0 72.59 ? ? ? ? ? ? 167 ASN AA CB 1 50 A A +ATOM 3059 C CG . ASN AA 1 50 ? 1.897 -19.917 52.756 1.0 72.14 ? ? ? ? ? ? 167 ASN AA CG 1 50 A A +ATOM 3060 O OD1 . ASN AA 1 50 ? 2.105 -19.835 53.967 1.0 80.82 ? ? ? ? ? ? 167 ASN AA OD1 1 50 A A +ATOM 3061 N ND2 . ASN AA 1 50 ? 1.820 -21.079 52.118 1.0 83.09 ? ? ? ? ? ? 167 ASN AA ND2 1 50 A A +ATOM 3062 N N . TYR AA 1 51 ? -0.439 -16.311 50.813 1.0 49.39 ? ? ? ? ? ? 168 TYR AA N 1 51 A A +ATOM 3063 C CA . TYR AA 1 51 ? -0.522 -15.116 49.989 1.0 39.76 ? ? ? ? ? ? 168 TYR AA CA 1 51 A A +ATOM 3064 C C . TYR AA 1 51 ? -0.966 -13.865 50.734 1.0 42.3 ? ? ? ? ? ? 168 TYR AA C 1 51 A A +ATOM 3065 O O . TYR AA 1 51 ? -2.019 -13.839 51.374 1.0 58.64 ? ? ? ? ? ? 168 TYR AA O 1 51 A A +ATOM 3066 C CB . TYR AA 1 51 ? -1.465 -15.341 48.806 1.0 46.65 ? ? ? ? ? ? 168 TYR AA CB 1 51 A A +ATOM 3067 C CG . TYR AA 1 51 ? -1.515 -14.154 47.880 1.0 39.97 ? ? ? ? ? ? 168 TYR AA CG 1 51 A A +ATOM 3068 C CD1 . TYR AA 1 51 ? -0.468 -13.896 47.002 1.0 66.54 ? ? ? ? ? ? 168 TYR AA CD1 1 51 A A +ATOM 3069 C CD2 . TYR AA 1 51 ? -2.576 -13.255 47.926 1.0 54.93 ? ? ? ? ? ? 168 TYR AA CD2 1 51 A A +ATOM 3070 C CE1 . TYR AA 1 51 ? -0.472 -12.775 46.192 1.0 67.76 ? ? ? ? ? ? 168 TYR AA CE1 1 51 A A +ATOM 3071 C CE2 . TYR AA 1 51 ? -2.592 -12.128 47.119 1.0 61.72 ? ? ? ? ? ? 168 TYR AA CE2 1 51 A A +ATOM 3072 C CZ . TYR AA 1 51 ? -1.533 -11.893 46.259 1.0 65.89 ? ? ? ? ? ? 168 TYR AA CZ 1 51 A A +ATOM 3073 O OH . TYR AA 1 51 ? -1.530 -10.774 45.463 1.0 88.35 ? ? ? ? ? ? 168 TYR AA OH 1 51 A A +ATOM 3074 N N . ARG AA 1 52 ? -0.147 -12.826 50.642 1.0 32.96 ? ? ? ? ? ? 169 ARG AA N 1 52 A A +ATOM 3075 C CA . ARG AA 1 52 ? -0.455 -11.552 51.268 1.0 40.34 ? ? ? ? ? ? 169 ARG AA CA 1 52 A A +ATOM 3076 C C . ARG AA 1 52 ? -0.537 -10.515 50.151 1.0 47.72 ? ? ? ? ? ? 169 ARG AA C 1 52 A A +ATOM 3077 O O . ARG AA 1 52 ? 0.241 -10.553 49.197 1.0 59.03 ? ? ? ? ? ? 169 ARG AA O 1 52 A A +ATOM 3078 C CB . ARG AA 1 52 ? 0.632 -11.173 52.271 1.0 41.42 ? ? ? ? ? ? 169 ARG AA CB 1 52 A A +ATOM 3079 C CG . ARG AA 1 52 ? 0.290 -11.522 53.708 1.0 58.13 ? ? ? ? ? ? 169 ARG AA CG 1 52 A A +ATOM 3080 C CD . ARG AA 1 52 ? 0.330 -13.022 53.937 1.0 63.85 ? ? ? ? ? ? 169 ARG AA CD 1 52 A A +ATOM 3081 N NE . ARG AA 1 52 ? 0.046 -13.372 55.326 1.0 72.67 ? ? ? ? ? ? 169 ARG AA NE 1 52 A A +ATOM 3082 C CZ . ARG AA 1 52 ? -1.022 -14.058 55.720 1.0 77.19 ? ? ? ? ? ? 169 ARG AA CZ 1 52 A A +ATOM 3083 N NH1 . ARG AA 1 52 ? -1.910 -14.468 54.827 1.0 77.86 ? ? ? ? ? ? 169 ARG AA NH1 1 52 A A +ATOM 3084 N NH2 . ARG AA 1 52 ? -1.206 -14.331 57.005 1.0 77.36 ? ? ? ? ? ? 169 ARG AA NH2 1 52 A A +ATOM 3085 N N . HIS AA 1 53 ? -1.491 -9.601 50.269 1.0 42.46 ? ? ? ? ? ? 170 HIS AA N 1 53 A A +ATOM 3086 C CA . HIS AA 1 53 ? -1.691 -8.564 49.267 1.0 40.05 ? ? ? ? ? ? 170 HIS AA CA 1 53 A A +ATOM 3087 C C . HIS AA 1 53 ? -0.402 -7.826 48.940 1.0 45.75 ? ? ? ? ? ? 170 HIS AA C 1 53 A A +ATOM 3088 O O . HIS AA 1 53 ? 0.486 -7.694 49.783 1.0 46.56 ? ? ? ? ? ? 170 HIS AA O 1 53 A A +ATOM 3089 C CB . HIS AA 1 53 ? -2.749 -7.566 49.755 1.0 51.11 ? ? ? ? ? ? 170 HIS AA CB 1 53 A A +ATOM 3090 C CG . HIS AA 1 53 ? -2.901 -6.361 48.880 1.0 53.11 ? ? ? ? ? ? 170 HIS AA CG 1 53 A A +ATOM 3091 N ND1 . HIS AA 1 53 ? -3.752 -6.329 47.795 1.0 37.55 ? ? ? ? ? ? 170 HIS AA ND1 1 53 A A +ATOM 3092 C CD2 . HIS AA 1 53 ? -2.315 -5.142 48.933 1.0 48.78 ? ? ? ? ? ? 170 HIS AA CD2 1 53 A A +ATOM 3093 C CE1 . HIS AA 1 53 ? -3.682 -5.142 47.220 1.0 46.68 ? ? ? ? ? ? 170 HIS AA CE1 1 53 A A +ATOM 3094 N NE2 . HIS AA 1 53 ? -2.818 -4.403 47.890 1.0 39.31 ? ? ? ? ? ? 170 HIS AA NE2 1 53 A A +ATOM 3095 N N . GLY AA 1 54 ? -0.307 -7.356 47.700 1.0 41.41 ? ? ? ? ? ? 171 GLY AA N 1 54 A A +ATOM 3096 C CA . GLY AA 1 54 ? 0.868 -6.619 47.275 1.0 62.11 ? ? ? ? ? ? 171 GLY AA CA 1 54 A A +ATOM 3097 C C . GLY AA 1 54 ? 1.877 -7.433 46.496 1.0 65.87 ? ? ? ? ? ? 171 GLY AA C 1 54 A A +ATOM 3098 O O . GLY AA 1 54 ? 2.488 -6.931 45.552 1.0 78.15 ? ? ? ? ? ? 171 GLY AA O 1 54 A A +ATOM 3099 N N . GLN AA 1 55 ? 2.062 -8.688 46.893 1.0 71.98 ? ? ? ? ? ? 172 GLN AA N 1 55 A A +ATOM 3100 C CA . GLN AA 1 55 ? 3.013 -9.564 46.223 1.0 75.85 ? ? ? ? ? ? 172 GLN AA CA 1 55 A A +ATOM 3101 C C . GLN AA 1 55 ? 2.348 -10.284 45.063 1.0 69.09 ? ? ? ? ? ? 172 GLN AA C 1 55 A A +ATOM 3102 O O . GLN AA 1 55 ? 1.156 -10.585 45.113 1.0 64.34 ? ? ? ? ? ? 172 GLN AA O 1 55 A A +ATOM 3103 C CB . GLN AA 1 55 ? 3.572 -10.589 47.207 1.0 77.26 ? ? ? ? ? ? 172 GLN AA CB 1 55 A A +ATOM 3104 C CG . GLN AA 1 55 ? 2.525 -11.530 47.762 1.0 59.13 ? ? ? ? ? ? 172 GLN AA CG 1 55 A A +ATOM 3105 C CD . GLN AA 1 55 ? 2.878 -12.019 49.144 1.0 53.97 ? ? ? ? ? ? 172 GLN AA CD 1 55 A A +ATOM 3106 O OE1 . GLN AA 1 55 ? 2.709 -13.194 49.462 1.0 56.19 ? ? ? ? ? ? 172 GLN AA OE1 1 55 A A +ATOM 3107 N NE2 . GLN AA 1 55 ? 3.372 -11.115 49.981 1.0 58.99 ? ? ? ? ? ? 172 GLN AA NE2 1 55 A A +ATOM 3108 N N . PRO AA 1 56 ? 3.117 -10.580 44.004 1.0 60.1 ? ? ? ? ? ? 173 PRO AA N 1 56 A A +ATOM 3109 C CA . PRO AA 1 56 ? 2.553 -11.272 42.839 1.0 51.4 ? ? ? ? ? ? 173 PRO AA CA 1 56 A A +ATOM 3110 C C . PRO AA 1 56 ? 2.049 -12.678 43.162 1.0 46.66 ? ? ? ? ? ? 173 PRO AA C 1 56 A A +ATOM 3111 O O . PRO AA 1 56 ? 2.642 -13.397 43.968 1.0 48.13 ? ? ? ? ? ? 173 PRO AA O 1 56 A A +ATOM 3112 C CB . PRO AA 1 56 ? 3.701 -11.270 41.828 1.0 56.78 ? ? ? ? ? ? 173 PRO AA CB 1 56 A A +ATOM 3113 C CG . PRO AA 1 56 ? 4.937 -11.089 42.646 1.0 66.08 ? ? ? ? ? ? 173 PRO AA CG 1 56 A A +ATOM 3114 C CD . PRO AA 1 56 ? 4.553 -10.288 43.845 1.0 57.41 ? ? ? ? ? ? 173 PRO AA CD 1 56 A A +ATOM 3115 N N . ILE AA 1 57 ? 0.939 -13.060 42.537 1.0 46.86 ? ? ? ? ? ? 174 ILE AA N 1 57 A A +ATOM 3116 C CA . ILE AA 1 57 ? 0.369 -14.379 42.754 1.0 58.88 ? ? ? ? ? ? 174 ILE AA CA 1 57 A A +ATOM 3117 C C . ILE AA 1 57 ? 1.347 -15.429 42.242 1.0 66.24 ? ? ? ? ? ? 174 ILE AA C 1 57 A A +ATOM 3118 O O . ILE AA 1 57 ? 1.744 -15.403 41.080 1.0 67.03 ? ? ? ? ? ? 174 ILE AA O 1 57 A A +ATOM 3119 C CB . ILE AA 1 57 ? -0.972 -14.535 42.006 1.0 53.24 ? ? ? ? ? ? 174 ILE AA CB 1 57 A A +ATOM 3120 C CG1 . ILE AA 1 57 ? -1.839 -13.299 42.225 1.0 38.78 ? ? ? ? ? ? 174 ILE AA CG1 1 57 A A +ATOM 3121 C CG2 . ILE AA 1 57 ? -1.696 -15.785 42.485 1.0 41.47 ? ? ? ? ? ? 174 ILE AA CG2 1 57 A A +ATOM 3122 C CD1 . ILE AA 1 57 ? -3.068 -13.260 41.345 1.0 52.33 ? ? ? ? ? ? 174 ILE AA CD1 1 57 A A +ATOM 3123 N N . PRO AA 1 58 ? 1.765 -16.357 43.117 1.0 69.49 ? ? ? ? ? ? 175 PRO AA N 1 58 A A +ATOM 3124 C CA . PRO AA 1 58 ? 2.709 -17.406 42.706 1.0 70.55 ? ? ? ? ? ? 175 PRO AA CA 1 58 A A +ATOM 3125 C C . PRO AA 1 58 ? 2.221 -18.216 41.507 1.0 70.56 ? ? ? ? ? ? 175 PRO AA C 1 58 A A +ATOM 3126 O O . PRO AA 1 58 ? 1.035 -18.527 41.398 1.0 61.0 ? ? ? ? ? ? 175 PRO AA O 1 58 A A +ATOM 3127 C CB . PRO AA 1 58 ? 2.866 -18.273 43.961 1.0 61.75 ? ? ? ? ? ? 175 PRO AA CB 1 58 A A +ATOM 3128 C CG . PRO AA 1 58 ? 1.717 -17.892 44.849 1.0 44.44 ? ? ? ? ? ? 175 PRO AA CG 1 58 A A +ATOM 3129 C CD . PRO AA 1 58 ? 1.389 -16.475 44.535 1.0 50.89 ? ? ? ? ? ? 175 PRO AA CD 1 58 A A +ATOM 3130 N N . ARG AA 1 59 ? 3.145 -18.557 40.610 1.0 68.23 ? ? ? ? ? ? 176 ARG AA N 1 59 A A +ATOM 3131 C CA . ARG AA 1 59 ? 2.795 -19.334 39.428 1.0 66.01 ? ? ? ? ? ? 176 ARG AA CA 1 59 A A +ATOM 3132 C C . ARG AA 1 59 ? 2.895 -20.818 39.745 1.0 55.42 ? ? ? ? ? ? 176 ARG AA C 1 59 A A +ATOM 3133 O O . ARG AA 1 59 ? 3.618 -21.217 40.656 1.0 55.67 ? ? ? ? ? ? 176 ARG AA O 1 59 A A +ATOM 3134 C CB . ARG AA 1 59 ? 3.723 -18.983 38.259 1.0 71.12 ? ? ? ? ? ? 176 ARG AA CB 1 59 A A +ATOM 3135 C CG . ARG AA 1 59 ? 3.696 -17.511 37.870 1.0 70.25 ? ? ? ? ? ? 176 ARG AA CG 1 59 A A +ATOM 3136 C CD . ARG AA 1 59 ? 4.716 -17.200 36.792 1.0 58.5 ? ? ? ? ? ? 176 ARG AA CD 1 59 A A +ATOM 3137 N NE . ARG AA 1 59 ? 4.220 -16.187 35.870 1.0 69.14 ? ? ? ? ? ? 176 ARG AA NE 1 59 A A +ATOM 3138 C CZ . ARG AA 1 59 ? 3.621 -16.456 34.716 1.0 65.87 ? ? ? ? ? ? 176 ARG AA CZ 1 59 A A +ATOM 3139 N NH1 . ARG AA 1 59 ? 3.440 -17.713 34.336 1.0 64.13 ? ? ? ? ? ? 176 ARG AA NH1 1 59 A A +ATOM 3140 N NH2 . ARG AA 1 59 ? 3.201 -15.467 33.943 1.0 57.7 ? ? ? ? ? ? 176 ARG AA NH2 1 59 A A +ATOM 3141 N N . VAL AA 1 60 ? 2.161 -21.628 38.991 1.0 40.96 ? ? ? ? ? ? 177 VAL AA N 1 60 A A +ATOM 3142 C CA . VAL AA 1 60 ? 2.161 -23.068 39.206 1.0 58.52 ? ? ? ? ? ? 177 VAL AA CA 1 60 A A +ATOM 3143 C C . VAL AA 1 60 ? 2.319 -23.849 37.901 1.0 60.43 ? ? ? ? ? ? 177 VAL AA C 1 60 A A +ATOM 3144 O O . VAL AA 1 60 ? 1.828 -23.437 36.849 1.0 62.67 ? ? ? ? ? ? 177 VAL AA O 1 60 A A +ATOM 3145 C CB . VAL AA 1 60 ? 0.855 -23.522 39.909 1.0 61.33 ? ? ? ? ? ? 177 VAL AA CB 1 60 A A +ATOM 3146 C CG1 . VAL AA 1 60 ? 0.795 -25.035 39.983 1.0 83.94 ? ? ? ? ? ? 177 VAL AA CG1 1 60 A A +ATOM 3147 C CG2 . VAL AA 1 60 ? 0.781 -22.928 41.302 1.0 53.69 ? ? ? ? ? ? 177 VAL AA CG2 1 60 A A +ATOM 3148 N N . GLU AA 1 61 ? 3.013 -24.979 37.987 1.0 45.91 ? ? ? ? ? ? 178 GLU AA N 1 61 A A +ATOM 3149 C CA . GLU AA 1 61 ? 3.245 -25.844 36.842 1.0 49.76 ? ? ? ? ? ? 178 GLU AA CA 1 61 A A +ATOM 3150 C C . GLU AA 1 61 ? 2.159 -26.920 36.809 1.0 52.05 ? ? ? ? ? ? 178 GLU AA C 1 61 A A +ATOM 3151 O O . GLU AA 1 61 ? 2.325 -28.000 37.374 1.0 55.89 ? ? ? ? ? ? 178 GLU AA O 1 61 A A +ATOM 3152 C CB . GLU AA 1 61 ? 4.626 -26.495 36.960 1.0 52.19 ? ? ? ? ? ? 178 GLU AA CB 1 61 A A +ATOM 3153 C CG . GLU AA 1 61 ? 5.327 -26.734 35.632 1.0 71.52 ? ? ? ? ? ? 178 GLU AA CG 1 61 A A +ATOM 3154 C CD . GLU AA 1 61 ? 6.799 -27.094 35.801 1.0 84.05 ? ? ? ? ? ? 178 GLU AA CD 1 61 A A +ATOM 3155 O OE1 . GLU AA 1 61 ? 7.097 -28.244 36.204 1.0 85.57 ? ? ? ? ? ? 178 GLU AA OE1 1 61 A A +ATOM 3156 O OE2 . GLU AA 1 61 ? 7.661 -26.227 35.533 1.0 80.92 ? ? ? ? ? ? 178 GLU AA OE2 1 61 A A +ATOM 3157 N N . TYR AA 1 62 ? 1.046 -26.620 36.149 1.0 48.56 ? ? ? ? ? ? 179 TYR AA N 1 62 A A +ATOM 3158 C CA . TYR AA 1 62 ? -0.067 -27.562 36.061 1.0 63.62 ? ? ? ? ? ? 179 TYR AA CA 1 62 A A +ATOM 3159 C C . TYR AA 1 62 ? 0.318 -28.851 35.347 1.0 66.92 ? ? ? ? ? ? 179 TYR AA C 1 62 A A +ATOM 3160 O O . TYR AA 1 62 ? 1.168 -28.843 34.461 1.0 79.31 ? ? ? ? ? ? 179 TYR AA O 1 62 A A +ATOM 3161 C CB . TYR AA 1 62 ? -1.252 -26.902 35.356 1.0 66.47 ? ? ? ? ? ? 179 TYR AA CB 1 62 A A +ATOM 3162 C CG . TYR AA 1 62 ? -1.852 -25.778 36.160 1.0 64.67 ? ? ? ? ? ? 179 TYR AA CG 1 62 A A +ATOM 3163 C CD1 . TYR AA 1 62 ? -3.046 -25.953 36.857 1.0 62.18 ? ? ? ? ? ? 179 TYR AA CD1 1 62 A A +ATOM 3164 C CD2 . TYR AA 1 62 ? -1.214 -24.542 36.247 1.0 72.84 ? ? ? ? ? ? 179 TYR AA CD2 1 62 A A +ATOM 3165 C CE1 . TYR AA 1 62 ? -3.589 -24.927 37.620 1.0 79.47 ? ? ? ? ? ? 179 TYR AA CE1 1 62 A A +ATOM 3166 C CE2 . TYR AA 1 62 ? -1.749 -23.507 37.008 1.0 77.72 ? ? ? ? ? ? 179 TYR AA CE2 1 62 A A +ATOM 3167 C CZ . TYR AA 1 62 ? -2.939 -23.707 37.692 1.0 80.12 ? ? ? ? ? ? 179 TYR AA CZ 1 62 A A +ATOM 3168 O OH . TYR AA 1 62 ? -3.489 -22.687 38.436 1.0 71.22 ? ? ? ? ? ? 179 TYR AA OH 1 62 A A +ATOM 3169 N N . MET AA 1 63 ? -0.315 -29.955 35.738 1.0 61.45 ? ? ? ? ? ? 180 MET AA N 1 63 A A +ATOM 3170 C CA . MET AA 1 63 ? -0.031 -31.261 35.147 1.0 62.82 ? ? ? ? ? ? 180 MET AA CA 1 63 A A +ATOM 3171 C C . MET AA 1 63 ? -0.952 -31.586 33.980 1.0 65.47 ? ? ? ? ? ? 180 MET AA C 1 63 A A +ATOM 3172 O O . MET AA 1 63 ? -2.045 -31.032 33.868 1.0 73.13 ? ? ? ? ? ? 180 MET AA O 1 63 A A +ATOM 3173 C CB . MET AA 1 63 ? -0.145 -32.354 36.212 1.0 67.13 ? ? ? ? ? ? 180 MET AA CB 1 63 A A +ATOM 3174 C CG . MET AA 1 63 ? 0.662 -32.079 37.472 1.0 66.76 ? ? ? ? ? ? 180 MET AA CG 1 63 A A +ATOM 3175 S SD . MET AA 1 63 ? 0.478 -33.346 38.755 1.0 65.33 ? ? ? ? ? ? 180 MET AA SD 1 63 A A +ATOM 3176 C CE . MET AA 1 63 ? -1.288 -33.681 38.698 1.0 31.44 ? ? ? ? ? ? 180 MET AA CE 1 63 A A +ATOM 3177 N N . GLU AA 1 64 ? -0.500 -32.496 33.120 1.0 60.02 ? ? ? ? ? ? 181 GLU AA N 1 64 A A +ATOM 3178 C CA . GLU AA 1 64 ? -1.268 -32.898 31.945 1.0 60.6 ? ? ? ? ? ? 181 GLU AA CA 1 64 A A +ATOM 3179 C C . GLU AA 1 64 ? -2.637 -33.467 32.282 1.0 62.39 ? ? ? ? ? ? 181 GLU AA C 1 64 A A +ATOM 3180 O O . GLU AA 1 64 ? -3.618 -33.186 31.594 1.0 55.85 ? ? ? ? ? ? 181 GLU AA O 1 64 A A +ATOM 3181 C CB . GLU AA 1 64 ? -0.490 -33.926 31.128 1.0 64.53 ? ? ? ? ? ? 181 GLU AA CB 1 64 A A +ATOM 3182 C CG . GLU AA 1 64 ? 0.253 -33.329 29.954 1.0 73.52 ? ? ? ? ? ? 181 GLU AA CG 1 64 A A +ATOM 3183 C CD . GLU AA 1 64 ? 1.422 -32.479 30.401 1.0 79.03 ? ? ? ? ? ? 181 GLU AA CD 1 64 A A +ATOM 3184 O OE1 . GLU AA 1 64 ? 1.864 -32.655 31.559 1.0 79.95 ? ? ? ? ? ? 181 GLU AA OE1 1 64 A A +ATOM 3185 O OE2 . GLU AA 1 64 ? 1.898 -31.644 29.600 1.0 75.62 ? ? ? ? ? ? 181 GLU AA OE2 1 64 A A +ATOM 3186 N N . GLU AA 1 65 ? -2.701 -34.286 33.325 1.0 65.1 ? ? ? ? ? ? 182 GLU AA N 1 65 A A +ATOM 3187 C CA . GLU AA 1 65 ? -3.972 -34.871 33.725 1.0 69.61 ? ? ? ? ? ? 182 GLU AA CA 1 65 A A +ATOM 3188 C C . GLU AA 1 65 ? -4.929 -33.718 34.011 1.0 76.9 ? ? ? ? ? ? 182 GLU AA C 1 65 A A +ATOM 3189 O O . GLU AA 1 65 ? -6.150 -33.865 33.927 1.0 82.04 ? ? ? ? ? ? 182 GLU AA O 1 65 A A +ATOM 3190 C CB . GLU AA 1 65 ? -3.790 -35.733 34.974 1.0 74.6 ? ? ? ? ? ? 182 GLU AA CB 1 65 A A +ATOM 3191 C CG . GLU AA 1 65 ? -2.920 -36.965 34.761 1.0 87.81 ? ? ? ? ? ? 182 GLU AA CG 1 65 A A +ATOM 3192 C CD . GLU AA 1 65 ? -1.442 -36.627 34.626 1.0 97.73 ? ? ? ? ? ? 182 GLU AA CD 1 65 A A +ATOM 3193 O OE1 . GLU AA 1 65 ? -0.717 -37.380 33.943 1.0 100.0 ? ? ? ? ? ? 182 GLU AA OE1 1 65 A A +ATOM 3194 O OE2 . GLU AA 1 65 ? -1.004 -35.610 35.203 1.0 92.34 ? ? ? ? ? ? 182 GLU AA OE2 1 65 A A +ATOM 3195 N N . GLU AA 1 66 ? -4.353 -32.565 34.343 1.0 71.44 ? ? ? ? ? ? 183 GLU AA N 1 66 A A +ATOM 3196 C CA . GLU AA 1 66 ? -5.120 -31.363 34.639 1.0 56.58 ? ? ? ? ? ? 183 GLU AA CA 1 66 A A +ATOM 3197 C C . GLU AA 1 66 ? -5.331 -30.587 33.344 1.0 59.61 ? ? ? ? ? ? 183 GLU AA C 1 66 A A +ATOM 3198 O O . GLU AA 1 66 ? -6.453 -30.217 33.003 1.0 61.56 ? ? ? ? ? ? 183 GLU AA O 1 66 A A +ATOM 3199 C CB . GLU AA 1 66 ? -4.368 -30.496 35.661 1.0 41.0 ? ? ? ? ? ? 183 GLU AA CB 1 66 A A +ATOM 3200 C CG . GLU AA 1 66 ? -4.049 -31.229 36.960 1.0 52.5 ? ? ? ? ? ? 183 GLU AA CG 1 66 A A +ATOM 3201 C CD . GLU AA 1 66 ? -3.249 -30.392 37.946 1.0 58.87 ? ? ? ? ? ? 183 GLU AA CD 1 66 A A +ATOM 3202 O OE1 . GLU AA 1 66 ? -2.241 -29.780 37.531 1.0 43.01 ? ? ? ? ? ? 183 GLU AA OE1 1 66 A A +ATOM 3203 O OE2 . GLU AA 1 66 ? -3.631 -30.352 39.139 1.0 52.0 ? ? ? ? ? ? 183 GLU AA OE2 1 66 A A +ATOM 3204 N N . LYS AA 1 67 ? -4.241 -30.354 32.620 1.0 53.06 ? ? ? ? ? ? 184 LYS AA N 1 67 A A +ATOM 3205 C CA . LYS AA 1 67 ? -4.300 -29.625 31.362 1.0 57.91 ? ? ? ? ? ? 184 LYS AA CA 1 67 A A +ATOM 3206 C C . LYS AA 1 67 ? -5.284 -30.273 30.397 1.0 64.25 ? ? ? ? ? ? 184 LYS AA C 1 67 A A +ATOM 3207 O O . LYS AA 1 67 ? -5.812 -29.612 29.501 1.0 65.13 ? ? ? ? ? ? 184 LYS AA O 1 67 A A +ATOM 3208 C CB . LYS AA 1 67 ? -2.913 -29.566 30.721 1.0 52.43 ? ? ? ? ? ? 184 LYS AA CB 1 67 A A +ATOM 3209 C CG . LYS AA 1 67 ? -1.964 -28.589 31.387 1.0 46.38 ? ? ? ? ? ? 184 LYS AA CG 1 67 A A +ATOM 3210 C CD . LYS AA 1 67 ? -0.651 -28.504 30.632 1.0 42.06 ? ? ? ? ? ? 184 LYS AA CD 1 67 A A +ATOM 3211 C CE . LYS AA 1 67 ? 0.285 -27.499 31.270 1.0 45.51 ? ? ? ? ? ? 184 LYS AA CE 1 67 A A +ATOM 3212 N NZ . LYS AA 1 67 ? 1.586 -27.417 30.553 1.0 53.49 ? ? ? ? ? ? 184 LYS AA NZ 1 67 A A +ATOM 3213 N N . LYS AA 1 68 ? -5.527 -31.569 30.576 1.0 58.11 ? ? ? ? ? ? 185 LYS AA N 1 68 A A +ATOM 3214 C CA . LYS AA 1 68 ? -6.462 -32.280 29.714 1.0 67.71 ? ? ? ? ? ? 185 LYS AA CA 1 68 A A +ATOM 3215 C C . LYS AA 1 68 ? -7.870 -31.859 30.095 1.0 61.16 ? ? ? ? ? ? 185 LYS AA C 1 68 A A +ATOM 3216 O O . LYS AA 1 68 ? -8.702 -31.560 29.236 1.0 73.17 ? ? ? ? ? ? 185 LYS AA O 1 68 A A +ATOM 3217 C CB . LYS AA 1 68 ? -6.323 -33.793 29.885 1.0 71.53 ? ? ? ? ? ? 185 LYS AA CB 1 68 A A +ATOM 3218 C CG . LYS AA 1 68 ? -7.308 -34.589 29.046 1.0 84.28 ? ? ? ? ? ? 185 LYS AA CG 1 68 A A +ATOM 3219 C CD . LYS AA 1 68 ? -7.329 -36.052 29.448 1.0 85.26 ? ? ? ? ? ? 185 LYS AA CD 1 68 A A +ATOM 3220 C CE . LYS AA 1 68 ? -8.073 -36.892 28.424 1.0 87.16 ? ? ? ? ? ? 185 LYS AA CE 1 68 A A +ATOM 3221 N NZ . LYS AA 1 68 ? -9.548 -36.689 28.492 1.0 87.22 ? ? ? ? ? ? 185 LYS AA NZ 1 68 A A +ATOM 3222 N N . THR AA 1 69 ? -8.129 -31.837 31.396 1.0 42.82 ? ? ? ? ? ? 186 THR AA N 1 69 A A +ATOM 3223 C CA . THR AA 1 69 ? -9.437 -31.447 31.899 1.0 62.42 ? ? ? ? ? ? 186 THR AA CA 1 69 A A +ATOM 3224 C C . THR AA 1 69 ? -9.731 -29.997 31.532 1.0 60.37 ? ? ? ? ? ? 186 THR AA C 1 69 A A +ATOM 3225 O O . THR AA 1 69 ? -10.878 -29.626 31.288 1.0 60.5 ? ? ? ? ? ? 186 THR AA O 1 69 A A +ATOM 3226 C CB . THR AA 1 69 ? -9.506 -31.603 33.426 1.0 66.13 ? ? ? ? ? ? 186 THR AA CB 1 69 A A +ATOM 3227 O OG1 . THR AA 1 69 ? -8.912 -32.850 33.806 1.0 53.16 ? ? ? ? ? ? 186 THR AA OG1 1 69 A A +ATOM 3228 C CG2 . THR AA 1 69 ? -10.952 -31.571 33.896 1.0 51.28 ? ? ? ? ? ? 186 THR AA CG2 1 69 A A +ATOM 3229 N N . TRP AA 1 70 ? -8.687 -29.178 31.501 1.0 58.38 ? ? ? ? ? ? 187 TRP AA N 1 70 A A +ATOM 3230 C CA . TRP AA 1 70 ? -8.843 -27.774 31.153 1.0 71.46 ? ? ? ? ? ? 187 TRP AA CA 1 70 A A +ATOM 3231 C C . TRP AA 1 70 ? -9.309 -27.672 29.703 1.0 76.26 ? ? ? ? ? ? 187 TRP AA C 1 70 A A +ATOM 3232 O O . TRP AA 1 70 ? -10.296 -27.000 29.402 1.0 74.65 ? ? ? ? ? ? 187 TRP AA O 1 70 A A +ATOM 3233 C CB . TRP AA 1 70 ? -7.512 -27.039 31.336 1.0 73.41 ? ? ? ? ? ? 187 TRP AA CB 1 70 A A +ATOM 3234 C CG . TRP AA 1 70 ? -7.449 -25.703 30.655 1.0 82.27 ? ? ? ? ? ? 187 TRP AA CG 1 70 A A +ATOM 3235 C CD1 . TRP AA 1 70 ? -6.791 -25.408 29.498 1.0 81.34 ? ? ? ? ? ? 187 TRP AA CD1 1 70 A A +ATOM 3236 C CD2 . TRP AA 1 70 ? -8.055 -24.477 31.097 1.0 85.83 ? ? ? ? ? ? 187 TRP AA CD2 1 70 A A +ATOM 3237 N NE1 . TRP AA 1 70 ? -6.943 -24.076 29.192 1.0 91.72 ? ? ? ? ? ? 187 TRP AA NE1 1 70 A A +ATOM 3238 C CE2 . TRP AA 1 70 ? -7.709 -23.482 30.157 1.0 88.31 ? ? ? ? ? ? 187 TRP AA CE2 1 70 A A +ATOM 3239 C CE3 . TRP AA 1 70 ? -8.845 -24.124 32.200 1.0 84.92 ? ? ? ? ? ? 187 TRP AA CE3 1 70 A A +ATOM 3240 C CZ2 . TRP AA 1 70 ? -8.135 -22.152 30.283 1.0 89.08 ? ? ? ? ? ? 187 TRP AA CZ2 1 70 A A +ATOM 3241 C CZ3 . TRP AA 1 70 ? -9.266 -22.799 32.324 1.0 82.88 ? ? ? ? ? ? 187 TRP AA CZ3 1 70 A A +ATOM 3242 C CH2 . TRP AA 1 70 ? -8.912 -21.832 31.367 1.0 80.38 ? ? ? ? ? ? 187 TRP AA CH2 1 70 A A +ATOM 3243 N N . GLY AA 1 71 ? -8.591 -28.353 28.814 1.0 79.18 ? ? ? ? ? ? 188 GLY AA N 1 71 A A +ATOM 3244 C CA . GLY AA 1 71 ? -8.930 -28.336 27.404 1.0 71.95 ? ? ? ? ? ? 188 GLY AA CA 1 71 A A +ATOM 3245 C C . GLY AA 1 71 ? -10.246 -29.018 27.083 1.0 74.01 ? ? ? ? ? ? 188 GLY AA C 1 71 A A +ATOM 3246 O O . GLY AA 1 71 ? -10.875 -28.711 26.070 1.0 90.17 ? ? ? ? ? ? 188 GLY AA O 1 71 A A +ATOM 3247 N N . THR AA 1 72 ? -10.665 -29.946 27.937 1.0 61.43 ? ? ? ? ? ? 189 THR AA N 1 72 A A +ATOM 3248 C CA . THR AA 1 72 ? -11.923 -30.650 27.722 1.0 79.14 ? ? ? ? ? ? 189 THR AA CA 1 72 A A +ATOM 3249 C C . THR AA 1 72 ? -13.087 -29.693 27.973 1.0 83.53 ? ? ? ? ? ? 189 THR AA C 1 72 A A +ATOM 3250 O O . THR AA 1 72 ? -14.165 -29.835 27.392 1.0 86.76 ? ? ? ? ? ? 189 THR AA O 1 72 A A +ATOM 3251 C CB . THR AA 1 72 ? -12.055 -31.869 28.659 1.0 77.79 ? ? ? ? ? ? 189 THR AA CB 1 72 A A +ATOM 3252 O OG1 . THR AA 1 72 ? -11.051 -32.836 28.325 1.0 73.16 ? ? ? ? ? ? 189 THR AA OG1 1 72 A A +ATOM 3253 C CG2 . THR AA 1 72 ? -13.431 -32.513 28.519 1.0 81.44 ? ? ? ? ? ? 189 THR AA CG2 1 72 A A +ATOM 3254 N N . VAL AA 1 73 ? -12.851 -28.715 28.842 1.0 86.25 ? ? ? ? ? ? 190 VAL AA N 1 73 A A +ATOM 3255 C CA . VAL AA 1 73 ? -13.864 -27.720 29.174 1.0 85.35 ? ? ? ? ? ? 190 VAL AA CA 1 73 A A +ATOM 3256 C C . VAL AA 1 73 ? -13.702 -26.503 28.266 1.0 83.6 ? ? ? ? ? ? 190 VAL AA C 1 73 A A +ATOM 3257 O O . VAL AA 1 73 ? -14.680 -25.855 27.888 1.0 75.22 ? ? ? ? ? ? 190 VAL AA O 1 73 A A +ATOM 3258 C CB . VAL AA 1 73 ? -13.742 -27.265 30.643 1.0 79.63 ? ? ? ? ? ? 190 VAL AA CB 1 73 A A +ATOM 3259 C CG1 . VAL AA 1 73 ? -14.969 -26.458 31.039 1.0 75.13 ? ? ? ? ? ? 190 VAL AA CG1 1 73 A A +ATOM 3260 C CG2 . VAL AA 1 73 ? -13.579 -28.467 31.548 1.0 75.09 ? ? ? ? ? ? 190 VAL AA CG2 1 73 A A +ATOM 3261 N N . PHE AA 1 74 ? -12.452 -26.203 27.924 1.0 79.24 ? ? ? ? ? ? 191 PHE AA N 1 74 A A +ATOM 3262 C CA . PHE AA 1 74 ? -12.125 -25.077 27.055 1.0 76.08 ? ? ? ? ? ? 191 PHE AA CA 1 74 A A +ATOM 3263 C C . PHE AA 1 74 ? -12.612 -25.334 25.631 1.0 85.23 ? ? ? ? ? ? 191 PHE AA C 1 74 A A +ATOM 3264 O O . PHE AA 1 74 ? -12.787 -24.404 24.848 1.0 99.86 ? ? ? ? ? ? 191 PHE AA O 1 74 A A +ATOM 3265 C CB . PHE AA 1 74 ? -10.614 -24.849 27.042 1.0 67.59 ? ? ? ? ? ? 191 PHE AA CB 1 74 A A +ATOM 3266 C CG . PHE AA 1 74 ? -10.193 -23.601 26.324 1.0 73.28 ? ? ? ? ? ? 191 PHE AA CG 1 74 A A +ATOM 3267 C CD1 . PHE AA 1 74 ? -10.011 -22.413 27.021 1.0 80.98 ? ? ? ? ? ? 191 PHE AA CD1 1 74 A A +ATOM 3268 C CD2 . PHE AA 1 74 ? -9.964 -23.615 24.952 1.0 79.62 ? ? ? ? ? ? 191 PHE AA CD2 1 74 A A +ATOM 3269 C CE1 . PHE AA 1 74 ? -9.604 -21.255 26.362 1.0 81.2 ? ? ? ? ? ? 191 PHE AA CE1 1 74 A A +ATOM 3270 C CE2 . PHE AA 1 74 ? -9.557 -22.462 24.283 1.0 79.7 ? ? ? ? ? ? 191 PHE AA CE2 1 74 A A +ATOM 3271 C CZ . PHE AA 1 74 ? -9.378 -21.280 24.990 1.0 80.86 ? ? ? ? ? ? 191 PHE AA CZ 1 74 A A +ATOM 3272 N N . LYS AA 1 75 ? -12.822 -26.602 25.297 1.0 89.68 ? ? ? ? ? ? 192 LYS AA N 1 75 A A +ATOM 3273 C CA . LYS AA 1 75 ? -13.292 -26.965 23.966 1.0 86.96 ? ? ? ? ? ? 192 LYS AA CA 1 75 A A +ATOM 3274 C C . LYS AA 1 75 ? -14.811 -27.047 23.954 1.0 83.34 ? ? ? ? ? ? 192 LYS AA C 1 75 A A +ATOM 3275 O O . LYS AA 1 75 ? -15.468 -26.503 23.068 1.0 91.7 ? ? ? ? ? ? 192 LYS AA O 1 75 A A +ATOM 3276 C CB . LYS AA 1 75 ? -12.713 -28.315 23.546 1.0 91.2 ? ? ? ? ? ? 192 LYS AA CB 1 75 A A +ATOM 3277 C CG . LYS AA 1 75 ? -13.125 -28.749 22.151 1.0 100.0 ? ? ? ? ? ? 192 LYS AA CG 1 75 A A +ATOM 3278 C CD . LYS AA 1 75 ? -12.542 -30.104 21.791 1.0 100.0 ? ? ? ? ? ? 192 LYS AA CD 1 75 A A +ATOM 3279 C CE . LYS AA 1 75 ? -11.098 -29.972 21.336 1.0 100.0 ? ? ? ? ? ? 192 LYS AA CE 1 75 A A +ATOM 3280 N NZ . LYS AA 1 75 ? -10.990 -29.435 19.949 1.0 100.0 ? ? ? ? ? ? 192 LYS AA NZ 1 75 A A +ATOM 3281 N N . THR AA 1 76 ? -15.356 -27.735 24.950 1.0 76.1 ? ? ? ? ? ? 193 THR AA N 1 76 A A +ATOM 3282 C CA . THR AA 1 76 ? -16.796 -27.907 25.069 1.0 90.5 ? ? ? ? ? ? 193 THR AA CA 1 76 A A +ATOM 3283 C C . THR AA 1 76 ? -17.557 -26.588 25.170 1.0 96.09 ? ? ? ? ? ? 193 THR AA C 1 76 A A +ATOM 3284 O O . THR AA 1 76 ? -18.674 -26.474 24.663 1.0 100.0 ? ? ? ? ? ? 193 THR AA O 1 76 A A +ATOM 3285 C CB . THR AA 1 76 ? -17.149 -28.748 26.306 1.0 100.0 ? ? ? ? ? ? 193 THR AA CB 1 76 A A +ATOM 3286 O OG1 . THR AA 1 76 ? -18.575 -28.813 26.450 1.0 100.0 ? ? ? ? ? ? 193 THR AA OG1 1 76 A A +ATOM 3287 C CG2 . THR AA 1 76 ? -16.554 -28.126 27.552 1.0 100.0 ? ? ? ? ? ? 193 THR AA CG2 1 76 A A +ATOM 3288 N N . LEU AA 1 77 ? -16.957 -25.597 25.823 1.0 90.36 ? ? ? ? ? ? 194 LEU AA N 1 77 A A +ATOM 3289 C CA . LEU AA 1 77 ? -17.609 -24.304 26.001 1.0 85.08 ? ? ? ? ? ? 194 LEU AA CA 1 77 A A +ATOM 3290 C C . LEU AA 1 77 ? -17.285 -23.259 24.932 1.0 82.86 ? ? ? ? ? ? 194 LEU AA C 1 77 A A +ATOM 3291 O O . LEU AA 1 77 ? -18.115 -22.403 24.625 1.0 85.6 ? ? ? ? ? ? 194 LEU AA O 1 77 A A +ATOM 3292 C CB . LEU AA 1 77 ? -17.273 -23.741 27.385 1.0 74.24 ? ? ? ? ? ? 194 LEU AA CB 1 77 A A +ATOM 3293 C CG . LEU AA 1 77 ? -17.803 -24.537 28.582 1.0 72.3 ? ? ? ? ? ? 194 LEU AA CG 1 77 A A +ATOM 3294 C CD1 . LEU AA 1 77 ? -17.270 -23.935 29.869 1.0 73.94 ? ? ? ? ? ? 194 LEU AA CD1 1 77 A A +ATOM 3295 C CD2 . LEU AA 1 77 ? -19.321 -24.525 28.583 1.0 77.3 ? ? ? ? ? ? 194 LEU AA CD2 1 77 A A +ATOM 3296 N N . LYS AA 1 78 ? -16.083 -23.326 24.369 1.0 79.81 ? ? ? ? ? ? 195 LYS AA N 1 78 A A +ATOM 3297 C CA . LYS AA 1 78 ? -15.669 -22.364 23.348 1.0 80.42 ? ? ? ? ? ? 195 LYS AA CA 1 78 A A +ATOM 3298 C C . LYS AA 1 78 ? -16.622 -22.322 22.161 1.0 86.3 ? ? ? ? ? ? 195 LYS AA C 1 78 A A +ATOM 3299 O O . LYS AA 1 78 ? -16.716 -21.312 21.460 1.0 84.76 ? ? ? ? ? ? 195 LYS AA O 1 78 A A +ATOM 3300 C CB . LYS AA 1 78 ? -14.265 -22.692 22.848 1.0 86.69 ? ? ? ? ? ? 195 LYS AA CB 1 78 A A +ATOM 3301 C CG . LYS AA 1 78 ? -13.703 -21.657 21.888 1.0 88.67 ? ? ? ? ? ? 195 LYS AA CG 1 78 A A +ATOM 3302 C CD . LYS AA 1 78 ? -12.203 -21.826 21.704 1.0 93.28 ? ? ? ? ? ? 195 LYS AA CD 1 78 A A +ATOM 3303 C CE . LYS AA 1 78 ? -11.703 -21.014 20.521 1.0 92.2 ? ? ? ? ? ? 195 LYS AA CE 1 78 A A +ATOM 3304 N NZ . LYS AA 1 78 ? -11.968 -19.559 20.691 1.0 88.53 ? ? ? ? ? ? 195 LYS AA NZ 1 78 A A +ATOM 3305 N N . SER AA 1 79 ? -17.319 -23.428 21.935 1.0 94.23 ? ? ? ? ? ? 196 SER AA N 1 79 A A +ATOM 3306 C CA . SER AA 1 79 ? -18.259 -23.522 20.827 1.0 100.0 ? ? ? ? ? ? 196 SER AA CA 1 79 A A +ATOM 3307 C C . SER AA 1 79 ? -19.571 -22.788 21.106 1.0 100.0 ? ? ? ? ? ? 196 SER AA C 1 79 A A +ATOM 3308 O O . SER AA 1 79 ? -20.126 -22.135 20.220 1.0 100.0 ? ? ? ? ? ? 196 SER AA O 1 79 A A +ATOM 3309 C CB . SER AA 1 79 ? -18.556 -24.991 20.520 1.0 100.0 ? ? ? ? ? ? 196 SER AA CB 1 79 A A +ATOM 3310 O OG . SER AA 1 79 ? -19.292 -25.593 21.574 1.0 85.8 ? ? ? ? ? ? 196 SER AA OG 1 79 A A +ATOM 3311 N N . LEU AA 1 80 ? -20.054 -22.889 22.341 1.0 96.32 ? ? ? ? ? ? 197 LEU AA N 1 80 A A +ATOM 3312 C CA . LEU AA 1 80 ? -21.316 -22.258 22.722 1.0 93.99 ? ? ? ? ? ? 197 LEU AA CA 1 80 A A +ATOM 3313 C C . LEU AA 1 80 ? -21.239 -20.811 23.191 1.0 88.37 ? ? ? ? ? ? 197 LEU AA C 1 80 A A +ATOM 3314 O O . LEU AA 1 80 ? -22.247 -20.252 23.618 1.0 81.94 ? ? ? ? ? ? 197 LEU AA O 1 80 A A +ATOM 3315 C CB . LEU AA 1 80 ? -22.000 -23.075 23.818 1.0 95.3 ? ? ? ? ? ? 197 LEU AA CB 1 80 A A +ATOM 3316 C CG . LEU AA 1 80 ? -22.064 -24.595 23.670 1.0 93.83 ? ? ? ? ? ? 197 LEU AA CG 1 80 A A +ATOM 3317 C CD1 . LEU AA 1 80 ? -22.819 -25.168 24.856 1.0 100.0 ? ? ? ? ? ? 197 LEU AA CD1 1 80 A A +ATOM 3318 C CD2 . LEU AA 1 80 ? -22.754 -24.973 22.367 1.0 100.0 ? ? ? ? ? ? 197 LEU AA CD2 1 80 A A +ATOM 3319 N N . TYR AA 1 81 ? -20.066 -20.192 23.114 1.0 87.34 ? ? ? ? ? ? 198 TYR AA N 1 81 A A +ATOM 3320 C CA . TYR AA 1 81 ? -19.945 -18.813 23.574 1.0 89.12 ? ? ? ? ? ? 198 TYR AA CA 1 81 A A +ATOM 3321 C C . TYR AA 1 81 ? -20.461 -17.776 22.587 1.0 85.78 ? ? ? ? ? ? 198 TYR AA C 1 81 A A +ATOM 3322 O O . TYR AA 1 81 ? -21.246 -16.903 22.954 1.0 80.49 ? ? ? ? ? ? 198 TYR AA O 1 81 A A +ATOM 3323 C CB . TYR AA 1 81 ? -18.497 -18.501 23.957 1.0 84.46 ? ? ? ? ? ? 198 TYR AA CB 1 81 A A +ATOM 3324 C CG . TYR AA 1 81 ? -18.138 -18.967 25.351 1.0 83.63 ? ? ? ? ? ? 198 TYR AA CG 1 81 A A +ATOM 3325 C CD1 . TYR AA 1 81 ? -19.110 -19.055 26.351 1.0 72.73 ? ? ? ? ? ? 198 TYR AA CD1 1 81 A A +ATOM 3326 C CD2 . TYR AA 1 81 ? -16.836 -19.353 25.664 1.0 78.08 ? ? ? ? ? ? 198 TYR AA CD2 1 81 A A +ATOM 3327 C CE1 . TYR AA 1 81 ? -18.793 -19.519 27.624 1.0 67.94 ? ? ? ? ? ? 198 TYR AA CE1 1 81 A A +ATOM 3328 C CE2 . TYR AA 1 81 ? -16.509 -19.818 26.934 1.0 72.97 ? ? ? ? ? ? 198 TYR AA CE2 1 81 A A +ATOM 3329 C CZ . TYR AA 1 81 ? -17.493 -19.898 27.907 1.0 71.06 ? ? ? ? ? ? 198 TYR AA CZ 1 81 A A +ATOM 3330 O OH . TYR AA 1 81 ? -17.171 -20.355 29.163 1.0 81.83 ? ? ? ? ? ? 198 TYR AA OH 1 81 A A +ATOM 3331 N N . LYS AA 1 82 ? -20.017 -17.855 21.339 1.0 92.31 ? ? ? ? ? ? 199 LYS AA N 1 82 A A +ATOM 3332 C CA . LYS AA 1 82 ? -20.483 -16.903 20.333 1.0 100.0 ? ? ? ? ? ? 199 LYS AA CA 1 82 A A +ATOM 3333 C C . LYS AA 1 82 ? -21.985 -17.087 20.163 1.0 100.0 ? ? ? ? ? ? 199 LYS AA C 1 82 A A +ATOM 3334 O O . LYS AA 1 82 ? -22.695 -16.194 19.690 1.0 100.0 ? ? ? ? ? ? 199 LYS AA O 1 82 A A +ATOM 3335 C CB . LYS AA 1 82 ? -19.783 -17.147 18.996 1.0 99.73 ? ? ? ? ? ? 199 LYS AA CB 1 82 A A +ATOM 3336 C CG . LYS AA 1 82 ? -19.765 -18.602 18.567 1.0 96.19 ? ? ? ? ? ? 199 LYS AA CG 1 82 A A +ATOM 3337 C CD . LYS AA 1 82 ? -18.726 -18.827 17.485 1.0 100.0 ? ? ? ? ? ? 199 LYS AA CD 1 82 A A +ATOM 3338 C CE . LYS AA 1 82 ? -17.325 -18.536 18.005 1.0 100.0 ? ? ? ? ? ? 199 LYS AA CE 1 82 A A +ATOM 3339 N NZ . LYS AA 1 82 ? -16.994 -19.346 19.216 1.0 100.0 ? ? ? ? ? ? 199 LYS AA NZ 1 82 A A +ATOM 3340 N N . THR AA 1 83 ? -22.463 -18.257 20.563 1.0 100.0 ? ? ? ? ? ? 200 THR AA N 1 83 A A +ATOM 3341 C CA . THR AA 1 83 ? -23.873 -18.579 20.456 1.0 98.21 ? ? ? ? ? ? 200 THR AA CA 1 83 A A +ATOM 3342 C C . THR AA 1 83 ? -24.681 -18.089 21.649 1.0 92.84 ? ? ? ? ? ? 200 THR AA C 1 83 A A +ATOM 3343 O O . THR AA 1 83 ? -25.482 -17.162 21.533 1.0 85.72 ? ? ? ? ? ? 200 THR AA O 1 83 A A +ATOM 3344 C CB . THR AA 1 83 ? -24.078 -20.096 20.325 1.0 100.0 ? ? ? ? ? ? 200 THR AA CB 1 83 A A +ATOM 3345 O OG1 . THR AA 1 83 ? -23.165 -20.617 19.352 1.0 100.0 ? ? ? ? ? ? 200 THR AA OG1 1 83 A A +ATOM 3346 C CG2 . THR AA 1 83 ? -25.509 -20.407 19.900 1.0 92.31 ? ? ? ? ? ? 200 THR AA CG2 1 83 A A +ATOM 3347 N N . HIS AA 1 84 ? -24.456 -18.718 22.798 1.0 91.59 ? ? ? ? ? ? 201 HIS AA N 1 84 A A +ATOM 3348 C CA . HIS AA 1 84 ? -25.186 -18.391 24.017 1.0 96.97 ? ? ? ? ? ? 201 HIS AA CA 1 84 A A +ATOM 3349 C C . HIS AA 1 84 ? -24.610 -17.287 24.913 1.0 98.81 ? ? ? ? ? ? 201 HIS AA C 1 84 A A +ATOM 3350 O O . HIS AA 1 84 ? -25.364 -16.570 25.575 1.0 100.0 ? ? ? ? ? ? 201 HIS AA O 1 84 A A +ATOM 3351 C CB . HIS AA 1 84 ? -25.375 -19.667 24.846 1.0 97.39 ? ? ? ? ? ? 201 HIS AA CB 1 84 A A +ATOM 3352 C CG . HIS AA 1 84 ? -26.025 -20.786 24.091 1.0 100.0 ? ? ? ? ? ? 201 HIS AA CG 1 84 A A +ATOM 3353 N ND1 . HIS AA 1 84 ? -27.146 -20.603 23.311 1.0 100.0 ? ? ? ? ? ? 201 HIS AA ND1 1 84 A A +ATOM 3354 C CD2 . HIS AA 1 84 ? -25.713 -22.100 24.001 1.0 100.0 ? ? ? ? ? ? 201 HIS AA CD2 1 84 A A +ATOM 3355 C CE1 . HIS AA 1 84 ? -27.500 -21.759 22.774 1.0 100.0 ? ? ? ? ? ? 201 HIS AA CE1 1 84 A A +ATOM 3356 N NE2 . HIS AA 1 84 ? -26.645 -22.683 23.178 1.0 100.0 ? ? ? ? ? ? 201 HIS AA NE2 1 84 A A +ATOM 3357 N N . ALA AA 1 85 ? -23.287 -17.146 24.943 1.0 99.97 ? ? ? ? ? ? 202 ALA AA N 1 85 A A +ATOM 3358 C CA . ALA AA 1 85 ? -22.655 -16.129 25.784 1.0 95.61 ? ? ? ? ? ? 202 ALA AA CA 1 85 A A +ATOM 3359 C C . ALA AA 1 85 ? -22.983 -14.706 25.342 1.0 92.19 ? ? ? ? ? ? 202 ALA AA C 1 85 A A +ATOM 3360 O O . ALA AA 1 85 ? -23.274 -14.458 24.172 1.0 83.66 ? ? ? ? ? ? 202 ALA AA O 1 85 A A +ATOM 3361 C CB . ALA AA 1 85 ? -21.146 -16.331 25.808 1.0 100.0 ? ? ? ? ? ? 202 ALA AA CB 1 85 A A +ATOM 3362 N N . CYS AA 1 86 ? -22.934 -13.777 26.294 1.0 88.73 ? ? ? ? ? ? 203 CYS AA N 1 86 A A +ATOM 3363 C CA . CYS AA 1 86 ? -23.229 -12.372 26.026 1.0 91.74 ? ? ? ? ? ? 203 CYS AA CA 1 86 A A +ATOM 3364 C C . CYS AA 1 86 ? -22.096 -11.663 25.285 1.0 89.57 ? ? ? ? ? ? 203 CYS AA C 1 86 A A +ATOM 3365 O O . CYS AA 1 86 ? -20.948 -12.113 25.292 1.0 90.42 ? ? ? ? ? ? 203 CYS AA O 1 86 A A +ATOM 3366 C CB . CYS AA 1 86 ? -23.538 -11.635 27.333 1.0 93.32 ? ? ? ? ? ? 203 CYS AA CB 1 86 A A +ATOM 3367 S SG . CYS AA 1 86 ? -22.107 -11.317 28.387 1.0 100.0 ? ? ? ? ? ? 203 CYS AA SG 1 86 A A +ATOM 3368 N N . TYR AA 1 87 ? -22.439 -10.547 24.651 1.0 89.75 ? ? ? ? ? ? 204 TYR AA N 1 87 A A +ATOM 3369 C CA . TYR AA 1 87 ? -21.493 -9.760 23.873 1.0 89.68 ? ? ? ? ? ? 204 TYR AA CA 1 87 A A +ATOM 3370 C C . TYR AA 1 87 ? -20.196 -9.418 24.596 1.0 92.54 ? ? ? ? ? ? 204 TYR AA C 1 87 A A +ATOM 3371 O O . TYR AA 1 87 ? -19.113 -9.750 24.120 1.0 100.0 ? ? ? ? ? ? 204 TYR AA O 1 87 A A +ATOM 3372 C CB . TYR AA 1 87 ? -22.171 -8.474 23.389 1.0 90.65 ? ? ? ? ? ? 204 TYR AA CB 1 87 A A +ATOM 3373 C CG . TYR AA 1 87 ? -21.211 -7.370 23.003 1.0 95.13 ? ? ? ? ? ? 204 TYR AA CG 1 87 A A +ATOM 3374 C CD1 . TYR AA 1 87 ? -20.216 -7.584 22.047 1.0 100.0 ? ? ? ? ? ? 204 TYR AA CD1 1 87 A A +ATOM 3375 C CD2 . TYR AA 1 87 ? -21.294 -6.110 23.595 1.0 100.0 ? ? ? ? ? ? 204 TYR AA CD2 1 87 A A +ATOM 3376 C CE1 . TYR AA 1 87 ? -19.327 -6.572 21.689 1.0 100.0 ? ? ? ? ? ? 204 TYR AA CE1 1 87 A A +ATOM 3377 C CE2 . TYR AA 1 87 ? -20.409 -5.089 23.245 1.0 100.0 ? ? ? ? ? ? 204 TYR AA CE2 1 87 A A +ATOM 3378 C CZ . TYR AA 1 87 ? -19.430 -5.329 22.291 1.0 100.0 ? ? ? ? ? ? 204 TYR AA CZ 1 87 A A +ATOM 3379 O OH . TYR AA 1 87 ? -18.557 -4.327 21.932 1.0 86.78 ? ? ? ? ? ? 204 TYR AA OH 1 87 A A +ATOM 3380 N N . GLU AA 1 88 ? -20.308 -8.744 25.737 1.0 96.85 ? ? ? ? ? ? 205 GLU AA N 1 88 A A +ATOM 3381 C CA . GLU AA 1 88 ? -19.130 -8.344 26.506 1.0 94.12 ? ? ? ? ? ? 205 GLU AA CA 1 88 A A +ATOM 3382 C C . GLU AA 1 88 ? -18.156 -9.503 26.679 1.0 92.18 ? ? ? ? ? ? 205 GLU AA C 1 88 A A +ATOM 3383 O O . GLU AA 1 88 ? -16.950 -9.300 26.839 1.0 76.01 ? ? ? ? ? ? 205 GLU AA O 1 88 A A +ATOM 3384 C CB . GLU AA 1 88 ? -19.548 -7.806 27.877 1.0 91.15 ? ? ? ? ? ? 205 GLU AA CB 1 88 A A +ATOM 3385 C CG . GLU AA 1 88 ? -20.523 -6.640 27.818 1.0 80.29 ? ? ? ? ? ? 205 GLU AA CG 1 88 A A +ATOM 3386 C CD . GLU AA 1 88 ? -21.914 -7.071 27.396 1.0 94.15 ? ? ? ? ? ? 205 GLU AA CD 1 88 A A +ATOM 3387 O OE1 . GLU AA 1 88 ? -22.687 -6.212 26.925 1.0 98.51 ? ? ? ? ? ? 205 GLU AA OE1 1 88 A A +ATOM 3388 O OE2 . GLU AA 1 88 ? -22.232 -8.272 27.537 1.0 100.0 ? ? ? ? ? ? 205 GLU AA OE2 1 88 A A +ATOM 3389 N N . TYR AA 1 89 ? -18.691 -10.721 26.640 1.0 90.46 ? ? ? ? ? ? 206 TYR AA N 1 89 A A +ATOM 3390 C CA . TYR AA 1 89 ? -17.886 -11.929 26.785 1.0 87.27 ? ? ? ? ? ? 206 TYR AA CA 1 89 A A +ATOM 3391 C C . TYR AA 1 89 ? -17.182 -12.227 25.471 1.0 87.37 ? ? ? ? ? ? 206 TYR AA C 1 89 A A +ATOM 3392 O O . TYR AA 1 89 ? -15.960 -12.373 25.426 1.0 90.91 ? ? ? ? ? ? 206 TYR AA O 1 89 A A +ATOM 3393 C CB . TYR AA 1 89 ? -18.781 -13.112 27.163 1.0 84.49 ? ? ? ? ? ? 206 TYR AA CB 1 89 A A +ATOM 3394 C CG . TYR AA 1 89 ? -18.039 -14.320 27.692 1.0 83.47 ? ? ? ? ? ? 206 TYR AA CG 1 89 A A +ATOM 3395 C CD1 . TYR AA 1 89 ? -18.252 -14.774 28.991 1.0 84.19 ? ? ? ? ? ? 206 TYR AA CD1 1 89 A A +ATOM 3396 C CD2 . TYR AA 1 89 ? -17.140 -15.020 26.888 1.0 81.07 ? ? ? ? ? ? 206 TYR AA CD2 1 89 A A +ATOM 3397 C CE1 . TYR AA 1 89 ? -17.591 -15.896 29.480 1.0 81.36 ? ? ? ? ? ? 206 TYR AA CE1 1 89 A A +ATOM 3398 C CE2 . TYR AA 1 89 ? -16.473 -16.146 27.368 1.0 88.23 ? ? ? ? ? ? 206 TYR AA CE2 1 89 A A +ATOM 3399 C CZ . TYR AA 1 89 ? -16.705 -16.578 28.665 1.0 88.88 ? ? ? ? ? ? 206 TYR AA CZ 1 89 A A +ATOM 3400 O OH . TYR AA 1 89 ? -16.052 -17.690 29.148 1.0 86.93 ? ? ? ? ? ? 206 TYR AA OH 1 89 A A +ATOM 3401 N N . ASN AA 1 90 ? -17.973 -12.318 24.404 1.0 83.68 ? ? ? ? ? ? 207 ASN AA N 1 90 A A +ATOM 3402 C CA . ASN AA 1 90 ? -17.459 -12.606 23.070 1.0 85.33 ? ? ? ? ? ? 207 ASN AA CA 1 90 A A +ATOM 3403 C C . ASN AA 1 90 ? -16.477 -11.544 22.587 1.0 87.45 ? ? ? ? ? ? 207 ASN AA C 1 90 A A +ATOM 3404 O O . ASN AA 1 90 ? -15.662 -11.802 21.701 1.0 84.26 ? ? ? ? ? ? 207 ASN AA O 1 90 A A +ATOM 3405 C CB . ASN AA 1 90 ? -18.617 -12.723 22.079 1.0 86.6 ? ? ? ? ? ? 207 ASN AA CB 1 90 A A +ATOM 3406 C CG . ASN AA 1 90 ? -19.554 -13.870 22.410 1.0 100.0 ? ? ? ? ? ? 207 ASN AA CG 1 90 A A +ATOM 3407 O OD1 . ASN AA 1 90 ? -19.145 -15.032 22.437 1.0 100.0 ? ? ? ? ? ? 207 ASN AA OD1 1 90 A A +ATOM 3408 N ND2 . ASN AA 1 90 ? -20.816 -13.549 22.667 1.0 100.0 ? ? ? ? ? ? 207 ASN AA ND2 1 90 A A +ATOM 3409 N N . HIS AA 1 91 ? -16.559 -10.355 23.177 1.0 89.56 ? ? ? ? ? ? 208 HIS AA N 1 91 A A +ATOM 3410 C CA . HIS AA 1 91 ? -15.675 -9.256 22.801 1.0 85.85 ? ? ? ? ? ? 208 HIS AA CA 1 91 A A +ATOM 3411 C C . HIS AA 1 91 ? -14.300 -9.390 23.444 1.0 76.51 ? ? ? ? ? ? 208 HIS AA C 1 91 A A +ATOM 3412 O O . HIS AA 1 91 ? -13.270 -9.293 22.773 1.0 63.62 ? ? ? ? ? ? 208 HIS AA O 1 91 A A +ATOM 3413 C CB . HIS AA 1 91 ? -16.291 -7.910 23.208 1.0 73.65 ? ? ? ? ? ? 208 HIS AA CB 1 91 A A +ATOM 3414 C CG . HIS AA 1 91 ? -15.307 -6.779 23.217 1.0 75.73 ? ? ? ? ? ? 208 HIS AA CG 1 91 A A +ATOM 3415 N ND1 . HIS AA 1 91 ? -15.065 -6.011 24.338 1.0 67.92 ? ? ? ? ? ? 208 HIS AA ND1 1 91 A A +ATOM 3416 C CD2 . HIS AA 1 91 ? -14.483 -6.303 22.255 1.0 87.75 ? ? ? ? ? ? 208 HIS AA CD2 1 91 A A +ATOM 3417 C CE1 . HIS AA 1 91 ? -14.135 -5.114 24.063 1.0 66.17 ? ? ? ? ? ? 208 HIS AA CE1 1 91 A A +ATOM 3418 N NE2 . HIS AA 1 91 ? -13.764 -5.269 22.804 1.0 74.7 ? ? ? ? ? ? 208 HIS AA NE2 1 91 A A +ATOM 3419 N N . ILE AA 1 92 ? -14.291 -9.616 24.750 1.0 70.01 ? ? ? ? ? ? 209 ILE AA N 1 92 A A +ATOM 3420 C CA . ILE AA 1 92 ? -13.046 -9.732 25.496 1.0 76.07 ? ? ? ? ? ? 209 ILE AA CA 1 92 A A +ATOM 3421 C C . ILE AA 1 92 ? -12.272 -11.036 25.306 1.0 81.86 ? ? ? ? ? ? 209 ILE AA C 1 92 A A +ATOM 3422 O O . ILE AA 1 92 ? -11.046 -11.058 25.435 1.0 81.22 ? ? ? ? ? ? 209 ILE AA O 1 92 A A +ATOM 3423 C CB . ILE AA 1 92 ? -13.301 -9.543 27.007 1.0 73.26 ? ? ? ? ? ? 209 ILE AA CB 1 92 A A +ATOM 3424 C CG1 . ILE AA 1 92 ? -11.966 -9.400 27.743 1.0 57.57 ? ? ? ? ? ? 209 ILE AA CG1 1 92 A A +ATOM 3425 C CG2 . ILE AA 1 92 ? -14.105 -10.722 27.549 1.0 70.08 ? ? ? ? ? ? 209 ILE AA CG2 1 92 A A +ATOM 3426 C CD1 . ILE AA 1 92 ? -11.161 -8.202 27.302 1.0 52.0 ? ? ? ? ? ? 209 ILE AA CD1 1 92 A A +ATOM 3427 N N . PHE AA 1 93 ? -12.982 -12.120 24.999 1.0 85.71 ? ? ? ? ? ? 210 PHE AA N 1 93 A A +ATOM 3428 C CA . PHE AA 1 93 ? -12.337 -13.419 24.826 1.0 75.69 ? ? ? ? ? ? 210 PHE AA CA 1 93 A A +ATOM 3429 C C . PHE AA 1 93 ? -11.109 -13.406 23.929 1.0 76.41 ? ? ? ? ? ? 210 PHE AA C 1 93 A A +ATOM 3430 O O . PHE AA 1 93 ? -10.012 -13.742 24.372 1.0 73.65 ? ? ? ? ? ? 210 PHE AA O 1 93 A A +ATOM 3431 C CB . PHE AA 1 93 ? -13.331 -14.456 24.305 1.0 72.53 ? ? ? ? ? ? 210 PHE AA CB 1 93 A A +ATOM 3432 C CG . PHE AA 1 93 ? -13.218 -15.792 24.985 1.0 89.37 ? ? ? ? ? ? 210 PHE AA CG 1 93 A A +ATOM 3433 C CD1 . PHE AA 1 93 ? -13.048 -16.959 24.246 1.0 100.0 ? ? ? ? ? ? 210 PHE AA CD1 1 93 A A +ATOM 3434 C CD2 . PHE AA 1 93 ? -13.282 -15.883 26.371 1.0 100.0 ? ? ? ? ? ? 210 PHE AA CD2 1 93 A A +ATOM 3435 C CE1 . PHE AA 1 93 ? -12.944 -18.200 24.881 1.0 100.0 ? ? ? ? ? ? 210 PHE AA CE1 1 93 A A +ATOM 3436 C CE2 . PHE AA 1 93 ? -13.179 -17.119 27.015 1.0 100.0 ? ? ? ? ? ? 210 PHE AA CE2 1 93 A A +ATOM 3437 C CZ . PHE AA 1 93 ? -13.011 -18.280 26.265 1.0 98.73 ? ? ? ? ? ? 210 PHE AA CZ 1 93 A A +ATOM 3438 N N . PRO AA 1 94 ? -11.270 -13.005 22.655 1.0 78.71 ? ? ? ? ? ? 211 PRO AA N 1 94 A A +ATOM 3439 C CA . PRO AA 1 94 ? -10.091 -12.997 21.782 1.0 72.51 ? ? ? ? ? ? 211 PRO AA CA 1 94 A A +ATOM 3440 C C . PRO AA 1 94 ? -8.915 -12.220 22.364 1.0 66.57 ? ? ? ? ? ? 211 PRO AA C 1 94 A A +ATOM 3441 O O . PRO AA 1 94 ? -7.770 -12.426 21.961 1.0 66.09 ? ? ? ? ? ? 211 PRO AA O 1 94 A A +ATOM 3442 C CB . PRO AA 1 94 ? -10.611 -12.386 20.482 1.0 88.21 ? ? ? ? ? ? 211 PRO AA CB 1 94 A A +ATOM 3443 C CG . PRO AA 1 94 ? -12.090 -12.579 20.524 1.0 89.51 ? ? ? ? ? ? 211 PRO AA CG 1 94 A A +ATOM 3444 C CD . PRO AA 1 94 ? -12.479 -12.527 21.966 1.0 79.55 ? ? ? ? ? ? 211 PRO AA CD 1 94 A A +ATOM 3445 N N . LEU AA 1 95 ? -9.199 -11.331 23.313 1.0 67.37 ? ? ? ? ? ? 212 LEU AA N 1 95 A A +ATOM 3446 C CA . LEU AA 1 95 ? -8.153 -10.536 23.954 1.0 76.53 ? ? ? ? ? ? 212 LEU AA CA 1 95 A A +ATOM 3447 C C . LEU AA 1 95 ? -7.555 -11.345 25.098 1.0 80.7 ? ? ? ? ? ? 212 LEU AA C 1 95 A A +ATOM 3448 O O . LEU AA 1 95 ? -6.372 -11.218 25.411 1.0 72.08 ? ? ? ? ? ? 212 LEU AA O 1 95 A A +ATOM 3449 C CB . LEU AA 1 95 ? -8.730 -9.226 24.500 1.0 72.65 ? ? ? ? ? ? 212 LEU AA CB 1 95 A A +ATOM 3450 C CG . LEU AA 1 95 ? -9.198 -8.182 23.483 1.0 53.72 ? ? ? ? ? ? 212 LEU AA CG 1 95 A A +ATOM 3451 C CD1 . LEU AA 1 95 ? -10.195 -7.248 24.147 1.0 47.91 ? ? ? ? ? ? 212 LEU AA CD1 1 95 A A +ATOM 3452 C CD2 . LEU AA 1 95 ? -7.999 -7.415 22.942 1.0 26.98 ? ? ? ? ? ? 212 LEU AA CD2 1 95 A A +ATOM 3453 N N . LEU AA 1 96 ? -8.390 -12.170 25.725 1.0 79.57 ? ? ? ? ? ? 213 LEU AA N 1 96 A A +ATOM 3454 C CA . LEU AA 1 96 ? -7.953 -13.025 26.824 1.0 73.46 ? ? ? ? ? ? 213 LEU AA CA 1 96 A A +ATOM 3455 C C . LEU AA 1 96 ? -7.098 -14.134 26.220 1.0 75.68 ? ? ? ? ? ? 213 LEU AA C 1 96 A A +ATOM 3456 O O . LEU AA 1 96 ? -6.058 -14.507 26.762 1.0 73.21 ? ? ? ? ? ? 213 LEU AA O 1 96 A A +ATOM 3457 C CB . LEU AA 1 96 ? -9.161 -13.643 27.526 1.0 60.67 ? ? ? ? ? ? 213 LEU AA CB 1 96 A A +ATOM 3458 C CG . LEU AA 1 96 ? -9.931 -12.760 28.508 1.0 68.02 ? ? ? ? ? ? 213 LEU AA CG 1 96 A A +ATOM 3459 C CD1 . LEU AA 1 96 ? -11.283 -13.402 28.811 1.0 61.82 ? ? ? ? ? ? 213 LEU AA CD1 1 96 A A +ATOM 3460 C CD2 . LEU AA 1 96 ? -9.116 -12.575 29.779 1.0 51.97 ? ? ? ? ? ? 213 LEU AA CD2 1 96 A A +ATOM 3461 N N . GLU AA 1 97 ? -7.559 -14.657 25.089 1.0 80.67 ? ? ? ? ? ? 214 GLU AA N 1 97 A A +ATOM 3462 C CA . GLU AA 1 97 ? -6.852 -15.716 24.390 1.0 78.9 ? ? ? ? ? ? 214 GLU AA CA 1 97 A A +ATOM 3463 C C . GLU AA 1 97 ? -5.519 -15.192 23.871 1.0 76.25 ? ? ? ? ? ? 214 GLU AA C 1 97 A A +ATOM 3464 O O . GLU AA 1 97 ? -4.478 -15.817 24.058 1.0 82.01 ? ? ? ? ? ? 214 GLU AA O 1 97 A A +ATOM 3465 C CB . GLU AA 1 97 ? -7.700 -16.233 23.224 1.0 84.27 ? ? ? ? ? ? 214 GLU AA CB 1 97 A A +ATOM 3466 C CG . GLU AA 1 97 ? -9.096 -16.679 23.628 1.0 97.39 ? ? ? ? ? ? 214 GLU AA CG 1 97 A A +ATOM 3467 C CD . GLU AA 1 97 ? -9.943 -17.097 22.439 1.0 100.0 ? ? ? ? ? ? 214 GLU AA CD 1 97 A A +ATOM 3468 O OE1 . GLU AA 1 97 ? -10.886 -16.354 22.086 1.0 100.0 ? ? ? ? ? ? 214 GLU AA OE1 1 97 A A +ATOM 3469 O OE2 . GLU AA 1 97 ? -9.667 -18.171 21.857 1.0 100.0 ? ? ? ? ? ? 214 GLU AA OE2 1 97 A A +ATOM 3470 N N . LYS AA 1 98 ? -5.560 -14.032 23.224 1.0 70.39 ? ? ? ? ? ? 215 LYS AA N 1 98 A A +ATOM 3471 C CA . LYS AA 1 98 ? -4.360 -13.427 22.665 1.0 70.4 ? ? ? ? ? ? 215 LYS AA CA 1 98 A A +ATOM 3472 C C . LYS AA 1 98 ? -3.421 -12.825 23.709 1.0 79.87 ? ? ? ? ? ? 215 LYS AA C 1 98 A A +ATOM 3473 O O . LYS AA 1 98 ? -2.264 -12.529 23.405 1.0 91.68 ? ? ? ? ? ? 215 LYS AA O 1 98 A A +ATOM 3474 C CB . LYS AA 1 98 ? -4.743 -12.337 21.661 1.0 72.12 ? ? ? ? ? ? 215 LYS AA CB 1 98 A A +ATOM 3475 C CG . LYS AA 1 98 ? -3.553 -11.754 20.915 1.0 92.07 ? ? ? ? ? ? 215 LYS AA CG 1 98 A A +ATOM 3476 C CD . LYS AA 1 98 ? -3.977 -10.687 19.919 1.0 96.37 ? ? ? ? ? ? 215 LYS AA CD 1 98 A A +ATOM 3477 C CE . LYS AA 1 98 ? -4.615 -11.310 18.686 1.0 100.0 ? ? ? ? ? ? 215 LYS AA CE 1 98 A A +ATOM 3478 N NZ . LYS AA 1 98 ? -3.671 -12.187 17.935 1.0 100.0 ? ? ? ? ? ? 215 LYS AA NZ 1 98 A A +ATOM 3479 N N . TYR AA 1 99 ? -3.902 -12.649 24.936 1.0 84.91 ? ? ? ? ? ? 216 TYR AA N 1 99 A A +ATOM 3480 C CA . TYR AA 1 99 ? -3.066 -12.042 25.966 1.0 91.21 ? ? ? ? ? ? 216 TYR AA CA 1 99 A A +ATOM 3481 C C . TYR AA 1 99 ? -2.735 -12.869 27.204 1.0 87.96 ? ? ? ? ? ? 216 TYR AA C 1 99 A A +ATOM 3482 O O . TYR AA 1 99 ? -1.563 -13.088 27.509 1.0 84.66 ? ? ? ? ? ? 216 TYR AA O 1 99 A A +ATOM 3483 C CB . TYR AA 1 99 ? -3.680 -10.704 26.382 1.0 94.0 ? ? ? ? ? ? 216 TYR AA CB 1 99 A A +ATOM 3484 C CG . TYR AA 1 99 ? -3.548 -9.650 25.311 1.0 100.0 ? ? ? ? ? ? 216 TYR AA CG 1 99 A A +ATOM 3485 C CD1 . TYR AA 1 99 ? -4.631 -9.307 24.499 1.0 96.76 ? ? ? ? ? ? 216 TYR AA CD1 1 99 A A +ATOM 3486 C CD2 . TYR AA 1 99 ? -2.328 -9.016 25.085 1.0 100.0 ? ? ? ? ? ? 216 TYR AA CD2 1 99 A A +ATOM 3487 C CE1 . TYR AA 1 99 ? -4.498 -8.361 23.486 1.0 96.2 ? ? ? ? ? ? 216 TYR AA CE1 1 99 A A +ATOM 3488 C CE2 . TYR AA 1 99 ? -2.184 -8.070 24.077 1.0 100.0 ? ? ? ? ? ? 216 TYR AA CE2 1 99 A A +ATOM 3489 C CZ . TYR AA 1 99 ? -3.270 -7.746 23.280 1.0 100.0 ? ? ? ? ? ? 216 TYR AA CZ 1 99 A A +ATOM 3490 O OH . TYR AA 1 99 ? -3.124 -6.811 22.277 1.0 100.0 ? ? ? ? ? ? 216 TYR AA OH 1 99 A A +ATOM 3491 N N . CYS AA 1 100 ? -3.753 -13.332 27.917 1.0 77.03 ? ? ? ? ? ? 217 CYS AA N 1 100 A A +ATOM 3492 C CA . CYS AA 1 100 ? -3.517 -14.108 29.128 1.0 82.44 ? ? ? ? ? ? 217 CYS AA CA 1 100 A A +ATOM 3493 C C . CYS AA 1 100 ? -3.332 -15.607 28.906 1.0 87.08 ? ? ? ? ? ? 217 CYS AA C 1 100 A A +ATOM 3494 O O . CYS AA 1 100 ? -3.512 -16.409 29.825 1.0 93.26 ? ? ? ? ? ? 217 CYS AA O 1 100 A A +ATOM 3495 C CB . CYS AA 1 100 ? -4.654 -13.869 30.120 1.0 89.04 ? ? ? ? ? ? 217 CYS AA CB 1 100 A A +ATOM 3496 S SG . CYS AA 1 100 ? -4.645 -12.215 30.832 1.0 100.0 ? ? ? ? ? ? 217 CYS AA SG 1 100 A A +ATOM 3497 N N . GLY AA 1 101 ? -2.964 -15.980 27.687 1.0 85.81 ? ? ? ? ? ? 218 GLY AA N 1 101 A A +ATOM 3498 C CA . GLY AA 1 101 ? -2.750 -17.379 27.378 1.0 87.04 ? ? ? ? ? ? 218 GLY AA CA 1 101 A A +ATOM 3499 C C . GLY AA 1 101 ? -3.977 -18.261 27.499 1.0 86.37 ? ? ? ? ? ? 218 GLY AA C 1 101 A A +ATOM 3500 O O . GLY AA 1 101 ? -3.899 -19.374 28.020 1.0 90.0 ? ? ? ? ? ? 218 GLY AA O 1 101 A A +ATOM 3501 N N . PHE AA 1 102 ? -5.113 -17.770 27.016 1.0 79.48 ? ? ? ? ? ? 219 PHE AA N 1 102 A A +ATOM 3502 C CA . PHE AA 1 102 ? -6.347 -18.543 27.070 1.0 73.33 ? ? ? ? ? ? 219 PHE AA CA 1 102 A A +ATOM 3503 C C . PHE AA 1 102 ? -6.416 -19.483 25.874 1.0 79.58 ? ? ? ? ? ? 219 PHE AA C 1 102 A A +ATOM 3504 O O . PHE AA 1 102 ? -6.938 -19.127 24.823 1.0 87.13 ? ? ? ? ? ? 219 PHE AA O 1 102 A A +ATOM 3505 C CB . PHE AA 1 102 ? -7.560 -17.608 27.084 1.0 54.87 ? ? ? ? ? ? 219 PHE AA CB 1 102 A A +ATOM 3506 C CG . PHE AA 1 102 ? -8.046 -17.268 28.469 1.0 54.38 ? ? ? ? ? ? 219 PHE AA CG 1 102 A A +ATOM 3507 C CD1 . PHE AA 1 102 ? -7.226 -16.569 29.355 1.0 47.42 ? ? ? ? ? ? 219 PHE AA CD1 1 102 A A +ATOM 3508 C CD2 . PHE AA 1 102 ? -9.315 -17.657 28.898 1.0 38.98 ? ? ? ? ? ? 219 PHE AA CD2 1 102 A A +ATOM 3509 C CE1 . PHE AA 1 102 ? -7.663 -16.254 30.645 1.0 33.19 ? ? ? ? ? ? 219 PHE AA CE1 1 102 A A +ATOM 3510 C CE2 . PHE AA 1 102 ? -9.762 -17.348 30.186 1.0 31.12 ? ? ? ? ? ? 219 PHE AA CE2 1 102 A A +ATOM 3511 C CZ . PHE AA 1 102 ? -8.935 -16.649 31.061 1.0 35.16 ? ? ? ? ? ? 219 PHE AA CZ 1 102 A A +ATOM 3512 N N . HIS AA 1 103 ? -5.869 -20.683 26.047 1.0 83.06 ? ? ? ? ? ? 220 HIS AA N 1 103 A A +ATOM 3513 C CA . HIS AA 1 103 ? -5.850 -21.702 25.001 1.0 90.4 ? ? ? ? ? ? 220 HIS AA CA 1 103 A A +ATOM 3514 C C . HIS AA 1 103 ? -6.060 -23.066 25.654 1.0 93.84 ? ? ? ? ? ? 220 HIS AA C 1 103 A A +ATOM 3515 O O . HIS AA 1 103 ? -5.609 -23.292 26.778 1.0 100.0 ? ? ? ? ? ? 220 HIS AA O 1 103 A A +ATOM 3516 C CB . HIS AA 1 103 ? -4.508 -21.680 24.267 1.0 90.54 ? ? ? ? ? ? 220 HIS AA CB 1 103 A A +ATOM 3517 C CG . HIS AA 1 103 ? -4.476 -22.525 23.033 1.0 100.0 ? ? ? ? ? ? 220 HIS AA CG 1 103 A A +ATOM 3518 N ND1 . HIS AA 1 103 ? -3.312 -23.067 22.531 1.0 100.0 ? ? ? ? ? ? 220 HIS AA ND1 1 103 A A +ATOM 3519 C CD2 . HIS AA 1 103 ? -5.465 -22.917 22.190 1.0 97.71 ? ? ? ? ? ? 220 HIS AA CD2 1 103 A A +ATOM 3520 C CE1 . HIS AA 1 103 ? -3.582 -23.751 21.436 1.0 100.0 ? ? ? ? ? ? 220 HIS AA CE1 1 103 A A +ATOM 3521 N NE2 . HIS AA 1 103 ? -4.882 -23.676 21.207 1.0 99.67 ? ? ? ? ? ? 220 HIS AA NE2 1 103 A A +ATOM 3522 N N . GLU AA 1 104 ? -6.734 -23.974 24.955 1.0 81.93 ? ? ? ? ? ? 221 GLU AA N 1 104 A A +ATOM 3523 C CA . GLU AA 1 104 ? -6.998 -25.299 25.508 1.0 73.21 ? ? ? ? ? ? 221 GLU AA CA 1 104 A A +ATOM 3524 C C . GLU AA 1 104 ? -5.745 -26.091 25.849 1.0 66.02 ? ? ? ? ? ? 221 GLU AA C 1 104 A A +ATOM 3525 O O . GLU AA 1 104 ? -5.819 -27.087 26.569 1.0 76.25 ? ? ? ? ? ? 221 GLU AA O 1 104 A A +ATOM 3526 C CB . GLU AA 1 104 ? -7.859 -26.112 24.544 1.0 74.49 ? ? ? ? ? ? 221 GLU AA CB 1 104 A A +ATOM 3527 C CG . GLU AA 1 104 ? -7.301 -26.198 23.140 1.0 91.38 ? ? ? ? ? ? 221 GLU AA CG 1 104 A A +ATOM 3528 C CD . GLU AA 1 104 ? -8.147 -27.077 22.243 1.0 100.0 ? ? ? ? ? ? 221 GLU AA CD 1 104 A A +ATOM 3529 O OE1 . GLU AA 1 104 ? -7.683 -27.422 21.134 1.0 100.0 ? ? ? ? ? ? 221 GLU AA OE1 1 104 A A +ATOM 3530 O OE2 . GLU AA 1 104 ? -9.278 -27.424 22.649 1.0 92.36 ? ? ? ? ? ? 221 GLU AA OE2 1 104 A A +ATOM 3531 N N . ASP AA 1 105 ? -4.596 -25.649 25.345 1.0 58.15 ? ? ? ? ? ? 222 ASP AA N 1 105 A A +ATOM 3532 C CA . ASP AA 1 105 ? -3.347 -26.358 25.603 1.0 64.41 ? ? ? ? ? ? 222 ASP AA CA 1 105 A A +ATOM 3533 C C . ASP AA 1 105 ? -2.554 -25.852 26.799 1.0 60.43 ? ? ? ? ? ? 222 ASP AA C 1 105 A A +ATOM 3534 O O . ASP AA 1 105 ? -1.580 -26.483 27.216 1.0 53.79 ? ? ? ? ? ? 222 ASP AA O 1 105 A A +ATOM 3535 C CB . ASP AA 1 105 ? -2.470 -26.330 24.355 1.0 82.99 ? ? ? ? ? ? 222 ASP AA CB 1 105 A A +ATOM 3536 C CG . ASP AA 1 105 ? -3.020 -27.201 23.246 1.0 97.61 ? ? ? ? ? ? 222 ASP AA CG 1 105 A A +ATOM 3537 O OD1 . ASP AA 1 105 ? -4.029 -26.797 22.631 1.0 100.0 ? ? ? ? ? ? 222 ASP AA OD1 1 105 A A +ATOM 3538 O OD2 . ASP AA 1 105 ? -2.453 -28.288 22.995 1.0 91.26 ? ? ? ? ? ? 222 ASP AA OD2 1 105 A A +ATOM 3539 N N . ASN AA 1 106 ? -2.966 -24.720 27.357 1.0 56.54 ? ? ? ? ? ? 223 ASN AA N 1 106 A A +ATOM 3540 C CA . ASN AA 1 106 ? -2.270 -24.166 28.510 1.0 56.77 ? ? ? ? ? ? 223 ASN AA CA 1 106 A A +ATOM 3541 C C . ASN AA 1 106 ? -3.212 -23.484 29.491 1.0 53.96 ? ? ? ? ? ? 223 ASN AA C 1 106 A A +ATOM 3542 O O . ASN AA 1 106 ? -4.068 -22.694 29.094 1.0 51.52 ? ? ? ? ? ? 223 ASN AA O 1 106 A A +ATOM 3543 C CB . ASN AA 1 106 ? -1.202 -23.168 28.063 1.0 72.23 ? ? ? ? ? ? 223 ASN AA CB 1 106 A A +ATOM 3544 C CG . ASN AA 1 106 ? -0.592 -22.409 29.233 1.0 93.67 ? ? ? ? ? ? 223 ASN AA CG 1 106 A A +ATOM 3545 O OD1 . ASN AA 1 106 ? -0.796 -21.203 29.378 1.0 100.0 ? ? ? ? ? ? 223 ASN AA OD1 1 106 A A +ATOM 3546 N ND2 . ASN AA 1 106 ? 0.157 -23.116 30.077 1.0 88.6 ? ? ? ? ? ? 223 ASN AA ND2 1 106 A A +ATOM 3547 N N . ILE AA 1 107 ? -3.048 -23.795 30.776 1.0 60.64 ? ? ? ? ? ? 224 ILE AA N 1 107 A A +ATOM 3548 C CA . ILE AA 1 107 ? -3.874 -23.199 31.821 1.0 57.31 ? ? ? ? ? ? 224 ILE AA CA 1 107 A A +ATOM 3549 C C . ILE AA 1 107 ? -3.317 -21.820 32.168 1.0 50.66 ? ? ? ? ? ? 224 ILE AA C 1 107 A A +ATOM 3550 O O . ILE AA 1 107 ? -2.154 -21.687 32.545 1.0 49.35 ? ? ? ? ? ? 224 ILE AA O 1 107 A A +ATOM 3551 C CB . ILE AA 1 107 ? -3.891 -24.075 33.087 1.0 49.19 ? ? ? ? ? ? 224 ILE AA CB 1 107 A A +ATOM 3552 C CG1 . ILE AA 1 107 ? -4.666 -25.366 32.809 1.0 46.06 ? ? ? ? ? ? 224 ILE AA CG1 1 107 A A +ATOM 3553 C CG2 . ILE AA 1 107 ? -4.534 -23.311 34.230 1.0 48.55 ? ? ? ? ? ? 224 ILE AA CG2 1 107 A A +ATOM 3554 C CD1 . ILE AA 1 107 ? -4.785 -26.285 34.008 1.0 49.6 ? ? ? ? ? ? 224 ILE AA CD1 1 107 A A +ATOM 3555 N N . PRO AA 1 108 ? -4.153 -20.775 32.057 1.0 38.91 ? ? ? ? ? ? 225 PRO AA N 1 108 A A +ATOM 3556 C CA . PRO AA 1 108 ? -3.742 -19.398 32.349 1.0 39.74 ? ? ? ? ? ? 225 PRO AA CA 1 108 A A +ATOM 3557 C C . PRO AA 1 108 ? -3.279 -19.151 33.780 1.0 43.17 ? ? ? ? ? ? 225 PRO AA C 1 108 A A +ATOM 3558 O O . PRO AA 1 108 ? -3.901 -19.618 34.734 1.0 45.06 ? ? ? ? ? ? 225 PRO AA O 1 108 A A +ATOM 3559 C CB . PRO AA 1 108 ? -4.974 -18.562 32.000 1.0 48.74 ? ? ? ? ? ? 225 PRO AA CB 1 108 A A +ATOM 3560 C CG . PRO AA 1 108 ? -5.862 -19.466 31.220 1.0 63.06 ? ? ? ? ? ? 225 PRO AA CG 1 108 A A +ATOM 3561 C CD . PRO AA 1 108 ? -5.569 -20.851 31.671 1.0 51.19 ? ? ? ? ? ? 225 PRO AA CD 1 108 A A +ATOM 3562 N N . GLN AA 1 109 ? -2.190 -18.397 33.914 1.0 38.21 ? ? ? ? ? ? 226 GLN AA N 1 109 A A +ATOM 3563 C CA . GLN AA 1 109 ? -1.632 -18.070 35.219 1.0 50.78 ? ? ? ? ? ? 226 GLN AA CA 1 109 A A +ATOM 3564 C C . GLN AA 1 109 ? -2.318 -16.846 35.822 1.0 50.49 ? ? ? ? ? ? 226 GLN AA C 1 109 A A +ATOM 3565 O O . GLN AA 1 109 ? -2.406 -15.795 35.187 1.0 46.1 ? ? ? ? ? ? 226 GLN AA O 1 109 A A +ATOM 3566 C CB . GLN AA 1 109 ? -0.123 -17.821 35.107 1.0 59.66 ? ? ? ? ? ? 226 GLN AA CB 1 109 A A +ATOM 3567 C CG . GLN AA 1 109 ? 0.703 -19.080 34.851 1.0 64.83 ? ? ? ? ? ? 226 GLN AA CG 1 109 A A +ATOM 3568 C CD . GLN AA 1 109 ? 0.761 -20.022 36.051 1.0 72.4 ? ? ? ? ? ? 226 GLN AA CD 1 109 A A +ATOM 3569 O OE1 . GLN AA 1 109 ? 1.769 -20.693 36.276 1.0 78.96 ? ? ? ? ? ? 226 GLN AA OE1 1 109 A A +ATOM 3570 N NE2 . GLN AA 1 109 ? -0.320 -20.076 36.824 1.0 81.37 ? ? ? ? ? ? 226 GLN AA NE2 1 109 A A +ATOM 3571 N N . LEU AA 1 110 ? -2.785 -16.999 37.060 1.0 53.52 ? ? ? ? ? ? 227 LEU AA N 1 110 A A +ATOM 3572 C CA . LEU AA 1 110 ? -3.484 -15.941 37.782 1.0 51.51 ? ? ? ? ? ? 227 LEU AA CA 1 110 A A +ATOM 3573 C C . LEU AA 1 110 ? -2.785 -14.586 37.796 1.0 54.39 ? ? ? ? ? ? 227 LEU AA C 1 110 A A +ATOM 3574 O O . LEU AA 1 110 ? -3.432 -13.552 37.620 1.0 47.39 ? ? ? ? ? ? 227 LEU AA O 1 110 A A +ATOM 3575 C CB . LEU AA 1 110 ? -3.759 -16.388 39.221 1.0 32.21 ? ? ? ? ? ? 227 LEU AA CB 1 110 A A +ATOM 3576 C CG . LEU AA 1 110 ? -4.635 -17.632 39.415 1.0 50.79 ? ? ? ? ? ? 227 LEU AA CG 1 110 A A +ATOM 3577 C CD1 . LEU AA 1 110 ? -5.361 -17.533 40.753 1.0 37.22 ? ? ? ? ? ? 227 LEU AA CD1 1 110 A A +ATOM 3578 C CD2 . LEU AA 1 110 ? -5.642 -17.760 38.280 1.0 43.31 ? ? ? ? ? ? 227 LEU AA CD2 1 110 A A +ATOM 3579 N N . GLU AA 1 111 ? -1.475 -14.580 38.012 1.0 52.15 ? ? ? ? ? ? 228 GLU AA N 1 111 A A +ATOM 3580 C CA . GLU AA 1 111 ? -0.738 -13.322 38.040 1.0 45.45 ? ? ? ? ? ? 228 GLU AA CA 1 111 A A +ATOM 3581 C C . GLU AA 1 111 ? -0.947 -12.561 36.739 1.0 46.15 ? ? ? ? ? ? 228 GLU AA C 1 111 A A +ATOM 3582 O O . GLU AA 1 111 ? -0.975 -11.332 36.725 1.0 43.58 ? ? ? ? ? ? 228 GLU AA O 1 111 A A +ATOM 3583 C CB . GLU AA 1 111 ? 0.751 -13.580 38.247 1.0 42.63 ? ? ? ? ? ? 228 GLU AA CB 1 111 A A +ATOM 3584 C CG . GLU AA 1 111 ? 1.372 -12.739 39.348 1.0 58.54 ? ? ? ? ? ? 228 GLU AA CG 1 111 A A +ATOM 3585 C CD . GLU AA 1 111 ? 0.878 -11.303 39.351 1.0 53.14 ? ? ? ? ? ? 228 GLU AA CD 1 111 A A +ATOM 3586 O OE1 . GLU AA 1 111 ? -0.194 -11.047 39.931 1.0 60.98 ? ? ? ? ? ? 228 GLU AA OE1 1 111 A A +ATOM 3587 O OE2 . GLU AA 1 111 ? 1.563 -10.430 38.780 1.0 59.24 ? ? ? ? ? ? 228 GLU AA OE2 1 111 A A +ATOM 3588 N N . ASP AA 1 112 ? -1.098 -13.307 35.650 1.0 39.29 ? ? ? ? ? ? 229 ASP AA N 1 112 A A +ATOM 3589 C CA . ASP AA 1 112 ? -1.306 -12.721 34.331 1.0 45.38 ? ? ? ? ? ? 229 ASP AA CA 1 112 A A +ATOM 3590 C C . ASP AA 1 112 ? -2.716 -12.165 34.228 1.0 42.03 ? ? ? ? ? ? 229 ASP AA C 1 112 A A +ATOM 3591 O O . ASP AA 1 112 ? -2.916 -10.993 33.903 1.0 43.4 ? ? ? ? ? ? 229 ASP AA O 1 112 A A +ATOM 3592 C CB . ASP AA 1 112 ? -1.090 -13.779 33.248 1.0 53.25 ? ? ? ? ? ? 229 ASP AA CB 1 112 A A +ATOM 3593 C CG . ASP AA 1 112 ? 0.339 -14.284 33.201 1.0 48.93 ? ? ? ? ? ? 229 ASP AA CG 1 112 A A +ATOM 3594 O OD1 . ASP AA 1 112 ? 1.250 -13.518 33.579 1.0 41.9 ? ? ? ? ? ? 229 ASP AA OD1 1 112 A A +ATOM 3595 O OD2 . ASP AA 1 112 ? 0.547 -15.445 32.787 1.0 50.62 ? ? ? ? ? ? 229 ASP AA OD2 1 112 A A +ATOM 3596 N N . VAL AA 1 113 ? -3.695 -13.016 34.510 1.0 27.1 ? ? ? ? ? ? 230 VAL AA N 1 113 A A +ATOM 3597 C CA . VAL AA 1 113 ? -5.095 -12.616 34.463 1.0 37.17 ? ? ? ? ? ? 230 VAL AA CA 1 113 A A +ATOM 3598 C C . VAL AA 1 113 ? -5.337 -11.417 35.377 1.0 36.33 ? ? ? ? ? ? 230 VAL AA C 1 113 A A +ATOM 3599 O O . VAL AA 1 113 ? -5.952 -10.429 34.975 1.0 24.34 ? ? ? ? ? ? 230 VAL AA O 1 113 A A +ATOM 3600 C CB . VAL AA 1 113 ? -6.014 -13.767 34.907 1.0 41.74 ? ? ? ? ? ? 230 VAL AA CB 1 113 A A +ATOM 3601 C CG1 . VAL AA 1 113 ? -7.469 -13.432 34.600 1.0 43.64 ? ? ? ? ? ? 230 VAL AA CG1 1 113 A A +ATOM 3602 C CG2 . VAL AA 1 113 ? -5.604 -15.046 34.216 1.0 49.93 ? ? ? ? ? ? 230 VAL AA CG2 1 113 A A +ATOM 3603 N N . SER AA 1 114 ? -4.853 -11.514 36.611 1.0 31.56 ? ? ? ? ? ? 231 SER AA N 1 114 A A +ATOM 3604 C CA . SER AA 1 114 ? -5.012 -10.431 37.570 1.0 45.89 ? ? ? ? ? ? 231 SER AA CA 1 114 A A +ATOM 3605 C C . SER AA 1 114 ? -4.371 -9.173 36.993 1.0 46.44 ? ? ? ? ? ? 231 SER AA C 1 114 A A +ATOM 3606 O O . SER AA 1 114 ? -5.025 -8.141 36.852 1.0 41.88 ? ? ? ? ? ? 231 SER AA O 1 114 A A +ATOM 3607 C CB . SER AA 1 114 ? -4.347 -10.796 38.901 1.0 50.12 ? ? ? ? ? ? 231 SER AA CB 1 114 A A +ATOM 3608 O OG . SER AA 1 114 ? -4.298 -9.678 39.772 1.0 48.07 ? ? ? ? ? ? 231 SER AA OG 1 114 A A +ATOM 3609 N N . GLN AA 1 115 ? -3.086 -9.275 36.656 1.0 43.04 ? ? ? ? ? ? 232 GLN AA N 1 115 A A +ATOM 3610 C CA . GLN AA 1 115 ? -2.365 -8.145 36.084 1.0 50.18 ? ? ? ? ? ? 232 GLN AA CA 1 115 A A +ATOM 3611 C C . GLN AA 1 115 ? -3.126 -7.548 34.905 1.0 60.01 ? ? ? ? ? ? 232 GLN AA C 1 115 A A +ATOM 3612 O O . GLN AA 1 115 ? -3.108 -6.343 34.684 1.0 67.03 ? ? ? ? ? ? 232 GLN AA O 1 115 A A +ATOM 3613 C CB . GLN AA 1 115 ? -0.960 -8.569 35.652 1.0 51.33 ? ? ? ? ? ? 232 GLN AA CB 1 115 A A +ATOM 3614 C CG . GLN AA 1 115 ? 0.096 -7.490 35.831 1.0 68.14 ? ? ? ? ? ? 232 GLN AA CG 1 115 A A +ATOM 3615 C CD . GLN AA 1 115 ? 0.229 -7.041 37.272 1.0 81.94 ? ? ? ? ? ? 232 GLN AA CD 1 115 A A +ATOM 3616 O OE1 . GLN AA 1 115 ? 0.326 -5.847 37.554 1.0 97.08 ? ? ? ? ? ? 232 GLN AA OE1 1 115 A A +ATOM 3617 N NE2 . GLN AA 1 115 ? 0.255 -7.826 38.344 1.0 20.0 ? ? ? ? ? ? 232 GLN AA NE2 1 115 A A +ATOM 3618 N N . PHE AA 1 116 ? -3.801 -8.422 34.162 1.0 57.14 ? ? ? ? ? ? 233 PHE AA N 1 116 A A +ATOM 3619 C CA . PHE AA 1 116 ? -4.566 -8.014 32.992 1.0 59.22 ? ? ? ? ? ? 233 PHE AA CA 1 116 A A +ATOM 3620 C C . PHE AA 1 116 ? -5.823 -7.266 33.412 1.0 56.05 ? ? ? ? ? ? 233 PHE AA C 1 116 A A +ATOM 3621 O O . PHE AA 1 116 ? -5.990 -6.084 33.112 1.0 68.44 ? ? ? ? ? ? 233 PHE AA O 1 116 A A +ATOM 3622 C CB . PHE AA 1 116 ? -4.959 -9.236 32.159 1.0 57.15 ? ? ? ? ? ? 233 PHE AA CB 1 116 A A +ATOM 3623 C CG . PHE AA 1 116 ? -5.790 -8.907 30.947 1.0 45.21 ? ? ? ? ? ? 233 PHE AA CG 1 116 A A +ATOM 3624 C CD1 . PHE AA 1 116 ? -5.501 -7.795 30.163 1.0 49.78 ? ? ? ? ? ? 233 PHE AA CD1 1 116 A A +ATOM 3625 C CD2 . PHE AA 1 116 ? -6.861 -9.716 30.584 1.0 49.92 ? ? ? ? ? ? 233 PHE AA CD2 1 116 A A +ATOM 3626 C CE1 . PHE AA 1 116 ? -6.265 -7.492 29.039 1.0 58.4 ? ? ? ? ? ? 233 PHE AA CE1 1 116 A A +ATOM 3627 C CE2 . PHE AA 1 116 ? -7.632 -9.423 29.462 1.0 48.9 ? ? ? ? ? ? 233 PHE AA CE2 1 116 A A +ATOM 3628 C CZ . PHE AA 1 116 ? -7.333 -8.310 28.688 1.0 48.87 ? ? ? ? ? ? 233 PHE AA CZ 1 116 A A +ATOM 3629 N N . LEU AA 1 117 ? -6.706 -7.977 34.101 1.0 40.06 ? ? ? ? ? ? 234 LEU AA N 1 117 A A +ATOM 3630 C CA . LEU AA 1 117 ? -7.964 -7.412 34.576 1.0 38.99 ? ? ? ? ? ? 234 LEU AA CA 1 117 A A +ATOM 3631 C C . LEU AA 1 117 ? -7.766 -6.039 35.207 1.0 50.84 ? ? ? ? ? ? 234 LEU AA C 1 117 A A +ATOM 3632 O O . LEU AA 1 117 ? -8.625 -5.162 35.095 1.0 56.22 ? ? ? ? ? ? 234 LEU AA O 1 117 A A +ATOM 3633 C CB . LEU AA 1 117 ? -8.602 -8.352 35.604 1.0 50.49 ? ? ? ? ? ? 234 LEU AA CB 1 117 A A +ATOM 3634 C CG . LEU AA 1 117 ? -9.407 -9.531 35.051 1.0 43.22 ? ? ? ? ? ? 234 LEU AA CG 1 117 A A +ATOM 3635 C CD1 . LEU AA 1 117 ? -9.708 -10.518 36.163 1.0 51.1 ? ? ? ? ? ? 234 LEU AA CD1 1 117 A A +ATOM 3636 C CD2 . LEU AA 1 117 ? -10.694 -9.022 34.436 1.0 30.63 ? ? ? ? ? ? 234 LEU AA CD2 1 117 A A +ATOM 3637 N N . GLN AA 1 118 ? -6.633 -5.856 35.875 1.0 41.81 ? ? ? ? ? ? 235 GLN AA N 1 118 A A +ATOM 3638 C CA . GLN AA 1 118 ? -6.350 -4.593 36.537 1.0 32.74 ? ? ? ? ? ? 235 GLN AA CA 1 118 A A +ATOM 3639 C C . GLN AA 1 118 ? -6.302 -3.414 35.576 1.0 30.32 ? ? ? ? ? ? 235 GLN AA C 1 118 A A +ATOM 3640 O O . GLN AA 1 118 ? -6.790 -2.331 35.897 1.0 43.72 ? ? ? ? ? ? 235 GLN AA O 1 118 A A +ATOM 3641 C CB . GLN AA 1 118 ? -5.041 -4.703 37.314 1.0 36.87 ? ? ? ? ? ? 235 GLN AA CB 1 118 A A +ATOM 3642 C CG . GLN AA 1 118 ? -5.131 -5.637 38.505 1.0 51.02 ? ? ? ? ? ? 235 GLN AA CG 1 118 A A +ATOM 3643 C CD . GLN AA 1 118 ? -3.831 -5.724 39.284 1.0 68.21 ? ? ? ? ? ? 235 GLN AA CD 1 118 A A +ATOM 3644 O OE1 . GLN AA 1 118 ? -3.269 -4.706 39.694 1.0 60.38 ? ? ? ? ? ? 235 GLN AA OE1 1 118 A A +ATOM 3645 N NE2 . GLN AA 1 118 ? -3.346 -6.945 39.494 1.0 66.98 ? ? ? ? ? ? 235 GLN AA NE2 1 118 A A +ATOM 3646 N N . THR AA 1 119 ? -5.722 -3.622 34.400 1.0 33.61 ? ? ? ? ? ? 236 THR AA N 1 119 A A +ATOM 3647 C CA . THR AA 1 119 ? -5.619 -2.552 33.410 1.0 38.05 ? ? ? ? ? ? 236 THR AA CA 1 119 A A +ATOM 3648 C C . THR AA 1 119 ? -6.947 -2.285 32.713 1.0 30.93 ? ? ? ? ? ? 236 THR AA C 1 119 A A +ATOM 3649 O O . THR AA 1 119 ? -7.146 -1.219 32.132 1.0 46.11 ? ? ? ? ? ? 236 THR AA O 1 119 A A +ATOM 3650 C CB . THR AA 1 119 ? -4.569 -2.884 32.339 1.0 34.8 ? ? ? ? ? ? 236 THR AA CB 1 119 A A +ATOM 3651 O OG1 . THR AA 1 119 ? -4.742 -4.240 31.915 1.0 51.78 ? ? ? ? ? ? 236 THR AA OG1 1 119 A A +ATOM 3652 C CG2 . THR AA 1 119 ? -3.167 -2.697 32.894 1.0 49.05 ? ? ? ? ? ? 236 THR AA CG2 1 119 A A +ATOM 3653 N N . CYS AA 1 120 ? -7.856 -3.255 32.772 1.0 16.22 ? ? ? ? ? ? 237 CYS AA N 1 120 A A +ATOM 3654 C CA . CYS AA 1 120 ? -9.173 -3.115 32.145 1.0 28.35 ? ? ? ? ? ? 237 CYS AA CA 1 120 A A +ATOM 3655 C C . CYS AA 1 120 ? -10.136 -2.342 33.037 1.0 31.88 ? ? ? ? ? ? 237 CYS AA C 1 120 A A +ATOM 3656 O O . CYS AA 1 120 ? -10.709 -1.333 32.627 1.0 16.59 ? ? ? ? ? ? 237 CYS AA O 1 120 A A +ATOM 3657 C CB . CYS AA 1 120 ? -9.788 -4.486 31.845 1.0 9.51 ? ? ? ? ? ? 237 CYS AA CB 1 120 A A +ATOM 3658 S SG . CYS AA 1 120 ? -8.722 -5.619 30.973 1.0 33.72 ? ? ? ? ? ? 237 CYS AA SG 1 120 A A +ATOM 3659 N N . THR AA 1 121 ? -10.301 -2.818 34.268 1.0 33.98 ? ? ? ? ? ? 238 THR AA N 1 121 A A +ATOM 3660 C CA . THR AA 1 121 ? -11.214 -2.191 35.212 1.0 28.31 ? ? ? ? ? ? 238 THR AA CA 1 121 A A +ATOM 3661 C C . THR AA 1 121 ? -10.563 -1.863 36.553 1.0 20.4 ? ? ? ? ? ? 238 THR AA C 1 121 A A +ATOM 3662 O O . THR AA 1 121 ? -11.007 -0.969 37.271 1.0 25.9 ? ? ? ? ? ? 238 THR AA O 1 121 A A +ATOM 3663 C CB . THR AA 1 121 ? -12.429 -3.101 35.455 1.0 22.53 ? ? ? ? ? ? 238 THR AA CB 1 121 A A +ATOM 3664 O OG1 . THR AA 1 121 ? -11.982 -4.347 35.992 1.0 28.52 ? ? ? ? ? ? 238 THR AA OG1 1 121 A A +ATOM 3665 C CG2 . THR AA 1 121 ? -13.162 -3.367 34.151 1.0 11.53 ? ? ? ? ? ? 238 THR AA CG2 1 121 A A +ATOM 3666 N N . GLY AA 1 122 ? -9.500 -2.582 36.881 1.0 18.84 ? ? ? ? ? ? 239 GLY AA N 1 122 A A +ATOM 3667 C CA . GLY AA 1 122 ? -8.825 -2.342 38.140 1.0 24.31 ? ? ? ? ? ? 239 GLY AA CA 1 122 A A +ATOM 3668 C C . GLY AA 1 122 ? -9.001 -3.519 39.078 1.0 34.75 ? ? ? ? ? ? 239 GLY AA C 1 122 A A +ATOM 3669 O O . GLY AA 1 122 ? -8.469 -3.533 40.193 1.0 30.25 ? ? ? ? ? ? 239 GLY AA O 1 122 A A +ATOM 3670 N N . PHE AA 1 123 ? -9.751 -4.513 38.614 1.0 33.76 ? ? ? ? ? ? 240 PHE AA N 1 123 A A +ATOM 3671 C CA . PHE AA 1 123 ? -10.014 -5.719 39.390 1.0 35.25 ? ? ? ? ? ? 240 PHE AA CA 1 123 A A +ATOM 3672 C C . PHE AA 1 123 ? -8.771 -6.587 39.477 1.0 34.59 ? ? ? ? ? ? 240 PHE AA C 1 123 A A +ATOM 3673 O O . PHE AA 1 123 ? -8.200 -6.981 38.460 1.0 41.61 ? ? ? ? ? ? 240 PHE AA O 1 123 A A +ATOM 3674 C CB . PHE AA 1 123 ? -11.143 -6.528 38.750 1.0 34.81 ? ? ? ? ? ? 240 PHE AA CB 1 123 A A +ATOM 3675 C CG . PHE AA 1 123 ? -12.409 -6.528 39.545 1.0 34.21 ? ? ? ? ? ? 240 PHE AA CG 1 123 A A +ATOM 3676 C CD1 . PHE AA 1 123 ? -13.304 -5.470 39.446 1.0 30.04 ? ? ? ? ? ? 240 PHE AA CD1 1 123 A A +ATOM 3677 C CD2 . PHE AA 1 123 ? -12.703 -7.579 40.402 1.0 16.01 ? ? ? ? ? ? 240 PHE AA CD2 1 123 A A +ATOM 3678 C CE1 . PHE AA 1 123 ? -14.476 -5.459 40.190 1.0 33.78 ? ? ? ? ? ? 240 PHE AA CE1 1 123 A A +ATOM 3679 C CE2 . PHE AA 1 123 ? -13.870 -7.581 41.150 1.0 32.94 ? ? ? ? ? ? 240 PHE AA CE2 1 123 A A +ATOM 3680 C CZ . PHE AA 1 123 ? -14.759 -6.518 41.044 1.0 20.13 ? ? ? ? ? ? 240 PHE AA CZ 1 123 A A +ATOM 3681 N N . ARG AA 1 124 ? -8.351 -6.881 40.700 1.0 42.92 ? ? ? ? ? ? 241 ARG AA N 1 124 A A +ATOM 3682 C CA . ARG AA 1 124 ? -7.183 -7.714 40.910 1.0 32.18 ? ? ? ? ? ? 241 ARG AA CA 1 124 A A +ATOM 3683 C C . ARG AA 1 124 ? -7.671 -9.041 41.441 1.0 27.59 ? ? ? ? ? ? 241 ARG AA C 1 124 A A +ATOM 3684 O O . ARG AA 1 124 ? -8.696 -9.105 42.110 1.0 28.12 ? ? ? ? ? ? 241 ARG AA O 1 124 A A +ATOM 3685 C CB . ARG AA 1 124 ? -6.245 -7.069 41.925 1.0 27.04 ? ? ? ? ? ? 241 ARG AA CB 1 124 A A +ATOM 3686 C CG . ARG AA 1 124 ? -6.946 -6.167 42.923 1.0 26.05 ? ? ? ? ? ? 241 ARG AA CG 1 124 A A +ATOM 3687 C CD . ARG AA 1 124 ? -5.946 -5.297 43.635 1.0 23.29 ? ? ? ? ? ? 241 ARG AA CD 1 124 A A +ATOM 3688 N NE . ARG AA 1 124 ? -5.308 -4.365 42.717 1.0 32.91 ? ? ? ? ? ? 241 ARG AA NE 1 124 A A +ATOM 3689 C CZ . ARG AA 1 124 ? -4.435 -3.439 43.096 1.0 44.01 ? ? ? ? ? ? 241 ARG AA CZ 1 124 A A +ATOM 3690 N NH1 . ARG AA 1 124 ? -4.103 -3.332 44.375 1.0 52.31 ? ? ? ? ? ? 241 ARG AA NH1 1 124 A A +ATOM 3691 N NH2 . ARG AA 1 124 ? -3.897 -2.617 42.203 1.0 54.45 ? ? ? ? ? ? 241 ARG AA NH2 1 124 A A +ATOM 3692 N N . LEU AA 1 125 ? -6.942 -10.104 41.138 1.0 34.78 ? ? ? ? ? ? 242 LEU AA N 1 125 A A +ATOM 3693 C CA . LEU AA 1 125 ? -7.330 -11.419 41.613 1.0 34.24 ? ? ? ? ? ? 242 LEU AA CA 1 125 A A +ATOM 3694 C C . LEU AA 1 125 ? -6.628 -11.718 42.929 1.0 35.4 ? ? ? ? ? ? 242 LEU AA C 1 125 A A +ATOM 3695 O O . LEU AA 1 125 ? -5.594 -11.133 43.239 1.0 28.24 ? ? ? ? ? ? 242 LEU AA O 1 125 A A +ATOM 3696 C CB . LEU AA 1 125 ? -6.966 -12.479 40.572 1.0 39.08 ? ? ? ? ? ? 242 LEU AA CB 1 125 A A +ATOM 3697 C CG . LEU AA 1 125 ? -7.877 -12.567 39.342 1.0 50.27 ? ? ? ? ? ? 242 LEU AA CG 1 125 A A +ATOM 3698 C CD1 . LEU AA 1 125 ? -7.387 -13.675 38.423 1.0 40.92 ? ? ? ? ? ? 242 LEU AA CD1 1 125 A A +ATOM 3699 C CD2 . LEU AA 1 125 ? -9.309 -12.843 39.773 1.0 54.53 ? ? ? ? ? ? 242 LEU AA CD2 1 125 A A +ATOM 3700 N N . ARG AA 1 126 ? -7.217 -12.617 43.710 1.0 36.98 ? ? ? ? ? ? 243 ARG AA N 1 126 A A +ATOM 3701 C CA . ARG AA 1 126 ? -6.644 -13.028 44.984 1.0 38.32 ? ? ? ? ? ? 243 ARG AA CA 1 126 A A +ATOM 3702 C C . ARG AA 1 126 ? -6.950 -14.503 45.180 1.0 46.23 ? ? ? ? ? ? 243 ARG AA C 1 126 A A +ATOM 3703 O O . ARG AA 1 126 ? -8.111 -14.908 45.198 1.0 58.57 ? ? ? ? ? ? 243 ARG AA O 1 126 A A +ATOM 3704 C CB . ARG AA 1 126 ? -7.231 -12.223 46.148 1.0 38.91 ? ? ? ? ? ? 243 ARG AA CB 1 126 A A +ATOM 3705 C CG . ARG AA 1 126 ? -6.381 -12.316 47.403 1.0 36.65 ? ? ? ? ? ? 243 ARG AA CG 1 126 A A +ATOM 3706 C CD . ARG AA 1 126 ? -7.082 -11.768 48.627 1.0 50.44 ? ? ? ? ? ? 243 ARG AA CD 1 126 A A +ATOM 3707 N NE . ARG AA 1 126 ? -6.353 -12.126 49.841 1.0 47.02 ? ? ? ? ? ? 243 ARG AA NE 1 126 A A +ATOM 3708 C CZ . ARG AA 1 126 ? -5.577 -11.292 50.522 1.0 42.93 ? ? ? ? ? ? 243 ARG AA CZ 1 126 A A +ATOM 3709 N NH1 . ARG AA 1 126 ? -5.421 -10.041 50.116 1.0 24.97 ? ? ? ? ? ? 243 ARG AA NH1 1 126 A A +ATOM 3710 N NH2 . ARG AA 1 126 ? -4.949 -11.713 51.607 1.0 57.01 ? ? ? ? ? ? 243 ARG AA NH2 1 126 A A +ATOM 3711 N N . PRO AA 1 127 ? -5.901 -15.331 45.320 1.0 42.99 ? ? ? ? ? ? 244 PRO AA N 1 127 A A +ATOM 3712 C CA . PRO AA 1 127 ? -6.089 -16.774 45.513 1.0 38.6 ? ? ? ? ? ? 244 PRO AA CA 1 127 A A +ATOM 3713 C C . PRO AA 1 127 ? -6.719 -17.130 46.860 1.0 46.2 ? ? ? ? ? ? 244 PRO AA C 1 127 A A +ATOM 3714 O O . PRO AA 1 127 ? -6.137 -16.890 47.916 1.0 54.57 ? ? ? ? ? ? 244 PRO AA O 1 127 A A +ATOM 3715 C CB . PRO AA 1 127 ? -4.678 -17.341 45.363 1.0 26.93 ? ? ? ? ? ? 244 PRO AA CB 1 127 A A +ATOM 3716 C CG . PRO AA 1 127 ? -3.780 -16.214 45.725 1.0 26.61 ? ? ? ? ? ? 244 PRO AA CG 1 127 A A +ATOM 3717 C CD . PRO AA 1 127 ? -4.477 -14.956 45.301 1.0 43.68 ? ? ? ? ? ? 244 PRO AA CD 1 127 A A +ATOM 3718 N N . VAL AA 1 128 ? -7.917 -17.705 46.812 1.0 40.08 ? ? ? ? ? ? 245 VAL AA N 1 128 A A +ATOM 3719 C CA . VAL AA 1 128 ? -8.630 -18.100 48.022 1.0 38.82 ? ? ? ? ? ? 245 VAL AA CA 1 128 A A +ATOM 3720 C C . VAL AA 1 128 ? -8.406 -19.587 48.281 1.0 44.01 ? ? ? ? ? ? 245 VAL AA C 1 128 A A +ATOM 3721 O O . VAL AA 1 128 ? -8.412 -20.392 47.349 1.0 36.98 ? ? ? ? ? ? 245 VAL AA O 1 128 A A +ATOM 3722 C CB . VAL AA 1 128 ? -10.154 -17.829 47.885 1.0 37.07 ? ? ? ? ? ? 245 VAL AA CB 1 128 A A +ATOM 3723 C CG1 . VAL AA 1 128 ? -10.796 -18.869 46.980 1.0 38.19 ? ? ? ? ? ? 245 VAL AA CG1 1 128 A A +ATOM 3724 C CG2 . VAL AA 1 128 ? -10.810 -17.835 49.248 1.0 39.24 ? ? ? ? ? ? 245 VAL AA CG2 1 128 A A +ATOM 3725 N N . ALA AA 1 129 ? -8.205 -19.948 49.544 1.0 54.02 ? ? ? ? ? ? 246 ALA AA N 1 129 A A +ATOM 3726 C CA . ALA AA 1 129 ? -7.988 -21.342 49.912 1.0 57.88 ? ? ? ? ? ? 246 ALA AA CA 1 129 A A +ATOM 3727 C C . ALA AA 1 129 ? -9.001 -22.250 49.213 1.0 60.78 ? ? ? ? ? ? 246 ALA AA C 1 129 A A +ATOM 3728 O O . ALA AA 1 129 ? -8.635 -23.073 48.373 1.0 67.19 ? ? ? ? ? ? 246 ALA AA O 1 129 A A +ATOM 3729 C CB . ALA AA 1 129 ? -8.098 -21.500 51.421 1.0 77.71 ? ? ? ? ? ? 246 ALA AA CB 1 129 A A +ATOM 3730 N N . GLY AA 1 130 ? -10.273 -22.087 49.563 1.0 52.89 ? ? ? ? ? ? 247 GLY AA N 1 130 A A +ATOM 3731 C CA . GLY AA 1 130 ? -11.322 -22.891 48.963 1.0 62.98 ? ? ? ? ? ? 247 GLY AA CA 1 130 A A +ATOM 3732 C C . GLY AA 1 130 ? -12.605 -22.098 48.795 1.0 67.72 ? ? ? ? ? ? 247 GLY AA C 1 130 A A +ATOM 3733 O O . GLY AA 1 130 ? -12.976 -21.722 47.682 1.0 80.51 ? ? ? ? ? ? 247 GLY AA O 1 130 A A +ATOM 3734 N N . LEU AA 1 131 ? -13.280 -21.840 49.909 1.0 65.11 ? ? ? ? ? ? 248 LEU AA N 1 131 A A +ATOM 3735 C CA . LEU AA 1 131 ? -14.529 -21.088 49.902 1.0 56.05 ? ? ? ? ? ? 248 LEU AA CA 1 131 A A +ATOM 3736 C C . LEU AA 1 131 ? -14.552 -20.132 51.089 1.0 61.16 ? ? ? ? ? ? 248 LEU AA C 1 131 A A +ATOM 3737 O O . LEU AA 1 131 ? -13.740 -20.255 52.008 1.0 74.12 ? ? ? ? ? ? 248 LEU AA O 1 131 A A +ATOM 3738 C CB . LEU AA 1 131 ? -15.719 -22.047 49.988 1.0 59.12 ? ? ? ? ? ? 248 LEU AA CB 1 131 A A +ATOM 3739 C CG . LEU AA 1 131 ? -16.107 -22.575 51.374 1.0 79.7 ? ? ? ? ? ? 248 LEU AA CG 1 131 A A +ATOM 3740 C CD1 . LEU AA 1 131 ? -17.451 -23.272 51.288 1.0 87.18 ? ? ? ? ? ? 248 LEU AA CD1 1 131 A A +ATOM 3741 C CD2 . LEU AA 1 131 ? -15.039 -23.521 51.889 1.0 72.88 ? ? ? ? ? ? 248 LEU AA CD2 1 131 A A +ATOM 3742 N N . LEU AA 1 132 ? -15.474 -19.177 51.066 1.0 46.27 ? ? ? ? ? ? 249 LEU AA N 1 132 A A +ATOM 3743 C CA . LEU AA 1 132 ? -15.604 -18.220 52.158 1.0 45.65 ? ? ? ? ? ? 249 LEU AA CA 1 132 A A +ATOM 3744 C C . LEU AA 1 132 ? -17.009 -17.639 52.225 1.0 47.53 ? ? ? ? ? ? 249 LEU AA C 1 132 A A +ATOM 3745 O O . LEU AA 1 132 ? -17.766 -17.708 51.261 1.0 50.63 ? ? ? ? ? ? 249 LEU AA O 1 132 A A +ATOM 3746 C CB . LEU AA 1 132 ? -14.582 -17.086 52.024 1.0 32.93 ? ? ? ? ? ? 249 LEU AA CB 1 132 A A +ATOM 3747 C CG . LEU AA 1 132 ? -13.980 -16.748 50.664 1.0 37.61 ? ? ? ? ? ? 249 LEU AA CG 1 132 A A +ATOM 3748 C CD1 . LEU AA 1 132 ? -15.073 -16.440 49.663 1.0 47.51 ? ? ? ? ? ? 249 LEU AA CD1 1 132 A A +ATOM 3749 C CD2 . LEU AA 1 132 ? -13.052 -15.561 50.831 1.0 20.77 ? ? ? ? ? ? 249 LEU AA CD2 1 132 A A +ATOM 3750 N N . SER AA 1 133 ? -17.354 -17.079 53.379 1.0 49.94 ? ? ? ? ? ? 250 SER AA N 1 133 A A +ATOM 3751 C CA . SER AA 1 133 ? -18.670 -16.496 53.602 1.0 58.56 ? ? ? ? ? ? 250 SER AA CA 1 133 A A +ATOM 3752 C C . SER AA 1 133 ? -19.055 -15.491 52.519 1.0 61.47 ? ? ? ? ? ? 250 SER AA C 1 133 A A +ATOM 3753 O O . SER AA 1 133 ? -18.189 -14.925 51.852 1.0 66.63 ? ? ? ? ? ? 250 SER AA O 1 133 A A +ATOM 3754 C CB . SER AA 1 133 ? -18.702 -15.818 54.975 1.0 56.4 ? ? ? ? ? ? 250 SER AA CB 1 133 A A +ATOM 3755 O OG . SER AA 1 133 ? -19.877 -15.050 55.146 1.0 80.26 ? ? ? ? ? ? 250 SER AA OG 1 133 A A +ATOM 3756 N N . SER AA 1 134 ? -20.358 -15.278 52.343 1.0 57.53 ? ? ? ? ? ? 251 SER AA N 1 134 A A +ATOM 3757 C CA . SER AA 1 134 ? -20.846 -14.330 51.350 1.0 45.91 ? ? ? ? ? ? 251 SER AA CA 1 134 A A +ATOM 3758 C C . SER AA 1 134 ? -20.391 -12.945 51.761 1.0 41.98 ? ? ? ? ? ? 251 SER AA C 1 134 A A +ATOM 3759 O O . SER AA 1 134 ? -20.061 -12.110 50.920 1.0 47.44 ? ? ? ? ? ? 251 SER AA O 1 134 A A +ATOM 3760 C CB . SER AA 1 134 ? -22.370 -14.361 51.283 1.0 59.78 ? ? ? ? ? ? 251 SER AA CB 1 134 A A +ATOM 3761 O OG . SER AA 1 134 ? -22.858 -15.688 51.378 1.0 81.13 ? ? ? ? ? ? 251 SER AA OG 1 134 A A +ATOM 3762 N N . ARG AA 1 135 ? -20.379 -12.710 53.068 1.0 30.74 ? ? ? ? ? ? 252 ARG AA N 1 135 A A +ATOM 3763 C CA . ARG AA 1 135 ? -19.959 -11.430 53.616 1.0 31.41 ? ? ? ? ? ? 252 ARG AA CA 1 135 A A +ATOM 3764 C C . ARG AA 1 135 ? -18.502 -11.167 53.261 1.0 23.75 ? ? ? ? ? ? 252 ARG AA C 1 135 A A +ATOM 3765 O O . ARG AA 1 135 ? -18.129 -10.049 52.913 1.0 34.67 ? ? ? ? ? ? 252 ARG AA O 1 135 A A +ATOM 3766 C CB . ARG AA 1 135 ? -20.127 -11.424 55.135 1.0 35.53 ? ? ? ? ? ? 252 ARG AA CB 1 135 A A +ATOM 3767 C CG . ARG AA 1 135 ? -19.640 -10.152 55.808 1.0 53.82 ? ? ? ? ? ? 252 ARG AA CG 1 135 A A +ATOM 3768 C CD . ARG AA 1 135 ? -19.826 -10.221 57.313 1.0 46.69 ? ? ? ? ? ? 252 ARG AA CD 1 135 A A +ATOM 3769 N NE . ARG AA 1 135 ? -21.226 -10.408 57.681 1.0 40.65 ? ? ? ? ? ? 252 ARG AA NE 1 135 A A +ATOM 3770 C CZ . ARG AA 1 135 ? -22.158 -9.466 57.581 1.0 48.03 ? ? ? ? ? ? 252 ARG AA CZ 1 135 A A +ATOM 3771 N NH1 . ARG AA 1 135 ? -21.843 -8.263 57.121 1.0 44.01 ? ? ? ? ? ? 252 ARG AA NH1 1 135 A A +ATOM 3772 N NH2 . ARG AA 1 135 ? -23.405 -9.725 57.942 1.0 50.32 ? ? ? ? ? ? 252 ARG AA NH2 1 135 A A +ATOM 3773 N N . ASP AA 1 136 ? -17.683 -12.209 53.352 1.0 16.34 ? ? ? ? ? ? 253 ASP AA N 1 136 A A +ATOM 3774 C CA . ASP AA 1 136 ? -16.257 -12.097 53.042 1.0 28.42 ? ? ? ? ? ? 253 ASP AA CA 1 136 A A +ATOM 3775 C C . ASP AA 1 136 ? -16.017 -11.964 51.547 1.0 29.16 ? ? ? ? ? ? 253 ASP AA C 1 136 A A +ATOM 3776 O O . ASP AA 1 136 ? -15.225 -11.133 51.105 1.0 33.43 ? ? ? ? ? ? 253 ASP AA O 1 136 A A +ATOM 3777 C CB . ASP AA 1 136 ? -15.510 -13.317 53.575 1.0 46.51 ? ? ? ? ? ? 253 ASP AA CB 1 136 A A +ATOM 3778 C CG . ASP AA 1 136 ? -15.617 -13.449 55.077 1.0 73.75 ? ? ? ? ? ? 253 ASP AA CG 1 136 A A +ATOM 3779 O OD1 . ASP AA 1 136 ? -16.682 -13.878 55.568 1.0 70.2 ? ? ? ? ? ? 253 ASP AA OD1 1 136 A A +ATOM 3780 O OD2 . ASP AA 1 136 ? -14.633 -13.119 55.768 1.0 82.65 ? ? ? ? ? ? 253 ASP AA OD2 1 136 A A +ATOM 3781 N N . PHE AA 1 137 ? -16.697 -12.799 50.775 1.0 36.9 ? ? ? ? ? ? 254 PHE AA N 1 137 A A +ATOM 3782 C CA . PHE AA 1 137 ? -16.576 -12.771 49.328 1.0 47.73 ? ? ? ? ? ? 254 PHE AA CA 1 137 A A +ATOM 3783 C C . PHE AA 1 137 ? -16.959 -11.376 48.839 1.0 53.7 ? ? ? ? ? ? 254 PHE AA C 1 137 A A +ATOM 3784 O O . PHE AA 1 137 ? -16.150 -10.675 48.228 1.0 62.08 ? ? ? ? ? ? 254 PHE AA O 1 137 A A +ATOM 3785 C CB . PHE AA 1 137 ? -17.508 -13.815 48.709 1.0 58.44 ? ? ? ? ? ? 254 PHE AA CB 1 137 A A +ATOM 3786 C CG . PHE AA 1 137 ? -17.211 -14.130 47.270 1.0 64.83 ? ? ? ? ? ? 254 PHE AA CG 1 137 A A +ATOM 3787 C CD1 . PHE AA 1 137 ? -16.195 -13.468 46.585 1.0 76.33 ? ? ? ? ? ? 254 PHE AA CD1 1 137 A A +ATOM 3788 C CD2 . PHE AA 1 137 ? -17.952 -15.098 46.597 1.0 86.07 ? ? ? ? ? ? 254 PHE AA CD2 1 137 A A +ATOM 3789 C CE1 . PHE AA 1 137 ? -15.926 -13.761 45.250 1.0 86.3 ? ? ? ? ? ? 254 PHE AA CE1 1 137 A A +ATOM 3790 C CE2 . PHE AA 1 137 ? -17.690 -15.399 45.259 1.0 100.0 ? ? ? ? ? ? 254 PHE AA CE2 1 137 A A +ATOM 3791 C CZ . PHE AA 1 137 ? -16.676 -14.730 44.586 1.0 95.87 ? ? ? ? ? ? 254 PHE AA CZ 1 137 A A +ATOM 3792 N N . LEU AA 1 138 ? -18.197 -10.980 49.120 1.0 40.62 ? ? ? ? ? ? 255 LEU AA N 1 138 A A +ATOM 3793 C CA . LEU AA 1 138 ? -18.703 -9.679 48.717 1.0 29.53 ? ? ? ? ? ? 255 LEU AA CA 1 138 A A +ATOM 3794 C C . LEU AA 1 138 ? -17.803 -8.550 49.197 1.0 35.98 ? ? ? ? ? ? 255 LEU AA C 1 138 A A +ATOM 3795 O O . LEU AA 1 138 ? -17.613 -7.559 48.492 1.0 44.56 ? ? ? ? ? ? 255 LEU AA O 1 138 A A +ATOM 3796 C CB . LEU AA 1 138 ? -20.117 -9.489 49.261 1.0 37.3 ? ? ? ? ? ? 255 LEU AA CB 1 138 A A +ATOM 3797 C CG . LEU AA 1 138 ? -21.247 -10.075 48.405 1.0 31.39 ? ? ? ? ? ? 255 LEU AA CG 1 138 A A +ATOM 3798 C CD1 . LEU AA 1 138 ? -20.758 -11.290 47.649 1.0 20.93 ? ? ? ? ? ? 255 LEU AA CD1 1 138 A A +ATOM 3799 C CD2 . LEU AA 1 138 ? -22.420 -10.434 49.293 1.0 19.28 ? ? ? ? ? ? 255 LEU AA CD2 1 138 A A +ATOM 3800 N N . GLY AA 1 139 ? -17.248 -8.701 50.395 1.0 23.82 ? ? ? ? ? ? 256 GLY AA N 1 139 A A +ATOM 3801 C CA . GLY AA 1 139 ? -16.375 -7.675 50.936 1.0 22.93 ? ? ? ? ? ? 256 GLY AA CA 1 139 A A +ATOM 3802 C C . GLY AA 1 139 ? -15.184 -7.391 50.039 1.0 27.16 ? ? ? ? ? ? 256 GLY AA C 1 139 A A +ATOM 3803 O O . GLY AA 1 139 ? -14.689 -6.265 49.978 1.0 13.49 ? ? ? ? ? ? 256 GLY AA O 1 139 A A +ATOM 3804 N N . GLY AA 1 140 ? -14.715 -8.414 49.335 1.0 21.45 ? ? ? ? ? ? 257 GLY AA N 1 140 A A +ATOM 3805 C CA . GLY AA 1 140 ? -13.584 -8.228 48.451 1.0 40.44 ? ? ? ? ? ? 257 GLY AA CA 1 140 A A +ATOM 3806 C C . GLY AA 1 140 ? -13.962 -7.363 47.267 1.0 40.36 ? ? ? ? ? ? 257 GLY AA C 1 140 A A +ATOM 3807 O O . GLY AA 1 140 ? -13.171 -6.556 46.792 1.0 47.8 ? ? ? ? ? ? 257 GLY AA O 1 140 A A +ATOM 3808 N N . LEU AA 1 141 ? -15.188 -7.537 46.793 1.0 40.24 ? ? ? ? ? ? 258 LEU AA N 1 141 A A +ATOM 3809 C CA . LEU AA 1 141 ? -15.690 -6.782 45.654 1.0 34.55 ? ? ? ? ? ? 258 LEU AA CA 1 141 A A +ATOM 3810 C C . LEU AA 1 141 ? -15.648 -5.275 45.893 1.0 24.3 ? ? ? ? ? ? 258 LEU AA C 1 141 A A +ATOM 3811 O O . LEU AA 1 141 ? -15.496 -4.500 44.953 1.0 33.84 ? ? ? ? ? ? 258 LEU AA O 1 141 A A +ATOM 3812 C CB . LEU AA 1 141 ? -17.123 -7.232 45.322 1.0 35.0 ? ? ? ? ? ? 258 LEU AA CB 1 141 A A +ATOM 3813 C CG . LEU AA 1 141 ? -17.309 -8.743 45.094 1.0 41.25 ? ? ? ? ? ? 258 LEU AA CG 1 141 A A +ATOM 3814 C CD1 . LEU AA 1 141 ? -18.793 -9.096 45.133 1.0 31.39 ? ? ? ? ? ? 258 LEU AA CD1 1 141 A A +ATOM 3815 C CD2 . LEU AA 1 141 ? -16.687 -9.147 43.766 1.0 28.27 ? ? ? ? ? ? 258 LEU AA CD2 1 141 A A +ATOM 3816 N N . ALA AA 1 142 ? -15.782 -4.865 47.149 1.0 13.11 ? ? ? ? ? ? 259 ALA AA N 1 142 A A +ATOM 3817 C CA . ALA AA 1 142 ? -15.767 -3.449 47.498 1.0 16.98 ? ? ? ? ? ? 259 ALA AA CA 1 142 A A +ATOM 3818 C C . ALA AA 1 142 ? -14.439 -2.810 47.135 1.0 19.95 ? ? ? ? ? ? 259 ALA AA C 1 142 A A +ATOM 3819 O O . ALA AA 1 142 ? -14.336 -1.588 47.052 1.0 33.25 ? ? ? ? ? ? 259 ALA AA O 1 142 A A +ATOM 3820 C CB . ALA AA 1 142 ? -16.034 -3.275 48.978 1.0 17.11 ? ? ? ? ? ? 259 ALA AA CB 1 142 A A +ATOM 3821 N N . PHE AA 1 143 ? -13.423 -3.641 46.924 1.0 17.1 ? ? ? ? ? ? 260 PHE AA N 1 143 A A +ATOM 3822 C CA . PHE AA 1 143 ? -12.091 -3.153 46.577 1.0 29.31 ? ? ? ? ? ? 260 PHE AA CA 1 143 A A +ATOM 3823 C C . PHE AA 1 143 ? -11.727 -3.602 45.177 1.0 25.66 ? ? ? ? ? ? 260 PHE AA C 1 143 A A +ATOM 3824 O O . PHE AA 1 143 ? -10.577 -3.467 44.754 1.0 36.3 ? ? ? ? ? ? 260 PHE AA O 1 143 A A +ATOM 3825 C CB . PHE AA 1 143 ? -11.047 -3.690 47.559 1.0 17.78 ? ? ? ? ? ? 260 PHE AA CB 1 143 A A +ATOM 3826 C CG . PHE AA 1 143 ? -11.381 -3.434 48.990 1.0 15.54 ? ? ? ? ? ? 260 PHE AA CG 1 143 A A +ATOM 3827 C CD1 . PHE AA 1 143 ? -12.322 -4.220 49.647 1.0 23.61 ? ? ? ? ? ? 260 PHE AA CD1 1 143 A A +ATOM 3828 C CD2 . PHE AA 1 143 ? -10.773 -2.397 49.678 1.0 9.2 ? ? ? ? ? ? 260 PHE AA CD2 1 143 A A +ATOM 3829 C CE1 . PHE AA 1 143 ? -12.656 -3.978 50.972 1.0 19.04 ? ? ? ? ? ? 260 PHE AA CE1 1 143 A A +ATOM 3830 C CE2 . PHE AA 1 143 ? -11.098 -2.146 51.004 1.0 28.72 ? ? ? ? ? ? 260 PHE AA CE2 1 143 A A +ATOM 3831 C CZ . PHE AA 1 143 ? -12.041 -2.940 51.654 1.0 32.54 ? ? ? ? ? ? 260 PHE AA CZ 1 143 A A +ATOM 3832 N N . ARG AA 1 144 ? -12.715 -4.137 44.466 1.0 30.74 ? ? ? ? ? ? 261 ARG AA N 1 144 A A +ATOM 3833 C CA . ARG AA 1 144 ? -12.511 -4.630 43.110 1.0 30.16 ? ? ? ? ? ? 261 ARG AA CA 1 144 A A +ATOM 3834 C C . ARG AA 1 144 ? -11.484 -5.749 43.158 1.0 28.65 ? ? ? ? ? ? 261 ARG AA C 1 144 A A +ATOM 3835 O O . ARG AA 1 144 ? -10.594 -5.838 42.311 1.0 34.8 ? ? ? ? ? ? 261 ARG AA O 1 144 A A +ATOM 3836 C CB . ARG AA 1 144 ? -12.034 -3.501 42.195 1.0 30.66 ? ? ? ? ? ? 261 ARG AA CB 1 144 A A +ATOM 3837 C CG . ARG AA 1 144 ? -13.065 -2.408 42.004 1.0 32.76 ? ? ? ? ? ? 261 ARG AA CG 1 144 A A +ATOM 3838 C CD . ARG AA 1 144 ? -12.959 -1.746 40.647 1.0 39.38 ? ? ? ? ? ? 261 ARG AA CD 1 144 A A +ATOM 3839 N NE . ARG AA 1 144 ? -13.898 -0.630 40.542 1.0 47.15 ? ? ? ? ? ? 261 ARG AA NE 1 144 A A +ATOM 3840 C CZ . ARG AA 1 144 ? -14.324 -0.097 39.402 1.0 30.86 ? ? ? ? ? ? 261 ARG AA CZ 1 144 A A +ATOM 3841 N NH1 . ARG AA 1 144 ? -13.890 -0.556 38.238 1.0 48.34 ? ? ? ? ? ? 261 ARG AA NH1 1 144 A A +ATOM 3842 N NH2 . ARG AA 1 144 ? -15.185 0.908 39.430 1.0 31.94 ? ? ? ? ? ? 261 ARG AA NH2 1 144 A A +ATOM 3843 N N . VAL AA 1 145 ? -11.626 -6.590 44.181 1.0 21.99 ? ? ? ? ? ? 262 VAL AA N 1 145 A A +ATOM 3844 C CA . VAL AA 1 145 ? -10.749 -7.734 44.401 1.0 24.05 ? ? ? ? ? ? 262 VAL AA CA 1 145 A A +ATOM 3845 C C . VAL AA 1 145 ? -11.586 -9.006 44.324 1.0 29.44 ? ? ? ? ? ? 262 VAL AA C 1 145 A A +ATOM 3846 O O . VAL AA 1 145 ? -12.589 -9.145 45.032 1.0 27.93 ? ? ? ? ? ? 262 VAL AA O 1 145 A A +ATOM 3847 C CB . VAL AA 1 145 ? -10.071 -7.671 45.790 1.0 11.44 ? ? ? ? ? ? 262 VAL AA CB 1 145 A A +ATOM 3848 C CG1 . VAL AA 1 145 ? -9.424 -8.995 46.117 1.0 21.4 ? ? ? ? ? ? 262 VAL AA CG1 1 145 A A +ATOM 3849 C CG2 . VAL AA 1 145 ? -9.031 -6.557 45.816 1.0 29.17 ? ? ? ? ? ? 262 VAL AA CG2 1 145 A A +ATOM 3850 N N . PHE AA 1 146 ? -11.176 -9.929 43.458 1.0 40.09 ? ? ? ? ? ? 263 PHE AA N 1 146 A A +ATOM 3851 C CA . PHE AA 1 146 ? -11.892 -11.187 43.283 1.0 42.03 ? ? ? ? ? ? 263 PHE AA CA 1 146 A A +ATOM 3852 C C . PHE AA 1 146 ? -11.129 -12.354 43.906 1.0 47.79 ? ? ? ? ? ? 263 PHE AA C 1 146 A A +ATOM 3853 O O . PHE AA 1 146 ? -9.954 -12.573 43.607 1.0 49.0 ? ? ? ? ? ? 263 PHE AA O 1 146 A A +ATOM 3854 C CB . PHE AA 1 146 ? -12.124 -11.457 41.794 1.0 28.47 ? ? ? ? ? ? 263 PHE AA CB 1 146 A A +ATOM 3855 C CG . PHE AA 1 146 ? -13.054 -12.604 41.524 1.0 32.77 ? ? ? ? ? ? 263 PHE AA CG 1 146 A A +ATOM 3856 C CD1 . PHE AA 1 146 ? -14.283 -12.692 42.176 1.0 52.86 ? ? ? ? ? ? 263 PHE AA CD1 1 146 A A +ATOM 3857 C CD2 . PHE AA 1 146 ? -12.702 -13.599 40.619 1.0 25.5 ? ? ? ? ? ? 263 PHE AA CD2 1 146 A A +ATOM 3858 C CE1 . PHE AA 1 146 ? -15.146 -13.755 41.930 1.0 46.81 ? ? ? ? ? ? 263 PHE AA CE1 1 146 A A +ATOM 3859 C CE2 . PHE AA 1 146 ? -13.557 -14.666 40.365 1.0 42.05 ? ? ? ? ? ? 263 PHE AA CE2 1 146 A A +ATOM 3860 C CZ . PHE AA 1 146 ? -14.782 -14.744 41.023 1.0 54.09 ? ? ? ? ? ? 263 PHE AA CZ 1 146 A A +ATOM 3861 N N . HIS AA 1 147 ? -11.798 -13.098 44.781 1.0 50.29 ? ? ? ? ? ? 264 HIS AA N 1 147 A A +ATOM 3862 C CA . HIS AA 1 147 ? -11.172 -14.241 45.430 1.0 55.68 ? ? ? ? ? ? 264 HIS AA CA 1 147 A A +ATOM 3863 C C . HIS AA 1 147 ? -11.330 -15.443 44.514 1.0 54.21 ? ? ? ? ? ? 264 HIS AA C 1 147 A A +ATOM 3864 O O . HIS AA 1 147 ? -12.403 -16.035 44.409 1.0 66.04 ? ? ? ? ? ? 264 HIS AA O 1 147 A A +ATOM 3865 C CB . HIS AA 1 147 ? -11.819 -14.481 46.797 1.0 60.8 ? ? ? ? ? ? 264 HIS AA CB 1 147 A A +ATOM 3866 C CG . HIS AA 1 147 ? -11.458 -13.446 47.814 1.0 53.37 ? ? ? ? ? ? 264 HIS AA CG 1 147 A A +ATOM 3867 N ND1 . HIS AA 1 147 ? -10.482 -13.641 48.764 1.0 58.65 ? ? ? ? ? ? 264 HIS AA ND1 1 147 A A +ATOM 3868 C CD2 . HIS AA 1 147 ? -11.908 -12.179 47.995 1.0 56.24 ? ? ? ? ? ? 264 HIS AA CD2 1 147 A A +ATOM 3869 C CE1 . HIS AA 1 147 ? -10.344 -12.541 49.487 1.0 37.58 ? ? ? ? ? ? 264 HIS AA CE1 1 147 A A +ATOM 3870 N NE2 . HIS AA 1 147 ? -11.197 -11.644 49.039 1.0 49.84 ? ? ? ? ? ? 264 HIS AA NE2 1 147 A A +ATOM 3871 N N . CYS AA 1 148 ? -10.239 -15.790 43.842 1.0 52.29 ? ? ? ? ? ? 265 CYS AA N 1 148 A A +ATOM 3872 C CA . CYS AA 1 148 ? -10.228 -16.890 42.886 1.0 59.81 ? ? ? ? ? ? 265 CYS AA CA 1 148 A A +ATOM 3873 C C . CYS AA 1 148 ? -9.540 -18.161 43.380 1.0 60.63 ? ? ? ? ? ? 265 CYS AA C 1 148 A A +ATOM 3874 O O . CYS AA 1 148 ? -8.647 -18.119 44.230 1.0 62.02 ? ? ? ? ? ? 265 CYS AA O 1 148 A A +ATOM 3875 C CB . CYS AA 1 148 ? -9.563 -16.411 41.592 1.0 56.39 ? ? ? ? ? ? 265 CYS AA CB 1 148 A A +ATOM 3876 S SG . CYS AA 1 148 ? -9.467 -17.625 40.268 1.0 81.8 ? ? ? ? ? ? 265 CYS AA SG 1 148 A A +ATOM 3877 N N . THR AA 1 149 ? -9.981 -19.292 42.832 1.0 57.33 ? ? ? ? ? ? 266 THR AA N 1 149 A A +ATOM 3878 C CA . THR AA 1 149 ? -9.431 -20.604 43.164 1.0 54.19 ? ? ? ? ? ? 266 THR AA CA 1 149 A A +ATOM 3879 C C . THR AA 1 149 ? -8.344 -20.956 42.148 1.0 45.74 ? ? ? ? ? ? 266 THR AA C 1 149 A A +ATOM 3880 O O . THR AA 1 149 ? -8.566 -20.887 40.940 1.0 43.17 ? ? ? ? ? ? 266 THR AA O 1 149 A A +ATOM 3881 C CB . THR AA 1 149 ? -10.522 -21.699 43.114 1.0 60.72 ? ? ? ? ? ? 266 THR AA CB 1 149 A A +ATOM 3882 O OG1 . THR AA 1 149 ? -10.883 -21.957 41.751 1.0 48.14 ? ? ? ? ? ? 266 THR AA OG1 1 149 A A +ATOM 3883 C CG2 . THR AA 1 149 ? -11.756 -21.257 43.884 1.0 67.4 ? ? ? ? ? ? 266 THR AA CG2 1 149 A A +ATOM 3884 N N . GLN AA 1 150 ? -7.170 -21.332 42.643 1.0 52.16 ? ? ? ? ? ? 267 GLN AA N 1 150 A A +ATOM 3885 C CA . GLN AA 1 150 ? -6.057 -21.683 41.773 1.0 44.22 ? ? ? ? ? ? 267 GLN AA CA 1 150 A A +ATOM 3886 C C . GLN AA 1 150 ? -6.114 -23.139 41.329 1.0 45.27 ? ? ? ? ? ? 267 GLN AA C 1 150 A A +ATOM 3887 O O . GLN AA 1 150 ? -5.511 -23.507 40.324 1.0 34.83 ? ? ? ? ? ? 267 GLN AA O 1 150 A A +ATOM 3888 C CB . GLN AA 1 150 ? -4.735 -21.419 42.491 1.0 36.86 ? ? ? ? ? ? 267 GLN AA CB 1 150 A A +ATOM 3889 C CG . GLN AA 1 150 ? -3.512 -21.720 41.653 1.0 27.09 ? ? ? ? ? ? 267 GLN AA CG 1 150 A A +ATOM 3890 C CD . GLN AA 1 150 ? -2.538 -20.554 41.603 1.0 50.69 ? ? ? ? ? ? 267 GLN AA CD 1 150 A A +ATOM 3891 O OE1 . GLN AA 1 150 ? -2.098 -20.052 42.641 1.0 43.07 ? ? ? ? ? ? 267 GLN AA OE1 1 150 A A +ATOM 3892 N NE2 . GLN AA 1 150 ? -2.191 -20.120 40.391 1.0 54.57 ? ? ? ? ? ? 267 GLN AA NE2 1 150 A A +ATOM 3893 N N . TYR AA 1 151 ? -6.847 -23.961 42.076 1.0 39.74 ? ? ? ? ? ? 268 TYR AA N 1 151 A A +ATOM 3894 C CA . TYR AA 1 151 ? -6.961 -25.382 41.766 1.0 41.65 ? ? ? ? ? ? 268 TYR AA CA 1 151 A A +ATOM 3895 C C . TYR AA 1 151 ? -7.931 -25.723 40.635 1.0 44.54 ? ? ? ? ? ? 268 TYR AA C 1 151 A A +ATOM 3896 O O . TYR AA 1 151 ? -8.493 -24.836 39.991 1.0 42.77 ? ? ? ? ? ? 268 TYR AA O 1 151 A A +ATOM 3897 C CB . TYR AA 1 151 ? -7.325 -26.172 43.033 1.0 47.36 ? ? ? ? ? ? 268 TYR AA CB 1 151 A A +ATOM 3898 C CG . TYR AA 1 151 ? -8.657 -25.818 43.661 1.0 47.68 ? ? ? ? ? ? 268 TYR AA CG 1 151 A A +ATOM 3899 C CD1 . TYR AA 1 151 ? -9.843 -26.380 43.188 1.0 41.55 ? ? ? ? ? ? 268 TYR AA CD1 1 151 A A +ATOM 3900 C CD2 . TYR AA 1 151 ? -8.725 -24.962 44.759 1.0 64.94 ? ? ? ? ? ? 268 TYR AA CD2 1 151 A A +ATOM 3901 C CE1 . TYR AA 1 151 ? -11.065 -26.100 43.794 1.0 32.05 ? ? ? ? ? ? 268 TYR AA CE1 1 151 A A +ATOM 3902 C CE2 . TYR AA 1 151 ? -9.943 -24.676 45.371 1.0 62.63 ? ? ? ? ? ? 268 TYR AA CE2 1 151 A A +ATOM 3903 C CZ . TYR AA 1 151 ? -11.108 -25.251 44.885 1.0 42.2 ? ? ? ? ? ? 268 TYR AA CZ 1 151 A A +ATOM 3904 O OH . TYR AA 1 151 ? -12.312 -24.983 45.499 1.0 37.44 ? ? ? ? ? ? 268 TYR AA OH 1 151 A A +ATOM 3905 N N . ILE AA 1 152 ? -8.121 -27.022 40.408 1.0 56.45 ? ? ? ? ? ? 269 ILE AA N 1 152 A A +ATOM 3906 C CA . ILE AA 1 152 ? -9.000 -27.509 39.346 1.0 60.67 ? ? ? ? ? ? 269 ILE AA CA 1 152 A A +ATOM 3907 C C . ILE AA 1 152 ? -9.738 -28.791 39.723 1.0 61.55 ? ? ? ? ? ? 269 ILE AA C 1 152 A A +ATOM 3908 O O . ILE AA 1 152 ? -9.237 -29.599 40.501 1.0 65.11 ? ? ? ? ? ? 269 ILE AA O 1 152 A A +ATOM 3909 C CB . ILE AA 1 152 ? -8.205 -27.802 38.067 1.0 50.21 ? ? ? ? ? ? 269 ILE AA CB 1 152 A A +ATOM 3910 C CG1 . ILE AA 1 152 ? -9.144 -28.320 36.978 1.0 55.34 ? ? ? ? ? ? 269 ILE AA CG1 1 152 A A +ATOM 3911 C CG2 . ILE AA 1 152 ? -7.128 -28.833 38.360 1.0 43.33 ? ? ? ? ? ? 269 ILE AA CG2 1 152 A A +ATOM 3912 C CD1 . ILE AA 1 152 ? -8.509 -28.408 35.616 1.0 70.88 ? ? ? ? ? ? 269 ILE AA CD1 1 152 A A +ATOM 3913 N N . ARG AA 1 153 ? -10.922 -28.976 39.149 1.0 70.19 ? ? ? ? ? ? 270 ARG AA N 1 153 A A +ATOM 3914 C CA . ARG AA 1 153 ? -11.735 -30.159 39.409 1.0 76.56 ? ? ? ? ? ? 270 ARG AA CA 1 153 A A +ATOM 3915 C C . ARG AA 1 153 ? -10.931 -31.417 39.101 1.0 74.71 ? ? ? ? ? ? 270 ARG AA C 1 153 A A +ATOM 3916 O O . ARG AA 1 153 ? -9.870 -31.348 38.480 1.0 68.44 ? ? ? ? ? ? 270 ARG AA O 1 153 A A +ATOM 3917 C CB . ARG AA 1 153 ? -12.986 -30.131 38.533 1.0 84.04 ? ? ? ? ? ? 270 ARG AA CB 1 153 A A +ATOM 3918 C CG . ARG AA 1 153 ? -12.687 -30.056 37.044 1.0 85.5 ? ? ? ? ? ? 270 ARG AA CG 1 153 A A +ATOM 3919 C CD . ARG AA 1 153 ? -13.956 -29.912 36.231 1.0 88.12 ? ? ? ? ? ? 270 ARG AA CD 1 153 A A +ATOM 3920 N NE . ARG AA 1 153 ? -14.284 -28.512 35.990 1.0 82.86 ? ? ? ? ? ? 270 ARG AA NE 1 153 A A +ATOM 3921 C CZ . ARG AA 1 153 ? -15.062 -28.089 35.001 1.0 79.01 ? ? ? ? ? ? 270 ARG AA CZ 1 153 A A +ATOM 3922 N NH1 . ARG AA 1 153 ? -15.593 -28.963 34.158 1.0 74.83 ? ? ? ? ? ? 270 ARG AA NH1 1 153 A A +ATOM 3923 N NH2 . ARG AA 1 153 ? -15.312 -26.796 34.855 1.0 64.13 ? ? ? ? ? ? 270 ARG AA NH2 1 153 A A +ATOM 3924 N N . HIS AA 1 154 ? -11.438 -32.565 39.538 1.0 73.45 ? ? ? ? ? ? 271 HIS AA N 1 154 A A +ATOM 3925 C CA . HIS AA 1 154 ? -10.754 -33.824 39.283 1.0 76.37 ? ? ? ? ? ? 271 HIS AA CA 1 154 A A +ATOM 3926 C C . HIS AA 1 154 ? -11.101 -34.324 37.890 1.0 80.1 ? ? ? ? ? ? 271 HIS AA C 1 154 A A +ATOM 3927 O O . HIS AA 1 154 ? -12.244 -34.214 37.447 1.0 90.33 ? ? ? ? ? ? 271 HIS AA O 1 154 A A +ATOM 3928 C CB . HIS AA 1 154 ? -11.143 -34.884 40.312 1.0 85.46 ? ? ? ? ? ? 271 HIS AA CB 1 154 A A +ATOM 3929 C CG . HIS AA 1 154 ? -10.284 -36.110 40.258 1.0 90.77 ? ? ? ? ? ? 271 HIS AA CG 1 154 A A +ATOM 3930 N ND1 . HIS AA 1 154 ? -10.783 -37.356 39.947 1.0 95.04 ? ? ? ? ? ? 271 HIS AA ND1 1 154 A A +ATOM 3931 C CD2 . HIS AA 1 154 ? -8.952 -36.273 40.442 1.0 89.61 ? ? ? ? ? ? 271 HIS AA CD2 1 154 A A +ATOM 3932 C CE1 . HIS AA 1 154 ? -9.794 -38.234 39.942 1.0 100.0 ? ? ? ? ? ? 271 HIS AA CE1 1 154 A A +ATOM 3933 N NE2 . HIS AA 1 154 ? -8.673 -37.601 40.240 1.0 89.7 ? ? ? ? ? ? 271 HIS AA NE2 1 154 A A +ATOM 3934 N N . GLY AA 1 155 ? -10.108 -34.883 37.210 1.0 78.16 ? ? ? ? ? ? 272 GLY AA N 1 155 A A +ATOM 3935 C CA . GLY AA 1 155 ? -10.314 -35.385 35.864 1.0 82.41 ? ? ? ? ? ? 272 GLY AA CA 1 155 A A +ATOM 3936 C C . GLY AA 1 155 ? -11.359 -36.474 35.689 1.0 76.8 ? ? ? ? ? ? 272 GLY AA C 1 155 A A +ATOM 3937 O O . GLY AA 1 155 ? -11.759 -36.757 34.560 1.0 83.1 ? ? ? ? ? ? 272 GLY AA O 1 155 A A +ATOM 3938 N N . SER AA 1 156 ? -11.804 -37.093 36.779 1.0 69.09 ? ? ? ? ? ? 273 SER AA N 1 156 A A +ATOM 3939 C CA . SER AA 1 156 ? -12.808 -38.155 36.676 1.0 68.79 ? ? ? ? ? ? 273 SER AA CA 1 156 A A +ATOM 3940 C C . SER AA 1 156 ? -14.020 -37.679 35.880 1.0 68.32 ? ? ? ? ? ? 273 SER AA C 1 156 A A +ATOM 3941 O O . SER AA 1 156 ? -14.419 -38.314 34.904 1.0 75.05 ? ? ? ? ? ? 273 SER AA O 1 156 A A +ATOM 3942 C CB . SER AA 1 156 ? -13.245 -38.625 38.071 1.0 77.85 ? ? ? ? ? ? 273 SER AA CB 1 156 A A +ATOM 3943 O OG . SER AA 1 156 ? -13.834 -37.579 38.824 1.0 83.43 ? ? ? ? ? ? 273 SER AA OG 1 156 A A +ATOM 3944 N N . LYS AA 1 157 ? -14.598 -36.560 36.304 1.0 66.77 ? ? ? ? ? ? 274 LYS AA N 1 157 A A +ATOM 3945 C CA . LYS AA 1 157 ? -15.750 -35.983 35.625 1.0 64.76 ? ? ? ? ? ? 274 LYS AA CA 1 157 A A +ATOM 3946 C C . LYS AA 1 157 ? -15.429 -34.540 35.237 1.0 67.12 ? ? ? ? ? ? 274 LYS AA C 1 157 A A +ATOM 3947 O O . LYS AA 1 157 ? -15.731 -33.600 35.972 1.0 66.67 ? ? ? ? ? ? 274 LYS AA O 1 157 A A +ATOM 3948 C CB . LYS AA 1 157 ? -16.978 -36.047 36.535 1.0 68.16 ? ? ? ? ? ? 274 LYS AA CB 1 157 A A +ATOM 3949 C CG . LYS AA 1 157 ? -17.618 -37.427 36.586 1.0 79.05 ? ? ? ? ? ? 274 LYS AA CG 1 157 A A +ATOM 3950 C CD . LYS AA 1 157 ? -18.049 -37.885 35.197 1.0 94.09 ? ? ? ? ? ? 274 LYS AA CD 1 157 A A +ATOM 3951 C CE . LYS AA 1 157 ? -18.566 -39.320 35.212 1.0 96.98 ? ? ? ? ? ? 274 LYS AA CE 1 157 A A +ATOM 3952 N NZ . LYS AA 1 157 ? -18.840 -39.832 33.840 1.0 100.0 ? ? ? ? ? ? 274 LYS AA NZ 1 157 A A +ATOM 3953 N N . PRO AA 1 158 ? -14.803 -34.357 34.062 1.0 61.91 ? ? ? ? ? ? 275 PRO AA N 1 158 A A +ATOM 3954 C CA . PRO AA 1 158 ? -14.411 -33.047 33.532 1.0 65.03 ? ? ? ? ? ? 275 PRO AA CA 1 158 A A +ATOM 3955 C C . PRO AA 1 158 ? -15.582 -32.189 33.063 1.0 72.4 ? ? ? ? ? ? 275 PRO AA C 1 158 A A +ATOM 3956 O O . PRO AA 1 158 ? -15.383 -31.131 32.463 1.0 89.09 ? ? ? ? ? ? 275 PRO AA O 1 158 A A +ATOM 3957 C CB . PRO AA 1 158 ? -13.458 -33.394 32.390 1.0 60.82 ? ? ? ? ? ? 275 PRO AA CB 1 158 A A +ATOM 3958 C CG . PRO AA 1 158 ? -13.905 -34.738 31.936 1.0 76.64 ? ? ? ? ? ? 275 PRO AA CG 1 158 A A +ATOM 3959 C CD . PRO AA 1 158 ? -14.438 -35.451 33.146 1.0 72.44 ? ? ? ? ? ? 275 PRO AA CD 1 158 A A +ATOM 3960 N N . MET AA 1 159 ? -16.801 -32.642 33.339 1.0 57.47 ? ? ? ? ? ? 276 MET AA N 1 159 A A +ATOM 3961 C CA . MET AA 1 159 ? -17.992 -31.899 32.944 1.0 67.57 ? ? ? ? ? ? 276 MET AA CA 1 159 A A +ATOM 3962 C C . MET AA 1 159 ? -18.830 -31.539 34.166 1.0 74.14 ? ? ? ? ? ? 276 MET AA C 1 159 A A +ATOM 3963 O O . MET AA 1 159 ? -19.989 -31.143 34.045 1.0 84.59 ? ? ? ? ? ? 276 MET AA O 1 159 A A +ATOM 3964 C CB . MET AA 1 159 ? -18.828 -32.727 31.965 1.0 79.9 ? ? ? ? ? ? 276 MET AA CB 1 159 A A +ATOM 3965 C CG . MET AA 1 159 ? -19.140 -32.022 30.651 1.0 82.99 ? ? ? ? ? ? 276 MET AA CG 1 159 A A +ATOM 3966 S SD . MET AA 1 159 ? -17.679 -31.388 29.799 1.0 94.71 ? ? ? ? ? ? 276 MET AA SD 1 159 A A +ATOM 3967 C CE . MET AA 1 159 ? -17.801 -29.648 30.171 1.0 100.0 ? ? ? ? ? ? 276 MET AA CE 1 159 A A +ATOM 3968 N N . TYR AA 1 160 ? -18.234 -31.669 35.345 1.0 81.71 ? ? ? ? ? ? 277 TYR AA N 1 160 A A +ATOM 3969 C CA . TYR AA 1 160 ? -18.933 -31.355 36.579 1.0 95.68 ? ? ? ? ? ? 277 TYR AA CA 1 160 A A +ATOM 3970 C C . TYR AA 1 160 ? -17.984 -30.983 37.716 1.0 96.34 ? ? ? ? ? ? 277 TYR AA C 1 160 A A +ATOM 3971 O O . TYR AA 1 160 ? -16.938 -31.610 37.904 1.0 94.33 ? ? ? ? ? ? 277 TYR AA O 1 160 A A +ATOM 3972 C CB . TYR AA 1 160 ? -19.800 -32.541 37.000 1.0 92.57 ? ? ? ? ? ? 277 TYR AA CB 1 160 A A +ATOM 3973 C CG . TYR AA 1 160 ? -20.081 -32.589 38.482 1.0 98.35 ? ? ? ? ? ? 277 TYR AA CG 1 160 A A +ATOM 3974 C CD1 . TYR AA 1 160 ? -21.004 -31.723 39.061 1.0 100.0 ? ? ? ? ? ? 277 TYR AA CD1 1 160 A A +ATOM 3975 C CD2 . TYR AA 1 160 ? -19.416 -33.495 39.309 1.0 93.13 ? ? ? ? ? ? 277 TYR AA CD2 1 160 A A +ATOM 3976 C CE1 . TYR AA 1 160 ? -21.259 -31.756 40.428 1.0 95.63 ? ? ? ? ? ? 277 TYR AA CE1 1 160 A A +ATOM 3977 C CE2 . TYR AA 1 160 ? -19.663 -33.537 40.676 1.0 94.92 ? ? ? ? ? ? 277 TYR AA CE2 1 160 A A +ATOM 3978 C CZ . TYR AA 1 160 ? -20.586 -32.665 41.229 1.0 95.01 ? ? ? ? ? ? 277 TYR AA CZ 1 160 A A +ATOM 3979 O OH . TYR AA 1 160 ? -20.842 -32.712 42.581 1.0 91.12 ? ? ? ? ? ? 277 TYR AA OH 1 160 A A +ATOM 3980 N N . THR AA 1 161 ? -18.365 -29.955 38.468 1.0 86.12 ? ? ? ? ? ? 278 THR AA N 1 161 A A +ATOM 3981 C CA . THR AA 1 161 ? -17.583 -29.485 39.607 1.0 75.54 ? ? ? ? ? ? 278 THR AA CA 1 161 A A +ATOM 3982 C C . THR AA 1 161 ? -18.545 -29.144 40.738 1.0 72.73 ? ? ? ? ? ? 278 THR AA C 1 161 A A +ATOM 3983 O O . THR AA 1 161 ? -19.518 -28.420 40.542 1.0 73.03 ? ? ? ? ? ? 278 THR AA O 1 161 A A +ATOM 3984 C CB . THR AA 1 161 ? -16.757 -28.235 39.255 1.0 82.17 ? ? ? ? ? ? 278 THR AA CB 1 161 A A +ATOM 3985 O OG1 . THR AA 1 161 ? -16.333 -28.316 37.888 1.0 98.31 ? ? ? ? ? ? 278 THR AA OG1 1 161 A A +ATOM 3986 C CG2 . THR AA 1 161 ? -15.540 -28.150 40.153 1.0 85.64 ? ? ? ? ? ? 278 THR AA CG2 1 161 A A +ATOM 3987 N N . PRO AA 1 162 ? -18.276 -29.655 41.946 1.0 78.92 ? ? ? ? ? ? 279 PRO AA N 1 162 A A +ATOM 3988 C CA . PRO AA 1 162 ? -19.149 -29.387 43.092 1.0 76.69 ? ? ? ? ? ? 279 PRO AA CA 1 162 A A +ATOM 3989 C C . PRO AA 1 162 ? -18.937 -28.001 43.682 1.0 70.76 ? ? ? ? ? ? 279 PRO AA C 1 162 A A +ATOM 3990 O O . PRO AA 1 162 ? -19.663 -27.573 44.575 1.0 64.88 ? ? ? ? ? ? 279 PRO AA O 1 162 A A +ATOM 3991 C CB . PRO AA 1 162 ? -18.789 -30.489 44.077 1.0 69.92 ? ? ? ? ? ? 279 PRO AA CB 1 162 A A +ATOM 3992 C CG . PRO AA 1 162 ? -17.362 -30.816 43.764 1.0 82.58 ? ? ? ? ? ? 279 PRO AA CG 1 162 A A +ATOM 3993 C CD . PRO AA 1 162 ? -17.117 -30.483 42.314 1.0 84.25 ? ? ? ? ? ? 279 PRO AA CD 1 162 A A +ATOM 3994 N N . GLU AA 1 163 ? -17.934 -27.299 43.162 1.0 68.53 ? ? ? ? ? ? 280 GLU AA N 1 163 A A +ATOM 3995 C CA . GLU AA 1 163 ? -17.613 -25.962 43.632 1.0 69.05 ? ? ? ? ? ? 280 GLU AA CA 1 163 A A +ATOM 3996 C C . GLU AA 1 163 ? -16.699 -25.251 42.639 1.0 63.34 ? ? ? ? ? ? 280 GLU AA C 1 163 A A +ATOM 3997 O O . GLU AA 1 163 ? -16.166 -25.870 41.725 1.0 60.75 ? ? ? ? ? ? 280 GLU AA O 1 163 A A +ATOM 3998 C CB . GLU AA 1 163 ? -16.947 -26.052 45.007 1.0 74.71 ? ? ? ? ? ? 280 GLU AA CB 1 163 A A +ATOM 3999 C CG . GLU AA 1 163 ? -15.455 -26.294 44.936 1.0 78.89 ? ? ? ? ? ? 280 GLU AA CG 1 163 A A +ATOM 4000 C CD . GLU AA 1 163 ? -15.111 -27.767 44.915 1.0 76.97 ? ? ? ? ? ? 280 GLU AA CD 1 163 A A +ATOM 4001 O OE1 . GLU AA 1 163 ? -15.271 -28.428 45.959 1.0 74.45 ? ? ? ? ? ? 280 GLU AA OE1 1 163 A A +ATOM 4002 O OE2 . GLU AA 1 163 ? -14.679 -28.265 43.858 1.0 77.77 ? ? ? ? ? ? 280 GLU AA OE2 1 163 A A +ATOM 4003 N N . PRO AA 1 164 ? -16.477 -23.939 42.836 1.0 59.44 ? ? ? ? ? ? 281 PRO AA N 1 164 A A +ATOM 4004 C CA . PRO AA 1 164 ? -15.618 -23.167 41.928 1.0 57.6 ? ? ? ? ? ? 281 PRO AA CA 1 164 A A +ATOM 4005 C C . PRO AA 1 164 ? -14.191 -23.672 41.755 1.0 49.97 ? ? ? ? ? ? 281 PRO AA C 1 164 A A +ATOM 4006 O O . PRO AA 1 164 ? -13.484 -23.914 42.728 1.0 53.11 ? ? ? ? ? ? 281 PRO AA O 1 164 A A +ATOM 4007 C CB . PRO AA 1 164 ? -15.646 -21.755 42.512 1.0 51.17 ? ? ? ? ? ? 281 PRO AA CB 1 164 A A +ATOM 4008 C CG . PRO AA 1 164 ? -16.793 -21.733 43.456 1.0 70.63 ? ? ? ? ? ? 281 PRO AA CG 1 164 A A +ATOM 4009 C CD . PRO AA 1 164 ? -16.982 -23.122 43.951 1.0 59.4 ? ? ? ? ? ? 281 PRO AA CD 1 164 A A +ATOM 4010 N N . ASP AA 1 165 ? -13.781 -23.816 40.497 1.0 45.57 ? ? ? ? ? ? 282 ASP AA N 1 165 A A +ATOM 4011 C CA . ASP AA 1 165 ? -12.434 -24.259 40.132 1.0 43.57 ? ? ? ? ? ? 282 ASP AA CA 1 165 A A +ATOM 4012 C C . ASP AA 1 165 ? -11.888 -23.241 39.139 1.0 36.46 ? ? ? ? ? ? 282 ASP AA C 1 165 A A +ATOM 4013 O O . ASP AA 1 165 ? -12.638 -22.399 38.649 1.0 47.96 ? ? ? ? ? ? 282 ASP AA O 1 165 A A +ATOM 4014 C CB . ASP AA 1 165 ? -12.479 -25.641 39.482 1.0 55.07 ? ? ? ? ? ? 282 ASP AA CB 1 165 A A +ATOM 4015 C CG . ASP AA 1 165 ? -13.059 -25.609 38.080 1.0 67.89 ? ? ? ? ? ? 282 ASP AA CG 1 165 A A +ATOM 4016 O OD1 . ASP AA 1 165 ? -12.523 -26.316 37.200 1.0 65.08 ? ? ? ? ? ? 282 ASP AA OD1 1 165 A A +ATOM 4017 O OD2 . ASP AA 1 165 ? -14.048 -24.878 37.859 1.0 75.95 ? ? ? ? ? ? 282 ASP AA OD2 1 165 A A +ATOM 4018 N N . ILE AA 1 166 ? -10.598 -23.318 38.830 1.0 33.07 ? ? ? ? ? ? 283 ILE AA N 1 166 A A +ATOM 4019 C CA . ILE AA 1 166 ? -9.988 -22.363 37.903 1.0 45.55 ? ? ? ? ? ? 283 ILE AA CA 1 166 A A +ATOM 4020 C C . ILE AA 1 166 ? -10.702 -22.223 36.551 1.0 52.96 ? ? ? ? ? ? 283 ILE AA C 1 166 A A +ATOM 4021 O O . ILE AA 1 166 ? -10.421 -21.300 35.781 1.0 56.77 ? ? ? ? ? ? 283 ILE AA O 1 166 A A +ATOM 4022 C CB . ILE AA 1 166 ? -8.508 -22.702 37.631 1.0 42.94 ? ? ? ? ? ? 283 ILE AA CB 1 166 A A +ATOM 4023 C CG1 . ILE AA 1 166 ? -7.812 -21.487 37.001 1.0 52.36 ? ? ? ? ? ? 283 ILE AA CG1 1 166 A A +ATOM 4024 C CG2 . ILE AA 1 166 ? -8.410 -23.921 36.722 1.0 38.58 ? ? ? ? ? ? 283 ILE AA CG2 1 166 A A +ATOM 4025 C CD1 . ILE AA 1 166 ? -6.301 -21.484 37.149 1.0 55.61 ? ? ? ? ? ? 283 ILE AA CD1 1 166 A A +ATOM 4026 N N . CYS AA 1 167 ? -11.622 -23.137 36.259 1.0 51.82 ? ? ? ? ? ? 284 CYS AA N 1 167 A A +ATOM 4027 C CA . CYS AA 1 167 ? -12.368 -23.079 35.009 1.0 56.36 ? ? ? ? ? ? 284 CYS AA CA 1 167 A A +ATOM 4028 C C . CYS AA 1 167 ? -13.563 -22.157 35.196 1.0 54.65 ? ? ? ? ? ? 284 CYS AA C 1 167 A A +ATOM 4029 O O . CYS AA 1 167 ? -13.810 -21.268 34.382 1.0 67.24 ? ? ? ? ? ? 284 CYS AA O 1 167 A A +ATOM 4030 C CB . CYS AA 1 167 ? -12.847 -24.477 34.612 1.0 74.89 ? ? ? ? ? ? 284 CYS AA CB 1 167 A A +ATOM 4031 S SG . CYS AA 1 167 ? -11.566 -25.751 34.656 1.0 99.53 ? ? ? ? ? ? 284 CYS AA SG 1 167 A A +ATOM 4032 N N . HIS AA 1 168 ? -14.300 -22.374 36.279 1.0 62.12 ? ? ? ? ? ? 285 HIS AA N 1 168 A A +ATOM 4033 C CA . HIS AA 1 168 ? -15.469 -21.559 36.582 1.0 64.94 ? ? ? ? ? ? 285 HIS AA CA 1 168 A A +ATOM 4034 C C . HIS AA 1 168 ? -15.064 -20.099 36.749 1.0 59.74 ? ? ? ? ? ? 285 HIS AA C 1 168 A A +ATOM 4035 O O . HIS AA 1 168 ? -15.721 -19.196 36.231 1.0 64.62 ? ? ? ? ? ? 285 HIS AA O 1 168 A A +ATOM 4036 C CB . HIS AA 1 168 ? -16.141 -22.075 37.858 1.0 61.21 ? ? ? ? ? ? 285 HIS AA CB 1 168 A A +ATOM 4037 C CG . HIS AA 1 168 ? -17.088 -21.101 38.487 1.0 76.62 ? ? ? ? ? ? 285 HIS AA CG 1 168 A A +ATOM 4038 N ND1 . HIS AA 1 168 ? -18.395 -20.961 38.075 1.0 93.0 ? ? ? ? ? ? 285 HIS AA ND1 1 168 A A +ATOM 4039 C CD2 . HIS AA 1 168 ? -16.920 -20.240 39.516 1.0 87.22 ? ? ? ? ? ? 285 HIS AA CD2 1 168 A A +ATOM 4040 C CE1 . HIS AA 1 168 ? -18.994 -20.054 38.825 1.0 100.0 ? ? ? ? ? ? 285 HIS AA CE1 1 168 A A +ATOM 4041 N NE2 . HIS AA 1 168 ? -18.122 -19.600 39.707 1.0 99.45 ? ? ? ? ? ? 285 HIS AA NE2 1 168 A A +ATOM 4042 N N . GLU AA 1 169 ? -13.965 -19.878 37.459 1.0 52.73 ? ? ? ? ? ? 286 GLU AA N 1 169 A A +ATOM 4043 C CA . GLU AA 1 169 ? -13.473 -18.531 37.714 1.0 57.66 ? ? ? ? ? ? 286 GLU AA CA 1 169 A A +ATOM 4044 C C . GLU AA 1 169 ? -12.921 -17.837 36.475 1.0 60.34 ? ? ? ? ? ? 286 GLU AA C 1 169 A A +ATOM 4045 O O . GLU AA 1 169 ? -13.168 -16.648 36.268 1.0 77.83 ? ? ? ? ? ? 286 GLU AA O 1 169 A A +ATOM 4046 C CB . GLU AA 1 169 ? -12.390 -18.564 38.795 1.0 61.13 ? ? ? ? ? ? 286 GLU AA CB 1 169 A A +ATOM 4047 C CG . GLU AA 1 169 ? -12.696 -19.492 39.954 1.0 76.3 ? ? ? ? ? ? 286 GLU AA CG 1 169 A A +ATOM 4048 C CD . GLU AA 1 169 ? -13.524 -18.830 41.036 1.0 85.35 ? ? ? ? ? ? 286 GLU AA CD 1 169 A A +ATOM 4049 O OE1 . GLU AA 1 169 ? -12.933 -18.301 42.000 1.0 72.35 ? ? ? ? ? ? 286 GLU AA OE1 1 169 A A +ATOM 4050 O OE2 . GLU AA 1 169 ? -14.767 -18.842 40.930 1.0 88.17 ? ? ? ? ? ? 286 GLU AA OE2 1 169 A A +ATOM 4051 N N . LEU AA 1 170 ? -12.180 -18.579 35.654 1.0 48.09 ? ? ? ? ? ? 287 LEU AA N 1 170 A A +ATOM 4052 C CA . LEU AA 1 170 ? -11.576 -18.017 34.443 1.0 60.37 ? ? ? ? ? ? 287 LEU AA CA 1 170 A A +ATOM 4053 C C . LEU AA 1 170 ? -12.481 -18.001 33.206 1.0 62.26 ? ? ? ? ? ? 287 LEU AA C 1 170 A A +ATOM 4054 O O . LEU AA 1 170 ? -12.497 -17.024 32.455 1.0 60.64 ? ? ? ? ? ? 287 LEU AA O 1 170 A A +ATOM 4055 C CB . LEU AA 1 170 ? -10.284 -18.762 34.107 1.0 55.75 ? ? ? ? ? ? 287 LEU AA CB 1 170 A A +ATOM 4056 C CG . LEU AA 1 170 ? -9.028 -18.436 34.923 1.0 61.06 ? ? ? ? ? ? 287 LEU AA CG 1 170 A A +ATOM 4057 C CD1 . LEU AA 1 170 ? -7.825 -19.092 34.266 1.0 59.23 ? ? ? ? ? ? 287 LEU AA CD1 1 170 A A +ATOM 4058 C CD2 . LEU AA 1 170 ? -8.827 -16.932 35.011 1.0 40.81 ? ? ? ? ? ? 287 LEU AA CD2 1 170 A A +ATOM 4059 N N . LEU AA 1 171 ? -13.224 -19.081 32.993 1.0 60.18 ? ? ? ? ? ? 288 LEU AA N 1 171 A A +ATOM 4060 C CA . LEU AA 1 171 ? -14.124 -19.175 31.847 1.0 54.52 ? ? ? ? ? ? 288 LEU AA CA 1 171 A A +ATOM 4061 C C . LEU AA 1 171 ? -15.562 -18.869 32.264 1.0 63.82 ? ? ? ? ? ? 288 LEU AA C 1 171 A A +ATOM 4062 O O . LEU AA 1 171 ? -16.512 -19.389 31.677 1.0 73.18 ? ? ? ? ? ? 288 LEU AA O 1 171 A A +ATOM 4063 C CB . LEU AA 1 171 ? -14.057 -20.580 31.231 1.0 56.91 ? ? ? ? ? ? 288 LEU AA CB 1 171 A A +ATOM 4064 C CG . LEU AA 1 171 ? -12.673 -21.141 30.892 1.0 46.12 ? ? ? ? ? ? 288 LEU AA CG 1 171 A A +ATOM 4065 C CD1 . LEU AA 1 171 ? -12.787 -22.614 30.537 1.0 35.1 ? ? ? ? ? ? 288 LEU AA CD1 1 171 A A +ATOM 4066 C CD2 . LEU AA 1 171 ? -12.072 -20.351 29.750 1.0 36.21 ? ? ? ? ? ? 288 LEU AA CD2 1 171 A A +ATOM 4067 N N . GLY AA 1 172 ? -15.717 -18.025 33.279 1.0 69.02 ? ? ? ? ? ? 289 GLY AA N 1 172 A A +ATOM 4068 C CA . GLY AA 1 172 ? -17.047 -17.681 33.741 1.0 74.13 ? ? ? ? ? ? 289 GLY AA CA 1 172 A A +ATOM 4069 C C . GLY AA 1 172 ? -17.131 -16.308 34.369 1.0 66.63 ? ? ? ? ? ? 289 GLY AA C 1 172 A A +ATOM 4070 O O . GLY AA 1 172 ? -17.912 -15.467 33.928 1.0 81.62 ? ? ? ? ? ? 289 GLY AA O 1 172 A A +ATOM 4071 N N . HIS AA 1 173 ? -16.325 -16.081 35.401 1.0 50.97 ? ? ? ? ? ? 290 HIS AA N 1 173 A A +ATOM 4072 C CA . HIS AA 1 173 ? -16.314 -14.803 36.104 1.0 46.5 ? ? ? ? ? ? 290 HIS AA CA 1 173 A A +ATOM 4073 C C . HIS AA 1 173 ? -15.419 -13.752 35.444 1.0 50.67 ? ? ? ? ? ? 290 HIS AA C 1 173 A A +ATOM 4074 O O . HIS AA 1 173 ? -15.885 -12.677 35.063 1.0 50.37 ? ? ? ? ? ? 290 HIS AA O 1 173 A A +ATOM 4075 C CB . HIS AA 1 173 ? -15.860 -15.010 37.551 1.0 52.24 ? ? ? ? ? ? 290 HIS AA CB 1 173 A A +ATOM 4076 C CG . HIS AA 1 173 ? -16.938 -15.518 38.459 1.0 62.48 ? ? ? ? ? ? 290 HIS AA CG 1 173 A A +ATOM 4077 N ND1 . HIS AA 1 173 ? -17.806 -14.683 39.127 1.0 64.94 ? ? ? ? ? ? 290 HIS AA ND1 1 173 A A +ATOM 4078 C CD2 . HIS AA 1 173 ? -17.281 -16.781 38.812 1.0 49.65 ? ? ? ? ? ? 290 HIS AA CD2 1 173 A A +ATOM 4079 C CE1 . HIS AA 1 173 ? -18.639 -15.407 39.854 1.0 64.48 ? ? ? ? ? ? 290 HIS AA CE1 1 173 A A +ATOM 4080 N NE2 . HIS AA 1 173 ? -18.342 -16.682 39.680 1.0 54.47 ? ? ? ? ? ? 290 HIS AA NE2 1 173 A A +ATOM 4081 N N . VAL AA 1 174 ? -14.132 -14.072 35.317 1.0 51.67 ? ? ? ? ? ? 291 VAL AA N 1 174 A A +ATOM 4082 C CA . VAL AA 1 174 ? -13.137 -13.171 34.735 1.0 60.23 ? ? ? ? ? ? 291 VAL AA CA 1 174 A A +ATOM 4083 C C . VAL AA 1 174 ? -13.575 -12.320 33.538 1.0 63.65 ? ? ? ? ? ? 291 VAL AA C 1 174 A A +ATOM 4084 O O . VAL AA 1 174 ? -13.439 -11.096 33.564 1.0 66.68 ? ? ? ? ? ? 291 VAL AA O 1 174 A A +ATOM 4085 C CB . VAL AA 1 174 ? -11.860 -13.954 34.342 1.0 68.66 ? ? ? ? ? ? 291 VAL AA CB 1 174 A A +ATOM 4086 C CG1 . VAL AA 1 174 ? -10.872 -13.045 33.623 1.0 51.75 ? ? ? ? ? ? 291 VAL AA CG1 1 174 A A +ATOM 4087 C CG2 . VAL AA 1 174 ? -11.218 -14.539 35.583 1.0 59.3 ? ? ? ? ? ? 291 VAL AA CG2 1 174 A A +ATOM 4088 N N . PRO AA 1 175 ? -14.109 -12.954 32.475 1.0 56.06 ? ? ? ? ? ? 292 PRO AA N 1 175 A A +ATOM 4089 C CA . PRO AA 1 175 ? -14.527 -12.162 31.309 1.0 52.02 ? ? ? ? ? ? 292 PRO AA CA 1 175 A A +ATOM 4090 C C . PRO AA 1 175 ? -15.512 -11.038 31.617 1.0 48.25 ? ? ? ? ? ? 292 PRO AA C 1 175 A A +ATOM 4091 O O . PRO AA 1 175 ? -15.535 -10.027 30.925 1.0 55.38 ? ? ? ? ? ? 292 PRO AA O 1 175 A A +ATOM 4092 C CB . PRO AA 1 175 ? -15.124 -13.197 30.351 1.0 50.93 ? ? ? ? ? ? 292 PRO AA CB 1 175 A A +ATOM 4093 C CG . PRO AA 1 175 ? -14.618 -14.509 30.823 1.0 66.89 ? ? ? ? ? ? 292 PRO AA CG 1 175 A A +ATOM 4094 C CD . PRO AA 1 175 ? -14.377 -14.389 32.295 1.0 48.46 ? ? ? ? ? ? 292 PRO AA CD 1 175 A A +ATOM 4095 N N . LEU AA 1 176 ? -16.326 -11.215 32.652 1.0 45.32 ? ? ? ? ? ? 293 LEU AA N 1 176 A A +ATOM 4096 C CA . LEU AA 1 176 ? -17.298 -10.196 33.018 1.0 40.66 ? ? ? ? ? ? 293 LEU AA CA 1 176 A A +ATOM 4097 C C . LEU AA 1 176 ? -16.630 -9.088 33.812 1.0 44.9 ? ? ? ? ? ? 293 LEU AA C 1 176 A A +ATOM 4098 O O . LEU AA 1 176 ? -17.012 -7.925 33.703 1.0 48.65 ? ? ? ? ? ? 293 LEU AA O 1 176 A A +ATOM 4099 C CB . LEU AA 1 176 ? -18.429 -10.813 33.845 1.0 39.05 ? ? ? ? ? ? 293 LEU AA CB 1 176 A A +ATOM 4100 C CG . LEU AA 1 176 ? -19.582 -11.443 33.056 1.0 46.07 ? ? ? ? ? ? 293 LEU AA CG 1 176 A A +ATOM 4101 C CD1 . LEU AA 1 176 ? -20.115 -10.460 32.027 1.0 37.81 ? ? ? ? ? ? 293 LEU AA CD1 1 176 A A +ATOM 4102 C CD2 . LEU AA 1 176 ? -19.097 -12.702 32.378 1.0 56.64 ? ? ? ? ? ? 293 LEU AA CD2 1 176 A A +ATOM 4103 N N . PHE AA 1 177 ? -15.629 -9.456 34.607 1.0 40.73 ? ? ? ? ? ? 294 PHE AA N 1 177 A A +ATOM 4104 C CA . PHE AA 1 177 ? -14.906 -8.488 35.423 1.0 34.87 ? ? ? ? ? ? 294 PHE AA CA 1 177 A A +ATOM 4105 C C . PHE AA 1 177 ? -13.967 -7.638 34.576 1.0 35.06 ? ? ? ? ? ? 294 PHE AA C 1 177 A A +ATOM 4106 O O . PHE AA 1 177 ? -13.245 -6.793 35.100 1.0 41.72 ? ? ? ? ? ? 294 PHE AA O 1 177 A A +ATOM 4107 C CB . PHE AA 1 177 ? -14.106 -9.201 36.515 1.0 47.1 ? ? ? ? ? ? 294 PHE AA CB 1 177 A A +ATOM 4108 C CG . PHE AA 1 177 ? -14.953 -9.754 37.624 1.0 41.71 ? ? ? ? ? ? 294 PHE AA CG 1 177 A A +ATOM 4109 C CD1 . PHE AA 1 177 ? -15.463 -8.924 38.613 1.0 40.38 ? ? ? ? ? ? 294 PHE AA CD1 1 177 A A +ATOM 4110 C CD2 . PHE AA 1 177 ? -15.241 -11.111 37.678 1.0 34.31 ? ? ? ? ? ? 294 PHE AA CD2 1 177 A A +ATOM 4111 C CE1 . PHE AA 1 177 ? -16.248 -9.437 39.641 1.0 44.21 ? ? ? ? ? ? 294 PHE AA CE1 1 177 A A +ATOM 4112 C CE2 . PHE AA 1 177 ? -16.026 -11.634 38.701 1.0 46.58 ? ? ? ? ? ? 294 PHE AA CE2 1 177 A A +ATOM 4113 C CZ . PHE AA 1 177 ? -16.530 -10.794 39.686 1.0 53.93 ? ? ? ? ? ? 294 PHE AA CZ 1 177 A A +ATOM 4114 N N . SER AA 1 178 ? -13.978 -7.867 33.266 1.0 31.86 ? ? ? ? ? ? 295 SER AA N 1 178 A A +ATOM 4115 C CA . SER AA 1 178 ? -13.138 -7.094 32.360 1.0 50.78 ? ? ? ? ? ? 295 SER AA CA 1 178 A A +ATOM 4116 C C . SER AA 1 178 ? -13.966 -5.951 31.786 1.0 49.82 ? ? ? ? ? ? 295 SER AA C 1 178 A A +ATOM 4117 O O . SER AA 1 178 ? -13.426 -5.017 31.194 1.0 58.5 ? ? ? ? ? ? 295 SER AA O 1 178 A A +ATOM 4118 C CB . SER AA 1 178 ? -12.618 -7.977 31.228 1.0 43.11 ? ? ? ? ? ? 295 SER AA CB 1 178 A A +ATOM 4119 O OG . SER AA 1 178 ? -13.686 -8.540 30.491 1.0 79.46 ? ? ? ? ? ? 295 SER AA OG 1 178 A A +ATOM 4120 N N . ASP AA 1 179 ? -15.279 -6.024 31.995 1.0 41.9 ? ? ? ? ? ? 296 ASP AA N 1 179 A A +ATOM 4121 C CA . ASP AA 1 179 ? -16.201 -5.009 31.500 1.0 35.45 ? ? ? ? ? ? 296 ASP AA CA 1 179 A A +ATOM 4122 C C . ASP AA 1 179 ? -16.405 -3.874 32.497 1.0 37.03 ? ? ? ? ? ? 296 ASP AA C 1 179 A A +ATOM 4123 O O . ASP AA 1 179 ? -16.794 -4.091 33.641 1.0 48.53 ? ? ? ? ? ? 296 ASP AA O 1 179 A A +ATOM 4124 C CB . ASP AA 1 179 ? -17.551 -5.640 31.160 1.0 61.62 ? ? ? ? ? ? 296 ASP AA CB 1 179 A A +ATOM 4125 C CG . ASP AA 1 179 ? -18.614 -4.606 30.832 1.0 66.1 ? ? ? ? ? ? 296 ASP AA CG 1 179 A A +ATOM 4126 O OD1 . ASP AA 1 179 ? -18.470 -3.907 29.806 1.0 74.5 ? ? ? ? ? ? 296 ASP AA OD1 1 179 A A +ATOM 4127 O OD2 . ASP AA 1 179 ? -19.593 -4.494 31.603 1.0 62.35 ? ? ? ? ? ? 296 ASP AA OD2 1 179 A A +ATOM 4128 N N . ARG AA 1 180 ? -16.146 -2.659 32.029 1.0 36.5 ? ? ? ? ? ? 297 ARG AA N 1 180 A A +ATOM 4129 C CA . ARG AA 1 180 ? -16.268 -1.446 32.826 1.0 37.44 ? ? ? ? ? ? 297 ARG AA CA 1 180 A A +ATOM 4130 C C . ARG AA 1 180 ? -17.536 -1.342 33.666 1.0 30.3 ? ? ? ? ? ? 297 ARG AA C 1 180 A A +ATOM 4131 O O . ARG AA 1 180 ? -17.472 -1.100 34.870 1.0 29.1 ? ? ? ? ? ? 297 ARG AA O 1 180 A A +ATOM 4132 C CB . ARG AA 1 180 ? -16.182 -0.228 31.903 1.0 67.03 ? ? ? ? ? ? 297 ARG AA CB 1 180 A A +ATOM 4133 C CG . ARG AA 1 180 ? -16.466 1.090 32.587 1.0 76.26 ? ? ? ? ? ? 297 ARG AA CG 1 180 A A +ATOM 4134 C CD . ARG AA 1 180 ? -15.248 1.568 33.342 1.0 87.04 ? ? ? ? ? ? 297 ARG AA CD 1 180 A A +ATOM 4135 N NE . ARG AA 1 180 ? -15.494 2.832 34.027 1.0 100.0 ? ? ? ? ? ? 297 ARG AA NE 1 180 A A +ATOM 4136 C CZ . ARG AA 1 180 ? -15.564 4.011 33.420 1.0 100.0 ? ? ? ? ? ? 297 ARG AA CZ 1 180 A A +ATOM 4137 N NH1 . ARG AA 1 180 ? -15.409 4.097 32.105 1.0 94.55 ? ? ? ? ? ? 297 ARG AA NH1 1 180 A A +ATOM 4138 N NH2 . ARG AA 1 180 ? -15.788 5.110 34.132 1.0 87.1 ? ? ? ? ? ? 297 ARG AA NH2 1 180 A A +ATOM 4139 N N . SER AA 1 181 ? -18.684 -1.500 33.021 1.0 33.65 ? ? ? ? ? ? 298 SER AA N 1 181 A A +ATOM 4140 C CA . SER AA 1 181 ? -19.966 -1.395 33.706 1.0 48.8 ? ? ? ? ? ? 298 SER AA CA 1 181 A A +ATOM 4141 C C . SER AA 1 181 ? -20.186 -2.487 34.745 1.0 55.8 ? ? ? ? ? ? 298 SER AA C 1 181 A A +ATOM 4142 O O . SER AA 1 181 ? -20.769 -2.237 35.801 1.0 69.35 ? ? ? ? ? ? 298 SER AA O 1 181 A A +ATOM 4143 C CB . SER AA 1 181 ? -21.111 -1.416 32.688 1.0 70.22 ? ? ? ? ? ? 298 SER AA CB 1 181 A A +ATOM 4144 O OG . SER AA 1 181 ? -20.942 -0.409 31.705 1.0 90.58 ? ? ? ? ? ? 298 SER AA OG 1 181 A A +ATOM 4145 N N . PHE AA 1 182 ? -19.715 -3.695 34.449 1.0 51.08 ? ? ? ? ? ? 299 PHE AA N 1 182 A A +ATOM 4146 C CA . PHE AA 1 182 ? -19.880 -4.815 35.371 1.0 47.74 ? ? ? ? ? ? 299 PHE AA CA 1 182 A A +ATOM 4147 C C . PHE AA 1 182 ? -19.099 -4.634 36.674 1.0 45.77 ? ? ? ? ? ? 299 PHE AA C 1 182 A A +ATOM 4148 O O . PHE AA 1 182 ? -19.596 -4.951 37.756 1.0 48.51 ? ? ? ? ? ? 299 PHE AA O 1 182 A A +ATOM 4149 C CB . PHE AA 1 182 ? -19.459 -6.125 34.696 1.0 40.1 ? ? ? ? ? ? 299 PHE AA CB 1 182 A A +ATOM 4150 C CG . PHE AA 1 182 ? -19.772 -7.351 35.510 1.0 44.36 ? ? ? ? ? ? 299 PHE AA CG 1 182 A A +ATOM 4151 C CD1 . PHE AA 1 182 ? -20.901 -8.114 35.240 1.0 48.96 ? ? ? ? ? ? 299 PHE AA CD1 1 182 A A +ATOM 4152 C CD2 . PHE AA 1 182 ? -18.943 -7.731 36.563 1.0 54.77 ? ? ? ? ? ? 299 PHE AA CD2 1 182 A A +ATOM 4153 C CE1 . PHE AA 1 182 ? -21.206 -9.239 36.011 1.0 47.65 ? ? ? ? ? ? 299 PHE AA CE1 1 182 A A +ATOM 4154 C CE2 . PHE AA 1 182 ? -19.237 -8.853 37.338 1.0 44.92 ? ? ? ? ? ? 299 PHE AA CE2 1 182 A A +ATOM 4155 C CZ . PHE AA 1 182 ? -20.370 -9.607 37.061 1.0 50.64 ? ? ? ? ? ? 299 PHE AA CZ 1 182 A A +ATOM 4156 N N . ALA AA 1 183 ? -17.874 -4.129 36.566 1.0 44.41 ? ? ? ? ? ? 300 ALA AA N 1 183 A A +ATOM 4157 C CA . ALA AA 1 183 ? -17.029 -3.914 37.734 1.0 21.58 ? ? ? ? ? ? 300 ALA AA CA 1 183 A A +ATOM 4158 C C . ALA AA 1 183 ? -17.693 -3.005 38.768 1.0 27.76 ? ? ? ? ? ? 300 ALA AA C 1 183 A A +ATOM 4159 O O . ALA AA 1 183 ? -17.843 -3.392 39.928 1.0 30.56 ? ? ? ? ? ? 300 ALA AA O 1 183 A A +ATOM 4160 C CB . ALA AA 1 183 ? -15.691 -3.332 37.304 1.0 28.65 ? ? ? ? ? ? 300 ALA AA CB 1 183 A A +ATOM 4161 N N . GLN AA 1 184 ? -18.089 -1.802 38.352 1.0 19.15 ? ? ? ? ? ? 301 GLN AA N 1 184 A A +ATOM 4162 C CA . GLN AA 1 184 ? -18.736 -0.859 39.262 1.0 29.43 ? ? ? ? ? ? 301 GLN AA CA 1 184 A A +ATOM 4163 C C . GLN AA 1 184 ? -19.929 -1.543 39.901 1.0 27.53 ? ? ? ? ? ? 301 GLN AA C 1 184 A A +ATOM 4164 O O . GLN AA 1 184 ? -20.164 -1.419 41.102 1.0 31.56 ? ? ? ? ? ? 301 GLN AA O 1 184 A A +ATOM 4165 C CB . GLN AA 1 184 ? -19.204 0.382 38.507 1.0 35.17 ? ? ? ? ? ? 301 GLN AA CB 1 184 A A +ATOM 4166 C CG . GLN AA 1 184 ? -18.105 1.111 37.768 1.0 61.01 ? ? ? ? ? ? 301 GLN AA CG 1 184 A A +ATOM 4167 C CD . GLN AA 1 184 ? -18.658 2.184 36.851 1.0 66.46 ? ? ? ? ? ? 301 GLN AA CD 1 184 A A +ATOM 4168 O OE1 . GLN AA 1 184 ? -19.772 2.064 36.343 1.0 69.57 ? ? ? ? ? ? 301 GLN AA OE1 1 184 A A +ATOM 4169 N NE2 . GLN AA 1 184 ? -17.884 3.239 36.637 1.0 80.16 ? ? ? ? ? ? 301 GLN AA NE2 1 184 A A +ATOM 4170 N N . PHE AA 1 185 ? -20.674 -2.273 39.080 1.0 25.62 ? ? ? ? ? ? 302 PHE AA N 1 185 A A +ATOM 4171 C CA . PHE AA 1 185 ? -21.850 -3.009 39.532 1.0 40.62 ? ? ? ? ? ? 302 PHE AA CA 1 185 A A +ATOM 4172 C C . PHE AA 1 185 ? -21.468 -3.950 40.675 1.0 40.18 ? ? ? ? ? ? 302 PHE AA C 1 185 A A +ATOM 4173 O O . PHE AA 1 185 ? -22.050 -3.902 41.758 1.0 50.94 ? ? ? ? ? ? 302 PHE AA O 1 185 A A +ATOM 4174 C CB . PHE AA 1 185 ? -22.439 -3.794 38.352 1.0 46.62 ? ? ? ? ? ? 302 PHE AA CB 1 185 A A +ATOM 4175 C CG . PHE AA 1 185 ? -23.345 -4.930 38.750 1.0 43.28 ? ? ? ? ? ? 302 PHE AA CG 1 185 A A +ATOM 4176 C CD1 . PHE AA 1 185 ? -24.235 -4.805 39.812 1.0 39.76 ? ? ? ? ? ? 302 PHE AA CD1 1 185 A A +ATOM 4177 C CD2 . PHE AA 1 185 ? -23.315 -6.127 38.041 1.0 59.26 ? ? ? ? ? ? 302 PHE AA CD2 1 185 A A +ATOM 4178 C CE1 . PHE AA 1 185 ? -25.079 -5.855 40.162 1.0 30.38 ? ? ? ? ? ? 302 PHE AA CE1 1 185 A A +ATOM 4179 C CE2 . PHE AA 1 185 ? -24.154 -7.181 38.382 1.0 52.72 ? ? ? ? ? ? 302 PHE AA CE2 1 185 A A +ATOM 4180 C CZ . PHE AA 1 185 ? -25.038 -7.045 39.444 1.0 53.46 ? ? ? ? ? ? 302 PHE AA CZ 1 185 A A +ATOM 4181 N N . SER AA 1 186 ? -20.486 -4.808 40.421 1.0 41.42 ? ? ? ? ? ? 303 SER AA N 1 186 A A +ATOM 4182 C CA . SER AA 1 186 ? -20.015 -5.751 41.425 1.0 35.49 ? ? ? ? ? ? 303 SER AA CA 1 186 A A +ATOM 4183 C C . SER AA 1 186 ? -19.615 -4.992 42.684 1.0 30.28 ? ? ? ? ? ? 303 SER AA C 1 186 A A +ATOM 4184 O O . SER AA 1 186 ? -20.069 -5.299 43.784 1.0 40.36 ? ? ? ? ? ? 303 SER AA O 1 186 A A +ATOM 4185 C CB . SER AA 1 186 ? -18.808 -6.524 40.889 1.0 41.52 ? ? ? ? ? ? 303 SER AA CB 1 186 A A +ATOM 4186 O OG . SER AA 1 186 ? -19.144 -7.244 39.716 1.0 55.45 ? ? ? ? ? ? 303 SER AA OG 1 186 A A +ATOM 4187 N N . GLN AA 1 187 ? -18.760 -3.993 42.506 1.0 2.0 ? ? ? ? ? ? 304 GLN AA N 1 187 A A +ATOM 4188 C CA . GLN AA 1 187 ? -18.279 -3.182 43.610 1.0 2.0 ? ? ? ? ? ? 304 GLN AA CA 1 187 A A +ATOM 4189 C C . GLN AA 1 187 ? -19.407 -2.634 44.469 1.0 13.01 ? ? ? ? ? ? 304 GLN AA C 1 187 A A +ATOM 4190 O O . GLN AA 1 187 ? -19.270 -2.531 45.686 1.0 21.06 ? ? ? ? ? ? 304 GLN AA O 1 187 A A +ATOM 4191 C CB . GLN AA 1 187 ? -17.445 -2.022 43.076 1.0 10.14 ? ? ? ? ? ? 304 GLN AA CB 1 187 A A +ATOM 4192 C CG . GLN AA 1 187 ? -16.715 -1.243 44.155 1.0 17.3 ? ? ? ? ? ? 304 GLN AA CG 1 187 A A +ATOM 4193 C CD . GLN AA 1 187 ? -15.667 -0.314 43.583 1.0 17.68 ? ? ? ? ? ? 304 GLN AA CD 1 187 A A +ATOM 4194 O OE1 . GLN AA 1 187 ? -15.621 -0.088 42.376 1.0 44.51 ? ? ? ? ? ? 304 GLN AA OE1 1 187 A A +ATOM 4195 N NE2 . GLN AA 1 187 ? -14.816 0.232 44.448 1.0 27.72 ? ? ? ? ? ? 304 GLN AA NE2 1 187 A A +ATOM 4196 N N . GLU AA 1 188 ? -20.513 -2.265 43.831 1.0 30.55 ? ? ? ? ? ? 305 GLU AA N 1 188 A A +ATOM 4197 C CA . GLU AA 1 188 ? -21.663 -1.728 44.552 1.0 57.3 ? ? ? ? ? ? 305 GLU AA CA 1 188 A A +ATOM 4198 C C . GLU AA 1 188 ? -22.091 -2.727 45.617 1.0 52.89 ? ? ? ? ? ? 305 GLU AA C 1 188 A A +ATOM 4199 O O . GLU AA 1 188 ? -22.246 -2.379 46.783 1.0 69.22 ? ? ? ? ? ? 305 GLU AA O 1 188 A A +ATOM 4200 C CB . GLU AA 1 188 ? -22.824 -1.465 43.588 1.0 68.9 ? ? ? ? ? ? 305 GLU AA CB 1 188 A A +ATOM 4201 C CG . GLU AA 1 188 ? -22.607 -0.289 42.646 1.0 71.26 ? ? ? ? ? ? 305 GLU AA CG 1 188 A A +ATOM 4202 C CD . GLU AA 1 188 ? -22.222 0.988 43.372 1.0 68.34 ? ? ? ? ? ? 305 GLU AA CD 1 188 A A +ATOM 4203 O OE1 . GLU AA 1 188 ? -21.250 1.649 42.946 1.0 64.13 ? ? ? ? ? ? 305 GLU AA OE1 1 188 A A +ATOM 4204 O OE2 . GLU AA 1 188 ? -22.892 1.332 44.368 1.0 41.57 ? ? ? ? ? ? 305 GLU AA OE2 1 188 A A +ATOM 4205 N N . ILE AA 1 189 ? -22.282 -3.972 45.203 1.0 22.83 ? ? ? ? ? ? 306 ILE AA N 1 189 A A +ATOM 4206 C CA . ILE AA 1 189 ? -22.676 -5.025 46.125 1.0 23.03 ? ? ? ? ? ? 306 ILE AA CA 1 189 A A +ATOM 4207 C C . ILE AA 1 189 ? -21.667 -5.120 47.268 1.0 35.89 ? ? ? ? ? ? 306 ILE AA C 1 189 A A +ATOM 4208 O O . ILE AA 1 189 ? -22.042 -5.272 48.432 1.0 35.29 ? ? ? ? ? ? 306 ILE AA O 1 189 A A +ATOM 4209 C CB . ILE AA 1 189 ? -22.739 -6.392 45.413 1.0 21.44 ? ? ? ? ? ? 306 ILE AA CB 1 189 A A +ATOM 4210 C CG1 . ILE AA 1 189 ? -23.383 -6.234 44.035 1.0 21.06 ? ? ? ? ? ? 306 ILE AA CG1 1 189 A A +ATOM 4211 C CG2 . ILE AA 1 189 ? -23.516 -7.380 46.258 1.0 25.83 ? ? ? ? ? ? 306 ILE AA CG2 1 189 A A +ATOM 4212 C CD1 . ILE AA 1 189 ? -23.411 -7.507 43.218 1.0 23.91 ? ? ? ? ? ? 306 ILE AA CD1 1 189 A A +ATOM 4213 N N . GLY AA 1 190 ? -20.383 -5.033 46.925 1.0 44.29 ? ? ? ? ? ? 307 GLY AA N 1 190 A A +ATOM 4214 C CA . GLY AA 1 190 ? -19.340 -5.103 47.933 1.0 47.84 ? ? ? ? ? ? 307 GLY AA CA 1 190 A A +ATOM 4215 C C . GLY AA 1 190 ? -19.491 -3.992 48.954 1.0 42.72 ? ? ? ? ? ? 307 GLY AA C 1 190 A A +ATOM 4216 O O . GLY AA 1 190 ? -19.447 -4.229 50.160 1.0 52.99 ? ? ? ? ? ? 307 GLY AA O 1 190 A A +ATOM 4217 N N . LEU AA 1 191 ? -19.689 -2.776 48.461 1.0 26.68 ? ? ? ? ? ? 308 LEU AA N 1 191 A A +ATOM 4218 C CA . LEU AA 1 191 ? -19.853 -1.624 49.325 1.0 24.4 ? ? ? ? ? ? 308 LEU AA CA 1 191 A A +ATOM 4219 C C . LEU AA 1 191 ? -21.146 -1.755 50.121 1.0 20.6 ? ? ? ? ? ? 308 LEU AA C 1 191 A A +ATOM 4220 O O . LEU AA 1 191 ? -21.255 -1.244 51.232 1.0 32.31 ? ? ? ? ? ? 308 LEU AA O 1 191 A A +ATOM 4221 C CB . LEU AA 1 191 ? -19.860 -0.358 48.475 1.0 18.68 ? ? ? ? ? ? 308 LEU AA CB 1 191 A A +ATOM 4222 C CG . LEU AA 1 191 ? -18.511 -0.110 47.804 1.0 22.99 ? ? ? ? ? ? 308 LEU AA CG 1 191 A A +ATOM 4223 C CD1 . LEU AA 1 191 ? -18.709 0.370 46.386 1.0 29.02 ? ? ? ? ? ? 308 LEU AA CD1 1 191 A A +ATOM 4224 C CD2 . LEU AA 1 191 ? -17.738 0.907 48.623 1.0 42.41 ? ? ? ? ? ? 308 LEU AA CD2 1 191 A A +ATOM 4225 N N . ALA AA 1 192 ? -22.119 -2.453 49.543 1.0 20.27 ? ? ? ? ? ? 309 ALA AA N 1 192 A A +ATOM 4226 C CA . ALA AA 1 192 ? -23.409 -2.663 50.193 1.0 32.97 ? ? ? ? ? ? 309 ALA AA CA 1 192 A A +ATOM 4227 C C . ALA AA 1 192 ? -23.247 -3.601 51.381 1.0 38.35 ? ? ? ? ? ? 309 ALA AA C 1 192 A A +ATOM 4228 O O . ALA AA 1 192 ? -23.618 -3.274 52.509 1.0 61.64 ? ? ? ? ? ? 309 ALA AA O 1 192 A A +ATOM 4229 C CB . ALA AA 1 192 ? -24.401 -3.254 49.202 1.0 44.37 ? ? ? ? ? ? 309 ALA AA CB 1 192 A A +ATOM 4230 N N . SER AA 1 193 ? -22.674 -4.767 51.111 1.0 45.34 ? ? ? ? ? ? 310 SER AA N 1 193 A A +ATOM 4231 C CA . SER AA 1 193 ? -22.455 -5.788 52.127 1.0 43.85 ? ? ? ? ? ? 310 SER AA CA 1 193 A A +ATOM 4232 C C . SER AA 1 193 ? -21.595 -5.343 53.308 1.0 44.66 ? ? ? ? ? ? 310 SER AA C 1 193 A A +ATOM 4233 O O . SER AA 1 193 ? -21.638 -5.957 54.370 1.0 43.51 ? ? ? ? ? ? 310 SER AA O 1 193 A A +ATOM 4234 C CB . SER AA 1 193 ? -21.818 -7.022 51.483 1.0 20.23 ? ? ? ? ? ? 310 SER AA CB 1 193 A A +ATOM 4235 O OG . SER AA 1 193 ? -20.523 -6.722 50.991 1.0 31.77 ? ? ? ? ? ? 310 SER AA OG 1 193 A A +ATOM 4236 N N . LEU AA 1 194 ? -20.818 -4.278 53.131 1.0 35.5 ? ? ? ? ? ? 311 LEU AA N 1 194 A A +ATOM 4237 C CA . LEU AA 1 194 ? -19.945 -3.809 54.206 1.0 34.72 ? ? ? ? ? ? 311 LEU AA CA 1 194 A A +ATOM 4238 C C . LEU AA 1 194 ? -20.703 -3.445 55.483 1.0 29.11 ? ? ? ? ? ? 311 LEU AA C 1 194 A A +ATOM 4239 O O . LEU AA 1 194 ? -21.332 -2.387 55.570 1.0 33.8 ? ? ? ? ? ? 311 LEU AA O 1 194 A A +ATOM 4240 C CB . LEU AA 1 194 ? -19.110 -2.611 53.731 1.0 34.25 ? ? ? ? ? ? 311 LEU AA CB 1 194 A A +ATOM 4241 C CG . LEU AA 1 194 ? -18.056 -2.903 52.656 1.0 28.71 ? ? ? ? ? ? 311 LEU AA CG 1 194 A A +ATOM 4242 C CD1 . LEU AA 1 194 ? -17.329 -1.626 52.280 1.0 38.96 ? ? ? ? ? ? 311 LEU AA CD1 1 194 A A +ATOM 4243 C CD2 . LEU AA 1 194 ? -17.075 -3.933 53.172 1.0 34.55 ? ? ? ? ? ? 311 LEU AA CD2 1 194 A A +ATOM 4244 N N . GLY AA 1 195 ? -20.639 -4.336 56.471 1.0 27.51 ? ? ? ? ? ? 312 GLY AA N 1 195 A A +ATOM 4245 C CA . GLY AA 1 195 ? -21.301 -4.099 57.739 1.0 27.15 ? ? ? ? ? ? 312 GLY AA CA 1 195 A A +ATOM 4246 C C . GLY AA 1 195 ? -22.793 -4.348 57.707 1.0 33.5 ? ? ? ? ? ? 312 GLY AA C 1 195 A A +ATOM 4247 O O . GLY AA 1 195 ? -23.495 -4.024 58.659 1.0 47.74 ? ? ? ? ? ? 312 GLY AA O 1 195 A A +ATOM 4248 N N . ALA AA 1 196 ? -23.274 -4.927 56.614 1.0 35.93 ? ? ? ? ? ? 313 ALA AA N 1 196 A A +ATOM 4249 C CA . ALA AA 1 196 ? -24.699 -5.210 56.466 1.0 42.84 ? ? ? ? ? ? 313 ALA AA CA 1 196 A A +ATOM 4250 C C . ALA AA 1 196 ? -25.135 -6.381 57.339 1.0 49.69 ? ? ? ? ? ? 313 ALA AA C 1 196 A A +ATOM 4251 O O . ALA AA 1 196 ? -24.377 -7.330 57.544 1.0 39.03 ? ? ? ? ? ? 313 ALA AA O 1 196 A A +ATOM 4252 C CB . ALA AA 1 196 ? -25.021 -5.500 55.008 1.0 58.23 ? ? ? ? ? ? 313 ALA AA CB 1 196 A A +ATOM 4253 N N . PRO AA 1 197 ? -26.374 -6.336 57.860 1.0 50.08 ? ? ? ? ? ? 314 PRO AA N 1 197 A A +ATOM 4254 C CA . PRO AA 1 197 ? -26.853 -7.432 58.708 1.0 41.23 ? ? ? ? ? ? 314 PRO AA CA 1 197 A A +ATOM 4255 C C . PRO AA 1 197 ? -27.066 -8.714 57.906 1.0 42.9 ? ? ? ? ? ? 314 PRO AA C 1 197 A A +ATOM 4256 O O . PRO AA 1 197 ? -27.441 -8.675 56.731 1.0 37.65 ? ? ? ? ? ? 314 PRO AA O 1 197 A A +ATOM 4257 C CB . PRO AA 1 197 ? -28.147 -6.890 59.313 1.0 37.63 ? ? ? ? ? ? 314 PRO AA CB 1 197 A A +ATOM 4258 C CG . PRO AA 1 197 ? -28.613 -5.857 58.353 1.0 50.98 ? ? ? ? ? ? 314 PRO AA CG 1 197 A A +ATOM 4259 C CD . PRO AA 1 197 ? -27.392 -5.284 57.680 1.0 52.52 ? ? ? ? ? ? 314 PRO AA CD 1 197 A A +ATOM 4260 N N . ASP AA 1 198 ? -26.817 -9.842 58.561 1.0 34.49 ? ? ? ? ? ? 315 ASP AA N 1 198 A A +ATOM 4261 C CA . ASP AA 1 198 ? -26.945 -11.160 57.945 1.0 49.06 ? ? ? ? ? ? 315 ASP AA CA 1 198 A A +ATOM 4262 C C . ASP AA 1 198 ? -28.087 -11.306 56.939 1.0 51.21 ? ? ? ? ? ? 315 ASP AA C 1 198 A A +ATOM 4263 O O . ASP AA 1 198 ? -27.865 -11.707 55.798 1.0 56.95 ? ? ? ? ? ? 315 ASP AA O 1 198 A A +ATOM 4264 C CB . ASP AA 1 198 ? -27.076 -12.228 59.034 1.0 48.54 ? ? ? ? ? ? 315 ASP AA CB 1 198 A A +ATOM 4265 C CG . ASP AA 1 198 ? -25.924 -12.203 60.017 1.0 70.86 ? ? ? ? ? ? 315 ASP AA CG 1 198 A A +ATOM 4266 O OD1 . ASP AA 1 198 ? -25.951 -11.371 60.947 1.0 86.04 ? ? ? ? ? ? 315 ASP AA OD1 1 198 A A +ATOM 4267 O OD2 . ASP AA 1 198 ? -24.990 -13.012 59.858 1.0 74.96 ? ? ? ? ? ? 315 ASP AA OD2 1 198 A A +ATOM 4268 N N . GLU AA 1 199 ? -29.305 -10.989 57.361 1.0 57.76 ? ? ? ? ? ? 316 GLU AA N 1 199 A A +ATOM 4269 C CA . GLU AA 1 199 ? -30.464 -11.111 56.480 1.0 63.9 ? ? ? ? ? ? 316 GLU AA CA 1 199 A A +ATOM 4270 C C . GLU AA 1 199 ? -30.218 -10.493 55.117 1.0 54.58 ? ? ? ? ? ? 316 GLU AA C 1 199 A A +ATOM 4271 O O . GLU AA 1 199 ? -30.556 -11.083 54.095 1.0 63.62 ? ? ? ? ? ? 316 GLU AA O 1 199 A A +ATOM 4272 C CB . GLU AA 1 199 ? -31.696 -10.449 57.099 1.0 76.14 ? ? ? ? ? ? 316 GLU AA CB 1 199 A A +ATOM 4273 C CG . GLU AA 1 199 ? -31.456 -9.037 57.569 1.0 99.2 ? ? ? ? ? ? 316 GLU AA CG 1 199 A A +ATOM 4274 C CD . GLU AA 1 199 ? -31.113 -8.977 59.041 1.0 100.0 ? ? ? ? ? ? 316 GLU AA CD 1 199 A A +ATOM 4275 O OE1 . GLU AA 1 199 ? -31.367 -7.927 59.665 1.0 100.0 ? ? ? ? ? ? 316 GLU AA OE1 1 199 A A +ATOM 4276 O OE2 . GLU AA 1 199 ? -30.591 -9.982 59.574 1.0 99.33 ? ? ? ? ? ? 316 GLU AA OE2 1 199 A A +ATOM 4277 N N . TYR AA 1 200 ? -29.638 -9.299 55.106 1.0 55.07 ? ? ? ? ? ? 317 TYR AA N 1 200 A A +ATOM 4278 C CA . TYR AA 1 200 ? -29.369 -8.611 53.853 1.0 62.74 ? ? ? ? ? ? 317 TYR AA CA 1 200 A A +ATOM 4279 C C . TYR AA 1 200 ? -28.146 -9.171 53.152 1.0 63.68 ? ? ? ? ? ? 317 TYR AA C 1 200 A A +ATOM 4280 O O . TYR AA 1 200 ? -28.053 -9.140 51.925 1.0 62.23 ? ? ? ? ? ? 317 TYR AA O 1 200 A A +ATOM 4281 C CB . TYR AA 1 200 ? -29.197 -7.116 54.105 1.0 62.04 ? ? ? ? ? ? 317 TYR AA CB 1 200 A A +ATOM 4282 C CG . TYR AA 1 200 ? -30.514 -6.408 54.271 1.0 73.8 ? ? ? ? ? ? 317 TYR AA CG 1 200 A A +ATOM 4283 C CD1 . TYR AA 1 200 ? -31.078 -6.242 55.533 1.0 72.45 ? ? ? ? ? ? 317 TYR AA CD1 1 200 A A +ATOM 4284 C CD2 . TYR AA 1 200 ? -31.222 -5.947 53.163 1.0 77.85 ? ? ? ? ? ? 317 TYR AA CD2 1 200 A A +ATOM 4285 C CE1 . TYR AA 1 200 ? -32.319 -5.639 55.689 1.0 84.03 ? ? ? ? ? ? 317 TYR AA CE1 1 200 A A +ATOM 4286 C CE2 . TYR AA 1 200 ? -32.465 -5.340 53.307 1.0 92.79 ? ? ? ? ? ? 317 TYR AA CE2 1 200 A A +ATOM 4287 C CZ . TYR AA 1 200 ? -33.006 -5.187 54.572 1.0 92.66 ? ? ? ? ? ? 317 TYR AA CZ 1 200 A A +ATOM 4288 O OH . TYR AA 1 200 ? -34.234 -4.582 54.716 1.0 96.95 ? ? ? ? ? ? 317 TYR AA OH 1 200 A A +ATOM 4289 N N . ILE AA 1 201 ? -27.199 -9.669 53.937 1.0 60.35 ? ? ? ? ? ? 318 ILE AA N 1 201 A A +ATOM 4290 C CA . ILE AA 1 201 ? -25.993 -10.258 53.375 1.0 54.44 ? ? ? ? ? ? 318 ILE AA CA 1 201 A A +ATOM 4291 C C . ILE AA 1 201 ? -26.433 -11.443 52.518 1.0 58.97 ? ? ? ? ? ? 318 ILE AA C 1 201 A A +ATOM 4292 O O . ILE AA 1 201 ? -26.027 -11.592 51.363 1.0 45.23 ? ? ? ? ? ? 318 ILE AA O 1 201 A A +ATOM 4293 C CB . ILE AA 1 201 ? -25.047 -10.762 54.491 1.0 35.8 ? ? ? ? ? ? 318 ILE AA CB 1 201 A A +ATOM 4294 C CG1 . ILE AA 1 201 ? -24.291 -9.585 55.111 1.0 44.13 ? ? ? ? ? ? 318 ILE AA CG1 1 201 A A +ATOM 4295 C CG2 . ILE AA 1 201 ? -24.066 -11.780 53.931 1.0 50.68 ? ? ? ? ? ? 318 ILE AA CG2 1 201 A A +ATOM 4296 C CD1 . ILE AA 1 201 ? -23.281 -8.932 54.186 1.0 43.38 ? ? ? ? ? ? 318 ILE AA CD1 1 201 A A +ATOM 4297 N N . GLU AA 1 202 ? -27.278 -12.283 53.107 1.0 63.96 ? ? ? ? ? ? 319 GLU AA N 1 202 A A +ATOM 4298 C CA . GLU AA 1 202 ? -27.801 -13.461 52.433 1.0 69.66 ? ? ? ? ? ? 319 GLU AA CA 1 202 A A +ATOM 4299 C C . GLU AA 1 202 ? -28.626 -13.052 51.215 1.0 71.97 ? ? ? ? ? ? 319 GLU AA C 1 202 A A +ATOM 4300 O O . GLU AA 1 202 ? -28.586 -13.710 50.175 1.0 78.92 ? ? ? ? ? ? 319 GLU AA O 1 202 A A +ATOM 4301 C CB . GLU AA 1 202 ? -28.659 -14.271 53.408 1.0 70.55 ? ? ? ? ? ? 319 GLU AA CB 1 202 A A +ATOM 4302 C CG . GLU AA 1 202 ? -29.194 -15.569 52.838 1.0 87.11 ? ? ? ? ? ? 319 GLU AA CG 1 202 A A +ATOM 4303 C CD . GLU AA 1 202 ? -30.704 -15.654 52.928 1.0 90.13 ? ? ? ? ? ? 319 GLU AA CD 1 202 A A +ATOM 4304 O OE1 . GLU AA 1 202 ? -31.206 -16.426 53.776 1.0 88.14 ? ? ? ? ? ? 319 GLU AA OE1 1 202 A A +ATOM 4305 O OE2 . GLU AA 1 202 ? -31.387 -14.947 52.154 1.0 100.0 ? ? ? ? ? ? 319 GLU AA OE2 1 202 A A +ATOM 4306 N N . LYS AA 1 203 ? -29.377 -11.963 51.358 1.0 71.83 ? ? ? ? ? ? 320 LYS AA N 1 203 A A +ATOM 4307 C CA . LYS AA 1 203 ? -30.206 -11.441 50.278 1.0 65.51 ? ? ? ? ? ? 320 LYS AA CA 1 203 A A +ATOM 4308 C C . LYS AA 1 203 ? -29.328 -11.030 49.099 1.0 64.01 ? ? ? ? ? ? 320 LYS AA C 1 203 A A +ATOM 4309 O O . LYS AA 1 203 ? -29.642 -11.329 47.948 1.0 72.7 ? ? ? ? ? ? 320 LYS AA O 1 203 A A +ATOM 4310 C CB . LYS AA 1 203 ? -31.006 -10.228 50.762 1.0 77.04 ? ? ? ? ? ? 320 LYS AA CB 1 203 A A +ATOM 4311 C CG . LYS AA 1 203 ? -32.235 -10.569 51.585 1.0 87.96 ? ? ? ? ? ? 320 LYS AA CG 1 203 A A +ATOM 4312 C CD . LYS AA 1 203 ? -32.978 -9.308 51.992 1.0 84.41 ? ? ? ? ? ? 320 LYS AA CD 1 203 A A +ATOM 4313 C CE . LYS AA 1 203 ? -34.242 -9.630 52.765 1.0 80.24 ? ? ? ? ? ? 320 LYS AA CE 1 203 A A +ATOM 4314 N NZ . LYS AA 1 203 ? -34.922 -8.395 53.238 1.0 68.82 ? ? ? ? ? ? 320 LYS AA NZ 1 203 A A +ATOM 4315 N N . LEU AA 1 204 ? -28.224 -10.342 49.392 1.0 61.92 ? ? ? ? ? ? 321 LEU AA N 1 204 A A +ATOM 4316 C CA . LEU AA 1 204 ? -27.294 -9.898 48.357 1.0 41.48 ? ? ? ? ? ? 321 LEU AA CA 1 204 A A +ATOM 4317 C C . LEU AA 1 204 ? -26.686 -11.114 47.666 1.0 49.38 ? ? ? ? ? ? 321 LEU AA C 1 204 A A +ATOM 4318 O O . LEU AA 1 204 ? -26.599 -11.164 46.440 1.0 40.94 ? ? ? ? ? ? 321 LEU AA O 1 204 A A +ATOM 4319 C CB . LEU AA 1 204 ? -26.184 -9.044 48.969 1.0 28.77 ? ? ? ? ? ? 321 LEU AA CB 1 204 A A +ATOM 4320 C CG . LEU AA 1 204 ? -26.576 -7.628 49.406 1.0 53.73 ? ? ? ? ? ? 321 LEU AA CG 1 204 A A +ATOM 4321 C CD1 . LEU AA 1 204 ? -25.616 -7.144 50.484 1.0 63.28 ? ? ? ? ? ? 321 LEU AA CD1 1 204 A A +ATOM 4322 C CD2 . LEU AA 1 204 ? -26.556 -6.689 48.205 1.0 45.22 ? ? ? ? ? ? 321 LEU AA CD2 1 204 A A +ATOM 4323 N N . ALA AA 1 205 ? -26.262 -12.091 48.461 1.0 50.27 ? ? ? ? ? ? 322 ALA AA N 1 205 A A +ATOM 4324 C CA . ALA AA 1 205 ? -25.688 -13.310 47.910 1.0 55.07 ? ? ? ? ? ? 322 ALA AA CA 1 205 A A +ATOM 4325 C C . ALA AA 1 205 ? -26.677 -13.876 46.901 1.0 53.68 ? ? ? ? ? ? 322 ALA AA C 1 205 A A +ATOM 4326 O O . ALA AA 1 205 ? -26.320 -14.172 45.763 1.0 62.64 ? ? ? ? ? ? 322 ALA AA O 1 205 A A +ATOM 4327 C CB . ALA AA 1 205 ? -25.439 -14.323 49.017 1.0 71.28 ? ? ? ? ? ? 322 ALA AA CB 1 205 A A +ATOM 4328 N N . THR AA 1 206 ? -27.926 -14.011 47.329 1.0 62.35 ? ? ? ? ? ? 323 THR AA N 1 206 A A +ATOM 4329 C CA . THR AA 1 206 ? -28.979 -14.533 46.469 1.0 72.61 ? ? ? ? ? ? 323 THR AA CA 1 206 A A +ATOM 4330 C C . THR AA 1 206 ? -29.080 -13.718 45.181 1.0 70.34 ? ? ? ? ? ? 323 THR AA C 1 206 A A +ATOM 4331 O O . THR AA 1 206 ? -29.315 -14.274 44.106 1.0 85.31 ? ? ? ? ? ? 323 THR AA O 1 206 A A +ATOM 4332 C CB . THR AA 1 206 ? -30.343 -14.512 47.185 1.0 77.67 ? ? ? ? ? ? 323 THR AA CB 1 206 A A +ATOM 4333 O OG1 . THR AA 1 206 ? -30.194 -15.026 48.515 1.0 80.21 ? ? ? ? ? ? 323 THR AA OG1 1 206 A A +ATOM 4334 C CG2 . THR AA 1 206 ? -31.354 -15.361 46.429 1.0 80.45 ? ? ? ? ? ? 323 THR AA CG2 1 206 A A +ATOM 4335 N N . ILE AA 1 207 ? -28.912 -12.401 45.293 1.0 51.98 ? ? ? ? ? ? 324 ILE AA N 1 207 A A +ATOM 4336 C CA . ILE AA 1 207 ? -28.967 -11.524 44.124 1.0 58.05 ? ? ? ? ? ? 324 ILE AA CA 1 207 A A +ATOM 4337 C C . ILE AA 1 207 ? -27.740 -11.827 43.271 1.0 66.0 ? ? ? ? ? ? 324 ILE AA C 1 207 A A +ATOM 4338 O O . ILE AA 1 207 ? -27.838 -12.018 42.060 1.0 82.1 ? ? ? ? ? ? 324 ILE AA O 1 207 A A +ATOM 4339 C CB . ILE AA 1 207 ? -28.923 -10.034 44.523 1.0 63.37 ? ? ? ? ? ? 324 ILE AA CB 1 207 A A +ATOM 4340 C CG1 . ILE AA 1 207 ? -30.097 -9.697 45.443 1.0 66.11 ? ? ? ? ? ? 324 ILE AA CG1 1 207 A A +ATOM 4341 C CG2 . ILE AA 1 207 ? -28.952 -9.162 43.274 1.0 49.75 ? ? ? ? ? ? 324 ILE AA CG2 1 207 A A +ATOM 4342 C CD1 . ILE AA 1 207 ? -31.453 -9.918 44.810 1.0 76.62 ? ? ? ? ? ? 324 ILE AA CD1 1 207 A A +ATOM 4343 N N . TYR AA 1 208 ? -26.586 -11.872 43.927 1.0 63.58 ? ? ? ? ? ? 325 TYR AA N 1 208 A A +ATOM 4344 C CA . TYR AA 1 208 ? -25.311 -12.166 43.279 1.0 74.13 ? ? ? ? ? ? 325 TYR AA CA 1 208 A A +ATOM 4345 C C . TYR AA 1 208 ? -25.459 -13.414 42.411 1.0 73.28 ? ? ? ? ? ? 325 TYR AA C 1 208 A A +ATOM 4346 O O . TYR AA 1 208 ? -24.847 -13.532 41.349 1.0 57.45 ? ? ? ? ? ? 325 TYR AA O 1 208 A A +ATOM 4347 C CB . TYR AA 1 208 ? -24.245 -12.388 44.360 1.0 87.95 ? ? ? ? ? ? 325 TYR AA CB 1 208 A A +ATOM 4348 C CG . TYR AA 1 208 ? -22.869 -12.764 43.858 1.0 94.17 ? ? ? ? ? ? 325 TYR AA CG 1 208 A A +ATOM 4349 C CD1 . TYR AA 1 208 ? -22.492 -14.101 43.733 1.0 86.2 ? ? ? ? ? ? 325 TYR AA CD1 1 208 A A +ATOM 4350 C CD2 . TYR AA 1 208 ? -21.924 -11.780 43.558 1.0 92.24 ? ? ? ? ? ? 325 TYR AA CD2 1 208 A A +ATOM 4351 C CE1 . TYR AA 1 208 ? -21.205 -14.452 43.323 1.0 86.39 ? ? ? ? ? ? 325 TYR AA CE1 1 208 A A +ATOM 4352 C CE2 . TYR AA 1 208 ? -20.635 -12.119 43.148 1.0 87.95 ? ? ? ? ? ? 325 TYR AA CE2 1 208 A A +ATOM 4353 C CZ . TYR AA 1 208 ? -20.283 -13.455 43.035 1.0 92.56 ? ? ? ? ? ? 325 TYR AA CZ 1 208 A A +ATOM 4354 O OH . TYR AA 1 208 ? -19.006 -13.789 42.645 1.0 100.0 ? ? ? ? ? ? 325 TYR AA OH 1 208 A A +ATOM 4355 N N . TRP AA 1 209 ? -26.280 -14.346 42.879 1.0 71.2 ? ? ? ? ? ? 326 TRP AA N 1 209 A A +ATOM 4356 C CA . TRP AA 1 209 ? -26.536 -15.590 42.173 1.0 76.56 ? ? ? ? ? ? 326 TRP AA CA 1 209 A A +ATOM 4357 C C . TRP AA 1 209 ? -27.299 -15.327 40.882 1.0 79.27 ? ? ? ? ? ? 326 TRP AA C 1 209 A A +ATOM 4358 O O . TRP AA 1 209 ? -26.770 -15.526 39.790 1.0 76.38 ? ? ? ? ? ? 326 TRP AA O 1 209 A A +ATOM 4359 C CB . TRP AA 1 209 ? -27.355 -16.530 43.060 1.0 79.57 ? ? ? ? ? ? 326 TRP AA CB 1 209 A A +ATOM 4360 C CG . TRP AA 1 209 ? -27.406 -17.945 42.566 1.0 95.51 ? ? ? ? ? ? 326 TRP AA CG 1 209 A A +ATOM 4361 C CD1 . TRP AA 1 209 ? -28.351 -18.499 41.747 1.0 90.06 ? ? ? ? ? ? 326 TRP AA CD1 1 209 A A +ATOM 4362 C CD2 . TRP AA 1 209 ? -26.498 -19.003 42.898 1.0 97.95 ? ? ? ? ? ? 326 TRP AA CD2 1 209 A A +ATOM 4363 N NE1 . TRP AA 1 209 ? -28.087 -19.832 41.551 1.0 85.64 ? ? ? ? ? ? 326 TRP AA NE1 1 209 A A +ATOM 4364 C CE2 . TRP AA 1 209 ? -26.955 -20.166 42.245 1.0 95.89 ? ? ? ? ? ? 326 TRP AA CE2 1 209 A A +ATOM 4365 C CE3 . TRP AA 1 209 ? -25.337 -19.074 43.683 1.0 100.0 ? ? ? ? ? ? 326 TRP AA CE3 1 209 A A +ATOM 4366 C CZ2 . TRP AA 1 209 ? -26.294 -21.396 42.354 1.0 99.19 ? ? ? ? ? ? 326 TRP AA CZ2 1 209 A A +ATOM 4367 C CZ3 . TRP AA 1 209 ? -24.678 -20.298 43.791 1.0 100.0 ? ? ? ? ? ? 326 TRP AA CZ3 1 209 A A +ATOM 4368 C CH2 . TRP AA 1 209 ? -25.163 -21.444 43.131 1.0 100.0 ? ? ? ? ? ? 326 TRP AA CH2 1 209 A A +ATOM 4369 N N . PHE AA 1 210 ? -28.544 -14.878 41.015 1.0 85.13 ? ? ? ? ? ? 327 PHE AA N 1 210 A A +ATOM 4370 C CA . PHE AA 1 210 ? -29.401 -14.600 39.864 1.0 88.36 ? ? ? ? ? ? 327 PHE AA CA 1 210 A A +ATOM 4371 C C . PHE AA 1 210 ? -28.902 -13.449 38.994 1.0 85.94 ? ? ? ? ? ? 327 PHE AA C 1 210 A A +ATOM 4372 O O . PHE AA 1 210 ? -29.656 -12.892 38.195 1.0 91.3 ? ? ? ? ? ? 327 PHE AA O 1 210 A A +ATOM 4373 C CB . PHE AA 1 210 ? -30.827 -14.291 40.337 1.0 95.87 ? ? ? ? ? ? 327 PHE AA CB 1 210 A A +ATOM 4374 C CG . PHE AA 1 210 ? -31.534 -15.471 40.943 1.0 100.0 ? ? ? ? ? ? 327 PHE AA CG 1 210 A A +ATOM 4375 C CD1 . PHE AA 1 210 ? -31.922 -16.551 40.153 1.0 95.08 ? ? ? ? ? ? 327 PHE AA CD1 1 210 A A +ATOM 4376 C CD2 . PHE AA 1 210 ? -31.818 -15.508 42.309 1.0 96.1 ? ? ? ? ? ? 327 PHE AA CD2 1 210 A A +ATOM 4377 C CE1 . PHE AA 1 210 ? -32.574 -17.647 40.711 1.0 100.0 ? ? ? ? ? ? 327 PHE AA CE1 1 210 A A +ATOM 4378 C CE2 . PHE AA 1 210 ? -32.467 -16.597 42.878 1.0 83.49 ? ? ? ? ? ? 327 PHE AA CE2 1 210 A A +ATOM 4379 C CZ . PHE AA 1 210 ? -32.845 -17.671 42.079 1.0 97.35 ? ? ? ? ? ? 327 PHE AA CZ 1 210 A A +ATOM 4380 N N . THR AA 1 211 ? -27.631 -13.095 39.161 1.0 76.73 ? ? ? ? ? ? 328 THR AA N 1 211 A A +ATOM 4381 C CA . THR AA 1 211 ? -27.025 -12.019 38.387 1.0 66.8 ? ? ? ? ? ? 328 THR AA CA 1 211 A A +ATOM 4382 C C . THR AA 1 211 ? -25.658 -12.445 37.893 1.0 62.01 ? ? ? ? ? ? 328 THR AA C 1 211 A A +ATOM 4383 O O . THR AA 1 211 ? -25.489 -12.819 36.737 1.0 53.07 ? ? ? ? ? ? 328 THR AA O 1 211 A A +ATOM 4384 C CB . THR AA 1 211 ? -26.876 -10.733 39.226 1.0 59.57 ? ? ? ? ? ? 328 THR AA CB 1 211 A A +ATOM 4385 O OG1 . THR AA 1 211 ? -26.155 -11.019 40.428 1.0 66.06 ? ? ? ? ? ? 328 THR AA OG1 1 211 A A +ATOM 4386 C CG2 . THR AA 1 211 ? -28.244 -10.168 39.578 1.0 61.12 ? ? ? ? ? ? 328 THR AA CG2 1 211 A A +ATOM 4387 N N . VAL AA 1 212 ? -24.687 -12.403 38.796 1.0 68.93 ? ? ? ? ? ? 329 VAL AA N 1 212 A A +ATOM 4388 C CA . VAL AA 1 212 ? -23.310 -12.768 38.480 1.0 72.84 ? ? ? ? ? ? 329 VAL AA CA 1 212 A A +ATOM 4389 C C . VAL AA 1 212 ? -23.133 -14.250 38.179 1.0 71.72 ? ? ? ? ? ? 329 VAL AA C 1 212 A A +ATOM 4390 O O . VAL AA 1 212 ? -22.469 -14.620 37.219 1.0 62.53 ? ? ? ? ? ? 329 VAL AA O 1 212 A A +ATOM 4391 C CB . VAL AA 1 212 ? -22.360 -12.376 39.645 1.0 74.58 ? ? ? ? ? ? 329 VAL AA CB 1 212 A A +ATOM 4392 C CG1 . VAL AA 1 212 ? -20.910 -12.709 39.282 1.0 74.82 ? ? ? ? ? ? 329 VAL AA CG1 1 212 A A +ATOM 4393 C CG2 . VAL AA 1 212 ? -22.504 -10.889 39.965 1.0 84.73 ? ? ? ? ? ? 329 VAL AA CG2 1 212 A A +ATOM 4394 N N . GLU AA 1 213 ? -23.737 -15.089 39.009 1.0 80.14 ? ? ? ? ? ? 330 GLU AA N 1 213 A A +ATOM 4395 C CA . GLU AA 1 213 ? -23.638 -16.530 38.844 1.0 92.46 ? ? ? ? ? ? 330 GLU AA CA 1 213 A A +ATOM 4396 C C . GLU AA 1 213 ? -24.535 -17.110 37.755 1.0 96.63 ? ? ? ? ? ? 330 GLU AA C 1 213 A A +ATOM 4397 O O . GLU AA 1 213 ? -24.056 -17.744 36.819 1.0 86.36 ? ? ? ? ? ? 330 GLU AA O 1 213 A A +ATOM 4398 C CB . GLU AA 1 213 ? -23.926 -17.219 40.177 1.0 92.3 ? ? ? ? ? ? 330 GLU AA CB 1 213 A A +ATOM 4399 C CG . GLU AA 1 213 ? -22.834 -17.014 41.206 1.0 97.63 ? ? ? ? ? ? 330 GLU AA CG 1 213 A A +ATOM 4400 C CD . GLU AA 1 213 ? -21.590 -17.821 40.892 1.0 99.92 ? ? ? ? ? ? 330 GLU AA CD 1 213 A A +ATOM 4401 O OE1 . GLU AA 1 213 ? -20.670 -17.848 41.740 1.0 100.0 ? ? ? ? ? ? 330 GLU AA OE1 1 213 A A +ATOM 4402 O OE2 . GLU AA 1 213 ? -21.533 -18.432 39.801 1.0 80.99 ? ? ? ? ? ? 330 GLU AA OE2 1 213 A A +ATOM 4403 N N . PHE AA 1 214 ? -25.840 -16.886 37.878 1.0 100.0 ? ? ? ? ? ? 331 PHE AA N 1 214 A A +ATOM 4404 C CA . PHE AA 1 214 ? -26.803 -17.401 36.907 1.0 100.0 ? ? ? ? ? ? 331 PHE AA CA 1 214 A A +ATOM 4405 C C . PHE AA 1 214 ? -27.758 -16.334 36.385 1.0 100.0 ? ? ? ? ? ? 331 PHE AA C 1 214 A A +ATOM 4406 O O . PHE AA 1 214 ? -28.980 -16.469 36.488 1.0 100.0 ? ? ? ? ? ? 331 PHE AA O 1 214 A A +ATOM 4407 C CB . PHE AA 1 214 ? -27.611 -18.543 37.527 1.0 100.0 ? ? ? ? ? ? 331 PHE AA CB 1 214 A A +ATOM 4408 C CG . PHE AA 1 214 ? -26.795 -19.763 37.829 1.0 100.0 ? ? ? ? ? ? 331 PHE AA CG 1 214 A A +ATOM 4409 C CD1 . PHE AA 1 214 ? -26.032 -19.837 38.991 1.0 99.45 ? ? ? ? ? ? 331 PHE AA CD1 1 214 A A +ATOM 4410 C CD2 . PHE AA 1 214 ? -26.777 -20.838 36.946 1.0 100.0 ? ? ? ? ? ? 331 PHE AA CD2 1 214 A A +ATOM 4411 C CE1 . PHE AA 1 214 ? -25.263 -20.964 39.268 1.0 100.0 ? ? ? ? ? ? 331 PHE AA CE1 1 214 A A +ATOM 4412 C CE2 . PHE AA 1 214 ? -26.011 -21.971 37.214 1.0 100.0 ? ? ? ? ? ? 331 PHE AA CE2 1 214 A A +ATOM 4413 C CZ . PHE AA 1 214 ? -25.253 -22.032 38.378 1.0 100.0 ? ? ? ? ? ? 331 PHE AA CZ 1 214 A A +ATOM 4414 N N . GLY AA 1 215 ? -27.200 -15.270 35.825 1.0 89.37 ? ? ? ? ? ? 332 GLY AA N 1 215 A A +ATOM 4415 C CA . GLY AA 1 215 ? -28.034 -14.205 35.307 1.0 80.87 ? ? ? ? ? ? 332 GLY AA CA 1 215 A A +ATOM 4416 C C . GLY AA 1 215 ? -28.054 -14.189 33.795 1.0 82.14 ? ? ? ? ? ? 332 GLY AA C 1 215 A A +ATOM 4417 O O . GLY AA 1 215 ? -27.147 -14.718 33.150 1.0 75.18 ? ? ? ? ? ? 332 GLY AA O 1 215 A A +ATOM 4418 N N . LEU AA 1 216 ? -29.098 -13.584 33.234 1.0 90.21 ? ? ? ? ? ? 333 LEU AA N 1 216 A A +ATOM 4419 C CA . LEU AA 1 216 ? -29.250 -13.466 31.788 1.0 96.85 ? ? ? ? ? ? 333 LEU AA CA 1 216 A A +ATOM 4420 C C . LEU AA 1 216 ? -29.463 -11.994 31.456 1.0 99.83 ? ? ? ? ? ? 333 LEU AA C 1 216 A A +ATOM 4421 O O . LEU AA 1 216 ? -30.261 -11.316 32.102 1.0 96.81 ? ? ? ? ? ? 333 LEU AA O 1 216 A A +ATOM 4422 C CB . LEU AA 1 216 ? -30.446 -14.288 31.307 1.0 99.98 ? ? ? ? ? ? 333 LEU AA CB 1 216 A A +ATOM 4423 C CG . LEU AA 1 216 ? -30.281 -15.807 31.396 1.0 100.0 ? ? ? ? ? ? 333 LEU AA CG 1 216 A A +ATOM 4424 C CD1 . LEU AA 1 216 ? -31.572 -16.480 30.966 1.0 93.61 ? ? ? ? ? ? 333 LEU AA CD1 1 216 A A +ATOM 4425 C CD2 . LEU AA 1 216 ? -29.127 -16.257 30.519 1.0 96.96 ? ? ? ? ? ? 333 LEU AA CD2 1 216 A A +ATOM 4426 N N . CYS AA 1 217 ? -28.755 -11.501 30.446 1.0 100.0 ? ? ? ? ? ? 334 CYS AA N 1 217 A A +ATOM 4427 C CA . CYS AA 1 217 ? -28.870 -10.097 30.065 1.0 96.68 ? ? ? ? ? ? 334 CYS AA CA 1 217 A A +ATOM 4428 C C . CYS AA 1 217 ? -29.694 -9.847 28.806 1.0 96.69 ? ? ? ? ? ? 334 CYS AA C 1 217 A A +ATOM 4429 O O . CYS AA 1 217 ? -30.171 -10.778 28.153 1.0 93.2 ? ? ? ? ? ? 334 CYS AA O 1 217 A A +ATOM 4430 C CB . CYS AA 1 217 ? -27.479 -9.487 29.882 1.0 89.59 ? ? ? ? ? ? 334 CYS AA CB 1 217 A A +ATOM 4431 S SG . CYS AA 1 217 ? -26.560 -10.135 28.456 1.0 98.82 ? ? ? ? ? ? 334 CYS AA SG 1 217 A A +ATOM 4432 N N . LYS AA 1 218 ? -29.839 -8.568 28.476 1.0 93.07 ? ? ? ? ? ? 335 LYS AA N 1 218 A A +ATOM 4433 C CA . LYS AA 1 218 ? -30.598 -8.137 27.311 1.0 92.31 ? ? ? ? ? ? 335 LYS AA CA 1 218 A A +ATOM 4434 C C . LYS AA 1 218 ? -29.694 -7.619 26.198 1.0 93.47 ? ? ? ? ? ? 335 LYS AA C 1 218 A A +ATOM 4435 O O . LYS AA 1 218 ? -28.940 -6.664 26.392 1.0 84.68 ? ? ? ? ? ? 335 LYS AA O 1 218 A A +ATOM 4436 C CB . LYS AA 1 218 ? -31.576 -7.039 27.717 1.0 92.51 ? ? ? ? ? ? 335 LYS AA CB 1 218 A A +ATOM 4437 C CG . LYS AA 1 218 ? -32.720 -7.531 28.572 1.0 94.2 ? ? ? ? ? ? 335 LYS AA CG 1 218 A A +ATOM 4438 C CD . LYS AA 1 218 ? -34.045 -7.320 27.865 1.0 100.0 ? ? ? ? ? ? 335 LYS AA CD 1 218 A A +ATOM 4439 C CE . LYS AA 1 218 ? -34.410 -8.522 27.007 1.0 100.0 ? ? ? ? ? ? 335 LYS AA CE 1 218 A A +ATOM 4440 N NZ . LYS AA 1 218 ? -33.519 -8.682 25.821 1.0 100.0 ? ? ? ? ? ? 335 LYS AA NZ 1 218 A A +ATOM 4441 N N . GLN AA 1 219 ? -29.784 -8.245 25.028 1.0 98.07 ? ? ? ? ? ? 336 GLN AA N 1 219 A A +ATOM 4442 C CA . GLN AA 1 219 ? -28.976 -7.842 23.881 1.0 100.0 ? ? ? ? ? ? 336 GLN AA CA 1 219 A A +ATOM 4443 C C . GLN AA 1 219 ? -29.857 -7.508 22.679 1.0 100.0 ? ? ? ? ? ? 336 GLN AA C 1 219 A A +ATOM 4444 O O . GLN AA 1 219 ? -29.826 -8.197 21.659 1.0 100.0 ? ? ? ? ? ? 336 GLN AA O 1 219 A A +ATOM 4445 C CB . GLN AA 1 219 ? -27.991 -8.956 23.514 1.0 100.0 ? ? ? ? ? ? 336 GLN AA CB 1 219 A A +ATOM 4446 C CG . GLN AA 1 219 ? -26.987 -9.274 24.614 1.0 97.01 ? ? ? ? ? ? 336 GLN AA CG 1 219 A A +ATOM 4447 C CD . GLN AA 1 219 ? -25.810 -8.316 24.630 1.0 92.6 ? ? ? ? ? ? 336 GLN AA CD 1 219 A A +ATOM 4448 O OE1 . GLN AA 1 219 ? -25.596 -7.556 23.684 1.0 92.65 ? ? ? ? ? ? 336 GLN AA OE1 1 219 A A +ATOM 4449 N NE2 . GLN AA 1 219 ? -25.035 -8.352 25.709 1.0 100.0 ? ? ? ? ? ? 336 GLN AA NE2 1 219 A A +ATOM 4450 N N . GLY AA 1 220 ? -30.634 -6.436 22.809 1.0 100.0 ? ? ? ? ? ? 337 GLY AA N 1 220 A A +ATOM 4451 C CA . GLY AA 1 220 ? -31.524 -6.021 21.741 1.0 97.11 ? ? ? ? ? ? 337 GLY AA CA 1 220 A A +ATOM 4452 C C . GLY AA 1 220 ? -32.918 -6.574 21.961 1.0 91.62 ? ? ? ? ? ? 337 GLY AA C 1 220 A A +ATOM 4453 O O . GLY AA 1 220 ? -33.750 -5.949 22.617 1.0 80.53 ? ? ? ? ? ? 337 GLY AA O 1 220 A A +ATOM 4454 N N . ASP AA 1 221 ? -33.173 -7.756 21.412 1.0 93.19 ? ? ? ? ? ? 338 ASP AA N 1 221 A A +ATOM 4455 C CA . ASP AA 1 221 ? -34.471 -8.403 21.562 1.0 97.91 ? ? ? ? ? ? 338 ASP AA CA 1 221 A A +ATOM 4456 C C . ASP AA 1 221 ? -34.237 -9.743 22.236 1.0 98.74 ? ? ? ? ? ? 338 ASP AA C 1 221 A A +ATOM 4457 O O . ASP AA 1 221 ? -34.997 -10.171 23.110 1.0 100.0 ? ? ? ? ? ? 338 ASP AA O 1 221 A A +ATOM 4458 C CB . ASP AA 1 221 ? -35.114 -8.635 20.193 1.0 100.0 ? ? ? ? ? ? 338 ASP AA CB 1 221 A A +ATOM 4459 C CG . ASP AA 1 221 ? -35.481 -7.342 19.496 1.0 100.0 ? ? ? ? ? ? 338 ASP AA CG 1 221 A A +ATOM 4460 O OD1 . ASP AA 1 221 ? -36.253 -6.554 20.083 1.0 100.0 ? ? ? ? ? ? 338 ASP AA OD1 1 221 A A +ATOM 4461 O OD2 . ASP AA 1 221 ? -35.002 -7.115 18.365 1.0 88.6 ? ? ? ? ? ? 338 ASP AA OD2 1 221 A A +ATOM 4462 N N . SER AA 1 222 ? -33.160 -10.390 21.812 1.0 100.0 ? ? ? ? ? ? 339 SER AA N 1 222 A A +ATOM 4463 C CA . SER AA 1 222 ? -32.778 -11.693 22.327 1.0 100.0 ? ? ? ? ? ? 339 SER AA CA 1 222 A A +ATOM 4464 C C . SER AA 1 222 ? -32.162 -11.624 23.718 1.0 100.0 ? ? ? ? ? ? 339 SER AA C 1 222 A A +ATOM 4465 O O . SER AA 1 222 ? -31.836 -10.546 24.221 1.0 81.59 ? ? ? ? ? ? 339 SER AA O 1 222 A A +ATOM 4466 C CB . SER AA 1 222 ? -31.791 -12.357 21.365 1.0 100.0 ? ? ? ? ? ? 339 SER AA CB 1 222 A A +ATOM 4467 O OG . SER AA 1 222 ? -30.707 -11.488 21.072 1.0 100.0 ? ? ? ? ? ? 339 SER AA OG 1 222 A A +ATOM 4468 N N . ILE AA 1 223 ? -32.004 -12.797 24.323 1.0 100.0 ? ? ? ? ? ? 340 ILE AA N 1 223 A A +ATOM 4469 C CA . ILE AA 1 223 ? -31.424 -12.921 25.650 1.0 100.0 ? ? ? ? ? ? 340 ILE AA CA 1 223 A A +ATOM 4470 C C . ILE AA 1 223 ? -30.138 -13.739 25.590 1.0 100.0 ? ? ? ? ? ? 340 ILE AA C 1 223 A A +ATOM 4471 O O . ILE AA 1 223 ? -30.078 -14.783 24.932 1.0 100.0 ? ? ? ? ? ? 340 ILE AA O 1 223 A A +ATOM 4472 C CB . ILE AA 1 223 ? -32.413 -13.603 26.630 1.0 89.23 ? ? ? ? ? ? 340 ILE AA CB 1 223 A A +ATOM 4473 C CG1 . ILE AA 1 223 ? -33.122 -12.534 27.461 1.0 72.49 ? ? ? ? ? ? 340 ILE AA CG1 1 223 A A +ATOM 4474 C CG2 . ILE AA 1 223 ? -31.680 -14.587 27.537 1.0 94.22 ? ? ? ? ? ? 340 ILE AA CG2 1 223 A A +ATOM 4475 C CD1 . ILE AA 1 223 ? -34.150 -11.748 26.684 1.0 58.91 ? ? ? ? ? ? 340 ILE AA CD1 1 223 A A +ATOM 4476 N N . LYS AA 1 224 ? -29.117 -13.256 26.287 1.0 98.6 ? ? ? ? ? ? 341 LYS AA N 1 224 A A +ATOM 4477 C CA . LYS AA 1 224 ? -27.831 -13.934 26.337 1.0 96.02 ? ? ? ? ? ? 341 LYS AA CA 1 224 A A +ATOM 4478 C C . LYS AA 1 224 ? -27.495 -14.322 27.774 1.0 99.82 ? ? ? ? ? ? 341 LYS AA C 1 224 A A +ATOM 4479 O O . LYS AA 1 224 ? -28.109 -13.829 28.726 1.0 96.22 ? ? ? ? ? ? 341 LYS AA O 1 224 A A +ATOM 4480 C CB . LYS AA 1 224 ? -26.732 -13.031 25.774 1.0 85.54 ? ? ? ? ? ? 341 LYS AA CB 1 224 A A +ATOM 4481 C CG . LYS AA 1 224 ? -26.811 -12.830 24.270 1.0 80.54 ? ? ? ? ? ? 341 LYS AA CG 1 224 A A +ATOM 4482 C CD . LYS AA 1 224 ? -26.446 -14.101 23.527 1.0 85.94 ? ? ? ? ? ? 341 LYS AA CD 1 224 A A +ATOM 4483 C CE . LYS AA 1 224 ? -26.297 -13.850 22.038 1.0 80.46 ? ? ? ? ? ? 341 LYS AA CE 1 224 A A +ATOM 4484 N NZ . LYS AA 1 224 ? -27.506 -13.195 21.473 1.0 92.52 ? ? ? ? ? ? 341 LYS AA NZ 1 224 A A +ATOM 4485 N N . ALA AA 1 225 ? -26.523 -15.216 27.926 1.0 100.0 ? ? ? ? ? ? 342 ALA AA N 1 225 A A +ATOM 4486 C CA . ALA AA 1 225 ? -26.105 -15.664 29.247 1.0 97.67 ? ? ? ? ? ? 342 ALA AA CA 1 225 A A +ATOM 4487 C C . ALA AA 1 225 ? -24.839 -14.931 29.669 1.0 100.0 ? ? ? ? ? ? 342 ALA AA C 1 225 A A +ATOM 4488 O O . ALA AA 1 225 ? -23.852 -14.899 28.934 1.0 96.17 ? ? ? ? ? ? 342 ALA AA O 1 225 A A +ATOM 4489 C CB . ALA AA 1 225 ? -25.863 -17.172 29.242 1.0 87.48 ? ? ? ? ? ? 342 ALA AA CB 1 225 A A +ATOM 4490 N N . TYR AA 1 226 ? -24.876 -14.329 30.851 1.0 100.0 ? ? ? ? ? ? 343 TYR AA N 1 226 A A +ATOM 4491 C CA . TYR AA 1 226 ? -23.724 -13.602 31.373 1.0 97.03 ? ? ? ? ? ? 343 TYR AA CA 1 226 A A +ATOM 4492 C C . TYR AA 1 226 ? -23.350 -14.145 32.748 1.0 96.93 ? ? ? ? ? ? 343 TYR AA C 1 226 A A +ATOM 4493 O O . TYR AA 1 226 ? -22.360 -13.725 33.347 1.0 90.8 ? ? ? ? ? ? 343 TYR AA O 1 226 A A +ATOM 4494 C CB . TYR AA 1 226 ? -24.029 -12.100 31.452 1.0 97.91 ? ? ? ? ? ? 343 TYR AA CB 1 226 A A +ATOM 4495 C CG . TYR AA 1 226 ? -24.869 -11.684 32.639 1.0 100.0 ? ? ? ? ? ? 343 TYR AA CG 1 226 A A +ATOM 4496 C CD1 . TYR AA 1 226 ? -26.261 -11.686 32.568 1.0 100.0 ? ? ? ? ? ? 343 TYR AA CD1 1 226 A A +ATOM 4497 C CD2 . TYR AA 1 226 ? -24.271 -11.270 33.828 1.0 95.4 ? ? ? ? ? ? 343 TYR AA CD2 1 226 A A +ATOM 4498 C CE1 . TYR AA 1 226 ? -27.035 -11.289 33.655 1.0 100.0 ? ? ? ? ? ? 343 TYR AA CE1 1 226 A A +ATOM 4499 C CE2 . TYR AA 1 226 ? -25.033 -10.871 34.917 1.0 94.37 ? ? ? ? ? ? 343 TYR AA CE2 1 226 A A +ATOM 4500 C CZ . TYR AA 1 226 ? -26.413 -10.884 34.826 1.0 100.0 ? ? ? ? ? ? 343 TYR AA CZ 1 226 A A +ATOM 4501 O OH . TYR AA 1 226 ? -27.168 -10.502 35.909 1.0 100.0 ? ? ? ? ? ? 343 TYR AA OH 1 226 A A +ATOM 4502 N N . GLY AA 1 227 ? -24.155 -15.084 33.238 1.0 96.05 ? ? ? ? ? ? 344 GLY AA N 1 227 A A +ATOM 4503 C CA . GLY AA 1 227 ? -23.897 -15.687 34.531 1.0 88.25 ? ? ? ? ? ? 344 GLY AA CA 1 227 A A +ATOM 4504 C C . GLY AA 1 227 ? -22.617 -16.500 34.490 1.0 87.24 ? ? ? ? ? ? 344 GLY AA C 1 227 A A +ATOM 4505 O O . GLY AA 1 227 ? -22.358 -17.223 33.522 1.0 70.32 ? ? ? ? ? ? 344 GLY AA O 1 227 A A +ATOM 4506 N N . ALA AA 1 228 ? -21.815 -16.381 35.542 1.0 90.18 ? ? ? ? ? ? 345 ALA AA N 1 228 A A +ATOM 4507 C CA . ALA AA 1 228 ? -20.550 -17.099 35.626 1.0 83.69 ? ? ? ? ? ? 345 ALA AA CA 1 228 A A +ATOM 4508 C C . ALA AA 1 228 ? -20.779 -18.596 35.769 1.0 74.01 ? ? ? ? ? ? 345 ALA AA C 1 228 A A +ATOM 4509 O O . ALA AA 1 228 ? -20.038 -19.400 35.207 1.0 65.65 ? ? ? ? ? ? 345 ALA AA O 1 228 A A +ATOM 4510 C CB . ALA AA 1 228 ? -19.741 -16.580 36.797 1.0 88.07 ? ? ? ? ? ? 345 ALA AA CB 1 228 A A +ATOM 4511 N N . GLY AA 1 229 ? -21.806 -18.965 36.525 1.0 74.04 ? ? ? ? ? ? 346 GLY AA N 1 229 A A +ATOM 4512 C CA . GLY AA 1 229 ? -22.115 -20.368 36.712 1.0 89.94 ? ? ? ? ? ? 346 GLY AA CA 1 229 A A +ATOM 4513 C C . GLY AA 1 229 ? -22.643 -20.978 35.427 1.0 96.5 ? ? ? ? ? ? 346 GLY AA C 1 229 A A +ATOM 4514 O O . GLY AA 1 229 ? -22.506 -22.180 35.196 1.0 100.0 ? ? ? ? ? ? 346 GLY AA O 1 229 A A +ATOM 4515 N N . LEU AA 1 230 ? -23.251 -20.144 34.588 1.0 100.0 ? ? ? ? ? ? 347 LEU AA N 1 230 A A +ATOM 4516 C CA . LEU AA 1 230 ? -23.801 -20.595 33.313 1.0 97.91 ? ? ? ? ? ? 347 LEU AA CA 1 230 A A +ATOM 4517 C C . LEU AA 1 230 ? -22.701 -20.821 32.282 1.0 92.74 ? ? ? ? ? ? 347 LEU AA C 1 230 A A +ATOM 4518 O O . LEU AA 1 230 ? -22.634 -21.868 31.643 1.0 97.68 ? ? ? ? ? ? 347 LEU AA O 1 230 A A +ATOM 4519 C CB . LEU AA 1 230 ? -24.780 -19.558 32.756 1.0 97.57 ? ? ? ? ? ? 347 LEU AA CB 1 230 A A +ATOM 4520 C CG . LEU AA 1 230 ? -26.040 -19.238 33.560 1.0 98.6 ? ? ? ? ? ? 347 LEU AA CG 1 230 A A +ATOM 4521 C CD1 . LEU AA 1 230 ? -26.685 -17.979 32.996 1.0 97.3 ? ? ? ? ? ? 347 LEU AA CD1 1 230 A A +ATOM 4522 C CD2 . LEU AA 1 230 ? -27.001 -20.415 33.503 1.0 86.84 ? ? ? ? ? ? 347 LEU AA CD2 1 230 A A +ATOM 4523 N N . LEU AA 1 231 ? -21.844 -19.819 32.126 1.0 92.32 ? ? ? ? ? ? 348 LEU AA N 1 231 A A +ATOM 4524 C CA . LEU AA 1 231 ? -20.750 -19.869 31.164 1.0 90.82 ? ? ? ? ? ? 348 LEU AA CA 1 231 A A +ATOM 4525 C C . LEU AA 1 231 ? -19.737 -20.984 31.394 1.0 85.36 ? ? ? ? ? ? 348 LEU AA C 1 231 A A +ATOM 4526 O O . LEU AA 1 231 ? -19.170 -21.509 30.440 1.0 82.64 ? ? ? ? ? ? 348 LEU AA O 1 231 A A +ATOM 4527 C CB . LEU AA 1 231 ? -20.034 -18.517 31.137 1.0 100.0 ? ? ? ? ? ? 348 LEU AA CB 1 231 A A +ATOM 4528 C CG . LEU AA 1 231 ? -20.935 -17.358 30.692 1.0 100.0 ? ? ? ? ? ? 348 LEU AA CG 1 231 A A +ATOM 4529 C CD1 . LEU AA 1 231 ? -20.409 -16.047 31.250 1.0 91.11 ? ? ? ? ? ? 348 LEU AA CD1 1 231 A A +ATOM 4530 C CD2 . LEU AA 1 231 ? -21.009 -17.322 29.174 1.0 96.11 ? ? ? ? ? ? 348 LEU AA CD2 1 231 A A +ATOM 4531 N N . SER AA 1 232 ? -19.501 -21.337 32.653 1.0 91.34 ? ? ? ? ? ? 349 SER AA N 1 232 A A +ATOM 4532 C CA . SER AA 1 232 ? -18.544 -22.392 32.969 1.0 95.94 ? ? ? ? ? ? 349 SER AA CA 1 232 A A +ATOM 4533 C C . SER AA 1 232 ? -19.194 -23.772 32.940 1.0 96.35 ? ? ? ? ? ? 349 SER AA C 1 232 A A +ATOM 4534 O O . SER AA 1 232 ? -18.503 -24.791 32.931 1.0 100.0 ? ? ? ? ? ? 349 SER AA O 1 232 A A +ATOM 4535 C CB . SER AA 1 232 ? -17.924 -22.146 34.346 1.0 96.27 ? ? ? ? ? ? 349 SER AA CB 1 232 A A +ATOM 4536 O OG . SER AA 1 232 ? -18.883 -22.294 35.381 1.0 100.0 ? ? ? ? ? ? 349 SER AA OG 1 232 A A +ATOM 4537 N N . SER AA 1 233 ? -20.523 -23.800 32.922 1.0 90.64 ? ? ? ? ? ? 350 SER AA N 1 233 A A +ATOM 4538 C CA . SER AA 1 233 ? -21.261 -25.060 32.899 1.0 87.36 ? ? ? ? ? ? 350 SER AA CA 1 233 A A +ATOM 4539 C C . SER AA 1 233 ? -21.876 -25.320 31.527 1.0 92.09 ? ? ? ? ? ? 350 SER AA C 1 233 A A +ATOM 4540 O O . SER AA 1 233 ? -22.749 -24.582 31.073 1.0 91.76 ? ? ? ? ? ? 350 SER AA O 1 233 A A +ATOM 4541 C CB . SER AA 1 233 ? -22.361 -25.047 33.960 1.0 83.6 ? ? ? ? ? ? 350 SER AA CB 1 233 A A +ATOM 4542 O OG . SER AA 1 233 ? -23.403 -25.942 33.620 1.0 49.23 ? ? ? ? ? ? 350 SER AA OG 1 233 A A +ATOM 4543 N N . PHE AA 1 234 ? -21.417 -26.387 30.879 1.0 100.0 ? ? ? ? ? ? 351 PHE AA N 1 234 A A +ATOM 4544 C CA . PHE AA 1 234 ? -21.890 -26.759 29.549 1.0 100.0 ? ? ? ? ? ? 351 PHE AA CA 1 234 A A +ATOM 4545 C C . PHE AA 1 234 ? -23.372 -27.127 29.468 1.0 97.44 ? ? ? ? ? ? 351 PHE AA C 1 234 A A +ATOM 4546 O O . PHE AA 1 234 ? -24.078 -26.696 28.558 1.0 91.23 ? ? ? ? ? ? 351 PHE AA O 1 234 A A +ATOM 4547 C CB . PHE AA 1 234 ? -21.063 -27.930 29.011 1.0 95.52 ? ? ? ? ? ? 351 PHE AA CB 1 234 A A +ATOM 4548 C CG . PHE AA 1 234 ? -21.624 -28.538 27.757 1.0 100.0 ? ? ? ? ? ? 351 PHE AA CG 1 234 A A +ATOM 4549 C CD1 . PHE AA 1 234 ? -21.518 -27.872 26.542 1.0 100.0 ? ? ? ? ? ? 351 PHE AA CD1 1 234 A A +ATOM 4550 C CD2 . PHE AA 1 234 ? -22.274 -29.768 27.791 1.0 99.81 ? ? ? ? ? ? 351 PHE AA CD2 1 234 A A +ATOM 4551 C CE1 . PHE AA 1 234 ? -22.050 -28.418 25.376 1.0 100.0 ? ? ? ? ? ? 351 PHE AA CE1 1 234 A A +ATOM 4552 C CE2 . PHE AA 1 234 ? -22.811 -30.324 26.631 1.0 100.0 ? ? ? ? ? ? 351 PHE AA CE2 1 234 A A +ATOM 4553 C CZ . PHE AA 1 234 ? -22.698 -29.647 25.420 1.0 100.0 ? ? ? ? ? ? 351 PHE AA CZ 1 234 A A +ATOM 4554 N N . GLY AA 1 235 ? -23.832 -27.934 30.417 1.0 100.0 ? ? ? ? ? ? 352 GLY AA N 1 235 A A +ATOM 4555 C CA . GLY AA 1 235 ? -25.217 -28.368 30.416 1.0 93.05 ? ? ? ? ? ? 352 GLY AA CA 1 235 A A +ATOM 4556 C C . GLY AA 1 235 ? -26.257 -27.285 30.625 1.0 87.07 ? ? ? ? ? ? 352 GLY AA C 1 235 A A +ATOM 4557 O O . GLY AA 1 235 ? -27.346 -27.350 30.058 1.0 85.59 ? ? ? ? ? ? 352 GLY AA O 1 235 A A +ATOM 4558 N N . GLU AA 1 236 ? -25.932 -26.287 31.437 1.0 88.12 ? ? ? ? ? ? 353 GLU AA N 1 236 A A +ATOM 4559 C CA . GLU AA 1 236 ? -26.873 -25.208 31.710 1.0 91.87 ? ? ? ? ? ? 353 GLU AA CA 1 236 A A +ATOM 4560 C C . GLU AA 1 236 ? -26.750 -24.046 30.737 1.0 83.67 ? ? ? ? ? ? 353 GLU AA C 1 236 A A +ATOM 4561 O O . GLU AA 1 236 ? -27.642 -23.205 30.648 1.0 74.09 ? ? ? ? ? ? 353 GLU AA O 1 236 A A +ATOM 4562 C CB . GLU AA 1 236 ? -26.690 -24.693 33.134 1.0 96.37 ? ? ? ? ? ? 353 GLU AA CB 1 236 A A +ATOM 4563 C CG . GLU AA 1 236 ? -27.973 -24.199 33.771 1.0 78.33 ? ? ? ? ? ? 353 GLU AA CG 1 236 A A +ATOM 4564 C CD . GLU AA 1 236 ? -27.947 -24.315 35.278 1.0 91.93 ? ? ? ? ? ? 353 GLU AA CD 1 236 A A +ATOM 4565 O OE1 . GLU AA 1 236 ? -28.889 -23.824 35.933 1.0 95.55 ? ? ? ? ? ? 353 GLU AA OE1 1 236 A A +ATOM 4566 O OE2 . GLU AA 1 236 ? -26.982 -24.902 35.809 1.0 99.96 ? ? ? ? ? ? 353 GLU AA OE2 1 236 A A +ATOM 4567 N N . LEU AA 1 237 ? -25.635 -23.997 30.020 1.0 84.35 ? ? ? ? ? ? 354 LEU AA N 1 237 A A +ATOM 4568 C CA . LEU AA 1 237 ? -25.404 -22.935 29.053 1.0 94.8 ? ? ? ? ? ? 354 LEU AA CA 1 237 A A +ATOM 4569 C C . LEU AA 1 237 ? -26.443 -23.022 27.939 1.0 98.39 ? ? ? ? ? ? 354 LEU AA C 1 237 A A +ATOM 4570 O O . LEU AA 1 237 ? -26.949 -22.006 27.461 1.0 97.83 ? ? ? ? ? ? 354 LEU AA O 1 237 A A +ATOM 4571 C CB . LEU AA 1 237 ? -23.995 -23.058 28.468 1.0 100.0 ? ? ? ? ? ? 354 LEU AA CB 1 237 A A +ATOM 4572 C CG . LEU AA 1 237 ? -23.538 -22.004 27.455 1.0 100.0 ? ? ? ? ? ? 354 LEU AA CG 1 237 A A +ATOM 4573 C CD1 . LEU AA 1 237 ? -23.732 -20.597 28.016 1.0 100.0 ? ? ? ? ? ? 354 LEU AA CD1 1 237 A A +ATOM 4574 C CD2 . LEU AA 1 237 ? -22.078 -22.257 27.119 1.0 96.48 ? ? ? ? ? ? 354 LEU AA CD2 1 237 A A +ATOM 4575 N N . GLN AA 1 238 ? -26.759 -24.247 27.535 1.0 100.0 ? ? ? ? ? ? 355 GLN AA N 1 238 A A +ATOM 4576 C CA . GLN AA 1 238 ? -27.739 -24.473 26.483 1.0 100.0 ? ? ? ? ? ? 355 GLN AA CA 1 238 A A +ATOM 4577 C C . GLN AA 1 238 ? -29.156 -24.541 27.045 1.0 99.16 ? ? ? ? ? ? 355 GLN AA C 1 238 A A +ATOM 4578 O O . GLN AA 1 238 ? -30.128 -24.311 26.325 1.0 100.0 ? ? ? ? ? ? 355 GLN AA O 1 238 A A +ATOM 4579 C CB . GLN AA 1 238 ? -27.415 -25.771 25.747 1.0 100.0 ? ? ? ? ? ? 355 GLN AA CB 1 238 A A +ATOM 4580 C CG . GLN AA 1 238 ? -26.778 -26.840 26.626 1.0 96.38 ? ? ? ? ? ? 355 GLN AA CG 1 238 A A +ATOM 4581 C CD . GLN AA 1 238 ? -26.167 -27.964 25.814 1.0 100.0 ? ? ? ? ? ? 355 GLN AA CD 1 238 A A +ATOM 4582 O OE1 . GLN AA 1 238 ? -26.499 -29.136 25.996 1.0 97.77 ? ? ? ? ? ? 355 GLN AA OE1 1 238 A A +ATOM 4583 N NE2 . GLN AA 1 238 ? -25.265 -27.608 24.906 1.0 100.0 ? ? ? ? ? ? 355 GLN AA NE2 1 238 A A +ATOM 4584 N N . TYR AA 1 239 ? -29.269 -24.849 28.334 1.0 86.51 ? ? ? ? ? ? 356 TYR AA N 1 239 A A +ATOM 4585 C CA . TYR AA 1 239 ? -30.572 -24.953 28.980 1.0 81.28 ? ? ? ? ? ? 356 TYR AA CA 1 239 A A +ATOM 4586 C C . TYR AA 1 239 ? -31.217 -23.601 29.275 1.0 81.58 ? ? ? ? ? ? 356 TYR AA C 1 239 A A +ATOM 4587 O O . TYR AA 1 239 ? -32.413 -23.412 29.057 1.0 79.85 ? ? ? ? ? ? 356 TYR AA O 1 239 A A +ATOM 4588 C CB . TYR AA 1 239 ? -30.463 -25.739 30.285 1.0 92.91 ? ? ? ? ? ? 356 TYR AA CB 1 239 A A +ATOM 4589 C CG . TYR AA 1 239 ? -31.637 -25.514 31.214 1.0 100.0 ? ? ? ? ? ? 356 TYR AA CG 1 239 A A +ATOM 4590 C CD1 . TYR AA 1 239 ? -32.926 -25.883 30.834 1.0 100.0 ? ? ? ? ? ? 356 TYR AA CD1 1 239 A A +ATOM 4591 C CD2 . TYR AA 1 239 ? -31.464 -24.922 32.466 1.0 100.0 ? ? ? ? ? ? 356 TYR AA CD2 1 239 A A +ATOM 4592 C CE1 . TYR AA 1 239 ? -34.013 -25.675 31.676 1.0 99.01 ? ? ? ? ? ? 356 TYR AA CE1 1 239 A A +ATOM 4593 C CE2 . TYR AA 1 239 ? -32.547 -24.710 33.318 1.0 100.0 ? ? ? ? ? ? 356 TYR AA CE2 1 239 A A +ATOM 4594 C CZ . TYR AA 1 239 ? -33.816 -25.088 32.916 1.0 100.0 ? ? ? ? ? ? 356 TYR AA CZ 1 239 A A +ATOM 4595 O OH . TYR AA 1 239 ? -34.885 -24.893 33.762 1.0 100.0 ? ? ? ? ? ? 356 TYR AA OH 1 239 A A +ATOM 4596 N N . CYS AA 1 240 ? -30.422 -22.672 29.791 1.0 90.52 ? ? ? ? ? ? 357 CYS AA N 1 240 A A +ATOM 4597 C CA . CYS AA 1 240 ? -30.913 -21.343 30.133 1.0 97.06 ? ? ? ? ? ? 357 CYS AA CA 1 240 A A +ATOM 4598 C C . CYS AA 1 240 ? -31.330 -20.542 28.903 1.0 100.0 ? ? ? ? ? ? 357 CYS AA C 1 240 A A +ATOM 4599 O O . CYS AA 1 240 ? -32.112 -19.596 29.006 1.0 100.0 ? ? ? ? ? ? 357 CYS AA O 1 240 A A +ATOM 4600 C CB . CYS AA 1 240 ? -29.837 -20.569 30.900 1.0 100.0 ? ? ? ? ? ? 357 CYS AA CB 1 240 A A +ATOM 4601 S SG . CYS AA 1 240 ? -28.310 -20.276 29.962 1.0 100.0 ? ? ? ? ? ? 357 CYS AA SG 1 240 A A +ATOM 4602 N N . LEU AA 1 241 ? -30.812 -20.930 27.741 1.0 98.65 ? ? ? ? ? ? 358 LEU AA N 1 241 A A +ATOM 4603 C CA . LEU AA 1 241 ? -31.115 -20.235 26.494 1.0 98.17 ? ? ? ? ? ? 358 LEU AA CA 1 241 A A +ATOM 4604 C C . LEU AA 1 241 ? -32.354 -20.778 25.784 1.0 100.0 ? ? ? ? ? ? 358 LEU AA C 1 241 A A +ATOM 4605 O O . LEU AA 1 241 ? -32.851 -20.167 24.836 1.0 100.0 ? ? ? ? ? ? 358 LEU AA O 1 241 A A +ATOM 4606 C CB . LEU AA 1 241 ? -29.908 -20.316 25.556 1.0 88.93 ? ? ? ? ? ? 358 LEU AA CB 1 241 A A +ATOM 4607 C CG . LEU AA 1 241 ? -29.266 -18.989 25.129 1.0 80.52 ? ? ? ? ? ? 358 LEU AA CG 1 241 A A +ATOM 4608 C CD1 . LEU AA 1 241 ? -30.190 -18.271 24.163 1.0 71.58 ? ? ? ? ? ? 358 LEU AA CD1 1 241 A A +ATOM 4609 C CD2 . LEU AA 1 241 ? -28.979 -18.125 26.345 1.0 66.0 ? ? ? ? ? ? 358 LEU AA CD2 1 241 A A +ATOM 4610 N N . SER AA 1 242 ? -32.859 -21.915 26.252 1.0 100.0 ? ? ? ? ? ? 359 SER AA N 1 242 A A +ATOM 4611 C CA . SER AA 1 242 ? -34.038 -22.529 25.648 1.0 98.89 ? ? ? ? ? ? 359 SER AA CA 1 242 A A +ATOM 4612 C C . SER AA 1 242 ? -35.349 -21.952 26.184 1.0 100.0 ? ? ? ? ? ? 359 SER AA C 1 242 A A +ATOM 4613 O O . SER AA 1 242 ? -35.349 -21.048 27.022 1.0 100.0 ? ? ? ? ? ? 359 SER AA O 1 242 A A +ATOM 4614 C CB . SER AA 1 242 ? -34.014 -24.046 25.867 1.0 97.9 ? ? ? ? ? ? 359 SER AA CB 1 242 A A +ATOM 4615 O OG . SER AA 1 242 ? -34.030 -24.369 27.247 1.0 98.54 ? ? ? ? ? ? 359 SER AA OG 1 242 A A +ATOM 4616 N N . GLU AA 1 243 ? -36.461 -22.490 25.691 1.0 100.0 ? ? ? ? ? ? 360 GLU AA N 1 243 A A +ATOM 4617 C CA . GLU AA 1 243 ? -37.789 -22.043 26.100 1.0 100.0 ? ? ? ? ? ? 360 GLU AA CA 1 243 A A +ATOM 4618 C C . GLU AA 1 243 ? -38.429 -22.991 27.110 1.0 97.86 ? ? ? ? ? ? 360 GLU AA C 1 243 A A +ATOM 4619 O O . GLU AA 1 243 ? -39.612 -23.318 27.008 1.0 100.0 ? ? ? ? ? ? 360 GLU AA O 1 243 A A +ATOM 4620 C CB . GLU AA 1 243 ? -38.693 -21.906 24.875 1.0 100.0 ? ? ? ? ? ? 360 GLU AA CB 1 243 A A +ATOM 4621 C CG . GLU AA 1 243 ? -38.418 -20.664 24.054 1.0 98.37 ? ? ? ? ? ? 360 GLU AA CG 1 243 A A +ATOM 4622 C CD . GLU AA 1 243 ? -38.874 -20.809 22.619 1.0 100.0 ? ? ? ? ? ? 360 GLU AA CD 1 243 A A +ATOM 4623 O OE1 . GLU AA 1 243 ? -40.067 -21.105 22.409 1.0 100.0 ? ? ? ? ? ? 360 GLU AA OE1 1 243 A A +ATOM 4624 O OE2 . GLU AA 1 243 ? -38.039 -20.632 21.705 1.0 100.0 ? ? ? ? ? ? 360 GLU AA OE2 1 243 A A +ATOM 4625 N N . LYS AA 1 244 ? -37.640 -23.429 28.083 1.0 98.71 ? ? ? ? ? ? 361 LYS AA N 1 244 A A +ATOM 4626 C CA . LYS AA 1 244 ? -38.133 -24.330 29.115 1.0 98.62 ? ? ? ? ? ? 361 LYS AA CA 1 244 A A +ATOM 4627 C C . LYS AA 1 244 ? -38.291 -23.594 30.448 1.0 100.0 ? ? ? ? ? ? 361 LYS AA C 1 244 A A +ATOM 4628 O O . LYS AA 1 244 ? -39.300 -23.757 31.139 1.0 98.32 ? ? ? ? ? ? 361 LYS AA O 1 244 A A +ATOM 4629 C CB . LYS AA 1 244 ? -37.182 -25.520 29.271 1.0 94.02 ? ? ? ? ? ? 361 LYS AA CB 1 244 A A +ATOM 4630 C CG . LYS AA 1 244 ? -37.030 -26.342 27.997 1.0 91.55 ? ? ? ? ? ? 361 LYS AA CG 1 244 A A +ATOM 4631 C CD . LYS AA 1 244 ? -36.166 -27.578 28.205 1.0 95.22 ? ? ? ? ? ? 361 LYS AA CD 1 244 A A +ATOM 4632 C CE . LYS AA 1 244 ? -36.120 -28.429 26.940 1.0 85.93 ? ? ? ? ? ? 361 LYS AA CE 1 244 A A +ATOM 4633 N NZ . LYS AA 1 244 ? -35.330 -29.679 27.117 1.0 81.42 ? ? ? ? ? ? 361 LYS AA NZ 1 244 A A +ATOM 4634 N N . PRO AA 1 245 ? -37.303 -22.752 30.815 1.0 100.0 ? ? ? ? ? ? 362 PRO AA N 1 245 A A +ATOM 4635 C CA . PRO AA 1 245 ? -37.363 -22.001 32.076 1.0 100.0 ? ? ? ? ? ? 362 PRO AA CA 1 245 A A +ATOM 4636 C C . PRO AA 1 245 ? -38.302 -20.799 31.978 1.0 97.24 ? ? ? ? ? ? 362 PRO AA C 1 245 A A +ATOM 4637 O O . PRO AA 1 245 ? -38.473 -20.225 30.903 1.0 98.12 ? ? ? ? ? ? 362 PRO AA O 1 245 A A +ATOM 4638 C CB . PRO AA 1 245 ? -35.916 -21.585 32.305 1.0 100.0 ? ? ? ? ? ? 362 PRO AA CB 1 245 A A +ATOM 4639 C CG . PRO AA 1 245 ? -35.349 -21.462 30.929 1.0 100.0 ? ? ? ? ? ? 362 PRO AA CG 1 245 A A +ATOM 4640 C CD . PRO AA 1 245 ? -36.084 -22.432 30.050 1.0 100.0 ? ? ? ? ? ? 362 PRO AA CD 1 245 A A +ATOM 4641 N N . LYS AA 1 246 ? -38.910 -20.424 33.101 1.0 95.94 ? ? ? ? ? ? 363 LYS AA N 1 246 A A +ATOM 4642 C CA . LYS AA 1 246 ? -39.830 -19.290 33.122 1.0 98.3 ? ? ? ? ? ? 363 LYS AA CA 1 246 A A +ATOM 4643 C C . LYS AA 1 246 ? -39.090 -18.016 33.531 1.0 99.01 ? ? ? ? ? ? 363 LYS AA C 1 246 A A +ATOM 4644 O O . LYS AA 1 246 ? -38.894 -17.743 34.716 1.0 100.0 ? ? ? ? ? ? 363 LYS AA O 1 246 A A +ATOM 4645 C CB . LYS AA 1 246 ? -40.995 -19.566 34.083 1.0 96.33 ? ? ? ? ? ? 363 LYS AA CB 1 246 A A +ATOM 4646 C CG . LYS AA 1 246 ? -40.592 -20.097 35.454 1.0 88.38 ? ? ? ? ? ? 363 LYS AA CG 1 246 A A +ATOM 4647 C CD . LYS AA 1 246 ? -41.302 -21.408 35.782 1.0 87.54 ? ? ? ? ? ? 363 LYS AA CD 1 246 A A +ATOM 4648 C CE . LYS AA 1 246 ? -42.806 -21.317 35.528 1.0 87.32 ? ? ? ? ? ? 363 LYS AA CE 1 246 A A +ATOM 4649 N NZ . LYS AA 1 246 ? -43.515 -20.542 36.582 1.0 93.79 ? ? ? ? ? ? 363 LYS AA NZ 1 246 A A +ATOM 4650 N N . LEU AA 1 247 ? -38.680 -17.246 32.528 1.0 98.43 ? ? ? ? ? ? 364 LEU AA N 1 247 A A +ATOM 4651 C CA . LEU AA 1 247 ? -37.947 -16.002 32.736 1.0 93.8 ? ? ? ? ? ? 364 LEU AA CA 1 247 A A +ATOM 4652 C C . LEU AA 1 247 ? -38.755 -14.926 33.443 1.0 94.63 ? ? ? ? ? ? 364 LEU AA C 1 247 A A +ATOM 4653 O O . LEU AA 1 247 ? -39.981 -14.873 33.334 1.0 97.05 ? ? ? ? ? ? 364 LEU AA O 1 247 A A +ATOM 4654 C CB . LEU AA 1 247 ? -37.463 -15.445 31.393 1.0 92.04 ? ? ? ? ? ? 364 LEU AA CB 1 247 A A +ATOM 4655 C CG . LEU AA 1 247 ? -36.507 -16.288 30.543 1.0 89.85 ? ? ? ? ? ? 364 LEU AA CG 1 247 A A +ATOM 4656 C CD1 . LEU AA 1 247 ? -35.406 -16.843 31.424 1.0 95.33 ? ? ? ? ? ? 364 LEU AA CD1 1 247 A A +ATOM 4657 C CD2 . LEU AA 1 247 ? -37.268 -17.404 29.846 1.0 96.01 ? ? ? ? ? ? 364 LEU AA CD2 1 247 A A +ATOM 4658 N N . LEU AA 1 248 ? -38.044 -14.068 34.165 1.0 93.72 ? ? ? ? ? ? 365 LEU AA N 1 248 A A +ATOM 4659 C CA . LEU AA 1 248 ? -38.655 -12.962 34.892 1.0 96.16 ? ? ? ? ? ? 365 LEU AA CA 1 248 A A +ATOM 4660 C C . LEU AA 1 248 ? -37.718 -11.755 34.849 1.0 99.86 ? ? ? ? ? ? 365 LEU AA C 1 248 A A +ATOM 4661 O O . LEU AA 1 248 ? -36.530 -11.889 34.558 1.0 95.59 ? ? ? ? ? ? 365 LEU AA O 1 248 A A +ATOM 4662 C CB . LEU AA 1 248 ? -38.939 -13.366 36.340 1.0 92.91 ? ? ? ? ? ? 365 LEU AA CB 1 248 A A +ATOM 4663 C CG . LEU AA 1 248 ? -40.016 -14.440 36.528 1.0 98.37 ? ? ? ? ? ? 365 LEU AA CG 1 248 A A +ATOM 4664 C CD1 . LEU AA 1 248 ? -40.069 -14.836 37.991 1.0 100.0 ? ? ? ? ? ? 365 LEU AA CD1 1 248 A A +ATOM 4665 C CD2 . LEU AA 1 248 ? -41.371 -13.922 36.056 1.0 99.54 ? ? ? ? ? ? 365 LEU AA CD2 1 248 A A +ATOM 4666 N N . PRO AA 1 249 ? -38.242 -10.554 35.148 1.0 100.0 ? ? ? ? ? ? 366 PRO AA N 1 249 A A +ATOM 4667 C CA . PRO AA 1 249 ? -37.413 -9.347 35.123 1.0 96.24 ? ? ? ? ? ? 366 PRO AA CA 1 249 A A +ATOM 4668 C C . PRO AA 1 249 ? -36.540 -9.185 36.357 1.0 92.66 ? ? ? ? ? ? 366 PRO AA C 1 249 A A +ATOM 4669 O O . PRO AA 1 249 ? -36.937 -9.537 37.467 1.0 93.04 ? ? ? ? ? ? 366 PRO AA O 1 249 A A +ATOM 4670 C CB . PRO AA 1 249 ? -38.431 -8.223 34.988 1.0 86.09 ? ? ? ? ? ? 366 PRO AA CB 1 249 A A +ATOM 4671 C CG . PRO AA 1 249 ? -39.642 -8.750 35.689 1.0 94.58 ? ? ? ? ? ? 366 PRO AA CG 1 249 A A +ATOM 4672 C CD . PRO AA 1 249 ? -39.628 -10.255 35.553 1.0 100.0 ? ? ? ? ? ? 366 PRO AA CD 1 249 A A +ATOM 4673 N N . LEU AA 1 250 ? -35.342 -8.650 36.158 1.0 90.26 ? ? ? ? ? ? 367 LEU AA N 1 250 A A +ATOM 4674 C CA . LEU AA 1 250 ? -34.437 -8.441 37.273 1.0 100.0 ? ? ? ? ? ? 367 LEU AA CA 1 250 A A +ATOM 4675 C C . LEU AA 1 250 ? -35.041 -7.391 38.201 1.0 100.0 ? ? ? ? ? ? 367 LEU AA C 1 250 A A +ATOM 4676 O O . LEU AA 1 250 ? -34.913 -6.186 37.970 1.0 96.26 ? ? ? ? ? ? 367 LEU AA O 1 250 A A +ATOM 4677 C CB . LEU AA 1 250 ? -33.057 -7.983 36.778 1.0 96.71 ? ? ? ? ? ? 367 LEU AA CB 1 250 A A +ATOM 4678 C CG . LEU AA 1 250 ? -32.028 -7.794 37.903 1.0 90.96 ? ? ? ? ? ? 367 LEU AA CG 1 250 A A +ATOM 4679 C CD1 . LEU AA 1 250 ? -31.716 -9.141 38.552 1.0 90.36 ? ? ? ? ? ? 367 LEU AA CD1 1 250 A A +ATOM 4680 C CD2 . LEU AA 1 250 ? -30.767 -7.158 37.351 1.0 83.71 ? ? ? ? ? ? 367 LEU AA CD2 1 250 A A +ATOM 4681 N N . GLU AA 1 251 ? -35.717 -7.865 39.244 1.0 100.0 ? ? ? ? ? ? 368 GLU AA N 1 251 A A +ATOM 4682 C CA . GLU AA 1 251 ? -36.353 -6.996 40.231 1.0 100.0 ? ? ? ? ? ? 368 GLU AA CA 1 251 A A +ATOM 4683 C C . GLU AA 1 251 ? -35.835 -7.376 41.618 1.0 100.0 ? ? ? ? ? ? 368 GLU AA C 1 251 A A +ATOM 4684 O O . GLU AA 1 251 ? -36.436 -8.195 42.313 1.0 100.0 ? ? ? ? ? ? 368 GLU AA O 1 251 A A +ATOM 4685 C CB . GLU AA 1 251 ? -37.871 -7.167 40.182 1.0 100.0 ? ? ? ? ? ? 368 GLU AA CB 1 251 A A +ATOM 4686 C CG . GLU AA 1 251 ? -38.655 -5.985 40.716 1.0 100.0 ? ? ? ? ? ? 368 GLU AA CG 1 251 A A +ATOM 4687 C CD . GLU AA 1 251 ? -40.143 -6.136 40.483 1.0 99.78 ? ? ? ? ? ? 368 GLU AA CD 1 251 A A +ATOM 4688 O OE1 . GLU AA 1 251 ? -40.921 -5.975 41.449 1.0 100.0 ? ? ? ? ? ? 368 GLU AA OE1 1 251 A A +ATOM 4689 O OE2 . GLU AA 1 251 ? -40.532 -6.422 39.330 1.0 90.93 ? ? ? ? ? ? 368 GLU AA OE2 1 251 A A +ATOM 4690 N N . LEU AA 1 252 ? -34.716 -6.771 42.008 1.0 100.0 ? ? ? ? ? ? 369 LEU AA N 1 252 A A +ATOM 4691 C CA . LEU AA 1 252 ? -34.075 -7.049 43.292 1.0 95.06 ? ? ? ? ? ? 369 LEU AA CA 1 252 A A +ATOM 4692 C C . LEU AA 1 252 ? -35.008 -7.145 44.497 1.0 94.49 ? ? ? ? ? ? 369 LEU AA C 1 252 A A +ATOM 4693 O O . LEU AA 1 252 ? -34.660 -7.764 45.506 1.0 89.42 ? ? ? ? ? ? 369 LEU AA O 1 252 A A +ATOM 4694 C CB . LEU AA 1 252 ? -32.991 -6.003 43.567 1.0 72.92 ? ? ? ? ? ? 369 LEU AA CB 1 252 A A +ATOM 4695 C CG . LEU AA 1 252 ? -31.695 -6.214 42.778 1.0 70.31 ? ? ? ? ? ? 369 LEU AA CG 1 252 A A +ATOM 4696 C CD1 . LEU AA 1 252 ? -31.950 -5.961 41.303 1.0 77.73 ? ? ? ? ? ? 369 LEU AA CD1 1 252 A A +ATOM 4697 C CD2 . LEU AA 1 252 ? -30.615 -5.289 43.310 1.0 56.07 ? ? ? ? ? ? 369 LEU AA CD2 1 252 A A +ATOM 4698 N N . GLU AA 1 253 ? -36.185 -6.540 44.401 1.0 95.61 ? ? ? ? ? ? 370 GLU AA N 1 253 A A +ATOM 4699 C CA . GLU AA 1 253 ? -37.129 -6.582 45.508 1.0 95.94 ? ? ? ? ? ? 370 GLU AA CA 1 253 A A +ATOM 4700 C C . GLU AA 1 253 ? -37.616 -8.005 45.758 1.0 100.0 ? ? ? ? ? ? 370 GLU AA C 1 253 A A +ATOM 4701 O O . GLU AA 1 253 ? -37.506 -8.526 46.870 1.0 92.14 ? ? ? ? ? ? 370 GLU AA O 1 253 A A +ATOM 4702 C CB . GLU AA 1 253 ? -38.326 -5.673 45.228 1.0 94.59 ? ? ? ? ? ? 370 GLU AA CB 1 253 A A +ATOM 4703 C CG . GLU AA 1 253 ? -38.771 -4.858 46.438 1.0 99.49 ? ? ? ? ? ? 370 GLU AA CG 1 253 A A +ATOM 4704 C CD . GLU AA 1 253 ? -39.081 -5.722 47.649 1.0 100.0 ? ? ? ? ? ? 370 GLU AA CD 1 253 A A +ATOM 4705 O OE1 . GLU AA 1 253 ? -40.237 -6.177 47.778 1.0 100.0 ? ? ? ? ? ? 370 GLU AA OE1 1 253 A A +ATOM 4706 O OE2 . GLU AA 1 253 ? -38.169 -5.945 48.473 1.0 98.6 ? ? ? ? ? ? 370 GLU AA OE2 1 253 A A +ATOM 4707 N N . LYS AA 1 254 ? -38.152 -8.630 44.716 1.0 100.0 ? ? ? ? ? ? 371 LYS AA N 1 254 A A +ATOM 4708 C CA . LYS AA 1 254 ? -38.672 -9.987 44.818 1.0 100.0 ? ? ? ? ? ? 371 LYS AA CA 1 254 A A +ATOM 4709 C C . LYS AA 1 254 ? -37.653 -11.045 44.400 1.0 100.0 ? ? ? ? ? ? 371 LYS AA C 1 254 A A +ATOM 4710 O O . LYS AA 1 254 ? -37.958 -12.239 44.372 1.0 100.0 ? ? ? ? ? ? 371 LYS AA O 1 254 A A +ATOM 4711 C CB . LYS AA 1 254 ? -39.938 -10.114 43.965 1.0 100.0 ? ? ? ? ? ? 371 LYS AA CB 1 254 A A +ATOM 4712 C CG . LYS AA 1 254 ? -41.018 -9.107 44.325 1.0 89.3 ? ? ? ? ? ? 371 LYS AA CG 1 254 A A +ATOM 4713 C CD . LYS AA 1 254 ? -41.478 -9.290 45.765 1.0 90.44 ? ? ? ? ? ? 371 LYS AA CD 1 254 A A +ATOM 4714 C CE . LYS AA 1 254 ? -42.523 -8.259 46.151 1.0 86.33 ? ? ? ? ? ? 371 LYS AA CE 1 254 A A +ATOM 4715 N NZ . LYS AA 1 254 ? -42.904 -8.388 47.582 1.0 76.33 ? ? ? ? ? ? 371 LYS AA NZ 1 254 A A +ATOM 4716 N N . THR AA 1 255 ? -36.442 -10.607 44.077 1.0 91.49 ? ? ? ? ? ? 372 THR AA N 1 255 A A +ATOM 4717 C CA . THR AA 1 255 ? -35.397 -11.536 43.665 1.0 86.86 ? ? ? ? ? ? 372 THR AA CA 1 255 A A +ATOM 4718 C C . THR AA 1 255 ? -34.634 -12.064 44.872 1.0 89.34 ? ? ? ? ? ? 372 THR AA C 1 255 A A +ATOM 4719 O O . THR AA 1 255 ? -34.140 -13.192 44.859 1.0 93.02 ? ? ? ? ? ? 372 THR AA O 1 255 A A +ATOM 4720 C CB . THR AA 1 255 ? -34.383 -10.870 42.713 1.0 80.77 ? ? ? ? ? ? 372 THR AA CB 1 255 A A +ATOM 4721 O OG1 . THR AA 1 255 ? -35.061 -10.380 41.550 1.0 73.3 ? ? ? ? ? ? 372 THR AA OG1 1 255 A A +ATOM 4722 C CG2 . THR AA 1 255 ? -33.323 -11.872 42.288 1.0 81.82 ? ? ? ? ? ? 372 THR AA CG2 1 255 A A +ATOM 4723 N N . ALA AA 1 256 ? -34.541 -11.241 45.913 1.0 90.66 ? ? ? ? ? ? 373 ALA AA N 1 256 A A +ATOM 4724 C CA . ALA AA 1 256 ? -33.834 -11.613 47.134 1.0 89.88 ? ? ? ? ? ? 373 ALA AA CA 1 256 A A +ATOM 4725 C C . ALA AA 1 256 ? -34.610 -12.644 47.951 1.0 93.94 ? ? ? ? ? ? 373 ALA AA C 1 256 A A +ATOM 4726 O O . ALA AA 1 256 ? -34.024 -13.434 48.696 1.0 96.1 ? ? ? ? ? ? 373 ALA AA O 1 256 A A +ATOM 4727 C CB . ALA AA 1 256 ? -33.570 -10.371 47.979 1.0 77.92 ? ? ? ? ? ? 373 ALA AA CB 1 256 A A +ATOM 4728 N N . ILE AA 1 257 ? -35.930 -12.629 47.810 1.0 93.44 ? ? ? ? ? ? 374 ILE AA N 1 257 A A +ATOM 4729 C CA . ILE AA 1 257 ? -36.785 -13.563 48.533 1.0 95.05 ? ? ? ? ? ? 374 ILE AA CA 1 257 A A +ATOM 4730 C C . ILE AA 1 257 ? -36.701 -14.950 47.914 1.0 99.9 ? ? ? ? ? ? 374 ILE AA C 1 257 A A +ATOM 4731 O O . ILE AA 1 257 ? -36.729 -15.963 48.614 1.0 99.6 ? ? ? ? ? ? 374 ILE AA O 1 257 A A +ATOM 4732 C CB . ILE AA 1 257 ? -38.251 -13.104 48.498 1.0 95.85 ? ? ? ? ? ? 374 ILE AA CB 1 257 A A +ATOM 4733 C CG1 . ILE AA 1 257 ? -38.351 -11.661 49.000 1.0 100.0 ? ? ? ? ? ? 374 ILE AA CG1 1 257 A A +ATOM 4734 C CG2 . ILE AA 1 257 ? -39.109 -14.039 49.341 1.0 100.0 ? ? ? ? ? ? 374 ILE AA CG2 1 257 A A +ATOM 4735 C CD1 . ILE AA 1 257 ? -39.575 -10.920 48.509 1.0 100.0 ? ? ? ? ? ? 374 ILE AA CD1 1 257 A A +ATOM 4736 N N . GLN AA 1 258 ? -36.590 -14.975 46.591 1.0 97.32 ? ? ? ? ? ? 375 GLN AA N 1 258 A A +ATOM 4737 C CA . GLN AA 1 258 ? -36.505 -16.208 45.818 1.0 100.0 ? ? ? ? ? ? 375 GLN AA CA 1 258 A A +ATOM 4738 C C . GLN AA 1 258 ? -35.536 -17.260 46.361 1.0 100.0 ? ? ? ? ? ? 375 GLN AA C 1 258 A A +ATOM 4739 O O . GLN AA 1 258 ? -34.351 -16.986 46.549 1.0 100.0 ? ? ? ? ? ? 375 GLN AA O 1 258 A A +ATOM 4740 C CB . GLN AA 1 258 ? -36.118 -15.872 44.378 1.0 100.0 ? ? ? ? ? ? 375 GLN AA CB 1 258 A A +ATOM 4741 C CG . GLN AA 1 258 ? -35.659 -17.071 43.578 1.0 100.0 ? ? ? ? ? ? 375 GLN AA CG 1 258 A A +ATOM 4742 C CD . GLN AA 1 258 ? -36.808 -17.959 43.164 1.0 100.0 ? ? ? ? ? ? 375 GLN AA CD 1 258 A A +ATOM 4743 O OE1 . GLN AA 1 258 ? -37.962 -17.697 43.505 1.0 100.0 ? ? ? ? ? ? 375 GLN AA OE1 1 258 A A +ATOM 4744 N NE2 . GLN AA 1 258 ? -36.503 -19.019 42.422 1.0 100.0 ? ? ? ? ? ? 375 GLN AA NE2 1 258 A A +ATOM 4745 N N . ASN AA 1 259 ? -36.051 -18.469 46.579 1.0 100.0 ? ? ? ? ? ? 376 ASN AA N 1 259 A A +ATOM 4746 C CA . ASN AA 1 259 ? -35.256 -19.588 47.083 1.0 100.0 ? ? ? ? ? ? 376 ASN AA CA 1 259 A A +ATOM 4747 C C . ASN AA 1 259 ? -34.803 -20.467 45.913 1.0 100.0 ? ? ? ? ? ? 376 ASN AA C 1 259 A A +ATOM 4748 O O . ASN AA 1 259 ? -35.589 -20.761 45.013 1.0 97.37 ? ? ? ? ? ? 376 ASN AA O 1 259 A A +ATOM 4749 C CB . ASN AA 1 259 ? -36.088 -20.420 48.065 1.0 93.27 ? ? ? ? ? ? 376 ASN AA CB 1 259 A A +ATOM 4750 C CG . ASN AA 1 259 ? -35.242 -21.071 49.141 1.0 91.62 ? ? ? ? ? ? 376 ASN AA CG 1 259 A A +ATOM 4751 O OD1 . ASN AA 1 259 ? -35.164 -22.297 49.225 1.0 86.47 ? ? ? ? ? ? 376 ASN AA OD1 1 259 A A +ATOM 4752 N ND2 . ASN AA 1 259 ? -34.606 -20.253 49.974 1.0 95.27 ? ? ? ? ? ? 376 ASN AA ND2 1 259 A A +ATOM 4753 N N . TYR AA 1 260 ? -33.540 -20.887 45.928 1.0 100.0 ? ? ? ? ? ? 377 TYR AA N 1 260 A A +ATOM 4754 C CA . TYR AA 1 260 ? -33.002 -21.715 44.847 1.0 100.0 ? ? ? ? ? ? 377 TYR AA CA 1 260 A A +ATOM 4755 C C . TYR AA 1 260 ? -32.259 -22.972 45.308 1.0 99.33 ? ? ? ? ? ? 377 TYR AA C 1 260 A A +ATOM 4756 O O . TYR AA 1 260 ? -31.861 -23.091 46.470 1.0 100.0 ? ? ? ? ? ? 377 TYR AA O 1 260 A A +ATOM 4757 C CB . TYR AA 1 260 ? -32.068 -20.877 43.966 1.0 97.62 ? ? ? ? ? ? 377 TYR AA CB 1 260 A A +ATOM 4758 C CG . TYR AA 1 260 ? -30.853 -20.345 44.697 1.0 100.0 ? ? ? ? ? ? 377 TYR AA CG 1 260 A A +ATOM 4759 C CD1 . TYR AA 1 260 ? -29.662 -21.073 44.734 1.0 100.0 ? ? ? ? ? ? 377 TYR AA CD1 1 260 A A +ATOM 4760 C CD2 . TYR AA 1 260 ? -30.897 -19.123 45.365 1.0 97.98 ? ? ? ? ? ? 377 TYR AA CD2 1 260 A A +ATOM 4761 C CE1 . TYR AA 1 260 ? -28.544 -20.595 45.416 1.0 98.13 ? ? ? ? ? ? 377 TYR AA CE1 1 260 A A +ATOM 4762 C CE2 . TYR AA 1 260 ? -29.784 -18.635 46.050 1.0 100.0 ? ? ? ? ? ? 377 TYR AA CE2 1 260 A A +ATOM 4763 C CZ . TYR AA 1 260 ? -28.610 -19.377 46.072 1.0 100.0 ? ? ? ? ? ? 377 TYR AA CZ 1 260 A A +ATOM 4764 O OH . TYR AA 1 260 ? -27.503 -18.902 46.739 1.0 91.5 ? ? ? ? ? ? 377 TYR AA OH 1 260 A A +ATOM 4765 N N . THR AA 1 261 ? -32.074 -23.904 44.374 1.0 91.74 ? ? ? ? ? ? 378 THR AA N 1 261 A A +ATOM 4766 C CA . THR AA 1 261 ? -31.372 -25.155 44.645 1.0 95.1 ? ? ? ? ? ? 378 THR AA CA 1 261 A A +ATOM 4767 C C . THR AA 1 261 ? -29.898 -24.960 44.318 1.0 95.66 ? ? ? ? ? ? 378 THR AA C 1 261 A A +ATOM 4768 O O . THR AA 1 261 ? -29.549 -24.145 43.466 1.0 92.13 ? ? ? ? ? ? 378 THR AA O 1 261 A A +ATOM 4769 C CB . THR AA 1 261 ? -31.912 -26.317 43.777 1.0 100.0 ? ? ? ? ? ? 378 THR AA CB 1 261 A A +ATOM 4770 O OG1 . THR AA 1 261 ? -31.171 -27.511 44.060 1.0 99.09 ? ? ? ? ? ? 378 THR AA OG1 1 261 A A +ATOM 4771 C CG2 . THR AA 1 261 ? -31.775 -25.987 42.293 1.0 98.52 ? ? ? ? ? ? 378 THR AA CG2 1 261 A A +ATOM 4772 N N . VAL AA 1 262 ? -29.038 -25.720 44.982 1.0 100.0 ? ? ? ? ? ? 379 VAL AA N 1 262 A A +ATOM 4773 C CA . VAL AA 1 262 ? -27.605 -25.604 44.760 1.0 99.46 ? ? ? ? ? ? 379 VAL AA CA 1 262 A A +ATOM 4774 C C . VAL AA 1 262 ? -27.051 -26.631 43.772 1.0 100.0 ? ? ? ? ? ? 379 VAL AA C 1 262 A A +ATOM 4775 O O . VAL AA 1 262 ? -26.230 -26.298 42.916 1.0 100.0 ? ? ? ? ? ? 379 VAL AA O 1 262 A A +ATOM 4776 C CB . VAL AA 1 262 ? -26.836 -25.747 46.092 1.0 100.0 ? ? ? ? ? ? 379 VAL AA CB 1 262 A A +ATOM 4777 C CG1 . VAL AA 1 262 ? -27.184 -27.078 46.758 1.0 96.93 ? ? ? ? ? ? 379 VAL AA CG1 1 262 A A +ATOM 4778 C CG2 . VAL AA 1 262 ? -25.337 -25.650 45.838 1.0 87.09 ? ? ? ? ? ? 379 VAL AA CG2 1 262 A A +ATOM 4779 N N . THR AA 1 263 ? -27.510 -27.873 43.888 1.0 100.0 ? ? ? ? ? ? 380 THR AA N 1 263 A A +ATOM 4780 C CA . THR AA 1 263 ? -27.024 -28.954 43.036 1.0 99.35 ? ? ? ? ? ? 380 THR AA CA 1 263 A A +ATOM 4781 C C . THR AA 1 263 ? -27.618 -29.054 41.636 1.0 97.45 ? ? ? ? ? ? 380 THR AA C 1 263 A A +ATOM 4782 O O . THR AA 1 263 ? -27.068 -29.750 40.782 1.0 94.83 ? ? ? ? ? ? 380 THR AA O 1 263 A A +ATOM 4783 C CB . THR AA 1 263 ? -27.227 -30.323 43.717 1.0 100.0 ? ? ? ? ? ? 380 THR AA CB 1 263 A A +ATOM 4784 O OG1 . THR AA 1 263 ? -28.618 -30.512 44.008 1.0 100.0 ? ? ? ? ? ? 380 THR AA OG1 1 263 A A +ATOM 4785 C CG2 . THR AA 1 263 ? -26.421 -30.403 45.005 1.0 100.0 ? ? ? ? ? ? 380 THR AA CG2 1 263 A A +ATOM 4786 N N . GLU AA 1 264 ? -28.727 -28.369 41.386 1.0 96.16 ? ? ? ? ? ? 381 GLU AA N 1 264 A A +ATOM 4787 C CA . GLU AA 1 264 ? -29.335 -28.466 40.070 1.0 94.77 ? ? ? ? ? ? 381 GLU AA CA 1 264 A A +ATOM 4788 C C . GLU AA 1 264 ? -29.730 -27.161 39.392 1.0 100.0 ? ? ? ? ? ? 381 GLU AA C 1 264 A A +ATOM 4789 O O . GLU AA 1 264 ? -29.493 -26.073 39.919 1.0 100.0 ? ? ? ? ? ? 381 GLU AA O 1 264 A A +ATOM 4790 C CB . GLU AA 1 264 ? -30.536 -29.404 40.139 1.0 90.67 ? ? ? ? ? ? 381 GLU AA CB 1 264 A A +ATOM 4791 C CG . GLU AA 1 264 ? -30.144 -30.862 40.296 1.0 96.58 ? ? ? ? ? ? 381 GLU AA CG 1 264 A A +ATOM 4792 C CD . GLU AA 1 264 ? -31.343 -31.762 40.450 1.0 99.52 ? ? ? ? ? ? 381 GLU AA CD 1 264 A A +ATOM 4793 O OE1 . GLU AA 1 264 ? -31.266 -32.724 41.243 1.0 100.0 ? ? ? ? ? ? 381 GLU AA OE1 1 264 A A +ATOM 4794 O OE2 . GLU AA 1 264 ? -32.364 -31.505 39.777 1.0 100.0 ? ? ? ? ? ? 381 GLU AA OE2 1 264 A A +ATOM 4795 N N . PHE AA 1 265 ? -30.331 -27.297 38.211 1.0 100.0 ? ? ? ? ? ? 382 PHE AA N 1 265 A A +ATOM 4796 C CA . PHE AA 1 265 ? -30.763 -26.165 37.387 1.0 99.86 ? ? ? ? ? ? 382 PHE AA CA 1 265 A A +ATOM 4797 C C . PHE AA 1 265 ? -31.911 -25.353 37.981 1.0 98.85 ? ? ? ? ? ? 382 PHE AA C 1 265 A A +ATOM 4798 O O . PHE AA 1 265 ? -32.823 -25.901 38.603 1.0 93.87 ? ? ? ? ? ? 382 PHE AA O 1 265 A A +ATOM 4799 C CB . PHE AA 1 265 ? -31.174 -26.655 35.993 1.0 85.54 ? ? ? ? ? ? 382 PHE AA CB 1 265 A A +ATOM 4800 C CG . PHE AA 1 265 ? -30.058 -27.297 35.206 1.0 91.55 ? ? ? ? ? ? 382 PHE AA CG 1 265 A A +ATOM 4801 C CD1 . PHE AA 1 265 ? -28.857 -27.652 35.814 1.0 88.06 ? ? ? ? ? ? 382 PHE AA CD1 1 265 A A +ATOM 4802 C CD2 . PHE AA 1 265 ? -30.219 -27.562 33.851 1.0 96.89 ? ? ? ? ? ? 382 PHE AA CD2 1 265 A A +ATOM 4803 C CE1 . PHE AA 1 265 ? -27.837 -28.262 35.084 1.0 88.79 ? ? ? ? ? ? 382 PHE AA CE1 1 265 A A +ATOM 4804 C CE2 . PHE AA 1 265 ? -29.205 -28.171 33.112 1.0 93.24 ? ? ? ? ? ? 382 PHE AA CE2 1 265 A A +ATOM 4805 C CZ . PHE AA 1 265 ? -28.013 -28.520 33.731 1.0 87.02 ? ? ? ? ? ? 382 PHE AA CZ 1 265 A A +ATOM 4806 N N . GLN AA 1 266 ? -31.863 -24.042 37.761 1.0 100.0 ? ? ? ? ? ? 383 GLN AA N 1 266 A A +ATOM 4807 C CA . GLN AA 1 266 ? -32.883 -23.131 38.267 1.0 100.0 ? ? ? ? ? ? 383 GLN AA CA 1 266 A A +ATOM 4808 C C . GLN AA 1 266 ? -33.889 -22.752 37.180 1.0 99.33 ? ? ? ? ? ? 383 GLN AA C 1 266 A A +ATOM 4809 O O . GLN AA 1 266 ? -33.513 -22.258 36.119 1.0 97.3 ? ? ? ? ? ? 383 GLN AA O 1 266 A A +ATOM 4810 C CB . GLN AA 1 266 ? -32.225 -21.858 38.819 1.0 97.24 ? ? ? ? ? ? 383 GLN AA CB 1 266 A A +ATOM 4811 C CG . GLN AA 1 266 ? -31.361 -22.084 40.049 1.0 93.63 ? ? ? ? ? ? 383 GLN AA CG 1 266 A A +ATOM 4812 C CD . GLN AA 1 266 ? -29.997 -22.645 39.704 1.0 100.0 ? ? ? ? ? ? 383 GLN AA CD 1 266 A A +ATOM 4813 O OE1 . GLN AA 1 266 ? -29.412 -23.406 40.474 1.0 100.0 ? ? ? ? ? ? 383 GLN AA OE1 1 266 A A +ATOM 4814 N NE2 . GLN AA 1 266 ? -29.484 -22.273 38.537 1.0 80.97 ? ? ? ? ? ? 383 GLN AA NE2 1 266 A A +ATOM 4815 N N . PRO AA 1 267 ? -35.192 -22.968 37.441 1.0 100.0 ? ? ? ? ? ? 384 PRO AA N 1 267 A A +ATOM 4816 C CA . PRO AA 1 267 ? -36.218 -22.630 36.448 1.0 100.0 ? ? ? ? ? ? 384 PRO AA CA 1 267 A A +ATOM 4817 C C . PRO AA 1 267 ? -36.314 -21.121 36.277 1.0 100.0 ? ? ? ? ? ? 384 PRO AA C 1 267 A A +ATOM 4818 O O . PRO AA 1 267 ? -36.795 -20.626 35.256 1.0 100.0 ? ? ? ? ? ? 384 PRO AA O 1 267 A A +ATOM 4819 C CB . PRO AA 1 267 ? -37.499 -23.224 37.032 1.0 100.0 ? ? ? ? ? ? 384 PRO AA CB 1 267 A A +ATOM 4820 C CG . PRO AA 1 267 ? -37.247 -23.274 38.501 1.0 100.0 ? ? ? ? ? ? 384 PRO AA CG 1 267 A A +ATOM 4821 C CD . PRO AA 1 267 ? -35.775 -23.507 38.681 1.0 100.0 ? ? ? ? ? ? 384 PRO AA CD 1 267 A A +ATOM 4822 N N . LEU AA 1 268 ? -35.834 -20.401 37.286 1.0 98.23 ? ? ? ? ? ? 385 LEU AA N 1 268 A A +ATOM 4823 C CA . LEU AA 1 268 ? -35.852 -18.946 37.279 1.0 96.1 ? ? ? ? ? ? 385 LEU AA CA 1 268 A A +ATOM 4824 C C . LEU AA 1 268 ? -34.488 -18.353 36.933 1.0 100.0 ? ? ? ? ? ? 385 LEU AA C 1 268 A A +ATOM 4825 O O . LEU AA 1 268 ? -33.465 -18.739 37.504 1.0 100.0 ? ? ? ? ? ? 385 LEU AA O 1 268 A A +ATOM 4826 C CB . LEU AA 1 268 ? -36.298 -18.421 38.648 1.0 91.24 ? ? ? ? ? ? 385 LEU AA CB 1 268 A A +ATOM 4827 C CG . LEU AA 1 268 ? -37.796 -18.373 38.963 1.0 94.27 ? ? ? ? ? ? 385 LEU AA CG 1 268 A A +ATOM 4828 C CD1 . LEU AA 1 268 ? -38.024 -17.327 40.039 1.0 78.81 ? ? ? ? ? ? 385 LEU AA CD1 1 268 A A +ATOM 4829 C CD2 . LEU AA 1 268 ? -38.610 -18.030 37.719 1.0 100.0 ? ? ? ? ? ? 385 LEU AA CD2 1 268 A A +ATOM 4830 N N . TYR AA 1 269 ? -34.492 -17.421 35.982 1.0 98.42 ? ? ? ? ? ? 386 TYR AA N 1 269 A A +ATOM 4831 C CA . TYR AA 1 269 ? -33.290 -16.718 35.533 1.0 90.07 ? ? ? ? ? ? 386 TYR AA CA 1 269 A A +ATOM 4832 C C . TYR AA 1 269 ? -33.727 -15.275 35.279 1.0 89.16 ? ? ? ? ? ? 386 TYR AA C 1 269 A A +ATOM 4833 O O . TYR AA 1 269 ? -34.318 -14.978 34.241 1.0 100.0 ? ? ? ? ? ? 386 TYR AA O 1 269 A A +ATOM 4834 C CB . TYR AA 1 269 ? -32.754 -17.311 34.223 1.0 82.19 ? ? ? ? ? ? 386 TYR AA CB 1 269 A A +ATOM 4835 C CG . TYR AA 1 269 ? -32.148 -18.698 34.334 1.0 90.41 ? ? ? ? ? ? 386 TYR AA CG 1 269 A A +ATOM 4836 C CD1 . TYR AA 1 269 ? -32.638 -19.749 33.560 1.0 97.78 ? ? ? ? ? ? 386 TYR AA CD1 1 269 A A +ATOM 4837 C CD2 . TYR AA 1 269 ? -31.062 -18.952 35.178 1.0 93.82 ? ? ? ? ? ? 386 TYR AA CD2 1 269 A A +ATOM 4838 C CE1 . TYR AA 1 269 ? -32.067 -21.018 33.617 1.0 100.0 ? ? ? ? ? ? 386 TYR AA CE1 1 269 A A +ATOM 4839 C CE2 . TYR AA 1 269 ? -30.481 -20.223 35.243 1.0 96.67 ? ? ? ? ? ? 386 TYR AA CE2 1 269 A A +ATOM 4840 C CZ . TYR AA 1 269 ? -30.988 -21.249 34.458 1.0 100.0 ? ? ? ? ? ? 386 TYR AA CZ 1 269 A A +ATOM 4841 O OH . TYR AA 1 269 ? -30.412 -22.498 34.508 1.0 100.0 ? ? ? ? ? ? 386 TYR AA OH 1 269 A A +ATOM 4842 N N . TYR AA 1 270 ? -33.444 -14.387 36.226 1.0 85.74 ? ? ? ? ? ? 387 TYR AA N 1 270 A A +ATOM 4843 C CA . TYR AA 1 270 ? -33.834 -12.984 36.095 1.0 92.52 ? ? ? ? ? ? 387 TYR AA CA 1 270 A A +ATOM 4844 C C . TYR AA 1 270 ? -33.101 -12.263 34.970 1.0 100.0 ? ? ? ? ? ? 387 TYR AA C 1 270 A A +ATOM 4845 O O . TYR AA 1 270 ? -31.872 -12.182 34.963 1.0 100.0 ? ? ? ? ? ? 387 TYR AA O 1 270 A A +ATOM 4846 C CB . TYR AA 1 270 ? -33.612 -12.250 37.421 1.0 87.5 ? ? ? ? ? ? 387 TYR AA CB 1 270 A A +ATOM 4847 C CG . TYR AA 1 270 ? -34.514 -12.755 38.517 1.0 78.83 ? ? ? ? ? ? 387 TYR AA CG 1 270 A A +ATOM 4848 C CD1 . TYR AA 1 270 ? -34.262 -13.973 39.140 1.0 77.83 ? ? ? ? ? ? 387 TYR AA CD1 1 270 A A +ATOM 4849 C CD2 . TYR AA 1 270 ? -35.650 -12.042 38.898 1.0 80.82 ? ? ? ? ? ? 387 TYR AA CD2 1 270 A A +ATOM 4850 C CE1 . TYR AA 1 270 ? -35.119 -14.475 40.116 1.0 96.01 ? ? ? ? ? ? 387 TYR AA CE1 1 270 A A +ATOM 4851 C CE2 . TYR AA 1 270 ? -36.517 -12.535 39.874 1.0 89.89 ? ? ? ? ? ? 387 TYR AA CE2 1 270 A A +ATOM 4852 C CZ . TYR AA 1 270 ? -36.246 -13.755 40.478 1.0 95.76 ? ? ? ? ? ? 387 TYR AA CZ 1 270 A A +ATOM 4853 O OH . TYR AA 1 270 ? -37.096 -14.263 41.439 1.0 80.81 ? ? ? ? ? ? 387 TYR AA OH 1 270 A A +ATOM 4854 N N . VAL AA 1 271 ? -33.875 -11.732 34.026 1.0 100.0 ? ? ? ? ? ? 388 VAL AA N 1 271 A A +ATOM 4855 C CA . VAL AA 1 271 ? -33.331 -11.025 32.871 1.0 97.26 ? ? ? ? ? ? 388 VAL AA CA 1 271 A A +ATOM 4856 C C . VAL AA 1 271 ? -33.078 -9.540 33.126 1.0 96.92 ? ? ? ? ? ? 388 VAL AA C 1 271 A A +ATOM 4857 O O . VAL AA 1 271 ? -34.017 -8.749 33.221 1.0 100.0 ? ? ? ? ? ? 388 VAL AA O 1 271 A A +ATOM 4858 C CB . VAL AA 1 271 ? -34.279 -11.155 31.658 1.0 97.4 ? ? ? ? ? ? 388 VAL AA CB 1 271 A A +ATOM 4859 C CG1 . VAL AA 1 271 ? -33.659 -10.495 30.434 1.0 98.41 ? ? ? ? ? ? 388 VAL AA CG1 1 271 A A +ATOM 4860 C CG2 . VAL AA 1 271 ? -34.575 -12.622 31.391 1.0 100.0 ? ? ? ? ? ? 388 VAL AA CG2 1 271 A A +ATOM 4861 N N . ALA AA 1 272 ? -31.804 -9.170 33.231 1.0 92.96 ? ? ? ? ? ? 389 ALA AA N 1 272 A A +ATOM 4862 C CA . ALA AA 1 272 ? -31.421 -7.782 33.461 1.0 87.23 ? ? ? ? ? ? 389 ALA AA CA 1 272 A A +ATOM 4863 C C . ALA AA 1 272 ? -31.264 -7.059 32.130 1.0 88.83 ? ? ? ? ? ? 389 ALA AA C 1 272 A A +ATOM 4864 O O . ALA AA 1 272 ? -30.769 -7.627 31.154 1.0 84.56 ? ? ? ? ? ? 389 ALA AA O 1 272 A A +ATOM 4865 C CB . ALA AA 1 272 ? -30.117 -7.718 34.238 1.0 83.42 ? ? ? ? ? ? 389 ALA AA CB 1 272 A A +ATOM 4866 N N . GLU AA 1 273 ? -31.699 -5.804 32.092 1.0 91.8 ? ? ? ? ? ? 390 GLU AA N 1 273 A A +ATOM 4867 C CA . GLU AA 1 273 ? -31.588 -5.009 30.878 1.0 91.37 ? ? ? ? ? ? 390 GLU AA CA 1 273 A A +ATOM 4868 C C . GLU AA 1 273 ? -30.110 -4.862 30.546 1.0 88.96 ? ? ? ? ? ? 390 GLU AA C 1 273 A A +ATOM 4869 O O . GLU AA 1 273 ? -29.674 -5.180 29.438 1.0 97.4 ? ? ? ? ? ? 390 GLU AA O 1 273 A A +ATOM 4870 C CB . GLU AA 1 273 ? -32.210 -3.632 31.089 1.0 94.09 ? ? ? ? ? ? 390 GLU AA CB 1 273 A A +ATOM 4871 C CG . GLU AA 1 273 ? -33.697 -3.674 31.375 1.0 100.0 ? ? ? ? ? ? 390 GLU AA CG 1 273 A A +ATOM 4872 C CD . GLU AA 1 273 ? -34.314 -2.289 31.452 1.0 100.0 ? ? ? ? ? ? 390 GLU AA CD 1 273 A A +ATOM 4873 O OE1 . GLU AA 1 273 ? -33.562 -1.293 31.335 1.0 100.0 ? ? ? ? ? ? 390 GLU AA OE1 1 273 A A +ATOM 4874 O OE2 . GLU AA 1 273 ? -35.551 -2.198 31.627 1.0 100.0 ? ? ? ? ? ? 390 GLU AA OE2 1 273 A A +ATOM 4875 N N . SER AA 1 274 ? -29.347 -4.382 31.523 1.0 77.84 ? ? ? ? ? ? 391 SER AA N 1 274 A A +ATOM 4876 C CA . SER AA 1 274 ? -27.913 -4.192 31.367 1.0 69.81 ? ? ? ? ? ? 391 SER AA CA 1 274 A A +ATOM 4877 C C . SER AA 1 274 ? -27.250 -4.173 32.737 1.0 65.41 ? ? ? ? ? ? 391 SER AA C 1 274 A A +ATOM 4878 O O . SER AA 1 274 ? -27.927 -4.093 33.762 1.0 67.04 ? ? ? ? ? ? 391 SER AA O 1 274 A A +ATOM 4879 C CB . SER AA 1 274 ? -27.625 -2.877 30.636 1.0 68.26 ? ? ? ? ? ? 391 SER AA CB 1 274 A A +ATOM 4880 O OG . SER AA 1 274 ? -26.258 -2.783 30.267 1.0 78.68 ? ? ? ? ? ? 391 SER AA OG 1 274 A A +ATOM 4881 N N . PHE AA 1 275 ? -25.925 -4.261 32.748 1.0 64.72 ? ? ? ? ? ? 392 PHE AA N 1 275 A A +ATOM 4882 C CA . PHE AA 1 275 ? -25.172 -4.241 33.996 1.0 63.71 ? ? ? ? ? ? 392 PHE AA CA 1 275 A A +ATOM 4883 C C . PHE AA 1 275 ? -25.211 -2.821 34.537 1.0 65.72 ? ? ? ? ? ? 392 PHE AA C 1 275 A A +ATOM 4884 O O . PHE AA 1 275 ? -25.227 -2.602 35.747 1.0 57.64 ? ? ? ? ? ? 392 PHE AA O 1 275 A A +ATOM 4885 C CB . PHE AA 1 275 ? -23.731 -4.685 33.742 1.0 63.72 ? ? ? ? ? ? 392 PHE AA CB 1 275 A A +ATOM 4886 C CG . PHE AA 1 275 ? -23.616 -5.813 32.759 1.0 79.95 ? ? ? ? ? ? 392 PHE AA CG 1 275 A A +ATOM 4887 C CD1 . PHE AA 1 275 ? -23.008 -5.617 31.523 1.0 96.25 ? ? ? ? ? ? 392 PHE AA CD1 1 275 A A +ATOM 4888 C CD2 . PHE AA 1 275 ? -24.131 -7.070 33.061 1.0 77.52 ? ? ? ? ? ? 392 PHE AA CD2 1 275 A A +ATOM 4889 C CE1 . PHE AA 1 275 ? -22.913 -6.659 30.601 1.0 100.0 ? ? ? ? ? ? 392 PHE AA CE1 1 275 A A +ATOM 4890 C CE2 . PHE AA 1 275 ? -24.043 -8.119 32.149 1.0 83.36 ? ? ? ? ? ? 392 PHE AA CE2 1 275 A A +ATOM 4891 C CZ . PHE AA 1 275 ? -23.433 -7.913 30.915 1.0 99.74 ? ? ? ? ? ? 392 PHE AA CZ 1 275 A A +ATOM 4892 N N . ASN AA 1 276 ? -25.235 -1.862 33.619 1.0 69.65 ? ? ? ? ? ? 393 ASN AA N 1 276 A A +ATOM 4893 C CA . ASN AA 1 276 ? -25.297 -0.452 33.970 1.0 67.8 ? ? ? ? ? ? 393 ASN AA CA 1 276 A A +ATOM 4894 C C . ASN AA 1 276 ? -26.644 -0.193 34.633 1.0 64.99 ? ? ? ? ? ? 393 ASN AA C 1 276 A A +ATOM 4895 O O . ASN AA 1 276 ? -26.768 0.648 35.521 1.0 61.92 ? ? ? ? ? ? 393 ASN AA O 1 276 A A +ATOM 4896 C CB . ASN AA 1 276 ? -25.172 0.403 32.707 1.0 55.58 ? ? ? ? ? ? 393 ASN AA CB 1 276 A A +ATOM 4897 C CG . ASN AA 1 276 ? -24.793 1.833 33.009 1.0 63.01 ? ? ? ? ? ? 393 ASN AA CG 1 276 A A +ATOM 4898 O OD1 . ASN AA 1 276 ? -25.335 2.452 33.924 1.0 73.68 ? ? ? ? ? ? 393 ASN AA OD1 1 276 A A +ATOM 4899 N ND2 . ASN AA 1 276 ? -23.855 2.370 32.238 1.0 72.87 ? ? ? ? ? ? 393 ASN AA ND2 1 276 A A +ATOM 4900 N N . ASP AA 1 277 ? -27.655 -0.931 34.197 1.0 60.25 ? ? ? ? ? ? 394 ASP AA N 1 277 A A +ATOM 4901 C CA . ASP AA 1 277 ? -28.995 -0.778 34.737 1.0 65.04 ? ? ? ? ? ? 394 ASP AA CA 1 277 A A +ATOM 4902 C C . ASP AA 1 277 ? -29.105 -1.327 36.151 1.0 69.42 ? ? ? ? ? ? 394 ASP AA C 1 277 A A +ATOM 4903 O O . ASP AA 1 277 ? -29.638 -0.672 37.047 1.0 72.92 ? ? ? ? ? ? 394 ASP AA O 1 277 A A +ATOM 4904 C CB . ASP AA 1 277 ? -30.001 -1.493 33.837 1.0 79.78 ? ? ? ? ? ? 394 ASP AA CB 1 277 A A +ATOM 4905 C CG . ASP AA 1 277 ? -31.418 -1.025 34.066 1.0 91.97 ? ? ? ? ? ? 394 ASP AA CG 1 277 A A +ATOM 4906 O OD1 . ASP AA 1 277 ? -31.653 0.201 34.017 1.0 91.8 ? ? ? ? ? ? 394 ASP AA OD1 1 277 A A +ATOM 4907 O OD2 . ASP AA 1 277 ? -32.295 -1.884 34.297 1.0 92.7 ? ? ? ? ? ? 394 ASP AA OD2 1 277 A A +ATOM 4908 N N . ALA AA 1 278 ? -28.599 -2.540 36.339 1.0 75.65 ? ? ? ? ? ? 395 ALA AA N 1 278 A A +ATOM 4909 C CA . ALA AA 1 278 ? -28.650 -3.205 37.635 1.0 62.68 ? ? ? ? ? ? 395 ALA AA CA 1 278 A A +ATOM 4910 C C . ALA AA 1 278 ? -27.856 -2.485 38.720 1.0 65.12 ? ? ? ? ? ? 395 ALA AA C 1 278 A A +ATOM 4911 O O . ALA AA 1 278 ? -28.309 -2.387 39.860 1.0 66.49 ? ? ? ? ? ? 395 ALA AA O 1 278 A A +ATOM 4912 C CB . ALA AA 1 278 ? -28.161 -4.636 37.494 1.0 43.25 ? ? ? ? ? ? 395 ALA AA CB 1 278 A A +ATOM 4913 N N . LYS AA 1 279 ? -26.672 -1.993 38.365 1.0 59.26 ? ? ? ? ? ? 396 LYS AA N 1 279 A A +ATOM 4914 C CA . LYS AA 1 279 ? -25.817 -1.281 39.315 1.0 46.21 ? ? ? ? ? ? 396 LYS AA CA 1 279 A A +ATOM 4915 C C . LYS AA 1 279 ? -26.613 -0.291 40.154 1.0 40.74 ? ? ? ? ? ? 396 LYS AA C 1 279 A A +ATOM 4916 O O . LYS AA 1 279 ? -26.343 -0.119 41.342 1.0 28.37 ? ? ? ? ? ? 396 LYS AA O 1 279 A A +ATOM 4917 C CB . LYS AA 1 279 ? -24.705 -0.531 38.578 1.0 51.44 ? ? ? ? ? ? 396 LYS AA CB 1 279 A A +ATOM 4918 C CG . LYS AA 1 279 ? -24.035 0.546 39.412 1.0 22.9 ? ? ? ? ? ? 396 LYS AA CG 1 279 A A +ATOM 4919 C CD . LYS AA 1 279 ? -22.853 1.135 38.677 1.0 31.36 ? ? ? ? ? ? 396 LYS AA CD 1 279 A A +ATOM 4920 C CE . LYS AA 1 279 ? -23.264 2.347 37.876 1.0 41.1 ? ? ? ? ? ? 396 LYS AA CE 1 279 A A +ATOM 4921 N NZ . LYS AA 1 279 ? -22.089 3.147 37.436 1.0 37.34 ? ? ? ? ? ? 396 LYS AA NZ 1 279 A A +ATOM 4922 N N . GLU AA 1 280 ? -27.581 0.369 39.522 1.0 41.13 ? ? ? ? ? ? 397 GLU AA N 1 280 A A +ATOM 4923 C CA . GLU AA 1 280 ? -28.426 1.339 40.207 1.0 49.25 ? ? ? ? ? ? 397 GLU AA CA 1 280 A A +ATOM 4924 C C . GLU AA 1 280 ? -29.365 0.612 41.163 1.0 51.92 ? ? ? ? ? ? 397 GLU AA C 1 280 A A +ATOM 4925 O O . GLU AA 1 280 ? -29.560 1.040 42.302 1.0 60.13 ? ? ? ? ? ? 397 GLU AA O 1 280 A A +ATOM 4926 C CB . GLU AA 1 280 ? -29.248 2.139 39.195 1.0 60.2 ? ? ? ? ? ? 397 GLU AA CB 1 280 A A +ATOM 4927 C CG . GLU AA 1 280 ? -28.421 2.733 38.078 1.0 82.81 ? ? ? ? ? ? 397 GLU AA CG 1 280 A A +ATOM 4928 C CD . GLU AA 1 280 ? -27.445 3.772 38.578 1.0 100.0 ? ? ? ? ? ? 397 GLU AA CD 1 280 A A +ATOM 4929 O OE1 . GLU AA 1 280 ? -27.779 4.484 39.550 1.0 100.0 ? ? ? ? ? ? 397 GLU AA OE1 1 280 A A +ATOM 4930 O OE2 . GLU AA 1 280 ? -26.345 3.878 37.998 1.0 100.0 ? ? ? ? ? ? 397 GLU AA OE2 1 280 A A +ATOM 4931 N N . LYS AA 1 281 ? -29.944 -0.489 40.690 1.0 47.17 ? ? ? ? ? ? 398 LYS AA N 1 281 A A +ATOM 4932 C CA . LYS AA 1 281 ? -30.859 -1.280 41.498 1.0 52.5 ? ? ? ? ? ? 398 LYS AA CA 1 281 A A +ATOM 4933 C C . LYS AA 1 281 ? -30.167 -1.688 42.795 1.0 49.29 ? ? ? ? ? ? 398 LYS AA C 1 281 A A +ATOM 4934 O O . LYS AA 1 281 ? -30.819 -2.014 43.786 1.0 56.88 ? ? ? ? ? ? 398 LYS AA O 1 281 A A +ATOM 4935 C CB . LYS AA 1 281 ? -31.295 -2.519 40.722 1.0 67.3 ? ? ? ? ? ? 398 LYS AA CB 1 281 A A +ATOM 4936 C CG . LYS AA 1 281 ? -31.552 -2.256 39.249 1.0 65.58 ? ? ? ? ? ? 398 LYS AA CG 1 281 A A +ATOM 4937 C CD . LYS AA 1 281 ? -32.956 -1.724 39.017 1.0 76.37 ? ? ? ? ? ? 398 LYS AA CD 1 281 A A +ATOM 4938 C CE . LYS AA 1 281 ? -33.372 -1.886 37.561 1.0 68.23 ? ? ? ? ? ? 398 LYS AA CE 1 281 A A +ATOM 4939 N NZ . LYS AA 1 281 ? -33.599 -3.315 37.213 1.0 72.84 ? ? ? ? ? ? 398 LYS AA NZ 1 281 A A +ATOM 4940 N N . VAL AA 1 282 ? -28.838 -1.653 42.777 1.0 44.34 ? ? ? ? ? ? 399 VAL AA N 1 282 A A +ATOM 4941 C CA . VAL AA 1 282 ? -28.033 -2.013 43.938 1.0 47.58 ? ? ? ? ? ? 399 VAL AA CA 1 282 A A +ATOM 4942 C C . VAL AA 1 282 ? -27.669 -0.779 44.764 1.0 47.85 ? ? ? ? ? ? 399 VAL AA C 1 282 A A +ATOM 4943 O O . VAL AA 1 282 ? -27.658 -0.823 45.996 1.0 49.4 ? ? ? ? ? ? 399 VAL AA O 1 282 A A +ATOM 4944 C CB . VAL AA 1 282 ? -26.736 -2.733 43.502 1.0 41.31 ? ? ? ? ? ? 399 VAL AA CB 1 282 A A +ATOM 4945 C CG1 . VAL AA 1 282 ? -26.340 -3.766 44.542 1.0 42.53 ? ? ? ? ? ? 399 VAL AA CG1 1 282 A A +ATOM 4946 C CG2 . VAL AA 1 282 ? -26.933 -3.398 42.148 1.0 35.0 ? ? ? ? ? ? 399 VAL AA CG2 1 282 A A +ATOM 4947 N N . ARG AA 1 283 ? -27.384 0.323 44.077 1.0 45.56 ? ? ? ? ? ? 400 ARG AA N 1 283 A A +ATOM 4948 C CA . ARG AA 1 283 ? -27.031 1.571 44.742 1.0 52.75 ? ? ? ? ? ? 400 ARG AA CA 1 283 A A +ATOM 4949 C C . ARG AA 1 283 ? -28.086 1.939 45.778 1.0 58.51 ? ? ? ? ? ? 400 ARG AA C 1 283 A A +ATOM 4950 O O . ARG AA 1 283 ? -27.785 2.107 46.958 1.0 63.72 ? ? ? ? ? ? 400 ARG AA O 1 283 A A +ATOM 4951 C CB . ARG AA 1 283 ? -26.907 2.698 43.716 1.0 55.93 ? ? ? ? ? ? 400 ARG AA CB 1 283 A A +ATOM 4952 C CG . ARG AA 1 283 ? -25.516 2.861 43.157 1.0 54.36 ? ? ? ? ? ? 400 ARG AA CG 1 283 A A +ATOM 4953 C CD . ARG AA 1 283 ? -25.227 4.311 42.834 1.0 58.44 ? ? ? ? ? ? 400 ARG AA CD 1 283 A A +ATOM 4954 N NE . ARG AA 1 283 ? -23.894 4.471 42.264 1.0 77.88 ? ? ? ? ? ? 400 ARG AA NE 1 283 A A +ATOM 4955 C CZ . ARG AA 1 283 ? -22.903 5.146 42.841 1.0 86.01 ? ? ? ? ? ? 400 ARG AA CZ 1 283 A A +ATOM 4956 N NH1 . ARG AA 1 283 ? -23.089 5.737 44.015 1.0 78.05 ? ? ? ? ? ? 400 ARG AA NH1 1 283 A A +ATOM 4957 N NH2 . ARG AA 1 283 ? -21.722 5.228 42.241 1.0 99.95 ? ? ? ? ? ? 400 ARG AA NH2 1 283 A A +ATOM 4958 N N . ASN AA 1 284 ? -29.327 2.054 45.318 1.0 75.85 ? ? ? ? ? ? 401 ASN AA N 1 284 A A +ATOM 4959 C CA . ASN AA 1 284 ? -30.454 2.400 46.177 1.0 77.91 ? ? ? ? ? ? 401 ASN AA CA 1 284 A A +ATOM 4960 C C . ASN AA 1 284 ? -30.748 1.304 47.195 1.0 68.26 ? ? ? ? ? ? 401 ASN AA C 1 284 A A +ATOM 4961 O O . ASN AA 1 284 ? -30.974 1.586 48.373 1.0 72.47 ? ? ? ? ? ? 401 ASN AA O 1 284 A A +ATOM 4962 C CB . ASN AA 1 284 ? -31.692 2.646 45.321 1.0 87.48 ? ? ? ? ? ? 401 ASN AA CB 1 284 A A +ATOM 4963 C CG . ASN AA 1 284 ? -31.653 1.879 44.017 1.0 93.59 ? ? ? ? ? ? 401 ASN AA CG 1 284 A A +ATOM 4964 O OD1 . ASN AA 1 284 ? -31.571 2.471 42.938 1.0 92.46 ? ? ? ? ? ? 401 ASN AA OD1 1 284 A A +ATOM 4965 N ND2 . ASN AA 1 284 ? -31.704 0.552 44.107 1.0 99.85 ? ? ? ? ? ? 401 ASN AA ND2 1 284 A A +ATOM 4966 N N . PHE AA 1 285 ? -30.762 0.054 46.737 1.0 43.4 ? ? ? ? ? ? 402 PHE AA N 1 285 A A +ATOM 4967 C CA . PHE AA 1 285 ? -31.020 -1.080 47.621 1.0 48.71 ? ? ? ? ? ? 402 PHE AA CA 1 285 A A +ATOM 4968 C C . PHE AA 1 285 ? -30.113 -0.968 48.840 1.0 54.14 ? ? ? ? ? ? 402 PHE AA C 1 285 A A +ATOM 4969 O O . PHE AA 1 285 ? -30.453 -1.431 49.928 1.0 52.45 ? ? ? ? ? ? 402 PHE AA O 1 285 A A +ATOM 4970 C CB . PHE AA 1 285 ? -30.748 -2.404 46.891 1.0 45.77 ? ? ? ? ? ? 402 PHE AA CB 1 285 A A +ATOM 4971 C CG . PHE AA 1 285 ? -31.135 -3.638 47.678 1.0 59.63 ? ? ? ? ? ? 402 PHE AA CG 1 285 A A +ATOM 4972 C CD1 . PHE AA 1 285 ? -30.830 -4.906 47.191 1.0 62.54 ? ? ? ? ? ? 402 PHE AA CD1 1 285 A A +ATOM 4973 C CD2 . PHE AA 1 285 ? -31.807 -3.537 48.893 1.0 48.87 ? ? ? ? ? ? 402 PHE AA CD2 1 285 A A +ATOM 4974 C CE1 . PHE AA 1 285 ? -31.185 -6.052 47.909 1.0 49.67 ? ? ? ? ? ? 402 PHE AA CE1 1 285 A A +ATOM 4975 C CE2 . PHE AA 1 285 ? -32.163 -4.675 49.613 1.0 49.79 ? ? ? ? ? ? 402 PHE AA CE2 1 285 A A +ATOM 4976 C CZ . PHE AA 1 285 ? -31.852 -5.933 49.118 1.0 33.15 ? ? ? ? ? ? 402 PHE AA CZ 1 285 A A +ATOM 4977 N N . ALA AA 1 286 ? -28.955 -0.346 48.651 1.0 68.74 ? ? ? ? ? ? 403 ALA AA N 1 286 A A +ATOM 4978 C CA . ALA AA 1 286 ? -28.012 -0.171 49.744 1.0 84.45 ? ? ? ? ? ? 403 ALA AA CA 1 286 A A +ATOM 4979 C C . ALA AA 1 286 ? -28.572 0.837 50.746 1.0 85.9 ? ? ? ? ? ? 403 ALA AA C 1 286 A A +ATOM 4980 O O . ALA AA 1 286 ? -28.416 0.678 51.960 1.0 82.18 ? ? ? ? ? ? 403 ALA AA O 1 286 A A +ATOM 4981 C CB . ALA AA 1 286 ? -26.668 0.302 49.200 1.0 89.73 ? ? ? ? ? ? 403 ALA AA CB 1 286 A A +ATOM 4982 N N . ALA AA 1 287 ? -29.224 1.875 50.231 1.0 77.85 ? ? ? ? ? ? 404 ALA AA N 1 287 A A +ATOM 4983 C CA . ALA AA 1 287 ? -29.814 2.904 51.080 1.0 64.27 ? ? ? ? ? ? 404 ALA AA CA 1 287 A A +ATOM 4984 C C . ALA AA 1 287 ? -30.972 2.300 51.852 1.0 64.71 ? ? ? ? ? ? 404 ALA AA C 1 287 A A +ATOM 4985 O O . ALA AA 1 287 ? -31.279 2.715 52.967 1.0 57.92 ? ? ? ? ? ? 404 ALA AA O 1 287 A A +ATOM 4986 C CB . ALA AA 1 287 ? -30.306 4.061 50.233 1.0 39.11 ? ? ? ? ? ? 404 ALA AA CB 1 287 A A +ATOM 4987 N N . THR AA 1 288 ? -31.609 1.308 51.241 1.0 63.15 ? ? ? ? ? ? 405 THR AA N 1 288 A A +ATOM 4988 C CA . THR AA 1 288 ? -32.736 0.623 51.854 1.0 66.29 ? ? ? ? ? ? 405 THR AA CA 1 288 A A +ATOM 4989 C C . THR AA 1 288 ? -32.245 -0.431 52.851 1.0 74.21 ? ? ? ? ? ? 405 THR AA C 1 288 A A +ATOM 4990 O O . THR AA 1 288 ? -33.042 -1.166 53.447 1.0 77.41 ? ? ? ? ? ? 405 THR AA O 1 288 A A +ATOM 4991 C CB . THR AA 1 288 ? -33.602 -0.053 50.782 1.0 66.02 ? ? ? ? ? ? 405 THR AA CB 1 288 A A +ATOM 4992 O OG1 . THR AA 1 288 ? -32.899 -1.179 50.243 1.0 68.61 ? ? ? ? ? ? 405 THR AA OG1 1 288 A A +ATOM 4993 C CG2 . THR AA 1 288 ? -33.909 0.926 49.654 1.0 50.34 ? ? ? ? ? ? 405 THR AA CG2 1 288 A A +ATOM 4994 N N . ILE AA 1 289 ? -30.929 -0.497 53.031 1.0 69.12 ? ? ? ? ? ? 406 ILE AA N 1 289 A A +ATOM 4995 C CA . ILE AA 1 289 ? -30.331 -1.455 53.958 1.0 63.63 ? ? ? ? ? ? 406 ILE AA CA 1 289 A A +ATOM 4996 C C . ILE AA 1 289 ? -30.091 -0.810 55.317 1.0 58.59 ? ? ? ? ? ? 406 ILE AA C 1 289 A A +ATOM 4997 O O . ILE AA 1 289 ? -29.476 0.252 55.411 1.0 54.64 ? ? ? ? ? ? 406 ILE AA O 1 289 A A +ATOM 4998 C CB . ILE AA 1 289 ? -28.965 -1.982 53.449 1.0 65.45 ? ? ? ? ? ? 406 ILE AA CB 1 289 A A +ATOM 4999 C CG1 . ILE AA 1 289 ? -29.141 -2.724 52.125 1.0 56.74 ? ? ? ? ? ? 406 ILE AA CG1 1 289 A A +ATOM 5000 C CG2 . ILE AA 1 289 ? -28.356 -2.927 54.480 1.0 52.19 ? ? ? ? ? ? 406 ILE AA CG2 1 289 A A +ATOM 5001 C CD1 . ILE AA 1 289 ? -27.828 -3.088 51.461 1.0 41.69 ? ? ? ? ? ? 406 ILE AA CD1 1 289 A A +ATOM 5002 N N . PRO AA 1 290 ? -30.573 -1.452 56.391 1.0 58.31 ? ? ? ? ? ? 407 PRO AA N 1 290 A A +ATOM 5003 C CA . PRO AA 1 290 ? -30.407 -0.941 57.755 1.0 58.51 ? ? ? ? ? ? 407 PRO AA CA 1 290 A A +ATOM 5004 C C . PRO AA 1 290 ? -28.947 -0.961 58.205 1.0 59.72 ? ? ? ? ? ? 407 PRO AA C 1 290 A A +ATOM 5005 O O . PRO AA 1 290 ? -28.415 -1.999 58.597 1.0 56.66 ? ? ? ? ? ? 407 PRO AA O 1 290 A A +ATOM 5006 C CB . PRO AA 1 290 ? -31.287 -1.865 58.596 1.0 64.77 ? ? ? ? ? ? 407 PRO AA CB 1 290 A A +ATOM 5007 C CG . PRO AA 1 290 ? -31.383 -3.116 57.809 1.0 71.72 ? ? ? ? ? ? 407 PRO AA CG 1 290 A A +ATOM 5008 C CD . PRO AA 1 290 ? -31.314 -2.722 56.365 1.0 63.55 ? ? ? ? ? ? 407 PRO AA CD 1 290 A A +ATOM 5009 N N . ARG AA 1 291 ? -28.307 0.201 58.139 1.0 57.5 ? ? ? ? ? ? 408 ARG AA N 1 291 A A +ATOM 5010 C CA . ARG AA 1 291 ? -26.907 0.334 58.533 1.0 54.43 ? ? ? ? ? ? 408 ARG AA CA 1 291 A A +ATOM 5011 C C . ARG AA 1 291 ? -26.704 1.643 59.285 1.0 45.32 ? ? ? ? ? ? 408 ARG AA C 1 291 A A +ATOM 5012 O O . ARG AA 1 291 ? -26.915 2.722 58.736 1.0 44.45 ? ? ? ? ? ? 408 ARG AA O 1 291 A A +ATOM 5013 C CB . ARG AA 1 291 ? -26.003 0.315 57.292 1.0 65.13 ? ? ? ? ? ? 408 ARG AA CB 1 291 A A +ATOM 5014 C CG . ARG AA 1 291 ? -25.534 -1.077 56.865 1.0 50.86 ? ? ? ? ? ? 408 ARG AA CG 1 291 A A +ATOM 5015 C CD . ARG AA 1 291 ? -24.355 -1.016 55.881 1.0 59.04 ? ? ? ? ? ? 408 ARG AA CD 1 291 A A +ATOM 5016 N NE . ARG AA 1 291 ? -24.734 -0.473 54.573 1.0 65.61 ? ? ? ? ? ? 408 ARG AA NE 1 291 A A +ATOM 5017 C CZ . ARG AA 1 291 ? -23.896 -0.300 53.550 1.0 41.74 ? ? ? ? ? ? 408 ARG AA CZ 1 291 A A +ATOM 5018 N NH1 . ARG AA 1 291 ? -22.616 -0.624 53.667 1.0 32.43 ? ? ? ? ? ? 408 ARG AA NH1 1 291 A A +ATOM 5019 N NH2 . ARG AA 1 291 ? -24.336 0.213 52.408 1.0 44.03 ? ? ? ? ? ? 408 ARG AA NH2 1 291 A A +ATOM 5020 N N . PRO AA 1 292 ? -26.279 1.562 60.554 1.0 39.23 ? ? ? ? ? ? 409 PRO AA N 1 292 A A +ATOM 5021 C CA . PRO AA 1 292 ? -26.059 2.776 61.348 1.0 39.23 ? ? ? ? ? ? 409 PRO AA CA 1 292 A A +ATOM 5022 C C . PRO AA 1 292 ? -24.927 3.633 60.807 1.0 44.36 ? ? ? ? ? ? 409 PRO AA C 1 292 A A +ATOM 5023 O O . PRO AA 1 292 ? -24.274 4.356 61.557 1.0 55.39 ? ? ? ? ? ? 409 PRO AA O 1 292 A A +ATOM 5024 C CB . PRO AA 1 292 ? -25.743 2.249 62.750 1.0 41.24 ? ? ? ? ? ? 409 PRO AA CB 1 292 A A +ATOM 5025 C CG . PRO AA 1 292 ? -26.075 0.797 62.723 1.0 61.62 ? ? ? ? ? ? 409 PRO AA CG 1 292 A A +ATOM 5026 C CD . PRO AA 1 292 ? -25.951 0.347 61.308 1.0 51.69 ? ? ? ? ? ? 409 PRO AA CD 1 292 A A +ATOM 5027 N N . PHE AA 1 293 ? -24.700 3.543 59.498 1.0 51.53 ? ? ? ? ? ? 410 PHE AA N 1 293 A A +ATOM 5028 C CA . PHE AA 1 293 ? -23.636 4.291 58.838 1.0 51.06 ? ? ? ? ? ? 410 PHE AA CA 1 293 A A +ATOM 5029 C C . PHE AA 1 293 ? -23.735 4.094 57.328 1.0 52.16 ? ? ? ? ? ? 410 PHE AA C 1 293 A A +ATOM 5030 O O . PHE AA 1 293 ? -24.655 3.440 56.832 1.0 55.17 ? ? ? ? ? ? 410 PHE AA O 1 293 A A +ATOM 5031 C CB . PHE AA 1 293 ? -22.272 3.788 59.316 1.0 49.76 ? ? ? ? ? ? 410 PHE AA CB 1 293 A A +ATOM 5032 C CG . PHE AA 1 293 ? -21.998 2.354 58.944 1.0 62.85 ? ? ? ? ? ? 410 PHE AA CG 1 293 A A +ATOM 5033 C CD1 . PHE AA 1 293 ? -22.510 1.313 59.711 1.0 61.48 ? ? ? ? ? ? 410 PHE AA CD1 1 293 A A +ATOM 5034 C CD2 . PHE AA 1 293 ? -21.273 2.043 57.798 1.0 73.01 ? ? ? ? ? ? 410 PHE AA CD2 1 293 A A +ATOM 5035 C CE1 . PHE AA 1 293 ? -22.311 -0.014 59.342 1.0 59.87 ? ? ? ? ? ? 410 PHE AA CE1 1 293 A A +ATOM 5036 C CE2 . PHE AA 1 293 ? -21.068 0.716 57.419 1.0 55.37 ? ? ? ? ? ? 410 PHE AA CE2 1 293 A A +ATOM 5037 C CZ . PHE AA 1 293 ? -21.588 -0.313 58.194 1.0 56.26 ? ? ? ? ? ? 410 PHE AA CZ 1 293 A A +ATOM 5038 N N . SER AA 1 294 ? -22.775 4.663 56.606 1.0 41.42 ? ? ? ? ? ? 411 SER AA N 1 294 A A +ATOM 5039 C CA . SER AA 1 294 ? -22.716 4.547 55.153 1.0 44.89 ? ? ? ? ? ? 411 SER AA CA 1 294 A A +ATOM 5040 C C . SER AA 1 294 ? -21.239 4.473 54.782 1.0 46.8 ? ? ? ? ? ? 411 SER AA C 1 294 A A +ATOM 5041 O O . SER AA 1 294 ? -20.412 5.143 55.398 1.0 38.91 ? ? ? ? ? ? 411 SER AA O 1 294 A A +ATOM 5042 C CB . SER AA 1 294 ? -23.374 5.764 54.496 1.0 60.81 ? ? ? ? ? ? 411 SER AA CB 1 294 A A +ATOM 5043 O OG . SER AA 1 294 ? -24.787 5.652 54.504 1.0 83.94 ? ? ? ? ? ? 411 SER AA OG 1 294 A A +ATOM 5044 N N . VAL AA 1 295 ? -20.909 3.657 53.788 1.0 47.12 ? ? ? ? ? ? 412 VAL AA N 1 295 A A +ATOM 5045 C CA . VAL AA 1 295 ? -19.519 3.496 53.370 1.0 41.5 ? ? ? ? ? ? 412 VAL AA CA 1 295 A A +ATOM 5046 C C . VAL AA 1 295 ? -19.171 4.273 52.104 1.0 40.55 ? ? ? ? ? ? 412 VAL AA C 1 295 A A +ATOM 5047 O O . VAL AA 1 295 ? -20.047 4.629 51.318 1.0 43.56 ? ? ? ? ? ? 412 VAL AA O 1 295 A A +ATOM 5048 C CB . VAL AA 1 295 ? -19.198 2.010 53.153 1.0 37.58 ? ? ? ? ? ? 412 VAL AA CB 1 295 A A +ATOM 5049 C CG1 . VAL AA 1 295 ? -19.298 1.273 54.476 1.0 29.68 ? ? ? ? ? ? 412 VAL AA CG1 1 295 A A +ATOM 5050 C CG2 . VAL AA 1 295 ? -20.165 1.408 52.149 1.0 32.03 ? ? ? ? ? ? 412 VAL AA CG2 1 295 A A +ATOM 5051 N N . ARG AA 1 296 ? -17.881 4.539 51.919 1.0 46.03 ? ? ? ? ? ? 413 ARG AA N 1 296 A A +ATOM 5052 C CA . ARG AA 1 296 ? -17.398 5.285 50.758 1.0 36.71 ? ? ? ? ? ? 413 ARG AA CA 1 296 A A +ATOM 5053 C C . ARG AA 1 296 ? -15.984 4.842 50.400 1.0 33.03 ? ? ? ? ? ? 413 ARG AA C 1 296 A A +ATOM 5054 O O . ARG AA 1 296 ? -15.060 4.997 51.195 1.0 37.61 ? ? ? ? ? ? 413 ARG AA O 1 296 A A +ATOM 5055 C CB . ARG AA 1 296 ? -17.414 6.785 51.067 1.0 43.97 ? ? ? ? ? ? 413 ARG AA CB 1 296 A A +ATOM 5056 C CG . ARG AA 1 296 ? -16.436 7.618 50.258 1.0 51.36 ? ? ? ? ? ? 413 ARG AA CG 1 296 A A +ATOM 5057 C CD . ARG AA 1 296 ? -16.875 9.073 50.203 1.0 61.85 ? ? ? ? ? ? 413 ARG AA CD 1 296 A A +ATOM 5058 N NE . ARG AA 1 296 ? -16.609 9.770 51.461 1.0 59.9 ? ? ? ? ? ? 413 ARG AA NE 1 296 A A +ATOM 5059 C CZ . ARG AA 1 296 ? -16.602 11.092 51.597 1.0 60.5 ? ? ? ? ? ? 413 ARG AA CZ 1 296 A A +ATOM 5060 N NH1 . ARG AA 1 296 ? -16.839 11.868 50.548 1.0 52.53 ? ? ? ? ? ? 413 ARG AA NH1 1 296 A A +ATOM 5061 N NH2 . ARG AA 1 296 ? -16.355 11.639 52.781 1.0 23.98 ? ? ? ? ? ? 413 ARG AA NH2 1 296 A A +ATOM 5062 N N . TYR AA 1 297 ? -15.815 4.290 49.202 1.0 32.09 ? ? ? ? ? ? 414 TYR AA N 1 297 A A +ATOM 5063 C CA . TYR AA 1 297 ? -14.498 3.825 48.780 1.0 32.39 ? ? ? ? ? ? 414 TYR AA CA 1 297 A A +ATOM 5064 C C . TYR AA 1 297 ? -13.639 4.893 48.099 1.0 31.53 ? ? ? ? ? ? 414 TYR AA C 1 297 A A +ATOM 5065 O O . TYR AA 1 297 ? -14.129 5.699 47.305 1.0 65.12 ? ? ? ? ? ? 414 TYR AA O 1 297 A A +ATOM 5066 C CB . TYR AA 1 297 ? -14.624 2.611 47.851 1.0 14.01 ? ? ? ? ? ? 414 TYR AA CB 1 297 A A +ATOM 5067 C CG . TYR AA 1 297 ? -13.300 1.919 47.619 1.0 25.23 ? ? ? ? ? ? 414 TYR AA CG 1 297 A A +ATOM 5068 C CD1 . TYR AA 1 297 ? -12.612 1.328 48.678 1.0 39.31 ? ? ? ? ? ? 414 TYR AA CD1 1 297 A A +ATOM 5069 C CD2 . TYR AA 1 297 ? -12.697 1.916 46.363 1.0 19.41 ? ? ? ? ? ? 414 TYR AA CD2 1 297 A A +ATOM 5070 C CE1 . TYR AA 1 297 ? -11.353 0.757 48.498 1.0 52.9 ? ? ? ? ? ? 414 TYR AA CE1 1 297 A A +ATOM 5071 C CE2 . TYR AA 1 297 ? -11.437 1.346 46.172 1.0 45.56 ? ? ? ? ? ? 414 TYR AA CE2 1 297 A A +ATOM 5072 C CZ . TYR AA 1 297 ? -10.769 0.771 47.246 1.0 48.02 ? ? ? ? ? ? 414 TYR AA CZ 1 297 A A +ATOM 5073 O OH . TYR AA 1 297 ? -9.512 0.230 47.080 1.0 55.29 ? ? ? ? ? ? 414 TYR AA OH 1 297 A A +ATOM 5074 N N . ASP AA 1 298 ? -12.350 4.889 48.429 1.0 44.74 ? ? ? ? ? ? 415 ASP AA N 1 298 A A +ATOM 5075 C CA . ASP AA 1 298 ? -11.381 5.826 47.864 1.0 45.65 ? ? ? ? ? ? 415 ASP AA CA 1 298 A A +ATOM 5076 C C . ASP AA 1 298 ? -10.330 5.031 47.080 1.0 54.5 ? ? ? ? ? ? 415 ASP AA C 1 298 A A +ATOM 5077 O O . ASP AA 1 298 ? -9.395 4.472 47.658 1.0 62.76 ? ? ? ? ? ? 415 ASP AA O 1 298 A A +ATOM 5078 C CB . ASP AA 1 298 ? -10.699 6.623 48.979 1.0 52.89 ? ? ? ? ? ? 415 ASP AA CB 1 298 A A +ATOM 5079 C CG . ASP AA 1 298 ? -9.700 7.636 48.454 1.0 39.17 ? ? ? ? ? ? 415 ASP AA CG 1 298 A A +ATOM 5080 O OD1 . ASP AA 1 298 ? -8.884 8.144 49.251 1.0 52.8 ? ? ? ? ? ? 415 ASP AA OD1 1 298 A A +ATOM 5081 O OD2 . ASP AA 1 298 ? -9.734 7.930 47.241 1.0 41.7 ? ? ? ? ? ? 415 ASP AA OD2 1 298 A A +ATOM 5082 N N . PRO AA 1 299 ? -10.474 4.975 45.746 1.0 40.81 ? ? ? ? ? ? 416 PRO AA N 1 299 A A +ATOM 5083 C CA . PRO AA 1 299 ? -9.525 4.237 44.907 1.0 19.09 ? ? ? ? ? ? 416 PRO AA CA 1 299 A A +ATOM 5084 C C . PRO AA 1 299 ? -8.112 4.813 44.936 1.0 20.61 ? ? ? ? ? ? 416 PRO AA C 1 299 A A +ATOM 5085 O O . PRO AA 1 299 ? -7.149 4.121 44.617 1.0 40.06 ? ? ? ? ? ? 416 PRO AA O 1 299 A A +ATOM 5086 C CB . PRO AA 1 299 ? -10.150 4.302 43.514 1.0 18.39 ? ? ? ? ? ? 416 PRO AA CB 1 299 A A +ATOM 5087 C CG . PRO AA 1 299 ? -11.044 5.488 43.550 1.0 36.47 ? ? ? ? ? ? 416 PRO AA CG 1 299 A A +ATOM 5088 C CD . PRO AA 1 299 ? -11.534 5.620 44.954 1.0 39.25 ? ? ? ? ? ? 416 PRO AA CD 1 299 A A +ATOM 5089 N N . TYR AA 1 300 ? -7.995 6.080 45.323 1.0 23.31 ? ? ? ? ? ? 417 TYR AA N 1 300 A A +ATOM 5090 C CA . TYR AA 1 300 ? -6.704 6.755 45.394 1.0 18.04 ? ? ? ? ? ? 417 TYR AA CA 1 300 A A +ATOM 5091 C C . TYR AA 1 300 ? -5.856 6.255 46.563 1.0 26.33 ? ? ? ? ? ? 417 TYR AA C 1 300 A A +ATOM 5092 O O . TYR AA 1 300 ? -4.631 6.211 46.469 1.0 42.27 ? ? ? ? ? ? 417 TYR AA O 1 300 A A +ATOM 5093 C CB . TYR AA 1 300 ? -6.917 8.261 45.504 1.0 34.2 ? ? ? ? ? ? 417 TYR AA CB 1 300 A A +ATOM 5094 C CG . TYR AA 1 300 ? -7.522 8.868 44.260 1.0 31.39 ? ? ? ? ? ? 417 TYR AA CG 1 300 A A +ATOM 5095 C CD1 . TYR AA 1 300 ? -8.888 9.121 44.174 1.0 44.97 ? ? ? ? ? ? 417 TYR AA CD1 1 300 A A +ATOM 5096 C CD2 . TYR AA 1 300 ? -6.727 9.188 43.162 1.0 43.77 ? ? ? ? ? ? 417 TYR AA CD2 1 300 A A +ATOM 5097 C CE1 . TYR AA 1 300 ? -9.447 9.676 43.021 1.0 60.75 ? ? ? ? ? ? 417 TYR AA CE1 1 300 A A +ATOM 5098 C CE2 . TYR AA 1 300 ? -7.278 9.743 42.006 1.0 47.93 ? ? ? ? ? ? 417 TYR AA CE2 1 300 A A +ATOM 5099 C CZ . TYR AA 1 300 ? -8.636 9.985 41.943 1.0 46.98 ? ? ? ? ? ? 417 TYR AA CZ 1 300 A A +ATOM 5100 O OH . TYR AA 1 300 ? -9.184 10.531 40.807 1.0 34.47 ? ? ? ? ? ? 417 TYR AA OH 1 300 A A +ATOM 5101 N N . THR AA 1 301 ? -6.508 5.884 47.664 1.0 29.23 ? ? ? ? ? ? 418 THR AA N 1 301 A A +ATOM 5102 C CA . THR AA 1 301 ? -5.807 5.366 48.842 1.0 22.36 ? ? ? ? ? ? 418 THR AA CA 1 301 A A +ATOM 5103 C C . THR AA 1 301 ? -6.216 3.928 49.142 1.0 20.46 ? ? ? ? ? ? 418 THR AA C 1 301 A A +ATOM 5104 O O . THR AA 1 301 ? -5.799 3.362 50.153 1.0 20.8 ? ? ? ? ? ? 418 THR AA O 1 301 A A +ATOM 5105 C CB . THR AA 1 301 ? -6.093 6.205 50.101 1.0 18.97 ? ? ? ? ? ? 418 THR AA CB 1 301 A A +ATOM 5106 O OG1 . THR AA 1 301 ? -7.493 6.162 50.397 1.0 50.92 ? ? ? ? ? ? 418 THR AA OG1 1 301 A A +ATOM 5107 C CG2 . THR AA 1 301 ? -5.663 7.640 49.890 1.0 37.66 ? ? ? ? ? ? 418 THR AA CG2 1 301 A A +ATOM 5108 N N . GLN AA 1 302 ? -7.021 3.347 48.251 1.0 37.04 ? ? ? ? ? ? 419 GLN AA N 1 302 A A +ATOM 5109 C CA . GLN AA 1 302 ? -7.500 1.974 48.407 1.0 38.68 ? ? ? ? ? ? 419 GLN AA CA 1 302 A A +ATOM 5110 C C . GLN AA 1 302 ? -7.993 1.819 49.833 1.0 41.44 ? ? ? ? ? ? 419 GLN AA C 1 302 A A +ATOM 5111 O O . GLN AA 1 302 ? -7.589 0.905 50.551 1.0 53.88 ? ? ? ? ? ? 419 GLN AA O 1 302 A A +ATOM 5112 C CB . GLN AA 1 302 ? -6.369 0.976 48.164 1.0 39.99 ? ? ? ? ? ? 419 GLN AA CB 1 302 A A +ATOM 5113 C CG . GLN AA 1 302 ? -5.823 0.964 46.752 1.0 43.23 ? ? ? ? ? ? 419 GLN AA CG 1 302 A A +ATOM 5114 C CD . GLN AA 1 302 ? -4.606 0.073 46.627 1.0 55.23 ? ? ? ? ? ? 419 GLN AA CD 1 302 A A +ATOM 5115 O OE1 . GLN AA 1 302 ? -3.566 0.334 47.234 1.0 66.54 ? ? ? ? ? ? 419 GLN AA OE1 1 302 A A +ATOM 5116 N NE2 . GLN AA 1 302 ? -4.727 -0.987 45.840 1.0 65.41 ? ? ? ? ? ? 419 GLN AA NE2 1 302 A A +ATOM 5117 N N . ARG AA 1 303 ? -8.871 2.723 50.241 1.0 36.0 ? ? ? ? ? ? 420 ARG AA N 1 303 A A +ATOM 5118 C CA . ARG AA 1 303 ? -9.389 2.702 51.595 1.0 36.42 ? ? ? ? ? ? 420 ARG AA CA 1 303 A A +ATOM 5119 C C . ARG AA 1 303 ? -10.880 2.989 51.640 1.0 28.89 ? ? ? ? ? ? 420 ARG AA C 1 303 A A +ATOM 5120 O O . ARG AA 1 303 ? -11.391 3.798 50.870 1.0 38.54 ? ? ? ? ? ? 420 ARG AA O 1 303 A A +ATOM 5121 C CB . ARG AA 1 303 ? -8.643 3.740 52.432 1.0 43.32 ? ? ? ? ? ? 420 ARG AA CB 1 303 A A +ATOM 5122 C CG . ARG AA 1 303 ? -8.305 3.293 53.838 1.0 46.86 ? ? ? ? ? ? 420 ARG AA CG 1 303 A A +ATOM 5123 C CD . ARG AA 1 303 ? -7.525 4.377 54.572 1.0 65.16 ? ? ? ? ? ? 420 ARG AA CD 1 303 A A +ATOM 5124 N NE . ARG AA 1 303 ? -6.597 5.074 53.682 1.0 68.48 ? ? ? ? ? ? 420 ARG AA NE 1 303 A A +ATOM 5125 C CZ . ARG AA 1 303 ? -5.404 5.539 54.049 1.0 71.5 ? ? ? ? ? ? 420 ARG AA CZ 1 303 A A +ATOM 5126 N NH1 . ARG AA 1 303 ? -4.979 5.382 55.297 1.0 63.28 ? ? ? ? ? ? 420 ARG AA NH1 1 303 A A +ATOM 5127 N NH2 . ARG AA 1 303 ? -4.634 6.154 53.161 1.0 60.1 ? ? ? ? ? ? 420 ARG AA NH2 1 303 A A +ATOM 5128 N N . ILE AA 1 304 ? -11.572 2.315 52.549 1.0 5.09 ? ? ? ? ? ? 421 ILE AA N 1 304 A A +ATOM 5129 C CA . ILE AA 1 304 ? -13.001 2.516 52.712 1.0 22.29 ? ? ? ? ? ? 421 ILE AA CA 1 304 A A +ATOM 5130 C C . ILE AA 1 304 ? -13.176 3.564 53.809 1.0 35.36 ? ? ? ? ? ? 421 ILE AA C 1 304 A A +ATOM 5131 O O . ILE AA 1 304 ? -12.420 3.569 54.785 1.0 37.76 ? ? ? ? ? ? 421 ILE AA O 1 304 A A +ATOM 5132 C CB . ILE AA 1 304 ? -13.713 1.204 53.158 1.0 17.55 ? ? ? ? ? ? 421 ILE AA CB 1 304 A A +ATOM 5133 C CG1 . ILE AA 1 304 ? -14.040 0.337 51.942 1.0 11.22 ? ? ? ? ? ? 421 ILE AA CG1 1 304 A A +ATOM 5134 C CG2 . ILE AA 1 304 ? -14.992 1.530 53.923 1.0 27.04 ? ? ? ? ? ? 421 ILE AA CG2 1 304 A A +ATOM 5135 C CD1 . ILE AA 1 304 ? -15.163 0.873 51.088 1.0 30.57 ? ? ? ? ? ? 421 ILE AA CD1 1 304 A A +ATOM 5136 N N . GLU AA 1 305 ? -14.154 4.458 53.643 1.0 44.17 ? ? ? ? ? ? 422 GLU AA N 1 305 A A +ATOM 5137 C CA . GLU AA 1 305 ? -14.437 5.475 54.655 1.0 42.82 ? ? ? ? ? ? 422 GLU AA CA 1 305 A A +ATOM 5138 C C . GLU AA 1 305 ? -15.829 5.211 55.208 1.0 56.06 ? ? ? ? ? ? 422 GLU AA C 1 305 A A +ATOM 5139 O O . GLU AA 1 305 ? -16.770 4.977 54.452 1.0 70.09 ? ? ? ? ? ? 422 GLU AA O 1 305 A A +ATOM 5140 C CB . GLU AA 1 305 ? -14.372 6.890 54.073 1.0 49.23 ? ? ? ? ? ? 422 GLU AA CB 1 305 A A +ATOM 5141 C CG . GLU AA 1 305 ? -14.408 7.969 55.154 1.0 66.49 ? ? ? ? ? ? 422 GLU AA CG 1 305 A A +ATOM 5142 C CD . GLU AA 1 305 ? -14.394 9.382 54.598 1.0 83.44 ? ? ? ? ? ? 422 GLU AA CD 1 305 A A +ATOM 5143 O OE1 . GLU AA 1 305 ? -14.656 10.327 55.374 1.0 61.26 ? ? ? ? ? ? 422 GLU AA OE1 1 305 A A +ATOM 5144 O OE2 . GLU AA 1 305 ? -14.120 9.547 53.390 1.0 86.85 ? ? ? ? ? ? 422 GLU AA OE2 1 305 A A +ATOM 5145 N N . VAL AA 1 306 ? -15.956 5.233 56.531 1.0 57.84 ? ? ? ? ? ? 423 VAL AA N 1 306 A A +ATOM 5146 C CA . VAL AA 1 306 ? -17.241 4.986 57.181 1.0 50.66 ? ? ? ? ? ? 423 VAL AA CA 1 306 A A +ATOM 5147 C C . VAL AA 1 306 ? -17.899 6.300 57.596 1.0 41.37 ? ? ? ? ? ? 423 VAL AA C 1 306 A A +ATOM 5148 O O . VAL AA 1 306 ? -17.361 7.046 58.406 1.0 26.86 ? ? ? ? ? ? 423 VAL AA O 1 306 A A +ATOM 5149 C CB . VAL AA 1 306 ? -17.059 4.075 58.416 1.0 38.04 ? ? ? ? ? ? 423 VAL AA CB 1 306 A A +ATOM 5150 C CG1 . VAL AA 1 306 ? -18.414 3.657 58.955 1.0 46.38 ? ? ? ? ? ? 423 VAL AA CG1 1 306 A A +ATOM 5151 C CG2 . VAL AA 1 306 ? -16.242 2.850 58.036 1.0 40.98 ? ? ? ? ? ? 423 VAL AA CG2 1 306 A A +ATOM 5152 N N . LEU AA 1 307 ? -19.066 6.576 57.029 1.0 46.86 ? ? ? ? ? ? 424 LEU AA N 1 307 A A +ATOM 5153 C CA . LEU AA 1 307 ? -19.771 7.809 57.327 1.0 44.59 ? ? ? ? ? ? 424 LEU AA CA 1 307 A A +ATOM 5154 C C . LEU AA 1 307 ? -20.984 7.622 58.227 1.0 54.91 ? ? ? ? ? ? 424 LEU AA C 1 307 A A +ATOM 5155 O O . LEU AA 1 307 ? -21.567 6.539 58.306 1.0 59.89 ? ? ? ? ? ? 424 LEU AA O 1 307 A A +ATOM 5156 C CB . LEU AA 1 307 ? -20.206 8.488 56.027 1.0 35.66 ? ? ? ? ? ? 424 LEU AA CB 1 307 A A +ATOM 5157 C CG . LEU AA 1 307 ? -19.087 9.019 55.136 1.0 33.05 ? ? ? ? ? ? 424 LEU AA CG 1 307 A A +ATOM 5158 C CD1 . LEU AA 1 307 ? -19.630 9.347 53.760 1.0 38.05 ? ? ? ? ? ? 424 LEU AA CD1 1 307 A A +ATOM 5159 C CD2 . LEU AA 1 307 ? -18.481 10.245 55.778 1.0 20.8 ? ? ? ? ? ? 424 LEU AA CD2 1 307 A A +ATOM 5160 N N . ASP AA 1 308 ? -21.357 8.705 58.903 1.0 42.91 ? ? ? ? ? ? 425 ASP AA N 1 308 A A +ATOM 5161 C CA . ASP AA 1 308 ? -22.500 8.727 59.802 1.0 36.38 ? ? ? ? ? ? 425 ASP AA CA 1 308 A A +ATOM 5162 C C . ASP AA 1 308 ? -23.700 9.280 59.038 1.0 36.99 ? ? ? ? ? ? 425 ASP AA C 1 308 A A +ATOM 5163 O O . ASP AA 1 308 ? -23.709 10.441 58.634 1.0 45.17 ? ? ? ? ? ? 425 ASP AA O 1 308 A A +ATOM 5164 C CB . ASP AA 1 308 ? -22.186 9.621 61.010 1.0 42.98 ? ? ? ? ? ? 425 ASP AA CB 1 308 A A +ATOM 5165 C CG . ASP AA 1 308 ? -23.419 10.301 61.569 1.0 50.49 ? ? ? ? ? ? 425 ASP AA CG 1 308 A A +ATOM 5166 O OD1 . ASP AA 1 308 ? -23.426 11.548 61.636 1.0 50.76 ? ? ? ? ? ? 425 ASP AA OD1 1 308 A A +ATOM 5167 O OD2 . ASP AA 1 308 ? -24.368 9.581 61.937 1.0 60.47 ? ? ? ? ? ? 425 ASP AA OD2 1 308 A A +ATOM 5168 N N . ASN AA 1 309 ? -24.707 8.434 58.837 1.0 36.35 ? ? ? ? ? ? 426 ASN AA N 1 309 A A +ATOM 5169 C CA . ASN AA 1 309 ? -25.926 8.787 58.120 1.0 56.38 ? ? ? ? ? ? 426 ASN AA CA 1 309 A A +ATOM 5170 C C . ASN AA 1 309 ? -26.209 10.293 58.000 1.0 54.47 ? ? ? ? ? ? 426 ASN AA C 1 309 A A +ATOM 5171 O O . ASN AA 1 309 ? -26.594 10.770 56.938 1.0 64.32 ? ? ? ? ? ? 426 ASN AA O 1 309 A A +ATOM 5172 C CB . ASN AA 1 309 ? -27.119 8.092 58.777 1.0 67.66 ? ? ? ? ? ? 426 ASN AA CB 1 309 A A +ATOM 5173 C CG . ASN AA 1 309 ? -26.724 7.333 60.033 1.0 86.65 ? ? ? ? ? ? 426 ASN AA CG 1 309 A A +ATOM 5174 O OD1 . ASN AA 1 309 ? -26.226 6.211 59.957 1.0 84.18 ? ? ? ? ? ? 426 ASN AA OD1 1 309 A A +ATOM 5175 N ND2 . ASN AA 1 309 ? -26.944 7.941 61.190 1.0 95.28 ? ? ? ? ? ? 426 ASN AA ND2 1 309 A A +ATOM 5176 N N . THR AA 1 310 ? -26.034 11.024 59.096 1.0 52.24 ? ? ? ? ? ? 427 THR AA N 1 310 A A +ATOM 5177 C CA . THR AA 1 310 ? -26.265 12.469 59.125 1.0 49.39 ? ? ? ? ? ? 427 THR AA CA 1 310 A A +ATOM 5178 C C . THR AA 1 310 ? -25.298 13.244 58.242 1.0 44.74 ? ? ? ? ? ? 427 THR AA C 1 310 A A +ATOM 5179 O O . THR AA 1 310 ? -25.710 14.073 57.435 1.0 42.41 ? ? ? ? ? ? 427 THR AA O 1 310 A A +ATOM 5180 C CB . THR AA 1 310 ? -26.142 13.002 60.557 1.0 60.18 ? ? ? ? ? ? 427 THR AA CB 1 310 A A +ATOM 5181 O OG1 . THR AA 1 310 ? -27.139 12.385 61.383 1.0 80.03 ? ? ? ? ? ? 427 THR AA OG1 1 310 A A +ATOM 5182 C CG2 . THR AA 1 310 ? -26.296 14.524 60.576 1.0 47.23 ? ? ? ? ? ? 427 THR AA CG2 1 310 A A +ATOM 5183 N N . GLN AA 1 311 ? -24.011 12.976 58.417 1.0 47.04 ? ? ? ? ? ? 428 GLN AA N 1 311 A A +ATOM 5184 C CA . GLN AA 1 311 ? -22.972 13.628 57.635 1.0 41.76 ? ? ? ? ? ? 428 GLN AA CA 1 311 A A +ATOM 5185 C C . GLN AA 1 311 ? -23.029 13.073 56.225 1.0 37.71 ? ? ? ? ? ? 428 GLN AA C 1 311 A A +ATOM 5186 O O . GLN AA 1 311 ? -22.617 13.728 55.273 1.0 37.38 ? ? ? ? ? ? 428 GLN AA O 1 311 A A +ATOM 5187 C CB . GLN AA 1 311 ? -21.596 13.364 58.241 1.0 57.95 ? ? ? ? ? ? 428 GLN AA CB 1 311 A A +ATOM 5188 C CG . GLN AA 1 311 ? -21.190 11.903 58.244 1.0 71.47 ? ? ? ? ? ? 428 GLN AA CG 1 311 A A +ATOM 5189 C CD . GLN AA 1 311 ? -20.186 11.590 59.337 1.0 77.03 ? ? ? ? ? ? 428 GLN AA CD 1 311 A A +ATOM 5190 O OE1 . GLN AA 1 311 ? -19.330 10.716 59.183 1.0 80.85 ? ? ? ? ? ? 428 GLN AA OE1 1 311 A A +ATOM 5191 N NE2 . GLN AA 1 311 ? -20.292 12.295 60.449 1.0 78.75 ? ? ? ? ? ? 428 GLN AA NE2 1 311 A A +ATOM 5192 N N . GLN AA 1 312 ? -23.536 11.850 56.101 1.0 32.32 ? ? ? ? ? ? 429 GLN AA N 1 312 A A +ATOM 5193 C CA . GLN AA 1 312 ? -23.673 11.214 54.799 1.0 44.95 ? ? ? ? ? ? 429 GLN AA CA 1 312 A A +ATOM 5194 C C . GLN AA 1 312 ? -24.743 11.999 54.036 1.0 53.81 ? ? ? ? ? ? 429 GLN AA C 1 312 A A +ATOM 5195 O O . GLN AA 1 312 ? -24.629 12.238 52.831 1.0 51.75 ? ? ? ? ? ? 429 GLN AA O 1 312 A A +ATOM 5196 C CB . GLN AA 1 312 ? -24.119 9.760 54.960 1.0 41.33 ? ? ? ? ? ? 429 GLN AA CB 1 312 A A +ATOM 5197 C CG . GLN AA 1 312 ? -23.746 8.863 53.795 1.0 62.27 ? ? ? ? ? ? 429 GLN AA CG 1 312 A A +ATOM 5198 C CD . GLN AA 1 312 ? -24.811 8.814 52.721 1.0 54.21 ? ? ? ? ? ? 429 GLN AA CD 1 312 A A +ATOM 5199 O OE1 . GLN AA 1 312 ? -24.550 9.122 51.558 1.0 48.76 ? ? ? ? ? ? 429 GLN AA OE1 1 312 A A +ATOM 5200 N NE2 . GLN AA 1 312 ? -26.019 8.421 53.104 1.0 50.57 ? ? ? ? ? ? 429 GLN AA NE2 1 312 A A +ATOM 5201 N N . LEU AA 1 313 ? -25.783 12.389 54.773 1.0 64.83 ? ? ? ? ? ? 430 LEU AA N 1 313 A A +ATOM 5202 C CA . LEU AA 1 313 ? -26.911 13.169 54.261 1.0 44.71 ? ? ? ? ? ? 430 LEU AA CA 1 313 A A +ATOM 5203 C C . LEU AA 1 313 ? -26.348 14.459 53.682 1.0 33.89 ? ? ? ? ? ? 430 LEU AA C 1 313 A A +ATOM 5204 O O . LEU AA 1 313 ? -26.550 14.771 52.511 1.0 32.98 ? ? ? ? ? ? 430 LEU AA O 1 313 A A +ATOM 5205 C CB . LEU AA 1 313 ? -27.869 13.502 55.417 1.0 25.78 ? ? ? ? ? ? 430 LEU AA CB 1 313 A A +ATOM 5206 C CG . LEU AA 1 313 ? -29.394 13.590 55.263 1.0 39.27 ? ? ? ? ? ? 430 LEU AA CG 1 313 A A +ATOM 5207 C CD1 . LEU AA 1 313 ? -29.906 12.646 54.183 1.0 34.15 ? ? ? ? ? ? 430 LEU AA CD1 1 313 A A +ATOM 5208 C CD2 . LEU AA 1 313 ? -30.030 13.251 56.606 1.0 18.5 ? ? ? ? ? ? 430 LEU AA CD2 1 313 A A +ATOM 5209 N N . LYS AA 1 314 ? -25.642 15.196 54.534 1.0 27.52 ? ? ? ? ? ? 431 LYS AA N 1 314 A A +ATOM 5210 C CA . LYS AA 1 314 ? -25.019 16.455 54.162 1.0 42.32 ? ? ? ? ? ? 431 LYS AA CA 1 314 A A +ATOM 5211 C C . LYS AA 1 314 ? -24.116 16.285 52.947 1.0 52.75 ? ? ? ? ? ? 431 LYS AA C 1 314 A A +ATOM 5212 O O . LYS AA 1 314 ? -24.078 17.145 52.068 1.0 62.72 ? ? ? ? ? ? 431 LYS AA O 1 314 A A +ATOM 5213 C CB . LYS AA 1 314 ? -24.196 16.991 55.331 1.0 52.8 ? ? ? ? ? ? 431 LYS AA CB 1 314 A A +ATOM 5214 C CG . LYS AA 1 314 ? -25.013 17.324 56.560 1.0 68.93 ? ? ? ? ? ? 431 LYS AA CG 1 314 A A +ATOM 5215 C CD . LYS AA 1 314 ? -24.200 18.142 57.545 1.0 86.73 ? ? ? ? ? ? 431 LYS AA CD 1 314 A A +ATOM 5216 C CE . LYS AA 1 314 ? -24.996 18.459 58.799 1.0 89.43 ? ? ? ? ? ? 431 LYS AA CE 1 314 A A +ATOM 5217 N NZ . LYS AA 1 314 ? -24.242 19.380 59.689 1.0 85.66 ? ? ? ? ? ? 431 LYS AA NZ 1 314 A A +ATOM 5218 N N . ILE AA 1 315 ? -23.385 15.174 52.905 1.0 54.13 ? ? ? ? ? ? 432 ILE AA N 1 315 A A +ATOM 5219 C CA . ILE AA 1 315 ? -22.480 14.899 51.794 1.0 49.64 ? ? ? ? ? ? 432 ILE AA CA 1 315 A A +ATOM 5220 C C . ILE AA 1 315 ? -23.256 14.804 50.484 1.0 50.77 ? ? ? ? ? ? 432 ILE AA C 1 315 A A +ATOM 5221 O O . ILE AA 1 315 ? -22.840 15.354 49.466 1.0 46.54 ? ? ? ? ? ? 432 ILE AA O 1 315 A A +ATOM 5222 C CB . ILE AA 1 315 ? -21.692 13.590 52.027 1.0 48.67 ? ? ? ? ? ? 432 ILE AA CB 1 315 A A +ATOM 5223 C CG1 . ILE AA 1 315 ? -20.654 13.799 53.133 1.0 39.82 ? ? ? ? ? ? 432 ILE AA CG1 1 315 A A +ATOM 5224 C CG2 . ILE AA 1 315 ? -21.003 13.153 50.746 1.0 52.52 ? ? ? ? ? ? 432 ILE AA CG2 1 315 A A +ATOM 5225 C CD1 . ILE AA 1 315 ? -20.017 15.178 53.143 1.0 39.19 ? ? ? ? ? ? 432 ILE AA CD1 1 315 A A +ATOM 5226 N N . LEU AA 1 316 ? -24.384 14.107 50.514 1.0 38.29 ? ? ? ? ? ? 433 LEU AA N 1 316 A A +ATOM 5227 C CA . LEU AA 1 316 ? -25.215 13.970 49.327 1.0 37.4 ? ? ? ? ? ? 433 LEU AA CA 1 316 A A +ATOM 5228 C C . LEU AA 1 316 ? -25.686 15.351 48.870 1.0 47.88 ? ? ? ? ? ? 433 LEU AA C 1 316 A A +ATOM 5229 O O . LEU AA 1 316 ? -25.593 15.698 47.691 1.0 44.2 ? ? ? ? ? ? 433 LEU AA O 1 316 A A +ATOM 5230 C CB . LEU AA 1 316 ? -26.430 13.098 49.636 1.0 17.6 ? ? ? ? ? ? 433 LEU AA CB 1 316 A A +ATOM 5231 C CG . LEU AA 1 316 ? -26.135 11.638 49.952 1.0 38.38 ? ? ? ? ? ? 433 LEU AA CG 1 316 A A +ATOM 5232 C CD1 . LEU AA 1 316 ? -27.035 11.172 51.080 1.0 51.77 ? ? ? ? ? ? 433 LEU AA CD1 1 316 A A +ATOM 5233 C CD2 . LEU AA 1 316 ? -26.351 10.805 48.703 1.0 44.05 ? ? ? ? ? ? 433 LEU AA CD2 1 316 A A +ATOM 5234 N N . ALA AA 1 317 ? -26.198 16.132 49.816 1.0 40.82 ? ? ? ? ? ? 434 ALA AA N 1 317 A A +ATOM 5235 C CA . ALA AA 1 317 ? -26.688 17.473 49.529 1.0 31.1 ? ? ? ? ? ? 434 ALA AA CA 1 317 A A +ATOM 5236 C C . ALA AA 1 317 ? -25.674 18.277 48.716 1.0 45.92 ? ? ? ? ? ? 434 ALA AA C 1 317 A A +ATOM 5237 O O . ALA AA 1 317 ? -25.980 18.764 47.626 1.0 57.7 ? ? ? ? ? ? 434 ALA AA O 1 317 A A +ATOM 5238 C CB . ALA AA 1 317 ? -27.004 18.198 50.835 1.0 50.7 ? ? ? ? ? ? 434 ALA AA CB 1 317 A A +ATOM 5239 N N . ASP AA 1 318 ? -24.469 18.419 49.260 1.0 39.05 ? ? ? ? ? ? 435 ASP AA N 1 318 A A +ATOM 5240 C CA . ASP AA 1 318 ? -23.410 19.166 48.593 1.0 44.06 ? ? ? ? ? ? 435 ASP AA CA 1 318 A A +ATOM 5241 C C . ASP AA 1 318 ? -23.151 18.592 47.208 1.0 51.97 ? ? ? ? ? ? 435 ASP AA C 1 318 A A +ATOM 5242 O O . ASP AA 1 318 ? -23.047 19.333 46.232 1.0 49.25 ? ? ? ? ? ? 435 ASP AA O 1 318 A A +ATOM 5243 C CB . ASP AA 1 318 ? -22.120 19.109 49.419 1.0 65.86 ? ? ? ? ? ? 435 ASP AA CB 1 318 A A +ATOM 5244 C CG . ASP AA 1 318 ? -22.290 19.693 50.809 1.0 82.38 ? ? ? ? ? ? 435 ASP AA CG 1 318 A A +ATOM 5245 O OD1 . ASP AA 1 318 ? -22.971 20.731 50.938 1.0 85.74 ? ? ? ? ? ? 435 ASP AA OD1 1 318 A A +ATOM 5246 O OD2 . ASP AA 1 318 ? -21.743 19.113 51.772 1.0 100.0 ? ? ? ? ? ? 435 ASP AA OD2 1 318 A A +ATOM 5247 N N . SER AA 1 319 ? -23.050 17.268 47.129 1.0 46.23 ? ? ? ? ? ? 436 SER AA N 1 319 A A +ATOM 5248 C CA . SER AA 1 319 ? -22.800 16.595 45.858 1.0 40.37 ? ? ? ? ? ? 436 SER AA CA 1 319 A A +ATOM 5249 C C . SER AA 1 319 ? -23.836 16.979 44.816 1.0 35.36 ? ? ? ? ? ? 436 SER AA C 1 319 A A +ATOM 5250 O O . SER AA 1 319 ? -23.492 17.321 43.687 1.0 27.25 ? ? ? ? ? ? 436 SER AA O 1 319 A A +ATOM 5251 C CB . SER AA 1 319 ? -22.815 15.077 46.035 1.0 40.94 ? ? ? ? ? ? 436 SER AA CB 1 319 A A +ATOM 5252 O OG . SER AA 1 319 ? -22.697 14.426 44.780 1.0 18.64 ? ? ? ? ? ? 436 SER AA OG 1 319 A A +ATOM 5253 N N . ILE AA 1 320 ? -25.106 16.903 45.195 1.0 43.24 ? ? ? ? ? ? 437 ILE AA N 1 320 A A +ATOM 5254 C CA . ILE AA 1 320 ? -26.190 17.252 44.284 1.0 35.72 ? ? ? ? ? ? 437 ILE AA CA 1 320 A A +ATOM 5255 C C . ILE AA 1 320 ? -26.085 18.724 43.917 1.0 25.6 ? ? ? ? ? ? 437 ILE AA C 1 320 A A +ATOM 5256 O O . ILE AA 1 320 ? -25.980 19.084 42.745 1.0 31.76 ? ? ? ? ? ? 437 ILE AA O 1 320 A A +ATOM 5257 C CB . ILE AA 1 320 ? -27.577 17.008 44.932 1.0 45.25 ? ? ? ? ? ? 437 ILE AA CB 1 320 A A +ATOM 5258 C CG1 . ILE AA 1 320 ? -27.613 15.627 45.590 1.0 47.42 ? ? ? ? ? ? 437 ILE AA CG1 1 320 A A +ATOM 5259 C CG2 . ILE AA 1 320 ? -28.680 17.113 43.875 1.0 52.02 ? ? ? ? ? ? 437 ILE AA CG2 1 320 A A +ATOM 5260 C CD1 . ILE AA 1 320 ? -28.919 15.306 46.270 1.0 59.4 ? ? ? ? ? ? 437 ILE AA CD1 1 320 A A +ATOM 5261 N N . ASN AA 1 321 ? -26.113 19.568 44.941 1.0 25.65 ? ? ? ? ? ? 438 ASN AA N 1 321 A A +ATOM 5262 C CA . ASN AA 1 321 ? -26.028 21.010 44.772 1.0 29.75 ? ? ? ? ? ? 438 ASN AA CA 1 321 A A +ATOM 5263 C C . ASN AA 1 321 ? -24.921 21.408 43.797 1.0 29.52 ? ? ? ? ? ? 438 ASN AA C 1 321 A A +ATOM 5264 O O . ASN AA 1 321 ? -25.067 22.363 43.035 1.0 40.32 ? ? ? ? ? ? 438 ASN AA O 1 321 A A +ATOM 5265 C CB . ASN AA 1 321 ? -25.796 21.668 46.134 1.0 22.2 ? ? ? ? ? ? 438 ASN AA CB 1 321 A A +ATOM 5266 C CG . ASN AA 1 321 ? -25.876 23.177 46.075 1.0 43.18 ? ? ? ? ? ? 438 ASN AA CG 1 321 A A +ATOM 5267 O OD1 . ASN AA 1 321 ? -26.963 23.753 46.027 1.0 53.6 ? ? ? ? ? ? 438 ASN AA OD1 1 321 A A +ATOM 5268 N ND2 . ASN AA 1 321 ? -24.721 23.828 46.081 1.0 75.69 ? ? ? ? ? ? 438 ASN AA ND2 1 321 A A +ATOM 5269 N N . SER AA 1 322 ? -23.818 20.667 43.823 1.0 26.55 ? ? ? ? ? ? 439 SER AA N 1 322 A A +ATOM 5270 C CA . SER AA 1 322 ? -22.689 20.953 42.948 1.0 30.2 ? ? ? ? ? ? 439 SER AA CA 1 322 A A +ATOM 5271 C C . SER AA 1 322 ? -22.969 20.553 41.504 1.0 33.18 ? ? ? ? ? ? 439 SER AA C 1 322 A A +ATOM 5272 O O . SER AA 1 322 ? -22.930 21.383 40.598 1.0 40.71 ? ? ? ? ? ? 439 SER AA O 1 322 A A +ATOM 5273 C CB . SER AA 1 322 ? -21.447 20.213 43.445 1.0 42.46 ? ? ? ? ? ? 439 SER AA CB 1 322 A A +ATOM 5274 O OG . SER AA 1 322 ? -20.281 20.646 42.764 1.0 54.88 ? ? ? ? ? ? 439 SER AA OG 1 322 A A +ATOM 5275 N N . GLU AA 1 323 ? -23.245 19.269 41.307 1.0 44.97 ? ? ? ? ? ? 440 GLU AA N 1 323 A A +ATOM 5276 C CA . GLU AA 1 323 ? -23.522 18.706 39.992 1.0 53.35 ? ? ? ? ? ? 440 GLU AA CA 1 323 A A +ATOM 5277 C C . GLU AA 1 323 ? -24.530 19.504 39.173 1.0 58.79 ? ? ? ? ? ? 440 GLU AA C 1 323 A A +ATOM 5278 O O . GLU AA 1 323 ? -24.366 19.674 37.964 1.0 53.68 ? ? ? ? ? ? 440 GLU AA O 1 323 A A +ATOM 5279 C CB . GLU AA 1 323 ? -24.013 17.269 40.157 1.0 60.44 ? ? ? ? ? ? 440 GLU AA CB 1 323 A A +ATOM 5280 C CG . GLU AA 1 323 ? -22.910 16.288 40.492 1.0 64.52 ? ? ? ? ? ? 440 GLU AA CG 1 323 A A +ATOM 5281 C CD . GLU AA 1 323 ? -22.399 15.570 39.263 1.0 89.45 ? ? ? ? ? ? 440 GLU AA CD 1 323 A A +ATOM 5282 O OE1 . GLU AA 1 323 ? -22.810 15.951 38.145 1.0 100.0 ? ? ? ? ? ? 440 GLU AA OE1 1 323 A A +ATOM 5283 O OE2 . GLU AA 1 323 ? -21.593 14.625 39.411 1.0 88.09 ? ? ? ? ? ? 440 GLU AA OE2 1 323 A A +ATOM 5284 N N . ILE AA 1 324 ? -25.574 19.987 39.837 1.0 59.7 ? ? ? ? ? ? 441 ILE AA N 1 324 A A +ATOM 5285 C CA . ILE AA 1 324 ? -26.614 20.759 39.171 1.0 60.5 ? ? ? ? ? ? 441 ILE AA CA 1 324 A A +ATOM 5286 C C . ILE AA 1 324 ? -26.119 22.096 38.623 1.0 64.02 ? ? ? ? ? ? 441 ILE AA C 1 324 A A +ATOM 5287 O O . ILE AA 1 324 ? -26.420 22.446 37.481 1.0 77.13 ? ? ? ? ? ? 441 ILE AA O 1 324 A A +ATOM 5288 C CB . ILE AA 1 324 ? -27.808 21.026 40.113 1.0 58.83 ? ? ? ? ? ? 441 ILE AA CB 1 324 A A +ATOM 5289 C CG1 . ILE AA 1 324 ? -28.949 21.663 39.322 1.0 47.01 ? ? ? ? ? ? 441 ILE AA CG1 1 324 A A +ATOM 5290 C CG2 . ILE AA 1 324 ? -27.392 21.936 41.258 1.0 65.37 ? ? ? ? ? ? 441 ILE AA CG2 1 324 A A +ATOM 5291 C CD1 . ILE AA 1 324 ? -29.574 20.736 38.315 1.0 35.89 ? ? ? ? ? ? 441 ILE AA CD1 1 324 A A +ATOM 5292 N N . GLY AA 1 325 ? -25.372 22.840 39.436 1.0 49.58 ? ? ? ? ? ? 442 GLY AA N 1 325 A A +ATOM 5293 C CA . GLY AA 1 325 ? -24.858 24.123 38.989 1.0 55.28 ? ? ? ? ? ? 442 GLY AA CA 1 325 A A +ATOM 5294 C C . GLY AA 1 325 ? -24.021 23.972 37.732 1.0 54.37 ? ? ? ? ? ? 442 GLY AA C 1 325 A A +ATOM 5295 O O . GLY AA 1 325 ? -24.056 24.817 36.835 1.0 52.7 ? ? ? ? ? ? 442 GLY AA O 1 325 A A +ATOM 5296 N N . ILE AA 1 326 ? -23.255 22.889 37.677 1.0 54.9 ? ? ? ? ? ? 443 ILE AA N 1 326 A A +ATOM 5297 C CA . ILE AA 1 326 ? -22.409 22.603 36.530 1.0 51.18 ? ? ? ? ? ? 443 ILE AA CA 1 326 A A +ATOM 5298 C C . ILE AA 1 326 ? -23.316 22.263 35.356 1.0 53.49 ? ? ? ? ? ? 443 ILE AA C 1 326 A A +ATOM 5299 O O . ILE AA 1 326 ? -23.041 22.638 34.218 1.0 50.05 ? ? ? ? ? ? 443 ILE AA O 1 326 A A +ATOM 5300 C CB . ILE AA 1 326 ? -21.468 21.415 36.823 1.0 48.17 ? ? ? ? ? ? 443 ILE AA CB 1 326 A A +ATOM 5301 C CG1 . ILE AA 1 326 ? -20.277 21.891 37.663 1.0 49.81 ? ? ? ? ? ? 443 ILE AA CG1 1 326 A A +ATOM 5302 C CG2 . ILE AA 1 326 ? -20.978 20.799 35.524 1.0 55.24 ? ? ? ? ? ? 443 ILE AA CG2 1 326 A A +ATOM 5303 C CD1 . ILE AA 1 326 ? -20.661 22.608 38.951 1.0 50.65 ? ? ? ? ? ? 443 ILE AA CD1 1 326 A A +ATOM 5304 N N . LEU AA 1 327 ? -24.397 21.543 35.653 1.0 43.2 ? ? ? ? ? ? 444 LEU AA N 1 327 A A +ATOM 5305 C CA . LEU AA 1 327 ? -25.383 21.158 34.651 1.0 32.45 ? ? ? ? ? ? 444 LEU AA CA 1 327 A A +ATOM 5306 C C . LEU AA 1 327 ? -25.998 22.450 34.128 1.0 45.17 ? ? ? ? ? ? 444 LEU AA C 1 327 A A +ATOM 5307 O O . LEU AA 1 327 ? -26.461 22.517 32.990 1.0 49.34 ? ? ? ? ? ? 444 LEU AA O 1 327 A A +ATOM 5308 C CB . LEU AA 1 327 ? -26.464 20.277 35.285 1.0 26.2 ? ? ? ? ? ? 444 LEU AA CB 1 327 A A +ATOM 5309 C CG . LEU AA 1 327 ? -27.500 19.595 34.382 1.0 15.2 ? ? ? ? ? ? 444 LEU AA CG 1 327 A A +ATOM 5310 C CD1 . LEU AA 1 327 ? -28.641 20.543 34.103 1.0 28.5 ? ? ? ? ? ? 444 LEU AA CD1 1 327 A A +ATOM 5311 C CD2 . LEU AA 1 327 ? -26.852 19.144 33.094 1.0 24.79 ? ? ? ? ? ? 444 LEU AA CD2 1 327 A A +ATOM 5312 N N . CYS AA 1 328 ? -25.982 23.475 34.976 1.0 37.67 ? ? ? ? ? ? 445 CYS AA N 1 328 A A +ATOM 5313 C CA . CYS AA 1 328 ? -26.508 24.787 34.625 1.0 47.14 ? ? ? ? ? ? 445 CYS AA CA 1 328 A A +ATOM 5314 C C . CYS AA 1 328 ? -25.529 25.470 33.677 1.0 58.91 ? ? ? ? ? ? 445 CYS AA C 1 328 A A +ATOM 5315 O O . CYS AA 1 328 ? -25.912 25.957 32.612 1.0 68.68 ? ? ? ? ? ? 445 CYS AA O 1 328 A A +ATOM 5316 C CB . CYS AA 1 328 ? -26.684 25.644 35.879 1.0 36.14 ? ? ? ? ? ? 445 CYS AA CB 1 328 A A +ATOM 5317 S SG . CYS AA 1 328 ? -28.341 25.599 36.577 1.0 51.83 ? ? ? ? ? ? 445 CYS AA SG 1 328 A A +ATOM 5318 N N . SER AA 1 329 ? -24.260 25.494 34.069 1.0 55.38 ? ? ? ? ? ? 446 SER AA N 1 329 A A +ATOM 5319 C CA . SER AA 1 329 ? -23.223 26.115 33.256 1.0 49.49 ? ? ? ? ? ? 446 SER AA CA 1 329 A A +ATOM 5320 C C . SER AA 1 329 ? -23.093 25.404 31.916 1.0 48.41 ? ? ? ? ? ? 446 SER AA C 1 329 A A +ATOM 5321 O O . SER AA 1 329 ? -22.922 26.043 30.876 1.0 41.89 ? ? ? ? ? ? 446 SER AA O 1 329 A A +ATOM 5322 C CB . SER AA 1 329 ? -21.889 26.071 33.995 1.0 31.22 ? ? ? ? ? ? 446 SER AA CB 1 329 A A +ATOM 5323 O OG . SER AA 1 329 ? -21.998 26.690 35.265 1.0 49.48 ? ? ? ? ? ? 446 SER AA OG 1 329 A A +ATOM 5324 N N . ALA AA 1 330 ? -23.164 24.077 31.949 1.0 46.09 ? ? ? ? ? ? 447 ALA AA N 1 330 A A +ATOM 5325 C CA . ALA AA 1 330 ? -23.067 23.269 30.737 1.0 42.91 ? ? ? ? ? ? 447 ALA AA CA 1 330 A A +ATOM 5326 C C . ALA AA 1 330 ? -24.112 23.717 29.713 1.0 51.1 ? ? ? ? ? ? 447 ALA AA C 1 330 A A +ATOM 5327 O O . ALA AA 1 330 ? -23.818 23.866 28.527 1.0 44.02 ? ? ? ? ? ? 447 ALA AA O 1 330 A A +ATOM 5328 C CB . ALA AA 1 330 ? -23.267 21.796 31.077 1.0 48.36 ? ? ? ? ? ? 447 ALA AA CB 1 330 A A +ATOM 5329 N N . LEU AA 1 331 ? -25.332 23.938 30.186 1.0 57.01 ? ? ? ? ? ? 448 LEU AA N 1 331 A A +ATOM 5330 C CA . LEU AA 1 331 ? -26.424 24.365 29.322 1.0 52.65 ? ? ? ? ? ? 448 LEU AA CA 1 331 A A +ATOM 5331 C C . LEU AA 1 331 ? -26.136 25.719 28.684 1.0 52.29 ? ? ? ? ? ? 448 LEU AA C 1 331 A A +ATOM 5332 O O . LEU AA 1 331 ? -26.368 25.913 27.492 1.0 54.42 ? ? ? ? ? ? 448 LEU AA O 1 331 A A +ATOM 5333 C CB . LEU AA 1 331 ? -27.727 24.448 30.122 1.0 43.89 ? ? ? ? ? ? 448 LEU AA CB 1 331 A A +ATOM 5334 C CG . LEU AA 1 331 ? -28.356 23.122 30.560 1.0 37.47 ? ? ? ? ? ? 448 LEU AA CG 1 331 A A +ATOM 5335 C CD1 . LEU AA 1 331 ? -29.563 23.409 31.422 1.0 28.39 ? ? ? ? ? ? 448 LEU AA CD1 1 331 A A +ATOM 5336 C CD2 . LEU AA 1 331 ? -28.756 22.302 29.353 1.0 21.1 ? ? ? ? ? ? 448 LEU AA CD2 1 331 A A +ATOM 5337 N N . GLN AA 1 332 ? -25.630 26.648 29.485 1.0 60.96 ? ? ? ? ? ? 449 GLN AA N 1 332 A A +ATOM 5338 C CA . GLN AA 1 332 ? -25.328 27.996 29.013 1.0 82.15 ? ? ? ? ? ? 449 GLN AA CA 1 332 A A +ATOM 5339 C C . GLN AA 1 332 ? -24.447 28.080 27.762 1.0 92.63 ? ? ? ? ? ? 449 GLN AA C 1 332 A A +ATOM 5340 O O . GLN AA 1 332 ? -24.773 28.796 26.815 1.0 94.93 ? ? ? ? ? ? 449 GLN AA O 1 332 A A +ATOM 5341 C CB . GLN AA 1 332 ? -24.687 28.801 30.144 1.0 83.67 ? ? ? ? ? ? 449 GLN AA CB 1 332 A A +ATOM 5342 C CG . GLN AA 1 332 ? -25.597 28.993 31.339 1.0 92.3 ? ? ? ? ? ? 449 GLN AA CG 1 332 A A +ATOM 5343 C CD . GLN AA 1 332 ? -26.985 29.445 30.933 1.0 100.0 ? ? ? ? ? ? 449 GLN AA CD 1 332 A A +ATOM 5344 O OE1 . GLN AA 1 332 ? -27.143 30.472 30.276 1.0 100.0 ? ? ? ? ? ? 449 GLN AA OE1 1 332 A A +ATOM 5345 N NE2 . GLN AA 1 332 ? -27.998 28.674 31.314 1.0 96.42 ? ? ? ? ? ? 449 GLN AA NE2 1 332 A A +ATOM 5346 N N . LYS AA 1 333 ? -23.330 27.359 27.760 1.0 91.95 ? ? ? ? ? ? 450 LYS AA N 1 333 A A +ATOM 5347 C CA . LYS AA 1 333 ? -22.416 27.390 26.621 1.0 93.47 ? ? ? ? ? ? 450 LYS AA CA 1 333 A A +ATOM 5348 C C . LYS AA 1 333 ? -22.952 26.636 25.405 1.0 93.85 ? ? ? ? ? ? 450 LYS AA C 1 333 A A +ATOM 5349 O O . LYS AA 1 333 ? -22.640 26.985 24.264 1.0 94.86 ? ? ? ? ? ? 450 LYS AA O 1 333 A A +ATOM 5350 C CB . LYS AA 1 333 ? -21.054 26.821 27.024 1.0 90.11 ? ? ? ? ? ? 450 LYS AA CB 1 333 A A +ATOM 5351 C CG . LYS AA 1 333 ? -21.128 25.518 27.791 1.0 100.0 ? ? ? ? ? ? 450 LYS AA CG 1 333 A A +ATOM 5352 C CD . LYS AA 1 333 ? -19.800 25.203 28.461 1.0 100.0 ? ? ? ? ? ? 450 LYS AA CD 1 333 A A +ATOM 5353 C CE . LYS AA 1 333 ? -19.937 24.000 29.377 1.0 100.0 ? ? ? ? ? ? 450 LYS AA CE 1 333 A A +ATOM 5354 N NZ . LYS AA 1 333 ? -18.659 23.626 30.032 1.0 93.35 ? ? ? ? ? ? 450 LYS AA NZ 1 333 A A +ATOM 5355 N N . ILE AA 1 334 ? -23.758 25.608 25.648 1.0 95.0 ? ? ? ? ? ? 451 ILE AA N 1 334 A A +ATOM 5356 C CA . ILE AA 1 334 ? -24.333 24.821 24.566 1.0 89.19 ? ? ? ? ? ? 451 ILE AA CA 1 334 A A +ATOM 5357 C C . ILE AA 1 334 ? -25.540 25.552 23.971 1.0 90.74 ? ? ? ? ? ? 451 ILE AA C 1 334 A A +ATOM 5358 O O . ILE AA 1 334 ? -26.425 24.942 23.371 1.0 83.74 ? ? ? ? ? ? 451 ILE AA O 1 334 A A +ATOM 5359 C CB . ILE AA 1 334 ? -24.746 23.401 25.063 1.0 86.0 ? ? ? ? ? ? 451 ILE AA CB 1 334 A A +ATOM 5360 C CG1 . ILE AA 1 334 ? -24.745 22.419 23.889 1.0 82.61 ? ? ? ? ? ? 451 ILE AA CG1 1 334 A A +ATOM 5361 C CG2 . ILE AA 1 334 ? -26.109 23.448 25.738 1.0 67.45 ? ? ? ? ? ? 451 ILE AA CG2 1 334 A A +ATOM 5362 C CD1 . ILE AA 1 334 ? -24.590 20.973 24.308 1.0 62.56 ? ? ? ? ? ? 451 ILE AA CD1 1 334 A A +ATOM 5363 N N . LYS AA 1 335 ? -25.561 26.871 24.148 1.0 92.93 ? ? ? ? ? ? 452 LYS AA N 1 335 A A +ATOM 5364 C CA . LYS AA 1 335 ? -26.625 27.732 23.633 1.0 99.91 ? ? ? ? ? ? 452 LYS AA CA 1 335 A A +ATOM 5365 C C . LYS AA 1 335 ? -28.045 27.406 24.110 1.0 100.0 ? ? ? ? ? ? 452 LYS AA C 1 335 A A +ATOM 5366 O O . LYS AA 1 335 ? -28.941 28.246 23.860 1.0 100.0 ? ? ? ? ? ? 452 LYS AA O 1 335 A A +ATOM 5367 C CB . LYS AA 1 335 ? -26.589 27.732 22.103 1.0 94.91 ? ? ? ? ? ? 452 LYS AA CB 1 335 A A +ATOM 5368 C CG . LYS AA 1 335 ? -25.610 28.729 21.518 1.0 87.47 ? ? ? ? ? ? 452 LYS AA CG 1 335 A A +ATOM 5369 C CD . LYS AA 1 335 ? -26.097 30.154 21.718 1.0 100.0 ? ? ? ? ? ? 452 LYS AA CD 1 335 A A +ATOM 5370 C CE . LYS AA 1 335 ? -25.049 31.159 21.268 1.0 99.94 ? ? ? ? ? ? 452 LYS AA CE 1 335 A A +ATOM 5371 N NZ . LYS AA 1 335 ? -23.917 31.233 22.232 1.0 100.0 ? ? ? ? ? ? 452 LYS AA NZ 1 335 A A +ATOM 5372 O OXT . LYS AA 1 335 ? -28.250 26.333 24.718 1.0 100.0 ? ? ? ? ? ? 452 LYS AA OXT 1 335 A A +ATOM 5373 N N . VAL B 1 1 ? -36.614 36.412 66.929 1.0 64.02 ? ? ? ? ? ? 118 VAL B N 1 1 B B +ATOM 5374 C CA . VAL B 1 1 ? -36.683 36.375 65.439 1.0 64.44 ? ? ? ? ? ? 118 VAL B CA 1 1 B B +ATOM 5375 C C . VAL B 1 1 ? -37.879 37.172 64.918 1.0 65.24 ? ? ? ? ? ? 118 VAL B C 1 1 B B +ATOM 5376 O O . VAL B 1 1 ? -39.025 36.909 65.293 1.0 63.74 ? ? ? ? ? ? 118 VAL B O 1 1 B B +ATOM 5377 C CB . VAL B 1 1 ? -36.803 34.928 64.931 1.0 65.74 ? ? ? ? ? ? 118 VAL B CB 1 1 B B +ATOM 5378 C CG1 . VAL B 1 1 ? -36.946 34.919 63.419 1.0 65.62 ? ? ? ? ? ? 118 VAL B CG1 1 1 B B +ATOM 5379 C CG2 . VAL B 1 1 ? -35.583 34.137 65.352 1.0 53.75 ? ? ? ? ? ? 118 VAL B CG2 1 1 B B +ATOM 5380 N N . PRO B 1 2 ? -37.626 38.140 64.017 1.0 55.61 ? ? ? ? ? ? 119 PRO B N 1 2 B B +ATOM 5381 C CA . PRO B 1 2 ? -38.696 38.972 63.454 1.0 61.71 ? ? ? ? ? ? 119 PRO B CA 1 2 B B +ATOM 5382 C C . PRO B 1 2 ? -39.839 38.152 62.887 1.0 64.92 ? ? ? ? ? ? 119 PRO B C 1 2 B B +ATOM 5383 O O . PRO B 1 2 ? -39.633 37.043 62.402 1.0 81.22 ? ? ? ? ? ? 119 PRO B O 1 2 B B +ATOM 5384 C CB . PRO B 1 2 ? -37.995 39.787 62.370 1.0 49.01 ? ? ? ? ? ? 119 PRO B CB 1 2 B B +ATOM 5385 C CG . PRO B 1 2 ? -36.563 39.771 62.741 1.0 55.79 ? ? ? ? ? ? 119 PRO B CG 1 2 B B +ATOM 5386 C CD . PRO B 1 2 ? -36.310 38.478 63.453 1.0 51.02 ? ? ? ? ? ? 119 PRO B CD 1 2 B B +ATOM 5387 N N . TRP B 1 3 ? -41.044 38.708 62.940 1.0 64.84 ? ? ? ? ? ? 120 TRP B N 1 3 B B +ATOM 5388 C CA . TRP B 1 3 ? -42.219 38.024 62.413 1.0 62.46 ? ? ? ? ? ? 120 TRP B CA 1 3 B B +ATOM 5389 C C . TRP B 1 3 ? -42.288 38.207 60.901 1.0 69.96 ? ? ? ? ? ? 120 TRP B C 1 3 B B +ATOM 5390 O O . TRP B 1 3 ? -41.996 39.285 60.382 1.0 76.89 ? ? ? ? ? ? 120 TRP B O 1 3 B B +ATOM 5391 C CB . TRP B 1 3 ? -43.497 38.580 63.050 1.0 59.09 ? ? ? ? ? ? 120 TRP B CB 1 3 B B +ATOM 5392 C CG . TRP B 1 3 ? -44.761 38.047 62.432 1.0 48.35 ? ? ? ? ? ? 120 TRP B CG 1 3 B B +ATOM 5393 C CD1 . TRP B 1 3 ? -45.516 37.005 62.883 1.0 34.32 ? ? ? ? ? ? 120 TRP B CD1 1 3 B B +ATOM 5394 C CD2 . TRP B 1 3 ? -45.403 38.520 61.240 1.0 46.82 ? ? ? ? ? ? 120 TRP B CD2 1 3 B B +ATOM 5395 N NE1 . TRP B 1 3 ? -46.592 36.803 62.051 1.0 51.44 ? ? ? ? ? ? 120 TRP B NE1 1 3 B B +ATOM 5396 C CE2 . TRP B 1 3 ? -46.546 37.719 61.033 1.0 51.56 ? ? ? ? ? ? 120 TRP B CE2 1 3 B B +ATOM 5397 C CE3 . TRP B 1 3 ? -45.128 39.552 60.330 1.0 33.47 ? ? ? ? ? ? 120 TRP B CE3 1 3 B B +ATOM 5398 C CZ2 . TRP B 1 3 ? -47.416 37.913 59.953 1.0 52.85 ? ? ? ? ? ? 120 TRP B CZ2 1 3 B B +ATOM 5399 C CZ3 . TRP B 1 3 ? -45.989 39.742 59.252 1.0 52.35 ? ? ? ? ? ? 120 TRP B CZ3 1 3 B B +ATOM 5400 C CH2 . TRP B 1 3 ? -47.118 38.924 59.073 1.0 61.87 ? ? ? ? ? ? 120 TRP B CH2 1 3 B B +ATOM 5401 N N . PHE B 1 4 ? -42.671 37.143 60.203 1.0 63.41 ? ? ? ? ? ? 121 PHE B N 1 4 B B +ATOM 5402 C CA . PHE B 1 4 ? -42.801 37.182 58.752 1.0 55.67 ? ? ? ? ? ? 121 PHE B CA 1 4 B B +ATOM 5403 C C . PHE B 1 4 ? -44.044 36.412 58.299 1.0 55.41 ? ? ? ? ? ? 121 PHE B C 1 4 B B +ATOM 5404 O O . PHE B 1 4 ? -44.474 35.453 58.951 1.0 47.46 ? ? ? ? ? ? 121 PHE B O 1 4 B B +ATOM 5405 C CB . PHE B 1 4 ? -41.544 36.607 58.083 1.0 69.65 ? ? ? ? ? ? 121 PHE B CB 1 4 B B +ATOM 5406 C CG . PHE B 1 4 ? -41.293 35.159 58.391 1.0 69.25 ? ? ? ? ? ? 121 PHE B CG 1 4 B B +ATOM 5407 C CD1 . PHE B 1 4 ? -41.925 34.160 57.658 1.0 68.38 ? ? ? ? ? ? 121 PHE B CD1 1 4 B B +ATOM 5408 C CD2 . PHE B 1 4 ? -40.413 34.794 59.403 1.0 67.23 ? ? ? ? ? ? 121 PHE B CD2 1 4 B B +ATOM 5409 C CE1 . PHE B 1 4 ? -41.687 32.818 57.927 1.0 65.36 ? ? ? ? ? ? 121 PHE B CE1 1 4 B B +ATOM 5410 C CE2 . PHE B 1 4 ? -40.168 33.454 59.681 1.0 80.74 ? ? ? ? ? ? 121 PHE B CE2 1 4 B B +ATOM 5411 C CZ . PHE B 1 4 ? -40.807 32.463 58.941 1.0 63.51 ? ? ? ? ? ? 121 PHE B CZ 1 4 B B +ATOM 5412 N N . PRO B 1 5 ? -44.642 36.832 57.170 1.0 45.57 ? ? ? ? ? ? 122 PRO B N 1 5 B B +ATOM 5413 C CA . PRO B 1 5 ? -45.843 36.181 56.627 1.0 40.03 ? ? ? ? ? ? 122 PRO B CA 1 5 B B +ATOM 5414 C C . PRO B 1 5 ? -45.626 34.738 56.170 1.0 48.47 ? ? ? ? ? ? 122 PRO B C 1 5 B B +ATOM 5415 O O . PRO B 1 5 ? -44.685 34.438 55.434 1.0 63.33 ? ? ? ? ? ? 122 PRO B O 1 5 B B +ATOM 5416 C CB . PRO B 1 5 ? -46.256 37.093 55.471 1.0 34.57 ? ? ? ? ? ? 122 PRO B CB 1 5 B B +ATOM 5417 C CG . PRO B 1 5 ? -45.005 37.797 55.088 1.0 38.44 ? ? ? ? ? ? 122 PRO B CG 1 5 B B +ATOM 5418 C CD . PRO B 1 5 ? -44.204 37.963 56.336 1.0 36.86 ? ? ? ? ? ? 122 PRO B CD 1 5 B B +ATOM 5419 N N . ARG B 1 6 ? -46.502 33.848 56.620 1.0 46.91 ? ? ? ? ? ? 123 ARG B N 1 6 B B +ATOM 5420 C CA . ARG B 1 6 ? -46.426 32.444 56.245 1.0 55.38 ? ? ? ? ? ? 123 ARG B CA 1 6 B B +ATOM 5421 C C . ARG B 1 6 ? -47.319 32.221 55.031 1.0 60.11 ? ? ? ? ? ? 123 ARG B C 1 6 B B +ATOM 5422 O O . ARG B 1 6 ? -47.008 31.409 54.163 1.0 74.63 ? ? ? ? ? ? 123 ARG B O 1 6 B B +ATOM 5423 C CB . ARG B 1 6 ? -46.893 31.558 57.403 1.0 82.66 ? ? ? ? ? ? 123 ARG B CB 1 6 B B +ATOM 5424 C CG . ARG B 1 6 ? -46.173 31.816 58.718 1.0 92.03 ? ? ? ? ? ? 123 ARG B CG 1 6 B B +ATOM 5425 C CD . ARG B 1 6 ? -44.746 31.300 58.673 1.0 83.78 ? ? ? ? ? ? 123 ARG B CD 1 6 B B +ATOM 5426 N NE . ARG B 1 6 ? -44.225 31.035 60.009 1.0 86.12 ? ? ? ? ? ? 123 ARG B NE 1 6 B B +ATOM 5427 C CZ . ARG B 1 6 ? -44.307 29.859 60.624 1.0 100.0 ? ? ? ? ? ? 123 ARG B CZ 1 6 B B +ATOM 5428 N NH1 . ARG B 1 6 ? -44.893 28.830 60.025 1.0 90.04 ? ? ? ? ? ? 123 ARG B NH1 1 6 B B +ATOM 5429 N NH2 . ARG B 1 6 ? -43.805 29.714 61.844 1.0 100.0 ? ? ? ? ? ? 123 ARG B NH2 1 6 B B +ATOM 5430 N N . THR B 1 7 ? -48.430 32.952 54.980 1.0 58.91 ? ? ? ? ? ? 124 THR B N 1 7 B B +ATOM 5431 C CA . THR B 1 7 ? -49.378 32.847 53.873 1.0 55.42 ? ? ? ? ? ? 124 THR B CA 1 7 B B +ATOM 5432 C C . THR B 1 7 ? -49.408 34.137 53.074 1.0 55.81 ? ? ? ? ? ? 124 THR B C 1 7 B B +ATOM 5433 O O . THR B 1 7 ? -49.051 35.204 53.576 1.0 56.63 ? ? ? ? ? ? 124 THR B O 1 7 B B +ATOM 5434 C CB . THR B 1 7 ? -50.814 32.576 54.357 1.0 49.31 ? ? ? ? ? ? 124 THR B CB 1 7 B B +ATOM 5435 O OG1 . THR B 1 7 ? -50.805 31.528 55.330 1.0 60.93 ? ? ? ? ? ? 124 THR B OG1 1 7 B B +ATOM 5436 C CG2 . THR B 1 7 ? -51.693 32.157 53.191 1.0 53.17 ? ? ? ? ? ? 124 THR B CG2 1 7 B B +ATOM 5437 N N . ILE B 1 8 ? -49.851 34.024 51.827 1.0 55.49 ? ? ? ? ? ? 125 ILE B N 1 8 B B +ATOM 5438 C CA . ILE B 1 8 ? -49.943 35.159 50.921 1.0 57.08 ? ? ? ? ? ? 125 ILE B CA 1 8 B B +ATOM 5439 C C . ILE B 1 8 ? -50.985 36.161 51.412 1.0 63.27 ? ? ? ? ? ? 125 ILE B C 1 8 B B +ATOM 5440 O O . ILE B 1 8 ? -50.861 37.365 51.181 1.0 54.52 ? ? ? ? ? ? 125 ILE B O 1 8 B B +ATOM 5441 C CB . ILE B 1 8 ? -50.322 34.688 49.498 1.0 50.66 ? ? ? ? ? ? 125 ILE B CB 1 8 B B +ATOM 5442 C CG1 . ILE B 1 8 ? -50.192 35.844 48.506 1.0 33.1 ? ? ? ? ? ? 125 ILE B CG1 1 8 B B +ATOM 5443 C CG2 . ILE B 1 8 ? -51.742 34.137 49.496 1.0 37.48 ? ? ? ? ? ? 125 ILE B CG2 1 8 B B +ATOM 5444 C CD1 . ILE B 1 8 ? -49.939 35.399 47.075 1.0 60.02 ? ? ? ? ? ? 125 ILE B CD1 1 8 B B +ATOM 5445 N N . GLN B 1 9 ? -52.008 35.654 52.095 1.0 61.65 ? ? ? ? ? ? 126 GLN B N 1 9 B B +ATOM 5446 C CA . GLN B 1 9 ? -53.078 36.498 52.614 1.0 67.34 ? ? ? ? ? ? 126 GLN B CA 1 9 B B +ATOM 5447 C C . GLN B 1 9 ? -52.652 37.218 53.887 1.0 61.48 ? ? ? ? ? ? 126 GLN B C 1 9 B B +ATOM 5448 O O . GLN B 1 9 ? -53.331 38.133 54.349 1.0 71.35 ? ? ? ? ? ? 126 GLN B O 1 9 B B +ATOM 5449 C CB . GLN B 1 9 ? -54.319 35.651 52.897 1.0 70.45 ? ? ? ? ? ? 126 GLN B CB 1 9 B B +ATOM 5450 C CG . GLN B 1 9 ? -54.785 34.826 51.713 1.0 85.51 ? ? ? ? ? ? 126 GLN B CG 1 9 B B +ATOM 5451 C CD . GLN B 1 9 ? -54.438 33.359 51.854 1.0 92.67 ? ? ? ? ? ? 126 GLN B CD 1 9 B B +ATOM 5452 O OE1 . GLN B 1 9 ? -54.557 32.781 52.934 1.0 100.0 ? ? ? ? ? ? 126 GLN B OE1 1 9 B B +ATOM 5453 N NE2 . GLN B 1 9 ? -54.011 32.745 50.758 1.0 88.41 ? ? ? ? ? ? 126 GLN B NE2 1 9 B B +ATOM 5454 N N . GLU B 1 10 ? -51.526 36.794 54.451 1.0 55.05 ? ? ? ? ? ? 127 GLU B N 1 10 B B +ATOM 5455 C CA . GLU B 1 10 ? -51.008 37.389 55.677 1.0 54.75 ? ? ? ? ? ? 127 GLU B CA 1 10 B B +ATOM 5456 C C . GLU B 1 10 ? -50.348 38.739 55.434 1.0 57.03 ? ? ? ? ? ? 127 GLU B C 1 10 B B +ATOM 5457 O O . GLU B 1 10 ? -49.892 39.393 56.372 1.0 52.57 ? ? ? ? ? ? 127 GLU B O 1 10 B B +ATOM 5458 C CB . GLU B 1 10 ? -50.005 36.446 56.332 1.0 56.8 ? ? ? ? ? ? 127 GLU B CB 1 10 B B +ATOM 5459 C CG . GLU B 1 10 ? -50.618 35.145 56.811 1.0 59.86 ? ? ? ? ? ? 127 GLU B CG 1 10 B B +ATOM 5460 C CD . GLU B 1 10 ? -49.856 34.547 57.975 1.0 72.86 ? ? ? ? ? ? 127 GLU B CD 1 10 B B +ATOM 5461 O OE1 . GLU B 1 10 ? -48.714 34.996 58.223 1.0 78.5 ? ? ? ? ? ? 127 GLU B OE1 1 10 B B +ATOM 5462 O OE2 . GLU B 1 10 ? -50.400 33.636 58.640 1.0 70.93 ? ? ? ? ? ? 127 GLU B OE2 1 10 B B +ATOM 5463 N N . LEU B 1 11 ? -50.294 39.144 54.169 1.0 57.23 ? ? ? ? ? ? 128 LEU B N 1 11 B B +ATOM 5464 C CA . LEU B 1 11 ? -49.698 40.419 53.797 1.0 65.38 ? ? ? ? ? ? 128 LEU B CA 1 11 B B +ATOM 5465 C C . LEU B 1 11 ? -50.710 41.527 54.082 1.0 76.67 ? ? ? ? ? ? 128 LEU B C 1 11 B B +ATOM 5466 O O . LEU B 1 11 ? -50.436 42.715 53.873 1.0 82.72 ? ? ? ? ? ? 128 LEU B O 1 11 B B +ATOM 5467 C CB . LEU B 1 11 ? -49.333 40.422 52.309 1.0 61.86 ? ? ? ? ? ? 128 LEU B CB 1 11 B B +ATOM 5468 C CG . LEU B 1 11 ? -48.313 39.383 51.832 1.0 74.01 ? ? ? ? ? ? 128 LEU B CG 1 11 B B +ATOM 5469 C CD1 . LEU B 1 11 ? -48.101 39.521 50.335 1.0 63.92 ? ? ? ? ? ? 128 LEU B CD1 1 11 B B +ATOM 5470 C CD2 . LEU B 1 11 ? -47.002 39.571 52.570 1.0 76.84 ? ? ? ? ? ? 128 LEU B CD2 1 11 B B +ATOM 5471 N N . ASP B 1 12 ? -51.882 41.124 54.566 1.0 73.58 ? ? ? ? ? ? 129 ASP B N 1 12 B B +ATOM 5472 C CA . ASP B 1 12 ? -52.945 42.064 54.884 1.0 72.89 ? ? ? ? ? ? 129 ASP B CA 1 12 B B +ATOM 5473 C C . ASP B 1 12 ? -52.602 42.919 56.100 1.0 77.94 ? ? ? ? ? ? 129 ASP B C 1 12 B B +ATOM 5474 O O . ASP B 1 12 ? -53.401 43.745 56.531 1.0 91.15 ? ? ? ? ? ? 129 ASP B O 1 12 B B +ATOM 5475 C CB . ASP B 1 12 ? -54.255 41.312 55.128 1.0 66.61 ? ? ? ? ? ? 129 ASP B CB 1 12 B B +ATOM 5476 C CG . ASP B 1 12 ? -54.823 40.704 53.860 1.0 77.18 ? ? ? ? ? ? 129 ASP B CG 1 12 B B +ATOM 5477 O OD1 . ASP B 1 12 ? -54.396 41.108 52.756 1.0 70.03 ? ? ? ? ? ? 129 ASP B OD1 1 12 B B +ATOM 5478 O OD2 . ASP B 1 12 ? -55.697 39.822 53.972 1.0 78.15 ? ? ? ? ? ? 129 ASP B OD2 1 12 B B +ATOM 5479 N N . ARG B 1 13 ? -51.402 42.748 56.638 1.0 77.77 ? ? ? ? ? ? 130 ARG B N 1 13 B B +ATOM 5480 C CA . ARG B 1 13 ? -50.997 43.522 57.800 1.0 77.83 ? ? ? ? ? ? 130 ARG B CA 1 13 B B +ATOM 5481 C C . ARG B 1 13 ? -50.283 44.811 57.406 1.0 89.16 ? ? ? ? ? ? 130 ARG B C 1 13 B B +ATOM 5482 O O . ARG B 1 13 ? -50.054 45.024 56.196 1.0 93.49 ? ? ? ? ? ? 130 ARG B O 1 13 B B +ATOM 5483 C CB . ARG B 1 13 ? -50.092 42.680 58.697 1.0 79.04 ? ? ? ? ? ? 130 ARG B CB 1 13 B B +ATOM 5484 C CG . ARG B 1 13 ? -50.452 41.203 58.733 1.0 92.88 ? ? ? ? ? ? 130 ARG B CG 1 13 B B +ATOM 5485 C CD . ARG B 1 13 ? -51.939 40.986 58.965 1.0 93.62 ? ? ? ? ? ? 130 ARG B CD 1 13 B B +ATOM 5486 N NE . ARG B 1 13 ? -52.345 41.366 60.316 1.0 100.0 ? ? ? ? ? ? 130 ARG B NE 1 13 B B +ATOM 5487 C CZ . ARG B 1 13 ? -52.151 40.616 61.397 1.0 100.0 ? ? ? ? ? ? 130 ARG B CZ 1 13 B B +ATOM 5488 N NH1 . ARG B 1 13 ? -51.557 39.435 61.289 1.0 100.0 ? ? ? ? ? ? 130 ARG B NH1 1 13 B B +ATOM 5489 N NH2 . ARG B 1 13 ? -52.554 41.046 62.586 1.0 96.27 ? ? ? ? ? ? 130 ARG B NH2 1 13 B B +ATOM 5490 N N . ALA B 1 27 ? -43.683 69.602 53.885 1.0 87.98 ? ? ? ? ? ? 144 ALA B N 1 27 B B +ATOM 5491 C CA . ALA B 1 27 ? -44.210 70.629 52.943 1.0 85.44 ? ? ? ? ? ? 144 ALA B CA 1 27 B B +ATOM 5492 C C . ALA B 1 27 ? -43.355 70.716 51.686 1.0 93.15 ? ? ? ? ? ? 144 ALA B C 1 27 B B +ATOM 5493 O O . ALA B 1 27 ? -43.809 71.203 50.650 1.0 100.0 ? ? ? ? ? ? 144 ALA B O 1 27 B B +ATOM 5494 C CB . ALA B 1 27 ? -44.261 71.989 53.627 1.0 82.44 ? ? ? ? ? ? 144 ALA B CB 1 27 B B +ATOM 5495 N N . ASP B 1 28 ? -42.115 70.243 51.776 1.0 96.64 ? ? ? ? ? ? 145 ASP B N 1 28 B B +ATOM 5496 C CA . ASP B 1 28 ? -41.212 70.275 50.628 1.0 97.12 ? ? ? ? ? ? 145 ASP B CA 1 28 B B +ATOM 5497 C C . ASP B 1 28 ? -41.808 69.497 49.456 1.0 91.65 ? ? ? ? ? ? 145 ASP B C 1 28 B B +ATOM 5498 O O . ASP B 1 28 ? -41.375 69.645 48.311 1.0 74.72 ? ? ? ? ? ? 145 ASP B O 1 28 B B +ATOM 5499 C CB . ASP B 1 28 ? -39.854 69.678 51.004 1.0 97.58 ? ? ? ? ? ? 145 ASP B CB 1 28 B B +ATOM 5500 C CG . ASP B 1 28 ? -39.949 68.214 51.385 1.0 100.0 ? ? ? ? ? ? 145 ASP B CG 1 28 B B +ATOM 5501 O OD1 . ASP B 1 28 ? -40.641 67.900 52.375 1.0 89.65 ? ? ? ? ? ? 145 ASP B OD1 1 28 B B +ATOM 5502 O OD2 . ASP B 1 28 ? -39.328 67.376 50.697 1.0 100.0 ? ? ? ? ? ? 145 ASP B OD2 1 28 B B +ATOM 5503 N N . HIS B 1 29 ? -42.807 68.672 49.752 1.0 93.74 ? ? ? ? ? ? 146 HIS B N 1 29 B B +ATOM 5504 C CA . HIS B 1 29 ? -43.469 67.860 48.739 1.0 95.79 ? ? ? ? ? ? 146 HIS B CA 1 29 B B +ATOM 5505 C C . HIS B 1 29 ? -44.316 68.717 47.803 1.0 87.42 ? ? ? ? ? ? 146 HIS B C 1 29 B B +ATOM 5506 O O . HIS B 1 29 ? -45.200 69.453 48.245 1.0 88.11 ? ? ? ? ? ? 146 HIS B O 1 29 B B +ATOM 5507 C CB . HIS B 1 29 ? -44.352 66.798 49.411 1.0 100.0 ? ? ? ? ? ? 146 HIS B CB 1 29 B B +ATOM 5508 C CG . HIS B 1 29 ? -45.083 65.911 48.448 1.0 100.0 ? ? ? ? ? ? 146 HIS B CG 1 29 B B +ATOM 5509 N ND1 . HIS B 1 29 ? -46.090 66.370 47.626 1.0 100.0 ? ? ? ? ? ? 146 HIS B ND1 1 29 B B +ATOM 5510 C CD2 . HIS B 1 29 ? -44.963 64.586 48.187 1.0 100.0 ? ? ? ? ? ? 146 HIS B CD2 1 29 B B +ATOM 5511 C CE1 . HIS B 1 29 ? -46.560 65.369 46.903 1.0 100.0 ? ? ? ? ? ? 146 HIS B CE1 1 29 B B +ATOM 5512 N NE2 . HIS B 1 29 ? -45.891 64.275 47.225 1.0 100.0 ? ? ? ? ? ? 146 HIS B NE2 1 29 B B +ATOM 5513 N N . PRO B 1 30 ? -44.052 68.629 46.489 1.0 74.48 ? ? ? ? ? ? 147 PRO B N 1 30 B B +ATOM 5514 C CA . PRO B 1 30 ? -44.819 69.415 45.516 1.0 79.69 ? ? ? ? ? ? 147 PRO B CA 1 30 B B +ATOM 5515 C C . PRO B 1 30 ? -46.277 68.964 45.494 1.0 84.11 ? ? ? ? ? ? 147 PRO B C 1 30 B B +ATOM 5516 O O . PRO B 1 30 ? -46.574 67.798 45.239 1.0 92.23 ? ? ? ? ? ? 147 PRO B O 1 30 B B +ATOM 5517 C CB . PRO B 1 30 ? -44.106 69.149 44.191 1.0 77.32 ? ? ? ? ? ? 147 PRO B CB 1 30 B B +ATOM 5518 C CG . PRO B 1 30 ? -43.387 67.857 44.399 1.0 77.89 ? ? ? ? ? ? 147 PRO B CG 1 30 B B +ATOM 5519 C CD . PRO B 1 30 ? -43.030 67.787 45.847 1.0 70.78 ? ? ? ? ? ? 147 PRO B CD 1 30 B B +ATOM 5520 N N . GLY B 1 31 ? -47.182 69.896 45.772 1.0 85.27 ? ? ? ? ? ? 148 GLY B N 1 31 B B +ATOM 5521 C CA . GLY B 1 31 ? -48.597 69.570 45.797 1.0 79.76 ? ? ? ? ? ? 148 GLY B CA 1 31 B B +ATOM 5522 C C . GLY B 1 31 ? -49.124 69.508 47.219 1.0 76.37 ? ? ? ? ? ? 148 GLY B C 1 31 B B +ATOM 5523 O O . GLY B 1 31 ? -50.289 69.181 47.448 1.0 76.12 ? ? ? ? ? ? 148 GLY B O 1 31 B B +ATOM 5524 N N . PHE B 1 32 ? -48.255 69.817 48.178 1.0 77.29 ? ? ? ? ? ? 149 PHE B N 1 32 B B +ATOM 5525 C CA . PHE B 1 32 ? -48.622 69.808 49.590 1.0 85.57 ? ? ? ? ? ? 149 PHE B CA 1 32 B B +ATOM 5526 C C . PHE B 1 32 ? -49.673 70.880 49.860 1.0 87.09 ? ? ? ? ? ? 149 PHE B C 1 32 B B +ATOM 5527 O O . PHE B 1 32 ? -50.528 70.725 50.735 1.0 81.98 ? ? ? ? ? ? 149 PHE B O 1 32 B B +ATOM 5528 C CB . PHE B 1 32 ? -47.379 70.069 50.449 1.0 93.71 ? ? ? ? ? ? 149 PHE B CB 1 32 B B +ATOM 5529 C CG . PHE B 1 32 ? -47.668 70.231 51.919 1.0 100.0 ? ? ? ? ? ? 149 PHE B CG 1 32 B B +ATOM 5530 C CD1 . PHE B 1 32 ? -47.973 69.126 52.709 1.0 100.0 ? ? ? ? ? ? 149 PHE B CD1 1 32 B B +ATOM 5531 C CD2 . PHE B 1 32 ? -47.608 71.485 52.520 1.0 100.0 ? ? ? ? ? ? 149 PHE B CD2 1 32 B B +ATOM 5532 C CE1 . PHE B 1 32 ? -48.211 69.268 54.078 1.0 100.0 ? ? ? ? ? ? 149 PHE B CE1 1 32 B B +ATOM 5533 C CE2 . PHE B 1 32 ? -47.845 71.635 53.889 1.0 97.35 ? ? ? ? ? ? 149 PHE B CE2 1 32 B B +ATOM 5534 C CZ . PHE B 1 32 ? -48.147 70.524 54.666 1.0 95.24 ? ? ? ? ? ? 149 PHE B CZ 1 32 B B +ATOM 5535 N N . LYS B 1 33 ? -49.608 71.963 49.092 1.0 81.0 ? ? ? ? ? ? 150 LYS B N 1 33 B B +ATOM 5536 C CA . LYS B 1 33 ? -50.543 73.070 49.245 1.0 78.43 ? ? ? ? ? ? 150 LYS B CA 1 33 B B +ATOM 5537 C C . LYS B 1 33 ? -51.815 72.865 48.421 1.0 85.73 ? ? ? ? ? ? 150 LYS B C 1 33 B B +ATOM 5538 O O . LYS B 1 33 ? -52.762 73.643 48.532 1.0 79.74 ? ? ? ? ? ? 150 LYS B O 1 33 B B +ATOM 5539 C CB . LYS B 1 33 ? -49.858 74.372 48.837 1.0 66.54 ? ? ? ? ? ? 150 LYS B CB 1 33 B B +ATOM 5540 C CG . LYS B 1 33 ? -48.435 74.477 49.361 1.0 77.6 ? ? ? ? ? ? 150 LYS B CG 1 33 B B +ATOM 5541 C CD . LYS B 1 33 ? -47.802 75.820 49.043 1.0 96.5 ? ? ? ? ? ? 150 LYS B CD 1 33 B B +ATOM 5542 C CE . LYS B 1 33 ? -46.537 76.027 49.871 1.0 100.0 ? ? ? ? ? ? 150 LYS B CE 1 33 B B +ATOM 5543 N NZ . LYS B 1 33 ? -45.926 77.369 49.658 1.0 100.0 ? ? ? ? ? ? 150 LYS B NZ 1 33 B B +ATOM 5544 N N . ASP B 1 34 ? -51.840 71.810 47.609 1.0 91.48 ? ? ? ? ? ? 151 ASP B N 1 34 B B +ATOM 5545 C CA . ASP B 1 34 ? -53.002 71.523 46.776 1.0 95.17 ? ? ? ? ? ? 151 ASP B CA 1 34 B B +ATOM 5546 C C . ASP B 1 34 ? -54.036 70.678 47.507 1.0 93.27 ? ? ? ? ? ? 151 ASP B C 1 34 B B +ATOM 5547 O O . ASP B 1 34 ? -53.836 69.484 47.716 1.0 93.13 ? ? ? ? ? ? 151 ASP B O 1 34 B B +ATOM 5548 C CB . ASP B 1 34 ? -52.579 70.808 45.492 1.0 99.66 ? ? ? ? ? ? 151 ASP B CB 1 34 B B +ATOM 5549 C CG . ASP B 1 34 ? -53.707 70.720 44.479 1.0 98.38 ? ? ? ? ? ? 151 ASP B CG 1 34 B B +ATOM 5550 O OD1 . ASP B 1 34 ? -54.866 70.478 44.888 1.0 75.71 ? ? ? ? ? ? 151 ASP B OD1 1 34 B B +ATOM 5551 O OD2 . ASP B 1 34 ? -53.440 70.888 43.272 1.0 94.6 ? ? ? ? ? ? 151 ASP B OD2 1 34 B B +ATOM 5552 N N . PRO B 1 35 ? -55.168 71.293 47.891 1.0 98.4 ? ? ? ? ? ? 152 PRO B N 1 35 B B +ATOM 5553 C CA . PRO B 1 35 ? -56.246 70.603 48.607 1.0 100.0 ? ? ? ? ? ? 152 PRO B CA 1 35 B B +ATOM 5554 C C . PRO B 1 35 ? -56.891 69.466 47.818 1.0 100.0 ? ? ? ? ? ? 152 PRO B C 1 35 B B +ATOM 5555 O O . PRO B 1 35 ? -57.368 68.493 48.405 1.0 97.06 ? ? ? ? ? ? 152 PRO B O 1 35 B B +ATOM 5556 C CB . PRO B 1 35 ? -57.251 71.715 48.926 1.0 97.64 ? ? ? ? ? ? 152 PRO B CB 1 35 B B +ATOM 5557 C CG . PRO B 1 35 ? -56.524 72.994 48.678 1.0 96.38 ? ? ? ? ? ? 152 PRO B CG 1 35 B B +ATOM 5558 C CD . PRO B 1 35 ? -55.492 72.704 47.641 1.0 97.39 ? ? ? ? ? ? 152 PRO B CD 1 35 B B +ATOM 5559 N N . VAL B 1 36 ? -56.912 69.591 46.493 1.0 97.45 ? ? ? ? ? ? 153 VAL B N 1 36 B B +ATOM 5560 C CA . VAL B 1 36 ? -57.506 68.556 45.647 1.0 97.98 ? ? ? ? ? ? 153 VAL B CA 1 36 B B +ATOM 5561 C C . VAL B 1 36 ? -56.565 67.359 45.566 1.0 97.63 ? ? ? ? ? ? 153 VAL B C 1 36 B B +ATOM 5562 O O . VAL B 1 36 ? -56.851 66.294 46.117 1.0 100.0 ? ? ? ? ? ? 153 VAL B O 1 36 B B +ATOM 5563 C CB . VAL B 1 36 ? -57.787 69.080 44.209 1.0 97.27 ? ? ? ? ? ? 153 VAL B CB 1 36 B B +ATOM 5564 C CG1 . VAL B 1 36 ? -58.065 67.910 43.261 1.0 77.64 ? ? ? ? ? ? 153 VAL B CG1 1 36 B B +ATOM 5565 C CG2 . VAL B 1 36 ? -58.980 70.026 44.225 1.0 100.0 ? ? ? ? ? ? 153 VAL B CG2 1 36 B B +ATOM 5566 N N . TYR B 1 37 ? -55.444 67.549 44.873 1.0 91.74 ? ? ? ? ? ? 154 TYR B N 1 37 B B +ATOM 5567 C CA . TYR B 1 37 ? -54.436 66.507 44.710 1.0 80.82 ? ? ? ? ? ? 154 TYR B CA 1 37 B B +ATOM 5568 C C . TYR B 1 37 ? -54.205 65.804 46.043 1.0 62.59 ? ? ? ? ? ? 154 TYR B C 1 37 B B +ATOM 5569 O O . TYR B 1 37 ? -54.020 64.589 46.103 1.0 57.9 ? ? ? ? ? ? 154 TYR B O 1 37 B B +ATOM 5570 C CB . TYR B 1 37 ? -53.133 67.135 44.198 1.0 87.47 ? ? ? ? ? ? 154 TYR B CB 1 37 B B +ATOM 5571 C CG . TYR B 1 37 ? -51.918 66.237 44.263 1.0 100.0 ? ? ? ? ? ? 154 TYR B CG 1 37 B B +ATOM 5572 C CD1 . TYR B 1 37 ? -51.844 65.071 43.499 1.0 100.0 ? ? ? ? ? ? 154 TYR B CD1 1 37 B B +ATOM 5573 C CD2 . TYR B 1 37 ? -50.829 66.566 45.071 1.0 100.0 ? ? ? ? ? ? 154 TYR B CD2 1 37 B B +ATOM 5574 C CE1 . TYR B 1 37 ? -50.712 64.256 43.538 1.0 98.74 ? ? ? ? ? ? 154 TYR B CE1 1 37 B B +ATOM 5575 C CE2 . TYR B 1 37 ? -49.695 65.759 45.116 1.0 100.0 ? ? ? ? ? ? 154 TYR B CE2 1 37 B B +ATOM 5576 C CZ . TYR B 1 37 ? -49.643 64.610 44.348 1.0 98.2 ? ? ? ? ? ? 154 TYR B CZ 1 37 B B +ATOM 5577 O OH . TYR B 1 37 ? -48.516 63.825 44.383 1.0 94.15 ? ? ? ? ? ? 154 TYR B OH 1 37 B B +ATOM 5578 N N . ARG B 1 38 ? -54.224 66.590 47.110 1.0 51.43 ? ? ? ? ? ? 155 ARG B N 1 38 B B +ATOM 5579 C CA . ARG B 1 38 ? -54.037 66.075 48.453 1.0 48.13 ? ? ? ? ? ? 155 ARG B CA 1 38 B B +ATOM 5580 C C . ARG B 1 38 ? -55.101 65.023 48.747 1.0 51.81 ? ? ? ? ? ? 155 ARG B C 1 38 B B +ATOM 5581 O O . ARG B 1 38 ? -54.787 63.853 48.971 1.0 73.68 ? ? ? ? ? ? 155 ARG B O 1 38 B B +ATOM 5582 C CB . ARG B 1 38 ? -54.152 67.220 49.455 1.0 63.48 ? ? ? ? ? ? 155 ARG B CB 1 38 B B +ATOM 5583 C CG . ARG B 1 38 ? -53.527 66.952 50.802 1.0 82.88 ? ? ? ? ? ? 155 ARG B CG 1 38 B B +ATOM 5584 C CD . ARG B 1 38 ? -53.716 68.157 51.704 1.0 99.89 ? ? ? ? ? ? 155 ARG B CD 1 38 B B +ATOM 5585 N NE . ARG B 1 38 ? -53.214 67.930 53.055 1.0 100.0 ? ? ? ? ? ? 155 ARG B NE 1 38 B B +ATOM 5586 C CZ . ARG B 1 38 ? -52.190 68.588 53.586 1.0 100.0 ? ? ? ? ? ? 155 ARG B CZ 1 38 B B +ATOM 5587 N NH1 . ARG B 1 38 ? -51.556 69.515 52.879 1.0 90.91 ? ? ? ? ? ? 155 ARG B NH1 1 38 B B +ATOM 5588 N NH2 . ARG B 1 38 ? -51.807 68.327 54.829 1.0 100.0 ? ? ? ? ? ? 155 ARG B NH2 1 38 B B +ATOM 5589 N N . ALA B 1 39 ? -56.362 65.450 48.744 1.0 55.36 ? ? ? ? ? ? 156 ALA B N 1 39 B B +ATOM 5590 C CA . ALA B 1 39 ? -57.484 64.560 49.021 1.0 66.74 ? ? ? ? ? ? 156 ALA B CA 1 39 B B +ATOM 5591 C C . ALA B 1 39 ? -57.583 63.466 47.969 1.0 63.72 ? ? ? ? ? ? 156 ALA B C 1 39 B B +ATOM 5592 O O . ALA B 1 39 ? -58.215 62.432 48.185 1.0 67.32 ? ? ? ? ? ? 156 ALA B O 1 39 B B +ATOM 5593 C CB . ALA B 1 39 ? -58.776 65.356 49.070 1.0 81.61 ? ? ? ? ? ? 156 ALA B CB 1 39 B B +ATOM 5594 N N . ARG B 1 40 ? -56.966 63.708 46.821 1.0 57.55 ? ? ? ? ? ? 157 ARG B N 1 40 B B +ATOM 5595 C CA . ARG B 1 40 ? -56.974 62.728 45.745 1.0 59.91 ? ? ? ? ? ? 157 ARG B CA 1 40 B B +ATOM 5596 C C . ARG B 1 40 ? -56.040 61.588 46.141 1.0 62.43 ? ? ? ? ? ? 157 ARG B C 1 40 B B +ATOM 5597 O O . ARG B 1 40 ? -56.393 60.409 46.042 1.0 38.28 ? ? ? ? ? ? 157 ARG B O 1 40 B B +ATOM 5598 C CB . ARG B 1 40 ? -56.486 63.371 44.443 1.0 50.9 ? ? ? ? ? ? 157 ARG B CB 1 40 B B +ATOM 5599 C CG . ARG B 1 40 ? -56.250 62.392 43.310 1.0 55.69 ? ? ? ? ? ? 157 ARG B CG 1 40 B B +ATOM 5600 C CD . ARG B 1 40 ? -57.549 62.063 42.600 1.0 44.8 ? ? ? ? ? ? 157 ARG B CD 1 40 B B +ATOM 5601 N NE . ARG B 1 40 ? -57.321 61.498 41.275 1.0 43.79 ? ? ? ? ? ? 157 ARG B NE 1 40 B B +ATOM 5602 C CZ . ARG B 1 40 ? -58.212 60.764 40.616 1.0 54.54 ? ? ? ? ? ? 157 ARG B CZ 1 40 B B +ATOM 5603 N NH1 . ARG B 1 40 ? -59.400 60.504 41.157 1.0 34.07 ? ? ? ? ? ? 157 ARG B NH1 1 40 B B +ATOM 5604 N NH2 . ARG B 1 40 ? -57.912 60.288 39.413 1.0 46.44 ? ? ? ? ? ? 157 ARG B NH2 1 40 B B +ATOM 5605 N N . ARG B 1 41 ? -54.848 61.955 46.604 1.0 59.5 ? ? ? ? ? ? 158 ARG B N 1 41 B B +ATOM 5606 C CA . ARG B 1 41 ? -53.848 60.979 47.019 1.0 62.03 ? ? ? ? ? ? 158 ARG B CA 1 41 B B +ATOM 5607 C C . ARG B 1 41 ? -54.275 60.227 48.278 1.0 55.94 ? ? ? ? ? ? 158 ARG B C 1 41 B B +ATOM 5608 O O . ARG B 1 41 ? -53.712 59.181 48.606 1.0 66.56 ? ? ? ? ? ? 158 ARG B O 1 41 B B +ATOM 5609 C CB . ARG B 1 41 ? -52.504 61.669 47.257 1.0 71.07 ? ? ? ? ? ? 158 ARG B CB 1 41 B B +ATOM 5610 C CG . ARG B 1 41 ? -51.331 60.703 47.377 1.0 80.09 ? ? ? ? ? ? 158 ARG B CG 1 41 B B +ATOM 5611 C CD . ARG B 1 41 ? -50.000 61.403 47.139 1.0 64.88 ? ? ? ? ? ? 158 ARG B CD 1 41 B B +ATOM 5612 N NE . ARG B 1 41 ? -48.891 60.676 47.748 1.0 60.68 ? ? ? ? ? ? 158 ARG B NE 1 41 B B +ATOM 5613 C CZ . ARG B 1 41 ? -47.609 60.917 47.497 1.0 64.02 ? ? ? ? ? ? 158 ARG B CZ 1 41 B B +ATOM 5614 N NH1 . ARG B 1 41 ? -47.267 61.867 46.638 1.0 58.33 ? ? ? ? ? ? 158 ARG B NH1 1 41 B B +ATOM 5615 N NH2 . ARG B 1 41 ? -46.668 60.198 48.092 1.0 54.6 ? ? ? ? ? ? 158 ARG B NH2 1 41 B B +ATOM 5616 N N . LYS B 1 42 ? -55.258 60.774 48.987 1.0 41.95 ? ? ? ? ? ? 159 LYS B N 1 42 B B +ATOM 5617 C CA . LYS B 1 42 ? -55.779 60.147 50.198 1.0 50.07 ? ? ? ? ? ? 159 LYS B CA 1 42 B B +ATOM 5618 C C . LYS B 1 42 ? -56.865 59.183 49.745 1.0 37.82 ? ? ? ? ? ? 159 LYS B C 1 42 B B +ATOM 5619 O O . LYS B 1 42 ? -57.219 58.231 50.439 1.0 49.51 ? ? ? ? ? ? 159 LYS B O 1 42 B B +ATOM 5620 C CB . LYS B 1 42 ? -56.375 61.204 51.129 1.0 67.92 ? ? ? ? ? ? 159 LYS B CB 1 42 B B +ATOM 5621 C CG . LYS B 1 42 ? -57.110 60.630 52.327 1.0 85.85 ? ? ? ? ? ? 159 LYS B CG 1 42 B B +ATOM 5622 C CD . LYS B 1 42 ? -57.559 61.732 53.271 1.0 93.61 ? ? ? ? ? ? 159 LYS B CD 1 42 B B +ATOM 5623 C CE . LYS B 1 42 ? -58.123 61.164 54.563 1.0 92.11 ? ? ? ? ? ? 159 LYS B CE 1 42 B B +ATOM 5624 N NZ . LYS B 1 42 ? -58.401 62.237 55.559 1.0 97.37 ? ? ? ? ? ? 159 LYS B NZ 1 42 B B +ATOM 5625 N N . GLN B 1 43 ? -57.382 59.460 48.556 1.0 29.47 ? ? ? ? ? ? 160 GLN B N 1 43 B B +ATOM 5626 C CA . GLN B 1 43 ? -58.414 58.655 47.934 1.0 49.18 ? ? ? ? ? ? 160 GLN B CA 1 43 B B +ATOM 5627 C C . GLN B 1 43 ? -57.770 57.350 47.496 1.0 57.94 ? ? ? ? ? ? 160 GLN B C 1 43 B B +ATOM 5628 O O . GLN B 1 43 ? -58.314 56.261 47.695 1.0 57.37 ? ? ? ? ? ? 160 GLN B O 1 43 B B +ATOM 5629 C CB . GLN B 1 43 ? -58.944 59.401 46.721 1.0 39.15 ? ? ? ? ? ? 160 GLN B CB 1 43 B B +ATOM 5630 C CG . GLN B 1 43 ? -60.240 58.896 46.178 1.0 58.25 ? ? ? ? ? ? 160 GLN B CG 1 43 B B +ATOM 5631 C CD . GLN B 1 43 ? -60.829 59.863 45.183 1.0 68.54 ? ? ? ? ? ? 160 GLN B CD 1 43 B B +ATOM 5632 O OE1 . GLN B 1 43 ? -60.154 60.785 44.721 1.0 38.86 ? ? ? ? ? ? 160 GLN B OE1 1 43 B B +ATOM 5633 N NE2 . GLN B 1 43 ? -62.096 59.666 44.849 1.0 77.6 ? ? ? ? ? ? 160 GLN B NE2 1 43 B B +ATOM 5634 N N . PHE B 1 44 ? -56.597 57.481 46.889 1.0 66.93 ? ? ? ? ? ? 161 PHE B N 1 44 B B +ATOM 5635 C CA . PHE B 1 44 ? -55.843 56.334 46.416 1.0 64.47 ? ? ? ? ? ? 161 PHE B CA 1 44 B B +ATOM 5636 C C . PHE B 1 44 ? -55.436 55.470 47.608 1.0 64.32 ? ? ? ? ? ? 161 PHE B C 1 44 B B +ATOM 5637 O O . PHE B 1 44 ? -55.665 54.261 47.608 1.0 69.2 ? ? ? ? ? ? 161 PHE B O 1 44 B B +ATOM 5638 C CB . PHE B 1 44 ? -54.596 56.803 45.659 1.0 65.94 ? ? ? ? ? ? 161 PHE B CB 1 44 B B +ATOM 5639 C CG . PHE B 1 44 ? -54.882 57.343 44.282 1.0 57.74 ? ? ? ? ? ? 161 PHE B CG 1 44 B B +ATOM 5640 C CD1 . PHE B 1 44 ? -54.476 58.627 43.928 1.0 56.22 ? ? ? ? ? ? 161 PHE B CD1 1 44 B B +ATOM 5641 C CD2 . PHE B 1 44 ? -55.549 56.570 43.337 1.0 55.99 ? ? ? ? ? ? 161 PHE B CD2 1 44 B B +ATOM 5642 C CE1 . PHE B 1 44 ? -54.729 59.135 42.655 1.0 59.72 ? ? ? ? ? ? 161 PHE B CE1 1 44 B B +ATOM 5643 C CE2 . PHE B 1 44 ? -55.808 57.070 42.059 1.0 60.29 ? ? ? ? ? ? 161 PHE B CE2 1 44 B B +ATOM 5644 C CZ . PHE B 1 44 ? -55.396 58.354 41.720 1.0 65.58 ? ? ? ? ? ? 161 PHE B CZ 1 44 B B +ATOM 5645 N N . ALA B 1 45 ? -54.842 56.095 48.623 1.0 50.76 ? ? ? ? ? ? 162 ALA B N 1 45 B B +ATOM 5646 C CA . ALA B 1 45 ? -54.402 55.381 49.822 1.0 60.51 ? ? ? ? ? ? 162 ALA B CA 1 45 B B +ATOM 5647 C C . ALA B 1 45 ? -55.524 54.551 50.444 1.0 68.51 ? ? ? ? ? ? 162 ALA B C 1 45 B B +ATOM 5648 O O . ALA B 1 45 ? -55.316 53.395 50.823 1.0 77.7 ? ? ? ? ? ? 162 ALA B O 1 45 B B +ATOM 5649 C CB . ALA B 1 45 ? -53.859 56.366 50.849 1.0 42.85 ? ? ? ? ? ? 162 ALA B CB 1 45 B B +ATOM 5650 N N . ASP B 1 46 ? -56.709 55.146 50.551 1.0 62.79 ? ? ? ? ? ? 163 ASP B N 1 46 B B +ATOM 5651 C CA . ASP B 1 46 ? -57.864 54.465 51.128 1.0 74.08 ? ? ? ? ? ? 163 ASP B CA 1 46 B B +ATOM 5652 C C . ASP B 1 46 ? -58.154 53.193 50.344 1.0 72.43 ? ? ? ? ? ? 163 ASP B C 1 46 B B +ATOM 5653 O O . ASP B 1 46 ? -58.538 52.171 50.918 1.0 82.91 ? ? ? ? ? ? 163 ASP B O 1 46 B B +ATOM 5654 C CB . ASP B 1 46 ? -59.091 55.380 51.103 1.0 86.21 ? ? ? ? ? ? 163 ASP B CB 1 46 B B +ATOM 5655 C CG . ASP B 1 46 ? -59.213 56.237 52.353 1.0 100.0 ? ? ? ? ? ? 163 ASP B CG 1 46 B B +ATOM 5656 O OD1 . ASP B 1 46 ? -59.670 55.720 53.396 1.0 100.0 ? ? ? ? ? ? 163 ASP B OD1 1 46 B B +ATOM 5657 O OD2 . ASP B 1 46 ? -58.856 57.432 52.291 1.0 100.0 ? ? ? ? ? ? 163 ASP B OD2 1 46 B B +ATOM 5658 N N . ILE B 1 47 ? -57.981 53.260 49.028 1.0 63.62 ? ? ? ? ? ? 164 ILE B N 1 47 B B +ATOM 5659 C CA . ILE B 1 47 ? -58.213 52.094 48.188 1.0 57.19 ? ? ? ? ? ? 164 ILE B CA 1 47 B B +ATOM 5660 C C . ILE B 1 47 ? -57.329 50.972 48.720 1.0 63.56 ? ? ? ? ? ? 164 ILE B C 1 47 B B +ATOM 5661 O O . ILE B 1 47 ? -57.780 49.839 48.887 1.0 51.27 ? ? ? ? ? ? 164 ILE B O 1 47 B B +ATOM 5662 C CB . ILE B 1 47 ? -57.828 52.360 46.718 1.0 54.96 ? ? ? ? ? ? 164 ILE B CB 1 47 B B +ATOM 5663 C CG1 . ILE B 1 47 ? -58.778 53.383 46.093 1.0 57.18 ? ? ? ? ? ? 164 ILE B CG1 1 47 B B +ATOM 5664 C CG2 . ILE B 1 47 ? -57.884 51.069 45.927 1.0 45.83 ? ? ? ? ? ? 164 ILE B CG2 1 47 B B +ATOM 5665 C CD1 . ILE B 1 47 ? -58.337 53.885 44.730 1.0 71.75 ? ? ? ? ? ? 164 ILE B CD1 1 47 B B +ATOM 5666 N N . ALA B 1 48 ? -56.069 51.315 48.990 1.0 54.17 ? ? ? ? ? ? 165 ALA B N 1 48 B B +ATOM 5667 C CA . ALA B 1 48 ? -55.078 50.373 49.506 1.0 56.78 ? ? ? ? ? ? 165 ALA B CA 1 48 B B +ATOM 5668 C C . ALA B 1 48 ? -55.517 49.765 50.831 1.0 62.38 ? ? ? ? ? ? 165 ALA B C 1 48 B B +ATOM 5669 O O . ALA B 1 48 ? -55.558 48.546 50.987 1.0 74.61 ? ? ? ? ? ? 165 ALA B O 1 48 B B +ATOM 5670 C CB . ALA B 1 48 ? -53.730 51.074 49.678 1.0 46.33 ? ? ? ? ? ? 165 ALA B CB 1 48 B B +ATOM 5671 N N . TYR B 1 49 ? -55.846 50.627 51.784 1.0 57.01 ? ? ? ? ? ? 166 TYR B N 1 49 B B +ATOM 5672 C CA . TYR B 1 49 ? -56.280 50.182 53.100 1.0 54.6 ? ? ? ? ? ? 166 TYR B CA 1 49 B B +ATOM 5673 C C . TYR B 1 49 ? -57.479 49.241 53.039 1.0 54.08 ? ? ? ? ? ? 166 TYR B C 1 49 B B +ATOM 5674 O O . TYR B 1 49 ? -57.658 48.395 53.911 1.0 56.28 ? ? ? ? ? ? 166 TYR B O 1 49 B B +ATOM 5675 C CB . TYR B 1 49 ? -56.627 51.392 53.965 1.0 52.61 ? ? ? ? ? ? 166 TYR B CB 1 49 B B +ATOM 5676 C CG . TYR B 1 49 ? -55.454 52.302 54.230 1.0 67.21 ? ? ? ? ? ? 166 TYR B CG 1 49 B B +ATOM 5677 C CD1 . TYR B 1 49 ? -55.543 53.673 53.996 1.0 76.45 ? ? ? ? ? ? 166 TYR B CD1 1 49 B B +ATOM 5678 C CD2 . TYR B 1 49 ? -54.258 51.798 54.730 1.0 79.48 ? ? ? ? ? ? 166 TYR B CD2 1 49 B B +ATOM 5679 C CE1 . TYR B 1 49 ? -54.471 54.522 54.258 1.0 72.28 ? ? ? ? ? ? 166 TYR B CE1 1 49 B B +ATOM 5680 C CE2 . TYR B 1 49 ? -53.179 52.636 54.995 1.0 79.73 ? ? ? ? ? ? 166 TYR B CE2 1 49 B B +ATOM 5681 C CZ . TYR B 1 49 ? -53.292 53.996 54.757 1.0 73.81 ? ? ? ? ? ? 166 TYR B CZ 1 49 B B +ATOM 5682 O OH . TYR B 1 49 ? -52.233 54.831 55.033 1.0 73.0 ? ? ? ? ? ? 166 TYR B OH 1 49 B B +ATOM 5683 N N . ASN B 1 50 ? -58.297 49.390 52.005 1.0 50.52 ? ? ? ? ? ? 167 ASN B N 1 50 B B +ATOM 5684 C CA . ASN B 1 50 ? -59.483 48.556 51.858 1.0 72.73 ? ? ? ? ? ? 167 ASN B CA 1 50 B B +ATOM 5685 C C . ASN B 1 50 ? -59.237 47.320 51.015 1.0 75.36 ? ? ? ? ? ? 167 ASN B C 1 50 B B +ATOM 5686 O O . ASN B 1 50 ? -60.066 46.411 50.974 1.0 80.4 ? ? ? ? ? ? 167 ASN B O 1 50 B B +ATOM 5687 C CB . ASN B 1 50 ? -60.618 49.360 51.227 1.0 88.5 ? ? ? ? ? ? 167 ASN B CB 1 50 B B +ATOM 5688 C CG . ASN B 1 50 ? -61.044 50.531 52.082 1.0 100.0 ? ? ? ? ? ? 167 ASN B CG 1 50 B B +ATOM 5689 O OD1 . ASN B 1 50 ? -61.402 50.364 53.249 1.0 100.0 ? ? ? ? ? ? 167 ASN B OD1 1 50 B B +ATOM 5690 N ND2 . ASN B 1 50 ? -61.008 51.727 51.506 1.0 100.0 ? ? ? ? ? ? 167 ASN B ND2 1 50 B B +ATOM 5691 N N . TYR B 1 51 ? -58.097 47.283 50.338 1.0 66.74 ? ? ? ? ? ? 168 TYR B N 1 51 B B +ATOM 5692 C CA . TYR B 1 51 ? -57.781 46.148 49.485 1.0 64.8 ? ? ? ? ? ? 168 TYR B CA 1 51 B B +ATOM 5693 C C . TYR B 1 51 ? -57.318 44.903 50.227 1.0 54.51 ? ? ? ? ? ? 168 TYR B C 1 51 B B +ATOM 5694 O O . TYR B 1 51 ? -56.361 44.940 51.002 1.0 61.97 ? ? ? ? ? ? 168 TYR B O 1 51 B B +ATOM 5695 C CB . TYR B 1 51 ? -56.717 46.528 48.455 1.0 79.84 ? ? ? ? ? ? 168 TYR B CB 1 51 B B +ATOM 5696 C CG . TYR B 1 51 ? -56.423 45.404 47.493 1.0 86.88 ? ? ? ? ? ? 168 TYR B CG 1 51 B B +ATOM 5697 C CD1 . TYR B 1 51 ? -57.311 45.098 46.462 1.0 90.58 ? ? ? ? ? ? 168 TYR B CD1 1 51 B B +ATOM 5698 C CD2 . TYR B 1 51 ? -55.290 44.608 47.646 1.0 83.02 ? ? ? ? ? ? 168 TYR B CD2 1 51 B B +ATOM 5699 C CE1 . TYR B 1 51 ? -57.086 44.026 45.615 1.0 75.51 ? ? ? ? ? ? 168 TYR B CE1 1 51 B B +ATOM 5700 C CE2 . TYR B 1 51 ? -55.054 43.530 46.803 1.0 82.8 ? ? ? ? ? ? 168 TYR B CE2 1 51 B B +ATOM 5701 C CZ . TYR B 1 51 ? -55.957 43.245 45.791 1.0 84.21 ? ? ? ? ? ? 168 TYR B CZ 1 51 B B +ATOM 5702 O OH . TYR B 1 51 ? -55.740 42.172 44.959 1.0 100.0 ? ? ? ? ? ? 168 TYR B OH 1 51 B B +ATOM 5703 N N . ARG B 1 52 ? -58.007 43.798 49.971 1.0 41.53 ? ? ? ? ? ? 169 ARG B N 1 52 B B +ATOM 5704 C CA . ARG B 1 52 ? -57.665 42.525 50.577 1.0 61.97 ? ? ? ? ? ? 169 ARG B CA 1 52 B B +ATOM 5705 C C . ARG B 1 52 ? -57.327 41.565 49.444 1.0 62.04 ? ? ? ? ? ? 169 ARG B C 1 52 B B +ATOM 5706 O O . ARG B 1 52 ? -57.967 41.582 48.393 1.0 60.29 ? ? ? ? ? ? 169 ARG B O 1 52 B B +ATOM 5707 C CB . ARG B 1 52 ? -58.841 41.992 51.396 1.0 69.44 ? ? ? ? ? ? 169 ARG B CB 1 52 B B +ATOM 5708 C CG . ARG B 1 52 ? -58.740 42.291 52.884 1.0 73.47 ? ? ? ? ? ? 169 ARG B CG 1 52 B B +ATOM 5709 C CD . ARG B 1 52 ? -58.968 43.764 53.171 1.0 61.39 ? ? ? ? ? ? 169 ARG B CD 1 52 B B +ATOM 5710 N NE . ARG B 1 52 ? -58.907 44.054 54.600 1.0 77.33 ? ? ? ? ? ? 169 ARG B NE 1 52 B B +ATOM 5711 C CZ . ARG B 1 52 ? -57.972 44.809 55.169 1.0 89.0 ? ? ? ? ? ? 169 ARG B CZ 1 52 B B +ATOM 5712 N NH1 . ARG B 1 52 ? -57.015 45.354 54.431 1.0 92.77 ? ? ? ? ? ? 169 ARG B NH1 1 52 B B +ATOM 5713 N NH2 . ARG B 1 52 ? -57.991 45.015 56.478 1.0 99.94 ? ? ? ? ? ? 169 ARG B NH2 1 52 B B +ATOM 5714 N N . HIS B 1 53 ? -56.310 40.738 49.659 1.0 68.52 ? ? ? ? ? ? 170 HIS B N 1 53 B B +ATOM 5715 C CA . HIS B 1 53 ? -55.876 39.781 48.651 1.0 74.68 ? ? ? ? ? ? 170 HIS B CA 1 53 B B +ATOM 5716 C C . HIS B 1 53 ? -57.032 38.941 48.115 1.0 73.45 ? ? ? ? ? ? 170 HIS B C 1 53 B B +ATOM 5717 O O . HIS B 1 53 ? -58.009 38.678 48.817 1.0 60.55 ? ? ? ? ? ? 170 HIS B O 1 53 B B +ATOM 5718 C CB . HIS B 1 53 ? -54.789 38.867 49.234 1.0 74.49 ? ? ? ? ? ? 170 HIS B CB 1 53 B B +ATOM 5719 C CG . HIS B 1 53 ? -54.401 37.734 48.335 1.0 80.04 ? ? ? ? ? ? 170 HIS B CG 1 53 B B +ATOM 5720 N ND1 . HIS B 1 53 ? -53.412 37.846 47.378 1.0 79.81 ? ? ? ? ? ? 170 HIS B ND1 1 53 B B +ATOM 5721 C CD2 . HIS B 1 53 ? -54.861 36.464 48.250 1.0 81.19 ? ? ? ? ? ? 170 HIS B CD2 1 53 B B +ATOM 5722 C CE1 . HIS B 1 53 ? -53.285 36.694 46.745 1.0 90.42 ? ? ? ? ? ? 170 HIS B CE1 1 53 B B +ATOM 5723 N NE2 . HIS B 1 53 ? -54.152 35.839 47.254 1.0 85.48 ? ? ? ? ? ? 170 HIS B NE2 1 53 B B +ATOM 5724 N N . GLY B 1 54 ? -56.911 38.531 46.856 1.0 76.84 ? ? ? ? ? ? 171 GLY B N 1 54 B B +ATOM 5725 C CA . GLY B 1 54 ? -57.941 37.715 46.240 1.0 81.18 ? ? ? ? ? ? 171 GLY B CA 1 54 B B +ATOM 5726 C C . GLY B 1 54 ? -58.910 38.474 45.356 1.0 81.66 ? ? ? ? ? ? 171 GLY B C 1 54 B B +ATOM 5727 O O . GLY B 1 54 ? -59.334 37.965 44.315 1.0 58.86 ? ? ? ? ? ? 171 GLY B O 1 54 B B +ATOM 5728 N N . GLN B 1 55 ? -59.268 39.687 45.769 1.0 85.56 ? ? ? ? ? ? 172 GLN B N 1 55 B B +ATOM 5729 C CA . GLN B 1 55 ? -60.198 40.510 45.007 1.0 76.95 ? ? ? ? ? ? 172 GLN B CA 1 55 B B +ATOM 5730 C C . GLN B 1 55 ? -59.452 41.357 43.991 1.0 70.7 ? ? ? ? ? ? 172 GLN B C 1 55 B B +ATOM 5731 O O . GLN B 1 55 ? -58.316 41.764 44.222 1.0 64.21 ? ? ? ? ? ? 172 GLN B O 1 55 B B +ATOM 5732 C CB . GLN B 1 55 ? -60.990 41.417 45.944 1.0 73.18 ? ? ? ? ? ? 172 GLN B CB 1 55 B B +ATOM 5733 C CG . GLN B 1 55 ? -60.135 42.427 46.672 1.0 89.81 ? ? ? ? ? ? 172 GLN B CG 1 55 B B +ATOM 5734 C CD . GLN B 1 55 ? -60.712 42.795 48.019 1.0 98.74 ? ? ? ? ? ? 172 GLN B CD 1 55 B B +ATOM 5735 O OE1 . GLN B 1 55 ? -60.700 43.959 48.414 1.0 100.0 ? ? ? ? ? ? 172 GLN B OE1 1 55 B B +ATOM 5736 N NE2 . GLN B 1 55 ? -61.220 41.800 48.736 1.0 100.0 ? ? ? ? ? ? 172 GLN B NE2 1 55 B B +ATOM 5737 N N . PRO B 1 56 ? -60.090 41.640 42.847 1.0 73.82 ? ? ? ? ? ? 173 PRO B N 1 56 B B +ATOM 5738 C CA . PRO B 1 56 ? -59.447 42.450 41.806 1.0 66.22 ? ? ? ? ? ? 173 PRO B CA 1 56 B B +ATOM 5739 C C . PRO B 1 56 ? -59.145 43.874 42.263 1.0 59.56 ? ? ? ? ? ? 173 PRO B C 1 56 B B +ATOM 5740 O O . PRO B 1 56 ? -59.913 44.477 43.012 1.0 40.19 ? ? ? ? ? ? 173 PRO B O 1 56 B B +ATOM 5741 C CB . PRO B 1 56 ? -60.440 42.399 40.640 1.0 54.59 ? ? ? ? ? ? 173 PRO B CB 1 56 B B +ATOM 5742 C CG . PRO B 1 56 ? -61.748 42.047 41.261 1.0 72.86 ? ? ? ? ? ? 173 PRO B CG 1 56 B B +ATOM 5743 C CD . PRO B 1 56 ? -61.450 41.218 42.470 1.0 76.58 ? ? ? ? ? ? 173 PRO B CD 1 56 B B +ATOM 5744 N N . ILE B 1 57 ? -58.007 44.397 41.816 1.0 62.65 ? ? ? ? ? ? 174 ILE B N 1 57 B B +ATOM 5745 C CA . ILE B 1 57 ? -57.602 45.749 42.169 1.0 60.69 ? ? ? ? ? ? 174 ILE B CA 1 57 B B +ATOM 5746 C C . ILE B 1 57 ? -58.601 46.732 41.570 1.0 67.23 ? ? ? ? ? ? 174 ILE B C 1 57 B B +ATOM 5747 O O . ILE B 1 57 ? -58.821 46.750 40.360 1.0 73.73 ? ? ? ? ? ? 174 ILE B O 1 57 B B +ATOM 5748 C CB . ILE B 1 57 ? -56.191 46.072 41.626 1.0 55.07 ? ? ? ? ? ? 174 ILE B CB 1 57 B B +ATOM 5749 C CG1 . ILE B 1 57 ? -55.239 44.910 41.908 1.0 58.47 ? ? ? ? ? ? 174 ILE B CG1 1 57 B B +ATOM 5750 C CG2 . ILE B 1 57 ? -55.674 47.360 42.252 1.0 60.31 ? ? ? ? ? ? 174 ILE B CG2 1 57 B B +ATOM 5751 C CD1 . ILE B 1 57 ? -53.902 45.031 41.211 1.0 68.31 ? ? ? ? ? ? 174 ILE B CD1 1 57 B B +ATOM 5752 N N . PRO B 1 58 ? -59.230 47.558 42.417 1.0 64.96 ? ? ? ? ? ? 175 PRO B N 1 58 B B +ATOM 5753 C CA . PRO B 1 58 ? -60.209 48.534 41.920 1.0 70.0 ? ? ? ? ? ? 175 PRO B CA 1 58 B B +ATOM 5754 C C . PRO B 1 58 ? -59.649 49.457 40.840 1.0 74.14 ? ? ? ? ? ? 175 PRO B C 1 58 B B +ATOM 5755 O O . PRO B 1 58 ? -58.503 49.894 40.921 1.0 73.56 ? ? ? ? ? ? 175 PRO B O 1 58 B B +ATOM 5756 C CB . PRO B 1 58 ? -60.632 49.302 43.177 1.0 61.64 ? ? ? ? ? ? 175 PRO B CB 1 58 B B +ATOM 5757 C CG . PRO B 1 58 ? -59.589 48.980 44.204 1.0 67.53 ? ? ? ? ? ? 175 PRO B CG 1 58 B B +ATOM 5758 C CD . PRO B 1 58 ? -59.066 47.629 43.877 1.0 61.93 ? ? ? ? ? ? 175 PRO B CD 1 58 B B +ATOM 5759 N N . ARG B 1 59 ? -60.464 49.750 39.829 1.0 66.46 ? ? ? ? ? ? 176 ARG B N 1 59 B B +ATOM 5760 C CA . ARG B 1 59 ? -60.037 50.627 38.746 1.0 61.16 ? ? ? ? ? ? 176 ARG B CA 1 59 B B +ATOM 5761 C C . ARG B 1 59 ? -60.332 52.077 39.113 1.0 59.92 ? ? ? ? ? ? 176 ARG B C 1 59 B B +ATOM 5762 O O . ARG B 1 59 ? -61.205 52.352 39.930 1.0 57.89 ? ? ? ? ? ? 176 ARG B O 1 59 B B +ATOM 5763 C CB . ARG B 1 59 ? -60.754 50.260 37.444 1.0 50.1 ? ? ? ? ? ? 176 ARG B CB 1 59 B B +ATOM 5764 C CG . ARG B 1 59 ? -60.523 48.826 37.001 1.0 58.89 ? ? ? ? ? ? 176 ARG B CG 1 59 B B +ATOM 5765 C CD . ARG B 1 59 ? -61.349 48.479 35.777 1.0 72.01 ? ? ? ? ? ? 176 ARG B CD 1 59 B B +ATOM 5766 N NE . ARG B 1 59 ? -60.631 47.568 34.895 1.0 70.85 ? ? ? ? ? ? 176 ARG B NE 1 59 B B +ATOM 5767 C CZ . ARG B 1 59 ? -59.918 47.957 33.845 1.0 83.18 ? ? ? ? ? ? 176 ARG B CZ 1 59 B B +ATOM 5768 N NH1 . ARG B 1 59 ? -59.825 49.245 33.542 1.0 84.71 ? ? ? ? ? ? 176 ARG B NH1 1 59 B B +ATOM 5769 N NH2 . ARG B 1 59 ? -59.295 47.057 33.099 1.0 91.27 ? ? ? ? ? ? 176 ARG B NH2 1 59 B B +ATOM 5770 N N . VAL B 1 60 ? -59.597 53.001 38.505 1.0 64.04 ? ? ? ? ? ? 177 VAL B N 1 60 B B +ATOM 5771 C CA . VAL B 1 60 ? -59.777 54.419 38.788 1.0 60.14 ? ? ? ? ? ? 177 VAL B CA 1 60 B B +ATOM 5772 C C . VAL B 1 60 ? -59.834 55.251 37.512 1.0 65.82 ? ? ? ? ? ? 177 VAL B C 1 60 B B +ATOM 5773 O O . VAL B 1 60 ? -59.168 54.945 36.524 1.0 63.14 ? ? ? ? ? ? 177 VAL B O 1 60 B B +ATOM 5774 C CB . VAL B 1 60 ? -58.631 54.951 39.678 1.0 56.5 ? ? ? ? ? ? 177 VAL B CB 1 60 B B +ATOM 5775 C CG1 . VAL B 1 60 ? -58.734 56.454 39.824 1.0 57.11 ? ? ? ? ? ? 177 VAL B CG1 1 60 B B +ATOM 5776 C CG2 . VAL B 1 60 ? -58.680 54.288 41.039 1.0 61.23 ? ? ? ? ? ? 177 VAL B CG2 1 60 B B +ATOM 5777 N N . GLU B 1 61 ? -60.639 56.307 37.548 1.0 67.94 ? ? ? ? ? ? 178 GLU B N 1 61 B B +ATOM 5778 C CA . GLU B 1 61 ? -60.795 57.208 36.415 1.0 66.12 ? ? ? ? ? ? 178 GLU B CA 1 61 B B +ATOM 5779 C C . GLU B 1 61 ? -59.830 58.385 36.581 1.0 66.76 ? ? ? ? ? ? 178 GLU B C 1 61 B B +ATOM 5780 O O . GLU B 1 61 ? -60.185 59.411 37.156 1.0 74.54 ? ? ? ? ? ? 178 GLU B O 1 61 B B +ATOM 5781 C CB . GLU B 1 61 ? -62.238 57.719 36.355 1.0 63.93 ? ? ? ? ? ? 178 GLU B CB 1 61 B B +ATOM 5782 C CG . GLU B 1 61 ? -62.767 57.963 34.953 1.0 81.95 ? ? ? ? ? ? 178 GLU B CG 1 61 B B +ATOM 5783 C CD . GLU B 1 61 ? -64.274 58.168 34.925 1.0 99.54 ? ? ? ? ? ? 178 GLU B CD 1 61 B B +ATOM 5784 O OE1 . GLU B 1 61 ? -64.737 59.259 35.329 1.0 100.0 ? ? ? ? ? ? 178 GLU B OE1 1 61 B B +ATOM 5785 O OE2 . GLU B 1 61 ? -64.995 57.238 34.501 1.0 90.8 ? ? ? ? ? ? 178 GLU B OE2 1 61 B B +ATOM 5786 N N . TYR B 1 62 ? -58.609 58.230 36.079 1.0 62.63 ? ? ? ? ? ? 179 TYR B N 1 62 B B +ATOM 5787 C CA . TYR B 1 62 ? -57.594 59.275 36.186 1.0 60.17 ? ? ? ? ? ? 179 TYR B CA 1 62 B B +ATOM 5788 C C . TYR B 1 62 ? -58.006 60.559 35.480 1.0 53.94 ? ? ? ? ? ? 179 TYR B C 1 62 B B +ATOM 5789 O O . TYR B 1 62 ? -58.723 60.521 34.483 1.0 65.06 ? ? ? ? ? ? 179 TYR B O 1 62 B B +ATOM 5790 C CB . TYR B 1 62 ? -56.267 58.766 35.623 1.0 57.21 ? ? ? ? ? ? 179 TYR B CB 1 62 B B +ATOM 5791 C CG . TYR B 1 62 ? -55.668 57.658 36.454 1.0 53.03 ? ? ? ? ? ? 179 TYR B CG 1 62 B B +ATOM 5792 C CD1 . TYR B 1 62 ? -54.604 57.908 37.321 1.0 62.41 ? ? ? ? ? ? 179 TYR B CD1 1 62 B B +ATOM 5793 C CD2 . TYR B 1 62 ? -56.181 56.364 36.395 1.0 55.44 ? ? ? ? ? ? 179 TYR B CD2 1 62 B B +ATOM 5794 C CE1 . TYR B 1 62 ? -54.065 56.898 38.109 1.0 61.06 ? ? ? ? ? ? 179 TYR B CE1 1 62 B B +ATOM 5795 C CE2 . TYR B 1 62 ? -55.649 55.345 37.179 1.0 67.16 ? ? ? ? ? ? 179 TYR B CE2 1 62 B B +ATOM 5796 C CZ . TYR B 1 62 ? -54.591 55.620 38.034 1.0 71.98 ? ? ? ? ? ? 179 TYR B CZ 1 62 B B +ATOM 5797 O OH . TYR B 1 62 ? -54.048 54.617 38.807 1.0 75.67 ? ? ? ? ? ? 179 TYR B OH 1 62 B B +ATOM 5798 N N . MET B 1 63 ? -57.549 61.694 36.004 1.0 44.48 ? ? ? ? ? ? 180 MET B N 1 63 B B +ATOM 5799 C CA . MET B 1 63 ? -57.883 62.998 35.434 1.0 51.59 ? ? ? ? ? ? 180 MET B CA 1 63 B B +ATOM 5800 C C . MET B 1 63 ? -56.842 63.481 34.433 1.0 50.91 ? ? ? ? ? ? 180 MET B C 1 63 B B +ATOM 5801 O O . MET B 1 63 ? -55.690 63.051 34.465 1.0 43.45 ? ? ? ? ? ? 180 MET B O 1 63 B B +ATOM 5802 C CB . MET B 1 63 ? -58.041 64.035 36.551 1.0 69.37 ? ? ? ? ? ? 180 MET B CB 1 63 B B +ATOM 5803 C CG . MET B 1 63 ? -58.992 63.605 37.664 1.0 76.18 ? ? ? ? ? ? 180 MET B CG 1 63 B B +ATOM 5804 S SD . MET B 1 63 ? -59.119 64.774 39.038 1.0 78.79 ? ? ? ? ? ? 180 MET B SD 1 63 B B +ATOM 5805 C CE . MET B 1 63 ? -57.390 65.309 39.234 1.0 79.39 ? ? ? ? ? ? 180 MET B CE 1 63 B B +ATOM 5806 N N . GLU B 1 64 ? -57.263 64.385 33.553 1.0 55.45 ? ? ? ? ? ? 181 GLU B N 1 64 B B +ATOM 5807 C CA . GLU B 1 64 ? -56.390 64.930 32.518 1.0 65.48 ? ? ? ? ? ? 181 GLU B CA 1 64 B B +ATOM 5808 C C . GLU B 1 64 ? -55.148 65.607 33.069 1.0 59.13 ? ? ? ? ? ? 181 GLU B C 1 64 B B +ATOM 5809 O O . GLU B 1 64 ? -54.062 65.471 32.511 1.0 57.9 ? ? ? ? ? ? 181 GLU B O 1 64 B B +ATOM 5810 C CB . GLU B 1 64 ? -57.158 65.924 31.645 1.0 73.55 ? ? ? ? ? ? 181 GLU B CB 1 64 B B +ATOM 5811 C CG . GLU B 1 64 ? -57.675 65.332 30.350 1.0 74.18 ? ? ? ? ? ? 181 GLU B CG 1 64 B B +ATOM 5812 C CD . GLU B 1 64 ? -58.807 64.355 30.585 1.0 84.6 ? ? ? ? ? ? 181 GLU B CD 1 64 B B +ATOM 5813 O OE1 . GLU B 1 64 ? -59.431 64.425 31.666 1.0 80.82 ? ? ? ? ? ? 181 GLU B OE1 1 64 B B +ATOM 5814 O OE2 . GLU B 1 64 ? -59.070 63.518 29.694 1.0 77.62 ? ? ? ? ? ? 181 GLU B OE2 1 64 B B +ATOM 5815 N N . GLU B 1 65 ? -55.311 66.356 34.153 1.0 60.69 ? ? ? ? ? ? 182 GLU B N 1 65 B B +ATOM 5816 C CA . GLU B 1 65 ? -54.173 67.037 34.754 1.0 72.25 ? ? ? ? ? ? 182 GLU B CA 1 65 B B +ATOM 5817 C C . GLU B 1 65 ? -53.154 65.964 35.122 1.0 76.67 ? ? ? ? ? ? 182 GLU B C 1 65 B B +ATOM 5818 O O . GLU B 1 65 ? -51.955 66.228 35.216 1.0 82.42 ? ? ? ? ? ? 182 GLU B O 1 65 B B +ATOM 5819 C CB . GLU B 1 65 ? -54.609 67.810 36.001 1.0 75.93 ? ? ? ? ? ? 182 GLU B CB 1 65 B B +ATOM 5820 C CG . GLU B 1 65 ? -55.565 68.966 35.718 1.0 89.1 ? ? ? ? ? ? 182 GLU B CG 1 65 B B +ATOM 5821 C CD . GLU B 1 65 ? -56.965 68.497 35.351 1.0 100.0 ? ? ? ? ? ? 182 GLU B CD 1 65 B B +ATOM 5822 O OE1 . GLU B 1 65 ? -57.657 69.213 34.595 1.0 100.0 ? ? ? ? ? ? 182 GLU B OE1 1 65 B B +ATOM 5823 O OE2 . GLU B 1 65 ? -57.373 67.412 35.817 1.0 100.0 ? ? ? ? ? ? 182 GLU B OE2 1 65 B B +ATOM 5824 N N . GLU B 1 66 ? -53.654 64.747 35.319 1.0 69.07 ? ? ? ? ? ? 183 GLU B N 1 66 B B +ATOM 5825 C CA . GLU B 1 66 ? -52.816 63.605 35.662 1.0 65.03 ? ? ? ? ? ? 183 GLU B CA 1 66 B B +ATOM 5826 C C . GLU B 1 66 ? -52.343 62.924 34.380 1.0 71.81 ? ? ? ? ? ? 183 GLU B C 1 66 B B +ATOM 5827 O O . GLU B 1 66 ? -51.150 62.675 34.200 1.0 72.45 ? ? ? ? ? ? 183 GLU B O 1 66 B B +ATOM 5828 C CB . GLU B 1 66 ? -53.605 62.613 36.525 1.0 56.35 ? ? ? ? ? ? 183 GLU B CB 1 66 B B +ATOM 5829 C CG . GLU B 1 66 ? -54.175 63.240 37.789 1.0 66.75 ? ? ? ? ? ? 183 GLU B CG 1 66 B B +ATOM 5830 C CD . GLU B 1 66 ? -55.011 62.277 38.612 1.0 66.56 ? ? ? ? ? ? 183 GLU B CD 1 66 B B +ATOM 5831 O OE1 . GLU B 1 66 ? -55.884 61.595 38.036 1.0 37.84 ? ? ? ? ? ? 183 GLU B OE1 1 66 B B +ATOM 5832 O OE2 . GLU B 1 66 ? -54.796 62.208 39.841 1.0 72.41 ? ? ? ? ? ? 183 GLU B OE2 1 66 B B +ATOM 5833 N N . LYS B 1 67 ? -53.289 62.633 33.491 1.0 71.29 ? ? ? ? ? ? 184 LYS B N 1 67 B B +ATOM 5834 C CA . LYS B 1 67 ? -52.982 61.986 32.221 1.0 59.63 ? ? ? ? ? ? 184 LYS B CA 1 67 B B +ATOM 5835 C C . LYS B 1 67 ? -51.944 62.782 31.433 1.0 64.36 ? ? ? ? ? ? 184 LYS B C 1 67 B B +ATOM 5836 O O . LYS B 1 67 ? -51.228 62.230 30.602 1.0 65.37 ? ? ? ? ? ? 184 LYS B O 1 67 B B +ATOM 5837 C CB . LYS B 1 67 ? -54.255 61.830 31.388 1.0 52.43 ? ? ? ? ? ? 184 LYS B CB 1 67 B B +ATOM 5838 C CG . LYS B 1 67 ? -55.182 60.725 31.869 1.0 52.57 ? ? ? ? ? ? 184 LYS B CG 1 67 B B +ATOM 5839 C CD . LYS B 1 67 ? -56.373 60.557 30.934 1.0 54.98 ? ? ? ? ? ? 184 LYS B CD 1 67 B B +ATOM 5840 C CE . LYS B 1 67 ? -57.288 59.434 31.398 1.0 56.14 ? ? ? ? ? ? 184 LYS B CE 1 67 B B +ATOM 5841 N NZ . LYS B 1 67 ? -58.481 59.279 30.521 1.0 60.61 ? ? ? ? ? ? 184 LYS B NZ 1 67 B B +ATOM 5842 N N . LYS B 1 68 ? -51.870 64.083 31.692 1.0 70.38 ? ? ? ? ? ? 185 LYS B N 1 68 B B +ATOM 5843 C CA . LYS B 1 68 ? -50.902 64.929 31.007 1.0 70.07 ? ? ? ? ? ? 185 LYS B CA 1 68 B B +ATOM 5844 C C . LYS B 1 68 ? -49.524 64.621 31.564 1.0 64.92 ? ? ? ? ? ? 185 LYS B C 1 68 B B +ATOM 5845 O O . LYS B 1 68 ? -48.561 64.449 30.816 1.0 65.78 ? ? ? ? ? ? 185 LYS B O 1 68 B B +ATOM 5846 C CB . LYS B 1 68 ? -51.222 66.407 31.231 1.0 79.66 ? ? ? ? ? ? 185 LYS B CB 1 68 B B +ATOM 5847 C CG . LYS B 1 68 ? -50.220 67.347 30.585 1.0 97.13 ? ? ? ? ? ? 185 LYS B CG 1 68 B B +ATOM 5848 C CD . LYS B 1 68 ? -50.411 68.780 31.052 1.0 95.14 ? ? ? ? ? ? 185 LYS B CD 1 68 B B +ATOM 5849 C CE . LYS B 1 68 ? -49.622 69.752 30.185 1.0 92.79 ? ? ? ? ? ? 185 LYS B CE 1 68 B B +ATOM 5850 N NZ . LYS B 1 68 ? -48.155 69.670 30.436 1.0 100.0 ? ? ? ? ? ? 185 LYS B NZ 1 68 B B +ATOM 5851 N N . THR B 1 69 ? -49.441 64.552 32.887 1.0 70.7 ? ? ? ? ? ? 186 THR B N 1 69 B B +ATOM 5852 C CA . THR B 1 69 ? -48.186 64.259 33.561 1.0 81.19 ? ? ? ? ? ? 186 THR B CA 1 69 B B +ATOM 5853 C C . THR B 1 69 ? -47.702 62.866 33.174 1.0 82.75 ? ? ? ? ? ? 186 THR B C 1 69 B B +ATOM 5854 O O . THR B 1 69 ? -46.502 62.616 33.076 1.0 80.57 ? ? ? ? ? ? 186 THR B O 1 69 B B +ATOM 5855 C CB . THR B 1 69 ? -48.352 64.325 35.090 1.0 79.41 ? ? ? ? ? ? 186 THR B CB 1 69 B B +ATOM 5856 O OG1 . THR B 1 69 ? -49.118 65.484 35.437 1.0 69.39 ? ? ? ? ? ? 186 THR B OG1 1 69 B B +ATOM 5857 C CG2 . THR B 1 69 ? -46.998 64.399 35.769 1.0 88.62 ? ? ? ? ? ? 186 THR B CG2 1 69 B B +ATOM 5858 N N . TRP B 1 70 ? -48.644 61.956 32.961 1.0 82.99 ? ? ? ? ? ? 187 TRP B N 1 70 B B +ATOM 5859 C CA . TRP B 1 70 ? -48.298 60.596 32.577 1.0 84.8 ? ? ? ? ? ? 187 TRP B CA 1 70 B B +ATOM 5860 C C . TRP B 1 70 ? -47.634 60.624 31.205 1.0 81.96 ? ? ? ? ? ? 187 TRP B C 1 70 B B +ATOM 5861 O O . TRP B 1 70 ? -46.548 60.075 31.019 1.0 67.97 ? ? ? ? ? ? 187 TRP B O 1 70 B B +ATOM 5862 C CB . TRP B 1 70 ? -49.559 59.724 32.539 1.0 92.87 ? ? ? ? ? ? 187 TRP B CB 1 70 B B +ATOM 5863 C CG . TRP B 1 70 ? -49.391 58.431 31.799 1.0 91.79 ? ? ? ? ? ? 187 TRP B CG 1 70 B B +ATOM 5864 C CD1 . TRP B 1 70 ? -49.854 58.140 30.548 1.0 84.37 ? ? ? ? ? ? 187 TRP B CD1 1 70 B B +ATOM 5865 C CD2 . TRP B 1 70 ? -48.739 57.241 32.271 1.0 98.8 ? ? ? ? ? ? 187 TRP B CD2 1 70 B B +ATOM 5866 N NE1 . TRP B 1 70 ? -49.531 56.848 30.212 1.0 99.49 ? ? ? ? ? ? 187 TRP B NE1 1 70 B B +ATOM 5867 C CE2 . TRP B 1 70 ? -48.847 56.275 31.248 1.0 100.0 ? ? ? ? ? ? 187 TRP B CE2 1 70 B B +ATOM 5868 C CE3 . TRP B 1 70 ? -48.073 56.903 33.458 1.0 99.8 ? ? ? ? ? ? 187 TRP B CE3 1 70 B B +ATOM 5869 C CZ2 . TRP B 1 70 ? -48.313 54.986 31.378 1.0 100.0 ? ? ? ? ? ? 187 TRP B CZ2 1 70 B B +ATOM 5870 C CZ3 . TRP B 1 70 ? -47.541 55.618 33.585 1.0 89.3 ? ? ? ? ? ? 187 TRP B CZ3 1 70 B B +ATOM 5871 C CH2 . TRP B 1 70 ? -47.668 54.677 32.550 1.0 96.22 ? ? ? ? ? ? 187 TRP B CH2 1 70 B B +ATOM 5872 N N . GLY B 1 71 ? -48.294 61.280 30.255 1.0 83.69 ? ? ? ? ? ? 188 GLY B N 1 71 B B +ATOM 5873 C CA . GLY B 1 71 ? -47.767 61.379 28.906 1.0 81.98 ? ? ? ? ? ? 188 GLY B CA 1 71 B B +ATOM 5874 C C . GLY B 1 71 ? -46.492 62.198 28.806 1.0 84.97 ? ? ? ? ? ? 188 GLY B C 1 71 B B +ATOM 5875 O O . GLY B 1 71 ? -45.698 62.009 27.885 1.0 84.72 ? ? ? ? ? ? 188 GLY B O 1 71 B B +ATOM 5876 N N . THR B 1 72 ? -46.290 63.113 29.748 1.0 82.41 ? ? ? ? ? ? 189 THR B N 1 72 B B +ATOM 5877 C CA . THR B 1 72 ? -45.092 63.943 29.742 1.0 86.07 ? ? ? ? ? ? 189 THR B CA 1 72 B B +ATOM 5878 C C . THR B 1 72 ? -43.887 63.085 30.120 1.0 92.27 ? ? ? ? ? ? 189 THR B C 1 72 B B +ATOM 5879 O O . THR B 1 72 ? -42.758 63.363 29.711 1.0 100.0 ? ? ? ? ? ? 189 THR B O 1 72 B B +ATOM 5880 C CB . THR B 1 72 ? -45.216 65.116 30.739 1.0 93.08 ? ? ? ? ? ? 189 THR B CB 1 72 B B +ATOM 5881 O OG1 . THR B 1 72 ? -46.256 66.001 30.306 1.0 87.08 ? ? ? ? ? ? 189 THR B OG1 1 72 B B +ATOM 5882 C CG2 . THR B 1 72 ? -43.908 65.893 30.823 1.0 99.21 ? ? ? ? ? ? 189 THR B CG2 1 72 B B +ATOM 5883 N N . VAL B 1 73 ? -44.139 62.040 30.904 1.0 94.3 ? ? ? ? ? ? 190 VAL B N 1 73 B B +ATOM 5884 C CA . VAL B 1 73 ? -43.084 61.127 31.335 1.0 94.99 ? ? ? ? ? ? 190 VAL B CA 1 73 B B +ATOM 5885 C C . VAL B 1 73 ? -42.996 59.950 30.367 1.0 100.0 ? ? ? ? ? ? 190 VAL B C 1 73 B B +ATOM 5886 O O . VAL B 1 73 ? -41.918 59.410 30.118 1.0 100.0 ? ? ? ? ? ? 190 VAL B O 1 73 B B +ATOM 5887 C CB . VAL B 1 73 ? -43.356 60.581 32.750 1.0 96.95 ? ? ? ? ? ? 190 VAL B CB 1 73 B B +ATOM 5888 C CG1 . VAL B 1 73 ? -42.119 59.871 33.275 1.0 100.0 ? ? ? ? ? ? 190 VAL B CG1 1 73 B B +ATOM 5889 C CG2 . VAL B 1 73 ? -43.757 61.710 33.676 1.0 93.72 ? ? ? ? ? ? 190 VAL B CG2 1 73 B B +ATOM 5890 N N . PHE B 1 74 ? -44.147 59.560 29.826 1.0 100.0 ? ? ? ? ? ? 191 PHE B N 1 74 B B +ATOM 5891 C CA . PHE B 1 74 ? -44.230 58.457 28.875 1.0 93.04 ? ? ? ? ? ? 191 PHE B CA 1 74 B B +ATOM 5892 C C . PHE B 1 74 ? -43.579 58.838 27.546 1.0 97.34 ? ? ? ? ? ? 191 PHE B C 1 74 B B +ATOM 5893 O O . PHE B 1 74 ? -43.198 57.974 26.760 1.0 100.0 ? ? ? ? ? ? 191 PHE B O 1 74 B B +ATOM 5894 C CB . PHE B 1 74 ? -45.693 58.087 28.639 1.0 89.23 ? ? ? ? ? ? 191 PHE B CB 1 74 B B +ATOM 5895 C CG . PHE B 1 74 ? -45.883 56.848 27.815 1.0 95.04 ? ? ? ? ? ? 191 PHE B CG 1 74 B B +ATOM 5896 C CD1 . PHE B 1 74 ? -46.034 55.607 28.427 1.0 100.0 ? ? ? ? ? ? 191 PHE B CD1 1 74 B B +ATOM 5897 C CD2 . PHE B 1 74 ? -45.930 56.921 26.425 1.0 91.88 ? ? ? ? ? ? 191 PHE B CD2 1 74 B B +ATOM 5898 C CE1 . PHE B 1 74 ? -46.233 54.453 27.666 1.0 100.0 ? ? ? ? ? ? 191 PHE B CE1 1 74 B B +ATOM 5899 C CE2 . PHE B 1 74 ? -46.128 55.776 25.654 1.0 95.25 ? ? ? ? ? ? 191 PHE B CE2 1 74 B B +ATOM 5900 C CZ . PHE B 1 74 ? -46.280 54.539 26.276 1.0 95.85 ? ? ? ? ? ? 191 PHE B CZ 1 74 B B +ATOM 5901 N N . LYS B 1 75 ? -43.463 60.137 27.295 1.0 99.92 ? ? ? ? ? ? 192 LYS B N 1 75 B B +ATOM 5902 C CA . LYS B 1 75 ? -42.850 60.620 26.063 1.0 91.4 ? ? ? ? ? ? 192 LYS B CA 1 75 B B +ATOM 5903 C C . LYS B 1 75 ? -41.360 60.847 26.269 1.0 88.92 ? ? ? ? ? ? 192 LYS B C 1 75 B B +ATOM 5904 O O . LYS B 1 75 ? -40.537 60.420 25.460 1.0 90.84 ? ? ? ? ? ? 192 LYS B O 1 75 B B +ATOM 5905 C CB . LYS B 1 75 ? -43.502 61.930 25.622 1.0 89.87 ? ? ? ? ? ? 192 LYS B CB 1 75 B B +ATOM 5906 C CG . LYS B 1 75 ? -42.948 62.483 24.322 1.0 89.83 ? ? ? ? ? ? 192 LYS B CG 1 75 B B +ATOM 5907 C CD . LYS B 1 75 ? -43.617 63.793 23.944 1.0 95.97 ? ? ? ? ? ? 192 LYS B CD 1 75 B B +ATOM 5908 C CE . LYS B 1 75 ? -44.966 63.552 23.284 1.0 100.0 ? ? ? ? ? ? 192 LYS B CE 1 75 B B +ATOM 5909 N NZ . LYS B 1 75 ? -44.828 63.083 21.877 1.0 92.77 ? ? ? ? ? ? 192 LYS B NZ 1 75 B B +ATOM 5910 N N . THR B 1 76 ? -41.025 61.524 27.363 1.0 81.15 ? ? ? ? ? ? 193 THR B N 1 76 B B +ATOM 5911 C CA . THR B 1 76 ? -39.640 61.830 27.698 1.0 85.66 ? ? ? ? ? ? 193 THR B CA 1 76 B B +ATOM 5912 C C . THR B 1 76 ? -38.766 60.586 27.848 1.0 94.76 ? ? ? ? ? ? 193 THR B C 1 76 B B +ATOM 5913 O O . THR B 1 76 ? -37.586 60.607 27.500 1.0 100.0 ? ? ? ? ? ? 193 THR B O 1 76 B B +ATOM 5914 C CB . THR B 1 76 ? -39.551 62.629 29.011 1.0 78.24 ? ? ? ? ? ? 193 THR B CB 1 76 B B +ATOM 5915 O OG1 . THR B 1 76 ? -38.175 62.821 29.363 1.0 84.32 ? ? ? ? ? ? 193 THR B OG1 1 76 B B +ATOM 5916 C CG2 . THR B 1 76 ? -40.244 61.883 30.127 1.0 86.03 ? ? ? ? ? ? 193 THR B CG2 1 76 B B +ATOM 5917 N N . LEU B 1 77 ? -39.348 59.505 28.361 1.0 100.0 ? ? ? ? ? ? 194 LEU B N 1 77 B B +ATOM 5918 C CA . LEU B 1 77 ? -38.602 58.265 28.573 1.0 100.0 ? ? ? ? ? ? 194 LEU B CA 1 77 B B +ATOM 5919 C C . LEU B 1 77 ? -38.678 57.253 27.426 1.0 93.7 ? ? ? ? ? ? 194 LEU B C 1 77 B B +ATOM 5920 O O . LEU B 1 77 ? -37.737 56.488 27.204 1.0 82.21 ? ? ? ? ? ? 194 LEU B O 1 77 B B +ATOM 5921 C CB . LEU B 1 77 ? -39.066 57.597 29.872 1.0 91.86 ? ? ? ? ? ? 194 LEU B CB 1 77 B B +ATOM 5922 C CG . LEU B 1 77 ? -38.785 58.369 31.166 1.0 86.06 ? ? ? ? ? ? 194 LEU B CG 1 77 B B +ATOM 5923 C CD1 . LEU B 1 77 ? -39.424 57.643 32.339 1.0 79.72 ? ? ? ? ? ? 194 LEU B CD1 1 77 B B +ATOM 5924 C CD2 . LEU B 1 77 ? -37.287 58.507 31.375 1.0 72.84 ? ? ? ? ? ? 194 LEU B CD2 1 77 B B +ATOM 5925 N N . LYS B 1 78 ? -39.792 57.245 26.703 1.0 90.86 ? ? ? ? ? ? 195 LYS B N 1 78 B B +ATOM 5926 C CA . LYS B 1 78 ? -39.966 56.314 25.594 1.0 93.04 ? ? ? ? ? ? 195 LYS B CA 1 78 B B +ATOM 5927 C C . LYS B 1 78 ? -38.857 56.433 24.554 1.0 98.88 ? ? ? ? ? ? 195 LYS B C 1 78 B B +ATOM 5928 O O . LYS B 1 78 ? -38.557 55.476 23.835 1.0 99.95 ? ? ? ? ? ? 195 LYS B O 1 78 B B +ATOM 5929 C CB . LYS B 1 78 ? -41.314 56.541 24.914 1.0 91.45 ? ? ? ? ? ? 195 LYS B CB 1 78 B B +ATOM 5930 C CG . LYS B 1 78 ? -41.628 55.517 23.837 1.0 94.15 ? ? ? ? ? ? 195 LYS B CG 1 78 B B +ATOM 5931 C CD . LYS B 1 78 ? -43.096 55.548 23.452 1.0 98.91 ? ? ? ? ? ? 195 LYS B CD 1 78 B B +ATOM 5932 C CE . LYS B 1 78 ? -43.339 54.760 22.173 1.0 100.0 ? ? ? ? ? ? 195 LYS B CE 1 78 B B +ATOM 5933 N NZ . LYS B 1 78 ? -42.958 53.326 22.314 1.0 100.0 ? ? ? ? ? ? 195 LYS B NZ 1 78 B B +ATOM 5934 N N . SER B 1 79 ? -38.254 57.613 24.473 1.0 100.0 ? ? ? ? ? ? 196 SER B N 1 79 B B +ATOM 5935 C CA . SER B 1 79 ? -37.185 57.854 23.514 1.0 100.0 ? ? ? ? ? ? 196 SER B CA 1 79 B B +ATOM 5936 C C . SER B 1 79 ? -35.855 57.233 23.940 1.0 100.0 ? ? ? ? ? ? 196 SER B C 1 79 B B +ATOM 5937 O O . SER B 1 79 ? -35.123 56.691 23.111 1.0 100.0 ? ? ? ? ? ? 196 SER B O 1 79 B B +ATOM 5938 C CB . SER B 1 79 ? -36.998 59.360 23.308 1.0 100.0 ? ? ? ? ? ? 196 SER B CB 1 79 B B +ATOM 5939 O OG . SER B 1 79 ? -36.493 59.977 24.484 1.0 100.0 ? ? ? ? ? ? 196 SER B OG 1 79 B B +ATOM 5940 N N . LEU B 1 80 ? -35.554 57.304 25.235 1.0 100.0 ? ? ? ? ? ? 197 LEU B N 1 80 B B +ATOM 5941 C CA . LEU B 1 80 ? -34.298 56.776 25.764 1.0 98.58 ? ? ? ? ? ? 197 LEU B CA 1 80 B B +ATOM 5942 C C . LEU B 1 80 ? -34.289 55.302 26.163 1.0 98.97 ? ? ? ? ? ? 197 LEU B C 1 80 B B +ATOM 5943 O O . LEU B 1 80 ? -33.298 54.820 26.710 1.0 92.55 ? ? ? ? ? ? 197 LEU B O 1 80 B B +ATOM 5944 C CB . LEU B 1 80 ? -33.853 57.598 26.977 1.0 95.15 ? ? ? ? ? ? 197 LEU B CB 1 80 B B +ATOM 5945 C CG . LEU B 1 80 ? -33.921 59.126 26.908 1.0 86.6 ? ? ? ? ? ? 197 LEU B CG 1 80 B B +ATOM 5946 C CD1 . LEU B 1 80 ? -33.402 59.698 28.215 1.0 88.71 ? ? ? ? ? ? 197 LEU B CD1 1 80 B B +ATOM 5947 C CD2 . LEU B 1 80 ? -33.098 59.641 25.740 1.0 83.91 ? ? ? ? ? ? 197 LEU B CD2 1 80 B B +ATOM 5948 N N . TYR B 1 81 ? -35.371 54.580 25.894 1.0 100.0 ? ? ? ? ? ? 198 TYR B N 1 81 B B +ATOM 5949 C CA . TYR B 1 81 ? -35.414 53.171 26.273 1.0 100.0 ? ? ? ? ? ? 198 TYR B CA 1 81 B B +ATOM 5950 C C . TYR B 1 81 ? -34.663 52.246 25.322 1.0 100.0 ? ? ? ? ? ? 198 TYR B C 1 81 B B +ATOM 5951 O O . TYR B 1 81 ? -33.847 51.434 25.759 1.0 98.32 ? ? ? ? ? ? 198 TYR B O 1 81 B B +ATOM 5952 C CB . TYR B 1 81 ? -36.862 52.709 26.428 1.0 100.0 ? ? ? ? ? ? 198 TYR B CB 1 81 B B +ATOM 5953 C CG . TYR B 1 81 ? -37.453 53.058 27.773 1.0 100.0 ? ? ? ? ? ? 198 TYR B CG 1 81 B B +ATOM 5954 C CD1 . TYR B 1 81 ? -36.640 53.178 28.904 1.0 100.0 ? ? ? ? ? ? 198 TYR B CD1 1 81 B B +ATOM 5955 C CD2 . TYR B 1 81 ? -38.820 53.301 27.914 1.0 95.8 ? ? ? ? ? ? 198 TYR B CD2 1 81 B B +ATOM 5956 C CE1 . TYR B 1 81 ? -37.172 53.533 30.140 1.0 100.0 ? ? ? ? ? ? 198 TYR B CE1 1 81 B B +ATOM 5957 C CE2 . TYR B 1 81 ? -39.363 53.656 29.145 1.0 99.81 ? ? ? ? ? ? 198 TYR B CE2 1 81 B B +ATOM 5958 C CZ . TYR B 1 81 ? -38.533 53.772 30.253 1.0 100.0 ? ? ? ? ? ? 198 TYR B CZ 1 81 B B +ATOM 5959 O OH . TYR B 1 81 ? -39.064 54.120 31.476 1.0 100.0 ? ? ? ? ? ? 198 TYR B OH 1 81 B B +ATOM 5960 N N . LYS B 1 82 ? -34.938 52.355 24.028 1.0 100.0 ? ? ? ? ? ? 199 LYS B N 1 82 B B +ATOM 5961 C CA . LYS B 1 82 ? -34.246 51.514 23.055 1.0 100.0 ? ? ? ? ? ? 199 LYS B CA 1 82 B B +ATOM 5962 C C . LYS B 1 82 ? -32.763 51.847 23.107 1.0 98.56 ? ? ? ? ? ? 199 LYS B C 1 82 B B +ATOM 5963 O O . LYS B 1 82 ? -31.910 51.053 22.702 1.0 100.0 ? ? ? ? ? ? 199 LYS B O 1 82 B B +ATOM 5964 C CB . LYS B 1 82 ? -34.780 51.771 21.647 1.0 100.0 ? ? ? ? ? ? 199 LYS B CB 1 82 B B +ATOM 5965 C CG . LYS B 1 82 ? -34.889 53.241 21.288 1.0 95.6 ? ? ? ? ? ? 199 LYS B CG 1 82 B B +ATOM 5966 C CD . LYS B 1 82 ? -35.785 53.433 20.077 1.0 100.0 ? ? ? ? ? ? 199 LYS B CD 1 82 B B +ATOM 5967 C CE . LYS B 1 82 ? -37.207 52.982 20.376 1.0 100.0 ? ? ? ? ? ? 199 LYS B CE 1 82 B B +ATOM 5968 N NZ . LYS B 1 82 ? -37.774 53.690 21.559 1.0 97.17 ? ? ? ? ? ? 199 LYS B NZ 1 82 B B +ATOM 5969 N N . THR B 1 83 ? -32.468 53.034 23.617 1.0 91.15 ? ? ? ? ? ? 200 THR B N 1 83 B B +ATOM 5970 C CA . THR B 1 83 ? -31.097 53.492 23.726 1.0 95.96 ? ? ? ? ? ? 200 THR B CA 1 83 B B +ATOM 5971 C C . THR B 1 83 ? -30.414 53.014 25.002 1.0 100.0 ? ? ? ? ? ? 200 THR B C 1 83 B B +ATOM 5972 O O . THR B 1 83 ? -29.512 52.175 24.960 1.0 100.0 ? ? ? ? ? ? 200 THR B O 1 83 B B +ATOM 5973 C CB . THR B 1 83 ? -31.030 55.027 23.691 1.0 89.26 ? ? ? ? ? ? 200 THR B CB 1 83 B B +ATOM 5974 O OG1 . THR B 1 83 ? -31.846 55.512 22.621 1.0 100.0 ? ? ? ? ? ? 200 THR B OG1 1 83 B B +ATOM 5975 C CG2 . THR B 1 83 ? -29.595 55.495 23.486 1.0 84.09 ? ? ? ? ? ? 200 THR B CG2 1 83 B B +ATOM 5976 N N . HIS B 1 84 ? -30.858 53.552 26.134 1.0 100.0 ? ? ? ? ? ? 201 HIS B N 1 84 B B +ATOM 5977 C CA . HIS B 1 84 ? -30.272 53.227 27.432 1.0 100.0 ? ? ? ? ? ? 201 HIS B CA 1 84 B B +ATOM 5978 C C . HIS B 1 84 ? -30.853 52.025 28.187 1.0 100.0 ? ? ? ? ? ? 201 HIS B C 1 84 B B +ATOM 5979 O O . HIS B 1 84 ? -30.129 51.347 28.921 1.0 100.0 ? ? ? ? ? ? 201 HIS B O 1 84 B B +ATOM 5980 C CB . HIS B 1 84 ? -30.327 54.467 28.334 1.0 98.58 ? ? ? ? ? ? 201 HIS B CB 1 84 B B +ATOM 5981 C CG . HIS B 1 84 ? -29.696 55.685 27.729 1.0 100.0 ? ? ? ? ? ? 201 HIS B CG 1 84 B B +ATOM 5982 N ND1 . HIS B 1 84 ? -28.465 55.654 27.108 1.0 100.0 ? ? ? ? ? ? 201 HIS B ND1 1 84 B B +ATOM 5983 C CD2 . HIS B 1 84 ? -30.123 56.967 27.655 1.0 94.96 ? ? ? ? ? ? 201 HIS B CD2 1 84 B B +ATOM 5984 C CE1 . HIS B 1 84 ? -28.161 56.867 26.679 1.0 100.0 ? ? ? ? ? ? 201 HIS B CE1 1 84 B B +ATOM 5985 N NE2 . HIS B 1 84 ? -29.150 57.682 26.998 1.0 95.85 ? ? ? ? ? ? 201 HIS B NE2 1 84 B B +ATOM 5986 N N . ALA B 1 85 ? -32.143 51.755 28.016 1.0 99.68 ? ? ? ? ? ? 202 ALA B N 1 85 B B +ATOM 5987 C CA . ALA B 1 85 ? -32.779 50.636 28.713 1.0 100.0 ? ? ? ? ? ? 202 ALA B CA 1 85 B B +ATOM 5988 C C . ALA B 1 85 ? -32.249 49.277 28.262 1.0 100.0 ? ? ? ? ? ? 202 ALA B C 1 85 B B +ATOM 5989 O O . ALA B 1 85 ? -31.786 49.123 27.132 1.0 100.0 ? ? ? ? ? ? 202 ALA B O 1 85 B B +ATOM 5990 C CB . ALA B 1 85 ? -34.286 50.693 28.525 1.0 100.0 ? ? ? ? ? ? 202 ALA B CB 1 85 B B +ATOM 5991 N N . CYS B 1 86 ? -32.325 48.294 29.158 1.0 100.0 ? ? ? ? ? ? 203 CYS B N 1 86 B B +ATOM 5992 C CA . CYS B 1 86 ? -31.852 46.942 28.869 1.0 100.0 ? ? ? ? ? ? 203 CYS B CA 1 86 B B +ATOM 5993 C C . CYS B 1 86 ? -32.794 46.178 27.945 1.0 100.0 ? ? ? ? ? ? 203 CYS B C 1 86 B B +ATOM 5994 O O . CYS B 1 86 ? -33.970 46.520 27.808 1.0 96.91 ? ? ? ? ? ? 203 CYS B O 1 86 B B +ATOM 5995 C CB . CYS B 1 86 ? -31.654 46.161 30.172 1.0 98.58 ? ? ? ? ? ? 203 CYS B CB 1 86 B B +ATOM 5996 S SG . CYS B 1 86 ? -33.178 45.661 31.002 1.0 100.0 ? ? ? ? ? ? 203 CYS B SG 1 86 B B +ATOM 5997 N N . TYR B 1 87 ? -32.258 45.134 27.322 1.0 96.51 ? ? ? ? ? ? 204 TYR B N 1 87 B B +ATOM 5998 C CA . TYR B 1 87 ? -33.006 44.308 26.384 1.0 100.0 ? ? ? ? ? ? 204 TYR B CA 1 87 B B +ATOM 5999 C C . TYR B 1 87 ? -34.351 43.802 26.903 1.0 100.0 ? ? ? ? ? ? 204 TYR B C 1 87 B B +ATOM 6000 O O . TYR B 1 87 ? -35.390 44.052 26.292 1.0 90.91 ? ? ? ? ? ? 204 TYR B O 1 87 B B +ATOM 6001 C CB . TYR B 1 87 ? -32.141 43.120 25.945 1.0 100.0 ? ? ? ? ? ? 204 TYR B CB 1 87 B B +ATOM 6002 C CG . TYR B 1 87 ? -32.922 41.955 25.379 1.0 100.0 ? ? ? ? ? ? 204 TYR B CG 1 87 B B +ATOM 6003 C CD1 . TYR B 1 87 ? -33.793 42.131 24.303 1.0 100.0 ? ? ? ? ? ? 204 TYR B CD1 1 87 B B +ATOM 6004 C CD2 . TYR B 1 87 ? -32.796 40.676 25.924 1.0 100.0 ? ? ? ? ? ? 204 TYR B CD2 1 87 B B +ATOM 6005 C CE1 . TYR B 1 87 ? -34.519 41.063 23.782 1.0 100.0 ? ? ? ? ? ? 204 TYR B CE1 1 87 B B +ATOM 6006 C CE2 . TYR B 1 87 ? -33.517 39.600 25.411 1.0 100.0 ? ? ? ? ? ? 204 TYR B CE2 1 87 B B +ATOM 6007 C CZ . TYR B 1 87 ? -34.376 39.802 24.340 1.0 100.0 ? ? ? ? ? ? 204 TYR B CZ 1 87 B B +ATOM 6008 O OH . TYR B 1 87 ? -35.084 38.746 23.817 1.0 100.0 ? ? ? ? ? ? 204 TYR B OH 1 87 B B +ATOM 6009 N N . GLU B 1 88 ? -34.328 43.083 28.021 1.0 97.1 ? ? ? ? ? ? 205 GLU B N 1 88 B B +ATOM 6010 C CA . GLU B 1 88 ? -35.553 42.530 28.597 1.0 92.62 ? ? ? ? ? ? 205 GLU B CA 1 88 B B +ATOM 6011 C C . GLU B 1 88 ? -36.654 43.579 28.684 1.0 92.8 ? ? ? ? ? ? 205 GLU B C 1 88 B B +ATOM 6012 O O . GLU B 1 88 ? -37.841 43.255 28.672 1.0 84.27 ? ? ? ? ? ? 205 GLU B O 1 88 B B +ATOM 6013 C CB . GLU B 1 88 ? -35.272 41.955 29.986 1.0 90.09 ? ? ? ? ? ? 205 GLU B CB 1 88 B B +ATOM 6014 C CG . GLU B 1 88 ? -34.184 40.892 30.008 1.0 94.04 ? ? ? ? ? ? 205 GLU B CG 1 88 B B +ATOM 6015 C CD . GLU B 1 88 ? -32.797 41.475 29.805 1.0 100.0 ? ? ? ? ? ? 205 GLU B CD 1 88 B B +ATOM 6016 O OE1 . GLU B 1 88 ? -31.881 40.718 29.418 1.0 100.0 ? ? ? ? ? ? 205 GLU B OE1 1 88 B B +ATOM 6017 O OE2 . GLU B 1 88 ? -32.623 42.693 30.035 1.0 100.0 ? ? ? ? ? ? 205 GLU B OE2 1 88 B B +ATOM 6018 N N . TYR B 1 89 ? -36.245 44.840 28.766 1.0 96.17 ? ? ? ? ? ? 206 TYR B N 1 89 B B +ATOM 6019 C CA . TYR B 1 89 ? -37.179 45.955 28.847 1.0 95.19 ? ? ? ? ? ? 206 TYR B CA 1 89 B B +ATOM 6020 C C . TYR B 1 89 ? -37.727 46.260 27.461 1.0 89.6 ? ? ? ? ? ? 206 TYR B C 1 89 B B +ATOM 6021 O O . TYR B 1 89 ? -38.939 46.291 27.248 1.0 82.02 ? ? ? ? ? ? 206 TYR B O 1 89 B B +ATOM 6022 C CB . TYR B 1 89 ? -36.468 47.196 29.398 1.0 96.64 ? ? ? ? ? ? 206 TYR B CB 1 89 B B +ATOM 6023 C CG . TYR B 1 89 ? -37.394 48.297 29.869 1.0 100.0 ? ? ? ? ? ? 206 TYR B CG 1 89 B B +ATOM 6024 C CD1 . TYR B 1 89 ? -37.405 48.698 31.205 1.0 96.4 ? ? ? ? ? ? 206 TYR B CD1 1 89 B B +ATOM 6025 C CD2 . TYR B 1 89 ? -38.247 48.952 28.977 1.0 100.0 ? ? ? ? ? ? 206 TYR B CD2 1 89 B B +ATOM 6026 C CE1 . TYR B 1 89 ? -38.238 49.723 31.640 1.0 92.61 ? ? ? ? ? ? 206 TYR B CE1 1 89 B B +ATOM 6027 C CE2 . TYR B 1 89 ? -39.084 49.980 29.403 1.0 88.45 ? ? ? ? ? ? 206 TYR B CE2 1 89 B B +ATOM 6028 C CZ . TYR B 1 89 ? -39.073 50.358 30.734 1.0 92.44 ? ? ? ? ? ? 206 TYR B CZ 1 89 B B +ATOM 6029 O OH . TYR B 1 89 ? -39.897 51.370 31.161 1.0 100.0 ? ? ? ? ? ? 206 TYR B OH 1 89 B B +ATOM 6030 N N . ASN B 1 90 ? -36.812 46.487 26.524 1.0 89.21 ? ? ? ? ? ? 207 ASN B N 1 90 B B +ATOM 6031 C CA . ASN B 1 90 ? -37.168 46.801 25.149 1.0 83.61 ? ? ? ? ? ? 207 ASN B CA 1 90 B B +ATOM 6032 C C . ASN B 1 90 ? -37.959 45.678 24.494 1.0 81.92 ? ? ? ? ? ? 207 ASN B C 1 90 B B +ATOM 6033 O O . ASN B 1 90 ? -38.674 45.907 23.519 1.0 87.79 ? ? ? ? ? ? 207 ASN B O 1 90 B B +ATOM 6034 C CB . ASN B 1 90 ? -35.902 47.084 24.337 1.0 84.88 ? ? ? ? ? ? 207 ASN B CB 1 90 B B +ATOM 6035 C CG . ASN B 1 90 ? -35.139 48.295 24.845 1.0 85.25 ? ? ? ? ? ? 207 ASN B CG 1 90 B B +ATOM 6036 O OD1 . ASN B 1 90 ? -35.662 49.409 24.853 1.0 93.52 ? ? ? ? ? ? 207 ASN B OD1 1 90 B B +ATOM 6037 N ND2 . ASN B 1 90 ? -33.899 48.083 25.273 1.0 56.4 ? ? ? ? ? ? 207 ASN B ND2 1 90 B B +ATOM 6038 N N . HIS B 1 91 ? -37.833 44.468 25.032 1.0 79.44 ? ? ? ? ? ? 208 HIS B N 1 91 B B +ATOM 6039 C CA . HIS B 1 91 ? -38.541 43.318 24.481 1.0 79.24 ? ? ? ? ? ? 208 HIS B CA 1 91 B B +ATOM 6040 C C . HIS B 1 91 ? -39.998 43.281 24.925 1.0 82.31 ? ? ? ? ? ? 208 HIS B C 1 91 B B +ATOM 6041 O O . HIS B 1 91 ? -40.906 43.124 24.110 1.0 88.47 ? ? ? ? ? ? 208 HIS B O 1 91 B B +ATOM 6042 C CB . HIS B 1 91 ? -37.857 42.014 24.900 1.0 71.64 ? ? ? ? ? ? 208 HIS B CB 1 91 B B +ATOM 6043 C CG . HIS B 1 91 ? -38.719 40.800 24.725 1.0 94.11 ? ? ? ? ? ? 208 HIS B CG 1 91 B B +ATOM 6044 N ND1 . HIS B 1 91 ? -39.030 39.951 25.765 1.0 100.0 ? ? ? ? ? ? 208 HIS B ND1 1 91 B B +ATOM 6045 C CD2 . HIS B 1 91 ? -39.352 40.307 23.635 1.0 97.39 ? ? ? ? ? ? 208 HIS B CD2 1 91 B B +ATOM 6046 C CE1 . HIS B 1 91 ? -39.817 38.986 25.323 1.0 100.0 ? ? ? ? ? ? 208 HIS B CE1 1 91 B B +ATOM 6047 N NE2 . HIS B 1 91 ? -40.029 39.178 24.033 1.0 97.55 ? ? ? ? ? ? 208 HIS B NE2 1 91 B B +ATOM 6048 N N . ILE B 1 92 ? -40.212 43.433 26.224 1.0 87.23 ? ? ? ? ? ? 209 ILE B N 1 92 B B +ATOM 6049 C CA . ILE B 1 92 ? -41.552 43.386 26.789 1.0 88.32 ? ? ? ? ? ? 209 ILE B CA 1 92 B B +ATOM 6050 C C . ILE B 1 92 ? -42.419 44.618 26.548 1.0 88.65 ? ? ? ? ? ? 209 ILE B C 1 92 B B +ATOM 6051 O O . ILE B 1 92 ? -43.648 44.517 26.506 1.0 79.81 ? ? ? ? ? ? 209 ILE B O 1 92 B B +ATOM 6052 C CB . ILE B 1 92 ? -41.487 43.134 28.311 1.0 92.64 ? ? ? ? ? ? 209 ILE B CB 1 92 B B +ATOM 6053 C CG1 . ILE B 1 92 ? -42.887 42.823 28.844 1.0 100.0 ? ? ? ? ? ? 209 ILE B CG1 1 92 B B +ATOM 6054 C CG2 . ILE B 1 92 ? -40.884 44.345 29.015 1.0 84.88 ? ? ? ? ? ? 209 ILE B CG2 1 92 B B +ATOM 6055 C CD1 . ILE B 1 92 ? -43.500 41.575 28.247 1.0 100.0 ? ? ? ? ? ? 209 ILE B CD1 1 92 B B +ATOM 6056 N N . PHE B 1 93 ? -41.786 45.777 26.387 1.0 92.19 ? ? ? ? ? ? 210 PHE B N 1 93 B B +ATOM 6057 C CA . PHE B 1 93 ? -42.529 47.018 26.187 1.0 91.92 ? ? ? ? ? ? 210 PHE B CA 1 93 B B +ATOM 6058 C C . PHE B 1 93 ? -43.615 46.943 25.123 1.0 96.44 ? ? ? ? ? ? 210 PHE B C 1 93 B B +ATOM 6059 O O . PHE B 1 93 ? -44.789 47.157 25.419 1.0 100.0 ? ? ? ? ? ? 210 PHE B O 1 93 B B +ATOM 6060 C CB . PHE B 1 93 ? -41.583 48.175 25.864 1.0 89.4 ? ? ? ? ? ? 210 PHE B CB 1 93 B B +ATOM 6061 C CG . PHE B 1 93 ? -41.924 49.453 26.582 1.0 97.33 ? ? ? ? ? ? 210 PHE B CG 1 93 B B +ATOM 6062 C CD1 . PHE B 1 93 ? -42.113 50.638 25.877 1.0 98.81 ? ? ? ? ? ? 210 PHE B CD1 1 93 B B +ATOM 6063 C CD2 . PHE B 1 93 ? -42.055 49.471 27.966 1.0 97.14 ? ? ? ? ? ? 210 PHE B CD2 1 93 B B +ATOM 6064 C CE1 . PHE B 1 93 ? -42.428 51.822 26.546 1.0 100.0 ? ? ? ? ? ? 210 PHE B CE1 1 93 B B +ATOM 6065 C CE2 . PHE B 1 93 ? -42.369 50.649 28.643 1.0 86.56 ? ? ? ? ? ? 210 PHE B CE2 1 93 B B +ATOM 6066 C CZ . PHE B 1 93 ? -42.555 51.826 27.930 1.0 85.39 ? ? ? ? ? ? 210 PHE B CZ 1 93 B B +ATOM 6067 N N . PRO B 1 94 ? -43.242 46.628 23.871 1.0 93.67 ? ? ? ? ? ? 211 PRO B N 1 94 B B +ATOM 6068 C CA . PRO B 1 94 ? -44.285 46.560 22.841 1.0 92.3 ? ? ? ? ? ? 211 PRO B CA 1 94 B B +ATOM 6069 C C . PRO B 1 94 ? -45.448 45.640 23.215 1.0 94.73 ? ? ? ? ? ? 211 PRO B C 1 94 B B +ATOM 6070 O O . PRO B 1 94 ? -46.543 45.758 22.660 1.0 82.46 ? ? ? ? ? ? 211 PRO B O 1 94 B B +ATOM 6071 C CB . PRO B 1 94 ? -43.533 46.083 21.600 1.0 98.76 ? ? ? ? ? ? 211 PRO B CB 1 94 B B +ATOM 6072 C CG . PRO B 1 94 ? -42.102 46.420 21.860 1.0 100.0 ? ? ? ? ? ? 211 PRO B CG 1 94 B B +ATOM 6073 C CD . PRO B 1 94 ? -41.909 46.306 23.340 1.0 92.28 ? ? ? ? ? ? 211 PRO B CD 1 94 B B +ATOM 6074 N N . LEU B 1 95 ? -45.208 44.729 24.159 1.0 99.82 ? ? ? ? ? ? 212 LEU B N 1 95 B B +ATOM 6075 C CA . LEU B 1 95 ? -46.246 43.802 24.615 1.0 97.01 ? ? ? ? ? ? 212 LEU B CA 1 95 B B +ATOM 6076 C C . LEU B 1 95 ? -47.076 44.486 25.697 1.0 97.71 ? ? ? ? ? ? 212 LEU B C 1 95 B B +ATOM 6077 O O . LEU B 1 95 ? -48.273 44.235 25.832 1.0 97.78 ? ? ? ? ? ? 212 LEU B O 1 95 B B +ATOM 6078 C CB . LEU B 1 95 ? -45.618 42.527 25.186 1.0 82.77 ? ? ? ? ? ? 212 LEU B CB 1 95 B B +ATOM 6079 C CG . LEU B 1 95 ? -44.915 41.595 24.197 1.0 72.26 ? ? ? ? ? ? 212 LEU B CG 1 95 B B +ATOM 6080 C CD1 . LEU B 1 95 ? -43.927 40.716 24.946 1.0 59.9 ? ? ? ? ? ? 212 LEU B CD1 1 95 B B +ATOM 6081 C CD2 . LEU B 1 95 ? -45.943 40.756 23.456 1.0 57.54 ? ? ? ? ? ? 212 LEU B CD2 1 95 B B +ATOM 6082 N N . LEU B 1 96 ? -46.421 45.345 26.474 1.0 96.22 ? ? ? ? ? ? 213 LEU B N 1 96 B B +ATOM 6083 C CA . LEU B 1 96 ? -47.088 46.091 27.533 1.0 93.39 ? ? ? ? ? ? 213 LEU B CA 1 96 B B +ATOM 6084 C C . LEU B 1 96 ? -47.961 47.145 26.864 1.0 93.86 ? ? ? ? ? ? 213 LEU B C 1 96 B B +ATOM 6085 O O . LEU B 1 96 ? -49.097 47.381 27.274 1.0 84.52 ? ? ? ? ? ? 213 LEU B O 1 96 B B +ATOM 6086 C CB . LEU B 1 96 ? -46.057 46.780 28.430 1.0 82.97 ? ? ? ? ? ? 213 LEU B CB 1 96 B B +ATOM 6087 C CG . LEU B 1 96 ? -45.335 45.925 29.472 1.0 75.57 ? ? ? ? ? ? 213 LEU B CG 1 96 B B +ATOM 6088 C CD1 . LEU B 1 96 ? -44.108 46.673 29.983 1.0 65.93 ? ? ? ? ? ? 213 LEU B CD1 1 96 B B +ATOM 6089 C CD2 . LEU B 1 96 ? -46.291 45.595 30.608 1.0 63.3 ? ? ? ? ? ? 213 LEU B CD2 1 96 B B +ATOM 6090 N N . GLU B 1 97 ? -47.410 47.775 25.830 1.0 97.38 ? ? ? ? ? ? 214 GLU B N 1 97 B B +ATOM 6091 C CA . GLU B 1 97 ? -48.115 48.806 25.084 1.0 94.83 ? ? ? ? ? ? 214 GLU B CA 1 97 B B +ATOM 6092 C C . GLU B 1 97 ? -49.301 48.194 24.358 1.0 95.6 ? ? ? ? ? ? 214 GLU B C 1 97 B B +ATOM 6093 O O . GLU B 1 97 ? -50.414 48.716 24.417 1.0 100.0 ? ? ? ? ? ? 214 GLU B O 1 97 B B +ATOM 6094 C CB . GLU B 1 97 ? -47.170 49.466 24.073 1.0 96.63 ? ? ? ? ? ? 214 GLU B CB 1 97 B B +ATOM 6095 C CG . GLU B 1 97 ? -45.891 50.020 24.688 1.0 100.0 ? ? ? ? ? ? 214 GLU B CG 1 97 B B +ATOM 6096 C CD . GLU B 1 97 ? -44.930 50.587 23.650 1.0 100.0 ? ? ? ? ? ? 214 GLU B CD 1 97 B B +ATOM 6097 O OE1 . GLU B 1 97 ? -43.874 49.960 23.406 1.0 99.52 ? ? ? ? ? ? 214 GLU B OE1 1 97 B B +ATOM 6098 O OE2 . GLU B 1 97 ? -45.230 51.660 23.079 1.0 100.0 ? ? ? ? ? ? 214 GLU B OE2 1 97 B B +ATOM 6099 N N . LYS B 1 98 ? -49.056 47.080 23.677 1.0 84.05 ? ? ? ? ? ? 215 LYS B N 1 98 B B +ATOM 6100 C CA . LYS B 1 98 ? -50.100 46.398 22.926 1.0 96.51 ? ? ? ? ? ? 215 LYS B CA 1 98 B B +ATOM 6101 C C . LYS B 1 98 ? -51.109 45.654 23.799 1.0 100.0 ? ? ? ? ? ? 215 LYS B C 1 98 B B +ATOM 6102 O O . LYS B 1 98 ? -52.183 45.276 23.325 1.0 100.0 ? ? ? ? ? ? 215 LYS B O 1 98 B B +ATOM 6103 C CB . LYS B 1 98 ? -49.474 45.408 21.940 1.0 90.98 ? ? ? ? ? ? 215 LYS B CB 1 98 B B +ATOM 6104 C CG . LYS B 1 98 ? -50.489 44.764 21.005 1.0 100.0 ? ? ? ? ? ? 215 LYS B CG 1 98 B B +ATOM 6105 C CD . LYS B 1 98 ? -49.831 43.802 20.030 1.0 100.0 ? ? ? ? ? ? 215 LYS B CD 1 98 B B +ATOM 6106 C CE . LYS B 1 98 ? -49.099 44.550 18.924 1.0 100.0 ? ? ? ? ? ? 215 LYS B CE 1 98 B B +ATOM 6107 N NZ . LYS B 1 98 ? -50.022 45.378 18.094 1.0 100.0 ? ? ? ? ? ? 215 LYS B NZ 1 98 B B +ATOM 6108 N N . TYR B 1 99 ? -50.779 45.448 25.071 1.0 100.0 ? ? ? ? ? ? 216 TYR B N 1 99 B B +ATOM 6109 C CA . TYR B 1 99 ? -51.682 44.709 25.945 1.0 100.0 ? ? ? ? ? ? 216 TYR B CA 1 99 B B +ATOM 6110 C C . TYR B 1 99 ? -52.264 45.431 27.157 1.0 100.0 ? ? ? ? ? ? 216 TYR B C 1 99 B B +ATOM 6111 O O . TYR B 1 99 ? -53.485 45.526 27.296 1.0 100.0 ? ? ? ? ? ? 216 TYR B O 1 99 B B +ATOM 6112 C CB . TYR B 1 99 ? -50.998 43.413 26.388 1.0 92.17 ? ? ? ? ? ? 216 TYR B CB 1 99 B B +ATOM 6113 C CG . TYR B 1 99 ? -50.873 42.412 25.266 1.0 100.0 ? ? ? ? ? ? 216 TYR B CG 1 99 B B +ATOM 6114 C CD1 . TYR B 1 99 ? -49.658 42.219 24.603 1.0 100.0 ? ? ? ? ? ? 216 TYR B CD1 1 99 B B +ATOM 6115 C CD2 . TYR B 1 99 ? -51.980 41.682 24.837 1.0 100.0 ? ? ? ? ? ? 216 TYR B CD2 1 99 B B +ATOM 6116 C CE1 . TYR B 1 99 ? -49.551 41.323 23.541 1.0 100.0 ? ? ? ? ? ? 216 TYR B CE1 1 99 B B +ATOM 6117 C CE2 . TYR B 1 99 ? -51.886 40.786 23.779 1.0 100.0 ? ? ? ? ? ? 216 TYR B CE2 1 99 B B +ATOM 6118 C CZ . TYR B 1 99 ? -50.671 40.611 23.132 1.0 100.0 ? ? ? ? ? ? 216 TYR B CZ 1 99 B B +ATOM 6119 O OH . TYR B 1 99 ? -50.578 39.727 22.077 1.0 100.0 ? ? ? ? ? ? 216 TYR B OH 1 99 B B +ATOM 6120 N N . CYS B 1 100 ? -51.404 45.942 28.030 1.0 93.36 ? ? ? ? ? ? 217 CYS B N 1 100 B B +ATOM 6121 C CA . CYS B 1 100 ? -51.883 46.621 29.230 1.0 100.0 ? ? ? ? ? ? 217 CYS B CA 1 100 B B +ATOM 6122 C C . CYS B 1 100 ? -52.194 48.107 29.050 1.0 99.81 ? ? ? ? ? ? 217 CYS B C 1 100 B B +ATOM 6123 O O . CYS B 1 100 ? -52.236 48.867 30.020 1.0 100.0 ? ? ? ? ? ? 217 CYS B O 1 100 B B +ATOM 6124 C CB . CYS B 1 100 ? -50.873 46.434 30.363 1.0 100.0 ? ? ? ? ? ? 217 CYS B CB 1 100 B B +ATOM 6125 S SG . CYS B 1 100 ? -50.793 44.744 31.003 1.0 99.81 ? ? ? ? ? ? 217 CYS B SG 1 100 B B +ATOM 6126 N N . GLY B 1 101 ? -52.418 48.514 27.807 1.0 96.48 ? ? ? ? ? ? 218 GLY B N 1 101 B B +ATOM 6127 C CA . GLY B 1 101 ? -52.733 49.903 27.532 1.0 100.0 ? ? ? ? ? ? 218 GLY B CA 1 101 B B +ATOM 6128 C C . GLY B 1 101 ? -51.628 50.890 27.859 1.0 100.0 ? ? ? ? ? ? 218 GLY B C 1 101 B B +ATOM 6129 O O . GLY B 1 101 ? -51.888 51.962 28.411 1.0 100.0 ? ? ? ? ? ? 218 GLY B O 1 101 B B +ATOM 6130 N N . PHE B 1 102 ? -50.394 50.535 27.516 1.0 91.88 ? ? ? ? ? ? 219 PHE B N 1 102 B B +ATOM 6131 C CA . PHE B 1 102 ? -49.259 51.413 27.774 1.0 85.18 ? ? ? ? ? ? 219 PHE B CA 1 102 B B +ATOM 6132 C C . PHE B 1 102 ? -49.121 52.424 26.638 1.0 81.64 ? ? ? ? ? ? 219 PHE B C 1 102 B B +ATOM 6133 O O . PHE B 1 102 ? -48.424 52.183 25.654 1.0 74.36 ? ? ? ? ? ? 219 PHE B O 1 102 B B +ATOM 6134 C CB . PHE B 1 102 ? -47.973 50.591 27.920 1.0 73.24 ? ? ? ? ? ? 219 PHE B CB 1 102 B B +ATOM 6135 C CG . PHE B 1 102 ? -47.648 50.217 29.345 1.0 69.87 ? ? ? ? ? ? 219 PHE B CG 1 102 B B +ATOM 6136 C CD1 . PHE B 1 102 ? -48.500 49.389 30.071 1.0 60.24 ? ? ? ? ? ? 219 PHE B CD1 1 102 B B +ATOM 6137 C CD2 . PHE B 1 102 ? -46.496 50.699 29.965 1.0 66.24 ? ? ? ? ? ? 219 PHE B CD2 1 102 B B +ATOM 6138 C CE1 . PHE B 1 102 ? -48.210 49.040 31.391 1.0 52.33 ? ? ? ? ? ? 219 PHE B CE1 1 102 B B +ATOM 6139 C CE2 . PHE B 1 102 ? -46.197 50.356 31.286 1.0 54.7 ? ? ? ? ? ? 219 PHE B CE2 1 102 B B +ATOM 6140 C CZ . PHE B 1 102 ? -47.058 49.527 31.999 1.0 60.48 ? ? ? ? ? ? 219 PHE B CZ 1 102 B B +ATOM 6141 N N . HIS B 1 103 ? -49.807 53.555 26.786 1.0 87.91 ? ? ? ? ? ? 220 HIS B N 1 103 B B +ATOM 6142 C CA . HIS B 1 103 ? -49.788 54.630 25.799 1.0 89.49 ? ? ? ? ? ? 220 HIS B CA 1 103 B B +ATOM 6143 C C . HIS B 1 103 ? -49.810 55.967 26.538 1.0 91.78 ? ? ? ? ? ? 220 HIS B C 1 103 B B +ATOM 6144 O O . HIS B 1 103 ? -50.430 56.085 27.595 1.0 100.0 ? ? ? ? ? ? 220 HIS B O 1 103 B B +ATOM 6145 C CB . HIS B 1 103 ? -51.011 54.519 24.887 1.0 91.7 ? ? ? ? ? ? 220 HIS B CB 1 103 B B +ATOM 6146 C CG . HIS B 1 103 ? -50.961 55.426 23.700 1.0 99.12 ? ? ? ? ? ? 220 HIS B CG 1 103 B B +ATOM 6147 N ND1 . HIS B 1 103 ? -52.098 55.885 23.067 1.0 100.0 ? ? ? ? ? ? 220 HIS B ND1 1 103 B B +ATOM 6148 C CD2 . HIS B 1 103 ? -49.915 55.956 23.025 1.0 98.33 ? ? ? ? ? ? 220 HIS B CD2 1 103 B B +ATOM 6149 C CE1 . HIS B 1 103 ? -51.752 56.657 22.054 1.0 100.0 ? ? ? ? ? ? 220 HIS B CE1 1 103 B B +ATOM 6150 N NE2 . HIS B 1 103 ? -50.434 56.718 22.004 1.0 100.0 ? ? ? ? ? ? 220 HIS B NE2 1 103 B B +ATOM 6151 N N . GLU B 1 104 ? -49.142 56.972 25.983 1.0 82.47 ? ? ? ? ? ? 221 GLU B N 1 104 B B +ATOM 6152 C CA . GLU B 1 104 ? -49.091 58.282 26.624 1.0 87.65 ? ? ? ? ? ? 221 GLU B CA 1 104 B B +ATOM 6153 C C . GLU B 1 104 ? -50.453 58.933 26.820 1.0 84.85 ? ? ? ? ? ? 221 GLU B C 1 104 B B +ATOM 6154 O O . GLU B 1 104 ? -50.577 59.890 27.585 1.0 90.1 ? ? ? ? ? ? 221 GLU B O 1 104 B B +ATOM 6155 C CB . GLU B 1 104 ? -48.195 59.228 25.827 1.0 94.21 ? ? ? ? ? ? 221 GLU B CB 1 104 B B +ATOM 6156 C CG . GLU B 1 104 ? -48.565 59.340 24.363 1.0 96.06 ? ? ? ? ? ? 221 GLU B CG 1 104 B B +ATOM 6157 C CD . GLU B 1 104 ? -47.697 60.344 23.630 1.0 100.0 ? ? ? ? ? ? 221 GLU B CD 1 104 B B +ATOM 6158 O OE1 . GLU B 1 104 ? -48.044 60.709 22.485 1.0 100.0 ? ? ? ? ? ? 221 GLU B OE1 1 104 B B +ATOM 6159 O OE2 . GLU B 1 104 ? -46.669 60.768 24.203 1.0 100.0 ? ? ? ? ? ? 221 GLU B OE2 1 104 B B +ATOM 6160 N N . ASP B 1 105 ? -51.472 58.415 26.140 1.0 81.47 ? ? ? ? ? ? 222 ASP B N 1 105 B B +ATOM 6161 C CA . ASP B 1 105 ? -52.811 58.986 26.249 1.0 89.8 ? ? ? ? ? ? 222 ASP B CA 1 105 B B +ATOM 6162 C C . ASP B 1 105 ? -53.705 58.340 27.301 1.0 83.18 ? ? ? ? ? ? 222 ASP B C 1 105 B B +ATOM 6163 O O . ASP B 1 105 ? -54.786 58.854 27.605 1.0 81.72 ? ? ? ? ? ? 222 ASP B O 1 105 B B +ATOM 6164 C CB . ASP B 1 105 ? -53.502 58.943 24.888 1.0 99.15 ? ? ? ? ? ? 222 ASP B CB 1 105 B B +ATOM 6165 C CG . ASP B 1 105 ? -52.897 59.924 23.903 1.0 100.0 ? ? ? ? ? ? 222 ASP B CG 1 105 B B +ATOM 6166 O OD1 . ASP B 1 105 ? -51.778 59.654 23.418 1.0 100.0 ? ? ? ? ? ? 222 ASP B OD1 1 105 B B +ATOM 6167 O OD2 . ASP B 1 105 ? -53.532 60.964 23.618 1.0 95.35 ? ? ? ? ? ? 222 ASP B OD2 1 105 B B +ATOM 6168 N N . ASN B 1 106 ? -53.264 57.219 27.862 1.0 71.97 ? ? ? ? ? ? 223 ASN B N 1 106 B B +ATOM 6169 C CA . ASN B 1 106 ? -54.054 56.540 28.880 1.0 72.54 ? ? ? ? ? ? 223 ASN B CA 1 106 B B +ATOM 6170 C C . ASN B 1 106 ? -53.190 55.895 29.955 1.0 72.39 ? ? ? ? ? ? 223 ASN B C 1 106 B B +ATOM 6171 O O . ASN B 1 106 ? -52.209 55.214 29.650 1.0 73.04 ? ? ? ? ? ? 223 ASN B O 1 106 B B +ATOM 6172 C CB . ASN B 1 106 ? -54.945 55.470 28.246 1.0 83.69 ? ? ? ? ? ? 223 ASN B CB 1 106 B B +ATOM 6173 C CG . ASN B 1 106 ? -55.626 54.594 29.283 1.0 99.58 ? ? ? ? ? ? 223 ASN B CG 1 106 B B +ATOM 6174 O OD1 . ASN B 1 106 ? -55.320 53.406 29.409 1.0 100.0 ? ? ? ? ? ? 223 ASN B OD1 1 106 B B +ATOM 6175 N ND2 . ASN B 1 106 ? -56.553 55.180 30.036 1.0 88.17 ? ? ? ? ? ? 223 ASN B ND2 1 106 B B +ATOM 6176 N N . ILE B 1 107 ? -53.557 56.115 31.214 1.0 67.74 ? ? ? ? ? ? 224 ILE B N 1 107 B B +ATOM 6177 C CA . ILE B 1 107 ? -52.821 55.538 32.334 1.0 61.97 ? ? ? ? ? ? 224 ILE B CA 1 107 B B +ATOM 6178 C C . ILE B 1 107 ? -53.280 54.093 32.536 1.0 66.83 ? ? ? ? ? ? 224 ILE B C 1 107 B B +ATOM 6179 O O . ILE B 1 107 ? -54.469 53.830 32.727 1.0 69.52 ? ? ? ? ? ? 224 ILE B O 1 107 B B +ATOM 6180 C CB . ILE B 1 107 ? -53.058 56.341 33.628 1.0 58.97 ? ? ? ? ? ? 224 ILE B CB 1 107 B B +ATOM 6181 C CG1 . ILE B 1 107 ? -52.377 57.710 33.518 1.0 50.83 ? ? ? ? ? ? 224 ILE B CG1 1 107 B B +ATOM 6182 C CG2 . ILE B 1 107 ? -52.507 55.575 34.818 1.0 64.9 ? ? ? ? ? ? 224 ILE B CG2 1 107 B B +ATOM 6183 C CD1 . ILE B 1 107 ? -52.521 58.571 34.755 1.0 53.55 ? ? ? ? ? ? 224 ILE B CD1 1 107 B B +ATOM 6184 N N . PRO B 1 108 ? -52.334 53.140 32.503 1.0 65.18 ? ? ? ? ? ? 225 PRO B N 1 108 B B +ATOM 6185 C CA . PRO B 1 108 ? -52.638 51.715 32.674 1.0 59.04 ? ? ? ? ? ? 225 PRO B CA 1 108 B B +ATOM 6186 C C . PRO B 1 108 ? -53.261 51.344 34.014 1.0 58.77 ? ? ? ? ? ? 225 PRO B C 1 108 B B +ATOM 6187 O O . PRO B 1 108 ? -52.815 51.802 35.067 1.0 54.44 ? ? ? ? ? ? 225 PRO B O 1 108 B B +ATOM 6188 C CB . PRO B 1 108 ? -51.290 51.024 32.473 1.0 54.6 ? ? ? ? ? ? 225 PRO B CB 1 108 B B +ATOM 6189 C CG . PRO B 1 108 ? -50.396 52.056 31.868 1.0 49.68 ? ? ? ? ? ? 225 PRO B CG 1 108 B B +ATOM 6190 C CD . PRO B 1 108 ? -50.893 53.376 32.331 1.0 55.63 ? ? ? ? ? ? 225 PRO B CD 1 108 B B +ATOM 6191 N N . GLN B 1 109 ? -54.282 50.490 33.961 1.0 53.98 ? ? ? ? ? ? 226 GLN B N 1 109 B B +ATOM 6192 C CA . GLN B 1 109 ? -54.979 50.035 35.161 1.0 63.11 ? ? ? ? ? ? 226 GLN B CA 1 109 B B +ATOM 6193 C C . GLN B 1 109 ? -54.264 48.848 35.804 1.0 59.81 ? ? ? ? ? ? 226 GLN B C 1 109 B B +ATOM 6194 O O . GLN B 1 109 ? -53.986 47.843 35.146 1.0 65.82 ? ? ? ? ? ? 226 GLN B O 1 109 B B +ATOM 6195 C CB . GLN B 1 109 ? -56.424 49.650 34.825 1.0 71.64 ? ? ? ? ? ? 226 GLN B CB 1 109 B B +ATOM 6196 C CG . GLN B 1 109 ? -57.325 50.835 34.505 1.0 76.63 ? ? ? ? ? ? 226 GLN B CG 1 109 B B +ATOM 6197 C CD . GLN B 1 109 ? -57.642 51.697 35.719 1.0 82.35 ? ? ? ? ? ? 226 GLN B CD 1 109 B B +ATOM 6198 O OE1 . GLN B 1 109 ? -58.736 52.252 35.828 1.0 90.41 ? ? ? ? ? ? 226 GLN B OE1 1 109 B B +ATOM 6199 N NE2 . GLN B 1 109 ? -56.686 51.812 36.636 1.0 88.22 ? ? ? ? ? ? 226 GLN B NE2 1 109 B B +ATOM 6200 N N . LEU B 1 110 ? -53.987 48.977 37.099 1.0 63.21 ? ? ? ? ? ? 227 LEU B N 1 110 B B +ATOM 6201 C CA . LEU B 1 110 ? -53.287 47.952 37.864 1.0 61.31 ? ? ? ? ? ? 227 LEU B CA 1 110 B B +ATOM 6202 C C . LEU B 1 110 ? -53.841 46.539 37.718 1.0 53.7 ? ? ? ? ? ? 227 LEU B C 1 110 B B +ATOM 6203 O O . LEU B 1 110 ? -53.076 45.582 37.593 1.0 46.0 ? ? ? ? ? ? 227 LEU B O 1 110 B B +ATOM 6204 C CB . LEU B 1 110 ? -53.253 48.339 39.348 1.0 47.53 ? ? ? ? ? ? 227 LEU B CB 1 110 B B +ATOM 6205 C CG . LEU B 1 110 ? -52.548 49.650 39.727 1.0 49.37 ? ? ? ? ? ? 227 LEU B CG 1 110 B B +ATOM 6206 C CD1 . LEU B 1 110 ? -52.004 49.538 41.141 1.0 50.49 ? ? ? ? ? ? 227 LEU B CD1 1 110 B B +ATOM 6207 C CD2 . LEU B 1 110 ? -51.418 49.951 38.753 1.0 52.51 ? ? ? ? ? ? 227 LEU B CD2 1 110 B B +ATOM 6208 N N . GLU B 1 111 ? -55.162 46.398 37.740 1.0 37.21 ? ? ? ? ? ? 228 GLU B N 1 111 B B +ATOM 6209 C CA . GLU B 1 111 ? -55.759 45.073 37.609 1.0 44.29 ? ? ? ? ? ? 228 GLU B CA 1 111 B B +ATOM 6210 C C . GLU B 1 111 ? -55.299 44.411 36.314 1.0 59.82 ? ? ? ? ? ? 228 GLU B C 1 111 B B +ATOM 6211 O O . GLU B 1 111 ? -55.149 43.190 36.244 1.0 57.37 ? ? ? ? ? ? 228 GLU B O 1 111 B B +ATOM 6212 C CB . GLU B 1 111 ? -57.283 45.167 37.621 1.0 42.37 ? ? ? ? ? ? 228 GLU B CB 1 111 B B +ATOM 6213 C CG . GLU B 1 111 ? -57.962 44.210 38.590 1.0 58.34 ? ? ? ? ? ? 228 GLU B CG 1 111 B B +ATOM 6214 C CD . GLU B 1 111 ? -57.339 42.830 38.602 1.0 49.22 ? ? ? ? ? ? 228 GLU B CD 1 111 B B +ATOM 6215 O OE1 . GLU B 1 111 ? -56.340 42.636 39.324 1.0 76.04 ? ? ? ? ? ? 228 GLU B OE1 1 111 B B +ATOM 6216 O OE2 . GLU B 1 111 ? -57.848 41.935 37.896 1.0 42.09 ? ? ? ? ? ? 228 GLU B OE2 1 111 B B +ATOM 6217 N N . ASP B 1 112 ? -55.074 45.230 35.292 1.0 63.59 ? ? ? ? ? ? 229 ASP B N 1 112 B B +ATOM 6218 C CA . ASP B 1 112 ? -54.630 44.742 33.994 1.0 54.71 ? ? ? ? ? ? 229 ASP B CA 1 112 B B +ATOM 6219 C C . ASP B 1 112 ? -53.171 44.326 34.075 1.0 42.14 ? ? ? ? ? ? 229 ASP B C 1 112 B B +ATOM 6220 O O . ASP B 1 112 ? -52.814 43.197 33.743 1.0 47.78 ? ? ? ? ? ? 229 ASP B O 1 112 B B +ATOM 6221 C CB . ASP B 1 112 ? -54.802 45.837 32.942 1.0 56.3 ? ? ? ? ? ? 229 ASP B CB 1 112 B B +ATOM 6222 C CG . ASP B 1 112 ? -56.256 46.215 32.727 1.0 59.21 ? ? ? ? ? ? 229 ASP B CG 1 112 B B +ATOM 6223 O OD1 . ASP B 1 112 ? -57.129 45.344 32.928 1.0 47.22 ? ? ? ? ? ? 229 ASP B OD1 1 112 B B +ATOM 6224 O OD2 . ASP B 1 112 ? -56.525 47.377 32.358 1.0 48.29 ? ? ? ? ? ? 229 ASP B OD2 1 112 B B +ATOM 6225 N N . VAL B 1 113 ? -52.330 45.252 34.518 1.0 24.14 ? ? ? ? ? ? 230 VAL B N 1 113 B B +ATOM 6226 C CA . VAL B 1 113 ? -50.903 44.986 34.658 1.0 28.23 ? ? ? ? ? ? 230 VAL B CA 1 113 B B +ATOM 6227 C C . VAL B 1 113 ? -50.677 43.766 35.552 1.0 25.59 ? ? ? ? ? ? 230 VAL B C 1 113 B B +ATOM 6228 O O . VAL B 1 113 ? -49.920 42.860 35.205 1.0 24.96 ? ? ? ? ? ? 230 VAL B O 1 113 B B +ATOM 6229 C CB . VAL B 1 113 ? -50.171 46.193 35.274 1.0 19.93 ? ? ? ? ? ? 230 VAL B CB 1 113 B B +ATOM 6230 C CG1 . VAL B 1 113 ? -48.666 46.012 35.166 1.0 36.37 ? ? ? ? ? ? 230 VAL B CG1 1 113 B B +ATOM 6231 C CG2 . VAL B 1 113 ? -50.609 47.457 34.587 1.0 31.35 ? ? ? ? ? ? 230 VAL B CG2 1 113 B B +ATOM 6232 N N . SER B 1 114 ? -51.332 43.748 36.707 1.0 22.23 ? ? ? ? ? ? 231 SER B N 1 114 B B +ATOM 6233 C CA . SER B 1 114 ? -51.197 42.632 37.630 1.0 28.79 ? ? ? ? ? ? 231 SER B CA 1 114 B B +ATOM 6234 C C . SER B 1 114 ? -51.616 41.352 36.911 1.0 37.48 ? ? ? ? ? ? 231 SER B C 1 114 B B +ATOM 6235 O O . SER B 1 114 ? -50.844 40.400 36.818 1.0 45.95 ? ? ? ? ? ? 231 SER B O 1 114 B B +ATOM 6236 C CB . SER B 1 114 ? -52.075 42.859 38.864 1.0 36.95 ? ? ? ? ? ? 231 SER B CB 1 114 B B +ATOM 6237 O OG . SER B 1 114 ? -52.123 41.705 39.682 1.0 42.47 ? ? ? ? ? ? 231 SER B OG 1 114 B B +ATOM 6238 N N . GLN B 1 115 ? -52.846 41.345 36.399 1.0 41.53 ? ? ? ? ? ? 232 GLN B N 1 115 B B +ATOM 6239 C CA . GLN B 1 115 ? -53.362 40.187 35.682 1.0 36.18 ? ? ? ? ? ? 232 GLN B CA 1 115 B B +ATOM 6240 C C . GLN B 1 115 ? -52.392 39.736 34.597 1.0 48.1 ? ? ? ? ? ? 232 GLN B C 1 115 B B +ATOM 6241 O O . GLN B 1 115 ? -52.249 38.551 34.327 1.0 63.22 ? ? ? ? ? ? 232 GLN B O 1 115 B B +ATOM 6242 C CB . GLN B 1 115 ? -54.732 40.498 35.076 1.0 36.85 ? ? ? ? ? ? 232 GLN B CB 1 115 B B +ATOM 6243 C CG . GLN B 1 115 ? -55.712 39.337 35.128 1.0 54.29 ? ? ? ? ? ? 232 GLN B CG 1 115 B B +ATOM 6244 C CD . GLN B 1 115 ? -55.817 38.725 36.510 1.0 65.82 ? ? ? ? ? ? 232 GLN B CD 1 115 B B +ATOM 6245 O OE1 . GLN B 1 115 ? -55.427 37.577 36.723 1.0 83.67 ? ? ? ? ? ? 232 GLN B OE1 1 115 B B +ATOM 6246 N NE2 . GLN B 1 115 ? -56.310 39.310 37.597 1.0 20.0 ? ? ? ? ? ? 232 GLN B NE2 1 115 B B +ATOM 6247 N N . PHE B 1 116 ? -51.721 40.714 33.990 1.0 50.16 ? ? ? ? ? ? 233 PHE B N 1 116 B B +ATOM 6248 C CA . PHE B 1 116 ? -50.756 40.444 32.931 1.0 48.93 ? ? ? ? ? ? 233 PHE B CA 1 116 B B +ATOM 6249 C C . PHE B 1 116 ? -49.500 39.800 33.494 1.0 44.11 ? ? ? ? ? ? 233 PHE B C 1 116 B B +ATOM 6250 O O . PHE B 1 116 ? -49.171 38.661 33.167 1.0 40.81 ? ? ? ? ? ? 233 PHE B O 1 116 B B +ATOM 6251 C CB . PHE B 1 116 ? -50.381 41.742 32.214 1.0 58.23 ? ? ? ? ? ? 233 PHE B CB 1 116 B B +ATOM 6252 C CG . PHE B 1 116 ? -49.363 41.562 31.121 1.0 63.87 ? ? ? ? ? ? 233 PHE B CG 1 116 B B +ATOM 6253 C CD1 . PHE B 1 116 ? -49.425 40.469 30.261 1.0 57.86 ? ? ? ? ? ? 233 PHE B CD1 1 116 B B +ATOM 6254 C CD2 . PHE B 1 116 ? -48.346 42.493 30.947 1.0 69.54 ? ? ? ? ? ? 233 PHE B CD2 1 116 B B +ATOM 6255 C CE1 . PHE B 1 116 ? -48.484 40.305 29.245 1.0 55.36 ? ? ? ? ? ? 233 PHE B CE1 1 116 B B +ATOM 6256 C CE2 . PHE B 1 116 ? -47.400 42.339 29.935 1.0 66.99 ? ? ? ? ? ? 233 PHE B CE2 1 116 B B +ATOM 6257 C CZ . PHE B 1 116 ? -47.470 41.243 29.082 1.0 58.0 ? ? ? ? ? ? 233 PHE B CZ 1 116 B B +ATOM 6258 N N . LEU B 1 117 ? -48.800 40.551 34.337 1.0 45.08 ? ? ? ? ? ? 234 LEU B N 1 117 B B +ATOM 6259 C CA . LEU B 1 117 ? -47.571 40.082 34.970 1.0 51.99 ? ? ? ? ? ? 234 LEU B CA 1 117 B B +ATOM 6260 C C . LEU B 1 117 ? -47.713 38.662 35.509 1.0 54.51 ? ? ? ? ? ? 234 LEU B C 1 117 B B +ATOM 6261 O O . LEU B 1 117 ? -46.764 37.878 35.482 1.0 67.55 ? ? ? ? ? ? 234 LEU B O 1 117 B B +ATOM 6262 C CB . LEU B 1 117 ? -47.179 41.020 36.117 1.0 26.78 ? ? ? ? ? ? 234 LEU B CB 1 117 B B +ATOM 6263 C CG . LEU B 1 117 ? -46.432 42.298 35.728 1.0 47.52 ? ? ? ? ? ? 234 LEU B CG 1 117 B B +ATOM 6264 C CD1 . LEU B 1 117 ? -46.381 43.245 36.911 1.0 47.8 ? ? ? ? ? ? 234 LEU B CD1 1 117 B B +ATOM 6265 C CD2 . LEU B 1 117 ? -45.030 41.951 35.268 1.0 66.07 ? ? ? ? ? ? 234 LEU B CD2 1 117 B B +ATOM 6266 N N . GLN B 1 118 ? -48.901 38.333 35.996 1.0 37.39 ? ? ? ? ? ? 235 GLN B N 1 118 B B +ATOM 6267 C CA . GLN B 1 118 ? -49.141 37.013 36.549 1.0 39.18 ? ? ? ? ? ? 235 GLN B CA 1 118 B B +ATOM 6268 C C . GLN B 1 118 ? -48.933 35.894 35.536 1.0 49.42 ? ? ? ? ? ? 235 GLN B C 1 118 B B +ATOM 6269 O O . GLN B 1 118 ? -48.373 34.848 35.870 1.0 66.03 ? ? ? ? ? ? 235 GLN B O 1 118 B B +ATOM 6270 C CB . GLN B 1 118 ? -50.552 36.952 37.133 1.0 42.47 ? ? ? ? ? ? 235 GLN B CB 1 118 B B +ATOM 6271 C CG . GLN B 1 118 ? -50.714 37.807 38.371 1.0 41.61 ? ? ? ? ? ? 235 GLN B CG 1 118 B B +ATOM 6272 C CD . GLN B 1 118 ? -52.106 37.724 38.962 1.0 51.52 ? ? ? ? ? ? 235 GLN B CD 1 118 B B +ATOM 6273 O OE1 . GLN B 1 118 ? -52.604 36.638 39.251 1.0 50.65 ? ? ? ? ? ? 235 GLN B OE1 1 118 B B +ATOM 6274 N NE2 . GLN B 1 118 ? -52.743 38.876 39.145 1.0 69.18 ? ? ? ? ? ? 235 GLN B NE2 1 118 B B +ATOM 6275 N N . THR B 1 119 ? -49.376 36.110 34.301 1.0 55.42 ? ? ? ? ? ? 236 THR B N 1 119 B B +ATOM 6276 C CA . THR B 1 119 ? -49.227 35.095 33.257 1.0 57.64 ? ? ? ? ? ? 236 THR B CA 1 119 B B +ATOM 6277 C C . THR B 1 119 ? -47.795 35.000 32.742 1.0 42.79 ? ? ? ? ? ? 236 THR B C 1 119 B B +ATOM 6278 O O . THR B 1 119 ? -47.411 33.993 32.145 1.0 40.67 ? ? ? ? ? ? 236 THR B O 1 119 B B +ATOM 6279 C CB . THR B 1 119 ? -50.148 35.387 32.064 1.0 57.79 ? ? ? ? ? ? 236 THR B CB 1 119 B B +ATOM 6280 O OG1 . THR B 1 119 ? -50.062 36.777 31.730 1.0 54.71 ? ? ? ? ? ? 236 THR B OG1 1 119 B B +ATOM 6281 C CG2 . THR B 1 119 ? -51.583 35.028 32.407 1.0 55.37 ? ? ? ? ? ? 236 THR B CG2 1 119 B B +ATOM 6282 N N . CYS B 1 120 ? -47.010 36.049 32.975 1.0 24.06 ? ? ? ? ? ? 237 CYS B N 1 120 B B +ATOM 6283 C CA . CYS B 1 120 ? -45.616 36.072 32.537 1.0 50.52 ? ? ? ? ? ? 237 CYS B CA 1 120 B B +ATOM 6284 C C . CYS B 1 120 ? -44.703 35.342 33.519 1.0 60.62 ? ? ? ? ? ? 237 CYS B C 1 120 B B +ATOM 6285 O O . CYS B 1 120 ? -43.974 34.419 33.143 1.0 60.8 ? ? ? ? ? ? 237 CYS B O 1 120 B B +ATOM 6286 C CB . CYS B 1 120 ? -45.119 37.511 32.386 1.0 39.35 ? ? ? ? ? ? 237 CYS B CB 1 120 B B +ATOM 6287 S SG . CYS B 1 120 ? -46.187 38.564 31.401 1.0 63.59 ? ? ? ? ? ? 237 CYS B SG 1 120 B B +ATOM 6288 N N . THR B 1 121 ? -44.755 35.756 34.783 1.0 56.56 ? ? ? ? ? ? 238 THR B N 1 121 B B +ATOM 6289 C CA . THR B 1 121 ? -43.916 35.160 35.815 1.0 48.5 ? ? ? ? ? ? 238 THR B CA 1 121 B B +ATOM 6290 C C . THR B 1 121 ? -44.710 34.700 37.035 1.0 51.09 ? ? ? ? ? ? 238 THR B C 1 121 B B +ATOM 6291 O O . THR B 1 121 ? -44.273 33.821 37.779 1.0 66.44 ? ? ? ? ? ? 238 THR B O 1 121 B B +ATOM 6292 C CB . THR B 1 121 ? -42.844 36.159 36.272 1.0 48.09 ? ? ? ? ? ? 238 THR B CB 1 121 B B +ATOM 6293 O OG1 . THR B 1 121 ? -43.480 37.325 36.804 1.0 63.68 ? ? ? ? ? ? 238 THR B OG1 1 121 B B +ATOM 6294 C CG2 . THR B 1 121 ? -41.971 36.572 35.097 1.0 54.75 ? ? ? ? ? ? 238 THR B CG2 1 121 B B +ATOM 6295 N N . GLY B 1 122 ? -45.883 35.287 37.229 1.0 45.86 ? ? ? ? ? ? 239 GLY B N 1 122 B B +ATOM 6296 C CA . GLY B 1 122 ? -46.698 34.919 38.370 1.0 37.78 ? ? ? ? ? ? 239 GLY B CA 1 122 B B +ATOM 6297 C C . GLY B 1 122 ? -46.763 36.054 39.370 1.0 36.96 ? ? ? ? ? ? 239 GLY B C 1 122 B B +ATOM 6298 O O . GLY B 1 122 ? -47.435 35.955 40.394 1.0 40.13 ? ? ? ? ? ? 239 GLY B O 1 122 B B +ATOM 6299 N N . PHE B 1 123 ? -46.058 37.137 39.064 1.0 37.98 ? ? ? ? ? ? 240 PHE B N 1 123 B B +ATOM 6300 C CA . PHE B 1 123 ? -46.026 38.309 39.926 1.0 39.99 ? ? ? ? ? ? 240 PHE B CA 1 123 B B +ATOM 6301 C C . PHE B 1 123 ? -47.352 39.051 39.876 1.0 51.84 ? ? ? ? ? ? 240 PHE B C 1 123 B B +ATOM 6302 O O . PHE B 1 123 ? -47.814 39.448 38.803 1.0 61.74 ? ? ? ? ? ? 240 PHE B O 1 123 B B +ATOM 6303 C CB . PHE B 1 123 ? -44.906 39.254 39.494 1.0 38.03 ? ? ? ? ? ? 240 PHE B CB 1 123 B B +ATOM 6304 C CG . PHE B 1 123 ? -43.769 39.327 40.465 1.0 45.56 ? ? ? ? ? ? 240 PHE B CG 1 123 B B +ATOM 6305 C CD1 . PHE B 1 123 ? -42.767 38.368 40.450 1.0 44.86 ? ? ? ? ? ? 240 PHE B CD1 1 123 B B +ATOM 6306 C CD2 . PHE B 1 123 ? -43.704 40.347 41.403 1.0 59.18 ? ? ? ? ? ? 240 PHE B CD2 1 123 B B +ATOM 6307 C CE1 . PHE B 1 123 ? -41.717 38.425 41.354 1.0 59.62 ? ? ? ? ? ? 240 PHE B CE1 1 123 B B +ATOM 6308 C CE2 . PHE B 1 123 ? -42.656 40.411 42.312 1.0 63.73 ? ? ? ? ? ? 240 PHE B CE2 1 123 B B +ATOM 6309 C CZ . PHE B 1 123 ? -41.661 39.449 42.288 1.0 53.74 ? ? ? ? ? ? 240 PHE B CZ 1 123 B B +ATOM 6310 N N . ARG B 1 124 ? -47.962 39.233 41.042 1.0 48.36 ? ? ? ? ? ? 241 ARG B N 1 124 B B +ATOM 6311 C CA . ARG B 1 124 ? -49.227 39.940 41.126 1.0 38.46 ? ? ? ? ? ? 241 ARG B CA 1 124 B B +ATOM 6312 C C . ARG B 1 124 ? -48.958 41.276 41.777 1.0 30.49 ? ? ? ? ? ? 241 ARG B C 1 124 B B +ATOM 6313 O O . ARG B 1 124 ? -48.049 41.398 42.589 1.0 40.37 ? ? ? ? ? ? 241 ARG B O 1 124 B B +ATOM 6314 C CB . ARG B 1 124 ? -50.225 39.153 41.966 1.0 27.27 ? ? ? ? ? ? 241 ARG B CB 1 124 B B +ATOM 6315 C CG . ARG B 1 124 ? -49.584 38.273 43.013 1.0 42.48 ? ? ? ? ? ? 241 ARG B CG 1 124 B B +ATOM 6316 C CD . ARG B 1 124 ? -50.587 37.280 43.539 1.0 38.82 ? ? ? ? ? ? 241 ARG B CD 1 124 B B +ATOM 6317 N NE . ARG B 1 124 ? -50.999 36.343 42.502 1.0 53.54 ? ? ? ? ? ? 241 ARG B NE 1 124 B B +ATOM 6318 C CZ . ARG B 1 124 ? -51.817 35.319 42.715 1.0 67.48 ? ? ? ? ? ? 241 ARG B CZ 1 124 B B +ATOM 6319 N NH1 . ARG B 1 124 ? -52.305 35.111 43.929 1.0 50.15 ? ? ? ? ? ? 241 ARG B NH1 1 124 B B +ATOM 6320 N NH2 . ARG B 1 124 ? -52.140 34.499 41.721 1.0 83.13 ? ? ? ? ? ? 241 ARG B NH2 1 124 B B +ATOM 6321 N N . LEU B 1 125 ? -49.742 42.281 41.417 1.0 31.8 ? ? ? ? ? ? 242 LEU B N 1 125 B B +ATOM 6322 C CA . LEU B 1 125 ? -49.560 43.596 41.999 1.0 30.17 ? ? ? ? ? ? 242 LEU B CA 1 125 B B +ATOM 6323 C C . LEU B 1 125 ? -50.465 43.753 43.212 1.0 43.05 ? ? ? ? ? ? 242 LEU B C 1 125 B B +ATOM 6324 O O . LEU B 1 125 ? -51.471 43.059 43.342 1.0 25.42 ? ? ? ? ? ? 242 LEU B O 1 125 B B +ATOM 6325 C CB . LEU B 1 125 ? -49.882 44.675 40.967 1.0 29.3 ? ? ? ? ? ? 242 LEU B CB 1 125 B B +ATOM 6326 C CG . LEU B 1 125 ? -48.821 44.923 39.891 1.0 49.41 ? ? ? ? ? ? 242 LEU B CG 1 125 B B +ATOM 6327 C CD1 . LEU B 1 125 ? -49.293 46.032 38.961 1.0 57.07 ? ? ? ? ? ? 242 LEU B CD1 1 125 B B +ATOM 6328 C CD2 . LEU B 1 125 ? -47.495 45.305 40.535 1.0 25.53 ? ? ? ? ? ? 242 LEU B CD2 1 125 B B +ATOM 6329 N N . ARG B 1 126 ? -50.078 44.651 44.111 1.0 51.99 ? ? ? ? ? ? 243 ARG B N 1 126 B B +ATOM 6330 C CA . ARG B 1 126 ? -50.855 44.939 45.311 1.0 51.87 ? ? ? ? ? ? 243 ARG B CA 1 126 B B +ATOM 6331 C C . ARG B 1 126 ? -50.732 46.426 45.613 1.0 58.5 ? ? ? ? ? ? 243 ARG B C 1 126 B B +ATOM 6332 O O . ARG B 1 126 ? -49.633 46.937 45.828 1.0 66.87 ? ? ? ? ? ? 243 ARG B O 1 126 B B +ATOM 6333 C CB . ARG B 1 126 ? -50.356 44.132 46.511 1.0 49.19 ? ? ? ? ? ? 243 ARG B CB 1 126 B B +ATOM 6334 C CG . ARG B 1 126 ? -51.373 44.078 47.636 1.0 47.76 ? ? ? ? ? ? 243 ARG B CG 1 126 B B +ATOM 6335 C CD . ARG B 1 126 ? -50.796 43.518 48.921 1.0 53.15 ? ? ? ? ? ? 243 ARG B CD 1 126 B B +ATOM 6336 N NE . ARG B 1 126 ? -51.715 43.734 50.035 1.0 66.41 ? ? ? ? ? ? 243 ARG B NE 1 126 B B +ATOM 6337 C CZ . ARG B 1 126 ? -52.489 42.791 50.563 1.0 58.98 ? ? ? ? ? ? 243 ARG B CZ 1 126 B B +ATOM 6338 N NH1 . ARG B 1 126 ? -52.463 41.556 50.078 1.0 72.19 ? ? ? ? ? ? 243 ARG B NH1 1 126 B B +ATOM 6339 N NH2 . ARG B 1 126 ? -53.300 43.082 51.570 1.0 47.51 ? ? ? ? ? ? 243 ARG B NH2 1 126 B B +ATOM 6340 N N . PRO B 1 127 ? -51.869 47.140 45.637 1.0 56.82 ? ? ? ? ? ? 244 PRO B N 1 127 B B +ATOM 6341 C CA . PRO B 1 127 ? -51.855 48.581 45.914 1.0 41.81 ? ? ? ? ? ? 244 PRO B CA 1 127 B B +ATOM 6342 C C . PRO B 1 127 ? -51.452 48.912 47.348 1.0 45.42 ? ? ? ? ? ? 244 PRO B C 1 127 B B +ATOM 6343 O O . PRO B 1 127 ? -52.141 48.551 48.299 1.0 45.79 ? ? ? ? ? ? 244 PRO B O 1 127 B B +ATOM 6344 C CB . PRO B 1 127 ? -53.284 49.019 45.593 1.0 22.99 ? ? ? ? ? ? 244 PRO B CB 1 127 B B +ATOM 6345 C CG . PRO B 1 127 ? -54.103 47.791 45.788 1.0 23.84 ? ? ? ? ? ? 244 PRO B CG 1 127 B B +ATOM 6346 C CD . PRO B 1 127 ? -53.233 46.629 45.415 1.0 33.55 ? ? ? ? ? ? 244 PRO B CD 1 127 B B +ATOM 6347 N N . VAL B 1 128 ? -50.326 49.603 47.495 1.0 46.64 ? ? ? ? ? ? 245 VAL B N 1 128 B B +ATOM 6348 C CA . VAL B 1 128 ? -49.831 49.989 48.811 1.0 57.89 ? ? ? ? ? ? 245 VAL B CA 1 128 B B +ATOM 6349 C C . VAL B 1 128 ? -50.239 51.429 49.097 1.0 73.52 ? ? ? ? ? ? 245 VAL B C 1 128 B B +ATOM 6350 O O . VAL B 1 128 ? -50.192 52.279 48.206 1.0 78.88 ? ? ? ? ? ? 245 VAL B O 1 128 B B +ATOM 6351 C CB . VAL B 1 128 ? -48.286 49.877 48.885 1.0 58.34 ? ? ? ? ? ? 245 VAL B CB 1 128 B B +ATOM 6352 C CG1 . VAL B 1 128 ? -47.636 51.023 48.126 1.0 67.35 ? ? ? ? ? ? 245 VAL B CG1 1 128 B B +ATOM 6353 C CG2 . VAL B 1 128 ? -47.833 49.873 50.335 1.0 52.31 ? ? ? ? ? ? 245 VAL B CG2 1 128 B B +ATOM 6354 N N . ALA B 1 129 ? -50.639 51.699 50.337 1.0 85.17 ? ? ? ? ? ? 246 ALA B N 1 129 B B +ATOM 6355 C CA . ALA B 1 129 ? -51.050 53.045 50.732 1.0 80.94 ? ? ? ? ? ? 246 ALA B CA 1 129 B B +ATOM 6356 C C . ALA B 1 129 ? -50.049 54.085 50.223 1.0 78.81 ? ? ? ? ? ? 246 ALA B C 1 129 B B +ATOM 6357 O O . ALA B 1 129 ? -50.377 54.917 49.373 1.0 72.96 ? ? ? ? ? ? 246 ALA B O 1 129 B B +ATOM 6358 C CB . ALA B 1 129 ? -51.166 53.128 52.251 1.0 83.46 ? ? ? ? ? ? 246 ALA B CB 1 129 B B +ATOM 6359 N N . GLY B 1 130 ? -48.828 54.030 50.747 1.0 73.3 ? ? ? ? ? ? 247 GLY B N 1 130 B B +ATOM 6360 C CA . GLY B 1 130 ? -47.796 54.961 50.332 1.0 72.06 ? ? ? ? ? ? 247 GLY B CA 1 130 B B +ATOM 6361 C C . GLY B 1 130 ? -46.437 54.292 50.317 1.0 70.96 ? ? ? ? ? ? 247 GLY B C 1 130 B B +ATOM 6362 O O . GLY B 1 130 ? -45.890 54.002 49.256 1.0 65.1 ? ? ? ? ? ? 247 GLY B O 1 130 B B +ATOM 6363 N N . LEU B 1 131 ? -45.895 54.045 51.505 1.0 82.56 ? ? ? ? ? ? 248 LEU B N 1 131 B B +ATOM 6364 C CA . LEU B 1 131 ? -44.588 53.411 51.644 1.0 87.46 ? ? ? ? ? ? 248 LEU B CA 1 131 B B +ATOM 6365 C C . LEU B 1 131 ? -44.627 52.395 52.780 1.0 80.78 ? ? ? ? ? ? 248 LEU B C 1 131 B B +ATOM 6366 O O . LEU B 1 131 ? -45.562 52.387 53.579 1.0 85.05 ? ? ? ? ? ? 248 LEU B O 1 131 B B +ATOM 6367 C CB . LEU B 1 131 ? -43.517 54.471 51.936 1.0 91.7 ? ? ? ? ? ? 248 LEU B CB 1 131 B B +ATOM 6368 C CG . LEU B 1 131 ? -43.373 54.956 53.384 1.0 100.0 ? ? ? ? ? ? 248 LEU B CG 1 131 B B +ATOM 6369 C CD1 . LEU B 1 131 ? -42.105 55.781 53.520 1.0 95.76 ? ? ? ? ? ? 248 LEU B CD1 1 131 B B +ATOM 6370 C CD2 . LEU B 1 131 ? -44.595 55.768 53.781 1.0 100.0 ? ? ? ? ? ? 248 LEU B CD2 1 131 B B +ATOM 6371 N N . LEU B 1 132 ? -43.616 51.535 52.842 1.0 67.02 ? ? ? ? ? ? 249 LEU B N 1 132 B B +ATOM 6372 C CA . LEU B 1 132 ? -43.534 50.532 53.895 1.0 63.13 ? ? ? ? ? ? 249 LEU B CA 1 132 B B +ATOM 6373 C C . LEU B 1 132 ? -42.101 50.081 54.136 1.0 65.19 ? ? ? ? ? ? 249 LEU B C 1 132 B B +ATOM 6374 O O . LEU B 1 132 ? -41.228 50.267 53.293 1.0 49.32 ? ? ? ? ? ? 249 LEU B O 1 132 B B +ATOM 6375 C CB . LEU B 1 132 ? -44.407 49.320 53.566 1.0 59.4 ? ? ? ? ? ? 249 LEU B CB 1 132 B B +ATOM 6376 C CG . LEU B 1 132 ? -44.772 49.008 52.117 1.0 57.14 ? ? ? ? ? ? 249 LEU B CG 1 132 B B +ATOM 6377 C CD1 . LEU B 1 132 ? -43.519 48.858 51.276 1.0 59.86 ? ? ? ? ? ? 249 LEU B CD1 1 132 B B +ATOM 6378 C CD2 . LEU B 1 132 ? -45.598 47.734 52.093 1.0 68.38 ? ? ? ? ? ? 249 LEU B CD2 1 132 B B +ATOM 6379 N N . SER B 1 133 ? -41.869 49.495 55.304 1.0 64.35 ? ? ? ? ? ? 250 SER B N 1 133 B B +ATOM 6380 C CA . SER B 1 133 ? -40.545 49.022 55.685 1.0 62.49 ? ? ? ? ? ? 250 SER B CA 1 133 B B +ATOM 6381 C C . SER B 1 133 ? -39.915 48.126 54.625 1.0 70.64 ? ? ? ? ? ? 250 SER B C 1 133 B B +ATOM 6382 O O . SER B 1 133 ? -40.619 47.521 53.818 1.0 78.71 ? ? ? ? ? ? 250 SER B O 1 133 B B +ATOM 6383 C CB . SER B 1 133 ? -40.635 48.260 57.004 1.0 45.86 ? ? ? ? ? ? 250 SER B CB 1 133 B B +ATOM 6384 O OG . SER B 1 133 ? -39.420 47.598 57.290 1.0 69.61 ? ? ? ? ? ? 250 SER B OG 1 133 B B +ATOM 6385 N N . SER B 1 134 ? -38.586 48.050 54.628 1.0 81.86 ? ? ? ? ? ? 251 SER B N 1 134 B B +ATOM 6386 C CA . SER B 1 134 ? -37.871 47.210 53.674 1.0 82.78 ? ? ? ? ? ? 251 SER B CA 1 134 B B +ATOM 6387 C C . SER B 1 134 ? -38.236 45.762 53.955 1.0 77.72 ? ? ? ? ? ? 251 SER B C 1 134 B B +ATOM 6388 O O . SER B 1 134 ? -38.366 44.947 53.039 1.0 65.78 ? ? ? ? ? ? 251 SER B O 1 134 B B +ATOM 6389 C CB . SER B 1 134 ? -36.359 47.383 53.825 1.0 73.43 ? ? ? ? ? ? 251 SER B CB 1 134 B B +ATOM 6390 O OG . SER B 1 134 ? -36.021 48.738 54.049 1.0 90.84 ? ? ? ? ? ? 251 SER B OG 1 134 B B +ATOM 6391 N N . ARG B 1 135 ? -38.394 45.451 55.238 1.0 62.78 ? ? ? ? ? ? 252 ARG B N 1 135 B B +ATOM 6392 C CA . ARG B 1 135 ? -38.750 44.107 55.656 1.0 58.79 ? ? ? ? ? ? 252 ARG B CA 1 135 B B +ATOM 6393 C C . ARG B 1 135 ? -40.112 43.729 55.086 1.0 63.08 ? ? ? ? ? ? 252 ARG B C 1 135 B B +ATOM 6394 O O . ARG B 1 135 ? -40.316 42.601 54.642 1.0 78.89 ? ? ? ? ? ? 252 ARG B O 1 135 B B +ATOM 6395 C CB . ARG B 1 135 ? -38.783 44.025 57.181 1.0 60.93 ? ? ? ? ? ? 252 ARG B CB 1 135 B B +ATOM 6396 C CG . ARG B 1 135 ? -39.238 42.677 57.719 1.0 79.31 ? ? ? ? ? ? 252 ARG B CG 1 135 B B +ATOM 6397 C CD . ARG B 1 135 ? -39.269 42.683 59.234 1.0 94.81 ? ? ? ? ? ? 252 ARG B CD 1 135 B B +ATOM 6398 N NE . ARG B 1 135 ? -37.958 42.987 59.801 1.0 99.4 ? ? ? ? ? ? 252 ARG B NE 1 135 B B +ATOM 6399 C CZ . ARG B 1 135 ? -36.929 42.145 59.797 1.0 85.17 ? ? ? ? ? ? 252 ARG B CZ 1 135 B B +ATOM 6400 N NH1 . ARG B 1 135 ? -37.058 40.943 59.253 1.0 76.66 ? ? ? ? ? ? 252 ARG B NH1 1 135 B B +ATOM 6401 N NH2 . ARG B 1 135 ? -35.775 42.503 60.344 1.0 73.12 ? ? ? ? ? ? 252 ARG B NH2 1 135 B B +ATOM 6402 N N . ASP B 1 136 ? -41.041 44.681 55.100 1.0 62.76 ? ? ? ? ? ? 253 ASP B N 1 136 B B +ATOM 6403 C CA . ASP B 1 136 ? -42.392 44.448 54.593 1.0 57.99 ? ? ? ? ? ? 253 ASP B CA 1 136 B B +ATOM 6404 C C . ASP B 1 136 ? -42.413 44.387 53.075 1.0 60.84 ? ? ? ? ? ? 253 ASP B C 1 136 B B +ATOM 6405 O O . ASP B 1 136 ? -43.062 43.521 52.484 1.0 47.13 ? ? ? ? ? ? 253 ASP B O 1 136 B B +ATOM 6406 C CB . ASP B 1 136 ? -43.325 45.558 55.063 1.0 62.86 ? ? ? ? ? ? 253 ASP B CB 1 136 B B +ATOM 6407 C CG . ASP B 1 136 ? -43.441 45.617 56.562 1.0 82.05 ? ? ? ? ? ? 253 ASP B CG 1 136 B B +ATOM 6408 O OD1 . ASP B 1 136 ? -42.508 46.147 57.205 1.0 84.11 ? ? ? ? ? ? 253 ASP B OD1 1 136 B B +ATOM 6409 O OD2 . ASP B 1 136 ? -44.463 45.131 57.095 1.0 82.41 ? ? ? ? ? ? 253 ASP B OD2 1 136 B B +ATOM 6410 N N . PHE B 1 137 ? -41.713 45.323 52.447 1.0 71.62 ? ? ? ? ? ? 254 PHE B N 1 137 B B +ATOM 6411 C CA . PHE B 1 137 ? -41.639 45.370 50.995 1.0 81.25 ? ? ? ? ? ? 254 PHE B CA 1 137 B B +ATOM 6412 C C . PHE B 1 137 ? -41.059 44.048 50.500 1.0 77.02 ? ? ? ? ? ? 254 PHE B C 1 137 B B +ATOM 6413 O O . PHE B 1 137 ? -41.704 43.313 49.748 1.0 80.3 ? ? ? ? ? ? 254 PHE B O 1 137 B B +ATOM 6414 C CB . PHE B 1 137 ? -40.743 46.534 50.559 1.0 85.08 ? ? ? ? ? ? 254 PHE B CB 1 137 B B +ATOM 6415 C CG . PHE B 1 137 ? -40.869 46.898 49.105 1.0 92.74 ? ? ? ? ? ? 254 PHE B CG 1 137 B B +ATOM 6416 C CD1 . PHE B 1 137 ? -41.713 46.185 48.257 1.0 100.0 ? ? ? ? ? ? 254 PHE B CD1 1 137 B B +ATOM 6417 C CD2 . PHE B 1 137 ? -40.139 47.963 48.585 1.0 100.0 ? ? ? ? ? ? 254 PHE B CD2 1 137 B B +ATOM 6418 C CE1 . PHE B 1 137 ? -41.824 46.527 46.912 1.0 100.0 ? ? ? ? ? ? 254 PHE B CE1 1 137 B B +ATOM 6419 C CE2 . PHE B 1 137 ? -40.244 48.313 47.240 1.0 100.0 ? ? ? ? ? ? 254 PHE B CE2 1 137 B B +ATOM 6420 C CZ . PHE B 1 137 ? -41.087 47.595 46.404 1.0 100.0 ? ? ? ? ? ? 254 PHE B CZ 1 137 B B +ATOM 6421 N N . LEU B 1 138 ? -39.838 43.755 50.936 1.0 65.08 ? ? ? ? ? ? 255 LEU B N 1 138 B B +ATOM 6422 C CA . LEU B 1 138 ? -39.150 42.530 50.552 1.0 52.4 ? ? ? ? ? ? 255 LEU B CA 1 138 B B +ATOM 6423 C C . LEU B 1 138 ? -39.988 41.289 50.850 1.0 49.55 ? ? ? ? ? ? 255 LEU B C 1 138 B B +ATOM 6424 O O . LEU B 1 138 ? -39.991 40.331 50.080 1.0 58.75 ? ? ? ? ? ? 255 LEU B O 1 138 B B +ATOM 6425 C CB . LEU B 1 138 ? -37.806 42.441 51.279 1.0 42.75 ? ? ? ? ? ? 255 LEU B CB 1 138 B B +ATOM 6426 C CG . LEU B 1 138 ? -36.633 43.180 50.622 1.0 49.61 ? ? ? ? ? ? 255 LEU B CG 1 138 B B +ATOM 6427 C CD1 . LEU B 1 138 ? -37.130 44.391 49.853 1.0 39.36 ? ? ? ? ? ? 255 LEU B CD1 1 138 B B +ATOM 6428 C CD2 . LEU B 1 138 ? -35.638 43.590 51.692 1.0 52.31 ? ? ? ? ? ? 255 LEU B CD2 1 138 B B +ATOM 6429 N N . GLY B 1 139 ? -40.700 41.308 51.971 1.0 48.37 ? ? ? ? ? ? 256 GLY B N 1 139 B B +ATOM 6430 C CA . GLY B 1 139 ? -41.526 40.169 52.330 1.0 51.48 ? ? ? ? ? ? 256 GLY B CA 1 139 B B +ATOM 6431 C C . GLY B 1 139 ? -42.554 39.836 51.262 1.0 56.98 ? ? ? ? ? ? 256 GLY B C 1 139 B B +ATOM 6432 O O . GLY B 1 139 ? -42.925 38.675 51.081 1.0 43.96 ? ? ? ? ? ? 256 GLY B O 1 139 B B +ATOM 6433 N N . GLY B 1 140 ? -43.023 40.856 50.552 1.0 63.18 ? ? ? ? ? ? 257 GLY B N 1 140 B B +ATOM 6434 C CA . GLY B 1 140 ? -44.003 40.626 49.510 1.0 66.05 ? ? ? ? ? ? 257 GLY B CA 1 140 B B +ATOM 6435 C C . GLY B 1 140 ? -43.383 39.868 48.355 1.0 56.41 ? ? ? ? ? ? 257 GLY B C 1 140 B B +ATOM 6436 O O . GLY B 1 140 ? -44.022 39.017 47.742 1.0 59.16 ? ? ? ? ? ? 257 GLY B O 1 140 B B +ATOM 6437 N N . LEU B 1 141 ? -42.123 40.176 48.067 1.0 37.56 ? ? ? ? ? ? 258 LEU B N 1 141 B B +ATOM 6438 C CA . LEU B 1 141 ? -41.396 39.543 46.973 1.0 32.65 ? ? ? ? ? ? 258 LEU B CA 1 141 B B +ATOM 6439 C C . LEU B 1 141 ? -41.315 38.027 47.127 1.0 32.75 ? ? ? ? ? ? 258 LEU B C 1 141 B B +ATOM 6440 O O . LEU B 1 141 ? -41.258 37.299 46.137 1.0 42.08 ? ? ? ? ? ? 258 LEU B O 1 141 B B +ATOM 6441 C CB . LEU B 1 141 ? -39.985 40.140 46.871 1.0 17.19 ? ? ? ? ? ? 258 LEU B CB 1 141 B B +ATOM 6442 C CG . LEU B 1 141 ? -39.918 41.665 46.736 1.0 48.83 ? ? ? ? ? ? 258 LEU B CG 1 141 B B +ATOM 6443 C CD1 . LEU B 1 141 ? -38.495 42.148 47.004 1.0 28.3 ? ? ? ? ? ? 258 LEU B CD1 1 141 B B +ATOM 6444 C CD2 . LEU B 1 141 ? -40.392 42.072 45.347 1.0 48.32 ? ? ? ? ? ? 258 LEU B CD2 1 141 B B +ATOM 6445 N N . ALA B 1 142 ? -41.310 37.557 48.370 1.0 32.23 ? ? ? ? ? ? 259 ALA B N 1 142 B B +ATOM 6446 C CA . ALA B 1 142 ? -41.233 36.127 48.658 1.0 28.79 ? ? ? ? ? ? 259 ALA B CA 1 142 B B +ATOM 6447 C C . ALA B 1 142 ? -42.428 35.387 48.086 1.0 30.15 ? ? ? ? ? ? 259 ALA B C 1 142 B B +ATOM 6448 O O . ALA B 1 142 ? -42.395 34.166 47.937 1.0 34.54 ? ? ? ? ? ? 259 ALA B O 1 142 B B +ATOM 6449 C CB . ALA B 1 142 ? -41.163 35.899 50.160 1.0 38.29 ? ? ? ? ? ? 259 ALA B CB 1 142 B B +ATOM 6450 N N . PHE B 1 143 ? -43.491 36.129 47.781 1.0 38.35 ? ? ? ? ? ? 260 PHE B N 1 143 B B +ATOM 6451 C CA . PHE B 1 143 ? -44.709 35.544 47.224 1.0 28.17 ? ? ? ? ? ? 260 PHE B CA 1 143 B B +ATOM 6452 C C . PHE B 1 143 ? -44.920 36.036 45.810 1.0 32.46 ? ? ? ? ? ? 260 PHE B C 1 143 B B +ATOM 6453 O O . PHE B 1 143 ? -45.983 35.822 45.225 1.0 29.36 ? ? ? ? ? ? 260 PHE B O 1 143 B B +ATOM 6454 C CB . PHE B 1 143 ? -45.922 35.926 48.068 1.0 23.46 ? ? ? ? ? ? 260 PHE B CB 1 143 B B +ATOM 6455 C CG . PHE B 1 143 ? -45.761 35.628 49.521 1.0 23.16 ? ? ? ? ? ? 260 PHE B CG 1 143 B B +ATOM 6456 C CD1 . PHE B 1 143 ? -44.996 36.455 50.331 1.0 21.32 ? ? ? ? ? ? 260 PHE B CD1 1 143 B B +ATOM 6457 C CD2 . PHE B 1 143 ? -46.362 34.507 50.083 1.0 30.85 ? ? ? ? ? ? 260 PHE B CD2 1 143 B B +ATOM 6458 C CE1 . PHE B 1 143 ? -44.832 36.167 51.684 1.0 42.56 ? ? ? ? ? ? 260 PHE B CE1 1 143 B B +ATOM 6459 C CE2 . PHE B 1 143 ? -46.204 34.209 51.436 1.0 18.09 ? ? ? ? ? ? 260 PHE B CE2 1 143 B B +ATOM 6460 C CZ . PHE B 1 143 ? -45.440 35.039 52.237 1.0 14.9 ? ? ? ? ? ? 260 PHE B CZ 1 143 B B +ATOM 6461 N N . ARG B 1 144 ? -43.901 36.699 45.268 1.0 43.21 ? ? ? ? ? ? 261 ARG B N 1 144 B B +ATOM 6462 C CA . ARG B 1 144 ? -43.965 37.245 43.920 1.0 52.93 ? ? ? ? ? ? 261 ARG B CA 1 144 B B +ATOM 6463 C C . ARG B 1 144 ? -45.102 38.263 43.874 1.0 61.31 ? ? ? ? ? ? 261 ARG B C 1 144 B B +ATOM 6464 O O . ARG B 1 144 ? -45.873 38.327 42.911 1.0 65.05 ? ? ? ? ? ? 261 ARG B O 1 144 B B +ATOM 6465 C CB . ARG B 1 144 ? -44.200 36.128 42.902 1.0 58.77 ? ? ? ? ? ? 261 ARG B CB 1 144 B B +ATOM 6466 C CG . ARG B 1 144 ? -43.047 35.151 42.812 1.0 65.11 ? ? ? ? ? ? 261 ARG B CG 1 144 B B +ATOM 6467 C CD . ARG B 1 144 ? -42.894 34.573 41.419 1.0 72.9 ? ? ? ? ? ? 261 ARG B CD 1 144 B B +ATOM 6468 N NE . ARG B 1 144 ? -41.849 33.556 41.401 1.0 66.8 ? ? ? ? ? ? 261 ARG B NE 1 144 B B +ATOM 6469 C CZ . ARG B 1 144 ? -41.228 33.131 40.309 1.0 62.18 ? ? ? ? ? ? 261 ARG B CZ 1 144 B B +ATOM 6470 N NH1 . ARG B 1 144 ? -41.533 33.639 39.124 1.0 64.89 ? ? ? ? ? ? 261 ARG B NH1 1 144 B B +ATOM 6471 N NH2 . ARG B 1 144 ? -40.283 32.206 40.408 1.0 78.44 ? ? ? ? ? ? 261 ARG B NH2 1 144 B B +ATOM 6472 N N . VAL B 1 145 ? -45.191 39.045 44.948 1.0 47.17 ? ? ? ? ? ? 262 VAL B N 1 145 B B +ATOM 6473 C CA . VAL B 1 145 ? -46.195 40.089 45.089 1.0 38.17 ? ? ? ? ? ? 262 VAL B CA 1 145 B B +ATOM 6474 C C . VAL B 1 145 ? -45.486 41.444 45.175 1.0 38.46 ? ? ? ? ? ? 262 VAL B C 1 145 B B +ATOM 6475 O O . VAL B 1 145 ? -44.604 41.640 46.015 1.0 35.95 ? ? ? ? ? ? 262 VAL B O 1 145 B B +ATOM 6476 C CB . VAL B 1 145 ? -47.040 39.881 46.367 1.0 16.94 ? ? ? ? ? ? 262 VAL B CB 1 145 B B +ATOM 6477 C CG1 . VAL B 1 145 ? -47.867 41.120 46.652 1.0 15.75 ? ? ? ? ? ? 262 VAL B CG1 1 145 B B +ATOM 6478 C CG2 . VAL B 1 145 ? -47.948 38.668 46.200 1.0 13.76 ? ? ? ? ? ? 262 VAL B CG2 1 145 B B +ATOM 6479 N N . PHE B 1 146 ? -45.870 42.371 44.303 1.0 44.65 ? ? ? ? ? ? 263 PHE B N 1 146 B B +ATOM 6480 C CA . PHE B 1 146 ? -45.265 43.695 44.289 1.0 56.23 ? ? ? ? ? ? 263 PHE B CA 1 146 B B +ATOM 6481 C C . PHE B 1 146 ? -46.218 44.747 44.843 1.0 64.47 ? ? ? ? ? ? 263 PHE B C 1 146 B B +ATOM 6482 O O . PHE B 1 146 ? -47.352 44.875 44.384 1.0 75.1 ? ? ? ? ? ? 263 PHE B O 1 146 B B +ATOM 6483 C CB . PHE B 1 146 ? -44.863 44.075 42.863 1.0 45.33 ? ? ? ? ? ? 263 PHE B CB 1 146 B B +ATOM 6484 C CG . PHE B 1 146 ? -44.028 45.324 42.779 1.0 54.31 ? ? ? ? ? ? 263 PHE B CG 1 146 B B +ATOM 6485 C CD1 . PHE B 1 146 ? -42.919 45.494 43.601 1.0 58.96 ? ? ? ? ? ? 263 PHE B CD1 1 146 B B +ATOM 6486 C CD2 . PHE B 1 146 ? -44.347 46.331 41.871 1.0 60.8 ? ? ? ? ? ? 263 PHE B CD2 1 146 B B +ATOM 6487 C CE1 . PHE B 1 146 ? -42.138 46.649 43.516 1.0 62.13 ? ? ? ? ? ? 263 PHE B CE1 1 146 B B +ATOM 6488 C CE2 . PHE B 1 146 ? -43.571 47.490 41.780 1.0 62.38 ? ? ? ? ? ? 263 PHE B CE2 1 146 B B +ATOM 6489 C CZ . PHE B 1 146 ? -42.467 47.649 42.603 1.0 62.3 ? ? ? ? ? ? 263 PHE B CZ 1 146 B B +ATOM 6490 N N . HIS B 1 147 ? -45.754 45.499 45.836 1.0 56.84 ? ? ? ? ? ? 264 HIS B N 1 147 B B +ATOM 6491 C CA . HIS B 1 147 ? -46.572 46.544 46.438 1.0 50.73 ? ? ? ? ? ? 264 HIS B CA 1 147 B B +ATOM 6492 C C . HIS B 1 147 ? -46.416 47.813 45.610 1.0 52.79 ? ? ? ? ? ? 264 HIS B C 1 147 B B +ATOM 6493 O O . HIS B 1 147 ? -45.410 48.518 45.693 1.0 42.06 ? ? ? ? ? ? 264 HIS B O 1 147 B B +ATOM 6494 C CB . HIS B 1 147 ? -46.148 46.764 47.895 1.0 60.26 ? ? ? ? ? ? 264 HIS B CB 1 147 B B +ATOM 6495 C CG . HIS B 1 147 ? -46.536 45.640 48.802 1.0 66.12 ? ? ? ? ? ? 264 HIS B CG 1 147 B B +ATOM 6496 N ND1 . HIS B 1 147 ? -47.659 45.679 49.601 1.0 64.49 ? ? ? ? ? ? 264 HIS B ND1 1 147 B B +ATOM 6497 C CD2 . HIS B 1 147 ? -45.978 44.420 48.998 1.0 62.27 ? ? ? ? ? ? 264 HIS B CD2 1 147 B B +ATOM 6498 C CE1 . HIS B 1 147 ? -47.775 44.531 50.250 1.0 54.65 ? ? ? ? ? ? 264 HIS B CE1 1 147 B B +ATOM 6499 N NE2 . HIS B 1 147 ? -46.769 43.755 49.900 1.0 65.71 ? ? ? ? ? ? 264 HIS B NE2 1 147 B B +ATOM 6500 N N . CYS B 1 148 ? -47.436 48.089 44.805 1.0 70.9 ? ? ? ? ? ? 265 CYS B N 1 148 B B +ATOM 6501 C CA . CYS B 1 148 ? -47.435 49.237 43.909 1.0 78.16 ? ? ? ? ? ? 265 CYS B CA 1 148 B B +ATOM 6502 C C . CYS B 1 148 ? -48.309 50.406 44.355 1.0 78.58 ? ? ? ? ? ? 265 CYS B C 1 148 B B +ATOM 6503 O O . CYS B 1 148 ? -49.303 50.231 45.063 1.0 77.71 ? ? ? ? ? ? 265 CYS B O 1 148 B B +ATOM 6504 C CB . CYS B 1 148 ? -47.867 48.774 42.515 1.0 71.85 ? ? ? ? ? ? 265 CYS B CB 1 148 B B +ATOM 6505 S SG . CYS B 1 148 ? -47.906 50.055 41.257 1.0 92.69 ? ? ? ? ? ? 265 CYS B SG 1 148 B B +ATOM 6506 N N . THR B 1 149 ? -47.912 51.601 43.928 1.0 70.23 ? ? ? ? ? ? 266 THR B N 1 149 B B +ATOM 6507 C CA . THR B 1 149 ? -48.629 52.833 44.233 1.0 59.7 ? ? ? ? ? ? 266 THR B CA 1 149 B B +ATOM 6508 C C . THR B 1 149 ? -49.603 53.135 43.092 1.0 54.47 ? ? ? ? ? ? 266 THR B C 1 149 B B +ATOM 6509 O O . THR B 1 149 ? -49.217 53.145 41.923 1.0 54.63 ? ? ? ? ? ? 266 THR B O 1 149 B B +ATOM 6510 C CB . THR B 1 149 ? -47.653 54.019 44.380 1.0 55.29 ? ? ? ? ? ? 266 THR B CB 1 149 B B +ATOM 6511 O OG1 . THR B 1 149 ? -47.137 54.381 43.093 1.0 37.72 ? ? ? ? ? ? 266 THR B OG1 1 149 B B +ATOM 6512 C CG2 . THR B 1 149 ? -46.496 53.642 45.286 1.0 59.9 ? ? ? ? ? ? 266 THR B CG2 1 149 B B +ATOM 6513 N N . GLN B 1 150 ? -50.865 53.378 43.433 1.0 44.15 ? ? ? ? ? ? 267 GLN B N 1 150 B B +ATOM 6514 C CA . GLN B 1 150 ? -51.881 53.671 42.428 1.0 43.6 ? ? ? ? ? ? 267 GLN B CA 1 150 B B +ATOM 6515 C C . GLN B 1 150 ? -51.917 55.148 42.057 1.0 41.75 ? ? ? ? ? ? 267 GLN B C 1 150 B B +ATOM 6516 O O . GLN B 1 150 ? -52.416 55.512 40.993 1.0 28.69 ? ? ? ? ? ? 267 GLN B O 1 150 B B +ATOM 6517 C CB . GLN B 1 150 ? -53.259 53.246 42.936 1.0 45.29 ? ? ? ? ? ? 267 GLN B CB 1 150 B B +ATOM 6518 C CG . GLN B 1 150 ? -54.383 53.474 41.944 1.0 34.06 ? ? ? ? ? ? 267 GLN B CG 1 150 B B +ATOM 6519 C CD . GLN B 1 150 ? -55.212 52.224 41.703 1.0 59.87 ? ? ? ? ? ? 267 GLN B CD 1 150 B B +ATOM 6520 O OE1 . GLN B 1 150 ? -55.741 51.619 42.642 1.0 57.98 ? ? ? ? ? ? 267 GLN B OE1 1 150 B B +ATOM 6521 N NE2 . GLN B 1 150 ? -55.335 51.833 40.436 1.0 68.1 ? ? ? ? ? ? 267 GLN B NE2 1 150 B B +ATOM 6522 N N . TYR B 1 151 ? -51.378 55.991 42.934 1.0 50.13 ? ? ? ? ? ? 268 TYR B N 1 151 B B +ATOM 6523 C CA . TYR B 1 151 ? -51.364 57.432 42.706 1.0 55.5 ? ? ? ? ? ? 268 TYR B CA 1 151 B B +ATOM 6524 C C . TYR B 1 151 ? -50.285 57.930 41.743 1.0 57.92 ? ? ? ? ? ? 268 TYR B C 1 151 B B +ATOM 6525 O O . TYR B 1 151 ? -49.548 57.141 41.150 1.0 50.68 ? ? ? ? ? ? 268 TYR B O 1 151 B B +ATOM 6526 C CB . TYR B 1 151 ? -51.261 58.174 44.046 1.0 64.16 ? ? ? ? ? ? 268 TYR B CB 1 151 B B +ATOM 6527 C CG . TYR B 1 151 ? -49.999 57.914 44.841 1.0 65.73 ? ? ? ? ? ? 268 TYR B CG 1 151 B B +ATOM 6528 C CD1 . TYR B 1 151 ? -48.819 58.605 44.559 1.0 64.71 ? ? ? ? ? ? 268 TYR B CD1 1 151 B B +ATOM 6529 C CD2 . TYR B 1 151 ? -49.996 57.011 45.907 1.0 79.87 ? ? ? ? ? ? 268 TYR B CD2 1 151 B B +ATOM 6530 C CE1 . TYR B 1 151 ? -47.669 58.411 45.321 1.0 76.68 ? ? ? ? ? ? 268 TYR B CE1 1 151 B B +ATOM 6531 C CE2 . TYR B 1 151 ? -48.850 56.809 46.677 1.0 90.35 ? ? ? ? ? ? 268 TYR B CE2 1 151 B B +ATOM 6532 C CZ . TYR B 1 151 ? -47.689 57.512 46.380 1.0 89.09 ? ? ? ? ? ? 268 TYR B CZ 1 151 B B +ATOM 6533 O OH . TYR B 1 151 ? -46.557 57.328 47.149 1.0 82.46 ? ? ? ? ? ? 268 TYR B OH 1 151 B B +ATOM 6534 N N . ILE B 1 152 ? -50.201 59.251 41.599 1.0 62.65 ? ? ? ? ? ? 269 ILE B N 1 152 B B +ATOM 6535 C CA . ILE B 1 152 ? -49.236 59.876 40.698 1.0 61.05 ? ? ? ? ? ? 269 ILE B CA 1 152 B B +ATOM 6536 C C . ILE B 1 152 ? -48.692 61.198 41.232 1.0 56.59 ? ? ? ? ? ? 269 ILE B C 1 152 B B +ATOM 6537 O O . ILE B 1 152 ? -49.374 61.906 41.971 1.0 53.39 ? ? ? ? ? ? 269 ILE B O 1 152 B B +ATOM 6538 C CB . ILE B 1 152 ? -49.871 60.159 39.327 1.0 70.67 ? ? ? ? ? ? 269 ILE B CB 1 152 B B +ATOM 6539 C CG1 . ILE B 1 152 ? -48.848 60.823 38.404 1.0 68.86 ? ? ? ? ? ? 269 ILE B CG1 1 152 B B +ATOM 6540 C CG2 . ILE B 1 152 ? -51.088 61.059 39.502 1.0 74.1 ? ? ? ? ? ? 269 ILE B CG2 1 152 B B +ATOM 6541 C CD1 . ILE B 1 152 ? -49.304 60.939 36.972 1.0 82.6 ? ? ? ? ? ? 269 ILE B CD1 1 152 B B +ATOM 6542 N N . ARG B 1 153 ? -47.467 61.530 40.836 1.0 64.18 ? ? ? ? ? ? 270 ARG B N 1 153 B B +ATOM 6543 C CA . ARG B 1 153 ? -46.820 62.764 41.259 1.0 70.1 ? ? ? ? ? ? 270 ARG B CA 1 153 B B +ATOM 6544 C C . ARG B 1 153 ? -47.694 63.956 40.893 1.0 79.83 ? ? ? ? ? ? 270 ARG B C 1 153 B B +ATOM 6545 O O . ARG B 1 153 ? -48.646 63.824 40.126 1.0 80.48 ? ? ? ? ? ? 270 ARG B O 1 153 B B +ATOM 6546 C CB . ARG B 1 153 ? -45.464 62.900 40.570 1.0 65.85 ? ? ? ? ? ? 270 ARG B CB 1 153 B B +ATOM 6547 C CG . ARG B 1 153 ? -45.550 62.888 39.054 1.0 66.82 ? ? ? ? ? ? 270 ARG B CG 1 153 B B +ATOM 6548 C CD . ARG B 1 153 ? -44.172 62.910 38.429 1.0 81.52 ? ? ? ? ? ? 270 ARG B CD 1 153 B B +ATOM 6549 N NE . ARG B 1 153 ? -43.675 61.562 38.172 1.0 87.21 ? ? ? ? ? ? 270 ARG B NE 1 153 B B +ATOM 6550 C CZ . ARG B 1 153 ? -42.731 61.273 37.284 1.0 88.22 ? ? ? ? ? ? 270 ARG B CZ 1 153 B B +ATOM 6551 N NH1 . ARG B 1 153 ? -42.178 62.238 36.562 1.0 90.32 ? ? ? ? ? ? 270 ARG B NH1 1 153 B B +ATOM 6552 N NH2 . ARG B 1 153 ? -42.338 60.019 37.118 1.0 75.36 ? ? ? ? ? ? 270 ARG B NH2 1 153 B B +ATOM 6553 N N . HIS B 1 154 ? -47.373 65.121 41.446 1.0 86.18 ? ? ? ? ? ? 271 HIS B N 1 154 B B +ATOM 6554 C CA . HIS B 1 154 ? -48.139 66.324 41.149 1.0 90.54 ? ? ? ? ? ? 271 HIS B CA 1 154 B B +ATOM 6555 C C . HIS B 1 154 ? -47.652 66.930 39.841 1.0 85.85 ? ? ? ? ? ? 271 HIS B C 1 154 B B +ATOM 6556 O O . HIS B 1 154 ? -46.453 66.954 39.564 1.0 64.73 ? ? ? ? ? ? 271 HIS B O 1 154 B B +ATOM 6557 C CB . HIS B 1 154 ? -48.003 67.355 42.272 1.0 95.52 ? ? ? ? ? ? 271 HIS B CB 1 154 B B +ATOM 6558 C CG . HIS B 1 154 ? -48.968 68.493 42.156 1.0 89.69 ? ? ? ? ? ? 271 HIS B CG 1 154 B B +ATOM 6559 N ND1 . HIS B 1 154 ? -48.561 69.798 41.981 1.0 76.85 ? ? ? ? ? ? 271 HIS B ND1 1 154 B B +ATOM 6560 C CD2 . HIS B 1 154 ? -50.322 68.519 42.161 1.0 91.52 ? ? ? ? ? ? 271 HIS B CD2 1 154 B B +ATOM 6561 C CE1 . HIS B 1 154 ? -49.624 70.578 41.882 1.0 88.56 ? ? ? ? ? ? 271 HIS B CE1 1 154 B B +ATOM 6562 N NE2 . HIS B 1 154 ? -50.704 69.825 41.988 1.0 92.65 ? ? ? ? ? ? 271 HIS B NE2 1 154 B B +ATOM 6563 N N . GLY B 1 155 ? -48.593 67.426 39.047 1.0 87.3 ? ? ? ? ? ? 272 GLY B N 1 155 B B +ATOM 6564 C CA . GLY B 1 155 ? -48.253 68.016 37.766 1.0 95.34 ? ? ? ? ? ? 272 GLY B CA 1 155 B B +ATOM 6565 C C . GLY B 1 155 ? -47.317 69.212 37.789 1.0 97.82 ? ? ? ? ? ? 272 GLY B C 1 155 B B +ATOM 6566 O O . GLY B 1 155 ? -46.806 69.603 36.740 1.0 89.23 ? ? ? ? ? ? 272 GLY B O 1 155 B B +ATOM 6567 N N . SER B 1 156 ? -47.087 69.801 38.960 1.0 99.95 ? ? ? ? ? ? 273 SER B N 1 156 B B +ATOM 6568 C CA . SER B 1 156 ? -46.199 70.960 39.055 1.0 94.57 ? ? ? ? ? ? 273 SER B CA 1 156 B B +ATOM 6569 C C . SER B 1 156 ? -44.850 70.649 38.420 1.0 82.28 ? ? ? ? ? ? 273 SER B C 1 156 B B +ATOM 6570 O O . SER B 1 156 ? -44.390 71.368 37.534 1.0 87.61 ? ? ? ? ? ? 273 SER B O 1 156 B B +ATOM 6571 C CB . SER B 1 156 ? -46.007 71.382 40.519 1.0 100.0 ? ? ? ? ? ? 273 SER B CB 1 156 B B +ATOM 6572 O OG . SER B 1 156 ? -45.427 70.348 41.293 1.0 92.2 ? ? ? ? ? ? 273 SER B OG 1 156 B B +ATOM 6573 N N . LYS B 1 157 ? -44.225 69.570 38.877 1.0 77.9 ? ? ? ? ? ? 274 LYS B N 1 157 B B +ATOM 6574 C CA . LYS B 1 157 ? -42.938 69.148 38.341 1.0 89.43 ? ? ? ? ? ? 274 LYS B CA 1 157 B B +ATOM 6575 C C . LYS B 1 157 ? -43.052 67.708 37.846 1.0 94.52 ? ? ? ? ? ? 274 LYS B C 1 157 B B +ATOM 6576 O O . LYS B 1 157 ? -42.761 66.758 38.575 1.0 86.19 ? ? ? ? ? ? 274 LYS B O 1 157 B B +ATOM 6577 C CB . LYS B 1 157 ? -41.853 69.272 39.414 1.0 89.55 ? ? ? ? ? ? 274 LYS B CB 1 157 B B +ATOM 6578 C CG . LYS B 1 157 ? -41.369 70.704 39.616 1.0 92.41 ? ? ? ? ? ? 274 LYS B CG 1 157 B B +ATOM 6579 C CD . LYS B 1 157 ? -40.805 71.285 38.324 1.0 99.23 ? ? ? ? ? ? 274 LYS B CD 1 157 B B +ATOM 6580 C CE . LYS B 1 157 ? -40.452 72.758 38.479 1.0 99.82 ? ? ? ? ? ? 274 LYS B CE 1 157 B B +ATOM 6581 N NZ . LYS B 1 157 ? -40.050 73.381 37.185 1.0 100.0 ? ? ? ? ? ? 274 LYS B NZ 1 157 B B +ATOM 6582 N N . PRO B 1 158 ? -43.491 67.538 36.586 1.0 100.0 ? ? ? ? ? ? 275 PRO B N 1 158 B B +ATOM 6583 C CA . PRO B 1 158 ? -43.669 66.230 35.944 1.0 100.0 ? ? ? ? ? ? 275 PRO B CA 1 158 B B +ATOM 6584 C C . PRO B 1 158 ? -42.367 65.507 35.607 1.0 92.42 ? ? ? ? ? ? 275 PRO B C 1 158 B B +ATOM 6585 O O . PRO B 1 158 ? -42.377 64.474 34.934 1.0 86.52 ? ? ? ? ? ? 275 PRO B O 1 158 B B +ATOM 6586 C CB . PRO B 1 158 ? -44.487 66.554 34.695 1.0 100.0 ? ? ? ? ? ? 275 PRO B CB 1 158 B B +ATOM 6587 C CG . PRO B 1 158 ? -44.133 67.963 34.375 1.0 100.0 ? ? ? ? ? ? 275 PRO B CG 1 158 B B +ATOM 6588 C CD . PRO B 1 158 ? -43.848 68.647 35.681 1.0 98.17 ? ? ? ? ? ? 275 PRO B CD 1 158 B B +ATOM 6589 N N . MET B 1 159 ? -41.249 66.049 36.081 1.0 81.69 ? ? ? ? ? ? 276 MET B N 1 159 B B +ATOM 6590 C CA . MET B 1 159 ? -39.947 65.444 35.826 1.0 91.13 ? ? ? ? ? ? 276 MET B CA 1 159 B B +ATOM 6591 C C . MET B 1 159 ? -39.250 65.096 37.138 1.0 93.32 ? ? ? ? ? ? 276 MET B C 1 159 B B +ATOM 6592 O O . MET B 1 159 ? -38.050 64.821 37.165 1.0 100.0 ? ? ? ? ? ? 276 MET B O 1 159 B B +ATOM 6593 C CB . MET B 1 159 ? -39.074 66.404 35.012 1.0 100.0 ? ? ? ? ? ? 276 MET B CB 1 159 B B +ATOM 6594 C CG . MET B 1 159 ? -38.520 65.815 33.721 1.0 100.0 ? ? ? ? ? ? 276 MET B CG 1 159 B B +ATOM 6595 S SD . MET B 1 159 ? -39.786 65.096 32.646 1.0 100.0 ? ? ? ? ? ? 276 MET B SD 1 159 B B +ATOM 6596 C CE . MET B 1 159 ? -39.536 63.354 32.966 1.0 100.0 ? ? ? ? ? ? 276 MET B CE 1 159 B B +ATOM 6597 N N . TYR B 1 160 ? -40.013 65.103 38.225 1.0 90.51 ? ? ? ? ? ? 277 TYR B N 1 160 B B +ATOM 6598 C CA . TYR B 1 160 ? -39.458 64.791 39.531 1.0 93.75 ? ? ? ? ? ? 277 TYR B CA 1 160 B B +ATOM 6599 C C . TYR B 1 160 ? -40.507 64.265 40.503 1.0 95.85 ? ? ? ? ? ? 277 TYR B C 1 160 B B +ATOM 6600 O O . TYR B 1 160 ? -41.626 64.780 40.570 1.0 94.33 ? ? ? ? ? ? 277 TYR B O 1 160 B B +ATOM 6601 C CB . TYR B 1 160 ? -38.790 66.032 40.123 1.0 100.0 ? ? ? ? ? ? 277 TYR B CB 1 160 B B +ATOM 6602 C CG . TYR B 1 160 ? -38.720 66.023 41.631 1.0 98.17 ? ? ? ? ? ? 277 TYR B CG 1 160 B B +ATOM 6603 C CD1 . TYR B 1 160 ? -37.804 65.212 42.297 1.0 100.0 ? ? ? ? ? ? 277 TYR B CD1 1 160 B B +ATOM 6604 C CD2 . TYR B 1 160 ? -39.574 66.819 42.393 1.0 88.77 ? ? ? ? ? ? 277 TYR B CD2 1 160 B B +ATOM 6605 C CE1 . TYR B 1 160 ? -37.740 65.193 43.684 1.0 100.0 ? ? ? ? ? ? 277 TYR B CE1 1 160 B B +ATOM 6606 C CE2 . TYR B 1 160 ? -39.519 66.807 43.780 1.0 94.7 ? ? ? ? ? ? 277 TYR B CE2 1 160 B B +ATOM 6607 C CZ . TYR B 1 160 ? -38.599 65.993 44.420 1.0 100.0 ? ? ? ? ? ? 277 TYR B CZ 1 160 B B +ATOM 6608 O OH . TYR B 1 160 ? -38.534 65.987 45.795 1.0 100.0 ? ? ? ? ? ? 277 TYR B OH 1 160 B B +ATOM 6609 N N . THR B 1 161 ? -40.128 63.236 41.253 1.0 95.17 ? ? ? ? ? ? 278 THR B N 1 161 B B +ATOM 6610 C CA . THR B 1 161 ? -41.008 62.633 42.248 1.0 98.21 ? ? ? ? ? ? 278 THR B CA 1 161 B B +ATOM 6611 C C . THR B 1 161 ? -40.183 62.325 43.493 1.0 93.52 ? ? ? ? ? ? 278 THR B C 1 161 B B +ATOM 6612 O O . THR B 1 161 ? -39.116 61.717 43.410 1.0 89.12 ? ? ? ? ? ? 278 THR B O 1 161 B B +ATOM 6613 C CB . THR B 1 161 ? -41.651 61.331 41.726 1.0 100.0 ? ? ? ? ? ? 278 THR B CB 1 161 B B +ATOM 6614 O OG1 . THR B 1 161 ? -41.895 61.454 40.319 1.0 100.0 ? ? ? ? ? ? 278 THR B OG1 1 161 B B +ATOM 6615 C CG2 . THR B 1 161 ? -42.968 61.078 42.438 1.0 97.39 ? ? ? ? ? ? 278 THR B CG2 1 161 B B +ATOM 6616 N N . PRO B 1 162 ? -40.672 62.739 44.672 1.0 96.39 ? ? ? ? ? ? 279 PRO B N 1 162 B B +ATOM 6617 C CA . PRO B 1 162 ? -39.940 62.489 45.918 1.0 95.92 ? ? ? ? ? ? 279 PRO B CA 1 162 B B +ATOM 6618 C C . PRO B 1 162 ? -40.085 61.053 46.409 1.0 87.33 ? ? ? ? ? ? 279 PRO B C 1 162 B B +ATOM 6619 O O . PRO B 1 162 ? -39.436 60.638 47.366 1.0 85.43 ? ? ? ? ? ? 279 PRO B O 1 162 B B +ATOM 6620 C CB . PRO B 1 162 ? -40.547 63.494 46.891 1.0 99.85 ? ? ? ? ? ? 279 PRO B CB 1 162 B B +ATOM 6621 C CG . PRO B 1 162 ? -41.942 63.711 46.390 1.0 93.17 ? ? ? ? ? ? 279 PRO B CG 1 162 B B +ATOM 6622 C CD . PRO B 1 162 ? -41.950 63.432 44.908 1.0 96.89 ? ? ? ? ? ? 279 PRO B CD 1 162 B B +ATOM 6623 N N . GLU B 1 163 ? -40.935 60.292 45.727 1.0 77.03 ? ? ? ? ? ? 280 GLU B N 1 163 B B +ATOM 6624 C CA . GLU B 1 163 ? -41.181 58.905 46.088 1.0 74.74 ? ? ? ? ? ? 280 GLU B CA 1 163 B B +ATOM 6625 C C . GLU B 1 163 ? -41.876 58.169 44.944 1.0 78.36 ? ? ? ? ? ? 280 GLU B C 1 163 B B +ATOM 6626 O O . GLU B 1 163 ? -42.347 58.786 43.991 1.0 70.27 ? ? ? ? ? ? 280 GLU B O 1 163 B B +ATOM 6627 C CB . GLU B 1 163 ? -42.037 58.851 47.355 1.0 68.54 ? ? ? ? ? ? 280 GLU B CB 1 163 B B +ATOM 6628 C CG . GLU B 1 163 ? -43.525 58.950 47.083 1.0 83.22 ? ? ? ? ? ? 280 GLU B CG 1 163 B B +ATOM 6629 C CD . GLU B 1 163 ? -44.013 60.384 47.074 1.0 90.41 ? ? ? ? ? ? 280 GLU B CD 1 163 B B +ATOM 6630 O OE1 . GLU B 1 163 ? -44.071 61.002 48.156 1.0 86.76 ? ? ? ? ? ? 280 GLU B OE1 1 163 B B +ATOM 6631 O OE2 . GLU B 1 163 ? -44.341 60.897 45.986 1.0 98.96 ? ? ? ? ? ? 280 GLU B OE2 1 163 B B +ATOM 6632 N N . PRO B 1 164 ? -41.981 56.834 45.048 1.0 79.29 ? ? ? ? ? ? 281 PRO B N 1 164 B B +ATOM 6633 C CA . PRO B 1 164 ? -42.623 56.037 43.996 1.0 81.83 ? ? ? ? ? ? 281 PRO B CA 1 164 B B +ATOM 6634 C C . PRO B 1 164 ? -44.057 56.416 43.641 1.0 72.28 ? ? ? ? ? ? 281 PRO B C 1 164 B B +ATOM 6635 O O . PRO B 1 164 ? -44.912 56.539 44.515 1.0 76.26 ? ? ? ? ? ? 281 PRO B O 1 164 B B +ATOM 6636 C CB . PRO B 1 164 ? -42.533 54.602 44.517 1.0 86.01 ? ? ? ? ? ? 281 PRO B CB 1 164 B B +ATOM 6637 C CG . PRO B 1 164 ? -41.529 54.635 45.610 1.0 95.32 ? ? ? ? ? ? 281 PRO B CG 1 164 B B +ATOM 6638 C CD . PRO B 1 164 ? -41.555 56.005 46.188 1.0 84.71 ? ? ? ? ? ? 281 PRO B CD 1 164 B B +ATOM 6639 N N . ASP B 1 165 ? -44.303 56.591 42.345 1.0 57.88 ? ? ? ? ? ? 282 ASP B N 1 165 B B +ATOM 6640 C CA . ASP B 1 165 ? -45.625 56.924 41.814 1.0 52.74 ? ? ? ? ? ? 282 ASP B CA 1 165 B B +ATOM 6641 C C . ASP B 1 165 ? -45.931 55.914 40.710 1.0 54.7 ? ? ? ? ? ? 282 ASP B C 1 165 B B +ATOM 6642 O O . ASP B 1 165 ? -45.044 55.168 40.297 1.0 58.09 ? ? ? ? ? ? 282 ASP B O 1 165 B B +ATOM 6643 C CB . ASP B 1 165 ? -45.633 58.341 41.240 1.0 66.43 ? ? ? ? ? ? 282 ASP B CB 1 165 B B +ATOM 6644 C CG . ASP B 1 165 ? -44.863 58.449 39.939 1.0 78.92 ? ? ? ? ? ? 282 ASP B CG 1 165 B B +ATOM 6645 O OD1 . ASP B 1 165 ? -45.340 59.148 39.023 1.0 87.37 ? ? ? ? ? ? 282 ASP B OD1 1 165 B B +ATOM 6646 O OD2 . ASP B 1 165 ? -43.782 57.838 39.832 1.0 86.33 ? ? ? ? ? ? 282 ASP B OD2 1 165 B B +ATOM 6647 N N . ILE B 1 166 ? -47.166 55.889 40.222 1.0 66.28 ? ? ? ? ? ? 283 ILE B N 1 166 B B +ATOM 6648 C CA . ILE B 1 166 ? -47.542 54.932 39.180 1.0 71.93 ? ? ? ? ? ? 283 ILE B CA 1 166 B B +ATOM 6649 C C . ILE B 1 166 ? -46.640 54.941 37.942 1.0 74.24 ? ? ? ? ? ? 283 ILE B C 1 166 B B +ATOM 6650 O O . ILE B 1 166 ? -46.714 54.043 37.103 1.0 73.66 ? ? ? ? ? ? 283 ILE B O 1 166 B B +ATOM 6651 C CB . ILE B 1 166 ? -49.000 55.144 38.717 1.0 62.68 ? ? ? ? ? ? 283 ILE B CB 1 166 B B +ATOM 6652 C CG1 . ILE B 1 166 ? -49.479 53.911 37.941 1.0 54.55 ? ? ? ? ? ? 283 ILE B CG1 1 166 B B +ATOM 6653 C CG2 . ILE B 1 166 ? -49.097 56.393 37.856 1.0 68.03 ? ? ? ? ? ? 283 ILE B CG2 1 166 B B +ATOM 6654 C CD1 . ILE B 1 166 ? -50.987 53.760 37.881 1.0 69.59 ? ? ? ? ? ? 283 ILE B CD1 1 166 B B +ATOM 6655 N N . CYS B 1 167 ? -45.790 55.954 37.823 1.0 73.07 ? ? ? ? ? ? 284 CYS B N 1 167 B B +ATOM 6656 C CA . CYS B 1 167 ? -44.882 56.037 36.689 1.0 79.04 ? ? ? ? ? ? 284 CYS B CA 1 167 B B +ATOM 6657 C C . CYS B 1 167 ? -43.635 55.222 37.000 1.0 74.38 ? ? ? ? ? ? 284 CYS B C 1 167 B B +ATOM 6658 O O . CYS B 1 167 ? -43.191 54.411 36.189 1.0 83.07 ? ? ? ? ? ? 284 CYS B O 1 167 B B +ATOM 6659 C CB . CYS B 1 167 ? -44.493 57.493 36.423 1.0 87.12 ? ? ? ? ? ? 284 CYS B CB 1 167 B B +ATOM 6660 S SG . CYS B 1 167 ? -45.886 58.633 36.313 1.0 100.0 ? ? ? ? ? ? 284 CYS B SG 1 167 B B +ATOM 6661 N N . HIS B 1 168 ? -43.074 55.445 38.183 1.0 63.84 ? ? ? ? ? ? 285 HIS B N 1 168 B B +ATOM 6662 C CA . HIS B 1 168 ? -41.878 54.729 38.610 1.0 71.0 ? ? ? ? ? ? 285 HIS B CA 1 168 B B +ATOM 6663 C C . HIS B 1 168 ? -42.148 53.226 38.658 1.0 74.3 ? ? ? ? ? ? 285 HIS B C 1 168 B B +ATOM 6664 O O . HIS B 1 168 ? -41.334 52.419 38.198 1.0 64.25 ? ? ? ? ? ? 285 HIS B O 1 168 B B +ATOM 6665 C CB . HIS B 1 168 ? -41.437 55.234 39.989 1.0 70.96 ? ? ? ? ? ? 285 HIS B CB 1 168 B B +ATOM 6666 C CG . HIS B 1 168 ? -40.495 54.315 40.704 1.0 80.88 ? ? ? ? ? ? 285 HIS B CG 1 168 B B +ATOM 6667 N ND1 . HIS B 1 168 ? -39.134 54.320 40.478 1.0 86.16 ? ? ? ? ? ? 285 HIS B ND1 1 168 B B +ATOM 6668 C CD2 . HIS B 1 168 ? -40.715 53.386 41.664 1.0 81.95 ? ? ? ? ? ? 285 HIS B CD2 1 168 B B +ATOM 6669 C CE1 . HIS B 1 168 ? -38.557 53.434 41.271 1.0 92.15 ? ? ? ? ? ? 285 HIS B CE1 1 168 B B +ATOM 6670 N NE2 . HIS B 1 168 ? -39.492 52.853 42.002 1.0 94.55 ? ? ? ? ? ? 285 HIS B NE2 1 168 B B +ATOM 6671 N N . GLU B 1 169 ? -43.306 52.861 39.197 1.0 72.7 ? ? ? ? ? ? 286 GLU B N 1 169 B B +ATOM 6672 C CA . GLU B 1 169 ? -43.688 51.463 39.321 1.0 68.31 ? ? ? ? ? ? 286 GLU B CA 1 169 B B +ATOM 6673 C C . GLU B 1 169 ? -43.988 50.795 37.985 1.0 66.37 ? ? ? ? ? ? 286 GLU B C 1 169 B B +ATOM 6674 O O . GLU B 1 169 ? -43.587 49.656 37.756 1.0 83.61 ? ? ? ? ? ? 286 GLU B O 1 169 B B +ATOM 6675 C CB . GLU B 1 169 ? -44.910 51.336 40.236 1.0 70.61 ? ? ? ? ? ? 286 GLU B CB 1 169 B B +ATOM 6676 C CG . GLU B 1 169 ? -44.863 52.224 41.468 1.0 90.67 ? ? ? ? ? ? 286 GLU B CG 1 169 B B +ATOM 6677 C CD . GLU B 1 169 ? -44.128 51.584 42.632 1.0 93.74 ? ? ? ? ? ? 286 GLU B CD 1 169 B B +ATOM 6678 O OE1 . GLU B 1 169 ? -44.787 50.956 43.484 1.0 87.42 ? ? ? ? ? ? 286 GLU B OE1 1 169 B B +ATOM 6679 O OE2 . GLU B 1 169 ? -42.890 51.714 42.705 1.0 87.7 ? ? ? ? ? ? 286 GLU B OE2 1 169 B B +ATOM 6680 N N . LEU B 1 170 ? -44.687 51.507 37.106 1.0 61.19 ? ? ? ? ? ? 287 LEU B N 1 170 B B +ATOM 6681 C CA . LEU B 1 170 ? -45.062 50.963 35.802 1.0 51.14 ? ? ? ? ? ? 287 LEU B CA 1 170 B B +ATOM 6682 C C . LEU B 1 170 ? -44.002 51.109 34.712 1.0 55.43 ? ? ? ? ? ? 287 LEU B C 1 170 B B +ATOM 6683 O O . LEU B 1 170 ? -43.787 50.187 33.928 1.0 52.39 ? ? ? ? ? ? 287 LEU B O 1 170 B B +ATOM 6684 C CB . LEU B 1 170 ? -46.365 51.608 35.328 1.0 52.01 ? ? ? ? ? ? 287 LEU B CB 1 170 B B +ATOM 6685 C CG . LEU B 1 170 ? -47.683 51.118 35.939 1.0 56.75 ? ? ? ? ? ? 287 LEU B CG 1 170 B B +ATOM 6686 C CD1 . LEU B 1 170 ? -48.849 51.689 35.139 1.0 51.84 ? ? ? ? ? ? 287 LEU B CD1 1 170 B B +ATOM 6687 C CD2 . LEU B 1 170 ? -47.735 49.597 35.942 1.0 26.43 ? ? ? ? ? ? 287 LEU B CD2 1 170 B B +ATOM 6688 N N . LEU B 1 171 ? -43.350 52.266 34.654 1.0 63.3 ? ? ? ? ? ? 288 LEU B N 1 171 B B +ATOM 6689 C CA . LEU B 1 171 ? -42.316 52.514 33.650 1.0 63.83 ? ? ? ? ? ? 288 LEU B CA 1 171 B B +ATOM 6690 C C . LEU B 1 171 ? -40.926 52.325 34.246 1.0 72.88 ? ? ? ? ? ? 288 LEU B C 1 171 B B +ATOM 6691 O O . LEU B 1 171 ? -39.964 52.971 33.824 1.0 76.97 ? ? ? ? ? ? 288 LEU B O 1 171 B B +ATOM 6692 C CB . LEU B 1 171 ? -42.440 53.938 33.094 1.0 59.92 ? ? ? ? ? ? 288 LEU B CB 1 171 B B +ATOM 6693 C CG . LEU B 1 171 ? -43.815 54.376 32.581 1.0 61.12 ? ? ? ? ? ? 288 LEU B CG 1 171 B B +ATOM 6694 C CD1 . LEU B 1 171 ? -43.798 55.868 32.298 1.0 71.68 ? ? ? ? ? ? 288 LEU B CD1 1 171 B B +ATOM 6695 C CD2 . LEU B 1 171 ? -44.174 53.598 31.328 1.0 63.71 ? ? ? ? ? ? 288 LEU B CD2 1 171 B B +ATOM 6696 N N . GLY B 1 172 ? -40.826 51.440 35.233 1.0 76.38 ? ? ? ? ? ? 289 GLY B N 1 172 B B +ATOM 6697 C CA . GLY B 1 172 ? -39.545 51.193 35.866 1.0 79.16 ? ? ? ? ? ? 289 GLY B CA 1 172 B B +ATOM 6698 C C . GLY B 1 172 ? -39.412 49.797 36.439 1.0 75.97 ? ? ? ? ? ? 289 GLY B C 1 172 B B +ATOM 6699 O O . GLY B 1 172 ? -38.494 49.057 36.079 1.0 79.25 ? ? ? ? ? ? 289 GLY B O 1 172 B B +ATOM 6700 N N . HIS B 1 173 ? -40.330 49.438 37.332 1.0 67.22 ? ? ? ? ? ? 290 HIS B N 1 173 B B +ATOM 6701 C CA . HIS B 1 173 ? -40.308 48.125 37.971 1.0 70.99 ? ? ? ? ? ? 290 HIS B CA 1 173 B B +ATOM 6702 C C . HIS B 1 173 ? -40.985 47.031 37.143 1.0 67.43 ? ? ? ? ? ? 290 HIS B C 1 173 B B +ATOM 6703 O O . HIS B 1 173 ? -40.361 46.033 36.780 1.0 77.17 ? ? ? ? ? ? 290 HIS B O 1 173 B B +ATOM 6704 C CB . HIS B 1 173 ? -40.976 48.202 39.350 1.0 67.02 ? ? ? ? ? ? 290 HIS B CB 1 173 B B +ATOM 6705 C CG . HIS B 1 173 ? -40.089 48.757 40.422 1.0 67.51 ? ? ? ? ? ? 290 HIS B CG 1 173 B B +ATOM 6706 N ND1 . HIS B 1 173 ? -39.238 47.972 41.167 1.0 73.03 ? ? ? ? ? ? 290 HIS B ND1 1 173 B B +ATOM 6707 C CD2 . HIS B 1 173 ? -39.924 50.024 40.873 1.0 69.16 ? ? ? ? ? ? 290 HIS B CD2 1 173 B B +ATOM 6708 C CE1 . HIS B 1 173 ? -38.584 48.728 42.031 1.0 74.93 ? ? ? ? ? ? 290 HIS B CE1 1 173 B B +ATOM 6709 N NE2 . HIS B 1 173 ? -38.982 49.978 41.873 1.0 78.02 ? ? ? ? ? ? 290 HIS B NE2 1 173 B B +ATOM 6710 N N . VAL B 1 174 ? -42.266 47.233 36.851 1.0 66.78 ? ? ? ? ? ? 291 VAL B N 1 174 B B +ATOM 6711 C CA . VAL B 1 174 ? -43.073 46.277 36.096 1.0 71.14 ? ? ? ? ? ? 291 VAL B CA 1 174 B B +ATOM 6712 C C . VAL B 1 174 ? -42.396 45.541 34.935 1.0 72.81 ? ? ? ? ? ? 291 VAL B C 1 174 B B +ATOM 6713 O O . VAL B 1 174 ? -42.426 44.309 34.882 1.0 57.34 ? ? ? ? ? ? 291 VAL B O 1 174 B B +ATOM 6714 C CB . VAL B 1 174 ? -44.356 46.958 35.561 1.0 69.21 ? ? ? ? ? ? 291 VAL B CB 1 174 B B +ATOM 6715 C CG1 . VAL B 1 174 ? -45.138 45.998 34.674 1.0 59.39 ? ? ? ? ? ? 291 VAL B CG1 1 174 B B +ATOM 6716 C CG2 . VAL B 1 174 ? -45.221 47.413 36.721 1.0 62.18 ? ? ? ? ? ? 291 VAL B CG2 1 174 B B +ATOM 6717 N N . PRO B 1 175 ? -41.778 46.282 33.992 1.0 73.61 ? ? ? ? ? ? 292 PRO B N 1 175 B B +ATOM 6718 C CA . PRO B 1 175 ? -41.130 45.603 32.861 1.0 71.67 ? ? ? ? ? ? 292 PRO B CA 1 175 B B +ATOM 6719 C C . PRO B 1 175 ? -40.092 44.563 33.254 1.0 72.48 ? ? ? ? ? ? 292 PRO B C 1 175 B B +ATOM 6720 O O . PRO B 1 175 ? -39.877 43.596 32.529 1.0 79.75 ? ? ? ? ? ? 292 PRO B O 1 175 B B +ATOM 6721 C CB . PRO B 1 175 ? -40.516 46.742 32.043 1.0 62.64 ? ? ? ? ? ? 292 PRO B CB 1 175 B B +ATOM 6722 C CG . PRO B 1 175 ? -41.202 47.969 32.497 1.0 69.22 ? ? ? ? ? ? 292 PRO B CG 1 175 B B +ATOM 6723 C CD . PRO B 1 175 ? -41.622 47.743 33.918 1.0 66.49 ? ? ? ? ? ? 292 PRO B CD 1 175 B B +ATOM 6724 N N . LEU B 1 176 ? -39.444 44.763 34.399 1.0 57.88 ? ? ? ? ? ? 293 LEU B N 1 176 B B +ATOM 6725 C CA . LEU B 1 176 ? -38.434 43.822 34.859 1.0 51.03 ? ? ? ? ? ? 293 LEU B CA 1 176 B B +ATOM 6726 C C . LEU B 1 176 ? -39.085 42.605 35.500 1.0 51.98 ? ? ? ? ? ? 293 LEU B C 1 176 B B +ATOM 6727 O O . LEU B 1 176 ? -38.580 41.489 35.392 1.0 55.82 ? ? ? ? ? ? 293 LEU B O 1 176 B B +ATOM 6728 C CB . LEU B 1 176 ? -37.500 44.498 35.863 1.0 52.91 ? ? ? ? ? ? 293 LEU B CB 1 176 B B +ATOM 6729 C CG . LEU B 1 176 ? -36.324 45.285 35.276 1.0 71.66 ? ? ? ? ? ? 293 LEU B CG 1 176 B B +ATOM 6730 C CD1 . LEU B 1 176 ? -35.552 44.418 34.289 1.0 78.03 ? ? ? ? ? ? 293 LEU B CD1 1 176 B B +ATOM 6731 C CD2 . LEU B 1 176 ? -36.843 46.533 34.592 1.0 61.55 ? ? ? ? ? ? 293 LEU B CD2 1 176 B B +ATOM 6732 N N . PHE B 1 177 ? -40.215 42.830 36.164 1.0 56.22 ? ? ? ? ? ? 294 PHE B N 1 177 B B +ATOM 6733 C CA . PHE B 1 177 ? -40.942 41.752 36.825 1.0 54.22 ? ? ? ? ? ? 294 PHE B CA 1 177 B B +ATOM 6734 C C . PHE B 1 177 ? -41.658 40.863 35.810 1.0 53.13 ? ? ? ? ? ? 294 PHE B C 1 177 B B +ATOM 6735 O O . PHE B 1 177 ? -42.345 39.913 36.182 1.0 51.22 ? ? ? ? ? ? 294 PHE B O 1 177 B B +ATOM 6736 C CB . PHE B 1 177 ? -41.962 42.328 37.817 1.0 55.75 ? ? ? ? ? ? 294 PHE B CB 1 177 B B +ATOM 6737 C CG . PHE B 1 177 ? -41.345 42.894 39.061 1.0 54.18 ? ? ? ? ? ? 294 PHE B CG 1 177 B B +ATOM 6738 C CD1 . PHE B 1 177 ? -40.886 42.056 40.074 1.0 42.65 ? ? ? ? ? ? 294 PHE B CD1 1 177 B B +ATOM 6739 C CD2 . PHE B 1 177 ? -41.209 44.269 39.214 1.0 62.02 ? ? ? ? ? ? 294 PHE B CD2 1 177 B B +ATOM 6740 C CE1 . PHE B 1 177 ? -40.297 42.581 41.223 1.0 44.22 ? ? ? ? ? ? 294 PHE B CE1 1 177 B B +ATOM 6741 C CE2 . PHE B 1 177 ? -40.622 44.805 40.358 1.0 61.59 ? ? ? ? ? ? 294 PHE B CE2 1 177 B B +ATOM 6742 C CZ . PHE B 1 177 ? -40.165 43.959 41.364 1.0 63.94 ? ? ? ? ? ? 294 PHE B CZ 1 177 B B +ATOM 6743 N N . SER B 1 178 ? -41.506 41.178 34.528 1.0 42.33 ? ? ? ? ? ? 295 SER B N 1 178 B B +ATOM 6744 C CA . SER B 1 178 ? -42.134 40.380 33.485 1.0 57.34 ? ? ? ? ? ? 295 SER B CA 1 178 B B +ATOM 6745 C C . SER B 1 178 ? -41.125 39.350 32.990 1.0 67.54 ? ? ? ? ? ? 295 SER B C 1 178 B B +ATOM 6746 O O . SER B 1 178 ? -41.484 38.402 32.290 1.0 70.27 ? ? ? ? ? ? 295 SER B O 1 178 B B +ATOM 6747 C CB . SER B 1 178 ? -42.578 41.271 32.328 1.0 57.63 ? ? ? ? ? ? 295 SER B CB 1 178 B B +ATOM 6748 O OG . SER B 1 178 ? -41.485 41.995 31.798 1.0 81.53 ? ? ? ? ? ? 295 SER B OG 1 178 B B +ATOM 6749 N N . ASP B 1 179 ? -39.864 39.540 33.377 1.0 69.04 ? ? ? ? ? ? 296 ASP B N 1 179 B B +ATOM 6750 C CA . ASP B 1 179 ? -38.781 38.648 32.974 1.0 69.72 ? ? ? ? ? ? 296 ASP B CA 1 179 B B +ATOM 6751 C C . ASP B 1 179 ? -38.601 37.480 33.939 1.0 73.53 ? ? ? ? ? ? 296 ASP B C 1 179 B B +ATOM 6752 O O . ASP B 1 179 ? -38.401 37.668 35.139 1.0 79.47 ? ? ? ? ? ? 296 ASP B O 1 179 B B +ATOM 6753 C CB . ASP B 1 179 ? -37.471 39.426 32.861 1.0 73.34 ? ? ? ? ? ? 296 ASP B CB 1 179 B B +ATOM 6754 C CG . ASP B 1 179 ? -36.278 38.523 32.636 1.0 87.96 ? ? ? ? ? ? 296 ASP B CG 1 179 B B +ATOM 6755 O OD1 . ASP B 1 179 ? -36.218 37.877 31.568 1.0 93.45 ? ? ? ? ? ? 296 ASP B OD1 1 179 B B +ATOM 6756 O OD2 . ASP B 1 179 ? -35.406 38.460 33.528 1.0 87.02 ? ? ? ? ? ? 296 ASP B OD2 1 179 B B +ATOM 6757 N N . ARG B 1 180 ? -38.665 36.274 33.384 1.0 66.35 ? ? ? ? ? ? 297 ARG B N 1 180 B B +ATOM 6758 C CA . ARG B 1 180 ? -38.534 35.031 34.136 1.0 61.68 ? ? ? ? ? ? 297 ARG B CA 1 180 B B +ATOM 6759 C C . ARG B 1 180 ? -37.387 34.994 35.141 1.0 59.82 ? ? ? ? ? ? 297 ARG B C 1 180 B B +ATOM 6760 O O . ARG B 1 180 ? -37.589 34.683 36.314 1.0 49.35 ? ? ? ? ? ? 297 ARG B O 1 180 B B +ATOM 6761 C CB . ARG B 1 180 ? -38.376 33.866 33.159 1.0 74.84 ? ? ? ? ? ? 297 ARG B CB 1 180 B B +ATOM 6762 C CG . ARG B 1 180 ? -38.056 32.547 33.820 1.0 80.99 ? ? ? ? ? ? 297 ARG B CG 1 180 B B +ATOM 6763 C CD . ARG B 1 180 ? -39.312 31.917 34.373 1.0 94.19 ? ? ? ? ? ? 297 ARG B CD 1 180 B B +ATOM 6764 N NE . ARG B 1 180 ? -39.033 30.645 35.031 1.0 100.0 ? ? ? ? ? ? 297 ARG B NE 1 180 B B +ATOM 6765 C CZ . ARG B 1 180 ? -38.772 29.509 34.391 1.0 100.0 ? ? ? ? ? ? 297 ARG B CZ 1 180 B B +ATOM 6766 N NH1 . ARG B 1 180 ? -38.749 29.480 33.064 1.0 100.0 ? ? ? ? ? ? 297 ARG B NH1 1 180 B B +ATOM 6767 N NH2 . ARG B 1 180 ? -38.534 28.401 35.082 1.0 100.0 ? ? ? ? ? ? 297 ARG B NH2 1 180 B B +ATOM 6768 N N . SER B 1 181 ? -36.182 35.295 34.675 1.0 62.25 ? ? ? ? ? ? 298 SER B N 1 181 B B +ATOM 6769 C CA . SER B 1 181 ? -35.008 35.270 35.537 1.0 74.66 ? ? ? ? ? ? 298 SER B CA 1 181 B B +ATOM 6770 C C . SER B 1 181 ? -35.052 36.317 36.644 1.0 74.28 ? ? ? ? ? ? 298 SER B C 1 181 B B +ATOM 6771 O O . SER B 1 181 ? -34.607 36.060 37.764 1.0 69.21 ? ? ? ? ? ? 298 SER B O 1 181 B B +ATOM 6772 C CB . SER B 1 181 ? -33.739 35.461 34.699 1.0 88.66 ? ? ? ? ? ? 298 SER B CB 1 181 B B +ATOM 6773 O OG . SER B 1 181 ? -33.660 34.503 33.655 1.0 96.26 ? ? ? ? ? ? 298 SER B OG 1 181 B B +ATOM 6774 N N . PHE B 1 182 ? -35.588 37.495 36.334 1.0 69.97 ? ? ? ? ? ? 299 PHE B N 1 182 B B +ATOM 6775 C CA . PHE B 1 182 ? -35.665 38.572 37.317 1.0 68.19 ? ? ? ? ? ? 299 PHE B CA 1 182 B B +ATOM 6776 C C . PHE B 1 182 ? -36.595 38.245 38.482 1.0 72.62 ? ? ? ? ? ? 299 PHE B C 1 182 B B +ATOM 6777 O O . PHE B 1 182 ? -36.286 38.551 39.634 1.0 71.2 ? ? ? ? ? ? 299 PHE B O 1 182 B B +ATOM 6778 C CB . PHE B 1 182 ? -36.122 39.874 36.653 1.0 62.01 ? ? ? ? ? ? 299 PHE B CB 1 182 B B +ATOM 6779 C CG . PHE B 1 182 ? -36.043 41.071 37.560 1.0 80.44 ? ? ? ? ? ? 299 PHE B CG 1 182 B B +ATOM 6780 C CD1 . PHE B 1 182 ? -34.970 41.954 37.481 1.0 85.38 ? ? ? ? ? ? 299 PHE B CD1 1 182 B B +ATOM 6781 C CD2 . PHE B 1 182 ? -37.038 41.313 38.502 1.0 94.09 ? ? ? ? ? ? 299 PHE B CD2 1 182 B B +ATOM 6782 C CE1 . PHE B 1 182 ? -34.888 43.060 38.330 1.0 86.12 ? ? ? ? ? ? 299 PHE B CE1 1 182 B B +ATOM 6783 C CE2 . PHE B 1 182 ? -36.966 42.415 39.354 1.0 93.02 ? ? ? ? ? ? 299 PHE B CE2 1 182 B B +ATOM 6784 C CZ . PHE B 1 182 ? -35.890 43.290 39.267 1.0 91.75 ? ? ? ? ? ? 299 PHE B CZ 1 182 B B +ATOM 6785 N N . ALA B 1 183 ? -37.733 37.630 38.181 1.0 74.86 ? ? ? ? ? ? 300 ALA B N 1 183 B B +ATOM 6786 C CA . ALA B 1 183 ? -38.706 37.270 39.209 1.0 72.38 ? ? ? ? ? ? 300 ALA B CA 1 183 B B +ATOM 6787 C C . ALA B 1 183 ? -38.104 36.367 40.287 1.0 73.94 ? ? ? ? ? ? 300 ALA B C 1 183 B B +ATOM 6788 O O . ALA B 1 183 ? -38.161 36.694 41.474 1.0 79.9 ? ? ? ? ? ? 300 ALA B O 1 183 B B +ATOM 6789 C CB . ALA B 1 183 ? -39.915 36.592 38.573 1.0 64.49 ? ? ? ? ? ? 300 ALA B CB 1 183 B B +ATOM 6790 N N . GLN B 1 184 ? -37.535 35.234 39.880 1.0 60.82 ? ? ? ? ? ? 301 GLN B N 1 184 B B +ATOM 6791 C CA . GLN B 1 184 ? -36.927 34.308 40.834 1.0 59.12 ? ? ? ? ? ? 301 GLN B CA 1 184 B B +ATOM 6792 C C . GLN B 1 184 ? -35.908 35.070 41.668 1.0 52.85 ? ? ? ? ? ? 301 GLN B C 1 184 B B +ATOM 6793 O O . GLN B 1 184 ? -35.829 34.906 42.886 1.0 42.05 ? ? ? ? ? ? 301 GLN B O 1 184 B B +ATOM 6794 C CB . GLN B 1 184 ? -36.232 33.165 40.096 1.0 75.11 ? ? ? ? ? ? 301 GLN B CB 1 184 B B +ATOM 6795 C CG . GLN B 1 184 ? -37.136 32.383 39.169 1.0 97.35 ? ? ? ? ? ? 301 GLN B CG 1 184 B B +ATOM 6796 C CD . GLN B 1 184 ? -36.359 31.421 38.296 1.0 100.0 ? ? ? ? ? ? 301 GLN B CD 1 184 B B +ATOM 6797 O OE1 . GLN B 1 184 ? -35.207 31.680 37.945 1.0 100.0 ? ? ? ? ? ? 301 GLN B OE1 1 184 B B +ATOM 6798 N NE2 . GLN B 1 184 ? -36.982 30.303 37.943 1.0 97.11 ? ? ? ? ? ? 301 GLN B NE2 1 184 B B +ATOM 6799 N N . PHE B 1 185 ? -35.130 35.906 40.988 1.0 49.6 ? ? ? ? ? ? 302 PHE B N 1 185 B B +ATOM 6800 C CA . PHE B 1 185 ? -34.107 36.725 41.629 1.0 54.69 ? ? ? ? ? ? 302 PHE B CA 1 185 B B +ATOM 6801 C C . PHE B 1 185 ? -34.740 37.556 42.748 1.0 59.93 ? ? ? ? ? ? 302 PHE B C 1 185 B B +ATOM 6802 O O . PHE B 1 185 ? -34.316 37.492 43.905 1.0 61.04 ? ? ? ? ? ? 302 PHE B O 1 185 B B +ATOM 6803 C CB . PHE B 1 185 ? -33.449 37.631 40.574 1.0 46.54 ? ? ? ? ? ? 302 PHE B CB 1 185 B B +ATOM 6804 C CG . PHE B 1 185 ? -32.724 38.822 41.142 1.0 61.15 ? ? ? ? ? ? 302 PHE B CG 1 185 B B +ATOM 6805 C CD1 . PHE B 1 185 ? -31.975 38.721 42.311 1.0 59.47 ? ? ? ? ? ? 302 PHE B CD1 1 185 B B +ATOM 6806 C CD2 . PHE B 1 185 ? -32.783 40.050 40.492 1.0 66.45 ? ? ? ? ? ? 302 PHE B CD2 1 185 B B +ATOM 6807 C CE1 . PHE B 1 185 ? -31.301 39.826 42.818 1.0 59.27 ? ? ? ? ? ? 302 PHE B CE1 1 185 B B +ATOM 6808 C CE2 . PHE B 1 185 ? -32.112 41.156 40.992 1.0 72.43 ? ? ? ? ? ? 302 PHE B CE2 1 185 B B +ATOM 6809 C CZ . PHE B 1 185 ? -31.369 41.044 42.157 1.0 66.68 ? ? ? ? ? ? 302 PHE B CZ 1 185 B B +ATOM 6810 N N . SER B 1 186 ? -35.757 38.335 42.394 1.0 60.89 ? ? ? ? ? ? 303 SER B N 1 186 B B +ATOM 6811 C CA . SER B 1 186 ? -36.458 39.170 43.359 1.0 54.2 ? ? ? ? ? ? 303 SER B CA 1 186 B B +ATOM 6812 C C . SER B 1 186 ? -36.943 38.297 44.511 1.0 47.38 ? ? ? ? ? ? 303 SER B C 1 186 B B +ATOM 6813 O O . SER B 1 186 ? -36.668 38.571 45.678 1.0 54.63 ? ? ? ? ? ? 303 SER B O 1 186 B B +ATOM 6814 C CB . SER B 1 186 ? -37.660 39.856 42.692 1.0 45.16 ? ? ? ? ? ? 303 SER B CB 1 186 B B +ATOM 6815 O OG . SER B 1 186 ? -37.253 40.686 41.618 1.0 39.85 ? ? ? ? ? ? 303 SER B OG 1 186 B B +ATOM 6816 N N . GLN B 1 187 ? -37.664 37.237 44.167 1.0 22.0 ? ? ? ? ? ? 304 GLN B N 1 187 B B +ATOM 6817 C CA . GLN B 1 187 ? -38.206 36.320 45.157 1.0 25.19 ? ? ? ? ? ? 304 GLN B CA 1 187 B B +ATOM 6818 C C . GLN B 1 187 ? -37.154 35.833 46.142 1.0 38.37 ? ? ? ? ? ? 304 GLN B C 1 187 B B +ATOM 6819 O O . GLN B 1 187 ? -37.442 35.651 47.326 1.0 53.2 ? ? ? ? ? ? 304 GLN B O 1 187 B B +ATOM 6820 C CB . GLN B 1 187 ? -38.841 35.120 44.466 1.0 7.89 ? ? ? ? ? ? 304 GLN B CB 1 187 B B +ATOM 6821 C CG . GLN B 1 187 ? -39.624 34.225 45.398 1.0 5.59 ? ? ? ? ? ? 304 GLN B CG 1 187 B B +ATOM 6822 C CD . GLN B 1 187 ? -40.481 33.238 44.646 1.0 17.21 ? ? ? ? ? ? 304 GLN B CD 1 187 B B +ATOM 6823 O OE1 . GLN B 1 187 ? -40.334 33.073 43.437 1.0 27.54 ? ? ? ? ? ? 304 GLN B OE1 1 187 B B +ATOM 6824 N NE2 . GLN B 1 187 ? -41.388 32.576 45.354 1.0 18.31 ? ? ? ? ? ? 304 GLN B NE2 1 187 B B +ATOM 6825 N N . GLU B 1 188 ? -35.940 35.604 45.649 1.0 43.72 ? ? ? ? ? ? 305 GLU B N 1 188 B B +ATOM 6826 C CA . GLU B 1 188 ? -34.851 35.143 46.503 1.0 61.99 ? ? ? ? ? ? 305 GLU B CA 1 188 B B +ATOM 6827 C C . GLU B 1 188 ? -34.678 36.116 47.664 1.0 69.94 ? ? ? ? ? ? 305 GLU B C 1 188 B B +ATOM 6828 O O . GLU B 1 188 ? -34.644 35.712 48.828 1.0 75.09 ? ? ? ? ? ? 305 GLU B O 1 188 B B +ATOM 6829 C CB . GLU B 1 188 ? -33.550 35.059 45.704 1.0 71.67 ? ? ? ? ? ? 305 GLU B CB 1 188 B B +ATOM 6830 C CG . GLU B 1 188 ? -33.516 33.930 44.690 1.0 74.16 ? ? ? ? ? ? 305 GLU B CG 1 188 B B +ATOM 6831 C CD . GLU B 1 188 ? -33.855 32.582 45.298 1.0 80.11 ? ? ? ? ? ? 305 GLU B CD 1 188 B B +ATOM 6832 O OE1 . GLU B 1 188 ? -34.687 31.861 44.711 1.0 94.32 ? ? ? ? ? ? 305 GLU B OE1 1 188 B B +ATOM 6833 O OE2 . GLU B 1 188 ? -33.293 32.243 46.359 1.0 74.94 ? ? ? ? ? ? 305 GLU B OE2 1 188 B B +ATOM 6834 N N . ILE B 1 189 ? -34.565 37.400 47.338 1.0 56.48 ? ? ? ? ? ? 306 ILE B N 1 189 B B +ATOM 6835 C CA . ILE B 1 189 ? -34.408 38.434 48.352 1.0 52.28 ? ? ? ? ? ? 306 ILE B CA 1 189 B B +ATOM 6836 C C . ILE B 1 189 ? -35.565 38.370 49.345 1.0 57.18 ? ? ? ? ? ? 306 ILE B C 1 189 B B +ATOM 6837 O O . ILE B 1 189 ? -35.371 38.503 50.556 1.0 64.85 ? ? ? ? ? ? 306 ILE B O 1 189 B B +ATOM 6838 C CB . ILE B 1 189 ? -34.389 39.839 47.719 1.0 55.36 ? ? ? ? ? ? 306 ILE B CB 1 189 B B +ATOM 6839 C CG1 . ILE B 1 189 ? -33.547 39.826 46.439 1.0 60.79 ? ? ? ? ? ? 306 ILE B CG1 1 189 B B +ATOM 6840 C CG2 . ILE B 1 189 ? -33.842 40.848 48.716 1.0 49.22 ? ? ? ? ? ? 306 ILE B CG2 1 189 B B +ATOM 6841 C CD1 . ILE B 1 189 ? -33.549 41.138 45.685 1.0 62.48 ? ? ? ? ? ? 306 ILE B CD1 1 189 B B +ATOM 6842 N N . GLY B 1 190 ? -36.771 38.164 48.821 1.0 48.52 ? ? ? ? ? ? 307 GLY B N 1 190 B B +ATOM 6843 C CA . GLY B 1 190 ? -37.943 38.087 49.671 1.0 57.63 ? ? ? ? ? ? 307 GLY B CA 1 190 B B +ATOM 6844 C C . GLY B 1 190 ? -37.827 36.946 50.656 1.0 60.82 ? ? ? ? ? ? 307 GLY B C 1 190 B B +ATOM 6845 O O . GLY B 1 190 ? -38.082 37.109 51.850 1.0 57.71 ? ? ? ? ? ? 307 GLY B O 1 190 B B +ATOM 6846 N N . LEU B 1 191 ? -37.423 35.787 50.145 1.0 64.07 ? ? ? ? ? ? 308 LEU B N 1 191 B B +ATOM 6847 C CA . LEU B 1 191 ? -37.262 34.596 50.967 1.0 55.82 ? ? ? ? ? ? 308 LEU B CA 1 191 B B +ATOM 6848 C C . LEU B 1 191 ? -36.110 34.797 51.946 1.0 53.47 ? ? ? ? ? ? 308 LEU B C 1 191 B B +ATOM 6849 O O . LEU B 1 191 ? -36.105 34.235 53.041 1.0 46.25 ? ? ? ? ? ? 308 LEU B O 1 191 B B +ATOM 6850 C CB . LEU B 1 191 ? -37.010 33.387 50.068 1.0 42.02 ? ? ? ? ? ? 308 LEU B CB 1 191 B B +ATOM 6851 C CG . LEU B 1 191 ? -38.229 33.049 49.205 1.0 47.91 ? ? ? ? ? ? 308 LEU B CG 1 191 B B +ATOM 6852 C CD1 . LEU B 1 191 ? -37.787 32.678 47.808 1.0 40.23 ? ? ? ? ? ? 308 LEU B CD1 1 191 B B +ATOM 6853 C CD2 . LEU B 1 191 ? -39.014 31.919 49.854 1.0 45.13 ? ? ? ? ? ? 308 LEU B CD2 1 191 B B +ATOM 6854 N N . ALA B 1 192 ? -35.137 35.607 51.539 1.0 49.57 ? ? ? ? ? ? 309 ALA B N 1 192 B B +ATOM 6855 C CA . ALA B 1 192 ? -33.983 35.906 52.378 1.0 42.49 ? ? ? ? ? ? 309 ALA B CA 1 192 B B +ATOM 6856 C C . ALA B 1 192 ? -34.414 36.753 53.572 1.0 41.22 ? ? ? ? ? ? 309 ALA B C 1 192 B B +ATOM 6857 O O . ALA B 1 192 ? -34.182 36.395 54.727 1.0 46.77 ? ? ? ? ? ? 309 ALA B O 1 192 B B +ATOM 6858 C CB . ALA B 1 192 ? -32.934 36.651 51.568 1.0 31.59 ? ? ? ? ? ? 309 ALA B CB 1 192 B B +ATOM 6859 N N . SER B 1 193 ? -35.054 37.876 53.272 1.0 33.82 ? ? ? ? ? ? 310 SER B N 1 193 B B +ATOM 6860 C CA . SER B 1 193 ? -35.522 38.811 54.283 1.0 40.75 ? ? ? ? ? ? 310 SER B CA 1 193 B B +ATOM 6861 C C . SER B 1 193 ? -36.486 38.221 55.311 1.0 39.25 ? ? ? ? ? ? 310 SER B C 1 193 B B +ATOM 6862 O O . SER B 1 193 ? -36.659 38.782 56.393 1.0 51.49 ? ? ? ? ? ? 310 SER B O 1 193 B B +ATOM 6863 C CB . SER B 1 193 ? -36.184 40.011 53.597 1.0 60.17 ? ? ? ? ? ? 310 SER B CB 1 193 B B +ATOM 6864 O OG . SER B 1 193 ? -37.361 39.622 52.908 1.0 62.03 ? ? ? ? ? ? 310 SER B OG 1 193 B B +ATOM 6865 N N . LEU B 1 194 ? -37.114 37.099 54.980 1.0 12.02 ? ? ? ? ? ? 311 LEU B N 1 194 B B +ATOM 6866 C CA . LEU B 1 194 ? -38.071 36.489 55.899 1.0 47.55 ? ? ? ? ? ? 311 LEU B CA 1 194 B B +ATOM 6867 C C . LEU B 1 194 ? -37.464 36.123 57.256 1.0 48.33 ? ? ? ? ? ? 311 LEU B C 1 194 B B +ATOM 6868 O O . LEU B 1 194 ? -36.754 35.126 57.386 1.0 59.22 ? ? ? ? ? ? 311 LEU B O 1 194 B B +ATOM 6869 C CB . LEU B 1 194 ? -38.706 35.251 55.259 1.0 52.66 ? ? ? ? ? ? 311 LEU B CB 1 194 B B +ATOM 6870 C CG . LEU B 1 194 ? -39.624 35.509 54.059 1.0 42.32 ? ? ? ? ? ? 311 LEU B CG 1 194 B B +ATOM 6871 C CD1 . LEU B 1 194 ? -40.166 34.194 53.529 1.0 54.87 ? ? ? ? ? ? 311 LEU B CD1 1 194 B B +ATOM 6872 C CD2 . LEU B 1 194 ? -40.766 36.413 54.471 1.0 61.47 ? ? ? ? ? ? 311 LEU B CD2 1 194 B B +ATOM 6873 N N . GLY B 1 195 ? -37.755 36.942 58.264 1.0 48.49 ? ? ? ? ? ? 312 GLY B N 1 195 B B +ATOM 6874 C CA . GLY B 1 195 ? -37.242 36.689 59.598 1.0 55.95 ? ? ? ? ? ? 312 GLY B CA 1 195 B B +ATOM 6875 C C . GLY B 1 195 ? -35.790 37.088 59.784 1.0 58.83 ? ? ? ? ? ? 312 GLY B C 1 195 B B +ATOM 6876 O O . GLY B 1 195 ? -35.192 36.781 60.814 1.0 54.63 ? ? ? ? ? ? 312 GLY B O 1 195 B B +ATOM 6877 N N . ALA B 1 196 ? -35.221 37.772 58.796 1.0 59.26 ? ? ? ? ? ? 313 ALA B N 1 196 B B +ATOM 6878 C CA . ALA B 1 196 ? -33.824 38.204 58.866 1.0 79.51 ? ? ? ? ? ? 313 ALA B CA 1 196 B B +ATOM 6879 C C . ALA B 1 196 ? -33.637 39.361 59.848 1.0 91.68 ? ? ? ? ? ? 313 ALA B C 1 196 B B +ATOM 6880 O O . ALA B 1 196 ? -34.514 40.217 59.993 1.0 100.0 ? ? ? ? ? ? 313 ALA B O 1 196 B B +ATOM 6881 C CB . ALA B 1 196 ? -33.335 38.612 57.484 1.0 78.37 ? ? ? ? ? ? 313 ALA B CB 1 196 B B +ATOM 6882 N N . PRO B 1 197 ? -32.478 39.410 60.528 1.0 87.52 ? ? ? ? ? ? 314 PRO B N 1 197 B B +ATOM 6883 C CA . PRO B 1 197 ? -32.241 40.495 61.487 1.0 80.1 ? ? ? ? ? ? 314 PRO B CA 1 197 B B +ATOM 6884 C C . PRO B 1 197 ? -32.055 41.836 60.783 1.0 78.7 ? ? ? ? ? ? 314 PRO B C 1 197 B B +ATOM 6885 O O . PRO B 1 197 ? -31.518 41.900 59.674 1.0 56.63 ? ? ? ? ? ? 314 PRO B O 1 197 B B +ATOM 6886 C CB . PRO B 1 197 ? -30.994 40.046 62.248 1.0 63.86 ? ? ? ? ? ? 314 PRO B CB 1 197 B B +ATOM 6887 C CG . PRO B 1 197 ? -30.290 39.128 61.313 1.0 49.98 ? ? ? ? ? ? 314 PRO B CG 1 197 B B +ATOM 6888 C CD . PRO B 1 197 ? -31.330 38.491 60.428 1.0 71.57 ? ? ? ? ? ? 314 PRO B CD 1 197 B B +ATOM 6889 N N . ASP B 1 198 ? -32.506 42.897 61.446 1.0 73.05 ? ? ? ? ? ? 315 ASP B N 1 198 B B +ATOM 6890 C CA . ASP B 1 198 ? -32.432 44.253 60.913 1.0 73.98 ? ? ? ? ? ? 315 ASP B CA 1 198 B B +ATOM 6891 C C . ASP B 1 198 ? -31.186 44.571 60.088 1.0 78.88 ? ? ? ? ? ? 315 ASP B C 1 198 B B +ATOM 6892 O O . ASP B 1 198 ? -31.294 45.020 58.945 1.0 76.97 ? ? ? ? ? ? 315 ASP B O 1 198 B B +ATOM 6893 C CB . ASP B 1 198 ? -32.566 45.261 62.056 1.0 71.53 ? ? ? ? ? ? 315 ASP B CB 1 198 B B +ATOM 6894 C CG . ASP B 1 198 ? -33.834 45.060 62.859 1.0 79.25 ? ? ? ? ? ? 315 ASP B CG 1 198 B B +ATOM 6895 O OD1 . ASP B 1 198 ? -33.845 44.180 63.743 1.0 75.19 ? ? ? ? ? ? 315 ASP B OD1 1 198 B B +ATOM 6896 O OD2 . ASP B 1 198 ? -34.820 45.782 62.604 1.0 85.56 ? ? ? ? ? ? 315 ASP B OD2 1 198 B B +ATOM 6897 N N . GLU B 1 199 ? -30.007 44.347 60.661 1.0 78.88 ? ? ? ? ? ? 316 GLU B N 1 199 B B +ATOM 6898 C CA . GLU B 1 199 ? -28.755 44.632 59.960 1.0 79.73 ? ? ? ? ? ? 316 GLU B CA 1 199 B B +ATOM 6899 C C . GLU B 1 199 ? -28.744 44.075 58.549 1.0 72.76 ? ? ? ? ? ? 316 GLU B C 1 199 B B +ATOM 6900 O O . GLU B 1 199 ? -28.324 44.751 57.613 1.0 65.25 ? ? ? ? ? ? 316 GLU B O 1 199 B B +ATOM 6901 C CB . GLU B 1 199 ? -27.564 44.053 60.721 1.0 79.8 ? ? ? ? ? ? 316 GLU B CB 1 199 B B +ATOM 6902 C CG . GLU B 1 199 ? -27.721 42.598 61.086 1.0 99.07 ? ? ? ? ? ? 316 GLU B CG 1 199 B B +ATOM 6903 C CD . GLU B 1 199 ? -28.252 42.420 62.490 1.0 100.0 ? ? ? ? ? ? 316 GLU B CD 1 199 B B +ATOM 6904 O OE1 . GLU B 1 199 ? -27.984 41.359 63.094 1.0 100.0 ? ? ? ? ? ? 316 GLU B OE1 1 199 B B +ATOM 6905 O OE2 . GLU B 1 199 ? -28.935 43.344 62.986 1.0 100.0 ? ? ? ? ? ? 316 GLU B OE2 1 199 B B +ATOM 6906 N N . TYR B 1 200 ? -29.196 42.835 58.401 1.0 72.58 ? ? ? ? ? ? 317 TYR B N 1 200 B B +ATOM 6907 C CA . TYR B 1 200 ? -29.220 42.195 57.096 1.0 79.65 ? ? ? ? ? ? 317 TYR B CA 1 200 B B +ATOM 6908 C C . TYR B 1 200 ? -30.387 42.677 56.255 1.0 80.27 ? ? ? ? ? ? 317 TYR B C 1 200 B B +ATOM 6909 O O . TYR B 1 200 ? -30.301 42.720 55.029 1.0 69.59 ? ? ? ? ? ? 317 TYR B O 1 200 B B +ATOM 6910 C CB . TYR B 1 200 ? -29.274 40.678 57.258 1.0 93.84 ? ? ? ? ? ? 317 TYR B CB 1 200 B B +ATOM 6911 C CG . TYR B 1 200 ? -27.928 40.089 57.577 1.0 96.59 ? ? ? ? ? ? 317 TYR B CG 1 200 B B +ATOM 6912 C CD1 . TYR B 1 200 ? -27.534 39.895 58.899 1.0 96.42 ? ? ? ? ? ? 317 TYR B CD1 1 200 B B +ATOM 6913 C CD2 . TYR B 1 200 ? -27.025 39.774 56.562 1.0 84.4 ? ? ? ? ? ? 317 TYR B CD2 1 200 B B +ATOM 6914 C CE1 . TYR B 1 200 ? -26.271 39.399 59.206 1.0 99.21 ? ? ? ? ? ? 317 TYR B CE1 1 200 B B +ATOM 6915 C CE2 . TYR B 1 200 ? -25.759 39.277 56.854 1.0 95.13 ? ? ? ? ? ? 317 TYR B CE2 1 200 B B +ATOM 6916 C CZ . TYR B 1 200 ? -25.387 39.095 58.178 1.0 100.0 ? ? ? ? ? ? 317 TYR B CZ 1 200 B B +ATOM 6917 O OH . TYR B 1 200 ? -24.133 38.603 58.467 1.0 100.0 ? ? ? ? ? ? 317 TYR B OH 1 200 B B +ATOM 6918 N N . ILE B 1 201 ? -31.484 43.022 56.918 1.0 81.29 ? ? ? ? ? ? 318 ILE B N 1 201 B B +ATOM 6919 C CA . ILE B 1 201 ? -32.655 43.525 56.216 1.0 79.03 ? ? ? ? ? ? 318 ILE B CA 1 201 B B +ATOM 6920 C C . ILE B 1 201 ? -32.227 44.796 55.486 1.0 85.15 ? ? ? ? ? ? 318 ILE B C 1 201 B B +ATOM 6921 O O . ILE B 1 201 ? -32.490 44.970 54.296 1.0 77.47 ? ? ? ? ? ? 318 ILE B O 1 201 B B +ATOM 6922 C CB . ILE B 1 201 ? -33.788 43.877 57.202 1.0 74.45 ? ? ? ? ? ? 318 ILE B CB 1 201 B B +ATOM 6923 C CG1 . ILE B 1 201 ? -34.489 42.602 57.670 1.0 56.83 ? ? ? ? ? ? 318 ILE B CG1 1 201 B B +ATOM 6924 C CG2 . ILE B 1 201 ? -34.782 44.824 56.541 1.0 78.83 ? ? ? ? ? ? 318 ILE B CG2 1 201 B B +ATOM 6925 C CD1 . ILE B 1 201 ? -35.292 41.913 56.589 1.0 79.43 ? ? ? ? ? ? 318 ILE B CD1 1 201 B B +ATOM 6926 N N . GLU B 1 202 ? -31.560 45.678 56.224 1.0 88.63 ? ? ? ? ? ? 319 GLU B N 1 202 B B +ATOM 6927 C CA . GLU B 1 202 ? -31.074 46.941 55.685 1.0 92.74 ? ? ? ? ? ? 319 GLU B CA 1 202 B B +ATOM 6928 C C . GLU B 1 202 ? -30.050 46.689 54.582 1.0 86.1 ? ? ? ? ? ? 319 GLU B C 1 202 B B +ATOM 6929 O O . GLU B 1 202 ? -30.008 47.406 53.581 1.0 76.49 ? ? ? ? ? ? 319 GLU B O 1 202 B B +ATOM 6930 C CB . GLU B 1 202 ? -30.447 47.773 56.806 1.0 96.66 ? ? ? ? ? ? 319 GLU B CB 1 202 B B +ATOM 6931 C CG . GLU B 1 202 ? -29.969 49.142 56.372 1.0 100.0 ? ? ? ? ? ? 319 GLU B CG 1 202 B B +ATOM 6932 C CD . GLU B 1 202 ? -28.500 49.363 56.677 1.0 100.0 ? ? ? ? ? ? 319 GLU B CD 1 202 B B +ATOM 6933 O OE1 . GLU B 1 202 ? -28.197 50.127 57.619 1.0 100.0 ? ? ? ? ? ? 319 GLU B OE1 1 202 B B +ATOM 6934 O OE2 . GLU B 1 202 ? -27.650 48.770 55.975 1.0 99.05 ? ? ? ? ? ? 319 GLU B OE2 1 202 B B +ATOM 6935 N N . LYS B 1 203 ? -29.224 45.666 54.781 1.0 87.1 ? ? ? ? ? ? 320 LYS B N 1 203 B B +ATOM 6936 C CA . LYS B 1 203 ? -28.202 45.292 53.809 1.0 92.68 ? ? ? ? ? ? 320 LYS B CA 1 203 B B +ATOM 6937 C C . LYS B 1 203 ? -28.864 44.866 52.500 1.0 88.4 ? ? ? ? ? ? 320 LYS B C 1 203 B B +ATOM 6938 O O . LYS B 1 203 ? -28.428 45.258 51.418 1.0 70.36 ? ? ? ? ? ? 320 LYS B O 1 203 B B +ATOM 6939 C CB . LYS B 1 203 ? -27.354 44.138 54.348 1.0 100.0 ? ? ? ? ? ? 320 LYS B CB 1 203 B B +ATOM 6940 C CG . LYS B 1 203 ? -26.291 44.550 55.355 1.0 100.0 ? ? ? ? ? ? 320 LYS B CG 1 203 B B +ATOM 6941 C CD . LYS B 1 203 ? -25.489 43.340 55.815 1.0 100.0 ? ? ? ? ? ? 320 LYS B CD 1 203 B B +ATOM 6942 C CE . LYS B 1 203 ? -24.377 43.729 56.778 1.0 96.33 ? ? ? ? ? ? 320 LYS B CE 1 203 B B +ATOM 6943 N NZ . LYS B 1 203 ? -23.638 42.536 57.283 1.0 59.54 ? ? ? ? ? ? 320 LYS B NZ 1 203 B B +ATOM 6944 N N . LEU B 1 204 ? -29.919 44.061 52.606 1.0 85.57 ? ? ? ? ? ? 321 LEU B N 1 204 B B +ATOM 6945 C CA . LEU B 1 204 ? -30.646 43.590 51.430 1.0 79.11 ? ? ? ? ? ? 321 LEU B CA 1 204 B B +ATOM 6946 C C . LEU B 1 204 ? -31.269 44.784 50.711 1.0 77.76 ? ? ? ? ? ? 321 LEU B C 1 204 B B +ATOM 6947 O O . LEU B 1 204 ? -31.179 44.896 49.487 1.0 54.13 ? ? ? ? ? ? 321 LEU B O 1 204 B B +ATOM 6948 C CB . LEU B 1 204 ? -31.744 42.602 51.836 1.0 75.56 ? ? ? ? ? ? 321 LEU B CB 1 204 B B +ATOM 6949 C CG . LEU B 1 204 ? -31.280 41.207 52.257 1.0 69.23 ? ? ? ? ? ? 321 LEU B CG 1 204 B B +ATOM 6950 C CD1 . LEU B 1 204 ? -32.328 40.581 53.162 1.0 72.14 ? ? ? ? ? ? 321 LEU B CD1 1 204 B B +ATOM 6951 C CD2 . LEU B 1 204 ? -31.037 40.348 51.026 1.0 32.48 ? ? ? ? ? ? 321 LEU B CD2 1 204 B B +ATOM 6952 N N . ALA B 1 205 ? -31.907 45.668 51.477 1.0 72.88 ? ? ? ? ? ? 322 ALA B N 1 205 B B +ATOM 6953 C CA . ALA B 1 205 ? -32.525 46.859 50.905 1.0 68.29 ? ? ? ? ? ? 322 ALA B CA 1 205 B B +ATOM 6954 C C . ALA B 1 205 ? -31.470 47.572 50.075 1.0 70.79 ? ? ? ? ? ? 322 ALA B C 1 205 B B +ATOM 6955 O O . ALA B 1 205 ? -31.694 47.902 48.912 1.0 76.89 ? ? ? ? ? ? 322 ALA B O 1 205 B B +ATOM 6956 C CB . ALA B 1 205 ? -33.030 47.779 52.009 1.0 56.42 ? ? ? ? ? ? 322 ALA B CB 1 205 B B +ATOM 6957 N N . THR B 1 206 ? -30.307 47.791 50.681 1.0 76.29 ? ? ? ? ? ? 323 THR B N 1 206 B B +ATOM 6958 C CA . THR B 1 206 ? -29.206 48.460 50.002 1.0 94.13 ? ? ? ? ? ? 323 THR B CA 1 206 B B +ATOM 6959 C C . THR B 1 206 ? -28.848 47.734 48.702 1.0 96.35 ? ? ? ? ? ? 323 THR B C 1 206 B B +ATOM 6960 O O . THR B 1 206 ? -28.527 48.369 47.692 1.0 98.99 ? ? ? ? ? ? 323 THR B O 1 206 B B +ATOM 6961 C CB . THR B 1 206 ? -27.961 48.528 50.907 1.0 100.0 ? ? ? ? ? ? 323 THR B CB 1 206 B B +ATOM 6962 O OG1 . THR B 1 206 ? -28.347 48.948 52.224 1.0 100.0 ? ? ? ? ? ? 323 THR B OG1 1 206 B B +ATOM 6963 C CG2 . THR B 1 206 ? -26.949 49.513 50.342 1.0 100.0 ? ? ? ? ? ? 323 THR B CG2 1 206 B B +ATOM 6964 N N . ILE B 1 207 ? -28.892 46.405 48.734 1.0 91.07 ? ? ? ? ? ? 324 ILE B N 1 207 B B +ATOM 6965 C CA . ILE B 1 207 ? -28.592 45.611 47.547 1.0 86.66 ? ? ? ? ? ? 324 ILE B CA 1 207 B B +ATOM 6966 C C . ILE B 1 207 ? -29.711 45.849 46.544 1.0 84.53 ? ? ? ? ? ? 324 ILE B C 1 207 B B +ATOM 6967 O O . ILE B 1 207 ? -29.464 46.127 45.374 1.0 75.58 ? ? ? ? ? ? 324 ILE B O 1 207 B B +ATOM 6968 C CB . ILE B 1 207 ? -28.541 44.105 47.871 1.0 88.67 ? ? ? ? ? ? 324 ILE B CB 1 207 B B +ATOM 6969 C CG1 . ILE B 1 207 ? -27.476 43.832 48.935 1.0 74.72 ? ? ? ? ? ? 324 ILE B CG1 1 207 B B +ATOM 6970 C CG2 . ILE B 1 207 ? -28.251 43.310 46.602 1.0 81.43 ? ? ? ? ? ? 324 ILE B CG2 1 207 B B +ATOM 6971 C CD1 . ILE B 1 207 ? -26.072 44.207 48.507 1.0 59.98 ? ? ? ? ? ? 324 ILE B CD1 1 207 B B +ATOM 6972 N N . TYR B 1 208 ? -30.943 45.734 47.030 1.0 84.3 ? ? ? ? ? ? 325 TYR B N 1 208 B B +ATOM 6973 C CA . TYR B 1 208 ? -32.140 45.944 46.221 1.0 87.69 ? ? ? ? ? ? 325 TYR B CA 1 208 B B +ATOM 6974 C C . TYR B 1 208 ? -32.006 47.251 45.441 1.0 84.03 ? ? ? ? ? ? 325 TYR B C 1 208 B B +ATOM 6975 O O . TYR B 1 208 ? -32.486 47.377 44.314 1.0 63.33 ? ? ? ? ? ? 325 TYR B O 1 208 B B +ATOM 6976 C CB . TYR B 1 208 ? -33.362 45.997 47.147 1.0 94.13 ? ? ? ? ? ? 325 TYR B CB 1 208 B B +ATOM 6977 C CG . TYR B 1 208 ? -34.686 46.270 46.468 1.0 100.0 ? ? ? ? ? ? 325 TYR B CG 1 208 B B +ATOM 6978 C CD1 . TYR B 1 208 ? -35.173 47.574 46.342 1.0 100.0 ? ? ? ? ? ? 325 TYR B CD1 1 208 B B +ATOM 6979 C CD2 . TYR B 1 208 ? -35.480 45.220 46.001 1.0 100.0 ? ? ? ? ? ? 325 TYR B CD2 1 208 B B +ATOM 6980 C CE1 . TYR B 1 208 ? -36.422 47.826 45.773 1.0 100.0 ? ? ? ? ? ? 325 TYR B CE1 1 208 B B +ATOM 6981 C CE2 . TYR B 1 208 ? -36.729 45.459 45.431 1.0 100.0 ? ? ? ? ? ? 325 TYR B CE2 1 208 B B +ATOM 6982 C CZ . TYR B 1 208 ? -37.194 46.763 45.322 1.0 100.0 ? ? ? ? ? ? 325 TYR B CZ 1 208 B B +ATOM 6983 O OH . TYR B 1 208 ? -38.435 46.999 44.777 1.0 100.0 ? ? ? ? ? ? 325 TYR B OH 1 208 B B +ATOM 6984 N N . TRP B 1 209 ? -31.344 48.221 46.060 1.0 84.11 ? ? ? ? ? ? 326 TRP B N 1 209 B B +ATOM 6985 C CA . TRP B 1 209 ? -31.126 49.519 45.449 1.0 86.01 ? ? ? ? ? ? 326 TRP B CA 1 209 B B +ATOM 6986 C C . TRP B 1 209 ? -30.174 49.407 44.268 1.0 87.9 ? ? ? ? ? ? 326 TRP B C 1 209 B B +ATOM 6987 O O . TRP B 1 209 ? -30.566 49.617 43.125 1.0 85.81 ? ? ? ? ? ? 326 TRP B O 1 209 B B +ATOM 6988 C CB . TRP B 1 209 ? -30.545 50.485 46.486 1.0 85.17 ? ? ? ? ? ? 326 TRP B CB 1 209 B B +ATOM 6989 C CG . TRP B 1 209 ? -30.574 51.927 46.068 1.0 99.7 ? ? ? ? ? ? 326 TRP B CG 1 209 B B +ATOM 6990 C CD1 . TRP B 1 209 ? -29.592 52.613 45.409 1.0 100.0 ? ? ? ? ? ? 326 TRP B CD1 1 209 B B +ATOM 6991 C CD2 . TRP B 1 209 ? -31.624 52.874 46.316 1.0 100.0 ? ? ? ? ? ? 326 TRP B CD2 1 209 B B +ATOM 6992 N NE1 . TRP B 1 209 ? -29.961 53.927 45.237 1.0 100.0 ? ? ? ? ? ? 326 TRP B NE1 1 209 B B +ATOM 6993 C CE2 . TRP B 1 209 ? -31.202 54.114 45.786 1.0 100.0 ? ? ? ? ? ? 326 TRP B CE2 1 209 B B +ATOM 6994 C CE3 . TRP B 1 209 ? -32.876 52.793 46.940 1.0 100.0 ? ? ? ? ? ? 326 TRP B CE3 1 209 B B +ATOM 6995 C CZ2 . TRP B 1 209 ? -31.990 55.266 45.856 1.0 98.96 ? ? ? ? ? ? 326 TRP B CZ2 1 209 B B +ATOM 6996 C CZ3 . TRP B 1 209 ? -33.659 53.942 47.011 1.0 100.0 ? ? ? ? ? ? 326 TRP B CZ3 1 209 B B +ATOM 6997 C CH2 . TRP B 1 209 ? -33.211 55.162 46.471 1.0 100.0 ? ? ? ? ? ? 326 TRP B CH2 1 209 B B +ATOM 6998 N N . PHE B 1 210 ? -28.919 49.067 44.555 1.0 88.82 ? ? ? ? ? ? 327 PHE B N 1 210 B B +ATOM 6999 C CA . PHE B 1 210 ? -27.885 48.942 43.525 1.0 93.56 ? ? ? ? ? ? 327 PHE B CA 1 210 B B +ATOM 7000 C C . PHE B 1 210 ? -28.148 47.816 42.534 1.0 89.91 ? ? ? ? ? ? 327 PHE B C 1 210 B B +ATOM 7001 O O . PHE B 1 210 ? -27.256 47.405 41.788 1.0 89.17 ? ? ? ? ? ? 327 PHE B O 1 210 B B +ATOM 7002 C CB . PHE B 1 210 ? -26.519 48.742 44.182 1.0 96.8 ? ? ? ? ? ? 327 PHE B CB 1 210 B B +ATOM 7003 C CG . PHE B 1 210 ? -26.029 49.950 44.931 1.0 100.0 ? ? ? ? ? ? 327 PHE B CG 1 210 B B +ATOM 7004 C CD1 . PHE B 1 210 ? -25.649 51.105 44.249 1.0 100.0 ? ? ? ? ? ? 327 PHE B CD1 1 210 B B +ATOM 7005 C CD2 . PHE B 1 210 ? -25.949 49.937 46.322 1.0 100.0 ? ? ? ? ? ? 327 PHE B CD2 1 210 B B +ATOM 7006 C CE1 . PHE B 1 210 ? -25.198 52.229 44.942 1.0 100.0 ? ? ? ? ? ? 327 PHE B CE1 1 210 B B +ATOM 7007 C CE2 . PHE B 1 210 ? -25.499 51.056 47.023 1.0 100.0 ? ? ? ? ? ? 327 PHE B CE2 1 210 B B +ATOM 7008 C CZ . PHE B 1 210 ? -25.125 52.206 46.331 1.0 100.0 ? ? ? ? ? ? 327 PHE B CZ 1 210 B B +ATOM 7009 N N . THR B 1 211 ? -29.376 47.320 42.530 1.0 89.94 ? ? ? ? ? ? 328 THR B N 1 211 B B +ATOM 7010 C CA . THR B 1 211 ? -29.755 46.252 41.621 1.0 88.6 ? ? ? ? ? ? 328 THR B CA 1 211 B B +ATOM 7011 C C . THR B 1 211 ? -31.089 46.585 40.962 1.0 92.98 ? ? ? ? ? ? 328 THR B C 1 211 B B +ATOM 7012 O O . THR B 1 211 ? -31.130 47.050 39.825 1.0 71.65 ? ? ? ? ? ? 328 THR B O 1 211 B B +ATOM 7013 C CB . THR B 1 211 ? -29.880 44.894 42.367 1.0 88.37 ? ? ? ? ? ? 328 THR B CB 1 211 B B +ATOM 7014 O OG1 . THR B 1 211 ? -30.752 45.037 43.496 1.0 87.1 ? ? ? ? ? ? 328 THR B OG1 1 211 B B +ATOM 7015 C CG2 . THR B 1 211 ? -28.519 44.418 42.849 1.0 78.14 ? ? ? ? ? ? 328 THR B CG2 1 211 B B +ATOM 7016 N N . VAL B 1 212 ? -32.170 46.368 41.702 1.0 100.0 ? ? ? ? ? ? 329 VAL B N 1 212 B B +ATOM 7017 C CA . VAL B 1 212 ? -33.524 46.623 41.221 1.0 100.0 ? ? ? ? ? ? 329 VAL B CA 1 212 B B +ATOM 7018 C C . VAL B 1 212 ? -33.808 48.103 40.967 1.0 99.41 ? ? ? ? ? ? 329 VAL B C 1 212 B B +ATOM 7019 O O . VAL B 1 212 ? -34.377 48.473 39.941 1.0 94.57 ? ? ? ? ? ? 329 VAL B O 1 212 B B +ATOM 7020 C CB . VAL B 1 212 ? -34.577 46.072 42.223 1.0 100.0 ? ? ? ? ? ? 329 VAL B CB 1 212 B B +ATOM 7021 C CG1 . VAL B 1 212 ? -35.979 46.280 41.675 1.0 100.0 ? ? ? ? ? ? 329 VAL B CG1 1 212 B B +ATOM 7022 C CG2 . VAL B 1 212 ? -34.332 44.595 42.464 1.0 89.69 ? ? ? ? ? ? 329 VAL B CG2 1 212 B B +ATOM 7023 N N . GLU B 1 213 ? -33.406 48.947 41.907 1.0 98.51 ? ? ? ? ? ? 330 GLU B N 1 213 B B +ATOM 7024 C CA . GLU B 1 213 ? -33.633 50.381 41.793 1.0 98.85 ? ? ? ? ? ? 330 GLU B CA 1 213 B B +ATOM 7025 C C . GLU B 1 213 ? -32.655 51.100 40.872 1.0 100.0 ? ? ? ? ? ? 330 GLU B C 1 213 B B +ATOM 7026 O O . GLU B 1 213 ? -33.064 51.734 39.904 1.0 98.41 ? ? ? ? ? ? 330 GLU B O 1 213 B B +ATOM 7027 C CB . GLU B 1 213 ? -33.601 51.010 43.184 1.0 99.44 ? ? ? ? ? ? 330 GLU B CB 1 213 B B +ATOM 7028 C CG . GLU B 1 213 ? -34.797 50.639 44.031 1.0 100.0 ? ? ? ? ? ? 330 GLU B CG 1 213 B B +ATOM 7029 C CD . GLU B 1 213 ? -36.060 51.342 43.580 1.0 100.0 ? ? ? ? ? ? 330 GLU B CD 1 213 B B +ATOM 7030 O OE1 . GLU B 1 213 ? -37.081 51.230 44.290 1.0 100.0 ? ? ? ? ? ? 330 GLU B OE1 1 213 B B +ATOM 7031 O OE2 . GLU B 1 213 ? -36.030 52.010 42.523 1.0 100.0 ? ? ? ? ? ? 330 GLU B OE2 1 213 B B +ATOM 7032 N N . PHE B 1 214 ? -31.364 50.997 41.174 1.0 100.0 ? ? ? ? ? ? 331 PHE B N 1 214 B B +ATOM 7033 C CA . PHE B 1 214 ? -30.333 51.653 40.371 1.0 100.0 ? ? ? ? ? ? 331 PHE B CA 1 214 B B +ATOM 7034 C C . PHE B 1 214 ? -29.212 50.711 39.941 1.0 100.0 ? ? ? ? ? ? 331 PHE B C 1 214 B B +ATOM 7035 O O . PHE B 1 214 ? -28.036 50.961 40.217 1.0 100.0 ? ? ? ? ? ? 331 PHE B O 1 214 B B +ATOM 7036 C CB . PHE B 1 214 ? -29.738 52.831 41.144 1.0 99.38 ? ? ? ? ? ? 331 PHE B CB 1 214 B B +ATOM 7037 C CG . PHE B 1 214 ? -30.709 53.948 41.375 1.0 99.09 ? ? ? ? ? ? 331 PHE B CG 1 214 B B +ATOM 7038 C CD1 . PHE B 1 214 ? -31.624 53.886 42.422 1.0 92.66 ? ? ? ? ? ? 331 PHE B CD1 1 214 B B +ATOM 7039 C CD2 . PHE B 1 214 ? -30.721 55.060 40.540 1.0 100.0 ? ? ? ? ? ? 331 PHE B CD2 1 214 B B +ATOM 7040 C CE1 . PHE B 1 214 ? -32.537 54.915 42.633 1.0 94.76 ? ? ? ? ? ? 331 PHE B CE1 1 214 B B +ATOM 7041 C CE2 . PHE B 1 214 ? -31.631 56.096 40.742 1.0 100.0 ? ? ? ? ? ? 331 PHE B CE2 1 214 B B +ATOM 7042 C CZ . PHE B 1 214 ? -32.540 56.022 41.792 1.0 100.0 ? ? ? ? ? ? 331 PHE B CZ 1 214 B B +ATOM 7043 N N . GLY B 1 215 ? -29.581 49.630 39.261 1.0 100.0 ? ? ? ? ? ? 332 GLY B N 1 215 B B +ATOM 7044 C CA . GLY B 1 215 ? -28.587 48.677 38.809 1.0 100.0 ? ? ? ? ? ? 332 GLY B CA 1 215 B B +ATOM 7045 C C . GLY B 1 215 ? -28.355 48.756 37.314 1.0 100.0 ? ? ? ? ? ? 332 GLY B C 1 215 B B +ATOM 7046 O O . GLY B 1 215 ? -29.209 49.240 36.564 1.0 100.0 ? ? ? ? ? ? 332 GLY B O 1 215 B B +ATOM 7047 N N . LEU B 1 216 ? -27.190 48.280 36.884 1.0 100.0 ? ? ? ? ? ? 333 LEU B N 1 216 B B +ATOM 7048 C CA . LEU B 1 216 ? -26.824 48.268 35.473 1.0 100.0 ? ? ? ? ? ? 333 LEU B CA 1 216 B B +ATOM 7049 C C . LEU B 1 216 ? -26.417 46.847 35.111 1.0 100.0 ? ? ? ? ? ? 333 LEU B C 1 216 B B +ATOM 7050 O O . LEU B 1 216 ? -25.650 46.214 35.834 1.0 100.0 ? ? ? ? ? ? 333 LEU B O 1 216 B B +ATOM 7051 C CB . LEU B 1 216 ? -25.664 49.233 35.212 1.0 100.0 ? ? ? ? ? ? 333 LEU B CB 1 216 B B +ATOM 7052 C CG . LEU B 1 216 ? -25.995 50.727 35.334 1.0 100.0 ? ? ? ? ? ? 333 LEU B CG 1 216 B B +ATOM 7053 C CD1 . LEU B 1 216 ? -24.735 51.545 35.112 1.0 100.0 ? ? ? ? ? ? 333 LEU B CD1 1 216 B B +ATOM 7054 C CD2 . LEU B 1 216 ? -27.061 51.117 34.323 1.0 84.61 ? ? ? ? ? ? 333 LEU B CD2 1 216 B B +ATOM 7055 N N . CYS B 1 217 ? -26.926 46.348 33.989 1.0 100.0 ? ? ? ? ? ? 334 CYS B N 1 217 B B +ATOM 7056 C CA . CYS B 1 217 ? -26.620 44.986 33.564 1.0 100.0 ? ? ? ? ? ? 334 CYS B CA 1 217 B B +ATOM 7057 C C . CYS B 1 217 ? -25.609 44.888 32.427 1.0 100.0 ? ? ? ? ? ? 334 CYS B C 1 217 B B +ATOM 7058 O O . CYS B 1 217 ? -25.142 45.896 31.892 1.0 93.62 ? ? ? ? ? ? 334 CYS B O 1 217 B B +ATOM 7059 C CB . CYS B 1 217 ? -27.905 44.265 33.153 1.0 100.0 ? ? ? ? ? ? 334 CYS B CB 1 217 B B +ATOM 7060 S SG . CYS B 1 217 ? -28.666 44.917 31.638 1.0 100.0 ? ? ? ? ? ? 334 CYS B SG 1 217 B B +ATOM 7061 N N . LYS B 1 218 ? -25.292 43.649 32.066 1.0 100.0 ? ? ? ? ? ? 335 LYS B N 1 218 B B +ATOM 7062 C CA . LYS B 1 218 ? -24.339 43.357 31.002 1.0 100.0 ? ? ? ? ? ? 335 LYS B CA 1 218 B B +ATOM 7063 C C . LYS B 1 218 ? -25.026 42.823 29.747 1.0 100.0 ? ? ? ? ? ? 335 LYS B C 1 218 B B +ATOM 7064 O O . LYS B 1 218 ? -25.701 41.791 29.787 1.0 97.61 ? ? ? ? ? ? 335 LYS B O 1 218 B B +ATOM 7065 C CB . LYS B 1 218 ? -23.321 42.329 31.494 1.0 100.0 ? ? ? ? ? ? 335 LYS B CB 1 218 B B +ATOM 7066 C CG . LYS B 1 218 ? -22.360 42.868 32.528 1.0 100.0 ? ? ? ? ? ? 335 LYS B CG 1 218 B B +ATOM 7067 C CD . LYS B 1 218 ? -20.937 42.832 32.003 1.0 100.0 ? ? ? ? ? ? 335 LYS B CD 1 218 B B +ATOM 7068 C CE . LYS B 1 218 ? -20.589 44.115 31.257 1.0 100.0 ? ? ? ? ? ? 335 LYS B CE 1 218 B B +ATOM 7069 N NZ . LYS B 1 218 ? -21.324 44.259 29.967 1.0 100.0 ? ? ? ? ? ? 335 LYS B NZ 1 218 B B +ATOM 7070 N N . GLN B 1 219 ? -24.842 43.523 28.633 1.0 95.53 ? ? ? ? ? ? 336 GLN B N 1 219 B B +ATOM 7071 C CA . GLN B 1 219 ? -25.443 43.109 27.370 1.0 99.94 ? ? ? ? ? ? 336 GLN B CA 1 219 B B +ATOM 7072 C C . GLN B 1 219 ? -24.378 42.927 26.290 1.0 100.0 ? ? ? ? ? ? 336 GLN B C 1 219 B B +ATOM 7073 O O . GLN B 1 219 ? -24.341 43.667 25.308 1.0 100.0 ? ? ? ? ? ? 336 GLN B O 1 219 B B +ATOM 7074 C CB . GLN B 1 219 ? -26.473 44.146 26.917 1.0 97.51 ? ? ? ? ? ? 336 GLN B CB 1 219 B B +ATOM 7075 C CG . GLN B 1 219 ? -27.642 44.306 27.879 1.0 100.0 ? ? ? ? ? ? 336 GLN B CG 1 219 B B +ATOM 7076 C CD . GLN B 1 219 ? -28.710 43.242 27.684 1.0 100.0 ? ? ? ? ? ? 336 GLN B CD 1 219 B B +ATOM 7077 O OE1 . GLN B 1 219 ? -28.713 42.519 26.685 1.0 100.0 ? ? ? ? ? ? 336 GLN B OE1 1 219 B B +ATOM 7078 N NE2 . GLN B 1 219 ? -29.628 43.145 28.642 1.0 100.0 ? ? ? ? ? ? 336 GLN B NE2 1 219 B B +ATOM 7079 N N . GLY B 1 220 ? -23.518 41.930 26.481 1.0 100.0 ? ? ? ? ? ? 337 GLY B N 1 220 B B +ATOM 7080 C CA . GLY B 1 220 ? -22.454 41.662 25.529 1.0 93.95 ? ? ? ? ? ? 337 GLY B CA 1 220 B B +ATOM 7081 C C . GLY B 1 220 ? -21.164 42.327 25.969 1.0 97.49 ? ? ? ? ? ? 337 GLY B C 1 220 B B +ATOM 7082 O O . GLY B 1 220 ? -20.369 41.742 26.702 1.0 94.1 ? ? ? ? ? ? 337 GLY B O 1 220 B B +ATOM 7083 N N . ASP B 1 221 ? -20.957 43.559 25.518 1.0 100.0 ? ? ? ? ? ? 338 ASP B N 1 221 B B +ATOM 7084 C CA . ASP B 1 221 ? -19.764 44.318 25.879 1.0 100.0 ? ? ? ? ? ? 338 ASP B CA 1 221 B B +ATOM 7085 C C . ASP B 1 221 ? -20.222 45.594 26.566 1.0 100.0 ? ? ? ? ? ? 338 ASP B C 1 221 B B +ATOM 7086 O O . ASP B 1 221 ? -19.634 46.045 27.551 1.0 100.0 ? ? ? ? ? ? 338 ASP B O 1 221 B B +ATOM 7087 C CB . ASP B 1 221 ? -18.961 44.686 24.629 1.0 100.0 ? ? ? ? ? ? 338 ASP B CB 1 221 B B +ATOM 7088 C CG . ASP B 1 221 ? -18.370 43.475 23.938 1.0 100.0 ? ? ? ? ? ? 338 ASP B CG 1 221 B B +ATOM 7089 O OD1 . ASP B 1 221 ? -17.615 42.728 24.596 1.0 100.0 ? ? ? ? ? ? 338 ASP B OD1 1 221 B B +ATOM 7090 O OD2 . ASP B 1 221 ? -18.660 43.272 22.738 1.0 98.72 ? ? ? ? ? ? 338 ASP B OD2 1 221 B B +ATOM 7091 N N . SER B 1 222 ? -21.293 46.160 26.024 1.0 100.0 ? ? ? ? ? ? 339 SER B N 1 222 B B +ATOM 7092 C CA . SER B 1 222 ? -21.873 47.391 26.536 1.0 100.0 ? ? ? ? ? ? 339 SER B CA 1 222 B B +ATOM 7093 C C . SER B 1 222 ? -22.663 47.188 27.822 1.0 100.0 ? ? ? ? ? ? 339 SER B C 1 222 B B +ATOM 7094 O O . SER B 1 222 ? -22.945 46.057 28.228 1.0 100.0 ? ? ? ? ? ? 339 SER B O 1 222 B B +ATOM 7095 C CB . SER B 1 222 ? -22.786 48.010 25.475 1.0 100.0 ? ? ? ? ? ? 339 SER B CB 1 222 B B +ATOM 7096 O OG . SER B 1 222 ? -23.727 47.060 24.999 1.0 100.0 ? ? ? ? ? ? 339 SER B OG 1 222 B B +ATOM 7097 N N . ILE B 1 223 ? -23.019 48.305 28.449 1.0 100.0 ? ? ? ? ? ? 340 ILE B N 1 223 B B +ATOM 7098 C CA . ILE B 1 223 ? -23.785 48.296 29.686 1.0 100.0 ? ? ? ? ? ? 340 ILE B CA 1 223 B B +ATOM 7099 C C . ILE B 1 223 ? -25.127 48.991 29.479 1.0 100.0 ? ? ? ? ? ? 340 ILE B C 1 223 B B +ATOM 7100 O O . ILE B 1 223 ? -25.204 50.061 28.864 1.0 99.68 ? ? ? ? ? ? 340 ILE B O 1 223 B B +ATOM 7101 C CB . ILE B 1 223 ? -23.012 49.006 30.832 1.0 97.56 ? ? ? ? ? ? 340 ILE B CB 1 223 B B +ATOM 7102 C CG1 . ILE B 1 223 ? -22.320 47.958 31.706 1.0 77.79 ? ? ? ? ? ? 340 ILE B CG1 1 223 B B +ATOM 7103 C CG2 . ILE B 1 223 ? -23.959 49.863 31.669 1.0 89.25 ? ? ? ? ? ? 340 ILE B CG2 1 223 B B +ATOM 7104 C CD1 . ILE B 1 223 ? -21.116 47.316 31.049 1.0 45.99 ? ? ? ? ? ? 340 ILE B CD1 1 223 B B +ATOM 7105 N N . LYS B 1 224 ? -26.179 48.371 30.001 1.0 100.0 ? ? ? ? ? ? 341 LYS B N 1 224 B B +ATOM 7106 C CA . LYS B 1 224 ? -27.525 48.917 29.896 1.0 100.0 ? ? ? ? ? ? 341 LYS B CA 1 224 B B +ATOM 7107 C C . LYS B 1 224 ? -28.089 49.186 31.289 1.0 100.0 ? ? ? ? ? ? 341 LYS B C 1 224 B B +ATOM 7108 O O . LYS B 1 224 ? -27.562 48.694 32.292 1.0 100.0 ? ? ? ? ? ? 341 LYS B O 1 224 B B +ATOM 7109 C CB . LYS B 1 224 ? -28.435 47.941 29.147 1.0 99.3 ? ? ? ? ? ? 341 LYS B CB 1 224 B B +ATOM 7110 C CG . LYS B 1 224 ? -28.138 47.838 27.663 1.0 92.41 ? ? ? ? ? ? 341 LYS B CG 1 224 B B +ATOM 7111 C CD . LYS B 1 224 ? -28.521 49.112 26.935 1.0 94.05 ? ? ? ? ? ? 341 LYS B CD 1 224 B B +ATOM 7112 C CE . LYS B 1 224 ? -28.442 48.933 25.430 1.0 96.81 ? ? ? ? ? ? 341 LYS B CE 1 224 B B +ATOM 7113 N NZ . LYS B 1 224 ? -27.106 48.426 25.012 1.0 100.0 ? ? ? ? ? ? 341 LYS B NZ 1 224 B B +ATOM 7114 N N . ALA B 1 225 ? -29.157 49.975 31.345 1.0 100.0 ? ? ? ? ? ? 342 ALA B N 1 225 B B +ATOM 7115 C CA . ALA B 1 225 ? -29.796 50.306 32.612 1.0 100.0 ? ? ? ? ? ? 342 ALA B CA 1 225 B B +ATOM 7116 C C . ALA B 1 225 ? -31.028 49.433 32.820 1.0 100.0 ? ? ? ? ? ? 342 ALA B C 1 225 B B +ATOM 7117 O O . ALA B 1 225 ? -31.896 49.349 31.952 1.0 100.0 ? ? ? ? ? ? 342 ALA B O 1 225 B B +ATOM 7118 C CB . ALA B 1 225 ? -30.187 51.782 32.632 1.0 100.0 ? ? ? ? ? ? 342 ALA B CB 1 225 B B +ATOM 7119 N N . TYR B 1 226 ? -31.091 48.770 33.969 1.0 100.0 ? ? ? ? ? ? 343 TYR B N 1 226 B B +ATOM 7120 C CA . TYR B 1 226 ? -32.225 47.909 34.288 1.0 100.0 ? ? ? ? ? ? 343 TYR B CA 1 226 B B +ATOM 7121 C C . TYR B 1 226 ? -32.834 48.333 35.617 1.0 100.0 ? ? ? ? ? ? 343 TYR B C 1 226 B B +ATOM 7122 O O . TYR B 1 226 ? -33.850 47.788 36.051 1.0 100.0 ? ? ? ? ? ? 343 TYR B O 1 226 B B +ATOM 7123 C CB . TYR B 1 226 ? -31.784 46.438 34.339 1.0 100.0 ? ? ? ? ? ? 343 TYR B CB 1 226 B B +ATOM 7124 C CG . TYR B 1 226 ? -31.074 46.031 35.612 1.0 100.0 ? ? ? ? ? ? 343 TYR B CG 1 226 B B +ATOM 7125 C CD1 . TYR B 1 226 ? -29.693 46.176 35.741 1.0 97.49 ? ? ? ? ? ? 343 TYR B CD1 1 226 B B +ATOM 7126 C CD2 . TYR B 1 226 ? -31.783 45.495 36.686 1.0 100.0 ? ? ? ? ? ? 343 TYR B CD2 1 226 B B +ATOM 7127 C CE1 . TYR B 1 226 ? -29.036 45.797 36.910 1.0 92.68 ? ? ? ? ? ? 343 TYR B CE1 1 226 B B +ATOM 7128 C CE2 . TYR B 1 226 ? -31.136 45.114 37.857 1.0 100.0 ? ? ? ? ? ? 343 TYR B CE2 1 226 B B +ATOM 7129 C CZ . TYR B 1 226 ? -29.763 45.270 37.962 1.0 99.5 ? ? ? ? ? ? 343 TYR B CZ 1 226 B B +ATOM 7130 O OH . TYR B 1 226 ? -29.120 44.908 39.122 1.0 100.0 ? ? ? ? ? ? 343 TYR B OH 1 226 B B +ATOM 7131 N N . GLY B 1 227 ? -32.202 49.313 36.255 1.0 100.0 ? ? ? ? ? ? 344 GLY B N 1 227 B B +ATOM 7132 C CA . GLY B 1 227 ? -32.695 49.812 37.524 1.0 96.04 ? ? ? ? ? ? 344 GLY B CA 1 227 B B +ATOM 7133 C C . GLY B 1 227 ? -34.029 50.508 37.342 1.0 100.0 ? ? ? ? ? ? 344 GLY B C 1 227 B B +ATOM 7134 O O . GLY B 1 227 ? -34.221 51.267 36.389 1.0 91.72 ? ? ? ? ? ? 344 GLY B O 1 227 B B +ATOM 7135 N N . ALA B 1 228 ? -34.954 50.248 38.260 1.0 100.0 ? ? ? ? ? ? 345 ALA B N 1 228 B B +ATOM 7136 C CA . ALA B 1 228 ? -36.286 50.839 38.204 1.0 94.41 ? ? ? ? ? ? 345 ALA B CA 1 228 B B +ATOM 7137 C C . ALA B 1 228 ? -36.234 52.341 38.441 1.0 95.61 ? ? ? ? ? ? 345 ALA B C 1 228 B B +ATOM 7138 O O . ALA B 1 228 ? -36.970 53.105 37.815 1.0 95.17 ? ? ? ? ? ? 345 ALA B O 1 228 B B +ATOM 7139 C CB . ALA B 1 228 ? -37.183 50.178 39.229 1.0 80.87 ? ? ? ? ? ? 345 ALA B CB 1 228 B B +ATOM 7140 N N . GLY B 1 229 ? -35.362 52.762 39.350 1.0 94.4 ? ? ? ? ? ? 346 GLY B N 1 229 B B +ATOM 7141 C CA . GLY B 1 229 ? -35.228 54.176 39.636 1.0 95.7 ? ? ? ? ? ? 346 GLY B CA 1 229 B B +ATOM 7142 C C . GLY B 1 229 ? -34.596 54.903 38.463 1.0 96.08 ? ? ? ? ? ? 346 GLY B C 1 229 B B +ATOM 7143 O O . GLY B 1 229 ? -34.825 56.095 38.265 1.0 100.0 ? ? ? ? ? ? 346 GLY B O 1 229 B B +ATOM 7144 N N . LEU B 1 230 ? -33.795 54.181 37.686 1.0 90.98 ? ? ? ? ? ? 347 LEU B N 1 230 B B +ATOM 7145 C CA . LEU B 1 230 ? -33.125 54.752 36.522 1.0 93.82 ? ? ? ? ? ? 347 LEU B CA 1 230 B B +ATOM 7146 C C . LEU B 1 230 ? -34.092 54.934 35.358 1.0 98.26 ? ? ? ? ? ? 347 LEU B C 1 230 B B +ATOM 7147 O O . LEU B 1 230 ? -34.172 56.007 34.764 1.0 100.0 ? ? ? ? ? ? 347 LEU B O 1 230 B B +ATOM 7148 C CB . LEU B 1 230 ? -31.982 53.843 36.063 1.0 96.72 ? ? ? ? ? ? 347 LEU B CB 1 230 B B +ATOM 7149 C CG . LEU B 1 230 ? -30.817 53.599 37.024 1.0 100.0 ? ? ? ? ? ? 347 LEU B CG 1 230 B B +ATOM 7150 C CD1 . LEU B 1 230 ? -29.974 52.442 36.503 1.0 96.93 ? ? ? ? ? ? 347 LEU B CD1 1 230 B B +ATOM 7151 C CD2 . LEU B 1 230 ? -29.981 54.864 37.158 1.0 100.0 ? ? ? ? ? ? 347 LEU B CD2 1 230 B B +ATOM 7152 N N . LEU B 1 231 ? -34.816 53.866 35.039 1.0 100.0 ? ? ? ? ? ? 348 LEU B N 1 231 B B +ATOM 7153 C CA . LEU B 1 231 ? -35.768 53.864 33.935 1.0 97.5 ? ? ? ? ? ? 348 LEU B CA 1 231 B B +ATOM 7154 C C . LEU B 1 231 ? -36.913 54.860 34.069 1.0 88.35 ? ? ? ? ? ? 348 LEU B C 1 231 B B +ATOM 7155 O O . LEU B 1 231 ? -37.398 55.384 33.067 1.0 81.45 ? ? ? ? ? ? 348 LEU B O 1 231 B B +ATOM 7156 C CB . LEU B 1 231 ? -36.332 52.454 33.746 1.0 100.0 ? ? ? ? ? ? 348 LEU B CB 1 231 B B +ATOM 7157 C CG . LEU B 1 231 ? -35.267 51.414 33.384 1.0 95.13 ? ? ? ? ? ? 348 LEU B CG 1 231 B B +ATOM 7158 C CD1 . LEU B 1 231 ? -35.729 50.031 33.803 1.0 82.59 ? ? ? ? ? ? 348 LEU B CD1 1 231 B B +ATOM 7159 C CD2 . LEU B 1 231 ? -34.987 51.475 31.892 1.0 100.0 ? ? ? ? ? ? 348 LEU B CD2 1 231 B B +ATOM 7160 N N . SER B 1 232 ? -37.352 55.114 35.297 1.0 85.54 ? ? ? ? ? ? 349 SER B N 1 232 B B +ATOM 7161 C CA . SER B 1 232 ? -38.444 56.053 35.523 1.0 93.03 ? ? ? ? ? ? 349 SER B CA 1 232 B B +ATOM 7162 C C . SER B 1 232 ? -37.941 57.489 35.642 1.0 100.0 ? ? ? ? ? ? 349 SER B C 1 232 B B +ATOM 7163 O O . SER B 1 232 ? -38.727 58.436 35.573 1.0 100.0 ? ? ? ? ? ? 349 SER B O 1 232 B B +ATOM 7164 C CB . SER B 1 232 ? -39.218 55.671 36.786 1.0 89.12 ? ? ? ? ? ? 349 SER B CB 1 232 B B +ATOM 7165 O OG . SER B 1 232 ? -38.435 55.854 37.952 1.0 84.89 ? ? ? ? ? ? 349 SER B OG 1 232 B B +ATOM 7166 N N . SER B 1 233 ? -36.629 57.647 35.813 1.0 100.0 ? ? ? ? ? ? 350 SER B N 1 233 B B +ATOM 7167 C CA . SER B 1 233 ? -36.025 58.972 35.946 1.0 94.48 ? ? ? ? ? ? 350 SER B CA 1 233 B B +ATOM 7168 C C . SER B 1 233 ? -35.258 59.366 34.690 1.0 88.87 ? ? ? ? ? ? 350 SER B C 1 233 B B +ATOM 7169 O O . SER B 1 233 ? -34.260 58.740 34.333 1.0 80.63 ? ? ? ? ? ? 350 SER B O 1 233 B B +ATOM 7170 C CB . SER B 1 233 ? -35.085 59.007 37.149 1.0 96.72 ? ? ? ? ? ? 350 SER B CB 1 233 B B +ATOM 7171 O OG . SER B 1 233 ? -34.109 60.021 36.998 1.0 82.26 ? ? ? ? ? ? 350 SER B OG 1 233 B B +ATOM 7172 N N . PHE B 1 234 ? -35.731 60.421 34.034 1.0 91.05 ? ? ? ? ? ? 351 PHE B N 1 234 B B +ATOM 7173 C CA . PHE B 1 234 ? -35.124 60.914 32.801 1.0 100.0 ? ? ? ? ? ? 351 PHE B CA 1 234 B B +ATOM 7174 C C . PHE B 1 234 ? -33.689 61.427 32.942 1.0 100.0 ? ? ? ? ? ? 351 PHE B C 1 234 B B +ATOM 7175 O O . PHE B 1 234 ? -32.827 61.116 32.120 1.0 100.0 ? ? ? ? ? ? 351 PHE B O 1 234 B B +ATOM 7176 C CB . PHE B 1 234 ? -35.987 62.027 32.199 1.0 100.0 ? ? ? ? ? ? 351 PHE B CB 1 234 B B +ATOM 7177 C CG . PHE B 1 234 ? -35.323 62.758 31.066 1.0 100.0 ? ? ? ? ? ? 351 PHE B CG 1 234 B B +ATOM 7178 C CD1 . PHE B 1 234 ? -35.195 62.155 29.819 1.0 100.0 ? ? ? ? ? ? 351 PHE B CD1 1 234 B B +ATOM 7179 C CD2 . PHE B 1 234 ? -34.811 64.040 31.247 1.0 100.0 ? ? ? ? ? ? 351 PHE B CD2 1 234 B B +ATOM 7180 C CE1 . PHE B 1 234 ? -34.566 62.815 28.769 1.0 100.0 ? ? ? ? ? ? 351 PHE B CE1 1 234 B B +ATOM 7181 C CE2 . PHE B 1 234 ? -34.179 64.711 30.203 1.0 100.0 ? ? ? ? ? ? 351 PHE B CE2 1 234 B B +ATOM 7182 C CZ . PHE B 1 234 ? -34.056 64.097 28.961 1.0 100.0 ? ? ? ? ? ? 351 PHE B CZ 1 234 B B +ATOM 7183 N N . GLY B 1 235 ? -33.444 62.220 33.980 1.0 100.0 ? ? ? ? ? ? 352 GLY B N 1 235 B B +ATOM 7184 C CA . GLY B 1 235 ? -32.122 62.784 34.192 1.0 97.48 ? ? ? ? ? ? 352 GLY B CA 1 235 B B +ATOM 7185 C C . GLY B 1 235 ? -31.017 61.793 34.504 1.0 95.87 ? ? ? ? ? ? 352 GLY B C 1 235 B B +ATOM 7186 O O . GLY B 1 235 ? -29.868 61.996 34.109 1.0 86.0 ? ? ? ? ? ? 352 GLY B O 1 235 B B +ATOM 7187 N N . GLU B 1 236 ? -31.353 60.721 35.215 1.0 93.46 ? ? ? ? ? ? 353 GLU B N 1 236 B B +ATOM 7188 C CA . GLU B 1 236 ? -30.356 59.719 35.573 1.0 93.61 ? ? ? ? ? ? 353 GLU B CA 1 236 B B +ATOM 7189 C C . GLU B 1 236 ? -30.228 58.607 34.541 1.0 92.61 ? ? ? ? ? ? 353 GLU B C 1 236 B B +ATOM 7190 O O . GLU B 1 236 ? -29.250 57.858 34.540 1.0 89.2 ? ? ? ? ? ? 353 GLU B O 1 236 B B +ATOM 7191 C CB . GLU B 1 236 ? -30.680 59.113 36.935 1.0 91.82 ? ? ? ? ? ? 353 GLU B CB 1 236 B B +ATOM 7192 C CG . GLU B 1 236 ? -29.449 58.705 37.722 1.0 80.75 ? ? ? ? ? ? 353 GLU B CG 1 236 B B +ATOM 7193 C CD . GLU B 1 236 ? -29.690 58.730 39.215 1.0 83.7 ? ? ? ? ? ? 353 GLU B CD 1 236 B B +ATOM 7194 O OE1 . GLU B 1 236 ? -28.797 58.294 39.970 1.0 78.05 ? ? ? ? ? ? 353 GLU B OE1 1 236 B B +ATOM 7195 O OE2 . GLU B 1 236 ? -30.775 59.190 39.632 1.0 90.12 ? ? ? ? ? ? 353 GLU B OE2 1 236 B B +ATOM 7196 N N . LEU B 1 237 ? -31.223 58.496 33.672 1.0 94.32 ? ? ? ? ? ? 354 LEU B N 1 237 B B +ATOM 7197 C CA . LEU B 1 237 ? -31.206 57.474 32.638 1.0 100.0 ? ? ? ? ? ? 354 LEU B CA 1 237 B B +ATOM 7198 C C . LEU B 1 237 ? -30.037 57.724 31.686 1.0 100.0 ? ? ? ? ? ? 354 LEU B C 1 237 B B +ATOM 7199 O O . LEU B 1 237 ? -29.366 56.788 31.243 1.0 100.0 ? ? ? ? ? ? 354 LEU B O 1 237 B B +ATOM 7200 C CB . LEU B 1 237 ? -32.529 57.493 31.870 1.0 100.0 ? ? ? ? ? ? 354 LEU B CB 1 237 B B +ATOM 7201 C CG . LEU B 1 237 ? -32.731 56.463 30.755 1.0 100.0 ? ? ? ? ? ? 354 LEU B CG 1 237 B B +ATOM 7202 C CD1 . LEU B 1 237 ? -32.472 55.051 31.272 1.0 100.0 ? ? ? ? ? ? 354 LEU B CD1 1 237 B B +ATOM 7203 C CD2 . LEU B 1 237 ? -34.153 56.591 30.229 1.0 100.0 ? ? ? ? ? ? 354 LEU B CD2 1 237 B B +ATOM 7204 N N . GLN B 1 238 ? -29.797 58.995 31.381 1.0 100.0 ? ? ? ? ? ? 355 GLN B N 1 238 B B +ATOM 7205 C CA . GLN B 1 238 ? -28.709 59.372 30.488 1.0 100.0 ? ? ? ? ? ? 355 GLN B CA 1 238 B B +ATOM 7206 C C . GLN B 1 238 ? -27.395 59.543 31.251 1.0 100.0 ? ? ? ? ? ? 355 GLN B C 1 238 B B +ATOM 7207 O O . GLN B 1 238 ? -26.312 59.445 30.669 1.0 100.0 ? ? ? ? ? ? 355 GLN B O 1 238 B B +ATOM 7208 C CB . GLN B 1 238 ? -29.056 60.673 29.768 1.0 100.0 ? ? ? ? ? ? 355 GLN B CB 1 238 B B +ATOM 7209 C CG . GLN B 1 238 ? -29.909 61.625 30.592 1.0 100.0 ? ? ? ? ? ? 355 GLN B CG 1 238 B B +ATOM 7210 C CD . GLN B 1 238 ? -30.520 62.725 29.748 1.0 100.0 ? ? ? ? ? ? 355 GLN B CD 1 238 B B +ATOM 7211 O OE1 . GLN B 1 238 ? -30.344 63.914 30.024 1.0 100.0 ? ? ? ? ? ? 355 GLN B OE1 1 238 B B +ATOM 7212 N NE2 . GLN B 1 238 ? -31.245 62.332 28.709 1.0 98.92 ? ? ? ? ? ? 355 GLN B NE2 1 238 B B +ATOM 7213 N N . TYR B 1 239 ? -27.495 59.789 32.555 1.0 100.0 ? ? ? ? ? ? 356 TYR B N 1 239 B B +ATOM 7214 C CA . TYR B 1 239 ? -26.309 59.978 33.385 1.0 100.0 ? ? ? ? ? ? 356 TYR B CA 1 239 B B +ATOM 7215 C C . TYR B 1 239 ? -25.576 58.675 33.710 1.0 100.0 ? ? ? ? ? ? 356 TYR B C 1 239 B B +ATOM 7216 O O . TYR B 1 239 ? -24.347 58.611 33.650 1.0 100.0 ? ? ? ? ? ? 356 TYR B O 1 239 B B +ATOM 7217 C CB . TYR B 1 239 ? -26.677 60.667 34.698 1.0 100.0 ? ? ? ? ? ? 356 TYR B CB 1 239 B B +ATOM 7218 C CG . TYR B 1 239 ? -25.622 60.495 35.771 1.0 100.0 ? ? ? ? ? ? 356 TYR B CG 1 239 B B +ATOM 7219 C CD1 . TYR B 1 239 ? -24.336 61.008 35.594 1.0 100.0 ? ? ? ? ? ? 356 TYR B CD1 1 239 B B +ATOM 7220 C CD2 . TYR B 1 239 ? -25.902 59.815 36.957 1.0 100.0 ? ? ? ? ? ? 356 TYR B CD2 1 239 B B +ATOM 7221 C CE1 . TYR B 1 239 ? -23.356 60.854 36.570 1.0 100.0 ? ? ? ? ? ? 356 TYR B CE1 1 239 B B +ATOM 7222 C CE2 . TYR B 1 239 ? -24.927 59.654 37.942 1.0 100.0 ? ? ? ? ? ? 356 TYR B CE2 1 239 B B +ATOM 7223 C CZ . TYR B 1 239 ? -23.657 60.178 37.742 1.0 100.0 ? ? ? ? ? ? 356 TYR B CZ 1 239 B B +ATOM 7224 O OH . TYR B 1 239 ? -22.696 60.041 38.719 1.0 100.0 ? ? ? ? ? ? 356 TYR B OH 1 239 B B +ATOM 7225 N N . CYS B 1 240 ? -26.337 57.648 34.070 1.0 98.65 ? ? ? ? ? ? 357 CYS B N 1 240 B B +ATOM 7226 C CA . CYS B 1 240 ? -25.765 56.353 34.421 1.0 100.0 ? ? ? ? ? ? 357 CYS B CA 1 240 B B +ATOM 7227 C C . CYS B 1 240 ? -25.103 55.664 33.229 1.0 100.0 ? ? ? ? ? ? 357 CYS B C 1 240 B B +ATOM 7228 O O . CYS B 1 240 ? -24.252 54.788 33.405 1.0 100.0 ? ? ? ? ? ? 357 CYS B O 1 240 B B +ATOM 7229 C CB . CYS B 1 240 ? -26.853 55.442 34.990 1.0 100.0 ? ? ? ? ? ? 357 CYS B CB 1 240 B B +ATOM 7230 S SG . CYS B 1 240 ? -28.183 55.062 33.819 1.0 100.0 ? ? ? ? ? ? 357 CYS B SG 1 240 B B +ATOM 7231 N N . LEU B 1 241 ? -25.490 56.069 32.021 1.0 100.0 ? ? ? ? ? ? 358 LEU B N 1 241 B B +ATOM 7232 C CA . LEU B 1 241 ? -24.953 55.481 30.798 1.0 100.0 ? ? ? ? ? ? 358 LEU B CA 1 241 B B +ATOM 7233 C C . LEU B 1 241 ? -23.689 56.179 30.295 1.0 100.0 ? ? ? ? ? ? 358 LEU B C 1 241 B B +ATOM 7234 O O . LEU B 1 241 ? -23.009 55.679 29.396 1.0 100.0 ? ? ? ? ? ? 358 LEU B O 1 241 B B +ATOM 7235 C CB . LEU B 1 241 ? -26.027 55.500 29.705 1.0 96.86 ? ? ? ? ? ? 358 LEU B CB 1 241 B B +ATOM 7236 C CG . LEU B 1 241 ? -26.470 54.148 29.129 1.0 99.6 ? ? ? ? ? ? 358 LEU B CG 1 241 B B +ATOM 7237 C CD1 . LEU B 1 241 ? -25.356 53.571 28.268 1.0 100.0 ? ? ? ? ? ? 358 LEU B CD1 1 241 B B +ATOM 7238 C CD2 . LEU B 1 241 ? -26.837 53.195 30.257 1.0 97.83 ? ? ? ? ? ? 358 LEU B CD2 1 241 B B +ATOM 7239 N N . SER B 1 242 ? -23.370 57.327 30.884 1.0 100.0 ? ? ? ? ? ? 359 SER B N 1 242 B B +ATOM 7240 C CA . SER B 1 242 ? -22.190 58.082 30.480 1.0 100.0 ? ? ? ? ? ? 359 SER B CA 1 242 B B +ATOM 7241 C C . SER B 1 242 ? -20.915 57.598 31.168 1.0 100.0 ? ? ? ? ? ? 359 SER B C 1 242 B B +ATOM 7242 O O . SER B 1 242 ? -20.940 56.646 31.954 1.0 96.18 ? ? ? ? ? ? 359 SER B O 1 242 B B +ATOM 7243 C CB . SER B 1 242 ? -22.398 59.576 30.759 1.0 100.0 ? ? ? ? ? ? 359 SER B CB 1 242 B B +ATOM 7244 O OG . SER B 1 242 ? -22.612 59.818 32.138 1.0 96.44 ? ? ? ? ? ? 359 SER B OG 1 242 B B +ATOM 7245 N N . GLU B 1 243 ? -19.804 58.265 30.864 1.0 100.0 ? ? ? ? ? ? 360 GLU B N 1 243 B B +ATOM 7246 C CA . GLU B 1 243 ? -18.503 57.923 31.435 1.0 100.0 ? ? ? ? ? ? 360 GLU B CA 1 243 B B +ATOM 7247 C C . GLU B 1 243 ? -18.099 58.867 32.564 1.0 100.0 ? ? ? ? ? ? 360 GLU B C 1 243 B B +ATOM 7248 O O . GLU B 1 243 ? -16.949 59.306 32.642 1.0 100.0 ? ? ? ? ? ? 360 GLU B O 1 243 B B +ATOM 7249 C CB . GLU B 1 243 ? -17.429 57.943 30.348 1.0 100.0 ? ? ? ? ? ? 360 GLU B CB 1 243 B B +ATOM 7250 C CG . GLU B 1 243 ? -17.462 56.733 29.434 1.0 100.0 ? ? ? ? ? ? 360 GLU B CG 1 243 B B +ATOM 7251 C CD . GLU B 1 243 ? -16.837 57.010 28.081 1.0 100.0 ? ? ? ? ? ? 360 GLU B CD 1 243 B B +ATOM 7252 O OE1 . GLU B 1 243 ? -15.660 57.430 28.051 1.0 100.0 ? ? ? ? ? ? 360 GLU B OE1 1 243 B B +ATOM 7253 O OE2 . GLU B 1 243 ? -17.522 56.814 27.050 1.0 100.0 ? ? ? ? ? ? 360 GLU B OE2 1 243 B B +ATOM 7254 N N . LYS B 1 244 ? -19.055 59.176 33.434 1.0 100.0 ? ? ? ? ? ? 361 LYS B N 1 244 B B +ATOM 7255 C CA . LYS B 1 244 ? -18.804 60.058 34.564 1.0 100.0 ? ? ? ? ? ? 361 LYS B CA 1 244 B B +ATOM 7256 C C . LYS B 1 244 ? -18.758 59.261 35.872 1.0 100.0 ? ? ? ? ? ? 361 LYS B C 1 244 B B +ATOM 7257 O O . LYS B 1 244 ? -17.870 59.469 36.704 1.0 100.0 ? ? ? ? ? ? 361 LYS B O 1 244 B B +ATOM 7258 C CB . LYS B 1 244 ? -19.885 61.146 34.638 1.0 100.0 ? ? ? ? ? ? 361 LYS B CB 1 244 B B +ATOM 7259 C CG . LYS B 1 244 ? -19.947 62.024 33.396 1.0 94.4 ? ? ? ? ? ? 361 LYS B CG 1 244 B B +ATOM 7260 C CD . LYS B 1 244 ? -20.954 63.155 33.538 1.0 96.23 ? ? ? ? ? ? 361 LYS B CD 1 244 B B +ATOM 7261 C CE . LYS B 1 244 ? -20.918 64.059 32.312 1.0 100.0 ? ? ? ? ? ? 361 LYS B CE 1 244 B B +ATOM 7262 N NZ . LYS B 1 244 ? -21.851 65.214 32.421 1.0 100.0 ? ? ? ? ? ? 361 LYS B NZ 1 244 B B +ATOM 7263 N N . PRO B 1 245 ? -19.700 58.312 36.058 1.0 100.0 ? ? ? ? ? ? 362 PRO B N 1 245 B B +ATOM 7264 C CA . PRO B 1 245 ? -19.736 57.503 37.282 1.0 100.0 ? ? ? ? ? ? 362 PRO B CA 1 245 B B +ATOM 7265 C C . PRO B 1 245 ? -18.673 56.411 37.267 1.0 100.0 ? ? ? ? ? ? 362 PRO B C 1 245 B B +ATOM 7266 O O . PRO B 1 245 ? -18.290 55.930 36.201 1.0 100.0 ? ? ? ? ? ? 362 PRO B O 1 245 B B +ATOM 7267 C CB . PRO B 1 245 ? -21.151 56.934 37.287 1.0 100.0 ? ? ? ? ? ? 362 PRO B CB 1 245 B B +ATOM 7268 C CG . PRO B 1 245 ? -21.505 56.828 35.836 1.0 100.0 ? ? ? ? ? ? 362 PRO B CG 1 245 B B +ATOM 7269 C CD . PRO B 1 245 ? -20.763 57.918 35.113 1.0 100.0 ? ? ? ? ? ? 362 PRO B CD 1 245 B B +ATOM 7270 N N . LYS B 1 246 ? -18.197 56.026 38.449 1.0 100.0 ? ? ? ? ? ? 363 LYS B N 1 246 B B +ATOM 7271 C CA . LYS B 1 246 ? -17.175 54.984 38.554 1.0 100.0 ? ? ? ? ? ? 363 LYS B CA 1 246 B B +ATOM 7272 C C . LYS B 1 246 ? -17.827 53.624 38.798 1.0 100.0 ? ? ? ? ? ? 363 LYS B C 1 246 B B +ATOM 7273 O O . LYS B 1 246 ? -18.153 53.265 39.933 1.0 97.58 ? ? ? ? ? ? 363 LYS B O 1 246 B B +ATOM 7274 C CB . LYS B 1 246 ? -16.187 55.316 39.681 1.0 100.0 ? ? ? ? ? ? 363 LYS B CB 1 246 B B +ATOM 7275 C CG . LYS B 1 246 ? -16.827 55.722 41.004 1.0 99.68 ? ? ? ? ? ? 363 LYS B CG 1 246 B B +ATOM 7276 C CD . LYS B 1 246 ? -16.303 57.071 41.489 1.0 100.0 ? ? ? ? ? ? 363 LYS B CD 1 246 B B +ATOM 7277 C CE . LYS B 1 246 ? -14.775 57.139 41.440 1.0 100.0 ? ? ? ? ? ? 363 LYS B CE 1 246 B B +ATOM 7278 N NZ . LYS B 1 246 ? -14.140 56.378 42.549 1.0 93.91 ? ? ? ? ? ? 363 LYS B NZ 1 246 B B +ATOM 7279 N N . LEU B 1 247 ? -18.012 52.877 37.712 1.0 100.0 ? ? ? ? ? ? 364 LEU B N 1 247 B B +ATOM 7280 C CA . LEU B 1 247 ? -18.638 51.559 37.755 1.0 100.0 ? ? ? ? ? ? 364 LEU B CA 1 247 B B +ATOM 7281 C C . LEU B 1 247 ? -17.831 50.526 38.524 1.0 100.0 ? ? ? ? ? ? 364 LEU B C 1 247 B B +ATOM 7282 O O . LEU B 1 247 ? -16.601 50.594 38.587 1.0 100.0 ? ? ? ? ? ? 364 LEU B O 1 247 B B +ATOM 7283 C CB . LEU B 1 247 ? -18.870 51.037 36.332 1.0 100.0 ? ? ? ? ? ? 364 LEU B CB 1 247 B B +ATOM 7284 C CG . LEU B 1 247 ? -19.783 51.828 35.390 1.0 100.0 ? ? ? ? ? ? 364 LEU B CG 1 247 B B +ATOM 7285 C CD1 . LEU B 1 247 ? -21.047 52.231 36.132 1.0 100.0 ? ? ? ? ? ? 364 LEU B CD1 1 247 B B +ATOM 7286 C CD2 . LEU B 1 247 ? -19.052 53.047 34.850 1.0 100.0 ? ? ? ? ? ? 364 LEU B CD2 1 247 B B +ATOM 7287 N N . LEU B 1 248 ? -18.547 49.564 39.097 1.0 100.0 ? ? ? ? ? ? 365 LEU B N 1 248 B B +ATOM 7288 C CA . LEU B 1 248 ? -17.934 48.480 39.855 1.0 100.0 ? ? ? ? ? ? 365 LEU B CA 1 248 B B +ATOM 7289 C C . LEU B 1 248 ? -18.729 47.191 39.623 1.0 100.0 ? ? ? ? ? ? 365 LEU B C 1 248 B B +ATOM 7290 O O . LEU B 1 248 ? -19.873 47.229 39.163 1.0 97.98 ? ? ? ? ? ? 365 LEU B O 1 248 B B +ATOM 7291 C CB . LEU B 1 248 ? -17.892 48.828 41.347 1.0 91.41 ? ? ? ? ? ? 365 LEU B CB 1 248 B B +ATOM 7292 C CG . LEU B 1 248 ? -16.962 49.983 41.732 1.0 87.27 ? ? ? ? ? ? 365 LEU B CG 1 248 B B +ATOM 7293 C CD1 . LEU B 1 248 ? -17.157 50.297 43.201 1.0 88.25 ? ? ? ? ? ? 365 LEU B CD1 1 248 B B +ATOM 7294 C CD2 . LEU B 1 248 ? -15.510 49.622 41.437 1.0 67.33 ? ? ? ? ? ? 365 LEU B CD2 1 248 B B +ATOM 7295 N N . PRO B 1 249 ? -18.130 46.030 39.945 1.0 100.0 ? ? ? ? ? ? 366 PRO B N 1 249 B B +ATOM 7296 C CA . PRO B 1 249 ? -18.821 44.752 39.748 1.0 100.0 ? ? ? ? ? ? 366 PRO B CA 1 249 B B +ATOM 7297 C C . PRO B 1 249 ? -19.833 44.443 40.842 1.0 100.0 ? ? ? ? ? ? 366 PRO B C 1 249 B B +ATOM 7298 O O . PRO B 1 249 ? -19.627 44.772 42.012 1.0 100.0 ? ? ? ? ? ? 366 PRO B O 1 249 B B +ATOM 7299 C CB . PRO B 1 249 ? -17.682 43.737 39.713 1.0 100.0 ? ? ? ? ? ? 366 PRO B CB 1 249 B B +ATOM 7300 C CG . PRO B 1 249 ? -16.635 44.337 40.597 1.0 100.0 ? ? ? ? ? ? 366 PRO B CG 1 249 B B +ATOM 7301 C CD . PRO B 1 249 ? -16.790 45.841 40.532 1.0 100.0 ? ? ? ? ? ? 366 PRO B CD 1 249 B B +ATOM 7302 N N . LEU B 1 250 ? -20.935 43.813 40.455 1.0 100.0 ? ? ? ? ? ? 367 LEU B N 1 250 B B +ATOM 7303 C CA . LEU B 1 250 ? -21.959 43.458 41.420 1.0 98.44 ? ? ? ? ? ? 367 LEU B CA 1 250 B B +ATOM 7304 C C . LEU B 1 250 ? -21.377 42.419 42.375 1.0 100.0 ? ? ? ? ? ? 367 LEU B C 1 250 B B +ATOM 7305 O O . LEU B 1 250 ? -21.341 41.224 42.070 1.0 100.0 ? ? ? ? ? ? 367 LEU B O 1 250 B B +ATOM 7306 C CB . LEU B 1 250 ? -23.197 42.897 40.710 1.0 98.95 ? ? ? ? ? ? 367 LEU B CB 1 250 B B +ATOM 7307 C CG . LEU B 1 250 ? -24.342 42.544 41.666 1.0 100.0 ? ? ? ? ? ? 367 LEU B CG 1 250 B B +ATOM 7308 C CD1 . LEU B 1 250 ? -24.873 43.813 42.318 1.0 100.0 ? ? ? ? ? ? 367 LEU B CD1 1 250 B B +ATOM 7309 C CD2 . LEU B 1 250 ? -25.443 41.823 40.916 1.0 100.0 ? ? ? ? ? ? 367 LEU B CD2 1 250 B B +ATOM 7310 N N . GLU B 1 251 ? -20.909 42.891 43.526 1.0 100.0 ? ? ? ? ? ? 368 GLU B N 1 251 B B +ATOM 7311 C CA . GLU B 1 251 ? -20.324 42.030 44.550 1.0 100.0 ? ? ? ? ? ? 368 GLU B CA 1 251 B B +ATOM 7312 C C . GLU B 1 251 ? -21.059 42.285 45.858 1.0 100.0 ? ? ? ? ? ? 368 GLU B C 1 251 B B +ATOM 7313 O O . GLU B 1 251 ? -20.647 43.121 46.663 1.0 100.0 ? ? ? ? ? ? 368 GLU B O 1 251 B B +ATOM 7314 C CB . GLU B 1 251 ? -18.838 42.347 44.724 1.0 100.0 ? ? ? ? ? ? 368 GLU B CB 1 251 B B +ATOM 7315 C CG . GLU B 1 251 ? -18.014 41.217 45.318 1.0 100.0 ? ? ? ? ? ? 368 GLU B CG 1 251 B B +ATOM 7316 C CD . GLU B 1 251 ? -16.525 41.520 45.305 1.0 100.0 ? ? ? ? ? ? 368 GLU B CD 1 251 B B +ATOM 7317 O OE1 . GLU B 1 251 ? -15.875 41.385 46.367 1.0 100.0 ? ? ? ? ? ? 368 GLU B OE1 1 251 B B +ATOM 7318 O OE2 . GLU B 1 251 ? -16.005 41.899 44.231 1.0 100.0 ? ? ? ? ? ? 368 GLU B OE2 1 251 B B +ATOM 7319 N N . LEU B 1 252 ? -22.152 41.556 46.058 1.0 100.0 ? ? ? ? ? ? 369 LEU B N 1 252 B B +ATOM 7320 C CA . LEU B 1 252 ? -22.987 41.698 47.250 1.0 100.0 ? ? ? ? ? ? 369 LEU B CA 1 252 B B +ATOM 7321 C C . LEU B 1 252 ? -22.245 41.812 48.581 1.0 97.87 ? ? ? ? ? ? 369 LEU B C 1 252 B B +ATOM 7322 O O . LEU B 1 252 ? -22.792 42.335 49.555 1.0 87.33 ? ? ? ? ? ? 369 LEU B O 1 252 B B +ATOM 7323 C CB . LEU B 1 252 ? -23.991 40.542 47.322 1.0 100.0 ? ? ? ? ? ? 369 LEU B CB 1 252 B B +ATOM 7324 C CG . LEU B 1 252 ? -25.182 40.672 46.364 1.0 100.0 ? ? ? ? ? ? 369 LEU B CG 1 252 B B +ATOM 7325 C CD1 . LEU B 1 252 ? -24.703 40.517 44.930 1.0 100.0 ? ? ? ? ? ? 369 LEU B CD1 1 252 B B +ATOM 7326 C CD2 . LEU B 1 252 ? -26.232 39.633 46.702 1.0 96.69 ? ? ? ? ? ? 369 LEU B CD2 1 252 B B +ATOM 7327 N N . GLU B 1 253 ? -21.010 41.323 48.629 1.0 100.0 ? ? ? ? ? ? 370 GLU B N 1 253 B B +ATOM 7328 C CA . GLU B 1 253 ? -20.232 41.388 49.859 1.0 100.0 ? ? ? ? ? ? 370 GLU B CA 1 253 B B +ATOM 7329 C C . GLU B 1 253 ? -19.931 42.834 50.237 1.0 100.0 ? ? ? ? ? ? 370 GLU B C 1 253 B B +ATOM 7330 O O . GLU B 1 253 ? -20.244 43.278 51.344 1.0 98.83 ? ? ? ? ? ? 370 GLU B O 1 253 B B +ATOM 7331 C CB . GLU B 1 253 ? -18.921 40.614 49.709 1.0 88.24 ? ? ? ? ? ? 370 GLU B CB 1 253 B B +ATOM 7332 C CG . GLU B 1 253 ? -18.566 39.781 50.932 1.0 93.23 ? ? ? ? ? ? 370 GLU B CG 1 253 B B +ATOM 7333 C CD . GLU B 1 253 ? -18.512 40.602 52.209 1.0 100.0 ? ? ? ? ? ? 370 GLU B CD 1 253 B B +ATOM 7334 O OE1 . GLU B 1 253 ? -17.436 41.161 52.512 1.0 100.0 ? ? ? ? ? ? 370 GLU B OE1 1 253 B B +ATOM 7335 O OE2 . GLU B 1 253 ? -19.545 40.686 52.910 1.0 100.0 ? ? ? ? ? ? 370 GLU B OE2 1 253 B B +ATOM 7336 N N . LYS B 1 254 ? -19.326 43.563 49.305 1.0 100.0 ? ? ? ? ? ? 371 LYS B N 1 254 B B +ATOM 7337 C CA . LYS B 1 254 ? -18.962 44.955 49.532 1.0 100.0 ? ? ? ? ? ? 371 LYS B CA 1 254 B B +ATOM 7338 C C . LYS B 1 254 ? -20.014 45.934 49.021 1.0 95.01 ? ? ? ? ? ? 371 LYS B C 1 254 B B +ATOM 7339 O O . LYS B 1 254 ? -19.826 47.150 49.082 1.0 91.53 ? ? ? ? ? ? 371 LYS B O 1 254 B B +ATOM 7340 C CB . LYS B 1 254 ? -17.613 45.241 48.870 1.0 100.0 ? ? ? ? ? ? 371 LYS B CB 1 254 B B +ATOM 7341 C CG . LYS B 1 254 ? -16.496 44.322 49.345 1.0 100.0 ? ? ? ? ? ? 371 LYS B CG 1 254 B B +ATOM 7342 C CD . LYS B 1 254 ? -16.262 44.471 50.845 1.0 100.0 ? ? ? ? ? ? 371 LYS B CD 1 254 B B +ATOM 7343 C CE . LYS B 1 254 ? -15.181 43.525 51.337 1.0 100.0 ? ? ? ? ? ? 371 LYS B CE 1 254 B B +ATOM 7344 N NZ . LYS B 1 254 ? -15.008 43.612 52.811 1.0 84.96 ? ? ? ? ? ? 371 LYS B NZ 1 254 B B +ATOM 7345 N N . THR B 1 255 ? -21.124 45.404 48.518 1.0 98.2 ? ? ? ? ? ? 372 THR B N 1 255 B B +ATOM 7346 C CA . THR B 1 255 ? -22.194 46.254 48.007 1.0 100.0 ? ? ? ? ? ? 372 THR B CA 1 255 B B +ATOM 7347 C C . THR B 1 255 ? -23.169 46.641 49.115 1.0 100.0 ? ? ? ? ? ? 372 THR B C 1 255 B B +ATOM 7348 O O . THR B 1 255 ? -23.771 47.715 49.077 1.0 97.61 ? ? ? ? ? ? 372 THR B O 1 255 B B +ATOM 7349 C CB . THR B 1 255 ? -22.994 45.556 46.890 1.0 100.0 ? ? ? ? ? ? 372 THR B CB 1 255 B B +ATOM 7350 O OG1 . THR B 1 255 ? -22.115 45.193 45.818 1.0 100.0 ? ? ? ? ? ? 372 THR B OG1 1 255 B B +ATOM 7351 C CG2 . THR B 1 255 ? -24.077 46.485 46.359 1.0 100.0 ? ? ? ? ? ? 372 THR B CG2 1 255 B B +ATOM 7352 N N . ALA B 1 256 ? -23.320 45.754 50.096 1.0 100.0 ? ? ? ? ? ? 373 ALA B N 1 256 B B +ATOM 7353 C CA . ALA B 1 256 ? -24.222 45.985 51.221 1.0 97.69 ? ? ? ? ? ? 373 ALA B CA 1 256 B B +ATOM 7354 C C . ALA B 1 256 ? -23.672 47.034 52.181 1.0 94.98 ? ? ? ? ? ? 373 ALA B C 1 256 B B +ATOM 7355 O O . ALA B 1 256 ? -24.431 47.716 52.874 1.0 84.2 ? ? ? ? ? ? 373 ALA B O 1 256 B B +ATOM 7356 C CB . ALA B 1 256 ? -24.468 44.678 51.965 1.0 91.73 ? ? ? ? ? ? 373 ALA B CB 1 256 B B +ATOM 7357 N N . ILE B 1 257 ? -22.350 47.155 52.222 1.0 100.0 ? ? ? ? ? ? 374 ILE B N 1 257 B B +ATOM 7358 C CA . ILE B 1 257 ? -21.699 48.120 53.099 1.0 100.0 ? ? ? ? ? ? 374 ILE B CA 1 257 B B +ATOM 7359 C C . ILE B 1 257 ? -21.835 49.526 52.537 1.0 98.56 ? ? ? ? ? ? 374 ILE B C 1 257 B B +ATOM 7360 O O . ILE B 1 257 ? -22.001 50.496 53.278 1.0 100.0 ? ? ? ? ? ? 374 ILE B O 1 257 B B +ATOM 7361 C CB . ILE B 1 257 ? -20.199 47.802 53.256 1.0 100.0 ? ? ? ? ? ? 374 ILE B CB 1 257 B B +ATOM 7362 C CG1 . ILE B 1 257 ? -20.021 46.349 53.708 1.0 100.0 ? ? ? ? ? ? 374 ILE B CG1 1 257 B B +ATOM 7363 C CG2 . ILE B 1 257 ? -19.563 48.762 54.252 1.0 100.0 ? ? ? ? ? ? 374 ILE B CG2 1 257 B B +ATOM 7364 C CD1 . ILE B 1 257 ? -18.670 45.759 53.368 1.0 100.0 ? ? ? ? ? ? 374 ILE B CD1 1 257 B B +ATOM 7365 N N . GLN B 1 258 ? -21.768 49.616 51.214 1.0 94.6 ? ? ? ? ? ? 375 GLN B N 1 258 B B +ATOM 7366 C CA . GLN B 1 258 ? -21.868 50.879 50.493 1.0 99.42 ? ? ? ? ? ? 375 GLN B CA 1 258 B B +ATOM 7367 C C . GLN B 1 258 ? -23.003 51.801 50.940 1.0 100.0 ? ? ? ? ? ? 375 GLN B C 1 258 B B +ATOM 7368 O O . GLN B 1 258 ? -24.168 51.407 50.950 1.0 100.0 ? ? ? ? ? ? 375 GLN B O 1 258 B B +ATOM 7369 C CB . GLN B 1 258 ? -22.019 50.594 49.002 1.0 100.0 ? ? ? ? ? ? 375 GLN B CB 1 258 B B +ATOM 7370 C CG . GLN B 1 258 ? -22.489 51.785 48.203 1.0 100.0 ? ? ? ? ? ? 375 GLN B CG 1 258 B B +ATOM 7371 C CD . GLN B 1 258 ? -21.395 52.801 47.993 1.0 100.0 ? ? ? ? ? ? 375 GLN B CD 1 258 B B +ATOM 7372 O OE1 . GLN B 1 258 ? -20.276 52.635 48.481 1.0 100.0 ? ? ? ? ? ? 375 GLN B OE1 1 258 B B +ATOM 7373 N NE2 . GLN B 1 258 ? -21.708 53.863 47.260 1.0 95.8 ? ? ? ? ? ? 375 GLN B NE2 1 258 B B +ATOM 7374 N N . ASN B 1 259 ? -22.649 53.039 51.280 1.0 100.0 ? ? ? ? ? ? 376 ASN B N 1 259 B B +ATOM 7375 C CA . ASN B 1 259 ? -23.615 54.047 51.716 1.0 100.0 ? ? ? ? ? ? 376 ASN B CA 1 259 B B +ATOM 7376 C C . ASN B 1 259 ? -23.991 54.943 50.531 1.0 100.0 ? ? ? ? ? ? 376 ASN B C 1 259 B B +ATOM 7377 O O . ASN B 1 259 ? -23.123 55.362 49.763 1.0 100.0 ? ? ? ? ? ? 376 ASN B O 1 259 B B +ATOM 7378 C CB . ASN B 1 259 ? -23.011 54.898 52.840 1.0 100.0 ? ? ? ? ? ? 376 ASN B CB 1 259 B B +ATOM 7379 C CG . ASN B 1 259 ? -24.056 55.400 53.820 1.0 100.0 ? ? ? ? ? ? 376 ASN B CG 1 259 B B +ATOM 7380 O OD1 . ASN B 1 259 ? -24.270 56.606 53.953 1.0 100.0 ? ? ? ? ? ? 376 ASN B OD1 1 259 B B +ATOM 7381 N ND2 . ASN B 1 259 ? -24.713 54.475 54.514 1.0 100.0 ? ? ? ? ? ? 376 ASN B ND2 1 259 B B +ATOM 7382 N N . TYR B 1 260 ? -25.281 55.240 50.387 1.0 100.0 ? ? ? ? ? ? 377 TYR B N 1 260 B B +ATOM 7383 C CA . TYR B 1 260 ? -25.750 56.074 49.278 1.0 100.0 ? ? ? ? ? ? 377 TYR B CA 1 260 B B +ATOM 7384 C C . TYR B 1 260 ? -26.676 57.224 49.685 1.0 100.0 ? ? ? ? ? ? 377 TYR B C 1 260 B B +ATOM 7385 O O . TYR B 1 260 ? -27.248 57.230 50.781 1.0 100.0 ? ? ? ? ? ? 377 TYR B O 1 260 B B +ATOM 7386 C CB . TYR B 1 260 ? -26.467 55.201 48.242 1.0 100.0 ? ? ? ? ? ? 377 TYR B CB 1 260 B B +ATOM 7387 C CG . TYR B 1 260 ? -27.708 54.521 48.776 1.0 100.0 ? ? ? ? ? ? 377 TYR B CG 1 260 B B +ATOM 7388 C CD1 . TYR B 1 260 ? -28.962 55.129 48.670 1.0 100.0 ? ? ? ? ? ? 377 TYR B CD1 1 260 B B +ATOM 7389 C CD2 . TYR B 1 260 ? -27.630 53.273 49.392 1.0 99.54 ? ? ? ? ? ? 377 TYR B CD2 1 260 B B +ATOM 7390 C CE1 . TYR B 1 260 ? -30.108 54.509 49.165 1.0 100.0 ? ? ? ? ? ? 377 TYR B CE1 1 260 B B +ATOM 7391 C CE2 . TYR B 1 260 ? -28.769 52.644 49.891 1.0 100.0 ? ? ? ? ? ? 377 TYR B CE2 1 260 B B +ATOM 7392 C CZ . TYR B 1 260 ? -30.006 53.267 49.773 1.0 100.0 ? ? ? ? ? ? 377 TYR B CZ 1 260 B B +ATOM 7393 O OH . TYR B 1 260 ? -31.140 52.649 50.250 1.0 96.8 ? ? ? ? ? ? 377 TYR B OH 1 260 B B +ATOM 7394 N N . THR B 1 261 ? -26.816 58.192 48.780 1.0 100.0 ? ? ? ? ? ? 378 THR B N 1 261 B B +ATOM 7395 C CA . THR B 1 261 ? -27.675 59.353 49.000 1.0 100.0 ? ? ? ? ? ? 378 THR B CA 1 261 B B +ATOM 7396 C C . THR B 1 261 ? -29.063 59.039 48.458 1.0 100.0 ? ? ? ? ? ? 378 THR B C 1 261 B B +ATOM 7397 O O . THR B 1 261 ? -29.207 58.243 47.527 1.0 100.0 ? ? ? ? ? ? 378 THR B O 1 261 B B +ATOM 7398 C CB . THR B 1 261 ? -27.144 60.608 48.271 1.0 100.0 ? ? ? ? ? ? 378 THR B CB 1 261 B B +ATOM 7399 O OG1 . THR B 1 261 ? -28.039 61.706 48.498 1.0 98.57 ? ? ? ? ? ? 378 THR B OG1 1 261 B B +ATOM 7400 C CG2 . THR B 1 261 ? -27.041 60.352 46.770 1.0 100.0 ? ? ? ? ? ? 378 THR B CG2 1 261 B B +ATOM 7401 N N . VAL B 1 262 ? -30.080 59.673 49.029 1.0 100.0 ? ? ? ? ? ? 379 VAL B N 1 262 B B +ATOM 7402 C CA . VAL B 1 262 ? -31.453 59.434 48.603 1.0 100.0 ? ? ? ? ? ? 379 VAL B CA 1 262 B B +ATOM 7403 C C . VAL B 1 262 ? -31.970 60.457 47.591 1.0 100.0 ? ? ? ? ? ? 379 VAL B C 1 262 B B +ATOM 7404 O O . VAL B 1 262 ? -32.625 60.095 46.611 1.0 100.0 ? ? ? ? ? ? 379 VAL B O 1 262 B B +ATOM 7405 C CB . VAL B 1 262 ? -32.409 59.428 49.817 1.0 100.0 ? ? ? ? ? ? 379 VAL B CB 1 262 B B +ATOM 7406 C CG1 . VAL B 1 262 ? -32.293 60.746 50.580 1.0 97.45 ? ? ? ? ? ? 379 VAL B CG1 1 262 B B +ATOM 7407 C CG2 . VAL B 1 262 ? -33.840 59.195 49.350 1.0 85.15 ? ? ? ? ? ? 379 VAL B CG2 1 262 B B +ATOM 7408 N N . THR B 1 263 ? -31.663 61.730 47.825 1.0 100.0 ? ? ? ? ? ? 380 THR B N 1 263 B B +ATOM 7409 C CA . THR B 1 263 ? -32.134 62.807 46.959 1.0 100.0 ? ? ? ? ? ? 380 THR B CA 1 263 B B +ATOM 7410 C C . THR B 1 263 ? -31.364 63.043 45.661 1.0 100.0 ? ? ? ? ? ? 380 THR B C 1 263 B B +ATOM 7411 O O . THR B 1 263 ? -31.858 63.737 44.770 1.0 89.12 ? ? ? ? ? ? 380 THR B O 1 263 B B +ATOM 7412 C CB . THR B 1 263 ? -32.173 64.149 47.723 1.0 99.55 ? ? ? ? ? ? 380 THR B CB 1 263 B B +ATOM 7413 O OG1 . THR B 1 263 ? -30.865 64.453 48.223 1.0 96.22 ? ? ? ? ? ? 380 THR B OG1 1 263 B B +ATOM 7414 C CG2 . THR B 1 263 ? -33.154 64.076 48.879 1.0 82.8 ? ? ? ? ? ? 380 THR B CG2 1 263 B B +ATOM 7415 N N . GLU B 1 264 ? -30.169 62.477 45.538 1.0 100.0 ? ? ? ? ? ? 381 GLU B N 1 264 B B +ATOM 7416 C CA . GLU B 1 264 ? -29.400 62.707 44.326 1.0 100.0 ? ? ? ? ? ? 381 GLU B CA 1 264 B B +ATOM 7417 C C . GLU B 1 264 ? -28.788 61.484 43.657 1.0 100.0 ? ? ? ? ? ? 381 GLU B C 1 264 B B +ATOM 7418 O O . GLU B 1 264 ? -28.987 60.350 44.094 1.0 100.0 ? ? ? ? ? ? 381 GLU B O 1 264 B B +ATOM 7419 C CB . GLU B 1 264 ? -28.318 63.750 44.604 1.0 100.0 ? ? ? ? ? ? 381 GLU B CB 1 264 B B +ATOM 7420 C CG . GLU B 1 264 ? -28.871 65.159 44.762 1.0 100.0 ? ? ? ? ? ? 381 GLU B CG 1 264 B B +ATOM 7421 C CD . GLU B 1 264 ? -27.800 66.161 45.127 1.0 100.0 ? ? ? ? ? ? 381 GLU B CD 1 264 B B +ATOM 7422 O OE1 . GLU B 1 264 ? -28.081 67.067 45.942 1.0 100.0 ? ? ? ? ? ? 381 GLU B OE1 1 264 B B +ATOM 7423 O OE2 . GLU B 1 264 ? -26.676 66.041 44.598 1.0 100.0 ? ? ? ? ? ? 381 GLU B OE2 1 264 B B +ATOM 7424 N N . PHE B 1 265 ? -28.045 61.743 42.582 1.0 100.0 ? ? ? ? ? ? 382 PHE B N 1 265 B B +ATOM 7425 C CA . PHE B 1 265 ? -27.394 60.707 41.781 1.0 100.0 ? ? ? ? ? ? 382 PHE B CA 1 265 B B +ATOM 7426 C C . PHE B 1 265 ? -26.262 59.980 42.499 1.0 99.99 ? ? ? ? ? ? 382 PHE B C 1 265 B B +ATOM 7427 O O . PHE B 1 265 ? -25.509 60.579 43.271 1.0 94.86 ? ? ? ? ? ? 382 PHE B O 1 265 B B +ATOM 7428 C CB . PHE B 1 265 ? -26.848 61.313 40.482 1.0 98.66 ? ? ? ? ? ? 382 PHE B CB 1 265 B B +ATOM 7429 C CG . PHE B 1 265 ? -27.906 61.893 39.571 1.0 100.0 ? ? ? ? ? ? 382 PHE B CG 1 265 B B +ATOM 7430 C CD1 . PHE B 1 265 ? -29.209 62.097 40.018 1.0 100.0 ? ? ? ? ? ? 382 PHE B CD1 1 265 B B +ATOM 7431 C CD2 . PHE B 1 265 ? -27.588 62.249 38.263 1.0 100.0 ? ? ? ? ? ? 382 PHE B CD2 1 265 B B +ATOM 7432 C CE1 . PHE B 1 265 ? -30.175 62.649 39.177 1.0 100.0 ? ? ? ? ? ? 382 PHE B CE1 1 265 B B +ATOM 7433 C CE2 . PHE B 1 265 ? -28.546 62.801 37.415 1.0 100.0 ? ? ? ? ? ? 382 PHE B CE2 1 265 B B +ATOM 7434 C CZ . PHE B 1 265 ? -29.842 63.001 37.872 1.0 100.0 ? ? ? ? ? ? 382 PHE B CZ 1 265 B B +ATOM 7435 N N . GLN B 1 266 ? -26.139 58.685 42.215 1.0 100.0 ? ? ? ? ? ? 383 GLN B N 1 266 B B +ATOM 7436 C CA . GLN B 1 266 ? -25.109 57.844 42.818 1.0 100.0 ? ? ? ? ? ? 383 GLN B CA 1 266 B B +ATOM 7437 C C . GLN B 1 266 ? -23.933 57.623 41.868 1.0 100.0 ? ? ? ? ? ? 383 GLN B C 1 266 B B +ATOM 7438 O O . GLN B 1 266 ? -24.109 57.147 40.746 1.0 98.41 ? ? ? ? ? ? 383 GLN B O 1 266 B B +ATOM 7439 C CB . GLN B 1 266 ? -25.706 56.490 43.214 1.0 99.99 ? ? ? ? ? ? 383 GLN B CB 1 266 B B +ATOM 7440 C CG . GLN B 1 266 ? -26.752 56.570 44.321 1.0 100.0 ? ? ? ? ? ? 383 GLN B CG 1 266 B B +ATOM 7441 C CD . GLN B 1 266 ? -28.109 57.018 43.811 1.0 100.0 ? ? ? ? ? ? 383 GLN B CD 1 266 B B +ATOM 7442 O OE1 . GLN B 1 266 ? -28.874 57.674 44.524 1.0 100.0 ? ? ? ? ? ? 383 GLN B OE1 1 266 B B +ATOM 7443 N NE2 . GLN B 1 266 ? -28.416 56.665 42.568 1.0 100.0 ? ? ? ? ? ? 383 GLN B NE2 1 266 B B +ATOM 7444 N N . PRO B 1 267 ? -22.708 57.951 42.318 1.0 100.0 ? ? ? ? ? ? 384 PRO B N 1 267 B B +ATOM 7445 C CA . PRO B 1 267 ? -21.526 57.769 41.465 1.0 100.0 ? ? ? ? ? ? 384 PRO B CA 1 267 B B +ATOM 7446 C C . PRO B 1 267 ? -21.255 56.288 41.239 1.0 100.0 ? ? ? ? ? ? 384 PRO B C 1 267 B B +ATOM 7447 O O . PRO B 1 267 ? -20.595 55.902 40.273 1.0 91.07 ? ? ? ? ? ? 384 PRO B O 1 267 B B +ATOM 7448 C CB . PRO B 1 267 ? -20.406 58.450 42.248 1.0 100.0 ? ? ? ? ? ? 384 PRO B CB 1 267 B B +ATOM 7449 C CG . PRO B 1 267 ? -20.860 58.391 43.672 1.0 100.0 ? ? ? ? ? ? 384 PRO B CG 1 267 B B +ATOM 7450 C CD . PRO B 1 267 ? -22.360 58.469 43.651 1.0 100.0 ? ? ? ? ? ? 384 PRO B CD 1 267 B B +ATOM 7451 N N . LEU B 1 268 ? -21.794 55.471 42.139 1.0 100.0 ? ? ? ? ? ? 385 LEU B N 1 268 B B +ATOM 7452 C CA . LEU B 1 268 ? -21.630 54.026 42.075 1.0 100.0 ? ? ? ? ? ? 385 LEU B CA 1 268 B B +ATOM 7453 C C . LEU B 1 268 ? -22.867 53.327 41.518 1.0 100.0 ? ? ? ? ? ? 385 LEU B C 1 268 B B +ATOM 7454 O O . LEU B 1 268 ? -23.995 53.578 41.958 1.0 100.0 ? ? ? ? ? ? 385 LEU B O 1 268 B B +ATOM 7455 C CB . LEU B 1 268 ? -21.319 53.467 43.470 1.0 100.0 ? ? ? ? ? ? 385 LEU B CB 1 268 B B +ATOM 7456 C CG . LEU B 1 268 ? -19.878 53.537 43.991 1.0 100.0 ? ? ? ? ? ? 385 LEU B CG 1 268 B B +ATOM 7457 C CD1 . LEU B 1 268 ? -19.696 52.454 45.040 1.0 93.37 ? ? ? ? ? ? 385 LEU B CD1 1 268 B B +ATOM 7458 C CD2 . LEU B 1 268 ? -18.867 53.350 42.860 1.0 98.7 ? ? ? ? ? ? 385 LEU B CD2 1 268 B B +ATOM 7459 N N . TYR B 1 269 ? -22.634 52.459 40.536 1.0 100.0 ? ? ? ? ? ? 386 TYR B N 1 269 B B +ATOM 7460 C CA . TYR B 1 269 ? -23.679 51.667 39.889 1.0 100.0 ? ? ? ? ? ? 386 TYR B CA 1 269 B B +ATOM 7461 C C . TYR B 1 269 ? -23.063 50.289 39.635 1.0 100.0 ? ? ? ? ? ? 386 TYR B C 1 269 B B +ATOM 7462 O O . TYR B 1 269 ? -22.306 50.107 38.679 1.0 87.69 ? ? ? ? ? ? 386 TYR B O 1 269 B B +ATOM 7463 C CB . TYR B 1 269 ? -24.094 52.288 38.546 1.0 100.0 ? ? ? ? ? ? 386 TYR B CB 1 269 B B +ATOM 7464 C CG . TYR B 1 269 ? -24.846 53.603 38.634 1.0 100.0 ? ? ? ? ? ? 386 TYR B CG 1 269 B B +ATOM 7465 C CD1 . TYR B 1 269 ? -24.363 54.739 37.984 1.0 100.0 ? ? ? ? ? ? 386 TYR B CD1 1 269 B B +ATOM 7466 C CD2 . TYR B 1 269 ? -26.059 53.705 39.329 1.0 100.0 ? ? ? ? ? ? 386 TYR B CD2 1 269 B B +ATOM 7467 C CE1 . TYR B 1 269 ? -25.063 55.942 38.017 1.0 100.0 ? ? ? ? ? ? 386 TYR B CE1 1 269 B B +ATOM 7468 C CE2 . TYR B 1 269 ? -26.769 54.908 39.367 1.0 99.27 ? ? ? ? ? ? 386 TYR B CE2 1 269 B B +ATOM 7469 C CZ . TYR B 1 269 ? -26.264 56.020 38.706 1.0 100.0 ? ? ? ? ? ? 386 TYR B CZ 1 269 B B +ATOM 7470 O OH . TYR B 1 269 ? -26.963 57.204 38.724 1.0 89.53 ? ? ? ? ? ? 386 TYR B OH 1 269 B B +ATOM 7471 N N . TYR B 1 270 ? -23.381 49.326 40.496 1.0 100.0 ? ? ? ? ? ? 387 TYR B N 1 270 B B +ATOM 7472 C CA . TYR B 1 270 ? -22.841 47.975 40.361 1.0 100.0 ? ? ? ? ? ? 387 TYR B CA 1 270 B B +ATOM 7473 C C . TYR B 1 270 ? -23.339 47.253 39.115 1.0 100.0 ? ? ? ? ? ? 387 TYR B C 1 270 B B +ATOM 7474 O O . TYR B 1 270 ? -24.541 47.049 38.935 1.0 100.0 ? ? ? ? ? ? 387 TYR B O 1 270 B B +ATOM 7475 C CB . TYR B 1 270 ? -23.168 47.150 41.608 1.0 100.0 ? ? ? ? ? ? 387 TYR B CB 1 270 B B +ATOM 7476 C CG . TYR B 1 270 ? -22.478 47.678 42.837 1.0 98.77 ? ? ? ? ? ? 387 TYR B CG 1 270 B B +ATOM 7477 C CD1 . TYR B 1 270 ? -22.939 48.831 43.472 1.0 100.0 ? ? ? ? ? ? 387 TYR B CD1 1 270 B B +ATOM 7478 C CD2 . TYR B 1 270 ? -21.340 47.055 43.344 1.0 100.0 ? ? ? ? ? ? 387 TYR B CD2 1 270 B B +ATOM 7479 C CE1 . TYR B 1 270 ? -22.281 49.356 44.579 1.0 100.0 ? ? ? ? ? ? 387 TYR B CE1 1 270 B B +ATOM 7480 C CE2 . TYR B 1 270 ? -20.674 47.571 44.453 1.0 100.0 ? ? ? ? ? ? 387 TYR B CE2 1 270 B B +ATOM 7481 C CZ . TYR B 1 270 ? -21.150 48.723 45.065 1.0 100.0 ? ? ? ? ? ? 387 TYR B CZ 1 270 B B +ATOM 7482 O OH . TYR B 1 270 ? -20.498 49.252 46.158 1.0 100.0 ? ? ? ? ? ? 387 TYR B OH 1 270 B B +ATOM 7483 N N . VAL B 1 271 ? -22.392 46.859 38.266 1.0 100.0 ? ? ? ? ? ? 388 VAL B N 1 271 B B +ATOM 7484 C CA . VAL B 1 271 ? -22.698 46.170 37.016 1.0 100.0 ? ? ? ? ? ? 388 VAL B CA 1 271 B B +ATOM 7485 C C . VAL B 1 271 ? -22.828 44.655 37.165 1.0 100.0 ? ? ? ? ? ? 388 VAL B C 1 271 B B +ATOM 7486 O O . VAL B 1 271 ? -21.831 43.953 37.350 1.0 100.0 ? ? ? ? ? ? 388 VAL B O 1 271 B B +ATOM 7487 C CB . VAL B 1 271 ? -21.614 46.463 35.957 1.0 100.0 ? ? ? ? ? ? 388 VAL B CB 1 271 B B +ATOM 7488 C CG1 . VAL B 1 271 ? -21.993 45.821 34.630 1.0 100.0 ? ? ? ? ? ? 388 VAL B CG1 1 271 B B +ATOM 7489 C CG2 . VAL B 1 271 ? -21.437 47.967 35.801 1.0 96.31 ? ? ? ? ? ? 388 VAL B CG2 1 271 B B +ATOM 7490 N N . ALA B 1 272 ? -24.061 44.160 37.077 1.0 100.0 ? ? ? ? ? ? 389 ALA B N 1 272 B B +ATOM 7491 C CA . ALA B 1 272 ? -24.330 42.729 37.185 1.0 100.0 ? ? ? ? ? ? 389 ALA B CA 1 272 B B +ATOM 7492 C C . ALA B 1 272 ? -24.231 42.069 35.813 1.0 100.0 ? ? ? ? ? ? 389 ALA B C 1 272 B B +ATOM 7493 O O . ALA B 1 272 ? -24.646 42.643 34.802 1.0 100.0 ? ? ? ? ? ? 389 ALA B O 1 272 B B +ATOM 7494 C CB . ALA B 1 272 ? -25.718 42.498 37.764 1.0 100.0 ? ? ? ? ? ? 389 ALA B CB 1 272 B B +ATOM 7495 N N . GLU B 1 273 ? -23.670 40.866 35.780 1.0 100.0 ? ? ? ? ? ? 390 GLU B N 1 273 B B +ATOM 7496 C CA . GLU B 1 273 ? -23.536 40.137 34.527 1.0 100.0 ? ? ? ? ? ? 390 GLU B CA 1 273 B B +ATOM 7497 C C . GLU B 1 273 ? -24.935 39.874 33.987 1.0 100.0 ? ? ? ? ? ? 390 GLU B C 1 273 B B +ATOM 7498 O O . GLU B 1 273 ? -25.251 40.212 32.846 1.0 100.0 ? ? ? ? ? ? 390 GLU B O 1 273 B B +ATOM 7499 C CB . GLU B 1 273 ? -22.810 38.811 34.763 1.0 100.0 ? ? ? ? ? ? 390 GLU B CB 1 273 B B +ATOM 7500 C CG . GLU B 1 273 ? -21.389 38.972 35.270 1.0 100.0 ? ? ? ? ? ? 390 GLU B CG 1 273 B B +ATOM 7501 C CD . GLU B 1 273 ? -20.652 37.647 35.374 1.0 100.0 ? ? ? ? ? ? 390 GLU B CD 1 273 B B +ATOM 7502 O OE1 . GLU B 1 273 ? -21.275 36.594 35.115 1.0 90.81 ? ? ? ? ? ? 390 GLU B OE1 1 273 B B +ATOM 7503 O OE2 . GLU B 1 273 ? -19.448 37.661 35.716 1.0 100.0 ? ? ? ? ? ? 390 GLU B OE2 1 273 B B +ATOM 7504 N N . SER B 1 274 ? -25.771 39.276 34.829 1.0 90.63 ? ? ? ? ? ? 391 SER B N 1 274 B B +ATOM 7505 C CA . SER B 1 274 ? -27.141 38.960 34.458 1.0 94.47 ? ? ? ? ? ? 391 SER B CA 1 274 B B +ATOM 7506 C C . SER B 1 274 ? -27.980 38.802 35.718 1.0 99.76 ? ? ? ? ? ? 391 SER B C 1 274 B B +ATOM 7507 O O . SER B 1 274 ? -27.444 38.736 36.824 1.0 100.0 ? ? ? ? ? ? 391 SER B O 1 274 B B +ATOM 7508 C CB . SER B 1 274 ? -27.179 37.665 33.642 1.0 93.37 ? ? ? ? ? ? 391 SER B CB 1 274 B B +ATOM 7509 O OG . SER B 1 274 ? -28.460 37.454 33.071 1.0 100.0 ? ? ? ? ? ? 391 SER B OG 1 274 B B +ATOM 7510 N N . PHE B 1 275 ? -29.297 38.755 35.546 1.0 99.74 ? ? ? ? ? ? 392 PHE B N 1 275 B B +ATOM 7511 C CA . PHE B 1 275 ? -30.208 38.592 36.673 1.0 93.22 ? ? ? ? ? ? 392 PHE B CA 1 275 B B +ATOM 7512 C C . PHE B 1 275 ? -30.104 37.152 37.151 1.0 96.1 ? ? ? ? ? ? 392 PHE B C 1 275 B B +ATOM 7513 O O . PHE B 1 275 ? -30.234 36.870 38.340 1.0 100.0 ? ? ? ? ? ? 392 PHE B O 1 275 B B +ATOM 7514 C CB . PHE B 1 275 ? -31.636 38.913 36.239 1.0 82.66 ? ? ? ? ? ? 392 PHE B CB 1 275 B B +ATOM 7515 C CG . PHE B 1 275 ? -31.727 40.079 35.298 1.0 93.42 ? ? ? ? ? ? 392 PHE B CG 1 275 B B +ATOM 7516 C CD1 . PHE B 1 275 ? -32.138 39.898 33.982 1.0 100.0 ? ? ? ? ? ? 392 PHE B CD1 1 275 B B +ATOM 7517 C CD2 . PHE B 1 275 ? -31.384 41.359 35.723 1.0 84.08 ? ? ? ? ? ? 392 PHE B CD2 1 275 B B +ATOM 7518 C CE1 . PHE B 1 275 ? -32.207 40.977 33.102 1.0 96.84 ? ? ? ? ? ? 392 PHE B CE1 1 275 B B +ATOM 7519 C CE2 . PHE B 1 275 ? -31.449 42.443 34.853 1.0 78.21 ? ? ? ? ? ? 392 PHE B CE2 1 275 B B +ATOM 7520 C CZ . PHE B 1 275 ? -31.860 42.253 33.540 1.0 87.99 ? ? ? ? ? ? 392 PHE B CZ 1 275 B B +ATOM 7521 N N . ASN B 1 276 ? -29.861 36.249 36.206 1.0 99.16 ? ? ? ? ? ? 393 ASN B N 1 276 B B +ATOM 7522 C CA . ASN B 1 276 ? -29.706 34.829 36.501 1.0 100.0 ? ? ? ? ? ? 393 ASN B CA 1 276 B B +ATOM 7523 C C . ASN B 1 276 ? -28.422 34.676 37.308 1.0 100.0 ? ? ? ? ? ? 393 ASN B C 1 276 B B +ATOM 7524 O O . ASN B 1 276 ? -28.301 33.810 38.181 1.0 95.97 ? ? ? ? ? ? 393 ASN B O 1 276 B B +ATOM 7525 C CB . ASN B 1 276 ? -29.574 34.046 35.193 1.0 100.0 ? ? ? ? ? ? 393 ASN B CB 1 276 B B +ATOM 7526 C CG . ASN B 1 276 ? -29.818 32.563 35.374 1.0 100.0 ? ? ? ? ? ? 393 ASN B CG 1 276 B B +ATOM 7527 O OD1 . ASN B 1 276 ? -29.332 31.949 36.326 1.0 100.0 ? ? ? ? ? ? 393 ASN B OD1 1 276 B B +ATOM 7528 N ND2 . ASN B 1 276 ? -30.578 31.976 34.454 1.0 100.0 ? ? ? ? ? ? 393 ASN B ND2 1 276 B B +ATOM 7529 N N . ASP B 1 277 ? -27.474 35.555 36.985 1.0 100.0 ? ? ? ? ? ? 394 ASP B N 1 277 B B +ATOM 7530 C CA . ASP B 1 277 ? -26.154 35.608 37.599 1.0 100.0 ? ? ? ? ? ? 394 ASP B CA 1 277 B B +ATOM 7531 C C . ASP B 1 277 ? -26.165 36.363 38.930 1.0 98.41 ? ? ? ? ? ? 394 ASP B C 1 277 B B +ATOM 7532 O O . ASP B 1 277 ? -25.612 35.884 39.925 1.0 76.46 ? ? ? ? ? ? 394 ASP B O 1 277 B B +ATOM 7533 C CB . ASP B 1 277 ? -25.181 36.266 36.615 1.0 100.0 ? ? ? ? ? ? 394 ASP B CB 1 277 B B +ATOM 7534 C CG . ASP B 1 277 ? -24.139 37.121 37.303 1.0 100.0 ? ? ? ? ? ? 394 ASP B CG 1 277 B B +ATOM 7535 O OD1 . ASP B 1 277 ? -23.088 36.566 37.686 1.0 100.0 ? ? ? ? ? ? 394 ASP B OD1 1 277 B B +ATOM 7536 O OD2 . ASP B 1 277 ? -24.369 38.341 37.458 1.0 94.84 ? ? ? ? ? ? 394 ASP B OD2 1 277 B B +ATOM 7537 N N . ALA B 1 278 ? -26.777 37.545 38.947 1.0 96.6 ? ? ? ? ? ? 395 ALA B N 1 278 B B +ATOM 7538 C CA . ALA B 1 278 ? -26.866 38.331 40.176 1.0 93.92 ? ? ? ? ? ? 395 ALA B CA 1 278 B B +ATOM 7539 C C . ALA B 1 278 ? -27.545 37.430 41.202 1.0 99.31 ? ? ? ? ? ? 395 ALA B C 1 278 B B +ATOM 7540 O O . ALA B 1 278 ? -27.199 37.420 42.385 1.0 99.13 ? ? ? ? ? ? 395 ALA B O 1 278 B B +ATOM 7541 C CB . ALA B 1 278 ? -27.701 39.591 39.946 1.0 72.96 ? ? ? ? ? ? 395 ALA B CB 1 278 B B +ATOM 7542 N N . LYS B 1 279 ? -28.504 36.656 40.708 1.0 100.0 ? ? ? ? ? ? 396 LYS B N 1 279 B B +ATOM 7543 C CA . LYS B 1 279 ? -29.276 35.721 41.515 1.0 100.0 ? ? ? ? ? ? 396 LYS B CA 1 279 B B +ATOM 7544 C C . LYS B 1 279 ? -28.398 34.840 42.395 1.0 96.15 ? ? ? ? ? ? 396 LYS B C 1 279 B B +ATOM 7545 O O . LYS B 1 279 ? -28.729 34.582 43.553 1.0 96.56 ? ? ? ? ? ? 396 LYS B O 1 279 B B +ATOM 7546 C CB . LYS B 1 279 ? -30.118 34.838 40.591 1.0 96.26 ? ? ? ? ? ? 396 LYS B CB 1 279 B B +ATOM 7547 C CG . LYS B 1 279 ? -30.888 33.736 41.284 1.0 100.0 ? ? ? ? ? ? 396 LYS B CG 1 279 B B +ATOM 7548 C CD . LYS B 1 279 ? -31.774 33.014 40.286 1.0 95.0 ? ? ? ? ? ? 396 LYS B CD 1 279 B B +ATOM 7549 C CE . LYS B 1 279 ? -32.632 31.972 40.969 1.0 100.0 ? ? ? ? ? ? 396 LYS B CE 1 279 B B +ATOM 7550 N NZ . LYS B 1 279 ? -31.803 30.870 41.524 1.0 100.0 ? ? ? ? ? ? 396 LYS B NZ 1 279 B B +ATOM 7551 N N . GLU B 1 280 ? -27.282 34.383 41.839 1.0 90.43 ? ? ? ? ? ? 397 GLU B N 1 280 B B +ATOM 7552 C CA . GLU B 1 280 ? -26.368 33.513 42.569 1.0 99.6 ? ? ? ? ? ? 397 GLU B CA 1 280 B B +ATOM 7553 C C . GLU B 1 280 ? -25.544 34.204 43.655 1.0 100.0 ? ? ? ? ? ? 397 GLU B C 1 280 B B +ATOM 7554 O O . GLU B 1 280 ? -25.231 33.598 44.680 1.0 100.0 ? ? ? ? ? ? 397 GLU B O 1 280 B B +ATOM 7555 C CB . GLU B 1 280 ? -25.455 32.798 41.578 1.0 93.35 ? ? ? ? ? ? 397 GLU B CB 1 280 B B +ATOM 7556 C CG . GLU B 1 280 ? -26.223 31.976 40.551 1.0 100.0 ? ? ? ? ? ? 397 GLU B CG 1 280 B B +ATOM 7557 C CD . GLU B 1 280 ? -27.115 30.924 41.195 1.0 100.0 ? ? ? ? ? ? 397 GLU B CD 1 280 B B +ATOM 7558 O OE1 . GLU B 1 280 ? -26.661 30.270 42.158 1.0 100.0 ? ? ? ? ? ? 397 GLU B OE1 1 280 B B +ATOM 7559 O OE2 . GLU B 1 280 ? -28.265 30.745 40.739 1.0 94.05 ? ? ? ? ? ? 397 GLU B OE2 1 280 B B +ATOM 7560 N N . LYS B 1 281 ? -25.173 35.460 43.432 1.0 100.0 ? ? ? ? ? ? 398 LYS B N 1 281 B B +ATOM 7561 C CA . LYS B 1 281 ? -24.419 36.186 44.452 1.0 95.06 ? ? ? ? ? ? 398 LYS B CA 1 281 B B +ATOM 7562 C C . LYS B 1 281 ? -25.435 36.580 45.527 1.0 87.87 ? ? ? ? ? ? 398 LYS B C 1 281 B B +ATOM 7563 O O . LYS B 1 281 ? -25.099 36.776 46.700 1.0 73.44 ? ? ? ? ? ? 398 LYS B O 1 281 B B +ATOM 7564 C CB . LYS B 1 281 ? -23.753 37.440 43.865 1.0 83.62 ? ? ? ? ? ? 398 LYS B CB 1 281 B B +ATOM 7565 C CG . LYS B 1 281 ? -24.212 37.836 42.465 1.0 72.13 ? ? ? ? ? ? 398 LYS B CG 1 281 B B +ATOM 7566 C CD . LYS B 1 281 ? -23.214 38.802 41.842 1.0 71.94 ? ? ? ? ? ? 398 LYS B CD 1 281 B B +ATOM 7567 C CE . LYS B 1 281 ? -23.507 39.044 40.373 1.0 67.41 ? ? ? ? ? ? 398 LYS B CE 1 281 B B +ATOM 7568 N NZ . LYS B 1 281 ? -22.359 39.677 39.656 1.0 66.81 ? ? ? ? ? ? 398 LYS B NZ 1 281 B B +ATOM 7569 N N . VAL B 1 282 ? -26.689 36.684 45.103 1.0 79.57 ? ? ? ? ? ? 399 VAL B N 1 282 B B +ATOM 7570 C CA . VAL B 1 282 ? -27.787 37.028 45.993 1.0 80.28 ? ? ? ? ? ? 399 VAL B CA 1 282 B B +ATOM 7571 C C . VAL B 1 282 ? -28.052 35.830 46.887 1.0 82.73 ? ? ? ? ? ? 399 VAL B C 1 282 B B +ATOM 7572 O O . VAL B 1 282 ? -28.169 35.958 48.104 1.0 82.05 ? ? ? ? ? ? 399 VAL B O 1 282 B B +ATOM 7573 C CB . VAL B 1 282 ? -29.052 37.354 45.185 1.0 85.05 ? ? ? ? ? ? 399 VAL B CB 1 282 B B +ATOM 7574 C CG1 . VAL B 1 282 ? -30.286 37.345 46.083 1.0 72.36 ? ? ? ? ? ? 399 VAL B CG1 1 282 B B +ATOM 7575 C CG2 . VAL B 1 282 ? -28.885 38.699 44.526 1.0 95.57 ? ? ? ? ? ? 399 VAL B CG2 1 282 B B +ATOM 7576 N N . ARG B 1 283 ? -28.160 34.664 46.262 1.0 92.2 ? ? ? ? ? ? 400 ARG B N 1 283 B B +ATOM 7577 C CA . ARG B 1 283 ? -28.385 33.430 46.995 1.0 96.0 ? ? ? ? ? ? 400 ARG B CA 1 283 B B +ATOM 7578 C C . ARG B 1 283 ? -27.243 33.317 47.986 1.0 94.18 ? ? ? ? ? ? 400 ARG B C 1 283 B B +ATOM 7579 O O . ARG B 1 283 ? -27.433 32.929 49.138 1.0 93.17 ? ? ? ? ? ? 400 ARG B O 1 283 B B +ATOM 7580 C CB . ARG B 1 283 ? -28.362 32.233 46.041 1.0 100.0 ? ? ? ? ? ? 400 ARG B CB 1 283 B B +ATOM 7581 C CG . ARG B 1 283 ? -29.705 31.924 45.399 1.0 100.0 ? ? ? ? ? ? 400 ARG B CG 1 283 B B +ATOM 7582 C CD . ARG B 1 283 ? -29.788 30.477 44.949 1.0 100.0 ? ? ? ? ? ? 400 ARG B CD 1 283 B B +ATOM 7583 N NE . ARG B 1 283 ? -29.609 29.557 46.069 1.0 100.0 ? ? ? ? ? ? 400 ARG B NE 1 283 B B +ATOM 7584 C CZ . ARG B 1 283 ? -30.592 28.861 46.627 1.0 100.0 ? ? ? ? ? ? 400 ARG B CZ 1 283 B B +ATOM 7585 N NH1 . ARG B 1 283 ? -31.836 28.981 46.177 1.0 93.15 ? ? ? ? ? ? 400 ARG B NH1 1 283 B B +ATOM 7586 N NH2 . ARG B 1 283 ? -30.332 28.046 47.640 1.0 100.0 ? ? ? ? ? ? 400 ARG B NH2 1 283 B B +ATOM 7587 N N . ASN B 1 284 ? -26.048 33.659 47.513 1.0 93.64 ? ? ? ? ? ? 401 ASN B N 1 284 B B +ATOM 7588 C CA . ASN B 1 284 ? -24.851 33.624 48.338 1.0 100.0 ? ? ? ? ? ? 401 ASN B CA 1 284 B B +ATOM 7589 C C . ASN B 1 284 ? -25.051 34.576 49.506 1.0 100.0 ? ? ? ? ? ? 401 ASN B C 1 284 B B +ATOM 7590 O O . ASN B 1 284 ? -24.904 34.192 50.668 1.0 100.0 ? ? ? ? ? ? 401 ASN B O 1 284 B B +ATOM 7591 C CB . ASN B 1 284 ? -23.631 34.053 47.522 1.0 100.0 ? ? ? ? ? ? 401 ASN B CB 1 284 B B +ATOM 7592 C CG . ASN B 1 284 ? -22.785 32.878 47.081 1.0 100.0 ? ? ? ? ? ? 401 ASN B CG 1 284 B B +ATOM 7593 O OD1 . ASN B 1 284 ? -21.574 33.002 46.900 1.0 100.0 ? ? ? ? ? ? 401 ASN B OD1 1 284 B B +ATOM 7594 N ND2 . ASN B 1 284 ? -23.422 31.723 46.909 1.0 100.0 ? ? ? ? ? ? 401 ASN B ND2 1 284 B B +ATOM 7595 N N . PHE B 1 285 ? -25.382 35.824 49.184 1.0 93.04 ? ? ? ? ? ? 402 PHE B N 1 285 B B +ATOM 7596 C CA . PHE B 1 285 ? -25.625 36.836 50.204 1.0 91.07 ? ? ? ? ? ? 402 PHE B CA 1 285 B B +ATOM 7597 C C . PHE B 1 285 ? -26.781 36.348 51.064 1.0 92.04 ? ? ? ? ? ? 402 PHE B C 1 285 B B +ATOM 7598 O O . PHE B 1 285 ? -26.919 36.732 52.227 1.0 74.85 ? ? ? ? ? ? 402 PHE B O 1 285 B B +ATOM 7599 C CB . PHE B 1 285 ? -25.997 38.168 49.557 1.0 86.42 ? ? ? ? ? ? 402 PHE B CB 1 285 B B +ATOM 7600 C CG . PHE B 1 285 ? -25.881 39.344 50.481 1.0 94.63 ? ? ? ? ? ? 402 PHE B CG 1 285 B B +ATOM 7601 C CD1 . PHE B 1 285 ? -24.634 39.795 50.893 1.0 96.48 ? ? ? ? ? ? 402 PHE B CD1 1 285 B B +ATOM 7602 C CD2 . PHE B 1 285 ? -27.016 40.004 50.939 1.0 98.63 ? ? ? ? ? ? 402 PHE B CD2 1 285 B B +ATOM 7603 C CE1 . PHE B 1 285 ? -24.517 40.889 51.746 1.0 97.75 ? ? ? ? ? ? 402 PHE B CE1 1 285 B B +ATOM 7604 C CE2 . PHE B 1 285 ? -26.910 41.099 51.793 1.0 98.92 ? ? ? ? ? ? 402 PHE B CE2 1 285 B B +ATOM 7605 C CZ . PHE B 1 285 ? -25.659 41.541 52.197 1.0 93.38 ? ? ? ? ? ? 402 PHE B CZ 1 285 B B +ATOM 7606 N N . ALA B 1 286 ? -27.613 35.501 50.467 1.0 91.11 ? ? ? ? ? ? 403 ALA B N 1 286 B B +ATOM 7607 C CA . ALA B 1 286 ? -28.760 34.928 51.151 1.0 78.32 ? ? ? ? ? ? 403 ALA B CA 1 286 B B +ATOM 7608 C C . ALA B 1 286 ? -28.242 33.843 52.081 1.0 75.97 ? ? ? ? ? ? 403 ALA B C 1 286 B B +ATOM 7609 O O . ALA B 1 286 ? -28.704 33.709 53.213 1.0 91.47 ? ? ? ? ? ? 403 ALA B O 1 286 B B +ATOM 7610 C CB . ALA B 1 286 ? -29.733 34.335 50.141 1.0 59.2 ? ? ? ? ? ? 403 ALA B CB 1 286 B B +ATOM 7611 N N . ALA B 1 287 ? -27.277 33.068 51.595 1.0 56.75 ? ? ? ? ? ? 404 ALA B N 1 287 B B +ATOM 7612 C CA . ALA B 1 287 ? -26.691 32.002 52.395 1.0 62.82 ? ? ? ? ? ? 404 ALA B CA 1 287 B B +ATOM 7613 C C . ALA B 1 287 ? -25.909 32.653 53.522 1.0 68.19 ? ? ? ? ? ? 404 ALA B C 1 287 B B +ATOM 7614 O O . ALA B 1 287 ? -25.646 32.036 54.556 1.0 76.83 ? ? ? ? ? ? 404 ALA B O 1 287 B B +ATOM 7615 C CB . ALA B 1 287 ? -25.772 31.147 51.544 1.0 78.44 ? ? ? ? ? ? 404 ALA B CB 1 287 B B +ATOM 7616 N N . THR B 1 288 ? -25.539 33.912 53.309 1.0 62.58 ? ? ? ? ? ? 405 THR B N 1 288 B B +ATOM 7617 C CA . THR B 1 288 ? -24.802 34.671 54.314 1.0 75.32 ? ? ? ? ? ? 405 THR B CA 1 288 B B +ATOM 7618 C C . THR B 1 288 ? -25.749 35.002 55.471 1.0 72.06 ? ? ? ? ? ? 405 THR B C 1 288 B B +ATOM 7619 O O . THR B 1 288 ? -25.349 35.016 56.637 1.0 73.32 ? ? ? ? ? ? 405 THR B O 1 288 B B +ATOM 7620 C CB . THR B 1 288 ? -24.254 35.989 53.728 1.0 73.78 ? ? ? ? ? ? 405 THR B CB 1 288 B B +ATOM 7621 O OG1 . THR B 1 288 ? -23.637 35.728 52.463 1.0 95.88 ? ? ? ? ? ? 405 THR B OG1 1 288 B B +ATOM 7622 C CG2 . THR B 1 288 ? -23.230 36.602 54.673 1.0 67.17 ? ? ? ? ? ? 405 THR B CG2 1 288 B B +ATOM 7623 N N . ILE B 1 289 ? -27.006 35.265 55.128 1.0 57.19 ? ? ? ? ? ? 406 ILE B N 1 289 B B +ATOM 7624 C CA . ILE B 1 289 ? -28.027 35.596 56.113 1.0 54.5 ? ? ? ? ? ? 406 ILE B CA 1 289 B B +ATOM 7625 C C . ILE B 1 289 ? -28.164 34.500 57.160 1.0 55.94 ? ? ? ? ? ? 406 ILE B C 1 289 B B +ATOM 7626 O O . ILE B 1 289 ? -28.687 33.415 56.883 1.0 57.55 ? ? ? ? ? ? 406 ILE B O 1 289 B B +ATOM 7627 C CB . ILE B 1 289 ? -29.407 35.802 55.447 1.0 71.06 ? ? ? ? ? ? 406 ILE B CB 1 289 B B +ATOM 7628 C CG1 . ILE B 1 289 ? -29.247 36.639 54.173 1.0 65.5 ? ? ? ? ? ? 406 ILE B CG1 1 289 B B +ATOM 7629 C CG2 . ILE B 1 289 ? -30.365 36.464 56.435 1.0 59.64 ? ? ? ? ? ? 406 ILE B CG2 1 289 B B +ATOM 7630 C CD1 . ILE B 1 289 ? -28.596 37.991 54.386 1.0 69.61 ? ? ? ? ? ? 406 ILE B CD1 1 289 B B +ATOM 7631 N N . PRO B 1 290 ? -27.716 34.779 58.391 1.0 54.54 ? ? ? ? ? ? 407 PRO B N 1 290 B B +ATOM 7632 C CA . PRO B 1 290 ? -27.789 33.812 59.489 1.0 49.13 ? ? ? ? ? ? 407 PRO B CA 1 290 B B +ATOM 7633 C C . PRO B 1 290 ? -29.197 33.673 60.073 1.0 47.38 ? ? ? ? ? ? 407 PRO B C 1 290 B B +ATOM 7634 O O . PRO B 1 290 ? -29.612 34.476 60.907 1.0 52.3 ? ? ? ? ? ? 407 PRO B O 1 290 B B +ATOM 7635 C CB . PRO B 1 290 ? -26.785 34.353 60.514 1.0 50.96 ? ? ? ? ? ? 407 PRO B CB 1 290 B B +ATOM 7636 C CG . PRO B 1 290 ? -26.207 35.625 59.904 1.0 61.37 ? ? ? ? ? ? 407 PRO B CG 1 290 B B +ATOM 7637 C CD . PRO B 1 290 ? -27.131 36.052 58.827 1.0 58.57 ? ? ? ? ? ? 407 PRO B CD 1 290 B B +ATOM 7638 N N . ARG B 1 291 ? -29.919 32.648 59.621 1.0 48.85 ? ? ? ? ? ? 408 ARG B N 1 291 B B +ATOM 7639 C CA . ARG B 1 291 ? -31.278 32.349 60.083 1.0 56.74 ? ? ? ? ? ? 408 ARG B CA 1 291 B B +ATOM 7640 C C . ARG B 1 291 ? -31.277 30.963 60.727 1.0 59.82 ? ? ? ? ? ? 408 ARG B C 1 291 B B +ATOM 7641 O O . ARG B 1 291 ? -30.673 30.032 60.194 1.0 73.93 ? ? ? ? ? ? 408 ARG B O 1 291 B B +ATOM 7642 C CB . ARG B 1 291 ? -32.258 32.353 58.902 1.0 79.31 ? ? ? ? ? ? 408 ARG B CB 1 291 B B +ATOM 7643 C CG . ARG B 1 291 ? -32.643 33.733 58.386 1.0 96.41 ? ? ? ? ? ? 408 ARG B CG 1 291 B B +ATOM 7644 C CD . ARG B 1 291 ? -34.139 33.826 58.093 1.0 89.26 ? ? ? ? ? ? 408 ARG B CD 1 291 B B +ATOM 7645 N NE . ARG B 1 291 ? -34.576 32.865 57.083 1.0 61.83 ? ? ? ? ? ? 408 ARG B NE 1 291 B B +ATOM 7646 C CZ . ARG B 1 291 ? -34.211 32.901 55.807 1.0 62.62 ? ? ? ? ? ? 408 ARG B CZ 1 291 B B +ATOM 7647 N NH1 . ARG B 1 291 ? -33.399 33.852 55.370 1.0 55.94 ? ? ? ? ? ? 408 ARG B NH1 1 291 B B +ATOM 7648 N NH2 . ARG B 1 291 ? -34.658 31.983 54.965 1.0 79.75 ? ? ? ? ? ? 408 ARG B NH2 1 291 B B +ATOM 7649 N N . PRO B 1 292 ? -31.982 30.798 61.862 1.0 50.99 ? ? ? ? ? ? 409 PRO B N 1 292 B B +ATOM 7650 C CA . PRO B 1 292 ? -32.009 29.489 62.531 1.0 53.84 ? ? ? ? ? ? 409 PRO B CA 1 292 B B +ATOM 7651 C C . PRO B 1 292 ? -32.743 28.393 61.765 1.0 64.96 ? ? ? ? ? ? 409 PRO B C 1 292 B B +ATOM 7652 O O . PRO B 1 292 ? -33.130 27.372 62.337 1.0 66.01 ? ? ? ? ? ? 409 PRO B O 1 292 B B +ATOM 7653 C CB . PRO B 1 292 ? -32.665 29.778 63.884 1.0 59.3 ? ? ? ? ? ? 409 PRO B CB 1 292 B B +ATOM 7654 C CG . PRO B 1 292 ? -32.847 31.274 63.948 1.0 71.67 ? ? ? ? ? ? 409 PRO B CG 1 292 B B +ATOM 7655 C CD . PRO B 1 292 ? -32.834 31.779 62.546 1.0 64.79 ? ? ? ? ? ? 409 PRO B CD 1 292 B B +ATOM 7656 N N . PHE B 1 293 ? -32.926 28.607 60.465 1.0 74.36 ? ? ? ? ? ? 410 PHE B N 1 293 B B +ATOM 7657 C CA . PHE B 1 293 ? -33.626 27.641 59.621 1.0 68.36 ? ? ? ? ? ? 410 PHE B CA 1 293 B B +ATOM 7658 C C . PHE B 1 293 ? -33.606 28.045 58.147 1.0 66.39 ? ? ? ? ? ? 410 PHE B C 1 293 B B +ATOM 7659 O O . PHE B 1 293 ? -32.862 28.942 57.732 1.0 56.3 ? ? ? ? ? ? 410 PHE B O 1 293 B B +ATOM 7660 C CB . PHE B 1 293 ? -35.087 27.514 60.078 1.0 63.35 ? ? ? ? ? ? 410 PHE B CB 1 293 B B +ATOM 7661 C CG . PHE B 1 293 ? -35.779 28.845 60.269 1.0 67.61 ? ? ? ? ? ? 410 PHE B CG 1 293 B B +ATOM 7662 C CD1 . PHE B 1 293 ? -35.455 29.934 59.460 1.0 68.04 ? ? ? ? ? ? 410 PHE B CD1 1 293 B B +ATOM 7663 C CD2 . PHE B 1 293 ? -36.733 29.021 61.269 1.0 71.61 ? ? ? ? ? ? 410 PHE B CD2 1 293 B B +ATOM 7664 C CE1 . PHE B 1 293 ? -36.065 31.171 59.642 1.0 63.36 ? ? ? ? ? ? 410 PHE B CE1 1 293 B B +ATOM 7665 C CE2 . PHE B 1 293 ? -37.353 30.259 61.460 1.0 60.66 ? ? ? ? ? ? 410 PHE B CE2 1 293 B B +ATOM 7666 C CZ . PHE B 1 293 ? -37.014 31.335 60.643 1.0 62.48 ? ? ? ? ? ? 410 PHE B CZ 1 293 B B +ATOM 7667 N N . SER B 1 294 ? -34.454 27.371 57.376 1.0 54.52 ? ? ? ? ? ? 411 SER B N 1 294 B B +ATOM 7668 C CA . SER B 1 294 ? -34.597 27.616 55.949 1.0 39.07 ? ? ? ? ? ? 411 SER B CA 1 294 B B +ATOM 7669 C C . SER B 1 294 ? -36.081 27.573 55.602 1.0 37.27 ? ? ? ? ? ? 411 SER B C 1 294 B B +ATOM 7670 O O . SER B 1 294 ? -36.830 26.781 56.176 1.0 36.77 ? ? ? ? ? ? 411 SER B O 1 294 B B +ATOM 7671 C CB . SER B 1 294 ? -33.851 26.545 55.156 1.0 30.32 ? ? ? ? ? ? 411 SER B CB 1 294 B B +ATOM 7672 O OG . SER B 1 294 ? -32.618 27.052 54.680 1.0 50.98 ? ? ? ? ? ? 411 SER B OG 1 294 B B +ATOM 7673 N N . VAL B 1 295 ? -36.505 28.421 54.670 1.0 35.39 ? ? ? ? ? ? 412 VAL B N 1 295 B B +ATOM 7674 C CA . VAL B 1 295 ? -37.907 28.462 54.269 1.0 24.54 ? ? ? ? ? ? 412 VAL B CA 1 295 B B +ATOM 7675 C C . VAL B 1 295 ? -38.051 28.197 52.782 1.0 32.26 ? ? ? ? ? ? 412 VAL B C 1 295 B B +ATOM 7676 O O . VAL B 1 295 ? -37.167 28.533 51.995 1.0 24.52 ? ? ? ? ? ? 412 VAL B O 1 295 B B +ATOM 7677 C CB . VAL B 1 295 ? -38.545 29.834 54.579 1.0 24.31 ? ? ? ? ? ? 412 VAL B CB 1 295 B B +ATOM 7678 C CG1 . VAL B 1 295 ? -38.834 29.952 56.065 1.0 23.33 ? ? ? ? ? ? 412 VAL B CG1 1 295 B B +ATOM 7679 C CG2 . VAL B 1 295 ? -37.624 30.951 54.124 1.0 32.01 ? ? ? ? ? ? 412 VAL B CG2 1 295 B B +ATOM 7680 N N . ARG B 1 296 ? -39.172 27.589 52.408 1.0 37.85 ? ? ? ? ? ? 413 ARG B N 1 296 B B +ATOM 7681 C CA . ARG B 1 296 ? -39.451 27.279 51.011 1.0 54.9 ? ? ? ? ? ? 413 ARG B CA 1 296 B B +ATOM 7682 C C . ARG B 1 296 ? -40.881 27.665 50.672 1.0 60.27 ? ? ? ? ? ? 413 ARG B C 1 296 B B +ATOM 7683 O O . ARG B 1 296 ? -41.797 27.404 51.446 1.0 52.18 ? ? ? ? ? ? 413 ARG B O 1 296 B B +ATOM 7684 C CB . ARG B 1 296 ? -39.251 25.786 50.742 1.0 57.85 ? ? ? ? ? ? 413 ARG B CB 1 296 B B +ATOM 7685 C CG . ARG B 1 296 ? -39.631 25.353 49.331 1.0 60.82 ? ? ? ? ? ? 413 ARG B CG 1 296 B B +ATOM 7686 C CD . ARG B 1 296 ? -40.979 24.642 49.292 1.0 66.38 ? ? ? ? ? ? 413 ARG B CD 1 296 B B +ATOM 7687 N NE . ARG B 1 296 ? -41.160 23.735 50.424 1.0 70.92 ? ? ? ? ? ? 413 ARG B NE 1 296 B B +ATOM 7688 C CZ . ARG B 1 296 ? -42.153 22.857 50.529 1.0 72.59 ? ? ? ? ? ? 413 ARG B CZ 1 296 B B +ATOM 7689 N NH1 . ARG B 1 296 ? -43.062 22.763 49.567 1.0 65.24 ? ? ? ? ? ? 413 ARG B NH1 1 296 B B +ATOM 7690 N NH2 . ARG B 1 296 ? -42.236 22.069 51.593 1.0 55.86 ? ? ? ? ? ? 413 ARG B NH2 1 296 B B +ATOM 7691 N N . TYR B 1 297 ? -41.066 28.295 49.515 1.0 56.8 ? ? ? ? ? ? 414 TYR B N 1 297 B B +ATOM 7692 C CA . TYR B 1 297 ? -42.394 28.715 49.083 1.0 55.62 ? ? ? ? ? ? 414 TYR B CA 1 297 B B +ATOM 7693 C C . TYR B 1 297 ? -43.104 27.626 48.279 1.0 53.33 ? ? ? ? ? ? 414 TYR B C 1 297 B B +ATOM 7694 O O . TYR B 1 297 ? -42.519 27.028 47.374 1.0 80.67 ? ? ? ? ? ? 414 TYR B O 1 297 B B +ATOM 7695 C CB . TYR B 1 297 ? -42.296 29.994 48.242 1.0 57.36 ? ? ? ? ? ? 414 TYR B CB 1 297 B B +ATOM 7696 C CG . TYR B 1 297 ? -43.637 30.549 47.814 1.0 71.59 ? ? ? ? ? ? 414 TYR B CG 1 297 B B +ATOM 7697 C CD1 . TYR B 1 297 ? -44.657 30.758 48.742 1.0 81.2 ? ? ? ? ? ? 414 TYR B CD1 1 297 B B +ATOM 7698 C CD2 . TYR B 1 297 ? -43.891 30.858 46.480 1.0 62.03 ? ? ? ? ? ? 414 TYR B CD2 1 297 B B +ATOM 7699 C CE1 . TYR B 1 297 ? -45.897 31.259 48.353 1.0 83.1 ? ? ? ? ? ? 414 TYR B CE1 1 297 B B +ATOM 7700 C CE2 . TYR B 1 297 ? -45.127 31.359 46.079 1.0 84.22 ? ? ? ? ? ? 414 TYR B CE2 1 297 B B +ATOM 7701 C CZ . TYR B 1 297 ? -46.126 31.558 47.020 1.0 89.09 ? ? ? ? ? ? 414 TYR B CZ 1 297 B B +ATOM 7702 O OH . TYR B 1 297 ? -47.349 32.057 46.630 1.0 94.04 ? ? ? ? ? ? 414 TYR B OH 1 297 B B +ATOM 7703 N N . ASP B 1 298 ? -44.367 27.373 48.620 1.0 46.78 ? ? ? ? ? ? 415 ASP B N 1 298 B B +ATOM 7704 C CA . ASP B 1 298 ? -45.180 26.370 47.931 1.0 45.75 ? ? ? ? ? ? 415 ASP B CA 1 298 B B +ATOM 7705 C C . ASP B 1 298 ? -46.236 27.085 47.094 1.0 37.93 ? ? ? ? ? ? 415 ASP B C 1 298 B B +ATOM 7706 O O . ASP B 1 298 ? -47.249 27.540 47.615 1.0 42.42 ? ? ? ? ? ? 415 ASP B O 1 298 B B +ATOM 7707 C CB . ASP B 1 298 ? -45.859 25.437 48.942 1.0 53.54 ? ? ? ? ? ? 415 ASP B CB 1 298 B B +ATOM 7708 C CG . ASP B 1 298 ? -46.218 24.085 48.344 1.0 72.49 ? ? ? ? ? ? 415 ASP B CG 1 298 B B +ATOM 7709 O OD1 . ASP B 1 298 ? -46.902 24.059 47.300 1.0 81.43 ? ? ? ? ? ? 415 ASP B OD1 1 298 B B +ATOM 7710 O OD2 . ASP B 1 298 ? -45.814 23.049 48.914 1.0 68.23 ? ? ? ? ? ? 415 ASP B OD2 1 298 B B +ATOM 7711 N N . PRO B 1 299 ? -46.001 27.195 45.779 1.0 34.92 ? ? ? ? ? ? 416 PRO B N 1 299 B B +ATOM 7712 C CA . PRO B 1 299 ? -46.923 27.860 44.856 1.0 40.44 ? ? ? ? ? ? 416 PRO B CA 1 299 B B +ATOM 7713 C C . PRO B 1 299 ? -48.309 27.243 44.755 1.0 37.13 ? ? ? ? ? ? 416 PRO B C 1 299 B B +ATOM 7714 O O . PRO B 1 299 ? -49.238 27.895 44.287 1.0 52.25 ? ? ? ? ? ? 416 PRO B O 1 299 B B +ATOM 7715 C CB . PRO B 1 299 ? -46.191 27.825 43.511 1.0 44.31 ? ? ? ? ? ? 416 PRO B CB 1 299 B B +ATOM 7716 C CG . PRO B 1 299 ? -44.790 27.484 43.823 1.0 49.92 ? ? ? ? ? ? 416 PRO B CG 1 299 B B +ATOM 7717 C CD . PRO B 1 299 ? -44.810 26.686 45.086 1.0 50.32 ? ? ? ? ? ? 416 PRO B CD 1 299 B B +ATOM 7718 N N . TYR B 1 300 ? -48.455 25.994 45.186 1.0 28.69 ? ? ? ? ? ? 417 TYR B N 1 300 B B +ATOM 7719 C CA . TYR B 1 300 ? -49.752 25.320 45.117 1.0 38.77 ? ? ? ? ? ? 417 TYR B CA 1 300 B B +ATOM 7720 C C . TYR B 1 300 ? -50.640 25.709 46.288 1.0 41.07 ? ? ? ? ? ? 417 TYR B C 1 300 B B +ATOM 7721 O O . TYR B 1 300 ? -51.817 26.021 46.110 1.0 53.69 ? ? ? ? ? ? 417 TYR B O 1 300 B B +ATOM 7722 C CB . TYR B 1 300 ? -49.567 23.797 45.091 1.0 36.92 ? ? ? ? ? ? 417 TYR B CB 1 300 B B +ATOM 7723 C CG . TYR B 1 300 ? -49.060 23.262 43.766 1.0 59.52 ? ? ? ? ? ? 417 TYR B CG 1 300 B B +ATOM 7724 C CD1 . TYR B 1 300 ? -47.699 23.266 43.468 1.0 74.44 ? ? ? ? ? ? 417 TYR B CD1 1 300 B B +ATOM 7725 C CD2 . TYR B 1 300 ? -49.940 22.764 42.803 1.0 63.68 ? ? ? ? ? ? 417 TYR B CD2 1 300 B B +ATOM 7726 C CE1 . TYR B 1 300 ? -47.228 22.794 42.244 1.0 65.02 ? ? ? ? ? ? 417 TYR B CE1 1 300 B B +ATOM 7727 C CE2 . TYR B 1 300 ? -49.474 22.289 41.574 1.0 54.57 ? ? ? ? ? ? 417 TYR B CE2 1 300 B B +ATOM 7728 C CZ . TYR B 1 300 ? -48.120 22.307 41.305 1.0 51.94 ? ? ? ? ? ? 417 TYR B CZ 1 300 B B +ATOM 7729 O OH . TYR B 1 300 ? -47.658 21.844 40.097 1.0 52.98 ? ? ? ? ? ? 417 TYR B OH 1 300 B B +ATOM 7730 N N . THR B 1 301 ? -50.070 25.681 47.487 1.0 46.91 ? ? ? ? ? ? 418 THR B N 1 301 B B +ATOM 7731 C CA . THR B 1 301 ? -50.803 26.039 48.695 1.0 55.02 ? ? ? ? ? ? 418 THR B CA 1 301 B B +ATOM 7732 C C . THR B 1 301 ? -50.545 27.502 49.022 1.0 52.04 ? ? ? ? ? ? 418 THR B C 1 301 B B +ATOM 7733 O O . THR B 1 301 ? -51.076 28.034 49.997 1.0 69.95 ? ? ? ? ? ? 418 THR B O 1 301 B B +ATOM 7734 C CB . THR B 1 301 ? -50.358 25.185 49.897 1.0 57.5 ? ? ? ? ? ? 418 THR B CB 1 301 B B +ATOM 7735 O OG1 . THR B 1 301 ? -48.956 25.374 50.127 1.0 56.66 ? ? ? ? ? ? 418 THR B OG1 1 301 B B +ATOM 7736 C CG2 . THR B 1 301 ? -50.623 23.725 49.629 1.0 61.75 ? ? ? ? ? ? 418 THR B CG2 1 301 B B +ATOM 7737 N N . GLN B 1 302 ? -49.729 28.148 48.195 1.0 45.36 ? ? ? ? ? ? 419 GLN B N 1 302 B B +ATOM 7738 C CA . GLN B 1 302 ? -49.376 29.551 48.384 1.0 52.53 ? ? ? ? ? ? 419 GLN B CA 1 302 B B +ATOM 7739 C C . GLN B 1 302 ? -49.104 29.867 49.854 1.0 48.4 ? ? ? ? ? ? 419 GLN B C 1 302 B B +ATOM 7740 O O . GLN B 1 302 ? -49.516 30.899 50.384 1.0 53.82 ? ? ? ? ? ? 419 GLN B O 1 302 B B +ATOM 7741 C CB . GLN B 1 302 ? -50.471 30.447 47.806 1.0 62.3 ? ? ? ? ? ? 419 GLN B CB 1 302 B B +ATOM 7742 C CG . GLN B 1 302 ? -50.455 30.436 46.279 1.0 92.4 ? ? ? ? ? ? 419 GLN B CG 1 302 B B +ATOM 7743 C CD . GLN B 1 302 ? -51.487 31.347 45.650 1.0 100.0 ? ? ? ? ? ? 419 GLN B CD 1 302 B B +ATOM 7744 O OE1 . GLN B 1 302 ? -52.414 31.815 46.313 1.0 100.0 ? ? ? ? ? ? 419 GLN B OE1 1 302 B B +ATOM 7745 N NE2 . GLN B 1 302 ? -51.331 31.601 44.353 1.0 100.0 ? ? ? ? ? ? 419 GLN B NE2 1 302 B B +ATOM 7746 N N . ARG B 1 303 ? -48.386 28.945 50.490 1.0 52.67 ? ? ? ? ? ? 420 ARG B N 1 303 B B +ATOM 7747 C CA . ARG B 1 303 ? -47.991 29.041 51.889 1.0 48.06 ? ? ? ? ? ? 420 ARG B CA 1 303 B B +ATOM 7748 C C . ARG B 1 303 ? -46.469 29.147 51.897 1.0 44.16 ? ? ? ? ? ? 420 ARG B C 1 303 B B +ATOM 7749 O O . ARG B 1 303 ? -45.822 28.907 50.879 1.0 52.33 ? ? ? ? ? ? 420 ARG B O 1 303 B B +ATOM 7750 C CB . ARG B 1 303 ? -48.362 27.764 52.637 1.0 52.96 ? ? ? ? ? ? 420 ARG B CB 1 303 B B +ATOM 7751 C CG . ARG B 1 303 ? -49.732 27.712 53.262 1.0 53.84 ? ? ? ? ? ? 420 ARG B CG 1 303 B B +ATOM 7752 C CD . ARG B 1 303 ? -49.979 26.280 53.697 1.0 76.17 ? ? ? ? ? ? 420 ARG B CD 1 303 B B +ATOM 7753 N NE . ARG B 1 303 ? -51.049 26.141 54.677 1.0 99.8 ? ? ? ? ? ? 420 ARG B NE 1 303 B B +ATOM 7754 C CZ . ARG B 1 303 ? -51.632 24.984 54.976 1.0 100.0 ? ? ? ? ? ? 420 ARG B CZ 1 303 B B +ATOM 7755 N NH1 . ARG B 1 303 ? -51.249 23.871 54.362 1.0 88.44 ? ? ? ? ? ? 420 ARG B NH1 1 303 B B +ATOM 7756 N NH2 . ARG B 1 303 ? -52.604 24.940 55.878 1.0 100.0 ? ? ? ? ? ? 420 ARG B NH2 1 303 B B +ATOM 7757 N N . ILE B 1 304 ? -45.903 29.499 53.045 1.0 26.85 ? ? ? ? ? ? 421 ILE B N 1 304 B B +ATOM 7758 C CA . ILE B 1 304 ? -44.456 29.582 53.188 1.0 12.67 ? ? ? ? ? ? 421 ILE B CA 1 304 B B +ATOM 7759 C C . ILE B 1 304 ? -44.092 28.423 54.108 1.0 36.59 ? ? ? ? ? ? 421 ILE B C 1 304 B B +ATOM 7760 O O . ILE B 1 304 ? -44.552 28.368 55.249 1.0 29.54 ? ? ? ? ? ? 421 ILE B O 1 304 B B +ATOM 7761 C CB . ILE B 1 304 ? -44.007 30.895 53.845 1.0 12.33 ? ? ? ? ? ? 421 ILE B CB 1 304 B B +ATOM 7762 C CG1 . ILE B 1 304 ? -43.703 31.935 52.766 1.0 18.57 ? ? ? ? ? ? 421 ILE B CG1 1 304 B B +ATOM 7763 C CG2 . ILE B 1 304 ? -42.772 30.652 54.702 1.0 5.84 ? ? ? ? ? ? 421 ILE B CG2 1 304 B B +ATOM 7764 C CD1 . ILE B 1 304 ? -42.415 31.683 52.017 1.0 21.32 ? ? ? ? ? ? 421 ILE B CD1 1 304 B B +ATOM 7765 N N . GLU B 1 305 ? -43.270 27.502 53.608 1.0 59.38 ? ? ? ? ? ? 422 GLU B N 1 305 B B +ATOM 7766 C CA . GLU B 1 305 ? -42.865 26.322 54.368 1.0 60.87 ? ? ? ? ? ? 422 GLU B CA 1 305 B B +ATOM 7767 C C . GLU B 1 305 ? -41.584 26.500 55.163 1.0 59.7 ? ? ? ? ? ? 422 GLU B C 1 305 B B +ATOM 7768 O O . GLU B 1 305 ? -40.531 26.814 54.606 1.0 65.41 ? ? ? ? ? ? 422 GLU B O 1 305 B B +ATOM 7769 C CB . GLU B 1 305 ? -42.691 25.123 53.430 1.0 67.51 ? ? ? ? ? ? 422 GLU B CB 1 305 B B +ATOM 7770 C CG . GLU B 1 305 ? -43.987 24.598 52.828 1.0 76.03 ? ? ? ? ? ? 422 GLU B CG 1 305 B B +ATOM 7771 C CD . GLU B 1 305 ? -44.869 23.902 53.848 1.0 84.53 ? ? ? ? ? ? 422 GLU B CD 1 305 B B +ATOM 7772 O OE1 . GLU B 1 305 ? -44.861 22.653 53.888 1.0 97.45 ? ? ? ? ? ? 422 GLU B OE1 1 305 B B +ATOM 7773 O OE2 . GLU B 1 305 ? -45.571 24.605 54.606 1.0 81.73 ? ? ? ? ? ? 422 GLU B OE2 1 305 B B +ATOM 7774 N N . VAL B 1 306 ? -41.682 26.282 56.471 1.0 61.14 ? ? ? ? ? ? 423 VAL B N 1 306 B B +ATOM 7775 C CA . VAL B 1 306 ? -40.528 26.389 57.351 1.0 66.29 ? ? ? ? ? ? 423 VAL B CA 1 306 B B +ATOM 7776 C C . VAL B 1 306 ? -39.871 25.013 57.410 1.0 63.63 ? ? ? ? ? ? 423 VAL B C 1 306 B B +ATOM 7777 O O . VAL B 1 306 ? -40.459 24.047 57.903 1.0 60.26 ? ? ? ? ? ? 423 VAL B O 1 306 B B +ATOM 7778 C CB . VAL B 1 306 ? -40.929 26.814 58.789 1.0 64.16 ? ? ? ? ? ? 423 VAL B CB 1 306 B B +ATOM 7779 C CG1 . VAL B 1 306 ? -39.685 27.189 59.579 1.0 54.84 ? ? ? ? ? ? 423 VAL B CG1 1 306 B B +ATOM 7780 C CG2 . VAL B 1 306 ? -41.898 27.979 58.747 1.0 70.94 ? ? ? ? ? ? 423 VAL B CG2 1 306 B B +ATOM 7781 N N . LEU B 1 307 ? -38.654 24.925 56.889 1.0 63.78 ? ? ? ? ? ? 424 LEU B N 1 307 B B +ATOM 7782 C CA . LEU B 1 307 ? -37.928 23.668 56.888 1.0 55.0 ? ? ? ? ? ? 424 LEU B CA 1 307 B B +ATOM 7783 C C . LEU B 1 307 ? -37.094 23.572 58.152 1.0 62.6 ? ? ? ? ? ? 424 LEU B C 1 307 B B +ATOM 7784 O O . LEU B 1 307 ? -36.039 24.200 58.263 1.0 69.94 ? ? ? ? ? ? 424 LEU B O 1 307 B B +ATOM 7785 C CB . LEU B 1 307 ? -37.033 23.578 55.647 1.0 55.01 ? ? ? ? ? ? 424 LEU B CB 1 307 B B +ATOM 7786 C CG . LEU B 1 307 ? -37.729 23.888 54.318 1.0 47.53 ? ? ? ? ? ? 424 LEU B CG 1 307 B B +ATOM 7787 C CD1 . LEU B 1 307 ? -36.681 24.167 53.261 1.0 44.35 ? ? ? ? ? ? 424 LEU B CD1 1 307 B B +ATOM 7788 C CD2 . LEU B 1 307 ? -38.630 22.731 53.910 1.0 31.73 ? ? ? ? ? ? 424 LEU B CD2 1 307 B B +ATOM 7789 N N . ASP B 1 308 ? -37.585 22.788 59.107 1.0 68.96 ? ? ? ? ? ? 425 ASP B N 1 308 B B +ATOM 7790 C CA . ASP B 1 308 ? -36.904 22.586 60.378 1.0 76.54 ? ? ? ? ? ? 425 ASP B CA 1 308 B B +ATOM 7791 C C . ASP B 1 308 ? -37.063 21.133 60.805 1.0 80.36 ? ? ? ? ? ? 425 ASP B C 1 308 B B +ATOM 7792 O O . ASP B 1 308 ? -36.247 20.607 61.560 1.0 92.65 ? ? ? ? ? ? 425 ASP B O 1 308 B B +ATOM 7793 C CB . ASP B 1 308 ? -37.497 23.502 61.452 1.0 75.64 ? ? ? ? ? ? 425 ASP B CB 1 308 B B +ATOM 7794 C CG . ASP B 1 308 ? -39.004 23.353 61.578 1.0 84.75 ? ? ? ? ? ? 425 ASP B CG 1 308 B B +ATOM 7795 O OD1 . ASP B 1 308 ? -39.722 23.768 60.647 1.0 93.24 ? ? ? ? ? ? 425 ASP B OD1 1 308 B B +ATOM 7796 O OD2 . ASP B 1 308 ? -39.474 22.821 62.606 1.0 91.9 ? ? ? ? ? ? 425 ASP B OD2 1 308 B B +ATOM 7797 N N . ASN B 1 309 ? -38.119 20.489 60.315 1.0 76.24 ? ? ? ? ? ? 426 ASN B N 1 309 B B +ATOM 7798 C CA . ASN B 1 309 ? -38.377 19.098 60.650 1.0 71.04 ? ? ? ? ? ? 426 ASN B CA 1 309 B B +ATOM 7799 C C . ASN B 1 309 ? -37.817 18.152 59.598 1.0 75.63 ? ? ? ? ? ? 426 ASN B C 1 309 B B +ATOM 7800 O O . ASN B 1 309 ? -37.666 18.521 58.434 1.0 83.46 ? ? ? ? ? ? 426 ASN B O 1 309 B B +ATOM 7801 C CB . ASN B 1 309 ? -39.875 18.853 60.803 1.0 80.23 ? ? ? ? ? ? 426 ASN B CB 1 309 B B +ATOM 7802 C CG . ASN B 1 309 ? -40.174 17.523 61.457 1.0 100.0 ? ? ? ? ? ? 426 ASN B CG 1 309 B B +ATOM 7803 O OD1 . ASN B 1 309 ? -41.212 16.912 61.209 1.0 100.0 ? ? ? ? ? ? 426 ASN B OD1 1 309 B B +ATOM 7804 N ND2 . ASN B 1 309 ? -39.257 17.064 62.304 1.0 100.0 ? ? ? ? ? ? 426 ASN B ND2 1 309 B B +ATOM 7805 N N . THR B 1 310 ? -37.520 16.925 60.017 1.0 81.33 ? ? ? ? ? ? 427 THR B N 1 310 B B +ATOM 7806 C CA . THR B 1 310 ? -36.971 15.920 59.115 1.0 80.19 ? ? ? ? ? ? 427 THR B CA 1 310 B B +ATOM 7807 C C . THR B 1 310 ? -37.966 15.469 58.053 1.0 70.69 ? ? ? ? ? ? 427 THR B C 1 310 B B +ATOM 7808 O O . THR B 1 310 ? -37.566 14.986 56.996 1.0 79.7 ? ? ? ? ? ? 427 THR B O 1 310 B B +ATOM 7809 C CB . THR B 1 310 ? -36.492 14.675 59.887 1.0 83.76 ? ? ? ? ? ? 427 THR B CB 1 310 B B +ATOM 7810 O OG1 . THR B 1 310 ? -37.585 14.122 60.628 1.0 87.74 ? ? ? ? ? ? 427 THR B OG1 1 310 B B +ATOM 7811 C CG2 . THR B 1 310 ? -35.366 15.041 60.837 1.0 76.68 ? ? ? ? ? ? 427 THR B CG2 1 310 B B +ATOM 7812 N N . GLN B 1 311 ? -39.258 15.618 58.329 1.0 49.69 ? ? ? ? ? ? 428 GLN B N 1 311 B B +ATOM 7813 C CA . GLN B 1 311 ? -40.274 15.222 57.358 1.0 52.53 ? ? ? ? ? ? 428 GLN B CA 1 311 B B +ATOM 7814 C C . GLN B 1 311 ? -40.512 16.362 56.377 1.0 51.11 ? ? ? ? ? ? 428 GLN B C 1 311 B B +ATOM 7815 O O . GLN B 1 311 ? -40.998 16.152 55.266 1.0 41.08 ? ? ? ? ? ? 428 GLN B O 1 311 B B +ATOM 7816 C CB . GLN B 1 311 ? -41.583 14.849 58.059 1.0 66.13 ? ? ? ? ? ? 428 GLN B CB 1 311 B B +ATOM 7817 C CG . GLN B 1 311 ? -41.884 13.350 58.049 1.0 90.15 ? ? ? ? ? ? 428 GLN B CG 1 311 B B +ATOM 7818 C CD . GLN B 1 311 ? -42.820 12.933 56.919 1.0 86.66 ? ? ? ? ? ? 428 GLN B CD 1 311 B B +ATOM 7819 O OE1 . GLN B 1 311 ? -43.249 13.758 56.110 1.0 83.0 ? ? ? ? ? ? 428 GLN B OE1 1 311 B B +ATOM 7820 N NE2 . GLN B 1 311 ? -43.141 11.644 56.863 1.0 61.4 ? ? ? ? ? ? 428 GLN B NE2 1 311 B B +ATOM 7821 N N . GLN B 1 312 ? -40.159 17.570 56.801 1.0 58.96 ? ? ? ? ? ? 429 GLN B N 1 312 B B +ATOM 7822 C CA . GLN B 1 312 ? -40.306 18.749 55.964 1.0 63.52 ? ? ? ? ? ? 429 GLN B CA 1 312 B B +ATOM 7823 C C . GLN B 1 312 ? -39.372 18.618 54.765 1.0 54.99 ? ? ? ? ? ? 429 GLN B C 1 312 B B +ATOM 7824 O O . GLN B 1 312 ? -39.667 19.103 53.674 1.0 69.7 ? ? ? ? ? ? 429 GLN B O 1 312 B B +ATOM 7825 C CB . GLN B 1 312 ? -39.948 20.008 56.761 1.0 79.59 ? ? ? ? ? ? 429 GLN B CB 1 312 B B +ATOM 7826 C CG . GLN B 1 312 ? -41.129 20.664 57.460 1.0 81.71 ? ? ? ? ? ? 429 GLN B CG 1 312 B B +ATOM 7827 C CD . GLN B 1 312 ? -42.184 21.154 56.489 1.0 78.96 ? ? ? ? ? ? 429 GLN B CD 1 312 B B +ATOM 7828 O OE1 . GLN B 1 312 ? -42.078 22.250 55.942 1.0 84.65 ? ? ? ? ? ? 429 GLN B OE1 1 312 B B +ATOM 7829 N NE2 . GLN B 1 312 ? -43.208 20.339 56.265 1.0 58.71 ? ? ? ? ? ? 429 GLN B NE2 1 312 B B +ATOM 7830 N N . LEU B 1 313 ? -38.242 17.953 54.983 1.0 40.34 ? ? ? ? ? ? 430 LEU B N 1 313 B B +ATOM 7831 C CA . LEU B 1 313 ? -37.248 17.758 53.936 1.0 44.53 ? ? ? ? ? ? 430 LEU B CA 1 313 B B +ATOM 7832 C C . LEU B 1 313 ? -37.571 16.560 53.047 1.0 49.41 ? ? ? ? ? ? 430 LEU B C 1 313 B B +ATOM 7833 O O . LEU B 1 313 ? -37.144 16.501 51.895 1.0 49.82 ? ? ? ? ? ? 430 LEU B O 1 313 B B +ATOM 7834 C CB . LEU B 1 313 ? -35.865 17.598 54.567 1.0 49.27 ? ? ? ? ? ? 430 LEU B CB 1 313 B B +ATOM 7835 C CG . LEU B 1 313 ? -35.478 18.807 55.429 1.0 46.92 ? ? ? ? ? ? 430 LEU B CG 1 313 B B +ATOM 7836 C CD1 . LEU B 1 313 ? -34.289 18.477 56.314 1.0 39.85 ? ? ? ? ? ? 430 LEU B CD1 1 313 B B +ATOM 7837 C CD2 . LEU B 1 313 ? -35.166 19.983 54.524 1.0 60.57 ? ? ? ? ? ? 430 LEU B CD2 1 313 B B +ATOM 7838 N N . LYS B 1 314 ? -38.325 15.608 53.590 1.0 50.79 ? ? ? ? ? ? 431 LYS B N 1 314 B B +ATOM 7839 C CA . LYS B 1 314 ? -38.714 14.420 52.841 1.0 49.15 ? ? ? ? ? ? 431 LYS B CA 1 314 B B +ATOM 7840 C C . LYS B 1 314 ? -39.484 14.846 51.597 1.0 44.82 ? ? ? ? ? ? 431 LYS B C 1 314 B B +ATOM 7841 O O . LYS B 1 314 ? -39.309 14.287 50.513 1.0 55.9 ? ? ? ? ? ? 431 LYS B O 1 314 B B +ATOM 7842 C CB . LYS B 1 314 ? -39.616 13.528 53.697 1.0 56.53 ? ? ? ? ? ? 431 LYS B CB 1 314 B B +ATOM 7843 C CG . LYS B 1 314 ? -38.895 12.614 54.665 1.0 62.29 ? ? ? ? ? ? 431 LYS B CG 1 314 B B +ATOM 7844 C CD . LYS B 1 314 ? -39.851 11.565 55.223 1.0 61.91 ? ? ? ? ? ? 431 LYS B CD 1 314 B B +ATOM 7845 C CE . LYS B 1 314 ? -39.242 10.789 56.381 1.0 75.65 ? ? ? ? ? ? 431 LYS B CE 1 314 B B +ATOM 7846 N NZ . LYS B 1 314 ? -40.178 9.751 56.894 1.0 72.22 ? ? ? ? ? ? 431 LYS B NZ 1 314 B B +ATOM 7847 N N . ILE B 1 315 ? -40.332 15.853 51.773 1.0 45.17 ? ? ? ? ? ? 432 ILE B N 1 315 B B +ATOM 7848 C CA . ILE B 1 315 ? -41.174 16.367 50.697 1.0 66.0 ? ? ? ? ? ? 432 ILE B CA 1 315 B B +ATOM 7849 C C . ILE B 1 315 ? -40.487 17.306 49.711 1.0 58.78 ? ? ? ? ? ? 432 ILE B C 1 315 B B +ATOM 7850 O O . ILE B 1 315 ? -40.816 17.309 48.528 1.0 60.28 ? ? ? ? ? ? 432 ILE B O 1 315 B B +ATOM 7851 C CB . ILE B 1 315 ? -42.422 17.066 51.269 1.0 80.32 ? ? ? ? ? ? 432 ILE B CB 1 315 B B +ATOM 7852 C CG1 . ILE B 1 315 ? -42.156 17.510 52.712 1.0 88.13 ? ? ? ? ? ? 432 ILE B CG1 1 315 B B +ATOM 7853 C CG2 . ILE B 1 315 ? -43.620 16.126 51.185 1.0 94.34 ? ? ? ? ? ? 432 ILE B CG2 1 315 B B +ATOM 7854 C CD1 . ILE B 1 315 ? -43.408 17.664 53.567 1.0 100.0 ? ? ? ? ? ? 432 ILE B CD1 1 315 B B +ATOM 7855 N N . LEU B 1 316 ? -39.556 18.120 50.189 1.0 48.19 ? ? ? ? ? ? 433 LEU B N 1 316 B B +ATOM 7856 C CA . LEU B 1 316 ? -38.847 19.015 49.284 1.0 46.48 ? ? ? ? ? ? 433 LEU B CA 1 316 B B +ATOM 7857 C C . LEU B 1 316 ? -37.998 18.106 48.397 1.0 50.62 ? ? ? ? ? ? 433 LEU B C 1 316 B B +ATOM 7858 O O . LEU B 1 316 ? -37.876 18.321 47.185 1.0 29.72 ? ? ? ? ? ? 433 LEU B O 1 316 B B +ATOM 7859 C CB . LEU B 1 316 ? -37.955 19.989 50.070 1.0 22.61 ? ? ? ? ? ? 433 LEU B CB 1 316 B B +ATOM 7860 C CG . LEU B 1 316 ? -36.949 20.838 49.276 1.0 25.63 ? ? ? ? ? ? 433 LEU B CG 1 316 B B +ATOM 7861 C CD1 . LEU B 1 316 ? -37.657 21.582 48.169 1.0 23.52 ? ? ? ? ? ? 433 LEU B CD1 1 316 B B +ATOM 7862 C CD2 . LEU B 1 316 ? -36.252 21.815 50.205 1.0 21.65 ? ? ? ? ? ? 433 LEU B CD2 1 316 B B +ATOM 7863 N N . ALA B 1 317 ? -37.426 17.077 49.020 1.0 47.79 ? ? ? ? ? ? 434 ALA B N 1 317 B B +ATOM 7864 C CA . ALA B 1 317 ? -36.602 16.112 48.311 1.0 41.3 ? ? ? ? ? ? 434 ALA B CA 1 317 B B +ATOM 7865 C C . ALA B 1 317 ? -37.425 15.524 47.179 1.0 40.66 ? ? ? ? ? ? 434 ALA B C 1 317 B B +ATOM 7866 O O . ALA B 1 317 ? -36.962 15.417 46.046 1.0 51.69 ? ? ? ? ? ? 434 ALA B O 1 317 B B +ATOM 7867 C CB . ALA B 1 317 ? -36.155 15.008 49.258 1.0 47.23 ? ? ? ? ? ? 434 ALA B CB 1 317 B B +ATOM 7868 N N . ASP B 1 318 ? -38.655 15.142 47.500 1.0 30.86 ? ? ? ? ? ? 435 ASP B N 1 318 B B +ATOM 7869 C CA . ASP B 1 318 ? -39.565 14.560 46.522 1.0 32.91 ? ? ? ? ? ? 435 ASP B CA 1 318 B B +ATOM 7870 C C . ASP B 1 318 ? -39.855 15.528 45.379 1.0 38.97 ? ? ? ? ? ? 435 ASP B C 1 318 B B +ATOM 7871 O O . ASP B 1 318 ? -39.901 15.130 44.216 1.0 34.99 ? ? ? ? ? ? 435 ASP B O 1 318 B B +ATOM 7872 C CB . ASP B 1 318 ? -40.871 14.161 47.202 1.0 43.61 ? ? ? ? ? ? 435 ASP B CB 1 318 B B +ATOM 7873 C CG . ASP B 1 318 ? -40.810 12.776 47.800 1.0 66.74 ? ? ? ? ? ? 435 ASP B CG 1 318 B B +ATOM 7874 O OD1 . ASP B 1 318 ? -40.589 11.814 47.036 1.0 84.71 ? ? ? ? ? ? 435 ASP B OD1 1 318 B B +ATOM 7875 O OD2 . ASP B 1 318 ? -40.981 12.651 49.032 1.0 83.09 ? ? ? ? ? ? 435 ASP B OD2 1 318 B B +ATOM 7876 N N . SER B 1 319 ? -40.046 16.799 45.715 1.0 34.82 ? ? ? ? ? ? 436 SER B N 1 319 B B +ATOM 7877 C CA . SER B 1 319 ? -40.329 17.809 44.707 1.0 43.47 ? ? ? ? ? ? 436 SER B CA 1 319 B B +ATOM 7878 C C . SER B 1 319 ? -39.190 17.826 43.701 1.0 53.51 ? ? ? ? ? ? 436 SER B C 1 319 B B +ATOM 7879 O O . SER B 1 319 ? -39.404 17.737 42.489 1.0 63.67 ? ? ? ? ? ? 436 SER B O 1 319 B B +ATOM 7880 C CB . SER B 1 319 ? -40.465 19.189 45.355 1.0 46.54 ? ? ? ? ? ? 436 SER B CB 1 319 B B +ATOM 7881 O OG . SER B 1 319 ? -41.375 19.151 46.437 1.0 76.55 ? ? ? ? ? ? 436 SER B OG 1 319 B B +ATOM 7882 N N . ILE B 1 320 ? -37.971 17.931 44.214 1.0 48.32 ? ? ? ? ? ? 437 ILE B N 1 320 B B +ATOM 7883 C CA . ILE B 1 320 ? -36.797 17.959 43.359 1.0 45.93 ? ? ? ? ? ? 437 ILE B CA 1 320 B B +ATOM 7884 C C . ILE B 1 320 ? -36.667 16.668 42.560 1.0 39.76 ? ? ? ? ? ? 437 ILE B C 1 320 B B +ATOM 7885 O O . ILE B 1 320 ? -36.589 16.693 41.333 1.0 48.97 ? ? ? ? ? ? 437 ILE B O 1 320 B B +ATOM 7886 C CB . ILE B 1 320 ? -35.533 18.176 44.198 1.0 43.57 ? ? ? ? ? ? 437 ILE B CB 1 320 B B +ATOM 7887 C CG1 . ILE B 1 320 ? -35.731 19.409 45.081 1.0 42.04 ? ? ? ? ? ? 437 ILE B CG1 1 320 B B +ATOM 7888 C CG2 . ILE B 1 320 ? -34.316 18.344 43.294 1.0 48.96 ? ? ? ? ? ? 437 ILE B CG2 1 320 B B +ATOM 7889 C CD1 . ILE B 1 320 ? -34.519 19.806 45.894 1.0 39.26 ? ? ? ? ? ? 437 ILE B CD1 1 320 B B +ATOM 7890 N N . ASN B 1 321 ? -36.656 15.543 43.264 1.0 33.67 ? ? ? ? ? ? 438 ASN B N 1 321 B B +ATOM 7891 C CA . ASN B 1 321 ? -36.529 14.237 42.630 1.0 30.51 ? ? ? ? ? ? 438 ASN B CA 1 321 B B +ATOM 7892 C C . ASN B 1 321 ? -37.346 14.111 41.349 1.0 39.75 ? ? ? ? ? ? 438 ASN B C 1 321 B B +ATOM 7893 O O . ASN B 1 321 ? -36.847 13.653 40.323 1.0 40.63 ? ? ? ? ? ? 438 ASN B O 1 321 B B +ATOM 7894 C CB . ASN B 1 321 ? -36.947 13.138 43.607 1.0 30.24 ? ? ? ? ? ? 438 ASN B CB 1 321 B B +ATOM 7895 C CG . ASN B 1 321 ? -36.557 11.754 43.128 1.0 36.18 ? ? ? ? ? ? 438 ASN B CG 1 321 B B +ATOM 7896 O OD1 . ASN B 1 321 ? -35.462 11.548 42.609 1.0 54.57 ? ? ? ? ? ? 438 ASN B OD1 1 321 B B +ATOM 7897 N ND2 . ASN B 1 321 ? -37.457 10.794 43.304 1.0 48.83 ? ? ? ? ? ? 438 ASN B ND2 1 321 B B +ATOM 7898 N N . SER B 1 322 ? -38.608 14.516 41.415 1.0 51.34 ? ? ? ? ? ? 439 SER B N 1 322 B B +ATOM 7899 C CA . SER B 1 322 ? -39.494 14.435 40.259 1.0 57.68 ? ? ? ? ? ? 439 SER B CA 1 322 B B +ATOM 7900 C C . SER B 1 322 ? -39.127 15.435 39.173 1.0 54.76 ? ? ? ? ? ? 439 SER B C 1 322 B B +ATOM 7901 O O . SER B 1 322 ? -39.203 15.128 37.984 1.0 62.9 ? ? ? ? ? ? 439 SER B O 1 322 B B +ATOM 7902 C CB . SER B 1 322 ? -40.943 14.675 40.687 1.0 56.79 ? ? ? ? ? ? 439 SER B CB 1 322 B B +ATOM 7903 O OG . SER B 1 322 ? -41.148 16.038 41.019 1.0 65.36 ? ? ? ? ? ? 439 SER B OG 1 322 B B +ATOM 7904 N N . GLU B 1 323 ? -38.733 16.634 39.589 1.0 51.44 ? ? ? ? ? ? 440 GLU B N 1 323 B B +ATOM 7905 C CA . GLU B 1 323 ? -38.371 17.692 38.651 1.0 62.89 ? ? ? ? ? ? 440 GLU B CA 1 323 B B +ATOM 7906 C C . GLU B 1 323 ? -37.122 17.366 37.837 1.0 62.26 ? ? ? ? ? ? 440 GLU B C 1 323 B B +ATOM 7907 O O . GLU B 1 323 ? -37.033 17.718 36.658 1.0 64.31 ? ? ? ? ? ? 440 GLU B O 1 323 B B +ATOM 7908 C CB . GLU B 1 323 ? -38.189 19.011 39.402 1.0 63.42 ? ? ? ? ? ? 440 GLU B CB 1 323 B B +ATOM 7909 C CG . GLU B 1 323 ? -39.501 19.692 39.771 1.0 61.16 ? ? ? ? ? ? 440 GLU B CG 1 323 B B +ATOM 7910 C CD . GLU B 1 323 ? -39.426 21.200 39.640 1.0 64.23 ? ? ? ? ? ? 440 GLU B CD 1 323 B B +ATOM 7911 O OE1 . GLU B 1 323 ? -38.774 21.837 40.494 1.0 63.45 ? ? ? ? ? ? 440 GLU B OE1 1 323 B B +ATOM 7912 O OE2 . GLU B 1 323 ? -40.014 21.749 38.684 1.0 72.09 ? ? ? ? ? ? 440 GLU B OE2 1 323 B B +ATOM 7913 N N . ILE B 1 324 ? -36.156 16.699 38.462 1.0 55.97 ? ? ? ? ? ? 441 ILE B N 1 324 B B +ATOM 7914 C CA . ILE B 1 324 ? -34.945 16.322 37.749 1.0 43.28 ? ? ? ? ? ? 441 ILE B CA 1 324 B B +ATOM 7915 C C . ILE B 1 324 ? -35.323 15.196 36.811 1.0 38.75 ? ? ? ? ? ? 441 ILE B C 1 324 B B +ATOM 7916 O O . ILE B 1 324 ? -34.890 15.164 35.660 1.0 43.38 ? ? ? ? ? ? 441 ILE B O 1 324 B B +ATOM 7917 C CB . ILE B 1 324 ? -33.846 15.805 38.690 1.0 32.29 ? ? ? ? ? ? 441 ILE B CB 1 324 B B +ATOM 7918 C CG1 . ILE B 1 324 ? -33.820 16.632 39.974 1.0 44.61 ? ? ? ? ? ? 441 ILE B CG1 1 324 B B +ATOM 7919 C CG2 . ILE B 1 324 ? -32.495 15.879 37.989 1.0 31.94 ? ? ? ? ? ? 441 ILE B CG2 1 324 B B +ATOM 7920 C CD1 . ILE B 1 324 ? -33.009 16.004 41.084 1.0 55.07 ? ? ? ? ? ? 441 ILE B CD1 1 324 B B +ATOM 7921 N N . GLY B 1 325 ? -36.138 14.276 37.319 1.0 34.13 ? ? ? ? ? ? 442 GLY B N 1 325 B B +ATOM 7922 C CA . GLY B 1 325 ? -36.581 13.151 36.517 1.0 41.01 ? ? ? ? ? ? 442 GLY B CA 1 325 B B +ATOM 7923 C C . GLY B 1 325 ? -37.110 13.663 35.192 1.0 42.69 ? ? ? ? ? ? 442 GLY B C 1 325 B B +ATOM 7924 O O . GLY B 1 325 ? -37.046 12.983 34.165 1.0 47.02 ? ? ? ? ? ? 442 GLY B O 1 325 B B +ATOM 7925 N N . ILE B 1 326 ? -37.639 14.880 35.223 1.0 24.56 ? ? ? ? ? ? 443 ILE B N 1 326 B B +ATOM 7926 C CA . ILE B 1 326 ? -38.163 15.516 34.026 1.0 33.86 ? ? ? ? ? ? 443 ILE B CA 1 326 B B +ATOM 7927 C C . ILE B 1 326 ? -36.970 16.035 33.231 1.0 24.72 ? ? ? ? ? ? 443 ILE B C 1 326 B B +ATOM 7928 O O . ILE B 1 326 ? -36.845 15.784 32.035 1.0 26.74 ? ? ? ? ? ? 443 ILE B O 1 326 B B +ATOM 7929 C CB . ILE B 1 326 ? -39.085 16.689 34.399 1.0 33.65 ? ? ? ? ? ? 443 ILE B CB 1 326 B B +ATOM 7930 C CG1 . ILE B 1 326 ? -40.372 16.143 35.020 1.0 18.45 ? ? ? ? ? ? 443 ILE B CG1 1 326 B B +ATOM 7931 C CG2 . ILE B 1 326 ? -39.386 17.535 33.174 1.0 31.9 ? ? ? ? ? ? 443 ILE B CG2 1 326 B B +ATOM 7932 C CD1 . ILE B 1 326 ? -41.346 17.198 35.466 1.0 28.89 ? ? ? ? ? ? 443 ILE B CD1 1 326 B B +ATOM 7933 N N . LEU B 1 327 ? -36.093 16.752 33.928 1.0 24.82 ? ? ? ? ? ? 444 LEU B N 1 327 B B +ATOM 7934 C CA . LEU B 1 327 ? -34.885 17.326 33.348 1.0 19.51 ? ? ? ? ? ? 444 LEU B CA 1 327 B B +ATOM 7935 C C . LEU B 1 327 ? -34.037 16.268 32.642 1.0 24.69 ? ? ? ? ? ? 444 LEU B C 1 327 B B +ATOM 7936 O O . LEU B 1 327 ? -33.402 16.549 31.622 1.0 14.93 ? ? ? ? ? ? 444 LEU B O 1 327 B B +ATOM 7937 C CB . LEU B 1 327 ? -34.068 18.008 34.451 1.0 17.16 ? ? ? ? ? ? 444 LEU B CB 1 327 B B +ATOM 7938 C CG . LEU B 1 327 ? -32.841 18.845 34.070 1.0 13.22 ? ? ? ? ? ? 444 LEU B CG 1 327 B B +ATOM 7939 C CD1 . LEU B 1 327 ? -32.948 19.380 32.654 1.0 5.57 ? ? ? ? ? ? 444 LEU B CD1 1 327 B B +ATOM 7940 C CD2 . LEU B 1 327 ? -32.719 19.986 35.052 1.0 25.1 ? ? ? ? ? ? 444 LEU B CD2 1 327 B B +ATOM 7941 N N . CYS B 1 328 ? -34.033 15.058 33.195 1.0 16.52 ? ? ? ? ? ? 445 CYS B N 1 328 B B +ATOM 7942 C CA . CYS B 1 328 ? -33.288 13.942 32.626 1.0 23.91 ? ? ? ? ? ? 445 CYS B CA 1 328 B B +ATOM 7943 C C . CYS B 1 328 ? -33.978 13.425 31.367 1.0 35.9 ? ? ? ? ? ? 445 CYS B C 1 328 B B +ATOM 7944 O O . CYS B 1 328 ? -33.385 13.413 30.291 1.0 52.53 ? ? ? ? ? ? 445 CYS B O 1 328 B B +ATOM 7945 C CB . CYS B 1 328 ? -33.177 12.806 33.636 1.0 21.95 ? ? ? ? ? ? 445 CYS B CB 1 328 B B +ATOM 7946 S SG . CYS B 1 328 ? -31.986 13.104 34.932 1.0 40.86 ? ? ? ? ? ? 445 CYS B SG 1 328 B B +ATOM 7947 N N . SER B 1 329 ? -35.231 12.996 31.509 1.0 36.2 ? ? ? ? ? ? 446 SER B N 1 329 B B +ATOM 7948 C CA . SER B 1 329 ? -36.011 12.475 30.384 1.0 35.38 ? ? ? ? ? ? 446 SER B CA 1 329 B B +ATOM 7949 C C . SER B 1 329 ? -35.928 13.433 29.200 1.0 32.96 ? ? ? ? ? ? 446 SER B C 1 329 B B +ATOM 7950 O O . SER B 1 329 ? -35.768 13.011 28.054 1.0 47.99 ? ? ? ? ? ? 446 SER B O 1 329 B B +ATOM 7951 C CB . SER B 1 329 ? -37.474 12.291 30.797 1.0 52.34 ? ? ? ? ? ? 446 SER B CB 1 329 B B +ATOM 7952 O OG . SER B 1 329 ? -37.602 11.335 31.836 1.0 95.09 ? ? ? ? ? ? 446 SER B OG 1 329 B B +ATOM 7953 N N . ALA B 1 330 ? -36.041 14.726 29.491 1.0 22.5 ? ? ? ? ? ? 447 ALA B N 1 330 B B +ATOM 7954 C CA . ALA B 1 330 ? -35.963 15.759 28.468 1.0 19.89 ? ? ? ? ? ? 447 ALA B CA 1 330 B B +ATOM 7955 C C . ALA B 1 330 ? -34.593 15.672 27.811 1.0 39.54 ? ? ? ? ? ? 447 ALA B C 1 330 B B +ATOM 7956 O O . ALA B 1 330 ? -34.479 15.496 26.596 1.0 45.35 ? ? ? ? ? ? 447 ALA B O 1 330 B B +ATOM 7957 C CB . ALA B 1 330 ? -36.155 17.138 29.093 1.0 21.1 ? ? ? ? ? ? 447 ALA B CB 1 330 B B +ATOM 7958 N N . LEU B 1 331 ? -33.553 15.788 28.631 1.0 52.94 ? ? ? ? ? ? 448 LEU B N 1 331 B B +ATOM 7959 C CA . LEU B 1 331 ? -32.177 15.724 28.153 1.0 46.98 ? ? ? ? ? ? 448 LEU B CA 1 331 B B +ATOM 7960 C C . LEU B 1 331 ? -31.920 14.453 27.357 1.0 43.58 ? ? ? ? ? ? 448 LEU B C 1 331 B B +ATOM 7961 O O . LEU B 1 331 ? -31.272 14.489 26.315 1.0 57.61 ? ? ? ? ? ? 448 LEU B O 1 331 B B +ATOM 7962 C CB . LEU B 1 331 ? -31.207 15.793 29.332 1.0 21.33 ? ? ? ? ? ? 448 LEU B CB 1 331 B B +ATOM 7963 C CG . LEU B 1 331 ? -30.956 17.199 29.876 1.0 30.43 ? ? ? ? ? ? 448 LEU B CG 1 331 B B +ATOM 7964 C CD1 . LEU B 1 331 ? -30.039 17.117 31.079 1.0 22.31 ? ? ? ? ? ? 448 LEU B CD1 1 331 B B +ATOM 7965 C CD2 . LEU B 1 331 ? -30.343 18.070 28.792 1.0 19.85 ? ? ? ? ? ? 448 LEU B CD2 1 331 B B +ATOM 7966 N N . GLN B 1 332 ? -32.423 13.331 27.857 1.0 31.83 ? ? ? ? ? ? 449 GLN B N 1 332 B B +ATOM 7967 C CA . GLN B 1 332 ? -32.240 12.050 27.188 1.0 51.09 ? ? ? ? ? ? 449 GLN B CA 1 332 B B +ATOM 7968 C C . GLN B 1 332 ? -32.799 12.068 25.771 1.0 57.6 ? ? ? ? ? ? 449 GLN B C 1 332 B B +ATOM 7969 O O . GLN B 1 332 ? -32.375 11.291 24.912 1.0 84.67 ? ? ? ? ? ? 449 GLN B O 1 332 B B +ATOM 7970 C CB . GLN B 1 332 ? -32.931 10.931 27.977 1.0 60.51 ? ? ? ? ? ? 449 GLN B CB 1 332 B B +ATOM 7971 C CG . GLN B 1 332 ? -32.390 10.716 29.379 1.0 85.66 ? ? ? ? ? ? 449 GLN B CG 1 332 B B +ATOM 7972 C CD . GLN B 1 332 ? -30.877 10.749 29.438 1.0 87.05 ? ? ? ? ? ? 449 GLN B CD 1 332 B B +ATOM 7973 O OE1 . GLN B 1 332 ? -30.292 11.439 30.274 1.0 92.85 ? ? ? ? ? ? 449 GLN B OE1 1 332 B B +ATOM 7974 N NE2 . GLN B 1 332 ? -30.233 10.001 28.549 1.0 86.96 ? ? ? ? ? ? 449 GLN B NE2 1 332 B B +ATOM 7975 N N . LYS B 1 333 ? -33.753 12.958 25.529 1.0 51.88 ? ? ? ? ? ? 450 LYS B N 1 333 B B +ATOM 7976 C CA . LYS B 1 333 ? -34.376 13.044 24.220 1.0 58.83 ? ? ? ? ? ? 450 LYS B CA 1 333 B B +ATOM 7977 C C . LYS B 1 333 ? -33.770 14.112 23.319 1.0 53.86 ? ? ? ? ? ? 450 LYS B C 1 333 B B +ATOM 7978 O O . LYS B 1 333 ? -34.303 14.392 22.245 1.0 60.53 ? ? ? ? ? ? 450 LYS B O 1 333 B B +ATOM 7979 C CB . LYS B 1 333 ? -35.873 13.299 24.388 1.0 52.01 ? ? ? ? ? ? 450 LYS B CB 1 333 B B +ATOM 7980 C CG . LYS B 1 333 ? -36.623 12.113 24.955 1.0 48.95 ? ? ? ? ? ? 450 LYS B CG 1 333 B B +ATOM 7981 C CD . LYS B 1 333 ? -38.073 12.453 25.219 1.0 31.16 ? ? ? ? ? ? 450 LYS B CD 1 333 B B +ATOM 7982 C CE . LYS B 1 333 ? -38.803 11.265 25.814 1.0 42.41 ? ? ? ? ? ? 450 LYS B CE 1 333 B B +ATOM 7983 N NZ . LYS B 1 333 ? -38.154 10.823 27.075 1.0 60.56 ? ? ? ? ? ? 450 LYS B NZ 1 333 B B +ATOM 7984 N N . ILE B 1 334 ? -32.655 14.699 23.747 1.0 54.92 ? ? ? ? ? ? 451 ILE B N 1 334 B B +ATOM 7985 C CA . ILE B 1 334 ? -32.010 15.740 22.954 1.0 69.53 ? ? ? ? ? ? 451 ILE B CA 1 334 B B +ATOM 7986 C C . ILE B 1 334 ? -30.631 15.361 22.425 1.0 70.22 ? ? ? ? ? ? 451 ILE B C 1 334 B B +ATOM 7987 O O . ILE B 1 334 ? -29.628 16.005 22.734 1.0 50.03 ? ? ? ? ? ? 451 ILE B O 1 334 B B +ATOM 7988 C CB . ILE B 1 334 ? -31.906 17.071 23.746 1.0 76.55 ? ? ? ? ? ? 451 ILE B CB 1 334 B B +ATOM 7989 C CG1 . ILE B 1 334 ? -31.476 18.198 22.800 1.0 81.46 ? ? ? ? ? ? 451 ILE B CG1 1 334 B B +ATOM 7990 C CG2 . ILE B 1 334 ? -30.936 16.924 24.910 1.0 52.0 ? ? ? ? ? ? 451 ILE B CG2 1 334 B B +ATOM 7991 C CD1 . ILE B 1 334 ? -32.445 18.456 21.660 1.0 67.09 ? ? ? ? ? ? 451 ILE B CD1 1 334 B B +ATOM 7992 N N . LYS B 1 335 ? -30.594 14.309 21.615 1.0 88.57 ? ? ? ? ? ? 452 LYS B N 1 335 B B +ATOM 7993 C CA . LYS B 1 335 ? -29.349 13.850 21.024 1.0 99.23 ? ? ? ? ? ? 452 LYS B CA 1 335 B B +ATOM 7994 C C . LYS B 1 335 ? -29.173 14.512 19.652 1.0 100.0 ? ? ? ? ? ? 452 LYS B C 1 335 B B +ATOM 7995 O O . LYS B 1 335 ? -28.190 15.265 19.474 1.0 100.0 ? ? ? ? ? ? 452 LYS B O 1 335 B B +ATOM 7996 C CB . LYS B 1 335 ? -29.371 12.324 20.877 1.0 91.96 ? ? ? ? ? ? 452 LYS B CB 1 335 B B +ATOM 7997 C CG . LYS B 1 335 ? -28.133 11.748 20.217 1.0 84.44 ? ? ? ? ? ? 452 LYS B CG 1 335 B B +ATOM 7998 C CD . LYS B 1 335 ? -28.153 10.228 20.240 1.0 72.11 ? ? ? ? ? ? 452 LYS B CD 1 335 B B +ATOM 7999 C CE . LYS B 1 335 ? -29.142 9.672 19.230 1.0 71.82 ? ? ? ? ? ? 452 LYS B CE 1 335 B B +ATOM 8000 N NZ . LYS B 1 335 ? -28.710 9.937 17.832 1.0 70.5 ? ? ? ? ? ? 452 LYS B NZ 1 335 B B +ATOM 8001 O OXT . LYS B 1 335 ? -30.029 14.278 18.772 1.0 100.0 ? ? ? ? ? ? 452 LYS B OXT 1 335 B B +ATOM 8002 N N . VAL BA 1 1 ? -49.841 13.503 17.071 1.0 64.02 ? ? ? ? ? ? 118 VAL BA N 1 1 B B +ATOM 8003 C CA . VAL BA 1 1 ? -49.843 13.581 18.561 1.0 64.44 ? ? ? ? ? ? 118 VAL BA CA 1 1 B B +ATOM 8004 C C . VAL BA 1 1 ? -51.131 14.218 19.082 1.0 65.24 ? ? ? ? ? ? 118 VAL BA C 1 1 B B +ATOM 8005 O O . VAL BA 1 1 ? -51.477 15.342 18.707 1.0 63.74 ? ? ? ? ? ? 118 VAL BA O 1 1 B B +ATOM 8006 C CB . VAL BA 1 1 ? -48.650 14.408 19.069 1.0 65.74 ? ? ? ? ? ? 118 VAL BA CB 1 1 B B +ATOM 8007 C CG1 . VAL BA 1 1 ? -48.714 14.537 20.581 1.0 65.62 ? ? ? ? ? ? 118 VAL BA CG1 1 1 B B +ATOM 8008 C CG2 . VAL BA 1 1 ? -47.355 13.747 18.648 1.0 53.75 ? ? ? ? ? ? 118 VAL BA CG2 1 1 B B +ATOM 8009 N N . PRO BA 1 2 ? -51.843 13.515 19.983 1.0 55.61 ? ? ? ? ? ? 119 PRO BA N 1 2 B B +ATOM 8010 C CA . PRO BA 1 2 ? -53.099 14.026 20.546 1.0 61.71 ? ? ? ? ? ? 119 PRO BA CA 1 2 B B +ATOM 8011 C C . PRO BA 1 2 ? -52.960 15.426 21.113 1.0 64.92 ? ? ? ? ? ? 119 PRO BA C 1 2 B B +ATOM 8012 O O . PRO BA 1 2 ? -51.897 15.802 21.598 1.0 81.22 ? ? ? ? ? ? 119 PRO BA O 1 2 B B +ATOM 8013 C CB . PRO BA 1 2 ? -53.454 13.011 21.630 1.0 49.01 ? ? ? ? ? ? 119 PRO BA CB 1 2 B B +ATOM 8014 C CG . PRO BA 1 2 ? -52.724 11.779 21.259 1.0 55.79 ? ? ? ? ? ? 119 PRO BA CG 1 2 B B +ATOM 8015 C CD . PRO BA 1 2 ? -51.478 12.206 20.547 1.0 51.02 ? ? ? ? ? ? 119 PRO BA CD 1 2 B B +ATOM 8016 N N . TRP BA 1 3 ? -54.044 16.191 21.060 1.0 64.84 ? ? ? ? ? ? 120 TRP BA N 1 3 B B +ATOM 8017 C CA . TRP BA 1 3 ? -54.039 17.551 21.587 1.0 62.46 ? ? ? ? ? ? 120 TRP BA CA 1 3 B B +ATOM 8018 C C . TRP BA 1 3 ? -54.232 17.519 23.099 1.0 69.96 ? ? ? ? ? ? 120 TRP BA C 1 3 B B +ATOM 8019 O O . TRP BA 1 3 ? -55.020 16.727 23.618 1.0 76.89 ? ? ? ? ? ? 120 TRP BA O 1 3 B B +ATOM 8020 C CB . TRP BA 1 3 ? -55.160 18.380 20.950 1.0 59.09 ? ? ? ? ? ? 120 TRP BA CB 1 3 B B +ATOM 8021 C CG . TRP BA 1 3 ? -55.330 19.741 21.568 1.0 48.35 ? ? ? ? ? ? 120 TRP BA CG 1 3 B B +ATOM 8022 C CD1 . TRP BA 1 3 ? -54.805 20.916 21.117 1.0 34.32 ? ? ? ? ? ? 120 TRP BA CD1 1 3 B B +ATOM 8023 C CD2 . TRP BA 1 3 ? -56.061 20.060 22.760 1.0 46.82 ? ? ? ? ? ? 120 TRP BA CD2 1 3 B B +ATOM 8024 N NE1 . TRP BA 1 3 ? -55.168 21.948 21.949 1.0 51.44 ? ? ? ? ? ? 120 TRP BA NE1 1 3 B B +ATOM 8025 C CE2 . TRP BA 1 3 ? -55.939 21.451 22.967 1.0 51.56 ? ? ? ? ? ? 120 TRP BA CE2 1 3 B B +ATOM 8026 C CE3 . TRP BA 1 3 ? -56.817 19.306 23.670 1.0 33.47 ? ? ? ? ? ? 120 TRP BA CE3 1 3 B B +ATOM 8027 C CZ2 . TRP BA 1 3 ? -56.542 22.107 24.047 1.0 52.85 ? ? ? ? ? ? 120 TRP BA CZ2 1 3 B B +ATOM 8028 C CZ3 . TRP BA 1 3 ? -57.412 19.957 24.748 1.0 52.35 ? ? ? ? ? ? 120 TRP BA CZ3 1 3 B B +ATOM 8029 C CH2 . TRP BA 1 3 ? -57.268 21.343 24.927 1.0 61.87 ? ? ? ? ? ? 120 TRP BA CH2 1 3 B B +ATOM 8030 N N . PHE BA 1 4 ? -53.502 18.383 23.797 1.0 63.41 ? ? ? ? ? ? 121 PHE BA N 1 4 B B +ATOM 8031 C CA . PHE BA 1 4 ? -53.601 18.476 25.248 1.0 55.67 ? ? ? ? ? ? 121 PHE BA CA 1 4 B B +ATOM 8032 C C . PHE BA 1 4 ? -53.556 19.937 25.701 1.0 55.41 ? ? ? ? ? ? 121 PHE BA C 1 4 B B +ATOM 8033 O O . PHE BA 1 4 ? -52.940 20.789 25.049 1.0 47.46 ? ? ? ? ? ? 121 PHE BA O 1 4 B B +ATOM 8034 C CB . PHE BA 1 4 ? -52.475 17.675 25.917 1.0 69.65 ? ? ? ? ? ? 121 PHE BA CB 1 4 B B +ATOM 8035 C CG . PHE BA 1 4 ? -51.095 18.181 25.609 1.0 69.25 ? ? ? ? ? ? 121 PHE BA CG 1 4 B B +ATOM 8036 C CD1 . PHE BA 1 4 ? -50.546 19.228 26.342 1.0 68.38 ? ? ? ? ? ? 121 PHE BA CD1 1 4 B B +ATOM 8037 C CD2 . PHE BA 1 4 ? -50.339 17.602 24.597 1.0 67.23 ? ? ? ? ? ? 121 PHE BA CD2 1 4 B B +ATOM 8038 C CE1 . PHE BA 1 4 ? -49.265 19.693 26.073 1.0 65.36 ? ? ? ? ? ? 121 PHE BA CE1 1 4 B B +ATOM 8039 C CE2 . PHE BA 1 4 ? -49.056 18.060 24.319 1.0 80.74 ? ? ? ? ? ? 121 PHE BA CE2 1 4 B B +ATOM 8040 C CZ . PHE BA 1 4 ? -48.517 19.108 25.059 1.0 63.51 ? ? ? ? ? ? 121 PHE BA CZ 1 4 B B +ATOM 8041 N N . PRO BA 1 5 ? -54.218 20.245 26.830 1.0 45.57 ? ? ? ? ? ? 122 PRO BA N 1 5 B B +ATOM 8042 C CA . PRO BA 1 5 ? -54.255 21.611 27.373 1.0 40.03 ? ? ? ? ? ? 122 PRO BA CA 1 5 B B +ATOM 8043 C C . PRO BA 1 5 ? -52.897 22.144 27.830 1.0 48.47 ? ? ? ? ? ? 122 PRO BA C 1 5 B B +ATOM 8044 O O . PRO BA 1 5 ? -52.167 21.479 28.566 1.0 63.33 ? ? ? ? ? ? 122 PRO BA O 1 5 B B +ATOM 8045 C CB . PRO BA 1 5 ? -55.251 21.512 28.529 1.0 34.57 ? ? ? ? ? ? 122 PRO BA CB 1 5 B B +ATOM 8046 C CG . PRO BA 1 5 ? -55.236 20.077 28.912 1.0 38.44 ? ? ? ? ? ? 122 PRO BA CG 1 5 B B +ATOM 8047 C CD . PRO BA 1 5 ? -54.979 19.300 27.664 1.0 36.86 ? ? ? ? ? ? 122 PRO BA CD 1 5 B B +ATOM 8048 N N . ARG BA 1 6 ? -52.564 23.348 27.380 1.0 46.91 ? ? ? ? ? ? 123 ARG BA N 1 6 B B +ATOM 8049 C CA . ARG BA 1 6 ? -51.310 23.984 27.755 1.0 55.38 ? ? ? ? ? ? 123 ARG BA CA 1 6 B B +ATOM 8050 C C . ARG BA 1 6 ? -51.564 24.869 28.969 1.0 60.11 ? ? ? ? ? ? 123 ARG BA C 1 6 B B +ATOM 8051 O O . ARG BA 1 6 ? -50.705 25.006 29.837 1.0 74.63 ? ? ? ? ? ? 123 ARG BA O 1 6 B B +ATOM 8052 C CB . ARG BA 1 6 ? -50.777 24.832 26.597 1.0 82.66 ? ? ? ? ? ? 123 ARG BA CB 1 6 B B +ATOM 8053 C CG . ARG BA 1 6 ? -50.640 24.079 25.282 1.0 92.03 ? ? ? ? ? ? 123 ARG BA CG 1 6 B B +ATOM 8054 C CD . ARG BA 1 6 ? -49.480 23.101 25.327 1.0 83.78 ? ? ? ? ? ? 123 ARG BA CD 1 6 B B +ATOM 8055 N NE . ARG BA 1 6 ? -48.990 22.782 23.991 1.0 86.12 ? ? ? ? ? ? 123 ARG BA NE 1 6 B B +ATOM 8056 C CZ . ARG BA 1 6 ? -48.012 23.441 23.376 1.0 100.0 ? ? ? ? ? ? 123 ARG BA CZ 1 6 B B +ATOM 8057 N NH1 . ARG BA 1 6 ? -47.414 24.463 23.975 1.0 90.04 ? ? ? ? ? ? 123 ARG BA NH1 1 6 B B +ATOM 8058 N NH2 . ARG BA 1 6 ? -47.636 23.079 22.156 1.0 100.0 ? ? ? ? ? ? 123 ARG BA NH2 1 6 B B +ATOM 8059 N N . THR BA 1 7 ? -52.752 25.466 29.020 1.0 58.91 ? ? ? ? ? ? 124 THR BA N 1 7 B B +ATOM 8060 C CA . THR BA 1 7 ? -53.135 26.339 30.127 1.0 55.42 ? ? ? ? ? ? 124 THR BA CA 1 7 B B +ATOM 8061 C C . THR BA 1 7 ? -54.268 25.720 30.926 1.0 55.81 ? ? ? ? ? ? 124 THR BA C 1 7 B B +ATOM 8062 O O . THR BA 1 7 ? -55.013 24.877 30.424 1.0 56.63 ? ? ? ? ? ? 124 THR BA O 1 7 B B +ATOM 8063 C CB . THR BA 1 7 ? -53.619 27.718 29.643 1.0 49.31 ? ? ? ? ? ? 124 THR BA CB 1 7 B B +ATOM 8064 O OG1 . THR BA 1 7 ? -52.707 28.234 28.670 1.0 60.93 ? ? ? ? ? ? 124 THR BA OG1 1 7 B B +ATOM 8065 C CG2 . THR BA 1 7 ? -53.695 28.689 30.809 1.0 53.17 ? ? ? ? ? ? 124 THR BA CG2 1 7 B B +ATOM 8066 N N . ILE BA 1 8 ? -54.391 26.160 32.173 1.0 55.49 ? ? ? ? ? ? 125 ILE BA N 1 8 B B +ATOM 8067 C CA . ILE BA 1 8 ? -55.420 25.672 33.079 1.0 57.08 ? ? ? ? ? ? 125 ILE BA CA 1 8 B B +ATOM 8068 C C . ILE BA 1 8 ? -56.809 26.074 32.588 1.0 63.27 ? ? ? ? ? ? 125 ILE BA C 1 8 B B +ATOM 8069 O O . ILE BA 1 8 ? -57.790 25.364 32.819 1.0 54.52 ? ? ? ? ? ? 125 ILE BA O 1 8 B B +ATOM 8070 C CB . ILE BA 1 8 ? -55.202 26.236 34.502 1.0 50.66 ? ? ? ? ? ? 125 ILE BA CB 1 8 B B +ATOM 8071 C CG1 . ILE BA 1 8 ? -56.138 25.546 35.494 1.0 33.1 ? ? ? ? ? ? 125 ILE BA CG1 1 8 B B +ATOM 8072 C CG2 . ILE BA 1 8 ? -55.435 27.741 34.504 1.0 37.48 ? ? ? ? ? ? 125 ILE BA CG2 1 8 B B +ATOM 8073 C CD1 . ILE BA 1 8 ? -55.626 25.549 36.925 1.0 60.02 ? ? ? ? ? ? 125 ILE BA CD1 1 8 B B +ATOM 8074 N N . GLN BA 1 9 ? -56.881 27.213 31.905 1.0 61.65 ? ? ? ? ? ? 126 GLN BA N 1 9 B B +ATOM 8075 C CA . GLN BA 1 9 ? -58.147 27.718 31.386 1.0 67.34 ? ? ? ? ? ? 126 GLN BA CA 1 9 B B +ATOM 8076 C C . GLN BA 1 9 ? -58.558 26.989 30.113 1.0 61.48 ? ? ? ? ? ? 126 GLN BA C 1 9 B B +ATOM 8077 O O . GLN BA 1 9 ? -59.690 27.120 29.651 1.0 71.35 ? ? ? ? ? ? 126 GLN BA O 1 9 B B +ATOM 8078 C CB . GLN BA 1 9 ? -58.034 29.216 31.103 1.0 70.45 ? ? ? ? ? ? 126 GLN BA CB 1 9 B B +ATOM 8079 C CG . GLN BA 1 9 ? -57.553 30.032 32.287 1.0 85.51 ? ? ? ? ? ? 126 GLN BA CG 1 9 B B +ATOM 8080 C CD . GLN BA 1 9 ? -56.109 30.465 32.146 1.0 92.67 ? ? ? ? ? ? 126 GLN BA CD 1 9 B B +ATOM 8081 O OE1 . GLN BA 1 9 ? -55.668 30.857 31.066 1.0 100.0 ? ? ? ? ? ? 126 GLN BA OE1 1 9 B B +ATOM 8082 N NE2 . GLN BA 1 9 ? -55.364 30.402 33.242 1.0 88.41 ? ? ? ? ? ? 126 GLN BA NE2 1 9 B B +ATOM 8083 N N . GLU BA 1 10 ? -57.628 26.226 29.549 1.0 55.05 ? ? ? ? ? ? 127 GLU BA N 1 10 B B +ATOM 8084 C CA . GLU BA 1 10 ? -57.884 25.480 28.323 1.0 54.75 ? ? ? ? ? ? 127 GLU BA CA 1 10 B B +ATOM 8085 C C . GLU BA 1 10 ? -58.723 24.233 28.566 1.0 57.03 ? ? ? ? ? ? 127 GLU BA C 1 10 B B +ATOM 8086 O O . GLU BA 1 10 ? -59.061 23.511 27.628 1.0 52.57 ? ? ? ? ? ? 127 GLU BA O 1 10 B B +ATOM 8087 C CB . GLU BA 1 10 ? -56.566 25.083 27.668 1.0 56.8 ? ? ? ? ? ? 127 GLU BA CB 1 10 B B +ATOM 8088 C CG . GLU BA 1 10 ? -55.745 26.264 27.189 1.0 59.86 ? ? ? ? ? ? 127 GLU BA CG 1 10 B B +ATOM 8089 C CD . GLU BA 1 10 ? -54.847 25.903 26.025 1.0 72.86 ? ? ? ? ? ? 127 GLU BA CD 1 10 B B +ATOM 8090 O OE1 . GLU BA 1 10 ? -54.664 24.690 25.777 1.0 78.5 ? ? ? ? ? ? 127 GLU BA OE1 1 10 B B +ATOM 8091 O OE2 . GLU BA 1 10 ? -54.330 26.830 25.360 1.0 70.93 ? ? ? ? ? ? 127 GLU BA OE2 1 10 B B +ATOM 8092 N N . LEU BA 1 11 ? -59.047 23.984 29.831 1.0 57.23 ? ? ? ? ? ? 128 LEU BA N 1 11 B B +ATOM 8093 C CA . LEU BA 1 11 ? -59.853 22.830 30.203 1.0 65.38 ? ? ? ? ? ? 128 LEU BA CA 1 11 B B +ATOM 8094 C C . LEU BA 1 11 ? -61.318 23.153 29.918 1.0 76.67 ? ? ? ? ? ? 128 LEU BA C 1 11 B B +ATOM 8095 O O . LEU BA 1 11 ? -62.210 22.321 30.127 1.0 82.72 ? ? ? ? ? ? 128 LEU BA O 1 11 B B +ATOM 8096 C CB . LEU BA 1 11 ? -59.673 22.513 31.691 1.0 61.86 ? ? ? ? ? ? 128 LEU BA CB 1 11 B B +ATOM 8097 C CG . LEU BA 1 11 ? -58.263 22.149 32.168 1.0 74.01 ? ? ? ? ? ? 128 LEU BA CG 1 11 B B +ATOM 8098 C CD1 . LEU BA 1 11 ? -58.277 21.896 33.665 1.0 63.92 ? ? ? ? ? ? 128 LEU BA CD1 1 11 B B +ATOM 8099 C CD2 . LEU BA 1 11 ? -57.770 20.919 31.430 1.0 76.84 ? ? ? ? ? ? 128 LEU BA CD2 1 11 B B +ATOM 8100 N N . ASP BA 1 12 ? -61.555 24.369 29.434 1.0 73.58 ? ? ? ? ? ? 129 ASP BA N 1 12 B B +ATOM 8101 C CA . ASP BA 1 12 ? -62.901 24.820 29.116 1.0 72.89 ? ? ? ? ? ? 129 ASP BA CA 1 12 B B +ATOM 8102 C C . ASP BA 1 12 ? -63.470 24.095 27.900 1.0 77.94 ? ? ? ? ? ? 129 ASP BA C 1 12 B B +ATOM 8103 O O . ASP BA 1 12 ? -64.585 24.374 27.469 1.0 91.15 ? ? ? ? ? ? 129 ASP BA O 1 12 B B +ATOM 8104 C CB . ASP BA 1 12 ? -62.905 26.330 28.872 1.0 66.61 ? ? ? ? ? ? 129 ASP BA CB 1 12 B B +ATOM 8105 C CG . ASP BA 1 12 ? -62.662 27.126 30.140 1.0 77.18 ? ? ? ? ? ? 129 ASP BA CG 1 12 B B +ATOM 8106 O OD1 . ASP BA 1 12 ? -62.799 26.554 31.244 1.0 70.03 ? ? ? ? ? ? 129 ASP BA OD1 1 12 B B +ATOM 8107 O OD2 . ASP BA 1 12 ? -62.335 28.324 30.028 1.0 78.15 ? ? ? ? ? ? 129 ASP BA OD2 1 12 B B +ATOM 8108 N N . ARG BA 1 13 ? -62.722 23.141 27.362 1.0 77.77 ? ? ? ? ? ? 130 ARG BA N 1 13 B B +ATOM 8109 C CA . ARG BA 1 13 ? -63.190 22.404 26.200 1.0 77.83 ? ? ? ? ? ? 130 ARG BA CA 1 13 B B +ATOM 8110 C C . ARG BA 1 13 ? -63.949 21.141 26.594 1.0 89.16 ? ? ? ? ? ? 130 ARG BA C 1 13 B B +ATOM 8111 O O . ARG BA 1 13 ? -64.019 20.836 27.804 1.0 93.49 ? ? ? ? ? ? 130 ARG BA O 1 13 B B +ATOM 8112 C CB . ARG BA 1 13 ? -62.008 22.041 25.303 1.0 79.04 ? ? ? ? ? ? 130 ARG BA CB 1 13 B B +ATOM 8113 C CG . ARG BA 1 13 ? -60.909 23.091 25.267 1.0 92.88 ? ? ? ? ? ? 130 ARG BA CG 1 13 B B +ATOM 8114 C CD . ARG BA 1 13 ? -61.464 24.487 25.035 1.0 93.62 ? ? ? ? ? ? 130 ARG BA CD 1 13 B B +ATOM 8115 N NE . ARG BA 1 13 ? -61.997 24.649 23.684 1.0 100.0 ? ? ? ? ? ? 130 ARG BA NE 1 13 B B +ATOM 8116 C CZ . ARG BA 1 13 ? -61.250 24.856 22.603 1.0 100.0 ? ? ? ? ? ? 130 ARG BA CZ 1 13 B B +ATOM 8117 N NH1 . ARG BA 1 13 ? -59.930 24.932 22.711 1.0 100.0 ? ? ? ? ? ? 130 ARG BA NH1 1 13 B B +ATOM 8118 N NH2 . ARG BA 1 13 ? -61.824 24.990 21.414 1.0 96.27 ? ? ? ? ? ? 130 ARG BA NH2 1 13 B B +ATOM 8119 N N . ALA BA 1 27 ? -82.119 3.030 30.115 1.0 87.98 ? ? ? ? ? ? 144 ALA BA N 1 27 B B +ATOM 8120 C CA . ALA BA 1 27 ? -83.272 2.972 31.057 1.0 85.44 ? ? ? ? ? ? 144 ALA BA CA 1 27 B B +ATOM 8121 C C . ALA BA 1 27 ? -82.919 2.189 32.314 1.0 93.15 ? ? ? ? ? ? 144 ALA BA C 1 27 B B +ATOM 8122 O O . ALA BA 1 27 ? -83.568 2.338 33.350 1.0 100.0 ? ? ? ? ? ? 144 ALA BA O 1 27 B B +ATOM 8123 C CB . ALA BA 1 27 ? -84.475 2.337 30.373 1.0 82.44 ? ? ? ? ? ? 144 ALA BA CB 1 27 B B +ATOM 8124 N N . ASP BA 1 28 ? -81.890 1.351 32.224 1.0 96.64 ? ? ? ? ? ? 145 ASP BA N 1 28 B B +ATOM 8125 C CA . ASP BA 1 28 ? -81.466 0.553 33.372 1.0 97.12 ? ? ? ? ? ? 145 ASP BA CA 1 28 B B +ATOM 8126 C C . ASP BA 1 28 ? -81.090 1.458 34.544 1.0 91.65 ? ? ? ? ? ? 145 ASP BA C 1 28 B B +ATOM 8127 O O . ASP BA 1 28 ? -81.002 1.009 35.689 1.0 74.72 ? ? ? ? ? ? 145 ASP BA O 1 28 B B +ATOM 8128 C CB . ASP BA 1 28 ? -80.270 -0.324 32.996 1.0 97.58 ? ? ? ? ? ? 145 ASP BA CB 1 28 B B +ATOM 8129 C CG . ASP BA 1 28 ? -79.050 0.490 32.615 1.0 100.0 ? ? ? ? ? ? 145 ASP BA CG 1 28 B B +ATOM 8130 O OD1 . ASP BA 1 28 ? -79.124 1.246 31.625 1.0 89.65 ? ? ? ? ? ? 145 ASP BA OD1 1 28 B B +ATOM 8131 O OD2 . ASP BA 1 28 ? -78.013 0.371 33.303 1.0 100.0 ? ? ? ? ? ? 145 ASP BA OD2 1 28 B B +ATOM 8132 N N . HIS BA 1 29 ? -80.875 2.736 34.248 1.0 93.74 ? ? ? ? ? ? 146 HIS BA N 1 29 B B +ATOM 8133 C CA . HIS BA 1 29 ? -80.503 3.715 35.261 1.0 95.79 ? ? ? ? ? ? 146 HIS BA CA 1 29 B B +ATOM 8134 C C . HIS BA 1 29 ? -81.669 4.020 36.197 1.0 87.42 ? ? ? ? ? ? 146 HIS BA C 1 29 B B +ATOM 8135 O O . HIS BA 1 29 ? -82.748 4.418 35.755 1.0 88.11 ? ? ? ? ? ? 146 HIS BA O 1 29 B B +ATOM 8136 C CB . HIS BA 1 29 ? -80.025 5.011 34.589 1.0 100.0 ? ? ? ? ? ? 146 HIS BA CB 1 29 B B +ATOM 8137 C CG . HIS BA 1 29 ? -79.622 6.088 35.552 1.0 100.0 ? ? ? ? ? ? 146 HIS BA CG 1 29 B B +ATOM 8138 N ND1 . HIS BA 1 29 ? -80.523 6.730 36.374 1.0 100.0 ? ? ? ? ? ? 146 HIS BA ND1 1 29 B B +ATOM 8139 C CD2 . HIS BA 1 29 ? -78.415 6.646 35.813 1.0 100.0 ? ? ? ? ? ? 146 HIS BA CD2 1 29 B B +ATOM 8140 C CE1 . HIS BA 1 29 ? -79.891 7.638 37.097 1.0 100.0 ? ? ? ? ? ? 146 HIS BA CE1 1 29 B B +ATOM 8141 N NE2 . HIS BA 1 29 ? -78.609 7.605 36.775 1.0 100.0 ? ? ? ? ? ? 146 HIS BA NE2 1 29 B B +ATOM 8142 N N . PRO BA 1 30 ? -81.460 3.836 37.511 1.0 74.48 ? ? ? ? ? ? 147 PRO BA N 1 30 B B +ATOM 8143 C CA . PRO BA 1 30 ? -82.525 4.107 38.484 1.0 79.69 ? ? ? ? ? ? 147 PRO BA CA 1 30 B B +ATOM 8144 C C . PRO BA 1 30 ? -82.863 5.595 38.506 1.0 84.11 ? ? ? ? ? ? 147 PRO BA C 1 30 B B +ATOM 8145 O O . PRO BA 1 30 ? -82.002 6.435 38.761 1.0 92.23 ? ? ? ? ? ? 147 PRO BA O 1 30 B B +ATOM 8146 C CB . PRO BA 1 30 ? -81.938 3.622 39.809 1.0 77.32 ? ? ? ? ? ? 147 PRO BA CB 1 30 B B +ATOM 8147 C CG . PRO BA 1 30 ? -80.459 3.646 39.601 1.0 77.89 ? ? ? ? ? ? 147 PRO BA CG 1 30 B B +ATOM 8148 C CD . PRO BA 1 30 ? -80.220 3.372 38.153 1.0 70.78 ? ? ? ? ? ? 147 PRO BA CD 1 30 B B +ATOM 8149 N N . GLY BA 1 31 ? -84.123 5.913 38.228 1.0 85.27 ? ? ? ? ? ? 148 GLY BA N 1 31 B B +ATOM 8150 C CA . GLY BA 1 31 ? -84.548 7.301 38.203 1.0 79.76 ? ? ? ? ? ? 148 GLY BA CA 1 31 B B +ATOM 8151 C C . GLY BA 1 31 ? -84.758 7.789 36.781 1.0 76.37 ? ? ? ? ? ? 148 GLY BA C 1 31 B B +ATOM 8152 O O . GLY BA 1 31 ? -85.057 8.961 36.552 1.0 76.12 ? ? ? ? ? ? 148 GLY BA O 1 31 B B +ATOM 8153 N N . PHE BA 1 32 ? -84.591 6.882 35.822 1.0 77.29 ? ? ? ? ? ? 149 PHE BA N 1 32 B B +ATOM 8154 C CA . PHE BA 1 32 ? -84.767 7.204 34.410 1.0 85.57 ? ? ? ? ? ? 149 PHE BA CA 1 32 B B +ATOM 8155 C C . PHE BA 1 32 ? -86.220 7.578 34.140 1.0 87.09 ? ? ? ? ? ? 149 PHE BA C 1 32 B B +ATOM 8156 O O . PHE BA 1 32 ? -86.514 8.396 33.265 1.0 81.98 ? ? ? ? ? ? 149 PHE BA O 1 32 B B +ATOM 8157 C CB . PHE BA 1 32 ? -84.371 5.997 33.551 1.0 93.71 ? ? ? ? ? ? 149 PHE BA CB 1 32 B B +ATOM 8158 C CG . PHE BA 1 32 ? -84.656 6.166 32.081 1.0 100.0 ? ? ? ? ? ? 149 PHE BA CG 1 32 B B +ATOM 8159 C CD1 . PHE BA 1 32 ? -83.851 6.983 31.291 1.0 100.0 ? ? ? ? ? ? 149 PHE BA CD1 1 32 B B +ATOM 8160 C CD2 . PHE BA 1 32 ? -85.712 5.487 31.480 1.0 100.0 ? ? ? ? ? ? 149 PHE BA CD2 1 32 B B +ATOM 8161 C CE1 . PHE BA 1 32 ? -84.093 7.118 29.922 1.0 100.0 ? ? ? ? ? ? 149 PHE BA CE1 1 32 B B +ATOM 8162 C CE2 . PHE BA 1 32 ? -85.960 5.617 30.111 1.0 97.35 ? ? ? ? ? ? 149 PHE BA CE2 1 32 B B +ATOM 8163 C CZ . PHE BA 1 32 ? -85.149 6.435 29.334 1.0 95.24 ? ? ? ? ? ? 149 PHE BA CZ 1 32 B B +ATOM 8164 N N . LYS BA 1 33 ? -87.126 6.980 34.908 1.0 81.0 ? ? ? ? ? ? 150 LYS BA N 1 33 B B +ATOM 8165 C CA . LYS BA 1 33 ? -88.552 7.237 34.755 1.0 78.43 ? ? ? ? ? ? 150 LYS BA CA 1 33 B B +ATOM 8166 C C . LYS BA 1 33 ? -89.010 8.441 35.579 1.0 85.73 ? ? ? ? ? ? 150 LYS BA C 1 33 B B +ATOM 8167 O O . LYS BA 1 33 ? -90.158 8.872 35.468 1.0 79.74 ? ? ? ? ? ? 150 LYS BA O 1 33 B B +ATOM 8168 C CB . LYS BA 1 33 ? -89.337 5.992 35.163 1.0 66.54 ? ? ? ? ? ? 150 LYS BA CB 1 33 B B +ATOM 8169 C CG . LYS BA 1 33 ? -88.716 4.707 34.639 1.0 77.6 ? ? ? ? ? ? 150 LYS BA CG 1 33 B B +ATOM 8170 C CD . LYS BA 1 33 ? -89.563 3.488 34.957 1.0 96.5 ? ? ? ? ? ? 150 LYS BA CD 1 33 B B +ATOM 8171 C CE . LYS BA 1 33 ? -89.110 2.289 34.129 1.0 100.0 ? ? ? ? ? ? 150 LYS BA CE 1 33 B B +ATOM 8172 N NZ . LYS BA 1 33 ? -89.967 1.089 34.342 1.0 100.0 ? ? ? ? ? ? 150 LYS BA NZ 1 33 B B +ATOM 8173 N N . ASP BA 1 34 ? -88.109 8.990 36.391 1.0 91.48 ? ? ? ? ? ? 151 ASP BA N 1 34 B B +ATOM 8174 C CA . ASP BA 1 34 ? -88.442 10.140 37.224 1.0 95.17 ? ? ? ? ? ? 151 ASP BA CA 1 34 B B +ATOM 8175 C C . ASP BA 1 34 ? -88.227 11.458 36.493 1.0 93.27 ? ? ? ? ? ? 151 ASP BA C 1 34 B B +ATOM 8176 O O . ASP BA 1 34 ? -87.093 11.881 36.284 1.0 93.13 ? ? ? ? ? ? 151 ASP BA O 1 34 B B +ATOM 8177 C CB . ASP BA 1 34 ? -87.611 10.131 38.508 1.0 99.66 ? ? ? ? ? ? 151 ASP BA CB 1 34 B B +ATOM 8178 C CG . ASP BA 1 34 ? -88.099 11.152 39.521 1.0 98.38 ? ? ? ? ? ? 151 ASP BA CG 1 34 B B +ATOM 8179 O OD1 . ASP BA 1 34 ? -88.469 12.276 39.112 1.0 75.71 ? ? ? ? ? ? 151 ASP BA OD1 1 34 B B +ATOM 8180 O OD2 . ASP BA 1 34 ? -88.111 10.836 40.728 1.0 94.6 ? ? ? ? ? ? 151 ASP BA OD2 1 34 B B +ATOM 8181 N N . PRO BA 1 35 ? -89.326 12.130 36.109 1.0 98.4 ? ? ? ? ? ? 152 PRO BA N 1 35 B B +ATOM 8182 C CA . PRO BA 1 35 ? -89.267 13.409 35.393 1.0 100.0 ? ? ? ? ? ? 152 PRO BA CA 1 35 B B +ATOM 8183 C C . PRO BA 1 35 ? -88.605 14.536 36.182 1.0 100.0 ? ? ? ? ? ? 152 PRO BA C 1 35 B B +ATOM 8184 O O . PRO BA 1 35 ? -88.001 15.436 35.595 1.0 97.06 ? ? ? ? ? ? 152 PRO BA O 1 35 B B +ATOM 8185 C CB . PRO BA 1 35 ? -90.733 13.723 35.074 1.0 97.64 ? ? ? ? ? ? 152 PRO BA CB 1 35 B B +ATOM 8186 C CG . PRO BA 1 35 ? -91.477 12.454 35.322 1.0 96.38 ? ? ? ? ? ? 152 PRO BA CG 1 35 B B +ATOM 8187 C CD . PRO BA 1 35 ? -90.710 11.705 36.359 1.0 97.39 ? ? ? ? ? ? 152 PRO BA CD 1 35 B B +ATOM 8188 N N . VAL BA 1 36 ? -88.724 14.492 37.507 1.0 97.45 ? ? ? ? ? ? 153 VAL BA N 1 36 B B +ATOM 8189 C CA . VAL BA 1 36 ? -88.124 15.524 38.353 1.0 97.98 ? ? ? ? ? ? 153 VAL BA CA 1 36 B B +ATOM 8190 C C . VAL BA 1 36 ? -86.617 15.307 38.434 1.0 97.63 ? ? ? ? ? ? 153 VAL BA C 1 36 B B +ATOM 8191 O O . VAL BA 1 36 ? -85.838 16.087 37.883 1.0 100.0 ? ? ? ? ? ? 153 VAL BA O 1 36 B B +ATOM 8192 C CB . VAL BA 1 36 ? -88.719 15.505 39.791 1.0 97.27 ? ? ? ? ? ? 153 VAL BA CB 1 36 B B +ATOM 8193 C CG1 . VAL BA 1 36 ? -87.844 16.331 40.739 1.0 77.64 ? ? ? ? ? ? 153 VAL BA CG1 1 36 B B +ATOM 8194 C CG2 . VAL BA 1 36 ? -90.134 16.065 39.775 1.0 100.0 ? ? ? ? ? ? 153 VAL BA CG2 1 36 B B +ATOM 8195 N N . TYR BA 1 37 ? -86.221 14.241 39.127 1.0 91.74 ? ? ? ? ? ? 154 TYR BA N 1 37 B B +ATOM 8196 C CA . TYR BA 1 37 ? -84.815 13.889 39.290 1.0 80.82 ? ? ? ? ? ? 154 TYR BA CA 1 37 B B +ATOM 8197 C C . TYR BA 1 37 ? -84.090 14.041 37.957 1.0 62.59 ? ? ? ? ? ? 154 TYR BA C 1 37 B B +ATOM 8198 O O . TYR BA 1 37 ? -82.946 14.488 37.897 1.0 57.9 ? ? ? ? ? ? 154 TYR BA O 1 37 B B +ATOM 8199 C CB . TYR BA 1 37 ? -84.707 12.447 39.802 1.0 87.47 ? ? ? ? ? ? 154 TYR BA CB 1 37 B B +ATOM 8200 C CG . TYR BA 1 37 ? -83.322 11.844 39.737 1.0 100.0 ? ? ? ? ? ? 154 TYR BA CG 1 37 B B +ATOM 8201 C CD1 . TYR BA 1 37 ? -82.275 12.363 40.501 1.0 100.0 ? ? ? ? ? ? 154 TYR BA CD1 1 37 B B +ATOM 8202 C CD2 . TYR BA 1 37 ? -83.062 10.736 38.929 1.0 100.0 ? ? ? ? ? ? 154 TYR BA CD2 1 37 B B +ATOM 8203 C CE1 . TYR BA 1 37 ? -81.003 11.790 40.462 1.0 98.74 ? ? ? ? ? ? 154 TYR BA CE1 1 37 B B +ATOM 8204 C CE2 . TYR BA 1 37 ? -81.796 10.158 38.884 1.0 100.0 ? ? ? ? ? ? 154 TYR BA CE2 1 37 B B +ATOM 8205 C CZ . TYR BA 1 37 ? -80.775 10.687 39.652 1.0 98.2 ? ? ? ? ? ? 154 TYR BA CZ 1 37 B B +ATOM 8206 O OH . TYR BA 1 37 ? -79.532 10.104 39.617 1.0 94.15 ? ? ? ? ? ? 154 TYR BA OH 1 37 B B +ATOM 8207 N N . ARG BA 1 38 ? -84.781 13.664 36.890 1.0 51.43 ? ? ? ? ? ? 155 ARG BA N 1 38 B B +ATOM 8208 C CA . ARG BA 1 38 ? -84.241 13.760 35.547 1.0 48.13 ? ? ? ? ? ? 155 ARG BA CA 1 38 B B +ATOM 8209 C C . ARG BA 1 38 ? -83.862 15.207 35.253 1.0 51.81 ? ? ? ? ? ? 155 ARG BA C 1 38 B B +ATOM 8210 O O . ARG BA 1 38 ? -82.692 15.520 35.029 1.0 73.68 ? ? ? ? ? ? 155 ARG BA O 1 38 B B +ATOM 8211 C CB . ARG BA 1 38 ? -85.290 13.287 34.545 1.0 63.48 ? ? ? ? ? ? 155 ARG BA CB 1 38 B B +ATOM 8212 C CG . ARG BA 1 38 ? -84.746 12.880 33.198 1.0 82.88 ? ? ? ? ? ? 155 ARG BA CG 1 38 B B +ATOM 8213 C CD . ARG BA 1 38 ? -85.884 12.441 32.296 1.0 99.89 ? ? ? ? ? ? 155 ARG BA CD 1 38 B B +ATOM 8214 N NE . ARG BA 1 38 ? -85.436 12.120 30.945 1.0 100.0 ? ? ? ? ? ? 155 ARG BA NE 1 38 B B +ATOM 8215 C CZ . ARG BA 1 38 ? -85.494 10.904 30.414 1.0 100.0 ? ? ? ? ? ? 155 ARG BA CZ 1 38 B B +ATOM 8216 N NH1 . ARG BA 1 38 ? -85.980 9.891 31.121 1.0 90.91 ? ? ? ? ? ? 155 ARG BA NH1 1 38 B B +ATOM 8217 N NH2 . ARG BA 1 38 ? -85.076 10.703 29.171 1.0 100.0 ? ? ? ? ? ? 155 ARG BA NH2 1 38 B B +ATOM 8218 N N . ALA BA 1 39 ? -84.862 16.086 35.256 1.0 55.36 ? ? ? ? ? ? 156 ALA BA N 1 39 B B +ATOM 8219 C CA . ALA BA 1 39 ? -84.653 17.503 34.979 1.0 66.74 ? ? ? ? ? ? 156 ALA BA CA 1 39 B B +ATOM 8220 C C . ALA BA 1 39 ? -83.755 18.135 36.031 1.0 63.72 ? ? ? ? ? ? 156 ALA BA C 1 39 B B +ATOM 8221 O O . ALA BA 1 39 ? -83.175 19.200 35.815 1.0 67.32 ? ? ? ? ? ? 156 ALA BA O 1 39 B B +ATOM 8222 C CB . ALA BA 1 39 ? -85.988 18.224 34.930 1.0 81.61 ? ? ? ? ? ? 156 ALA BA CB 1 39 B B +ATOM 8223 N N . ARG BA 1 40 ? -83.656 17.480 37.179 1.0 57.55 ? ? ? ? ? ? 157 ARG BA N 1 40 B B +ATOM 8224 C CA . ARG BA 1 40 ? -82.811 17.977 38.255 1.0 59.91 ? ? ? ? ? ? 157 ARG BA CA 1 40 B B +ATOM 8225 C C . ARG BA 1 40 ? -81.357 17.738 37.859 1.0 62.43 ? ? ? ? ? ? 157 ARG BA C 1 40 B B +ATOM 8226 O O . ARG BA 1 40 ? -80.512 18.633 37.958 1.0 38.28 ? ? ? ? ? ? 157 ARG BA O 1 40 B B +ATOM 8227 C CB . ARG BA 1 40 ? -83.124 17.233 39.557 1.0 50.9 ? ? ? ? ? ? 157 ARG BA CB 1 40 B B +ATOM 8228 C CG . ARG BA 1 40 ? -82.158 17.518 40.690 1.0 55.69 ? ? ? ? ? ? 157 ARG BA CG 1 40 B B +ATOM 8229 C CD . ARG BA 1 40 ? -82.523 18.807 41.400 1.0 44.8 ? ? ? ? ? ? 157 ARG BA CD 1 40 B B +ATOM 8230 N NE . ARG BA 1 40 ? -81.919 18.892 42.725 1.0 43.79 ? ? ? ? ? ? 157 ARG BA NE 1 40 B B +ATOM 8231 C CZ . ARG BA 1 40 ? -81.729 20.031 43.384 1.0 54.54 ? ? ? ? ? ? 157 ARG BA CZ 1 40 B B +ATOM 8232 N NH1 . ARG BA 1 40 ? -82.098 21.190 42.843 1.0 34.07 ? ? ? ? ? ? 157 ARG BA NH1 1 40 B B +ATOM 8233 N NH2 . ARG BA 1 40 ? -81.167 20.009 44.587 1.0 46.44 ? ? ? ? ? ? 157 ARG BA NH2 1 40 B B +ATOM 8234 N N . ARG BA 1 41 ? -81.079 16.522 37.396 1.0 59.5 ? ? ? ? ? ? 158 ARG BA N 1 41 B B +ATOM 8235 C CA . ARG BA 1 41 ? -79.733 16.144 36.981 1.0 62.03 ? ? ? ? ? ? 158 ARG BA CA 1 41 B B +ATOM 8236 C C . ARG BA 1 41 ? -79.296 16.890 35.722 1.0 55.94 ? ? ? ? ? ? 158 ARG BA C 1 41 B B +ATOM 8237 O O . ARG BA 1 41 ? -78.108 16.925 35.394 1.0 66.56 ? ? ? ? ? ? 158 ARG BA O 1 41 B B +ATOM 8238 C CB . ARG BA 1 41 ? -79.659 14.635 36.743 1.0 71.07 ? ? ? ? ? ? 158 ARG BA CB 1 41 B B +ATOM 8239 C CG . ARG BA 1 41 ? -78.236 14.102 36.623 1.0 80.09 ? ? ? ? ? ? 158 ARG BA CG 1 41 B B +ATOM 8240 C CD . ARG BA 1 41 ? -78.177 12.600 36.861 1.0 64.88 ? ? ? ? ? ? 158 ARG BA CD 1 41 B B +ATOM 8241 N NE . ARG BA 1 41 ? -76.992 12.003 36.252 1.0 60.68 ? ? ? ? ? ? 158 ARG BA NE 1 41 B B +ATOM 8242 C CZ . ARG BA 1 41 ? -76.560 10.772 36.503 1.0 64.02 ? ? ? ? ? ? 158 ARG BA CZ 1 41 B B +ATOM 8243 N NH1 . ARG BA 1 41 ? -77.212 10.001 37.362 1.0 58.33 ? ? ? ? ? ? 158 ARG BA NH1 1 41 B B +ATOM 8244 N NH2 . ARG BA 1 41 ? -75.467 10.317 35.908 1.0 54.6 ? ? ? ? ? ? 158 ARG BA NH2 1 41 B B +ATOM 8245 N N . LYS BA 1 42 ? -80.261 17.468 35.013 1.0 41.95 ? ? ? ? ? ? 159 LYS BA N 1 42 B B +ATOM 8246 C CA . LYS BA 1 42 ? -79.978 18.233 33.802 1.0 50.07 ? ? ? ? ? ? 159 LYS BA CA 1 42 B B +ATOM 8247 C C . LYS BA 1 42 ? -79.686 19.655 34.255 1.0 37.82 ? ? ? ? ? ? 159 LYS BA C 1 42 B B +ATOM 8248 O O . LYS BA 1 42 ? -79.039 20.438 33.561 1.0 49.51 ? ? ? ? ? ? 159 LYS BA O 1 42 B B +ATOM 8249 C CB . LYS BA 1 42 ? -81.192 18.220 32.871 1.0 67.92 ? ? ? ? ? ? 159 LYS BA CB 1 42 B B +ATOM 8250 C CG . LYS BA 1 42 ? -81.062 19.144 31.673 1.0 85.85 ? ? ? ? ? ? 159 LYS BA CG 1 42 B B +ATOM 8251 C CD . LYS BA 1 42 ? -82.241 18.982 30.729 1.0 93.61 ? ? ? ? ? ? 159 LYS BA CD 1 42 B B +ATOM 8252 C CE . LYS BA 1 42 ? -82.031 19.754 29.437 1.0 92.11 ? ? ? ? ? ? 159 LYS BA CE 1 42 B B +ATOM 8253 N NZ . LYS BA 1 42 ? -83.099 19.458 28.441 1.0 97.37 ? ? ? ? ? ? 159 LYS BA NZ 1 42 B B +ATOM 8254 N N . GLN BA 1 43 ? -80.185 19.964 35.444 1.0 29.47 ? ? ? ? ? ? 160 GLN BA N 1 43 B B +ATOM 8255 C CA . GLN BA 1 43 ? -80.004 21.261 36.066 1.0 49.18 ? ? ? ? ? ? 160 GLN BA CA 1 43 B B +ATOM 8256 C C . GLN BA 1 43 ? -78.552 21.355 36.504 1.0 57.94 ? ? ? ? ? ? 160 GLN BA C 1 43 B B +ATOM 8257 O O . GLN BA 1 43 ? -77.880 22.371 36.305 1.0 57.37 ? ? ? ? ? ? 160 GLN BA O 1 43 B B +ATOM 8258 C CB . GLN BA 1 43 ? -80.915 21.347 37.279 1.0 39.15 ? ? ? ? ? ? 160 GLN BA CB 1 43 B B +ATOM 8259 C CG . GLN BA 1 43 ? -81.125 22.721 37.822 1.0 58.25 ? ? ? ? ? ? 160 GLN BA CG 1 43 B B +ATOM 8260 C CD . GLN BA 1 43 ? -82.257 22.748 38.817 1.0 68.54 ? ? ? ? ? ? 160 GLN BA CD 1 43 B B +ATOM 8261 O OE1 . GLN BA 1 43 ? -82.718 21.702 39.279 1.0 38.86 ? ? ? ? ? ? 160 GLN BA OE1 1 43 B B +ATOM 8262 N NE2 . GLN BA 1 43 ? -82.720 23.944 39.151 1.0 77.6 ? ? ? ? ? ? 160 GLN BA NE2 1 43 B B +ATOM 8263 N N . PHE BA 1 44 ? -78.079 20.274 37.111 1.0 66.93 ? ? ? ? ? ? 161 PHE BA N 1 44 B B +ATOM 8264 C CA . PHE BA 1 44 ? -76.708 20.194 37.584 1.0 64.47 ? ? ? ? ? ? 161 PHE BA CA 1 44 B B +ATOM 8265 C C . PHE BA 1 44 ? -75.756 20.274 36.392 1.0 64.32 ? ? ? ? ? ? 161 PHE BA C 1 44 B B +ATOM 8266 O O . PHE BA 1 44 ? -74.824 21.077 36.392 1.0 69.2 ? ? ? ? ? ? 161 PHE BA O 1 44 B B +ATOM 8267 C CB . PHE BA 1 44 ? -76.491 18.880 38.341 1.0 65.94 ? ? ? ? ? ? 161 PHE BA CB 1 44 B B +ATOM 8268 C CG . PHE BA 1 44 ? -77.101 18.858 39.718 1.0 57.74 ? ? ? ? ? ? 161 PHE BA CG 1 44 B B +ATOM 8269 C CD1 . PHE BA 1 44 ? -78.010 17.864 40.072 1.0 56.22 ? ? ? ? ? ? 161 PHE BA CD1 1 44 B B +ATOM 8270 C CD2 . PHE BA 1 44 ? -76.766 19.822 40.663 1.0 55.99 ? ? ? ? ? ? 161 PHE BA CD2 1 44 B B +ATOM 8271 C CE1 . PHE BA 1 44 ? -78.577 17.829 41.345 1.0 59.72 ? ? ? ? ? ? 161 PHE BA CE1 1 44 B B +ATOM 8272 C CE2 . PHE BA 1 44 ? -77.328 19.796 41.941 1.0 60.29 ? ? ? ? ? ? 161 PHE BA CE2 1 44 B B +ATOM 8273 C CZ . PHE BA 1 44 ? -78.234 18.797 42.280 1.0 65.58 ? ? ? ? ? ? 161 PHE BA CZ 1 44 B B +ATOM 8274 N N . ALA BA 1 45 ? -76.001 19.447 35.377 1.0 50.76 ? ? ? ? ? ? 162 ALA BA N 1 45 B B +ATOM 8275 C CA . ALA BA 1 45 ? -75.162 19.423 34.178 1.0 60.51 ? ? ? ? ? ? 162 ALA BA CA 1 45 B B +ATOM 8276 C C . ALA BA 1 45 ? -75.005 20.810 33.556 1.0 68.51 ? ? ? ? ? ? 162 ALA BA C 1 45 B B +ATOM 8277 O O . ALA BA 1 45 ? -73.899 21.208 33.177 1.0 77.7 ? ? ? ? ? ? 162 ALA BA O 1 45 B B +ATOM 8278 C CB . ALA BA 1 45 ? -75.744 18.460 33.151 1.0 42.85 ? ? ? ? ? ? 162 ALA BA CB 1 45 B B +ATOM 8279 N N . ASP BA 1 46 ? -76.112 21.538 33.449 1.0 62.79 ? ? ? ? ? ? 163 ASP BA N 1 46 B B +ATOM 8280 C CA . ASP BA 1 46 ? -76.100 22.879 32.872 1.0 74.08 ? ? ? ? ? ? 163 ASP BA CA 1 46 B B +ATOM 8281 C C . ASP BA 1 46 ? -75.143 23.766 33.656 1.0 72.43 ? ? ? ? ? ? 163 ASP BA C 1 46 B B +ATOM 8282 O O . ASP BA 1 46 ? -74.450 24.610 33.082 1.0 82.91 ? ? ? ? ? ? 163 ASP BA O 1 46 B B +ATOM 8283 C CB . ASP BA 1 46 ? -77.506 23.484 32.897 1.0 86.21 ? ? ? ? ? ? 163 ASP BA CB 1 46 B B +ATOM 8284 C CG . ASP BA 1 46 ? -78.309 23.161 31.647 1.0 100.0 ? ? ? ? ? ? 163 ASP BA CG 1 46 B B +ATOM 8285 O OD1 . ASP BA 1 46 ? -78.090 23.816 30.604 1.0 100.0 ? ? ? ? ? ? 163 ASP BA OD1 1 46 B B +ATOM 8286 O OD2 . ASP BA 1 46 ? -79.166 22.255 31.709 1.0 100.0 ? ? ? ? ? ? 163 ASP BA OD2 1 46 B B +ATOM 8287 N N . ILE BA 1 47 ? -75.115 23.583 34.972 1.0 63.62 ? ? ? ? ? ? 164 ILE BA N 1 47 B B +ATOM 8288 C CA . ILE BA 1 47 ? -74.221 24.367 35.812 1.0 57.19 ? ? ? ? ? ? 164 ILE BA CA 1 47 B B +ATOM 8289 C C . ILE BA 1 47 ? -72.808 24.162 35.280 1.0 63.56 ? ? ? ? ? ? 164 ILE BA C 1 47 B B +ATOM 8290 O O . ILE BA 1 47 ? -72.052 25.119 35.113 1.0 51.27 ? ? ? ? ? ? 164 ILE BA O 1 47 B B +ATOM 8291 C CB . ILE BA 1 47 ? -74.259 23.901 37.282 1.0 54.96 ? ? ? ? ? ? 164 ILE BA CB 1 47 B B +ATOM 8292 C CG1 . ILE BA 1 47 ? -75.620 24.212 37.907 1.0 57.18 ? ? ? ? ? ? 164 ILE BA CG1 1 47 B B +ATOM 8293 C CG2 . ILE BA 1 47 ? -73.169 24.595 38.073 1.0 45.83 ? ? ? ? ? ? 164 ILE BA CG2 1 47 B B +ATOM 8294 C CD1 . ILE BA 1 47 ? -75.834 23.579 39.270 1.0 71.75 ? ? ? ? ? ? 164 ILE BA CD1 1 47 B B +ATOM 8295 N N . ALA BA 1 48 ? -72.475 22.900 35.010 1.0 54.17 ? ? ? ? ? ? 165 ALA BA N 1 48 B B +ATOM 8296 C CA . ALA BA 1 48 ? -71.163 22.512 34.494 1.0 56.78 ? ? ? ? ? ? 165 ALA BA CA 1 48 B B +ATOM 8297 C C . ALA BA 1 48 ? -70.856 23.197 33.169 1.0 62.38 ? ? ? ? ? ? 165 ALA BA C 1 48 B B +ATOM 8298 O O . ALA BA 1 48 ? -69.821 23.842 33.013 1.0 74.61 ? ? ? ? ? ? 165 ALA BA O 1 48 B B +ATOM 8299 C CB . ALA BA 1 48 ? -71.096 20.995 34.322 1.0 46.33 ? ? ? ? ? ? 165 ALA BA CB 1 48 B B +ATOM 8300 N N . TYR BA 1 49 ? -71.767 23.051 32.216 1.0 57.01 ? ? ? ? ? ? 166 TYR BA N 1 49 B B +ATOM 8301 C CA . TYR BA 1 49 ? -71.599 23.649 30.900 1.0 54.6 ? ? ? ? ? ? 166 TYR BA CA 1 49 B B +ATOM 8302 C C . TYR BA 1 49 ? -71.383 25.158 30.961 1.0 54.08 ? ? ? ? ? ? 166 TYR BA C 1 49 B B +ATOM 8303 O O . TYR BA 1 49 ? -70.740 25.736 30.089 1.0 56.28 ? ? ? ? ? ? 166 TYR BA O 1 49 B B +ATOM 8304 C CB . TYR BA 1 49 ? -72.820 23.344 30.035 1.0 52.61 ? ? ? ? ? ? 166 TYR BA CB 1 49 B B +ATOM 8305 C CG . TYR BA 1 49 ? -73.022 21.874 29.770 1.0 67.21 ? ? ? ? ? ? 166 TYR BA CG 1 49 B B +ATOM 8306 C CD1 . TYR BA 1 49 ? -74.254 21.265 30.004 1.0 76.45 ? ? ? ? ? ? 166 TYR BA CD1 1 49 B B +ATOM 8307 C CD2 . TYR BA 1 49 ? -71.987 21.090 29.270 1.0 79.48 ? ? ? ? ? ? 166 TYR BA CD2 1 49 B B +ATOM 8308 C CE1 . TYR BA 1 49 ? -74.453 19.912 29.742 1.0 72.28 ? ? ? ? ? ? 166 TYR BA CE1 1 49 B B +ATOM 8309 C CE2 . TYR BA 1 49 ? -72.174 19.736 29.005 1.0 79.73 ? ? ? ? ? ? 166 TYR BA CE2 1 49 B B +ATOM 8310 C CZ . TYR BA 1 49 ? -73.408 19.154 29.243 1.0 73.81 ? ? ? ? ? ? 166 TYR BA CZ 1 49 B B +ATOM 8311 O OH . TYR BA 1 49 ? -73.602 17.820 28.967 1.0 73.0 ? ? ? ? ? ? 166 TYR BA OH 1 49 B B +ATOM 8312 N N . ASN BA 1 50 ? -71.921 25.792 31.995 1.0 50.52 ? ? ? ? ? ? 167 ASN BA N 1 50 B B +ATOM 8313 C CA . ASN BA 1 50 ? -71.792 27.236 32.142 1.0 72.73 ? ? ? ? ? ? 167 ASN BA CA 1 50 B B +ATOM 8314 C C . ASN BA 1 50 ? -70.599 27.641 32.985 1.0 75.36 ? ? ? ? ? ? 167 ASN BA C 1 50 B B +ATOM 8315 O O . ASN BA 1 50 ? -70.226 28.813 33.026 1.0 80.4 ? ? ? ? ? ? 167 ASN BA O 1 50 B B +ATOM 8316 C CB . ASN BA 1 50 ? -73.056 27.817 32.773 1.0 88.5 ? ? ? ? ? ? 167 ASN BA CB 1 50 B B +ATOM 8317 C CG . ASN BA 1 50 ? -74.283 27.600 31.918 1.0 100.0 ? ? ? ? ? ? 167 ASN BA CG 1 50 B B +ATOM 8318 O OD1 . ASN BA 1 50 ? -74.318 27.994 30.751 1.0 100.0 ? ? ? ? ? ? 167 ASN BA OD1 1 50 B B +ATOM 8319 N ND2 . ASN BA 1 50 ? -75.301 26.971 32.494 1.0 100.0 ? ? ? ? ? ? 167 ASN BA ND2 1 50 B B +ATOM 8320 N N . TYR BA 1 51 ? -69.997 26.672 33.662 1.0 66.74 ? ? ? ? ? ? 168 TYR BA N 1 51 B B +ATOM 8321 C CA . TYR BA 1 51 ? -68.856 26.966 34.515 1.0 64.8 ? ? ? ? ? ? 168 TYR BA CA 1 51 B B +ATOM 8322 C C . TYR BA 1 51 ? -67.546 27.187 33.773 1.0 54.51 ? ? ? ? ? ? 168 TYR BA C 1 51 B B +ATOM 8323 O O . TYR BA 1 51 ? -67.100 26.340 32.998 1.0 61.97 ? ? ? ? ? ? 168 TYR BA O 1 51 B B +ATOM 8324 C CB . TYR BA 1 51 ? -68.653 25.854 35.545 1.0 79.84 ? ? ? ? ? ? 168 TYR BA CB 1 51 B B +ATOM 8325 C CG . TYR BA 1 51 ? -67.533 26.162 36.507 1.0 86.88 ? ? ? ? ? ? 168 TYR BA CG 1 51 B B +ATOM 8326 C CD1 . TYR BA 1 51 ? -67.712 27.084 37.538 1.0 90.58 ? ? ? ? ? ? 168 TYR BA CD1 1 51 B B +ATOM 8327 C CD2 . TYR BA 1 51 ? -66.277 25.579 36.354 1.0 83.02 ? ? ? ? ? ? 168 TYR BA CD2 1 51 B B +ATOM 8328 C CE1 . TYR BA 1 51 ? -66.671 27.425 38.385 1.0 75.51 ? ? ? ? ? ? 168 TYR BA CE1 1 51 B B +ATOM 8329 C CE2 . TYR BA 1 51 ? -65.225 25.913 37.197 1.0 82.8 ? ? ? ? ? ? 168 TYR BA CE2 1 51 B B +ATOM 8330 C CZ . TYR BA 1 51 ? -65.430 26.838 38.209 1.0 84.21 ? ? ? ? ? ? 168 TYR BA CZ 1 51 B B +ATOM 8331 O OH . TYR BA 1 51 ? -64.392 27.186 39.041 1.0 100.0 ? ? ? ? ? ? 168 TYR BA OH 1 51 B B +ATOM 8332 N N . ARG BA 1 52 ? -66.934 28.337 34.029 1.0 41.53 ? ? ? ? ? ? 169 ARG BA N 1 52 B B +ATOM 8333 C CA . ARG BA 1 52 ? -65.660 28.677 33.423 1.0 61.97 ? ? ? ? ? ? 169 ARG BA CA 1 52 B B +ATOM 8334 C C . ARG BA 1 52 ? -64.660 28.864 34.556 1.0 62.04 ? ? ? ? ? ? 169 ARG BA C 1 52 B B +ATOM 8335 O O . ARG BA 1 52 ? -64.995 29.410 35.607 1.0 60.29 ? ? ? ? ? ? 169 ARG BA O 1 52 B B +ATOM 8336 C CB . ARG BA 1 52 ? -65.787 29.962 32.604 1.0 69.44 ? ? ? ? ? ? 169 ARG BA CB 1 52 B B +ATOM 8337 C CG . ARG BA 1 52 ? -65.995 29.725 31.116 1.0 73.47 ? ? ? ? ? ? 169 ARG BA CG 1 52 B B +ATOM 8338 C CD . ARG BA 1 52 ? -67.385 29.186 30.829 1.0 61.39 ? ? ? ? ? ? 169 ARG BA CD 1 52 B B +ATOM 8339 N NE . ARG BA 1 52 ? -67.605 28.988 29.400 1.0 77.33 ? ? ? ? ? ? 169 ARG BA NE 1 52 B B +ATOM 8340 C CZ . ARG BA 1 52 ? -67.792 27.801 28.831 1.0 89.0 ? ? ? ? ? ? 169 ARG BA CZ 1 52 B B +ATOM 8341 N NH1 . ARG BA 1 52 ? -67.785 26.699 29.569 1.0 92.77 ? ? ? ? ? ? 169 ARG BA NH1 1 52 B B +ATOM 8342 N NH2 . ARG BA 1 52 ? -67.980 27.714 27.522 1.0 99.94 ? ? ? ? ? ? 169 ARG BA NH2 1 52 B B +ATOM 8343 N N . HIS BA 1 53 ? -63.435 28.397 34.341 1.0 68.52 ? ? ? ? ? ? 170 HIS BA N 1 53 B B +ATOM 8344 C CA . HIS BA 1 53 ? -62.389 28.500 35.349 1.0 74.68 ? ? ? ? ? ? 170 HIS BA CA 1 53 B B +ATOM 8345 C C . HIS BA 1 53 ? -62.240 29.921 35.885 1.0 73.45 ? ? ? ? ? ? 170 HIS BA C 1 53 B B +ATOM 8346 O O . HIS BA 1 53 ? -62.501 30.898 35.183 1.0 60.55 ? ? ? ? ? ? 170 HIS BA O 1 53 B B +ATOM 8347 C CB . HIS BA 1 53 ? -61.054 28.015 34.766 1.0 74.49 ? ? ? ? ? ? 170 HIS BA CB 1 53 B B +ATOM 8348 C CG . HIS BA 1 53 ? -59.879 28.246 35.665 1.0 80.04 ? ? ? ? ? ? 170 HIS BA CG 1 53 B B +ATOM 8349 N ND1 . HIS BA 1 53 ? -59.482 27.333 36.622 1.0 79.81 ? ? ? ? ? ? 170 HIS BA ND1 1 53 B B +ATOM 8350 C CD2 . HIS BA 1 53 ? -59.009 29.279 35.750 1.0 81.19 ? ? ? ? ? ? 170 HIS BA CD2 1 53 B B +ATOM 8351 C CE1 . HIS BA 1 53 ? -58.420 27.799 37.255 1.0 90.42 ? ? ? ? ? ? 170 HIS BA CE1 1 53 B B +ATOM 8352 N NE2 . HIS BA 1 53 ? -58.113 28.978 36.746 1.0 85.48 ? ? ? ? ? ? 170 HIS BA NE2 1 53 B B +ATOM 8353 N N . GLY BA 1 54 ? -61.824 30.021 37.144 1.0 76.84 ? ? ? ? ? ? 171 GLY BA N 1 54 B B +ATOM 8354 C CA . GLY BA 1 54 ? -61.633 31.321 37.760 1.0 81.18 ? ? ? ? ? ? 171 GLY BA CA 1 54 B B +ATOM 8355 C C . GLY BA 1 54 ? -62.774 31.781 38.644 1.0 81.66 ? ? ? ? ? ? 171 GLY BA C 1 54 B B +ATOM 8356 O O . GLY BA 1 54 ? -62.546 32.402 39.685 1.0 58.86 ? ? ? ? ? ? 171 GLY BA O 1 54 B B +ATOM 8357 N N . GLN BA 1 55 ? -64.004 31.484 38.231 1.0 85.56 ? ? ? ? ? ? 172 GLN BA N 1 55 B B +ATOM 8358 C CA . GLN BA 1 55 ? -65.182 31.878 38.993 1.0 76.95 ? ? ? ? ? ? 172 GLN BA CA 1 55 B B +ATOM 8359 C C . GLN BA 1 55 ? -65.542 30.808 40.009 1.0 70.7 ? ? ? ? ? ? 172 GLN BA C 1 55 B B +ATOM 8360 O O . GLN BA 1 55 ? -65.327 29.621 39.778 1.0 64.21 ? ? ? ? ? ? 172 GLN BA O 1 55 B B +ATOM 8361 C CB . GLN BA 1 55 ? -66.363 32.110 38.056 1.0 73.18 ? ? ? ? ? ? 172 GLN BA CB 1 55 B B +ATOM 8362 C CG . GLN BA 1 55 ? -66.810 30.865 37.328 1.0 89.81 ? ? ? ? ? ? 172 GLN BA CG 1 55 B B +ATOM 8363 C CD . GLN BA 1 55 ? -67.418 31.181 35.981 1.0 98.74 ? ? ? ? ? ? 172 GLN BA CD 1 55 B B +ATOM 8364 O OE1 . GLN BA 1 55 ? -68.420 30.588 35.586 1.0 100.0 ? ? ? ? ? ? 172 GLN BA OE1 1 55 B B +ATOM 8365 N NE2 . GLN BA 1 55 ? -66.810 32.118 35.264 1.0 100.0 ? ? ? ? ? ? 172 GLN BA NE2 1 55 B B +ATOM 8366 N N . PRO BA 1 56 ? -66.106 31.219 41.153 1.0 73.82 ? ? ? ? ? ? 173 PRO BA N 1 56 B B +ATOM 8367 C CA . PRO BA 1 56 ? -66.486 30.258 42.194 1.0 66.22 ? ? ? ? ? ? 173 PRO BA CA 1 56 B B +ATOM 8368 C C . PRO BA 1 56 ? -67.568 29.284 41.737 1.0 59.56 ? ? ? ? ? ? 173 PRO BA C 1 56 B B +ATOM 8369 O O . PRO BA 1 56 ? -68.475 29.648 40.988 1.0 40.19 ? ? ? ? ? ? 173 PRO BA O 1 56 B B +ATOM 8370 C CB . PRO BA 1 56 ? -66.939 31.143 43.360 1.0 54.59 ? ? ? ? ? ? 173 PRO BA CB 1 56 B B +ATOM 8371 C CG . PRO BA 1 56 ? -67.288 32.452 42.739 1.0 72.86 ? ? ? ? ? ? 173 PRO BA CG 1 56 B B +ATOM 8372 C CD . PRO BA 1 56 ? -66.421 32.608 41.530 1.0 76.58 ? ? ? ? ? ? 173 PRO BA CD 1 56 B B +ATOM 8373 N N . ILE BA 1 57 ? -67.452 28.037 42.184 1.0 62.65 ? ? ? ? ? ? 174 ILE BA N 1 57 B B +ATOM 8374 C CA . ILE BA 1 57 ? -68.421 27.010 41.831 1.0 60.69 ? ? ? ? ? ? 174 ILE BA CA 1 57 B B +ATOM 8375 C C . ILE BA 1 57 ? -69.772 27.384 42.430 1.0 67.23 ? ? ? ? ? ? 174 ILE BA C 1 57 B B +ATOM 8376 O O . ILE BA 1 57 ? -69.897 27.565 43.640 1.0 73.73 ? ? ? ? ? ? 174 ILE BA O 1 57 B B +ATOM 8377 C CB . ILE BA 1 57 ? -67.995 25.627 42.374 1.0 55.07 ? ? ? ? ? ? 174 ILE BA CB 1 57 B B +ATOM 8378 C CG1 . ILE BA 1 57 ? -66.513 25.383 42.092 1.0 58.47 ? ? ? ? ? ? 174 ILE BA CG1 1 57 B B +ATOM 8379 C CG2 . ILE BA 1 57 ? -68.852 24.535 41.748 1.0 60.31 ? ? ? ? ? ? 174 ILE BA CG2 1 57 B B +ATOM 8380 C CD1 . ILE BA 1 57 ? -65.949 24.165 42.789 1.0 68.31 ? ? ? ? ? ? 174 ILE BA CD1 1 57 B B +ATOM 8381 N N . PRO BA 1 58 ? -70.801 27.516 41.583 1.0 64.96 ? ? ? ? ? ? 175 PRO BA N 1 58 B B +ATOM 8382 C CA . PRO BA 1 58 ? -72.136 27.876 42.080 1.0 70.0 ? ? ? ? ? ? 175 PRO BA CA 1 58 B B +ATOM 8383 C C . PRO BA 1 58 ? -72.656 26.929 43.160 1.0 74.14 ? ? ? ? ? ? 175 PRO BA C 1 58 B B +ATOM 8384 O O . PRO BA 1 58 ? -72.461 25.718 43.079 1.0 73.56 ? ? ? ? ? ? 175 PRO BA O 1 58 B B +ATOM 8385 C CB . PRO BA 1 58 ? -73.013 27.858 40.823 1.0 61.64 ? ? ? ? ? ? 175 PRO BA CB 1 58 B B +ATOM 8386 C CG . PRO BA 1 58 ? -72.212 27.116 39.796 1.0 67.53 ? ? ? ? ? ? 175 PRO BA CG 1 58 B B +ATOM 8387 C CD . PRO BA 1 58 ? -70.781 27.338 40.123 1.0 61.93 ? ? ? ? ? ? 175 PRO BA CD 1 58 B B +ATOM 8388 N N . ARG BA 1 59 ? -73.317 27.488 44.171 1.0 66.46 ? ? ? ? ? ? 176 ARG BA N 1 59 B B +ATOM 8389 C CA . ARG BA 1 59 ? -73.863 26.680 45.254 1.0 61.16 ? ? ? ? ? ? 176 ARG BA CA 1 59 B B +ATOM 8390 C C . ARG BA 1 59 ? -75.266 26.211 44.887 1.0 59.92 ? ? ? ? ? ? 176 ARG BA C 1 59 B B +ATOM 8391 O O . ARG BA 1 59 ? -75.941 26.829 44.070 1.0 57.89 ? ? ? ? ? ? 176 ARG BA O 1 59 B B +ATOM 8392 C CB . ARG BA 1 59 ? -73.903 27.485 46.556 1.0 50.1 ? ? ? ? ? ? 176 ARG BA CB 1 59 B B +ATOM 8393 C CG . ARG BA 1 59 ? -72.546 28.001 46.999 1.0 58.89 ? ? ? ? ? ? 176 ARG BA CG 1 59 B B +ATOM 8394 C CD . ARG BA 1 59 ? -72.659 28.890 48.223 1.0 72.01 ? ? ? ? ? ? 176 ARG BA CD 1 59 B B +ATOM 8395 N NE . ARG BA 1 59 ? -71.511 28.724 49.105 1.0 70.85 ? ? ? ? ? ? 176 ARG BA NE 1 59 B B +ATOM 8396 C CZ . ARG BA 1 59 ? -71.491 27.912 50.155 1.0 83.18 ? ? ? ? ? ? 176 ARG BA CZ 1 59 B B +ATOM 8397 N NH1 . ARG BA 1 59 ? -72.560 27.187 50.458 1.0 84.71 ? ? ? ? ? ? 176 ARG BA NH1 1 59 B B +ATOM 8398 N NH2 . ARG BA 1 59 ? -70.400 27.822 50.901 1.0 91.27 ? ? ? ? ? ? 176 ARG BA NH2 1 59 B B +ATOM 8399 N N . VAL BA 1 60 ? -75.699 25.112 45.495 1.0 64.04 ? ? ? ? ? ? 177 VAL BA N 1 60 B B +ATOM 8400 C CA . VAL BA 1 60 ? -77.017 24.559 45.212 1.0 60.14 ? ? ? ? ? ? 177 VAL BA CA 1 60 B B +ATOM 8401 C C . VAL BA 1 60 ? -77.766 24.192 46.488 1.0 65.82 ? ? ? ? ? ? 177 VAL BA C 1 60 B B +ATOM 8402 O O . VAL BA 1 60 ? -77.168 23.768 47.476 1.0 63.14 ? ? ? ? ? ? 177 VAL BA O 1 60 B B +ATOM 8403 C CB . VAL BA 1 60 ? -76.904 23.300 44.322 1.0 56.5 ? ? ? ? ? ? 177 VAL BA CB 1 60 B B +ATOM 8404 C CG1 . VAL BA 1 60 ? -78.258 22.638 44.176 1.0 57.11 ? ? ? ? ? ? 177 VAL BA CG1 1 60 B B +ATOM 8405 C CG2 . VAL BA 1 60 ? -76.355 23.674 42.961 1.0 61.23 ? ? ? ? ? ? 177 VAL BA CG2 1 60 B B +ATOM 8406 N N . GLU BA 1 61 ? -79.083 24.361 46.452 1.0 67.94 ? ? ? ? ? ? 178 GLU BA N 1 61 B B +ATOM 8407 C CA . GLU BA 1 61 ? -79.941 24.046 47.585 1.0 66.12 ? ? ? ? ? ? 178 GLU BA CA 1 61 B B +ATOM 8408 C C . GLU BA 1 61 ? -80.478 22.622 47.419 1.0 66.76 ? ? ? ? ? ? 178 GLU BA C 1 61 B B +ATOM 8409 O O . GLU BA 1 61 ? -81.544 22.416 46.844 1.0 74.54 ? ? ? ? ? ? 178 GLU BA O 1 61 B B +ATOM 8410 C CB . GLU BA 1 61 ? -81.105 25.040 47.645 1.0 63.93 ? ? ? ? ? ? 178 GLU BA CB 1 61 B B +ATOM 8411 C CG . GLU BA 1 61 ? -81.581 25.376 49.047 1.0 81.95 ? ? ? ? ? ? 178 GLU BA CG 1 61 B B +ATOM 8412 C CD . GLU BA 1 61 ? -82.512 26.579 49.075 1.0 99.54 ? ? ? ? ? ? 178 GLU BA CD 1 61 B B +ATOM 8413 O OE1 . GLU BA 1 61 ? -83.688 26.434 48.671 1.0 100.0 ? ? ? ? ? ? 178 GLU BA OE1 1 61 B B +ATOM 8414 O OE2 . GLU BA 1 61 ? -82.067 27.668 49.499 1.0 90.8 ? ? ? ? ? ? 178 GLU BA OE2 1 61 B B +ATOM 8415 N N . TYR BA 1 62 ? -79.733 21.642 47.921 1.0 62.63 ? ? ? ? ? ? 179 TYR BA N 1 62 B B +ATOM 8416 C CA . TYR BA 1 62 ? -80.131 20.240 47.814 1.0 60.17 ? ? ? ? ? ? 179 TYR BA CA 1 62 B B +ATOM 8417 C C . TYR BA 1 62 ? -81.449 19.955 48.520 1.0 53.94 ? ? ? ? ? ? 179 TYR BA C 1 62 B B +ATOM 8418 O O . TYR BA 1 62 ? -81.774 20.595 49.517 1.0 65.06 ? ? ? ? ? ? 179 TYR BA O 1 62 B B +ATOM 8419 C CB . TYR BA 1 62 ? -79.026 19.346 48.377 1.0 57.21 ? ? ? ? ? ? 179 TYR BA CB 1 62 B B +ATOM 8420 C CG . TYR BA 1 62 ? -77.767 19.381 47.546 1.0 53.03 ? ? ? ? ? ? 179 TYR BA CG 1 62 B B +ATOM 8421 C CD1 . TYR BA 1 62 ? -77.452 18.334 46.679 1.0 62.41 ? ? ? ? ? ? 179 TYR BA CD1 1 62 B B +ATOM 8422 C CD2 . TYR BA 1 62 ? -76.903 20.472 47.605 1.0 55.44 ? ? ? ? ? ? 179 TYR BA CD2 1 62 B B +ATOM 8423 C CE1 . TYR BA 1 62 ? -76.308 18.373 45.891 1.0 61.06 ? ? ? ? ? ? 179 TYR BA CE1 1 62 B B +ATOM 8424 C CE2 . TYR BA 1 62 ? -75.755 20.521 46.821 1.0 67.16 ? ? ? ? ? ? 179 TYR BA CE2 1 62 B B +ATOM 8425 C CZ . TYR BA 1 62 ? -75.464 19.467 45.966 1.0 71.98 ? ? ? ? ? ? 179 TYR BA CZ 1 62 B B +ATOM 8426 O OH . TYR BA 1 62 ? -74.324 19.498 45.193 1.0 75.67 ? ? ? ? ? ? 179 TYR BA OH 1 62 B B +ATOM 8427 N N . MET BA 1 63 ? -82.203 18.992 47.996 1.0 44.48 ? ? ? ? ? ? 180 MET BA N 1 63 B B +ATOM 8428 C CA . MET BA 1 63 ? -83.499 18.629 48.566 1.0 51.59 ? ? ? ? ? ? 180 MET BA CA 1 63 B B +ATOM 8429 C C . MET BA 1 63 ? -83.397 17.486 49.567 1.0 50.91 ? ? ? ? ? ? 180 MET BA C 1 63 B B +ATOM 8430 O O . MET BA 1 63 ? -82.449 16.703 49.535 1.0 43.45 ? ? ? ? ? ? 180 MET BA O 1 63 B B +ATOM 8431 C CB . MET BA 1 63 ? -84.476 18.247 47.449 1.0 69.37 ? ? ? ? ? ? 180 MET BA CB 1 63 B B +ATOM 8432 C CG . MET BA 1 63 ? -84.580 19.286 46.336 1.0 76.18 ? ? ? ? ? ? 180 MET BA CG 1 63 B B +ATOM 8433 S SD . MET BA 1 63 ? -85.655 18.812 44.962 1.0 78.79 ? ? ? ? ? ? 180 MET BA SD 1 63 B B +ATOM 8434 C CE . MET BA 1 63 ? -85.254 17.047 44.766 1.0 79.39 ? ? ? ? ? ? 180 MET BA CE 1 63 B B +ATOM 8435 N N . GLU BA 1 64 ? -84.391 17.399 50.447 1.0 55.45 ? ? ? ? ? ? 181 GLU BA N 1 64 B B +ATOM 8436 C CA . GLU BA 1 64 ? -84.426 16.370 51.482 1.0 65.48 ? ? ? ? ? ? 181 GLU BA CA 1 64 B B +ATOM 8437 C C . GLU BA 1 64 ? -84.391 14.956 50.931 1.0 59.13 ? ? ? ? ? ? 181 GLU BA C 1 64 B B +ATOM 8438 O O . GLU BA 1 64 ? -83.731 14.084 51.489 1.0 57.9 ? ? ? ? ? ? 181 GLU BA O 1 64 B B +ATOM 8439 C CB . GLU BA 1 64 ? -85.671 16.538 52.355 1.0 73.55 ? ? ? ? ? ? 181 GLU BA CB 1 64 B B +ATOM 8440 C CG . GLU BA 1 64 ? -85.417 17.282 53.650 1.0 74.18 ? ? ? ? ? ? 181 GLU BA CG 1 64 B B +ATOM 8441 C CD . GLU BA 1 64 ? -85.137 18.751 53.415 1.0 84.6 ? ? ? ? ? ? 181 GLU BA CD 1 64 B B +ATOM 8442 O OE1 . GLU BA 1 64 ? -85.509 19.256 52.334 1.0 80.82 ? ? ? ? ? ? 181 GLU BA OE1 1 64 B B +ATOM 8443 O OE2 . GLU BA 1 64 ? -84.543 19.397 54.306 1.0 77.62 ? ? ? ? ? ? 181 GLU BA OE2 1 64 B B +ATOM 8444 N N . GLU BA 1 65 ? -85.121 14.723 49.847 1.0 60.69 ? ? ? ? ? ? 182 GLU BA N 1 65 B B +ATOM 8445 C CA . GLU BA 1 65 ? -85.142 13.397 49.246 1.0 72.25 ? ? ? ? ? ? 182 GLU BA CA 1 65 B B +ATOM 8446 C C . GLU BA 1 65 ? -83.703 13.051 48.878 1.0 76.67 ? ? ? ? ? ? 182 GLU BA C 1 65 B B +ATOM 8447 O O . GLU BA 1 65 ? -83.333 11.880 48.784 1.0 82.42 ? ? ? ? ? ? 182 GLU BA O 1 65 B B +ATOM 8448 C CB . GLU BA 1 65 ? -86.030 13.388 47.999 1.0 75.93 ? ? ? ? ? ? 182 GLU BA CB 1 65 B B +ATOM 8449 C CG . GLU BA 1 65 ? -87.509 13.638 48.282 1.0 89.1 ? ? ? ? ? ? 182 GLU BA CG 1 65 B B +ATOM 8450 C CD . GLU BA 1 65 ? -87.803 15.085 48.649 1.0 100.0 ? ? ? ? ? ? 182 GLU BA CD 1 65 B B +ATOM 8451 O OE1 . GLU BA 1 65 ? -88.769 15.326 49.405 1.0 100.0 ? ? ? ? ? ? 182 GLU BA OE1 1 65 B B +ATOM 8452 O OE2 . GLU BA 1 65 ? -87.067 15.980 48.183 1.0 100.0 ? ? ? ? ? ? 182 GLU BA OE2 1 65 B B +ATOM 8453 N N . GLU BA 1 66 ? -82.900 14.092 48.681 1.0 69.07 ? ? ? ? ? ? 183 GLU BA N 1 66 B B +ATOM 8454 C CA . GLU BA 1 66 ? -81.492 13.937 48.338 1.0 65.03 ? ? ? ? ? ? 183 GLU BA CA 1 66 B B +ATOM 8455 C C . GLU BA 1 66 ? -80.665 13.868 49.620 1.0 71.81 ? ? ? ? ? ? 183 GLU BA C 1 66 B B +ATOM 8456 O O . GLU BA 1 66 ? -79.853 12.960 49.800 1.0 72.45 ? ? ? ? ? ? 183 GLU BA O 1 66 B B +ATOM 8457 C CB . GLU BA 1 66 ? -81.027 15.117 47.475 1.0 56.35 ? ? ? ? ? ? 183 GLU BA CB 1 66 B B +ATOM 8458 C CG . GLU BA 1 66 ? -81.855 15.297 46.211 1.0 66.75 ? ? ? ? ? ? 183 GLU BA CG 1 66 B B +ATOM 8459 C CD . GLU BA 1 66 ? -81.439 16.502 45.388 1.0 66.56 ? ? ? ? ? ? 183 GLU BA CD 1 66 B B +ATOM 8460 O OE1 . GLU BA 1 66 ? -81.285 17.599 45.964 1.0 37.84 ? ? ? ? ? ? 183 GLU BA OE1 1 66 B B +ATOM 8461 O OE2 . GLU BA 1 66 ? -81.272 16.351 44.159 1.0 72.41 ? ? ? ? ? ? 183 GLU BA OE2 1 66 B B +ATOM 8462 N N . LYS BA 1 67 ? -80.886 14.833 50.509 1.0 71.29 ? ? ? ? ? ? 184 LYS BA N 1 67 B B +ATOM 8463 C CA . LYS BA 1 67 ? -80.172 14.891 51.779 1.0 59.63 ? ? ? ? ? ? 184 LYS BA CA 1 67 B B +ATOM 8464 C C . LYS BA 1 67 ? -80.343 13.594 52.567 1.0 64.36 ? ? ? ? ? ? 184 LYS BA C 1 67 B B +ATOM 8465 O O . LYS BA 1 67 ? -79.507 13.250 53.398 1.0 65.37 ? ? ? ? ? ? 184 LYS BA O 1 67 B B +ATOM 8466 C CB . LYS BA 1 67 ? -80.674 16.071 52.612 1.0 52.43 ? ? ? ? ? ? 184 LYS BA CB 1 67 B B +ATOM 8467 C CG . LYS BA 1 67 ? -80.180 17.427 52.131 1.0 52.57 ? ? ? ? ? ? 184 LYS BA CG 1 67 B B +ATOM 8468 C CD . LYS BA 1 67 ? -80.630 18.542 53.066 1.0 54.98 ? ? ? ? ? ? 184 LYS BA CD 1 67 B B +ATOM 8469 C CE . LYS BA 1 67 ? -80.115 19.896 52.602 1.0 56.14 ? ? ? ? ? ? 184 LYS BA CE 1 67 B B +ATOM 8470 N NZ . LYS BA 1 67 ? -80.578 21.007 53.479 1.0 60.61 ? ? ? ? ? ? 184 LYS BA NZ 1 67 B B +ATOM 8471 N N . LYS BA 1 68 ? -81.433 12.879 52.308 1.0 70.38 ? ? ? ? ? ? 185 LYS BA N 1 68 B B +ATOM 8472 C CA . LYS BA 1 68 ? -81.681 11.618 52.993 1.0 70.07 ? ? ? ? ? ? 185 LYS BA CA 1 68 B B +ATOM 8473 C C . LYS BA 1 68 ? -80.725 10.579 52.436 1.0 64.92 ? ? ? ? ? ? 185 LYS BA C 1 68 B B +ATOM 8474 O O . LYS BA 1 68 ? -80.095 9.831 53.184 1.0 65.78 ? ? ? ? ? ? 185 LYS BA O 1 68 B B +ATOM 8475 C CB . LYS BA 1 68 ? -83.121 11.156 52.769 1.0 79.66 ? ? ? ? ? ? 185 LYS BA CB 1 68 B B +ATOM 8476 C CG . LYS BA 1 68 ? -83.434 9.818 53.415 1.0 97.13 ? ? ? ? ? ? 185 LYS BA CG 1 68 B B +ATOM 8477 C CD . LYS BA 1 68 ? -84.771 9.267 52.948 1.0 95.14 ? ? ? ? ? ? 185 LYS BA CD 1 68 B B +ATOM 8478 C CE . LYS BA 1 68 ? -85.218 8.098 53.815 1.0 92.79 ? ? ? ? ? ? 185 LYS BA CE 1 68 B B +ATOM 8479 N NZ . LYS BA 1 68 ? -84.413 6.868 53.564 1.0 100.0 ? ? ? ? ? ? 185 LYS BA NZ 1 68 B B +ATOM 8480 N N . THR BA 1 69 ? -80.624 10.541 51.113 1.0 70.7 ? ? ? ? ? ? 186 THR BA N 1 69 B B +ATOM 8481 C CA . THR BA 1 69 ? -79.743 9.601 50.439 1.0 81.19 ? ? ? ? ? ? 186 THR BA CA 1 69 B B +ATOM 8482 C C . THR BA 1 69 ? -78.295 9.878 50.826 1.0 82.75 ? ? ? ? ? ? 186 THR BA C 1 69 B B +ATOM 8483 O O . THR BA 1 69 ? -77.478 8.964 50.924 1.0 80.57 ? ? ? ? ? ? 186 THR BA O 1 69 B B +ATOM 8484 C CB . THR BA 1 69 ? -79.883 9.712 48.910 1.0 79.41 ? ? ? ? ? ? 186 THR BA CB 1 69 B B +ATOM 8485 O OG1 . THR BA 1 69 ? -81.270 9.795 48.563 1.0 69.39 ? ? ? ? ? ? 186 THR BA OG1 1 69 B B +ATOM 8486 C CG2 . THR BA 1 69 ? -79.270 8.502 48.231 1.0 88.62 ? ? ? ? ? ? 186 THR BA CG2 1 69 B B +ATOM 8487 N N . TRP BA 1 70 ? -77.977 11.149 51.039 1.0 82.99 ? ? ? ? ? ? 187 TRP BA N 1 70 B B +ATOM 8488 C CA . TRP BA 1 70 ? -76.627 11.529 51.423 1.0 84.8 ? ? ? ? ? ? 187 TRP BA CA 1 70 B B +ATOM 8489 C C . TRP BA 1 70 ? -76.319 10.940 52.795 1.0 81.96 ? ? ? ? ? ? 187 TRP BA C 1 70 B B +ATOM 8490 O O . TRP BA 1 70 ? -75.300 10.274 52.981 1.0 67.97 ? ? ? ? ? ? 187 TRP BA O 1 70 B B +ATOM 8491 C CB . TRP BA 1 70 ? -76.502 13.057 51.461 1.0 92.87 ? ? ? ? ? ? 187 TRP BA CB 1 70 B B +ATOM 8492 C CG . TRP BA 1 70 ? -75.298 13.558 52.201 1.0 91.79 ? ? ? ? ? ? 187 TRP BA CG 1 70 B B +ATOM 8493 C CD1 . TRP BA 1 70 ? -75.278 14.105 53.452 1.0 84.37 ? ? ? ? ? ? 187 TRP BA CD1 1 70 B B +ATOM 8494 C CD2 . TRP BA 1 70 ? -73.942 13.589 51.729 1.0 98.8 ? ? ? ? ? ? 187 TRP BA CD2 1 70 B B +ATOM 8495 N NE1 . TRP BA 1 70 ? -73.997 14.471 53.788 1.0 99.49 ? ? ? ? ? ? 187 TRP BA NE1 1 70 B B +ATOM 8496 C CE2 . TRP BA 1 70 ? -73.159 14.165 52.752 1.0 100.0 ? ? ? ? ? ? 187 TRP BA CE2 1 70 B B +ATOM 8497 C CE3 . TRP BA 1 70 ? -73.316 13.181 50.542 1.0 99.8 ? ? ? ? ? ? 187 TRP BA CE3 1 70 B B +ATOM 8498 C CZ2 . TRP BA 1 70 ? -71.776 14.347 52.622 1.0 100.0 ? ? ? ? ? ? 187 TRP BA CZ2 1 70 B B +ATOM 8499 C CZ3 . TRP BA 1 70 ? -71.937 13.363 50.415 1.0 89.3 ? ? ? ? ? ? 187 TRP BA CZ3 1 70 B B +ATOM 8500 C CH2 . TRP BA 1 70 ? -71.186 13.943 51.450 1.0 96.22 ? ? ? ? ? ? 187 TRP BA CH2 1 70 B B +ATOM 8501 N N . GLY BA 1 71 ? -77.217 11.184 53.745 1.0 83.69 ? ? ? ? ? ? 188 GLY BA N 1 71 B B +ATOM 8502 C CA . GLY BA 1 71 ? -77.039 10.678 55.094 1.0 81.98 ? ? ? ? ? ? 188 GLY BA CA 1 71 B B +ATOM 8503 C C . GLY BA 1 71 ? -77.111 9.164 55.194 1.0 84.97 ? ? ? ? ? ? 188 GLY BA C 1 71 B B +ATOM 8504 O O . GLY BA 1 71 ? -76.550 8.571 56.115 1.0 84.72 ? ? ? ? ? ? 188 GLY BA O 1 71 B B +ATOM 8505 N N . THR BA 1 72 ? -77.802 8.532 54.252 1.0 82.41 ? ? ? ? ? ? 189 THR BA N 1 72 B B +ATOM 8506 C CA . THR BA 1 72 ? -77.922 7.079 54.258 1.0 86.07 ? ? ? ? ? ? 189 THR BA CA 1 72 B B +ATOM 8507 C C . THR BA 1 72 ? -76.577 6.465 53.880 1.0 92.27 ? ? ? ? ? ? 189 THR BA C 1 72 B B +ATOM 8508 O O . THR BA 1 72 ? -76.253 5.348 54.289 1.0 100.0 ? ? ? ? ? ? 189 THR BA O 1 72 B B +ATOM 8509 C CB . THR BA 1 72 ? -79.000 6.600 53.261 1.0 93.08 ? ? ? ? ? ? 189 THR BA CB 1 72 B B +ATOM 8510 O OG1 . THR BA 1 72 ? -80.287 7.058 53.694 1.0 87.08 ? ? ? ? ? ? 189 THR BA OG1 1 72 B B +ATOM 8511 C CG2 . THR BA 1 72 ? -79.019 5.079 53.177 1.0 99.21 ? ? ? ? ? ? 189 THR BA CG2 1 72 B B +ATOM 8512 N N . VAL BA 1 73 ? -75.798 7.205 53.096 1.0 94.3 ? ? ? ? ? ? 190 VAL BA N 1 73 B B +ATOM 8513 C CA . VAL BA 1 73 ? -74.480 6.748 52.665 1.0 94.99 ? ? ? ? ? ? 190 VAL BA CA 1 73 B B +ATOM 8514 C C . VAL BA 1 73 ? -73.416 7.261 53.633 1.0 100.0 ? ? ? ? ? ? 190 VAL BA C 1 73 B B +ATOM 8515 O O . VAL BA 1 73 ? -72.410 6.597 53.882 1.0 100.0 ? ? ? ? ? ? 190 VAL BA O 1 73 B B +ATOM 8516 C CB . VAL BA 1 73 ? -74.143 7.257 51.250 1.0 96.95 ? ? ? ? ? ? 190 VAL BA CB 1 73 B B +ATOM 8517 C CG1 . VAL BA 1 73 ? -72.909 6.541 50.725 1.0 100.0 ? ? ? ? ? ? 190 VAL BA CG1 1 73 B B +ATOM 8518 C CG2 . VAL BA 1 73 ? -75.321 7.040 50.324 1.0 93.72 ? ? ? ? ? ? 190 VAL BA CG2 1 73 B B +ATOM 8519 N N . PHE BA 1 74 ? -73.654 8.452 54.174 1.0 100.0 ? ? ? ? ? ? 191 PHE BA N 1 74 B B +ATOM 8520 C CA . PHE BA 1 74 ? -72.740 9.076 55.125 1.0 93.04 ? ? ? ? ? ? 191 PHE BA CA 1 74 B B +ATOM 8521 C C . PHE BA 1 74 ? -72.745 8.322 56.454 1.0 97.34 ? ? ? ? ? ? 191 PHE BA C 1 74 B B +ATOM 8522 O O . PHE BA 1 74 ? -71.806 8.424 57.240 1.0 100.0 ? ? ? ? ? ? 191 PHE BA O 1 74 B B +ATOM 8523 C CB . PHE BA 1 74 ? -73.151 10.528 55.361 1.0 89.23 ? ? ? ? ? ? 191 PHE BA CB 1 74 B B +ATOM 8524 C CG . PHE BA 1 74 ? -72.173 11.312 56.185 1.0 95.04 ? ? ? ? ? ? 191 PHE BA CG 1 74 B B +ATOM 8525 C CD1 . PHE BA 1 74 ? -71.174 12.063 55.573 1.0 100.0 ? ? ? ? ? ? 191 PHE BA CD1 1 74 B B +ATOM 8526 C CD2 . PHE BA 1 74 ? -72.260 11.316 57.575 1.0 91.88 ? ? ? ? ? ? 191 PHE BA CD2 1 74 B B +ATOM 8527 C CE1 . PHE BA 1 74 ? -70.274 12.812 56.334 1.0 100.0 ? ? ? ? ? ? 191 PHE BA CE1 1 74 B B +ATOM 8528 C CE2 . PHE BA 1 74 ? -71.367 12.060 58.346 1.0 95.25 ? ? ? ? ? ? 191 PHE BA CE2 1 74 B B +ATOM 8529 C CZ . PHE BA 1 74 ? -70.372 12.810 57.724 1.0 95.85 ? ? ? ? ? ? 191 PHE BA CZ 1 74 B B +ATOM 8530 N N . LYS BA 1 75 ? -73.812 7.572 56.705 1.0 99.92 ? ? ? ? ? ? 192 LYS BA N 1 75 B B +ATOM 8531 C CA . LYS BA 1 75 ? -73.923 6.799 57.937 1.0 91.4 ? ? ? ? ? ? 192 LYS BA CA 1 75 B B +ATOM 8532 C C . LYS BA 1 75 ? -73.375 5.395 57.731 1.0 88.92 ? ? ? ? ? ? 192 LYS BA C 1 75 B B +ATOM 8533 O O . LYS BA 1 75 ? -72.594 4.896 58.540 1.0 90.84 ? ? ? ? ? ? 192 LYS BA O 1 75 B B +ATOM 8534 C CB . LYS BA 1 75 ? -75.384 6.709 58.378 1.0 89.87 ? ? ? ? ? ? 192 LYS BA CB 1 75 B B +ATOM 8535 C CG . LYS BA 1 75 ? -75.586 5.953 59.678 1.0 89.83 ? ? ? ? ? ? 192 LYS BA CG 1 75 B B +ATOM 8536 C CD . LYS BA 1 75 ? -77.055 5.877 60.056 1.0 95.97 ? ? ? ? ? ? 192 LYS BA CD 1 75 B B +ATOM 8537 C CE . LYS BA 1 75 ? -77.521 7.166 60.716 1.0 100.0 ? ? ? ? ? ? 192 LYS BA CE 1 75 B B +ATOM 8538 N NZ . LYS BA 1 75 ? -77.045 7.281 62.123 1.0 92.77 ? ? ? ? ? ? 192 LYS BA NZ 1 75 B B +ATOM 8539 N N . THR BA 1 76 ? -73.794 4.767 56.637 1.0 81.15 ? ? ? ? ? ? 193 THR BA N 1 76 B B +ATOM 8540 C CA . THR BA 1 76 ? -73.366 3.414 56.302 1.0 85.66 ? ? ? ? ? ? 193 THR BA CA 1 76 B B +ATOM 8541 C C . THR BA 1 76 ? -71.852 3.279 56.152 1.0 94.76 ? ? ? ? ? ? 193 THR BA C 1 76 B B +ATOM 8542 O O . THR BA 1 76 ? -71.280 2.247 56.500 1.0 100.0 ? ? ? ? ? ? 193 THR BA O 1 76 B B +ATOM 8543 C CB . THR BA 1 76 ? -74.014 2.938 54.989 1.0 78.24 ? ? ? ? ? ? 193 THR BA CB 1 76 B B +ATOM 8544 O OG1 . THR BA 1 76 ? -73.492 1.650 54.637 1.0 84.32 ? ? ? ? ? ? 193 THR BA OG1 1 76 B B +ATOM 8545 C CG2 . THR BA 1 76 ? -73.714 3.911 53.873 1.0 86.03 ? ? ? ? ? ? 193 THR BA CG2 1 76 B B +ATOM 8546 N N . LEU BA 1 77 ? -71.207 4.324 55.639 1.0 100.0 ? ? ? ? ? ? 194 LEU BA N 1 77 B B +ATOM 8547 C CA . LEU BA 1 77 ? -69.760 4.298 55.427 1.0 100.0 ? ? ? ? ? ? 194 LEU BA CA 1 77 B B +ATOM 8548 C C . LEU BA 1 77 ? -68.922 4.870 56.574 1.0 93.7 ? ? ? ? ? ? 194 LEU BA C 1 77 B B +ATOM 8549 O O . LEU BA 1 77 ? -67.789 4.437 56.796 1.0 82.21 ? ? ? ? ? ? 194 LEU BA O 1 77 B B +ATOM 8550 C CB . LEU BA 1 77 ? -69.413 5.034 54.128 1.0 91.86 ? ? ? ? ? ? 194 LEU BA CB 1 77 B B +ATOM 8551 C CG . LEU BA 1 77 ? -69.942 4.404 52.834 1.0 86.06 ? ? ? ? ? ? 194 LEU BA CG 1 77 B B +ATOM 8552 C CD1 . LEU BA 1 77 ? -69.632 5.321 51.661 1.0 79.72 ? ? ? ? ? ? 194 LEU BA CD1 1 77 B B +ATOM 8553 C CD2 . LEU BA 1 77 ? -69.312 3.038 52.625 1.0 72.84 ? ? ? ? ? ? 194 LEU BA CD2 1 77 B B +ATOM 8554 N N . LYS BA 1 78 ? -69.472 5.838 57.297 1.0 90.86 ? ? ? ? ? ? 195 LYS BA N 1 78 B B +ATOM 8555 C CA . LYS BA 1 78 ? -68.752 6.455 58.406 1.0 93.04 ? ? ? ? ? ? 195 LYS BA CA 1 78 B B +ATOM 8556 C C . LYS BA 1 78 ? -68.301 5.435 59.446 1.0 98.88 ? ? ? ? ? ? 195 LYS BA C 1 78 B B +ATOM 8557 O O . LYS BA 1 78 ? -67.322 5.653 60.165 1.0 99.95 ? ? ? ? ? ? 195 LYS BA O 1 78 B B +ATOM 8558 C CB . LYS BA 1 78 ? -69.623 7.508 59.086 1.0 91.45 ? ? ? ? ? ? 195 LYS BA CB 1 78 B B +ATOM 8559 C CG . LYS BA 1 78 ? -68.893 8.292 60.163 1.0 94.15 ? ? ? ? ? ? 195 LYS BA CG 1 78 B B +ATOM 8560 C CD . LYS BA 1 78 ? -69.654 9.548 60.548 1.0 98.91 ? ? ? ? ? ? 195 LYS BA CD 1 78 B B +ATOM 8561 C CE . LYS BA 1 78 ? -69.093 10.153 61.827 1.0 100.0 ? ? ? ? ? ? 195 LYS BA CE 1 78 B B +ATOM 8562 N NZ . LYS BA 1 78 ? -67.661 10.540 61.686 1.0 100.0 ? ? ? ? ? ? 195 LYS BA NZ 1 78 B B +ATOM 8563 N N . SER BA 1 79 ? -69.021 4.322 59.527 1.0 100.0 ? ? ? ? ? ? 196 SER BA N 1 79 B B +ATOM 8564 C CA . SER BA 1 79 ? -68.696 3.276 60.486 1.0 100.0 ? ? ? ? ? ? 196 SER BA CA 1 79 B B +ATOM 8565 C C . SER BA 1 79 ? -67.493 2.435 60.060 1.0 100.0 ? ? ? ? ? ? 196 SER BA C 1 79 B B +ATOM 8566 O O . SER BA 1 79 ? -66.657 2.072 60.889 1.0 100.0 ? ? ? ? ? ? 196 SER BA O 1 79 B B +ATOM 8567 C CB . SER BA 1 79 ? -69.906 2.361 60.692 1.0 100.0 ? ? ? ? ? ? 196 SER BA CB 1 79 B B +ATOM 8568 O OG . SER BA 1 79 ? -70.188 1.615 59.516 1.0 100.0 ? ? ? ? ? ? 196 SER BA OG 1 79 B B +ATOM 8569 N N . LEU BA 1 80 ? -67.404 2.139 58.765 1.0 100.0 ? ? ? ? ? ? 197 LEU BA N 1 80 B B +ATOM 8570 C CA . LEU BA 1 80 ? -66.318 1.315 58.236 1.0 98.58 ? ? ? ? ? ? 197 LEU BA CA 1 80 B B +ATOM 8571 C C . LEU BA 1 80 ? -65.037 2.044 57.837 1.0 98.97 ? ? ? ? ? ? 197 LEU BA C 1 80 B B +ATOM 8572 O O . LEU BA 1 80 ? -64.125 1.427 57.290 1.0 92.55 ? ? ? ? ? ? 197 LEU BA O 1 80 B B +ATOM 8573 C CB . LEU BA 1 80 ? -66.808 0.519 57.023 1.0 95.15 ? ? ? ? ? ? 197 LEU BA CB 1 80 B B +ATOM 8574 C CG . LEU BA 1 80 ? -68.165 -0.187 57.092 1.0 86.6 ? ? ? ? ? ? 197 LEU BA CG 1 80 B B +ATOM 8575 C CD1 . LEU BA 1 80 ? -68.401 -0.922 55.785 1.0 88.71 ? ? ? ? ? ? 197 LEU BA CD1 1 80 B B +ATOM 8576 C CD2 . LEU BA 1 80 ? -68.200 -1.157 58.260 1.0 83.91 ? ? ? ? ? ? 197 LEU BA CD2 1 80 B B +ATOM 8577 N N . TYR BA 1 81 ? -64.953 3.342 58.106 1.0 100.0 ? ? ? ? ? ? 198 TYR BA N 1 81 B B +ATOM 8578 C CA . TYR BA 1 81 ? -63.754 4.084 57.727 1.0 100.0 ? ? ? ? ? ? 198 TYR BA CA 1 81 B B +ATOM 8579 C C . TYR BA 1 81 ? -62.578 3.896 58.678 1.0 100.0 ? ? ? ? ? ? 198 TYR BA C 1 81 B B +ATOM 8580 O O . TYR BA 1 81 ? -61.467 3.595 58.241 1.0 98.32 ? ? ? ? ? ? 198 TYR BA O 1 81 B B +ATOM 8581 C CB . TYR BA 1 81 ? -64.078 5.569 57.572 1.0 100.0 ? ? ? ? ? ? 198 TYR BA CB 1 81 B B +ATOM 8582 C CG . TYR BA 1 81 ? -64.676 5.906 56.227 1.0 100.0 ? ? ? ? ? ? 198 TYR BA CG 1 81 B B +ATOM 8583 C CD1 . TYR BA 1 81 ? -64.373 5.142 55.096 1.0 100.0 ? ? ? ? ? ? 198 TYR BA CD1 1 81 B B +ATOM 8584 C CD2 . TYR BA 1 81 ? -65.570 6.969 56.086 1.0 95.8 ? ? ? ? ? ? 198 TYR BA CD2 1 81 B B +ATOM 8585 C CE1 . TYR BA 1 81 ? -64.947 5.425 53.860 1.0 100.0 ? ? ? ? ? ? 198 TYR BA CE1 1 81 B B +ATOM 8586 C CE2 . TYR BA 1 81 ? -66.149 7.261 54.855 1.0 99.81 ? ? ? ? ? ? 198 TYR BA CE2 1 81 B B +ATOM 8587 C CZ . TYR BA 1 81 ? -65.834 6.485 53.747 1.0 100.0 ? ? ? ? ? ? 198 TYR BA CZ 1 81 B B +ATOM 8588 O OH . TYR BA 1 81 ? -66.401 6.770 52.524 1.0 100.0 ? ? ? ? ? ? 198 TYR BA OH 1 81 B B +ATOM 8589 N N . LYS BA 1 82 ? -62.810 4.080 59.972 1.0 100.0 ? ? ? ? ? ? 199 LYS BA N 1 82 B B +ATOM 8590 C CA . LYS BA 1 82 ? -61.735 3.901 60.945 1.0 100.0 ? ? ? ? ? ? 199 LYS BA CA 1 82 B B +ATOM 8591 C C . LYS BA 1 82 ? -61.282 2.450 60.893 1.0 98.56 ? ? ? ? ? ? 199 LYS BA C 1 82 B B +ATOM 8592 O O . LYS BA 1 82 ? -60.168 2.108 61.298 1.0 100.0 ? ? ? ? ? ? 199 LYS BA O 1 82 B B +ATOM 8593 C CB . LYS BA 1 82 ? -62.225 4.235 62.353 1.0 100.0 ? ? ? ? ? ? 199 LYS BA CB 1 82 B B +ATOM 8594 C CG . LYS BA 1 82 ? -63.553 3.594 62.712 1.0 95.6 ? ? ? ? ? ? 199 LYS BA CG 1 82 B B +ATOM 8595 C CD . LYS BA 1 82 ? -64.167 4.274 63.923 1.0 100.0 ? ? ? ? ? ? 199 LYS BA CD 1 82 B B +ATOM 8596 C CE . LYS BA 1 82 ? -64.487 5.731 63.624 1.0 100.0 ? ? ? ? ? ? 199 LYS BA CE 1 82 B B +ATOM 8597 N NZ . LYS BA 1 82 ? -65.384 5.868 62.441 1.0 97.17 ? ? ? ? ? ? 199 LYS BA NZ 1 82 B B +ATOM 8598 N N . THR BA 1 83 ? -62.163 1.601 60.383 1.0 91.15 ? ? ? ? ? ? 200 THR BA N 1 83 B B +ATOM 8599 C CA . THR BA 1 83 ? -61.874 0.185 60.274 1.0 95.96 ? ? ? ? ? ? 200 THR BA CA 1 83 B B +ATOM 8600 C C . THR BA 1 83 ? -61.118 -0.168 58.998 1.0 100.0 ? ? ? ? ? ? 200 THR BA C 1 83 B B +ATOM 8601 O O . THR BA 1 83 ? -59.941 -0.529 59.040 1.0 100.0 ? ? ? ? ? ? 200 THR BA O 1 83 B B +ATOM 8602 C CB . THR BA 1 83 ? -63.170 -0.641 60.309 1.0 89.26 ? ? ? ? ? ? 200 THR BA CB 1 83 B B +ATOM 8603 O OG1 . THR BA 1 83 ? -63.998 -0.177 61.379 1.0 100.0 ? ? ? ? ? ? 200 THR BA OG1 1 83 B B +ATOM 8604 C CG2 . THR BA 1 83 ? -62.858 -2.117 60.514 1.0 84.09 ? ? ? ? ? ? 200 THR BA CG2 1 83 B B +ATOM 8605 N N . HIS BA 1 84 ? -61.806 -0.052 57.866 1.0 100.0 ? ? ? ? ? ? 201 HIS BA N 1 84 B B +ATOM 8606 C CA . HIS BA 1 84 ? -61.232 -0.397 56.568 1.0 100.0 ? ? ? ? ? ? 201 HIS BA CA 1 84 B B +ATOM 8607 C C . HIS BA 1 84 ? -60.481 0.707 55.813 1.0 100.0 ? ? ? ? ? ? 201 HIS BA C 1 84 B B +ATOM 8608 O O . HIS BA 1 84 ? -59.532 0.419 55.079 1.0 100.0 ? ? ? ? ? ? 201 HIS BA O 1 84 B B +ATOM 8609 C CB . HIS BA 1 84 ? -62.333 -0.970 55.666 1.0 98.58 ? ? ? ? ? ? 201 HIS BA CB 1 84 B B +ATOM 8610 C CG . HIS BA 1 84 ? -63.073 -2.125 56.271 1.0 100.0 ? ? ? ? ? ? 201 HIS BA CG 1 84 B B +ATOM 8611 N ND1 . HIS BA 1 84 ? -62.430 -3.176 56.892 1.0 100.0 ? ? ? ? ? ? 201 HIS BA ND1 1 84 B B +ATOM 8612 C CD2 . HIS BA 1 84 ? -64.396 -2.396 56.345 1.0 94.96 ? ? ? ? ? ? 201 HIS BA CD2 1 84 B B +ATOM 8613 C CE1 . HIS BA 1 84 ? -63.329 -4.045 57.321 1.0 100.0 ? ? ? ? ? ? 201 HIS BA CE1 1 84 B B +ATOM 8614 N NE2 . HIS BA 1 84 ? -64.529 -3.596 57.002 1.0 95.85 ? ? ? ? ? ? 201 HIS BA NE2 1 84 B B +ATOM 8615 N N . ALA BA 1 85 ? -60.893 1.959 55.984 1.0 99.68 ? ? ? ? ? ? 202 ALA BA N 1 85 B B +ATOM 8616 C CA . ALA BA 1 85 ? -60.242 3.069 55.287 1.0 100.0 ? ? ? ? ? ? 202 ALA BA CA 1 85 B B +ATOM 8617 C C . ALA BA 1 85 ? -58.800 3.290 55.738 1.0 100.0 ? ? ? ? ? ? 202 ALA BA C 1 85 B B +ATOM 8618 O O . ALA BA 1 85 ? -58.435 2.966 56.868 1.0 100.0 ? ? ? ? ? ? 202 ALA BA O 1 85 B B +ATOM 8619 C CB . ALA BA 1 85 ? -61.044 4.346 55.475 1.0 100.0 ? ? ? ? ? ? 202 ALA BA CB 1 85 B B +ATOM 8620 N N . CYS BA 1 86 ? -57.986 3.847 54.842 1.0 100.0 ? ? ? ? ? ? 203 CYS BA N 1 86 B B +ATOM 8621 C CA . CYS BA 1 86 ? -56.579 4.114 55.131 1.0 100.0 ? ? ? ? ? ? 203 CYS BA CA 1 86 B B +ATOM 8622 C C . CYS BA 1 86 ? -56.388 5.311 56.055 1.0 100.0 ? ? ? ? ? ? 203 CYS BA C 1 86 B B +ATOM 8623 O O . CYS BA 1 86 ? -57.273 6.159 56.192 1.0 96.91 ? ? ? ? ? ? 203 CYS BA O 1 86 B B +ATOM 8624 C CB . CYS BA 1 86 ? -55.804 4.333 53.828 1.0 98.58 ? ? ? ? ? ? 203 CYS BA CB 1 86 B B +ATOM 8625 S SG . CYS BA 1 86 ? -56.133 5.902 52.998 1.0 100.0 ? ? ? ? ? ? 203 CYS BA SG 1 86 B B +ATOM 8626 N N . TYR BA 1 87 ? -55.216 5.369 56.678 1.0 96.51 ? ? ? ? ? ? 204 TYR BA N 1 87 B B +ATOM 8627 C CA . TYR BA 1 87 ? -54.875 6.430 57.616 1.0 100.0 ? ? ? ? ? ? 204 TYR BA CA 1 87 B B +ATOM 8628 C C . TYR BA 1 87 ? -55.109 7.848 57.097 1.0 100.0 ? ? ? ? ? ? 204 TYR BA C 1 87 B B +ATOM 8629 O O . TYR BA 1 87 ? -55.845 8.623 57.708 1.0 90.91 ? ? ? ? ? ? 204 TYR BA O 1 87 B B +ATOM 8630 C CB . TYR BA 1 87 ? -53.414 6.275 58.055 1.0 100.0 ? ? ? ? ? ? 204 TYR BA CB 1 87 B B +ATOM 8631 C CG . TYR BA 1 87 ? -52.795 7.534 58.621 1.0 100.0 ? ? ? ? ? ? 204 TYR BA CG 1 87 B B +ATOM 8632 C CD1 . TYR BA 1 87 ? -53.383 8.200 59.697 1.0 100.0 ? ? ? ? ? ? 204 TYR BA CD1 1 87 B B +ATOM 8633 C CD2 . TYR BA 1 87 ? -51.624 8.064 58.076 1.0 100.0 ? ? ? ? ? ? 204 TYR BA CD2 1 87 B B +ATOM 8634 C CE1 . TYR BA 1 87 ? -52.821 9.363 60.218 1.0 100.0 ? ? ? ? ? ? 204 TYR BA CE1 1 87 B B +ATOM 8635 C CE2 . TYR BA 1 87 ? -51.053 9.227 58.589 1.0 100.0 ? ? ? ? ? ? 204 TYR BA CE2 1 87 B B +ATOM 8636 C CZ . TYR BA 1 87 ? -51.658 9.869 59.660 1.0 100.0 ? ? ? ? ? ? 204 TYR BA CZ 1 87 B B +ATOM 8637 O OH . TYR BA 1 87 ? -51.097 11.011 60.183 1.0 100.0 ? ? ? ? ? ? 204 TYR BA OH 1 87 B B +ATOM 8638 N N . GLU BA 1 88 ? -54.475 8.187 55.979 1.0 97.1 ? ? ? ? ? ? 205 GLU BA N 1 88 B B +ATOM 8639 C CA . GLU BA 1 88 ? -54.609 9.525 55.403 1.0 92.62 ? ? ? ? ? ? 205 GLU BA CA 1 88 B B +ATOM 8640 C C . GLU BA 1 88 ? -56.068 9.954 55.316 1.0 92.8 ? ? ? ? ? ? 205 GLU BA C 1 88 B B +ATOM 8641 O O . GLU BA 1 88 ? -56.380 11.144 55.328 1.0 84.27 ? ? ? ? ? ? 205 GLU BA O 1 88 B B +ATOM 8642 C CB . GLU BA 1 88 ? -53.970 9.569 54.014 1.0 90.09 ? ? ? ? ? ? 205 GLU BA CB 1 88 B B +ATOM 8643 C CG . GLU BA 1 88 ? -52.506 9.158 53.992 1.0 94.04 ? ? ? ? ? ? 205 GLU BA CG 1 88 B B +ATOM 8644 C CD . GLU BA 1 88 ? -52.317 7.666 54.195 1.0 100.0 ? ? ? ? ? ? 205 GLU BA CD 1 88 B B +ATOM 8645 O OE1 . GLU BA 1 88 ? -51.203 7.251 54.582 1.0 100.0 ? ? ? ? ? ? 205 GLU BA OE1 1 88 B B +ATOM 8646 O OE2 . GLU BA 1 88 ? -53.285 6.906 53.965 1.0 100.0 ? ? ? ? ? ? 205 GLU BA OE2 1 88 B B +ATOM 8647 N N . TYR BA 1 89 ? -56.955 8.969 55.234 1.0 96.17 ? ? ? ? ? ? 206 TYR BA N 1 89 B B +ATOM 8648 C CA . TYR BA 1 89 ? -58.388 9.220 55.153 1.0 95.19 ? ? ? ? ? ? 206 TYR BA CA 1 89 B B +ATOM 8649 C C . TYR BA 1 89 ? -58.926 9.543 56.539 1.0 89.6 ? ? ? ? ? ? 206 TYR BA C 1 89 B B +ATOM 8650 O O . TYR BA 1 89 ? -59.559 10.577 56.752 1.0 82.02 ? ? ? ? ? ? 206 TYR BA O 1 89 B B +ATOM 8651 C CB . TYR BA 1 89 ? -59.107 7.984 54.602 1.0 96.64 ? ? ? ? ? ? 206 TYR BA CB 1 89 B B +ATOM 8652 C CG . TYR BA 1 89 ? -60.523 8.236 54.131 1.0 100.0 ? ? ? ? ? ? 206 TYR BA CG 1 89 B B +ATOM 8653 C CD1 . TYR BA 1 89 ? -60.876 8.045 52.795 1.0 96.4 ? ? ? ? ? ? 206 TYR BA CD1 1 89 B B +ATOM 8654 C CD2 . TYR BA 1 89 ? -61.517 8.647 55.023 1.0 100.0 ? ? ? ? ? ? 206 TYR BA CD2 1 89 B B +ATOM 8655 C CE1 . TYR BA 1 89 ? -62.180 8.254 52.360 1.0 92.61 ? ? ? ? ? ? 206 TYR BA CE1 1 89 B B +ATOM 8656 C CE2 . TYR BA 1 89 ? -62.826 8.858 54.597 1.0 88.45 ? ? ? ? ? ? 206 TYR BA CE2 1 89 B B +ATOM 8657 C CZ . TYR BA 1 89 ? -63.148 8.659 53.266 1.0 92.44 ? ? ? ? ? ? 206 TYR BA CZ 1 89 B B +ATOM 8658 O OH . TYR BA 1 89 ? -64.436 8.867 52.839 1.0 100.0 ? ? ? ? ? ? 206 TYR BA OH 1 89 B B +ATOM 8659 N N . ASN BA 1 90 ? -58.665 8.637 57.476 1.0 89.21 ? ? ? ? ? ? 207 ASN BA N 1 90 B B +ATOM 8660 C CA . ASN BA 1 90 ? -59.115 8.788 58.851 1.0 83.61 ? ? ? ? ? ? 207 ASN BA CA 1 90 B B +ATOM 8661 C C . ASN BA 1 90 ? -58.538 10.034 59.506 1.0 81.92 ? ? ? ? ? ? 207 ASN BA C 1 90 B B +ATOM 8662 O O . ASN BA 1 90 ? -59.094 10.539 60.481 1.0 87.79 ? ? ? ? ? ? 207 ASN BA O 1 90 B B +ATOM 8663 C CB . ASN BA 1 90 ? -58.727 7.550 59.663 1.0 84.88 ? ? ? ? ? ? 207 ASN BA CB 1 90 B B +ATOM 8664 C CG . ASN BA 1 90 ? -59.394 6.284 59.155 1.0 85.25 ? ? ? ? ? ? 207 ASN BA CG 1 90 B B +ATOM 8665 O OD1 . ASN BA 1 90 ? -60.620 6.180 59.147 1.0 93.52 ? ? ? ? ? ? 207 ASN BA OD1 1 90 B B +ATOM 8666 N ND2 . ASN BA 1 90 ? -58.591 5.316 58.727 1.0 56.4 ? ? ? ? ? ? 207 ASN BA ND2 1 90 B B +ATOM 8667 N N . HIS BA 1 91 ? -57.427 10.530 58.968 1.0 79.44 ? ? ? ? ? ? 208 HIS BA N 1 91 B B +ATOM 8668 C CA . HIS BA 1 91 ? -56.785 11.718 59.519 1.0 79.24 ? ? ? ? ? ? 208 HIS BA CA 1 91 B B +ATOM 8669 C C . HIS BA 1 91 ? -57.481 12.999 59.075 1.0 82.31 ? ? ? ? ? ? 208 HIS BA C 1 91 B B +ATOM 8670 O O . HIS BA 1 91 ? -57.799 13.864 59.890 1.0 88.47 ? ? ? ? ? ? 208 HIS BA O 1 91 B B +ATOM 8671 C CB . HIS BA 1 91 ? -55.314 11.778 59.100 1.0 71.64 ? ? ? ? ? ? 208 HIS BA CB 1 91 B B +ATOM 8672 C CG . HIS BA 1 91 ? -54.693 13.132 59.275 1.0 94.11 ? ? ? ? ? ? 208 HIS BA CG 1 91 B B +ATOM 8673 N ND1 . HIS BA 1 91 ? -54.114 13.825 58.235 1.0 100.0 ? ? ? ? ? ? 208 HIS BA ND1 1 91 B B +ATOM 8674 C CD2 . HIS BA 1 91 ? -54.583 13.926 60.365 1.0 97.39 ? ? ? ? ? ? 208 HIS BA CD2 1 91 B B +ATOM 8675 C CE1 . HIS BA 1 91 ? -53.671 14.990 58.677 1.0 100.0 ? ? ? ? ? ? 208 HIS BA CE1 1 91 B B +ATOM 8676 N NE2 . HIS BA 1 91 ? -53.944 15.077 59.967 1.0 97.55 ? ? ? ? ? ? 208 HIS BA NE2 1 91 B B +ATOM 8677 N N . ILE BA 1 92 ? -57.720 13.108 57.776 1.0 87.23 ? ? ? ? ? ? 209 ILE BA N 1 92 B B +ATOM 8678 C CA . ILE BA 1 92 ? -58.349 14.292 57.211 1.0 88.32 ? ? ? ? ? ? 209 ILE BA CA 1 92 B B +ATOM 8679 C C . ILE BA 1 92 ? -59.850 14.427 57.452 1.0 88.65 ? ? ? ? ? ? 209 ILE BA C 1 92 B B +ATOM 8680 O O . ILE BA 1 92 ? -60.377 15.542 57.494 1.0 79.81 ? ? ? ? ? ? 209 ILE BA O 1 92 B B +ATOM 8681 C CB . ILE BA 1 92 ? -58.099 14.362 55.689 1.0 92.64 ? ? ? ? ? ? 209 ILE BA CB 1 92 B B +ATOM 8682 C CG1 . ILE BA 1 92 ? -58.529 15.730 55.156 1.0 100.0 ? ? ? ? ? ? 209 ILE BA CG1 1 92 B B +ATOM 8683 C CG2 . ILE BA 1 92 ? -58.846 13.234 54.985 1.0 84.88 ? ? ? ? ? ? 209 ILE BA CG2 1 92 B B +ATOM 8684 C CD1 . ILE BA 1 92 ? -57.755 16.885 55.753 1.0 100.0 ? ? ? ? ? ? 209 ILE BA CD1 1 92 B B +ATOM 8685 N N . PHE BA 1 93 ? -60.537 13.299 57.613 1.0 92.19 ? ? ? ? ? ? 210 PHE BA N 1 93 B B +ATOM 8686 C CA . PHE BA 1 93 ? -61.983 13.322 57.813 1.0 91.92 ? ? ? ? ? ? 210 PHE BA CA 1 93 B B +ATOM 8687 C C . PHE BA 1 93 ? -62.461 14.300 58.877 1.0 96.44 ? ? ? ? ? ? 210 PHE BA C 1 93 B B +ATOM 8688 O O . PHE BA 1 93 ? -63.234 15.210 58.581 1.0 100.0 ? ? ? ? ? ? 210 PHE BA O 1 93 B B +ATOM 8689 C CB . PHE BA 1 93 ? -62.512 11.924 58.136 1.0 89.4 ? ? ? ? ? ? 210 PHE BA CB 1 93 B B +ATOM 8690 C CG . PHE BA 1 93 ? -63.790 11.581 57.418 1.0 97.33 ? ? ? ? ? ? 210 PHE BA CG 1 93 B B +ATOM 8691 C CD1 . PHE BA 1 93 ? -64.910 11.152 58.123 1.0 98.81 ? ? ? ? ? ? 210 PHE BA CD1 1 93 B B +ATOM 8692 C CD2 . PHE BA 1 93 ? -63.871 11.685 56.034 1.0 97.14 ? ? ? ? ? ? 210 PHE BA CD2 1 93 B B +ATOM 8693 C CE1 . PHE BA 1 93 ? -66.093 10.833 57.454 1.0 100.0 ? ? ? ? ? ? 210 PHE BA CE1 1 93 B B +ATOM 8694 C CE2 . PHE BA 1 93 ? -65.048 11.368 55.357 1.0 86.56 ? ? ? ? ? ? 210 PHE BA CE2 1 93 B B +ATOM 8695 C CZ . PHE BA 1 93 ? -66.160 10.941 56.070 1.0 85.39 ? ? ? ? ? ? 210 PHE BA CZ 1 93 B B +ATOM 8696 N N . PRO BA 1 94 ? -62.002 14.135 60.129 1.0 93.67 ? ? ? ? ? ? 211 PRO BA N 1 94 B B +ATOM 8697 C CA . PRO BA 1 94 ? -62.465 15.072 61.159 1.0 92.3 ? ? ? ? ? ? 211 PRO BA CA 1 94 B B +ATOM 8698 C C . PRO BA 1 94 ? -62.249 16.539 60.785 1.0 94.73 ? ? ? ? ? ? 211 PRO BA C 1 94 B B +ATOM 8699 O O . PRO BA 1 94 ? -62.899 17.428 61.340 1.0 82.46 ? ? ? ? ? ? 211 PRO BA O 1 94 B B +ATOM 8700 C CB . PRO BA 1 94 ? -61.676 14.659 62.400 1.0 98.76 ? ? ? ? ? ? 211 PRO BA CB 1 94 B B +ATOM 8701 C CG . PRO BA 1 94 ? -61.252 13.251 62.140 1.0 100.0 ? ? ? ? ? ? 211 PRO BA CG 1 94 B B +ATOM 8702 C CD . PRO BA 1 94 ? -61.057 13.141 60.660 1.0 92.28 ? ? ? ? ? ? 211 PRO BA CD 1 94 B B +ATOM 8703 N N . LEU BA 1 95 ? -61.340 16.787 59.841 1.0 99.82 ? ? ? ? ? ? 212 LEU BA N 1 95 B B +ATOM 8704 C CA . LEU BA 1 95 ? -61.057 18.149 59.385 1.0 97.01 ? ? ? ? ? ? 212 LEU BA CA 1 95 B B +ATOM 8705 C C . LEU BA 1 95 ? -62.064 18.526 58.303 1.0 97.71 ? ? ? ? ? ? 212 LEU BA C 1 95 B B +ATOM 8706 O O . LEU BA 1 95 ? -62.445 19.688 58.168 1.0 97.78 ? ? ? ? ? ? 212 LEU BA O 1 95 B B +ATOM 8707 C CB . LEU BA 1 95 ? -59.638 18.243 58.814 1.0 82.77 ? ? ? ? ? ? 212 LEU BA CB 1 95 B B +ATOM 8708 C CG . LEU BA 1 95 ? -58.480 18.100 59.803 1.0 72.26 ? ? ? ? ? ? 212 LEU BA CG 1 95 B B +ATOM 8709 C CD1 . LEU BA 1 95 ? -57.225 17.684 59.054 1.0 59.9 ? ? ? ? ? ? 212 LEU BA CD1 1 95 B B +ATOM 8710 C CD2 . LEU BA 1 95 ? -58.267 19.410 60.544 1.0 57.54 ? ? ? ? ? ? 212 LEU BA CD2 1 95 B B +ATOM 8711 N N . LEU BA 1 96 ? -62.480 17.529 57.526 1.0 96.22 ? ? ? ? ? ? 213 LEU BA N 1 96 B B +ATOM 8712 C CA . LEU BA 1 96 ? -63.460 17.734 56.467 1.0 93.39 ? ? ? ? ? ? 213 LEU BA CA 1 96 B B +ATOM 8713 C C . LEU BA 1 96 ? -64.809 17.963 57.136 1.0 93.86 ? ? ? ? ? ? 213 LEU BA C 1 96 B B +ATOM 8714 O O . LEU BA 1 96 ? -65.582 18.829 56.726 1.0 84.52 ? ? ? ? ? ? 213 LEU BA O 1 96 B B +ATOM 8715 C CB . LEU BA 1 96 ? -63.541 16.497 55.570 1.0 82.97 ? ? ? ? ? ? 213 LEU BA CB 1 96 B B +ATOM 8716 C CG . LEU BA 1 96 ? -62.440 16.299 54.528 1.0 75.57 ? ? ? ? ? ? 213 LEU BA CG 1 96 B B +ATOM 8717 C CD1 . LEU BA 1 96 ? -62.474 14.862 54.017 1.0 65.93 ? ? ? ? ? ? 213 LEU BA CD1 1 96 B B +ATOM 8718 C CD2 . LEU BA 1 96 ? -62.632 17.292 53.392 1.0 63.3 ? ? ? ? ? ? 213 LEU BA CD2 1 96 B B +ATOM 8719 N N . GLU BA 1 97 ? -65.079 17.171 58.170 1.0 97.38 ? ? ? ? ? ? 214 GLU BA N 1 97 B B +ATOM 8720 C CA . GLU BA 1 97 ? -66.325 17.266 58.916 1.0 94.83 ? ? ? ? ? ? 214 GLU BA CA 1 97 B B +ATOM 8721 C C . GLU BA 1 97 ? -66.388 18.599 59.642 1.0 95.6 ? ? ? ? ? ? 214 GLU BA C 1 97 B B +ATOM 8722 O O . GLU BA 1 97 ? -67.396 19.302 59.583 1.0 100.0 ? ? ? ? ? ? 214 GLU BA O 1 97 B B +ATOM 8723 C CB . GLU BA 1 97 ? -66.424 16.117 59.927 1.0 96.63 ? ? ? ? ? ? 214 GLU BA CB 1 97 B B +ATOM 8724 C CG . GLU BA 1 97 ? -66.264 14.733 59.312 1.0 100.0 ? ? ? ? ? ? 214 GLU BA CG 1 97 B B +ATOM 8725 C CD . GLU BA 1 97 ? -66.275 13.617 60.350 1.0 100.0 ? ? ? ? ? ? 214 GLU BA CD 1 97 B B +ATOM 8726 O OE1 . GLU BA 1 97 ? -65.204 13.016 60.594 1.0 99.52 ? ? ? ? ? ? 214 GLU BA OE1 1 97 B B +ATOM 8727 O OE2 . GLU BA 1 97 ? -67.354 13.340 60.921 1.0 100.0 ? ? ? ? ? ? 214 GLU BA OE2 1 97 B B +ATOM 8728 N N . LYS BA 1 98 ? -65.300 18.944 60.323 1.0 84.05 ? ? ? ? ? ? 215 LYS BA N 1 98 B B +ATOM 8729 C CA . LYS BA 1 98 ? -65.232 20.189 61.074 1.0 96.51 ? ? ? ? ? ? 215 LYS BA CA 1 98 B B +ATOM 8730 C C . LYS BA 1 98 ? -65.092 21.435 60.201 1.0 100.0 ? ? ? ? ? ? 215 LYS BA C 1 98 B B +ATOM 8731 O O . LYS BA 1 98 ? -65.302 22.554 60.675 1.0 100.0 ? ? ? ? ? ? 215 LYS BA O 1 98 B B +ATOM 8732 C CB . LYS BA 1 98 ? -64.061 20.142 62.060 1.0 90.98 ? ? ? ? ? ? 215 LYS BA CB 1 98 B B +ATOM 8733 C CG . LYS BA 1 98 ? -64.011 21.343 62.995 1.0 100.0 ? ? ? ? ? ? 215 LYS BA CG 1 98 B B +ATOM 8734 C CD . LYS BA 1 98 ? -62.849 21.254 63.970 1.0 100.0 ? ? ? ? ? ? 215 LYS BA CD 1 98 B B +ATOM 8735 C CE . LYS BA 1 98 ? -63.131 20.246 65.076 1.0 100.0 ? ? ? ? ? ? 215 LYS BA CE 1 98 B B +ATOM 8736 N NZ . LYS BA 1 98 ? -64.310 20.631 65.906 1.0 100.0 ? ? ? ? ? ? 215 LYS BA NZ 1 98 B B +ATOM 8737 N N . TYR BA 1 99 ? -64.749 21.252 58.929 1.0 100.0 ? ? ? ? ? ? 216 TYR BA N 1 99 B B +ATOM 8738 C CA . TYR BA 1 99 ? -64.560 22.403 58.055 1.0 100.0 ? ? ? ? ? ? 216 TYR BA CA 1 99 B B +ATOM 8739 C C . TYR BA 1 99 ? -65.476 22.546 56.843 1.0 100.0 ? ? ? ? ? ? 216 TYR BA C 1 99 B B +ATOM 8740 O O . TYR BA 1 99 ? -66.169 23.556 56.704 1.0 100.0 ? ? ? ? ? ? 216 TYR BA O 1 99 B B +ATOM 8741 C CB . TYR BA 1 99 ? -63.096 22.459 57.612 1.0 92.17 ? ? ? ? ? ? 216 TYR BA CB 1 99 B B +ATOM 8742 C CG . TYR BA 1 99 ? -62.166 22.851 58.734 1.0 100.0 ? ? ? ? ? ? 216 TYR BA CG 1 99 B B +ATOM 8743 C CD1 . TYR BA 1 99 ? -61.392 21.896 59.397 1.0 100.0 ? ? ? ? ? ? 216 TYR BA CD1 1 99 B B +ATOM 8744 C CD2 . TYR BA 1 99 ? -62.088 24.175 59.163 1.0 100.0 ? ? ? ? ? ? 216 TYR BA CD2 1 99 B B +ATOM 8745 C CE1 . TYR BA 1 99 ? -60.562 22.251 60.459 1.0 100.0 ? ? ? ? ? ? 216 TYR BA CE1 1 99 B B +ATOM 8746 C CE2 . TYR BA 1 99 ? -61.265 24.542 60.221 1.0 100.0 ? ? ? ? ? ? 216 TYR BA CE2 1 99 B B +ATOM 8747 C CZ . TYR BA 1 99 ? -60.506 23.577 60.868 1.0 100.0 ? ? ? ? ? ? 216 TYR BA CZ 1 99 B B +ATOM 8748 O OH . TYR BA 1 99 ? -59.694 23.938 61.923 1.0 100.0 ? ? ? ? ? ? 216 TYR BA OH 1 99 B B +ATOM 8749 N N . CYS BA 1 100 ? -65.489 21.546 55.970 1.0 93.36 ? ? ? ? ? ? 217 CYS BA N 1 100 B B +ATOM 8750 C CA . CYS BA 1 100 ? -66.316 21.621 54.770 1.0 100.0 ? ? ? ? ? ? 217 CYS BA CA 1 100 B B +ATOM 8751 C C . CYS BA 1 100 ? -67.759 21.148 54.950 1.0 99.81 ? ? ? ? ? ? 217 CYS BA C 1 100 B B +ATOM 8752 O O . CYS BA 1 100 ? -68.438 20.804 53.980 1.0 100.0 ? ? ? ? ? ? 217 CYS BA O 1 100 B B +ATOM 8753 C CB . CYS BA 1 100 ? -65.650 20.840 53.637 1.0 100.0 ? ? ? ? ? ? 217 CYS BA CB 1 100 B B +ATOM 8754 S SG . CYS BA 1 100 ? -64.146 21.616 52.997 1.0 99.81 ? ? ? ? ? ? 217 CYS BA SG 1 100 B B +ATOM 8755 N N . GLY BA 1 101 ? -68.223 21.138 56.193 1.0 96.48 ? ? ? ? ? ? 218 GLY BA N 1 101 B B +ATOM 8756 C CA . GLY BA 1 101 ? -69.584 20.717 56.468 1.0 100.0 ? ? ? ? ? ? 218 GLY BA CA 1 101 B B +ATOM 8757 C C . GLY BA 1 101 ? -69.886 19.266 56.141 1.0 100.0 ? ? ? ? ? ? 218 GLY BA C 1 101 B B +ATOM 8758 O O . GLY BA 1 101 ? -70.944 18.955 55.589 1.0 100.0 ? ? ? ? ? ? 218 GLY BA O 1 101 B B +ATOM 8759 N N . PHE BA 1 102 ? -68.962 18.375 56.484 1.0 91.88 ? ? ? ? ? ? 219 PHE BA N 1 102 B B +ATOM 8760 C CA . PHE BA 1 102 ? -69.154 16.953 56.226 1.0 85.18 ? ? ? ? ? ? 219 PHE BA CA 1 102 B B +ATOM 8761 C C . PHE BA 1 102 ? -69.961 16.328 57.362 1.0 81.64 ? ? ? ? ? ? 219 PHE BA C 1 102 B B +ATOM 8762 O O . PHE BA 1 102 ? -69.404 15.845 58.346 1.0 74.36 ? ? ? ? ? ? 219 PHE BA O 1 102 B B +ATOM 8763 C CB . PHE BA 1 102 ? -67.800 16.250 56.080 1.0 73.24 ? ? ? ? ? ? 219 PHE BA CB 1 102 B B +ATOM 8764 C CG . PHE BA 1 102 ? -67.313 16.156 54.655 1.0 69.87 ? ? ? ? ? ? 219 PHE BA CG 1 102 B B +ATOM 8765 C CD1 . PHE BA 1 102 ? -67.022 17.308 53.929 1.0 60.24 ? ? ? ? ? ? 219 PHE BA CD1 1 102 B B +ATOM 8766 C CD2 . PHE BA 1 102 ? -67.155 14.917 54.035 1.0 66.24 ? ? ? ? ? ? 219 PHE BA CD2 1 102 B B +ATOM 8767 C CE1 . PHE BA 1 102 ? -66.575 17.231 52.609 1.0 52.33 ? ? ? ? ? ? 219 PHE BA CE1 1 102 B B +ATOM 8768 C CE2 . PHE BA 1 102 ? -66.708 14.830 52.714 1.0 54.7 ? ? ? ? ? ? 219 PHE BA CE2 1 102 B B +ATOM 8769 C CZ . PHE BA 1 102 ? -66.421 15.990 52.001 1.0 60.48 ? ? ? ? ? ? 219 PHE BA CZ 1 102 B B +ATOM 8770 N N . HIS BA 1 103 ? -71.283 16.357 57.214 1.0 87.91 ? ? ? ? ? ? 220 HIS BA N 1 103 B B +ATOM 8771 C CA . HIS BA 1 103 ? -72.205 15.803 58.201 1.0 89.49 ? ? ? ? ? ? 220 HIS BA CA 1 103 B B +ATOM 8772 C C . HIS BA 1 103 ? -73.374 15.153 57.462 1.0 91.78 ? ? ? ? ? ? 220 HIS BA C 1 103 B B +ATOM 8773 O O . HIS BA 1 103 ? -73.786 15.631 56.405 1.0 100.0 ? ? ? ? ? ? 220 HIS BA O 1 103 B B +ATOM 8774 C CB . HIS BA 1 103 ? -72.720 16.917 59.113 1.0 91.7 ? ? ? ? ? ? 220 HIS BA CB 1 103 B B +ATOM 8775 C CG . HIS BA 1 103 ? -73.481 16.421 60.300 1.0 99.12 ? ? ? ? ? ? 220 HIS BA CG 1 103 B B +ATOM 8776 N ND1 . HIS BA 1 103 ? -74.447 17.176 60.933 1.0 100.0 ? ? ? ? ? ? 220 HIS BA ND1 1 103 B B +ATOM 8777 C CD2 . HIS BA 1 103 ? -73.417 15.250 60.975 1.0 98.33 ? ? ? ? ? ? 220 HIS BA CD2 1 103 B B +ATOM 8778 C CE1 . HIS BA 1 103 ? -74.942 16.490 61.946 1.0 100.0 ? ? ? ? ? ? 220 HIS BA CE1 1 103 B B +ATOM 8779 N NE2 . HIS BA 1 103 ? -74.336 15.318 61.996 1.0 100.0 ? ? ? ? ? ? 220 HIS BA NE2 1 103 B B +ATOM 8780 N N . GLU BA 1 104 ? -73.910 14.072 58.017 1.0 82.47 ? ? ? ? ? ? 221 GLU BA N 1 104 B B +ATOM 8781 C CA . GLU BA 1 104 ? -75.019 13.373 57.376 1.0 87.65 ? ? ? ? ? ? 221 GLU BA CA 1 104 B B +ATOM 8782 C C . GLU BA 1 104 ? -76.264 14.227 57.180 1.0 84.85 ? ? ? ? ? ? 221 GLU BA C 1 104 B B +ATOM 8783 O O . GLU BA 1 104 ? -77.155 13.856 56.415 1.0 90.1 ? ? ? ? ? ? 221 GLU BA O 1 104 B B +ATOM 8784 C CB . GLU BA 1 104 ? -75.390 12.124 58.173 1.0 94.21 ? ? ? ? ? ? 221 GLU BA CB 1 104 B B +ATOM 8785 C CG . GLU BA 1 104 ? -75.672 12.389 59.637 1.0 96.06 ? ? ? ? ? ? 221 GLU BA CG 1 104 B B +ATOM 8786 C CD . GLU BA 1 104 ? -76.108 11.135 60.370 1.0 100.0 ? ? ? ? ? ? 221 GLU BA CD 1 104 B B +ATOM 8787 O OE1 . GLU BA 1 104 ? -76.598 11.253 61.515 1.0 100.0 ? ? ? ? ? ? 221 GLU BA OE1 1 104 B B +ATOM 8788 O OE2 . GLU BA 1 104 ? -75.961 10.033 59.797 1.0 100.0 ? ? ? ? ? ? 221 GLU BA OE2 1 104 B B +ATOM 8789 N N . ASP BA 1 105 ? -76.325 15.369 57.860 1.0 81.47 ? ? ? ? ? ? 222 ASP BA N 1 105 B B +ATOM 8790 C CA . ASP BA 1 105 ? -77.489 16.243 57.751 1.0 89.8 ? ? ? ? ? ? 222 ASP BA CA 1 105 B B +ATOM 8791 C C . ASP BA 1 105 ? -77.376 17.340 56.699 1.0 83.18 ? ? ? ? ? ? 222 ASP BA C 1 105 B B +ATOM 8792 O O . ASP BA 1 105 ? -78.362 18.019 56.395 1.0 81.72 ? ? ? ? ? ? 222 ASP BA O 1 105 B B +ATOM 8793 C CB . ASP BA 1 105 ? -77.797 16.863 59.112 1.0 99.15 ? ? ? ? ? ? 222 ASP BA CB 1 105 B B +ATOM 8794 C CG . ASP BA 1 105 ? -78.344 15.848 60.097 1.0 100.0 ? ? ? ? ? ? 222 ASP BA CG 1 105 B B +ATOM 8795 O OD1 . ASP BA 1 105 ? -77.551 15.014 60.582 1.0 100.0 ? ? ? ? ? ? 222 ASP BA OD1 1 105 B B +ATOM 8796 O OD2 . ASP BA 1 105 ? -79.562 15.878 60.382 1.0 95.35 ? ? ? ? ? ? 222 ASP BA OD2 1 105 B B +ATOM 8797 N N . ASN BA 1 106 ? -76.185 17.518 56.138 1.0 71.97 ? ? ? ? ? ? 223 ASN BA N 1 106 B B +ATOM 8798 C CA . ASN BA 1 106 ? -75.992 18.542 55.120 1.0 72.54 ? ? ? ? ? ? 223 ASN BA CA 1 106 B B +ATOM 8799 C C . ASN BA 1 106 ? -75.001 18.116 54.045 1.0 72.39 ? ? ? ? ? ? 223 ASN BA C 1 106 B B +ATOM 8800 O O . ASN BA 1 106 ? -73.921 17.607 54.350 1.0 73.04 ? ? ? ? ? ? 223 ASN BA O 1 106 B B +ATOM 8801 C CB . ASN BA 1 106 ? -75.511 19.849 55.754 1.0 83.69 ? ? ? ? ? ? 223 ASN BA CB 1 106 B B +ATOM 8802 C CG . ASN BA 1 106 ? -75.093 20.877 54.717 1.0 99.58 ? ? ? ? ? ? 223 ASN BA CG 1 106 B B +ATOM 8803 O OD1 . ASN BA 1 106 ? -73.911 21.206 54.591 1.0 100.0 ? ? ? ? ? ? 223 ASN BA OD1 1 106 B B +ATOM 8804 N ND2 . ASN BA 1 106 ? -76.064 21.386 53.964 1.0 88.17 ? ? ? ? ? ? 223 ASN BA ND2 1 106 B B +ATOM 8805 N N . ILE BA 1 107 ? -75.376 18.324 52.786 1.0 67.74 ? ? ? ? ? ? 224 ILE BA N 1 107 B B +ATOM 8806 C CA . ILE BA 1 107 ? -74.508 17.975 51.666 1.0 61.97 ? ? ? ? ? ? 224 ILE BA CA 1 107 B B +ATOM 8807 C C . ILE BA 1 107 ? -73.486 19.095 51.464 1.0 66.83 ? ? ? ? ? ? 224 ILE BA C 1 107 B B +ATOM 8808 O O . ILE BA 1 107 ? -73.853 20.257 51.273 1.0 69.52 ? ? ? ? ? ? 224 ILE BA O 1 107 B B +ATOM 8809 C CB . ILE BA 1 107 ? -75.322 17.779 50.372 1.0 58.97 ? ? ? ? ? ? 224 ILE BA CB 1 107 B B +ATOM 8810 C CG1 . ILE BA 1 107 ? -76.167 16.505 50.482 1.0 50.83 ? ? ? ? ? ? 224 ILE BA CG1 1 107 B B +ATOM 8811 C CG2 . ILE BA 1 107 ? -74.383 17.685 49.182 1.0 64.9 ? ? ? ? ? ? 224 ILE BA CG2 1 107 B B +ATOM 8812 C CD1 . ILE BA 1 107 ? -76.984 16.199 49.245 1.0 53.55 ? ? ? ? ? ? 224 ILE BA CD1 1 107 B B +ATOM 8813 N N . PRO BA 1 108 ? -72.188 18.753 51.497 1.0 65.18 ? ? ? ? ? ? 225 PRO BA N 1 108 B B +ATOM 8814 C CA . PRO BA 1 108 ? -71.106 19.728 51.326 1.0 59.04 ? ? ? ? ? ? 225 PRO BA CA 1 108 B B +ATOM 8815 C C . PRO BA 1 108 ? -71.096 20.453 49.986 1.0 58.77 ? ? ? ? ? ? 225 PRO BA C 1 108 B B +ATOM 8816 O O . PRO BA 1 108 ? -71.269 19.838 48.933 1.0 54.44 ? ? ? ? ? ? 225 PRO BA O 1 108 B B +ATOM 8817 C CB . PRO BA 1 108 ? -69.833 18.906 51.527 1.0 54.6 ? ? ? ? ? ? 225 PRO BA CB 1 108 B B +ATOM 8818 C CG . PRO BA 1 108 ? -70.280 17.616 52.132 1.0 49.68 ? ? ? ? ? ? 225 PRO BA CG 1 108 B B +ATOM 8819 C CD . PRO BA 1 108 ? -71.671 17.387 51.669 1.0 55.63 ? ? ? ? ? ? 225 PRO BA CD 1 108 B B +ATOM 8820 N N . GLN BA 1 109 ? -70.867 21.765 50.039 1.0 53.98 ? ? ? ? ? ? 226 GLN BA N 1 109 B B +ATOM 8821 C CA . GLN BA 1 109 ? -70.821 22.596 48.839 1.0 63.11 ? ? ? ? ? ? 226 GLN BA CA 1 109 B B +ATOM 8822 C C . GLN BA 1 109 ? -69.436 22.570 48.196 1.0 59.81 ? ? ? ? ? ? 226 GLN BA C 1 109 B B +ATOM 8823 O O . GLN BA 1 109 ? -68.426 22.832 48.854 1.0 65.82 ? ? ? ? ? ? 226 GLN BA O 1 109 B B +ATOM 8824 C CB . GLN BA 1 109 ? -71.210 24.040 49.175 1.0 71.64 ? ? ? ? ? ? 226 GLN BA CB 1 109 B B +ATOM 8825 C CG . GLN BA 1 109 ? -72.687 24.227 49.495 1.0 76.63 ? ? ? ? ? ? 226 GLN BA CG 1 109 B B +ATOM 8826 C CD . GLN BA 1 109 ? -73.592 24.071 48.281 1.0 82.35 ? ? ? ? ? ? 226 GLN BA CD 1 109 B B +ATOM 8827 O OE1 . GLN BA 1 109 ? -74.620 24.741 48.172 1.0 90.41 ? ? ? ? ? ? 226 GLN BA OE1 1 109 B B +ATOM 8828 N NE2 . GLN BA 1 109 ? -73.214 23.186 47.364 1.0 88.22 ? ? ? ? ? ? 226 GLN BA NE2 1 109 B B +ATOM 8829 N N . LEU BA 1 110 ? -69.409 22.266 46.901 1.0 63.21 ? ? ? ? ? ? 227 LEU BA N 1 110 B B +ATOM 8830 C CA . LEU BA 1 110 ? -68.171 22.172 46.136 1.0 61.31 ? ? ? ? ? ? 227 LEU BA CA 1 110 B B +ATOM 8831 C C . LEU BA 1 110 ? -67.224 23.358 46.282 1.0 53.7 ? ? ? ? ? ? 227 LEU BA C 1 110 B B +ATOM 8832 O O . LEU BA 1 110 ? -66.013 23.174 46.407 1.0 46.0 ? ? ? ? ? ? 227 LEU BA O 1 110 B B +ATOM 8833 C CB . LEU BA 1 110 ? -68.489 21.949 44.652 1.0 47.53 ? ? ? ? ? ? 227 LEU BA CB 1 110 B B +ATOM 8834 C CG . LEU BA 1 110 ? -69.272 20.683 44.273 1.0 49.37 ? ? ? ? ? ? 227 LEU BA CG 1 110 B B +ATOM 8835 C CD1 . LEU BA 1 110 ? -68.903 20.268 42.859 1.0 50.49 ? ? ? ? ? ? 227 LEU BA CD1 1 110 B B +ATOM 8836 C CD2 . LEU BA 1 110 ? -68.968 19.554 45.247 1.0 52.51 ? ? ? ? ? ? 227 LEU BA CD2 1 110 B B +ATOM 8837 N N . GLU BA 1 111 ? -67.763 24.573 46.260 1.0 37.21 ? ? ? ? ? ? 228 GLU BA N 1 111 B B +ATOM 8838 C CA . GLU BA 1 111 ? -66.914 25.752 46.391 1.0 44.29 ? ? ? ? ? ? 228 GLU BA CA 1 111 B B +ATOM 8839 C C . GLU BA 1 111 ? -66.111 25.685 47.686 1.0 59.82 ? ? ? ? ? ? 228 GLU BA C 1 111 B B +ATOM 8840 O O . GLU BA 1 111 ? -64.978 26.165 47.756 1.0 57.37 ? ? ? ? ? ? 228 GLU BA O 1 111 B B +ATOM 8841 C CB . GLU BA 1 111 ? -67.757 27.025 46.379 1.0 42.37 ? ? ? ? ? ? 228 GLU BA CB 1 111 B B +ATOM 8842 C CG . GLU BA 1 111 ? -67.268 28.092 45.410 1.0 58.34 ? ? ? ? ? ? 228 GLU BA CG 1 111 B B +ATOM 8843 C CD . GLU BA 1 111 ? -65.761 28.242 45.398 1.0 49.22 ? ? ? ? ? ? 228 GLU BA CD 1 111 B B +ATOM 8844 O OE1 . GLU BA 1 111 ? -65.094 27.474 44.676 1.0 76.04 ? ? ? ? ? ? 228 GLU BA OE1 1 111 B B +ATOM 8845 O OE2 . GLU BA 1 111 ? -65.241 29.130 46.104 1.0 42.09 ? ? ? ? ? ? 228 GLU BA OE2 1 111 B B +ATOM 8846 N N . ASP BA 1 112 ? -66.707 25.080 48.708 1.0 63.59 ? ? ? ? ? ? 229 ASP BA N 1 112 B B +ATOM 8847 C CA . ASP BA 1 112 ? -66.063 24.940 50.006 1.0 54.71 ? ? ? ? ? ? 229 ASP BA CA 1 112 B B +ATOM 8848 C C . ASP BA 1 112 ? -64.973 23.884 49.925 1.0 42.14 ? ? ? ? ? ? 229 ASP BA C 1 112 B B +ATOM 8849 O O . ASP BA 1 112 ? -63.817 24.140 50.257 1.0 47.78 ? ? ? ? ? ? 229 ASP BA O 1 112 B B +ATOM 8850 C CB . ASP BA 1 112 ? -67.097 24.541 51.058 1.0 56.3 ? ? ? ? ? ? 229 ASP BA CB 1 112 B B +ATOM 8851 C CG . ASP BA 1 112 ? -68.151 25.612 51.273 1.0 59.21 ? ? ? ? ? ? 229 ASP BA CG 1 112 B B +ATOM 8852 O OD1 . ASP BA 1 112 ? -67.834 26.803 51.072 1.0 47.22 ? ? ? ? ? ? 229 ASP BA OD1 1 112 B B +ATOM 8853 O OD2 . ASP BA 1 112 ? -69.292 25.264 51.642 1.0 48.29 ? ? ? ? ? ? 229 ASP BA OD2 1 112 B B +ATOM 8854 N N . VAL BA 1 113 ? -65.354 22.693 49.482 1.0 24.14 ? ? ? ? ? ? 230 VAL BA N 1 113 B B +ATOM 8855 C CA . VAL BA 1 113 ? -64.411 21.590 49.342 1.0 28.23 ? ? ? ? ? ? 230 VAL BA CA 1 113 B B +ATOM 8856 C C . VAL BA 1 113 ? -63.241 22.005 48.448 1.0 25.59 ? ? ? ? ? ? 230 VAL BA C 1 113 B B +ATOM 8857 O O . VAL BA 1 113 ? -62.078 21.802 48.795 1.0 24.96 ? ? ? ? ? ? 230 VAL BA O 1 113 B B +ATOM 8858 C CB . VAL BA 1 113 ? -65.090 20.353 48.726 1.0 19.93 ? ? ? ? ? ? 230 VAL BA CB 1 113 B B +ATOM 8859 C CG1 . VAL BA 1 113 ? -64.181 19.140 48.834 1.0 36.37 ? ? ? ? ? ? 230 VAL BA CG1 1 113 B B +ATOM 8860 C CG2 . VAL BA 1 113 ? -66.403 20.100 49.413 1.0 31.35 ? ? ? ? ? ? 230 VAL BA CG2 1 113 B B +ATOM 8861 N N . SER BA 1 114 ? -63.553 22.581 47.293 1.0 22.23 ? ? ? ? ? ? 231 SER BA N 1 114 B B +ATOM 8862 C CA . SER BA 1 114 ? -62.519 23.022 46.370 1.0 28.79 ? ? ? ? ? ? 231 SER BA CA 1 114 B B +ATOM 8863 C C . SER BA 1 114 ? -61.620 24.025 47.089 1.0 37.48 ? ? ? ? ? ? 231 SER BA C 1 114 B B +ATOM 8864 O O . SER BA 1 114 ? -60.409 23.832 47.182 1.0 45.95 ? ? ? ? ? ? 231 SER BA O 1 114 B B +ATOM 8865 C CB . SER BA 1 114 ? -63.154 23.669 45.136 1.0 36.95 ? ? ? ? ? ? 231 SER BA CB 1 114 B B +ATOM 8866 O OG . SER BA 1 114 ? -62.179 24.287 44.318 1.0 42.47 ? ? ? ? ? ? 231 SER BA OG 1 114 B B +ATOM 8867 N N . GLN BA 1 115 ? -62.229 25.093 47.601 1.0 41.53 ? ? ? ? ? ? 232 GLN BA N 1 115 B B +ATOM 8868 C CA . GLN BA 1 115 ? -61.484 26.119 48.318 1.0 36.18 ? ? ? ? ? ? 232 GLN BA CA 1 115 B B +ATOM 8869 C C . GLN BA 1 115 ? -60.608 25.505 49.403 1.0 48.1 ? ? ? ? ? ? 232 GLN BA C 1 115 B B +ATOM 8870 O O . GLN BA 1 115 ? -59.511 25.973 49.673 1.0 63.22 ? ? ? ? ? ? 232 GLN BA O 1 115 B B +ATOM 8871 C CB . GLN BA 1 115 ? -62.438 27.150 48.924 1.0 36.85 ? ? ? ? ? ? 232 GLN BA CB 1 115 B B +ATOM 8872 C CG . GLN BA 1 115 ? -61.923 28.580 48.872 1.0 54.29 ? ? ? ? ? ? 232 GLN BA CG 1 115 B B +ATOM 8873 C CD . GLN BA 1 115 ? -61.445 28.976 47.490 1.0 65.82 ? ? ? ? ? ? 232 GLN BA CD 1 115 B B +ATOM 8874 O OE1 . GLN BA 1 115 ? -60.256 29.213 47.277 1.0 83.67 ? ? ? ? ? ? 232 GLN BA OE1 1 115 B B +ATOM 8875 N NE2 . GLN BA 1 115 ? -62.198 29.111 46.403 1.0 20.0 ? ? ? ? ? ? 232 GLN BA NE2 1 115 B B +ATOM 8876 N N . PHE BA 1 116 ? -61.120 24.435 50.010 1.0 50.16 ? ? ? ? ? ? 233 PHE BA N 1 116 B B +ATOM 8877 C CA . PHE BA 1 116 ? -60.404 23.734 51.069 1.0 48.93 ? ? ? ? ? ? 233 PHE BA CA 1 116 B B +ATOM 8878 C C . PHE BA 1 116 ? -59.218 22.968 50.506 1.0 44.11 ? ? ? ? ? ? 233 PHE BA C 1 116 B B +ATOM 8879 O O . PHE BA 1 116 ? -58.067 23.253 50.833 1.0 40.81 ? ? ? ? ? ? 233 PHE BA O 1 116 B B +ATOM 8880 C CB . PHE BA 1 116 ? -61.340 22.760 51.786 1.0 58.23 ? ? ? ? ? ? 233 PHE BA CB 1 116 B B +ATOM 8881 C CG . PHE BA 1 116 ? -60.675 21.969 52.879 1.0 63.87 ? ? ? ? ? ? 233 PHE BA CG 1 116 B B +ATOM 8882 C CD1 . PHE BA 1 116 ? -59.760 22.569 53.739 1.0 57.86 ? ? ? ? ? ? 233 PHE BA CD1 1 116 B B +ATOM 8883 C CD2 . PHE BA 1 116 ? -60.973 20.622 53.053 1.0 69.54 ? ? ? ? ? ? 233 PHE BA CD2 1 116 B B +ATOM 8884 C CE1 . PHE BA 1 116 ? -59.147 21.836 54.755 1.0 55.36 ? ? ? ? ? ? 233 PHE BA CE1 1 116 B B +ATOM 8885 C CE2 . PHE BA 1 116 ? -60.367 19.880 54.065 1.0 66.99 ? ? ? ? ? ? 233 PHE BA CE2 1 116 B B +ATOM 8886 C CZ . PHE BA 1 116 ? -59.452 20.489 54.918 1.0 58.0 ? ? ? ? ? ? 233 PHE BA CZ 1 116 B B +ATOM 8887 N N . LEU BA 1 117 ? -59.518 21.987 49.663 1.0 45.08 ? ? ? ? ? ? 234 LEU BA N 1 117 B B +ATOM 8888 C CA . LEU BA 1 117 ? -58.498 21.157 49.030 1.0 51.99 ? ? ? ? ? ? 234 LEU BA CA 1 117 B B +ATOM 8889 C C . LEU BA 1 117 ? -57.339 21.990 48.491 1.0 54.51 ? ? ? ? ? ? 234 LEU BA C 1 117 B B +ATOM 8890 O O . LEU BA 1 117 ? -56.185 21.560 48.518 1.0 67.55 ? ? ? ? ? ? 234 LEU BA O 1 117 B B +ATOM 8891 C CB . LEU BA 1 117 ? -59.114 20.348 47.883 1.0 26.78 ? ? ? ? ? ? 234 LEU BA CB 1 117 B B +ATOM 8892 C CG . LEU BA 1 117 ? -59.847 19.062 48.272 1.0 47.52 ? ? ? ? ? ? 234 LEU BA CG 1 117 B B +ATOM 8893 C CD1 . LEU BA 1 117 ? -60.642 18.545 47.089 1.0 47.8 ? ? ? ? ? ? 234 LEU BA CD1 1 117 B B +ATOM 8894 C CD2 . LEU BA 1 117 ? -58.846 18.022 48.732 1.0 66.07 ? ? ? ? ? ? 234 LEU BA CD2 1 117 B B +ATOM 8895 N N . GLN BA 1 118 ? -57.648 23.183 48.004 1.0 37.39 ? ? ? ? ? ? 235 GLN BA N 1 118 B B +ATOM 8896 C CA . GLN BA 1 118 ? -56.625 24.051 47.451 1.0 39.18 ? ? ? ? ? ? 235 GLN BA CA 1 118 B B +ATOM 8897 C C . GLN BA 1 118 ? -55.552 24.430 48.464 1.0 49.42 ? ? ? ? ? ? 235 GLN BA C 1 118 B B +ATOM 8898 O O . GLN BA 1 118 ? -54.366 24.468 48.130 1.0 66.03 ? ? ? ? ? ? 235 GLN BA O 1 118 B B +ATOM 8899 C CB . GLN BA 1 118 ? -57.277 25.303 46.867 1.0 42.47 ? ? ? ? ? ? 235 GLN BA CB 1 118 B B +ATOM 8900 C CG . GLN BA 1 118 ? -58.099 25.016 45.629 1.0 41.61 ? ? ? ? ? ? 235 GLN BA CG 1 118 B B +ATOM 8901 C CD . GLN BA 1 118 ? -58.723 26.263 45.038 1.0 51.52 ? ? ? ? ? ? 235 GLN BA CD 1 118 B B +ATOM 8902 O OE1 . GLN BA 1 118 ? -58.031 27.237 44.749 1.0 50.65 ? ? ? ? ? ? 235 GLN BA OE1 1 118 B B +ATOM 8903 N NE2 . GLN BA 1 118 ? -60.039 26.239 44.855 1.0 69.18 ? ? ? ? ? ? 235 GLN BA NE2 1 118 B B +ATOM 8904 N N . THR BA 1 119 ? -55.960 24.706 49.699 1.0 55.42 ? ? ? ? ? ? 236 THR BA N 1 119 B B +ATOM 8905 C CA . THR BA 1 119 ? -55.007 25.084 50.743 1.0 57.64 ? ? ? ? ? ? 236 THR BA CA 1 119 B B +ATOM 8906 C C . THR BA 1 119 ? -54.208 23.892 51.258 1.0 42.79 ? ? ? ? ? ? 236 THR BA C 1 119 B B +ATOM 8907 O O . THR BA 1 119 ? -53.144 24.063 51.855 1.0 40.67 ? ? ? ? ? ? 236 THR BA O 1 119 B B +ATOM 8908 C CB . THR BA 1 119 ? -55.720 25.736 51.936 1.0 57.79 ? ? ? ? ? ? 236 THR BA CB 1 119 B B +ATOM 8909 O OG1 . THR BA 1 119 ? -56.881 24.966 52.270 1.0 54.71 ? ? ? ? ? ? 236 THR BA OG1 1 119 B B +ATOM 8910 C CG2 . THR BA 1 119 ? -56.127 27.158 51.593 1.0 55.37 ? ? ? ? ? ? 236 THR BA CG2 1 119 B B +ATOM 8911 N N . CYS BA 1 120 ? -54.724 22.687 51.025 1.0 24.06 ? ? ? ? ? ? 237 CYS BA N 1 120 B B +ATOM 8912 C CA . CYS BA 1 120 ? -54.047 21.469 51.463 1.0 50.52 ? ? ? ? ? ? 237 CYS BA CA 1 120 B B +ATOM 8913 C C . CYS BA 1 120 ? -52.959 21.043 50.481 1.0 60.62 ? ? ? ? ? ? 237 CYS BA C 1 120 B B +ATOM 8914 O O . CYS BA 1 120 ? -51.795 20.873 50.857 1.0 60.8 ? ? ? ? ? ? 237 CYS BA O 1 120 B B +ATOM 8915 C CB . CYS BA 1 120 ? -55.045 20.319 51.614 1.0 39.35 ? ? ? ? ? ? 237 CYS BA CB 1 120 B B +ATOM 8916 S SG . CYS BA 1 120 ? -56.491 20.717 52.599 1.0 63.59 ? ? ? ? ? ? 237 CYS BA SG 1 120 B B +ATOM 8917 N N . THR BA 1 121 ? -53.343 20.881 49.217 1.0 56.56 ? ? ? ? ? ? 238 THR BA N 1 121 B B +ATOM 8918 C CA . THR BA 1 121 ? -52.407 20.452 48.185 1.0 48.5 ? ? ? ? ? ? 238 THR BA CA 1 121 B B +ATOM 8919 C C . THR BA 1 121 ? -52.406 21.370 46.965 1.0 51.09 ? ? ? ? ? ? 238 THR BA C 1 121 B B +ATOM 8920 O O . THR BA 1 121 ? -51.426 21.431 46.221 1.0 66.44 ? ? ? ? ? ? 238 THR BA O 1 121 B B +ATOM 8921 C CB . THR BA 1 121 ? -52.737 19.024 47.728 1.0 48.09 ? ? ? ? ? ? 238 THR BA CB 1 121 B B +ATOM 8922 O OG1 . THR BA 1 121 ? -54.064 18.992 47.196 1.0 63.68 ? ? ? ? ? ? 238 THR BA OG1 1 121 B B +ATOM 8923 C CG2 . THR BA 1 121 ? -52.658 18.062 48.903 1.0 54.75 ? ? ? ? ? ? 238 THR BA CG2 1 121 B B +ATOM 8924 N N . GLY BA 1 122 ? -53.501 22.092 46.771 1.0 45.86 ? ? ? ? ? ? 239 GLY BA N 1 122 B B +ATOM 8925 C CA . GLY BA 1 122 ? -53.590 22.982 45.630 1.0 37.78 ? ? ? ? ? ? 239 GLY BA CA 1 122 B B +ATOM 8926 C C . GLY BA 1 122 ? -54.605 22.471 44.630 1.0 36.96 ? ? ? ? ? ? 239 GLY BA C 1 122 B B +ATOM 8927 O O . GLY BA 1 122 ? -54.855 23.102 43.606 1.0 40.13 ? ? ? ? ? ? 239 GLY BA O 1 122 B B +ATOM 8928 N N . PHE BA 1 123 ? -55.191 21.319 44.936 1.0 37.98 ? ? ? ? ? ? 240 PHE BA N 1 123 B B +ATOM 8929 C CA . PHE BA 1 123 ? -56.190 20.705 44.074 1.0 39.99 ? ? ? ? ? ? 240 PHE BA CA 1 123 B B +ATOM 8930 C C . PHE BA 1 123 ? -57.495 21.483 44.124 1.0 51.84 ? ? ? ? ? ? 240 PHE BA C 1 123 B B +ATOM 8931 O O . PHE BA 1 123 ? -58.070 21.684 45.197 1.0 61.74 ? ? ? ? ? ? 240 PHE BA O 1 123 B B +ATOM 8932 C CB . PHE BA 1 123 ? -56.448 19.263 44.506 1.0 38.03 ? ? ? ? ? ? 240 PHE BA CB 1 123 B B +ATOM 8933 C CG . PHE BA 1 123 ? -55.943 18.242 43.535 1.0 45.56 ? ? ? ? ? ? 240 PHE BA CG 1 123 B B +ATOM 8934 C CD1 . PHE BA 1 123 ? -54.611 17.853 43.550 1.0 44.86 ? ? ? ? ? ? 240 PHE BA CD1 1 123 B B +ATOM 8935 C CD2 . PHE BA 1 123 ? -56.794 17.675 42.597 1.0 59.18 ? ? ? ? ? ? 240 PHE BA CD2 1 123 B B +ATOM 8936 C CE1 . PHE BA 1 123 ? -54.136 16.915 42.646 1.0 59.62 ? ? ? ? ? ? 240 PHE BA CE1 1 123 B B +ATOM 8937 C CE2 . PHE BA 1 123 ? -56.325 16.736 41.688 1.0 63.73 ? ? ? ? ? ? 240 PHE BA CE2 1 123 B B +ATOM 8938 C CZ . PHE BA 1 123 ? -54.994 16.355 41.712 1.0 53.74 ? ? ? ? ? ? 240 PHE BA CZ 1 123 B B +ATOM 8939 N N . ARG BA 1 124 ? -57.958 21.920 42.958 1.0 48.36 ? ? ? ? ? ? 241 ARG BA N 1 124 B B +ATOM 8940 C CA . ARG BA 1 124 ? -59.203 22.662 42.874 1.0 38.46 ? ? ? ? ? ? 241 ARG BA CA 1 124 B B +ATOM 8941 C C . ARG BA 1 124 ? -60.225 21.761 42.223 1.0 30.49 ? ? ? ? ? ? 241 ARG BA C 1 124 B B +ATOM 8942 O O . ARG BA 1 124 ? -59.876 20.913 41.411 1.0 40.37 ? ? ? ? ? ? 241 ARG BA O 1 124 B B +ATOM 8943 C CB . ARG BA 1 124 ? -59.020 23.920 42.034 1.0 27.27 ? ? ? ? ? ? 241 ARG BA CB 1 124 B B +ATOM 8944 C CG . ARG BA 1 124 ? -57.937 23.805 40.987 1.0 42.48 ? ? ? ? ? ? 241 ARG BA CG 1 124 B B +ATOM 8945 C CD . ARG BA 1 124 ? -57.579 25.170 40.461 1.0 38.82 ? ? ? ? ? ? 241 ARG BA CD 1 124 B B +ATOM 8946 N NE . ARG BA 1 124 ? -56.973 25.995 41.498 1.0 53.54 ? ? ? ? ? ? 241 ARG BA NE 1 124 B B +ATOM 8947 C CZ . ARG BA 1 124 ? -56.496 27.215 41.285 1.0 67.48 ? ? ? ? ? ? 241 ARG BA CZ 1 124 B B +ATOM 8948 N NH1 . ARG BA 1 124 ? -56.560 27.742 40.071 1.0 50.15 ? ? ? ? ? ? 241 ARG BA NH1 1 124 B B +ATOM 8949 N NH2 . ARG BA 1 124 ? -55.947 27.905 42.279 1.0 83.13 ? ? ? ? ? ? 241 ARG BA NH2 1 124 B B +ATOM 8950 N N . LEU BA 1 125 ? -61.487 21.937 42.583 1.0 31.8 ? ? ? ? ? ? 242 LEU BA N 1 125 B B +ATOM 8951 C CA . LEU BA 1 125 ? -62.535 21.122 42.001 1.0 30.17 ? ? ? ? ? ? 242 LEU BA CA 1 125 B B +ATOM 8952 C C . LEU BA 1 125 ? -63.124 21.827 40.788 1.0 43.05 ? ? ? ? ? ? 242 LEU BA C 1 125 B B +ATOM 8953 O O . LEU BA 1 125 ? -63.026 23.046 40.658 1.0 25.42 ? ? ? ? ? ? 242 LEU BA O 1 125 B B +ATOM 8954 C CB . LEU BA 1 125 ? -63.631 20.862 43.033 1.0 29.3 ? ? ? ? ? ? 242 LEU BA CB 1 125 B B +ATOM 8955 C CG . LEU BA 1 125 ? -63.315 19.819 44.109 1.0 49.41 ? ? ? ? ? ? 242 LEU BA CG 1 125 B B +ATOM 8956 C CD1 . LEU BA 1 125 ? -64.511 19.673 45.039 1.0 57.07 ? ? ? ? ? ? 242 LEU BA CD1 1 125 B B +ATOM 8957 C CD2 . LEU BA 1 125 ? -62.983 18.479 43.465 1.0 25.53 ? ? ? ? ? ? 242 LEU BA CD2 1 125 B B +ATOM 8958 N N . ARG BA 1 126 ? -63.708 21.043 39.889 1.0 51.99 ? ? ? ? ? ? 243 ARG BA N 1 126 B B +ATOM 8959 C CA . ARG BA 1 126 ? -64.346 21.572 38.689 1.0 51.87 ? ? ? ? ? ? 243 ARG BA CA 1 126 B B +ATOM 8960 C C . ARG BA 1 126 ? -65.572 20.722 38.387 1.0 58.5 ? ? ? ? ? ? 243 ARG BA C 1 126 B B +ATOM 8961 O O . ARG BA 1 126 ? -65.465 19.515 38.172 1.0 66.87 ? ? ? ? ? ? 243 ARG BA O 1 126 B B +ATOM 8962 C CB . ARG BA 1 126 ? -63.397 21.544 37.489 1.0 49.19 ? ? ? ? ? ? 243 ARG BA CB 1 126 B B +ATOM 8963 C CG . ARG BA 1 126 ? -63.859 22.451 36.364 1.0 47.76 ? ? ? ? ? ? 243 ARG BA CG 1 126 B B +ATOM 8964 C CD . ARG BA 1 126 ? -63.086 22.232 35.079 1.0 53.15 ? ? ? ? ? ? 243 ARG BA CD 1 126 B B +ATOM 8965 N NE . ARG BA 1 126 ? -63.732 22.920 33.965 1.0 66.41 ? ? ? ? ? ? 243 ARG BA NE 1 126 B B +ATOM 8966 C CZ . ARG BA 1 126 ? -63.303 24.061 33.437 1.0 58.98 ? ? ? ? ? ? 243 ARG BA CZ 1 126 B B +ATOM 8967 N NH1 . ARG BA 1 126 ? -62.220 24.656 33.922 1.0 72.19 ? ? ? ? ? ? 243 ARG BA NH1 1 126 B B +ATOM 8968 N NH2 . ARG BA 1 126 ? -63.960 24.618 32.430 1.0 47.51 ? ? ? ? ? ? 243 ARG BA NH2 1 126 B B +ATOM 8969 N N . PRO BA 1 127 ? -66.759 21.350 38.363 1.0 56.82 ? ? ? ? ? ? 244 PRO BA N 1 127 B B +ATOM 8970 C CA . PRO BA 1 127 ? -68.000 20.617 38.086 1.0 41.81 ? ? ? ? ? ? 244 PRO BA CA 1 127 B B +ATOM 8971 C C . PRO BA 1 127 ? -68.085 20.103 36.652 1.0 45.42 ? ? ? ? ? ? 244 PRO BA C 1 127 B B +ATOM 8972 O O . PRO BA 1 127 ? -68.117 20.880 35.701 1.0 45.79 ? ? ? ? ? ? 244 PRO BA O 1 127 B B +ATOM 8973 C CB . PRO BA 1 127 ? -69.094 21.636 38.407 1.0 22.99 ? ? ? ? ? ? 244 PRO BA CB 1 127 B B +ATOM 8974 C CG . PRO BA 1 127 ? -68.440 22.959 38.212 1.0 23.84 ? ? ? ? ? ? 244 PRO BA CG 1 127 B B +ATOM 8975 C CD . PRO BA 1 127 ? -66.998 22.787 38.585 1.0 33.55 ? ? ? ? ? ? 244 PRO BA CD 1 127 B B +ATOM 8976 N N . VAL BA 1 128 ? -68.120 18.782 36.505 1.0 46.64 ? ? ? ? ? ? 245 VAL BA N 1 128 B B +ATOM 8977 C CA . VAL BA 1 128 ? -68.207 18.160 35.189 1.0 57.89 ? ? ? ? ? ? 245 VAL BA CA 1 128 B B +ATOM 8978 C C . VAL BA 1 128 ? -69.658 17.794 34.903 1.0 73.52 ? ? ? ? ? ? 245 VAL BA C 1 128 B B +ATOM 8979 O O . VAL BA 1 128 ? -70.371 17.328 35.794 1.0 78.88 ? ? ? ? ? ? 245 VAL BA O 1 128 B B +ATOM 8980 C CB . VAL BA 1 128 ? -67.338 16.878 35.115 1.0 58.34 ? ? ? ? ? ? 245 VAL BA CB 1 128 B B +ATOM 8981 C CG1 . VAL BA 1 128 ? -68.005 15.742 35.874 1.0 67.35 ? ? ? ? ? ? 245 VAL BA CG1 1 128 B B +ATOM 8982 C CG2 . VAL BA 1 128 ? -67.108 16.488 33.665 1.0 52.31 ? ? ? ? ? ? 245 VAL BA CG2 1 128 B B +ATOM 8983 N N . ALA BA 1 129 ? -70.092 18.005 33.663 1.0 85.17 ? ? ? ? ? ? 246 ALA BA N 1 129 B B +ATOM 8984 C CA . ALA BA 1 129 ? -71.463 17.688 33.268 1.0 80.94 ? ? ? ? ? ? 246 ALA BA CA 1 129 B B +ATOM 8985 C C . ALA BA 1 129 ? -71.863 16.301 33.777 1.0 78.81 ? ? ? ? ? ? 246 ALA BA C 1 129 B B +ATOM 8986 O O . ALA BA 1 129 ? -72.748 16.169 34.627 1.0 72.96 ? ? ? ? ? ? 246 ALA BA O 1 129 B B +ATOM 8987 C CB . ALA BA 1 129 ? -71.593 17.747 31.749 1.0 83.46 ? ? ? ? ? ? 246 ALA BA CB 1 129 B B +ATOM 8988 N N . GLY BA 1 130 ? -71.205 15.271 33.253 1.0 73.3 ? ? ? ? ? ? 247 GLY BA N 1 130 B B +ATOM 8989 C CA . GLY BA 1 130 ? -71.496 13.912 33.668 1.0 72.06 ? ? ? ? ? ? 247 GLY BA CA 1 130 B B +ATOM 8990 C C . GLY BA 1 130 ? -70.237 13.070 33.683 1.0 70.96 ? ? ? ? ? ? 247 GLY BA C 1 130 B B +ATOM 8991 O O . GLY BA 1 130 ? -69.712 12.741 34.744 1.0 65.1 ? ? ? ? ? ? 247 GLY BA O 1 130 B B +ATOM 8992 N N . LEU BA 1 131 ? -69.752 12.724 32.495 1.0 82.56 ? ? ? ? ? ? 248 LEU BA N 1 131 B B +ATOM 8993 C CA . LEU BA 1 131 ? -68.549 11.909 32.356 1.0 87.46 ? ? ? ? ? ? 248 LEU BA CA 1 131 B B +ATOM 8994 C C . LEU BA 1 131 ? -67.689 12.451 31.220 1.0 80.78 ? ? ? ? ? ? 248 LEU BA C 1 131 B B +ATOM 8995 O O . LEU BA 1 131 ? -68.149 13.264 30.421 1.0 85.05 ? ? ? ? ? ? 248 LEU BA O 1 131 B B +ATOM 8996 C CB . LEU BA 1 131 ? -68.932 10.451 32.064 1.0 91.7 ? ? ? ? ? ? 248 LEU BA CB 1 131 B B +ATOM 8997 C CG . LEU BA 1 131 ? -69.280 10.084 30.616 1.0 100.0 ? ? ? ? ? ? 248 LEU BA CG 1 131 B B +ATOM 8998 C CD1 . LEU BA 1 131 ? -69.360 8.573 30.480 1.0 95.76 ? ? ? ? ? ? 248 LEU BA CD1 1 131 B B +ATOM 8999 C CD2 . LEU BA 1 131 ? -70.594 10.736 30.219 1.0 100.0 ? ? ? ? ? ? 248 LEU BA CD2 1 131 B B +ATOM 9000 N N . LEU BA 1 132 ? -66.439 12.005 31.158 1.0 67.02 ? ? ? ? ? ? 249 LEU BA N 1 132 B B +ATOM 9001 C CA . LEU BA 1 132 ? -65.529 12.436 30.105 1.0 63.13 ? ? ? ? ? ? 249 LEU BA CA 1 132 B B +ATOM 9002 C C . LEU BA 1 132 ? -64.422 11.420 29.864 1.0 65.19 ? ? ? ? ? ? 249 LEU BA C 1 132 B B +ATOM 9003 O O . LEU BA 1 132 ? -64.146 10.571 30.707 1.0 49.32 ? ? ? ? ? ? 249 LEU BA O 1 132 B B +ATOM 9004 C CB . LEU BA 1 132 ? -64.916 13.798 30.434 1.0 59.4 ? ? ? ? ? ? 249 LEU BA CB 1 132 B B +ATOM 9005 C CG . LEU BA 1 132 ? -64.828 14.270 31.883 1.0 57.14 ? ? ? ? ? ? 249 LEU BA CG 1 132 B B +ATOM 9006 C CD1 . LEU BA 1 132 ? -64.072 13.260 32.724 1.0 59.86 ? ? ? ? ? ? 249 LEU BA CD1 1 132 B B +ATOM 9007 C CD2 . LEU BA 1 132 ? -64.138 15.622 31.907 1.0 68.38 ? ? ? ? ? ? 249 LEU BA CD2 1 132 B B +ATOM 9008 N N . SER BA 1 133 ? -63.798 11.512 28.696 1.0 64.35 ? ? ? ? ? ? 250 SER BA N 1 133 B B +ATOM 9009 C CA . SER BA 1 133 ? -62.727 10.602 28.315 1.0 62.49 ? ? ? ? ? ? 250 SER BA CA 1 133 B B +ATOM 9010 C C . SER BA 1 133 ? -61.636 10.504 29.375 1.0 70.64 ? ? ? ? ? ? 250 SER BA C 1 133 B B +ATOM 9011 O O . SER BA 1 133 ? -61.464 11.417 30.182 1.0 78.71 ? ? ? ? ? ? 250 SER BA O 1 133 B B +ATOM 9012 C CB . SER BA 1 133 ? -62.112 11.061 26.996 1.0 45.86 ? ? ? ? ? ? 250 SER BA CB 1 133 B B +ATOM 9013 O OG . SER BA 1 133 ? -60.931 10.340 26.710 1.0 69.61 ? ? ? ? ? ? 250 SER BA OG 1 133 B B +ATOM 9014 N N . SER BA 1 134 ? -60.906 9.391 29.372 1.0 81.86 ? ? ? ? ? ? 251 SER BA N 1 134 B B +ATOM 9015 C CA . SER BA 1 134 ? -59.821 9.192 30.326 1.0 82.78 ? ? ? ? ? ? 251 SER BA CA 1 134 B B +ATOM 9016 C C . SER BA 1 134 ? -58.749 10.232 30.045 1.0 77.72 ? ? ? ? ? ? 251 SER BA C 1 134 B B +ATOM 9017 O O . SER BA 1 134 ? -58.108 10.752 30.961 1.0 65.78 ? ? ? ? ? ? 251 SER BA O 1 134 B B +ATOM 9018 C CB . SER BA 1 134 ? -59.214 7.796 30.175 1.0 73.43 ? ? ? ? ? ? 251 SER BA CB 1 134 B B +ATOM 9019 O OG . SER BA 1 134 ? -60.219 6.826 29.951 1.0 90.84 ? ? ? ? ? ? 251 SER BA OG 1 134 B B +ATOM 9020 N N . ARG BA 1 135 ? -58.559 10.525 28.762 1.0 62.78 ? ? ? ? ? ? 252 ARG BA N 1 135 B B +ATOM 9021 C CA . ARG BA 1 135 ? -57.573 11.505 28.344 1.0 58.79 ? ? ? ? ? ? 252 ARG BA CA 1 135 B B +ATOM 9022 C C . ARG BA 1 135 ? -57.926 12.874 28.914 1.0 63.08 ? ? ? ? ? ? 252 ARG BA C 1 135 B B +ATOM 9023 O O . ARG BA 1 135 ? -57.052 13.614 29.358 1.0 78.89 ? ? ? ? ? ? 252 ARG BA O 1 135 B B +ATOM 9024 C CB . ARG BA 1 135 ? -57.518 11.575 26.819 1.0 60.93 ? ? ? ? ? ? 252 ARG BA CB 1 135 B B +ATOM 9025 C CG . ARG BA 1 135 ? -56.578 12.643 26.281 1.0 79.31 ? ? ? ? ? ? 252 ARG BA CG 1 135 B B +ATOM 9026 C CD . ARG BA 1 135 ? -56.599 12.666 24.766 1.0 94.81 ? ? ? ? ? ? 252 ARG BA CD 1 135 B B +ATOM 9027 N NE . ARG BA 1 135 ? -56.207 11.379 24.199 1.0 99.4 ? ? ? ? ? ? 252 ARG BA NE 1 135 B B +ATOM 9028 C CZ . ARG BA 1 135 ? -54.963 10.909 24.203 1.0 85.17 ? ? ? ? ? ? 252 ARG BA CZ 1 135 B B +ATOM 9029 N NH1 . ARG BA 1 135 ? -53.987 11.622 24.747 1.0 76.66 ? ? ? ? ? ? 252 ARG BA NH1 1 135 B B +ATOM 9030 N NH2 . ARG BA 1 135 ? -54.696 9.731 23.656 1.0 73.12 ? ? ? ? ? ? 252 ARG BA NH2 1 135 B B +ATOM 9031 N N . ASP BA 1 136 ? -59.215 13.202 28.900 1.0 62.76 ? ? ? ? ? ? 253 ASP BA N 1 136 B B +ATOM 9032 C CA . ASP BA 1 136 ? -59.689 14.489 29.407 1.0 57.99 ? ? ? ? ? ? 253 ASP BA CA 1 136 B B +ATOM 9033 C C . ASP BA 1 136 ? -59.647 14.537 30.925 1.0 60.84 ? ? ? ? ? ? 253 ASP BA C 1 136 B B +ATOM 9034 O O . ASP BA 1 136 ? -59.221 15.532 31.516 1.0 47.13 ? ? ? ? ? ? 253 ASP BA O 1 136 B B +ATOM 9035 C CB . ASP BA 1 136 ? -61.117 14.742 28.937 1.0 62.86 ? ? ? ? ? ? 253 ASP BA CB 1 136 B B +ATOM 9036 C CG . ASP BA 1 136 ? -61.226 14.813 27.438 1.0 82.05 ? ? ? ? ? ? 253 ASP BA CG 1 136 B B +ATOM 9037 O OD1 . ASP BA 1 136 ? -61.218 13.740 26.795 1.0 84.11 ? ? ? ? ? ? 253 ASP BA OD1 1 136 B B +ATOM 9038 O OD2 . ASP BA 1 136 ? -61.316 15.941 26.905 1.0 82.41 ? ? ? ? ? ? 253 ASP BA OD2 1 136 B B +ATOM 9039 N N . PHE BA 1 137 ? -60.107 13.463 31.553 1.0 71.62 ? ? ? ? ? ? 254 PHE BA N 1 137 B B +ATOM 9040 C CA . PHE BA 1 137 ? -60.111 13.375 33.005 1.0 81.25 ? ? ? ? ? ? 254 PHE BA CA 1 137 B B +ATOM 9041 C C . PHE BA 1 137 ? -58.676 13.534 33.500 1.0 77.02 ? ? ? ? ? ? 254 PHE BA C 1 137 B B +ATOM 9042 O O . PHE BA 1 137 ? -58.362 14.460 34.252 1.0 80.3 ? ? ? ? ? ? 254 PHE BA O 1 137 B B +ATOM 9043 C CB . PHE BA 1 137 ? -60.671 12.017 33.441 1.0 85.08 ? ? ? ? ? ? 254 PHE BA CB 1 137 B B +ATOM 9044 C CG . PHE BA 1 137 ? -61.049 11.945 34.895 1.0 92.74 ? ? ? ? ? ? 254 PHE BA CG 1 137 B B +ATOM 9045 C CD1 . PHE BA 1 137 ? -60.854 13.032 35.743 1.0 100.0 ? ? ? ? ? ? 254 PHE BA CD1 1 137 B B +ATOM 9046 C CD2 . PHE BA 1 137 ? -61.607 10.780 35.415 1.0 100.0 ? ? ? ? ? ? 254 PHE BA CD2 1 137 B B +ATOM 9047 C CE1 . PHE BA 1 137 ? -61.206 12.957 37.088 1.0 100.0 ? ? ? ? ? ? 254 PHE BA CE1 1 137 B B +ATOM 9048 C CE2 . PHE BA 1 137 ? -61.962 10.696 36.760 1.0 100.0 ? ? ? ? ? ? 254 PHE BA CE2 1 137 B B +ATOM 9049 C CZ . PHE BA 1 137 ? -61.762 11.785 37.596 1.0 100.0 ? ? ? ? ? ? 254 PHE BA CZ 1 137 B B +ATOM 9050 N N . LEU BA 1 138 ? -57.812 12.623 33.064 1.0 65.08 ? ? ? ? ? ? 255 LEU BA N 1 138 B B +ATOM 9051 C CA . LEU BA 1 138 ? -56.407 12.640 33.448 1.0 52.4 ? ? ? ? ? ? 255 LEU BA CA 1 138 B B +ATOM 9052 C C . LEU BA 1 138 ? -55.751 13.986 33.150 1.0 49.55 ? ? ? ? ? ? 255 LEU BA C 1 138 B B +ATOM 9053 O O . LEU BA 1 138 ? -54.923 14.468 33.920 1.0 58.75 ? ? ? ? ? ? 255 LEU BA O 1 138 B B +ATOM 9054 C CB . LEU BA 1 138 ? -55.658 11.520 32.721 1.0 42.75 ? ? ? ? ? ? 255 LEU BA CB 1 138 B B +ATOM 9055 C CG . LEU BA 1 138 ? -55.711 10.135 33.378 1.0 49.61 ? ? ? ? ? ? 255 LEU BA CG 1 138 B B +ATOM 9056 C CD1 . LEU BA 1 138 ? -57.009 9.960 34.147 1.0 39.36 ? ? ? ? ? ? 255 LEU BA CD1 1 138 B B +ATOM 9057 C CD2 . LEU BA 1 138 ? -55.569 9.068 32.308 1.0 52.31 ? ? ? ? ? ? 255 LEU BA CD2 1 138 B B +ATOM 9058 N N . GLY BA 1 139 ? -56.124 14.593 32.029 1.0 48.37 ? ? ? ? ? ? 256 GLY BA N 1 139 B B +ATOM 9059 C CA . GLY BA 1 139 ? -55.550 15.878 31.670 1.0 51.48 ? ? ? ? ? ? 256 GLY BA CA 1 139 B B +ATOM 9060 C C . GLY BA 1 139 ? -55.776 16.935 32.738 1.0 56.98 ? ? ? ? ? ? 256 GLY BA C 1 139 B B +ATOM 9061 O O . GLY BA 1 139 ? -54.956 17.837 32.919 1.0 43.96 ? ? ? ? ? ? 256 GLY BA O 1 139 B B +ATOM 9062 N N . GLY BA 1 140 ? -56.894 16.831 33.448 1.0 63.18 ? ? ? ? ? ? 257 GLY BA N 1 140 B B +ATOM 9063 C CA . GLY BA 1 140 ? -57.185 17.795 34.490 1.0 66.05 ? ? ? ? ? ? 257 GLY BA CA 1 140 B B +ATOM 9064 C C . GLY BA 1 140 ? -56.218 17.637 35.645 1.0 56.41 ? ? ? ? ? ? 257 GLY BA C 1 140 B B +ATOM 9065 O O . GLY BA 1 140 ? -55.801 18.616 36.258 1.0 59.16 ? ? ? ? ? ? 257 GLY BA O 1 140 B B +ATOM 9066 N N . LEU BA 1 141 ? -55.855 16.392 35.933 1.0 37.56 ? ? ? ? ? ? 258 LEU BA N 1 141 B B +ATOM 9067 C CA . LEU BA 1 141 ? -54.943 16.078 37.027 1.0 32.65 ? ? ? ? ? ? 258 LEU BA CA 1 141 B B +ATOM 9068 C C . LEU BA 1 141 ? -53.590 16.766 36.873 1.0 32.75 ? ? ? ? ? ? 258 LEU BA C 1 141 B B +ATOM 9069 O O . LEU BA 1 141 ? -52.931 17.081 37.863 1.0 42.08 ? ? ? ? ? ? 258 LEU BA O 1 141 B B +ATOM 9070 C CB . LEU BA 1 141 ? -54.755 14.558 37.129 1.0 17.19 ? ? ? ? ? ? 258 LEU BA CB 1 141 B B +ATOM 9071 C CG . LEU BA 1 141 ? -56.042 13.738 37.264 1.0 48.83 ? ? ? ? ? ? 258 LEU BA CG 1 141 B B +ATOM 9072 C CD1 . LEU BA 1 141 ? -55.749 12.264 36.996 1.0 28.3 ? ? ? ? ? ? 258 LEU BA CD1 1 141 B B +ATOM 9073 C CD2 . LEU BA 1 141 ? -56.631 13.944 38.653 1.0 48.32 ? ? ? ? ? ? 258 LEU BA CD2 1 141 B B +ATOM 9074 N N . ALA BA 1 142 ? -53.180 16.997 35.630 1.0 32.23 ? ? ? ? ? ? 259 ALA BA N 1 142 B B +ATOM 9075 C CA . ALA BA 1 142 ? -51.903 17.645 35.342 1.0 28.79 ? ? ? ? ? ? 259 ALA BA CA 1 142 B B +ATOM 9076 C C . ALA BA 1 142 ? -51.860 19.050 35.914 1.0 30.15 ? ? ? ? ? ? 259 ALA BA C 1 142 B B +ATOM 9077 O O . ALA BA 1 142 ? -50.786 19.632 36.063 1.0 34.54 ? ? ? ? ? ? 259 ALA BA O 1 142 B B +ATOM 9078 C CB . ALA BA 1 142 ? -51.671 17.699 33.840 1.0 38.29 ? ? ? ? ? ? 259 ALA BA CB 1 142 B B +ATOM 9079 N N . PHE BA 1 143 ? -53.034 19.600 36.219 1.0 38.35 ? ? ? ? ? ? 260 PHE BA N 1 143 B B +ATOM 9080 C CA . PHE BA 1 143 ? -53.137 20.947 36.776 1.0 28.17 ? ? ? ? ? ? 260 PHE BA CA 1 143 B B +ATOM 9081 C C . PHE BA 1 143 ? -53.668 20.884 38.190 1.0 32.46 ? ? ? ? ? ? 260 PHE BA C 1 143 B B +ATOM 9082 O O . PHE BA 1 143 ? -54.014 21.911 38.775 1.0 29.36 ? ? ? ? ? ? 260 PHE BA O 1 143 B B +ATOM 9083 C CB . PHE BA 1 143 ? -54.074 21.807 35.932 1.0 23.46 ? ? ? ? ? ? 260 PHE BA CB 1 143 B B +ATOM 9084 C CG . PHE BA 1 143 ? -53.735 21.816 34.479 1.0 23.16 ? ? ? ? ? ? 260 PHE BA CG 1 143 B B +ATOM 9085 C CD1 . PHE BA 1 143 ? -54.069 20.740 33.669 1.0 21.32 ? ? ? ? ? ? 260 PHE BA CD1 1 143 B B +ATOM 9086 C CD2 . PHE BA 1 143 ? -53.065 22.897 33.917 1.0 30.85 ? ? ? ? ? ? 260 PHE BA CD2 1 143 B B +ATOM 9087 C CE1 . PHE BA 1 143 ? -53.738 20.742 32.316 1.0 42.56 ? ? ? ? ? ? 260 PHE BA CE1 1 143 B B +ATOM 9088 C CE2 . PHE BA 1 143 ? -52.728 22.909 32.564 1.0 18.09 ? ? ? ? ? ? 260 PHE BA CE2 1 143 B B +ATOM 9089 C CZ . PHE BA 1 143 ? -53.065 21.833 31.763 1.0 14.9 ? ? ? ? ? ? 260 PHE BA CZ 1 143 B B +ATOM 9090 N N . ARG BA 1 144 ? -53.733 19.670 38.732 1.0 43.21 ? ? ? ? ? ? 261 ARG BA N 1 144 B B +ATOM 9091 C CA . ARG BA 1 144 ? -54.238 19.452 40.080 1.0 52.93 ? ? ? ? ? ? 261 ARG BA CA 1 144 B B +ATOM 9092 C C . ARG BA 1 144 ? -55.688 19.928 40.126 1.0 61.31 ? ? ? ? ? ? 261 ARG BA C 1 144 B B +ATOM 9093 O O . ARG BA 1 144 ? -56.129 20.564 41.089 1.0 65.05 ? ? ? ? ? ? 261 ARG BA O 1 144 B B +ATOM 9094 C CB . ARG BA 1 144 ? -53.388 20.214 41.098 1.0 58.77 ? ? ? ? ? ? 261 ARG BA CB 1 144 B B +ATOM 9095 C CG . ARG BA 1 144 ? -51.965 19.704 41.188 1.0 65.11 ? ? ? ? ? ? 261 ARG BA CG 1 144 B B +ATOM 9096 C CD . ARG BA 1 144 ? -51.388 19.861 42.581 1.0 72.9 ? ? ? ? ? ? 261 ARG BA CD 1 144 B B +ATOM 9097 N NE . ARG BA 1 144 ? -49.985 19.464 42.599 1.0 66.8 ? ? ? ? ? ? 261 ARG BA NE 1 144 B B +ATOM 9098 C CZ . ARG BA 1 144 ? -49.306 19.139 43.691 1.0 62.18 ? ? ? ? ? ? 261 ARG BA CZ 1 144 B B +ATOM 9099 N NH1 . ARG BA 1 144 ? -49.899 19.149 44.876 1.0 64.89 ? ? ? ? ? ? 261 ARG BA NH1 1 144 B B +ATOM 9100 N NH2 . ARG BA 1 144 ? -48.033 18.783 43.592 1.0 78.44 ? ? ? ? ? ? 261 ARG BA NH2 1 144 B B +ATOM 9101 N N . VAL BA 1 145 ? -56.409 19.614 39.052 1.0 47.17 ? ? ? ? ? ? 262 VAL BA N 1 145 B B +ATOM 9102 C CA . VAL BA 1 145 ? -57.816 19.962 38.911 1.0 38.17 ? ? ? ? ? ? 262 VAL BA CA 1 145 B B +ATOM 9103 C C . VAL BA 1 145 ? -58.635 18.670 38.825 1.0 38.46 ? ? ? ? ? ? 262 VAL BA C 1 145 B B +ATOM 9104 O O . VAL BA 1 145 ? -58.363 17.808 37.985 1.0 35.95 ? ? ? ? ? ? 262 VAL BA O 1 145 B B +ATOM 9105 C CB . VAL BA 1 145 ? -58.058 20.797 37.633 1.0 16.94 ? ? ? ? ? ? 262 VAL BA CB 1 145 B B +ATOM 9106 C CG1 . VAL BA 1 145 ? -59.544 20.894 37.348 1.0 15.75 ? ? ? ? ? ? 262 VAL BA CG1 1 145 B B +ATOM 9107 C CG2 . VAL BA 1 145 ? -57.461 22.190 37.800 1.0 13.76 ? ? ? ? ? ? 262 VAL BA CG2 1 145 B B +ATOM 9108 N N . PHE BA 1 146 ? -59.629 18.539 39.697 1.0 44.65 ? ? ? ? ? ? 263 PHE BA N 1 146 B B +ATOM 9109 C CA . PHE BA 1 146 ? -60.473 17.353 39.711 1.0 56.23 ? ? ? ? ? ? 263 PHE BA CA 1 146 B B +ATOM 9110 C C . PHE BA 1 146 ? -61.861 17.652 39.157 1.0 64.47 ? ? ? ? ? ? 263 PHE BA C 1 146 B B +ATOM 9111 O O . PHE BA 1 146 ? -62.539 18.571 39.616 1.0 75.1 ? ? ? ? ? ? 263 PHE BA O 1 146 B B +ATOM 9112 C CB . PHE BA 1 146 ? -60.602 16.815 41.137 1.0 45.33 ? ? ? ? ? ? 263 PHE BA CB 1 146 B B +ATOM 9113 C CG . PHE BA 1 146 ? -61.266 15.467 41.221 1.0 54.31 ? ? ? ? ? ? 263 PHE BA CG 1 146 B B +ATOM 9114 C CD1 . PHE BA 1 146 ? -60.858 14.422 40.399 1.0 58.96 ? ? ? ? ? ? 263 PHE BA CD1 1 146 B B +ATOM 9115 C CD2 . PHE BA 1 146 ? -62.297 15.240 42.129 1.0 60.8 ? ? ? ? ? ? 263 PHE BA CD2 1 146 B B +ATOM 9116 C CE1 . PHE BA 1 146 ? -61.468 13.168 40.484 1.0 62.13 ? ? ? ? ? ? 263 PHE BA CE1 1 146 B B +ATOM 9117 C CE2 . PHE BA 1 146 ? -62.913 13.989 42.220 1.0 62.38 ? ? ? ? ? ? 263 PHE BA CE2 1 146 B B +ATOM 9118 C CZ . PHE BA 1 146 ? -62.499 12.953 41.397 1.0 62.3 ? ? ? ? ? ? 263 PHE BA CZ 1 146 B B +ATOM 9119 N N . HIS BA 1 147 ? -62.280 16.875 38.164 1.0 56.84 ? ? ? ? ? ? 264 HIS BA N 1 147 B B +ATOM 9120 C CA . HIS BA 1 147 ? -63.594 17.061 37.562 1.0 50.73 ? ? ? ? ? ? 264 HIS BA CA 1 147 B B +ATOM 9121 C C . HIS BA 1 147 ? -64.615 16.291 38.390 1.0 52.79 ? ? ? ? ? ? 264 HIS BA C 1 147 B B +ATOM 9122 O O . HIS BA 1 147 ? -64.723 15.067 38.307 1.0 42.06 ? ? ? ? ? ? 264 HIS BA O 1 147 B B +ATOM 9123 C CB . HIS BA 1 147 ? -63.573 16.583 36.105 1.0 60.26 ? ? ? ? ? ? 264 HIS BA CB 1 147 B B +ATOM 9124 C CG . HIS BA 1 147 ? -62.793 17.481 35.198 1.0 66.12 ? ? ? ? ? ? 264 HIS BA CG 1 147 B B +ATOM 9125 N ND1 . HIS BA 1 147 ? -63.389 18.434 34.399 1.0 64.49 ? ? ? ? ? ? 264 HIS BA ND1 1 147 B B +ATOM 9126 C CD2 . HIS BA 1 147 ? -61.458 17.608 35.002 1.0 62.27 ? ? ? ? ? ? 264 HIS BA CD2 1 147 B B +ATOM 9127 C CE1 . HIS BA 1 147 ? -62.452 19.109 33.750 1.0 54.65 ? ? ? ? ? ? 264 HIS BA CE1 1 147 B B +ATOM 9128 N NE2 . HIS BA 1 147 ? -61.277 18.626 34.100 1.0 65.71 ? ? ? ? ? ? 264 HIS BA NE2 1 147 B B +ATOM 9129 N N . CYS BA 1 148 ? -65.364 17.036 39.195 1.0 70.9 ? ? ? ? ? ? 265 CYS BA N 1 148 B B +ATOM 9130 C CA . CYS BA 1 148 ? -66.358 16.461 40.091 1.0 78.16 ? ? ? ? ? ? 265 CYS BA CA 1 148 B B +ATOM 9131 C C . CYS BA 1 148 ? -67.807 16.634 39.645 1.0 78.58 ? ? ? ? ? ? 265 CYS BA C 1 148 B B +ATOM 9132 O O . CYS BA 1 148 ? -68.153 17.582 38.937 1.0 77.71 ? ? ? ? ? ? 265 CYS BA O 1 148 B B +ATOM 9133 C CB . CYS BA 1 148 ? -66.173 17.067 41.485 1.0 71.85 ? ? ? ? ? ? 265 CYS BA CB 1 148 B B +ATOM 9134 S SG . CYS BA 1 148 ? -67.302 16.460 42.743 1.0 92.69 ? ? ? ? ? ? 265 CYS BA SG 1 148 B B +ATOM 9135 N N . THR BA 1 149 ? -68.644 15.693 40.072 1.0 70.23 ? ? ? ? ? ? 266 THR BA N 1 149 B B +ATOM 9136 C CA . THR BA 1 149 ? -70.069 15.697 39.767 1.0 59.7 ? ? ? ? ? ? 266 THR BA CA 1 149 B B +ATOM 9137 C C . THR BA 1 149 ? -70.818 16.390 40.908 1.0 54.47 ? ? ? ? ? ? 266 THR BA C 1 149 B B +ATOM 9138 O O . THR BA 1 149 ? -70.633 16.051 42.077 1.0 54.63 ? ? ? ? ? ? 266 THR BA O 1 149 B B +ATOM 9139 C CB . THR BA 1 149 ? -70.608 14.259 39.620 1.0 55.29 ? ? ? ? ? ? 266 THR BA CB 1 149 B B +ATOM 9140 O OG1 . THR BA 1 149 ? -70.664 13.631 40.907 1.0 37.72 ? ? ? ? ? ? 266 THR BA OG1 1 149 B B +ATOM 9141 C CG2 . THR BA 1 149 ? -69.703 13.446 38.714 1.0 59.9 ? ? ? ? ? ? 266 THR BA CG2 1 149 B B +ATOM 9142 N N . GLN BA 1 150 ? -71.659 17.361 40.567 1.0 44.15 ? ? ? ? ? ? 267 GLN BA N 1 150 B B +ATOM 9143 C CA . GLN BA 1 150 ? -72.421 18.095 41.572 1.0 43.6 ? ? ? ? ? ? 267 GLN BA CA 1 150 B B +ATOM 9144 C C . GLN BA 1 150 ? -73.718 17.387 41.943 1.0 41.75 ? ? ? ? ? ? 267 GLN BA C 1 150 B B +ATOM 9145 O O . GLN BA 1 150 ? -74.283 17.638 43.007 1.0 28.69 ? ? ? ? ? ? 267 GLN BA O 1 150 B B +ATOM 9146 C CB . GLN BA 1 150 ? -72.742 19.501 41.064 1.0 45.29 ? ? ? ? ? ? 267 GLN BA CB 1 150 B B +ATOM 9147 C CG . GLN BA 1 150 ? -73.501 20.360 42.056 1.0 34.06 ? ? ? ? ? ? 267 GLN BA CG 1 150 B B +ATOM 9148 C CD . GLN BA 1 150 ? -72.833 21.703 42.297 1.0 59.87 ? ? ? ? ? ? 267 GLN BA CD 1 150 B B +ATOM 9149 O OE1 . GLN BA 1 150 ? -72.574 22.464 41.358 1.0 57.98 ? ? ? ? ? ? 267 GLN BA OE1 1 150 B B +ATOM 9150 N NE2 . GLN BA 1 150 ? -72.556 22.005 43.564 1.0 68.1 ? ? ? ? ? ? 267 GLN BA NE2 1 150 B B +ATOM 9151 N N . TYR BA 1 151 ? -74.179 16.499 41.066 1.0 50.13 ? ? ? ? ? ? 268 TYR BA N 1 151 B B +ATOM 9152 C CA . TYR BA 1 151 ? -75.420 15.767 41.294 1.0 55.5 ? ? ? ? ? ? 268 TYR BA CA 1 151 B B +ATOM 9153 C C . TYR BA 1 151 ? -75.311 14.583 42.257 1.0 57.92 ? ? ? ? ? ? 268 TYR BA C 1 151 B B +ATOM 9154 O O . TYR BA 1 151 ? -74.260 14.339 42.850 1.0 50.68 ? ? ? ? ? ? 268 TYR BA O 1 151 B B +ATOM 9155 C CB . TYR BA 1 151 ? -76.011 15.306 39.954 1.0 64.16 ? ? ? ? ? ? 268 TYR BA CB 1 151 B B +ATOM 9156 C CG . TYR BA 1 151 ? -75.154 14.343 39.159 1.0 65.73 ? ? ? ? ? ? 268 TYR BA CG 1 151 B B +ATOM 9157 C CD1 . TYR BA 1 151 ? -75.163 12.976 39.441 1.0 64.71 ? ? ? ? ? ? 268 TYR BA CD1 1 151 B B +ATOM 9158 C CD2 . TYR BA 1 151 ? -74.371 14.792 38.093 1.0 79.87 ? ? ? ? ? ? 268 TYR BA CD2 1 151 B B +ATOM 9159 C CE1 . TYR BA 1 151 ? -74.420 12.077 38.679 1.0 76.68 ? ? ? ? ? ? 268 TYR BA CE1 1 151 B B +ATOM 9160 C CE2 . TYR BA 1 151 ? -73.623 13.901 37.323 1.0 90.35 ? ? ? ? ? ? 268 TYR BA CE2 1 151 B B +ATOM 9161 C CZ . TYR BA 1 151 ? -73.651 12.544 37.620 1.0 89.09 ? ? ? ? ? ? 268 TYR BA CZ 1 151 B B +ATOM 9162 O OH . TYR BA 1 151 ? -72.926 11.656 36.851 1.0 82.46 ? ? ? ? ? ? 268 TYR BA OH 1 151 B B +ATOM 9163 N N . ILE BA 1 152 ? -76.413 13.850 42.401 1.0 62.65 ? ? ? ? ? ? 269 ILE BA N 1 152 B B +ATOM 9164 C CA . ILE BA 1 152 ? -76.472 12.702 43.302 1.0 61.05 ? ? ? ? ? ? 269 ILE BA CA 1 152 B B +ATOM 9165 C C . ILE BA 1 152 ? -77.345 11.570 42.768 1.0 56.59 ? ? ? ? ? ? 269 ILE BA C 1 152 B B +ATOM 9166 O O . ILE BA 1 152 ? -78.299 11.806 42.029 1.0 53.39 ? ? ? ? ? ? 269 ILE BA O 1 152 B B +ATOM 9167 C CB . ILE BA 1 152 ? -77.035 13.110 44.673 1.0 70.67 ? ? ? ? ? ? 269 ILE BA CB 1 152 B B +ATOM 9168 C CG1 . ILE BA 1 152 ? -77.098 11.892 45.596 1.0 68.86 ? ? ? ? ? ? 269 ILE BA CG1 1 152 B B +ATOM 9169 C CG2 . ILE BA 1 152 ? -78.423 13.714 44.498 1.0 74.1 ? ? ? ? ? ? 269 ILE BA CG2 1 152 B B +ATOM 9170 C CD1 . ILE BA 1 152 ? -77.427 12.229 47.028 1.0 82.6 ? ? ? ? ? ? 269 ILE BA CD1 1 152 B B +ATOM 9171 N N . ARG BA 1 153 ? -77.020 10.343 43.164 1.0 64.18 ? ? ? ? ? ? 270 ARG BA N 1 153 B B +ATOM 9172 C CA . ARG BA 1 153 ? -77.765 9.165 42.741 1.0 70.1 ? ? ? ? ? ? 270 ARG BA CA 1 153 B B +ATOM 9173 C C . ARG BA 1 153 ? -79.235 9.326 43.107 1.0 79.83 ? ? ? ? ? ? 270 ARG BA C 1 153 B B +ATOM 9174 O O . ARG BA 1 153 ? -79.596 10.217 43.874 1.0 80.48 ? ? ? ? ? ? 270 ARG BA O 1 153 B B +ATOM 9175 C CB . ARG BA 1 153 ? -77.205 7.923 43.430 1.0 65.85 ? ? ? ? ? ? 270 ARG BA CB 1 153 B B +ATOM 9176 C CG . ARG BA 1 153 ? -77.238 8.003 44.946 1.0 66.82 ? ? ? ? ? ? 270 ARG BA CG 1 153 B B +ATOM 9177 C CD . ARG BA 1 153 ? -76.568 6.799 45.571 1.0 81.52 ? ? ? ? ? ? 270 ARG BA CD 1 153 B B +ATOM 9178 N NE . ARG BA 1 153 ? -75.152 7.043 45.828 1.0 87.21 ? ? ? ? ? ? 270 ARG BA NE 1 153 B B +ATOM 9179 C CZ . ARG BA 1 153 ? -74.429 6.370 46.716 1.0 88.22 ? ? ? ? ? ? 270 ARG BA CZ 1 153 B B +ATOM 9180 N NH1 . ARG BA 1 153 ? -74.989 5.408 47.438 1.0 90.32 ? ? ? ? ? ? 270 ARG BA NH1 1 153 B B +ATOM 9181 N NH2 . ARG BA 1 153 ? -73.147 6.656 46.882 1.0 75.36 ? ? ? ? ? ? 270 ARG BA NH2 1 153 B B +ATOM 9182 N N . HIS BA 1 154 ? -80.083 8.466 42.554 1.0 86.18 ? ? ? ? ? ? 271 HIS BA N 1 154 B B +ATOM 9183 C CA . HIS BA 1 154 ? -81.508 8.528 42.851 1.0 90.54 ? ? ? ? ? ? 271 HIS BA CA 1 154 B B +ATOM 9184 C C . HIS BA 1 154 ? -81.789 7.803 44.159 1.0 85.85 ? ? ? ? ? ? 271 HIS BA C 1 154 B B +ATOM 9185 O O . HIS BA 1 154 ? -81.210 6.752 44.436 1.0 64.73 ? ? ? ? ? ? 271 HIS BA O 1 154 B B +ATOM 9186 C CB . HIS BA 1 154 ? -82.333 7.894 41.728 1.0 95.52 ? ? ? ? ? ? 271 HIS BA CB 1 154 B B +ATOM 9187 C CG . HIS BA 1 154 ? -83.801 8.161 41.844 1.0 89.69 ? ? ? ? ? ? 271 HIS BA CG 1 154 B B +ATOM 9188 N ND1 . HIS BA 1 154 ? -84.727 7.156 42.019 1.0 76.85 ? ? ? ? ? ? 271 HIS BA ND1 1 154 B B +ATOM 9189 C CD2 . HIS BA 1 154 ? -84.500 9.321 41.839 1.0 91.52 ? ? ? ? ? ? 271 HIS BA CD2 1 154 B B +ATOM 9190 C CE1 . HIS BA 1 154 ? -85.934 7.687 42.118 1.0 88.56 ? ? ? ? ? ? 271 HIS BA CE1 1 154 B B +ATOM 9191 N NE2 . HIS BA 1 154 ? -85.822 8.998 42.012 1.0 92.65 ? ? ? ? ? ? 271 HIS BA NE2 1 154 B B +ATOM 9192 N N . GLY BA 1 155 ? -82.689 8.370 44.953 1.0 87.3 ? ? ? ? ? ? 272 GLY BA N 1 155 B B +ATOM 9193 C CA . GLY BA 1 155 ? -83.030 7.780 46.234 1.0 95.34 ? ? ? ? ? ? 272 GLY BA CA 1 155 B B +ATOM 9194 C C . GLY BA 1 155 ? -83.598 6.372 46.211 1.0 97.82 ? ? ? ? ? ? 272 GLY BA C 1 155 B B +ATOM 9195 O O . GLY BA 1 155 ? -83.681 5.734 47.260 1.0 89.23 ? ? ? ? ? ? 272 GLY BA O 1 155 B B +ATOM 9196 N N . SER BA 1 156 ? -83.993 5.878 45.040 1.0 99.95 ? ? ? ? ? ? 273 SER BA N 1 156 B B +ATOM 9197 C CA . SER BA 1 156 ? -84.553 4.530 44.945 1.0 94.57 ? ? ? ? ? ? 273 SER BA CA 1 156 B B +ATOM 9198 C C . SER BA 1 156 ? -83.609 3.517 45.580 1.0 82.28 ? ? ? ? ? ? 273 SER BA C 1 156 B B +ATOM 9199 O O . SER BA 1 156 ? -84.002 2.759 46.466 1.0 87.61 ? ? ? ? ? ? 273 SER BA O 1 156 B B +ATOM 9200 C CB . SER BA 1 156 ? -84.822 4.152 43.481 1.0 100.0 ? ? ? ? ? ? 273 SER BA CB 1 156 B B +ATOM 9201 O OG . SER BA 1 156 ? -83.637 4.167 42.707 1.0 92.2 ? ? ? ? ? ? 273 SER BA OG 1 156 B B +ATOM 9202 N N . LYS BA 1 157 ? -82.362 3.515 45.123 1.0 77.9 ? ? ? ? ? ? 274 LYS BA N 1 157 B B +ATOM 9203 C CA . LYS BA 1 157 ? -81.353 2.611 45.659 1.0 89.43 ? ? ? ? ? ? 274 LYS BA CA 1 157 B B +ATOM 9204 C C . LYS BA 1 157 ? -80.163 3.430 46.154 1.0 94.52 ? ? ? ? ? ? 274 LYS BA C 1 157 B B +ATOM 9205 O O . LYS BA 1 157 ? -79.195 3.653 45.425 1.0 86.19 ? ? ? ? ? ? 274 LYS BA O 1 157 B B +ATOM 9206 C CB . LYS BA 1 157 ? -80.918 1.610 44.586 1.0 89.55 ? ? ? ? ? ? 274 LYS BA CB 1 157 B B +ATOM 9207 C CG . LYS BA 1 157 ? -81.916 0.475 44.384 1.0 92.41 ? ? ? ? ? ? 274 LYS BA CG 1 157 B B +ATOM 9208 C CD . LYS BA 1 157 ? -82.137 -0.304 45.676 1.0 99.23 ? ? ? ? ? ? 274 LYS BA CD 1 157 B B +ATOM 9209 C CE . LYS BA 1 157 ? -83.236 -1.347 45.521 1.0 99.82 ? ? ? ? ? ? 274 LYS BA CE 1 157 B B +ATOM 9210 N NZ . LYS BA 1 157 ? -83.575 -2.006 46.815 1.0 100.0 ? ? ? ? ? ? 274 LYS BA NZ 1 157 B B +ATOM 9211 N N . PRO BA 1 158 ? -80.235 3.895 47.414 1.0 100.0 ? ? ? ? ? ? 275 PRO BA N 1 158 B B +ATOM 9212 C CA . PRO BA 1 158 ? -79.191 4.703 48.056 1.0 100.0 ? ? ? ? ? ? 275 PRO BA CA 1 158 B B +ATOM 9213 C C . PRO BA 1 158 ? -77.914 3.937 48.393 1.0 92.42 ? ? ? ? ? ? 275 PRO BA C 1 158 B B +ATOM 9214 O O . PRO BA 1 158 ? -77.025 4.463 49.066 1.0 86.52 ? ? ? ? ? ? 275 PRO BA O 1 158 B B +ATOM 9215 C CB . PRO BA 1 158 ? -79.881 5.250 49.305 1.0 100.0 ? ? ? ? ? ? 275 PRO BA CB 1 158 B B +ATOM 9216 C CG . PRO BA 1 158 ? -80.924 4.239 49.625 1.0 100.0 ? ? ? ? ? ? 275 PRO BA CG 1 158 B B +ATOM 9217 C CD . PRO BA 1 158 ? -81.374 3.650 48.319 1.0 98.17 ? ? ? ? ? ? 275 PRO BA CD 1 158 B B +ATOM 9218 N N . MET BA 1 159 ? -77.825 2.698 47.919 1.0 81.69 ? ? ? ? ? ? 276 MET BA N 1 159 B B +ATOM 9219 C CA . MET BA 1 159 ? -76.650 1.873 48.174 1.0 91.13 ? ? ? ? ? ? 276 MET BA CA 1 159 B B +ATOM 9220 C C . MET BA 1 159 ? -76.000 1.443 46.862 1.0 93.32 ? ? ? ? ? ? 276 MET BA C 1 159 B B +ATOM 9221 O O . MET BA 1 159 ? -75.162 0.542 46.835 1.0 100.0 ? ? ? ? ? ? 276 MET BA O 1 159 B B +ATOM 9222 C CB . MET BA 1 159 ? -77.045 0.637 48.988 1.0 100.0 ? ? ? ? ? ? 276 MET BA CB 1 159 B B +ATOM 9223 C CG . MET BA 1 159 ? -76.257 0.452 50.279 1.0 100.0 ? ? ? ? ? ? 276 MET BA CG 1 159 B B +ATOM 9224 S SD . MET BA 1 159 ? -76.268 1.908 51.354 1.0 100.0 ? ? ? ? ? ? 276 MET BA SD 1 159 B B +ATOM 9225 C CE . MET BA 1 159 ? -74.634 2.562 51.034 1.0 100.0 ? ? ? ? ? ? 276 MET BA CE 1 159 B B +ATOM 9226 N N . TYR BA 1 160 ? -76.387 2.101 45.775 1.0 90.51 ? ? ? ? ? ? 277 TYR BA N 1 160 B B +ATOM 9227 C CA . TYR BA 1 160 ? -75.840 1.776 44.469 1.0 93.75 ? ? ? ? ? ? 277 TYR BA CA 1 160 B B +ATOM 9228 C C . TYR BA 1 160 ? -75.909 2.948 43.497 1.0 95.85 ? ? ? ? ? ? 277 TYR BA C 1 160 B B +ATOM 9229 O O . TYR BA 1 160 ? -76.914 3.659 43.430 1.0 94.33 ? ? ? ? ? ? 277 TYR BA O 1 160 B B +ATOM 9230 C CB . TYR BA 1 160 ? -76.580 0.577 43.877 1.0 100.0 ? ? ? ? ? ? 277 TYR BA CB 1 160 B B +ATOM 9231 C CG . TYR BA 1 160 ? -76.538 0.521 42.369 1.0 98.17 ? ? ? ? ? ? 277 TYR BA CG 1 160 B B +ATOM 9232 C CD1 . TYR BA 1 160 ? -75.377 0.133 41.703 1.0 100.0 ? ? ? ? ? ? 277 TYR BA CD1 1 160 B B +ATOM 9233 C CD2 . TYR BA 1 160 ? -77.654 0.863 41.607 1.0 88.77 ? ? ? ? ? ? 277 TYR BA CD2 1 160 B B +ATOM 9234 C CE1 . TYR BA 1 160 ? -75.329 0.087 40.316 1.0 100.0 ? ? ? ? ? ? 277 TYR BA CE1 1 160 B B +ATOM 9235 C CE2 . TYR BA 1 160 ? -77.616 0.821 40.220 1.0 94.7 ? ? ? ? ? ? 277 TYR BA CE2 1 160 B B +ATOM 9236 C CZ . TYR BA 1 160 ? -76.451 0.431 39.580 1.0 100.0 ? ? ? ? ? ? 277 TYR BA CZ 1 160 B B +ATOM 9237 O OH . TYR BA 1 160 ? -76.413 0.378 38.205 1.0 100.0 ? ? ? ? ? ? 277 TYR BA OH 1 160 B B +ATOM 9238 N N . THR BA 1 161 ? -74.828 3.134 42.747 1.0 95.17 ? ? ? ? ? ? 278 THR BA N 1 161 B B +ATOM 9239 C CA . THR BA 1 161 ? -74.746 4.197 41.752 1.0 98.21 ? ? ? ? ? ? 278 THR BA CA 1 161 B B +ATOM 9240 C C . THR BA 1 161 ? -74.067 3.637 40.507 1.0 93.52 ? ? ? ? ? ? 278 THR BA C 1 161 B B +ATOM 9241 O O . THR BA 1 161 ? -73.006 3.017 40.590 1.0 89.12 ? ? ? ? ? ? 278 THR BA O 1 161 B B +ATOM 9242 C CB . THR BA 1 161 ? -73.940 5.405 42.274 1.0 100.0 ? ? ? ? ? ? 278 THR BA CB 1 161 B B +ATOM 9243 O OG1 . THR BA 1 161 ? -74.168 5.555 43.681 1.0 100.0 ? ? ? ? ? ? 278 THR BA OG1 1 161 B B +ATOM 9244 C CG2 . THR BA 1 161 ? -74.379 6.672 41.562 1.0 97.39 ? ? ? ? ? ? 278 THR BA CG2 1 161 B B +ATOM 9245 N N . PRO BA 1 162 ? -74.670 3.853 39.328 1.0 96.39 ? ? ? ? ? ? 279 PRO BA N 1 162 B B +ATOM 9246 C CA . PRO BA 1 162 ? -74.087 3.345 38.082 1.0 95.92 ? ? ? ? ? ? 279 PRO BA CA 1 162 B B +ATOM 9247 C C . PRO BA 1 162 ? -72.916 4.188 37.591 1.0 87.33 ? ? ? ? ? ? 279 PRO BA C 1 162 B B +ATOM 9248 O O . PRO BA 1 162 ? -72.232 3.834 36.634 1.0 85.43 ? ? ? ? ? ? 279 PRO BA O 1 162 B B +ATOM 9249 C CB . PRO BA 1 162 ? -75.261 3.368 37.109 1.0 99.85 ? ? ? ? ? ? 279 PRO BA CB 1 162 B B +ATOM 9250 C CG . PRO BA 1 162 ? -76.146 4.467 37.610 1.0 93.17 ? ? ? ? ? ? 279 PRO BA CG 1 162 B B +ATOM 9251 C CD . PRO BA 1 162 ? -75.909 4.614 39.092 1.0 96.89 ? ? ? ? ? ? 279 PRO BA CD 1 162 B B +ATOM 9252 N N . GLU BA 1 163 ? -72.682 5.305 38.273 1.0 77.03 ? ? ? ? ? ? 280 GLU BA N 1 163 B B +ATOM 9253 C CA . GLU BA 1 163 ? -71.604 6.211 37.912 1.0 74.74 ? ? ? ? ? ? 280 GLU BA CA 1 163 B B +ATOM 9254 C C . GLU BA 1 163 ? -71.314 7.181 39.056 1.0 78.36 ? ? ? ? ? ? 280 GLU BA C 1 163 B B +ATOM 9255 O O . GLU BA 1 163 ? -72.084 7.281 40.009 1.0 70.27 ? ? ? ? ? ? 280 GLU BA O 1 163 B B +ATOM 9256 C CB . GLU BA 1 163 ? -71.985 6.980 36.645 1.0 68.54 ? ? ? ? ? ? 280 GLU BA CB 1 163 B B +ATOM 9257 C CG . GLU BA 1 163 ? -72.815 8.219 36.917 1.0 83.22 ? ? ? ? ? ? 280 GLU BA CG 1 163 B B +ATOM 9258 C CD . GLU BA 1 163 ? -74.301 7.924 36.926 1.0 90.41 ? ? ? ? ? ? 280 GLU BA CD 1 163 B B +ATOM 9259 O OE1 . GLU BA 1 163 ? -74.865 7.666 35.844 1.0 86.76 ? ? ? ? ? ? 280 GLU BA OE1 1 163 B B +ATOM 9260 O OE2 . GLU BA 1 163 ? -74.909 7.952 38.014 1.0 98.96 ? ? ? ? ? ? 280 GLU BA OE2 1 163 B B +ATOM 9261 N N . PRO BA 1 164 ? -70.210 7.940 38.952 1.0 79.29 ? ? ? ? ? ? 281 PRO BA N 1 164 B B +ATOM 9262 C CA . PRO BA 1 164 ? -69.841 8.894 40.004 1.0 81.83 ? ? ? ? ? ? 281 PRO BA CA 1 164 B B +ATOM 9263 C C . PRO BA 1 164 ? -70.886 9.946 40.359 1.0 72.28 ? ? ? ? ? ? 281 PRO BA C 1 164 B B +ATOM 9264 O O . PRO BA 1 164 ? -71.420 10.625 39.485 1.0 76.26 ? ? ? ? ? ? 281 PRO BA O 1 164 B B +ATOM 9265 C CB . PRO BA 1 164 ? -68.553 9.534 39.483 1.0 86.01 ? ? ? ? ? ? 281 PRO BA CB 1 164 B B +ATOM 9266 C CG . PRO BA 1 164 ? -68.080 8.648 38.390 1.0 95.32 ? ? ? ? ? ? 281 PRO BA CG 1 164 B B +ATOM 9267 C CD . PRO BA 1 164 ? -69.279 7.985 37.812 1.0 84.71 ? ? ? ? ? ? 281 PRO BA CD 1 164 B B +ATOM 9268 N N . ASP BA 1 165 ? -71.161 10.072 41.655 1.0 57.88 ? ? ? ? ? ? 282 ASP BA N 1 165 B B +ATOM 9269 C CA . ASP BA 1 165 ? -72.110 11.050 42.186 1.0 52.74 ? ? ? ? ? ? 282 ASP BA CA 1 165 B B +ATOM 9270 C C . ASP BA 1 165 ? -71.388 11.820 43.290 1.0 54.7 ? ? ? ? ? ? 282 ASP BA C 1 165 B B +ATOM 9271 O O . ASP BA 1 165 ? -70.299 11.425 43.703 1.0 58.09 ? ? ? ? ? ? 282 ASP BA O 1 165 B B +ATOM 9272 C CB . ASP BA 1 165 ? -73.341 10.349 42.760 1.0 66.43 ? ? ? ? ? ? 282 ASP BA CB 1 165 B B +ATOM 9273 C CG . ASP BA 1 165 ? -73.050 9.628 44.061 1.0 78.92 ? ? ? ? ? ? 282 ASP BA CG 1 165 B B +ATOM 9274 O OD1 . ASP BA 1 165 ? -73.894 9.692 44.977 1.0 87.37 ? ? ? ? ? ? 282 ASP BA OD1 1 165 B B +ATOM 9275 O OD2 . ASP BA 1 165 ? -71.980 8.997 44.168 1.0 86.33 ? ? ? ? ? ? 282 ASP BA OD2 1 165 B B +ATOM 9276 N N . ILE BA 1 166 ? -71.984 12.902 43.778 1.0 66.28 ? ? ? ? ? ? 283 ILE BA N 1 166 B B +ATOM 9277 C CA . ILE BA 1 166 ? -71.344 13.707 44.820 1.0 71.93 ? ? ? ? ? ? 283 ILE BA CA 1 166 B B +ATOM 9278 C C . ILE BA 1 166 ? -70.900 12.921 46.058 1.0 74.24 ? ? ? ? ? ? 283 ILE BA C 1 166 B B +ATOM 9279 O O . ILE BA 1 166 ? -70.160 13.434 46.897 1.0 73.66 ? ? ? ? ? ? 283 ILE BA O 1 166 B B +ATOM 9280 C CB . ILE BA 1 166 ? -72.256 14.863 45.283 1.0 62.68 ? ? ? ? ? ? 283 ILE BA CB 1 166 B B +ATOM 9281 C CG1 . ILE BA 1 166 ? -71.428 15.895 46.059 1.0 54.55 ? ? ? ? ? ? 283 ILE BA CG1 1 166 B B +ATOM 9282 C CG2 . ILE BA 1 166 ? -73.386 14.323 46.144 1.0 68.03 ? ? ? ? ? ? 283 ILE BA CG2 1 166 B B +ATOM 9283 C CD1 . ILE BA 1 166 ? -72.051 17.276 46.119 1.0 69.59 ? ? ? ? ? ? 283 ILE BA CD1 1 166 B B +ATOM 9284 N N . CYS BA 1 167 ? -71.353 11.678 46.177 1.0 73.07 ? ? ? ? ? ? 284 CYS BA N 1 167 B B +ATOM 9285 C CA . CYS BA 1 167 ? -70.970 10.850 47.311 1.0 79.04 ? ? ? ? ? ? 284 CYS BA CA 1 167 B B +ATOM 9286 C C . CYS BA 1 167 ? -69.641 10.178 47.000 1.0 74.38 ? ? ? ? ? ? 284 CYS BA C 1 167 B B +ATOM 9287 O O . CYS BA 1 167 ? -68.717 10.199 47.811 1.0 83.07 ? ? ? ? ? ? 284 CYS BA O 1 167 B B +ATOM 9288 C CB . CYS BA 1 167 ? -72.037 9.786 47.577 1.0 87.12 ? ? ? ? ? ? 284 CYS BA CB 1 167 B B +ATOM 9289 S SG . CYS BA 1 167 ? -73.721 10.422 47.687 1.0 100.0 ? ? ? ? ? ? 284 CYS BA SG 1 167 B B +ATOM 9290 N N . HIS BA 1 168 ? -69.554 9.581 45.817 1.0 63.84 ? ? ? ? ? ? 285 HIS BA N 1 168 B B +ATOM 9291 C CA . HIS BA 1 168 ? -68.336 8.903 45.390 1.0 71.0 ? ? ? ? ? ? 285 HIS BA CA 1 168 B B +ATOM 9292 C C . HIS BA 1 168 ? -67.169 9.888 45.342 1.0 74.3 ? ? ? ? ? ? 285 HIS BA C 1 168 B B +ATOM 9293 O O . HIS BA 1 168 ? -66.063 9.587 45.802 1.0 64.25 ? ? ? ? ? ? 285 HIS BA O 1 168 B B +ATOM 9294 C CB . HIS BA 1 168 ? -68.553 8.268 44.011 1.0 70.96 ? ? ? ? ? ? 285 HIS BA CB 1 168 B B +ATOM 9295 C CG . HIS BA 1 168 ? -67.286 7.912 43.296 1.0 80.88 ? ? ? ? ? ? 285 HIS BA CG 1 168 B B +ATOM 9296 N ND1 . HIS BA 1 168 ? -66.609 6.731 43.522 1.0 86.16 ? ? ? ? ? ? 285 HIS BA ND1 1 168 B B +ATOM 9297 C CD2 . HIS BA 1 168 ? -66.591 8.567 42.336 1.0 81.95 ? ? ? ? ? ? 285 HIS BA CD2 1 168 B B +ATOM 9298 C CE1 . HIS BA 1 168 ? -65.554 6.674 42.729 1.0 92.15 ? ? ? ? ? ? 285 HIS BA CE1 1 168 B B +ATOM 9299 N NE2 . HIS BA 1 168 ? -65.518 7.775 41.998 1.0 94.55 ? ? ? ? ? ? 285 HIS BA NE2 1 168 B B +ATOM 9300 N N . GLU BA 1 169 ? -67.432 11.074 44.803 1.0 72.7 ? ? ? ? ? ? 286 GLU BA N 1 169 B B +ATOM 9301 C CA . GLU BA 1 169 ? -66.412 12.103 44.679 1.0 68.31 ? ? ? ? ? ? 286 GLU BA CA 1 169 B B +ATOM 9302 C C . GLU BA 1 169 ? -65.984 12.697 46.015 1.0 66.37 ? ? ? ? ? ? 286 GLU BA C 1 169 B B +ATOM 9303 O O . GLU BA 1 169 ? -64.797 12.919 46.244 1.0 83.61 ? ? ? ? ? ? 286 GLU BA O 1 169 B B +ATOM 9304 C CB . GLU BA 1 169 ? -66.913 13.225 43.764 1.0 70.61 ? ? ? ? ? ? 286 GLU BA CB 1 169 B B +ATOM 9305 C CG . GLU BA 1 169 ? -67.659 12.740 42.532 1.0 90.67 ? ? ? ? ? ? 286 GLU BA CG 1 169 B B +ATOM 9306 C CD . GLU BA 1 169 ? -66.737 12.424 41.368 1.0 93.74 ? ? ? ? ? ? 286 GLU BA CD 1 169 B B +ATOM 9307 O OE1 . GLU BA 1 169 ? -66.523 13.309 40.516 1.0 87.42 ? ? ? ? ? ? 286 GLU BA OE1 1 169 B B +ATOM 9308 O OE2 . GLU BA 1 169 ? -66.231 11.287 41.295 1.0 87.7 ? ? ? ? ? ? 286 GLU BA OE2 1 169 B B +ATOM 9309 N N . LEU BA 1 170 ? -66.950 12.947 46.894 1.0 61.19 ? ? ? ? ? ? 287 LEU BA N 1 170 B B +ATOM 9310 C CA . LEU BA 1 170 ? -66.666 13.543 48.198 1.0 51.14 ? ? ? ? ? ? 287 LEU BA CA 1 170 B B +ATOM 9311 C C . LEU BA 1 170 ? -66.263 12.552 49.288 1.0 55.43 ? ? ? ? ? ? 287 LEU BA C 1 170 B B +ATOM 9312 O O . LEU BA 1 170 ? -65.357 12.827 50.072 1.0 52.39 ? ? ? ? ? ? 287 LEU BA O 1 170 B B +ATOM 9313 C CB . LEU BA 1 170 ? -67.876 14.349 48.672 1.0 52.01 ? ? ? ? ? ? 287 LEU BA CB 1 170 B B +ATOM 9314 C CG . LEU BA 1 170 ? -68.111 15.736 48.061 1.0 56.75 ? ? ? ? ? ? 287 LEU BA CG 1 170 B B +ATOM 9315 C CD1 . LEU BA 1 170 ? -69.188 16.460 48.861 1.0 51.84 ? ? ? ? ? ? 287 LEU BA CD1 1 170 B B +ATOM 9316 C CD2 . LEU BA 1 170 ? -66.820 16.541 48.058 1.0 26.43 ? ? ? ? ? ? 287 LEU BA CD2 1 170 B B +ATOM 9317 N N . LEU BA 1 171 ? -66.939 11.409 49.346 1.0 63.3 ? ? ? ? ? ? 288 LEU BA N 1 171 B B +ATOM 9318 C CA . LEU BA 1 171 ? -66.636 10.390 50.350 1.0 63.83 ? ? ? ? ? ? 288 LEU BA CA 1 171 B B +ATOM 9319 C C . LEU BA 1 171 ? -65.778 9.280 49.754 1.0 72.88 ? ? ? ? ? ? 288 LEU BA C 1 171 B B +ATOM 9320 O O . LEU BA 1 171 ? -65.856 8.124 50.176 1.0 76.97 ? ? ? ? ? ? 288 LEU BA O 1 171 B B +ATOM 9321 C CB . LEU BA 1 171 ? -67.932 9.785 50.906 1.0 59.92 ? ? ? ? ? ? 288 LEU BA CB 1 171 B B +ATOM 9322 C CG . LEU BA 1 171 ? -68.998 10.757 51.419 1.0 61.12 ? ? ? ? ? ? 288 LEU BA CG 1 171 B B +ATOM 9323 C CD1 . LEU BA 1 171 ? -70.282 9.996 51.702 1.0 71.68 ? ? ? ? ? ? 288 LEU BA CD1 1 171 B B +ATOM 9324 C CD2 . LEU BA 1 171 ? -68.504 11.457 52.672 1.0 63.71 ? ? ? ? ? ? 288 LEU BA CD2 1 171 B B +ATOM 9325 N N . GLY BA 1 172 ? -64.961 9.636 48.767 1.0 76.38 ? ? ? ? ? ? 289 GLY BA N 1 172 B B +ATOM 9326 C CA . GLY BA 1 172 ? -64.107 8.650 48.134 1.0 79.16 ? ? ? ? ? ? 289 GLY BA CA 1 172 B B +ATOM 9327 C C . GLY BA 1 172 ? -62.831 9.233 47.561 1.0 75.97 ? ? ? ? ? ? 289 GLY BA C 1 172 B B +ATOM 9328 O O . GLY BA 1 172 ? -61.732 8.808 47.921 1.0 79.25 ? ? ? ? ? ? 289 GLY BA O 1 172 B B +ATOM 9329 N N . HIS BA 1 173 ? -62.980 10.208 46.668 1.0 67.22 ? ? ? ? ? ? 290 HIS BA N 1 173 B B +ATOM 9330 C CA . HIS BA 1 173 ? -61.831 10.845 46.029 1.0 70.99 ? ? ? ? ? ? 290 HIS BA CA 1 173 B B +ATOM 9331 C C . HIS BA 1 173 ? -61.223 11.979 46.857 1.0 67.43 ? ? ? ? ? ? 290 HIS BA C 1 173 B B +ATOM 9332 O O . HIS BA 1 173 ? -60.046 11.937 47.220 1.0 77.17 ? ? ? ? ? ? 290 HIS BA O 1 173 B B +ATOM 9333 C CB . HIS BA 1 173 ? -62.232 11.385 44.650 1.0 67.02 ? ? ? ? ? ? 290 HIS BA CB 1 173 B B +ATOM 9334 C CG . HIS BA 1 173 ? -62.269 10.340 43.578 1.0 67.51 ? ? ? ? ? ? 290 HIS BA CG 1 173 B B +ATOM 9335 N ND1 . HIS BA 1 173 ? -61.164 9.995 42.833 1.0 73.03 ? ? ? ? ? ? 290 HIS BA ND1 1 173 B B +ATOM 9336 C CD2 . HIS BA 1 173 ? -63.284 9.563 43.127 1.0 69.16 ? ? ? ? ? ? 290 HIS BA CD2 1 173 B B +ATOM 9337 C CE1 . HIS BA 1 173 ? -61.492 9.051 41.969 1.0 74.93 ? ? ? ? ? ? 290 HIS BA CE1 1 173 B B +ATOM 9338 N NE2 . HIS BA 1 173 ? -62.773 8.770 42.127 1.0 78.02 ? ? ? ? ? ? 290 HIS BA NE2 1 173 B B +ATOM 9339 N N . VAL BA 1 174 ? -62.038 12.987 47.149 1.0 66.78 ? ? ? ? ? ? 291 VAL BA N 1 174 B B +ATOM 9340 C CA . VAL BA 1 174 ? -61.614 14.164 47.904 1.0 71.14 ? ? ? ? ? ? 291 VAL BA CA 1 174 B B +ATOM 9341 C C . VAL BA 1 174 ? -60.638 13.946 49.065 1.0 72.81 ? ? ? ? ? ? 291 VAL BA C 1 174 B B +ATOM 9342 O O . VAL BA 1 174 ? -59.586 14.587 49.118 1.0 57.34 ? ? ? ? ? ? 291 VAL BA O 1 174 B B +ATOM 9343 C CB . VAL BA 1 174 ? -62.845 14.934 48.439 1.0 69.21 ? ? ? ? ? ? 291 VAL BA CB 1 174 B B +ATOM 9344 C CG1 . VAL BA 1 174 ? -62.404 16.092 49.326 1.0 59.39 ? ? ? ? ? ? 291 VAL BA CG1 1 174 B B +ATOM 9345 C CG2 . VAL BA 1 174 ? -63.671 15.456 47.279 1.0 62.18 ? ? ? ? ? ? 291 VAL BA CG2 1 174 B B +ATOM 9346 N N . PRO BA 1 175 ? -60.970 13.040 50.008 1.0 73.61 ? ? ? ? ? ? 292 PRO BA N 1 175 B B +ATOM 9347 C CA . PRO BA 1 175 ? -60.058 12.818 51.139 1.0 71.67 ? ? ? ? ? ? 292 PRO BA CA 1 175 B B +ATOM 9348 C C . PRO BA 1 175 ? -58.639 12.439 50.746 1.0 72.48 ? ? ? ? ? ? 292 PRO BA C 1 175 B B +ATOM 9349 O O . PRO BA 1 175 ? -57.694 12.736 51.471 1.0 79.75 ? ? ? ? ? ? 292 PRO BA O 1 175 B B +ATOM 9350 C CB . PRO BA 1 175 ? -60.738 11.717 51.957 1.0 62.64 ? ? ? ? ? ? 292 PRO BA CB 1 175 B B +ATOM 9351 C CG . PRO BA 1 175 ? -62.143 11.697 51.503 1.0 69.22 ? ? ? ? ? ? 292 PRO BA CG 1 175 B B +ATOM 9352 C CD . PRO BA 1 175 ? -62.158 12.174 50.082 1.0 66.49 ? ? ? ? ? ? 292 PRO BA CD 1 175 B B +ATOM 9353 N N . LEU BA 1 176 ? -58.488 11.778 49.601 1.0 57.88 ? ? ? ? ? ? 293 LEU BA N 1 176 B B +ATOM 9354 C CA . LEU BA 1 176 ? -57.168 11.374 49.141 1.0 51.03 ? ? ? ? ? ? 293 LEU BA CA 1 176 B B +ATOM 9355 C C . LEU BA 1 176 ? -56.440 12.546 48.500 1.0 51.98 ? ? ? ? ? ? 293 LEU BA C 1 176 B B +ATOM 9356 O O . LEU BA 1 176 ? -55.221 12.667 48.608 1.0 55.82 ? ? ? ? ? ? 293 LEU BA O 1 176 B B +ATOM 9357 C CB . LEU BA 1 176 ? -57.286 10.227 48.137 1.0 52.91 ? ? ? ? ? ? 293 LEU BA CB 1 176 B B +ATOM 9358 C CG . LEU BA 1 176 ? -57.380 8.815 48.724 1.0 71.66 ? ? ? ? ? ? 293 LEU BA CG 1 176 B B +ATOM 9359 C CD1 . LEU BA 1 176 ? -56.243 8.580 49.711 1.0 78.03 ? ? ? ? ? ? 293 LEU BA CD1 1 176 B B +ATOM 9360 C CD2 . LEU BA 1 176 ? -58.720 8.640 49.408 1.0 61.55 ? ? ? ? ? ? 293 LEU BA CD2 1 176 B B +ATOM 9361 N N . PHE BA 1 177 ? -57.199 13.412 47.836 1.0 56.22 ? ? ? ? ? ? 294 PHE BA N 1 177 B B +ATOM 9362 C CA . PHE BA 1 177 ? -56.629 14.581 47.175 1.0 54.22 ? ? ? ? ? ? 294 PHE BA CA 1 177 B B +ATOM 9363 C C . PHE BA 1 177 ? -56.217 15.645 48.190 1.0 53.13 ? ? ? ? ? ? 294 PHE BA C 1 177 B B +ATOM 9364 O O . PHE BA 1 177 ? -55.738 16.715 47.818 1.0 51.22 ? ? ? ? ? ? 294 PHE BA O 1 177 B B +ATOM 9365 C CB . PHE BA 1 177 ? -57.638 15.176 46.183 1.0 55.75 ? ? ? ? ? ? 294 PHE BA CB 1 177 B B +ATOM 9366 C CG . PHE BA 1 177 ? -57.820 14.359 44.939 1.0 54.18 ? ? ? ? ? ? 294 PHE BA CG 1 177 B B +ATOM 9367 C CD1 . PHE BA 1 177 ? -56.865 14.380 43.926 1.0 42.65 ? ? ? ? ? ? 294 PHE BA CD1 1 177 B B +ATOM 9368 C CD2 . PHE BA 1 177 ? -58.943 13.554 44.786 1.0 62.02 ? ? ? ? ? ? 294 PHE BA CD2 1 177 B B +ATOM 9369 C CE1 . PHE BA 1 177 ? -57.025 13.608 42.777 1.0 44.22 ? ? ? ? ? ? 294 PHE BA CE1 1 177 B B +ATOM 9370 C CE2 . PHE BA 1 177 ? -59.113 12.777 43.642 1.0 61.59 ? ? ? ? ? ? 294 PHE BA CE2 1 177 B B +ATOM 9371 C CZ . PHE BA 1 177 ? -58.152 12.804 42.636 1.0 63.94 ? ? ? ? ? ? 294 PHE BA CZ 1 177 B B +ATOM 9372 N N . SER BA 1 178 ? -56.414 15.356 49.472 1.0 42.33 ? ? ? ? ? ? 295 SER BA N 1 178 B B +ATOM 9373 C CA . SER BA 1 178 ? -56.037 16.299 50.515 1.0 57.34 ? ? ? ? ? ? 295 SER BA CA 1 178 B B +ATOM 9374 C C . SER BA 1 178 ? -54.641 15.940 51.010 1.0 67.54 ? ? ? ? ? ? 295 SER BA C 1 178 B B +ATOM 9375 O O . SER BA 1 178 ? -53.999 16.725 51.710 1.0 70.27 ? ? ? ? ? ? 295 SER BA O 1 178 B B +ATOM 9376 C CB . SER BA 1 178 ? -57.031 16.238 51.672 1.0 57.63 ? ? ? ? ? ? 295 SER BA CB 1 178 B B +ATOM 9377 O OG . SER BA 1 178 ? -57.111 14.930 52.202 1.0 81.53 ? ? ? ? ? ? 295 SER BA OG 1 178 B B +ATOM 9378 N N . ASP BA 1 179 ? -54.175 14.753 50.623 1.0 69.04 ? ? ? ? ? ? 296 ASP BA N 1 179 B B +ATOM 9379 C CA . ASP BA 1 179 ? -52.861 14.261 51.026 1.0 69.72 ? ? ? ? ? ? 296 ASP BA CA 1 179 B B +ATOM 9380 C C . ASP BA 1 179 ? -51.759 14.689 50.061 1.0 73.53 ? ? ? ? ? ? 296 ASP BA C 1 179 B B +ATOM 9381 O O . ASP BA 1 179 ? -51.822 14.422 48.861 1.0 79.47 ? ? ? ? ? ? 296 ASP BA O 1 179 B B +ATOM 9382 C CB . ASP BA 1 179 ? -52.879 12.738 51.139 1.0 73.34 ? ? ? ? ? ? 296 ASP BA CB 1 179 B B +ATOM 9383 C CG . ASP BA 1 179 ? -51.501 12.156 51.364 1.0 87.96 ? ? ? ? ? ? 296 ASP BA CG 1 179 B B +ATOM 9384 O OD1 . ASP BA 1 179 ? -50.911 12.427 52.432 1.0 93.45 ? ? ? ? ? ? 296 ASP BA OD1 1 179 B B +ATOM 9385 O OD2 . ASP BA 1 179 ? -51.010 11.432 50.472 1.0 87.02 ? ? ? ? ? ? 296 ASP BA OD2 1 179 B B +ATOM 9386 N N . ARG BA 1 180 ? -50.747 15.348 50.616 1.0 66.35 ? ? ? ? ? ? 297 ARG BA N 1 180 B B +ATOM 9387 C CA . ARG BA 1 180 ? -49.605 15.856 49.864 1.0 61.68 ? ? ? ? ? ? 297 ARG BA CA 1 180 B B +ATOM 9388 C C . ARG BA 1 180 ? -48.999 14.881 48.859 1.0 59.82 ? ? ? ? ? ? 297 ARG BA C 1 180 B B +ATOM 9389 O O . ARG BA 1 180 ? -48.831 15.212 47.686 1.0 49.35 ? ? ? ? ? ? 297 ARG BA O 1 180 B B +ATOM 9390 C CB . ARG BA 1 180 ? -48.517 16.302 50.841 1.0 74.84 ? ? ? ? ? ? 297 ARG BA CB 1 180 B B +ATOM 9391 C CG . ARG BA 1 180 ? -47.215 16.684 50.180 1.0 80.99 ? ? ? ? ? ? 297 ARG BA CG 1 180 B B +ATOM 9392 C CD . ARG BA 1 180 ? -47.297 18.087 49.627 1.0 94.19 ? ? ? ? ? ? 297 ARG BA CD 1 180 B B +ATOM 9393 N NE . ARG BA 1 180 ? -46.056 18.481 48.969 1.0 100.0 ? ? ? ? ? ? 297 ARG BA NE 1 180 B B +ATOM 9394 C CZ . ARG BA 1 180 ? -44.942 18.823 49.609 1.0 100.0 ? ? ? ? ? ? 297 ARG BA CZ 1 180 B B +ATOM 9395 N NH1 . ARG BA 1 180 ? -44.905 18.818 50.936 1.0 100.0 ? ? ? ? ? ? 297 ARG BA NH1 1 180 B B +ATOM 9396 N NH2 . ARG BA 1 180 ? -43.863 19.171 48.918 1.0 100.0 ? ? ? ? ? ? 297 ARG BA NH2 1 180 B B +ATOM 9397 N N . SER BA 1 181 ? -48.657 13.687 49.325 1.0 62.25 ? ? ? ? ? ? 298 SER BA N 1 181 B B +ATOM 9398 C CA . SER BA 1 181 ? -48.049 12.683 48.463 1.0 74.66 ? ? ? ? ? ? 298 SER BA CA 1 181 B B +ATOM 9399 C C . SER BA 1 181 ? -48.977 12.197 47.356 1.0 74.28 ? ? ? ? ? ? 298 SER BA C 1 181 B B +ATOM 9400 O O . SER BA 1 181 ? -48.532 11.941 46.236 1.0 69.21 ? ? ? ? ? ? 298 SER BA O 1 181 B B +ATOM 9401 C CB . SER BA 1 181 ? -47.580 11.488 49.301 1.0 88.66 ? ? ? ? ? ? 298 SER BA CB 1 181 B B +ATOM 9402 O OG . SER BA 1 181 ? -46.710 11.899 50.345 1.0 96.26 ? ? ? ? ? ? 298 SER BA OG 1 181 B B +ATOM 9403 N N . PHE BA 1 182 ? -50.266 12.073 47.666 1.0 69.97 ? ? ? ? ? ? 299 PHE BA N 1 182 B B +ATOM 9404 C CA . PHE BA 1 182 ? -51.237 11.601 46.683 1.0 68.19 ? ? ? ? ? ? 299 PHE BA CA 1 182 B B +ATOM 9405 C C . PHE BA 1 182 ? -51.419 12.570 45.518 1.0 72.62 ? ? ? ? ? ? 299 PHE BA C 1 182 B B +ATOM 9406 O O . PHE BA 1 182 ? -51.529 12.149 44.366 1.0 71.2 ? ? ? ? ? ? 299 PHE BA O 1 182 B B +ATOM 9407 C CB . PHE BA 1 182 ? -52.593 11.346 47.347 1.0 62.01 ? ? ? ? ? ? 299 PHE BA CB 1 182 B B +ATOM 9408 C CG . PHE BA 1 182 ? -53.590 10.679 46.440 1.0 80.44 ? ? ? ? ? ? 299 PHE BA CG 1 182 B B +ATOM 9409 C CD1 . PHE BA 1 182 ? -53.818 9.308 46.519 1.0 85.38 ? ? ? ? ? ? 299 PHE BA CD1 1 182 B B +ATOM 9410 C CD2 . PHE BA 1 182 ? -54.297 11.419 45.498 1.0 94.09 ? ? ? ? ? ? 299 PHE BA CD2 1 182 B B +ATOM 9411 C CE1 . PHE BA 1 182 ? -54.735 8.684 45.670 1.0 86.12 ? ? ? ? ? ? 299 PHE BA CE1 1 182 B B +ATOM 9412 C CE2 . PHE BA 1 182 ? -55.215 10.806 44.646 1.0 93.02 ? ? ? ? ? ? 299 PHE BA CE2 1 182 B B +ATOM 9413 C CZ . PHE BA 1 182 ? -55.435 9.437 44.733 1.0 91.75 ? ? ? ? ? ? 299 PHE BA CZ 1 182 B B +ATOM 9414 N N . ALA BA 1 183 ? -51.455 13.863 45.819 1.0 74.86 ? ? ? ? ? ? 300 ALA BA N 1 183 B B +ATOM 9415 C CA . ALA BA 1 183 ? -51.630 14.885 44.791 1.0 72.38 ? ? ? ? ? ? 300 ALA BA CA 1 183 B B +ATOM 9416 C C . ALA BA 1 183 ? -50.547 14.816 43.713 1.0 73.94 ? ? ? ? ? ? 300 ALA BA C 1 183 B B +ATOM 9417 O O . ALA BA 1 183 ? -50.858 14.701 42.526 1.0 79.9 ? ? ? ? ? ? 300 ALA BA O 1 183 B B +ATOM 9418 C CB . ALA BA 1 183 ? -51.647 16.271 45.427 1.0 64.49 ? ? ? ? ? ? 300 ALA BA CB 1 183 B B +ATOM 9419 N N . GLN BA 1 184 ? -49.281 14.889 44.120 1.0 60.82 ? ? ? ? ? ? 301 GLN BA N 1 184 B B +ATOM 9420 C CA . GLN BA 1 184 ? -48.175 14.826 43.166 1.0 59.12 ? ? ? ? ? ? 301 GLN BA CA 1 184 B B +ATOM 9421 C C . GLN BA 1 184 ? -48.326 13.562 42.332 1.0 52.85 ? ? ? ? ? ? 301 GLN BA C 1 184 B B +ATOM 9422 O O . GLN BA 1 184 ? -48.144 13.576 41.114 1.0 42.05 ? ? ? ? ? ? 301 GLN BA O 1 184 B B +ATOM 9423 C CB . GLN BA 1 184 ? -46.838 14.795 43.904 1.0 75.11 ? ? ? ? ? ? 301 GLN BA CB 1 184 B B +ATOM 9424 C CG . GLN BA 1 184 ? -46.613 15.969 44.831 1.0 97.35 ? ? ? ? ? ? 301 GLN BA CG 1 184 B B +ATOM 9425 C CD . GLN BA 1 184 ? -45.391 15.777 45.704 1.0 100.0 ? ? ? ? ? ? 301 GLN BA CD 1 184 B B +ATOM 9426 O OE1 . GLN BA 1 184 ? -45.039 14.650 46.055 1.0 100.0 ? ? ? ? ? ? 301 GLN BA OE1 1 184 B B +ATOM 9427 N NE2 . GLN BA 1 184 ? -44.734 16.876 46.057 1.0 97.11 ? ? ? ? ? ? 301 GLN BA NE2 1 184 B B +ATOM 9428 N N . PHE BA 1 185 ? -48.661 12.470 43.012 1.0 49.6 ? ? ? ? ? ? 302 PHE BA N 1 185 B B +ATOM 9429 C CA . PHE BA 1 185 ? -48.858 11.175 42.371 1.0 54.69 ? ? ? ? ? ? 302 PHE BA CA 1 185 B B +ATOM 9430 C C . PHE BA 1 185 ? -49.894 11.308 41.252 1.0 59.93 ? ? ? ? ? ? 302 PHE BA C 1 185 B B +ATOM 9431 O O . PHE BA 1 185 ? -49.627 10.973 40.095 1.0 61.04 ? ? ? ? ? ? 302 PHE BA O 1 185 B B +ATOM 9432 C CB . PHE BA 1 185 ? -49.314 10.152 43.426 1.0 46.54 ? ? ? ? ? ? 302 PHE BA CB 1 185 B B +ATOM 9433 C CG . PHE BA 1 185 ? -49.983 8.929 42.858 1.0 61.15 ? ? ? ? ? ? 302 PHE BA CG 1 185 B B +ATOM 9434 C CD1 . PHE BA 1 185 ? -49.521 8.331 41.689 1.0 59.47 ? ? ? ? ? ? 302 PHE BA CD1 1 185 B B +ATOM 9435 C CD2 . PHE BA 1 185 ? -51.076 8.366 43.508 1.0 66.45 ? ? ? ? ? ? 302 PHE BA CD2 1 185 B B +ATOM 9436 C CE1 . PHE BA 1 185 ? -50.141 7.194 41.182 1.0 59.27 ? ? ? ? ? ? 302 PHE BA CE1 1 185 B B +ATOM 9437 C CE2 . PHE BA 1 185 ? -51.698 7.232 43.008 1.0 72.43 ? ? ? ? ? ? 302 PHE BA CE2 1 185 B B +ATOM 9438 C CZ . PHE BA 1 185 ? -51.230 6.644 41.843 1.0 66.68 ? ? ? ? ? ? 302 PHE BA CZ 1 185 B B +ATOM 9439 N N . SER BA 1 186 ? -51.078 11.799 41.606 1.0 60.89 ? ? ? ? ? ? 303 SER BA N 1 186 B B +ATOM 9440 C CA . SER BA 1 186 ? -52.151 11.989 40.641 1.0 54.2 ? ? ? ? ? ? 303 SER BA CA 1 186 B B +ATOM 9441 C C . SER BA 1 186 ? -51.638 12.845 39.489 1.0 47.38 ? ? ? ? ? ? 303 SER BA C 1 186 B B +ATOM 9442 O O . SER BA 1 186 ? -51.737 12.470 38.322 1.0 54.63 ? ? ? ? ? ? 303 SER BA O 1 186 B B +ATOM 9443 C CB . SER BA 1 186 ? -53.346 12.687 41.308 1.0 45.16 ? ? ? ? ? ? 303 SER BA CB 1 186 B B +ATOM 9444 O OG . SER BA 1 186 ? -53.862 11.919 42.382 1.0 39.85 ? ? ? ? ? ? 303 SER BA OG 1 186 B B +ATOM 9445 N N . GLN BA 1 187 ? -51.080 13.999 39.833 1.0 22.0 ? ? ? ? ? ? 304 GLN BA N 1 187 B B +ATOM 9446 C CA . GLN BA 1 187 ? -50.557 14.927 38.843 1.0 25.19 ? ? ? ? ? ? 304 GLN BA CA 1 187 B B +ATOM 9447 C C . GLN BA 1 187 ? -49.609 14.260 37.858 1.0 38.37 ? ? ? ? ? ? 304 GLN BA C 1 187 B B +ATOM 9448 O O . GLN BA 1 187 ? -49.596 14.600 36.674 1.0 53.2 ? ? ? ? ? ? 304 GLN BA O 1 187 B B +ATOM 9449 C CB . GLN BA 1 187 ? -49.835 16.077 39.534 1.0 7.89 ? ? ? ? ? ? 304 GLN BA CB 1 187 B B +ATOM 9450 C CG . GLN BA 1 187 ? -49.452 17.203 38.602 1.0 5.59 ? ? ? ? ? ? 304 GLN BA CG 1 187 B B +ATOM 9451 C CD . GLN BA 1 187 ? -49.025 18.439 39.354 1.0 17.21 ? ? ? ? ? ? 304 GLN BA CD 1 187 B B +ATOM 9452 O OE1 . GLN BA 1 187 ? -48.809 18.394 40.563 1.0 27.54 ? ? ? ? ? ? 304 GLN BA OE1 1 187 B B +ATOM 9453 N NE2 . GLN BA 1 187 ? -48.906 19.555 38.646 1.0 18.31 ? ? ? ? ? ? 304 GLN BA NE2 1 187 B B +ATOM 9454 N N . GLU BA 1 188 ? -48.804 13.323 38.351 1.0 43.72 ? ? ? ? ? ? 305 GLU BA N 1 188 B B +ATOM 9455 C CA . GLU BA 1 188 ? -47.860 12.610 37.497 1.0 61.99 ? ? ? ? ? ? 305 GLU BA CA 1 188 B B +ATOM 9456 C C . GLU BA 1 188 ? -48.616 11.974 36.336 1.0 69.94 ? ? ? ? ? ? 305 GLU BA C 1 188 B B +ATOM 9457 O O . GLU BA 1 188 ? -48.249 12.147 35.172 1.0 75.09 ? ? ? ? ? ? 305 GLU BA O 1 188 B B +ATOM 9458 C CB . GLU BA 1 188 ? -47.137 11.526 38.296 1.0 71.67 ? ? ? ? ? ? 305 GLU BA CB 1 188 B B +ATOM 9459 C CG . GLU BA 1 188 ? -46.142 12.061 39.310 1.0 74.16 ? ? ? ? ? ? 305 GLU BA CG 1 188 B B +ATOM 9460 C CD . GLU BA 1 188 ? -45.144 13.028 38.702 1.0 80.11 ? ? ? ? ? ? 305 GLU BA CD 1 188 B B +ATOM 9461 O OE1 . GLU BA 1 188 ? -44.936 14.109 39.289 1.0 94.32 ? ? ? ? ? ? 305 GLU BA OE1 1 188 B B +ATOM 9462 O OE2 . GLU BA 1 188 ? -44.570 12.711 37.641 1.0 74.94 ? ? ? ? ? ? 305 GLU BA OE2 1 188 B B +ATOM 9463 N N . ILE BA 1 189 ? -49.672 11.234 36.662 1.0 56.48 ? ? ? ? ? ? 306 ILE BA N 1 189 B B +ATOM 9464 C CA . ILE BA 1 189 ? -50.489 10.581 35.648 1.0 52.28 ? ? ? ? ? ? 306 ILE BA CA 1 189 B B +ATOM 9465 C C . ILE BA 1 189 ? -51.012 11.615 34.655 1.0 57.18 ? ? ? ? ? ? 306 ILE BA C 1 189 B B +ATOM 9466 O O . ILE BA 1 189 ? -51.030 11.381 33.444 1.0 64.85 ? ? ? ? ? ? 306 ILE BA O 1 189 B B +ATOM 9467 C CB . ILE BA 1 189 ? -51.696 9.862 36.281 1.0 55.36 ? ? ? ? ? ? 306 ILE BA CB 1 189 B B +ATOM 9468 C CG1 . ILE BA 1 189 ? -51.264 9.140 37.561 1.0 60.79 ? ? ? ? ? ? 306 ILE BA CG1 1 189 B B +ATOM 9469 C CG2 . ILE BA 1 189 ? -52.296 8.884 35.284 1.0 49.22 ? ? ? ? ? ? 306 ILE BA CG2 1 189 B B +ATOM 9470 C CD1 . ILE BA 1 189 ? -52.401 8.485 38.315 1.0 62.48 ? ? ? ? ? ? 306 ILE BA CD1 1 189 B B +ATOM 9471 N N . GLY BA 1 190 ? -51.436 12.763 35.179 1.0 48.52 ? ? ? ? ? ? 307 GLY BA N 1 190 B B +ATOM 9472 C CA . GLY BA 1 190 ? -51.956 13.816 34.329 1.0 57.63 ? ? ? ? ? ? 307 GLY BA CA 1 190 B B +ATOM 9473 C C . GLY BA 1 190 ? -50.910 14.286 33.344 1.0 60.82 ? ? ? ? ? ? 307 GLY BA C 1 190 B B +ATOM 9474 O O . GLY BA 1 190 ? -51.178 14.425 32.150 1.0 57.71 ? ? ? ? ? ? 307 GLY BA O 1 190 B B +ATOM 9475 N N . LEU BA 1 191 ? -49.704 14.516 33.855 1.0 64.07 ? ? ? ? ? ? 308 LEU BA N 1 191 B B +ATOM 9476 C CA . LEU BA 1 191 ? -48.592 14.972 33.033 1.0 55.82 ? ? ? ? ? ? 308 LEU BA CA 1 191 B B +ATOM 9477 C C . LEU BA 1 191 ? -48.190 13.874 32.054 1.0 53.47 ? ? ? ? ? ? 308 LEU BA C 1 191 B B +ATOM 9478 O O . LEU BA 1 191 ? -47.701 14.150 30.959 1.0 46.25 ? ? ? ? ? ? 308 LEU BA O 1 191 B B +ATOM 9479 C CB . LEU BA 1 191 ? -47.419 15.358 33.932 1.0 42.02 ? ? ? ? ? ? 308 LEU BA CB 1 191 B B +ATOM 9480 C CG . LEU BA 1 191 ? -47.736 16.583 34.795 1.0 47.91 ? ? ? ? ? ? 308 LEU BA CG 1 191 B B +ATOM 9481 C CD1 . LEU BA 1 191 ? -47.193 16.386 36.192 1.0 40.23 ? ? ? ? ? ? 308 LEU BA CD1 1 191 B B +ATOM 9482 C CD2 . LEU BA 1 191 ? -47.150 17.828 34.146 1.0 45.13 ? ? ? ? ? ? 308 LEU BA CD2 1 191 B B +ATOM 9483 N N . ALA BA 1 192 ? -48.405 12.626 32.461 1.0 49.57 ? ? ? ? ? ? 309 ALA BA N 1 192 B B +ATOM 9484 C CA . ALA BA 1 192 ? -48.087 11.477 31.622 1.0 42.49 ? ? ? ? ? ? 309 ALA BA CA 1 192 B B +ATOM 9485 C C . ALA BA 1 192 ? -49.036 11.427 30.428 1.0 41.22 ? ? ? ? ? ? 309 ALA BA C 1 192 B B +ATOM 9486 O O . ALA BA 1 192 ? -48.610 11.405 29.273 1.0 46.77 ? ? ? ? ? ? 309 ALA BA O 1 192 B B +ATOM 9487 C CB . ALA BA 1 192 ? -48.208 10.196 32.432 1.0 31.59 ? ? ? ? ? ? 309 ALA BA CB 1 192 B B +ATOM 9488 N N . SER BA 1 193 ? -50.329 11.420 30.728 1.0 33.82 ? ? ? ? ? ? 310 SER BA N 1 193 B B +ATOM 9489 C CA . SER BA 1 193 ? -51.372 11.357 29.717 1.0 40.75 ? ? ? ? ? ? 310 SER BA CA 1 193 B B +ATOM 9490 C C . SER BA 1 193 ? -51.343 12.487 28.689 1.0 39.25 ? ? ? ? ? ? 310 SER BA C 1 193 B B +ATOM 9491 O O . SER BA 1 193 ? -51.916 12.357 27.607 1.0 51.49 ? ? ? ? ? ? 310 SER BA O 1 193 B B +ATOM 9492 C CB . SER BA 1 193 ? -52.743 11.331 30.403 1.0 60.17 ? ? ? ? ? ? 310 SER BA CB 1 193 B B +ATOM 9493 O OG . SER BA 1 193 ? -52.994 12.545 31.092 1.0 62.03 ? ? ? ? ? ? 310 SER BA OG 1 193 B B +ATOM 9494 N N . LEU BA 1 194 ? -50.686 13.592 29.020 1.0 12.02 ? ? ? ? ? ? 311 LEU BA N 1 194 B B +ATOM 9495 C CA . LEU BA 1 194 ? -50.636 14.726 28.101 1.0 47.55 ? ? ? ? ? ? 311 LEU BA CA 1 194 B B +ATOM 9496 C C . LEU BA 1 194 ? -50.015 14.383 26.744 1.0 48.33 ? ? ? ? ? ? 311 LEU BA C 1 194 B B +ATOM 9497 O O . LEU BA 1 194 ? -48.797 14.267 26.614 1.0 59.22 ? ? ? ? ? ? 311 LEU BA O 1 194 B B +ATOM 9498 C CB . LEU BA 1 194 ? -49.881 15.895 28.741 1.0 52.66 ? ? ? ? ? ? 311 LEU BA CB 1 194 B B +ATOM 9499 C CG . LEU BA 1 194 ? -50.564 16.561 29.941 1.0 42.32 ? ? ? ? ? ? 311 LEU BA CG 1 194 B B +ATOM 9500 C CD1 . LEU BA 1 194 ? -49.696 17.688 30.471 1.0 54.87 ? ? ? ? ? ? 311 LEU BA CD1 1 194 B B +ATOM 9501 C CD2 . LEU BA 1 194 ? -51.918 17.098 29.529 1.0 61.47 ? ? ? ? ? ? 311 LEU BA CD2 1 194 B B +ATOM 9502 N N . GLY BA 1 195 ? -50.870 14.226 25.736 1.0 48.49 ? ? ? ? ? ? 312 GLY BA N 1 195 B B +ATOM 9503 C CA . GLY BA 1 195 ? -50.395 13.908 24.402 1.0 55.95 ? ? ? ? ? ? 312 GLY BA CA 1 195 B B +ATOM 9504 C C . GLY BA 1 195 ? -50.014 12.451 24.216 1.0 58.83 ? ? ? ? ? ? 312 GLY BA C 1 195 B B +ATOM 9505 O O . GLY BA 1 195 ? -49.449 12.087 23.186 1.0 54.63 ? ? ? ? ? ? 312 GLY BA O 1 195 B B +ATOM 9506 N N . ALA BA 1 196 ? -50.322 11.616 25.204 1.0 59.26 ? ? ? ? ? ? 313 ALA BA N 1 196 B B +ATOM 9507 C CA . ALA BA 1 196 ? -49.998 10.190 25.134 1.0 79.51 ? ? ? ? ? ? 313 ALA BA CA 1 196 B B +ATOM 9508 C C . ALA BA 1 196 ? -50.906 9.450 24.152 1.0 91.68 ? ? ? ? ? ? 313 ALA BA C 1 196 B B +ATOM 9509 O O . ALA BA 1 196 ? -52.086 9.782 24.007 1.0 100.0 ? ? ? ? ? ? 313 ALA BA O 1 196 B B +ATOM 9510 C CB . ALA BA 1 196 ? -50.106 9.563 26.516 1.0 78.37 ? ? ? ? ? ? 313 ALA BA CB 1 196 B B +ATOM 9511 N N . PRO BA 1 197 ? -50.369 8.422 23.472 1.0 87.52 ? ? ? ? ? ? 314 PRO BA N 1 197 B B +ATOM 9512 C CA . PRO BA 1 197 ? -51.190 7.674 22.513 1.0 80.1 ? ? ? ? ? ? 314 PRO BA CA 1 197 B B +ATOM 9513 C C . PRO BA 1 197 ? -52.259 6.842 23.217 1.0 78.7 ? ? ? ? ? ? 314 PRO BA C 1 197 B B +ATOM 9514 O O . PRO BA 1 197 ? -52.045 6.345 24.326 1.0 56.63 ? ? ? ? ? ? 314 PRO BA O 1 197 B B +ATOM 9515 C CB . PRO BA 1 197 ? -50.178 6.819 21.752 1.0 63.86 ? ? ? ? ? ? 314 PRO BA CB 1 197 B B +ATOM 9516 C CG . PRO BA 1 197 ? -49.031 6.668 22.687 1.0 49.98 ? ? ? ? ? ? 314 PRO BA CG 1 197 B B +ATOM 9517 C CD . PRO BA 1 197 ? -48.999 7.887 23.572 1.0 71.57 ? ? ? ? ? ? 314 PRO BA CD 1 197 B B +ATOM 9518 N N . ASP BA 1 198 ? -53.403 6.703 22.554 1.0 73.05 ? ? ? ? ? ? 315 ASP BA N 1 198 B B +ATOM 9519 C CA . ASP BA 1 198 ? -54.540 5.960 23.087 1.0 73.98 ? ? ? ? ? ? 315 ASP BA CA 1 198 B B +ATOM 9520 C C . ASP BA 1 198 ? -54.193 4.722 23.912 1.0 78.88 ? ? ? ? ? ? 315 ASP BA C 1 198 B B +ATOM 9521 O O . ASP BA 1 198 ? -54.635 4.591 25.055 1.0 76.97 ? ? ? ? ? ? 315 ASP BA O 1 198 B B +ATOM 9522 C CB . ASP BA 1 198 ? -55.480 5.572 21.944 1.0 71.53 ? ? ? ? ? ? 315 ASP BA CB 1 198 B B +ATOM 9523 C CG . ASP BA 1 198 ? -55.940 6.771 21.141 1.0 79.25 ? ? ? ? ? ? 315 ASP BA CG 1 198 B B +ATOM 9524 O OD1 . ASP BA 1 198 ? -55.184 7.221 20.257 1.0 75.19 ? ? ? ? ? ? 315 ASP BA OD1 1 198 B B +ATOM 9525 O OD2 . ASP BA 1 198 ? -57.058 7.264 21.396 1.0 85.56 ? ? ? ? ? ? 315 ASP BA OD2 1 198 B B +ATOM 9526 N N . GLU BA 1 199 ? -53.409 3.813 23.339 1.0 78.88 ? ? ? ? ? ? 316 GLU BA N 1 199 B B +ATOM 9527 C CA . GLU BA 1 199 ? -53.030 2.587 24.040 1.0 79.73 ? ? ? ? ? ? 316 GLU BA CA 1 199 B B +ATOM 9528 C C . GLU BA 1 199 ? -52.542 2.856 25.451 1.0 72.76 ? ? ? ? ? ? 316 GLU BA C 1 199 B B +ATOM 9529 O O . GLU BA 1 199 ? -52.918 2.154 26.387 1.0 65.25 ? ? ? ? ? ? 316 GLU BA O 1 199 B B +ATOM 9530 C CB . GLU BA 1 199 ? -51.933 1.845 23.279 1.0 79.8 ? ? ? ? ? ? 316 GLU BA CB 1 199 B B +ATOM 9531 C CG . GLU BA 1 199 ? -50.751 2.708 22.914 1.0 99.07 ? ? ? ? ? ? 316 GLU BA CG 1 199 B B +ATOM 9532 C CD . GLU BA 1 199 ? -50.863 3.257 21.510 1.0 100.0 ? ? ? ? ? ? 316 GLU BA CD 1 199 B B +ATOM 9533 O OE1 . GLU BA 1 199 ? -49.810 3.555 20.906 1.0 100.0 ? ? ? ? ? ? 316 GLU BA OE1 1 199 B B +ATOM 9534 O OE2 . GLU BA 1 199 ? -52.005 3.386 21.014 1.0 100.0 ? ? ? ? ? ? 316 GLU BA OE2 1 199 B B +ATOM 9535 N N . TYR BA 1 200 ? -51.694 3.867 25.599 1.0 72.58 ? ? ? ? ? ? 317 TYR BA N 1 200 B B +ATOM 9536 C CA . TYR BA 1 200 ? -51.152 4.208 26.904 1.0 79.65 ? ? ? ? ? ? 317 TYR BA CA 1 200 B B +ATOM 9537 C C . TYR BA 1 200 ? -52.153 4.977 27.745 1.0 80.27 ? ? ? ? ? ? 317 TYR BA C 1 200 B B +ATOM 9538 O O . TYR BA 1 200 ? -52.147 4.881 28.971 1.0 69.59 ? ? ? ? ? ? 317 TYR BA O 1 200 B B +ATOM 9539 C CB . TYR BA 1 200 ? -49.865 5.013 26.742 1.0 93.84 ? ? ? ? ? ? 317 TYR BA CB 1 200 B B +ATOM 9540 C CG . TYR BA 1 200 ? -48.682 4.142 26.423 1.0 96.59 ? ? ? ? ? ? 317 TYR BA CG 1 200 B B +ATOM 9541 C CD1 . TYR BA 1 200 ? -48.317 3.898 25.101 1.0 96.42 ? ? ? ? ? ? 317 TYR BA CD1 1 200 B B +ATOM 9542 C CD2 . TYR BA 1 200 ? -47.958 3.517 27.438 1.0 84.4 ? ? ? ? ? ? 317 TYR BA CD2 1 200 B B +ATOM 9543 C CE1 . TYR BA 1 200 ? -47.256 3.052 24.794 1.0 99.21 ? ? ? ? ? ? 317 TYR BA CE1 1 200 B B +ATOM 9544 C CE2 . TYR BA 1 200 ? -46.894 2.669 27.146 1.0 95.13 ? ? ? ? ? ? 317 TYR BA CE2 1 200 B B +ATOM 9545 C CZ . TYR BA 1 200 ? -46.551 2.438 25.822 1.0 100.0 ? ? ? ? ? ? 317 TYR BA CZ 1 200 B B +ATOM 9546 O OH . TYR BA 1 200 ? -45.498 1.598 25.533 1.0 100.0 ? ? ? ? ? ? 317 TYR BA OH 1 200 B B +ATOM 9547 N N . ILE BA 1 201 ? -53.000 5.755 27.082 1.0 81.29 ? ? ? ? ? ? 318 ILE BA N 1 201 B B +ATOM 9548 C CA . ILE BA 1 201 ? -54.021 6.518 27.784 1.0 79.03 ? ? ? ? ? ? 318 ILE BA CA 1 201 B B +ATOM 9549 C C . ILE BA 1 201 ? -54.908 5.511 28.514 1.0 85.15 ? ? ? ? ? ? 318 ILE BA C 1 201 B B +ATOM 9550 O O . ILE BA 1 201 ? -55.190 5.652 29.704 1.0 77.47 ? ? ? ? ? ? 318 ILE BA O 1 201 B B +ATOM 9551 C CB . ILE BA 1 201 ? -54.893 7.323 26.798 1.0 74.45 ? ? ? ? ? ? 318 ILE BA CB 1 201 B B +ATOM 9552 C CG1 . ILE BA 1 201 ? -54.139 8.567 26.330 1.0 56.83 ? ? ? ? ? ? 318 ILE BA CG1 1 201 B B +ATOM 9553 C CG2 . ILE BA 1 201 ? -56.210 7.710 27.459 1.0 78.83 ? ? ? ? ? ? 318 ILE BA CG2 1 201 B B +ATOM 9554 C CD1 . ILE BA 1 201 ? -53.944 9.607 27.411 1.0 79.43 ? ? ? ? ? ? 318 ILE BA CD1 1 201 B B +ATOM 9555 N N . GLU BA 1 202 ? -55.338 4.493 27.776 1.0 88.63 ? ? ? ? ? ? 319 GLU BA N 1 202 B B +ATOM 9556 C CA . GLU BA 1 202 ? -56.189 3.440 28.315 1.0 92.74 ? ? ? ? ? ? 319 GLU BA CA 1 202 B B +ATOM 9557 C C . GLU BA 1 202 ? -55.459 2.680 29.418 1.0 86.1 ? ? ? ? ? ? 319 GLU BA C 1 202 B B +ATOM 9558 O O . GLU BA 1 202 ? -56.059 2.285 30.419 1.0 76.49 ? ? ? ? ? ? 319 GLU BA O 1 202 B B +ATOM 9559 C CB . GLU BA 1 202 ? -56.596 2.481 27.194 1.0 96.66 ? ? ? ? ? ? 319 GLU BA CB 1 202 B B +ATOM 9560 C CG . GLU BA 1 202 ? -57.543 1.383 27.628 1.0 100.0 ? ? ? ? ? ? 319 GLU BA CG 1 202 B B +ATOM 9561 C CD . GLU BA 1 202 ? -57.000 0.000 27.323 1.0 100.0 ? ? ? ? ? ? 319 GLU BA CD 1 202 B B +ATOM 9562 O OE1 . GLU BA 1 202 ? -57.510 -0.644 26.381 1.0 100.0 ? ? ? ? ? ? 319 GLU BA OE1 1 202 B B +ATOM 9563 O OE2 . GLU BA 1 202 ? -56.061 -0.439 28.025 1.0 99.05 ? ? ? ? ? ? 319 GLU BA OE2 1 202 B B +ATOM 9564 N N . LYS BA 1 203 ? -54.160 2.476 29.219 1.0 87.1 ? ? ? ? ? ? 320 LYS BA N 1 203 B B +ATOM 9565 C CA . LYS BA 1 203 ? -53.325 1.778 30.191 1.0 92.68 ? ? ? ? ? ? 320 LYS BA CA 1 203 B B +ATOM 9566 C C . LYS BA 1 203 ? -53.287 2.564 31.500 1.0 88.4 ? ? ? ? ? ? 320 LYS BA C 1 203 B B +ATOM 9567 O O . LYS BA 1 203 ? -53.409 1.990 32.582 1.0 70.36 ? ? ? ? ? ? 320 LYS BA O 1 203 B B +ATOM 9568 C CB . LYS BA 1 203 ? -51.902 1.620 29.652 1.0 100.0 ? ? ? ? ? ? 320 LYS BA CB 1 203 B B +ATOM 9569 C CG . LYS BA 1 203 ? -51.727 0.494 28.645 1.0 100.0 ? ? ? ? ? ? 320 LYS BA CG 1 203 B B +ATOM 9570 C CD . LYS BA 1 203 ? -50.278 0.404 28.185 1.0 100.0 ? ? ? ? ? ? 320 LYS BA CD 1 203 B B +ATOM 9571 C CE . LYS BA 1 203 ? -50.059 -0.753 27.222 1.0 96.33 ? ? ? ? ? ? 320 LYS BA CE 1 203 B B +ATOM 9572 N NZ . LYS BA 1 203 ? -48.656 -0.797 26.717 1.0 59.54 ? ? ? ? ? ? 320 LYS BA NZ 1 203 B B +ATOM 9573 N N . LEU BA 1 204 ? -53.117 3.880 31.394 1.0 85.57 ? ? ? ? ? ? 321 LEU BA N 1 204 B B +ATOM 9574 C CA . LEU BA 1 204 ? -53.073 4.745 32.570 1.0 79.11 ? ? ? ? ? ? 321 LEU BA CA 1 204 B B +ATOM 9575 C C . LEU BA 1 204 ? -54.419 4.688 33.289 1.0 77.76 ? ? ? ? ? ? 321 LEU BA C 1 204 B B +ATOM 9576 O O . LEU BA 1 204 ? -54.471 4.554 34.513 1.0 54.13 ? ? ? ? ? ? 321 LEU BA O 1 204 B B +ATOM 9577 C CB . LEU BA 1 204 ? -52.766 6.190 32.164 1.0 75.56 ? ? ? ? ? ? 321 LEU BA CB 1 204 B B +ATOM 9578 C CG . LEU BA 1 204 ? -51.326 6.486 31.743 1.0 69.23 ? ? ? ? ? ? 321 LEU BA CG 1 204 B B +ATOM 9579 C CD1 . LEU BA 1 204 ? -51.308 7.706 30.838 1.0 72.14 ? ? ? ? ? ? 321 LEU BA CD1 1 204 B B +ATOM 9580 C CD2 . LEU BA 1 204 ? -50.461 6.705 32.974 1.0 32.48 ? ? ? ? ? ? 321 LEU BA CD2 1 204 B B +ATOM 9581 N N . ALA BA 1 205 ? -55.503 4.798 32.523 1.0 72.88 ? ? ? ? ? ? 322 ALA BA N 1 205 B B +ATOM 9582 C CA . ALA BA 1 205 ? -56.844 4.738 33.095 1.0 68.29 ? ? ? ? ? ? 322 ALA BA CA 1 205 B B +ATOM 9583 C C . ALA BA 1 205 ? -56.934 3.468 33.925 1.0 70.79 ? ? ? ? ? ? 322 ALA BA C 1 205 B B +ATOM 9584 O O . ALA BA 1 205 ? -57.331 3.497 35.088 1.0 76.89 ? ? ? ? ? ? 322 ALA BA O 1 205 B B +ATOM 9585 C CB . ALA BA 1 205 ? -57.893 4.715 31.991 1.0 56.42 ? ? ? ? ? ? 322 ALA BA CB 1 205 B B +ATOM 9586 N N . THR BA 1 206 ? -56.542 2.351 33.319 1.0 76.29 ? ? ? ? ? ? 323 THR BA N 1 206 B B +ATOM 9587 C CA . THR BA 1 206 ? -56.571 1.063 33.998 1.0 94.13 ? ? ? ? ? ? 323 THR BA CA 1 206 B B +ATOM 9588 C C . THR BA 1 206 ? -55.763 1.116 35.298 1.0 96.35 ? ? ? ? ? ? 323 THR BA C 1 206 B B +ATOM 9589 O O . THR BA 1 206 ? -56.152 0.521 36.308 1.0 98.99 ? ? ? ? ? ? 323 THR BA O 1 206 B B +ATOM 9590 C CB . THR BA 1 206 ? -56.007 -0.049 33.093 1.0 100.0 ? ? ? ? ? ? 323 THR BA CB 1 206 B B +ATOM 9591 O OG1 . THR BA 1 206 ? -56.564 0.075 31.776 1.0 100.0 ? ? ? ? ? ? 323 THR BA OG1 1 206 B B +ATOM 9592 C CG2 . THR BA 1 206 ? -56.354 -1.418 33.658 1.0 100.0 ? ? ? ? ? ? 323 THR BA CG2 1 206 B B +ATOM 9593 N N . ILE BA 1 207 ? -54.634 1.819 35.266 1.0 91.07 ? ? ? ? ? ? 324 ILE BA N 1 207 B B +ATOM 9594 C CA . ILE BA 1 207 ? -53.796 1.956 36.453 1.0 86.66 ? ? ? ? ? ? 324 ILE BA CA 1 207 B B +ATOM 9595 C C . ILE BA 1 207 ? -54.562 2.806 37.456 1.0 84.53 ? ? ? ? ? ? 324 ILE BA C 1 207 B B +ATOM 9596 O O . ILE BA 1 207 ? -54.679 2.453 38.626 1.0 75.58 ? ? ? ? ? ? 324 ILE BA O 1 207 B B +ATOM 9597 C CB . ILE BA 1 207 ? -52.467 2.665 36.129 1.0 88.67 ? ? ? ? ? ? 324 ILE BA CB 1 207 B B +ATOM 9598 C CG1 . ILE BA 1 207 ? -51.698 1.879 35.065 1.0 74.72 ? ? ? ? ? ? 324 ILE BA CG1 1 207 B B +ATOM 9599 C CG2 . ILE BA 1 207 ? -51.633 2.811 37.398 1.0 81.43 ? ? ? ? ? ? 324 ILE BA CG2 1 207 B B +ATOM 9600 C CD1 . ILE BA 1 207 ? -51.320 0.476 35.493 1.0 59.98 ? ? ? ? ? ? 324 ILE BA CD1 1 207 B B +ATOM 9601 N N . TYR BA 1 208 ? -55.078 3.930 36.970 1.0 84.3 ? ? ? ? ? ? 325 TYR BA N 1 208 B B +ATOM 9602 C CA . TYR BA 1 208 ? -55.859 4.862 37.779 1.0 87.69 ? ? ? ? ? ? 325 TYR BA CA 1 208 B B +ATOM 9603 C C . TYR BA 1 208 ? -56.924 4.093 38.559 1.0 84.03 ? ? ? ? ? ? 325 TYR BA C 1 208 B B +ATOM 9604 O O . TYR BA 1 208 ? -57.273 4.445 39.686 1.0 63.33 ? ? ? ? ? ? 325 TYR BA O 1 208 B B +ATOM 9605 C CB . TYR BA 1 208 ? -56.516 5.894 36.853 1.0 94.13 ? ? ? ? ? ? 325 TYR BA CB 1 208 B B +ATOM 9606 C CG . TYR BA 1 208 ? -57.414 6.904 37.532 1.0 100.0 ? ? ? ? ? ? 325 TYR BA CG 1 208 B B +ATOM 9607 C CD1 . TYR BA 1 208 ? -58.787 6.674 37.658 1.0 100.0 ? ? ? ? ? ? 325 TYR BA CD1 1 208 B B +ATOM 9608 C CD2 . TYR BA 1 208 ? -56.902 8.117 37.999 1.0 100.0 ? ? ? ? ? ? 325 TYR BA CD2 1 208 B B +ATOM 9609 C CE1 . TYR BA 1 208 ? -59.630 7.629 38.227 1.0 100.0 ? ? ? ? ? ? 325 TYR BA CE1 1 208 B B +ATOM 9610 C CE2 . TYR BA 1 208 ? -57.733 9.079 38.569 1.0 100.0 ? ? ? ? ? ? 325 TYR BA CE2 1 208 B B +ATOM 9611 C CZ . TYR BA 1 208 ? -59.095 8.829 38.678 1.0 100.0 ? ? ? ? ? ? 325 TYR BA CZ 1 208 B B +ATOM 9612 O OH . TYR BA 1 208 ? -59.920 9.786 39.223 1.0 100.0 ? ? ? ? ? ? 325 TYR BA OH 1 208 B B +ATOM 9613 N N . TRP BA 1 209 ? -57.433 3.034 37.940 1.0 84.11 ? ? ? ? ? ? 326 TRP BA N 1 209 B B +ATOM 9614 C CA . TRP BA 1 209 ? -58.448 2.196 38.551 1.0 86.01 ? ? ? ? ? ? 326 TRP BA CA 1 209 B B +ATOM 9615 C C . TRP BA 1 209 ? -57.875 1.428 39.732 1.0 87.9 ? ? ? ? ? ? 326 TRP BA C 1 209 B B +ATOM 9616 O O . TRP BA 1 209 ? -58.253 1.662 40.875 1.0 85.81 ? ? ? ? ? ? 326 TRP BA O 1 209 B B +ATOM 9617 C CB . TRP BA 1 209 ? -58.994 1.210 37.514 1.0 85.17 ? ? ? ? ? ? 326 TRP BA CB 1 209 B B +ATOM 9618 C CG . TRP BA 1 209 ? -60.257 0.514 37.932 1.0 99.7 ? ? ? ? ? ? 326 TRP BA CG 1 209 B B +ATOM 9619 C CD1 . TRP BA 1 209 ? -60.360 -0.679 38.591 1.0 100.0 ? ? ? ? ? ? 326 TRP BA CD1 1 209 B B +ATOM 9620 C CD2 . TRP BA 1 209 ? -61.602 0.950 37.684 1.0 100.0 ? ? ? ? ? ? 326 TRP BA CD2 1 209 B B +ATOM 9621 N NE1 . TRP BA 1 209 ? -61.683 -1.017 38.763 1.0 100.0 ? ? ? ? ? ? 326 TRP BA NE1 1 209 B B +ATOM 9622 C CE2 . TRP BA 1 209 ? -62.465 -0.035 38.214 1.0 100.0 ? ? ? ? ? ? 326 TRP BA CE2 1 209 B B +ATOM 9623 C CE3 . TRP BA 1 209 ? -62.158 2.075 37.060 1.0 100.0 ? ? ? ? ? ? 326 TRP BA CE3 1 209 B B +ATOM 9624 C CZ2 . TRP BA 1 209 ? -63.857 0.071 38.144 1.0 98.96 ? ? ? ? ? ? 326 TRP BA CZ2 1 209 B B +ATOM 9625 C CZ3 . TRP BA 1 209 ? -63.545 2.179 36.989 1.0 100.0 ? ? ? ? ? ? 326 TRP BA CZ3 1 209 B B +ATOM 9626 C CH2 . TRP BA 1 209 ? -64.377 1.181 37.529 1.0 100.0 ? ? ? ? ? ? 326 TRP BA CH2 1 209 B B +ATOM 9627 N N . PHE BA 1 210 ? -56.953 0.511 39.445 1.0 88.82 ? ? ? ? ? ? 327 PHE BA N 1 210 B B +ATOM 9628 C CA . PHE BA 1 210 ? -56.328 -0.322 40.475 1.0 93.56 ? ? ? ? ? ? 327 PHE BA CA 1 210 B B +ATOM 9629 C C . PHE BA 1 210 ? -55.484 0.469 41.466 1.0 89.91 ? ? ? ? ? ? 327 PHE BA C 1 210 B B +ATOM 9630 O O . PHE BA 1 210 ? -54.682 -0.098 42.212 1.0 89.17 ? ? ? ? ? ? 327 PHE BA O 1 210 B B +ATOM 9631 C CB . PHE BA 1 210 ? -55.471 -1.405 39.818 1.0 96.8 ? ? ? ? ? ? 327 PHE BA CB 1 210 B B +ATOM 9632 C CG . PHE BA 1 210 ? -56.272 -2.433 39.069 1.0 100.0 ? ? ? ? ? ? 327 PHE BA CG 1 210 B B +ATOM 9633 C CD1 . PHE BA 1 210 ? -57.083 -3.340 39.751 1.0 100.0 ? ? ? ? ? ? 327 PHE BA CD1 1 210 B B +ATOM 9634 C CD2 . PHE BA 1 210 ? -56.221 -2.496 37.678 1.0 100.0 ? ? ? ? ? ? 327 PHE BA CD2 1 210 B B +ATOM 9635 C CE1 . PHE BA 1 210 ? -57.831 -4.292 39.058 1.0 100.0 ? ? ? ? ? ? 327 PHE BA CE1 1 210 B B +ATOM 9636 C CE2 . PHE BA 1 210 ? -56.965 -3.445 36.977 1.0 100.0 ? ? ? ? ? ? 327 PHE BA CE2 1 210 B B +ATOM 9637 C CZ . PHE BA 1 210 ? -57.774 -4.344 37.669 1.0 100.0 ? ? ? ? ? ? 327 PHE BA CZ 1 210 B B +ATOM 9638 N N . THR BA 1 211 ? -55.668 1.780 41.470 1.0 89.94 ? ? ? ? ? ? 328 THR BA N 1 211 B B +ATOM 9639 C CA . THR BA 1 211 ? -54.933 2.643 42.379 1.0 88.6 ? ? ? ? ? ? 328 THR BA CA 1 211 B B +ATOM 9640 C C . THR BA 1 211 ? -55.888 3.631 43.038 1.0 92.98 ? ? ? ? ? ? 328 THR BA C 1 211 B B +ATOM 9641 O O . THR BA 1 211 ? -56.311 3.434 44.175 1.0 71.65 ? ? ? ? ? ? 328 THR BA O 1 211 B B +ATOM 9642 C CB . THR BA 1 211 ? -53.819 3.430 41.633 1.0 88.37 ? ? ? ? ? ? 328 THR BA CB 1 211 B B +ATOM 9643 O OG1 . THR BA 1 211 ? -54.379 4.114 40.504 1.0 87.1 ? ? ? ? ? ? 328 THR BA OG1 1 211 B B +ATOM 9644 C CG2 . THR BA 1 211 ? -52.727 2.489 41.151 1.0 78.14 ? ? ? ? ? ? 328 THR BA CG2 1 211 B B +ATOM 9645 N N . VAL BA 1 212 ? -56.241 4.676 42.298 1.0 100.0 ? ? ? ? ? ? 329 VAL BA N 1 212 B B +ATOM 9646 C CA . VAL BA 1 212 ? -57.139 5.721 42.779 1.0 100.0 ? ? ? ? ? ? 329 VAL BA CA 1 212 B B +ATOM 9647 C C . VAL BA 1 212 ? -58.562 5.227 43.033 1.0 99.41 ? ? ? ? ? ? 329 VAL BA C 1 212 B B +ATOM 9648 O O . VAL BA 1 212 ? -59.167 5.535 44.059 1.0 94.57 ? ? ? ? ? ? 329 VAL BA O 1 212 B B +ATOM 9649 C CB . VAL BA 1 212 ? -57.188 6.909 41.777 1.0 100.0 ? ? ? ? ? ? 329 VAL BA CB 1 212 B B +ATOM 9650 C CG1 . VAL BA 1 212 ? -58.069 8.019 42.325 1.0 100.0 ? ? ? ? ? ? 329 VAL BA CG1 1 212 B B +ATOM 9651 C CG2 . VAL BA 1 212 ? -55.786 7.435 41.536 1.0 89.69 ? ? ? ? ? ? 329 VAL BA CG2 1 212 B B +ATOM 9652 N N . GLU BA 1 213 ? -59.092 4.457 42.093 1.0 98.51 ? ? ? ? ? ? 330 GLU BA N 1 213 B B +ATOM 9653 C CA . GLU BA 1 213 ? -60.448 3.937 42.207 1.0 98.85 ? ? ? ? ? ? 330 GLU BA CA 1 213 B B +ATOM 9654 C C . GLU BA 1 213 ? -60.581 2.730 43.128 1.0 100.0 ? ? ? ? ? ? 330 GLU BA C 1 213 B B +ATOM 9655 O O . GLU BA 1 213 ? -61.335 2.767 44.096 1.0 98.41 ? ? ? ? ? ? 330 GLU BA O 1 213 B B +ATOM 9656 C CB . GLU BA 1 213 ? -60.976 3.594 40.816 1.0 99.44 ? ? ? ? ? ? 330 GLU BA CB 1 213 B B +ATOM 9657 C CG . GLU BA 1 213 ? -61.253 4.816 39.969 1.0 100.0 ? ? ? ? ? ? 330 GLU BA CG 1 213 B B +ATOM 9658 C CD . GLU BA 1 213 ? -62.493 5.558 40.420 1.0 100.0 ? ? ? ? ? ? 330 GLU BA CD 1 213 B B +ATOM 9659 O OE1 . GLU BA 1 213 ? -62.907 6.498 39.710 1.0 100.0 ? ? ? ? ? ? 330 GLU BA OE1 1 213 B B +ATOM 9660 O OE2 . GLU BA 1 213 ? -63.057 5.198 41.477 1.0 100.0 ? ? ? ? ? ? 330 GLU BA OE2 1 213 B B +ATOM 9661 N N . PHE BA 1 214 ? -59.847 1.664 42.826 1.0 100.0 ? ? ? ? ? ? 331 PHE BA N 1 214 B B +ATOM 9662 C CA . PHE BA 1 214 ? -59.899 0.443 43.629 1.0 100.0 ? ? ? ? ? ? 331 PHE BA CA 1 214 B B +ATOM 9663 C C . PHE BA 1 214 ? -58.523 -0.057 44.059 1.0 100.0 ? ? ? ? ? ? 331 PHE BA C 1 214 B B +ATOM 9664 O O . PHE BA 1 214 ? -58.152 -1.201 43.783 1.0 100.0 ? ? ? ? ? ? 331 PHE BA O 1 214 B B +ATOM 9665 C CB . PHE BA 1 214 ? -60.622 -0.662 42.856 1.0 99.38 ? ? ? ? ? ? 331 PHE BA CB 1 214 B B +ATOM 9666 C CG . PHE BA 1 214 ? -62.075 -0.379 42.625 1.0 99.09 ? ? ? ? ? ? 331 PHE BA CG 1 214 B B +ATOM 9667 C CD1 . PHE BA 1 214 ? -62.479 0.444 41.578 1.0 92.66 ? ? ? ? ? ? 331 PHE BA CD1 1 214 B B +ATOM 9668 C CD2 . PHE BA 1 214 ? -63.044 -0.925 43.460 1.0 100.0 ? ? ? ? ? ? 331 PHE BA CD2 1 214 B B +ATOM 9669 C CE1 . PHE BA 1 214 ? -63.826 0.720 41.367 1.0 94.76 ? ? ? ? ? ? 331 PHE BA CE1 1 214 B B +ATOM 9670 C CE2 . PHE BA 1 214 ? -64.396 -0.655 43.258 1.0 100.0 ? ? ? ? ? ? 331 PHE BA CE2 1 214 B B +ATOM 9671 C CZ . PHE BA 1 214 ? -64.786 0.169 42.208 1.0 100.0 ? ? ? ? ? ? 331 PHE BA CZ 1 214 B B +ATOM 9672 N N . GLY BA 1 215 ? -57.771 0.803 44.739 1.0 100.0 ? ? ? ? ? ? 332 GLY BA N 1 215 B B +ATOM 9673 C CA . GLY BA 1 215 ? -56.449 0.419 45.191 1.0 100.0 ? ? ? ? ? ? 332 GLY BA CA 1 215 B B +ATOM 9674 C C . GLY BA 1 215 ? -56.401 0.178 46.686 1.0 100.0 ? ? ? ? ? ? 332 GLY BA C 1 215 B B +ATOM 9675 O O . GLY BA 1 215 ? -57.248 0.676 47.436 1.0 100.0 ? ? ? ? ? ? 332 GLY BA O 1 215 B B +ATOM 9676 N N . LEU BA 1 216 ? -55.407 -0.593 47.116 1.0 100.0 ? ? ? ? ? ? 333 LEU BA N 1 216 B B +ATOM 9677 C CA . LEU BA 1 216 ? -55.213 -0.904 48.527 1.0 100.0 ? ? ? ? ? ? 333 LEU BA CA 1 216 B B +ATOM 9678 C C . LEU BA 1 216 ? -53.779 -0.546 48.889 1.0 100.0 ? ? ? ? ? ? 333 LEU BA C 1 216 B B +ATOM 9679 O O . LEU BA 1 216 ? -52.847 -0.893 48.166 1.0 100.0 ? ? ? ? ? ? 333 LEU BA O 1 216 B B +ATOM 9680 C CB . LEU BA 1 216 ? -55.469 -2.391 48.788 1.0 100.0 ? ? ? ? ? ? 333 LEU BA CB 1 216 B B +ATOM 9681 C CG . LEU BA 1 216 ? -56.928 -2.851 48.666 1.0 100.0 ? ? ? ? ? ? 333 LEU BA CG 1 216 B B +ATOM 9682 C CD1 . LEU BA 1 216 ? -57.007 -4.351 48.888 1.0 100.0 ? ? ? ? ? ? 333 LEU BA CD1 1 216 B B +ATOM 9683 C CD2 . LEU BA 1 216 ? -57.799 -2.123 49.677 1.0 84.61 ? ? ? ? ? ? 333 LEU BA CD2 1 216 B B +ATOM 9684 N N . CYS BA 1 217 ? -53.602 0.145 50.011 1.0 100.0 ? ? ? ? ? ? 334 CYS BA N 1 217 B B +ATOM 9685 C CA . CYS BA 1 217 ? -52.269 0.561 50.436 1.0 100.0 ? ? ? ? ? ? 334 CYS BA CA 1 217 B B +ATOM 9686 C C . CYS BA 1 217 ? -51.679 -0.266 51.573 1.0 100.0 ? ? ? ? ? ? 334 CYS BA C 1 217 B B +ATOM 9687 O O . CYS BA 1 217 ? -52.318 -1.174 52.108 1.0 93.62 ? ? ? ? ? ? 334 CYS BA O 1 217 B B +ATOM 9688 C CB . CYS BA 1 217 ? -52.287 2.034 50.847 1.0 100.0 ? ? ? ? ? ? 334 CYS BA CB 1 217 B B +ATOM 9689 S SG . CYS BA 1 217 ? -53.232 2.367 52.362 1.0 100.0 ? ? ? ? ? ? 334 CYS BA SG 1 217 B B +ATOM 9690 N N . LYS BA 1 218 ? -50.447 0.079 51.934 1.0 100.0 ? ? ? ? ? ? 335 LYS BA N 1 218 B B +ATOM 9691 C CA . LYS BA 1 218 ? -49.718 -0.600 52.998 1.0 100.0 ? ? ? ? ? ? 335 LYS BA CA 1 218 B B +ATOM 9692 C C . LYS BA 1 218 ? -49.599 0.262 54.253 1.0 100.0 ? ? ? ? ? ? 335 LYS BA C 1 218 B B +ATOM 9693 O O . LYS BA 1 218 ? -49.043 1.362 54.213 1.0 97.61 ? ? ? ? ? ? 335 LYS BA O 1 218 B B +ATOM 9694 C CB . LYS BA 1 218 ? -48.318 -0.968 52.506 1.0 100.0 ? ? ? ? ? ? 335 LYS BA CB 1 218 B B +ATOM 9695 C CG . LYS BA 1 218 ? -48.305 -2.070 51.472 1.0 100.0 ? ? ? ? ? ? 335 LYS BA CG 1 218 B B +ATOM 9696 C CD . LYS BA 1 218 ? -47.562 -3.284 51.997 1.0 100.0 ? ? ? ? ? ? 335 LYS BA CD 1 218 B B +ATOM 9697 C CE . LYS BA 1 218 ? -48.499 -4.227 52.743 1.0 100.0 ? ? ? ? ? ? 335 LYS BA CE 1 218 B B +ATOM 9698 N NZ . LYS BA 1 218 ? -48.991 -3.662 54.033 1.0 100.0 ? ? ? ? ? ? 335 LYS BA NZ 1 218 B B +ATOM 9699 N N . GLN BA 1 219 ? -50.113 -0.248 55.367 1.0 95.53 ? ? ? ? ? ? 336 GLN BA N 1 219 B B +ATOM 9700 C CA . GLN BA 1 219 ? -50.055 0.480 56.630 1.0 99.94 ? ? ? ? ? ? 336 GLN BA CA 1 219 B B +ATOM 9701 C C . GLN BA 1 219 ? -49.365 -0.352 57.710 1.0 100.0 ? ? ? ? ? ? 336 GLN BA C 1 219 B B +ATOM 9702 O O . GLN BA 1 219 ? -49.987 -0.754 58.692 1.0 100.0 ? ? ? ? ? ? 336 GLN BA O 1 219 B B +ATOM 9703 C CB . GLN BA 1 219 ? -51.468 0.853 57.083 1.0 97.51 ? ? ? ? ? ? 336 GLN BA CB 1 219 B B +ATOM 9704 C CG . GLN BA 1 219 ? -52.191 1.786 56.121 1.0 100.0 ? ? ? ? ? ? 336 GLN BA CG 1 219 B B +ATOM 9705 C CD . GLN BA 1 219 ? -51.804 3.243 56.316 1.0 100.0 ? ? ? ? ? ? 336 GLN BA CD 1 219 B B +ATOM 9706 O OE1 . GLN BA 1 219 ? -51.179 3.607 57.315 1.0 100.0 ? ? ? ? ? ? 336 GLN BA OE1 1 219 B B +ATOM 9707 N NE2 . GLN BA 1 219 ? -52.179 4.086 55.358 1.0 100.0 ? ? ? ? ? ? 336 GLN BA NE2 1 219 B B +ATOM 9708 N N . GLY BA 1 220 ? -48.071 -0.598 57.519 1.0 100.0 ? ? ? ? ? ? 337 GLY BA N 1 220 B B +ATOM 9709 C CA . GLY BA 1 220 ? -47.307 -1.385 58.471 1.0 93.95 ? ? ? ? ? ? 337 GLY BA CA 1 220 B B +ATOM 9710 C C . GLY BA 1 220 ? -47.238 -2.835 58.031 1.0 97.49 ? ? ? ? ? ? 337 GLY BA C 1 220 B B +ATOM 9711 O O . GLY BA 1 220 ? -46.334 -3.231 57.298 1.0 94.1 ? ? ? ? ? ? 337 GLY BA O 1 220 B B +ATOM 9712 N N . ASP BA 1 221 ? -48.202 -3.630 58.482 1.0 100.0 ? ? ? ? ? ? 338 ASP BA N 1 221 B B +ATOM 9713 C CA . ASP BA 1 221 ? -48.263 -5.043 58.121 1.0 100.0 ? ? ? ? ? ? 338 ASP BA CA 1 221 B B +ATOM 9714 C C . ASP BA 1 221 ? -49.597 -5.284 57.434 1.0 100.0 ? ? ? ? ? ? 338 ASP BA C 1 221 B B +ATOM 9715 O O . ASP BA 1 221 ? -49.693 -6.019 56.449 1.0 100.0 ? ? ? ? ? ? 338 ASP BA O 1 221 B B +ATOM 9716 C CB . ASP BA 1 221 ? -48.180 -5.922 59.371 1.0 100.0 ? ? ? ? ? ? 338 ASP BA CB 1 221 B B +ATOM 9717 C CG . ASP BA 1 221 ? -46.835 -5.829 60.062 1.0 100.0 ? ? ? ? ? ? 338 ASP BA CG 1 221 B B +ATOM 9718 O OD1 . ASP BA 1 221 ? -45.811 -6.109 59.404 1.0 100.0 ? ? ? ? ? ? 338 ASP BA OD1 1 221 B B +ATOM 9719 O OD2 . ASP BA 1 221 ? -46.805 -5.476 61.262 1.0 98.72 ? ? ? ? ? ? 338 ASP BA OD2 1 221 B B +ATOM 9720 N N . SER BA 1 222 ? -50.622 -4.640 57.976 1.0 100.0 ? ? ? ? ? ? 339 SER BA N 1 222 B B +ATOM 9721 C CA . SER BA 1 222 ? -51.978 -4.753 57.464 1.0 100.0 ? ? ? ? ? ? 339 SER BA CA 1 222 B B +ATOM 9722 C C . SER BA 1 222 ? -52.198 -3.967 56.178 1.0 100.0 ? ? ? ? ? ? 339 SER BA C 1 222 B B +ATOM 9723 O O . SER BA 1 222 ? -51.359 -3.158 55.772 1.0 100.0 ? ? ? ? ? ? 339 SER BA O 1 222 B B +ATOM 9724 C CB . SER BA 1 222 ? -52.971 -4.272 58.525 1.0 100.0 ? ? ? ? ? ? 339 SER BA CB 1 222 B B +ATOM 9725 O OG . SER BA 1 222 ? -52.619 -2.982 59.001 1.0 100.0 ? ? ? ? ? ? 339 SER BA OG 1 222 B B +ATOM 9726 N N . ILE BA 1 223 ? -53.343 -4.217 55.551 1.0 100.0 ? ? ? ? ? ? 340 ILE BA N 1 223 B B +ATOM 9727 C CA . ILE BA 1 223 ? -53.718 -3.550 54.314 1.0 100.0 ? ? ? ? ? ? 340 ILE BA CA 1 223 B B +ATOM 9728 C C . ILE BA 1 223 ? -54.991 -2.735 54.521 1.0 100.0 ? ? ? ? ? ? 340 ILE BA C 1 223 B B +ATOM 9729 O O . ILE BA 1 223 ? -55.956 -3.203 55.136 1.0 99.68 ? ? ? ? ? ? 340 ILE BA O 1 223 B B +ATOM 9730 C CB . ILE BA 1 223 ? -53.946 -4.574 53.168 1.0 97.56 ? ? ? ? ? ? 340 ILE BA CB 1 223 B B +ATOM 9731 C CG1 . ILE BA 1 223 ? -52.693 -4.649 52.294 1.0 77.79 ? ? ? ? ? ? 340 ILE BA CG1 1 223 B B +ATOM 9732 C CG2 . ILE BA 1 223 ? -55.162 -4.182 52.331 1.0 89.25 ? ? ? ? ? ? 340 ILE BA CG2 1 223 B B +ATOM 9733 C CD1 . ILE BA 1 223 ? -51.535 -5.371 52.951 1.0 45.99 ? ? ? ? ? ? 340 ILE BA CD1 1 223 B B +ATOM 9734 N N . LYS BA 1 224 ? -54.980 -1.514 53.999 1.0 100.0 ? ? ? ? ? ? 341 LYS BA N 1 224 B B +ATOM 9735 C CA . LYS BA 1 224 ? -56.126 -0.621 54.104 1.0 100.0 ? ? ? ? ? ? 341 LYS BA CA 1 224 B B +ATOM 9736 C C . LYS BA 1 224 ? -56.641 -0.267 52.711 1.0 100.0 ? ? ? ? ? ? 341 LYS BA C 1 224 B B +ATOM 9737 O O . LYS BA 1 224 ? -55.951 -0.478 51.708 1.0 100.0 ? ? ? ? ? ? 341 LYS BA O 1 224 B B +ATOM 9738 C CB . LYS BA 1 224 ? -55.736 0.655 54.853 1.0 99.3 ? ? ? ? ? ? 341 LYS BA CB 1 224 B B +ATOM 9739 C CG . LYS BA 1 224 ? -55.498 0.449 56.337 1.0 92.41 ? ? ? ? ? ? 341 LYS BA CG 1 224 B B +ATOM 9740 C CD . LYS BA 1 224 ? -56.793 0.144 57.065 1.0 94.05 ? ? ? ? ? ? 341 LYS BA CD 1 224 B B +ATOM 9741 C CE . LYS BA 1 224 ? -56.598 0.165 58.570 1.0 96.81 ? ? ? ? ? ? 341 LYS BA CE 1 224 B B +ATOM 9742 N NZ . LYS BA 1 224 ? -55.491 -0.739 58.988 1.0 100.0 ? ? ? ? ? ? 341 LYS BA NZ 1 224 B B +ATOM 9743 N N . ALA BA 1 225 ? -57.858 0.263 52.655 1.0 100.0 ? ? ? ? ? ? 342 ALA BA N 1 225 B B +ATOM 9744 C CA . ALA BA 1 225 ? -58.464 0.651 51.388 1.0 100.0 ? ? ? ? ? ? 342 ALA BA CA 1 225 B B +ATOM 9745 C C . ALA BA 1 225 ? -58.324 2.155 51.180 1.0 100.0 ? ? ? ? ? ? 342 ALA BA C 1 225 B B +ATOM 9746 O O . ALA BA 1 225 ? -58.685 2.948 52.048 1.0 100.0 ? ? ? ? ? ? 342 ALA BA O 1 225 B B +ATOM 9747 C CB . ALA BA 1 225 ? -59.938 0.252 51.368 1.0 100.0 ? ? ? ? ? ? 342 ALA BA CB 1 225 B B +ATOM 9748 N N . TYR BA 1 226 ? -57.782 2.541 50.031 1.0 100.0 ? ? ? ? ? ? 343 TYR BA N 1 226 B B +ATOM 9749 C CA . TYR BA 1 226 ? -57.603 3.953 49.712 1.0 100.0 ? ? ? ? ? ? 343 TYR BA CA 1 226 B B +ATOM 9750 C C . TYR BA 1 226 ? -58.275 4.269 48.383 1.0 100.0 ? ? ? ? ? ? 343 TYR BA C 1 226 B B +ATOM 9751 O O . TYR BA 1 226 ? -58.311 5.421 47.949 1.0 100.0 ? ? ? ? ? ? 343 TYR BA O 1 226 B B +ATOM 9752 C CB . TYR BA 1 226 ? -56.108 4.307 49.661 1.0 100.0 ? ? ? ? ? ? 343 TYR BA CB 1 226 B B +ATOM 9753 C CG . TYR BA 1 226 ? -55.401 3.895 48.388 1.0 100.0 ? ? ? ? ? ? 343 TYR BA CG 1 226 B B +ATOM 9754 C CD1 . TYR BA 1 226 ? -54.836 2.627 48.259 1.0 97.49 ? ? ? ? ? ? 343 TYR BA CD1 1 226 B B +ATOM 9755 C CD2 . TYR BA 1 226 ? -55.291 4.777 47.314 1.0 100.0 ? ? ? ? ? ? 343 TYR BA CD2 1 226 B B +ATOM 9756 C CE1 . TYR BA 1 226 ? -54.179 2.247 47.090 1.0 92.68 ? ? ? ? ? ? 343 TYR BA CE1 1 226 B B +ATOM 9757 C CE2 . TYR BA 1 226 ? -54.638 4.408 46.143 1.0 100.0 ? ? ? ? ? ? 343 TYR BA CE2 1 226 B B +ATOM 9758 C CZ . TYR BA 1 226 ? -54.086 3.141 46.038 1.0 99.5 ? ? ? ? ? ? 343 TYR BA CZ 1 226 B B +ATOM 9759 O OH . TYR BA 1 226 ? -53.451 2.765 44.878 1.0 100.0 ? ? ? ? ? ? 343 TYR BA OH 1 226 B B +ATOM 9760 N N . GLY BA 1 227 ? -58.807 3.231 47.745 1.0 100.0 ? ? ? ? ? ? 344 GLY BA N 1 227 B B +ATOM 9761 C CA . GLY BA 1 227 ? -59.486 3.409 46.476 1.0 96.04 ? ? ? ? ? ? 344 GLY BA CA 1 227 B B +ATOM 9762 C C . GLY BA 1 227 ? -60.756 4.216 46.658 1.0 100.0 ? ? ? ? ? ? 344 GLY BA C 1 227 B B +ATOM 9763 O O . GLY BA 1 227 ? -61.509 4.003 47.611 1.0 91.72 ? ? ? ? ? ? 344 GLY BA O 1 227 B B +ATOM 9764 N N . ALA BA 1 228 ? -60.993 5.147 45.740 1.0 100.0 ? ? ? ? ? ? 345 ALA BA N 1 228 B B +ATOM 9765 C CA . ALA BA 1 228 ? -62.171 6.005 45.796 1.0 94.41 ? ? ? ? ? ? 345 ALA BA CA 1 228 B B +ATOM 9766 C C . ALA BA 1 228 ? -63.446 5.209 45.559 1.0 95.61 ? ? ? ? ? ? 345 ALA BA C 1 228 B B +ATOM 9767 O O . ALA BA 1 228 ? -64.475 5.464 46.185 1.0 95.17 ? ? ? ? ? ? 345 ALA BA O 1 228 B B +ATOM 9768 C CB . ALA BA 1 228 ? -62.047 7.112 44.771 1.0 80.87 ? ? ? ? ? ? 345 ALA BA CB 1 228 B B +ATOM 9769 N N . GLY BA 1 229 ? -63.374 4.243 44.650 1.0 94.4 ? ? ? ? ? ? 346 GLY BA N 1 229 B B +ATOM 9770 C CA . GLY BA 1 229 ? -64.532 3.420 44.364 1.0 95.7 ? ? ? ? ? ? 346 GLY BA CA 1 229 B B +ATOM 9771 C C . GLY BA 1 229 ? -64.845 2.510 45.537 1.0 96.08 ? ? ? ? ? ? 346 GLY BA C 1 229 B B +ATOM 9772 O O . GLY BA 1 229 ? -65.992 2.112 45.735 1.0 100.0 ? ? ? ? ? ? 346 GLY BA O 1 229 B B +ATOM 9773 N N . LEU BA 1 230 ? -63.820 2.177 46.314 1.0 90.98 ? ? ? ? ? ? 347 LEU BA N 1 230 B B +ATOM 9774 C CA . LEU BA 1 230 ? -63.979 1.311 47.478 1.0 93.82 ? ? ? ? ? ? 347 LEU BA CA 1 230 B B +ATOM 9775 C C . LEU BA 1 230 ? -64.620 2.058 48.642 1.0 98.26 ? ? ? ? ? ? 347 LEU BA C 1 230 B B +ATOM 9776 O O . LEU BA 1 230 ? -65.589 1.590 49.236 1.0 100.0 ? ? ? ? ? ? 347 LEU BA O 1 230 B B +ATOM 9777 C CB . LEU BA 1 230 ? -62.620 0.776 47.937 1.0 96.72 ? ? ? ? ? ? 347 LEU BA CB 1 230 B B +ATOM 9778 C CG . LEU BA 1 230 ? -61.827 -0.111 46.976 1.0 100.0 ? ? ? ? ? ? 347 LEU BA CG 1 230 B B +ATOM 9779 C CD1 . LEU BA 1 230 ? -60.403 -0.263 47.497 1.0 96.93 ? ? ? ? ? ? 347 LEU BA CD1 1 230 B B +ATOM 9780 C CD2 . LEU BA 1 230 ? -62.504 -1.468 46.842 1.0 100.0 ? ? ? ? ? ? 347 LEU BA CD2 1 230 B B +ATOM 9781 N N . LEU BA 1 231 ? -64.057 3.219 48.961 1.0 100.0 ? ? ? ? ? ? 348 LEU BA N 1 231 B B +ATOM 9782 C CA . LEU BA 1 231 ? -64.532 4.044 50.065 1.0 97.5 ? ? ? ? ? ? 348 LEU BA CA 1 231 B B +ATOM 9783 C C . LEU BA 1 231 ? -65.967 4.538 49.931 1.0 88.35 ? ? ? ? ? ? 348 LEU BA C 1 231 B B +ATOM 9784 O O . LEU BA 1 231 ? -66.663 4.696 50.933 1.0 81.45 ? ? ? ? ? ? 348 LEU BA O 1 231 B B +ATOM 9785 C CB . LEU BA 1 231 ? -63.592 5.237 50.254 1.0 100.0 ? ? ? ? ? ? 348 LEU BA CB 1 231 B B +ATOM 9786 C CG . LEU BA 1 231 ? -62.159 4.835 50.616 1.0 95.13 ? ? ? ? ? ? 348 LEU BA CG 1 231 B B +ATOM 9787 C CD1 . LEU BA 1 231 ? -61.193 5.927 50.197 1.0 82.59 ? ? ? ? ? ? 348 LEU BA CD1 1 231 B B +ATOM 9788 C CD2 . LEU BA 1 231 ? -62.072 4.562 52.108 1.0 100.0 ? ? ? ? ? ? 348 LEU BA CD2 1 231 B B +ATOM 9789 N N . SER BA 1 232 ? -66.406 4.791 48.703 1.0 85.54 ? ? ? ? ? ? 349 SER BA N 1 232 B B +ATOM 9790 C CA . SER BA 1 232 ? -67.765 5.267 48.477 1.0 93.03 ? ? ? ? ? ? 349 SER BA CA 1 232 B B +ATOM 9791 C C . SER BA 1 232 ? -68.757 4.113 48.358 1.0 100.0 ? ? ? ? ? ? 349 SER BA C 1 232 B B +ATOM 9792 O O . SER BA 1 232 ? -69.971 4.321 48.427 1.0 100.0 ? ? ? ? ? ? 349 SER BA O 1 232 B B +ATOM 9793 C CB . SER BA 1 232 ? -67.822 6.128 47.214 1.0 89.12 ? ? ? ? ? ? 349 SER BA CB 1 232 B B +ATOM 9794 O OG . SER BA 1 232 ? -67.588 5.359 46.048 1.0 84.89 ? ? ? ? ? ? 349 SER BA OG 1 232 B B +ATOM 9795 N N . SER BA 1 233 ? -68.238 2.898 48.187 1.0 100.0 ? ? ? ? ? ? 350 SER BA N 1 233 B B +ATOM 9796 C CA . SER BA 1 233 ? -69.084 1.713 48.054 1.0 94.48 ? ? ? ? ? ? 350 SER BA CA 1 233 B B +ATOM 9797 C C . SER BA 1 233 ? -69.041 0.851 49.310 1.0 88.87 ? ? ? ? ? ? 350 SER BA C 1 233 B B +ATOM 9798 O O . SER BA 1 233 ? -68.000 0.300 49.667 1.0 80.63 ? ? ? ? ? ? 350 SER BA O 1 233 B B +ATOM 9799 C CB . SER BA 1 233 ? -68.644 0.881 46.851 1.0 96.72 ? ? ? ? ? ? 350 SER BA CB 1 233 B B +ATOM 9800 O OG . SER BA 1 233 ? -69.034 -0.471 47.002 1.0 82.26 ? ? ? ? ? ? 350 SER BA OG 1 233 B B +ATOM 9801 N N . PHE BA 1 234 ? -70.192 0.733 49.966 1.0 91.05 ? ? ? ? ? ? 351 PHE BA N 1 234 B B +ATOM 9802 C CA . PHE BA 1 234 ? -70.315 -0.039 51.199 1.0 100.0 ? ? ? ? ? ? 351 PHE BA CA 1 234 B B +ATOM 9803 C C . PHE BA 1 234 ? -70.042 -1.538 51.058 1.0 100.0 ? ? ? ? ? ? 351 PHE BA C 1 234 B B +ATOM 9804 O O . PHE BA 1 234 ? -69.342 -2.129 51.880 1.0 100.0 ? ? ? ? ? ? 351 PHE BA O 1 234 B B +ATOM 9805 C CB . PHE BA 1 234 ? -71.710 0.152 51.801 1.0 100.0 ? ? ? ? ? ? 351 PHE BA CB 1 234 B B +ATOM 9806 C CG . PHE BA 1 234 ? -72.012 -0.788 52.934 1.0 100.0 ? ? ? ? ? ? 351 PHE BA CG 1 234 B B +ATOM 9807 C CD1 . PHE BA 1 234 ? -71.425 -0.598 54.181 1.0 100.0 ? ? ? ? ? ? 351 PHE BA CD1 1 234 B B +ATOM 9808 C CD2 . PHE BA 1 234 ? -72.866 -1.873 52.753 1.0 100.0 ? ? ? ? ? ? 351 PHE BA CD2 1 234 B B +ATOM 9809 C CE1 . PHE BA 1 234 ? -71.682 -1.472 55.231 1.0 100.0 ? ? ? ? ? ? 351 PHE BA CE1 1 234 B B +ATOM 9810 C CE2 . PHE BA 1 234 ? -73.131 -2.756 53.797 1.0 100.0 ? ? ? ? ? ? 351 PHE BA CE2 1 234 B B +ATOM 9811 C CZ . PHE BA 1 234 ? -72.538 -2.555 55.039 1.0 100.0 ? ? ? ? ? ? 351 PHE BA CZ 1 234 B B +ATOM 9812 N N . GLY BA 1 235 ? -70.606 -2.147 50.020 1.0 100.0 ? ? ? ? ? ? 352 GLY BA N 1 235 B B +ATOM 9813 C CA . GLY BA 1 235 ? -70.434 -3.574 49.808 1.0 97.48 ? ? ? ? ? ? 352 GLY BA CA 1 235 B B +ATOM 9814 C C . GLY BA 1 235 ? -69.023 -4.035 49.496 1.0 95.87 ? ? ? ? ? ? 352 GLY BA C 1 235 B B +ATOM 9815 O O . GLY BA 1 235 ? -68.624 -5.132 49.891 1.0 86.0 ? ? ? ? ? ? 352 GLY BA O 1 235 B B +ATOM 9816 N N . GLU BA 1 236 ? -68.262 -3.208 48.785 1.0 93.46 ? ? ? ? ? ? 353 GLU BA N 1 236 B B +ATOM 9817 C CA . GLU BA 1 236 ? -66.896 -3.570 48.427 1.0 93.61 ? ? ? ? ? ? 353 GLU BA CA 1 236 B B +ATOM 9818 C C . GLU BA 1 236 ? -65.869 -3.125 49.459 1.0 92.61 ? ? ? ? ? ? 353 GLU BA C 1 236 B B +ATOM 9819 O O . GLU BA 1 236 ? -64.731 -3.598 49.460 1.0 89.2 ? ? ? ? ? ? 353 GLU BA O 1 236 B B +ATOM 9820 C CB . GLU BA 1 236 ? -66.533 -2.987 47.065 1.0 91.82 ? ? ? ? ? ? 353 GLU BA CB 1 236 B B +ATOM 9821 C CG . GLU BA 1 236 ? -65.565 -3.849 46.278 1.0 80.75 ? ? ? ? ? ? 353 GLU BA CG 1 236 B B +ATOM 9822 C CD . GLU BA 1 236 ? -65.707 -3.653 44.785 1.0 83.7 ? ? ? ? ? ? 353 GLU BA CD 1 236 B B +ATOM 9823 O OE1 . GLU BA 1 236 ? -64.883 -4.208 44.030 1.0 78.05 ? ? ? ? ? ? 353 GLU BA OE1 1 236 B B +ATOM 9824 O OE2 . GLU BA 1 236 ? -66.648 -2.943 44.368 1.0 90.12 ? ? ? ? ? ? 353 GLU BA OE2 1 236 B B +ATOM 9825 N N . LEU BA 1 237 ? -66.271 -2.208 50.328 1.0 94.32 ? ? ? ? ? ? 354 LEU BA N 1 237 B B +ATOM 9826 C CA . LEU BA 1 237 ? -65.377 -1.712 51.362 1.0 100.0 ? ? ? ? ? ? 354 LEU BA CA 1 237 B B +ATOM 9827 C C . LEU BA 1 237 ? -65.009 -2.849 52.314 1.0 100.0 ? ? ? ? ? ? 354 LEU BA C 1 237 B B +ATOM 9828 O O . LEU BA 1 237 ? -63.863 -2.962 52.757 1.0 100.0 ? ? ? ? ? ? 354 LEU BA O 1 237 B B +ATOM 9829 C CB . LEU BA 1 237 ? -66.055 -0.576 52.130 1.0 100.0 ? ? ? ? ? ? 354 LEU BA CB 1 237 B B +ATOM 9830 C CG . LEU BA 1 237 ? -65.264 0.114 53.245 1.0 100.0 ? ? ? ? ? ? 354 LEU BA CG 1 237 B B +ATOM 9831 C CD1 . LEU BA 1 237 ? -63.912 0.596 52.728 1.0 100.0 ? ? ? ? ? ? 354 LEU BA CD1 1 237 B B +ATOM 9832 C CD2 . LEU BA 1 237 ? -66.086 1.282 53.771 1.0 100.0 ? ? ? ? ? ? 354 LEU BA CD2 1 237 B B +ATOM 9833 N N . GLN BA 1 238 ? -65.990 -3.693 52.619 1.0 100.0 ? ? ? ? ? ? 355 GLN BA N 1 238 B B +ATOM 9834 C CA . GLN BA 1 238 ? -65.772 -4.823 53.512 1.0 100.0 ? ? ? ? ? ? 355 GLN BA CA 1 238 B B +ATOM 9835 C C . GLN BA 1 238 ? -65.263 -6.047 52.749 1.0 100.0 ? ? ? ? ? ? 355 GLN BA C 1 238 B B +ATOM 9836 O O . GLN BA 1 238 ? -64.637 -6.936 53.331 1.0 100.0 ? ? ? ? ? ? 355 GLN BA O 1 238 B B +ATOM 9837 C CB . GLN BA 1 238 ? -67.072 -5.173 54.232 1.0 100.0 ? ? ? ? ? ? 355 GLN BA CB 1 238 B B +ATOM 9838 C CG . GLN BA 1 238 ? -68.323 -4.911 53.408 1.0 100.0 ? ? ? ? ? ? 355 GLN BA CG 1 238 B B +ATOM 9839 C CD . GLN BA 1 238 ? -69.581 -4.931 54.252 1.0 100.0 ? ? ? ? ? ? 355 GLN BA CD 1 238 B B +ATOM 9840 O OE1 . GLN BA 1 238 ? -70.523 -5.678 53.976 1.0 100.0 ? ? ? ? ? ? 355 GLN BA OE1 1 238 B B +ATOM 9841 N NE2 . GLN BA 1 238 ? -69.604 -4.107 55.291 1.0 98.92 ? ? ? ? ? ? 355 GLN BA NE2 1 238 B B +ATOM 9842 N N . TYR BA 1 239 ? -65.526 -6.083 51.445 1.0 100.0 ? ? ? ? ? ? 356 TYR BA N 1 239 B B +ATOM 9843 C CA . TYR BA 1 239 ? -65.097 -7.205 50.615 1.0 100.0 ? ? ? ? ? ? 356 TYR BA CA 1 239 B B +ATOM 9844 C C . TYR BA 1 239 ? -63.602 -7.188 50.290 1.0 100.0 ? ? ? ? ? ? 356 TYR BA C 1 239 B B +ATOM 9845 O O . TYR BA 1 239 ? -62.932 -8.220 50.350 1.0 100.0 ? ? ? ? ? ? 356 TYR BA O 1 239 B B +ATOM 9846 C CB . TYR BA 1 239 ? -65.878 -7.231 49.302 1.0 100.0 ? ? ? ? ? ? 356 TYR BA CB 1 239 B B +ATOM 9847 C CG . TYR BA 1 239 ? -65.201 -8.058 48.229 1.0 100.0 ? ? ? ? ? ? 356 TYR BA CG 1 239 B B +ATOM 9848 C CD1 . TYR BA 1 239 ? -65.002 -9.428 48.406 1.0 100.0 ? ? ? ? ? ? 356 TYR BA CD1 1 239 B B +ATOM 9849 C CD2 . TYR BA 1 239 ? -64.752 -7.476 47.043 1.0 100.0 ? ? ? ? ? ? 356 TYR BA CD2 1 239 B B +ATOM 9850 C CE1 . TYR BA 1 239 ? -64.379 -10.200 47.430 1.0 100.0 ? ? ? ? ? ? 356 TYR BA CE1 1 239 B B +ATOM 9851 C CE2 . TYR BA 1 239 ? -64.125 -8.240 46.058 1.0 100.0 ? ? ? ? ? ? 356 TYR BA CE2 1 239 B B +ATOM 9852 C CZ . TYR BA 1 239 ? -63.944 -9.601 46.258 1.0 100.0 ? ? ? ? ? ? 356 TYR BA CZ 1 239 B B +ATOM 9853 O OH . TYR BA 1 239 ? -63.345 -10.365 45.281 1.0 100.0 ? ? ? ? ? ? 356 TYR BA OH 1 239 B B +ATOM 9854 N N . CYS BA 1 240 ? -63.093 -6.015 49.930 1.0 98.65 ? ? ? ? ? ? 357 CYS BA N 1 240 B B +ATOM 9855 C CA . CYS BA 1 240 ? -61.686 -5.863 49.579 1.0 100.0 ? ? ? ? ? ? 357 CYS BA CA 1 240 B B +ATOM 9856 C C . CYS BA 1 240 ? -60.758 -6.092 50.771 1.0 100.0 ? ? ? ? ? ? 357 CYS BA C 1 240 B B +ATOM 9857 O O . CYS BA 1 240 ? -59.574 -6.391 50.595 1.0 100.0 ? ? ? ? ? ? 357 CYS BA O 1 240 B B +ATOM 9858 C CB . CYS BA 1 240 ? -61.441 -4.466 49.010 1.0 100.0 ? ? ? ? ? ? 357 CYS BA CB 1 240 B B +ATOM 9859 S SG . CYS BA 1 240 ? -61.777 -3.124 50.181 1.0 100.0 ? ? ? ? ? ? 357 CYS BA SG 1 240 B B +ATOM 9860 N N . LEU BA 1 241 ? -61.302 -5.960 51.979 1.0 100.0 ? ? ? ? ? ? 358 LEU BA N 1 241 B B +ATOM 9861 C CA . LEU BA 1 241 ? -60.524 -6.131 53.202 1.0 100.0 ? ? ? ? ? ? 358 LEU BA CA 1 241 B B +ATOM 9862 C C . LEU BA 1 241 ? -60.497 -7.574 53.705 1.0 100.0 ? ? ? ? ? ? 358 LEU BA C 1 241 B B +ATOM 9863 O O . LEU BA 1 241 ? -59.724 -7.913 54.604 1.0 100.0 ? ? ? ? ? ? 358 LEU BA O 1 241 B B +ATOM 9864 C CB . LEU BA 1 241 ? -61.078 -5.210 54.295 1.0 96.86 ? ? ? ? ? ? 358 LEU BA CB 1 241 B B +ATOM 9865 C CG . LEU BA 1 241 ? -60.129 -4.150 54.871 1.0 99.6 ? ? ? ? ? ? 358 LEU BA CG 1 241 B B +ATOM 9866 C CD1 . LEU BA 1 241 ? -59.072 -4.827 55.732 1.0 100.0 ? ? ? ? ? ? 358 LEU BA CD1 1 241 B B +ATOM 9867 C CD2 . LEU BA 1 241 ? -59.487 -3.356 53.743 1.0 97.83 ? ? ? ? ? ? 358 LEU BA CD2 1 241 B B +ATOM 9868 N N . SER BA 1 242 ? -61.332 -8.424 53.116 1.0 100.0 ? ? ? ? ? ? 359 SER BA N 1 242 B B +ATOM 9869 C CA . SER BA 1 242 ? -61.395 -9.824 53.520 1.0 100.0 ? ? ? ? ? ? 359 SER BA CA 1 242 B B +ATOM 9870 C C . SER BA 1 242 ? -60.339 -10.686 52.832 1.0 100.0 ? ? ? ? ? ? 359 SER BA C 1 242 B B +ATOM 9871 O O . SER BA 1 242 ? -59.527 -10.188 52.046 1.0 96.18 ? ? ? ? ? ? 359 SER BA O 1 242 B B +ATOM 9872 C CB . SER BA 1 242 ? -62.793 -10.391 53.241 1.0 100.0 ? ? ? ? ? ? 359 SER BA CB 1 242 B B +ATOM 9873 O OG . SER BA 1 242 ? -63.110 -10.326 51.862 1.0 96.44 ? ? ? ? ? ? 359 SER BA OG 1 242 B B +ATOM 9874 N N . GLU BA 1 243 ? -60.361 -11.982 53.136 1.0 100.0 ? ? ? ? ? ? 360 GLU BA N 1 243 B B +ATOM 9875 C CA . GLU BA 1 243 ? -59.414 -12.937 52.565 1.0 100.0 ? ? ? ? ? ? 360 GLU BA CA 1 243 B B +ATOM 9876 C C . GLU BA 1 243 ? -60.030 -13.759 51.436 1.0 100.0 ? ? ? ? ? ? 360 GLU BA C 1 243 B B +ATOM 9877 O O . GLU BA 1 243 ? -59.835 -14.975 51.358 1.0 100.0 ? ? ? ? ? ? 360 GLU BA O 1 243 B B +ATOM 9878 C CB . GLU BA 1 243 ? -58.895 -13.878 53.652 1.0 100.0 ? ? ? ? ? ? 360 GLU BA CB 1 243 B B +ATOM 9879 C CG . GLU BA 1 243 ? -57.863 -13.244 54.566 1.0 100.0 ? ? ? ? ? ? 360 GLU BA CG 1 243 B B +ATOM 9880 C CD . GLU BA 1 243 ? -57.791 -13.924 55.919 1.0 100.0 ? ? ? ? ? ? 360 GLU BA CD 1 243 B B +ATOM 9881 O OE1 . GLU BA 1 243 ? -57.566 -15.153 55.949 1.0 100.0 ? ? ? ? ? ? 360 GLU BA OE1 1 243 B B +ATOM 9882 O OE2 . GLU BA 1 243 ? -57.963 -13.233 56.950 1.0 100.0 ? ? ? ? ? ? 360 GLU BA OE2 1 243 B B +ATOM 9883 N N . LYS BA 1 244 ? -60.775 -13.086 50.566 1.0 100.0 ? ? ? ? ? ? 361 LYS BA N 1 244 B B +ATOM 9884 C CA . LYS BA 1 244 ? -61.414 -13.744 49.436 1.0 100.0 ? ? ? ? ? ? 361 LYS BA CA 1 244 B B +ATOM 9885 C C . LYS BA 1 244 ? -60.701 -13.386 48.128 1.0 100.0 ? ? ? ? ? ? 361 LYS BA C 1 244 B B +ATOM 9886 O O . LYS BA 1 244 ? -60.437 -14.259 47.296 1.0 100.0 ? ? ? ? ? ? 361 LYS BA O 1 244 B B +ATOM 9887 C CB . LYS BA 1 244 ? -62.896 -13.352 49.362 1.0 100.0 ? ? ? ? ? ? 361 LYS BA CB 1 244 B B +ATOM 9888 C CG . LYS BA 1 244 ? -63.688 -13.737 50.604 1.0 94.4 ? ? ? ? ? ? 361 LYS BA CG 1 244 B B +ATOM 9889 C CD . LYS BA 1 244 ? -65.171 -13.431 50.462 1.0 96.23 ? ? ? ? ? ? 361 LYS BA CD 1 244 B B +ATOM 9890 C CE . LYS BA 1 244 ? -65.936 -13.914 51.688 1.0 100.0 ? ? ? ? ? ? 361 LYS BA CE 1 244 B B +ATOM 9891 N NZ . LYS BA 1 244 ? -67.402 -13.683 51.579 1.0 100.0 ? ? ? ? ? ? 361 LYS BA NZ 1 244 B B +ATOM 9892 N N . PRO BA 1 245 ? -60.350 -12.095 47.942 1.0 100.0 ? ? ? ? ? ? 362 PRO BA N 1 245 B B +ATOM 9893 C CA . PRO BA 1 245 ? -59.667 -11.660 46.718 1.0 100.0 ? ? ? ? ? ? 362 PRO BA CA 1 245 B B +ATOM 9894 C C . PRO BA 1 245 ? -58.190 -12.034 46.733 1.0 100.0 ? ? ? ? ? ? 362 PRO BA C 1 245 B B +ATOM 9895 O O . PRO BA 1 245 ? -57.582 -12.125 47.799 1.0 100.0 ? ? ? ? ? ? 362 PRO BA O 1 245 B B +ATOM 9896 C CB . PRO BA 1 245 ? -59.882 -10.150 46.713 1.0 100.0 ? ? ? ? ? ? 362 PRO BA CB 1 245 B B +ATOM 9897 C CG . PRO BA 1 245 ? -59.967 -9.790 48.164 1.0 100.0 ? ? ? ? ? ? 362 PRO BA CG 1 245 B B +ATOM 9898 C CD . PRO BA 1 245 ? -60.540 -10.978 48.887 1.0 100.0 ? ? ? ? ? ? 362 PRO BA CD 1 245 B B +ATOM 9899 N N . LYS BA 1 246 ? -57.618 -12.254 45.551 1.0 100.0 ? ? ? ? ? ? 363 LYS BA N 1 246 B B +ATOM 9900 C CA . LYS BA 1 246 ? -56.205 -12.618 45.446 1.0 100.0 ? ? ? ? ? ? 363 LYS BA CA 1 246 B B +ATOM 9901 C C . LYS BA 1 246 ? -55.353 -11.373 45.202 1.0 100.0 ? ? ? ? ? ? 363 LYS BA C 1 246 B B +ATOM 9902 O O . LYS BA 1 246 ? -55.205 -10.912 44.067 1.0 97.58 ? ? ? ? ? ? 363 LYS BA O 1 246 B B +ATOM 9903 C CB . LYS BA 1 246 ? -55.999 -13.640 44.319 1.0 100.0 ? ? ? ? ? ? 363 LYS BA CB 1 246 B B +ATOM 9904 C CG . LYS BA 1 246 ? -56.670 -13.288 42.996 1.0 99.68 ? ? ? ? ? ? 363 LYS BA CG 1 246 B B +ATOM 9905 C CD . LYS BA 1 246 ? -57.576 -14.417 42.511 1.0 100.0 ? ? ? ? ? ? 363 LYS BA CD 1 246 B B +ATOM 9906 C CE . LYS BA 1 246 ? -56.871 -15.774 42.560 1.0 100.0 ? ? ? ? ? ? 363 LYS BA CE 1 246 B B +ATOM 9907 N NZ . LYS BA 1 246 ? -55.895 -15.943 41.451 1.0 93.91 ? ? ? ? ? ? 363 LYS BA NZ 1 246 B B +ATOM 9908 N N . LEU BA 1 247 ? -54.799 -10.840 46.288 1.0 100.0 ? ? ? ? ? ? 364 LEU BA N 1 247 B B +ATOM 9909 C CA . LEU BA 1 247 ? -53.970 -9.639 46.245 1.0 100.0 ? ? ? ? ? ? 364 LEU BA CA 1 247 B B +ATOM 9910 C C . LEU BA 1 247 ? -52.672 -9.821 45.476 1.0 100.0 ? ? ? ? ? ? 364 LEU BA C 1 247 B B +ATOM 9911 O O . LEU BA 1 247 ? -52.116 -10.920 45.413 1.0 100.0 ? ? ? ? ? ? 364 LEU BA O 1 247 B B +ATOM 9912 C CB . LEU BA 1 247 ? -53.634 -9.177 47.668 1.0 100.0 ? ? ? ? ? ? 364 LEU BA CB 1 247 B B +ATOM 9913 C CG . LEU BA 1 247 ? -54.776 -8.781 48.610 1.0 100.0 ? ? ? ? ? ? 364 LEU BA CG 1 247 B B +ATOM 9914 C CD1 . LEU BA 1 247 ? -55.757 -7.888 47.868 1.0 100.0 ? ? ? ? ? ? 364 LEU BA CD1 1 247 B B +ATOM 9915 C CD2 . LEU BA 1 247 ? -55.466 -10.024 49.150 1.0 100.0 ? ? ? ? ? ? 364 LEU BA CD2 1 247 B B +ATOM 9916 N N . LEU BA 1 248 ? -52.197 -8.720 44.903 1.0 100.0 ? ? ? ? ? ? 365 LEU BA N 1 248 B B +ATOM 9917 C CA . LEU BA 1 248 ? -50.952 -8.709 44.145 1.0 100.0 ? ? ? ? ? ? 365 LEU BA CA 1 248 B B +ATOM 9918 C C . LEU BA 1 248 ? -50.233 -7.376 44.377 1.0 100.0 ? ? ? ? ? ? 365 LEU BA C 1 248 B B +ATOM 9919 O O . LEU BA 1 248 ? -50.838 -6.404 44.837 1.0 97.98 ? ? ? ? ? ? 365 LEU BA O 1 248 B B +ATOM 9920 C CB . LEU BA 1 248 ? -51.232 -8.919 42.653 1.0 91.41 ? ? ? ? ? ? 365 LEU BA CB 1 248 B B +ATOM 9921 C CG . LEU BA 1 248 ? -51.768 -10.302 42.268 1.0 87.27 ? ? ? ? ? ? 365 LEU BA CG 1 248 B B +ATOM 9922 C CD1 . LEU BA 1 248 ? -52.137 -10.290 40.799 1.0 88.25 ? ? ? ? ? ? 365 LEU BA CD1 1 248 B B +ATOM 9923 C CD2 . LEU BA 1 248 ? -50.729 -11.379 42.563 1.0 67.33 ? ? ? ? ? ? 365 LEU BA CD2 1 248 B B +ATOM 9924 N N . PRO BA 1 249 ? -48.928 -7.314 44.055 1.0 100.0 ? ? ? ? ? ? 366 PRO BA N 1 249 B B +ATOM 9925 C CA . PRO BA 1 249 ? -48.167 -6.077 44.252 1.0 100.0 ? ? ? ? ? ? 366 PRO BA CA 1 249 B B +ATOM 9926 C C . PRO BA 1 249 ? -48.405 -5.046 43.158 1.0 100.0 ? ? ? ? ? ? 366 PRO BA C 1 249 B B +ATOM 9927 O O . PRO BA 1 249 ? -48.587 -5.389 41.988 1.0 100.0 ? ? ? ? ? ? 366 PRO BA O 1 249 B B +ATOM 9928 C CB . PRO BA 1 249 ? -46.718 -6.555 44.287 1.0 100.0 ? ? ? ? ? ? 366 PRO BA CB 1 249 B B +ATOM 9929 C CG . PRO BA 1 249 ? -46.714 -7.762 43.403 1.0 100.0 ? ? ? ? ? ? 366 PRO BA CG 1 249 B B +ATOM 9930 C CD . PRO BA 1 249 ? -48.094 -8.380 43.468 1.0 100.0 ? ? ? ? ? ? 366 PRO BA CD 1 249 B B +ATOM 9931 N N . LEU BA 1 250 ? -48.411 -3.776 43.545 1.0 100.0 ? ? ? ? ? ? 367 LEU BA N 1 250 B B +ATOM 9932 C CA . LEU BA 1 250 ? -48.615 -2.712 42.580 1.0 98.44 ? ? ? ? ? ? 367 LEU BA CA 1 250 B B +ATOM 9933 C C . LEU BA 1 250 ? -47.424 -2.696 41.625 1.0 100.0 ? ? ? ? ? ? 367 LEU BA C 1 250 B B +ATOM 9934 O O . LEU BA 1 250 ? -46.372 -2.130 41.930 1.0 100.0 ? ? ? ? ? ? 367 LEU BA O 1 250 B B +ATOM 9935 C CB . LEU BA 1 250 ? -48.748 -1.359 43.290 1.0 98.95 ? ? ? ? ? ? 367 LEU BA CB 1 250 B B +ATOM 9936 C CG . LEU BA 1 250 ? -49.015 -0.191 42.334 1.0 100.0 ? ? ? ? ? ? 367 LEU BA CG 1 250 B B +ATOM 9937 C CD1 . LEU BA 1 250 ? -50.380 -0.366 41.682 1.0 100.0 ? ? ? ? ? ? 367 LEU BA CD1 1 250 B B +ATOM 9938 C CD2 . LEU BA 1 250 ? -48.941 1.123 43.084 1.0 100.0 ? ? ? ? ? ? 367 LEU BA CD2 1 250 B B +ATOM 9939 N N . GLU BA 1 251 ? -47.599 -3.338 40.474 1.0 100.0 ? ? ? ? ? ? 368 GLU BA N 1 251 B B +ATOM 9940 C CA . GLU BA 1 251 ? -46.561 -3.414 39.450 1.0 100.0 ? ? ? ? ? ? 368 GLU BA CA 1 251 B B +ATOM 9941 C C . GLU BA 1 251 ? -47.149 -2.905 38.142 1.0 100.0 ? ? ? ? ? ? 368 GLU BA C 1 251 B B +ATOM 9942 O O . GLU BA 1 251 ? -47.667 -3.680 37.337 1.0 100.0 ? ? ? ? ? ? 368 GLU BA O 1 251 B B +ATOM 9943 C CB . GLU BA 1 251 ? -46.093 -4.859 39.276 1.0 100.0 ? ? ? ? ? ? 368 GLU BA CB 1 251 B B +ATOM 9944 C CG . GLU BA 1 251 ? -44.702 -5.008 38.682 1.0 100.0 ? ? ? ? ? ? 368 GLU BA CG 1 251 B B +ATOM 9945 C CD . GLU BA 1 251 ? -44.220 -6.449 38.695 1.0 100.0 ? ? ? ? ? ? 368 GLU BA CD 1 251 B B +ATOM 9946 O OE1 . GLU BA 1 251 ? -43.778 -6.944 37.633 1.0 100.0 ? ? ? ? ? ? 368 GLU BA OE1 1 251 B B +ATOM 9947 O OE2 . GLU BA 1 251 ? -44.288 -7.089 39.769 1.0 100.0 ? ? ? ? ? ? 368 GLU BA OE2 1 251 B B +ATOM 9948 N N . LEU BA 1 252 ? -47.065 -1.594 37.942 1.0 100.0 ? ? ? ? ? ? 369 LEU BA N 1 252 B B +ATOM 9949 C CA . LEU BA 1 252 ? -47.605 -0.942 36.750 1.0 100.0 ? ? ? ? ? ? 369 LEU BA CA 1 252 B B +ATOM 9950 C C . LEU BA 1 252 ? -47.333 -1.641 35.419 1.0 97.87 ? ? ? ? ? ? 369 LEU BA C 1 252 B B +ATOM 9951 O O . LEU BA 1 252 ? -48.059 -1.429 34.445 1.0 87.33 ? ? ? ? ? ? 369 LEU BA O 1 252 B B +ATOM 9952 C CB . LEU BA 1 252 ? -47.106 0.506 36.678 1.0 100.0 ? ? ? ? ? ? 369 LEU BA CB 1 252 B B +ATOM 9953 C CG . LEU BA 1 252 ? -47.814 1.472 37.636 1.0 100.0 ? ? ? ? ? ? 369 LEU BA CG 1 252 B B +ATOM 9954 C CD1 . LEU BA 1 252 ? -47.440 1.135 39.070 1.0 100.0 ? ? ? ? ? ? 369 LEU BA CD1 1 252 B B +ATOM 9955 C CD2 . LEU BA 1 252 ? -47.439 2.901 37.298 1.0 96.69 ? ? ? ? ? ? 369 LEU BA CD2 1 252 B B +ATOM 9956 N N . GLU BA 1 253 ? -46.292 -2.466 35.371 1.0 100.0 ? ? ? ? ? ? 370 GLU BA N 1 253 B B +ATOM 9957 C CA . GLU BA 1 253 ? -45.959 -3.173 34.141 1.0 100.0 ? ? ? ? ? ? 370 GLU BA CA 1 253 B B +ATOM 9958 C C . GLU BA 1 253 ? -47.061 -4.156 33.763 1.0 100.0 ? ? ? ? ? ? 370 GLU BA C 1 253 B B +ATOM 9959 O O . GLU BA 1 253 ? -47.602 -4.107 32.656 1.0 98.83 ? ? ? ? ? ? 370 GLU BA O 1 253 B B +ATOM 9960 C CB . GLU BA 1 253 ? -44.633 -3.921 34.291 1.0 88.24 ? ? ? ? ? ? 370 GLU BA CB 1 253 B B +ATOM 9961 C CG . GLU BA 1 253 ? -43.734 -3.812 33.068 1.0 93.23 ? ? ? ? ? ? 370 GLU BA CG 1 253 B B +ATOM 9962 C CD . GLU BA 1 253 ? -44.418 -4.269 31.791 1.0 100.0 ? ? ? ? ? ? 370 GLU BA CD 1 253 B B +ATOM 9963 O OE1 . GLU BA 1 253 ? -44.364 -5.480 31.488 1.0 100.0 ? ? ? ? ? ? 370 GLU BA OE1 1 253 B B +ATOM 9964 O OE2 . GLU BA 1 253 ? -45.008 -3.417 31.090 1.0 100.0 ? ? ? ? ? ? 370 GLU BA OE2 1 253 B B +ATOM 9965 N N . LYS BA 1 254 ? -47.390 -5.045 34.695 1.0 100.0 ? ? ? ? ? ? 371 LYS BA N 1 254 B B +ATOM 9966 C CA . LYS BA 1 254 ? -48.413 -6.056 34.468 1.0 100.0 ? ? ? ? ? ? 371 LYS BA CA 1 254 B B +ATOM 9967 C C . LYS BA 1 254 ? -49.787 -5.634 34.979 1.0 95.01 ? ? ? ? ? ? 371 LYS BA C 1 254 B B +ATOM 9968 O O . LYS BA 1 254 ? -50.746 -6.405 34.918 1.0 91.53 ? ? ? ? ? ? 371 LYS BA O 1 254 B B +ATOM 9969 C CB . LYS BA 1 254 ? -47.986 -7.367 35.130 1.0 100.0 ? ? ? ? ? ? 371 LYS BA CB 1 254 B B +ATOM 9970 C CG . LYS BA 1 254 ? -46.632 -7.875 34.655 1.0 100.0 ? ? ? ? ? ? 371 LYS BA CG 1 254 B B +ATOM 9971 C CD . LYS BA 1 254 ? -46.644 -8.152 33.155 1.0 100.0 ? ? ? ? ? ? 371 LYS BA CD 1 254 B B +ATOM 9972 C CE . LYS BA 1 254 ? -45.284 -8.615 32.663 1.0 100.0 ? ? ? ? ? ? 371 LYS BA CE 1 254 B B +ATOM 9973 N NZ . LYS BA 1 254 ? -45.273 -8.809 31.189 1.0 84.96 ? ? ? ? ? ? 371 LYS BA NZ 1 254 B B +ATOM 9974 N N . THR BA 1 255 ? -49.883 -4.408 35.482 1.0 98.2 ? ? ? ? ? ? 372 THR BA N 1 255 B B +ATOM 9975 C CA . THR BA 1 255 ? -51.154 -3.906 35.993 1.0 100.0 ? ? ? ? ? ? 372 THR BA CA 1 255 B B +ATOM 9976 C C . THR BA 1 255 ? -51.977 -3.256 34.885 1.0 100.0 ? ? ? ? ? ? 372 THR BA C 1 255 B B +ATOM 9977 O O . THR BA 1 255 ? -53.208 -3.271 34.923 1.0 97.61 ? ? ? ? ? ? 372 THR BA O 1 255 B B +ATOM 9978 C CB . THR BA 1 255 ? -50.950 -2.865 37.110 1.0 100.0 ? ? ? ? ? ? 372 THR BA CB 1 255 B B +ATOM 9979 O OG1 . THR BA 1 255 ? -50.196 -3.444 38.182 1.0 100.0 ? ? ? ? ? ? 372 THR BA OG1 1 255 B B +ATOM 9980 C CG2 . THR BA 1 255 ? -52.296 -2.391 37.641 1.0 100.0 ? ? ? ? ? ? 372 THR BA CG2 1 255 B B +ATOM 9981 N N . ALA BA 1 256 ? -51.284 -2.681 33.904 1.0 100.0 ? ? ? ? ? ? 373 ALA BA N 1 256 B B +ATOM 9982 C CA . ALA BA 1 256 ? -51.935 -2.016 32.779 1.0 97.69 ? ? ? ? ? ? 373 ALA BA CA 1 256 B B +ATOM 9983 C C . ALA BA 1 256 ? -52.569 -3.016 31.819 1.0 94.98 ? ? ? ? ? ? 373 ALA BA C 1 256 B B +ATOM 9984 O O . ALA BA 1 256 ? -53.539 -2.700 31.126 1.0 84.2 ? ? ? ? ? ? 373 ALA BA O 1 256 B B +ATOM 9985 C CB . ALA BA 1 256 ? -50.926 -1.149 32.035 1.0 91.73 ? ? ? ? ? ? 373 ALA BA CB 1 256 B B +ATOM 9986 N N . ILE BA 1 257 ? -52.012 -4.222 31.778 1.0 100.0 ? ? ? ? ? ? 374 ILE BA N 1 257 B B +ATOM 9987 C CA . ILE BA 1 257 ? -52.523 -5.268 30.901 1.0 100.0 ? ? ? ? ? ? 374 ILE BA CA 1 257 B B +ATOM 9988 C C . ILE BA 1 257 ? -53.808 -5.853 31.463 1.0 98.56 ? ? ? ? ? ? 374 ILE BA C 1 257 B B +ATOM 9989 O O . ILE BA 1 257 ? -54.731 -6.195 30.722 1.0 100.0 ? ? ? ? ? ? 374 ILE BA O 1 257 B B +ATOM 9990 C CB . ILE BA 1 257 ? -51.497 -6.408 30.744 1.0 100.0 ? ? ? ? ? ? 374 ILE BA CB 1 257 B B +ATOM 9991 C CG1 . ILE BA 1 257 ? -50.150 -5.836 30.292 1.0 100.0 ? ? ? ? ? ? 374 ILE BA CG1 1 257 B B +ATOM 9992 C CG2 . ILE BA 1 257 ? -52.011 -7.439 29.748 1.0 100.0 ? ? ? ? ? ? 374 ILE BA CG2 1 257 B B +ATOM 9993 C CD1 . ILE BA 1 257 ? -48.963 -6.711 30.632 1.0 100.0 ? ? ? ? ? ? 374 ILE BA CD1 1 257 B B +ATOM 9994 N N . GLN BA 1 258 ? -53.853 -5.956 32.786 1.0 94.6 ? ? ? ? ? ? 375 GLN BA N 1 258 B B +ATOM 9995 C CA . GLN BA 1 258 ? -54.997 -6.501 33.507 1.0 99.42 ? ? ? ? ? ? 375 GLN BA CA 1 258 B B +ATOM 9996 C C . GLN BA 1 258 ? -56.362 -5.979 33.060 1.0 100.0 ? ? ? ? ? ? 375 GLN BA C 1 258 B B +ATOM 9997 O O . GLN BA 1 258 ? -56.604 -4.773 33.050 1.0 100.0 ? ? ? ? ? ? 375 GLN BA O 1 258 B B +ATOM 9998 C CB . GLN BA 1 258 ? -54.825 -6.228 34.998 1.0 100.0 ? ? ? ? ? ? 375 GLN BA CB 1 258 B B +ATOM 9999 C CG . GLN BA 1 258 ? -56.092 -6.416 35.797 1.0 100.0 ? ? ? ? ? ? 375 GLN BA CG 1 258 B B +ATOM 10000 C CD . GLN BA 1 258 ? -56.425 -7.872 36.007 1.0 100.0 ? ? ? ? ? ? 375 GLN BA CD 1 258 B B +ATOM 10001 O OE1 . GLN BA 1 258 ? -55.721 -8.758 35.519 1.0 100.0 ? ? ? ? ? ? 375 GLN BA OE1 1 258 B B +ATOM 10002 N NE2 . GLN BA 1 258 ? -57.501 -8.132 36.740 1.0 95.8 ? ? ? ? ? ? 375 GLN BA NE2 1 258 B B +ATOM 10003 N N . ASN BA 1 259 ? -57.258 -6.905 32.720 1.0 100.0 ? ? ? ? ? ? 376 ASN BA N 1 259 B B +ATOM 10004 C CA . ASN BA 1 259 ? -58.614 -6.572 32.284 1.0 100.0 ? ? ? ? ? ? 376 ASN BA CA 1 259 B B +ATOM 10005 C C . ASN BA 1 259 ? -59.578 -6.695 33.469 1.0 100.0 ? ? ? ? ? ? 376 ASN BA C 1 259 B B +ATOM 10006 O O . ASN BA 1 259 ? -59.506 -7.656 34.237 1.0 100.0 ? ? ? ? ? ? 376 ASN BA O 1 259 B B +ATOM 10007 C CB . ASN BA 1 259 ? -59.049 -7.521 31.160 1.0 100.0 ? ? ? ? ? ? 376 ASN BA CB 1 259 B B +ATOM 10008 C CG . ASN BA 1 259 ? -60.006 -6.867 30.180 1.0 100.0 ? ? ? ? ? ? 376 ASN BA CG 1 259 B B +ATOM 10009 O OD1 . ASN BA 1 259 ? -61.157 -7.285 30.047 1.0 100.0 ? ? ? ? ? ? 376 ASN BA OD1 1 259 B B +ATOM 10010 N ND2 . ASN BA 1 259 ? -59.533 -5.835 29.486 1.0 100.0 ? ? ? ? ? ? 376 ASN BA ND2 1 259 B B +ATOM 10011 N N . TYR BA 1 260 ? -60.480 -5.726 33.613 1.0 100.0 ? ? ? ? ? ? 377 TYR BA N 1 260 B B +ATOM 10012 C CA . TYR BA 1 260 ? -61.437 -5.737 34.722 1.0 100.0 ? ? ? ? ? ? 377 TYR BA CA 1 260 B B +ATOM 10013 C C . TYR BA 1 260 ? -62.895 -5.510 34.315 1.0 100.0 ? ? ? ? ? ? 377 TYR BA C 1 260 B B +ATOM 10014 O O . TYR BA 1 260 ? -63.187 -5.018 33.219 1.0 100.0 ? ? ? ? ? ? 377 TYR BA O 1 260 B B +ATOM 10015 C CB . TYR BA 1 260 ? -61.039 -4.679 35.758 1.0 100.0 ? ? ? ? ? ? 377 TYR BA CB 1 260 B B +ATOM 10016 C CG . TYR BA 1 260 ? -61.071 -3.265 35.224 1.0 100.0 ? ? ? ? ? ? 377 TYR BA CG 1 260 B B +ATOM 10017 C CD1 . TYR BA 1 260 ? -62.224 -2.483 35.330 1.0 100.0 ? ? ? ? ? ? 377 TYR BA CD1 1 260 B B +ATOM 10018 C CD2 . TYR BA 1 260 ? -59.951 -2.708 34.608 1.0 99.54 ? ? ? ? ? ? 377 TYR BA CD2 1 260 B B +ATOM 10019 C CE1 . TYR BA 1 260 ? -62.260 -1.180 34.835 1.0 100.0 ? ? ? ? ? ? 377 TYR BA CE1 1 260 B B +ATOM 10020 C CE2 . TYR BA 1 260 ? -59.976 -1.407 34.109 1.0 100.0 ? ? ? ? ? ? 377 TYR BA CE2 1 260 B B +ATOM 10021 C CZ . TYR BA 1 260 ? -61.134 -0.648 34.227 1.0 100.0 ? ? ? ? ? ? 377 TYR BA CZ 1 260 B B +ATOM 10022 O OH . TYR BA 1 260 ? -61.165 0.644 33.750 1.0 96.8 ? ? ? ? ? ? 377 TYR BA OH 1 260 B B +ATOM 10023 N N . THR BA 1 261 ? -63.804 -5.873 35.220 1.0 100.0 ? ? ? ? ? ? 378 THR BA N 1 261 B B +ATOM 10024 C CA . THR BA 1 261 ? -65.239 -5.709 35.000 1.0 100.0 ? ? ? ? ? ? 378 THR BA CA 1 261 B B +ATOM 10025 C C . THR BA 1 261 ? -65.661 -4.350 35.542 1.0 100.0 ? ? ? ? ? ? 378 THR BA C 1 261 B B +ATOM 10026 O O . THR BA 1 261 ? -65.043 -3.827 36.473 1.0 100.0 ? ? ? ? ? ? 378 THR BA O 1 261 B B +ATOM 10027 C CB . THR BA 1 261 ? -66.060 -6.797 35.729 1.0 100.0 ? ? ? ? ? ? 378 THR BA CB 1 261 B B +ATOM 10028 O OG1 . THR BA 1 261 ? -67.458 -6.571 35.502 1.0 98.57 ? ? ? ? ? ? 378 THR BA OG1 1 261 B B +ATOM 10029 C CG2 . THR BA 1 261 ? -65.787 -6.758 37.230 1.0 100.0 ? ? ? ? ? ? 378 THR BA CG2 1 261 B B +ATOM 10030 N N . VAL BA 1 262 ? -66.718 -3.786 34.971 1.0 100.0 ? ? ? ? ? ? 379 VAL BA N 1 262 B B +ATOM 10031 C CA . VAL BA 1 262 ? -67.198 -2.478 35.397 1.0 100.0 ? ? ? ? ? ? 379 VAL BA CA 1 262 B B +ATOM 10032 C C . VAL BA 1 262 ? -68.342 -2.542 36.409 1.0 100.0 ? ? ? ? ? ? 379 VAL BA C 1 262 B B +ATOM 10033 O O . VAL BA 1 262 ? -68.356 -1.793 37.389 1.0 100.0 ? ? ? ? ? ? 379 VAL BA O 1 262 B B +ATOM 10034 C CB . VAL BA 1 262 ? -67.671 -1.647 34.183 1.0 100.0 ? ? ? ? ? ? 379 VAL BA CB 1 262 B B +ATOM 10035 C CG1 . VAL BA 1 262 ? -68.754 -2.406 33.420 1.0 97.45 ? ? ? ? ? ? 379 VAL BA CG1 1 262 B B +ATOM 10036 C CG2 . VAL BA 1 262 ? -68.184 -0.291 34.650 1.0 85.15 ? ? ? ? ? ? 379 VAL BA CG2 1 262 B B +ATOM 10037 N N . THR BA 1 263 ? -69.291 -3.444 36.175 1.0 100.0 ? ? ? ? ? ? 380 THR BA N 1 263 B B +ATOM 10038 C CA . THR BA 1 263 ? -70.459 -3.575 37.041 1.0 100.0 ? ? ? ? ? ? 380 THR BA CA 1 263 B B +ATOM 10039 C C . THR BA 1 263 ? -70.279 -4.359 38.339 1.0 100.0 ? ? ? ? ? ? 380 THR BA C 1 263 B B +ATOM 10040 O O . THR BA 1 263 ? -71.127 -4.279 39.230 1.0 89.12 ? ? ? ? ? ? 380 THR BA O 1 263 B B +ATOM 10041 C CB . THR BA 1 263 ? -71.641 -4.212 36.277 1.0 99.55 ? ? ? ? ? ? 380 THR BA CB 1 263 B B +ATOM 10042 O OG1 . THR BA 1 263 ? -71.250 -5.497 35.777 1.0 96.22 ? ? ? ? ? ? 380 THR BA OG1 1 263 B B +ATOM 10043 C CG2 . THR BA 1 263 ? -72.068 -3.326 35.121 1.0 82.8 ? ? ? ? ? ? 380 THR BA CG2 1 263 B B +ATOM 10044 N N . GLU BA 1 264 ? -69.191 -5.111 38.462 1.0 100.0 ? ? ? ? ? ? 381 GLU BA N 1 264 B B +ATOM 10045 C CA . GLU BA 1 264 ? -69.006 -5.892 39.674 1.0 100.0 ? ? ? ? ? ? 381 GLU BA CA 1 264 B B +ATOM 10046 C C . GLU BA 1 264 ? -67.641 -5.811 40.343 1.0 100.0 ? ? ? ? ? ? 381 GLU BA C 1 264 B B +ATOM 10047 O O . GLU BA 1 264 ? -66.758 -5.072 39.906 1.0 100.0 ? ? ? ? ? ? 381 GLU BA O 1 264 B B +ATOM 10048 C CB . GLU BA 1 264 ? -69.368 -7.351 39.396 1.0 100.0 ? ? ? ? ? ? 381 GLU BA CB 1 264 B B +ATOM 10049 C CG . GLU BA 1 264 ? -70.865 -7.576 39.238 1.0 100.0 ? ? ? ? ? ? 381 GLU BA CG 1 264 B B +ATOM 10050 C CD . GLU BA 1 264 ? -71.197 -9.005 38.873 1.0 100.0 ? ? ? ? ? ? 381 GLU BA CD 1 264 B B +ATOM 10051 O OE1 . GLU BA 1 264 ? -72.122 -9.215 38.058 1.0 100.0 ? ? ? ? ? ? 381 GLU BA OE1 1 264 B B +ATOM 10052 O OE2 . GLU BA 1 264 ? -70.531 -9.918 39.402 1.0 100.0 ? ? ? ? ? ? 381 GLU BA OE2 1 264 B B +ATOM 10053 N N . PHE BA 1 265 ? -67.494 -6.584 41.418 1.0 100.0 ? ? ? ? ? ? 382 PHE BA N 1 265 B B +ATOM 10054 C CA . PHE BA 1 265 ? -66.271 -6.630 42.219 1.0 100.0 ? ? ? ? ? ? 382 PHE BA CA 1 265 B B +ATOM 10055 C C . PHE BA 1 265 ? -65.075 -7.246 41.501 1.0 99.99 ? ? ? ? ? ? 382 PHE BA C 1 265 B B +ATOM 10056 O O . PHE BA 1 265 ? -65.217 -8.198 40.729 1.0 94.86 ? ? ? ? ? ? 382 PHE BA O 1 265 B B +ATOM 10057 C CB . PHE BA 1 265 ? -66.523 -7.405 43.518 1.0 98.66 ? ? ? ? ? ? 382 PHE BA CB 1 265 B B +ATOM 10058 C CG . PHE BA 1 265 ? -67.554 -6.779 44.429 1.0 100.0 ? ? ? ? ? ? 382 PHE BA CG 1 265 B B +ATOM 10059 C CD1 . PHE BA 1 265 ? -68.382 -5.753 43.982 1.0 100.0 ? ? ? ? ? ? 382 PHE BA CD1 1 265 B B +ATOM 10060 C CD2 . PHE BA 1 265 ? -67.703 -7.233 45.737 1.0 100.0 ? ? ? ? ? ? 382 PHE BA CD2 1 265 B B +ATOM 10061 C CE1 . PHE BA 1 265 ? -69.343 -5.192 44.823 1.0 100.0 ? ? ? ? ? ? 382 PHE BA CE1 1 265 B B +ATOM 10062 C CE2 . PHE BA 1 265 ? -68.660 -6.679 46.585 1.0 100.0 ? ? ? ? ? ? 382 PHE BA CE2 1 265 B B +ATOM 10063 C CZ . PHE BA 1 265 ? -69.481 -5.657 46.128 1.0 100.0 ? ? ? ? ? ? 382 PHE BA CZ 1 265 B B +ATOM 10064 N N . GLN BA 1 266 ? -63.892 -6.705 41.785 1.0 100.0 ? ? ? ? ? ? 383 GLN BA N 1 266 B B +ATOM 10065 C CA . GLN BA 1 266 ? -62.649 -7.177 41.182 1.0 100.0 ? ? ? ? ? ? 383 GLN BA CA 1 266 B B +ATOM 10066 C C . GLN BA 1 266 ? -61.869 -8.085 42.132 1.0 100.0 ? ? ? ? ? ? 383 GLN BA C 1 266 B B +ATOM 10067 O O . GLN BA 1 266 ? -61.545 -7.694 43.254 1.0 98.41 ? ? ? ? ? ? 383 GLN BA O 1 266 B B +ATOM 10068 C CB . GLN BA 1 266 ? -61.775 -5.983 40.786 1.0 99.99 ? ? ? ? ? ? 383 GLN BA CB 1 266 B B +ATOM 10069 C CG . GLN BA 1 266 ? -62.367 -5.117 39.679 1.0 100.0 ? ? ? ? ? ? 383 GLN BA CG 1 266 B B +ATOM 10070 C CD . GLN BA 1 266 ? -63.434 -4.166 40.189 1.0 100.0 ? ? ? ? ? ? 383 GLN BA CD 1 266 B B +ATOM 10071 O OE1 . GLN BA 1 266 ? -64.384 -3.831 39.476 1.0 100.0 ? ? ? ? ? ? 383 GLN BA OE1 1 266 B B +ATOM 10072 N NE2 . GLN BA 1 266 ? -63.281 -3.724 41.432 1.0 100.0 ? ? ? ? ? ? 383 GLN BA NE2 1 266 B B +ATOM 10073 N N . PRO BA 1 267 ? -61.541 -9.310 41.682 1.0 100.0 ? ? ? ? ? ? 384 PRO BA N 1 267 B B +ATOM 10074 C CA . PRO BA 1 267 ? -60.792 -10.242 42.535 1.0 100.0 ? ? ? ? ? ? 384 PRO BA CA 1 267 B B +ATOM 10075 C C . PRO BA 1 267 ? -59.374 -9.737 42.761 1.0 100.0 ? ? ? ? ? ? 384 PRO BA C 1 267 B B +ATOM 10076 O O . PRO BA 1 267 ? -58.710 -10.115 43.727 1.0 91.07 ? ? ? ? ? ? 384 PRO BA O 1 267 B B +ATOM 10077 C CB . PRO BA 1 267 ? -60.822 -11.553 41.752 1.0 100.0 ? ? ? ? ? ? 384 PRO BA CB 1 267 B B +ATOM 10078 C CG . PRO BA 1 267 ? -60.998 -11.130 40.328 1.0 100.0 ? ? ? ? ? ? 384 PRO BA CG 1 267 B B +ATOM 10079 C CD . PRO BA 1 267 ? -61.816 -9.870 40.349 1.0 100.0 ? ? ? ? ? ? 384 PRO BA CD 1 267 B B +ATOM 10080 N N . LEU BA 1 268 ? -58.936 -8.861 41.861 1.0 100.0 ? ? ? ? ? ? 385 LEU BA N 1 268 B B +ATOM 10081 C CA . LEU BA 1 268 ? -57.603 -8.281 41.925 1.0 100.0 ? ? ? ? ? ? 385 LEU BA CA 1 268 B B +ATOM 10082 C C . LEU BA 1 268 ? -57.616 -6.860 42.482 1.0 100.0 ? ? ? ? ? ? 385 LEU BA C 1 268 B B +ATOM 10083 O O . LEU BA 1 268 ? -58.397 -6.009 42.042 1.0 100.0 ? ? ? ? ? ? 385 LEU BA O 1 268 B B +ATOM 10084 C CB . LEU BA 1 268 ? -56.963 -8.271 40.530 1.0 100.0 ? ? ? ? ? ? 385 LEU BA CB 1 268 B B +ATOM 10085 C CG . LEU BA 1 268 ? -56.303 -9.554 40.009 1.0 100.0 ? ? ? ? ? ? 385 LEU BA CG 1 268 B B +ATOM 10086 C CD1 . LEU BA 1 268 ? -55.274 -9.170 38.960 1.0 93.37 ? ? ? ? ? ? 385 LEU BA CD1 1 268 B B +ATOM 10087 C CD2 . LEU BA 1 268 ? -55.636 -10.336 41.140 1.0 98.7 ? ? ? ? ? ? 385 LEU BA CD2 1 268 B B +ATOM 10088 N N . TYR BA 1 269 ? -56.748 -6.628 43.464 1.0 100.0 ? ? ? ? ? ? 386 TYR BA N 1 269 B B +ATOM 10089 C CA . TYR BA 1 269 ? -56.584 -5.327 44.111 1.0 100.0 ? ? ? ? ? ? 386 TYR BA CA 1 269 B B +ATOM 10090 C C . TYR BA 1 269 ? -55.083 -5.171 44.365 1.0 100.0 ? ? ? ? ? ? 386 TYR BA C 1 269 B B +ATOM 10091 O O . TYR BA 1 269 ? -54.547 -5.736 45.321 1.0 87.69 ? ? ? ? ? ? 386 TYR BA O 1 269 B B +ATOM 10092 C CB . TYR BA 1 269 ? -57.330 -5.278 45.454 1.0 100.0 ? ? ? ? ? ? 386 TYR BA CB 1 269 B B +ATOM 10093 C CG . TYR BA 1 269 ? -58.845 -5.284 45.366 1.0 100.0 ? ? ? ? ? ? 386 TYR BA CG 1 269 B B +ATOM 10094 C CD1 . TYR BA 1 269 ? -59.587 -6.271 46.016 1.0 100.0 ? ? ? ? ? ? 386 TYR BA CD1 1 269 B B +ATOM 10095 C CD2 . TYR BA 1 269 ? -59.539 -4.285 44.671 1.0 100.0 ? ? ? ? ? ? 386 TYR BA CD2 1 269 B B +ATOM 10096 C CE1 . TYR BA 1 269 ? -60.979 -6.266 45.983 1.0 100.0 ? ? ? ? ? ? 386 TYR BA CE1 1 269 B B +ATOM 10097 C CE2 . TYR BA 1 269 ? -60.936 -4.271 44.633 1.0 99.27 ? ? ? ? ? ? 386 TYR BA CE2 1 269 B B +ATOM 10098 C CZ . TYR BA 1 269 ? -61.647 -5.265 45.294 1.0 100.0 ? ? ? ? ? ? 386 TYR BA CZ 1 269 B B +ATOM 10099 O OH . TYR BA 1 269 ? -63.022 -5.251 45.276 1.0 89.53 ? ? ? ? ? ? 386 TYR BA OH 1 269 B B +ATOM 10100 N N . TYR BA 1 270 ? -54.408 -4.414 43.504 1.0 100.0 ? ? ? ? ? ? 387 TYR BA N 1 270 B B +ATOM 10101 C CA . TYR BA 1 270 ? -52.968 -4.207 43.639 1.0 100.0 ? ? ? ? ? ? 387 TYR BA CA 1 270 B B +ATOM 10102 C C . TYR BA 1 270 ? -52.592 -3.414 44.885 1.0 100.0 ? ? ? ? ? ? 387 TYR BA C 1 270 B B +ATOM 10103 O O . TYR BA 1 270 ? -53.016 -2.271 45.065 1.0 100.0 ? ? ? ? ? ? 387 TYR BA O 1 270 B B +ATOM 10104 C CB . TYR BA 1 270 ? -52.417 -3.511 42.392 1.0 100.0 ? ? ? ? ? ? 387 TYR BA CB 1 270 B B +ATOM 10105 C CG . TYR BA 1 270 ? -52.529 -4.372 41.163 1.0 98.77 ? ? ? ? ? ? 387 TYR BA CG 1 270 B B +ATOM 10106 C CD1 . TYR BA 1 270 ? -53.758 -4.550 40.528 1.0 100.0 ? ? ? ? ? ? 387 TYR BA CD1 1 270 B B +ATOM 10107 C CD2 . TYR BA 1 270 ? -51.421 -5.047 40.656 1.0 100.0 ? ? ? ? ? ? 387 TYR BA CD2 1 270 B B +ATOM 10108 C CE1 . TYR BA 1 270 ? -53.884 -5.382 39.421 1.0 100.0 ? ? ? ? ? ? 387 TYR BA CE1 1 270 B B +ATOM 10109 C CE2 . TYR BA 1 270 ? -51.535 -5.881 39.547 1.0 100.0 ? ? ? ? ? ? 387 TYR BA CE2 1 270 B B +ATOM 10110 C CZ . TYR BA 1 270 ? -52.770 -6.045 38.935 1.0 100.0 ? ? ? ? ? ? 387 TYR BA CZ 1 270 B B +ATOM 10111 O OH . TYR BA 1 270 ? -52.902 -6.874 37.842 1.0 100.0 ? ? ? ? ? ? 387 TYR BA OH 1 270 B B +ATOM 10112 N N . VAL BA 1 271 ? -51.777 -4.037 45.734 1.0 100.0 ? ? ? ? ? ? 388 VAL BA N 1 271 B B +ATOM 10113 C CA . VAL BA 1 271 ? -51.333 -3.428 46.984 1.0 100.0 ? ? ? ? ? ? 388 VAL BA CA 1 271 B B +ATOM 10114 C C . VAL BA 1 271 ? -50.086 -2.558 46.835 1.0 100.0 ? ? ? ? ? ? 388 VAL BA C 1 271 B B +ATOM 10115 O O . VAL BA 1 271 ? -48.980 -3.070 46.650 1.0 100.0 ? ? ? ? ? ? 388 VAL BA O 1 271 B B +ATOM 10116 C CB . VAL BA 1 271 ? -51.045 -4.513 48.043 1.0 100.0 ? ? ? ? ? ? 388 VAL BA CB 1 271 B B +ATOM 10117 C CG1 . VAL BA 1 271 ? -50.679 -3.864 49.370 1.0 100.0 ? ? ? ? ? ? 388 VAL BA CG1 1 271 B B +ATOM 10118 C CG2 . VAL BA 1 271 ? -52.259 -5.419 48.199 1.0 96.31 ? ? ? ? ? ? 388 VAL BA CG2 1 271 B B +ATOM 10119 N N . ALA BA 1 272 ? -50.274 -1.243 46.923 1.0 100.0 ? ? ? ? ? ? 389 ALA BA N 1 272 B B +ATOM 10120 C CA . ALA BA 1 272 ? -49.169 -0.294 46.815 1.0 100.0 ? ? ? ? ? ? 389 ALA BA CA 1 272 B B +ATOM 10121 C C . ALA BA 1 272 ? -48.548 -0.050 48.187 1.0 100.0 ? ? ? ? ? ? 389 ALA BA C 1 272 B B +ATOM 10122 O O . ALA BA 1 272 ? -49.253 0.023 49.198 1.0 100.0 ? ? ? ? ? ? 389 ALA BA O 1 272 B B +ATOM 10123 C CB . ALA BA 1 272 ? -49.663 1.023 46.236 1.0 100.0 ? ? ? ? ? ? 389 ALA BA CB 1 272 B B +ATOM 10124 N N . GLU BA 1 273 ? -47.226 0.066 48.220 1.0 100.0 ? ? ? ? ? ? 390 GLU BA N 1 273 B B +ATOM 10125 C CA . GLU BA 1 273 ? -46.528 0.314 49.473 1.0 100.0 ? ? ? ? ? ? 390 GLU BA CA 1 273 B B +ATOM 10126 C C . GLU BA 1 273 ? -46.999 1.657 50.013 1.0 100.0 ? ? ? ? ? ? 390 GLU BA C 1 273 B B +ATOM 10127 O O . GLU BA 1 273 ? -47.450 1.762 51.154 1.0 100.0 ? ? ? ? ? ? 390 GLU BA O 1 273 B B +ATOM 10128 C CB . GLU BA 1 273 ? -45.016 0.349 49.237 1.0 100.0 ? ? ? ? ? ? 390 GLU BA CB 1 273 B B +ATOM 10129 C CG . GLU BA 1 273 ? -44.445 -0.963 48.730 1.0 100.0 ? ? ? ? ? ? 390 GLU BA CG 1 273 B B +ATOM 10130 C CD . GLU BA 1 273 ? -42.929 -0.938 48.626 1.0 100.0 ? ? ? ? ? ? 390 GLU BA CD 1 273 B B +ATOM 10131 O OE1 . GLU BA 1 273 ? -42.329 0.128 48.885 1.0 90.81 ? ? ? ? ? ? 390 GLU BA OE1 1 273 B B +ATOM 10132 O OE2 . GLU BA 1 273 ? -42.339 -1.988 48.284 1.0 100.0 ? ? ? ? ? ? 390 GLU BA OE2 1 273 B B +ATOM 10133 N N . SER BA 1 274 ? -46.900 2.680 49.171 1.0 90.63 ? ? ? ? ? ? 391 SER BA N 1 274 B B +ATOM 10134 C CA . SER BA 1 274 ? -47.311 4.025 49.542 1.0 94.47 ? ? ? ? ? ? 391 SER BA CA 1 274 B B +ATOM 10135 C C . SER BA 1 274 ? -47.594 4.830 48.282 1.0 99.76 ? ? ? ? ? ? 391 SER BA C 1 274 B B +ATOM 10136 O O . SER BA 1 274 ? -47.268 4.399 47.176 1.0 100.0 ? ? ? ? ? ? 391 SER BA O 1 274 B B +ATOM 10137 C CB . SER BA 1 274 ? -46.208 4.705 50.358 1.0 93.37 ? ? ? ? ? ? 391 SER BA CB 1 274 B B +ATOM 10138 O OG . SER BA 1 274 ? -46.666 5.920 50.929 1.0 100.0 ? ? ? ? ? ? 391 SER BA OG 1 274 B B +ATOM 10139 N N . PHE BA 1 275 ? -48.211 5.994 48.454 1.0 99.74 ? ? ? ? ? ? 392 PHE BA N 1 275 B B +ATOM 10140 C CA . PHE BA 1 275 ? -48.526 6.865 47.327 1.0 93.22 ? ? ? ? ? ? 392 PHE BA CA 1 275 B B +ATOM 10141 C C . PHE BA 1 275 ? -47.227 7.495 46.849 1.0 96.1 ? ? ? ? ? ? 392 PHE BA C 1 275 B B +ATOM 10142 O O . PHE BA 1 275 ? -47.047 7.748 45.660 1.0 100.0 ? ? ? ? ? ? 392 PHE BA O 1 275 B B +ATOM 10143 C CB . PHE BA 1 275 ? -49.518 7.941 47.761 1.0 82.66 ? ? ? ? ? ? 392 PHE BA CB 1 275 B B +ATOM 10144 C CG . PHE BA 1 275 ? -50.573 7.437 48.702 1.0 93.42 ? ? ? ? ? ? 392 PHE BA CG 1 275 B B +ATOM 10145 C CD1 . PHE BA 1 275 ? -50.622 7.883 50.018 1.0 100.0 ? ? ? ? ? ? 392 PHE BA CD1 1 275 B B +ATOM 10146 C CD2 . PHE BA 1 275 ? -51.510 6.500 48.277 1.0 84.08 ? ? ? ? ? ? 392 PHE BA CD2 1 275 B B +ATOM 10147 C CE1 . PHE BA 1 275 ? -51.591 7.404 50.898 1.0 96.84 ? ? ? ? ? ? 392 PHE BA CE1 1 275 B B +ATOM 10148 C CE2 . PHE BA 1 275 ? -52.481 6.014 49.147 1.0 78.21 ? ? ? ? ? ? 392 PHE BA CE2 1 275 B B +ATOM 10149 C CZ . PHE BA 1 275 ? -52.522 6.465 50.460 1.0 87.99 ? ? ? ? ? ? 392 PHE BA CZ 1 275 B B +ATOM 10150 N N . ASN BA 1 276 ? -46.323 7.736 47.794 1.0 99.16 ? ? ? ? ? ? 393 ASN BA N 1 276 B B +ATOM 10151 C CA . ASN BA 1 276 ? -45.016 8.312 47.499 1.0 100.0 ? ? ? ? ? ? 393 ASN BA CA 1 276 B B +ATOM 10152 C C . ASN BA 1 276 ? -44.241 7.276 46.692 1.0 100.0 ? ? ? ? ? ? 393 ASN BA C 1 276 B B +ATOM 10153 O O . ASN BA 1 276 ? -43.431 7.604 45.819 1.0 95.97 ? ? ? ? ? ? 393 ASN BA O 1 276 B B +ATOM 10154 C CB . ASN BA 1 276 ? -44.272 8.589 48.807 1.0 100.0 ? ? ? ? ? ? 393 ASN BA CB 1 276 B B +ATOM 10155 C CG . ASN BA 1 276 ? -43.109 9.542 48.626 1.0 100.0 ? ? ? ? ? ? 393 ASN BA CG 1 276 B B +ATOM 10156 O OD1 . ASN BA 1 276 ? -42.335 9.428 47.674 1.0 100.0 ? ? ? ? ? ? 393 ASN BA OD1 1 276 B B +ATOM 10157 N ND2 . ASN BA 1 276 ? -42.981 10.493 49.546 1.0 100.0 ? ? ? ? ? ? 393 ASN BA ND2 1 276 B B +ATOM 10158 N N . ASP BA 1 277 ? -44.529 6.016 47.015 1.0 100.0 ? ? ? ? ? ? 394 ASP BA N 1 277 B B +ATOM 10159 C CA . ASP BA 1 277 ? -43.914 4.846 46.401 1.0 100.0 ? ? ? ? ? ? 394 ASP BA CA 1 277 B B +ATOM 10160 C C . ASP BA 1 277 ? -44.574 4.478 45.070 1.0 98.41 ? ? ? ? ? ? 394 ASP BA C 1 277 B B +ATOM 10161 O O . ASP BA 1 277 ? -43.882 4.239 44.075 1.0 76.46 ? ? ? ? ? ? 394 ASP BA O 1 277 B B +ATOM 10162 C CB . ASP BA 1 277 ? -43.998 3.674 47.385 1.0 100.0 ? ? ? ? ? ? 394 ASP BA CB 1 277 B B +ATOM 10163 C CG . ASP BA 1 277 ? -44.217 2.344 46.697 1.0 100.0 ? ? ? ? ? ? 394 ASP BA CG 1 277 B B +ATOM 10164 O OD1 . ASP BA 1 277 ? -43.211 1.712 46.314 1.0 100.0 ? ? ? ? ? ? 394 ASP BA OD1 1 277 B B +ATOM 10165 O OD2 . ASP BA 1 277 ? -45.389 1.934 46.542 1.0 94.84 ? ? ? ? ? ? 394 ASP BA OD2 1 277 B B +ATOM 10166 N N . ALA BA 1 278 ? -45.903 4.417 45.053 1.0 96.6 ? ? ? ? ? ? 395 ALA BA N 1 278 B B +ATOM 10167 C CA . ALA BA 1 278 ? -46.629 4.101 43.824 1.0 93.92 ? ? ? ? ? ? 395 ALA BA CA 1 278 B B +ATOM 10168 C C . ALA BA 1 278 ? -46.188 5.140 42.798 1.0 99.31 ? ? ? ? ? ? 395 ALA BA C 1 278 B B +ATOM 10169 O O . ALA BA 1 278 ? -46.006 4.845 41.615 1.0 99.13 ? ? ? ? ? ? 395 ALA BA O 1 278 B B +ATOM 10170 C CB . ALA BA 1 278 ? -48.137 4.194 44.054 1.0 72.96 ? ? ? ? ? ? 395 ALA BA CB 1 278 B B +ATOM 10171 N N . LYS BA 1 279 ? -45.997 6.357 43.292 1.0 100.0 ? ? ? ? ? ? 396 LYS BA N 1 279 B B +ATOM 10172 C CA . LYS BA 1 279 ? -45.573 7.493 42.485 1.0 100.0 ? ? ? ? ? ? 396 LYS BA CA 1 279 B B +ATOM 10173 C C . LYS BA 1 279 ? -44.371 7.173 41.605 1.0 96.15 ? ? ? ? ? ? 396 LYS BA C 1 279 B B +ATOM 10174 O O . LYS BA 1 279 ? -44.313 7.589 40.447 1.0 96.56 ? ? ? ? ? ? 396 LYS BA O 1 279 B B +ATOM 10175 C CB . LYS BA 1 279 ? -45.230 8.664 43.409 1.0 96.26 ? ? ? ? ? ? 396 LYS BA CB 1 279 B B +ATOM 10176 C CG . LYS BA 1 279 ? -44.660 9.882 42.716 1.0 100.0 ? ? ? ? ? ? 396 LYS BA CG 1 279 B B +ATOM 10177 C CD . LYS BA 1 279 ? -44.478 11.010 43.714 1.0 95.0 ? ? ? ? ? ? 396 LYS BA CD 1 279 B B +ATOM 10178 C CE . LYS BA 1 279 ? -44.005 12.274 43.031 1.0 100.0 ? ? ? ? ? ? 396 LYS BA CE 1 279 B B +ATOM 10179 N NZ . LYS BA 1 279 ? -42.636 12.107 42.476 1.0 100.0 ? ? ? ? ? ? 396 LYS BA NZ 1 279 B B +ATOM 10180 N N . GLU BA 1 280 ? -43.418 6.435 42.161 1.0 90.43 ? ? ? ? ? ? 397 GLU BA N 1 280 B B +ATOM 10181 C CA . GLU BA 1 280 ? -42.207 6.079 41.431 1.0 99.6 ? ? ? ? ? ? 397 GLU BA CA 1 280 B B +ATOM 10182 C C . GLU BA 1 280 ? -42.394 5.020 40.345 1.0 100.0 ? ? ? ? ? ? 397 GLU BA C 1 280 B B +ATOM 10183 O O . GLU BA 1 280 ? -41.712 5.052 39.320 1.0 100.0 ? ? ? ? ? ? 397 GLU BA O 1 280 B B +ATOM 10184 C CB . GLU BA 1 280 ? -41.131 5.646 42.422 1.0 93.35 ? ? ? ? ? ? 397 GLU BA CB 1 280 B B +ATOM 10185 C CG . GLU BA 1 280 ? -40.804 6.722 43.449 1.0 100.0 ? ? ? ? ? ? 397 GLU BA CG 1 280 B B +ATOM 10186 C CD . GLU BA 1 280 ? -40.338 8.020 42.805 1.0 100.0 ? ? ? ? ? ? 397 GLU BA CD 1 280 B B +ATOM 10187 O OE1 . GLU BA 1 280 ? -39.545 7.954 41.842 1.0 100.0 ? ? ? ? ? ? 397 GLU BA OE1 1 280 B B +ATOM 10188 O OE2 . GLU BA 1 280 ? -40.758 9.106 43.261 1.0 94.05 ? ? ? ? ? ? 397 GLU BA OE2 1 280 B B +ATOM 10189 N N . LYS BA 1 281 ? -43.296 4.070 40.568 1.0 100.0 ? ? ? ? ? ? 398 LYS BA N 1 281 B B +ATOM 10190 C CA . LYS BA 1 281 ? -43.547 3.054 39.548 1.0 95.06 ? ? ? ? ? ? 398 LYS BA CA 1 281 B B +ATOM 10191 C C . LYS BA 1 281 ? -44.397 3.737 38.473 1.0 87.87 ? ? ? ? ? ? 398 LYS BA C 1 281 B B +ATOM 10192 O O . LYS BA 1 281 ? -44.398 3.348 37.300 1.0 73.44 ? ? ? ? ? ? 398 LYS BA O 1 281 B B +ATOM 10193 C CB . LYS BA 1 281 ? -44.300 1.851 40.135 1.0 83.62 ? ? ? ? ? ? 398 LYS BA CB 1 281 B B +ATOM 10194 C CG . LYS BA 1 281 ? -44.873 2.050 41.535 1.0 72.13 ? ? ? ? ? ? 398 LYS BA CG 1 281 B B +ATOM 10195 C CD . LYS BA 1 281 ? -45.211 0.703 42.158 1.0 71.94 ? ? ? ? ? ? 398 LYS BA CD 1 281 B B +ATOM 10196 C CE . LYS BA 1 281 ? -45.567 0.836 43.627 1.0 67.41 ? ? ? ? ? ? 398 LYS BA CE 1 281 B B +ATOM 10197 N NZ . LYS BA 1 281 ? -45.541 -0.475 44.344 1.0 66.81 ? ? ? ? ? ? 398 LYS BA NZ 1 281 B B +ATOM 10198 N N . VAL BA 1 282 ? -45.114 4.771 38.897 1.0 79.57 ? ? ? ? ? ? 399 VAL BA N 1 282 B B +ATOM 10199 C CA . VAL BA 1 282 ? -45.961 5.550 38.007 1.0 80.28 ? ? ? ? ? ? 399 VAL BA CA 1 282 B B +ATOM 10200 C C . VAL BA 1 282 ? -45.056 6.379 37.113 1.0 82.73 ? ? ? ? ? ? 399 VAL BA C 1 282 B B +ATOM 10201 O O . VAL BA 1 282 ? -45.225 6.416 35.896 1.0 82.05 ? ? ? ? ? ? 399 VAL BA O 1 282 B B +ATOM 10202 C CB . VAL BA 1 282 ? -46.876 6.483 38.815 1.0 85.05 ? ? ? ? ? ? 399 VAL BA CB 1 282 B B +ATOM 10203 C CG1 . VAL BA 1 282 ? -47.485 7.556 37.917 1.0 72.36 ? ? ? ? ? ? 399 VAL BA CG1 1 282 B B +ATOM 10204 C CG2 . VAL BA 1 282 ? -47.957 5.666 39.474 1.0 95.57 ? ? ? ? ? ? 399 VAL BA CG2 1 282 B B +ATOM 10205 N N . ARG BA 1 283 ? -44.100 7.055 37.738 1.0 92.2 ? ? ? ? ? ? 400 ARG BA N 1 283 B B +ATOM 10206 C CA . ARG BA 1 283 ? -43.144 7.867 37.005 1.0 96.0 ? ? ? ? ? ? 400 ARG BA CA 1 283 B B +ATOM 10207 C C . ARG BA 1 283 ? -42.475 6.935 36.014 1.0 94.18 ? ? ? ? ? ? 400 ARG BA C 1 283 B B +ATOM 10208 O O . ARG BA 1 283 ? -42.234 7.293 34.862 1.0 93.17 ? ? ? ? ? ? 400 ARG BA O 1 283 B B +ATOM 10209 C CB . ARG BA 1 283 ? -42.096 8.446 37.959 1.0 100.0 ? ? ? ? ? ? 400 ARG BA CB 1 283 B B +ATOM 10210 C CG . ARG BA 1 283 ? -42.499 9.763 38.601 1.0 100.0 ? ? ? ? ? ? 400 ARG BA CG 1 283 B B +ATOM 10211 C CD . ARG BA 1 283 ? -41.288 10.559 39.051 1.0 100.0 ? ? ? ? ? ? 400 ARG BA CD 1 283 B B +ATOM 10212 N NE . ARG BA 1 283 ? -40.402 10.864 37.931 1.0 100.0 ? ? ? ? ? ? 400 ARG BA NE 1 283 B B +ATOM 10213 C CZ . ARG BA 1 283 ? -40.290 12.063 37.373 1.0 100.0 ? ? ? ? ? ? 400 ARG BA CZ 1 283 B B +ATOM 10214 N NH1 . ARG BA 1 283 ? -41.016 13.080 37.823 1.0 93.15 ? ? ? ? ? ? 400 ARG BA NH1 1 283 B B +ATOM 10215 N NH2 . ARG BA 1 283 ? -39.455 12.245 36.360 1.0 100.0 ? ? ? ? ? ? 400 ARG BA NH2 1 283 B B +ATOM 10216 N N . ASN BA 1 284 ? -42.174 5.729 36.487 1.0 93.64 ? ? ? ? ? ? 401 ASN BA N 1 284 B B +ATOM 10217 C CA . ASN BA 1 284 ? -41.545 4.710 35.662 1.0 100.0 ? ? ? ? ? ? 401 ASN BA CA 1 284 B B +ATOM 10218 C C . ASN BA 1 284 ? -42.469 4.407 34.494 1.0 100.0 ? ? ? ? ? ? 401 ASN BA C 1 284 B B +ATOM 10219 O O . ASN BA 1 284 ? -42.063 4.471 33.332 1.0 100.0 ? ? ? ? ? ? 401 ASN BA O 1 284 B B +ATOM 10220 C CB . ASN BA 1 284 ? -41.306 3.439 36.478 1.0 100.0 ? ? ? ? ? ? 401 ASN BA CB 1 284 B B +ATOM 10221 C CG . ASN BA 1 284 ? -39.866 3.293 36.919 1.0 100.0 ? ? ? ? ? ? 401 ASN BA CG 1 284 B B +ATOM 10222 O OD1 . ASN BA 1 284 ? -39.368 2.183 37.100 1.0 100.0 ? ? ? ? ? ? 401 ASN BA OD1 1 284 B B +ATOM 10223 N ND2 . ASN BA 1 284 ? -39.184 4.423 37.091 1.0 100.0 ? ? ? ? ? ? 401 ASN BA ND2 1 284 B B +ATOM 10224 N N . PHE BA 1 285 ? -43.715 4.069 34.816 1.0 93.04 ? ? ? ? ? ? 402 PHE BA N 1 285 B B +ATOM 10225 C CA . PHE BA 1 285 ? -44.713 3.774 33.796 1.0 91.07 ? ? ? ? ? ? 402 PHE BA CA 1 285 B B +ATOM 10226 C C . PHE BA 1 285 ? -44.869 5.019 32.936 1.0 92.04 ? ? ? ? ? ? 402 PHE BA C 1 285 B B +ATOM 10227 O O . PHE BA 1 285 ? -45.270 4.947 31.773 1.0 74.85 ? ? ? ? ? ? 402 PHE BA O 1 285 B B +ATOM 10228 C CB . PHE BA 1 285 ? -46.053 3.430 34.443 1.0 86.42 ? ? ? ? ? ? 402 PHE BA CB 1 285 B B +ATOM 10229 C CG . PHE BA 1 285 ? -47.013 2.742 33.519 1.0 94.63 ? ? ? ? ? ? 402 PHE BA CG 1 285 B B +ATOM 10230 C CD1 . PHE BA 1 285 ? -46.780 1.436 33.107 1.0 96.48 ? ? ? ? ? ? 402 PHE BA CD1 1 285 B B +ATOM 10231 C CD2 . PHE BA 1 285 ? -48.152 3.395 33.061 1.0 98.63 ? ? ? ? ? ? 402 PHE BA CD2 1 285 B B +ATOM 10232 C CE1 . PHE BA 1 285 ? -47.669 0.788 32.254 1.0 97.75 ? ? ? ? ? ? 402 PHE BA CE1 1 285 B B +ATOM 10233 C CE2 . PHE BA 1 285 ? -49.048 2.755 32.207 1.0 98.92 ? ? ? ? ? ? 402 PHE BA CE2 1 285 B B +ATOM 10234 C CZ . PHE BA 1 285 ? -48.805 1.451 31.803 1.0 93.38 ? ? ? ? ? ? 402 PHE BA CZ 1 285 B B +ATOM 10235 N N . ALA BA 1 286 ? -44.551 6.163 33.533 1.0 91.11 ? ? ? ? ? ? 403 ALA BA N 1 286 B B +ATOM 10236 C CA . ALA BA 1 286 ? -44.629 7.443 32.849 1.0 78.32 ? ? ? ? ? ? 403 ALA BA CA 1 286 B B +ATOM 10237 C C . ALA BA 1 286 ? -43.430 7.537 31.919 1.0 75.97 ? ? ? ? ? ? 403 ALA BA C 1 286 B B +ATOM 10238 O O . ALA BA 1 286 ? -43.545 8.004 30.787 1.0 91.47 ? ? ? ? ? ? 403 ALA BA O 1 286 B B +ATOM 10239 C CB . ALA BA 1 286 ? -44.601 8.582 33.859 1.0 59.2 ? ? ? ? ? ? 403 ALA BA CB 1 286 B B +ATOM 10240 N N . ALA BA 1 287 ? -42.276 7.089 32.405 1.0 56.75 ? ? ? ? ? ? 404 ALA BA N 1 287 B B +ATOM 10241 C CA . ALA BA 1 287 ? -41.060 7.114 31.605 1.0 62.82 ? ? ? ? ? ? 404 ALA BA CA 1 287 B B +ATOM 10242 C C . ALA BA 1 287 ? -41.233 6.111 30.478 1.0 68.19 ? ? ? ? ? ? 404 ALA BA C 1 287 B B +ATOM 10243 O O . ALA BA 1 287 ? -40.567 6.192 29.444 1.0 76.83 ? ? ? ? ? ? 404 ALA BA O 1 287 B B +ATOM 10244 C CB . ALA BA 1 287 ? -39.860 6.746 32.456 1.0 78.44 ? ? ? ? ? ? 404 ALA BA CB 1 287 B B +ATOM 10245 N N . THR BA 1 288 ? -42.138 5.161 30.691 1.0 62.58 ? ? ? ? ? ? 405 THR BA N 1 288 B B +ATOM 10246 C CA . THR BA 1 288 ? -42.427 4.144 29.686 1.0 75.32 ? ? ? ? ? ? 405 THR BA CA 1 288 B B +ATOM 10247 C C . THR BA 1 288 ? -43.187 4.798 28.529 1.0 72.06 ? ? ? ? ? ? 405 THR BA C 1 288 B B +ATOM 10248 O O . THR BA 1 288 ? -42.999 4.445 27.363 1.0 73.32 ? ? ? ? ? ? 405 THR BA O 1 288 B B +ATOM 10249 C CB . THR BA 1 288 ? -43.294 3.010 30.272 1.0 73.78 ? ? ? ? ? ? 405 THR BA CB 1 288 B B +ATOM 10250 O OG1 . THR BA 1 288 ? -42.760 2.606 31.537 1.0 95.88 ? ? ? ? ? ? 405 THR BA OG1 1 288 B B +ATOM 10251 C CG2 . THR BA 1 288 ? -43.313 1.817 29.327 1.0 67.17 ? ? ? ? ? ? 405 THR BA CG2 1 288 B B +ATOM 10252 N N . ILE BA 1 289 ? -44.043 5.755 28.872 1.0 57.19 ? ? ? ? ? ? 406 ILE BA N 1 289 B B +ATOM 10253 C CA . ILE BA 1 289 ? -44.841 6.474 27.887 1.0 54.5 ? ? ? ? ? ? 406 ILE BA CA 1 289 B B +ATOM 10254 C C . ILE BA 1 289 ? -43.960 7.141 26.840 1.0 55.94 ? ? ? ? ? ? 406 ILE BA C 1 289 B B +ATOM 10255 O O . ILE BA 1 289 ? -43.282 8.136 27.117 1.0 57.55 ? ? ? ? ? ? 406 ILE BA O 1 289 B B +ATOM 10256 C CB . ILE BA 1 289 ? -45.709 7.566 28.553 1.0 71.06 ? ? ? ? ? ? 406 ILE BA CB 1 289 B B +ATOM 10257 C CG1 . ILE BA 1 289 ? -46.354 7.009 29.827 1.0 65.5 ? ? ? ? ? ? 406 ILE BA CG1 1 289 B B +ATOM 10258 C CG2 . ILE BA 1 289 ? -46.761 8.065 27.565 1.0 59.64 ? ? ? ? ? ? 406 ILE BA CG2 1 289 B B +ATOM 10259 C CD1 . ILE BA 1 289 ? -47.199 5.769 29.614 1.0 69.61 ? ? ? ? ? ? 406 ILE BA CD1 1 289 B B +ATOM 10260 N N . PRO BA 1 290 ? -43.977 6.613 25.609 1.0 54.54 ? ? ? ? ? ? 407 PRO BA N 1 290 B B +ATOM 10261 C CA . PRO BA 1 290 ? -43.177 7.160 24.511 1.0 49.13 ? ? ? ? ? ? 407 PRO BA CA 1 290 B B +ATOM 10262 C C . PRO BA 1 290 ? -43.760 8.449 23.927 1.0 47.38 ? ? ? ? ? ? 407 PRO BA C 1 290 B B +ATOM 10263 O O . PRO BA 1 290 ? -44.663 8.407 23.093 1.0 52.3 ? ? ? ? ? ? 407 PRO BA O 1 290 B B +ATOM 10264 C CB . PRO BA 1 290 ? -43.143 6.020 23.486 1.0 50.96 ? ? ? ? ? ? 407 PRO BA CB 1 290 B B +ATOM 10265 C CG . PRO BA 1 290 ? -43.956 4.883 24.096 1.0 61.37 ? ? ? ? ? ? 407 PRO BA CG 1 290 B B +ATOM 10266 C CD . PRO BA 1 290 ? -44.787 5.470 25.173 1.0 58.57 ? ? ? ? ? ? 407 PRO BA CD 1 290 B B +ATOM 10267 N N . ARG BA 1 291 ? -43.233 9.587 24.379 1.0 48.85 ? ? ? ? ? ? 408 ARG BA N 1 291 B B +ATOM 10268 C CA . ARG BA 1 291 ? -43.654 10.913 23.917 1.0 56.74 ? ? ? ? ? ? 408 ARG BA CA 1 291 B B +ATOM 10269 C C . ARG BA 1 291 ? -42.453 11.605 23.273 1.0 59.82 ? ? ? ? ? ? 408 ARG BA C 1 291 B B +ATOM 10270 O O . ARG BA 1 291 ? -41.345 11.548 23.806 1.0 73.93 ? ? ? ? ? ? 408 ARG BA O 1 291 B B +ATOM 10271 C CB . ARG BA 1 291 ? -44.148 11.760 25.098 1.0 79.31 ? ? ? ? ? ? 408 ARG BA CB 1 291 B B +ATOM 10272 C CG . ARG BA 1 291 ? -45.535 11.403 25.614 1.0 96.41 ? ? ? ? ? ? 408 ARG BA CG 1 291 B B +ATOM 10273 C CD . ARG BA 1 291 ? -46.364 12.652 25.907 1.0 89.26 ? ? ? ? ? ? 408 ARG BA CD 1 291 B B +ATOM 10274 N NE . ARG BA 1 291 ? -45.750 13.511 26.917 1.0 61.83 ? ? ? ? ? ? 408 ARG BA NE 1 291 B B +ATOM 10275 C CZ . ARG BA 1 291 ? -45.599 13.177 28.193 1.0 62.62 ? ? ? ? ? ? 408 ARG BA CZ 1 291 B B +ATOM 10276 N NH1 . ARG BA 1 291 ? -46.016 11.998 28.630 1.0 55.94 ? ? ? ? ? ? 408 ARG BA NH1 1 291 B B +ATOM 10277 N NH2 . ARG BA 1 291 ? -45.027 14.023 29.035 1.0 79.75 ? ? ? ? ? ? 408 ARG BA NH2 1 291 B B +ATOM 10278 N N . PRO BA 1 292 ? -42.663 12.298 22.138 1.0 50.99 ? ? ? ? ? ? 409 PRO BA N 1 292 B B +ATOM 10279 C CA . PRO BA 1 292 ? -41.543 12.976 21.469 1.0 53.84 ? ? ? ? ? ? 409 PRO BA CA 1 292 B B +ATOM 10280 C C . PRO BA 1 292 ? -40.961 14.160 22.235 1.0 64.96 ? ? ? ? ? ? 409 PRO BA C 1 292 B B +ATOM 10281 O O . PRO BA 1 292 ? -40.270 15.005 21.663 1.0 66.01 ? ? ? ? ? ? 409 PRO BA O 1 292 B B +ATOM 10282 C CB . PRO BA 1 292 ? -42.121 13.400 20.116 1.0 59.3 ? ? ? ? ? ? 409 PRO BA CB 1 292 B B +ATOM 10283 C CG . PRO BA 1 292 ? -43.508 12.809 20.052 1.0 71.67 ? ? ? ? ? ? 409 PRO BA CG 1 292 B B +ATOM 10284 C CD . PRO BA 1 292 ? -43.938 12.546 21.454 1.0 64.79 ? ? ? ? ? ? 409 PRO BA CD 1 292 B B +ATOM 10285 N N . PHE BA 1 293 ? -41.237 14.211 23.535 1.0 74.36 ? ? ? ? ? ? 410 PHE BA N 1 293 B B +ATOM 10286 C CA . PHE BA 1 293 ? -40.751 15.300 24.379 1.0 68.36 ? ? ? ? ? ? 410 PHE BA CA 1 293 B B +ATOM 10287 C C . PHE BA 1 293 ? -41.091 15.081 25.853 1.0 66.39 ? ? ? ? ? ? 410 PHE BA C 1 293 B B +ATOM 10288 O O . PHE BA 1 293 ? -41.496 13.988 26.268 1.0 56.3 ? ? ? ? ? ? 410 PHE BA O 1 293 B B +ATOM 10289 C CB . PHE BA 1 293 ? -41.371 16.629 23.922 1.0 63.35 ? ? ? ? ? ? 410 PHE BA CB 1 293 B B +ATOM 10290 C CG . PHE BA 1 293 ? -42.870 16.563 23.731 1.0 67.61 ? ? ? ? ? ? 410 PHE BA CG 1 293 B B +ATOM 10291 C CD1 . PHE BA 1 293 ? -43.651 15.738 24.540 1.0 68.04 ? ? ? ? ? ? 410 PHE BA CD1 1 293 B B +ATOM 10292 C CD2 . PHE BA 1 293 ? -43.499 17.301 22.731 1.0 71.61 ? ? ? ? ? ? 410 PHE BA CD2 1 293 B B +ATOM 10293 C CE1 . PHE BA 1 293 ? -45.027 15.648 24.358 1.0 63.36 ? ? ? ? ? ? 410 PHE BA CE1 1 293 B B +ATOM 10294 C CE2 . PHE BA 1 293 ? -44.882 17.219 22.540 1.0 60.66 ? ? ? ? ? ? 410 PHE BA CE2 1 293 B B +ATOM 10295 C CZ . PHE BA 1 293 ? -45.644 16.388 23.357 1.0 62.48 ? ? ? ? ? ? 410 PHE BA CZ 1 293 B B +ATOM 10296 N N . SER BA 1 294 ? -40.931 16.153 26.624 1.0 54.52 ? ? ? ? ? ? 411 SER BA N 1 294 B B +ATOM 10297 C CA . SER BA 1 294 ? -41.215 16.154 28.051 1.0 39.07 ? ? ? ? ? ? 411 SER BA CA 1 294 B B +ATOM 10298 C C . SER BA 1 294 ? -41.919 17.461 28.398 1.0 37.27 ? ? ? ? ? ? 411 SER BA C 1 294 B B +ATOM 10299 O O . SER BA 1 294 ? -41.608 18.505 27.824 1.0 36.77 ? ? ? ? ? ? 411 SER BA O 1 294 B B +ATOM 10300 C CB . SER BA 1 294 ? -39.914 16.043 28.844 1.0 30.32 ? ? ? ? ? ? 411 SER BA CB 1 294 B B +ATOM 10301 O OG . SER BA 1 294 ? -39.737 14.722 29.320 1.0 50.98 ? ? ? ? ? ? 411 SER BA OG 1 294 B B +ATOM 10302 N N . VAL BA 1 295 ? -42.866 17.404 29.330 1.0 35.39 ? ? ? ? ? ? 412 VAL BA N 1 295 B B +ATOM 10303 C CA . VAL BA 1 295 ? -43.602 18.597 29.731 1.0 24.54 ? ? ? ? ? ? 412 VAL BA CA 1 295 B B +ATOM 10304 C C . VAL BA 1 295 ? -43.445 18.855 31.218 1.0 32.26 ? ? ? ? ? ? 412 VAL BA C 1 295 B B +ATOM 10305 O O . VAL BA 1 295 ? -43.294 17.921 32.005 1.0 24.52 ? ? ? ? ? ? 412 VAL BA O 1 295 B B +ATOM 10306 C CB . VAL BA 1 295 ? -45.110 18.464 29.421 1.0 24.31 ? ? ? ? ? ? 412 VAL BA CB 1 295 B B +ATOM 10307 C CG1 . VAL BA 1 295 ? -45.356 18.655 27.935 1.0 23.33 ? ? ? ? ? ? 412 VAL BA CG1 1 295 B B +ATOM 10308 C CG2 . VAL BA 1 295 ? -45.616 17.108 29.876 1.0 32.01 ? ? ? ? ? ? 412 VAL BA CG2 1 295 B B +ATOM 10309 N N . ARG BA 1 296 ? -43.479 20.129 31.592 1.0 37.85 ? ? ? ? ? ? 413 ARG BA N 1 296 B B +ATOM 10310 C CA . ARG BA 1 296 ? -43.350 20.526 32.989 1.0 54.9 ? ? ? ? ? ? 413 ARG BA CA 1 296 B B +ATOM 10311 C C . ARG BA 1 296 ? -44.399 21.571 33.328 1.0 60.27 ? ? ? ? ? ? 413 ARG BA C 1 296 B B +ATOM 10312 O O . ARG BA 1 296 ? -44.631 22.495 32.554 1.0 52.18 ? ? ? ? ? ? 413 ARG BA O 1 296 B B +ATOM 10313 C CB . ARG BA 1 296 ? -41.957 21.099 33.258 1.0 57.85 ? ? ? ? ? ? 413 ARG BA CB 1 296 B B +ATOM 10314 C CG . ARG BA 1 296 ? -41.772 21.645 34.669 1.0 60.82 ? ? ? ? ? ? 413 ARG BA CG 1 296 B B +ATOM 10315 C CD . ARG BA 1 296 ? -41.830 23.168 34.708 1.0 66.38 ? ? ? ? ? ? 413 ARG BA CD 1 296 B B +ATOM 10316 N NE . ARG BA 1 296 ? -41.135 23.778 33.576 1.0 70.92 ? ? ? ? ? ? 413 ARG BA NE 1 296 B B +ATOM 10317 C CZ . ARG BA 1 296 ? -40.871 25.077 33.471 1.0 72.59 ? ? ? ? ? ? 413 ARG BA CZ 1 296 B B +ATOM 10318 N NH1 . ARG BA 1 296 ? -41.244 25.911 34.433 1.0 65.24 ? ? ? ? ? ? 413 ARG BA NH1 1 296 B B +ATOM 10319 N NH2 . ARG BA 1 296 ? -40.230 25.543 32.407 1.0 55.86 ? ? ? ? ? ? 413 ARG BA NH2 1 296 B B +ATOM 10320 N N . TYR BA 1 297 ? -45.037 21.417 34.485 1.0 56.8 ? ? ? ? ? ? 414 TYR BA N 1 297 B B +ATOM 10321 C CA . TYR BA 1 297 ? -46.065 22.357 34.917 1.0 55.62 ? ? ? ? ? ? 414 TYR BA CA 1 297 B B +ATOM 10322 C C . TYR BA 1 297 ? -45.477 23.516 35.721 1.0 53.33 ? ? ? ? ? ? 414 TYR BA C 1 297 B B +ATOM 10323 O O . TYR BA 1 297 ? -44.666 23.309 36.626 1.0 80.67 ? ? ? ? ? ? 414 TYR BA O 1 297 B B +ATOM 10324 C CB . TYR BA 1 297 ? -47.124 21.632 35.758 1.0 57.36 ? ? ? ? ? ? 414 TYR BA CB 1 297 B B +ATOM 10325 C CG . TYR BA 1 297 ? -48.275 22.516 36.186 1.0 71.59 ? ? ? ? ? ? 414 TYR BA CG 1 297 B B +ATOM 10326 C CD1 . TYR BA 1 297 ? -48.966 23.295 35.258 1.0 81.2 ? ? ? ? ? ? 414 TYR BA CD1 1 297 B B +ATOM 10327 C CD2 . TYR BA 1 297 ? -48.669 22.582 37.520 1.0 62.03 ? ? ? ? ? ? 414 TYR BA CD2 1 297 B B +ATOM 10328 C CE1 . TYR BA 1 297 ? -50.020 24.118 35.647 1.0 83.1 ? ? ? ? ? ? 414 TYR BA CE1 1 297 B B +ATOM 10329 C CE2 . TYR BA 1 297 ? -49.721 23.402 37.921 1.0 84.22 ? ? ? ? ? ? 414 TYR BA CE2 1 297 B B +ATOM 10330 C CZ . TYR BA 1 297 ? -50.393 24.167 36.980 1.0 89.09 ? ? ? ? ? ? 414 TYR BA CZ 1 297 B B +ATOM 10331 O OH . TYR BA 1 297 ? -51.437 24.977 37.370 1.0 94.04 ? ? ? ? ? ? 414 TYR BA OH 1 297 B B +ATOM 10332 N N . ASP BA 1 298 ? -45.889 24.736 35.380 1.0 46.78 ? ? ? ? ? ? 415 ASP BA N 1 298 B B +ATOM 10333 C CA . ASP BA 1 298 ? -45.427 25.942 36.069 1.0 45.75 ? ? ? ? ? ? 415 ASP BA CA 1 298 B B +ATOM 10334 C C . ASP BA 1 298 ? -46.574 26.499 36.906 1.0 37.93 ? ? ? ? ? ? 415 ASP BA C 1 298 B B +ATOM 10335 O O . ASP BA 1 298 ? -47.475 27.149 36.385 1.0 42.42 ? ? ? ? ? ? 415 ASP BA O 1 298 B B +ATOM 10336 C CB . ASP BA 1 298 ? -44.959 26.997 35.058 1.0 53.54 ? ? ? ? ? ? 415 ASP BA CB 1 298 B B +ATOM 10337 C CG . ASP BA 1 298 ? -43.967 27.983 35.656 1.0 72.49 ? ? ? ? ? ? 415 ASP BA CG 1 298 B B +ATOM 10338 O OD1 . ASP BA 1 298 ? -44.287 28.589 36.700 1.0 81.43 ? ? ? ? ? ? 415 ASP BA OD1 1 298 B B +ATOM 10339 O OD2 . ASP BA 1 298 ? -42.868 28.152 35.086 1.0 68.23 ? ? ? ? ? ? 415 ASP BA OD2 1 298 B B +ATOM 10340 N N . PRO BA 1 299 ? -46.552 26.241 38.221 1.0 34.92 ? ? ? ? ? ? 416 PRO BA N 1 299 B B +ATOM 10341 C CA . PRO BA 1 299 ? -47.589 26.707 39.144 1.0 40.44 ? ? ? ? ? ? 416 PRO BA CA 1 299 B B +ATOM 10342 C C . PRO BA 1 299 ? -47.748 28.215 39.245 1.0 37.13 ? ? ? ? ? ? 416 PRO BA C 1 299 B B +ATOM 10343 O O . PRO BA 1 299 ? -48.777 28.694 39.713 1.0 52.25 ? ? ? ? ? ? 416 PRO BA O 1 299 B B +ATOM 10344 C CB . PRO BA 1 299 ? -47.193 26.090 40.489 1.0 44.31 ? ? ? ? ? ? 416 PRO BA CB 1 299 B B +ATOM 10345 C CG . PRO BA 1 299 ? -46.197 25.047 40.177 1.0 49.92 ? ? ? ? ? ? 416 PRO BA CG 1 299 B B +ATOM 10346 C CD . PRO BA 1 299 ? -45.516 25.464 38.914 1.0 50.32 ? ? ? ? ? ? 416 PRO BA CD 1 299 B B +ATOM 10347 N N . TYR BA 1 300 ? -46.739 28.966 38.814 1.0 28.69 ? ? ? ? ? ? 417 TYR BA N 1 300 B B +ATOM 10348 C CA . TYR BA 1 300 ? -46.804 30.426 38.883 1.0 38.77 ? ? ? ? ? ? 417 TYR BA CA 1 300 B B +ATOM 10349 C C . TYR BA 1 300 ? -47.585 31.001 37.712 1.0 41.07 ? ? ? ? ? ? 417 TYR BA C 1 300 B B +ATOM 10350 O O . TYR BA 1 300 ? -48.443 31.864 37.890 1.0 53.69 ? ? ? ? ? ? 417 TYR BA O 1 300 B B +ATOM 10351 C CB . TYR BA 1 300 ? -45.392 31.028 38.909 1.0 36.92 ? ? ? ? ? ? 417 TYR BA CB 1 300 B B +ATOM 10352 C CG . TYR BA 1 300 ? -44.675 30.856 40.234 1.0 59.52 ? ? ? ? ? ? 417 TYR BA CG 1 300 B B +ATOM 10353 C CD1 . TYR BA 1 300 ? -43.998 29.676 40.532 1.0 74.44 ? ? ? ? ? ? 417 TYR BA CD1 1 300 B B +ATOM 10354 C CD2 . TYR BA 1 300 ? -44.684 31.867 41.197 1.0 63.68 ? ? ? ? ? ? 417 TYR BA CD2 1 300 B B +ATOM 10355 C CE1 . TYR BA 1 300 ? -43.354 29.504 41.756 1.0 65.02 ? ? ? ? ? ? 417 TYR BA CE1 1 300 B B +ATOM 10356 C CE2 . TYR BA 1 300 ? -44.040 31.701 42.426 1.0 54.57 ? ? ? ? ? ? 417 TYR BA CE2 1 300 B B +ATOM 10357 C CZ . TYR BA 1 300 ? -43.378 30.520 42.695 1.0 51.94 ? ? ? ? ? ? 417 TYR BA CZ 1 300 B B +ATOM 10358 O OH . TYR BA 1 300 ? -42.746 30.351 43.903 1.0 52.98 ? ? ? ? ? ? 417 TYR BA OH 1 300 B B +ATOM 10359 N N . THR BA 1 301 ? -47.275 30.521 36.513 1.0 46.91 ? ? ? ? ? ? 418 THR BA N 1 301 B B +ATOM 10360 C CA . THR BA 1 301 ? -47.952 30.977 35.305 1.0 55.02 ? ? ? ? ? ? 418 THR BA CA 1 301 B B +ATOM 10361 C C . THR BA 1 301 ? -49.090 30.022 34.978 1.0 52.04 ? ? ? ? ? ? 418 THR BA C 1 301 B B +ATOM 10362 O O . THR BA 1 301 ? -49.816 30.216 34.003 1.0 69.95 ? ? ? ? ? ? 418 THR BA O 1 301 B B +ATOM 10363 C CB . THR BA 1 301 ? -46.990 31.019 34.103 1.0 57.5 ? ? ? ? ? ? 418 THR BA CB 1 301 B B +ATOM 10364 O OG1 . THR BA 1 301 ? -46.453 29.710 33.873 1.0 56.66 ? ? ? ? ? ? 418 THR BA OG1 1 301 B B +ATOM 10365 C CG2 . THR BA 1 301 ? -45.858 31.978 34.371 1.0 61.75 ? ? ? ? ? ? 418 THR BA CG2 1 301 B B +ATOM 10366 N N . GLN BA 1 302 ? -49.241 28.993 35.805 1.0 45.36 ? ? ? ? ? ? 419 GLN BA N 1 302 B B +ATOM 10367 C CA . GLN BA 1 302 ? -50.280 27.985 35.616 1.0 52.53 ? ? ? ? ? ? 419 GLN BA CA 1 302 B B +ATOM 10368 C C . GLN BA 1 302 ? -50.418 27.592 34.146 1.0 48.4 ? ? ? ? ? ? 419 GLN BA C 1 302 B B +ATOM 10369 O O . GLN BA 1 302 ? -51.517 27.433 33.616 1.0 53.82 ? ? ? ? ? ? 419 GLN BA O 1 302 B B +ATOM 10370 C CB . GLN BA 1 302 ? -51.603 28.486 36.194 1.0 62.3 ? ? ? ? ? ? 419 GLN BA CB 1 302 B B +ATOM 10371 C CG . GLN BA 1 302 ? -51.586 28.477 37.721 1.0 92.4 ? ? ? ? ? ? 419 GLN BA CG 1 302 B B +ATOM 10372 C CD . GLN BA 1 302 ? -52.891 28.916 38.350 1.0 100.0 ? ? ? ? ? ? 419 GLN BA CD 1 302 B B +ATOM 10373 O OE1 . GLN BA 1 302 ? -53.760 29.484 37.687 1.0 100.0 ? ? ? ? ? ? 419 GLN BA OE1 1 302 B B +ATOM 10374 N NE2 . GLN BA 1 302 ? -53.033 28.653 39.647 1.0 100.0 ? ? ? ? ? ? 419 GLN BA NE2 1 302 B B +ATOM 10375 N N . ARG BA 1 303 ? -49.260 27.431 33.510 1.0 52.67 ? ? ? ? ? ? 420 ARG BA N 1 303 B B +ATOM 10376 C CA . ARG BA 1 303 ? -49.146 27.041 32.111 1.0 48.06 ? ? ? ? ? ? 420 ARG BA CA 1 303 B B +ATOM 10377 C C . ARG BA 1 303 ? -48.477 25.670 32.103 1.0 44.16 ? ? ? ? ? ? 420 ARG BA C 1 303 B B +ATOM 10378 O O . ARG BA 1 303 ? -47.945 25.230 33.121 1.0 52.33 ? ? ? ? ? ? 420 ARG BA O 1 303 B B +ATOM 10379 C CB . ARG BA 1 303 ? -48.225 28.001 31.363 1.0 52.96 ? ? ? ? ? ? 420 ARG BA CB 1 303 B B +ATOM 10380 C CG . ARG BA 1 303 ? -48.865 29.213 30.738 1.0 53.84 ? ? ? ? ? ? 420 ARG BA CG 1 303 B B +ATOM 10381 C CD . ARG BA 1 303 ? -47.749 30.143 30.303 1.0 76.17 ? ? ? ? ? ? 420 ARG BA CD 1 303 B B +ATOM 10382 N NE . ARG BA 1 303 ? -48.163 31.139 29.323 1.0 99.8 ? ? ? ? ? ? 420 ARG BA NE 1 303 B B +ATOM 10383 C CZ . ARG BA 1 303 ? -47.453 32.223 29.024 1.0 100.0 ? ? ? ? ? ? 420 ARG BA CZ 1 303 B B +ATOM 10384 N NH1 . ARG BA 1 303 ? -46.297 32.447 29.638 1.0 88.44 ? ? ? ? ? ? 420 ARG BA NH1 1 303 B B +ATOM 10385 N NH2 . ARG BA 1 303 ? -47.901 33.086 28.122 1.0 100.0 ? ? ? ? ? ? 420 ARG BA NH2 1 303 B B +ATOM 10386 N N . ILE BA 1 304 ? -48.498 25.004 30.955 1.0 26.85 ? ? ? ? ? ? 421 ILE BA N 1 304 B B +ATOM 10387 C CA . ILE BA 1 304 ? -47.847 23.709 30.812 1.0 12.67 ? ? ? ? ? ? 421 ILE BA CA 1 304 B B +ATOM 10388 C C . ILE BA 1 304 ? -46.661 23.973 29.892 1.0 36.59 ? ? ? ? ? ? 421 ILE BA C 1 304 B B +ATOM 10389 O O . ILE BA 1 304 ? -46.843 24.399 28.751 1.0 29.54 ? ? ? ? ? ? 421 ILE BA O 1 304 B B +ATOM 10390 C CB . ILE BA 1 304 ? -48.759 22.664 30.155 1.0 12.33 ? ? ? ? ? ? 421 ILE BA CB 1 304 B B +ATOM 10391 C CG1 . ILE BA 1 304 ? -49.508 21.880 31.234 1.0 18.57 ? ? ? ? ? ? 421 ILE BA CG1 1 304 B B +ATOM 10392 C CG2 . ILE BA 1 304 ? -47.931 21.716 29.298 1.0 5.84 ? ? ? ? ? ? 421 ILE BA CG2 1 304 B B +ATOM 10393 C CD1 . ILE BA 1 304 ? -48.646 20.891 31.983 1.0 21.32 ? ? ? ? ? ? 421 ILE BA CD1 1 304 B B +ATOM 10394 N N . GLU BA 1 305 ? -45.452 23.722 30.392 1.0 59.38 ? ? ? ? ? ? 422 GLU BA N 1 305 B B +ATOM 10395 C CA . GLU BA 1 305 ? -44.228 23.961 29.632 1.0 60.87 ? ? ? ? ? ? 422 GLU BA CA 1 305 B B +ATOM 10396 C C . GLU BA 1 305 ? -43.742 22.763 28.837 1.0 59.7 ? ? ? ? ? ? 422 GLU BA C 1 305 B B +ATOM 10397 O O . GLU BA 1 305 ? -43.487 21.694 29.394 1.0 65.41 ? ? ? ? ? ? 422 GLU BA O 1 305 B B +ATOM 10398 C CB . GLU BA 1 305 ? -43.103 24.410 30.570 1.0 67.51 ? ? ? ? ? ? 422 GLU BA CB 1 305 B B +ATOM 10399 C CG . GLU BA 1 305 ? -43.296 25.795 31.172 1.0 76.03 ? ? ? ? ? ? 422 GLU BA CG 1 305 B B +ATOM 10400 C CD . GLU BA 1 305 ? -43.134 26.907 30.152 1.0 84.53 ? ? ? ? ? ? 422 GLU BA CD 1 305 B B +ATOM 10401 O OE1 . GLU BA 1 305 ? -42.049 27.524 30.112 1.0 97.45 ? ? ? ? ? ? 422 GLU BA OE1 1 305 B B +ATOM 10402 O OE2 . GLU BA 1 305 ? -44.094 27.163 29.394 1.0 81.73 ? ? ? ? ? ? 422 GLU BA OE2 1 305 B B +ATOM 10403 N N . VAL BA 1 306 ? -43.602 22.957 27.529 1.0 61.14 ? ? ? ? ? ? 423 VAL BA N 1 306 B B +ATOM 10404 C CA . VAL BA 1 306 ? -43.118 21.904 26.649 1.0 66.29 ? ? ? ? ? ? 423 VAL BA CA 1 306 B B +ATOM 10405 C C . VAL BA 1 306 ? -41.597 22.023 26.590 1.0 63.63 ? ? ? ? ? ? 423 VAL BA C 1 306 B B +ATOM 10406 O O . VAL BA 1 306 ? -41.055 23.015 26.097 1.0 60.26 ? ? ? ? ? ? 423 VAL BA O 1 306 B B +ATOM 10407 C CB . VAL BA 1 306 ? -43.686 22.039 25.211 1.0 64.16 ? ? ? ? ? ? 423 VAL BA CB 1 306 B B +ATOM 10408 C CG1 . VAL BA 1 306 ? -43.389 20.774 24.421 1.0 54.84 ? ? ? ? ? ? 423 VAL BA CG1 1 306 B B +ATOM 10409 C CG2 . VAL BA 1 306 ? -45.180 22.295 25.253 1.0 70.94 ? ? ? ? ? ? 423 VAL BA CG2 1 306 B B +ATOM 10410 N N . LEU BA 1 307 ? -40.913 21.013 27.111 1.0 63.78 ? ? ? ? ? ? 424 LEU BA N 1 307 B B +ATOM 10411 C CA . LEU BA 1 307 ? -39.461 21.013 27.112 1.0 55.0 ? ? ? ? ? ? 424 LEU BA CA 1 307 B B +ATOM 10412 C C . LEU BA 1 307 ? -38.961 20.338 25.848 1.0 62.6 ? ? ? ? ? ? 424 LEU BA C 1 307 B B +ATOM 10413 O O . LEU BA 1 307 ? -38.977 19.111 25.737 1.0 69.94 ? ? ? ? ? ? 424 LEU BA O 1 307 B B +ATOM 10414 C CB . LEU BA 1 307 ? -38.936 20.283 28.353 1.0 55.01 ? ? ? ? ? ? 424 LEU BA CB 1 307 B B +ATOM 10415 C CG . LEU BA 1 307 ? -39.552 20.730 29.682 1.0 47.53 ? ? ? ? ? ? 424 LEU BA CG 1 307 B B +ATOM 10416 C CD1 . LEU BA 1 307 ? -39.270 19.683 30.739 1.0 44.35 ? ? ? ? ? ? 424 LEU BA CD1 1 307 B B +ATOM 10417 C CD2 . LEU BA 1 307 ? -39.001 22.089 30.090 1.0 31.73 ? ? ? ? ? ? 424 LEU BA CD2 1 307 B B +ATOM 10418 N N . ASP BA 1 308 ? -38.527 21.156 24.893 1.0 68.96 ? ? ? ? ? ? 425 ASP BA N 1 308 B B +ATOM 10419 C CA . ASP BA 1 308 ? -38.012 20.667 23.622 1.0 76.54 ? ? ? ? ? ? 425 ASP BA CA 1 308 B B +ATOM 10420 C C . ASP BA 1 308 ? -36.833 21.531 23.195 1.0 80.36 ? ? ? ? ? ? 425 ASP BA C 1 308 B B +ATOM 10421 O O . ASP BA 1 308 ? -35.970 21.087 22.440 1.0 92.65 ? ? ? ? ? ? 425 ASP BA O 1 308 B B +ATOM 10422 C CB . ASP BA 1 308 ? -39.102 20.722 22.548 1.0 75.64 ? ? ? ? ? ? 425 ASP BA CB 1 308 B B +ATOM 10423 C CG . ASP BA 1 308 ? -39.726 22.102 22.422 1.0 84.75 ? ? ? ? ? ? 425 ASP BA CG 1 308 B B +ATOM 10424 O OD1 . ASP BA 1 308 ? -40.445 22.516 23.353 1.0 93.24 ? ? ? ? ? ? 425 ASP BA OD1 1 308 B B +ATOM 10425 O OD2 . ASP BA 1 308 ? -39.501 22.775 21.394 1.0 91.9 ? ? ? ? ? ? 425 ASP BA OD2 1 308 B B +ATOM 10426 N N . ASN BA 1 309 ? -36.803 22.768 23.685 1.0 76.24 ? ? ? ? ? ? 426 ASN BA N 1 309 B B +ATOM 10427 C CA . ASN BA 1 309 ? -35.728 23.686 23.350 1.0 71.04 ? ? ? ? ? ? 426 ASN BA CA 1 309 B B +ATOM 10428 C C . ASN BA 1 309 ? -34.629 23.674 24.402 1.0 75.63 ? ? ? ? ? ? 426 ASN BA C 1 309 B B +ATOM 10429 O O . ASN BA 1 309 ? -34.873 23.359 25.566 1.0 83.46 ? ? ? ? ? ? 426 ASN BA O 1 309 B B +ATOM 10430 C CB . ASN BA 1 309 ? -36.265 25.106 23.197 1.0 80.23 ? ? ? ? ? ? 426 ASN BA CB 1 309 B B +ATOM 10431 C CG . ASN BA 1 309 ? -35.262 26.030 22.543 1.0 100.0 ? ? ? ? ? ? 426 ASN BA CG 1 309 B B +ATOM 10432 O OD1 . ASN BA 1 309 ? -35.252 27.235 22.791 1.0 100.0 ? ? ? ? ? ? 426 ASN BA OD1 1 309 B B +ATOM 10433 N ND2 . ASN BA 1 309 ? -34.406 25.466 21.696 1.0 100.0 ? ? ? ? ? ? 426 ASN BA ND2 1 309 B B +ATOM 10434 N N . THR BA 1 310 ? -33.417 24.031 23.983 1.0 81.33 ? ? ? ? ? ? 427 THR BA N 1 310 B B +ATOM 10435 C CA . THR BA 1 310 ? -32.273 24.058 24.885 1.0 80.19 ? ? ? ? ? ? 427 THR BA CA 1 310 B B +ATOM 10436 C C . THR BA 1 310 ? -32.380 25.145 25.947 1.0 70.69 ? ? ? ? ? ? 427 THR BA C 1 310 B B +ATOM 10437 O O . THR BA 1 310 ? -31.761 25.040 27.004 1.0 79.7 ? ? ? ? ? ? 427 THR BA O 1 310 B B +ATOM 10438 C CB . THR BA 1 310 ? -30.955 24.265 24.113 1.0 83.76 ? ? ? ? ? ? 427 THR BA CB 1 310 B B +ATOM 10439 O OG1 . THR BA 1 310 ? -31.023 25.489 23.372 1.0 87.74 ? ? ? ? ? ? 427 THR BA OG1 1 310 B B +ATOM 10440 C CG2 . THR BA 1 310 ? -30.709 23.107 23.163 1.0 76.68 ? ? ? ? ? ? 427 THR BA CG2 1 310 B B +ATOM 10441 N N . GLN BA 1 311 ? -33.155 26.189 25.671 1.0 49.69 ? ? ? ? ? ? 428 GLN BA N 1 311 B B +ATOM 10442 C CA . GLN BA 1 311 ? -33.320 27.267 26.642 1.0 52.53 ? ? ? ? ? ? 428 GLN BA CA 1 311 B B +ATOM 10443 C C . GLN BA 1 311 ? -34.426 26.903 27.623 1.0 51.11 ? ? ? ? ? ? 428 GLN BA C 1 311 B B +ATOM 10444 O O . GLN BA 1 311 ? -34.487 27.429 28.734 1.0 41.08 ? ? ? ? ? ? 428 GLN BA O 1 311 B B +ATOM 10445 C CB . GLN BA 1 311 ? -33.651 28.587 25.941 1.0 66.13 ? ? ? ? ? ? 428 GLN BA CB 1 311 B B +ATOM 10446 C CG . GLN BA 1 311 ? -32.503 29.598 25.951 1.0 90.15 ? ? ? ? ? ? 428 GLN BA CG 1 311 B B +ATOM 10447 C CD . GLN BA 1 311 ? -32.610 30.617 27.081 1.0 86.66 ? ? ? ? ? ? 428 GLN BA CD 1 311 B B +ATOM 10448 O OE1 . GLN BA 1 311 ? -33.539 30.576 27.890 1.0 83.0 ? ? ? ? ? ? 428 GLN BA OE1 1 311 B B +ATOM 10449 N NE2 . GLN BA 1 311 ? -31.654 31.539 27.137 1.0 61.4 ? ? ? ? ? ? 428 GLN BA NE2 1 311 B B +ATOM 10450 N N . GLN BA 1 312 ? -35.296 25.994 27.199 1.0 58.96 ? ? ? ? ? ? 429 GLN BA N 1 312 B B +ATOM 10451 C CA . GLN BA 1 312 ? -36.390 25.532 28.036 1.0 63.52 ? ? ? ? ? ? 429 GLN BA CA 1 312 B B +ATOM 10452 C C . GLN BA 1 312 ? -35.810 24.788 29.235 1.0 54.99 ? ? ? ? ? ? 429 GLN BA C 1 312 B B +ATOM 10453 O O . GLN BA 1 312 ? -36.377 24.801 30.326 1.0 69.7 ? ? ? ? ? ? 429 GLN BA O 1 312 B B +ATOM 10454 C CB . GLN BA 1 312 ? -37.301 24.592 27.239 1.0 79.59 ? ? ? ? ? ? 429 GLN BA CB 1 312 B B +ATOM 10455 C CG . GLN BA 1 312 ? -38.460 25.287 26.540 1.0 81.71 ? ? ? ? ? ? 429 GLN BA CG 1 312 B B +ATOM 10456 C CD . GLN BA 1 312 ? -39.412 25.955 27.511 1.0 78.96 ? ? ? ? ? ? 429 GLN BA CD 1 312 B B +ATOM 10457 O OE1 . GLN BA 1 312 ? -40.308 25.316 28.058 1.0 84.65 ? ? ? ? ? ? 429 GLN BA OE1 1 312 B B +ATOM 10458 N NE2 . GLN BA 1 312 ? -39.218 27.250 27.735 1.0 58.71 ? ? ? ? ? ? 429 GLN BA NE2 1 312 B B +ATOM 10459 N N . LEU BA 1 313 ? -34.669 24.142 29.017 1.0 40.34 ? ? ? ? ? ? 430 LEU BA N 1 313 B B +ATOM 10460 C CA . LEU BA 1 313 ? -34.003 23.379 30.064 1.0 44.53 ? ? ? ? ? ? 430 LEU BA CA 1 313 B B +ATOM 10461 C C . LEU BA 1 313 ? -33.127 24.257 30.953 1.0 49.41 ? ? ? ? ? ? 430 LEU BA C 1 313 B B +ATOM 10462 O O . LEU BA 1 313 ? -32.862 23.917 32.105 1.0 49.82 ? ? ? ? ? ? 430 LEU BA O 1 313 B B +ATOM 10463 C CB . LEU BA 1 313 ? -33.173 22.261 29.433 1.0 49.27 ? ? ? ? ? ? 430 LEU BA CB 1 313 B B +ATOM 10464 C CG . LEU BA 1 313 ? -34.026 21.321 28.571 1.0 46.92 ? ? ? ? ? ? 430 LEU BA CG 1 313 B B +ATOM 10465 C CD1 . LEU BA 1 313 ? -33.146 20.457 27.686 1.0 39.85 ? ? ? ? ? ? 430 LEU BA CD1 1 313 B B +ATOM 10466 C CD2 . LEU BA 1 313 ? -34.889 20.463 29.476 1.0 60.57 ? ? ? ? ? ? 430 LEU BA CD2 1 313 B B +ATOM 10467 N N . LYS BA 1 314 ? -32.679 25.386 30.410 1.0 50.79 ? ? ? ? ? ? 431 LYS BA N 1 314 B B +ATOM 10468 C CA . LYS BA 1 314 ? -31.845 26.317 31.159 1.0 49.15 ? ? ? ? ? ? 431 LYS BA CA 1 314 B B +ATOM 10469 C C . LYS BA 1 314 ? -32.599 26.771 32.403 1.0 44.82 ? ? ? ? ? ? 431 LYS BA C 1 314 B B +ATOM 10470 O O . LYS BA 1 314 ? -32.027 26.899 33.487 1.0 55.9 ? ? ? ? ? ? 431 LYS BA O 1 314 B B +ATOM 10471 C CB . LYS BA 1 314 ? -31.524 27.544 30.303 1.0 56.53 ? ? ? ? ? ? 431 LYS BA CB 1 314 B B +ATOM 10472 C CG . LYS BA 1 314 ? -30.372 27.377 29.335 1.0 62.29 ? ? ? ? ? ? 431 LYS BA CG 1 314 B B +ATOM 10473 C CD . LYS BA 1 314 ? -29.941 28.729 28.777 1.0 61.91 ? ? ? ? ? ? 431 LYS BA CD 1 314 B B +ATOM 10474 C CE . LYS BA 1 314 ? -28.965 28.590 27.619 1.0 75.65 ? ? ? ? ? ? 431 LYS BA CE 1 314 B B +ATOM 10475 N NZ . LYS BA 1 314 ? -28.534 29.920 27.106 1.0 72.22 ? ? ? ? ? ? 431 LYS BA NZ 1 314 B B +ATOM 10476 N N . ILE BA 1 315 ? -33.895 27.002 32.227 1.0 45.17 ? ? ? ? ? ? 432 ILE BA N 1 315 B B +ATOM 10477 C CA . ILE BA 1 315 ? -34.761 27.474 33.303 1.0 66.0 ? ? ? ? ? ? 432 ILE BA CA 1 315 B B +ATOM 10478 C C . ILE BA 1 315 ? -35.231 26.410 34.289 1.0 58.78 ? ? ? ? ? ? 432 ILE BA C 1 315 B B +ATOM 10479 O O . ILE BA 1 315 ? -35.398 26.693 35.472 1.0 60.28 ? ? ? ? ? ? 432 ILE BA O 1 315 B B +ATOM 10480 C CB . ILE BA 1 315 ? -35.991 28.206 32.731 1.0 80.32 ? ? ? ? ? ? 432 ILE BA CB 1 315 B B +ATOM 10481 C CG1 . ILE BA 1 315 ? -36.242 27.753 31.288 1.0 88.13 ? ? ? ? ? ? 432 ILE BA CG1 1 315 B B +ATOM 10482 C CG2 . ILE BA 1 315 ? -35.776 29.713 32.815 1.0 94.34 ? ? ? ? ? ? 432 ILE BA CG2 1 315 B B +ATOM 10483 C CD1 . ILE BA 1 315 ? -37.001 28.760 30.433 1.0 100.0 ? ? ? ? ? ? 432 ILE BA CD1 1 315 B B +ATOM 10484 N N . LEU BA 1 316 ? -35.470 25.197 33.811 1.0 48.19 ? ? ? ? ? ? 433 LEU BA N 1 316 B B +ATOM 10485 C CA . LEU BA 1 316 ? -35.891 24.135 34.716 1.0 46.48 ? ? ? ? ? ? 433 LEU BA CA 1 316 B B +ATOM 10486 C C . LEU BA 1 316 ? -34.679 23.854 35.603 1.0 50.62 ? ? ? ? ? ? 433 LEU BA C 1 316 B B +ATOM 10487 O O . LEU BA 1 316 ? -34.804 23.641 36.815 1.0 29.72 ? ? ? ? ? ? 433 LEU BA O 1 316 B B +ATOM 10488 C CB . LEU BA 1 316 ? -36.288 22.875 33.930 1.0 22.61 ? ? ? ? ? ? 433 LEU BA CB 1 316 B B +ATOM 10489 C CG . LEU BA 1 316 ? -36.521 21.580 34.724 1.0 25.63 ? ? ? ? ? ? 433 LEU BA CG 1 316 B B +ATOM 10490 C CD1 . LEU BA 1 316 ? -37.519 21.821 35.831 1.0 23.52 ? ? ? ? ? ? 433 LEU BA CD1 1 316 B B +ATOM 10491 C CD2 . LEU BA 1 316 ? -37.018 20.488 33.795 1.0 21.65 ? ? ? ? ? ? 433 LEU BA CD2 1 316 B B +ATOM 10492 N N . ALA BA 1 317 ? -33.502 23.873 34.980 1.0 47.79 ? ? ? ? ? ? 434 ALA BA N 1 317 B B +ATOM 10493 C CA . ALA BA 1 317 ? -32.254 23.642 35.689 1.0 41.3 ? ? ? ? ? ? 434 ALA BA CA 1 317 B B +ATOM 10494 C C . ALA BA 1 317 ? -32.157 24.649 36.821 1.0 40.66 ? ? ? ? ? ? 434 ALA BA C 1 317 B B +ATOM 10495 O O . ALA BA 1 317 ? -31.833 24.302 37.954 1.0 51.69 ? ? ? ? ? ? 434 ALA BA O 1 317 B B +ATOM 10496 C CB . ALA BA 1 317 ? -31.075 23.807 34.742 1.0 47.23 ? ? ? ? ? ? 434 ALA BA CB 1 317 B B +ATOM 10497 N N . ASP BA 1 318 ? -32.441 25.905 36.500 1.0 30.86 ? ? ? ? ? ? 435 ASP BA N 1 318 B B +ATOM 10498 C CA . ASP BA 1 318 ? -32.392 26.984 37.478 1.0 32.91 ? ? ? ? ? ? 435 ASP BA CA 1 318 B B +ATOM 10499 C C . ASP BA 1 318 ? -33.375 26.751 38.621 1.0 38.97 ? ? ? ? ? ? 435 ASP BA C 1 318 B B +ATOM 10500 O O . ASP BA 1 318 ? -33.053 26.990 39.784 1.0 34.99 ? ? ? ? ? ? 435 ASP BA O 1 318 B B +ATOM 10501 C CB . ASP BA 1 318 ? -32.699 28.315 36.798 1.0 43.61 ? ? ? ? ? ? 435 ASP BA CB 1 318 B B +ATOM 10502 C CG . ASP BA 1 318 ? -31.469 28.954 36.200 1.0 66.74 ? ? ? ? ? ? 435 ASP BA CG 1 318 B B +ATOM 10503 O OD1 . ASP BA 1 318 ? -30.526 29.244 36.964 1.0 84.71 ? ? ? ? ? ? 435 ASP BA OD1 1 318 B B +ATOM 10504 O OD2 . ASP BA 1 318 ? -31.447 29.165 34.968 1.0 83.09 ? ? ? ? ? ? 435 ASP BA OD2 1 318 B B +ATOM 10505 N N . SER BA 1 319 ? -34.571 26.281 38.285 1.0 34.82 ? ? ? ? ? ? 436 SER BA N 1 319 B B +ATOM 10506 C CA . SER BA 1 319 ? -35.588 26.021 39.293 1.0 43.47 ? ? ? ? ? ? 436 SER BA CA 1 319 B B +ATOM 10507 C C . SER BA 1 319 ? -35.033 25.027 40.299 1.0 53.51 ? ? ? ? ? ? 436 SER BA C 1 319 B B +ATOM 10508 O O . SER BA 1 319 ? -35.063 25.256 41.511 1.0 63.67 ? ? ? ? ? ? 436 SER BA O 1 319 B B +ATOM 10509 C CB . SER BA 1 319 ? -36.851 25.449 38.645 1.0 46.54 ? ? ? ? ? ? 436 SER BA CB 1 319 B B +ATOM 10510 O OG . SER BA 1 319 ? -37.273 26.256 37.563 1.0 76.55 ? ? ? ? ? ? 436 SER BA OG 1 319 B B +ATOM 10511 N N . ILE BA 1 320 ? -34.514 23.918 39.786 1.0 48.32 ? ? ? ? ? ? 437 ILE BA N 1 320 B B +ATOM 10512 C CA . ILE BA 1 320 ? -33.951 22.888 40.641 1.0 45.93 ? ? ? ? ? ? 437 ILE BA CA 1 320 B B +ATOM 10513 C C . ILE BA 1 320 ? -32.768 23.421 41.440 1.0 39.76 ? ? ? ? ? ? 437 ILE BA C 1 320 B B +ATOM 10514 O O . ILE BA 1 320 ? -32.751 23.341 42.667 1.0 48.97 ? ? ? ? ? ? 437 ILE BA O 1 320 B B +ATOM 10515 C CB . ILE BA 1 320 ? -33.507 21.684 39.802 1.0 43.57 ? ? ? ? ? ? 437 ILE BA CB 1 320 B B +ATOM 10516 C CG1 . ILE BA 1 320 ? -34.674 21.239 38.919 1.0 42.04 ? ? ? ? ? ? 437 ILE BA CG1 1 320 B B +ATOM 10517 C CG2 . ILE BA 1 320 ? -33.044 20.547 40.706 1.0 48.96 ? ? ? ? ? ? 437 ILE BA CG2 1 320 B B +ATOM 10518 C CD1 . ILE BA 1 320 ? -34.412 19.991 38.106 1.0 39.26 ? ? ? ? ? ? 437 ILE BA CD1 1 320 B B +ATOM 10519 N N . ASN BA 1 321 ? -31.789 23.974 40.736 1.0 33.67 ? ? ? ? ? ? 438 ASN BA N 1 321 B B +ATOM 10520 C CA . ASN BA 1 321 ? -30.594 24.517 41.370 1.0 30.51 ? ? ? ? ? ? 438 ASN BA CA 1 321 B B +ATOM 10521 C C . ASN BA 1 321 ? -30.893 25.287 42.651 1.0 39.75 ? ? ? ? ? ? 438 ASN BA C 1 321 B B +ATOM 10522 O O . ASN BA 1 321 ? -30.247 25.084 43.677 1.0 40.63 ? ? ? ? ? ? 438 ASN BA O 1 321 B B +ATOM 10523 C CB . ASN BA 1 321 ? -29.851 25.428 40.393 1.0 30.24 ? ? ? ? ? ? 438 ASN BA CB 1 321 B B +ATOM 10524 C CG . ASN BA 1 321 ? -28.458 25.782 40.872 1.0 36.18 ? ? ? ? ? ? 438 ASN BA CG 1 321 B B +ATOM 10525 O OD1 . ASN BA 1 321 ? -27.732 24.937 41.391 1.0 54.57 ? ? ? ? ? ? 438 ASN BA OD1 1 321 B B +ATOM 10526 N ND2 . ASN BA 1 321 ? -28.076 27.042 40.696 1.0 48.83 ? ? ? ? ? ? 438 ASN BA ND2 1 321 B B +ATOM 10527 N N . SER BA 1 322 ? -31.875 26.178 42.585 1.0 51.34 ? ? ? ? ? ? 439 SER BA N 1 322 B B +ATOM 10528 C CA . SER BA 1 322 ? -32.248 26.985 43.741 1.0 57.68 ? ? ? ? ? ? 439 SER BA CA 1 322 B B +ATOM 10529 C C . SER BA 1 322 ? -32.931 26.167 44.827 1.0 54.76 ? ? ? ? ? ? 439 SER BA C 1 322 B B +ATOM 10530 O O . SER BA 1 322 ? -32.703 26.387 46.016 1.0 62.9 ? ? ? ? ? ? 439 SER BA O 1 322 B B +ATOM 10531 C CB . SER BA 1 322 ? -33.180 28.120 43.313 1.0 56.79 ? ? ? ? ? ? 439 SER BA CB 1 322 B B +ATOM 10532 O OG . SER BA 1 322 ? -34.463 27.616 42.981 1.0 65.36 ? ? ? ? ? ? 439 SER BA OG 1 322 B B +ATOM 10533 N N . GLU BA 1 323 ? -33.772 25.227 44.411 1.0 51.44 ? ? ? ? ? ? 440 GLU BA N 1 323 B B +ATOM 10534 C CA . GLU BA 1 323 ? -34.507 24.384 45.349 1.0 62.89 ? ? ? ? ? ? 440 GLU BA CA 1 323 B B +ATOM 10535 C C . GLU BA 1 323 ? -33.600 23.466 46.163 1.0 62.26 ? ? ? ? ? ? 440 GLU BA C 1 323 B B +ATOM 10536 O O . GLU BA 1 323 ? -33.861 23.213 47.342 1.0 64.31 ? ? ? ? ? ? 440 GLU BA O 1 323 B B +ATOM 10537 C CB . GLU BA 1 323 ? -35.559 23.567 44.598 1.0 63.42 ? ? ? ? ? ? 440 GLU BA CB 1 323 B B +ATOM 10538 C CG . GLU BA 1 323 ? -36.804 24.363 44.229 1.0 61.16 ? ? ? ? ? ? 440 GLU BA CG 1 323 B B +ATOM 10539 C CD . GLU BA 1 323 ? -38.073 23.544 44.360 1.0 64.23 ? ? ? ? ? ? 440 GLU BA CD 1 323 B B +ATOM 10540 O OE1 . GLU BA 1 323 ? -38.298 22.661 43.506 1.0 63.45 ? ? ? ? ? ? 440 GLU BA OE1 1 323 B B +ATOM 10541 O OE2 . GLU BA 1 323 ? -38.842 23.779 45.316 1.0 72.09 ? ? ? ? ? ? 440 GLU BA OE2 1 323 B B +ATOM 10542 N N . ILE BA 1 324 ? -32.540 22.963 45.538 1.0 55.97 ? ? ? ? ? ? 441 ILE BA N 1 324 B B +ATOM 10543 C CA . ILE BA 1 324 ? -31.608 22.102 46.251 1.0 43.28 ? ? ? ? ? ? 441 ILE BA CA 1 324 B B +ATOM 10544 C C . ILE BA 1 324 ? -30.822 22.993 47.189 1.0 38.75 ? ? ? ? ? ? 441 ILE BA C 1 324 B B +ATOM 10545 O O . ILE BA 1 324 ? -30.577 22.634 48.340 1.0 43.38 ? ? ? ? ? ? 441 ILE BA O 1 324 B B +ATOM 10546 C CB . ILE BA 1 324 ? -30.611 21.409 45.310 1.0 32.29 ? ? ? ? ? ? 441 ILE BA CB 1 324 B B +ATOM 10547 C CG1 . ILE BA 1 324 ? -31.314 20.973 44.026 1.0 44.61 ? ? ? ? ? ? 441 ILE BA CG1 1 324 B B +ATOM 10548 C CG2 . ILE BA 1 324 ? -29.999 20.202 46.011 1.0 31.94 ? ? ? ? ? ? 441 ILE BA CG2 1 324 B B +ATOM 10549 C CD1 . ILE BA 1 324 ? -30.364 20.585 42.916 1.0 55.07 ? ? ? ? ? ? 441 ILE BA CD1 1 324 B B +ATOM 10550 N N . GLY BA 1 325 ? -30.432 24.158 46.681 1.0 34.13 ? ? ? ? ? ? 442 GLY BA N 1 325 B B +ATOM 10551 C CA . GLY BA 1 325 ? -29.680 25.105 47.483 1.0 41.01 ? ? ? ? ? ? 442 GLY BA CA 1 325 B B +ATOM 10552 C C . GLY BA 1 325 ? -30.388 25.307 48.808 1.0 42.69 ? ? ? ? ? ? 442 GLY BA C 1 325 B B +ATOM 10553 O O . GLY BA 1 325 ? -29.767 25.591 49.835 1.0 47.02 ? ? ? ? ? ? 442 GLY BA O 1 325 B B +ATOM 10554 N N . ILE BA 1 326 ? -31.706 25.156 48.777 1.0 24.56 ? ? ? ? ? ? 443 ILE BA N 1 326 B B +ATOM 10555 C CA . ILE BA 1 326 ? -32.519 25.292 49.974 1.0 33.86 ? ? ? ? ? ? 443 ILE BA CA 1 326 B B +ATOM 10556 C C . ILE BA 1 326 ? -32.372 23.999 50.769 1.0 24.72 ? ? ? ? ? ? 443 ILE BA C 1 326 B B +ATOM 10557 O O . ILE BA 1 326 ? -32.092 24.017 51.965 1.0 26.74 ? ? ? ? ? ? 443 ILE BA O 1 326 B B +ATOM 10558 C CB . ILE BA 1 326 ? -33.996 25.504 49.601 1.0 33.65 ? ? ? ? ? ? 443 ILE BA CB 1 326 B B +ATOM 10559 C CG1 . ILE BA 1 326 ? -34.166 26.892 48.980 1.0 18.45 ? ? ? ? ? ? 443 ILE BA CG1 1 326 B B +ATOM 10560 C CG2 . ILE BA 1 326 ? -34.879 25.342 50.826 1.0 31.9 ? ? ? ? ? ? 443 ILE BA CG2 1 326 B B +ATOM 10561 C CD1 . ILE BA 1 326 ? -35.567 27.208 48.534 1.0 28.89 ? ? ? ? ? ? 443 ILE BA CD1 1 326 B B +ATOM 10562 N N . LEU BA 1 327 ? -32.554 22.881 50.072 1.0 24.82 ? ? ? ? ? ? 444 LEU BA N 1 327 B B +ATOM 10563 C CA . LEU BA 1 327 ? -32.447 21.548 50.652 1.0 19.51 ? ? ? ? ? ? 444 LEU BA CA 1 327 B B +ATOM 10564 C C . LEU BA 1 327 ? -31.107 21.343 51.358 1.0 24.69 ? ? ? ? ? ? 444 LEU BA C 1 327 B B +ATOM 10565 O O . LEU BA 1 327 ? -31.033 20.652 52.378 1.0 14.93 ? ? ? ? ? ? 444 LEU BA O 1 327 B B +ATOM 10566 C CB . LEU BA 1 327 ? -32.629 20.500 49.549 1.0 17.16 ? ? ? ? ? ? 444 LEU BA CB 1 327 B B +ATOM 10567 C CG . LEU BA 1 327 ? -32.741 19.019 49.930 1.0 13.22 ? ? ? ? ? ? 444 LEU BA CG 1 327 B B +ATOM 10568 C CD1 . LEU BA 1 327 ? -33.258 18.844 51.346 1.0 5.57 ? ? ? ? ? ? 444 LEU BA CD1 1 327 B B +ATOM 10569 C CD2 . LEU BA 1 327 ? -33.668 18.342 48.948 1.0 25.1 ? ? ? ? ? ? 444 LEU BA CD2 1 327 B B +ATOM 10570 N N . CYS BA 1 328 ? -30.057 21.944 50.805 1.0 16.52 ? ? ? ? ? ? 445 CYS BA N 1 328 B B +ATOM 10571 C CA . CYS BA 1 328 ? -28.718 21.857 51.374 1.0 23.91 ? ? ? ? ? ? 445 CYS BA CA 1 328 B B +ATOM 10572 C C . CYS BA 1 328 ? -28.615 22.713 52.633 1.0 35.9 ? ? ? ? ? ? 445 CYS BA C 1 328 B B +ATOM 10573 O O . CYS BA 1 328 ? -28.308 22.206 53.709 1.0 52.53 ? ? ? ? ? ? 445 CYS BA O 1 328 B B +ATOM 10574 C CB . CYS BA 1 328 ? -27.679 22.329 50.364 1.0 21.95 ? ? ? ? ? ? 445 CYS BA CB 1 328 B B +ATOM 10575 S SG . CYS BA 1 328 ? -27.341 21.149 49.068 1.0 40.86 ? ? ? ? ? ? 445 CYS BA SG 1 328 B B +ATOM 10576 N N . SER BA 1 329 ? -28.870 24.013 52.491 1.0 36.2 ? ? ? ? ? ? 446 SER BA N 1 329 B B +ATOM 10577 C CA . SER BA 1 329 ? -28.809 24.949 53.616 1.0 35.38 ? ? ? ? ? ? 446 SER BA CA 1 329 B B +ATOM 10578 C C . SER BA 1 329 ? -29.597 24.398 54.800 1.0 32.96 ? ? ? ? ? ? 446 SER BA C 1 329 B B +ATOM 10579 O O . SER BA 1 329 ? -29.152 24.470 55.946 1.0 47.99 ? ? ? ? ? ? 446 SER BA O 1 329 B B +ATOM 10580 C CB . SER BA 1 329 ? -29.381 26.308 53.203 1.0 52.34 ? ? ? ? ? ? 446 SER BA CB 1 329 B B +ATOM 10581 O OG . SER BA 1 329 ? -28.617 26.897 52.164 1.0 95.09 ? ? ? ? ? ? 446 SER BA OG 1 329 B B +ATOM 10582 N N . ALA BA 1 330 ? -30.774 23.849 54.509 1.0 22.5 ? ? ? ? ? ? 447 ALA BA N 1 330 B B +ATOM 10583 C CA . ALA BA 1 330 ? -31.629 23.265 55.532 1.0 19.89 ? ? ? ? ? ? 447 ALA BA CA 1 330 B B +ATOM 10584 C C . ALA BA 1 330 ? -30.869 22.122 56.189 1.0 39.54 ? ? ? ? ? ? 447 ALA BA C 1 330 B B +ATOM 10585 O O . ALA BA 1 330 ? -30.659 22.112 57.404 1.0 45.35 ? ? ? ? ? ? 447 ALA BA O 1 330 B B +ATOM 10586 C CB . ALA BA 1 330 ? -32.919 22.742 54.907 1.0 21.1 ? ? ? ? ? ? 447 ALA BA CB 1 330 B B +ATOM 10587 N N . LEU BA 1 331 ? -30.449 21.164 55.369 1.0 52.94 ? ? ? ? ? ? 448 LEU BA N 1 331 B B +ATOM 10588 C CA . LEU BA 1 331 ? -29.706 20.004 55.847 1.0 46.98 ? ? ? ? ? ? 448 LEU BA CA 1 331 B B +ATOM 10589 C C . LEU BA 1 331 ? -28.477 20.417 56.643 1.0 43.58 ? ? ? ? ? ? 448 LEU BA C 1 331 B B +ATOM 10590 O O . LEU BA 1 331 ? -28.184 19.838 57.685 1.0 57.61 ? ? ? ? ? ? 448 LEU BA O 1 331 B B +ATOM 10591 C CB . LEU BA 1 331 ? -29.281 19.130 54.668 1.0 21.33 ? ? ? ? ? ? 448 LEU BA CB 1 331 B B +ATOM 10592 C CG . LEU BA 1 331 ? -30.373 18.209 54.124 1.0 30.43 ? ? ? ? ? ? 448 LEU BA CG 1 331 B B +ATOM 10593 C CD1 . LEU BA 1 331 ? -29.843 17.456 52.921 1.0 22.31 ? ? ? ? ? ? 448 LEU BA CD1 1 331 B B +ATOM 10594 C CD2 . LEU BA 1 331 ? -30.821 17.243 55.208 1.0 19.85 ? ? ? ? ? ? 448 LEU BA CD2 1 331 B B +ATOM 10595 N N . GLN BA 1 332 ? -27.756 21.414 56.143 1.0 31.83 ? ? ? ? ? ? 449 GLN BA N 1 332 B B +ATOM 10596 C CA . GLN BA 1 332 ? -26.556 21.896 56.812 1.0 51.09 ? ? ? ? ? ? 449 GLN BA CA 1 332 B B +ATOM 10597 C C . GLN BA 1 332 ? -26.851 22.371 58.229 1.0 57.6 ? ? ? ? ? ? 449 GLN BA C 1 332 B B +ATOM 10598 O O . GLN BA 1 332 ? -25.966 22.392 59.088 1.0 84.67 ? ? ? ? ? ? 449 GLN BA O 1 332 B B +ATOM 10599 C CB . GLN BA 1 332 ? -25.932 23.054 56.023 1.0 60.51 ? ? ? ? ? ? 449 GLN BA CB 1 332 B B +ATOM 10600 C CG . GLN BA 1 332 ? -25.475 22.693 54.621 1.0 85.66 ? ? ? ? ? ? 449 GLN BA CG 1 332 B B +ATOM 10601 C CD . GLN BA 1 332 ? -24.747 21.366 54.562 1.0 87.05 ? ? ? ? ? ? 449 GLN BA CD 1 332 B B +ATOM 10602 O OE1 . GLN BA 1 332 ? -25.052 20.514 53.726 1.0 92.85 ? ? ? ? ? ? 449 GLN BA OE1 1 332 B B +ATOM 10603 N NE2 . GLN BA 1 332 ? -23.778 21.182 55.451 1.0 86.96 ? ? ? ? ? ? 449 GLN BA NE2 1 332 B B +ATOM 10604 N N . LYS BA 1 333 ? -28.098 22.752 58.471 1.0 51.88 ? ? ? ? ? ? 450 LYS BA N 1 333 B B +ATOM 10605 C CA . LYS BA 1 333 ? -28.484 23.248 59.780 1.0 58.83 ? ? ? ? ? ? 450 LYS BA CA 1 333 B B +ATOM 10606 C C . LYS BA 1 333 ? -29.106 22.190 60.681 1.0 53.86 ? ? ? ? ? ? 450 LYS BA C 1 333 B B +ATOM 10607 O O . LYS BA 1 333 ? -29.615 22.511 61.755 1.0 60.53 ? ? ? ? ? ? 450 LYS BA O 1 333 B B +ATOM 10608 C CB . LYS BA 1 333 ? -29.454 24.417 59.612 1.0 52.01 ? ? ? ? ? ? 450 LYS BA CB 1 333 B B +ATOM 10609 C CG . LYS BA 1 333 ? -28.802 25.660 59.045 1.0 48.95 ? ? ? ? ? ? 450 LYS BA CG 1 333 B B +ATOM 10610 C CD . LYS BA 1 333 ? -29.821 26.746 58.781 1.0 31.16 ? ? ? ? ? ? 450 LYS BA CD 1 333 B B +ATOM 10611 C CE . LYS BA 1 333 ? -29.157 27.972 58.186 1.0 42.41 ? ? ? ? ? ? 450 LYS BA CE 1 333 B B +ATOM 10612 N NZ . LYS BA 1 333 ? -28.450 27.631 56.925 1.0 60.56 ? ? ? ? ? ? 450 LYS BA NZ 1 333 B B +ATOM 10613 N N . ILE BA 1 334 ? -29.057 20.931 60.253 1.0 54.92 ? ? ? ? ? ? 451 ILE BA N 1 334 B B +ATOM 10614 C CA . ILE BA 1 334 ? -29.636 19.851 61.046 1.0 69.53 ? ? ? ? ? ? 451 ILE BA CA 1 334 B B +ATOM 10615 C C . ILE BA 1 334 ? -28.619 18.847 61.575 1.0 70.22 ? ? ? ? ? ? 451 ILE BA C 1 334 B B +ATOM 10616 O O . ILE BA 1 334 ? -28.675 17.656 61.266 1.0 50.03 ? ? ? ? ? ? 451 ILE BA O 1 334 B B +ATOM 10617 C CB . ILE BA 1 334 ? -30.737 19.096 60.254 1.0 76.55 ? ? ? ? ? ? 451 ILE BA CB 1 334 B B +ATOM 10618 C CG1 . ILE BA 1 334 ? -31.498 18.160 61.200 1.0 81.46 ? ? ? ? ? ? 451 ILE BA CG1 1 334 B B +ATOM 10619 C CG2 . ILE BA 1 334 ? -30.125 18.329 59.090 1.0 52.0 ? ? ? ? ? ? 451 ILE BA CG2 1 334 B B +ATOM 10620 C CD1 . ILE BA 1 334 ? -32.206 18.870 62.340 1.0 67.09 ? ? ? ? ? ? 451 ILE BA CD1 1 334 B B +ATOM 10621 N N . LYS BA 1 335 ? -27.689 19.341 62.385 1.0 88.57 ? ? ? ? ? ? 452 LYS BA N 1 335 B B +ATOM 10622 C CA . LYS BA 1 335 ? -26.669 18.492 62.976 1.0 99.23 ? ? ? ? ? ? 452 LYS BA CA 1 335 B B +ATOM 10623 C C . LYS BA 1 335 ? -27.154 18.009 64.348 1.0 100.0 ? ? ? ? ? ? 452 LYS BA C 1 335 B B +ATOM 10624 O O . LYS BA 1 335 ? -27.315 16.781 64.526 1.0 100.0 ? ? ? ? ? ? 452 LYS BA O 1 335 B B +ATOM 10625 C CB . LYS BA 1 335 ? -25.358 19.274 63.123 1.0 91.96 ? ? ? ? ? ? 452 LYS BA CB 1 335 B B +ATOM 10626 C CG . LYS BA 1 335 ? -24.241 18.490 63.783 1.0 84.44 ? ? ? ? ? ? 452 LYS BA CG 1 335 B B +ATOM 10627 C CD . LYS BA 1 335 ? -22.934 19.267 63.760 1.0 72.11 ? ? ? ? ? ? 452 LYS BA CD 1 335 B B +ATOM 10628 C CE . LYS BA 1 335 ? -22.947 20.402 64.770 1.0 71.82 ? ? ? ? ? ? 452 LYS BA CE 1 335 B B +ATOM 10629 N NZ . LYS BA 1 335 ? -22.961 19.895 66.168 1.0 70.5 ? ? ? ? ? ? 452 LYS BA NZ 1 335 B B +ATOM 10630 O OXT . LYS BA 1 335 ? -27.380 18.867 65.228 1.0 100.0 ? ? ? ? ? ? 452 LYS BA OXT 1 335 B B +HETATM 10631 FE FE . FE C 2 . ? 6.443 25.284 42.925 1.0 84.26 ? ? ? ? ? ? 453 FE C FE 1 453 C A +HETATM 10632 FE FE . FE CA 2 . ? -18.675 -18.222 41.075 1.0 84.26 ? ? ? ? ? ? 453 FE CA FE 1 453 C A +HETATM 10633 FE FE . FE D 2 . ? -39.037 51.235 43.684 1.0 91.31 ? ? ? ? ? ? 454 FE D FE 1 454 D B +HETATM 10634 FE FE . FE DA 2 . ? -63.889 8.190 40.316 1.0 91.31 ? ? ? ? ? ? 454 FE DA FE 1 454 D B +# diff --git a/tests/CIF/2pm7_updated.cif b/tests/testdata/mmcif/2pm7_updated.cif similarity index 100% rename from tests/CIF/2pm7_updated.cif rename to tests/testdata/mmcif/2pm7_updated.cif diff --git a/tests/CIF/2w4o.cif b/tests/testdata/mmcif/2w4o.cif similarity index 100% rename from tests/CIF/2w4o.cif rename to tests/testdata/mmcif/2w4o.cif diff --git a/tests/CIF/2w4o_with_error.cif b/tests/testdata/mmcif/2w4o_with_error.cif similarity index 100% rename from tests/CIF/2w4o_with_error.cif rename to tests/testdata/mmcif/2w4o_with_error.cif diff --git a/tests/CIF/3ehk_updated.cif b/tests/testdata/mmcif/3ehk_updated.cif similarity index 100% rename from tests/CIF/3ehk_updated.cif rename to tests/testdata/mmcif/3ehk_updated.cif diff --git a/tests/CIF/3fad.cif b/tests/testdata/mmcif/3fad.cif similarity index 100% rename from tests/CIF/3fad.cif rename to tests/testdata/mmcif/3fad.cif diff --git a/tests/CIF/3fqd_updated.cif b/tests/testdata/mmcif/3fqd_updated.cif similarity index 100% rename from tests/CIF/3fqd_updated.cif rename to tests/testdata/mmcif/3fqd_updated.cif diff --git a/tests/CIF/3mn5.cif b/tests/testdata/mmcif/3mn5.cif similarity index 100% rename from tests/CIF/3mn5.cif rename to tests/testdata/mmcif/3mn5.cif diff --git a/tests/CIF/4abo_updated.cif b/tests/testdata/mmcif/4abo_updated.cif similarity index 100% rename from tests/CIF/4abo_updated.cif rename to tests/testdata/mmcif/4abo_updated.cif diff --git a/tests/CIF/4ibw.cif b/tests/testdata/mmcif/4ibw.cif similarity index 100% rename from tests/CIF/4ibw.cif rename to tests/testdata/mmcif/4ibw.cif diff --git a/tests/CIF/4v9d_updated.cif b/tests/testdata/mmcif/4v9d_updated.cif similarity index 100% rename from tests/CIF/4v9d_updated.cif rename to tests/testdata/mmcif/4v9d_updated.cif diff --git a/tests/CIF/4why_updated.cif b/tests/testdata/mmcif/4why_updated.cif similarity index 100% rename from tests/CIF/4why_updated.cif rename to tests/testdata/mmcif/4why_updated.cif diff --git a/tests/testdata/pdb/1ejg.pdb b/tests/testdata/pdb/1ejg.pdb new file mode 100644 index 0000000..1002d5b --- /dev/null +++ b/tests/testdata/pdb/1ejg.pdb @@ -0,0 +1,1494 @@ +HEADER PLANT PROTEIN 02-MAR-00 1EJG +TITLE CRAMBIN AT ULTRA-HIGH RESOLUTION: VALENCE ELECTRON DENSITY. +COMPND MOL_ID: 1; +COMPND 2 MOLECULE: CRAMBIN (PRO22,SER22/LEU25,ILE25); +COMPND 3 CHAIN: A; +COMPND 4 FRAGMENT: CRAMBIN +SOURCE MOL_ID: 1; +SOURCE 2 ORGANISM_SCIENTIFIC: CRAMBE HISPANICA SUBSP. ABYSSINICA; +SOURCE 3 ORGANISM_TAXID: 3721; +SOURCE 4 STRAIN: SUBSP. ABYSSINICA +KEYWDS VALENCE ELECTRON DENSITY, MULTI-SUBSTATE, MULTIPOLE REFINEMENT, PLANT +KEYWDS 2 PROTEIN +EXPDTA X-RAY DIFFRACTION +AUTHOR C.JELSCH,M.M.TEETER,V.LAMZIN,V.PICHON-LESME,B.BLESSING,C.LECOMTE +REVDAT 6 05-FEB-14 1EJG 1 ATOM CONECT +REVDAT 5 13-JUL-11 1EJG 1 VERSN +REVDAT 4 24-FEB-09 1EJG 1 VERSN +REVDAT 3 01-APR-03 1EJG 1 JRNL +REVDAT 2 10-MAY-00 1EJG 1 COMPND ATOM +REVDAT 1 05-APR-00 1EJG 0 +JRNL AUTH C.JELSCH,M.M.TEETER,V.LAMZIN,V.PICHON-PESME,R.H.BLESSING, +JRNL AUTH 2 C.LECOMTE +JRNL TITL ACCURATE PROTEIN CRYSTALLOGRAPHY AT ULTRA-HIGH RESOLUTION: +JRNL TITL 2 VALENCE ELECTRON DISTRIBUTION IN CRAMBIN. +JRNL REF PROC.NATL.ACAD.SCI.USA V. 97 3171 2000 +JRNL REFN ISSN 0027-8424 +JRNL PMID 10737790 +JRNL DOI 10.1073/PNAS.97.7.3171 +REMARK 2 +REMARK 2 RESOLUTION. 0.54 ANGSTROMS. +REMARK 3 +REMARK 3 REFINEMENT. +REMARK 3 PROGRAM : MOLLY +REMARK 3 +REMARK 3 DATA USED IN REFINEMENT. +REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.54 +REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.37 +REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 +REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL +REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL +REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.6 +REMARK 3 NUMBER OF REFLECTIONS : 100989 +REMARK 3 +REMARK 3 FIT TO DATA USED IN REFINEMENT. +REMARK 3 CROSS-VALIDATION METHOD : NULL +REMARK 3 FREE R VALUE TEST SET SELECTION : 1 REFLECTION OUT OF 20 +REMARK 3 R VALUE (WORKING SET) : 0.090 +REMARK 3 FREE R VALUE : 0.094 +REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 +REMARK 3 FREE R VALUE TEST SET COUNT : 11220 +REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL +REMARK 3 +REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. +REMARK 3 TOTAL NUMBER OF BINS USED : NULL +REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 0.54 +REMARK 3 BIN RESOLUTION RANGE LOW (A) : 0.57 +REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL +REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 17547 +REMARK 3 BIN R VALUE (WORKING SET) : 0.1970 +REMARK 3 BIN FREE R VALUE : 0.2050 +REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00 +REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL +REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL +REMARK 3 +REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. +REMARK 3 PROTEIN ATOMS : 340 +REMARK 3 NUCLEIC ACID ATOMS : 0 +REMARK 3 HETEROGEN ATOMS : 0 +REMARK 3 SOLVENT ATOMS : 0 +REMARK 3 +REMARK 3 B VALUES. +REMARK 3 FROM WILSON PLOT (A**2) : 2.80 +REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL +REMARK 3 OVERALL ANISOTROPIC B VALUE. +REMARK 3 B11 (A**2) : NULL +REMARK 3 B22 (A**2) : NULL +REMARK 3 B33 (A**2) : NULL +REMARK 3 B12 (A**2) : NULL +REMARK 3 B13 (A**2) : NULL +REMARK 3 B23 (A**2) : NULL +REMARK 3 +REMARK 3 ESTIMATED COORDINATE ERROR. +REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL +REMARK 3 ESD FROM SIGMAA (A) : NULL +REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL +REMARK 3 +REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. +REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL +REMARK 3 ESD FROM C-V SIGMAA (A) : NULL +REMARK 3 +REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. +REMARK 3 BOND LENGTHS (A) : 0.023 +REMARK 3 BOND ANGLES (DEGREES) : 2.700 +REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL +REMARK 3 IMPROPER ANGLES (DEGREES) : NULL +REMARK 3 +REMARK 3 ISOTROPIC THERMAL MODEL : NULL +REMARK 3 +REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA +REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL +REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL +REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL +REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL +REMARK 3 +REMARK 3 NCS MODEL : NULL +REMARK 3 +REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT +REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL +REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL +REMARK 3 +REMARK 3 PARAMETER FILE 1 : SHELXL97 DICTIONARY +REMARK 3 PARAMETER FILE 2 : NULL +REMARK 3 TOPOLOGY FILE 1 : NULL +REMARK 3 TOPOLOGY FILE 2 : NULL +REMARK 3 +REMARK 3 OTHER REFINEMENT REMARKS: SHELX97 FOLLOWED BY MOLLY (N.K.HANSEN & +REMARK 3 P.COPPENS ACTA CRYSTALLOGR. A34, 909-921) REFINEMENT OF ELECTRON +REMARK 3 DENSITY. +REMARK 4 +REMARK 4 1EJG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 +REMARK 100 +REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAR-00. +REMARK 100 THE RCSB ID CODE IS RCSB010638. +REMARK 200 +REMARK 200 EXPERIMENTAL DETAILS +REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION +REMARK 200 DATE OF DATA COLLECTION : 31-MAY-97 +REMARK 200 TEMPERATURE (KELVIN) : 100.0 +REMARK 200 PH : 7 +REMARK 200 NUMBER OF CRYSTALS USED : 1 +REMARK 200 +REMARK 200 SYNCHROTRON (Y/N) : Y +REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG +REMARK 200 BEAMLINE : BW7A +REMARK 200 X-RAY GENERATOR MODEL : NULL +REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M +REMARK 200 WAVELENGTH OR RANGE (A) : 0.54 +REMARK 200 MONOCHROMATOR : NULL +REMARK 200 OPTICS : NULL +REMARK 200 +REMARK 200 DETECTOR TYPE : IMAGE PLATE +REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH +REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SOFTWARE AT SYNCHROTRON +REMARK 200 DATA SCALING SOFTWARE : DREAR +REMARK 200 +REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79868 +REMARK 200 RESOLUTION RANGE HIGH (A) : 0.540 +REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 +REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000 +REMARK 200 +REMARK 200 OVERALL. +REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6 +REMARK 200 DATA REDUNDANCY : 4.500 +REMARK 200 R MERGE (I) : 0.05500 +REMARK 200 R SYM (I) : NULL +REMARK 200 FOR THE DATA SET : 8.2000 +REMARK 200 +REMARK 200 IN THE HIGHEST RESOLUTION SHELL. +REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.54 +REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.55 +REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 +REMARK 200 DATA REDUNDANCY IN SHELL : 3.80 +REMARK 200 R MERGE FOR SHELL (I) : 0.14760 +REMARK 200 R SYM FOR SHELL (I) : NULL +REMARK 200 FOR SHELL : NULL +REMARK 200 +REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH +REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL +REMARK 200 SOFTWARE USED: ALREADY SOLVED +REMARK 200 STARTING MODEL: NULL +REMARK 200 +REMARK 200 REMARK: NULL +REMARK 280 +REMARK 280 CRYSTAL +REMARK 280 SOLVENT CONTENT, VS (%): 30.00 +REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.40 +REMARK 280 +REMARK 280 CRYSTALLIZATION CONDITIONS: THE PROTEIN (40 MG/ML IN 80% ETHANOL) +REMARK 280 IS EQUILIBRATED AGAINST 60% ETHANOL. NOT BUFFERED., PH 7, VAPOR +REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K +REMARK 290 +REMARK 290 CRYSTALLOGRAPHIC SYMMETRY +REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 +REMARK 290 +REMARK 290 SYMOP SYMMETRY +REMARK 290 NNNMMM OPERATOR +REMARK 290 1555 X,Y,Z +REMARK 290 2555 -X,Y+1/2,-Z +REMARK 290 +REMARK 290 WHERE NNN -> OPERATOR NUMBER +REMARK 290 MMM -> TRANSLATION VECTOR +REMARK 290 +REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS +REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM +REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY +REMARK 290 RELATED MOLECULES. +REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 +REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 +REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 +REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 +REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 9.24900 +REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 +REMARK 290 +REMARK 290 REMARK: NULL +REMARK 300 +REMARK 300 BIOMOLECULE: 1 +REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM +REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN +REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON +REMARK 300 BURIED SURFACE AREA. +REMARK 350 +REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN +REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE +REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS +REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND +REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. +REMARK 350 +REMARK 350 BIOMOLECULE: 1 +REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC +REMARK 350 APPLY THE FOLLOWING TO CHAINS: A +REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 +REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 +REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 +REMARK 500 +REMARK 500 GEOMETRY AND STEREOCHEMISTRY +REMARK 500 SUBTOPIC: COVALENT BOND ANGLES +REMARK 500 +REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES +REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE +REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN +REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). +REMARK 500 +REMARK 500 STANDARD TABLE: +REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) +REMARK 500 +REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 +REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 +REMARK 500 +REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 +REMARK 500 THR A 39 CA - CB - CG2 ANGL. DEV. = -9.8 DEGREES +REMARK 500 ASP A 43 CA - CB - CG ANGL. DEV. = 13.5 DEGREES +REMARK 500 +REMARK 500 REMARK: NULL +REMARK 900 +REMARK 900 RELATED ENTRIES +REMARK 900 RELATED ID: 1CBN RELATED DB: PDB +REMARK 900 CRAMBIN AT 130K AND 0.83 A. TWO SEQUENCE FORMS. +REMARK 900 RELATED ID: 1CRN RELATED DB: PDB +REMARK 900 CRAMBIN AT 1.5 A AND ROOM TEMPERATURE. TWO SEQUENCE FORMS. +REMARK 900 RELATED ID: 1AB1 RELATED DB: PDB +REMARK 900 CRAMBIN AT 150 K IN THE PURE SER22/ILE25 SEQUENCE FORMS. +REMARK 900 RELATED ID: 1CNR RELATED DB: PDB +REMARK 900 CRAMBIN AT 150K AND 1.05 A RESOLUTION. PURE PRO22/LEU25 +REMARK 900 FORM OF CRAMBIN. +DBREF 1EJG A 1 46 UNP P01542 CRAM_CRAAB 1 46 +SEQADV 1EJG SER A 22 UNP P01542 PRO 22 MICROHETEROGENEITY +SEQADV 1EJG ILE A 25 UNP P01542 LEU 25 MICROHETEROGENEITY +SEQRES 1 A 46 THR THR CYS CYS PRO SER ILE VAL ALA ARG SER ASN PHE +SEQRES 2 A 46 ASN VAL CYS ARG LEU PRO GLY THR PRO GLU ALA LEU CYS +SEQRES 3 A 46 ALA THR TYR THR GLY CYS ILE ILE ILE PRO GLY ALA THR +SEQRES 4 A 46 CYS PRO GLY ASP TYR ALA ASN +HELIX 1 1 SER A 6 LEU A 18 1 13 +HELIX 2 2 PRO A 22 GLY A 31 1 10 +SHEET 1 A 2 THR A 2 CYS A 3 0 +SHEET 2 A 2 ILE A 33 ILE A 34 -1 O ILE A 33 N CYS A 3 +SSBOND 1 CYS A 3 CYS A 40 1555 1555 2.03 +SSBOND 2 CYS A 4 CYS A 32 1555 1555 2.05 +SSBOND 3 CYS A 16 CYS A 26 1555 1555 2.04 +CRYST1 40.824 18.498 22.371 90.00 90.47 90.00 P 1 21 1 2 +ORIGX1 1.000000 0.000000 0.000000 0.00000 +ORIGX2 0.000000 1.000000 0.000000 0.00000 +ORIGX3 0.000000 0.000000 1.000000 0.00000 +SCALE1 0.024495 0.000000 0.000201 0.00000 +SCALE2 0.000000 0.054060 0.000000 0.00000 +SCALE3 0.000000 0.000000 0.044702 0.00000 +ATOM 1 N ATHR A 1 16.885 14.078 3.427 0.82 4.48 +ANISOU 1 N ATHR A 1 434 531 735 201 133 -28 +ATOM 2 N BTHR A 1 17.553 14.234 4.214 0.18 5.51 +ATOM 3 CA ATHR A 1 16.938 12.834 4.234 0.82 3.12 +ANISOU 3 CA ATHR A 1 305 437 441 39 103 -65 +ATOM 4 CA BTHR A 1 16.985 12.901 4.228 0.18 16.71 +ATOM 5 C THR A 1 15.642 12.760 4.985 1.00 3.28 +ANISOU 5 C THR A 1 338 431 477 -32 137 -43 +ATOM 6 O THR A 1 15.150 13.818 5.439 1.00 5.91 +ANISOU 6 O THR A 1 476 455 1311 -213 289 -42 +ATOM 7 CB ATHR A 1 18.103 12.875 5.202 0.82 4.05 +ANISOU 7 CB ATHR A 1 249 662 627 23 60 -110 +ATOM 8 CB BTHR A 1 17.983 11.950 4.917 0.18 8.95 +ATOM 9 OG1ATHR A 1 19.256 13.004 4.401 0.82 5.75 +ANISOU 9 OG1ATHR A 1 294 1049 842 134 158 -125 +ATOM 10 OG1BTHR A 1 17.792 10.543 4.939 0.18 9.94 +ATOM 11 CG2ATHR A 1 18.173 11.582 6.055 0.82 5.30 +ANISOU 11 CG2ATHR A 1 343 850 818 215 -11 -32 +ATOM 12 CG2BTHR A 1 18.117 12.174 6.499 0.18 6.78 +ATOM 13 H1 ATHR A 1 17.705 14.139 2.840 0.82 6.68 H +ATOM 14 H1 BTHR A 1 18.510 14.188 3.898 0.18 7.89 H +ATOM 15 H2 ATHR A 1 16.879 14.894 4.049 0.82 6.68 H +ATOM 16 H2 BTHR A 1 17.525 14.622 5.144 0.18 7.89 H +ATOM 17 H3 ATHR A 1 16.057 14.105 2.859 0.82 6.68 H +ATOM 18 H3 BTHR A 1 17.021 14.820 3.588 0.18 7.89 H +ATOM 19 HA ATHR A 1 17.013 11.969 3.577 0.82 3.83 H +ATOM 20 HA BTHR A 1 16.841 12.569 3.191 0.18 6.31 H +ATOM 21 HB ATHR A 1 17.995 13.758 5.848 0.82 4.83 H +ATOM 22 HB BTHR A 1 18.972 12.139 4.475 0.18 6.31 H +ATOM 23 HG1ATHR A 1 19.852 13.644 4.803 0.82 8.74 H +ATOM 24 HG1BTHR A 1 17.772 10.206 4.033 0.18 7.89 H +ATOM 25 HG21ATHR A 1 19.024 11.659 6.737 0.82 7.89 H +ATOM 26 HG21BTHR A 1 17.805 11.261 7.025 0.18 7.89 H +ATOM 27 HG22ATHR A 1 18.290 10.718 5.396 0.82 7.89 H +ATOM 28 HG22BTHR A 1 17.475 13.012 6.806 0.18 7.89 H +ATOM 29 HG23ATHR A 1 17.241 11.481 6.636 0.82 7.89 H +ATOM 30 HG23BTHR A 1 19.162 12.403 6.749 0.18 7.89 H +ATOM 31 N THR A 2 15.069 11.586 5.134 1.00 2.84 N +ANISOU 31 N THR A 2 325 445 309 -46 132 -59 N +ATOM 32 CA ATHR A 2 13.856 11.498 5.932 0.67 2.54 C +ANISOU 32 CA ATHR A 2 266 380 316 18 89 -29 C +ATOM 33 CA BTHR A 2 13.843 11.266 5.843 0.33 2.68 C +ANISOU 33 CA BTHR A 2 243 500 273 -18 30 -90 C +ATOM 34 C THR A 2 14.172 10.757 7.221 1.00 2.52 C +ANISOU 34 C THR A 2 244 442 270 -3 84 -20 C +ATOM 35 O THR A 2 15.006 9.857 7.315 1.00 3.12 O +ANISOU 35 O THR A 2 321 531 334 -22 120 69 O +ATOM 36 CB ATHR A 2 12.785 10.742 5.129 0.67 4.28 C +ANISOU 36 CB ATHR A 2 380 828 416 222 -76 -280 C +ATOM 37 CB BTHR A 2 13.014 10.211 5.070 0.33 6.00 C +ANISOU 37 CB BTHR A 2 455 1292 533 -381 15 -400 C +ATOM 38 OG1ATHR A 2 13.312 9.437 4.770 0.67 5.18 O +ANISOU 38 OG1ATHR A 2 1082 608 278 52 -81 -546 O +ATOM 39 OG1BTHR A 2 12.661 10.876 3.761 0.33 7.04 O +ANISOU 39 OG1BTHR A 2 776 1532 368 -344 167 -537 O +ATOM 40 CG2ATHR A 2 12.315 11.612 3.973 0.67 5.81 C +ANISOU 40 CG2ATHR A 2 696 1012 497 311 -225 -310 C +ATOM 41 CG2BTHR A 2 11.751 9.803 5.800 0.33 11.66 C +ANISOU 41 CG2BTHR A 2 770 2618 1042 468 28 -955 C +ATOM 42 H THR A 2 15.465 10.769 4.694 1.00 3.42 H +ATOM 43 HA ATHR A 2 13.508 12.532 6.154 0.67 3.05 H +ATOM 44 HA BTHR A 2 13.237 12.147 5.938 0.33 3.42 H +ATOM 45 HB ATHR A 2 11.925 10.594 5.819 0.67 5.10 H +ATOM 46 HB BTHR A 2 13.558 9.302 4.866 0.33 7.43 H +ATOM 47 HG1ATHR A 2 14.200 9.345 5.125 0.67 7.86 H +ATOM 48 HG1BTHR A 2 13.454 11.073 3.278 0.33 11.01 H +ATOM 49 HG21ATHR A 2 11.570 11.067 3.373 0.67 8.54 H +ATOM 50 HG21BTHR A 2 11.118 9.118 5.255 0.33 16.13 H +ATOM 51 HG22ATHR A 2 13.159 11.901 3.347 0.67 8.54 H +ATOM 52 HG22BTHR A 2 11.082 10.771 5.953 0.33 16.13 H +ATOM 53 HG23ATHR A 2 11.828 12.539 4.368 0.67 8.54 H +ATOM 54 HG23BTHR A 2 11.949 9.454 6.810 0.33 16.13 H +ATOM 55 N CYS A 3 13.438 11.192 8.264 1.00 2.26 N +ANISOU 55 N CYS A 3 254 330 274 18 95 -33 N +ATOM 56 CA CYS A 3 13.607 10.675 9.600 1.00 2.06 C +ANISOU 56 CA CYS A 3 223 287 270 2 80 -69 C +ATOM 57 C CYS A 3 12.210 10.413 10.164 1.00 1.94 C +ANISOU 57 C CYS A 3 214 221 301 -6 89 -42 C +ATOM 58 O CYS A 3 11.324 11.246 9.996 1.00 2.78 O +ANISOU 58 O CYS A 3 284 240 529 99 166 4 O +ATOM 59 CB CYS A 3 14.300 11.703 10.523 1.00 2.35 C +ANISOU 59 CB CYS A 3 271 295 327 -12 52 -77 C +ATOM 60 SG CYS A 3 15.846 12.374 9.880 1.00 3.32 S +ANISOU 60 SG CYS A 3 336 478 449 125 9 -211 S +ATOM 61 H CYS A 3 12.743 11.906 8.104 1.00 2.71 H +ATOM 62 HA CYS A 3 14.185 9.741 9.573 1.00 2.47 H +ATOM 63 HB2 CYS A 3 13.605 12.535 10.703 1.00 2.81 H +ATOM 64 HB3 CYS A 3 14.502 11.224 11.491 1.00 2.81 H +ATOM 65 N CYS A 4 12.015 9.277 10.850 1.00 1.74 N +ANISOU 65 N CYS A 4 187 240 231 -8 66 -40 N +ATOM 66 CA CYS A 4 10.681 8.944 11.326 1.00 1.60 C +ANISOU 66 CA CYS A 4 172 211 225 -2 52 -36 C +ATOM 67 C CYS A 4 10.683 8.745 12.838 1.00 1.63 C +ANISOU 67 C CYS A 4 168 226 222 -6 45 -26 C +ATOM 68 O CYS A 4 11.651 8.272 13.418 1.00 2.08 O +ANISOU 68 O CYS A 4 184 337 267 5 31 14 O +ATOM 69 CB CYS A 4 10.155 7.684 10.617 1.00 1.78 C +ANISOU 69 CB CYS A 4 237 216 222 -6 35 -45 C +ATOM 70 SG CYS A 4 9.833 7.934 8.843 1.00 2.03 S +ANISOU 70 SG CYS A 4 303 238 229 -52 41 -26 S +ATOM 71 H CYS A 4 12.789 8.657 11.035 1.00 2.08 H +ATOM 72 HA CYS A 4 10.009 9.781 11.088 1.00 1.93 H +ATOM 73 HB2 CYS A 4 10.891 6.876 10.734 1.00 2.14 H +ATOM 74 HB3 CYS A 4 9.225 7.362 11.105 1.00 2.14 H +ATOM 75 N PRO A 5 9.546 9.093 13.475 1.00 1.64 N +ANISOU 75 N PRO A 5 178 227 218 -10 50 -22 N +ATOM 76 CA PRO A 5 9.500 9.079 14.937 1.00 1.85 C +ANISOU 76 CA PRO A 5 216 270 214 -47 45 -74 C +ATOM 77 C PRO A 5 9.373 7.688 15.546 1.00 2.01 C +ANISOU 77 C PRO A 5 264 304 195 -5 30 -52 C +ATOM 78 O PRO A 5 9.640 7.542 16.748 1.00 3.15 O +ANISOU 78 O PRO A 5 544 447 203 11 -23 -132 O +ATOM 79 CB PRO A 5 8.267 9.939 15.267 1.00 2.28 C +ANISOU 79 CB PRO A 5 307 306 252 -66 114 -31 C +ATOM 80 CG PRO A 5 7.364 9.742 14.044 1.00 2.26 C +ANISOU 80 CG PRO A 5 199 335 322 -14 96 13 C +ATOM 81 CD PRO A 5 8.360 9.748 12.898 1.00 1.83 C +ANISOU 81 CD PRO A 5 184 251 258 -6 56 2 C +ATOM 82 HA PRO A 5 10.401 9.568 15.334 1.00 2.21 H +ATOM 83 HB2 PRO A 5 7.773 9.587 16.184 1.00 2.72 H +ATOM 84 HB3 PRO A 5 8.542 10.995 15.390 1.00 2.72 H +ATOM 85 HG2 PRO A 5 6.823 8.787 14.098 1.00 2.70 H +ATOM 86 HG3 PRO A 5 6.640 10.563 13.947 1.00 2.70 H +ATOM 87 HD2 PRO A 5 7.976 9.183 12.037 1.00 2.19 H +ATOM 88 HD3 PRO A 5 8.590 10.774 12.580 1.00 2.19 H +ATOM 89 N SER A 6 8.926 6.705 14.756 1.00 1.84 N +ANISOU 89 N SER A 6 232 268 198 15 19 -46 N +ATOM 90 CA SER A 6 8.755 5.347 15.231 1.00 1.70 C +ANISOU 90 CA SER A 6 207 255 183 21 26 15 C +ATOM 91 C SER A 6 8.832 4.429 14.008 1.00 1.84 C +ANISOU 91 C SER A 6 215 281 200 3 41 37 C +ATOM 92 O SER A 6 8.757 4.867 12.860 1.00 2.14 O +ANISOU 92 O SER A 6 284 326 200 19 54 23 O +ATOM 93 CB SER A 6 7.409 5.161 15.930 1.00 1.78 C +ANISOU 93 CB SER A 6 248 219 206 13 67 5 C +ATOM 94 OG SER A 6 6.371 5.265 14.953 1.00 2.15 O +ANISOU 94 OG SER A 6 201 330 283 60 59 2 O +ATOM 95 H SER A 6 8.700 6.916 13.796 1.00 2.20 H +ATOM 96 HA SER A 6 9.567 5.098 15.928 1.00 2.03 H +ATOM 97 HB2 SER A 6 7.371 4.176 16.415 1.00 2.13 H +ATOM 98 HB3 SER A 6 7.277 5.932 16.702 1.00 2.13 H +ATOM 99 HG SER A 6 5.560 4.870 15.300 1.00 3.21 H +ATOM 100 N ILE A 7 8.936 3.129 14.302 1.00 2.20 N +ANISOU 100 N ILE A 7 350 283 202 -11 40 105 N +ATOM 101 CA AILE A 7 8.829 2.039 13.300 0.55 2.58 C +ANISOU 101 CA AILE A 7 516 264 200 -6 151 84 C +ATOM 102 CA BILE A 7 9.104 2.209 13.197 0.45 2.14 C +ANISOU 102 CA BILE A 7 381 195 233 9 131 47 C +ATOM 103 C AILE A 7 7.559 2.141 12.460 0.55 2.53 C +ANISOU 103 C AILE A 7 595 230 137 20 117 131 C +ATOM 104 C BILE A 7 7.839 2.105 12.369 0.45 2.15 C +ANISOU 104 C BILE A 7 396 209 211 -103 150 -38 C +ATOM 105 O AILE A 7 7.573 2.124 11.205 0.55 2.78 O +ANISOU 105 O AILE A 7 602 310 145 24 113 111 O +ATOM 106 O BILE A 7 7.990 2.102 11.154 0.45 2.53 O +ANISOU 106 O BILE A 7 359 395 206 -115 130 -115 O +ATOM 107 CB AILE A 7 8.928 0.644 13.932 0.55 3.24 C +ANISOU 107 CB AILE A 7 571 217 440 -4 180 112 C +ATOM 108 CB BILE A 7 9.491 0.865 13.815 0.45 2.71 C +ANISOU 108 CB BILE A 7 506 148 373 -28 88 72 C +ATOM 109 CG1AILE A 7 10.309 0.385 14.573 0.55 5.58 C +ANISOU 109 CG1AILE A 7 545 414 1161 51 125 259 C +ATOM 110 CG1BILE A 7 10.981 0.969 14.362 0.45 3.52 C +ANISOU 110 CG1BILE A 7 451 354 532 134 107 211 C +ATOM 111 CG2AILE A 7 8.510 -0.464 12.908 0.55 4.24 C +ANISOU 111 CG2AILE A 7 843 247 518 -70 159 109 C +ATOM 112 CG2BILE A 7 9.389 -0.211 12.797 0.45 4.65 C +ANISOU 112 CG2BILE A 7 943 293 527 -181 -35 169 C +ATOM 113 CD1AILE A 7 11.430 0.295 13.473 0.55 7.60 C +ANISOU 113 CD1AILE A 7 582 653 1651 -377 357 116 C +ATOM 114 CD1BILE A 7 11.345 -0.312 15.110 0.45 4.98 C +ANISOU 114 CD1BILE A 7 834 563 496 251 159 405 C +ATOM 115 H ILE A 7 9.078 2.878 15.269 1.00 2.65 H +ATOM 116 HA AILE A 7 9.714 2.123 12.623 0.55 3.11 H +ATOM 117 HA BILE A 7 9.909 2.595 12.552 0.45 2.54 H +ATOM 118 HB AILE A 7 8.200 0.598 14.759 0.55 3.92 H +ATOM 119 HB BILE A 7 8.815 0.671 14.655 0.45 3.28 H +ATOM 120 HG12AILE A 7 10.550 1.170 15.240 0.55 6.88 H +ATOM 121 HG12BILE A 7 11.630 1.137 13.512 0.45 4.23 H +ATOM 122 HG13AILE A 7 10.274 -0.579 15.106 0.55 6.88 H +ATOM 123 HG13BILE A 7 11.028 1.816 15.040 0.45 4.23 H +ATOM 124 HG21AILE A 7 7.863 0.004 12.146 0.55 6.50 H +ATOM 125 HG21BILE A 7 9.566 -1.189 13.311 0.45 7.18 H +ATOM 126 HG22AILE A 7 7.955 -1.251 13.426 0.55 6.50 H +ATOM 127 HG22BILE A 7 10.130 -0.079 12.019 0.45 7.18 H +ATOM 128 HG23AILE A 7 9.402 -0.873 12.434 0.55 6.50 H +ATOM 129 HG23BILE A 7 8.377 -0.228 12.371 0.45 7.18 H +ATOM 130 HD11AILE A 7 12.389 0.055 13.960 0.55 11.57 H +ATOM 131 HD11BILE A 7 12.440 -0.265 15.300 0.45 7.62 H +ATOM 132 HD12AILE A 7 11.499 1.217 12.922 0.55 11.57 H +ATOM 133 HD12BILE A 7 11.152 -1.180 14.450 0.45 7.62 H +ATOM 134 HD13AILE A 7 11.196 -0.544 12.761 0.55 11.57 H +ATOM 135 HD13BILE A 7 10.803 -0.391 16.024 0.45 7.62 H +ATOM 136 N AVAL A 8 6.382 2.222 13.070 0.55 1.92 N +ANISOU 136 N AVAL A 8 421 149 160 33 -23 -35 N +ATOM 137 N BVAL A 8 6.695 2.072 13.037 0.45 1.88 N +ATOM 138 CA AVAL A 8 5.099 2.259 12.380 0.55 2.32 C +ANISOU 138 CA AVAL A 8 397 258 224 16 -22 -120 C +ATOM 139 CA BVAL A 8 5.471 2.048 12.164 0.45 1.94 C +ATOM 140 C VAL A 8 5.208 3.386 11.373 1.00 2.63 C +ANISOU 140 C VAL A 8 380 402 213 71 -42 -209 C +ATOM 141 O VAL A 8 4.712 3.302 10.238 1.00 2.67 O +ANISOU 141 O VAL A 8 378 434 200 39 -31 -178 O +ATOM 142 CB AVAL A 8 3.944 2.394 13.375 0.55 3.36 C +ANISOU 142 CB AVAL A 8 376 635 262 186 4 -244 C +ATOM 143 CB BVAL A 8 4.263 1.630 13.035 0.45 3.05 C +ATOM 144 CG1AVAL A 8 2.629 2.981 12.701 0.55 4.22 C +ANISOU 144 CG1AVAL A 8 326 856 420 159 34 -159 C +ATOM 145 CG1BVAL A 8 3.580 2.930 13.664 0.45 3.89 C +ATOM 146 CG2AVAL A 8 3.635 1.036 13.955 0.55 4.82 C +ANISOU 146 CG2AVAL A 8 771 684 376 230 -61 -385 C +ATOM 147 CG2BVAL A 8 3.136 1.077 12.028 0.45 4.17 C +ATOM 148 H AVAL A 8 6.374 2.231 14.084 0.55 2.27 H +ATOM 149 H BVAL A 8 6.648 2.059 14.045 0.45 5.91 H +ATOM 150 HA AVAL A 8 4.948 1.364 11.845 0.55 2.65 H +ATOM 151 HA BVAL A 8 5.622 1.256 11.418 0.45 5.91 H +ATOM 152 HB AVAL A 8 4.204 3.077 14.197 0.55 4.16 H +ATOM 153 HB BVAL A 8 4.536 0.891 13.800 0.45 5.91 H +ATOM 154 HG11AVAL A 8 2.862 3.979 12.286 0.55 6.22 H +ATOM 155 HG11BVAL A 8 2.659 2.642 14.189 0.45 7.38 H +ATOM 156 HG12AVAL A 8 1.845 3.103 13.478 0.55 6.22 H +ATOM 157 HG12BVAL A 8 3.337 3.640 12.861 0.45 7.38 H +ATOM 158 HG13AVAL A 8 2.286 2.318 11.926 0.55 6.22 H +ATOM 159 HG13BVAL A 8 4.275 3.401 14.373 0.45 7.38 H +ATOM 160 HG21AVAL A 8 4.536 0.671 14.467 0.55 7.38 H +ATOM 161 HG21BVAL A 8 2.262 0.744 12.605 0.45 7.38 H +ATOM 162 HG22AVAL A 8 3.367 0.343 13.145 0.55 7.38 H +ATOM 163 HG22BVAL A 8 3.540 0.231 11.455 0.45 7.38 H +ATOM 164 HG23AVAL A 8 2.805 1.098 14.673 0.55 7.38 H +ATOM 165 HG23BVAL A 8 2.836 1.878 11.338 0.45 7.38 H +ATOM 166 N ALA A 9 5.668 4.556 11.848 1.00 2.19 N +ANISOU 166 N ALA A 9 303 382 147 23 -5 -114 N +ATOM 167 CA ALA A 9 5.637 5.732 10.997 1.00 1.92 C +ANISOU 167 CA ALA A 9 219 314 195 -8 14 -7 C +ATOM 168 C ALA A 9 6.496 5.510 9.742 1.00 1.64 C +ANISOU 168 C ALA A 9 233 220 169 -6 8 -17 C +ATOM 169 O ALA A 9 6.087 5.887 8.640 1.00 1.98 O +ANISOU 169 O ALA A 9 284 267 198 19 -8 33 O +ATOM 170 CB ALA A 9 6.088 6.968 11.772 1.00 2.30 C +ANISOU 170 CB ALA A 9 305 295 273 -42 18 13 C +ATOM 171 H ALA A 9 6.031 4.617 12.787 1.00 2.64 H +ATOM 172 HA ALA A 9 4.599 5.892 10.675 1.00 2.30 H +ATOM 173 HB1 ALA A 9 5.450 7.098 12.658 1.00 3.45 H +ATOM 174 HB2 ALA A 9 6.005 7.855 11.128 1.00 3.45 H +ATOM 175 HB3 ALA A 9 7.132 6.841 12.089 1.00 3.45 H +ATOM 176 N ARG A 10 7.685 4.898 9.905 1.00 1.59 N +ANISOU 176 N ARG A 10 228 214 160 -6 -3 -23 N +ATOM 177 CA ARG A 10 8.505 4.573 8.737 1.00 1.56 C +ANISOU 177 CA ARG A 10 203 197 192 -2 2 -28 C +ATOM 178 C ARG A 10 7.811 3.576 7.811 1.00 1.58 C +ANISOU 178 C ARG A 10 218 210 170 0 -9 -18 C +ATOM 179 O ARG A 10 7.840 3.742 6.580 1.00 1.79 O +ANISOU 179 O ARG A 10 258 262 158 0 0 -15 O +ATOM 180 CB ARG A 10 9.857 4.014 9.199 1.00 1.82 C +ANISOU 180 CB ARG A 10 213 273 203 -14 -21 -17 C +ATOM 181 CG ARG A 10 10.767 3.570 8.047 1.00 2.09 C +ANISOU 181 CG ARG A 10 265 275 252 -40 14 -7 C +ATOM 182 CD ARG A 10 11.272 4.693 7.139 1.00 2.37 C +ANISOU 182 CD ARG A 10 302 349 246 -45 64 -50 C +ATOM 183 NE AARG A 10 12.137 5.620 7.824 0.67 2.14 N +ANISOU 183 NE AARG A 10 312 293 206 6 49 -48 N +ATOM 184 NE BARG A 10 12.206 5.472 8.032 0.33 2.43 N +ANISOU 184 NE BARG A 10 353 303 266 -13 64 -104 N +ATOM 185 CZ AARG A 10 12.683 6.719 7.295 0.67 2.69 C +ANISOU 185 CZ AARG A 10 452 275 294 -68 157 -106 C +ATOM 186 CZ BARG A 10 12.925 6.393 7.470 0.33 5.04 C +ANISOU 186 CZ BARG A 10 983 436 494 -9 255 -368 C +ATOM 187 NH1AARG A 10 12.436 7.053 6.053 0.67 3.34 N +ANISOU 187 NH1AARG A 10 594 333 340 10 131 -106 N +ATOM 188 NH1BARG A 10 12.990 6.670 6.157 0.33 5.59 N +ANISOU 188 NH1BARG A 10 955 719 447 -84 213 -444 N +ATOM 189 NH2AARG A 10 13.443 7.503 8.090 0.67 3.48 N +ANISOU 189 NH2AARG A 10 599 360 364 -116 149 -204 N +ATOM 190 NH2BARG A 10 13.755 7.127 8.237 0.33 8.43 N +ANISOU 190 NH2BARG A 10 1708 931 562 -265 514 -1062 N +ATOM 191 H ARG A 10 8.009 4.663 10.831 1.00 1.90 H +ATOM 192 HA ARG A 10 8.688 5.499 8.174 1.00 1.87 H +ATOM 193 HB2 ARG A 10 10.377 4.784 9.785 1.00 2.18 H +ATOM 194 HB3 ARG A 10 9.677 3.155 9.860 1.00 2.18 H +ATOM 195 HG2 ARG A 10 11.636 3.050 8.472 1.00 2.50 H +ATOM 196 HG3 ARG A 10 10.217 2.846 7.430 1.00 2.50 H +ATOM 197 HD2 ARG A 10 11.818 4.251 6.293 1.00 2.82 H +ATOM 198 HD3 ARG A 10 10.410 5.240 6.732 1.00 2.82 H +ATOM 199 HE AARG A 10 12.350 5.422 8.790 0.67 2.56 H +ATOM 200 HE BARG A 10 12.268 5.285 9.022 0.33 2.87 H +ATOM 201 HH11AARG A 10 11.830 6.478 5.487 0.67 4.04 H +ATOM 202 HH11BARG A 10 12.442 6.135 5.501 0.33 6.91 H +ATOM 203 HH12AARG A 10 12.853 7.884 5.661 0.67 4.04 H +ATOM 204 HH12BARG A 10 13.587 7.414 5.828 0.33 6.91 H +ATOM 205 HH21AARG A 10 13.831 8.362 7.729 0.67 4.22 H +ATOM 206 HH21BARG A 10 13.808 6.956 9.229 0.33 10.67 H +ATOM 207 HH22AARG A 10 13.622 7.230 9.044 0.67 4.22 H +ATOM 208 HH22BARG A 10 14.322 7.849 7.818 0.33 10.67 H +ATOM 209 N SER A 11 7.211 2.522 8.369 1.00 1.73 N +ANISOU 209 N SER A 11 258 217 181 -5 -33 -53 N +ATOM 210 CA SER A 11 6.538 1.562 7.510 1.00 1.77 C +ANISOU 210 CA SER A 11 253 193 224 -16 -48 -32 C +ATOM 211 C SER A 11 5.415 2.243 6.711 1.00 1.70 C +ANISOU 211 C SER A 11 255 194 194 -5 -40 -35 C +ATOM 212 O SER A 11 5.227 1.995 5.517 1.00 2.01 O +ANISOU 212 O SER A 11 318 248 196 -40 -58 0 O +ATOM 213 CB SER A 11 5.967 0.416 8.335 1.00 2.24 C +ANISOU 213 CB SER A 11 299 206 343 51 -87 -47 C +ATOM 214 OG SER A 11 7.043 -0.267 8.962 1.00 3.47 O +ANISOU 214 OG SER A 11 384 310 621 199 -148 -11 O +ATOM 215 H SER A 11 7.224 2.395 9.370 1.00 2.07 H +ATOM 216 HA SER A 11 7.271 1.152 6.802 1.00 2.12 H +ATOM 217 HB2 SER A 11 5.276 0.807 9.095 1.00 2.69 H +ATOM 218 HB3 SER A 11 5.411 -0.275 7.685 1.00 2.69 H +ATOM 219 HG SER A 11 6.697 -1.005 9.482 1.00 5.17 H +ATOM 220 N ASN A 12 4.661 3.116 7.382 1.00 1.73 N +ANISOU 220 N ASN A 12 256 227 172 22 -7 -24 N +ATOM 221 CA AASN A 12 3.595 3.898 6.756 0.37 1.76 C +ANISOU 221 CA AASN A 12 218 269 181 26 6 -23 C +ATOM 222 CA BASN A 12 3.587 3.804 6.673 0.63 1.83 C +ANISOU 222 CA BASN A 12 234 246 215 37 33 9 C +ATOM 223 C ASN A 12 4.154 4.793 5.647 1.00 1.79 C +ANISOU 223 C ASN A 12 283 231 164 19 22 12 C +ATOM 224 O ASN A 12 3.549 4.958 4.581 1.00 2.30 O +ANISOU 224 O ASN A 12 371 336 164 41 -13 -33 O +ATOM 225 CB AASN A 12 2.831 4.764 7.756 0.37 1.88 C +ANISOU 225 CB AASN A 12 239 240 234 57 73 -25 C +ATOM 226 CB BASN A 12 2.681 4.487 7.692 0.63 2.39 C +ANISOU 226 CB BASN A 12 317 363 228 38 91 39 C +ATOM 227 CG AASN A 12 1.901 3.956 8.670 0.37 2.03 C +ANISOU 227 CG AASN A 12 252 248 271 77 79 -28 C +ATOM 228 CG BASN A 12 1.884 3.461 8.515 0.63 2.82 C +ANISOU 228 CG BASN A 12 336 444 292 74 126 21 C +ATOM 229 OD1AASN A 12 1.513 2.854 8.302 0.37 3.92 O +ANISOU 229 OD1AASN A 12 600 328 560 -55 307 -200 O +ATOM 230 OD1BASN A 12 1.651 2.334 8.091 0.63 3.87 O +ANISOU 230 OD1BASN A 12 507 455 507 78 167 -112 O +ATOM 231 ND2AASN A 12 1.534 4.536 9.789 0.37 2.49 N +ANISOU 231 ND2AASN A 12 306 377 262 35 79 -57 N +ATOM 232 ND2BASN A 12 1.461 3.901 9.686 0.63 4.09 N +ANISOU 232 ND2BASN A 12 563 622 369 31 267 16 N +ATOM 233 H ASN A 12 4.835 3.242 8.368 1.00 2.07 H +ATOM 234 HA AASN A 12 2.882 3.196 6.300 0.37 2.13 H +ATOM 235 HA BASN A 12 2.994 3.052 6.135 0.63 2.21 H +ATOM 236 HB2AASN A 12 3.553 5.313 8.377 0.37 2.34 H +ATOM 237 HB2BASN A 12 3.292 5.101 8.368 0.63 2.92 H +ATOM 238 HB3AASN A 12 2.234 5.503 7.204 0.37 2.34 H +ATOM 239 HB3BASN A 12 1.982 5.154 7.167 0.63 2.92 H +ATOM 240 HD21AASN A 12 0.890 4.070 10.410 0.37 3.02 H +ATOM 241 HD21BASN A 12 0.915 3.299 10.284 0.63 4.90 H +ATOM 242 HD22AASN A 12 1.897 5.447 10.027 0.37 3.02 H +ATOM 243 HD22BASN A 12 1.683 4.839 9.983 0.63 4.90 H +ATOM 244 N PHE A 13 5.288 5.434 5.950 1.00 1.78 N +ANISOU 244 N PHE A 13 300 221 154 20 21 -5 N +ATOM 245 CA PHE A 13 5.940 6.322 4.994 1.00 1.70 C +ANISOU 245 CA PHE A 13 283 198 164 10 8 -19 C +ATOM 246 C PHE A 13 6.312 5.548 3.719 1.00 1.55 C +ANISOU 246 C PHE A 13 239 216 131 19 2 -26 C +ATOM 247 O PHE A 13 6.092 6.018 2.611 1.00 1.78 O +ANISOU 247 O PHE A 13 286 238 153 34 -6 -35 O +ATOM 248 CB PHE A 13 7.176 6.946 5.672 1.00 2.08 C +ANISOU 248 CB PHE A 13 361 234 194 6 -41 -67 C +ATOM 249 CG APHE A 13 7.941 7.888 4.755 0.40 2.00 C +ANISOU 249 CG APHE A 13 302 247 210 25 -120 -117 C +ATOM 250 CG BPHE A 13 7.848 8.003 4.844 0.60 2.19 C +ANISOU 250 CG BPHE A 13 300 252 279 19 47 -23 C +ATOM 251 CD1APHE A 13 8.984 7.309 3.949 0.40 3.11 C +ANISOU 251 CD1APHE A 13 430 387 362 -63 32 -164 C +ATOM 252 CD1BPHE A 13 8.844 7.684 3.917 0.60 2.62 C +ANISOU 252 CD1BPHE A 13 375 278 341 -104 95 -68 C +ATOM 253 CD2APHE A 13 7.610 9.268 4.690 0.40 2.48 C +ANISOU 253 CD2APHE A 13 417 260 264 66 -130 -86 C +ATOM 254 CD2BPHE A 13 7.486 9.333 5.057 0.60 2.28 C +ANISOU 254 CD2BPHE A 13 304 255 307 27 -19 -4 C +ATOM 255 CE1APHE A 13 9.674 8.201 3.099 0.40 4.71 C +ANISOU 255 CE1APHE A 13 661 931 196 -57 23 -506 C +ATOM 256 CE1BPHE A 13 9.430 8.686 3.153 0.60 3.77 C +ANISOU 256 CE1BPHE A 13 517 556 360 -64 146 -260 C +ATOM 257 CE2APHE A 13 8.310 10.117 3.816 0.40 4.07 C +ANISOU 257 CE2APHE A 13 716 487 340 198 -188 -289 C +ATOM 258 CE2BPHE A 13 8.071 10.331 4.281 0.60 2.95 C +ANISOU 258 CE2BPHE A 13 364 288 466 134 -116 -67 C +ATOM 259 CZ APHE A 13 9.375 9.576 3.044 0.40 4.83 C +ANISOU 259 CZ APHE A 13 493 993 348 279 -102 -442 C +ATOM 260 CZ BPHE A 13 9.036 9.997 3.302 0.60 3.50 C +ANISOU 260 CZ BPHE A 13 411 532 384 203 -57 -187 C +ATOM 261 H PHE A 13 5.701 5.301 6.861 1.00 2.13 H +ATOM 262 HA PHE A 13 5.240 7.126 4.726 1.00 2.05 H +ATOM 263 HB2 PHE A 13 6.853 7.500 6.565 1.00 2.49 H +ATOM 264 HB3 PHE A 13 7.848 6.142 6.001 1.00 2.49 H +ATOM 265 HD1APHE A 13 9.228 6.238 3.992 0.40 3.59 H +ATOM 266 HD1BPHE A 13 9.164 6.640 3.792 0.60 3.14 H +ATOM 267 HD2APHE A 13 6.806 9.671 5.323 0.40 2.94 H +ATOM 268 HD2BPHE A 13 6.748 9.591 5.830 0.60 2.74 H +ATOM 269 HE1APHE A 13 10.474 7.807 2.456 0.40 5.62 H +ATOM 270 HE1BPHE A 13 10.214 8.431 2.425 0.60 4.57 H +ATOM 271 HE2APHE A 13 8.040 11.178 3.731 0.40 4.92 H +ATOM 272 HE2BPHE A 13 7.781 11.381 4.429 0.60 3.59 H +ATOM 273 HZ APHE A 13 9.970 10.238 2.399 0.40 5.90 H +ATOM 274 HZ BPHE A 13 9.469 10.780 2.663 0.60 4.21 H +ATOM 275 N ASN A 14 6.892 4.356 3.906 1.00 1.62 N +ANISOU 275 N ASN A 14 238 222 154 3 -7 -12 N +ATOM 276 CA ASN A 14 7.323 3.600 2.746 1.00 1.56 C +ANISOU 276 CA ASN A 14 202 236 152 3 -3 -19 C +ATOM 277 C ASN A 14 6.137 3.150 1.887 1.00 1.55 C +ANISOU 277 C ASN A 14 186 233 168 -2 1 -23 C +ATOM 278 O ASN A 14 6.248 3.117 0.663 1.00 2.17 O +ANISOU 278 O ASN A 14 227 411 187 -9 16 -83 O +ATOM 279 CB ASN A 14 8.188 2.417 3.167 1.00 1.96 C +ANISOU 279 CB ASN A 14 228 261 254 -19 -42 8 C +ATOM 280 CG ASN A 14 9.563 2.858 3.654 1.00 2.40 C +ANISOU 280 CG ASN A 14 230 344 337 -21 -73 5 C +ATOM 281 OD1 ASN A 14 10.051 3.925 3.246 1.00 3.33 O +ANISOU 281 OD1 ASN A 14 280 436 546 38 -108 -101 O +ATOM 282 ND2 ASN A 14 10.180 2.025 4.475 1.00 3.15 N +ANISOU 282 ND2 ASN A 14 308 442 445 1 -145 63 N +ATOM 283 H ASN A 14 7.026 3.990 4.837 1.00 1.94 H +ATOM 284 HA ASN A 14 7.946 4.263 2.131 1.00 1.87 H +ATOM 285 HB2 ASN A 14 7.680 1.866 3.971 1.00 2.35 H +ATOM 286 HB3 ASN A 14 8.308 1.735 2.314 1.00 2.35 H +ATOM 287 HD21 ASN A 14 11.107 2.241 4.810 1.00 3.78 H +ATOM 288 HD22 ASN A 14 9.724 1.174 4.767 1.00 3.78 H +ATOM 289 N VAL A 15 4.992 2.817 2.503 1.00 1.46 N +ANISOU 289 N VAL A 15 193 202 157 10 2 -23 N +ATOM 290 CA VAL A 15 3.809 2.515 1.695 1.00 1.45 C +ANISOU 290 CA VAL A 15 204 181 163 19 -4 -35 C +ATOM 291 C VAL A 15 3.309 3.772 0.970 1.00 1.47 C +ANISOU 291 C VAL A 15 210 181 168 28 6 -34 C +ATOM 292 O VAL A 15 2.967 3.733 -0.207 1.00 1.77 O +ANISOU 292 O VAL A 15 264 218 189 23 -28 -42 O +ATOM 293 CB VAL A 15 2.718 1.853 2.546 1.00 1.79 C +ANISOU 293 CB VAL A 15 214 217 249 79 14 -37 C +ATOM 294 CG1 VAL A 15 1.390 1.798 1.795 1.00 2.75 C +ANISOU 294 CG1 VAL A 15 219 348 477 176 -55 -89 C +ATOM 295 CG2 VAL A 15 3.171 0.458 2.966 1.00 2.43 C +ANISOU 295 CG2 VAL A 15 310 229 381 126 -37 -45 C +ATOM 296 H VAL A 15 4.948 2.775 3.510 1.00 1.74 H +ATOM 297 HA VAL A 15 4.112 1.790 0.927 1.00 1.73 H +ATOM 298 HB VAL A 15 2.576 2.457 3.453 1.00 2.15 H +ATOM 299 HG11 VAL A 15 1.086 2.816 1.514 1.00 4.07 H +ATOM 300 HG12 VAL A 15 0.621 1.353 2.443 1.00 4.07 H +ATOM 301 HG13 VAL A 15 1.506 1.187 0.890 1.00 4.07 H +ATOM 302 HG21 VAL A 15 4.124 0.530 3.509 1.00 3.65 H +ATOM 303 HG22 VAL A 15 3.304 -0.169 2.073 1.00 3.65 H +ATOM 304 HG23 VAL A 15 2.411 0.007 3.619 1.00 3.65 H +ATOM 305 N CYS A 16 3.265 4.910 1.697 1.00 1.55 N +ANISOU 305 N CYS A 16 224 181 184 27 6 -12 N +ATOM 306 CA CYS A 16 2.853 6.168 1.085 1.00 1.54 C +ANISOU 306 CA CYS A 16 194 192 199 21 7 0 C +ATOM 307 C CYS A 16 3.680 6.497 -0.171 1.00 1.45 C +ANISOU 307 C CYS A 16 190 182 178 26 -12 -4 C +ATOM 308 O CYS A 16 3.159 7.037 -1.146 1.00 1.80 O +ANISOU 308 O CYS A 16 243 242 198 56 -33 7 O +ATOM 309 CB CYS A 16 2.981 7.257 2.155 1.00 1.93 C +ANISOU 309 CB CYS A 16 284 205 245 -7 16 -2 C +ATOM 310 SG CYS A 16 2.571 8.931 1.593 1.00 2.20 S +ANISOU 310 SG CYS A 16 275 199 360 -33 -49 28 S +ATOM 311 H CYS A 16 3.519 4.890 2.673 1.00 1.87 H +ATOM 312 HA CYS A 16 1.796 6.085 0.795 1.00 1.85 H +ATOM 313 HB2 CYS A 16 2.321 7.000 2.996 1.00 2.33 H +ATOM 314 HB3 CYS A 16 4.013 7.258 2.533 1.00 2.33 H +ATOM 315 N ARG A 17 4.980 6.166 -0.135 1.00 1.46 N +ANISOU 315 N ARG A 17 186 194 172 36 -5 -11 N +ATOM 316 CA ARG A 17 5.850 6.474 -1.244 1.00 1.51 C +ANISOU 316 CA ARG A 17 188 180 205 23 7 -35 C +ATOM 317 C ARG A 17 5.641 5.554 -2.455 1.00 1.61 C +ANISOU 317 C ARG A 17 207 222 182 18 9 -48 C +ATOM 318 O ARG A 17 6.033 5.932 -3.563 1.00 2.20 O +ANISOU 318 O ARG A 17 313 315 204 0 60 -132 O +ATOM 319 CB ARG A 17 7.317 6.413 -0.802 1.00 1.71 C +ANISOU 319 CB ARG A 17 191 215 241 24 1 -29 C +ATOM 320 CG ARG A 17 7.692 7.571 0.124 1.00 1.91 C +ANISOU 320 CG ARG A 17 229 260 238 17 -10 -75 C +ATOM 321 CD ARG A 17 7.903 8.893 -0.615 1.00 2.03 C +ANISOU 321 CD ARG A 17 211 211 348 -1 66 -44 C +ATOM 322 NE ARG A 17 9.156 8.833 -1.364 1.00 2.13 N +ANISOU 322 NE ARG A 17 191 268 350 54 54 -13 N +ATOM 323 CZ ARG A 17 9.472 9.600 -2.396 1.00 1.95 C +ANISOU 323 CZ ARG A 17 222 259 257 -7 47 -35 C +ATOM 324 NH1 ARG A 17 8.585 10.416 -2.966 1.00 2.59 N +ANISOU 324 NH1 ARG A 17 284 377 323 89 75 20 N +ATOM 325 NH2 ARG A 17 10.713 9.561 -2.889 1.00 2.55 N +ANISOU 325 NH2 ARG A 17 253 383 330 10 98 -13 N +ATOM 326 H ARG A 17 5.352 5.696 0.676 1.00 1.75 H +ATOM 327 HA ARG A 17 5.637 7.504 -1.563 1.00 1.81 H +ATOM 328 HB2 ARG A 17 7.498 5.462 -0.282 1.00 2.04 H +ATOM 329 HB3 ARG A 17 7.963 6.439 -1.691 1.00 2.04 H +ATOM 330 HG2 ARG A 17 6.896 7.703 0.870 1.00 2.29 H +ATOM 331 HG3 ARG A 17 8.615 7.312 0.662 1.00 2.29 H +ATOM 332 HD2 ARG A 17 7.065 9.072 -1.303 1.00 2.43 H +ATOM 333 HD3 ARG A 17 7.939 9.721 0.107 1.00 2.43 H +ATOM 334 HE ARG A 17 9.838 8.150 -1.070 1.00 2.55 H +ATOM 335 HH11 ARG A 17 7.642 10.462 -2.611 1.00 3.10 H +ATOM 336 HH12 ARG A 17 8.858 10.988 -3.751 1.00 3.10 H +ATOM 337 HH21 ARG A 17 11.402 8.951 -2.474 1.00 3.07 H +ATOM 338 HH22 ARG A 17 10.962 10.142 -3.675 1.00 3.07 H +ATOM 339 N LEU A 18 5.053 4.360 -2.271 1.00 1.65 N +ANISOU 339 N LEU A 18 236 199 192 15 9 -33 N +ATOM 340 CA LEU A 18 4.954 3.418 -3.387 1.00 1.68 C +ANISOU 340 CA LEU A 18 252 179 208 7 4 -13 C +ATOM 341 C LEU A 18 4.321 4.013 -4.638 1.00 1.55 C +ANISOU 341 C LEU A 18 227 171 189 2 26 -27 C +ATOM 342 O LEU A 18 4.849 3.780 -5.744 1.00 1.81 O +ANISOU 342 O LEU A 18 266 209 213 -3 50 1 O +ATOM 343 CB LEU A 18 4.203 2.149 -2.980 1.00 2.10 C +ANISOU 343 CB LEU A 18 328 197 272 52 -18 -44 C +ATOM 344 CG LEU A 18 4.942 1.212 -2.020 1.00 2.28 C +ANISOU 344 CG LEU A 18 391 228 244 53 -25 -24 C +ATOM 345 CD1 LEU A 18 3.987 0.098 -1.586 1.00 3.65 C +ANISOU 345 CD1 LEU A 18 586 317 483 185 -73 -133 C +ATOM 346 CD2 LEU A 18 6.197 0.625 -2.641 1.00 3.47 C +ANISOU 346 CD2 LEU A 18 481 328 509 97 29 128 C +ATOM 347 H LEU A 18 4.681 4.113 -1.366 1.00 2.00 H +ATOM 348 HA LEU A 18 5.978 3.119 -3.651 1.00 2.01 H +ATOM 349 HB2 LEU A 18 3.254 2.444 -2.511 1.00 2.53 H +ATOM 350 HB3 LEU A 18 3.958 1.585 -3.891 1.00 2.53 H +ATOM 351 HG LEU A 18 5.232 1.787 -1.129 1.00 2.72 H +ATOM 352 HD11 LEU A 18 3.070 0.542 -1.173 1.00 5.44 H +ATOM 353 HD12 LEU A 18 4.472 -0.522 -0.819 1.00 5.44 H +ATOM 354 HD13 LEU A 18 3.733 -0.526 -2.454 1.00 5.44 H +ATOM 355 HD21 LEU A 18 6.879 1.438 -2.928 1.00 5.25 H +ATOM 356 HD22 LEU A 18 5.926 0.042 -3.533 1.00 5.25 H +ATOM 357 HD23 LEU A 18 6.695 -0.030 -1.913 1.00 5.25 H +ATOM 358 N PRO A 19 3.209 4.754 -4.571 1.00 1.63 N +ANISOU 358 N PRO A 19 218 219 181 -2 21 -17 N +ATOM 359 CA PRO A 19 2.660 5.337 -5.804 1.00 1.75 C +ANISOU 359 CA PRO A 19 233 217 214 0 -13 -11 C +ATOM 360 C PRO A 19 3.434 6.548 -6.317 1.00 2.08 C +ANISOU 360 C PRO A 19 273 263 254 57 8 -16 C +ATOM 361 O PRO A 19 3.086 7.062 -7.379 1.00 3.61 O +ANISOU 361 O PRO A 19 463 536 373 246 -81 -117 O +ATOM 362 CB PRO A 19 1.226 5.736 -5.413 1.00 2.27 C +ANISOU 362 CB PRO A 19 216 355 292 -1 -24 0 C +ATOM 363 CG APRO A 19 1.283 5.912 -3.890 0.85 2.25 C +ANISOU 363 CG APRO A 19 236 320 296 -23 27 20 C +ATOM 364 CG BPRO A 19 0.975 5.129 -4.119 0.15 2.42 C +ATOM 365 CD PRO A 19 2.249 4.859 -3.446 1.00 2.24 C +ANISOU 365 CD PRO A 19 255 401 192 -2 41 50 C +ATOM 366 HA PRO A 19 2.625 4.567 -6.588 1.00 2.08 H +ATOM 367 HB2APRO A 19 0.932 6.673 -5.906 0.85 2.72 H +ATOM 368 HB2BPRO A 19 1.110 6.800 -5.370 0.15 2.69 H +ATOM 369 HB3APRO A 19 0.511 4.948 -5.690 0.85 2.72 H +ATOM 370 HB3BPRO A 19 0.580 5.380 -6.120 0.15 2.69 H +ATOM 371 HG2APRO A 19 1.644 6.915 -3.622 0.85 2.69 H +ATOM 372 HG2BPRO A 19 0.366 5.805 -3.504 0.15 2.69 H +ATOM 373 HG3APRO A 19 0.294 5.755 -3.437 0.85 2.69 H +ATOM 374 HG3BPRO A 19 0.419 4.190 -4.251 0.15 2.69 H +ATOM 375 HD2APRO A 19 2.760 5.160 -2.521 0.85 2.68 H +ATOM 376 HD2BPRO A 19 2.521 5.681 -2.769 0.15 2.68 H +ATOM 377 HD3APRO A 19 1.737 3.902 -3.277 0.85 2.68 H +ATOM 378 HD3BPRO A 19 2.205 3.922 -2.874 0.15 2.68 H +ATOM 379 N GLY A 20 4.420 7.027 -5.559 1.00 1.87 N +ANISOU 379 N GLY A 20 264 178 266 -17 67 -25 N +ATOM 380 CA GLY A 20 5.223 8.167 -5.960 1.00 2.48 C +ANISOU 380 CA GLY A 20 345 186 408 -34 195 -40 C +ATOM 381 C GLY A 20 4.902 9.466 -5.248 1.00 1.98 C +ANISOU 381 C GLY A 20 242 170 338 -9 99 -29 C +ATOM 382 O GLY A 20 5.443 10.505 -5.620 1.00 3.00 O +ANISOU 382 O GLY A 20 519 204 415 -12 232 -94 O +ATOM 383 H GLY A 20 4.614 6.582 -4.675 1.00 2.24 H +ATOM 384 HA2 GLY A 20 6.281 7.926 -5.785 1.00 2.95 H +ATOM 385 HA3 GLY A 20 5.093 8.321 -7.041 1.00 2.95 H +ATOM 386 N THR A 21 4.056 9.404 -4.216 1.00 1.67 N +ANISOU 386 N THR A 21 228 168 235 -19 40 -32 N +ATOM 387 CA THR A 21 3.664 10.576 -3.461 1.00 1.43 C +ANISOU 387 CA THR A 21 177 164 200 -2 -2 -6 C +ATOM 388 C THR A 21 4.915 11.347 -3.001 1.00 1.58 C +ANISOU 388 C THR A 21 176 184 240 0 -2 -21 C +ATOM 389 O THR A 21 5.844 10.729 -2.478 1.00 2.25 O +ANISOU 389 O THR A 21 193 270 389 73 -61 -34 O +ATOM 390 CB THR A 21 2.932 10.113 -2.178 1.00 1.52 C +ANISOU 390 CB THR A 21 163 180 234 11 0 -6 C +ATOM 391 OG1 THR A 21 1.964 9.124 -2.552 1.00 1.89 O +ANISOU 391 OG1 THR A 21 210 214 293 43 -32 -50 O +ATOM 392 CG2 THR A 21 2.280 11.274 -1.459 1.00 2.12 C +ANISOU 392 CG2 THR A 21 241 246 318 -29 68 19 C +ATOM 393 H THR A 21 3.676 8.507 -3.952 1.00 2.00 H +ATOM 394 HA THR A 21 3.014 11.225 -4.064 1.00 1.71 H +ATOM 395 HB THR A 21 3.666 9.650 -1.503 1.00 1.83 H +ATOM 396 HG1 THR A 21 2.092 8.329 -2.016 1.00 2.85 H +ATOM 397 HG21 THR A 21 1.606 11.800 -2.148 1.00 3.17 H +ATOM 398 HG22 THR A 21 3.056 11.968 -1.105 1.00 3.17 H +ATOM 399 HG23 THR A 21 1.706 10.898 -0.600 1.00 3.17 H +ATOM 400 N PRO A 22 4.915 12.683 -3.102 1.00 1.83 N +ANISOU 400 N PRO A 22 220 185 289 -20 -2 -33 N +ATOM 401 CA APRO A 22 6.042 13.429 -2.601 0.57 1.82 C +ANISOU 401 CA APRO A 22 339 145 204 -56 75 -144 C +ATOM 402 C APRO A 22 6.387 13.122 -1.160 0.57 1.66 C +ANISOU 402 C APRO A 22 230 195 204 -82 85 -119 C +ATOM 403 O APRO A 22 5.480 13.006 -0.345 0.57 2.09 O +ANISOU 403 O APRO A 22 224 322 246 -51 60 -58 O +ATOM 404 CB APRO A 22 5.655 14.896 -2.744 0.57 2.86 C +ANISOU 404 CB APRO A 22 591 108 387 -50 -5 -173 C +ATOM 405 CG APRO A 22 4.661 14.854 -4.058 0.57 2.66 C +ANISOU 405 CG APRO A 22 420 174 417 69 20 -27 C +ATOM 406 CD APRO A 22 3.957 13.505 -3.910 0.57 2.27 C +ANISOU 406 CD APRO A 22 317 174 370 60 -1 -4 C +ATOM 407 HA APRO A 22 6.915 13.244 -3.241 0.57 1.93 H +ATOM 408 HB2APRO A 22 5.112 15.266 -1.863 0.57 3.34 H +ATOM 409 HB3APRO A 22 6.516 15.539 -2.944 0.57 3.34 H +ATOM 410 HG2APRO A 22 3.919 15.683 -4.043 0.57 3.20 H +ATOM 411 HG3APRO A 22 5.214 14.903 -5.002 0.57 3.20 H +ATOM 412 HD2APRO A 22 2.984 13.625 -3.389 0.57 2.69 H +ATOM 413 HD3APRO A 22 3.752 13.060 -4.903 0.57 2.69 H +ATOM 414 CA BSER A 22 6.034 13.399 -2.687 0.21 1.55 C +ATOM 415 CA CSER A 22 6.112 13.653 -2.656 0.22 2.31 C +ATOM 416 C BSER A 22 6.367 13.062 -1.223 0.21 2.92 C +ATOM 417 C CSER A 22 6.354 13.275 -1.187 0.22 1.92 C +ATOM 418 O BSER A 22 5.412 13.050 -0.345 0.21 1.87 O +ATOM 419 O CSER A 22 5.636 12.705 -0.270 0.22 1.77 O +ATOM 420 CB BSER A 22 5.409 14.835 -2.876 0.21 2.60 C +ATOM 421 CB CSER A 22 5.605 15.097 -2.687 0.22 3.56 C +ATOM 422 OG BSER A 22 4.760 15.243 -1.635 0.21 2.11 O +ATOM 423 OG CSER A 22 6.750 15.771 -2.280 0.22 6.38 O +ATOM 424 HA BSER A 22 6.897 13.240 -3.349 0.21 4.26 H +ATOM 425 HA CSER A 22 7.013 13.518 -3.271 0.22 4.26 H +ATOM 426 N GLU A 23 7.651 13.190 -0.860 1.00 1.86 N +ANISOU 426 N GLU A 23 256 245 205 -32 61 -70 N +ATOM 427 CA GLU A 23 8.108 13.002 0.513 1.00 1.81 C +ANISOU 427 CA GLU A 23 246 213 227 -17 62 -30 C +ATOM 428 C GLU A 23 7.394 13.968 1.459 1.00 1.66 C +ANISOU 428 C GLU A 23 214 206 209 -5 46 -21 C +ATOM 429 O GLU A 23 7.064 13.585 2.589 1.00 1.97 O +ANISOU 429 O GLU A 23 274 260 212 25 62 12 O +ATOM 430 CB GLU A 23 9.620 13.168 0.681 1.00 2.12 C +ANISOU 430 CB GLU A 23 243 280 281 -40 55 1 C +ATOM 431 CG AGLU A 23 10.459 12.148 -0.048 0.58 2.73 C +ANISOU 431 CG AGLU A 23 372 317 349 12 163 64 C +ATOM 432 CG BGLU A 23 10.414 11.969 0.088 0.42 1.79 C +ANISOU 432 CG BGLU A 23 262 182 235 22 34 -17 C +ATOM 433 CD AGLU A 23 11.942 12.208 0.242 0.58 4.60 C +ANISOU 433 CD AGLU A 23 404 1001 343 -141 78 99 C +ATOM 434 CD BGLU A 23 11.911 12.048 0.452 0.42 2.33 C +ANISOU 434 CD BGLU A 23 240 305 341 52 40 113 C +ATOM 435 OE1AGLU A 23 12.418 13.330 0.541 0.58 7.57 O +ANISOU 435 OE1AGLU A 23 395 1235 1244 -482 236 -77 O +ATOM 436 OE1BGLU A 23 12.430 13.113 0.795 0.42 2.70 O +ANISOU 436 OE1BGLU A 23 191 409 425 74 -50 24 O +ATOM 437 OE2AGLU A 23 12.629 11.211 0.128 0.58 7.42 O +ANISOU 437 OE2AGLU A 23 455 1209 1155 128 244 304 O +ATOM 438 OE2BGLU A 23 12.514 10.945 0.316 0.42 4.43 O +ANISOU 438 OE2BGLU A 23 553 501 629 -196 -205 354 O +ATOM 439 H GLU A 23 8.361 13.404 -1.574 1.00 2.23 H +ATOM 440 HA GLU A 23 7.842 11.977 0.808 1.00 2.17 H +ATOM 441 HB2 GLU A 23 9.902 14.169 0.326 1.00 2.55 H +ATOM 442 HB3 GLU A 23 9.860 13.116 1.752 1.00 2.55 H +ATOM 443 HG2AGLU A 23 10.094 11.146 0.214 0.58 3.27 H +ATOM 444 HG2BGLU A 23 9.996 11.029 0.473 0.42 2.13 H +ATOM 445 HG3AGLU A 23 10.310 12.283 -1.128 0.58 3.27 H +ATOM 446 HG3BGLU A 23 10.306 11.966 -1.006 0.42 2.13 H +ATOM 447 N ALA A 24 7.188 15.227 1.041 1.00 1.63 N +ANISOU 447 N ALA A 24 244 204 172 -11 41 -31 N +ATOM 448 CA ALA A 24 6.619 16.195 1.970 1.00 1.65 C +ANISOU 448 CA ALA A 24 227 186 213 -23 25 -26 C +ATOM 449 C ALA A 24 5.192 15.819 2.387 1.00 1.51 C +ANISOU 449 C ALA A 24 221 179 172 12 15 -6 C +ATOM 450 O ALA A 24 4.795 16.037 3.532 1.00 1.85 O +ANISOU 450 O ALA A 24 233 263 205 -30 25 -19 O +ATOM 451 CB ALA A 24 6.663 17.597 1.363 1.00 2.43 C +ANISOU 451 CB ALA A 24 351 195 377 23 72 -56 C +ATOM 452 H ALA A 24 7.422 15.499 0.098 1.00 1.96 H +ATOM 453 HA ALA A 24 7.244 16.200 2.874 1.00 1.98 H +ATOM 454 HB1 ALA A 24 7.696 17.841 1.079 1.00 3.63 H +ATOM 455 HB2 ALA A 24 6.304 18.327 2.101 1.00 3.63 H +ATOM 456 HB3 ALA A 24 6.021 17.630 0.472 1.00 3.63 H +ATOM 457 N ALEU A 25 4.398 15.289 1.441 0.57 1.61 N +ANISOU 457 N ALEU A 25 226 194 191 4 15 -28 N +ATOM 458 CA ALEU A 25 3.048 14.822 1.781 0.57 1.48 C +ANISOU 458 CA ALEU A 25 201 173 186 9 -3 -4 C +ATOM 459 C ALEU A 25 3.113 13.568 2.640 0.57 1.50 C +ANISOU 459 C ALEU A 25 194 194 179 25 16 -3 C +ATOM 460 O ALEU A 25 2.332 13.396 3.580 0.57 2.01 O +ANISOU 460 O ALEU A 25 272 281 210 49 75 28 O +ATOM 461 CB ALEU A 25 2.209 14.621 0.512 0.57 1.70 C +ANISOU 461 CB ALEU A 25 254 190 201 30 -48 22 C +ATOM 462 CG ALEU A 25 1.717 15.929 -0.108 0.57 1.80 C +ANISOU 462 CG ALEU A 25 184 242 258 83 -13 47 C +ATOM 463 CD1ALEU A 25 1.207 15.625 -1.514 0.57 3.58 C +ANISOU 463 CD1ALEU A 25 497 578 285 -4 -115 240 C +ATOM 464 CD2ALEU A 25 0.595 16.583 0.794 0.57 2.15 C +ANISOU 464 CD2ALEU A 25 178 251 386 -37 -34 53 C +ATOM 465 H ALEU A 25 4.733 15.199 0.495 0.57 1.94 H +ATOM 466 HA ALEU A 25 2.567 15.612 2.380 0.57 1.77 H +ATOM 467 HB2ALEU A 25 2.806 14.080 -0.225 0.57 1.61 H +ATOM 468 HB3ALEU A 25 1.337 13.994 0.770 0.57 1.61 H +ATOM 469 HG ALEU A 25 2.565 16.642 -0.141 0.57 2.02 H +ATOM 470 HD11ALEU A 25 0.243 16.147 -1.682 0.57 5.46 H +ATOM 471 HD12ALEU A 25 1.105 14.573 -1.667 0.57 5.46 H +ATOM 472 HD13ALEU A 25 1.941 16.049 -2.253 0.57 5.46 H +ATOM 473 HD21ALEU A 25 0.118 17.396 0.216 0.57 3.21 H +ATOM 474 HD22ALEU A 25 1.043 16.996 1.701 0.57 3.21 H +ATOM 475 HD23ALEU A 25 -0.145 15.824 1.041 0.57 3.21 H +ATOM 476 N BILE A 25 4.398 15.289 1.441 0.21 1.61 N +ANISOU 476 N BILE A 25 226 194 191 4 15 -28 N +ATOM 477 N CILE A 25 4.398 15.289 1.441 0.22 1.61 N +ANISOU 477 N CILE A 25 226 194 191 4 15 -28 N +ATOM 478 CA BILE A 25 3.048 14.822 1.781 0.21 1.48 C +ANISOU 478 CA BILE A 25 201 173 186 9 -3 -4 C +ATOM 479 CA CILE A 25 3.048 14.822 1.781 0.22 1.48 C +ANISOU 479 CA CILE A 25 201 173 186 9 -3 -4 C +ATOM 480 C BILE A 25 3.113 13.568 2.640 0.21 1.50 C +ANISOU 480 C BILE A 25 194 194 179 25 16 -3 C +ATOM 481 C CILE A 25 3.113 13.568 2.640 0.22 1.50 C +ANISOU 481 C CILE A 25 194 194 179 25 16 -3 C +ATOM 482 O BILE A 25 2.332 13.396 3.580 0.21 2.01 O +ANISOU 482 O BILE A 25 272 281 210 49 75 28 O +ATOM 483 O CILE A 25 2.332 13.396 3.580 0.22 2.01 O +ANISOU 483 O CILE A 25 272 281 210 49 75 28 O +ATOM 484 CB BILE A 25 2.225 14.590 0.511 0.21 1.67 C +ATOM 485 CB CILE A 25 2.194 14.590 0.526 0.22 2.08 C +ATOM 486 CG1BILE A 25 1.931 15.856 -0.269 0.21 2.53 C +ATOM 487 CG1CILE A 25 1.693 15.919 -0.061 0.22 2.48 C +ATOM 488 CG2BILE A 25 0.955 13.756 0.691 0.21 2.16 C +ATOM 489 CG2CILE A 25 0.939 13.672 0.877 0.22 2.83 C +ATOM 490 CD1BILE A 25 0.819 16.720 0.588 0.21 1.98 C +ATOM 491 CD1CILE A 25 1.188 15.934 -1.404 0.22 3.60 C +ATOM 492 H BILE A 25 4.733 15.199 0.495 0.21 1.94 H +ATOM 493 H CILE A 25 4.733 15.199 0.495 0.22 1.94 H +ATOM 494 HA BILE A 25 2.567 15.612 2.380 0.21 1.77 H +ATOM 495 HA CILE A 25 2.567 15.612 2.380 0.22 1.77 H +ATOM 496 HB BILE A 25 2.872 13.991 -0.145 0.21 4.26 H +ATOM 497 HB CILE A 25 2.808 14.078 -0.229 0.22 4.26 H +ATOM 498 HG12BILE A 25 1.534 15.605 -1.263 0.21 4.26 H +ATOM 499 HG12CILE A 25 0.897 16.295 0.598 0.22 4.26 H +ATOM 500 HG13BILE A 25 2.851 16.443 -0.399 0.21 4.26 H +ATOM 501 HG13CILE A 25 2.521 16.639 -0.008 0.22 4.26 H +ATOM 502 HG21BILE A 25 1.203 12.817 1.205 0.21 5.32 H +ATOM 503 HG21CILE A 25 0.421 13.388 -0.050 0.22 5.32 H +ATOM 504 HG22BILE A 25 0.522 13.531 -0.294 0.21 5.32 H +ATOM 505 HG22CILE A 25 1.282 12.766 1.397 0.22 5.32 H +ATOM 506 HG23BILE A 25 0.227 14.321 1.290 0.21 5.32 H +ATOM 507 HG23CILE A 25 0.249 14.228 1.527 0.22 5.32 H +ATOM 508 HD11BILE A 25 0.481 17.578 -0.010 0.21 5.32 H +ATOM 509 HD12BILE A 25 1.275 17.081 1.521 0.21 5.32 H +ATOM 510 HD13BILE A 25 -0.041 16.078 0.825 0.21 5.32 H +ATOM 511 N CYS A 26 4.028 12.634 2.294 1.00 1.57 N +ANISOU 511 N CYS A 26 215 187 192 32 27 4 N +ATOM 512 CA CYS A 26 4.137 11.461 3.154 1.00 1.52 C +ANISOU 512 CA CYS A 26 213 184 179 24 5 -11 C +ATOM 513 C CYS A 26 4.607 11.823 4.564 1.00 1.58 C +ANISOU 513 C CYS A 26 228 208 162 22 18 -7 C +ATOM 514 O CYS A 26 4.231 11.137 5.527 1.00 2.03 O +ANISOU 514 O CYS A 26 309 259 201 54 17 -60 O +ATOM 515 CB CYS A 26 5.038 10.395 2.541 1.00 1.82 C +ANISOU 515 CB CYS A 26 257 205 228 0 5 17 C +ATOM 516 SG CYS A 26 4.363 9.697 1.004 1.00 2.01 S +ANISOU 516 SG CYS A 26 362 216 186 0 6 14 S +ATOM 517 H CYS A 26 4.606 12.743 1.485 1.00 1.87 H +ATOM 518 HA CYS A 26 3.132 11.025 3.248 1.00 1.81 H +ATOM 519 HB2 CYS A 26 6.023 10.835 2.331 1.00 2.18 H +ATOM 520 HB3 CYS A 26 5.181 9.584 3.269 1.00 2.18 H +ATOM 521 N ALA A 27 5.399 12.889 4.697 1.00 1.58 N +ANISOU 521 N ALA A 27 213 227 161 19 11 -17 N +ATOM 522 CA ALA A 27 5.848 13.355 6.011 1.00 1.58 C +ANISOU 522 CA ALA A 27 192 236 170 23 -1 -5 C +ATOM 523 C ALA A 27 4.662 13.846 6.849 1.00 1.61 C +ANISOU 523 C ALA A 27 202 216 193 27 8 1 C +ATOM 524 O ALA A 27 4.481 13.369 7.973 1.00 2.00 O +ANISOU 524 O ALA A 27 243 343 174 42 12 24 O +ATOM 525 CB ALA A 27 6.896 14.453 5.817 1.00 2.02 C +ANISOU 525 CB ALA A 27 246 302 218 32 -1 -62 C +ATOM 526 H ALA A 27 5.696 13.387 3.871 1.00 1.89 H +ATOM 527 HA ALA A 27 6.324 12.513 6.533 1.00 1.89 H +ATOM 528 HB1 ALA A 27 7.723 14.066 5.206 1.00 3.03 H +ATOM 529 HB2 ALA A 27 7.281 14.770 6.796 1.00 3.03 H +ATOM 530 HB3 ALA A 27 6.436 15.312 5.308 1.00 3.03 H +ATOM 531 N THR A 28 3.855 14.766 6.317 1.00 1.80 N +ANISOU 531 N THR A 28 245 254 182 26 15 39 N +ATOM 532 CA THR A 28 2.711 15.207 7.154 1.00 2.02 C +ANISOU 532 CA THR A 28 247 255 263 9 37 47 C +ATOM 533 C THR A 28 1.709 14.078 7.372 1.00 2.17 C +ANISOU 533 C THR A 28 311 254 259 20 88 35 C +ATOM 534 O THR A 28 1.005 14.078 8.394 1.00 3.76 O +ANISOU 534 O THR A 28 623 383 419 -45 310 -81 O +ATOM 535 CB THR A 28 2.024 16.440 6.551 1.00 2.05 C +ANISOU 535 CB THR A 28 226 215 338 1 -1 9 C +ATOM 536 OG1 THR A 28 1.701 16.141 5.201 1.00 2.19 O +ANISOU 536 OG1 THR A 28 244 241 345 5 -30 17 O +ATOM 537 CG2 THR A 28 2.895 17.679 6.662 1.00 2.85 C +ANISOU 537 CG2 THR A 28 306 269 506 -17 -53 -49 C +ATOM 538 H THR A 28 4.002 15.153 5.404 1.00 2.16 H +ATOM 539 HA THR A 28 3.109 15.487 8.125 1.00 2.41 H +ATOM 540 HB THR A 28 1.090 16.619 7.102 1.00 2.46 H +ATOM 541 HG1 THR A 28 0.931 16.659 4.931 1.00 3.28 H +ATOM 542 HG21 THR A 28 2.374 18.534 6.209 1.00 4.24 H +ATOM 543 HG22 THR A 28 3.844 17.507 6.135 1.00 4.24 H +ATOM 544 HG23 THR A 28 3.096 17.891 7.721 1.00 4.24 H +ATOM 545 N TYR A 29 1.615 13.121 6.447 1.00 1.81 N +ANISOU 545 N TYR A 29 202 265 219 40 21 29 N +ATOM 546 CA TYR A 29 0.683 12.006 6.638 1.00 2.09 C +ANISOU 546 CA TYR A 29 178 346 269 104 6 0 C +ATOM 547 C TYR A 29 1.098 11.099 7.795 1.00 1.98 C +ANISOU 547 C TYR A 29 184 340 225 88 36 25 C +ATOM 548 O TYR A 29 0.235 10.553 8.485 1.00 3.44 O +ANISOU 548 O TYR A 29 217 653 437 311 80 28 O +ATOM 549 CB TYR A 29 0.610 11.302 5.324 1.00 3.00 C +ANISOU 549 CB TYR A 29 393 453 291 72 -28 -149 C +ATOM 550 CG ATYR A 29 0.080 9.859 5.257 0.36 2.22 C +ATOM 551 CG BTYR A 29 -0.574 10.377 5.324 0.31 1.83 C +ATOM 552 CG CTYR A 29 -0.126 9.896 5.414 0.33 5.29 C +ATOM 553 CD1ATYR A 29 -1.270 9.619 5.525 0.36 2.53 C +ATOM 554 CD1BTYR A 29 -1.804 10.544 5.928 0.31 2.68 C +ATOM 555 CD1CTYR A 29 -1.474 9.767 5.525 0.33 6.05 C +ATOM 556 CD2ATYR A 29 0.939 8.787 4.966 0.36 2.12 C +ATOM 557 CD2BTYR A 29 -0.364 9.249 4.564 0.31 8.57 C +ATOM 558 CD2CTYR A 29 0.569 8.620 5.369 0.33 7.83 C +ATOM 559 CE1ATYR A 29 -1.759 8.287 5.481 0.36 2.69 C +ATOM 560 CE1BTYR A 29 -2.782 9.582 5.794 0.31 2.70 C +ATOM 561 CE1CTYR A 29 -2.209 8.565 5.593 0.33 5.76 C +ATOM 562 CE2ATYR A 29 0.450 7.473 4.944 0.36 2.09 C +ATOM 563 CE2BTYR A 29 -1.342 8.324 4.429 0.31 10.63 C +ATOM 564 CE2CTYR A 29 -0.126 7.362 5.458 0.33 7.19 C +ATOM 565 CZ ATYR A 29 -0.900 7.233 5.212 0.36 2.14 C +ATOM 566 CZ BTYR A 29 -2.572 8.472 5.033 0.31 5.29 C +ATOM 567 CZ CTYR A 29 -1.474 7.381 5.570 0.33 6.65 C +ATOM 568 OH ATYR A 29 -1.390 5.956 5.212 0.36 2.52 O +ATOM 569 OH BTYR A 29 -3.510 7.492 4.877 0.31 7.13 O +ATOM 570 OH CTYR A 29 -2.251 6.252 5.660 0.33 7.72 O +ATOM 571 H TYR A 29 2.187 13.164 5.617 1.00 2.17 H +ATOM 572 HA TYR A 29 -0.310 12.421 6.863 1.00 2.50 H +ATOM 573 HB2 TYR A 29 -0.017 11.913 4.659 1.00 3.68 H +ATOM 574 HB3 TYR A 29 1.622 11.300 4.897 1.00 3.68 H +ATOM 575 HD1ATYR A 29 -1.945 10.451 5.769 0.36 3.68 H +ATOM 576 HD1BTYR A 29 -2.004 11.448 6.519 0.31 3.68 H +ATOM 577 HD1CTYR A 29 -2.054 10.699 5.568 0.33 3.68 H +ATOM 578 HD2ATYR A 29 2.001 8.978 4.755 0.36 3.68 H +ATOM 579 HD2BTYR A 29 0.603 9.099 4.063 0.31 3.68 H +ATOM 580 HD2CTYR A 29 1.662 8.615 5.263 0.33 3.68 H +ATOM 581 HE1ATYR A 29 -2.826 8.091 5.660 0.36 3.68 H +ATOM 582 HE1BTYR A 29 -3.745 9.713 6.308 0.31 3.68 H +ATOM 583 HE1CTYR A 29 -3.306 8.562 5.659 0.33 3.68 H +ATOM 584 HE2ATYR A 29 1.125 6.636 4.716 0.36 3.68 H +ATOM 585 HE2BTYR A 29 -1.151 7.429 3.821 0.31 3.68 H +ATOM 586 HE2CTYR A 29 0.425 6.411 5.436 0.33 3.68 H +ATOM 587 HH ATYR A 29 -0.676 5.337 5.006 0.36 4.60 H +ATOM 588 HH BTYR A 29 -4.307 7.726 5.372 0.31 4.60 H +ATOM 589 HH CTYR A 29 -3.152 6.458 5.376 0.33 4.60 H +ATOM 590 N THR A 30 2.412 10.896 7.976 1.00 1.83 N +ANISOU 590 N THR A 30 182 250 262 82 26 10 N +ATOM 591 CA THR A 30 2.926 9.885 8.890 1.00 2.32 C +ANISOU 591 CA THR A 30 234 283 364 159 62 36 C +ATOM 592 C THR A 30 3.531 10.416 10.185 1.00 2.73 C +ANISOU 592 C THR A 30 227 477 332 210 30 29 C +ATOM 593 O THR A 30 3.704 9.609 11.108 1.00 4.05 O +ANISOU 593 O THR A 30 449 707 380 332 0 37 O +ATOM 594 CB THR A 30 4.031 9.054 8.197 1.00 3.05 C +ANISOU 594 CB THR A 30 324 290 544 190 141 102 C +ATOM 595 OG1 THR A 30 5.123 9.910 7.843 1.00 2.66 O +ANISOU 595 OG1 THR A 30 230 431 348 165 42 68 O +ATOM 596 CG2 THR A 30 3.499 8.284 7.008 1.00 4.52 C +ANISOU 596 CG2 THR A 30 613 251 852 -75 252 -57 C +ATOM 597 H THR A 30 3.067 11.463 7.460 1.00 2.20 H +ATOM 598 HA THR A 30 2.101 9.207 9.151 1.00 2.77 H +ATOM 599 HB THR A 30 4.405 8.323 8.928 1.00 3.68 H +ATOM 600 HG1 THR A 30 4.859 10.481 7.108 1.00 3.93 H +ATOM 601 HG21 THR A 30 4.315 7.705 6.553 1.00 6.77 H +ATOM 602 HG22 THR A 30 3.091 8.987 6.269 1.00 6.77 H +ATOM 603 HG23 THR A 30 2.706 7.600 7.340 1.00 6.77 H +ATOM 604 N GLY A 31 3.931 11.687 10.203 1.00 2.56 N +ANISOU 604 N GLY A 31 203 496 272 119 16 3 N +ATOM 605 CA GLY A 31 4.732 12.209 11.290 1.00 3.13 C +ANISOU 605 CA GLY A 31 231 727 229 24 38 49 C +ATOM 606 C GLY A 31 6.229 12.148 11.039 1.00 2.12 C +ANISOU 606 C GLY A 31 221 372 212 22 15 24 C +ATOM 607 O GLY A 31 6.995 12.658 11.864 1.00 2.49 O +ANISOU 607 O GLY A 31 288 419 239 -65 -14 60 O +ATOM 608 H GLY A 31 3.671 12.298 9.443 1.00 3.08 H +ATOM 609 HA2 GLY A 31 4.446 13.255 11.469 1.00 3.72 H +ATOM 610 HA3 GLY A 31 4.503 11.640 12.202 1.00 3.72 H +ATOM 611 N CYS A 32 6.670 11.511 9.952 1.00 1.96 N +ANISOU 611 N CYS A 32 202 347 195 15 23 -44 N +ATOM 612 CA CYS A 32 8.069 11.595 9.568 1.00 1.82 C +ANISOU 612 CA CYS A 32 198 260 231 -9 30 -42 C +ATOM 613 C CYS A 32 8.384 13.045 9.130 1.00 1.88 C +ANISOU 613 C CYS A 32 227 253 231 -6 37 -14 C +ATOM 614 O CYS A 32 7.488 13.854 8.918 1.00 2.55 O +ANISOU 614 O CYS A 32 262 348 359 95 -6 18 O +ATOM 615 CB CYS A 32 8.382 10.621 8.435 1.00 1.92 C +ANISOU 615 CB CYS A 32 249 256 223 -4 35 -35 C +ATOM 616 SG CYS A 32 8.012 8.869 8.821 1.00 2.05 S +ANISOU 616 SG CYS A 32 247 246 283 0 -21 -76 S +ATOM 617 H CYS A 32 6.029 10.967 9.394 1.00 2.35 H +ATOM 618 HA CYS A 32 8.693 11.342 10.437 1.00 2.18 H +ATOM 619 HB2 CYS A 32 7.803 10.915 7.548 1.00 2.31 H +ATOM 620 HB3 CYS A 32 9.447 10.708 8.181 1.00 2.31 H +ATOM 621 N ILE A 33 9.688 13.311 8.988 1.00 2.20 N +ANISOU 621 N ILE A 33 235 204 395 -32 98 -13 N +ATOM 622 CA ILE A 33 10.176 14.645 8.666 1.00 2.19 C +ANISOU 622 CA ILE A 33 277 206 349 -24 107 -22 C +ATOM 623 C ILE A 33 11.242 14.531 7.578 1.00 2.20 C +ANISOU 623 C ILE A 33 233 279 322 -29 77 -35 C +ATOM 624 O ILE A 33 11.868 13.485 7.382 1.00 2.85 O +ANISOU 624 O ILE A 33 357 311 413 -3 161 20 O +ATOM 625 CB ILE A 33 10.748 15.355 9.917 1.00 2.70 C +ANISOU 625 CB ILE A 33 439 191 395 -44 65 -50 C +ATOM 626 CG1 ILE A 33 11.996 14.655 10.484 1.00 3.08 C +ANISOU 626 CG1 ILE A 33 489 297 384 0 -27 -71 C +ATOM 627 CG2 ILE A 33 9.654 15.480 10.971 1.00 3.59 C +ANISOU 627 CG2 ILE A 33 662 336 362 -85 146 70 C +ATOM 628 CD1 ILE A 33 12.693 15.430 11.579 1.00 4.51 C +ANISOU 628 CD1 ILE A 33 767 424 520 -10 -153 -211 C +ATOM 629 H ILE A 33 10.355 12.563 9.108 1.00 2.63 H +ATOM 630 HA ILE A 33 9.337 15.241 8.279 1.00 2.63 H +ATOM 631 HB ILE A 33 11.042 16.371 9.619 1.00 3.24 H +ATOM 632 HG12 ILE A 33 11.700 13.673 10.880 1.00 3.73 H +ATOM 633 HG13 ILE A 33 12.707 14.483 9.665 1.00 3.73 H +ATOM 634 HG21 ILE A 33 8.779 15.981 10.533 1.00 5.36 H +ATOM 635 HG22 ILE A 33 10.028 16.071 11.819 1.00 5.36 H +ATOM 636 HG23 ILE A 33 9.366 14.479 11.321 1.00 5.36 H +ATOM 637 HD11 ILE A 33 13.561 14.857 11.937 1.00 6.68 H +ATOM 638 HD12 ILE A 33 11.996 15.596 12.412 1.00 6.68 H +ATOM 639 HD13 ILE A 33 13.031 16.398 11.185 1.00 6.68 H +ATOM 640 N ILE A 34 11.452 15.662 6.905 1.00 2.63 N +ANISOU 640 N ILE A 34 241 321 436 39 116 -7 N +ATOM 641 CA ILE A 34 12.511 15.815 5.919 1.00 2.58 C +ANISOU 641 CA ILE A 34 224 389 368 38 73 -38 C +ATOM 642 C ILE A 34 13.505 16.814 6.473 1.00 2.65 C +ANISOU 642 C ILE A 34 225 324 454 92 30 -25 C +ATOM 643 O ILE A 34 13.103 17.913 6.899 1.00 3.64 O +ANISOU 643 O ILE A 34 306 371 703 -9 -11 13 O +ATOM 644 CB AILE A 34 11.943 16.410 4.601 0.77 2.58 C +ANISOU 644 CB AILE A 34 249 394 337 -51 8 -52 C +ATOM 645 CB BILE A 34 11.930 15.960 4.530 0.23 2.82 C +ATOM 646 CG1AILE A 34 10.907 15.505 3.988 0.77 3.88 C +ANISOU 646 CG1AILE A 34 306 504 662 -216 -93 -39 C +ATOM 647 CG1BILE A 34 10.646 15.066 4.227 0.23 3.42 C +ATOM 648 CG2AILE A 34 13.188 16.567 3.597 0.77 4.54 C +ANISOU 648 CG2AILE A 34 354 1129 242 28 24 -103 C +ATOM 649 CG2BILE A 34 12.953 15.674 3.361 0.23 5.02 C +ATOM 650 CD1AILE A 34 10.214 16.126 2.774 0.77 4.86 C +ANISOU 650 CD1AILE A 34 362 1061 423 -390 -112 106 C +ATOM 651 CD1BILE A 34 10.915 13.658 4.166 0.23 4.90 C +ATOM 652 H ILE A 34 10.850 16.457 7.091 1.00 3.16 H +ATOM 653 HA ILE A 34 12.999 14.860 5.732 1.00 3.11 H +ATOM 654 HB AILE A 34 11.546 17.419 4.767 0.77 3.18 H +ATOM 655 HB BILE A 34 11.594 17.042 4.417 0.23 5.82 H +ATOM 656 HG12AILE A 34 11.379 14.558 3.690 0.77 4.67 H +ATOM 657 HG12BILE A 34 10.000 15.400 4.720 0.23 5.82 H +ATOM 658 HG13AILE A 34 10.168 15.285 4.769 0.77 4.67 H +ATOM 659 HG13BILE A 34 10.570 15.490 3.330 0.23 5.82 H +ATOM 660 HG21AILE A 34 13.924 17.239 4.042 0.77 6.79 H +ATOM 661 HG21BILE A 34 12.468 16.057 2.467 0.23 7.28 H +ATOM 662 HG22AILE A 34 12.804 17.021 2.656 0.77 6.79 H +ATOM 663 HG22BILE A 34 13.188 14.712 3.412 0.23 7.28 H +ATOM 664 HG23AILE A 34 13.602 15.595 3.398 0.77 6.79 H +ATOM 665 HG23BILE A 34 13.798 16.386 3.626 0.23 7.28 H +ATOM 666 HD11AILE A 34 9.436 15.451 2.406 0.77 7.28 H +ATOM 667 HD11BILE A 34 9.905 13.064 4.008 0.23 7.28 H +ATOM 668 HD12AILE A 34 10.947 16.322 1.983 0.77 7.28 H +ATOM 669 HD12BILE A 34 11.310 13.266 5.107 0.23 7.28 H +ATOM 670 HD13AILE A 34 9.746 17.087 3.076 0.77 7.28 H +ATOM 671 HD13BILE A 34 11.540 13.357 3.329 0.23 7.28 H +ATOM 672 N ILE A 35 14.790 16.458 6.442 1.00 2.97 N +ANISOU 672 N ILE A 35 215 362 549 72 49 -34 N +ATOM 673 CA ILE A 35 15.847 17.376 6.893 1.00 3.14 C +ANISOU 673 CA ILE A 35 266 456 470 71 28 -82 C +ATOM 674 C ILE A 35 16.855 17.522 5.750 1.00 3.18 C +ANISOU 674 C ILE A 35 230 395 581 126 61 -35 C +ATOM 675 O ILE A 35 17.024 16.622 4.923 1.00 3.74 O +ANISOU 675 O ILE A 35 309 467 642 60 112 -69 O +ATOM 676 CB ILE A 35 16.545 16.890 8.176 1.00 4.30 C +ANISOU 676 CB ILE A 35 375 709 549 195 -60 -200 C +ATOM 677 CG1 ILE A 35 17.227 15.531 7.987 1.00 4.97 C +ANISOU 677 CG1 ILE A 35 434 695 757 364 -155 -134 C +ATOM 678 CG2 ILE A 35 15.532 16.851 9.299 1.00 6.65 C +ANISOU 678 CG2 ILE A 35 625 1404 496 182 17 -321 C +ATOM 679 CD1 ILE A 35 18.146 15.152 9.138 1.00 7.82 C +ANISOU 679 CD1 ILE A 35 588 1219 1163 767 -423 -377 C +ATOM 680 H ILE A 35 15.032 15.548 6.123 1.00 3.56 H +ATOM 681 HA ILE A 35 15.402 18.361 7.092 1.00 3.77 H +ATOM 682 HB ILE A 35 17.318 17.624 8.441 1.00 5.14 H +ATOM 683 HG12 ILE A 35 16.455 14.757 7.878 1.00 6.02 H +ATOM 684 HG13 ILE A 35 17.812 15.553 7.057 1.00 6.02 H +ATOM 685 HG21 ILE A 35 15.093 17.849 9.432 1.00 9.79 H +ATOM 686 HG22 ILE A 35 16.028 16.541 10.230 1.00 9.79 H +ATOM 687 HG23 ILE A 35 14.738 16.132 9.051 1.00 9.79 H +ATOM 688 HD11 ILE A 35 18.613 14.179 8.930 1.00 11.67 H +ATOM 689 HD12 ILE A 35 17.562 15.087 10.067 1.00 11.67 H +ATOM 690 HD13 ILE A 35 18.928 15.917 9.251 1.00 11.67 H +ATOM 691 N PRO A 36 17.593 18.645 5.733 1.00 3.57 N +ANISOU 691 N PRO A 36 284 402 669 147 52 -59 N +ATOM 692 CA PRO A 36 18.581 18.845 4.683 1.00 3.77 C +ANISOU 692 CA PRO A 36 308 513 609 202 20 -109 C +ATOM 693 C PRO A 36 19.866 18.079 4.953 1.00 4.27 C +ANISOU 693 C PRO A 36 260 597 764 159 58 -96 C +ATOM 694 O PRO A 36 20.605 17.835 3.982 1.00 6.26 O +ANISOU 694 O PRO A 36 421 977 981 89 245 -54 O +ATOM 695 CB APRO A 36 18.725 20.367 4.596 0.68 4.58 C +ANISOU 695 CB APRO A 36 438 532 770 346 -48 -139 C +ATOM 696 CB BPRO A 36 19.047 20.307 4.847 0.32 7.48 C +ANISOU 696 CB BPRO A 36 625 447 1769 246 491 -144 C +ATOM 697 CG APRO A 36 18.403 20.829 6.030 0.68 4.64 C +ANISOU 697 CG APRO A 36 511 431 821 136 -227 -208 C +ATOM 698 CG BPRO A 36 18.192 20.880 5.853 0.32 7.85 C +ANISOU 698 CG BPRO A 36 982 586 1414 -40 390 -362 C +ATOM 699 CD PRO A 36 17.286 19.902 6.471 1.00 4.70 C +ANISOU 699 CD PRO A 36 470 447 866 18 44 -109 C +ATOM 700 HA PRO A 36 18.154 18.485 3.736 1.00 4.52 H +ATOM 701 HB2APRO A 36 19.746 20.653 4.307 0.68 5.43 H +ATOM 702 HB2BPRO A 36 20.098 20.345 5.166 0.32 8.94 H +ATOM 703 HB3APRO A 36 18.015 20.792 3.873 0.68 5.43 H +ATOM 704 HB3BPRO A 36 18.947 20.854 3.898 0.32 8.94 H +ATOM 705 HG2APRO A 36 19.281 20.726 6.683 0.68 5.53 H +ATOM 706 HG2BPRO A 36 18.817 21.332 6.637 0.32 9.50 H +ATOM 707 HG3APRO A 36 18.072 21.877 6.041 0.68 5.53 H +ATOM 708 HG3BPRO A 36 17.594 21.682 5.399 0.32 9.50 H +ATOM 709 HD2 PRO A 36 17.309 19.741 7.558 1.00 5.61 H +ATOM 710 HD3 PRO A 36 16.302 20.301 6.186 1.00 5.61 H +ATOM 711 N GLY A 37 20.154 17.799 6.202 1.00 4.59 N +ANISOU 711 N GLY A 37 281 589 872 257 -88 -91 N +ATOM 712 CA GLY A 37 21.334 17.013 6.608 1.00 6.65 C +ANISOU 712 CA GLY A 37 318 583 1627 402 -328 -165 C +ATOM 713 C GLY A 37 21.082 15.528 6.415 1.00 5.02 C +ANISOU 713 C GLY A 37 252 600 1056 272 -141 -118 C +ATOM 714 O GLY A 37 20.097 15.097 5.840 1.00 6.64 O +ANISOU 714 O GLY A 37 391 663 1469 188 -374 -94 O +ATOM 715 H GLY A 37 19.534 18.130 6.933 1.00 5.48 H +ATOM 716 HA2 GLY A 37 22.187 17.355 5.979 1.00 7.83 H +ATOM 717 HA3 GLY A 37 21.574 17.256 7.647 1.00 7.83 H +ATOM 718 N ALA A 38 22.008 14.746 6.971 1.00 4.34 N +ANISOU 718 N ALA A 38 276 539 832 236 -85 -113 N +ATOM 719 CA ALA A 38 21.995 13.320 6.837 1.00 4.98 C +ANISOU 719 CA ALA A 38 363 554 972 156 -141 -110 C +ATOM 720 C ALA A 38 21.843 12.609 8.193 1.00 5.36 C +ANISOU 720 C ALA A 38 334 532 1168 324 -76 -102 C +ATOM 721 O ALA A 38 21.806 11.376 8.221 1.00 7.76 O +ANISOU 721 O ALA A 38 889 535 1524 383 -155 -99 O +ATOM 722 CB ALA A 38 23.235 12.802 6.109 1.00 6.76 C +ANISOU 722 CB ALA A 38 632 839 1096 -39 38 -48 C +ATOM 723 H ALA A 38 22.755 15.183 7.494 1.00 5.19 H +ATOM 724 HA ALA A 38 21.120 13.055 6.227 1.00 5.95 H +ATOM 725 HB1 ALA A 38 23.289 13.257 5.110 1.00 9.94 H +ATOM 726 HB2 ALA A 38 23.172 11.710 6.011 1.00 9.94 H +ATOM 727 HB3 ALA A 38 24.134 13.068 6.682 1.00 9.94 H +ATOM 728 N THR A 39 21.787 13.377 9.290 1.00 4.88 N +ANISOU 728 N THR A 39 218 678 956 429 -8 -48 N +ATOM 729 CA THR A 39 21.840 12.801 10.610 1.00 5.83 C +ANISOU 729 CA THR A 39 211 946 1059 605 2 -86 C +ATOM 730 C THR A 39 20.535 13.026 11.330 1.00 4.95 C +ANISOU 730 C THR A 39 264 715 899 364 -32 -131 C +ATOM 731 O THR A 39 20.250 14.149 11.772 1.00 6.84 O +ANISOU 731 O THR A 39 578 710 1308 172 -23 -278 O +ATOM 732 CB ATHR A 39 23.123 13.277 11.318 0.57 7.03 C +ANISOU 732 CB ATHR A 39 62 1559 1048 754 -8 -64 C +ATOM 733 CB BTHR A 39 22.850 13.578 11.475 0.43 5.67 C +ANISOU 733 CB BTHR A 39 144 1182 827 556 8 6 C +ATOM 734 OG1ATHR A 39 24.242 13.046 10.381 0.57 5.41 O +ANISOU 734 OG1ATHR A 39 241 829 985 532 5 -48 O +ATOM 735 OG1BTHR A 39 24.173 13.586 10.841 0.43 3.62 O +ANISOU 735 OG1BTHR A 39 175 468 729 233 15 -44 O +ATOM 736 CG2ATHR A 39 23.351 12.187 12.361 0.57 6.86 C +ANISOU 736 CG2ATHR A 39 420 1462 722 530 15 60 C +ATOM 737 CG2BTHR A 39 23.191 12.939 12.903 0.43 5.02 C +ANISOU 737 CG2BTHR A 39 356 965 586 271 20 -38 C +ATOM 738 H THR A 39 21.706 14.378 9.190 1.00 5.83 H +ATOM 739 HA THR A 39 21.940 11.715 10.475 1.00 6.89 H +ATOM 740 HB BTHR A 39 22.501 14.611 11.609 0.43 6.13 H +ATOM 741 HG21BTHR A 39 23.929 13.568 13.419 0.43 7.66 H +ATOM 742 HG22BTHR A 39 23.602 11.930 12.764 0.43 7.66 H +ATOM 743 HG23BTHR A 39 22.274 12.881 13.506 0.43 7.66 H +ATOM 744 N CYS A 40 19.748 11.982 11.477 1.00 4.08 N +ANISOU 744 N CYS A 40 236 598 713 197 67 -62 N +ATOM 745 CA CYS A 40 18.460 12.120 12.139 1.00 3.64 C +ANISOU 745 CA CYS A 40 226 564 591 106 12 -48 C +ATOM 746 C CYS A 40 18.660 12.202 13.669 1.00 3.83 C +ANISOU 746 C CYS A 40 242 596 616 31 -56 -14 C +ATOM 747 O CYS A 40 19.515 11.523 14.227 1.00 4.96 O +ANISOU 747 O CYS A 40 319 845 719 -9 -116 134 O +ATOM 748 CB CYS A 40 17.591 10.914 11.825 1.00 3.70 C +ANISOU 748 CB CYS A 40 243 613 549 100 36 -91 C +ATOM 749 SG CYS A 40 17.124 10.807 10.067 1.00 4.08 S +ANISOU 749 SG CYS A 40 295 711 543 2 146 -61 S +ATOM 750 H CYS A 40 20.039 11.081 11.128 1.00 4.91 H +ATOM 751 HA CYS A 40 17.962 13.033 11.784 1.00 4.36 H +ATOM 752 HB2 CYS A 40 18.133 10.000 12.107 1.00 4.44 H +ATOM 753 HB3 CYS A 40 16.678 10.963 12.435 1.00 4.44 H +ATOM 754 N PRO A 41 17.847 13.009 14.329 1.00 4.47 N +ANISOU 754 N PRO A 41 271 627 798 -71 -62 -1 N +ATOM 755 CA PRO A 41 17.975 13.139 15.787 1.00 4.95 C +ANISOU 755 CA PRO A 41 378 686 816 -185 -69 -72 C +ATOM 756 C PRO A 41 17.355 11.965 16.530 1.00 4.16 C +ANISOU 756 C PRO A 41 287 660 631 -214 -60 19 C +ATOM 757 O PRO A 41 16.627 11.147 15.969 1.00 4.00 O +ANISOU 757 O PRO A 41 296 672 549 -189 -27 -11 O +ATOM 758 CB PRO A 41 17.215 14.451 16.070 1.00 6.44 C +ANISOU 758 CB PRO A 41 693 607 1145 -292 -4 -91 C +ATOM 759 CG PRO A 41 16.102 14.430 15.016 1.00 5.94 C +ANISOU 759 CG PRO A 41 523 553 1180 -76 62 111 C +ATOM 760 CD PRO A 41 16.799 13.881 13.768 1.00 5.16 C +ANISOU 760 CD PRO A 41 404 583 970 63 -15 50 C +ATOM 761 HA PRO A 41 19.033 13.246 16.065 1.00 5.97 H +ATOM 762 HB2 PRO A 41 16.800 14.459 17.088 1.00 7.65 H +ATOM 763 HB3 PRO A 41 17.869 15.325 15.941 1.00 7.65 H +ATOM 764 HG2 PRO A 41 15.277 13.774 15.328 1.00 7.13 H +ATOM 765 HG3 PRO A 41 15.709 15.440 14.837 1.00 7.13 H +ATOM 766 HD2 PRO A 41 16.100 13.309 13.143 1.00 6.20 H +ATOM 767 HD3 PRO A 41 17.236 14.692 13.169 1.00 6.20 H +ATOM 768 N GLY A 42 17.643 11.915 17.853 1.00 4.91 N +ANISOU 768 N GLY A 42 421 742 702 -247 -217 119 N +ATOM 769 CA GLY A 42 17.226 10.779 18.683 1.00 5.06 C +ANISOU 769 CA GLY A 42 535 691 695 -181 -270 265 C +ATOM 770 C GLY A 42 15.746 10.584 18.832 1.00 4.15 C +ANISOU 770 C GLY A 42 578 515 480 -107 -188 204 C +ATOM 771 O GLY A 42 15.331 9.485 19.187 1.00 6.31 O +ANISOU 771 O GLY A 42 720 442 1235 -32 -364 174 O +ATOM 772 H GLY A 42 18.156 12.674 18.276 1.00 5.91 H +ATOM 773 HA2 GLY A 42 17.653 9.863 18.253 1.00 6.06 H +ATOM 774 HA3 GLY A 42 17.660 10.906 19.684 1.00 6.06 H +ATOM 775 N ASP A 43 14.940 11.626 18.615 1.00 3.30 N +ANISOU 775 N ASP A 43 444 478 330 -98 -69 150 N +ATOM 776 CA ASP A 43 13.491 11.518 18.676 1.00 3.12 C +ANISOU 776 CA ASP A 43 454 452 278 -52 3 135 C +ATOM 777 C ASP A 43 12.866 11.265 17.292 1.00 2.37 C +ANISOU 777 C ASP A 43 322 311 264 -36 63 47 C +ATOM 778 O ASP A 43 11.637 11.131 17.212 1.00 2.79 O +ANISOU 778 O ASP A 43 321 408 331 -20 129 0 O +ATOM 779 CB AASP A 43 13.091 12.931 19.136 0.25 3.47 C +ATOM 780 CB BASP A 43 12.802 12.630 19.421 0.75 2.76 C +ANISOU 780 CB BASP A 43 398 376 273 -49 99 1 C +ATOM 781 CG AASP A 43 13.560 14.348 18.472 0.25 3.47 C +ATOM 782 CG BASP A 43 13.085 14.014 18.859 0.75 2.63 C +ANISOU 782 CG BASP A 43 302 318 379 -88 45 4 C +ATOM 783 OD1AASP A 43 14.415 14.363 17.612 0.25 4.15 O +ATOM 784 OD1BASP A 43 14.068 14.164 18.085 0.75 3.64 O +ANISOU 784 OD1BASP A 43 474 336 572 -10 221 3 O +ATOM 785 OD2AASP A 43 12.986 15.459 18.868 0.25 5.01 O +ANISOU 785 OD2AASP A 43 625 613 664 19 323 131 O +ATOM 786 OD2BASP A 43 12.311 14.944 19.211 0.75 3.43 O +ANISOU 786 OD2BASP A 43 402 366 533 -88 109 66 O +ATOM 787 H ASP A 43 15.352 12.521 18.399 1.00 3.95 H +ATOM 788 HA ASP A 43 13.177 10.756 19.403 1.00 3.76 H +ATOM 789 HB2AASP A 43 11.992 12.947 19.118 0.25 3.76 H +ATOM 790 HB2BASP A 43 11.717 12.453 19.397 0.75 3.36 H +ATOM 791 HB3AASP A 43 13.380 12.990 20.194 0.25 3.76 H +ATOM 792 HB3BASP A 43 13.121 12.603 20.473 0.75 3.36 H +ATOM 793 N TYR A 44 13.711 11.175 16.260 1.00 2.18 N +ANISOU 793 N TYR A 44 245 301 280 -51 46 8 N +ATOM 794 CA TYR A 44 13.267 10.722 14.926 1.00 1.98 C +ANISOU 794 CA TYR A 44 197 260 294 -47 49 -21 C +ATOM 795 C TYR A 44 14.251 9.661 14.439 1.00 2.25 C +ANISOU 795 C TYR A 44 187 297 369 -68 91 -27 C +ATOM 796 O TYR A 44 14.931 9.812 13.426 1.00 2.78 O +ANISOU 796 O TYR A 44 291 383 379 -75 149 -36 O +ATOM 797 CB TYR A 44 13.132 11.883 13.924 1.00 2.40 C +ANISOU 797 CB TYR A 44 286 336 288 -1 79 -24 C +ATOM 798 CG TYR A 44 11.978 12.797 14.251 1.00 2.26 C +ANISOU 798 CG TYR A 44 262 274 319 -1 20 -37 C +ATOM 799 CD1 TYR A 44 12.083 13.835 15.179 1.00 2.62 C +ANISOU 799 CD1 TYR A 44 295 304 397 -52 -29 -27 C +ATOM 800 CD2 TYR A 44 10.765 12.585 13.608 1.00 2.35 C +ANISOU 800 CD2 TYR A 44 286 316 289 -48 10 -29 C +ATOM 801 CE1 TYR A 44 10.989 14.643 15.462 1.00 2.71 C +ANISOU 801 CE1 TYR A 44 327 280 420 -67 -25 -18 C +ATOM 802 CE2 TYR A 44 9.649 13.380 13.883 1.00 2.41 C +ANISOU 802 CE2 TYR A 44 275 339 301 -40 -15 -15 C +ATOM 803 CZ TYR A 44 9.770 14.410 14.819 1.00 2.30 C +ANISOU 803 CZ TYR A 44 298 250 325 -2 10 -9 C +ATOM 804 OH TYR A 44 8.716 15.223 15.106 1.00 2.78 O +ANISOU 804 OH TYR A 44 327 312 416 -57 -7 29 O +ATOM 805 H TYR A 44 14.672 11.391 16.410 1.00 2.60 H +ATOM 806 HA TYR A 44 12.279 10.275 15.025 1.00 2.38 H +ATOM 807 HB2 TYR A 44 14.063 12.462 13.920 1.00 2.87 H +ATOM 808 HB3 TYR A 44 12.987 11.459 12.924 1.00 2.87 H +ATOM 809 HD1 TYR A 44 13.039 14.015 15.690 1.00 3.16 H +ATOM 810 HD2 TYR A 44 10.682 11.777 12.868 1.00 2.81 H +ATOM 811 HE1 TYR A 44 11.081 15.462 16.189 1.00 3.27 H +ATOM 812 HE2 TYR A 44 8.693 13.197 13.372 1.00 2.90 H +ATOM 813 HH TYR A 44 7.946 14.945 14.590 1.00 4.17 H +ATOM 814 N ALA A 45 14.353 8.612 15.274 1.00 2.25 N +ANISOU 814 N ALA A 45 182 307 365 -72 40 17 N +ATOM 815 CA ALA A 45 15.411 7.633 15.171 1.00 2.49 C +ANISOU 815 CA ALA A 45 180 369 397 -116 -10 42 C +ATOM 816 C ALA A 45 15.176 6.504 14.196 1.00 2.46 C +ANISOU 816 C ALA A 45 176 378 378 -116 -10 65 C +ATOM 817 O ALA A 45 16.091 5.695 13.991 1.00 3.45 O +ANISOU 817 O ALA A 45 191 479 638 -268 -65 110 O +ATOM 818 CB ALA A 45 15.631 7.055 16.574 1.00 3.41 C +ANISOU 818 CB ALA A 45 363 531 401 -107 -58 175 C +ATOM 819 H ALA A 45 13.657 8.499 15.996 1.00 2.69 H +ATOM 820 HA ALA A 45 16.330 8.156 14.871 1.00 2.99 H +ATOM 821 HB1 ALA A 45 15.811 7.874 17.284 1.00 5.14 H +ATOM 822 HB2 ALA A 45 16.501 6.383 16.561 1.00 5.14 H +ATOM 823 HB3 ALA A 45 14.739 6.493 16.883 1.00 5.14 H +ATOM 824 N ASN A 46 13.968 6.428 13.644 1.00 2.37 N +ANISOU 824 N ASN A 46 160 311 428 -111 -2 51 N +ATOM 825 CA ASN A 46 13.545 5.347 12.780 1.00 2.48 C +ANISOU 825 CA ASN A 46 174 316 450 -105 -41 37 C +ATOM 826 C ASN A 46 13.314 5.798 11.331 1.00 2.63 C +ANISOU 826 C ASN A 46 202 343 454 -112 -48 28 C +ATOM 827 O ASN A 46 13.722 6.914 10.977 1.00 2.76 O +ANISOU 827 O ASN A 46 279 370 398 -115 41 10 O +ATOM 828 CB ASN A 46 12.289 4.685 13.379 1.00 3.21 C +ANISOU 828 CB ASN A 46 220 418 579 21 -49 -5 C +ATOM 829 CG AASN A 46 12.552 4.058 14.708 0.57 3.22 C +ANISOU 829 CG AASN A 46 357 332 534 -12 20 37 C +ATOM 830 CG BASN A 46 12.511 4.381 14.835 0.43 4.18 C +ANISOU 830 CG BASN A 46 263 817 507 -121 -76 13 C +ATOM 831 OD1AASN A 46 11.884 4.464 15.644 0.57 4.43 O +ANISOU 831 OD1AASN A 46 447 749 487 -27 45 91 O +ATOM 832 OD1BASN A 46 11.976 5.015 15.832 0.43 6.89 O +ANISOU 832 OD1BASN A 46 532 1372 713 -377 163 -101 O +ATOM 833 ND2AASN A 46 13.527 3.162 14.799 0.57 4.29 N +ANISOU 833 ND2AASN A 46 569 571 487 56 -7 254 N +ATOM 834 ND2BASN A 46 13.361 3.391 15.159 0.43 6.66 N +ANISOU 834 ND2BASN A 46 512 1486 532 164 31 436 N +ATOM 835 OXT ASN A 46 12.720 4.982 10.590 1.00 3.55 O +ANISOU 835 OXT ASN A 46 401 392 553 -114 -149 -52 O +ATOM 836 H ASN A 46 13.308 7.167 13.839 1.00 2.84 H +ATOM 837 HA ASN A 46 14.347 4.595 12.771 1.00 2.97 H +ATOM 838 HB2 ASN A 46 11.501 5.442 13.488 1.00 3.85 H +ATOM 839 HB3 ASN A 46 11.923 3.915 12.684 1.00 3.85 H +ATOM 840 HD21AASN A 46 13.764 2.762 15.695 0.57 5.14 H +ATOM 841 HD21BASN A 46 13.547 3.183 16.129 0.43 7.99 H +ATOM 842 HD22AASN A 46 14.032 2.880 13.972 0.57 5.14 H +ATOM 843 HD22BASN A 46 13.813 2.856 14.433 0.43 7.99 H +TER 844 ASN A 46 +CONECT 60 749 +CONECT 70 616 +CONECT 310 516 +CONECT 516 310 +CONECT 616 70 +CONECT 749 60 +MASTER 226 0 0 2 2 0 0 6 340 1 6 4 +END \ No newline at end of file diff --git a/tests/testdata/pdb/2pah.pdb b/tests/testdata/pdb/2pah.pdb new file mode 100644 index 0000000..3189e20 --- /dev/null +++ b/tests/testdata/pdb/2pah.pdb @@ -0,0 +1,5803 @@ +HEADER HYDROXYLASE 26-MAY-98 2PAH +TITLE TETRAMERIC HUMAN PHENYLALANINE HYDROXYLASE +COMPND MOL_ID: 1; +COMPND 2 MOLECULE: PROTEIN (PHENYLALANINE HYDROXYLASE); +COMPND 3 CHAIN: A, B; +COMPND 4 FRAGMENT: RESIDUES 118-452; +COMPND 5 SYNONYM: PAH; +COMPND 6 EC: 1.14.16.1; +COMPND 7 ENGINEERED: YES; +COMPND 8 OTHER_DETAILS: ACTIVE SITE IRON ATOM FE +SOURCE MOL_ID: 1; +SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; +SOURCE 3 ORGANISM_COMMON: HUMAN; +SOURCE 4 ORGANISM_TAXID: 9606; +SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; +SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693; +SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; +SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-3A-D +KEYWDS HYDROXYLASE, PHENYLKETONURIA +EXPDTA X-RAY DIFFRACTION +AUTHOR R.C.STEVENS,F.FUSETTI,H.ERLANDSEN +REVDAT 3 13-JUL-11 2PAH 1 VERSN +REVDAT 2 24-FEB-09 2PAH 1 VERSN +REVDAT 1 06-OCT-99 2PAH 0 +JRNL AUTH F.FUSETTI,H.ERLANDSEN,T.FLATMARK,R.C.STEVENS +JRNL TITL STRUCTURE OF TETRAMERIC HUMAN PHENYLALANINE HYDROXYLASE AND +JRNL TITL 2 ITS IMPLICATIONS FOR PHENYLKETONURIA. +JRNL REF J.BIOL.CHEM. V. 273 16962 1998 +JRNL REFN ISSN 0021-9258 +JRNL PMID 9642259 +JRNL DOI 10.1074/JBC.273.27.16962 +REMARK 2 +REMARK 2 RESOLUTION. 3.10 ANGSTROMS. +REMARK 3 +REMARK 3 REFINEMENT. +REMARK 3 PROGRAM : X-PLOR 3.8 +REMARK 3 AUTHORS : BRUNGER +REMARK 3 +REMARK 3 DATA USED IN REFINEMENT. +REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 +REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 +REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 +REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000000.000 +REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010 +REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9 +REMARK 3 NUMBER OF REFLECTIONS : 18446 +REMARK 3 +REMARK 3 FIT TO DATA USED IN REFINEMENT. +REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT +REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM +REMARK 3 R VALUE (WORKING SET) : 0.251 +REMARK 3 FREE R VALUE : 0.326 +REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 +REMARK 3 FREE R VALUE TEST SET COUNT : 1800 +REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL +REMARK 3 +REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. +REMARK 3 TOTAL NUMBER OF BINS USED : 6 +REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.10 +REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.20 +REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.00 +REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL +REMARK 3 BIN R VALUE (WORKING SET) : 0.2510 +REMARK 3 BIN FREE R VALUE : 0.3260 +REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00 +REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL +REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL +REMARK 3 +REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. +REMARK 3 PROTEIN ATOMS : 5315 +REMARK 3 NUCLEIC ACID ATOMS : 0 +REMARK 3 HETEROGEN ATOMS : 2 +REMARK 3 SOLVENT ATOMS : 0 +REMARK 3 +REMARK 3 B VALUES. +REMARK 3 FROM WILSON PLOT (A**2) : 33.00 +REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.00 +REMARK 3 OVERALL ANISOTROPIC B VALUE. +REMARK 3 B11 (A**2) : 0.00000 +REMARK 3 B22 (A**2) : 0.00000 +REMARK 3 B33 (A**2) : 0.00000 +REMARK 3 B12 (A**2) : 0.00000 +REMARK 3 B13 (A**2) : 0.00000 +REMARK 3 B23 (A**2) : 0.00000 +REMARK 3 +REMARK 3 ESTIMATED COORDINATE ERROR. +REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL +REMARK 3 ESD FROM SIGMAA (A) : NULL +REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL +REMARK 3 +REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. +REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL +REMARK 3 ESD FROM C-V SIGMAA (A) : NULL +REMARK 3 +REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. +REMARK 3 BOND LENGTHS (A) : 0.006 +REMARK 3 BOND ANGLES (DEGREES) : 1.70 +REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL +REMARK 3 IMPROPER ANGLES (DEGREES) : NULL +REMARK 3 +REMARK 3 ISOTROPIC THERMAL MODEL : NULL +REMARK 3 +REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA +REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL +REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL +REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL +REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL +REMARK 3 +REMARK 3 NCS MODEL : RESTRAINTS +REMARK 3 +REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT +REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL +REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL +REMARK 3 +REMARK 3 PARAMETER FILE 1 : PARAM19X.PRO +REMARK 3 PARAMETER FILE 2 : PARHCSDX.PRO +REMARK 3 PARAMETER FILE 3 : NULL +REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO +REMARK 3 TOPOLOGY FILE 2 : TOPHCSDX.PRO +REMARK 3 TOPOLOGY FILE 3 : NULL +REMARK 3 +REMARK 3 OTHER REFINEMENT REMARKS: NULL +REMARK 4 +REMARK 4 2PAH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 +REMARK 100 +REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-99. +REMARK 100 THE RCSB ID CODE IS RCSB008000. +REMARK 200 +REMARK 200 EXPERIMENTAL DETAILS +REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION +REMARK 200 DATE OF DATA COLLECTION : JUL-97 +REMARK 200 TEMPERATURE (KELVIN) : 100.0 +REMARK 200 PH : 7.0 +REMARK 200 NUMBER OF CRYSTALS USED : 1 +REMARK 200 +REMARK 200 SYNCHROTRON (Y/N) : Y +REMARK 200 RADIATION SOURCE : SSRL +REMARK 200 BEAMLINE : BL7-1 +REMARK 200 X-RAY GENERATOR MODEL : NULL +REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M +REMARK 200 WAVELENGTH OR RANGE (A) : 1.08 +REMARK 200 MONOCHROMATOR : NULL +REMARK 200 OPTICS : MIRRORS +REMARK 200 +REMARK 200 DETECTOR TYPE : IMAGE PLATE +REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH +REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO +REMARK 200 DATA SCALING SOFTWARE : SCALEPACK +REMARK 200 +REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 120922 +REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 +REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 +REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 +REMARK 200 +REMARK 200 OVERALL. +REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 +REMARK 200 DATA REDUNDANCY : 6.500 +REMARK 200 R MERGE (I) : 0.07500 +REMARK 200 R SYM (I) : 0.07500 +REMARK 200 FOR THE DATA SET : 10.0000 +REMARK 200 +REMARK 200 IN THE HIGHEST RESOLUTION SHELL. +REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10 +REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20 +REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0 +REMARK 200 DATA REDUNDANCY IN SHELL : 2.00 +REMARK 200 R MERGE FOR SHELL (I) : 0.25000 +REMARK 200 R SYM FOR SHELL (I) : 0.25000 +REMARK 200 FOR SHELL : 2.000 +REMARK 200 +REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH +REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT +REMARK 200 SOFTWARE USED: AMORE +REMARK 200 STARTING MODEL: 1TOH +REMARK 200 +REMARK 200 REMARK: NULL +REMARK 280 +REMARK 280 CRYSTAL +REMARK 280 SOLVENT CONTENT, VS (%): 60.00 +REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36 +REMARK 280 +REMARK 280 CRYSTALLIZATION CONDITIONS: 0.6 M MGSO4, 0.2 M NAK TARTRATE, 10% +REMARK 280 PEG-4000, 0.1 M BIS-TRIS PROPANE (PH 7.0) +REMARK 290 +REMARK 290 CRYSTALLOGRAPHIC SYMMETRY +REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 1 2 +REMARK 290 +REMARK 290 SYMOP SYMMETRY +REMARK 290 NNNMMM OPERATOR +REMARK 290 1555 X,Y,Z +REMARK 290 2555 -Y,X-Y,Z+1/3 +REMARK 290 3555 -X+Y,-X,Z+2/3 +REMARK 290 4555 -Y,-X,-Z+2/3 +REMARK 290 5555 -X+Y,Y,-Z+1/3 +REMARK 290 6555 X,X-Y,-Z +REMARK 290 +REMARK 290 WHERE NNN -> OPERATOR NUMBER +REMARK 290 MMM -> TRANSLATION VECTOR +REMARK 290 +REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS +REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM +REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY +REMARK 290 RELATED MOLECULES. +REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 +REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 +REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 +REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 +REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 +REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.00000 +REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 +REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 +REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 84.00000 +REMARK 290 SMTRY1 4 0.500000 -0.866025 0.000000 0.00000 +REMARK 290 SMTRY2 4 -0.866025 -0.500000 0.000000 0.00000 +REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 84.00000 +REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000 +REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 +REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 42.00000 +REMARK 290 SMTRY1 6 0.500000 0.866025 0.000000 0.00000 +REMARK 290 SMTRY2 6 0.866025 -0.500000 0.000000 0.00000 +REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 +REMARK 290 +REMARK 290 REMARK: NULL +REMARK 300 +REMARK 300 BIOMOLECULE: 1 +REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM +REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN +REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON +REMARK 300 BURIED SURFACE AREA. +REMARK 350 +REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN +REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE +REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS +REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND +REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. +REMARK 350 +REMARK 350 BIOMOLECULE: 1 +REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC +REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC +REMARK 350 SOFTWARE USED: PISA,PQS +REMARK 350 TOTAL BURIED SURFACE AREA: 10460 ANGSTROM**2 +REMARK 350 SURFACE AREA OF THE COMPLEX: 55710 ANGSTROM**2 +REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL +REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B +REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 +REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 +REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 +REMARK 350 BIOMT1 2 0.500000 -0.866025 0.000000 0.00000 +REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 0.00000 +REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 84.00000 +REMARK 465 +REMARK 465 MISSING RESIDUES +REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE +REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN +REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) +REMARK 465 +REMARK 465 M RES C SSSEQI +REMARK 465 SER A 137 +REMARK 465 TYR A 138 +REMARK 465 GLY A 139 +REMARK 465 ALA A 140 +REMARK 465 GLU A 141 +REMARK 465 LEU A 142 +REMARK 465 PHE B 131 +REMARK 465 ALA B 132 +REMARK 465 ASN B 133 +REMARK 465 GLN B 134 +REMARK 465 ILE B 135 +REMARK 465 LEU B 136 +REMARK 465 SER B 137 +REMARK 465 TYR B 138 +REMARK 465 GLY B 139 +REMARK 465 ALA B 140 +REMARK 465 GLU B 141 +REMARK 465 LEU B 142 +REMARK 465 ASP B 143 +REMARK 500 +REMARK 500 GEOMETRY AND STEREOCHEMISTRY +REMARK 500 SUBTOPIC: TORSION ANGLES +REMARK 500 +REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: +REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; +REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). +REMARK 500 +REMARK 500 STANDARD TABLE: +REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) +REMARK 500 +REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- +REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 +REMARK 500 +REMARK 500 M RES CSSEQI PSI PHI +REMARK 500 ALA A 132 57.70 -107.19 +REMARK 500 GLN A 134 -54.73 141.10 +REMARK 500 ALA A 144 -47.30 -21.61 +REMARK 500 LEU A 311 103.08 -58.76 +REMARK 500 PHE A 327 17.17 -65.34 +REMARK 500 THR A 328 -77.76 -135.23 +REMARK 500 GLU A 360 43.51 -101.42 +REMARK 500 LEU A 367 96.50 -65.99 +REMARK 500 PRO A 409 28.05 -65.37 +REMARK 500 PHE A 410 -176.35 -173.66 +REMARK 500 ASN A 426 -44.41 -19.37 +REMARK 500 ILE A 451 23.52 -79.87 +REMARK 500 ASP B 129 3.38 -69.64 +REMARK 500 VAL B 153 -70.16 -75.39 +REMARK 500 LEU B 288 30.01 -99.84 +REMARK 500 LEU B 311 103.23 -58.98 +REMARK 500 PHE B 327 15.10 -64.96 +REMARK 500 THR B 328 -78.87 -133.65 +REMARK 500 GLU B 360 43.30 -101.69 +REMARK 500 LEU B 367 97.01 -65.80 +REMARK 500 ILE B 406 108.93 -56.97 +REMARK 500 PRO B 409 18.81 -67.97 +REMARK 500 PHE B 410 -166.44 -174.99 +REMARK 500 ASP B 425 -24.61 -141.80 +REMARK 500 ILE B 451 60.89 -114.63 +REMARK 500 +REMARK 500 REMARK: NULL +REMARK 620 +REMARK 620 METAL COORDINATION +REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; +REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): +REMARK 620 +REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL +REMARK 620 FE A 453 FE +REMARK 620 N RES CSSEQI ATOM +REMARK 620 1 HIS A 285 NE2 +REMARK 620 2 HIS A 290 NE2 90.4 +REMARK 620 3 GLU A 330 OE1 125.9 103.1 +REMARK 620 N 1 2 +REMARK 620 +REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL +REMARK 620 FE B 454 FE +REMARK 620 N RES CSSEQI ATOM +REMARK 620 1 HIS B 285 NE2 +REMARK 620 2 HIS B 290 NE2 79.1 +REMARK 620 3 GLU B 330 OE1 113.2 102.6 +REMARK 620 N 1 2 +REMARK 800 +REMARK 800 SITE +REMARK 800 SITE_IDENTIFIER: FE1 +REMARK 800 EVIDENCE_CODE: AUTHOR +REMARK 800 SITE_DESCRIPTION: NULL +REMARK 800 +REMARK 800 SITE_IDENTIFIER: FE2 +REMARK 800 EVIDENCE_CODE: AUTHOR +REMARK 800 SITE_DESCRIPTION: NULL +REMARK 800 +REMARK 800 SITE_IDENTIFIER: AC1 +REMARK 800 EVIDENCE_CODE: SOFTWARE +REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 453 +REMARK 800 +REMARK 800 SITE_IDENTIFIER: AC2 +REMARK 800 EVIDENCE_CODE: SOFTWARE +REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 454 +DBREF 2PAH A 118 452 UNP P00439 PH4H_HUMAN 118 452 +DBREF 2PAH B 118 452 UNP P00439 PH4H_HUMAN 118 452 +SEQRES 1 A 335 VAL PRO TRP PHE PRO ARG THR ILE GLN GLU LEU ASP ARG +SEQRES 2 A 335 PHE ALA ASN GLN ILE LEU SER TYR GLY ALA GLU LEU ASP +SEQRES 3 A 335 ALA ASP HIS PRO GLY PHE LYS ASP PRO VAL TYR ARG ALA +SEQRES 4 A 335 ARG ARG LYS GLN PHE ALA ASP ILE ALA TYR ASN TYR ARG +SEQRES 5 A 335 HIS GLY GLN PRO ILE PRO ARG VAL GLU TYR MET GLU GLU +SEQRES 6 A 335 GLU LYS LYS THR TRP GLY THR VAL PHE LYS THR LEU LYS +SEQRES 7 A 335 SER LEU TYR LYS THR HIS ALA CYS TYR GLU TYR ASN HIS +SEQRES 8 A 335 ILE PHE PRO LEU LEU GLU LYS TYR CYS GLY PHE HIS GLU +SEQRES 9 A 335 ASP ASN ILE PRO GLN LEU GLU ASP VAL SER GLN PHE LEU +SEQRES 10 A 335 GLN THR CYS THR GLY PHE ARG LEU ARG PRO VAL ALA GLY +SEQRES 11 A 335 LEU LEU SER SER ARG ASP PHE LEU GLY GLY LEU ALA PHE +SEQRES 12 A 335 ARG VAL PHE HIS CYS THR GLN TYR ILE ARG HIS GLY SER +SEQRES 13 A 335 LYS PRO MET TYR THR PRO GLU PRO ASP ILE CYS HIS GLU +SEQRES 14 A 335 LEU LEU GLY HIS VAL PRO LEU PHE SER ASP ARG SER PHE +SEQRES 15 A 335 ALA GLN PHE SER GLN GLU ILE GLY LEU ALA SER LEU GLY +SEQRES 16 A 335 ALA PRO ASP GLU TYR ILE GLU LYS LEU ALA THR ILE TYR +SEQRES 17 A 335 TRP PHE THR VAL GLU PHE GLY LEU CYS LYS GLN GLY ASP +SEQRES 18 A 335 SER ILE LYS ALA TYR GLY ALA GLY LEU LEU SER SER PHE +SEQRES 19 A 335 GLY GLU LEU GLN TYR CYS LEU SER GLU LYS PRO LYS LEU +SEQRES 20 A 335 LEU PRO LEU GLU LEU GLU LYS THR ALA ILE GLN ASN TYR +SEQRES 21 A 335 THR VAL THR GLU PHE GLN PRO LEU TYR TYR VAL ALA GLU +SEQRES 22 A 335 SER PHE ASN ASP ALA LYS GLU LYS VAL ARG ASN PHE ALA +SEQRES 23 A 335 ALA THR ILE PRO ARG PRO PHE SER VAL ARG TYR ASP PRO +SEQRES 24 A 335 TYR THR GLN ARG ILE GLU VAL LEU ASP ASN THR GLN GLN +SEQRES 25 A 335 LEU LYS ILE LEU ALA ASP SER ILE ASN SER GLU ILE GLY +SEQRES 26 A 335 ILE LEU CYS SER ALA LEU GLN LYS ILE LYS +SEQRES 1 B 335 VAL PRO TRP PHE PRO ARG THR ILE GLN GLU LEU ASP ARG +SEQRES 2 B 335 PHE ALA ASN GLN ILE LEU SER TYR GLY ALA GLU LEU ASP +SEQRES 3 B 335 ALA ASP HIS PRO GLY PHE LYS ASP PRO VAL TYR ARG ALA +SEQRES 4 B 335 ARG ARG LYS GLN PHE ALA ASP ILE ALA TYR ASN TYR ARG +SEQRES 5 B 335 HIS GLY GLN PRO ILE PRO ARG VAL GLU TYR MET GLU GLU +SEQRES 6 B 335 GLU LYS LYS THR TRP GLY THR VAL PHE LYS THR LEU LYS +SEQRES 7 B 335 SER LEU TYR LYS THR HIS ALA CYS TYR GLU TYR ASN HIS +SEQRES 8 B 335 ILE PHE PRO LEU LEU GLU LYS TYR CYS GLY PHE HIS GLU +SEQRES 9 B 335 ASP ASN ILE PRO GLN LEU GLU ASP VAL SER GLN PHE LEU +SEQRES 10 B 335 GLN THR CYS THR GLY PHE ARG LEU ARG PRO VAL ALA GLY +SEQRES 11 B 335 LEU LEU SER SER ARG ASP PHE LEU GLY GLY LEU ALA PHE +SEQRES 12 B 335 ARG VAL PHE HIS CYS THR GLN TYR ILE ARG HIS GLY SER +SEQRES 13 B 335 LYS PRO MET TYR THR PRO GLU PRO ASP ILE CYS HIS GLU +SEQRES 14 B 335 LEU LEU GLY HIS VAL PRO LEU PHE SER ASP ARG SER PHE +SEQRES 15 B 335 ALA GLN PHE SER GLN GLU ILE GLY LEU ALA SER LEU GLY +SEQRES 16 B 335 ALA PRO ASP GLU TYR ILE GLU LYS LEU ALA THR ILE TYR +SEQRES 17 B 335 TRP PHE THR VAL GLU PHE GLY LEU CYS LYS GLN GLY ASP +SEQRES 18 B 335 SER ILE LYS ALA TYR GLY ALA GLY LEU LEU SER SER PHE +SEQRES 19 B 335 GLY GLU LEU GLN TYR CYS LEU SER GLU LYS PRO LYS LEU +SEQRES 20 B 335 LEU PRO LEU GLU LEU GLU LYS THR ALA ILE GLN ASN TYR +SEQRES 21 B 335 THR VAL THR GLU PHE GLN PRO LEU TYR TYR VAL ALA GLU +SEQRES 22 B 335 SER PHE ASN ASP ALA LYS GLU LYS VAL ARG ASN PHE ALA +SEQRES 23 B 335 ALA THR ILE PRO ARG PRO PHE SER VAL ARG TYR ASP PRO +SEQRES 24 B 335 TYR THR GLN ARG ILE GLU VAL LEU ASP ASN THR GLN GLN +SEQRES 25 B 335 LEU LYS ILE LEU ALA ASP SER ILE ASN SER GLU ILE GLY +SEQRES 26 B 335 ILE LEU CYS SER ALA LEU GLN LYS ILE LYS +HET FE A 453 1 +HET FE B 454 1 +HETNAM FE FE (III) ION +FORMUL 3 FE 2(FE 3+) +HELIX 1 1 ILE A 125 ASP A 129 5 5 +HELIX 2 2 PRO A 147 LYS A 150 5 4 +HELIX 3 3 TYR A 154 ASN A 167 1 14 +HELIX 4 4 GLU A 181 LYS A 195 1 15 +HELIX 5 5 TYR A 204 TYR A 216 1 13 +HELIX 6 6 LEU A 227 CYS A 237 1 11 +HELIX 7 7 ASP A 253 PHE A 260 1 8 +HELIX 8 8 GLY A 272 LYS A 274 5 3 +HELIX 9 9 HIS A 285 GLY A 289 1 5 +HELIX 10 10 VAL A 291 SER A 295 1 5 +HELIX 11 11 ARG A 297 SER A 310 1 14 +HELIX 12 12 ASP A 315 THR A 328 1 14 +HELIX 13 13 LEU A 347 SER A 349 5 3 +HELIX 14 14 PHE A 351 LEU A 358 1 8 +HELIX 15 15 PHE A 392 ALA A 404 1 13 +HELIX 16 16 ASN A 426 LYS A 450 1 25 +HELIX 17 17 GLN B 126 LEU B 128 5 3 +HELIX 18 18 PRO B 147 LYS B 150 5 4 +HELIX 19 19 TYR B 154 ASN B 167 1 14 +HELIX 20 20 GLU B 181 LYS B 195 1 15 +HELIX 21 21 TYR B 204 TYR B 216 1 13 +HELIX 22 22 LEU B 227 CYS B 237 1 11 +HELIX 23 23 ASP B 253 PHE B 260 1 8 +HELIX 24 24 GLY B 272 LYS B 274 5 3 +HELIX 25 25 HIS B 285 GLY B 289 1 5 +HELIX 26 26 VAL B 291 SER B 295 1 5 +HELIX 27 27 ARG B 297 SER B 310 1 14 +HELIX 28 28 ASP B 315 THR B 328 1 14 +HELIX 29 29 LEU B 347 SER B 349 5 3 +HELIX 30 30 PHE B 351 LEU B 354 1 4 +HELIX 31 31 PHE B 392 THR B 405 1 14 +HELIX 32 32 LEU B 430 GLN B 449 1 20 +SHEET 1 A 2 ARG A 241 PRO A 244 0 +SHEET 2 A 2 VAL A 262 CYS A 265 1 N PHE A 263 O ARG A 241 +SHEET 1 B 2 LEU A 333 GLN A 336 0 +SHEET 2 B 2 SER A 339 ALA A 342 -1 N LYS A 341 O CYS A 334 +SHEET 1 C 2 SER A 411 ASP A 415 0 +SHEET 2 C 2 ARG A 420 LEU A 424 -1 N LEU A 424 O SER A 411 +SHEET 1 D 2 ARG B 241 PRO B 244 0 +SHEET 2 D 2 VAL B 262 CYS B 265 1 N PHE B 263 O ARG B 241 +SHEET 1 E 2 LEU B 333 GLN B 336 0 +SHEET 2 E 2 SER B 339 ALA B 342 -1 N LYS B 341 O CYS B 334 +SHEET 1 F 2 SER B 411 ASP B 415 0 +SHEET 2 F 2 ARG B 420 LEU B 424 -1 N LEU B 424 O SER B 411 +LINK NE2 HIS A 285 FE FE A 453 1555 1555 2.02 +LINK NE2 HIS A 290 FE FE A 453 1555 1555 2.10 +LINK OE1 GLU A 330 FE FE A 453 1555 1555 2.14 +LINK NE2 HIS B 285 FE FE B 454 1555 1555 2.38 +LINK NE2 HIS B 290 FE FE B 454 1555 1555 2.21 +LINK OE1 GLU B 330 FE FE B 454 1555 1555 2.05 +SITE 1 FE1 3 HIS A 285 HIS A 290 GLU A 330 +SITE 1 FE2 3 HIS B 285 HIS B 290 GLU B 330 +SITE 1 AC1 3 HIS A 285 HIS A 290 GLU A 330 +SITE 1 AC2 3 HIS B 285 HIS B 290 GLU B 330 +CRYST1 119.500 119.500 126.000 90.00 90.00 120.00 P 31 1 2 12 +ORIGX1 1.000000 0.000000 0.000000 0.00000 +ORIGX2 0.000000 1.000000 0.000000 0.00000 +ORIGX3 0.000000 0.000000 1.000000 0.00000 +SCALE1 0.008368 0.004831 0.000000 0.00000 +SCALE2 0.000000 0.009663 0.000000 0.00000 +SCALE3 0.000000 0.000000 0.007936 0.00000 +ATOM 1 N VAL A 118 -7.069 21.943 18.770 1.00 56.51 N +ATOM 2 CA VAL A 118 -7.077 21.688 20.244 1.00 59.09 C +ATOM 3 C VAL A 118 -5.756 21.077 20.700 1.00 44.63 C +ATOM 4 O VAL A 118 -5.346 20.029 20.204 1.00 59.84 O +ATOM 5 CB VAL A 118 -8.218 20.724 20.638 1.00 53.90 C +ATOM 6 CG1 VAL A 118 -8.154 20.417 22.126 1.00 24.03 C +ATOM 7 CG2 VAL A 118 -9.555 21.344 20.287 1.00 72.82 C +ATOM 8 N PRO A 119 -5.090 21.711 21.683 1.00 27.43 N +ATOM 9 CA PRO A 119 -3.808 21.216 22.195 1.00 20.13 C +ATOM 10 C PRO A 119 -3.864 19.750 22.588 1.00 30.85 C +ATOM 11 O PRO A 119 -4.908 19.250 22.999 1.00 42.83 O +ATOM 12 CB PRO A 119 -3.520 22.117 23.394 1.00 7.28 C +ATOM 13 CG PRO A 119 -4.316 23.335 23.159 1.00 31.66 C +ATOM 14 CD PRO A 119 -5.536 22.916 22.397 1.00 41.73 C +ATOM 15 N TRP A 120 -2.731 19.068 22.464 1.00 36.51 N +ATOM 16 CA TRP A 120 -2.647 17.659 22.821 1.00 33.96 C +ATOM 17 C TRP A 120 -2.475 17.514 24.327 1.00 42.42 C +ATOM 18 O TRP A 120 -1.735 18.278 24.950 1.00 43.61 O +ATOM 19 CB TRP A 120 -1.460 16.995 22.109 1.00 27.89 C +ATOM 20 CG TRP A 120 -1.200 15.578 22.560 1.00 23.25 C +ATOM 21 CD1 TRP A 120 -1.645 14.433 21.962 1.00 45.51 C +ATOM 22 CD2 TRP A 120 -0.460 15.161 23.718 1.00 22.82 C +ATOM 23 NE1 TRP A 120 -1.234 13.330 22.677 1.00 46.58 N +ATOM 24 CE2 TRP A 120 -0.504 13.751 23.759 1.00 27.53 C +ATOM 25 CE3 TRP A 120 0.229 15.844 24.731 1.00 15.24 C +ATOM 26 CZ2 TRP A 120 0.120 13.009 24.767 1.00 36.09 C +ATOM 27 CZ3 TRP A 120 0.854 15.105 25.731 1.00 30.46 C +ATOM 28 CH2 TRP A 120 0.790 13.703 25.743 1.00 36.66 C +ATOM 29 N PHE A 121 -3.165 16.535 24.906 1.00 36.52 N +ATOM 30 CA PHE A 121 -3.068 16.272 26.337 1.00 34.42 C +ATOM 31 C PHE A 121 -3.023 14.773 26.610 1.00 36.94 C +ATOM 32 O PHE A 121 -3.565 13.973 25.839 1.00 28.54 O +ATOM 33 CB PHE A 121 -4.241 16.911 27.091 1.00 43.63 C +ATOM 34 CG PHE A 121 -5.582 16.364 26.709 1.00 43.79 C +ATOM 35 CD1 PHE A 121 -6.071 15.206 27.305 1.00 49.28 C +ATOM 36 CD2 PHE A 121 -6.365 17.013 25.762 1.00 41.43 C +ATOM 37 CE1 PHE A 121 -7.320 14.702 26.965 1.00 37.53 C +ATOM 38 CE2 PHE A 121 -7.614 16.518 25.416 1.00 43.57 C +ATOM 39 CZ PHE A 121 -8.093 15.357 26.020 1.00 44.15 C +ATOM 40 N PRO A 122 -2.359 14.374 27.711 1.00 30.16 N +ATOM 41 CA PRO A 122 -2.238 12.962 28.089 1.00 28.65 C +ATOM 42 C PRO A 122 -3.555 12.293 28.458 1.00 26.18 C +ATOM 43 O PRO A 122 -4.329 12.824 29.246 1.00 40.25 O +ATOM 44 CB PRO A 122 -1.255 12.984 29.258 1.00 24.50 C +ATOM 45 CG PRO A 122 -1.356 14.355 29.802 1.00 21.80 C +ATOM 46 CD PRO A 122 -1.656 15.256 28.656 1.00 11.45 C +ATOM 47 N ARG A 123 -3.801 11.124 27.872 1.00 42.98 N +ATOM 48 CA ARG A 123 -5.016 10.367 28.145 1.00 51.56 C +ATOM 49 C ARG A 123 -4.721 9.356 29.246 1.00 49.43 C +ATOM 50 O ARG A 123 -5.581 9.053 30.070 1.00 52.64 O +ATOM 51 CB ARG A 123 -5.482 9.631 26.885 1.00 79.49 C +ATOM 52 CG ARG A 123 -5.655 10.524 25.665 1.00 80.86 C +ATOM 53 CD ARG A 123 -6.878 11.411 25.805 1.00 89.46 C +ATOM 54 NE ARG A 123 -7.375 11.859 24.508 1.00100.00 N +ATOM 55 CZ ARG A 123 -8.308 11.226 23.804 1.00100.00 C +ATOM 56 NH1 ARG A 123 -8.850 10.109 24.271 1.00100.00 N +ATOM 57 NH2 ARG A 123 -8.698 11.710 22.632 1.00100.00 N +ATOM 58 N THR A 124 -3.494 8.844 29.247 1.00 38.40 N +ATOM 59 CA THR A 124 -3.057 7.868 30.237 1.00 39.91 C +ATOM 60 C THR A 124 -1.964 8.454 31.112 1.00 31.37 C +ATOM 61 O THR A 124 -1.270 9.395 30.716 1.00 40.84 O +ATOM 62 CB THR A 124 -2.486 6.592 29.589 1.00 49.36 C +ATOM 63 OG1 THR A 124 -3.354 6.151 28.541 1.00 66.48 O +ATOM 64 CG2 THR A 124 -2.354 5.486 30.631 1.00 58.27 C +ATOM 65 N ILE A 125 -1.823 7.877 32.303 1.00 31.21 N +ATOM 66 CA ILE A 125 -0.827 8.303 33.279 1.00 32.65 C +ATOM 67 C ILE A 125 0.589 8.044 32.765 1.00 38.63 C +ATOM 68 O ILE A 125 1.529 8.769 33.109 1.00 41.02 O +ATOM 69 CB ILE A 125 -1.015 7.556 34.616 1.00 22.18 C +ATOM 70 CG1 ILE A 125 -0.129 8.177 35.694 1.00 31.62 C +ATOM 71 CG2 ILE A 125 -0.692 6.085 34.435 1.00 23.10 C +ATOM 72 CD1 ILE A 125 -0.645 7.967 37.107 1.00 42.67 C +ATOM 73 N GLN A 126 0.734 7.010 31.939 1.00 26.14 N +ATOM 74 CA GLN A 126 2.032 6.653 31.380 1.00 31.21 C +ATOM 75 C GLN A 126 2.403 7.554 30.206 1.00 26.00 C +ATOM 76 O GLN A 126 3.541 7.545 29.740 1.00 35.26 O +ATOM 77 CB GLN A 126 2.023 5.193 30.921 1.00 52.92 C +ATOM 78 CG GLN A 126 1.589 4.205 31.987 1.00 74.24 C +ATOM 79 CD GLN A 126 0.175 3.707 31.775 1.00 86.27 C +ATOM 80 OE1 GLN A 126 -0.231 3.420 30.648 1.00100.00 O +ATOM 81 NE2 GLN A 126 -0.583 3.598 32.859 1.00 91.63 N +ATOM 82 N GLU A 127 1.429 8.324 29.733 1.00 24.99 N +ATOM 83 CA GLU A 127 1.639 9.225 28.608 1.00 29.20 C +ATOM 84 C GLU A 127 2.400 10.479 29.004 1.00 26.32 C +ATOM 85 O GLU A 127 2.711 11.316 28.160 1.00 34.58 O +ATOM 86 CB GLU A 127 0.299 9.615 27.995 1.00 29.55 C +ATOM 87 CG GLU A 127 -0.444 8.454 27.368 1.00 48.32 C +ATOM 88 CD GLU A 127 -1.363 8.892 26.246 1.00 52.90 C +ATOM 89 OE1 GLU A 127 -1.628 10.109 26.136 1.00 51.84 O +ATOM 90 OE2 GLU A 127 -1.817 8.021 25.472 1.00 41.20 O +ATOM 91 N LEU A 128 2.692 10.601 30.292 1.00 25.59 N +ATOM 92 CA LEU A 128 3.427 11.750 30.806 1.00 40.76 C +ATOM 93 C LEU A 128 4.913 11.562 30.504 1.00 42.92 C +ATOM 94 O LEU A 128 5.744 12.418 30.813 1.00 43.06 O +ATOM 95 CB LEU A 128 3.215 11.877 32.321 1.00 57.74 C +ATOM 96 CG LEU A 128 1.780 12.086 32.826 1.00 61.98 C +ATOM 97 CD1 LEU A 128 1.774 12.145 34.339 1.00 55.34 C +ATOM 98 CD2 LEU A 128 1.204 13.361 32.244 1.00 61.21 C +ATOM 99 N ASP A 129 5.233 10.421 29.900 1.00 30.80 N +ATOM 100 CA ASP A 129 6.604 10.086 29.546 1.00 26.65 C +ATOM 101 C ASP A 129 7.058 10.948 28.391 1.00 34.53 C +ATOM 102 O ASP A 129 8.226 10.912 27.990 1.00 55.86 O +ATOM 103 CB ASP A 129 6.695 8.623 29.131 1.00 32.05 C +ATOM 104 CG ASP A 129 6.496 7.674 30.285 1.00 37.31 C +ATOM 105 OD1 ASP A 129 6.596 8.115 31.447 1.00 22.36 O +ATOM 106 OD2 ASP A 129 6.245 6.480 30.028 1.00 43.85 O +ATOM 107 N ARG A 130 6.105 11.696 27.844 1.00 26.69 N +ATOM 108 CA ARG A 130 6.359 12.576 26.715 1.00 43.72 C +ATOM 109 C ARG A 130 6.875 13.921 27.205 1.00 42.68 C +ATOM 110 O ARG A 130 7.537 14.647 26.464 1.00 51.14 O +ATOM 111 CB ARG A 130 5.076 12.757 25.892 1.00 48.35 C +ATOM 112 CG ARG A 130 4.785 11.589 24.935 1.00 88.58 C +ATOM 113 CD ARG A 130 3.644 11.888 23.953 1.00100.00 C +ATOM 114 NE ARG A 130 3.410 10.773 23.031 1.00100.00 N +ATOM 115 CZ ARG A 130 2.274 10.557 22.369 1.00 90.45 C +ATOM 116 NH1 ARG A 130 1.246 11.377 22.516 1.00 86.66 N +ATOM 117 NH2 ARG A 130 2.163 9.515 21.555 1.00 74.81 N +ATOM 118 N PHE A 131 6.575 14.243 28.459 1.00 47.82 N +ATOM 119 CA PHE A 131 7.023 15.494 29.059 1.00 49.03 C +ATOM 120 C PHE A 131 8.537 15.450 29.242 1.00 48.51 C +ATOM 121 O PHE A 131 9.243 16.411 28.945 1.00 53.68 O +ATOM 122 CB PHE A 131 6.352 15.700 30.422 1.00 56.74 C +ATOM 123 CG PHE A 131 4.881 15.992 30.342 1.00 54.59 C +ATOM 124 CD1 PHE A 131 4.077 15.849 31.467 1.00 67.99 C +ATOM 125 CD2 PHE A 131 4.299 16.418 29.154 1.00 28.70 C +ATOM 126 CE1 PHE A 131 2.716 16.123 31.409 1.00 47.89 C +ATOM 127 CE2 PHE A 131 2.938 16.694 29.089 1.00 49.87 C +ATOM 128 CZ PHE A 131 2.147 16.547 30.220 1.00 43.98 C +ATOM 129 N ALA A 132 9.030 14.321 29.744 1.00 48.67 N +ATOM 130 CA ALA A 132 10.458 14.127 29.961 1.00 62.55 C +ATOM 131 C ALA A 132 10.961 13.163 28.909 1.00 67.09 C +ATOM 132 O ALA A 132 11.498 12.106 29.222 1.00 80.85 O +ATOM 133 CB ALA A 132 10.705 13.564 31.348 1.00 75.74 C +ATOM 134 N ASN A 133 10.766 13.523 27.648 1.00 70.09 N +ATOM 135 CA ASN A 133 11.192 12.692 26.532 1.00 77.55 C +ATOM 136 C ASN A 133 12.697 12.475 26.577 1.00 84.87 C +ATOM 137 O ASN A 133 13.163 11.351 26.791 1.00 84.52 O +ATOM 138 CB ASN A 133 10.793 13.360 25.215 1.00 77.32 C +ATOM 139 CG ASN A 133 10.979 12.455 24.020 1.00 93.97 C +ATOM 140 OD1 ASN A 133 10.554 11.310 24.017 1.00100.00 O +ATOM 141 ND2 ASN A 133 11.619 12.985 22.988 1.00 99.59 N +ATOM 142 N GLN A 134 13.436 13.567 26.394 1.00 82.31 N +ATOM 143 CA GLN A 134 14.897 13.608 26.369 1.00 87.10 C +ATOM 144 C GLN A 134 15.133 14.618 25.254 1.00 82.51 C +ATOM 145 O GLN A 134 15.796 15.639 25.444 1.00 86.33 O +ATOM 146 CB GLN A 134 15.499 12.251 25.985 1.00 96.70 C +ATOM 147 CG GLN A 134 16.954 12.291 25.518 1.00100.00 C +ATOM 148 CD GLN A 134 17.800 13.261 26.319 1.00100.00 C +ATOM 149 OE1 GLN A 134 17.982 14.408 25.922 1.00100.00 O +ATOM 150 NE2 GLN A 134 18.321 12.806 27.446 1.00100.00 N +ATOM 151 N ILE A 135 14.547 14.339 24.094 1.00 75.59 N +ATOM 152 CA ILE A 135 14.653 15.234 22.957 1.00 68.45 C +ATOM 153 C ILE A 135 13.510 16.208 23.190 1.00 75.79 C +ATOM 154 O ILE A 135 12.703 16.006 24.112 1.00 75.72 O +ATOM 155 CB ILE A 135 14.427 14.500 21.634 1.00 65.37 C +ATOM 156 CG1 ILE A 135 15.303 13.246 21.571 1.00 63.40 C +ATOM 157 CG2 ILE A 135 14.738 15.424 20.468 1.00 58.73 C +ATOM 158 CD1 ILE A 135 15.063 12.393 20.366 1.00 63.25 C +ATOM 159 N LEU A 136 13.450 17.256 22.377 1.00 79.56 N +ATOM 160 CA LEU A 136 12.402 18.270 22.496 1.00 82.00 C +ATOM 161 C LEU A 136 12.634 19.188 23.697 1.00 78.51 C +ATOM 162 O LEU A 136 11.651 19.482 24.393 1.00 77.87 O +ATOM 163 CB LEU A 136 11.024 17.598 22.610 1.00 62.69 C +ATOM 164 CG LEU A 136 10.392 16.880 21.402 1.00 64.59 C +ATOM 165 CD1 LEU A 136 11.402 16.030 20.685 1.00 57.81 C +ATOM 166 CD2 LEU A 136 9.257 16.021 21.897 1.00 49.28 C +ATOM 167 N ASP A 143 21.929 30.291 32.414 1.00 84.31 N +ATOM 168 CA ASP A 143 21.764 31.776 32.435 1.00 99.88 C +ATOM 169 C ASP A 143 22.677 32.437 33.459 1.00 98.47 C +ATOM 170 O ASP A 143 22.379 32.454 34.651 1.00 96.96 O +ATOM 171 CB ASP A 143 20.312 32.148 32.738 1.00100.00 C +ATOM 172 CG ASP A 143 19.880 33.427 32.037 1.00100.00 C +ATOM 173 OD1 ASP A 143 20.746 34.102 31.435 1.00100.00 O +ATOM 174 OD2 ASP A 143 18.675 33.756 32.084 1.00100.00 O +ATOM 175 N ALA A 144 23.779 32.993 32.963 1.00 92.92 N +ATOM 176 CA ALA A 144 24.795 33.667 33.771 1.00 94.63 C +ATOM 177 C ALA A 144 24.384 34.188 35.153 1.00 98.79 C +ATOM 178 O ALA A 144 25.097 33.966 36.132 1.00100.00 O +ATOM 179 CB ALA A 144 25.413 34.800 32.958 1.00 94.11 C +ATOM 180 N ASP A 145 23.253 34.884 35.238 1.00 92.37 N +ATOM 181 CA ASP A 145 22.790 35.439 36.517 1.00 86.15 C +ATOM 182 C ASP A 145 22.543 34.345 37.554 1.00 77.55 C +ATOM 183 O ASP A 145 22.449 34.617 38.752 1.00 75.84 O +ATOM 184 CB ASP A 145 21.504 36.243 36.309 1.00 94.52 C +ATOM 185 CG ASP A 145 20.351 35.380 35.837 1.00100.00 C +ATOM 186 OD1 ASP A 145 20.462 34.782 34.746 1.00100.00 O +ATOM 187 OD2 ASP A 145 19.333 35.297 36.556 1.00100.00 O +ATOM 188 N HIS A 146 22.446 33.106 37.084 1.00 70.06 N +ATOM 189 CA HIS A 146 22.203 31.960 37.951 1.00 70.17 C +ATOM 190 C HIS A 146 23.421 31.637 38.805 1.00 66.10 C +ATOM 191 O HIS A 146 24.515 31.413 38.289 1.00 69.28 O +ATOM 192 CB HIS A 146 21.826 30.738 37.107 1.00 88.83 C +ATOM 193 CG HIS A 146 21.565 29.500 37.908 1.00 92.84 C +ATOM 194 ND1 HIS A 146 22.552 28.842 38.610 1.00 78.79 N +ATOM 195 CD2 HIS A 146 20.429 28.786 38.101 1.00 92.70 C +ATOM 196 CE1 HIS A 146 22.037 27.778 39.200 1.00 79.37 C +ATOM 197 NE2 HIS A 146 20.750 27.722 38.907 1.00 85.27 N +ATOM 198 N PRO A 147 23.241 31.612 40.135 1.00 72.24 N +ATOM 199 CA PRO A 147 24.356 31.309 41.039 1.00 76.33 C +ATOM 200 C PRO A 147 24.838 29.877 40.830 1.00 83.68 C +ATOM 201 O PRO A 147 24.071 28.925 40.966 1.00100.00 O +ATOM 202 CB PRO A 147 23.767 31.536 42.433 1.00 80.01 C +ATOM 203 CG PRO A 147 22.295 31.400 42.251 1.00 83.34 C +ATOM 204 CD PRO A 147 21.984 31.855 40.860 1.00 79.41 C +ATOM 205 N GLY A 148 26.113 29.732 40.487 1.00 76.43 N +ATOM 206 CA GLY A 148 26.666 28.412 40.249 1.00 74.50 C +ATOM 207 C GLY A 148 26.874 28.156 38.769 1.00 68.35 C +ATOM 208 O GLY A 148 27.273 27.063 38.367 1.00 69.42 O +ATOM 209 N PHE A 149 26.591 29.171 37.957 1.00 66.68 N +ATOM 210 CA PHE A 149 26.751 29.075 36.511 1.00 79.10 C +ATOM 211 C PHE A 149 28.222 28.884 36.159 1.00 85.64 C +ATOM 212 O PHE A 149 28.557 28.230 35.173 1.00 87.84 O +ATOM 213 CB PHE A 149 26.213 30.350 35.845 1.00 86.78 C +ATOM 214 CG PHE A 149 26.459 30.425 34.359 1.00 93.25 C +ATOM 215 CD1 PHE A 149 25.712 29.654 33.473 1.00 94.59 C +ATOM 216 CD2 PHE A 149 27.421 31.288 33.844 1.00 96.74 C +ATOM 217 CE1 PHE A 149 25.916 29.745 32.095 1.00 84.73 C +ATOM 218 CE2 PHE A 149 27.631 31.385 32.467 1.00 92.82 C +ATOM 219 CZ PHE A 149 26.878 30.611 31.594 1.00 85.29 C +ATOM 220 N LYS A 150 29.096 29.452 36.983 1.00 87.59 N +ATOM 221 CA LYS A 150 30.534 29.364 36.764 1.00 76.77 C +ATOM 222 C LYS A 150 31.131 28.107 37.392 1.00 78.87 C +ATOM 223 O LYS A 150 32.307 27.808 37.195 1.00 83.74 O +ATOM 224 CB LYS A 150 31.209 30.611 37.336 1.00 86.37 C +ATOM 225 CG LYS A 150 30.447 31.895 37.020 1.00 90.40 C +ATOM 226 CD LYS A 150 31.179 33.139 37.496 1.00100.00 C +ATOM 227 CE LYS A 150 30.593 34.392 36.852 1.00100.00 C +ATOM 228 NZ LYS A 150 31.333 35.632 37.228 1.00100.00 N +ATOM 229 N ASP A 151 30.315 27.366 38.138 1.00 82.59 N +ATOM 230 CA ASP A 151 30.782 26.148 38.788 1.00 81.68 C +ATOM 231 C ASP A 151 30.669 24.932 37.877 1.00 75.99 C +ATOM 232 O ASP A 151 29.576 24.423 37.638 1.00 80.97 O +ATOM 233 CB ASP A 151 30.000 25.888 40.076 1.00 81.66 C +ATOM 234 CG ASP A 151 30.622 24.794 40.917 1.00 87.43 C +ATOM 235 OD1 ASP A 151 31.089 23.787 40.339 1.00 84.99 O +ATOM 236 OD2 ASP A 151 30.645 24.935 42.156 1.00100.00 O +ATOM 237 N PRO A 152 31.812 24.440 37.374 1.00 70.56 N +ATOM 238 CA PRO A 152 31.856 23.277 36.482 1.00 76.86 C +ATOM 239 C PRO A 152 31.335 21.987 37.109 1.00 79.85 C +ATOM 240 O PRO A 152 30.806 21.123 36.409 1.00 82.69 O +ATOM 241 CB PRO A 152 33.332 23.164 36.094 1.00 87.13 C +ATOM 242 CG PRO A 152 33.958 24.456 36.513 1.00 88.74 C +ATOM 243 CD PRO A 152 33.154 24.964 37.659 1.00 82.23 C +ATOM 244 N VAL A 153 31.490 21.852 38.424 1.00 81.47 N +ATOM 245 CA VAL A 153 31.024 20.654 39.117 1.00 88.21 C +ATOM 246 C VAL A 153 29.507 20.706 39.261 1.00 90.32 C +ATOM 247 O VAL A 153 28.788 19.938 38.623 1.00 87.73 O +ATOM 248 CB VAL A 153 31.665 20.520 40.525 1.00 82.85 C +ATOM 249 CG1 VAL A 153 30.909 19.483 41.355 1.00 91.99 C +ATOM 250 CG2 VAL A 153 33.122 20.114 40.395 1.00 86.49 C +ATOM 251 N TYR A 154 29.033 21.618 40.104 1.00 95.50 N +ATOM 252 CA TYR A 154 27.605 21.797 40.348 1.00 92.74 C +ATOM 253 C TYR A 154 26.863 21.772 39.021 1.00 80.78 C +ATOM 254 O TYR A 154 25.765 21.228 38.913 1.00 79.24 O +ATOM 255 CB TYR A 154 27.373 23.131 41.067 1.00100.00 C +ATOM 256 CG TYR A 154 25.934 23.595 41.119 1.00100.00 C +ATOM 257 CD1 TYR A 154 24.968 22.869 41.816 1.00 98.95 C +ATOM 258 CD2 TYR A 154 25.544 24.779 40.492 1.00 92.20 C +ATOM 259 CE1 TYR A 154 23.648 23.312 41.889 1.00 94.85 C +ATOM 260 CE2 TYR A 154 24.227 25.229 40.558 1.00 95.72 C +ATOM 261 CZ TYR A 154 23.287 24.494 41.259 1.00 95.18 C +ATOM 262 OH TYR A 154 21.993 24.949 41.335 1.00100.00 O +ATOM 263 N ARG A 155 27.481 22.370 38.013 1.00 62.91 N +ATOM 264 CA ARG A 155 26.907 22.414 36.679 1.00 59.41 C +ATOM 265 C ARG A 155 26.650 20.991 36.184 1.00 55.79 C +ATOM 266 O ARG A 155 25.505 20.599 35.949 1.00 65.02 O +ATOM 267 CB ARG A 155 27.872 23.121 35.732 1.00 59.75 C +ATOM 268 CG ARG A 155 27.245 23.666 34.473 1.00 68.07 C +ATOM 269 CD ARG A 155 28.304 24.336 33.625 1.00 79.80 C +ATOM 270 NE ARG A 155 27.785 24.801 32.344 1.00 93.15 N +ATOM 271 CZ ARG A 155 27.704 26.081 31.996 1.00 98.65 C +ATOM 272 NH1 ARG A 155 28.107 27.023 32.836 1.00 99.79 N +ATOM 273 NH2 ARG A 155 27.230 26.421 30.804 1.00100.00 N +ATOM 274 N ALA A 156 27.727 20.226 36.024 1.00 47.55 N +ATOM 275 CA ALA A 156 27.642 18.848 35.552 1.00 43.67 C +ATOM 276 C ALA A 156 26.852 17.981 36.524 1.00 48.10 C +ATOM 277 O ALA A 156 26.384 16.897 36.172 1.00 40.44 O +ATOM 278 CB ALA A 156 29.038 18.280 35.364 1.00 58.64 C +ATOM 279 N ARG A 157 26.725 18.451 37.759 1.00 52.11 N +ATOM 280 CA ARG A 157 25.975 17.717 38.764 1.00 51.03 C +ATOM 281 C ARG A 157 24.493 17.868 38.439 1.00 53.36 C +ATOM 282 O ARG A 157 23.746 16.890 38.447 1.00 43.40 O +ATOM 283 CB ARG A 157 26.265 18.278 40.160 1.00 38.02 C +ATOM 284 CG ARG A 157 25.354 17.749 41.247 1.00 41.41 C +ATOM 285 CD ARG A 157 25.845 16.412 41.749 1.00 44.18 C +ATOM 286 NE ARG A 157 25.289 16.082 43.058 1.00 39.11 N +ATOM 287 CZ ARG A 157 25.229 14.849 43.553 1.00 47.49 C +ATOM 288 NH1 ARG A 157 25.692 13.824 42.847 1.00 44.14 N +ATOM 289 NH2 ARG A 157 24.706 14.639 44.753 1.00 31.56 N +ATOM 290 N ARG A 158 24.084 19.101 38.139 1.00 46.66 N +ATOM 291 CA ARG A 158 22.692 19.401 37.816 1.00 53.07 C +ATOM 292 C ARG A 158 22.279 18.807 36.477 1.00 50.94 C +ATOM 293 O ARG A 158 21.092 18.699 36.178 1.00 77.16 O +ATOM 294 CB ARG A 158 22.465 20.915 37.807 1.00 58.71 C +ATOM 295 CG ARG A 158 20.996 21.313 37.798 1.00 73.28 C +ATOM 296 CD ARG A 158 20.800 22.746 38.262 1.00 52.26 C +ATOM 297 NE ARG A 158 19.541 23.305 37.772 1.00 66.00 N +ATOM 298 CZ ARG A 158 18.999 24.434 38.216 1.00 73.11 C +ATOM 299 NH1 ARG A 158 19.600 25.134 39.167 1.00 77.08 N +ATOM 300 NH2 ARG A 158 17.848 24.863 37.715 1.00 79.76 N +ATOM 301 N LYS A 159 23.267 18.443 35.668 1.00 46.70 N +ATOM 302 CA LYS A 159 23.013 17.837 34.366 1.00 49.83 C +ATOM 303 C LYS A 159 22.877 16.342 34.612 1.00 46.38 C +ATOM 304 O LYS A 159 22.287 15.609 33.822 1.00 52.99 O +ATOM 305 CB LYS A 159 24.184 18.105 33.422 1.00 70.21 C +ATOM 306 CG LYS A 159 24.115 17.340 32.116 1.00 82.30 C +ATOM 307 CD LYS A 159 25.243 17.756 31.189 1.00 91.14 C +ATOM 308 CE LYS A 159 25.069 17.172 29.795 1.00 92.35 C +ATOM 309 NZ LYS A 159 26.072 17.722 28.838 1.00100.00 N +ATOM 310 N GLN A 160 23.442 15.910 35.732 1.00 40.78 N +ATOM 311 CA GLN A 160 23.414 14.521 36.160 1.00 42.90 C +ATOM 312 C GLN A 160 21.995 14.224 36.609 1.00 45.11 C +ATOM 313 O GLN A 160 21.417 13.187 36.281 1.00 54.18 O +ATOM 314 CB GLN A 160 24.373 14.348 37.333 1.00 52.45 C +ATOM 315 CG GLN A 160 24.724 12.933 37.672 1.00 46.55 C +ATOM 316 CD GLN A 160 25.879 12.875 38.639 1.00 56.61 C +ATOM 317 OE1 GLN A 160 26.249 13.885 39.237 1.00 57.95 O +ATOM 318 NE2 GLN A 160 26.463 11.696 38.795 1.00 56.32 N +ATOM 319 N PHE A 161 21.444 15.156 37.376 1.00 45.78 N +ATOM 320 CA PHE A 161 20.092 15.029 37.885 1.00 51.09 C +ATOM 321 C PHE A 161 19.106 15.022 36.715 1.00 55.48 C +ATOM 322 O PHE A 161 18.252 14.139 36.621 1.00 55.24 O +ATOM 323 CB PHE A 161 19.778 16.192 38.832 1.00 49.99 C +ATOM 324 CG PHE A 161 20.428 16.073 40.185 1.00 43.25 C +ATOM 325 CD1 PHE A 161 21.244 17.090 40.666 1.00 52.12 C +ATOM 326 CD2 PHE A 161 20.215 14.952 40.983 1.00 46.64 C +ATOM 327 CE1 PHE A 161 21.841 16.997 41.919 1.00 64.08 C +ATOM 328 CE2 PHE A 161 20.808 14.845 42.242 1.00 59.01 C +ATOM 329 CZ PHE A 161 21.622 15.872 42.710 1.00 72.77 C +ATOM 330 N ALA A 162 19.236 16.003 35.824 1.00 53.32 N +ATOM 331 CA ALA A 162 18.357 16.113 34.661 1.00 50.06 C +ATOM 332 C ALA A 162 18.314 14.825 33.846 1.00 43.46 C +ATOM 333 O ALA A 162 17.244 14.374 33.438 1.00 46.93 O +ATOM 334 CB ALA A 162 18.806 17.269 33.777 1.00 22.20 C +ATOM 335 N ASP A 163 19.482 14.239 33.607 1.00 37.62 N +ATOM 336 CA ASP A 163 19.575 13.006 32.837 1.00 55.82 C +ATOM 337 C ASP A 163 18.737 11.924 33.499 1.00 55.29 C +ATOM 338 O ASP A 163 18.116 11.104 32.820 1.00 55.64 O +ATOM 339 CB ASP A 163 21.033 12.546 32.742 1.00 73.47 C +ATOM 340 CG ASP A 163 21.755 13.130 31.541 1.00 88.52 C +ATOM 341 OD1 ASP A 163 21.558 12.618 30.418 1.00 86.66 O +ATOM 342 OD2 ASP A 163 22.525 14.098 31.724 1.00100.00 O +ATOM 343 N ILE A 164 18.730 11.918 34.829 1.00 54.93 N +ATOM 344 CA ILE A 164 17.948 10.931 35.569 1.00 54.88 C +ATOM 345 C ILE A 164 16.504 11.062 35.104 1.00 49.54 C +ATOM 346 O ILE A 164 15.835 10.066 34.823 1.00 36.54 O +ATOM 347 CB ILE A 164 17.994 11.183 37.099 1.00 59.60 C +ATOM 348 CG1 ILE A 164 19.398 10.914 37.648 1.00 68.70 C +ATOM 349 CG2 ILE A 164 17.004 10.274 37.801 1.00 56.46 C +ATOM 350 CD1 ILE A 164 19.594 11.372 39.084 1.00 53.83 C +ATOM 351 N ALA A 165 16.046 12.310 35.022 1.00 43.80 N +ATOM 352 CA ALA A 165 14.686 12.633 34.598 1.00 42.24 C +ATOM 353 C ALA A 165 14.406 12.121 33.193 1.00 44.69 C +ATOM 354 O ALA A 165 13.435 11.402 32.965 1.00 61.71 O +ATOM 355 CB ALA A 165 14.467 14.148 34.654 1.00 26.07 C +ATOM 356 N TYR A 166 15.265 12.493 32.253 1.00 43.01 N +ATOM 357 CA TYR A 166 15.113 12.080 30.866 1.00 31.65 C +ATOM 358 C TYR A 166 15.043 10.564 30.707 1.00 45.23 C +ATOM 359 O TYR A 166 14.423 10.061 29.770 1.00 46.70 O +ATOM 360 CB TYR A 166 16.273 12.626 30.037 1.00 40.40 C +ATOM 361 CG TYR A 166 16.327 14.131 29.984 1.00 45.05 C +ATOM 362 CD1 TYR A 166 17.503 14.817 30.274 1.00 46.24 C +ATOM 363 CD2 TYR A 166 15.205 14.871 29.628 1.00 48.86 C +ATOM 364 CE1 TYR A 166 17.561 16.205 30.205 1.00 53.79 C +ATOM 365 CE2 TYR A 166 15.250 16.257 29.556 1.00 47.99 C +ATOM 366 CZ TYR A 166 16.430 16.919 29.845 1.00 51.43 C +ATOM 367 OH TYR A 166 16.480 18.293 29.753 1.00 60.63 O +ATOM 368 N ASN A 167 15.679 9.840 31.623 1.00 54.06 N +ATOM 369 CA ASN A 167 15.696 8.382 31.566 1.00 65.84 C +ATOM 370 C ASN A 167 14.576 7.741 32.365 1.00 62.84 C +ATOM 371 O ASN A 167 14.321 6.543 32.241 1.00 73.35 O +ATOM 372 CB ASN A 167 17.032 7.854 32.081 1.00 72.59 C +ATOM 373 CG ASN A 167 18.197 8.315 31.244 1.00 72.14 C +ATOM 374 OD1 ASN A 167 18.230 8.095 30.033 1.00 80.82 O +ATOM 375 ND2 ASN A 167 19.165 8.963 31.882 1.00 83.09 N +ATOM 376 N TYR A 168 13.906 8.536 33.187 1.00 49.39 N +ATOM 377 CA TYR A 168 12.830 8.010 34.011 1.00 39.76 C +ATOM 378 C TYR A 168 11.525 7.769 33.266 1.00 42.30 C +ATOM 379 O TYR A 168 10.976 8.668 32.626 1.00 58.64 O +ATOM 380 CB TYR A 168 12.553 8.939 35.194 1.00 46.65 C +ATOM 381 CG TYR A 168 11.500 8.389 36.120 1.00 39.97 C +ATOM 382 CD1 TYR A 168 11.800 7.353 36.998 1.00 66.54 C +ATOM 383 CD2 TYR A 168 10.191 8.858 36.074 1.00 54.93 C +ATOM 384 CE1 TYR A 168 10.828 6.796 37.808 1.00 67.76 C +ATOM 385 CE2 TYR A 168 9.207 8.309 36.881 1.00 61.72 C +ATOM 386 CZ TYR A 168 9.533 7.274 37.741 1.00 65.89 C +ATOM 387 OH TYR A 168 8.566 6.712 38.537 1.00 88.35 O +ATOM 388 N ARG A 169 11.034 6.540 33.358 1.00 32.96 N +ATOM 389 CA ARG A 169 9.777 6.170 32.732 1.00 40.34 C +ATOM 390 C ARG A 169 8.838 5.723 33.849 1.00 47.72 C +ATOM 391 O ARG A 169 9.260 5.068 34.803 1.00 59.03 O +ATOM 392 CB ARG A 169 9.992 5.039 31.729 1.00 41.42 C +ATOM 393 CG ARG A 169 10.123 5.510 30.292 1.00 58.13 C +ATOM 394 CD ARG A 169 11.442 6.225 30.063 1.00 63.85 C +ATOM 395 NE ARG A 169 11.604 6.646 28.674 1.00 72.67 N +ATOM 396 CZ ARG A 169 11.664 7.914 28.280 1.00 77.19 C +ATOM 397 NH1 ARG A 169 11.575 8.888 29.173 1.00 77.86 N +ATOM 398 NH2 ARG A 169 11.808 8.210 26.995 1.00 77.36 N +ATOM 399 N HIS A 170 7.569 6.092 33.731 1.00 42.46 N +ATOM 400 CA HIS A 170 6.571 5.746 34.733 1.00 40.05 C +ATOM 401 C HIS A 170 6.577 4.261 35.060 1.00 45.75 C +ATOM 402 O HIS A 170 6.906 3.426 34.217 1.00 46.56 O +ATOM 403 CB HIS A 170 5.178 6.164 34.245 1.00 51.11 C +ATOM 404 CG HIS A 170 4.058 5.693 35.120 1.00 53.11 C +ATOM 405 ND1 HIS A 170 3.605 6.414 36.205 1.00 37.55 N +ATOM 406 CD2 HIS A 170 3.295 4.576 35.067 1.00 48.78 C +ATOM 407 CE1 HIS A 170 2.612 5.760 36.780 1.00 46.68 C +ATOM 408 NE2 HIS A 170 2.404 4.642 36.110 1.00 39.31 N +ATOM 409 N GLY A 171 6.217 3.944 36.300 1.00 41.41 N +ATOM 410 CA GLY A 171 6.166 2.558 36.725 1.00 62.11 C +ATOM 411 C GLY A 171 7.376 2.091 37.504 1.00 65.87 C +ATOM 412 O GLY A 171 7.246 1.311 38.448 1.00 78.15 O +ATOM 413 N GLN A 172 8.555 2.558 37.107 1.00 71.98 N +ATOM 414 CA GLN A 172 9.789 2.172 37.777 1.00 75.85 C +ATOM 415 C GLN A 172 10.080 3.109 38.937 1.00 69.09 C +ATOM 416 O GLN A 172 9.745 4.292 38.887 1.00 64.34 O +ATOM 417 CB GLN A 172 10.956 2.201 36.793 1.00 77.26 C +ATOM 418 CG GLN A 172 11.248 3.578 36.238 1.00 59.13 C +ATOM 419 CD GLN A 172 11.848 3.517 34.856 1.00 53.97 C +ATOM 420 OE1 GLN A 172 12.781 4.251 34.538 1.00 56.19 O +ATOM 421 NE2 GLN A 172 11.312 2.637 34.019 1.00 58.99 N +ATOM 422 N PRO A 173 10.721 2.591 39.996 1.00 60.10 N +ATOM 423 CA PRO A 173 11.038 3.425 41.161 1.00 51.40 C +ATOM 424 C PRO A 173 12.004 4.565 40.838 1.00 46.66 C +ATOM 425 O PRO A 173 12.923 4.410 40.032 1.00 48.13 O +ATOM 426 CB PRO A 173 11.611 2.430 42.172 1.00 56.78 C +ATOM 427 CG PRO A 173 12.072 1.269 41.354 1.00 66.08 C +ATOM 428 CD PRO A 173 11.186 1.201 40.155 1.00 57.41 C +ATOM 429 N ILE A 174 11.780 5.717 41.463 1.00 46.86 N +ATOM 430 CA ILE A 174 12.637 6.870 41.246 1.00 58.88 C +ATOM 431 C ILE A 174 14.035 6.548 41.758 1.00 66.24 C +ATOM 432 O ILE A 174 14.212 6.191 42.920 1.00 67.03 O +ATOM 433 CB ILE A 174 12.102 8.109 41.994 1.00 53.24 C +ATOM 434 CG1 ILE A 174 10.598 8.242 41.775 1.00 38.78 C +ATOM 435 CG2 ILE A 174 12.822 9.361 41.515 1.00 41.47 C +ATOM 436 CD1 ILE A 174 9.949 9.287 42.655 1.00 52.33 C +ATOM 437 N PRO A 175 15.048 6.650 40.883 1.00 69.49 N +ATOM 438 CA PRO A 175 16.428 6.357 41.294 1.00 70.55 C +ATOM 439 C PRO A 175 16.886 7.184 42.493 1.00 70.56 C +ATOM 440 O PRO A 175 16.562 8.367 42.602 1.00 61.00 O +ATOM 441 CB PRO A 175 17.258 6.655 40.039 1.00 61.75 C +ATOM 442 CG PRO A 175 16.354 7.459 39.151 1.00 44.44 C +ATOM 443 CD PRO A 175 14.962 7.035 39.465 1.00 50.89 C +ATOM 444 N ARG A 176 17.643 6.555 43.390 1.00 68.23 N +ATOM 445 CA ARG A 176 18.141 7.246 44.572 1.00 66.01 C +ATOM 446 C ARG A 176 19.476 7.902 44.255 1.00 55.42 C +ATOM 447 O ARG A 176 20.184 7.475 43.344 1.00 55.67 O +ATOM 448 CB ARG A 176 18.301 6.267 45.741 1.00 71.12 C +ATOM 449 CG ARG A 176 17.013 5.555 46.130 1.00 70.25 C +ATOM 450 CD ARG A 176 17.253 4.516 47.208 1.00 58.50 C +ATOM 451 NE ARG A 176 16.128 4.439 48.130 1.00 69.14 N +ATOM 452 CZ ARG A 176 16.062 5.092 49.284 1.00 65.87 C +ATOM 453 NH1 ARG A 176 17.060 5.878 49.664 1.00 64.13 N +ATOM 454 NH2 ARG A 176 14.995 4.961 50.057 1.00 57.70 N +ATOM 455 N VAL A 177 19.811 8.943 45.009 1.00 40.96 N +ATOM 456 CA VAL A 177 21.058 9.663 44.794 1.00 58.52 C +ATOM 457 C VAL A 177 21.813 9.916 46.099 1.00 60.43 C +ATOM 458 O VAL A 177 21.211 10.135 47.151 1.00 62.67 O +ATOM 459 CB VAL A 177 20.798 11.020 44.091 1.00 61.33 C +ATOM 460 CG1 VAL A 177 22.079 11.829 44.017 1.00 83.94 C +ATOM 461 CG2 VAL A 177 20.247 10.788 42.698 1.00 53.69 C +ATOM 462 N GLU A 178 23.139 9.880 46.013 1.00 45.91 N +ATOM 463 CA GLU A 178 24.004 10.112 47.158 1.00 49.76 C +ATOM 464 C GLU A 178 24.393 11.590 47.191 1.00 52.05 C +ATOM 465 O GLU A 178 25.411 11.986 46.626 1.00 55.89 O +ATOM 466 CB GLU A 178 25.258 9.241 47.040 1.00 52.19 C +ATOM 467 CG GLU A 178 25.816 8.754 48.368 1.00 71.52 C +ATOM 468 CD GLU A 178 26.864 7.659 48.199 1.00 84.05 C +ATOM 469 OE1 GLU A 178 28.008 7.976 47.796 1.00 85.57 O +ATOM 470 OE2 GLU A 178 26.544 6.479 48.467 1.00 80.92 O +ATOM 471 N TYR A 179 23.577 12.404 47.851 1.00 48.56 N +ATOM 472 CA TYR A 179 23.836 13.839 47.939 1.00 63.62 C +ATOM 473 C TYR A 179 25.145 14.150 48.653 1.00 66.92 C +ATOM 474 O TYR A 179 25.563 13.410 49.539 1.00 79.31 O +ATOM 475 CB TYR A 179 22.672 14.535 48.644 1.00 66.47 C +ATOM 476 CG TYR A 179 21.398 14.493 47.840 1.00 64.67 C +ATOM 477 CD1 TYR A 179 20.953 15.614 47.143 1.00 62.18 C +ATOM 478 CD2 TYR A 179 20.647 13.322 47.753 1.00 72.84 C +ATOM 479 CE1 TYR A 179 19.793 15.572 46.380 1.00 79.47 C +ATOM 480 CE2 TYR A 179 19.483 13.268 46.992 1.00 77.72 C +ATOM 481 CZ TYR A 179 19.061 14.399 46.308 1.00 80.12 C +ATOM 482 OH TYR A 179 17.903 14.365 45.564 1.00 71.22 O +ATOM 483 N MET A 180 25.784 15.250 48.262 1.00 61.45 N +ATOM 484 CA MET A 180 27.057 15.657 48.853 1.00 62.82 C +ATOM 485 C MET A 180 26.878 16.617 50.020 1.00 65.47 C +ATOM 486 O MET A 180 25.852 17.287 50.132 1.00 73.13 O +ATOM 487 CB MET A 180 27.947 16.303 47.788 1.00 67.13 C +ATOM 488 CG MET A 180 28.112 15.466 46.528 1.00 66.76 C +ATOM 489 SD MET A 180 29.117 16.259 45.245 1.00 65.33 S +ATOM 490 CE MET A 180 28.525 17.956 45.302 1.00 31.44 C +ATOM 491 N GLU A 181 27.892 16.681 50.880 1.00 60.02 N +ATOM 492 CA GLU A 181 27.857 17.547 52.055 1.00 60.60 C +ATOM 493 C GLU A 181 27.665 19.017 51.718 1.00 62.39 C +ATOM 494 O GLU A 181 26.931 19.726 52.406 1.00 55.85 O +ATOM 495 CB GLU A 181 29.136 17.387 52.872 1.00 64.53 C +ATOM 496 CG GLU A 181 28.990 16.445 54.046 1.00 73.52 C +ATOM 497 CD GLU A 181 28.839 15.008 53.599 1.00 79.03 C +ATOM 498 OE1 GLU A 181 29.212 14.713 52.441 1.00 79.95 O +ATOM 499 OE2 GLU A 181 28.354 14.178 54.400 1.00 75.62 O +ATOM 500 N GLU A 182 28.342 19.482 50.675 1.00 65.10 N +ATOM 501 CA GLU A 182 28.213 20.875 50.275 1.00 69.61 C +ATOM 502 C GLU A 182 26.736 21.128 49.989 1.00 76.90 C +ATOM 503 O GLU A 182 26.253 22.259 50.073 1.00 82.04 O +ATOM 504 CB GLU A 182 29.051 21.149 49.026 1.00 74.60 C +ATOM 505 CG GLU A 182 30.553 21.011 49.239 1.00 87.81 C +ATOM 506 CD GLU A 182 30.999 19.562 49.374 1.00 97.73 C +ATOM 507 OE1 GLU A 182 32.013 19.311 50.057 1.00100.00 O +ATOM 508 OE2 GLU A 182 30.337 18.674 48.797 1.00 92.34 O +ATOM 509 N GLU A 183 26.026 20.052 49.657 1.00 71.44 N +ATOM 510 CA GLU A 183 24.601 20.115 49.361 1.00 56.58 C +ATOM 511 C GLU A 183 23.824 19.910 50.656 1.00 59.61 C +ATOM 512 O GLU A 183 22.942 20.697 50.997 1.00 61.56 O +ATOM 513 CB GLU A 183 24.226 19.031 48.339 1.00 41.00 C +ATOM 514 CG GLU A 183 25.021 19.121 47.040 1.00 52.50 C +ATOM 515 CD GLU A 183 24.696 18.010 46.054 1.00 58.87 C +ATOM 516 OE1 GLU A 183 24.670 16.831 46.469 1.00 43.01 O +ATOM 517 OE2 GLU A 183 24.470 18.321 44.861 1.00 52.00 O +ATOM 518 N LYS A 184 24.167 18.850 51.380 1.00 53.06 N +ATOM 519 CA LYS A 184 23.506 18.536 52.638 1.00 57.91 C +ATOM 520 C LYS A 184 23.575 19.713 53.603 1.00 64.25 C +ATOM 521 O LYS A 184 22.739 19.839 54.499 1.00 65.13 O +ATOM 522 CB LYS A 184 24.148 17.306 53.279 1.00 52.43 C +ATOM 523 CG LYS A 184 23.777 15.996 52.613 1.00 46.38 C +ATOM 524 CD LYS A 184 24.360 14.816 53.368 1.00 42.06 C +ATOM 525 CE LYS A 184 23.957 13.503 52.730 1.00 45.51 C +ATOM 526 NZ LYS A 184 24.537 12.335 53.447 1.00 53.49 N +ATOM 527 N LYS A 185 24.576 20.571 53.424 1.00 58.11 N +ATOM 528 CA LYS A 185 24.724 21.736 54.286 1.00 67.71 C +ATOM 529 C LYS A 185 23.656 22.745 53.905 1.00 61.16 C +ATOM 530 O LYS A 185 22.981 23.316 54.764 1.00 73.17 O +ATOM 531 CB LYS A 185 26.104 22.372 54.115 1.00 71.53 C +ATOM 532 CG LYS A 185 26.301 23.624 54.954 1.00 84.28 C +ATOM 533 CD LYS A 185 27.557 24.373 54.552 1.00 85.26 C +ATOM 534 CE LYS A 185 27.913 25.437 55.576 1.00 87.16 C +ATOM 535 NZ LYS A 185 27.000 26.613 55.508 1.00 87.22 N +ATOM 536 N THR A 186 23.507 22.958 52.604 1.00 42.82 N +ATOM 537 CA THR A 186 22.516 23.896 52.101 1.00 62.42 C +ATOM 538 C THR A 186 21.113 23.426 52.468 1.00 60.37 C +ATOM 539 O THR A 186 20.218 24.234 52.712 1.00 60.50 O +ATOM 540 CB THR A 186 22.616 24.034 50.574 1.00 66.13 C +ATOM 541 OG1 THR A 186 23.993 24.143 50.194 1.00 53.16 O +ATOM 542 CG2 THR A 186 21.865 25.270 50.104 1.00 51.28 C +ATOM 543 N TRP A 187 20.925 22.112 52.499 1.00 58.38 N +ATOM 544 CA TRP A 187 19.632 21.545 52.847 1.00 71.46 C +ATOM 545 C TRP A 187 19.310 21.898 54.297 1.00 76.26 C +ATOM 546 O TRP A 187 18.235 22.417 54.598 1.00 74.65 O +ATOM 547 CB TRP A 187 19.661 20.025 52.664 1.00 73.41 C +ATOM 548 CG TRP A 187 18.535 19.303 53.345 1.00 82.27 C +ATOM 549 CD1 TRP A 187 18.608 18.585 54.502 1.00 81.34 C +ATOM 550 CD2 TRP A 187 17.170 19.214 52.903 1.00 85.83 C +ATOM 551 NE1 TRP A 187 17.379 18.051 54.808 1.00 91.72 N +ATOM 552 CE2 TRP A 187 16.482 18.417 53.843 1.00 88.31 C +ATOM 553 CE3 TRP A 187 16.469 19.722 51.800 1.00 84.92 C +ATOM 554 CZ2 TRP A 187 15.117 18.121 53.717 1.00 89.08 C +ATOM 555 CZ3 TRP A 187 15.111 19.424 51.676 1.00 82.88 C +ATOM 556 CH2 TRP A 187 14.451 18.634 52.633 1.00 80.38 C +ATOM 557 N GLY A 188 20.259 21.617 55.186 1.00 79.18 N +ATOM 558 CA GLY A 188 20.075 21.902 56.596 1.00 71.95 C +ATOM 559 C GLY A 188 20.007 23.382 56.917 1.00 74.01 C +ATOM 560 O GLY A 188 19.427 23.773 57.930 1.00 90.17 O +ATOM 561 N THR A 189 20.602 24.209 56.063 1.00 61.43 N +ATOM 562 CA THR A 189 20.582 25.651 56.278 1.00 79.14 C +ATOM 563 C THR A 189 19.171 26.180 56.027 1.00 83.53 C +ATOM 564 O THR A 189 18.755 27.185 56.608 1.00 86.76 O +ATOM 565 CB THR A 189 21.572 26.374 55.341 1.00 77.79 C +ATOM 566 OG1 THR A 189 22.911 25.988 55.675 1.00 73.16 O +ATOM 567 CG2 THR A 189 21.442 27.888 55.481 1.00 81.44 C +ATOM 568 N VAL A 190 18.442 25.487 55.158 1.00 86.25 N +ATOM 569 CA VAL A 190 17.074 25.867 54.826 1.00 85.35 C +ATOM 570 C VAL A 190 16.101 25.118 55.734 1.00 83.60 C +ATOM 571 O VAL A 190 15.051 25.641 56.112 1.00 75.22 O +ATOM 572 CB VAL A 190 16.741 25.533 53.357 1.00 79.63 C +ATOM 573 CG1 VAL A 190 15.429 26.193 52.961 1.00 75.13 C +ATOM 574 CG2 VAL A 190 17.864 25.993 52.452 1.00 75.09 C +ATOM 575 N PHE A 191 16.467 23.885 56.076 1.00 79.24 N +ATOM 576 CA PHE A 191 15.655 23.039 56.945 1.00 76.08 C +ATOM 577 C PHE A 191 15.634 23.589 58.369 1.00 85.23 C +ATOM 578 O PHE A 191 14.741 23.276 59.152 1.00 99.86 O +ATOM 579 CB PHE A 191 16.213 21.616 56.958 1.00 67.59 C +ATOM 580 CG PHE A 191 15.343 20.628 57.676 1.00 73.28 C +ATOM 581 CD1 PHE A 191 14.405 19.876 56.979 1.00 80.98 C +ATOM 582 CD2 PHE A 191 15.469 20.437 59.048 1.00 79.62 C +ATOM 583 CE1 PHE A 191 13.605 18.945 57.638 1.00 81.20 C +ATOM 584 CE2 PHE A 191 14.674 19.508 59.717 1.00 79.70 C +ATOM 585 CZ PHE A 191 13.740 18.761 59.010 1.00 80.86 C +ATOM 586 N LYS A 192 16.627 24.405 58.703 1.00 89.68 N +ATOM 587 CA LYS A 192 16.706 24.994 60.034 1.00 86.96 C +ATOM 588 C LYS A 192 16.018 26.350 60.046 1.00 83.34 C +ATOM 589 O LYS A 192 15.218 26.647 60.932 1.00 91.70 O +ATOM 590 CB LYS A 192 18.165 25.167 60.454 1.00 91.20 C +ATOM 591 CG LYS A 192 18.335 25.741 61.849 1.00100.00 C +ATOM 592 CD LYS A 192 19.800 25.914 62.209 1.00100.00 C +ATOM 593 CE LYS A 192 20.408 24.597 62.664 1.00100.00 C +ATOM 594 NZ LYS A 192 19.996 24.235 64.051 1.00100.00 N +ATOM 595 N THR A 193 16.341 27.166 59.050 1.00 76.10 N +ATOM 596 CA THR A 193 15.770 28.499 58.931 1.00 90.50 C +ATOM 597 C THR A 193 14.247 28.499 58.830 1.00 96.09 C +ATOM 598 O THR A 193 13.590 29.409 59.337 1.00100.00 O +ATOM 599 CB THR A 193 16.322 29.226 57.694 1.00100.00 C +ATOM 600 OG1 THR A 193 15.665 30.493 57.550 1.00100.00 O +ATOM 601 CG2 THR A 193 16.081 28.399 56.448 1.00100.00 C +ATOM 602 N LEU A 194 13.689 27.484 58.177 1.00 90.36 N +ATOM 603 CA LEU A 194 12.243 27.402 57.999 1.00 85.08 C +ATOM 604 C LEU A 194 11.500 26.599 59.068 1.00 82.86 C +ATOM 605 O LEU A 194 10.344 26.890 59.375 1.00 85.60 O +ATOM 606 CB LEU A 194 11.924 26.829 56.615 1.00 74.24 C +ATOM 607 CG LEU A 194 12.348 27.686 55.418 1.00 72.30 C +ATOM 608 CD1 LEU A 194 12.093 26.924 54.131 1.00 73.94 C +ATOM 609 CD2 LEU A 194 11.579 28.995 55.417 1.00 77.30 C +ATOM 610 N LYS A 195 12.159 25.591 59.631 1.00 79.81 N +ATOM 611 CA LYS A 195 11.533 24.752 60.652 1.00 80.42 C +ATOM 612 C LYS A 195 11.021 25.556 61.839 1.00 86.30 C +ATOM 613 O LYS A 195 10.099 25.133 62.540 1.00 84.76 O +ATOM 614 CB LYS A 195 12.519 23.700 61.152 1.00 86.69 C +ATOM 615 CG LYS A 195 11.904 22.696 62.112 1.00 88.67 C +ATOM 616 CD LYS A 195 12.800 21.481 62.296 1.00 93.28 C +ATOM 617 CE LYS A 195 12.347 20.642 63.479 1.00 92.20 C +ATOM 618 NZ LYS A 195 10.955 20.144 63.309 1.00 88.53 N +ATOM 619 N SER A 196 11.630 26.713 62.065 1.00 94.23 N +ATOM 620 CA SER A 196 11.241 27.574 63.173 1.00100.00 C +ATOM 621 C SER A 196 9.950 28.343 62.894 1.00100.00 C +ATOM 622 O SER A 196 9.106 28.497 63.780 1.00100.00 O +ATOM 623 CB SER A 196 12.365 28.566 63.480 1.00100.00 C +ATOM 624 OG SER A 196 12.518 29.504 62.426 1.00 85.80 O +ATOM 625 N LEU A 197 9.795 28.812 61.659 1.00 96.32 N +ATOM 626 CA LEU A 197 8.618 29.589 61.278 1.00 93.99 C +ATOM 627 C LEU A 197 7.403 28.799 60.809 1.00 88.37 C +ATOM 628 O LEU A 197 6.415 29.392 60.382 1.00 81.94 O +ATOM 629 CB LEU A 197 8.984 30.590 60.182 1.00 95.30 C +ATOM 630 CG LEU A 197 10.268 31.406 60.330 1.00 93.83 C +ATOM 631 CD1 LEU A 197 10.387 32.346 59.144 1.00100.00 C +ATOM 632 CD2 LEU A 197 10.250 32.192 61.633 1.00100.00 C +ATOM 633 N TYR A 198 7.454 27.474 60.886 1.00 87.34 N +ATOM 634 CA TYR A 198 6.320 26.679 60.426 1.00 89.12 C +ATOM 635 C TYR A 198 5.164 26.608 61.413 1.00 85.78 C +ATOM 636 O TYR A 198 4.016 26.851 61.046 1.00 80.49 O +ATOM 637 CB TYR A 198 6.774 25.270 60.043 1.00 84.46 C +ATOM 638 CG TYR A 198 7.357 25.191 58.649 1.00 83.63 C +ATOM 639 CD1 TYR A 198 6.947 26.077 57.649 1.00 72.73 C +ATOM 640 CD2 TYR A 198 8.342 24.257 58.336 1.00 78.08 C +ATOM 641 CE1 TYR A 198 7.507 26.035 56.376 1.00 67.94 C +ATOM 642 CE2 TYR A 198 8.909 24.206 57.066 1.00 72.97 C +ATOM 643 CZ TYR A 198 8.486 25.098 56.093 1.00 71.06 C +ATOM 644 OH TYR A 198 9.042 25.048 54.837 1.00 81.83 O +ATOM 645 N LYS A 199 5.454 26.263 62.661 1.00 92.31 N +ATOM 646 CA LYS A 199 4.397 26.190 63.667 1.00100.00 C +ATOM 647 C LYS A 199 3.805 27.583 63.837 1.00100.00 C +ATOM 648 O LYS A 199 2.677 27.751 64.310 1.00100.00 O +ATOM 649 CB LYS A 199 4.958 25.706 65.004 1.00 99.73 C +ATOM 650 CG LYS A 199 6.227 26.418 65.433 1.00 96.19 C +ATOM 651 CD LYS A 199 6.942 25.631 66.515 1.00100.00 C +ATOM 652 CE LYS A 199 7.390 24.272 65.995 1.00100.00 C +ATOM 653 NZ LYS A 199 8.257 24.390 64.784 1.00100.00 N +ATOM 654 N THR A 200 4.580 28.582 63.437 1.00100.00 N +ATOM 655 CA THR A 200 4.153 29.964 63.544 1.00 98.21 C +ATOM 656 C THR A 200 3.325 30.419 62.351 1.00 92.84 C +ATOM 657 O THR A 200 2.122 30.649 62.467 1.00 85.72 O +ATOM 658 CB THR A 200 5.365 30.900 63.675 1.00100.00 C +ATOM 659 OG1 THR A 200 6.272 30.370 64.648 1.00100.00 O +ATOM 660 CG2 THR A 200 4.919 32.295 64.100 1.00 92.31 C +ATOM 661 N HIS A 201 3.982 30.538 61.202 1.00 91.59 N +ATOM 662 CA HIS A 201 3.334 31.007 59.983 1.00 96.97 C +ATOM 663 C HIS A 201 2.666 29.956 59.087 1.00 98.81 C +ATOM 664 O HIS A 201 1.668 30.251 58.425 1.00100.00 O +ATOM 665 CB HIS A 201 4.344 31.809 59.154 1.00 97.39 C +ATOM 666 CG HIS A 201 4.989 32.931 59.909 1.00100.00 C +ATOM 667 ND1 HIS A 201 4.270 33.811 60.689 1.00100.00 N +ATOM 668 CD2 HIS A 201 6.283 33.318 59.999 1.00100.00 C +ATOM 669 CE1 HIS A 201 5.094 34.695 61.226 1.00100.00 C +ATOM 670 NE2 HIS A 201 6.321 34.417 60.822 1.00100.00 N +ATOM 671 N ALA A 202 3.205 28.740 59.057 1.00 99.97 N +ATOM 672 CA ALA A 202 2.641 27.684 58.216 1.00 95.61 C +ATOM 673 C ALA A 202 1.244 27.257 58.658 1.00 92.19 C +ATOM 674 O ALA A 202 0.884 27.385 59.828 1.00 83.66 O +ATOM 675 CB ALA A 202 3.570 26.478 58.192 1.00100.00 C +ATOM 676 N CYS A 203 0.464 26.750 57.706 1.00 88.73 N +ATOM 677 CA CYS A 203 -0.900 26.303 57.974 1.00 91.74 C +ATOM 678 C CYS A 203 -0.947 24.967 58.715 1.00 89.57 C +ATOM 679 O CYS A 203 0.016 24.198 58.708 1.00 90.42 O +ATOM 680 CB CYS A 203 -1.693 26.202 56.667 1.00 93.32 C +ATOM 681 SG CYS A 203 -1.253 24.804 55.613 1.00100.00 S +ATOM 682 N TYR A 204 -2.085 24.706 59.349 1.00 89.75 N +ATOM 683 CA TYR A 204 -2.294 23.494 60.127 1.00 89.68 C +ATOM 684 C TYR A 204 -1.942 22.199 59.404 1.00 92.54 C +ATOM 685 O TYR A 204 -1.113 21.427 59.880 1.00100.00 O +ATOM 686 CB TYR A 204 -3.747 23.438 60.611 1.00 90.65 C +ATOM 687 CG TYR A 204 -4.223 22.054 60.997 1.00 95.13 C +ATOM 688 CD1 TYR A 204 -3.540 21.300 61.953 1.00100.00 C +ATOM 689 CD2 TYR A 204 -5.355 21.496 60.405 1.00100.00 C +ATOM 690 CE1 TYR A 204 -3.972 20.024 62.311 1.00100.00 C +ATOM 691 CE2 TYR A 204 -5.797 20.219 60.755 1.00100.00 C +ATOM 692 CZ TYR A 204 -5.100 19.491 61.709 1.00100.00 C +ATOM 693 OH TYR A 204 -5.531 18.234 62.068 1.00 86.78 O +ATOM 694 N GLU A 205 -2.581 21.959 58.263 1.00 96.85 N +ATOM 695 CA GLU A 205 -2.339 20.739 57.494 1.00 94.12 C +ATOM 696 C GLU A 205 -0.848 20.475 57.321 1.00 92.18 C +ATOM 697 O GLU A 205 -0.421 19.329 57.161 1.00 76.01 O +ATOM 698 CB GLU A 205 -3.014 20.832 56.123 1.00 91.15 C +ATOM 699 CG GLU A 205 -4.511 21.094 56.182 1.00 80.29 C +ATOM 700 CD GLU A 205 -4.833 22.514 56.604 1.00 94.15 C +ATOM 701 OE1 GLU A 205 -5.964 22.753 57.075 1.00 98.51 O +ATOM 702 OE2 GLU A 205 -3.952 23.390 56.463 1.00100.00 O +ATOM 703 N TYR A 206 -0.061 21.547 57.360 1.00 90.46 N +ATOM 704 CA TYR A 206 1.388 21.454 57.215 1.00 87.27 C +ATOM 705 C TYR A 206 1.998 20.994 58.529 1.00 87.37 C +ATOM 706 O TYR A 206 2.735 20.008 58.574 1.00 90.91 O +ATOM 707 CB TYR A 206 1.965 22.821 56.837 1.00 84.49 C +ATOM 708 CG TYR A 206 3.382 22.782 56.308 1.00 83.47 C +ATOM 709 CD1 TYR A 206 3.669 23.194 55.009 1.00 84.19 C +ATOM 710 CD2 TYR A 206 4.438 22.354 57.112 1.00 81.07 C +ATOM 711 CE1 TYR A 206 4.971 23.182 54.520 1.00 81.36 C +ATOM 712 CE2 TYR A 206 5.746 22.339 56.632 1.00 88.23 C +ATOM 713 CZ TYR A 206 6.005 22.756 55.335 1.00 88.88 C +ATOM 714 OH TYR A 206 7.294 22.747 54.852 1.00 86.93 O +ATOM 715 N ASN A 207 1.681 21.724 59.596 1.00 83.68 N +ATOM 716 CA ASN A 207 2.188 21.423 60.930 1.00 85.33 C +ATOM 717 C ASN A 207 1.759 20.042 61.413 1.00 87.45 C +ATOM 718 O ASN A 207 2.390 19.465 62.299 1.00 84.26 O +ATOM 719 CB ASN A 207 1.710 22.484 61.921 1.00 86.60 C +ATOM 720 CG ASN A 207 2.235 23.869 61.590 1.00100.00 C +ATOM 721 OD1 ASN A 207 3.446 24.096 61.563 1.00100.00 O +ATOM 722 ND2 ASN A 207 1.326 24.802 61.333 1.00100.00 N +ATOM 723 N HIS A 208 0.688 19.518 60.823 1.00 89.56 N +ATOM 724 CA HIS A 208 0.178 18.203 61.199 1.00 85.85 C +ATOM 725 C HIS A 208 0.982 17.079 60.556 1.00 76.51 C +ATOM 726 O HIS A 208 1.413 16.139 61.227 1.00 63.62 O +ATOM 727 CB HIS A 208 -1.295 18.063 60.792 1.00 73.65 C +ATOM 728 CG HIS A 208 -1.783 16.646 60.783 1.00 75.73 C +ATOM 729 ND1 HIS A 208 -2.327 16.052 59.662 1.00 67.92 N +ATOM 730 CD2 HIS A 208 -1.783 15.694 61.745 1.00 87.75 C +ATOM 731 CE1 HIS A 208 -2.639 14.798 59.937 1.00 66.17 C +ATOM 732 NE2 HIS A 208 -2.319 14.555 61.196 1.00 74.70 N +ATOM 733 N ILE A 209 1.182 17.184 59.250 1.00 70.01 N +ATOM 734 CA ILE A 209 1.905 16.164 58.504 1.00 76.07 C +ATOM 735 C ILE A 209 3.421 16.146 58.694 1.00 81.86 C +ATOM 736 O ILE A 209 4.054 15.095 58.565 1.00 81.22 O +ATOM 737 CB ILE A 209 1.614 16.291 56.993 1.00 73.26 C +ATOM 738 CG1 ILE A 209 2.157 15.063 56.257 1.00 57.57 C +ATOM 739 CG2 ILE A 209 2.233 17.576 56.451 1.00 70.08 C +ATOM 740 CD1 ILE A 209 1.523 13.767 56.698 1.00 52.00 C +ATOM 741 N PHE A 210 4.005 17.303 59.001 1.00 85.71 N +ATOM 742 CA PHE A 210 5.453 17.394 59.174 1.00 75.69 C +ATOM 743 C PHE A 210 6.055 16.324 60.071 1.00 76.41 C +ATOM 744 O PHE A 210 6.895 15.542 59.628 1.00 73.65 O +ATOM 745 CB PHE A 210 5.854 18.773 59.695 1.00 72.53 C +ATOM 746 CG PHE A 210 7.067 19.343 59.015 1.00 89.37 C +ATOM 747 CD1 PHE A 210 8.163 19.780 59.754 1.00100.00 C +ATOM 748 CD2 PHE A 210 7.114 19.444 57.629 1.00100.00 C +ATOM 749 CE1 PHE A 210 9.290 20.310 59.119 1.00100.00 C +ATOM 750 CE2 PHE A 210 8.236 19.973 56.985 1.00100.00 C +ATOM 751 CZ PHE A 210 9.325 20.408 57.735 1.00 98.73 C +ATOM 752 N PRO A 211 5.628 16.263 61.345 1.00 78.71 N +ATOM 753 CA PRO A 211 6.210 15.238 62.218 1.00 72.51 C +ATOM 754 C PRO A 211 6.125 13.831 61.636 1.00 66.57 C +ATOM 755 O PRO A 211 6.876 12.942 62.039 1.00 66.09 O +ATOM 756 CB PRO A 211 5.421 15.382 63.518 1.00 88.21 C +ATOM 757 CG PRO A 211 4.849 16.760 63.476 1.00 89.51 C +ATOM 758 CD PRO A 211 4.609 17.071 62.034 1.00 79.55 C +ATOM 759 N LEU A 212 5.213 13.632 60.687 1.00 67.37 N +ATOM 760 CA LEU A 212 5.048 12.329 60.046 1.00 76.53 C +ATOM 761 C LEU A 212 6.048 12.215 58.902 1.00 80.70 C +ATOM 762 O LEU A 212 6.529 11.127 58.589 1.00 72.08 O +ATOM 763 CB LEU A 212 3.625 12.174 59.500 1.00 72.65 C +ATOM 764 CG LEU A 212 2.487 12.057 60.517 1.00 53.72 C +ATOM 765 CD1 LEU A 212 1.180 12.453 59.853 1.00 47.91 C +ATOM 766 CD2 LEU A 212 2.422 10.635 61.058 1.00 26.98 C +ATOM 767 N LEU A 213 6.345 13.351 58.275 1.00 79.57 N +ATOM 768 CA LEU A 213 7.304 13.400 57.176 1.00 73.46 C +ATOM 769 C LEU A 213 8.691 13.214 57.780 1.00 75.68 C +ATOM 770 O LEU A 213 9.534 12.500 57.238 1.00 73.21 O +ATOM 771 CB LEU A 213 7.235 14.755 56.474 1.00 60.67 C +ATOM 772 CG LEU A 213 6.085 14.981 55.492 1.00 68.02 C +ATOM 773 CD1 LEU A 213 5.965 16.472 55.189 1.00 61.82 C +ATOM 774 CD2 LEU A 213 6.332 14.182 54.221 1.00 51.97 C +ATOM 775 N GLU A 214 8.914 13.875 58.911 1.00 80.67 N +ATOM 776 CA GLU A 214 10.185 13.792 59.610 1.00 78.90 C +ATOM 777 C GLU A 214 10.397 12.375 60.129 1.00 76.25 C +ATOM 778 O GLU A 214 11.459 11.787 59.942 1.00 82.01 O +ATOM 779 CB GLU A 214 10.208 14.785 60.776 1.00 84.27 C +ATOM 780 CG GLU A 214 9.896 16.217 60.372 1.00 97.39 C +ATOM 781 CD GLU A 214 9.835 17.160 61.561 1.00100.00 C +ATOM 782 OE1 GLU A 214 8.720 17.605 61.914 1.00100.00 O +ATOM 783 OE2 GLU A 214 10.903 17.457 62.143 1.00100.00 O +ATOM 784 N LYS A 215 9.372 11.831 60.776 1.00 70.39 N +ATOM 785 CA LYS A 215 9.448 10.489 61.335 1.00 70.40 C +ATOM 786 C LYS A 215 9.396 9.375 60.291 1.00 79.87 C +ATOM 787 O LYS A 215 9.718 8.225 60.595 1.00 91.68 O +ATOM 788 CB LYS A 215 8.313 10.276 62.339 1.00 72.12 C +ATOM 789 CG LYS A 215 8.403 8.954 63.085 1.00 92.07 C +ATOM 790 CD LYS A 215 7.267 8.788 64.081 1.00 96.37 C +ATOM 791 CE LYS A 215 7.487 9.652 65.314 1.00100.00 C +ATOM 792 NZ LYS A 215 8.719 9.273 66.065 1.00100.00 N +ATOM 793 N TYR A 216 9.003 9.704 59.064 1.00 84.91 N +ATOM 794 CA TYR A 216 8.896 8.676 58.034 1.00 91.21 C +ATOM 795 C TYR A 216 9.778 8.803 56.796 1.00 87.96 C +ATOM 796 O TYR A 216 10.553 7.897 56.491 1.00 84.66 O +ATOM 797 CB TYR A 216 7.430 8.539 57.618 1.00 94.00 C +ATOM 798 CG TYR A 216 6.583 7.898 58.689 1.00100.00 C +ATOM 799 CD1 TYR A 216 5.745 8.664 59.501 1.00 96.76 C +ATOM 800 CD2 TYR A 216 6.644 6.524 58.915 1.00100.00 C +ATOM 801 CE1 TYR A 216 4.992 8.076 60.514 1.00 96.20 C +ATOM 802 CE2 TYR A 216 5.897 5.926 59.923 1.00100.00 C +ATOM 803 CZ TYR A 216 5.073 6.705 60.720 1.00100.00 C +ATOM 804 OH TYR A 216 4.337 6.111 61.723 1.00100.00 O +ATOM 805 N CYS A 217 9.669 9.916 56.083 1.00 77.03 N +ATOM 806 CA CYS A 217 10.459 10.100 54.872 1.00 82.44 C +ATOM 807 C CYS A 217 11.850 10.689 55.094 1.00 87.08 C +ATOM 808 O CYS A 217 12.455 11.246 54.175 1.00 93.26 O +ATOM 809 CB CYS A 217 9.684 10.965 53.880 1.00 89.04 C +ATOM 810 SG CYS A 217 8.256 10.130 53.168 1.00100.00 S +ATOM 811 N GLY A 218 12.357 10.557 56.313 1.00 85.81 N +ATOM 812 CA GLY A 218 13.676 11.071 56.622 1.00 87.04 C +ATOM 813 C GLY A 218 13.826 12.575 56.501 1.00 86.37 C +ATOM 814 O GLY A 218 14.829 13.064 55.980 1.00 90.00 O +ATOM 815 N PHE A 219 12.833 13.313 56.984 1.00 79.48 N +ATOM 816 CA PHE A 219 12.885 14.768 56.930 1.00 73.33 C +ATOM 817 C PHE A 219 13.665 15.298 58.126 1.00 79.58 C +ATOM 818 O PHE A 219 13.096 15.572 59.177 1.00 87.13 O +ATOM 819 CB PHE A 219 11.469 15.351 56.916 1.00 54.87 C +ATOM 820 CG PHE A 219 10.931 15.602 55.531 1.00 54.38 C +ATOM 821 CD1 PHE A 219 10.736 14.542 54.645 1.00 47.42 C +ATOM 822 CD2 PHE A 219 10.634 16.896 55.102 1.00 38.98 C +ATOM 823 CE1 PHE A 219 10.245 14.764 53.355 1.00 33.19 C +ATOM 824 CE2 PHE A 219 10.143 17.128 53.814 1.00 31.12 C +ATOM 825 CZ PHE A 219 9.951 16.062 52.939 1.00 35.16 C +ATOM 826 N HIS A 220 14.978 15.424 57.953 1.00 83.06 N +ATOM 827 CA HIS A 220 15.870 15.917 58.999 1.00 90.40 C +ATOM 828 C HIS A 220 16.946 16.781 58.346 1.00 93.84 C +ATOM 829 O HIS A 220 17.367 16.504 57.222 1.00100.00 O +ATOM 830 CB HIS A 220 16.521 14.744 59.733 1.00 90.54 C +ATOM 831 CG HIS A 220 17.269 15.139 60.967 1.00100.00 C +ATOM 832 ND1 HIS A 220 18.320 14.402 61.469 1.00100.00 N +ATOM 833 CD2 HIS A 220 17.114 16.191 61.810 1.00 97.71 C +ATOM 834 CE1 HIS A 220 18.778 14.978 62.564 1.00100.00 C +ATOM 835 NE2 HIS A 220 18.063 16.066 62.793 1.00 99.67 N +ATOM 836 N GLU A 221 17.395 17.819 59.045 1.00 81.93 N +ATOM 837 CA GLU A 221 18.410 18.710 58.492 1.00 73.21 C +ATOM 838 C GLU A 221 19.723 18.021 58.151 1.00 66.02 C +ATOM 839 O GLU A 221 20.549 18.583 57.431 1.00 76.25 O +ATOM 840 CB GLU A 221 18.684 19.862 59.456 1.00 74.49 C +ATOM 841 CG GLU A 221 19.037 19.422 60.860 1.00 91.38 C +ATOM 842 CD GLU A 221 19.376 20.594 61.757 1.00100.00 C +ATOM 843 OE1 GLU A 221 19.907 20.365 62.866 1.00100.00 O +ATOM 844 OE2 GLU A 221 19.111 21.747 61.351 1.00 92.36 O +ATOM 845 N ASP A 222 19.915 16.805 58.655 1.00 58.15 N +ATOM 846 CA ASP A 222 21.153 16.077 58.397 1.00 64.41 C +ATOM 847 C ASP A 222 21.111 15.138 57.201 1.00 60.43 C +ATOM 848 O ASP A 222 22.145 14.610 56.784 1.00 53.79 O +ATOM 849 CB ASP A 222 21.568 15.304 59.645 1.00 82.99 C +ATOM 850 CG ASP A 222 22.047 16.216 60.754 1.00 97.61 C +ATOM 851 OD1 ASP A 222 21.192 16.888 61.369 1.00100.00 O +ATOM 852 OD2 ASP A 222 23.272 16.268 61.005 1.00 91.26 O +ATOM 853 N ASN A 223 19.925 14.929 56.643 1.00 56.54 N +ATOM 854 CA ASN A 223 19.793 14.049 55.490 1.00 56.77 C +ATOM 855 C ASN A 223 18.732 14.524 54.509 1.00 53.96 C +ATOM 856 O ASN A 223 17.620 14.870 54.906 1.00 51.52 O +ATOM 857 CB ASN A 223 19.463 12.625 55.937 1.00 72.23 C +ATOM 858 CG ASN A 223 19.111 11.717 54.767 1.00 93.67 C +ATOM 859 OD1 ASN A 223 17.964 11.291 54.622 1.00100.00 O +ATOM 860 ND2 ASN A 223 20.098 11.422 53.923 1.00 88.60 N +ATOM 861 N ILE A 224 19.083 14.537 53.224 1.00 60.64 N +ATOM 862 CA ILE A 224 18.154 14.955 52.179 1.00 57.31 C +ATOM 863 C ILE A 224 17.238 13.783 51.832 1.00 50.66 C +ATOM 864 O ILE A 224 17.705 12.709 51.455 1.00 49.35 O +ATOM 865 CB ILE A 224 18.904 15.407 50.913 1.00 49.19 C +ATOM 866 CG1 ILE A 224 19.634 16.724 51.191 1.00 46.06 C +ATOM 867 CG2 ILE A 224 17.921 15.582 49.770 1.00 48.55 C +ATOM 868 CD1 ILE A 224 20.371 17.287 49.992 1.00 49.60 C +ATOM 869 N PRO A 225 15.915 13.984 51.943 1.00 38.91 N +ATOM 870 CA PRO A 225 14.928 12.939 51.651 1.00 39.74 C +ATOM 871 C PRO A 225 14.946 12.415 50.220 1.00 43.17 C +ATOM 872 O PRO A 225 15.039 13.187 49.266 1.00 45.06 O +ATOM 873 CB PRO A 225 13.588 13.588 52.000 1.00 48.74 C +ATOM 874 CG PRO A 225 13.927 14.810 52.780 1.00 63.06 C +ATOM 875 CD PRO A 225 15.273 15.248 52.329 1.00 51.19 C +ATOM 876 N GLN A 226 14.837 11.095 50.086 1.00 38.21 N +ATOM 877 CA GLN A 226 14.833 10.448 48.781 1.00 50.78 C +ATOM 878 C GLN A 226 13.430 10.430 48.178 1.00 50.49 C +ATOM 879 O GLN A 226 12.476 9.981 48.813 1.00 46.10 O +ATOM 880 CB GLN A 226 15.372 9.017 48.893 1.00 59.66 C +ATOM 881 CG GLN A 226 16.875 8.931 49.149 1.00 64.83 C +ATOM 882 CD GLN A 226 17.720 9.352 47.949 1.00 72.40 C +ATOM 883 OE1 GLN A 226 18.805 8.814 47.724 1.00 78.96 O +ATOM 884 NE2 GLN A 226 17.226 10.315 47.176 1.00 81.37 N +ATOM 885 N LEU A 227 13.329 10.911 46.940 1.00 53.52 N +ATOM 886 CA LEU A 227 12.063 10.988 46.218 1.00 51.51 C +ATOM 887 C LEU A 227 11.239 9.705 46.204 1.00 54.39 C +ATOM 888 O LEU A 227 10.021 9.748 46.380 1.00 47.39 O +ATOM 889 CB LEU A 227 12.313 11.449 44.779 1.00 32.21 C +ATOM 890 CG LEU A 227 12.952 12.830 44.585 1.00 50.79 C +ATOM 891 CD1 LEU A 227 12.504 13.409 43.247 1.00 37.22 C +ATOM 892 CD2 LEU A 227 12.560 13.766 45.720 1.00 43.31 C +ATOM 893 N GLU A 228 11.889 8.567 45.988 1.00 52.15 N +ATOM 894 CA GLU A 228 11.168 7.300 45.960 1.00 45.45 C +ATOM 895 C GLU A 228 10.405 7.101 47.261 1.00 46.15 C +ATOM 896 O GLU A 228 9.326 6.510 47.275 1.00 43.58 O +ATOM 897 CB GLU A 228 12.136 6.139 45.753 1.00 42.63 C +ATOM 898 CG GLU A 228 11.718 5.181 44.652 1.00 58.54 C +ATOM 899 CD GLU A 228 10.228 4.891 44.649 1.00 53.14 C +ATOM 900 OE1 GLU A 228 9.470 5.692 44.069 1.00 60.98 O +ATOM 901 OE2 GLU A 228 9.814 3.861 45.220 1.00 59.24 O +ATOM 902 N ASP A 229 10.975 7.604 48.350 1.00 39.29 N +ATOM 903 CA ASP A 229 10.364 7.492 49.669 1.00 45.38 C +ATOM 904 C ASP A 229 9.177 8.435 49.772 1.00 42.03 C +ATOM 905 O ASP A 229 8.062 8.022 50.097 1.00 43.40 O +ATOM 906 CB ASP A 229 11.388 7.834 50.752 1.00 53.25 C +ATOM 907 CG ASP A 229 12.540 6.849 50.799 1.00 48.93 C +ATOM 908 OD1 ASP A 229 12.332 5.676 50.421 1.00 41.90 O +ATOM 909 OD2 ASP A 229 13.649 7.249 51.213 1.00 50.62 O +ATOM 910 N VAL A 230 9.425 9.708 49.490 1.00 27.10 N +ATOM 911 CA VAL A 230 8.378 10.720 49.537 1.00 37.17 C +ATOM 912 C VAL A 230 7.219 10.330 48.623 1.00 36.33 C +ATOM 913 O VAL A 230 6.056 10.369 49.025 1.00 24.34 O +ATOM 914 CB VAL A 230 8.916 12.092 49.093 1.00 41.74 C +ATOM 915 CG1 VAL A 230 7.898 13.184 49.400 1.00 43.64 C +ATOM 916 CG2 VAL A 230 10.228 12.376 49.784 1.00 49.93 C +ATOM 917 N SER A 231 7.545 9.960 47.389 1.00 31.56 N +ATOM 918 CA SER A 231 6.527 9.556 46.430 1.00 45.89 C +ATOM 919 C SER A 231 5.759 8.372 47.007 1.00 46.44 C +ATOM 920 O SER A 231 4.538 8.422 47.148 1.00 41.88 O +ATOM 921 CB SER A 231 7.176 9.163 45.099 1.00 50.12 C +ATOM 922 OG SER A 231 6.233 8.561 44.228 1.00 48.07 O +ATOM 923 N GLN A 232 6.489 7.310 47.344 1.00 43.04 N +ATOM 924 CA GLN A 232 5.871 6.121 47.916 1.00 50.18 C +ATOM 925 C GLN A 232 4.974 6.481 49.095 1.00 60.01 C +ATOM 926 O GLN A 232 3.939 5.863 49.316 1.00 67.03 O +ATOM 927 CB GLN A 232 6.941 5.116 48.348 1.00 51.33 C +ATOM 928 CG GLN A 232 6.535 3.662 48.169 1.00 68.14 C +ATOM 929 CD GLN A 232 6.212 3.322 46.728 1.00 81.94 C +ATOM 930 OE1 GLN A 232 5.227 2.641 46.446 1.00 97.08 O +ATOM 931 NE2 GLN A 232 6.905 3.692 45.656 1.00 20.00 N +ATOM 932 N PHE A 233 5.393 7.503 49.838 1.00 57.14 N +ATOM 933 CA PHE A 233 4.657 7.961 51.008 1.00 59.22 C +ATOM 934 C PHE A 233 3.381 8.676 50.588 1.00 56.05 C +ATOM 935 O PHE A 233 2.274 8.229 50.888 1.00 68.44 O +ATOM 936 CB PHE A 233 5.519 8.912 51.841 1.00 57.15 C +ATOM 937 CG PHE A 233 4.819 9.468 53.053 1.00 45.21 C +ATOM 938 CD1 PHE A 233 4.000 8.661 53.837 1.00 49.78 C +ATOM 939 CD2 PHE A 233 4.984 10.800 53.416 1.00 49.92 C +ATOM 940 CE1 PHE A 233 3.356 9.172 54.961 1.00 58.40 C +ATOM 941 CE2 PHE A 233 4.345 11.321 54.538 1.00 48.90 C +ATOM 942 CZ PHE A 233 3.530 10.506 55.312 1.00 48.87 C +ATOM 943 N LEU A 234 3.555 9.796 49.899 1.00 40.06 N +ATOM 944 CA LEU A 234 2.437 10.603 49.424 1.00 38.99 C +ATOM 945 C LEU A 234 1.347 9.745 48.793 1.00 50.84 C +ATOM 946 O LEU A 234 0.158 10.050 48.905 1.00 56.22 O +ATOM 947 CB LEU A 234 2.932 11.626 48.396 1.00 50.49 C +ATOM 948 CG LEU A 234 3.551 12.912 48.949 1.00 43.22 C +ATOM 949 CD1 LEU A 234 4.255 13.666 47.837 1.00 51.10 C +ATOM 950 CD2 LEU A 234 2.466 13.772 49.564 1.00 30.63 C +ATOM 951 N GLN A 235 1.755 8.672 48.125 1.00 41.81 N +ATOM 952 CA GLN A 235 0.803 7.796 47.463 1.00 32.74 C +ATOM 953 C GLN A 235 -0.194 7.165 48.424 1.00 30.32 C +ATOM 954 O GLN A 235 -1.376 7.046 48.103 1.00 43.72 O +ATOM 955 CB GLN A 235 1.553 6.717 46.686 1.00 36.87 C +ATOM 956 CG GLN A 235 2.316 7.262 45.495 1.00 51.02 C +ATOM 957 CD GLN A 235 3.042 6.180 44.716 1.00 68.21 C +ATOM 958 OE1 GLN A 235 2.441 5.184 44.306 1.00 60.38 O +ATOM 959 NE2 GLN A 235 4.342 6.370 44.506 1.00 66.98 N +ATOM 960 N THR A 236 0.276 6.766 49.600 1.00 33.61 N +ATOM 961 CA THR A 236 -0.599 6.142 50.590 1.00 38.05 C +ATOM 962 C THR A 236 -1.495 7.159 51.287 1.00 30.93 C +ATOM 963 O THR A 236 -2.517 6.798 51.868 1.00 46.11 O +ATOM 964 CB THR A 236 0.213 5.399 51.661 1.00 34.80 C +ATOM 965 OG1 THR A 236 1.301 6.227 52.085 1.00 51.78 O +ATOM 966 CG2 THR A 236 0.752 4.091 51.106 1.00 49.05 C +ATOM 967 N CYS A 237 -1.109 8.431 51.228 1.00 16.22 N +ATOM 968 CA CYS A 237 -1.889 9.501 51.855 1.00 28.35 C +ATOM 969 C CYS A 237 -3.040 9.949 50.963 1.00 31.88 C +ATOM 970 O CYS A 237 -4.200 9.941 51.373 1.00 16.59 O +ATOM 971 CB CYS A 237 -1.009 10.720 52.155 1.00 9.51 C +ATOM 972 SG CYS A 237 0.505 10.363 53.027 1.00 33.72 S +ATOM 973 N THR A 238 -2.710 10.330 49.732 1.00 33.98 N +ATOM 974 CA THR A 238 -3.710 10.807 48.788 1.00 28.31 C +ATOM 975 C THR A 238 -3.668 10.079 47.447 1.00 20.40 C +ATOM 976 O THR A 238 -4.664 10.017 46.729 1.00 25.90 O +ATOM 977 CB THR A 238 -3.529 12.314 48.545 1.00 22.53 C +ATOM 978 OG1 THR A 238 -2.226 12.550 48.008 1.00 28.52 O +ATOM 979 CG2 THR A 238 -3.665 13.082 49.849 1.00 11.53 C +ATOM 980 N GLY A 239 -2.514 9.518 47.119 1.00 18.84 N +ATOM 981 CA GLY A 239 -2.384 8.814 45.860 1.00 24.31 C +ATOM 982 C GLY A 239 -1.453 9.554 44.922 1.00 34.75 C +ATOM 983 O GLY A 239 -1.175 9.101 43.807 1.00 30.25 O +ATOM 984 N PHE A 240 -0.967 10.701 45.386 1.00 33.76 N +ATOM 985 CA PHE A 240 -0.054 11.532 44.610 1.00 35.25 C +ATOM 986 C PHE A 240 1.319 10.889 44.523 1.00 34.59 C +ATOM 987 O PHE A 240 1.946 10.592 45.540 1.00 41.61 O +ATOM 988 CB PHE A 240 0.082 12.914 45.250 1.00 34.81 C +ATOM 989 CG PHE A 240 -0.551 14.010 44.455 1.00 34.21 C +ATOM 990 CD1 PHE A 240 -1.915 14.256 44.554 1.00 30.04 C +ATOM 991 CD2 PHE A 240 0.212 14.791 43.598 1.00 16.01 C +ATOM 992 CE1 PHE A 240 -2.510 15.266 43.810 1.00 33.78 C +ATOM 993 CE2 PHE A 240 -0.370 15.802 42.850 1.00 32.94 C +ATOM 994 CZ PHE A 240 -1.735 16.041 42.956 1.00 20.13 C +ATOM 995 N ARG A 241 1.784 10.673 43.300 1.00 42.92 N +ATOM 996 CA ARG A 241 3.089 10.078 43.090 1.00 32.18 C +ATOM 997 C ARG A 241 3.994 11.164 42.559 1.00 27.59 C +ATOM 998 O ARG A 241 3.537 12.083 41.890 1.00 28.12 O +ATOM 999 CB ARG A 241 2.999 8.943 42.075 1.00 27.04 C +ATOM 1000 CG ARG A 241 1.868 9.099 41.077 1.00 26.05 C +ATOM 1001 CD ARG A 241 1.614 7.798 40.365 1.00 23.29 C +ATOM 1002 NE ARG A 241 1.126 6.779 41.283 1.00 32.91 N +ATOM 1003 CZ ARG A 241 0.761 5.560 40.904 1.00 44.01 C +ATOM 1004 NH1 ARG A 241 0.834 5.219 39.625 1.00 52.31 N +ATOM 1005 NH2 ARG A 241 0.318 4.684 41.797 1.00 54.45 N +ATOM 1006 N LEU A 242 5.279 11.064 42.862 1.00 34.78 N +ATOM 1007 CA LEU A 242 6.224 12.057 42.387 1.00 34.24 C +ATOM 1008 C LEU A 242 6.834 11.599 41.071 1.00 35.40 C +ATOM 1009 O LEU A 242 6.844 10.411 40.761 1.00 28.24 O +ATOM 1010 CB LEU A 242 7.324 12.272 43.428 1.00 39.08 C +ATOM 1011 CG LEU A 242 6.945 13.105 44.658 1.00 50.27 C +ATOM 1012 CD1 LEU A 242 8.149 13.235 45.577 1.00 40.92 C +ATOM 1013 CD2 LEU A 242 6.468 14.483 44.227 1.00 54.53 C +ATOM 1014 N ARG A 243 7.318 12.558 40.290 1.00 36.98 N +ATOM 1015 CA ARG A 243 7.960 12.268 39.016 1.00 38.32 C +ATOM 1016 C ARG A 243 9.085 13.270 38.820 1.00 46.23 C +ATOM 1017 O ARG A 243 8.855 14.478 38.802 1.00 58.57 O +ATOM 1018 CB ARG A 243 6.970 12.374 37.852 1.00 38.91 C +ATOM 1019 CG ARG A 243 7.475 11.684 36.597 1.00 36.65 C +ATOM 1020 CD ARG A 243 6.650 12.017 35.373 1.00 50.44 C +ATOM 1021 NE ARG A 243 7.325 11.565 34.159 1.00 47.02 N +ATOM 1022 CZ ARG A 243 6.990 10.476 33.478 1.00 42.93 C +ATOM 1023 NH1 ARG A 243 5.985 9.715 33.884 1.00 24.97 N +ATOM 1024 NH2 ARG A 243 7.669 10.142 32.393 1.00 57.01 N +ATOM 1025 N PRO A 244 10.327 12.776 38.680 1.00 42.99 N +ATOM 1026 CA PRO A 244 11.482 13.660 38.487 1.00 38.60 C +ATOM 1027 C PRO A 244 11.475 14.384 37.140 1.00 46.20 C +ATOM 1028 O PRO A 244 11.559 13.760 36.084 1.00 54.57 O +ATOM 1029 CB PRO A 244 12.679 12.722 38.637 1.00 26.93 C +ATOM 1030 CG PRO A 244 12.152 11.381 38.275 1.00 26.61 C +ATOM 1031 CD PRO A 244 10.714 11.355 38.699 1.00 43.68 C +ATOM 1032 N VAL A 245 11.374 15.709 37.188 1.00 40.08 N +ATOM 1033 CA VAL A 245 11.360 16.524 35.978 1.00 38.82 C +ATOM 1034 C VAL A 245 12.760 17.073 35.719 1.00 44.01 C +ATOM 1035 O VAL A 245 13.454 17.481 36.651 1.00 36.98 O +ATOM 1036 CB VAL A 245 10.364 17.708 36.115 1.00 37.07 C +ATOM 1037 CG1 VAL A 245 10.943 18.784 37.020 1.00 38.19 C +ATOM 1038 CG2 VAL A 245 10.041 18.279 34.752 1.00 39.24 C +ATOM 1039 N ALA A 246 13.173 17.080 34.456 1.00 54.02 N +ATOM 1040 CA ALA A 246 14.489 17.589 34.088 1.00 57.88 C +ATOM 1041 C ALA A 246 14.769 18.920 34.787 1.00 60.78 C +ATOM 1042 O ALA A 246 15.664 19.015 35.627 1.00 67.19 O +ATOM 1043 CB ALA A 246 14.571 17.763 32.579 1.00 77.71 C +ATOM 1044 N GLY A 247 13.992 19.940 34.437 1.00 52.89 N +ATOM 1045 CA GLY A 247 14.163 21.251 35.037 1.00 62.98 C +ATOM 1046 C GLY A 247 12.835 21.965 35.205 1.00 67.72 C +ATOM 1047 O GLY A 247 12.324 22.099 36.318 1.00 80.51 O +ATOM 1048 N LEU A 248 12.274 22.421 34.091 1.00 65.11 N +ATOM 1049 CA LEU A 248 10.998 23.126 34.098 1.00 56.05 C +ATOM 1050 C LEU A 248 10.159 22.668 32.911 1.00 61.16 C +ATOM 1051 O LEU A 248 10.671 22.027 31.992 1.00 74.12 O +ATOM 1052 CB LEU A 248 11.234 24.637 34.012 1.00 59.12 C +ATOM 1053 CG LEU A 248 11.497 25.237 32.626 1.00 79.70 C +ATOM 1054 CD1 LEU A 248 11.429 26.749 32.712 1.00 87.18 C +ATOM 1055 CD2 LEU A 248 12.850 24.785 32.111 1.00 72.88 C +ATOM 1056 N LEU A 249 8.871 22.989 32.934 1.00 46.27 N +ATOM 1057 CA LEU A 249 7.977 22.623 31.842 1.00 45.65 C +ATOM 1058 C LEU A 249 6.771 23.550 31.775 1.00 47.53 C +ATOM 1059 O LEU A 249 6.452 24.240 32.739 1.00 50.63 O +ATOM 1060 CB LEU A 249 7.506 21.172 31.976 1.00 32.93 C +ATOM 1061 CG LEU A 249 7.514 20.481 33.336 1.00 37.61 C +ATOM 1062 CD1 LEU A 249 6.701 21.274 34.337 1.00 47.51 C +ATOM 1063 CD2 LEU A 249 6.950 19.084 33.169 1.00 20.77 C +ATOM 1064 N SER A 250 6.114 23.569 30.621 1.00 49.94 N +ATOM 1065 CA SER A 250 4.951 24.417 30.398 1.00 58.56 C +ATOM 1066 C SER A 250 3.888 24.248 31.481 1.00 61.47 C +ATOM 1067 O SER A 250 3.831 23.215 32.148 1.00 66.63 O +ATOM 1068 CB SER A 250 4.348 24.105 29.025 1.00 56.40 C +ATOM 1069 OG SER A 250 3.095 24.739 28.854 1.00 80.26 O +ATOM 1070 N SER A 251 3.052 25.269 31.657 1.00 57.53 N +ATOM 1071 CA SER A 251 1.987 25.218 32.650 1.00 45.91 C +ATOM 1072 C SER A 251 1.015 24.131 32.239 1.00 41.98 C +ATOM 1073 O SER A 251 0.457 23.428 33.080 1.00 47.44 O +ATOM 1074 CB SER A 251 1.252 26.554 32.717 1.00 59.78 C +ATOM 1075 OG SER A 251 2.157 27.639 32.622 1.00 81.13 O +ATOM 1076 N ARG A 252 0.818 24.004 30.932 1.00 30.74 N +ATOM 1077 CA ARG A 252 -0.081 23.000 30.384 1.00 31.41 C +ATOM 1078 C ARG A 252 0.420 21.607 30.739 1.00 23.75 C +ATOM 1079 O ARG A 252 -0.362 20.725 31.087 1.00 34.67 O +ATOM 1080 CB ARG A 252 -0.170 23.143 28.865 1.00 35.53 C +ATOM 1081 CG ARG A 252 -1.028 22.085 28.192 1.00 53.82 C +ATOM 1082 CD ARG A 252 -1.061 22.280 26.687 1.00 46.69 C +ATOM 1083 NE ARG A 252 -1.599 23.586 26.319 1.00 40.65 N +ATOM 1084 CZ ARG A 252 -2.881 23.922 26.419 1.00 48.03 C +ATOM 1085 NH1 ARG A 252 -3.765 23.048 26.879 1.00 44.01 N +ATOM 1086 NH2 ARG A 252 -3.281 25.132 26.058 1.00 50.32 N +ATOM 1087 N ASP A 253 1.732 21.418 30.648 1.00 16.34 N +ATOM 1088 CA ASP A 253 2.348 20.128 30.958 1.00 28.42 C +ATOM 1089 C ASP A 253 2.353 19.853 32.453 1.00 29.16 C +ATOM 1090 O ASP A 253 2.029 18.752 32.895 1.00 33.43 O +ATOM 1091 CB ASP A 253 3.778 20.091 30.425 1.00 46.51 C +ATOM 1092 CG ASP A 253 3.839 20.249 28.923 1.00 73.75 C +ATOM 1093 OD1 ASP A 253 3.678 21.386 28.432 1.00 70.20 O +ATOM 1094 OD2 ASP A 253 4.045 19.232 28.232 1.00 82.65 O +ATOM 1095 N PHE A 254 2.736 20.860 33.225 1.00 36.90 N +ATOM 1096 CA PHE A 254 2.772 20.741 34.672 1.00 47.73 C +ATOM 1097 C PHE A 254 1.372 20.375 35.161 1.00 53.70 C +ATOM 1098 O PHE A 254 1.170 19.324 35.772 1.00 62.08 O +ATOM 1099 CB PHE A 254 3.210 22.070 35.291 1.00 58.44 C +ATOM 1100 CG PHE A 254 3.632 21.970 36.730 1.00 64.83 C +ATOM 1101 CD1 PHE A 254 3.566 20.759 37.415 1.00 76.33 C +ATOM 1102 CD2 PHE A 254 4.099 23.096 37.403 1.00 86.07 C +ATOM 1103 CE1 PHE A 254 3.954 20.673 38.750 1.00 86.30 C +ATOM 1104 CE2 PHE A 254 4.491 23.020 38.741 1.00100.00 C +ATOM 1105 CZ PHE A 254 4.419 21.807 39.414 1.00 95.87 C +ATOM 1106 N LEU A 255 0.411 21.249 34.880 1.00 40.62 N +ATOM 1107 CA LEU A 255 -0.969 21.037 35.283 1.00 29.53 C +ATOM 1108 C LEU A 255 -1.497 19.693 34.803 1.00 35.98 C +ATOM 1109 O LEU A 255 -2.260 19.033 35.508 1.00 44.56 O +ATOM 1110 CB LEU A 255 -1.841 22.166 34.739 1.00 37.30 C +ATOM 1111 CG LEU A 255 -1.898 23.438 35.595 1.00 31.39 C +ATOM 1112 CD1 LEU A 255 -0.602 23.622 36.351 1.00 20.93 C +ATOM 1113 CD2 LEU A 255 -2.174 24.633 34.707 1.00 19.28 C +ATOM 1114 N GLY A 256 -1.089 19.288 33.605 1.00 23.82 N +ATOM 1115 CA GLY A 256 -1.541 18.019 33.064 1.00 22.93 C +ATOM 1116 C GLY A 256 -1.191 16.845 33.961 1.00 27.16 C +ATOM 1117 O GLY A 256 -1.919 15.853 34.022 1.00 13.49 O +ATOM 1118 N GLY A 257 -0.071 16.951 34.665 1.00 21.45 N +ATOM 1119 CA GLY A 257 0.334 15.878 35.549 1.00 40.44 C +ATOM 1120 C GLY A 257 -0.604 15.773 36.733 1.00 40.36 C +ATOM 1121 O GLY A 257 -0.908 14.684 37.208 1.00 47.80 O +ATOM 1122 N LEU A 258 -1.067 16.922 37.207 1.00 40.24 N +ATOM 1123 CA LEU A 258 -1.972 16.979 38.346 1.00 34.55 C +ATOM 1124 C LEU A 258 -3.256 16.189 38.107 1.00 24.30 C +ATOM 1125 O LEU A 258 -3.851 15.670 39.047 1.00 33.84 O +ATOM 1126 CB LEU A 258 -2.298 18.445 38.678 1.00 35.00 C +ATOM 1127 CG LEU A 258 -1.083 19.362 38.906 1.00 41.25 C +ATOM 1128 CD1 LEU A 258 -1.519 20.823 38.867 1.00 31.39 C +ATOM 1129 CD2 LEU A 258 -0.422 19.025 40.234 1.00 28.27 C +ATOM 1130 N ALA A 259 -3.678 16.100 36.851 1.00 13.11 N +ATOM 1131 CA ALA A 259 -4.896 15.379 36.502 1.00 16.98 C +ATOM 1132 C ALA A 259 -4.786 13.910 36.865 1.00 19.95 C +ATOM 1133 O ALA A 259 -5.793 13.209 36.948 1.00 33.25 O +ATOM 1134 CB ALA A 259 -5.181 15.523 35.022 1.00 17.11 C +ATOM 1135 N PHE A 260 -3.558 13.445 37.076 1.00 17.10 N +ATOM 1136 CA PHE A 260 -3.315 12.047 37.423 1.00 29.31 C +ATOM 1137 C PHE A 260 -2.744 11.957 38.823 1.00 25.66 C +ATOM 1138 O PHE A 260 -2.286 10.894 39.246 1.00 36.30 O +ATOM 1139 CB PHE A 260 -2.328 11.412 36.441 1.00 17.78 C +ATOM 1140 CG PHE A 260 -2.717 11.573 35.010 1.00 15.54 C +ATOM 1141 CD1 PHE A 260 -2.506 12.781 34.353 1.00 23.61 C +ATOM 1142 CD2 PHE A 260 -3.310 10.528 34.322 1.00 9.20 C +ATOM 1143 CE1 PHE A 260 -2.883 12.949 33.028 1.00 19.04 C +ATOM 1144 CE2 PHE A 260 -3.690 10.684 32.996 1.00 28.72 C +ATOM 1145 CZ PHE A 260 -3.475 11.898 32.346 1.00 32.54 C +ATOM 1146 N ARG A 261 -2.775 13.080 39.534 1.00 30.74 N +ATOM 1147 CA ARG A 261 -2.246 13.150 40.890 1.00 30.16 C +ATOM 1148 C ARG A 261 -0.763 12.820 40.842 1.00 28.65 C +ATOM 1149 O ARG A 261 -0.241 12.094 41.689 1.00 34.80 O +ATOM 1150 CB ARG A 261 -2.985 12.172 41.805 1.00 30.66 C +ATOM 1151 CG ARG A 261 -4.447 12.519 41.996 1.00 32.76 C +ATOM 1152 CD ARG A 261 -4.968 12.096 43.353 1.00 39.38 C +ATOM 1153 NE ARG A 261 -6.403 12.351 43.458 1.00 47.15 N +ATOM 1154 CZ ARG A 261 -7.078 12.453 44.598 1.00 30.86 C +ATOM 1155 NH1 ARG A 261 -6.463 12.307 45.762 1.00 48.34 N +ATOM 1156 NH2 ARG A 261 -8.379 12.697 44.570 1.00 31.94 N +ATOM 1157 N VAL A 262 -0.106 13.363 39.819 1.00 21.99 N +ATOM 1158 CA VAL A 262 1.323 13.176 39.599 1.00 24.05 C +ATOM 1159 C VAL A 262 2.006 14.537 39.676 1.00 29.44 C +ATOM 1160 O VAL A 262 1.625 15.475 38.968 1.00 27.93 O +ATOM 1161 CB VAL A 262 1.608 12.557 38.210 1.00 11.44 C +ATOM 1162 CG1 VAL A 262 3.078 12.659 37.883 1.00 21.40 C +ATOM 1163 CG2 VAL A 262 1.163 11.099 38.184 1.00 29.17 C +ATOM 1164 N PHE A 263 3.011 14.643 40.542 1.00 40.09 N +ATOM 1165 CA PHE A 263 3.742 15.892 40.717 1.00 42.03 C +ATOM 1166 C PHE A 263 5.134 15.815 40.094 1.00 47.79 C +ATOM 1167 O PHE A 263 5.911 14.907 40.393 1.00 49.00 O +ATOM 1168 CB PHE A 263 3.860 16.228 42.206 1.00 28.47 C +ATOM 1169 CG PHE A 263 4.388 17.607 42.476 1.00 32.77 C +ATOM 1170 CD1 PHE A 263 3.850 18.715 41.824 1.00 52.86 C +ATOM 1171 CD2 PHE A 263 5.426 17.800 43.381 1.00 25.50 C +ATOM 1172 CE1 PHE A 263 4.339 19.994 42.070 1.00 46.81 C +ATOM 1173 CE2 PHE A 263 5.923 19.074 43.635 1.00 42.05 C +ATOM 1174 CZ PHE A 263 5.378 20.174 42.977 1.00 54.09 C +ATOM 1175 N HIS A 264 5.444 16.766 39.219 1.00 50.29 N +ATOM 1176 CA HIS A 264 6.747 16.796 38.570 1.00 55.68 C +ATOM 1177 C HIS A 264 7.709 17.534 39.486 1.00 54.21 C +ATOM 1178 O HIS A 264 7.685 18.759 39.591 1.00 66.04 O +ATOM 1179 CB HIS A 264 6.632 17.476 37.203 1.00 60.80 C +ATOM 1180 CG HIS A 264 5.915 16.646 36.186 1.00 53.37 C +ATOM 1181 ND1 HIS A 264 6.573 15.898 35.236 1.00 58.65 N +ATOM 1182 CD2 HIS A 264 4.593 16.402 36.005 1.00 56.24 C +ATOM 1183 CE1 HIS A 264 5.689 15.229 34.513 1.00 37.58 C +ATOM 1184 NE2 HIS A 264 4.485 15.519 34.961 1.00 49.84 N +ATOM 1185 N CYS A 265 8.555 16.762 40.158 1.00 52.29 N +ATOM 1186 CA CYS A 265 9.513 17.303 41.114 1.00 59.81 C +ATOM 1187 C CYS A 265 10.958 17.343 40.620 1.00 60.63 C +ATOM 1188 O CYS A 265 11.368 16.548 39.770 1.00 62.02 O +ATOM 1189 CB CYS A 265 9.431 16.487 42.408 1.00 56.39 C +ATOM 1190 SG CYS A 265 10.530 17.011 43.732 1.00 81.80 S +ATOM 1191 N THR A 266 11.717 18.290 41.168 1.00 57.33 N +ATOM 1192 CA THR A 266 13.128 18.470 40.836 1.00 54.19 C +ATOM 1193 C THR A 266 13.977 17.704 41.852 1.00 45.74 C +ATOM 1194 O THR A 266 13.806 17.862 43.060 1.00 43.17 O +ATOM 1195 CB THR A 266 13.531 19.962 40.886 1.00 60.72 C +ATOM 1196 OG1 THR A 266 13.574 20.404 42.249 1.00 48.14 O +ATOM 1197 CG2 THR A 266 12.531 20.809 40.116 1.00 67.40 C +ATOM 1198 N GLN A 267 14.889 16.875 41.357 1.00 52.16 N +ATOM 1199 CA GLN A 267 15.749 16.087 42.227 1.00 44.22 C +ATOM 1200 C GLN A 267 16.982 16.864 42.671 1.00 45.27 C +ATOM 1201 O GLN A 267 17.602 16.526 43.676 1.00 34.83 O +ATOM 1202 CB GLN A 267 16.182 14.810 41.509 1.00 36.86 C +ATOM 1203 CG GLN A 267 17.054 13.902 42.347 1.00 27.09 C +ATOM 1204 CD GLN A 267 16.531 12.475 42.397 1.00 50.69 C +ATOM 1205 OE1 GLN A 267 16.316 11.843 41.359 1.00 43.07 O +ATOM 1206 NE2 GLN A 267 16.329 11.958 43.609 1.00 54.57 N +ATOM 1207 N TYR A 268 17.328 17.910 41.924 1.00 39.74 N +ATOM 1208 CA TYR A 268 18.501 18.720 42.234 1.00 41.65 C +ATOM 1209 C TYR A 268 18.311 19.730 43.365 1.00 44.54 C +ATOM 1210 O TYR A 268 17.262 19.773 44.009 1.00 42.77 O +ATOM 1211 CB TYR A 268 19.003 19.430 40.967 1.00 47.36 C +ATOM 1212 CG TYR A 268 18.031 20.406 40.339 1.00 47.68 C +ATOM 1213 CD1 TYR A 268 17.924 21.714 40.812 1.00 41.55 C +ATOM 1214 CD2 TYR A 268 17.255 20.037 39.241 1.00 64.94 C +ATOM 1215 CE1 TYR A 268 17.071 22.633 40.206 1.00 32.05 C +ATOM 1216 CE2 TYR A 268 16.398 20.949 38.629 1.00 62.63 C +ATOM 1217 CZ TYR A 268 16.314 22.245 39.115 1.00 42.20 C +ATOM 1218 OH TYR A 268 15.480 23.154 38.501 1.00 37.44 O +ATOM 1219 N ILE A 269 19.341 20.544 43.592 1.00 56.45 N +ATOM 1220 CA ILE A 269 19.323 21.549 44.654 1.00 60.67 C +ATOM 1221 C ILE A 269 20.065 22.829 44.277 1.00 61.55 C +ATOM 1222 O ILE A 269 21.015 22.799 43.499 1.00 65.11 O +ATOM 1223 CB ILE A 269 19.975 21.007 45.933 1.00 50.21 C +ATOM 1224 CG1 ILE A 269 19.954 22.079 47.022 1.00 55.34 C +ATOM 1225 CG2 ILE A 269 21.406 20.589 45.640 1.00 43.33 C +ATOM 1226 CD1 ILE A 269 20.348 21.573 48.384 1.00 70.88 C +ATOM 1227 N ARG A 270 19.633 23.947 44.851 1.00 70.19 N +ATOM 1228 CA ARG A 270 20.251 25.242 44.591 1.00 76.56 C +ATOM 1229 C ARG A 270 21.742 25.175 44.899 1.00 74.71 C +ATOM 1230 O ARG A 270 22.213 24.222 45.520 1.00 68.44 O +ATOM 1231 CB ARG A 270 19.601 26.312 45.467 1.00 84.04 C +ATOM 1232 CG ARG A 270 19.686 26.015 46.956 1.00 85.50 C +ATOM 1233 CD ARG A 270 18.927 27.042 47.769 1.00 88.12 C +ATOM 1234 NE ARG A 270 17.550 26.626 48.010 1.00 82.86 N +ATOM 1235 CZ ARG A 270 16.795 27.089 48.999 1.00 79.01 C +ATOM 1236 NH1 ARG A 270 17.286 27.985 49.842 1.00 74.83 N +ATOM 1237 NH2 ARG A 270 15.550 26.659 49.145 1.00 64.13 N +ATOM 1238 N HIS A 271 22.483 26.188 44.462 1.00 73.45 N +ATOM 1239 CA HIS A 271 23.916 26.225 44.717 1.00 76.37 C +ATOM 1240 C HIS A 271 24.175 26.776 46.110 1.00 80.10 C +ATOM 1241 O HIS A 271 23.508 27.711 46.553 1.00 90.33 O +ATOM 1242 CB HIS A 271 24.639 27.092 43.688 1.00 85.46 C +ATOM 1243 CG HIS A 271 26.130 26.961 43.742 1.00 90.77 C +ATOM 1244 ND1 HIS A 271 26.960 28.016 44.053 1.00 95.04 N +ATOM 1245 CD2 HIS A 271 26.937 25.889 43.558 1.00 89.61 C +ATOM 1246 CE1 HIS A 271 28.215 27.599 44.058 1.00100.00 C +ATOM 1247 NE2 HIS A 271 28.227 26.312 43.760 1.00 89.70 N +ATOM 1248 N GLY A 272 25.156 26.195 46.790 1.00 78.16 N +ATOM 1249 CA GLY A 272 25.487 26.625 48.136 1.00 82.41 C +ATOM 1250 C GLY A 272 25.908 28.074 48.311 1.00 76.80 C +ATOM 1251 O GLY A 272 25.953 28.562 49.440 1.00 83.10 O +ATOM 1252 N SER A 273 26.222 28.769 47.221 1.00 69.09 N +ATOM 1253 CA SER A 273 26.639 30.169 47.324 1.00 68.79 C +ATOM 1254 C SER A 273 25.621 30.981 48.120 1.00 68.32 C +ATOM 1255 O SER A 273 25.972 31.644 49.096 1.00 75.05 O +ATOM 1256 CB SER A 273 26.828 30.783 45.929 1.00 77.85 C +ATOM 1257 OG SER A 273 25.628 30.770 45.176 1.00 83.43 O +ATOM 1258 N LYS A 274 24.363 30.922 47.696 1.00 66.77 N +ATOM 1259 CA LYS A 274 23.287 31.631 48.375 1.00 64.76 C +ATOM 1260 C LYS A 274 22.198 30.632 48.763 1.00 67.12 C +ATOM 1261 O LYS A 274 21.233 30.423 48.028 1.00 66.67 O +ATOM 1262 CB LYS A 274 22.728 32.727 47.465 1.00 68.16 C +ATOM 1263 CG LYS A 274 23.604 33.971 47.414 1.00 79.05 C +ATOM 1264 CD LYS A 274 23.785 34.574 48.803 1.00 94.09 C +ATOM 1265 CE LYS A 274 24.769 35.738 48.788 1.00 96.98 C +ATOM 1266 NZ LYS A 274 25.076 36.232 50.160 1.00100.00 N +ATOM 1267 N PRO A 275 22.353 29.998 49.938 1.00 61.91 N +ATOM 1268 CA PRO A 275 21.414 29.004 50.468 1.00 65.03 C +ATOM 1269 C PRO A 275 20.085 29.589 50.937 1.00 72.40 C +ATOM 1270 O PRO A 275 19.269 28.888 51.537 1.00 89.09 O +ATOM 1271 CB PRO A 275 22.191 28.352 51.610 1.00 60.82 C +ATOM 1272 CG PRO A 275 23.131 29.411 52.064 1.00 76.64 C +ATOM 1273 CD PRO A 275 23.482 30.229 50.854 1.00 72.44 C +ATOM 1274 N MET A 276 19.868 30.871 50.661 1.00 57.47 N +ATOM 1275 CA MET A 276 18.629 31.531 51.056 1.00 67.57 C +ATOM 1276 C MET A 276 17.898 32.077 49.834 1.00 74.14 C +ATOM 1277 O MET A 276 16.976 32.882 49.955 1.00 84.59 O +ATOM 1278 CB MET A 276 18.928 32.669 52.035 1.00 79.90 C +ATOM 1279 CG MET A 276 18.162 32.587 53.349 1.00 82.99 C +ATOM 1280 SD MET A 276 18.343 31.004 54.201 1.00 94.71 S +ATOM 1281 CE MET A 276 16.776 30.240 53.829 1.00100.00 C +ATOM 1282 N TYR A 277 18.309 31.625 48.655 1.00 81.71 N +ATOM 1283 CA TYR A 277 17.688 32.074 47.421 1.00 95.68 C +ATOM 1284 C TYR A 277 17.840 31.066 46.284 1.00 96.34 C +ATOM 1285 O TYR A 277 18.906 30.474 46.096 1.00 94.33 O +ATOM 1286 CB TYR A 277 18.281 33.418 47.000 1.00 92.57 C +ATOM 1287 CG TYR A 277 18.183 33.685 45.518 1.00 98.35 C +ATOM 1288 CD1 TYR A 277 16.971 34.051 44.939 1.00100.00 C +ATOM 1289 CD2 TYR A 277 19.300 33.562 44.691 1.00 93.13 C +ATOM 1290 CE1 TYR A 277 16.872 34.289 43.572 1.00 95.63 C +ATOM 1291 CE2 TYR A 277 19.213 33.797 43.324 1.00 94.92 C +ATOM 1292 CZ TYR A 277 17.996 34.161 42.771 1.00 95.01 C +ATOM 1293 OH TYR A 277 17.908 34.406 41.419 1.00 91.12 O +ATOM 1294 N THR A 278 16.759 30.882 45.532 1.00 86.12 N +ATOM 1295 CA THR A 278 16.743 29.970 44.393 1.00 75.54 C +ATOM 1296 C THR A 278 15.967 30.632 43.262 1.00 72.73 C +ATOM 1297 O THR A 278 14.854 31.113 43.458 1.00 73.03 O +ATOM 1298 CB THR A 278 16.074 28.630 44.745 1.00 82.17 C +ATOM 1299 OG1 THR A 278 16.356 28.303 46.112 1.00 98.31 O +ATOM 1300 CG2 THR A 278 16.609 27.533 43.847 1.00 85.64 C +ATOM 1301 N PRO A 279 16.544 30.655 42.054 1.00 78.92 N +ATOM 1302 CA PRO A 279 15.875 31.277 40.908 1.00 76.69 C +ATOM 1303 C PRO A 279 14.781 30.400 40.318 1.00 70.76 C +ATOM 1304 O PRO A 279 14.047 30.815 39.425 1.00 64.88 O +ATOM 1305 CB PRO A 279 17.010 31.516 39.923 1.00 69.92 C +ATOM 1306 CG PRO A 279 18.006 30.444 40.236 1.00 82.58 C +ATOM 1307 CD PRO A 279 17.841 30.065 41.686 1.00 84.25 C +ATOM 1308 N GLU A 280 14.674 29.181 40.838 1.00 68.53 N +ATOM 1309 CA GLU A 280 13.677 28.234 40.368 1.00 69.05 C +ATOM 1310 C GLU A 280 13.519 27.087 41.361 1.00 63.34 C +ATOM 1311 O GLU A 280 14.321 26.935 42.275 1.00 60.75 O +ATOM 1312 CB GLU A 280 14.088 27.702 38.993 1.00 74.71 C +ATOM 1313 CG GLU A 280 15.044 26.532 39.064 1.00 78.89 C +ATOM 1314 CD GLU A 280 16.491 26.970 39.085 1.00 76.97 C +ATOM 1315 OE1 GLU A 280 16.984 27.439 38.041 1.00 74.45 O +ATOM 1316 OE2 GLU A 280 17.139 26.845 40.142 1.00 77.77 O +ATOM 1317 N PRO A 281 12.493 26.239 41.164 1.00 59.44 N +ATOM 1318 CA PRO A 281 12.254 25.109 42.072 1.00 57.60 C +ATOM 1319 C PRO A 281 13.405 24.126 42.245 1.00 49.97 C +ATOM 1320 O PRO A 281 13.968 23.634 41.272 1.00 53.11 O +ATOM 1321 CB PRO A 281 11.017 24.427 41.488 1.00 51.17 C +ATOM 1322 CG PRO A 281 10.425 25.410 40.544 1.00 70.63 C +ATOM 1323 CD PRO A 281 11.533 26.268 40.049 1.00 59.40 C +ATOM 1324 N ASP A 282 13.735 23.843 43.503 1.00 45.57 N +ATOM 1325 CA ASP A 282 14.792 22.898 43.868 1.00 43.57 C +ATOM 1326 C ASP A 282 14.183 21.916 44.861 1.00 36.46 C +ATOM 1327 O ASP A 282 13.079 22.144 45.351 1.00 47.96 O +ATOM 1328 CB ASP A 282 15.966 23.628 44.518 1.00 55.07 C +ATOM 1329 CG ASP A 282 15.648 24.114 45.920 1.00 67.89 C +ATOM 1330 OD1 ASP A 282 16.529 24.003 46.800 1.00 65.08 O +ATOM 1331 OD2 ASP A 282 14.521 24.605 46.141 1.00 75.95 O +ATOM 1332 N ILE A 283 14.895 20.837 45.170 1.00 33.07 N +ATOM 1333 CA ILE A 283 14.373 19.831 46.097 1.00 45.55 C +ATOM 1334 C ILE A 283 13.895 20.380 47.449 1.00 52.96 C +ATOM 1335 O ILE A 283 13.236 19.675 48.219 1.00 56.77 O +ATOM 1336 CB ILE A 283 15.407 18.719 46.369 1.00 42.94 C +ATOM 1337 CG1 ILE A 283 14.702 17.509 46.999 1.00 52.36 C +ATOM 1338 CG2 ILE A 283 16.511 19.244 47.278 1.00 38.58 C +ATOM 1339 CD1 ILE A 283 15.455 16.199 46.851 1.00 55.61 C +ATOM 1340 N CYS A 284 14.226 21.633 47.741 1.00 51.82 N +ATOM 1341 CA CYS A 284 13.803 22.250 48.991 1.00 56.36 C +ATOM 1342 C CYS A 284 12.407 22.824 48.804 1.00 54.65 C +ATOM 1343 O CYS A 284 11.514 22.594 49.618 1.00 67.24 O +ATOM 1344 CB CYS A 284 14.774 23.364 49.388 1.00 74.89 C +ATOM 1345 SG CYS A 284 16.518 22.892 49.344 1.00 99.53 S +ATOM 1346 N HIS A 285 12.226 23.571 47.721 1.00 62.12 N +ATOM 1347 CA HIS A 285 10.936 24.176 47.418 1.00 64.94 C +ATOM 1348 C HIS A 285 9.874 23.095 47.251 1.00 59.74 C +ATOM 1349 O HIS A 285 8.764 23.213 47.769 1.00 64.62 O +ATOM 1350 CB HIS A 285 11.047 25.016 46.142 1.00 61.21 C +ATOM 1351 CG HIS A 285 9.730 25.349 45.513 1.00 76.62 C +ATOM 1352 ND1 HIS A 285 8.955 26.411 45.925 1.00 93.00 N +ATOM 1353 CD2 HIS A 285 9.068 24.773 44.484 1.00 87.22 C +ATOM 1354 CE1 HIS A 285 7.870 26.476 45.175 1.00100.00 C +ATOM 1355 NE2 HIS A 285 7.913 25.494 44.293 1.00 99.45 N +ATOM 1356 N GLU A 286 10.232 22.033 46.541 1.00 52.73 N +ATOM 1357 CA GLU A 286 9.312 20.934 46.286 1.00 57.66 C +ATOM 1358 C GLU A 286 8.987 20.109 47.525 1.00 60.34 C +ATOM 1359 O GLU A 286 7.834 19.728 47.732 1.00 77.83 O +ATOM 1360 CB GLU A 286 9.882 20.012 45.205 1.00 61.13 C +ATOM 1361 CG GLU A 286 10.533 20.741 44.046 1.00 76.30 C +ATOM 1362 CD GLU A 286 9.545 21.127 42.964 1.00 85.35 C +ATOM 1363 OE1 GLU A 286 9.383 20.351 42.000 1.00 72.35 O +ATOM 1364 OE2 GLU A 286 8.934 22.209 43.070 1.00 88.17 O +ATOM 1365 N LEU A 287 10.000 19.838 48.346 1.00 48.09 N +ATOM 1366 CA LEU A 287 9.815 19.033 49.557 1.00 60.37 C +ATOM 1367 C LEU A 287 9.349 19.809 50.794 1.00 62.26 C +ATOM 1368 O LEU A 287 8.495 19.335 51.545 1.00 60.64 O +ATOM 1369 CB LEU A 287 11.107 18.287 49.893 1.00 55.75 C +ATOM 1370 CG LEU A 287 11.452 17.036 49.077 1.00 61.06 C +ATOM 1371 CD1 LEU A 287 12.622 16.323 49.734 1.00 59.23 C +ATOM 1372 CD2 LEU A 287 10.250 16.110 48.989 1.00 40.81 C +ATOM 1373 N LEU A 288 9.913 20.993 51.007 1.00 60.18 N +ATOM 1374 CA LEU A 288 9.544 21.819 52.153 1.00 54.52 C +ATOM 1375 C LEU A 288 8.560 22.911 51.736 1.00 63.82 C +ATOM 1376 O LEU A 288 8.535 23.994 52.323 1.00 73.18 O +ATOM 1377 CB LEU A 288 10.794 22.464 52.769 1.00 56.91 C +ATOM 1378 CG LEU A 288 11.972 21.546 53.108 1.00 46.12 C +ATOM 1379 CD1 LEU A 288 13.191 22.381 53.463 1.00 35.10 C +ATOM 1380 CD2 LEU A 288 11.588 20.630 54.250 1.00 36.21 C +ATOM 1381 N GLY A 289 7.752 22.624 50.721 1.00 69.02 N +ATOM 1382 CA GLY A 289 6.789 23.604 50.259 1.00 74.13 C +ATOM 1383 C GLY A 289 5.558 22.990 49.631 1.00 66.63 C +ATOM 1384 O GLY A 289 4.439 23.246 50.072 1.00 81.62 O +ATOM 1385 N HIS A 290 5.764 22.178 48.599 1.00 50.97 N +ATOM 1386 CA HIS A 290 4.663 21.530 47.896 1.00 46.50 C +ATOM 1387 C HIS A 290 4.200 20.229 48.556 1.00 50.67 C +ATOM 1388 O HIS A 290 3.036 20.095 48.937 1.00 50.37 O +ATOM 1389 CB HIS A 290 5.069 21.240 46.449 1.00 52.24 C +ATOM 1390 CG HIS A 290 4.970 22.428 45.541 1.00 62.48 C +ATOM 1391 ND1 HIS A 290 3.813 22.762 44.873 1.00 64.94 N +ATOM 1392 CD2 HIS A 290 5.892 23.356 45.188 1.00 49.65 C +ATOM 1393 CE1 HIS A 290 4.023 23.845 44.146 1.00 64.48 C +ATOM 1394 NE2 HIS A 290 5.276 24.226 44.320 1.00 54.47 N +ATOM 1395 N VAL A 291 5.121 19.275 48.683 1.00 51.67 N +ATOM 1396 CA VAL A 291 4.838 17.962 49.265 1.00 60.23 C +ATOM 1397 C VAL A 291 3.882 17.916 50.462 1.00 63.65 C +ATOM 1398 O VAL A 291 2.890 17.187 50.436 1.00 66.68 O +ATOM 1399 CB VAL A 291 6.155 17.248 49.658 1.00 68.66 C +ATOM 1400 CG1 VAL A 291 5.861 15.938 50.377 1.00 51.75 C +ATOM 1401 CG2 VAL A 291 6.982 16.984 48.417 1.00 59.30 C +ATOM 1402 N PRO A 292 4.164 18.696 51.525 1.00 56.06 N +ATOM 1403 CA PRO A 292 3.269 18.662 52.691 1.00 52.02 C +ATOM 1404 C PRO A 292 1.803 18.953 52.383 1.00 48.25 C +ATOM 1405 O PRO A 292 0.916 18.467 53.075 1.00 55.38 O +ATOM 1406 CB PRO A 292 3.867 19.696 53.649 1.00 50.93 C +ATOM 1407 CG PRO A 292 5.256 19.914 53.177 1.00 66.89 C +ATOM 1408 CD PRO A 292 5.273 19.645 51.705 1.00 48.46 C +ATOM 1409 N LEU A 293 1.550 19.746 51.348 1.00 45.32 N +ATOM 1410 CA LEU A 293 0.181 20.079 50.982 1.00 40.66 C +ATOM 1411 C LEU A 293 -0.445 18.946 50.188 1.00 44.90 C +ATOM 1412 O LEU A 293 -1.643 18.695 50.297 1.00 48.65 O +ATOM 1413 CB LEU A 293 0.150 21.367 50.155 1.00 39.05 C +ATOM 1414 CG LEU A 293 0.119 22.680 50.944 1.00 46.07 C +ATOM 1415 CD1 LEU A 293 -0.999 22.650 51.973 1.00 37.81 C +ATOM 1416 CD2 LEU A 293 1.452 22.890 51.622 1.00 56.64 C +ATOM 1417 N PHE A 294 0.375 18.263 49.393 1.00 40.73 N +ATOM 1418 CA PHE A 294 -0.102 17.153 48.577 1.00 34.87 C +ATOM 1419 C PHE A 294 -0.369 15.915 49.424 1.00 35.06 C +ATOM 1420 O PHE A 294 -0.740 14.867 48.900 1.00 41.72 O +ATOM 1421 CB PHE A 294 0.915 16.817 47.485 1.00 47.10 C +ATOM 1422 CG PHE A 294 0.971 17.827 46.376 1.00 41.71 C +ATOM 1423 CD1 PHE A 294 -0.003 17.853 45.387 1.00 40.38 C +ATOM 1424 CD2 PHE A 294 2.002 18.755 46.322 1.00 34.31 C +ATOM 1425 CE1 PHE A 294 0.049 18.790 44.359 1.00 44.21 C +ATOM 1426 CE2 PHE A 294 2.062 19.696 45.299 1.00 46.58 C +ATOM 1427 CZ PHE A 294 1.083 19.712 44.314 1.00 53.93 C +ATOM 1428 N SER A 295 -0.176 16.039 50.734 1.00 31.86 N +ATOM 1429 CA SER A 295 -0.425 14.925 51.640 1.00 50.78 C +ATOM 1430 C SER A 295 -1.829 15.070 52.214 1.00 49.82 C +ATOM 1431 O SER A 295 -2.368 14.136 52.806 1.00 58.50 O +ATOM 1432 CB SER A 295 0.599 14.916 52.772 1.00 43.11 C +ATOM 1433 OG SER A 295 0.553 16.123 53.509 1.00 79.46 O +ATOM 1434 N ASP A 296 -2.423 16.244 52.005 1.00 41.90 N +ATOM 1435 CA ASP A 296 -3.763 16.535 52.500 1.00 35.45 C +ATOM 1436 C ASP A 296 -4.847 16.144 51.503 1.00 37.03 C +ATOM 1437 O ASP A 296 -4.854 16.590 50.359 1.00 48.53 O +ATOM 1438 CB ASP A 296 -3.891 18.020 52.840 1.00 61.62 C +ATOM 1439 CG ASP A 296 -5.318 18.423 53.168 1.00 66.10 C +ATOM 1440 OD1 ASP A 296 -5.852 17.949 54.194 1.00 74.50 O +ATOM 1441 OD2 ASP A 296 -5.904 19.215 52.397 1.00 62.35 O +ATOM 1442 N ARG A 297 -5.770 15.312 51.971 1.00 36.50 N +ATOM 1443 CA ARG A 297 -6.882 14.811 51.174 1.00 37.44 C +ATOM 1444 C ARG A 297 -7.606 15.857 50.334 1.00 30.30 C +ATOM 1445 O ARG A 297 -7.783 15.681 49.130 1.00 29.10 O +ATOM 1446 CB ARG A 297 -7.893 14.128 52.097 1.00 67.03 C +ATOM 1447 CG ARG A 297 -9.177 13.715 51.413 1.00 76.26 C +ATOM 1448 CD ARG A 297 -8.982 12.421 50.658 1.00 87.04 C +ATOM 1449 NE ARG A 297 -10.199 12.002 49.973 1.00100.00 N +ATOM 1450 CZ ARG A 297 -11.256 11.473 50.580 1.00100.00 C +ATOM 1451 NH1 ARG A 297 -11.252 11.296 51.895 1.00 94.55 N +ATOM 1452 NH2 ARG A 297 -12.319 11.118 49.868 1.00 87.10 N +ATOM 1453 N SER A 298 -8.043 16.931 50.979 1.00 33.65 N +ATOM 1454 CA SER A 298 -8.775 17.989 50.294 1.00 48.80 C +ATOM 1455 C SER A 298 -7.939 18.725 49.255 1.00 55.80 C +ATOM 1456 O SER A 298 -8.447 19.105 48.199 1.00 69.35 O +ATOM 1457 CB SER A 298 -9.329 18.991 51.312 1.00 70.22 C +ATOM 1458 OG SER A 298 -10.117 18.341 52.295 1.00 90.58 O +ATOM 1459 N PHE A 299 -6.658 18.921 49.551 1.00 51.08 N +ATOM 1460 CA PHE A 299 -5.770 19.624 48.629 1.00 47.74 C +ATOM 1461 C PHE A 299 -5.536 18.857 47.326 1.00 45.77 C +ATOM 1462 O PHE A 299 -5.510 19.446 46.244 1.00 48.51 O +ATOM 1463 CB PHE A 299 -4.425 19.914 49.304 1.00 40.10 C +ATOM 1464 CG PHE A 299 -3.520 20.798 48.490 1.00 44.36 C +ATOM 1465 CD1 PHE A 299 -3.424 22.158 48.760 1.00 48.96 C +ATOM 1466 CD2 PHE A 299 -2.776 20.271 47.437 1.00 54.77 C +ATOM 1467 CE1 PHE A 299 -2.602 22.984 47.989 1.00 47.65 C +ATOM 1468 CE2 PHE A 299 -1.952 21.086 46.662 1.00 44.92 C +ATOM 1469 CZ PHE A 299 -1.865 22.445 46.939 1.00 50.64 C +ATOM 1470 N ALA A 300 -5.361 17.544 47.434 1.00 44.41 N +ATOM 1471 CA ALA A 300 -5.125 16.704 46.266 1.00 21.58 C +ATOM 1472 C ALA A 300 -6.244 16.825 45.232 1.00 27.76 C +ATOM 1473 O ALA A 300 -5.984 17.149 44.072 1.00 30.56 O +ATOM 1474 CB ALA A 300 -4.960 15.255 46.696 1.00 28.65 C +ATOM 1475 N GLN A 301 -7.484 16.566 45.648 1.00 19.15 N +ATOM 1476 CA GLN A 301 -8.624 16.655 44.738 1.00 29.43 C +ATOM 1477 C GLN A 301 -8.628 18.031 44.099 1.00 27.53 C +ATOM 1478 O GLN A 301 -8.853 18.172 42.898 1.00 31.56 O +ATOM 1479 CB GLN A 301 -9.933 16.440 45.493 1.00 35.17 C +ATOM 1480 CG GLN A 301 -10.015 15.124 46.232 1.00 61.01 C +ATOM 1481 CD GLN A 301 -11.220 15.066 47.149 1.00 66.46 C +ATOM 1482 OE1 GLN A 301 -11.674 16.091 47.657 1.00 69.57 O +ATOM 1483 NE2 GLN A 301 -11.747 13.868 47.363 1.00 80.16 N +ATOM 1484 N PHE A 302 -8.369 19.041 44.920 1.00 25.62 N +ATOM 1485 CA PHE A 302 -8.319 20.427 44.468 1.00 40.62 C +ATOM 1486 C PHE A 302 -7.313 20.567 43.325 1.00 40.18 C +ATOM 1487 O PHE A 302 -7.646 21.047 42.242 1.00 50.94 O +ATOM 1488 CB PHE A 302 -7.934 21.330 45.648 1.00 46.62 C +ATOM 1489 CG PHE A 302 -7.403 22.682 45.250 1.00 43.28 C +ATOM 1490 CD1 PHE A 302 -7.956 23.391 44.188 1.00 39.76 C +ATOM 1491 CD2 PHE A 302 -6.352 23.255 45.959 1.00 59.26 C +ATOM 1492 CE1 PHE A 302 -7.469 24.646 43.838 1.00 30.38 C +ATOM 1493 CE2 PHE A 302 -5.858 24.509 45.618 1.00 52.72 C +ATOM 1494 CZ PHE A 302 -6.418 25.206 44.556 1.00 53.46 C +ATOM 1495 N SER A 303 -6.079 20.146 43.579 1.00 41.42 N +ATOM 1496 CA SER A 303 -5.027 20.209 42.575 1.00 35.49 C +ATOM 1497 C SER A 303 -5.484 19.483 41.316 1.00 30.28 C +ATOM 1498 O SER A 303 -5.446 20.030 40.216 1.00 40.36 O +ATOM 1499 CB SER A 303 -3.754 19.550 43.111 1.00 41.52 C +ATOM 1500 OG SER A 303 -3.298 20.201 44.284 1.00 55.45 O +ATOM 1501 N GLN A 304 -5.922 18.243 41.494 1.00 2.00 N +ATOM 1502 CA GLN A 304 -6.384 17.421 40.390 1.00 2.00 C +ATOM 1503 C GLN A 304 -7.422 18.124 39.531 1.00 13.01 C +ATOM 1504 O GLN A 304 -7.443 17.954 38.314 1.00 21.06 O +ATOM 1505 CB GLN A 304 -6.971 16.119 40.924 1.00 10.14 C +ATOM 1506 CG GLN A 304 -7.281 15.097 39.845 1.00 17.30 C +ATOM 1507 CD GLN A 304 -7.561 13.725 40.417 1.00 17.68 C +ATOM 1508 OE1 GLN A 304 -7.734 13.572 41.624 1.00 44.51 O +ATOM 1509 NE2 GLN A 304 -7.609 12.715 39.552 1.00 27.72 N +ATOM 1510 N GLU A 305 -8.295 18.897 40.169 1.00 30.55 N +ATOM 1511 CA GLU A 305 -9.335 19.625 39.448 1.00 57.30 C +ATOM 1512 C GLU A 305 -8.684 20.495 38.383 1.00 52.89 C +ATOM 1513 O GLU A 305 -9.063 20.455 37.217 1.00 69.22 O +ATOM 1514 CB GLU A 305 -10.143 20.499 40.412 1.00 68.90 C +ATOM 1515 CG GLU A 305 -11.053 19.723 41.354 1.00 71.26 C +ATOM 1516 CD GLU A 305 -11.967 18.751 40.628 1.00 68.34 C +ATOM 1517 OE1 GLU A 305 -12.053 17.579 41.054 1.00 64.13 O +ATOM 1518 OE2 GLU A 305 -12.600 19.159 39.632 1.00 41.57 O +ATOM 1519 N ILE A 306 -7.701 21.283 38.797 1.00 22.83 N +ATOM 1520 CA ILE A 306 -6.986 22.151 37.875 1.00 23.03 C +ATOM 1521 C ILE A 306 -6.399 21.324 36.732 1.00 35.89 C +ATOM 1522 O ILE A 306 -6.455 21.725 35.568 1.00 35.29 O +ATOM 1523 CB ILE A 306 -5.834 22.889 38.587 1.00 21.44 C +ATOM 1524 CG1 ILE A 306 -6.293 23.367 39.965 1.00 21.06 C +ATOM 1525 CG2 ILE A 306 -5.367 24.055 37.742 1.00 25.83 C +ATOM 1526 CD1 ILE A 306 -5.204 24.028 40.782 1.00 23.91 C +ATOM 1527 N GLY A 307 -5.833 20.169 37.075 1.00 44.29 N +ATOM 1528 CA GLY A 307 -5.251 19.300 36.067 1.00 47.84 C +ATOM 1529 C GLY A 307 -6.288 18.876 35.046 1.00 42.72 C +ATOM 1530 O GLY A 307 -6.061 18.956 33.840 1.00 52.99 O +ATOM 1531 N LEU A 308 -7.440 18.439 35.539 1.00 26.68 N +ATOM 1532 CA LEU A 308 -8.520 18.005 34.675 1.00 24.40 C +ATOM 1533 C LEU A 308 -9.053 19.191 33.879 1.00 20.60 C +ATOM 1534 O LEU A 308 -9.550 19.030 32.768 1.00 32.31 O +ATOM 1535 CB LEU A 308 -9.620 17.378 35.525 1.00 18.68 C +ATOM 1536 CG LEU A 308 -9.160 16.086 36.196 1.00 22.99 C +ATOM 1537 CD1 LEU A 308 -9.675 16.018 37.614 1.00 29.02 C +ATOM 1538 CD2 LEU A 308 -9.655 14.908 35.377 1.00 42.41 C +ATOM 1539 N ALA A 309 -8.935 20.382 34.457 1.00 20.27 N +ATOM 1540 CA ALA A 309 -9.398 21.604 33.807 1.00 32.97 C +ATOM 1541 C ALA A 309 -8.505 21.933 32.619 1.00 38.35 C +ATOM 1542 O ALA A 309 -8.974 22.091 31.491 1.00 61.64 O +ATOM 1543 CB ALA A 309 -9.383 22.759 34.798 1.00 44.37 C +ATOM 1544 N SER A 310 -7.209 22.020 32.889 1.00 45.34 N +ATOM 1545 CA SER A 310 -6.215 22.340 31.873 1.00 43.85 C +ATOM 1546 C SER A 310 -6.170 21.373 30.692 1.00 44.66 C +ATOM 1547 O SER A 310 -5.660 21.718 29.630 1.00 43.51 O +ATOM 1548 CB SER A 310 -4.828 22.406 32.517 1.00 20.23 C +ATOM 1549 OG SER A 310 -4.440 21.135 33.009 1.00 31.77 O +ATOM 1550 N LEU A 311 -6.704 20.168 30.869 1.00 35.50 N +ATOM 1551 CA LEU A 311 -6.674 19.177 29.794 1.00 34.72 C +ATOM 1552 C LEU A 311 -7.368 19.652 28.517 1.00 29.11 C +ATOM 1553 O LEU A 311 -8.599 19.667 28.430 1.00 33.80 O +ATOM 1554 CB LEU A 311 -7.294 17.855 30.269 1.00 34.25 C +ATOM 1555 CG LEU A 311 -6.514 17.088 31.344 1.00 28.71 C +ATOM 1556 CD1 LEU A 311 -7.256 15.820 31.720 1.00 38.96 C +ATOM 1557 CD2 LEU A 311 -5.131 16.754 30.828 1.00 34.55 C +ATOM 1558 N GLY A 312 -6.564 20.042 27.529 1.00 27.51 N +ATOM 1559 CA GLY A 312 -7.101 20.497 26.261 1.00 27.15 C +ATOM 1560 C GLY A 312 -7.631 21.913 26.293 1.00 33.50 C +ATOM 1561 O GLY A 312 -8.263 22.359 25.341 1.00 47.74 O +ATOM 1562 N ALA A 313 -7.370 22.620 27.386 1.00 35.93 N +ATOM 1563 CA ALA A 313 -7.838 23.995 27.534 1.00 42.84 C +ATOM 1564 C ALA A 313 -7.041 24.958 26.661 1.00 49.69 C +ATOM 1565 O ALA A 313 -5.841 24.776 26.456 1.00 39.03 O +ATOM 1566 CB ALA A 313 -7.748 24.419 28.992 1.00 58.23 C +ATOM 1567 N PRO A 314 -7.700 26.009 26.140 1.00 50.08 N +ATOM 1568 CA PRO A 314 -6.990 26.972 25.292 1.00 41.23 C +ATOM 1569 C PRO A 314 -5.987 27.797 26.094 1.00 42.90 C +ATOM 1570 O PRO A 314 -6.208 28.102 27.269 1.00 37.65 O +ATOM 1571 CB PRO A 314 -8.107 27.821 24.687 1.00 37.63 C +ATOM 1572 CG PRO A 314 -9.234 27.708 25.647 1.00 50.98 C +ATOM 1573 CD PRO A 314 -9.120 26.364 26.320 1.00 52.52 C +ATOM 1574 N ASP A 315 -4.885 28.145 25.439 1.00 34.49 N +ATOM 1575 CA ASP A 315 -3.808 28.915 26.055 1.00 49.06 C +ATOM 1576 C ASP A 315 -4.252 29.977 27.061 1.00 51.21 C +ATOM 1577 O ASP A 315 -3.794 29.985 28.202 1.00 56.95 O +ATOM 1578 CB ASP A 315 -2.948 29.563 24.966 1.00 48.54 C +ATOM 1579 CG ASP A 315 -2.394 28.552 23.983 1.00 70.86 C +ATOM 1580 OD1 ASP A 315 -3.128 28.160 23.053 1.00 86.04 O +ATOM 1581 OD2 ASP A 315 -1.226 28.148 24.142 1.00 74.96 O +ATOM 1582 N GLU A 316 -5.136 30.873 26.639 1.00 57.76 N +ATOM 1583 CA GLU A 316 -5.610 31.938 27.520 1.00 63.90 C +ATOM 1584 C GLU A 316 -6.022 31.416 28.883 1.00 54.58 C +ATOM 1585 O GLU A 316 -5.680 32.004 29.905 1.00 63.62 O +ATOM 1586 CB GLU A 316 -6.799 32.674 26.901 1.00 76.14 C +ATOM 1587 CG GLU A 316 -7.902 31.760 26.431 1.00 99.20 C +ATOM 1588 CD GLU A 316 -7.782 31.433 24.959 1.00100.00 C +ATOM 1589 OE1 GLU A 316 -8.819 31.128 24.335 1.00100.00 O +ATOM 1590 OE2 GLU A 316 -6.651 31.483 24.426 1.00 99.33 O +ATOM 1591 N TYR A 317 -6.766 30.317 28.894 1.00 55.07 N +ATOM 1592 CA TYR A 317 -7.227 29.740 30.147 1.00 62.74 C +ATOM 1593 C TYR A 317 -6.131 28.961 30.848 1.00 63.68 C +ATOM 1594 O TYR A 317 -6.111 28.865 32.075 1.00 62.23 O +ATOM 1595 CB TYR A 317 -8.436 28.843 29.895 1.00 62.04 C +ATOM 1596 CG TYR A 317 -9.707 29.630 29.729 1.00 73.80 C +ATOM 1597 CD1 TYR A 317 -10.133 30.035 28.467 1.00 72.45 C +ATOM 1598 CD2 TYR A 317 -10.461 30.012 30.837 1.00 77.85 C +ATOM 1599 CE1 TYR A 317 -11.276 30.808 28.311 1.00 84.03 C +ATOM 1600 CE2 TYR A 317 -11.608 30.785 30.693 1.00 92.79 C +ATOM 1601 CZ TYR A 317 -12.011 31.178 29.428 1.00 92.66 C +ATOM 1602 OH TYR A 317 -13.149 31.938 29.284 1.00 96.95 O +ATOM 1603 N ILE A 318 -5.226 28.390 30.063 1.00 60.35 N +ATOM 1604 CA ILE A 318 -4.113 27.639 30.625 1.00 54.44 C +ATOM 1605 C ILE A 318 -3.306 28.613 31.482 1.00 58.97 C +ATOM 1606 O ILE A 318 -2.974 28.336 32.637 1.00 45.23 O +ATOM 1607 CB ILE A 318 -3.203 27.072 29.509 1.00 35.80 C +ATOM 1608 CG1 ILE A 318 -3.844 25.829 28.889 1.00 44.13 C +ATOM 1609 CG2 ILE A 318 -1.831 26.732 30.069 1.00 50.68 C +ATOM 1610 CD1 ILE A 318 -3.905 24.628 29.814 1.00 43.38 C +ATOM 1611 N GLU A 319 -3.002 29.765 30.893 1.00 63.96 N +ATOM 1612 CA GLU A 319 -2.243 30.807 31.567 1.00 69.66 C +ATOM 1613 C GLU A 319 -3.010 31.317 32.785 1.00 71.97 C +ATOM 1614 O GLU A 319 -2.420 31.611 33.825 1.00 78.92 O +ATOM 1615 CB GLU A 319 -1.970 31.955 30.592 1.00 70.55 C +ATOM 1616 CG GLU A 319 -1.114 33.067 31.162 1.00 87.11 C +ATOM 1617 CD GLU A 319 -1.795 34.418 31.072 1.00 90.13 C +ATOM 1618 OE1 GLU A 319 -1.378 35.238 30.224 1.00 88.14 O +ATOM 1619 OE2 GLU A 319 -2.749 34.656 31.846 1.00100.00 O +ATOM 1620 N LYS A 320 -4.328 31.423 32.642 1.00 71.83 N +ATOM 1621 CA LYS A 320 -5.195 31.880 33.722 1.00 65.51 C +ATOM 1622 C LYS A 320 -5.112 30.914 34.901 1.00 64.01 C +ATOM 1623 O LYS A 320 -5.010 31.335 36.052 1.00 72.70 O +ATOM 1624 CB LYS A 320 -6.645 31.966 33.238 1.00 77.04 C +ATOM 1625 CG LYS A 320 -6.965 33.201 32.415 1.00 87.96 C +ATOM 1626 CD LYS A 320 -8.428 33.214 32.008 1.00 84.41 C +ATOM 1627 CE LYS A 320 -8.781 34.470 31.235 1.00 80.24 C +ATOM 1628 NZ LYS A 320 -10.191 34.441 30.762 1.00 68.82 N +ATOM 1629 N LEU A 321 -5.156 29.614 34.608 1.00 61.92 N +ATOM 1630 CA LEU A 321 -5.075 28.586 35.643 1.00 41.48 C +ATOM 1631 C LEU A 321 -3.718 28.668 36.334 1.00 49.38 C +ATOM 1632 O LEU A 321 -3.631 28.618 37.560 1.00 40.94 O +ATOM 1633 CB LEU A 321 -5.260 27.198 35.031 1.00 28.77 C +ATOM 1634 CG LEU A 321 -6.682 26.829 34.594 1.00 53.73 C +ATOM 1635 CD1 LEU A 321 -6.621 25.756 33.516 1.00 63.28 C +ATOM 1636 CD2 LEU A 321 -7.485 26.343 35.795 1.00 45.22 C +ATOM 1637 N ALA A 322 -2.660 28.789 35.539 1.00 50.27 N +ATOM 1638 CA ALA A 322 -1.317 28.902 36.090 1.00 55.07 C +ATOM 1639 C ALA A 322 -1.321 30.041 37.099 1.00 53.68 C +ATOM 1640 O ALA A 322 -0.887 29.880 38.237 1.00 62.64 O +ATOM 1641 CB ALA A 322 -0.315 29.192 34.983 1.00 71.28 C +ATOM 1642 N THR A 323 -1.829 31.190 36.671 1.00 62.35 N +ATOM 1643 CA THR A 323 -1.903 32.363 37.531 1.00 72.61 C +ATOM 1644 C THR A 323 -2.660 32.043 38.819 1.00 70.34 C +ATOM 1645 O THR A 323 -2.296 32.525 39.894 1.00 85.31 O +ATOM 1646 CB THR A 323 -2.604 33.534 36.815 1.00 77.67 C +ATOM 1647 OG1 THR A 323 -2.084 33.662 35.485 1.00 80.21 O +ATOM 1648 CG2 THR A 323 -2.374 34.834 37.571 1.00 80.45 C +ATOM 1649 N ILE A 324 -3.716 31.239 38.707 1.00 51.98 N +ATOM 1650 CA ILE A 324 -4.503 30.848 39.876 1.00 58.05 C +ATOM 1651 C ILE A 324 -3.628 29.937 40.729 1.00 66.00 C +ATOM 1652 O ILE A 324 -3.511 30.117 41.940 1.00 82.10 O +ATOM 1653 CB ILE A 324 -5.772 30.065 39.477 1.00 63.37 C +ATOM 1654 CG1 ILE A 324 -6.651 30.913 38.557 1.00 66.11 C +ATOM 1655 CG2 ILE A 324 -6.541 29.654 40.726 1.00 49.75 C +ATOM 1656 CD1 ILE A 324 -7.137 32.198 39.190 1.00 76.62 C +ATOM 1657 N TYR A 325 -3.011 28.960 40.073 1.00 63.58 N +ATOM 1658 CA TYR A 325 -2.119 28.003 40.721 1.00 74.13 C +ATOM 1659 C TYR A 325 -1.112 28.755 41.589 1.00 73.28 C +ATOM 1660 O TYR A 325 -0.704 28.284 42.651 1.00 57.45 O +ATOM 1661 CB TYR A 325 -1.394 27.191 39.640 1.00 87.95 C +ATOM 1662 CG TYR A 325 -0.381 26.187 40.142 1.00 94.17 C +ATOM 1663 CD1 TYR A 325 0.966 26.529 40.267 1.00 86.20 C +ATOM 1664 CD2 TYR A 325 -0.760 24.877 40.442 1.00 92.24 C +ATOM 1665 CE1 TYR A 325 1.913 25.590 40.677 1.00 86.39 C +ATOM 1666 CE2 TYR A 325 0.178 23.930 40.852 1.00 87.95 C +ATOM 1667 CZ TYR A 325 1.511 24.293 40.965 1.00 92.56 C +ATOM 1668 OH TYR A 325 2.439 23.354 41.355 1.00100.00 O +ATOM 1669 N TRP A 326 -0.716 29.932 41.121 1.00 71.20 N +ATOM 1670 CA TRP A 326 0.233 30.776 41.827 1.00 76.56 C +ATOM 1671 C TRP A 326 -0.376 31.305 43.118 1.00 79.27 C +ATOM 1672 O TRP A 326 0.061 30.946 44.210 1.00 76.38 O +ATOM 1673 CB TRP A 326 0.638 31.955 40.940 1.00 79.57 C +ATOM 1674 CG TRP A 326 1.838 32.707 41.434 1.00 95.51 C +ATOM 1675 CD1 TRP A 326 1.845 33.802 42.253 1.00 90.06 C +ATOM 1676 CD2 TRP A 326 3.208 32.449 41.102 1.00 97.95 C +ATOM 1677 NE1 TRP A 326 3.132 34.240 42.449 1.00 85.64 N +ATOM 1678 CE2 TRP A 326 3.987 33.427 41.755 1.00 95.89 C +ATOM 1679 CE3 TRP A 326 3.850 31.479 40.317 1.00100.00 C +ATOM 1680 CZ2 TRP A 326 5.383 33.469 41.646 1.00 99.19 C +ATOM 1681 CZ3 TRP A 326 5.240 31.521 40.209 1.00100.00 C +ATOM 1682 CH2 TRP A 326 5.989 32.514 40.869 1.00100.00 C +ATOM 1683 N PHE A 327 -1.387 32.159 42.985 1.00 85.13 N +ATOM 1684 CA PHE A 327 -2.057 32.762 44.136 1.00 88.36 C +ATOM 1685 C PHE A 327 -2.804 31.754 45.006 1.00 85.94 C +ATOM 1686 O PHE A 327 -3.663 32.129 45.805 1.00 91.30 O +ATOM 1687 CB PHE A 327 -3.037 33.842 43.663 1.00 95.87 C +ATOM 1688 CG PHE A 327 -2.369 35.045 43.057 1.00100.00 C +ATOM 1689 CD1 PHE A 327 -1.628 35.921 43.847 1.00 95.08 C +ATOM 1690 CD2 PHE A 327 -2.479 35.309 41.691 1.00 96.10 C +ATOM 1691 CE1 PHE A 327 -1.004 37.033 43.289 1.00100.00 C +ATOM 1692 CE2 PHE A 327 -1.860 36.416 41.122 1.00 83.49 C +ATOM 1693 CZ PHE A 327 -1.119 37.280 41.921 1.00 97.35 C +ATOM 1694 N THR A 328 -2.475 30.477 44.839 1.00 76.73 N +ATOM 1695 CA THR A 328 -3.104 29.414 45.613 1.00 66.80 C +ATOM 1696 C THR A 328 -2.051 28.443 46.107 1.00 62.01 C +ATOM 1697 O THR A 328 -1.643 28.483 47.263 1.00 53.07 O +ATOM 1698 CB THR A 328 -4.143 28.642 44.774 1.00 59.57 C +ATOM 1699 OG1 THR A 328 -3.535 28.160 43.572 1.00 66.06 O +ATOM 1700 CG2 THR A 328 -5.316 29.544 44.422 1.00 61.12 C +ATOM 1701 N VAL A 329 -1.602 27.581 45.204 1.00 68.93 N +ATOM 1702 CA VAL A 329 -0.597 26.571 45.520 1.00 72.84 C +ATOM 1703 C VAL A 329 0.774 27.159 45.821 1.00 71.72 C +ATOM 1704 O VAL A 329 1.427 26.769 46.781 1.00 62.53 O +ATOM 1705 CB VAL A 329 -0.462 25.552 44.355 1.00 74.58 C +ATOM 1706 CG1 VAL A 329 0.551 24.463 44.718 1.00 74.82 C +ATOM 1707 CG2 VAL A 329 -1.822 24.933 44.035 1.00 84.73 C +ATOM 1708 N GLU A 330 1.199 28.101 44.991 1.00 80.14 N +ATOM 1709 CA GLU A 330 2.497 28.736 45.156 1.00 92.46 C +ATOM 1710 C GLU A 330 2.550 29.803 46.245 1.00 96.63 C +ATOM 1711 O GLU A 330 3.339 29.705 47.181 1.00 86.36 O +ATOM 1712 CB GLU A 330 2.949 29.330 43.823 1.00 92.30 C +ATOM 1713 CG GLU A 330 3.317 28.282 42.794 1.00 97.63 C +ATOM 1714 CD GLU A 330 4.639 27.608 43.108 1.00 99.92 C +ATOM 1715 OE1 GLU A 330 5.122 26.825 42.260 1.00100.00 O +ATOM 1716 OE2 GLU A 330 5.196 27.864 44.199 1.00 80.99 O +ATOM 1717 N PHE A 331 1.704 30.821 46.122 1.00100.00 N +ATOM 1718 CA PHE A 331 1.668 31.912 47.093 1.00100.00 C +ATOM 1719 C PHE A 331 0.267 32.206 47.615 1.00100.00 C +ATOM 1720 O PHE A 331 -0.227 33.332 47.512 1.00100.00 O +ATOM 1721 CB PHE A 331 2.253 33.183 46.473 1.00100.00 C +ATOM 1722 CG PHE A 331 3.718 33.087 46.171 1.00100.00 C +ATOM 1723 CD1 PHE A 331 4.163 32.463 45.009 1.00 99.45 C +ATOM 1724 CD2 PHE A 331 4.658 33.609 47.054 1.00100.00 C +ATOM 1725 CE1 PHE A 331 5.524 32.360 44.732 1.00100.00 C +ATOM 1726 CE2 PHE A 331 6.022 33.512 46.786 1.00100.00 C +ATOM 1727 CZ PHE A 331 6.454 32.886 45.622 1.00100.00 C +ATOM 1728 N GLY A 332 -0.376 31.191 48.175 1.00 89.37 N +ATOM 1729 CA GLY A 332 -1.715 31.381 48.693 1.00 80.87 C +ATOM 1730 C GLY A 332 -1.739 31.390 50.205 1.00 82.14 C +ATOM 1731 O GLY A 332 -0.827 30.869 50.850 1.00 75.18 O +ATOM 1732 N LEU A 333 -2.785 31.991 50.766 1.00 90.21 N +ATOM 1733 CA LEU A 333 -2.963 32.064 52.212 1.00 96.85 C +ATOM 1734 C LEU A 333 -4.344 31.513 52.544 1.00 99.83 C +ATOM 1735 O LEU A 333 -5.331 31.865 51.898 1.00 96.81 O +ATOM 1736 CB LEU A 333 -2.849 33.511 52.693 1.00 99.98 C +ATOM 1737 CG LEU A 333 -1.451 34.128 52.604 1.00100.00 C +ATOM 1738 CD1 LEU A 333 -1.514 35.582 53.034 1.00 93.61 C +ATOM 1739 CD2 LEU A 333 -0.484 33.353 53.481 1.00 96.96 C +ATOM 1740 N CYS A 334 -4.417 30.653 53.554 1.00100.00 N +ATOM 1741 CA CYS A 334 -5.691 30.051 53.935 1.00 96.68 C +ATOM 1742 C CYS A 334 -6.319 30.639 55.194 1.00 96.69 C +ATOM 1743 O CYS A 334 -5.752 31.518 55.847 1.00 93.20 O +ATOM 1744 CB CYS A 334 -5.523 28.541 54.118 1.00 89.59 C +ATOM 1745 SG CYS A 334 -4.503 28.069 55.544 1.00 98.82 S +ATOM 1746 N LYS A 335 -7.499 30.125 55.524 1.00 93.07 N +ATOM 1747 CA LYS A 335 -8.252 30.567 56.689 1.00 92.31 C +ATOM 1748 C LYS A 335 -8.249 29.525 57.802 1.00 93.47 C +ATOM 1749 O LYS A 335 -8.699 28.395 57.608 1.00 84.68 O +ATOM 1750 CB LYS A 335 -9.692 30.865 56.283 1.00 92.51 C +ATOM 1751 CG LYS A 335 -9.838 32.102 55.428 1.00 94.20 C +ATOM 1752 CD LYS A 335 -10.683 33.144 56.135 1.00100.00 C +ATOM 1753 CE LYS A 335 -9.825 34.061 56.993 1.00100.00 C +ATOM 1754 NZ LYS A 335 -9.241 33.369 58.179 1.00100.00 N +ATOM 1755 N GLN A 336 -7.751 29.916 58.972 1.00 98.07 N +ATOM 1756 CA GLN A 336 -7.697 29.015 60.119 1.00100.00 C +ATOM 1757 C GLN A 336 -8.427 29.611 61.321 1.00100.00 C +ATOM 1758 O GLN A 336 -7.814 29.929 62.341 1.00100.00 O +ATOM 1759 CB GLN A 336 -6.240 28.719 60.486 1.00100.00 C +ATOM 1760 CG GLN A 336 -5.462 28.008 59.386 1.00 97.01 C +ATOM 1761 CD GLN A 336 -5.703 26.510 59.370 1.00 92.60 C +ATOM 1762 OE1 GLN A 336 -6.254 25.945 60.316 1.00 92.65 O +ATOM 1763 NE2 GLN A 336 -5.285 25.857 58.291 1.00100.00 N +ATOM 1764 N GLY A 337 -9.743 29.748 61.191 1.00100.00 N +ATOM 1765 CA GLY A 337 -10.548 30.311 62.259 1.00 97.11 C +ATOM 1766 C GLY A 337 -10.766 31.795 62.039 1.00 91.62 C +ATOM 1767 O GLY A 337 -11.723 32.203 61.383 1.00 80.53 O +ATOM 1768 N ASP A 338 -9.870 32.607 62.588 1.00 93.19 N +ATOM 1769 CA ASP A 338 -9.958 34.054 62.438 1.00 97.91 C +ATOM 1770 C ASP A 338 -8.681 34.522 61.764 1.00 98.74 C +ATOM 1771 O ASP A 338 -8.690 35.394 60.890 1.00100.00 O +ATOM 1772 CB ASP A 338 -10.079 34.727 63.807 1.00100.00 C +ATOM 1773 CG ASP A 338 -11.382 34.399 64.504 1.00100.00 C +ATOM 1774 OD1 ASP A 338 -12.450 34.673 63.917 1.00100.00 O +ATOM 1775 OD2 ASP A 338 -11.339 33.870 65.635 1.00 88.60 O +ATOM 1776 N SER A 339 -7.582 33.912 62.188 1.00100.00 N +ATOM 1777 CA SER A 339 -6.263 34.233 61.673 1.00100.00 C +ATOM 1778 C SER A 339 -6.014 33.665 60.282 1.00100.00 C +ATOM 1779 O SER A 339 -6.785 32.844 59.779 1.00 81.59 O +ATOM 1780 CB SER A 339 -5.194 33.710 62.635 1.00100.00 C +ATOM 1781 OG SER A 339 -5.404 32.337 62.928 1.00100.00 O +ATOM 1782 N ILE A 340 -4.920 34.115 59.677 1.00100.00 N +ATOM 1783 CA ILE A 340 -4.522 33.675 58.350 1.00100.00 C +ATOM 1784 C ILE A 340 -3.171 32.970 58.410 1.00100.00 C +ATOM 1785 O ILE A 340 -2.237 33.440 59.068 1.00100.00 O +ATOM 1786 CB ILE A 340 -4.426 34.872 57.370 1.00 89.23 C +ATOM 1787 CG1 ILE A 340 -5.706 34.952 56.539 1.00 72.49 C +ATOM 1788 CG2 ILE A 340 -3.207 34.729 56.463 1.00 94.22 C +ATOM 1789 CD1 ILE A 340 -6.901 35.449 57.316 1.00 58.91 C +ATOM 1790 N LYS A 341 -3.079 31.844 57.713 1.00 98.60 N +ATOM 1791 CA LYS A 341 -1.848 31.069 57.663 1.00 96.02 C +ATOM 1792 C LYS A 341 -1.344 30.972 56.226 1.00 99.82 C +ATOM 1793 O LYS A 341 -2.078 31.258 55.274 1.00 96.22 O +ATOM 1794 CB LYS A 341 -2.081 29.666 58.226 1.00 85.54 C +ATOM 1795 CG LYS A 341 -2.294 29.634 59.730 1.00 80.54 C +ATOM 1796 CD LYS A 341 -1.011 29.953 60.473 1.00 85.94 C +ATOM 1797 CE LYS A 341 -1.154 29.699 61.962 1.00 80.46 C +ATOM 1798 NZ LYS A 341 -2.326 30.418 62.527 1.00 92.52 N +ATOM 1799 N ALA A 342 -0.084 30.578 56.074 1.00100.00 N +ATOM 1800 CA ALA A 342 0.513 30.440 54.753 1.00 97.67 C +ATOM 1801 C ALA A 342 0.511 28.977 54.331 1.00100.00 C +ATOM 1802 O ALA A 342 0.977 28.106 55.066 1.00 96.17 O +ATOM 1803 CB ALA A 342 1.940 30.984 54.758 1.00 87.48 C +ATOM 1804 N TYR A 343 -0.029 28.708 53.149 1.00100.00 N +ATOM 1805 CA TYR A 343 -0.082 27.347 52.627 1.00 97.03 C +ATOM 1806 C TYR A 343 0.575 27.294 51.252 1.00 96.93 C +ATOM 1807 O TYR A 343 0.706 26.227 50.653 1.00 90.80 O +ATOM 1808 CB TYR A 343 -1.536 26.860 52.548 1.00 97.91 C +ATOM 1809 CG TYR A 343 -2.316 27.379 51.361 1.00100.00 C +ATOM 1810 CD1 TYR A 343 -3.010 28.586 51.432 1.00100.00 C +ATOM 1811 CD2 TYR A 343 -2.375 26.654 50.172 1.00 95.40 C +ATOM 1812 CE1 TYR A 343 -3.741 29.057 50.345 1.00100.00 C +ATOM 1813 CE2 TYR A 343 -3.102 27.115 49.083 1.00 94.37 C +ATOM 1814 CZ TYR A 343 -3.781 28.316 49.174 1.00100.00 C +ATOM 1815 OH TYR A 343 -4.489 28.779 48.091 1.00100.00 O +ATOM 1816 N GLY A 344 0.985 28.461 50.762 1.00 96.05 N +ATOM 1817 CA GLY A 344 1.637 28.539 49.469 1.00 88.25 C +ATOM 1818 C GLY A 344 2.981 27.837 49.510 1.00 87.24 C +ATOM 1819 O GLY A 344 3.737 27.974 50.478 1.00 70.32 O +ATOM 1820 N ALA A 345 3.279 27.083 48.458 1.00 90.18 N +ATOM 1821 CA ALA A 345 4.533 26.346 48.374 1.00 83.69 C +ATOM 1822 C ALA A 345 5.715 27.293 48.231 1.00 74.01 C +ATOM 1823 O ALA A 345 6.782 27.053 48.793 1.00 65.65 O +ATOM 1824 CB ALA A 345 4.488 25.386 47.203 1.00 88.07 C +ATOM 1825 N GLY A 346 5.521 28.367 47.475 1.00 74.04 N +ATOM 1826 CA GLY A 346 6.582 29.336 47.288 1.00 89.94 C +ATOM 1827 C GLY A 346 6.846 30.099 48.573 1.00 96.50 C +ATOM 1828 O GLY A 346 7.955 30.581 48.804 1.00100.00 O +ATOM 1829 N LEU A 347 5.820 30.208 49.412 1.00100.00 N +ATOM 1830 CA LEU A 347 5.935 30.910 50.687 1.00 97.91 C +ATOM 1831 C LEU A 347 6.681 30.070 51.718 1.00 92.74 C +ATOM 1832 O LEU A 347 7.621 30.536 52.357 1.00 97.68 O +ATOM 1833 CB LEU A 347 4.548 31.239 51.244 1.00 97.57 C +ATOM 1834 CG LEU A 347 3.641 32.170 50.440 1.00 98.60 C +ATOM 1835 CD1 LEU A 347 2.228 32.099 51.004 1.00 97.30 C +ATOM 1836 CD2 LEU A 347 4.179 33.591 50.497 1.00 86.84 C +ATOM 1837 N LEU A 348 6.242 28.827 51.874 1.00 92.32 N +ATOM 1838 CA LEU A 348 6.832 27.905 52.836 1.00 90.82 C +ATOM 1839 C LEU A 348 8.304 27.585 52.606 1.00 85.36 C +ATOM 1840 O LEU A 348 9.042 27.356 53.560 1.00 82.64 O +ATOM 1841 CB LEU A 348 6.019 26.608 52.863 1.00100.00 C +ATOM 1842 CG LEU A 348 4.565 26.809 53.308 1.00100.00 C +ATOM 1843 CD1 LEU A 348 3.693 25.698 52.750 1.00 91.11 C +ATOM 1844 CD2 LEU A 348 4.497 26.855 54.826 1.00 96.11 C +ATOM 1845 N SER A 349 8.728 27.557 51.347 1.00 91.34 N +ATOM 1846 CA SER A 349 10.120 27.256 51.031 1.00 95.94 C +ATOM 1847 C SER A 349 10.990 28.508 51.060 1.00 96.35 C +ATOM 1848 O SER A 349 12.218 28.419 51.069 1.00100.00 O +ATOM 1849 CB SER A 349 10.217 26.596 49.654 1.00 96.27 C +ATOM 1850 OG SER A 349 9.866 27.500 48.619 1.00100.00 O +ATOM 1851 N SER A 350 10.350 29.674 51.078 1.00 90.64 N +ATOM 1852 CA SER A 350 11.072 30.943 51.101 1.00 87.36 C +ATOM 1853 C SER A 350 10.990 31.605 52.473 1.00 92.09 C +ATOM 1854 O SER A 350 9.914 31.992 52.927 1.00 91.76 O +ATOM 1855 CB SER A 350 10.511 31.889 50.040 1.00 83.60 C +ATOM 1856 OG SER A 350 10.765 33.239 50.380 1.00 49.23 O +ATOM 1857 N PHE A 351 12.143 31.741 53.121 1.00100.00 N +ATOM 1858 CA PHE A 351 12.229 32.337 54.451 1.00100.00 C +ATOM 1859 C PHE A 351 11.807 33.804 54.532 1.00 97.44 C +ATOM 1860 O PHE A 351 11.081 34.200 55.442 1.00 91.23 O +ATOM 1861 CB PHE A 351 13.657 32.206 54.989 1.00 95.52 C +ATOM 1862 CG PHE A 351 13.903 32.996 56.243 1.00100.00 C +ATOM 1863 CD1 PHE A 351 13.379 32.571 57.458 1.00100.00 C +ATOM 1864 CD2 PHE A 351 14.643 34.174 56.209 1.00 99.81 C +ATOM 1865 CE1 PHE A 351 13.586 33.305 58.624 1.00100.00 C +ATOM 1866 CE2 PHE A 351 14.856 34.917 57.369 1.00100.00 C +ATOM 1867 CZ PHE A 351 14.326 34.481 58.580 1.00100.00 C +ATOM 1868 N GLY A 352 12.276 34.606 53.583 1.00100.00 N +ATOM 1869 CA GLY A 352 11.959 36.023 53.584 1.00 93.05 C +ATOM 1870 C GLY A 352 10.501 36.382 53.375 1.00 87.07 C +ATOM 1871 O GLY A 352 10.013 37.357 53.942 1.00 85.59 O +ATOM 1872 N GLU A 353 9.799 35.601 52.563 1.00 88.12 N +ATOM 1873 CA GLU A 353 8.394 35.877 52.290 1.00 91.87 C +ATOM 1874 C GLU A 353 7.450 35.189 53.263 1.00 83.67 C +ATOM 1875 O GLU A 353 6.275 35.541 53.352 1.00 74.09 O +ATOM 1876 CB GLU A 353 8.040 35.461 50.866 1.00 96.37 C +ATOM 1877 CG GLU A 353 6.970 36.325 50.229 1.00 78.33 C +ATOM 1878 CD GLU A 353 7.084 36.360 48.722 1.00 91.93 C +ATOM 1879 OE1 GLU A 353 6.188 36.931 48.067 1.00 95.55 O +ATOM 1880 OE2 GLU A 353 8.075 35.818 48.191 1.00 99.96 O +ATOM 1881 N LEU A 354 7.965 34.199 53.980 1.00 84.35 N +ATOM 1882 CA LEU A 354 7.160 33.468 54.947 1.00 94.80 C +ATOM 1883 C LEU A 354 6.716 34.411 56.061 1.00 98.39 C +ATOM 1884 O LEU A 354 5.583 34.341 56.539 1.00 97.83 O +ATOM 1885 CB LEU A 354 7.971 32.309 55.532 1.00100.00 C +ATOM 1886 CG LEU A 354 7.287 31.387 56.545 1.00100.00 C +ATOM 1887 CD1 LEU A 354 5.972 30.851 55.984 1.00100.00 C +ATOM 1888 CD2 LEU A 354 8.236 30.248 56.881 1.00 96.48 C +ATOM 1889 N GLN A 355 7.619 35.297 56.465 1.00100.00 N +ATOM 1890 CA GLN A 355 7.325 36.259 57.517 1.00100.00 C +ATOM 1891 C GLN A 355 6.675 37.520 56.955 1.00 99.16 C +ATOM 1892 O GLN A 355 5.990 38.247 57.675 1.00100.00 O +ATOM 1893 CB GLN A 355 8.611 36.628 58.253 1.00100.00 C +ATOM 1894 CG GLN A 355 9.855 36.610 57.374 1.00 96.38 C +ATOM 1895 CD GLN A 355 11.134 36.643 58.186 1.00100.00 C +ATOM 1896 OE1 GLN A 355 11.983 37.517 58.004 1.00 97.77 O +ATOM 1897 NE2 GLN A 355 11.277 35.684 59.094 1.00100.00 N +ATOM 1898 N TYR A 356 6.886 37.772 55.666 1.00 86.51 N +ATOM 1899 CA TYR A 356 6.324 38.953 55.020 1.00 81.28 C +ATOM 1900 C TYR A 356 4.831 38.835 54.725 1.00 81.58 C +ATOM 1901 O TYR A 356 4.069 39.776 54.943 1.00 79.85 O +ATOM 1902 CB TYR A 356 7.059 39.251 53.715 1.00 92.91 C +ATOM 1903 CG TYR A 356 6.277 40.155 52.786 1.00100.00 C +ATOM 1904 CD1 TYR A 356 5.952 41.456 53.166 1.00100.00 C +ATOM 1905 CD2 TYR A 356 5.851 39.709 51.534 1.00100.00 C +ATOM 1906 CE1 TYR A 356 5.229 42.294 52.324 1.00 99.01 C +ATOM 1907 CE2 TYR A 356 5.126 40.541 50.682 1.00100.00 C +ATOM 1908 CZ TYR A 356 4.819 41.830 51.084 1.00100.00 C +ATOM 1909 OH TYR A 356 4.115 42.658 50.238 1.00100.00 O +ATOM 1910 N CYS A 357 4.424 37.682 54.209 1.00 90.52 N +ATOM 1911 CA CYS A 357 3.027 37.443 53.867 1.00 97.06 C +ATOM 1912 C CYS A 357 2.125 37.404 55.097 1.00100.00 C +ATOM 1913 O CYS A 357 0.915 37.608 54.994 1.00100.00 O +ATOM 1914 CB CYS A 357 2.895 36.124 53.100 1.00100.00 C +ATOM 1915 SG CYS A 357 3.405 34.655 54.038 1.00100.00 S +ATOM 1916 N LEU A 358 2.720 37.149 56.259 1.00 98.65 N +ATOM 1917 CA LEU A 358 1.967 37.064 57.506 1.00 98.17 C +ATOM 1918 C LEU A 358 1.817 38.408 58.216 1.00100.00 C +ATOM 1919 O LEU A 358 1.040 38.533 59.164 1.00100.00 O +ATOM 1920 CB LEU A 358 2.640 36.059 58.444 1.00 88.93 C +ATOM 1921 CG LEU A 358 1.812 34.840 58.871 1.00 80.52 C +ATOM 1922 CD1 LEU A 358 0.728 35.281 59.837 1.00 71.58 C +ATOM 1923 CD2 LEU A 358 1.207 34.159 57.655 1.00 66.00 C +ATOM 1924 N SER A 359 2.550 39.414 57.748 1.00100.00 N +ATOM 1925 CA SER A 359 2.492 40.742 58.352 1.00 98.89 C +ATOM 1926 C SER A 359 1.337 41.589 57.816 1.00100.00 C +ATOM 1927 O SER A 359 0.554 41.137 56.978 1.00100.00 O +ATOM 1928 CB SER A 359 3.817 41.480 58.133 1.00 97.90 C +ATOM 1929 OG SER A 359 4.089 41.655 56.753 1.00 98.54 O +ATOM 1930 N GLU A 360 1.246 42.821 58.309 1.00100.00 N +ATOM 1931 CA GLU A 360 0.195 43.748 57.900 1.00100.00 C +ATOM 1932 C GLU A 360 0.696 44.776 56.890 1.00 97.86 C +ATOM 1933 O GLU A 360 0.388 45.964 56.992 1.00100.00 O +ATOM 1934 CB GLU A 360 -0.375 44.462 59.125 1.00100.00 C +ATOM 1935 CG GLU A 360 -1.314 43.603 59.946 1.00 98.37 C +ATOM 1936 CD GLU A 360 -1.416 44.070 61.381 1.00100.00 C +ATOM 1937 OE1 GLU A 360 -1.756 45.252 61.591 1.00100.00 O +ATOM 1938 OE2 GLU A 360 -1.152 43.259 62.295 1.00100.00 O +ATOM 1939 N LYS A 361 1.470 44.312 55.917 1.00 98.71 N +ATOM 1940 CA LYS A 361 2.004 45.189 54.885 1.00 98.62 C +ATOM 1941 C LYS A 361 1.287 44.958 53.552 1.00100.00 C +ATOM 1942 O LYS A 361 0.924 45.913 52.861 1.00 98.32 O +ATOM 1943 CB LYS A 361 3.510 44.960 54.729 1.00 94.02 C +ATOM 1944 CG LYS A 361 4.298 45.240 56.003 1.00 91.55 C +ATOM 1945 CD LYS A 361 5.800 45.110 55.795 1.00 95.22 C +ATOM 1946 CE LYS A 361 6.560 45.495 57.060 1.00 85.93 C +ATOM 1947 NZ LYS A 361 8.038 45.436 56.883 1.00 81.42 N +ATOM 1948 N PRO A 362 1.052 43.681 53.185 1.00100.00 N +ATOM 1949 CA PRO A 362 0.372 43.358 51.924 1.00100.00 C +ATOM 1950 C PRO A 362 -1.138 43.570 52.022 1.00 97.24 C +ATOM 1951 O PRO A 362 -1.721 43.431 53.097 1.00 98.12 O +ATOM 1952 CB PRO A 362 0.735 41.896 51.695 1.00100.00 C +ATOM 1953 CG PRO A 362 0.912 41.344 53.071 1.00100.00 C +ATOM 1954 CD PRO A 362 1.385 42.466 53.950 1.00100.00 C +ATOM 1955 N LYS A 363 -1.767 43.909 50.899 1.00 95.94 N +ATOM 1956 CA LYS A 363 -3.210 44.139 50.878 1.00 98.30 C +ATOM 1957 C LYS A 363 -3.943 42.861 50.469 1.00 99.01 C +ATOM 1958 O LYS A 363 -4.081 42.555 49.284 1.00100.00 O +ATOM 1959 CB LYS A 363 -3.553 45.286 49.917 1.00 96.33 C +ATOM 1960 CG LYS A 363 -2.891 45.202 48.546 1.00 88.38 C +ATOM 1961 CD LYS A 363 -2.111 46.473 48.218 1.00 87.54 C +ATOM 1962 CE LYS A 363 -2.942 47.729 48.472 1.00 87.32 C +ATOM 1963 NZ LYS A 363 -3.967 47.956 47.418 1.00 93.79 N +ATOM 1964 N LEU A 364 -4.405 42.121 51.472 1.00 98.43 N +ATOM 1965 CA LEU A 364 -5.115 40.864 51.264 1.00 93.80 C +ATOM 1966 C LEU A 364 -6.451 41.026 50.557 1.00 94.63 C +ATOM 1967 O LEU A 364 -7.110 42.061 50.666 1.00 97.05 O +ATOM 1968 CB LEU A 364 -5.356 40.166 52.607 1.00 92.04 C +ATOM 1969 CG LEU A 364 -4.148 39.760 53.457 1.00 89.85 C +ATOM 1970 CD1 LEU A 364 -3.116 39.084 52.576 1.00 95.33 C +ATOM 1971 CD2 LEU A 364 -3.562 40.977 54.154 1.00 96.01 C +ATOM 1972 N LEU A 365 -6.839 39.981 49.835 1.00 93.72 N +ATOM 1973 CA LEU A 365 -8.102 39.957 49.108 1.00 96.16 C +ATOM 1974 C LEU A 365 -8.679 38.542 49.151 1.00 99.86 C +ATOM 1975 O LEU A 365 -7.969 37.580 49.442 1.00 95.59 O +ATOM 1976 CB LEU A 365 -7.894 40.405 47.660 1.00 92.91 C +ATOM 1977 CG LEU A 365 -7.503 41.875 47.472 1.00 98.37 C +ATOM 1978 CD1 LEU A 365 -7.186 42.119 46.009 1.00100.00 C +ATOM 1979 CD2 LEU A 365 -8.629 42.789 47.944 1.00 99.54 C +ATOM 1980 N PRO A 366 -9.981 38.396 48.852 1.00100.00 N +ATOM 1981 CA PRO A 366 -10.612 37.074 48.877 1.00 96.24 C +ATOM 1982 C PRO A 366 -10.316 36.237 47.643 1.00 92.66 C +ATOM 1983 O PRO A 366 -10.209 36.757 46.533 1.00 93.04 O +ATOM 1984 CB PRO A 366 -12.094 37.394 49.012 1.00 86.09 C +ATOM 1985 CG PRO A 366 -12.243 38.706 48.311 1.00 94.58 C +ATOM 1986 CD PRO A 366 -10.933 39.446 48.447 1.00100.00 C +ATOM 1987 N LEU A 367 -10.180 34.932 47.842 1.00 90.26 N +ATOM 1988 CA LEU A 367 -9.908 34.044 46.727 1.00100.00 C +ATOM 1989 C LEU A 367 -11.120 34.042 45.799 1.00100.00 C +ATOM 1990 O LEU A 367 -12.099 33.329 46.030 1.00 96.26 O +ATOM 1991 CB LEU A 367 -9.615 32.620 47.222 1.00 96.71 C +ATOM 1992 CG LEU A 367 -9.264 31.634 46.097 1.00 90.96 C +ATOM 1993 CD1 LEU A 367 -7.942 32.037 45.448 1.00 90.36 C +ATOM 1994 CD2 LEU A 367 -9.184 30.224 46.649 1.00 83.71 C +ATOM 1995 N GLU A 368 -11.047 34.864 44.756 1.00100.00 N +ATOM 1996 CA GLU A 368 -12.118 34.980 43.769 1.00100.00 C +ATOM 1997 C GLU A 368 -11.530 34.722 42.382 1.00100.00 C +ATOM 1998 O GLU A 368 -11.121 35.652 41.687 1.00100.00 O +ATOM 1999 CB GLU A 368 -12.729 36.381 43.818 1.00100.00 C +ATOM 2000 CG GLU A 368 -14.144 36.469 43.284 1.00100.00 C +ATOM 2001 CD GLU A 368 -14.758 37.833 43.517 1.00 99.78 C +ATOM 2002 OE1 GLU A 368 -15.286 38.426 42.551 1.00100.00 O +ATOM 2003 OE2 GLU A 368 -14.704 38.313 44.670 1.00 90.93 O +ATOM 2004 N LEU A 369 -11.494 33.450 41.992 1.00100.00 N +ATOM 2005 CA LEU A 369 -10.933 33.034 40.708 1.00 95.06 C +ATOM 2006 C LEU A 369 -11.316 33.890 39.503 1.00 94.49 C +ATOM 2007 O LEU A 369 -10.606 33.899 38.494 1.00 89.42 O +ATOM 2008 CB LEU A 369 -11.297 31.572 40.433 1.00 72.92 C +ATOM 2009 CG LEU A 369 -10.466 30.556 41.222 1.00 70.31 C +ATOM 2010 CD1 LEU A 369 -10.813 30.650 42.697 1.00 77.73 C +ATOM 2011 CD2 LEU A 369 -10.727 29.158 40.690 1.00 56.07 C +ATOM 2012 N GLU A 370 -12.429 34.607 39.599 1.00 95.61 N +ATOM 2013 CA GLU A 370 -12.864 35.446 38.492 1.00 95.94 C +ATOM 2014 C GLU A 370 -11.875 36.579 38.242 1.00100.00 C +ATOM 2015 O GLU A 370 -11.369 36.744 37.130 1.00 92.14 O +ATOM 2016 CB GLU A 370 -14.250 36.028 38.772 1.00 94.59 C +ATOM 2017 CG GLU A 370 -15.178 36.006 37.562 1.00 99.49 C +ATOM 2018 CD GLU A 370 -14.585 36.706 36.351 1.00100.00 C +ATOM 2019 OE1 GLU A 370 -14.769 37.935 36.222 1.00100.00 O +ATOM 2020 OE2 GLU A 370 -13.936 36.028 35.527 1.00 98.60 O +ATOM 2021 N LYS A 371 -11.602 37.356 39.284 1.00100.00 N +ATOM 2022 CA LYS A 371 -10.687 38.485 39.182 1.00100.00 C +ATOM 2023 C LYS A 371 -9.261 38.131 39.600 1.00100.00 C +ATOM 2024 O LYS A 371 -8.380 38.992 39.628 1.00100.00 O +ATOM 2025 CB LYS A 371 -11.210 39.644 40.035 1.00100.00 C +ATOM 2026 CG LYS A 371 -12.622 40.076 39.675 1.00 89.30 C +ATOM 2027 CD LYS A 371 -12.694 40.566 38.235 1.00 90.44 C +ATOM 2028 CE LYS A 371 -14.109 40.956 37.849 1.00 86.33 C +ATOM 2029 NZ LYS A 371 -14.188 41.350 36.418 1.00 76.33 N +ATOM 2030 N THR A 372 -9.035 36.863 39.923 1.00 91.49 N +ATOM 2031 CA THR A 372 -7.708 36.423 40.335 1.00 86.86 C +ATOM 2032 C THR A 372 -6.869 36.026 39.128 1.00 89.34 C +ATOM 2033 O THR A 372 -5.645 36.162 39.141 1.00 93.02 O +ATOM 2034 CB THR A 372 -7.778 35.212 41.287 1.00 80.77 C +ATOM 2035 OG1 THR A 372 -8.541 35.554 42.450 1.00 73.30 O +ATOM 2036 CG2 THR A 372 -6.380 34.795 41.712 1.00 81.82 C +ATOM 2037 N ALA A 373 -7.536 35.534 38.087 1.00 90.66 N +ATOM 2038 CA ALA A 373 -6.860 35.107 36.866 1.00 89.88 C +ATOM 2039 C ALA A 373 -6.355 36.295 36.049 1.00 93.94 C +ATOM 2040 O ALA A 373 -5.378 36.182 35.304 1.00 96.10 O +ATOM 2041 CB ALA A 373 -7.803 34.258 36.021 1.00 77.92 C +ATOM 2042 N ILE A 374 -7.028 37.431 36.190 1.00 93.44 N +ATOM 2043 CA ILE A 374 -6.647 38.638 35.467 1.00 95.05 C +ATOM 2044 C ILE A 374 -5.403 39.259 36.086 1.00 99.90 C +ATOM 2045 O ILE A 374 -4.540 39.790 35.386 1.00 99.60 O +ATOM 2046 CB ILE A 374 -7.777 39.678 35.502 1.00 95.85 C +ATOM 2047 CG1 ILE A 374 -9.077 39.043 35.000 1.00100.00 C +ATOM 2048 CG2 ILE A 374 -7.397 40.889 34.659 1.00100.00 C +ATOM 2049 CD1 ILE A 374 -10.331 39.733 35.491 1.00100.00 C +ATOM 2050 N GLN A 375 -5.326 39.175 37.409 1.00 97.32 N +ATOM 2051 CA GLN A 375 -4.216 39.718 38.182 1.00100.00 C +ATOM 2052 C GLN A 375 -2.820 39.405 37.639 1.00100.00 C +ATOM 2053 O GLN A 375 -2.465 38.242 37.451 1.00100.00 O +ATOM 2054 CB GLN A 375 -4.313 39.215 39.622 1.00100.00 C +ATOM 2055 CG GLN A 375 -3.045 39.417 40.422 1.00100.00 C +ATOM 2056 CD GLN A 375 -2.851 40.856 40.836 1.00100.00 C +ATOM 2057 OE1 GLN A 375 -3.655 41.724 40.495 1.00100.00 O +ATOM 2058 NE2 GLN A 375 -1.781 41.122 41.578 1.00100.00 N +ATOM 2059 N ASN A 376 -2.031 40.456 37.421 1.00100.00 N +ATOM 2060 CA ASN A 376 -0.664 40.327 36.917 1.00100.00 C +ATOM 2061 C ASN A 376 0.323 40.374 38.087 1.00100.00 C +ATOM 2062 O ASN A 376 0.185 41.202 38.987 1.00 97.37 O +ATOM 2063 CB ASN A 376 -0.360 41.463 35.935 1.00 93.27 C +ATOM 2064 CG ASN A 376 0.627 41.056 34.859 1.00 91.62 C +ATOM 2065 OD1 ASN A 376 1.728 41.601 34.775 1.00 86.47 O +ATOM 2066 ND2 ASN A 376 0.237 40.096 34.026 1.00 95.27 N +ATOM 2067 N TYR A 377 1.319 39.490 38.072 1.00100.00 N +ATOM 2068 CA TYR A 377 2.305 39.438 39.153 1.00100.00 C +ATOM 2069 C TYR A 377 3.765 39.423 38.692 1.00 99.33 C +ATOM 2070 O TYR A 377 4.067 39.138 37.530 1.00100.00 O +ATOM 2071 CB TYR A 377 2.046 38.210 40.034 1.00 97.62 C +ATOM 2072 CG TYR A 377 2.193 36.892 39.303 1.00100.00 C +ATOM 2073 CD1 TYR A 377 3.419 36.225 39.266 1.00100.00 C +ATOM 2074 CD2 TYR A 377 1.112 36.319 38.635 1.00 97.98 C +ATOM 2075 CE1 TYR A 377 3.564 35.017 38.584 1.00 98.13 C +ATOM 2076 CE2 TYR A 377 1.246 35.111 37.950 1.00100.00 C +ATOM 2077 CZ TYR A 377 2.476 34.466 37.928 1.00100.00 C +ATOM 2078 OH TYR A 377 2.618 33.269 37.261 1.00 91.50 O +ATOM 2079 N THR A 378 4.664 39.729 39.626 1.00 91.74 N +ATOM 2080 CA THR A 378 6.099 39.746 39.355 1.00 95.10 C +ATOM 2081 C THR A 378 6.667 38.373 39.682 1.00 95.66 C +ATOM 2082 O THR A 378 6.136 37.663 40.534 1.00 92.13 O +ATOM 2083 CB THR A 378 6.835 40.795 40.223 1.00100.00 C +ATOM 2084 OG1 THR A 378 8.240 40.750 39.940 1.00 99.09 O +ATOM 2085 CG2 THR A 378 6.618 40.511 41.707 1.00 98.52 C +ATOM 2086 N VAL A 379 7.755 38.008 39.018 1.00100.00 N +ATOM 2087 CA VAL A 379 8.371 36.709 39.240 1.00 99.46 C +ATOM 2088 C VAL A 379 9.538 36.742 40.228 1.00100.00 C +ATOM 2089 O VAL A 379 9.660 35.865 41.084 1.00100.00 O +ATOM 2090 CB VAL A 379 8.880 36.114 37.908 1.00100.00 C +ATOM 2091 CG1 VAL A 379 9.858 37.081 37.242 1.00 96.93 C +ATOM 2092 CG2 VAL A 379 9.545 34.767 38.162 1.00 87.09 C +ATOM 2093 N THR A 380 10.384 37.761 40.112 1.00100.00 N +ATOM 2094 CA THR A 380 11.563 37.881 40.964 1.00 99.35 C +ATOM 2095 C THR A 380 11.352 38.445 42.364 1.00 97.45 C +ATOM 2096 O THR A 380 12.230 38.317 43.218 1.00 94.83 O +ATOM 2097 CB THR A 380 12.647 38.741 40.283 1.00100.00 C +ATOM 2098 OG1 THR A 380 12.115 40.040 39.992 1.00100.00 O +ATOM 2099 CG2 THR A 380 13.119 38.083 38.995 1.00100.00 C +ATOM 2100 N GLU A 381 10.205 39.063 42.614 1.00 96.16 N +ATOM 2101 CA GLU A 381 9.985 39.638 43.930 1.00 94.77 C +ATOM 2102 C GLU A 381 8.657 39.327 44.608 1.00100.00 C +ATOM 2103 O GLU A 381 7.833 38.578 44.081 1.00100.00 O +ATOM 2104 CB GLU A 381 10.197 41.147 43.861 1.00 90.67 C +ATOM 2105 CG GLU A 381 11.655 41.536 43.704 1.00 96.58 C +ATOM 2106 CD GLU A 381 11.835 43.025 43.550 1.00 99.52 C +ATOM 2107 OE1 GLU A 381 12.707 43.439 42.757 1.00100.00 O +ATOM 2108 OE2 GLU A 381 11.102 43.781 44.223 1.00100.00 O +ATOM 2109 N PHE A 382 8.474 39.916 45.789 1.00100.00 N +ATOM 2110 CA PHE A 382 7.278 39.724 46.613 1.00 99.86 C +ATOM 2111 C PHE A 382 6.001 40.312 46.019 1.00 98.85 C +ATOM 2112 O PHE A 382 6.020 41.376 45.397 1.00 93.87 O +ATOM 2113 CB PHE A 382 7.497 40.325 48.007 1.00 85.54 C +ATOM 2114 CG PHE A 382 8.611 39.680 48.794 1.00 91.55 C +ATOM 2115 CD1 PHE A 382 9.519 38.817 48.186 1.00 88.06 C +ATOM 2116 CD2 PHE A 382 8.760 39.951 50.149 1.00 96.89 C +ATOM 2117 CE1 PHE A 382 10.557 38.239 48.916 1.00 88.79 C +ATOM 2118 CE2 PHE A 382 9.794 39.378 50.888 1.00 93.24 C +ATOM 2119 CZ PHE A 382 10.693 38.520 50.269 1.00 87.02 C +ATOM 2120 N GLN A 383 4.890 39.615 46.239 1.00100.00 N +ATOM 2121 CA GLN A 383 3.590 40.043 45.733 1.00100.00 C +ATOM 2122 C GLN A 383 2.759 40.725 46.820 1.00 99.33 C +ATOM 2123 O GLN A 383 2.519 40.152 47.881 1.00 97.30 O +ATOM 2124 CB GLN A 383 2.817 38.837 45.181 1.00 97.24 C +ATOM 2125 CG GLN A 383 3.445 38.202 43.951 1.00 93.63 C +ATOM 2126 CD GLN A 383 4.613 37.301 44.296 1.00100.00 C +ATOM 2127 OE1 GLN A 383 5.564 37.175 43.526 1.00100.00 O +ATOM 2128 NE2 GLN A 383 4.547 36.670 45.463 1.00 80.97 N +ATOM 2129 N PRO A 384 2.295 41.961 46.559 1.00100.00 N +ATOM 2130 CA PRO A 384 1.489 42.681 47.552 1.00100.00 C +ATOM 2131 C PRO A 384 0.134 42.009 47.723 1.00100.00 C +ATOM 2132 O PRO A 384 -0.535 42.178 48.744 1.00100.00 O +ATOM 2133 CB PRO A 384 1.363 44.087 46.968 1.00100.00 C +ATOM 2134 CG PRO A 384 1.532 43.894 45.499 1.00100.00 C +ATOM 2135 CD PRO A 384 2.470 42.735 45.319 1.00100.00 C +ATOM 2136 N LEU A 385 -0.249 41.234 46.714 1.00 98.23 N +ATOM 2137 CA LEU A 385 -1.518 40.522 46.721 1.00 96.10 C +ATOM 2138 C LEU A 385 -1.350 39.044 47.067 1.00100.00 C +ATOM 2139 O LEU A 385 -0.504 38.351 46.496 1.00100.00 O +ATOM 2140 CB LEU A 385 -2.196 40.645 45.352 1.00 91.24 C +ATOM 2141 CG LEU A 385 -2.987 41.919 45.037 1.00 94.27 C +ATOM 2142 CD1 LEU A 385 -4.006 41.593 43.961 1.00 78.81 C +ATOM 2143 CD2 LEU A 385 -3.691 42.452 46.281 1.00100.00 C +ATOM 2144 N TYR A 386 -2.159 38.581 48.018 1.00 98.42 N +ATOM 2145 CA TYR A 386 -2.167 37.189 48.467 1.00 90.07 C +ATOM 2146 C TYR A 386 -3.635 36.846 48.721 1.00 89.16 C +ATOM 2147 O TYR A 386 -4.188 37.209 49.759 1.00100.00 O +ATOM 2148 CB TYR A 386 -1.385 37.021 49.777 1.00 82.19 C +ATOM 2149 CG TYR A 386 0.119 37.190 49.666 1.00 90.41 C +ATOM 2150 CD1 TYR A 386 0.784 38.140 50.440 1.00 97.78 C +ATOM 2151 CD2 TYR A 386 0.882 36.377 48.822 1.00 93.82 C +ATOM 2152 CE1 TYR A 386 2.169 38.280 50.383 1.00100.00 C +ATOM 2153 CE2 TYR A 386 2.273 36.509 48.757 1.00 96.67 C +ATOM 2154 CZ TYR A 386 2.908 37.461 49.542 1.00100.00 C +ATOM 2155 OH TYR A 386 4.278 37.587 49.492 1.00100.00 O +ATOM 2156 N TYR A 387 -4.263 36.157 47.774 1.00 85.74 N +ATOM 2157 CA TYR A 387 -5.672 35.793 47.905 1.00 92.52 C +ATOM 2158 C TYR A 387 -5.930 34.798 49.030 1.00100.00 C +ATOM 2159 O TYR A 387 -5.386 33.693 49.037 1.00100.00 O +ATOM 2160 CB TYR A 387 -6.197 35.234 46.579 1.00 87.50 C +ATOM 2161 CG TYR A 387 -6.211 36.267 45.483 1.00 78.83 C +ATOM 2162 CD1 TYR A 387 -5.030 36.658 44.860 1.00 77.83 C +ATOM 2163 CD2 TYR A 387 -7.396 36.895 45.102 1.00 80.82 C +ATOM 2164 CE1 TYR A 387 -5.024 37.651 43.884 1.00 96.01 C +ATOM 2165 CE2 TYR A 387 -7.403 37.892 44.126 1.00 89.89 C +ATOM 2166 CZ TYR A 387 -6.211 38.267 43.522 1.00 95.76 C +ATOM 2167 OH TYR A 387 -6.196 39.257 42.561 1.00 80.81 O +ATOM 2168 N VAL A 388 -6.777 35.203 49.974 1.00100.00 N +ATOM 2169 CA VAL A 388 -7.118 34.378 51.129 1.00 97.26 C +ATOM 2170 C VAL A 388 -8.277 33.417 50.874 1.00 96.92 C +ATOM 2171 O VAL A 388 -9.432 33.834 50.779 1.00100.00 O +ATOM 2172 CB VAL A 388 -7.479 35.264 52.342 1.00 97.40 C +ATOM 2173 CG1 VAL A 388 -7.740 34.397 53.566 1.00 98.41 C +ATOM 2174 CG2 VAL A 388 -6.357 36.254 52.609 1.00100.00 C +ATOM 2175 N ALA A 389 -7.960 32.128 50.769 1.00 92.96 N +ATOM 2176 CA ALA A 389 -8.971 31.103 50.539 1.00 87.23 C +ATOM 2177 C ALA A 389 -9.519 30.605 51.870 1.00 88.83 C +ATOM 2178 O ALA A 389 -8.779 30.460 52.846 1.00 84.56 O +ATOM 2179 CB ALA A 389 -8.375 29.941 49.762 1.00 83.42 C +ATOM 2180 N GLU A 390 -10.823 30.354 51.908 1.00 91.80 N +ATOM 2181 CA GLU A 390 -11.456 29.860 53.122 1.00 91.37 C +ATOM 2182 C GLU A 390 -10.844 28.507 53.454 1.00 88.96 C +ATOM 2183 O GLU A 390 -10.351 28.288 54.562 1.00 97.40 O +ATOM 2184 CB GLU A 390 -12.960 29.711 52.911 1.00 94.09 C +ATOM 2185 CG GLU A 390 -13.667 31.019 52.625 1.00100.00 C +ATOM 2186 CD GLU A 390 -15.175 30.861 52.548 1.00100.00 C +ATOM 2187 OE1 GLU A 390 -15.661 29.712 52.665 1.00100.00 O +ATOM 2188 OE2 GLU A 390 -15.872 31.887 52.373 1.00100.00 O +ATOM 2189 N SER A 391 -10.879 27.606 52.477 1.00 77.84 N +ATOM 2190 CA SER A 391 -10.326 26.269 52.633 1.00 69.81 C +ATOM 2191 C SER A 391 -10.011 25.686 51.263 1.00 65.41 C +ATOM 2192 O SER A 391 -10.419 26.232 50.238 1.00 67.04 O +ATOM 2193 CB SER A 391 -11.321 25.362 53.364 1.00 68.26 C +ATOM 2194 OG SER A 391 -10.719 24.131 53.733 1.00 78.68 O +ATOM 2195 N PHE A 392 -9.272 24.582 51.252 1.00 64.72 N +ATOM 2196 CA PHE A 392 -8.913 23.920 50.004 1.00 63.71 C +ATOM 2197 C PHE A 392 -10.162 23.244 49.463 1.00 65.72 C +ATOM 2198 O PHE A 392 -10.360 23.148 48.253 1.00 57.64 O +ATOM 2199 CB PHE A 392 -7.808 22.894 50.258 1.00 63.72 C +ATOM 2200 CG PHE A 392 -6.774 23.358 51.241 1.00 79.95 C +ATOM 2201 CD1 PHE A 392 -6.639 22.734 52.477 1.00 96.25 C +ATOM 2202 CD2 PHE A 392 -5.943 24.433 50.939 1.00 77.52 C +ATOM 2203 CE1 PHE A 392 -5.690 23.173 53.399 1.00100.00 C +ATOM 2204 CE2 PHE A 392 -4.990 24.881 51.851 1.00 83.36 C +ATOM 2205 CZ PHE A 392 -4.864 24.250 53.085 1.00 99.74 C +ATOM 2206 N ASN A 393 -11.005 22.785 50.381 1.00 69.65 N +ATOM 2207 CA ASN A 393 -12.257 22.134 50.030 1.00 67.80 C +ATOM 2208 C ASN A 393 -13.155 23.171 49.367 1.00 64.99 C +ATOM 2209 O ASN A 393 -13.945 22.858 48.479 1.00 61.92 O +ATOM 2210 CB ASN A 393 -12.935 21.598 51.293 1.00 55.58 C +ATOM 2211 CG ASN A 393 -13.984 20.555 50.991 1.00 63.01 C +ATOM 2212 OD1 ASN A 393 -14.791 20.715 50.076 1.00 73.68 O +ATOM 2213 ND2 ASN A 393 -13.980 19.474 51.762 1.00 72.87 N +ATOM 2214 N ASP A 394 -13.021 24.416 49.803 1.00 60.25 N +ATOM 2215 CA ASP A 394 -13.824 25.499 49.263 1.00 65.04 C +ATOM 2216 C ASP A 394 -13.403 25.869 47.849 1.00 69.42 C +ATOM 2217 O ASP A 394 -14.237 26.003 46.953 1.00 72.92 O +ATOM 2218 CB ASP A 394 -13.708 26.728 50.163 1.00 79.78 C +ATOM 2219 CG ASP A 394 -14.821 27.721 49.934 1.00 91.97 C +ATOM 2220 OD1 ASP A 394 -16.001 27.312 49.983 1.00 91.80 O +ATOM 2221 OD2 ASP A 394 -14.516 28.910 49.703 1.00 92.70 O +ATOM 2222 N ALA A 395 -12.100 26.037 47.661 1.00 75.65 N +ATOM 2223 CA ALA A 395 -11.549 26.414 46.365 1.00 62.68 C +ATOM 2224 C ALA A 395 -11.776 25.367 45.280 1.00 65.12 C +ATOM 2225 O ALA A 395 -12.087 25.710 44.140 1.00 66.49 O +ATOM 2226 CB ALA A 395 -10.066 26.706 46.506 1.00 43.25 C +ATOM 2227 N LYS A 396 -11.610 24.095 45.635 1.00 59.26 N +ATOM 2228 CA LYS A 396 -11.799 22.999 44.685 1.00 46.21 C +ATOM 2229 C LYS A 396 -13.055 23.193 43.846 1.00 40.74 C +ATOM 2230 O LYS A 396 -13.068 22.873 42.658 1.00 28.37 O +ATOM 2231 CB LYS A 396 -11.893 21.661 45.422 1.00 51.44 C +ATOM 2232 CG LYS A 396 -12.490 20.542 44.588 1.00 22.90 C +ATOM 2233 CD LYS A 396 -12.410 19.224 45.323 1.00 31.36 C +ATOM 2234 CE LYS A 396 -13.665 18.974 46.124 1.00 41.10 C +ATOM 2235 NZ LYS A 396 -13.770 17.556 46.564 1.00 37.34 N +ATOM 2236 N GLU A 397 -14.110 23.701 44.478 1.00 41.13 N +ATOM 2237 CA GLU A 397 -15.373 23.948 43.793 1.00 49.25 C +ATOM 2238 C GLU A 397 -15.213 25.125 42.837 1.00 51.92 C +ATOM 2239 O GLU A 397 -15.681 25.080 41.698 1.00 60.13 O +ATOM 2240 CB GLU A 397 -16.476 24.260 44.805 1.00 60.20 C +ATOM 2241 CG GLU A 397 -16.578 23.247 45.922 1.00 82.81 C +ATOM 2242 CD GLU A 397 -16.989 21.882 45.422 1.00100.00 C +ATOM 2243 OE1 GLU A 397 -17.773 21.815 44.450 1.00100.00 O +ATOM 2244 OE2 GLU A 397 -16.531 20.876 46.002 1.00100.00 O +ATOM 2245 N LYS A 398 -14.549 26.177 43.310 1.00 47.17 N +ATOM 2246 CA LYS A 398 -14.321 27.365 42.502 1.00 52.50 C +ATOM 2247 C LYS A 398 -13.622 26.969 41.205 1.00 49.29 C +ATOM 2248 O LYS A 398 -13.665 27.697 40.214 1.00 56.88 O +ATOM 2249 CB LYS A 398 -13.466 28.362 43.278 1.00 67.30 C +ATOM 2250 CG LYS A 398 -13.822 28.453 44.751 1.00 65.58 C +ATOM 2251 CD LYS A 398 -14.985 29.403 44.983 1.00 76.37 C +ATOM 2252 CE LYS A 398 -15.053 29.844 46.439 1.00 68.23 C +ATOM 2253 NZ LYS A 398 -13.928 30.755 46.787 1.00 72.84 N +ATOM 2254 N VAL A 399 -12.988 25.801 41.223 1.00 44.34 N +ATOM 2255 CA VAL A 399 -12.273 25.284 40.062 1.00 47.58 C +ATOM 2256 C VAL A 399 -13.160 24.352 39.236 1.00 47.85 C +ATOM 2257 O VAL A 399 -13.116 24.364 38.004 1.00 49.40 O +ATOM 2258 CB VAL A 399 -11.001 24.521 40.498 1.00 41.31 C +ATOM 2259 CG1 VAL A 399 -9.908 24.694 39.458 1.00 42.53 C +ATOM 2260 CG2 VAL A 399 -10.524 25.024 41.852 1.00 35.00 C +ATOM 2261 N ARG A 400 -13.972 23.554 39.923 1.00 45.56 N +ATOM 2262 CA ARG A 400 -14.876 22.624 39.258 1.00 52.75 C +ATOM 2263 C ARG A 400 -15.722 23.354 38.222 1.00 58.51 C +ATOM 2264 O ARG A 400 -15.717 23.009 37.042 1.00 63.72 O +ATOM 2265 CB ARG A 400 -15.790 21.953 40.284 1.00 55.93 C +ATOM 2266 CG ARG A 400 -15.236 20.667 40.843 1.00 54.36 C +ATOM 2267 CD ARG A 400 -16.347 19.692 41.166 1.00 58.44 C +ATOM 2268 NE ARG A 400 -15.819 18.457 41.736 1.00 77.88 N +ATOM 2269 CZ ARG A 400 -15.908 17.262 41.159 1.00 86.01 C +ATOM 2270 NH1 ARG A 400 -16.513 17.127 39.985 1.00 78.05 N +ATOM 2271 NH2 ARG A 400 -15.389 16.198 41.759 1.00 99.95 N +ATOM 2272 N ASN A 401 -16.442 24.371 38.682 1.00 75.85 N +ATOM 2273 CA ASN A 401 -17.305 25.174 37.823 1.00 77.91 C +ATOM 2274 C ASN A 401 -16.503 25.977 36.805 1.00 68.26 C +ATOM 2275 O ASN A 401 -16.860 26.031 35.627 1.00 72.47 O +ATOM 2276 CB ASN A 401 -18.137 26.123 38.679 1.00 87.48 C +ATOM 2277 CG ASN A 401 -17.454 26.473 39.983 1.00 93.59 C +ATOM 2278 OD1 ASN A 401 -17.926 26.106 41.062 1.00 92.46 O +ATOM 2279 ND2 ASN A 401 -16.330 27.181 39.893 1.00 99.85 N +ATOM 2280 N PHE A 402 -15.428 26.614 37.263 1.00 43.40 N +ATOM 2281 CA PHE A 402 -14.575 27.404 36.379 1.00 48.71 C +ATOM 2282 C PHE A 402 -14.218 26.563 35.160 1.00 54.14 C +ATOM 2283 O PHE A 402 -13.987 27.089 34.072 1.00 52.45 O +ATOM 2284 CB PHE A 402 -13.292 27.831 37.109 1.00 45.77 C +ATOM 2285 CG PHE A 402 -12.417 28.783 36.322 1.00 59.63 C +ATOM 2286 CD1 PHE A 402 -11.166 29.153 36.809 1.00 62.54 C +ATOM 2287 CD2 PHE A 402 -12.840 29.314 35.107 1.00 48.87 C +ATOM 2288 CE1 PHE A 402 -10.351 30.033 36.091 1.00 49.67 C +ATOM 2289 CE2 PHE A 402 -12.033 30.191 34.387 1.00 49.79 C +ATOM 2290 CZ PHE A 402 -10.788 30.551 34.882 1.00 33.15 C +ATOM 2291 N ALA A 403 -14.178 25.249 35.349 1.00 68.74 N +ATOM 2292 CA ALA A 403 -13.858 24.345 34.256 1.00 84.45 C +ATOM 2293 C ALA A 403 -15.011 24.325 33.254 1.00 85.90 C +ATOM 2294 O ALA A 403 -14.795 24.270 32.040 1.00 82.18 O +ATOM 2295 CB ALA A 403 -13.596 22.944 34.800 1.00 89.73 C +ATOM 2296 N ALA A 404 -16.236 24.371 33.769 1.00 77.85 N +ATOM 2297 CA ALA A 404 -17.422 24.368 32.920 1.00 64.27 C +ATOM 2298 C ALA A 404 -17.478 25.673 32.148 1.00 64.71 C +ATOM 2299 O ALA A 404 -17.991 25.731 31.033 1.00 57.92 O +ATOM 2300 CB ALA A 404 -18.670 24.215 33.767 1.00 39.11 C +ATOM 2301 N THR A 405 -16.937 26.720 32.759 1.00 63.15 N +ATOM 2302 CA THR A 405 -16.908 28.039 32.146 1.00 66.29 C +ATOM 2303 C THR A 405 -15.749 28.141 31.149 1.00 74.21 C +ATOM 2304 O THR A 405 -15.511 29.198 30.553 1.00 77.41 O +ATOM 2305 CB THR A 405 -16.755 29.127 33.218 1.00 66.02 C +ATOM 2306 OG1 THR A 405 -15.429 29.081 33.757 1.00 68.61 O +ATOM 2307 CG2 THR A 405 -17.756 28.903 34.346 1.00 50.34 C +ATOM 2308 N ILE A 406 -15.034 27.034 30.969 1.00 69.12 N +ATOM 2309 CA ILE A 406 -13.906 26.995 30.042 1.00 63.63 C +ATOM 2310 C ILE A 406 -14.344 26.465 28.683 1.00 58.59 C +ATOM 2311 O ILE A 406 -14.956 25.401 28.589 1.00 54.64 O +ATOM 2312 CB ILE A 406 -12.766 26.076 30.551 1.00 65.45 C +ATOM 2313 CG1 ILE A 406 -12.211 26.599 31.875 1.00 56.74 C +ATOM 2314 CG2 ILE A 406 -11.643 26.021 29.520 1.00 52.19 C +ATOM 2315 CD1 ILE A 406 -11.240 25.644 32.539 1.00 41.69 C +ATOM 2316 N PRO A 407 -14.029 27.203 27.609 1.00 58.31 N +ATOM 2317 CA PRO A 407 -14.389 26.804 26.245 1.00 58.51 C +ATOM 2318 C PRO A 407 -13.641 25.549 25.795 1.00 59.72 C +ATOM 2319 O PRO A 407 -12.476 25.608 25.403 1.00 56.66 O +ATOM 2320 CB PRO A 407 -14.029 28.028 25.404 1.00 64.77 C +ATOM 2321 CG PRO A 407 -12.993 28.736 26.191 1.00 71.72 C +ATOM 2322 CD PRO A 407 -13.300 28.480 27.635 1.00 63.55 C +ATOM 2323 N ARG A 408 -14.327 24.414 25.861 1.00 57.50 N +ATOM 2324 CA ARG A 408 -13.743 23.135 25.467 1.00 54.43 C +ATOM 2325 C ARG A 408 -14.775 22.305 24.715 1.00 45.32 C +ATOM 2326 O ARG A 408 -15.815 21.948 25.264 1.00 44.45 O +ATOM 2327 CB ARG A 408 -13.274 22.362 26.708 1.00 65.13 C +ATOM 2328 CG ARG A 408 -11.834 22.652 27.135 1.00 50.86 C +ATOM 2329 CD ARG A 408 -11.298 21.600 28.119 1.00 59.04 C +ATOM 2330 NE ARG A 408 -11.957 21.657 29.427 1.00 65.61 N +ATOM 2331 CZ ARG A 408 -11.688 20.845 30.450 1.00 41.74 C +ATOM 2332 NH1 ARG A 408 -10.768 19.898 30.333 1.00 32.43 N +ATOM 2333 NH2 ARG A 408 -12.352 20.969 31.592 1.00 44.03 N +ATOM 2334 N PRO A 409 -14.492 21.977 23.446 1.00 39.23 N +ATOM 2335 CA PRO A 409 -15.434 21.180 22.652 1.00 39.23 C +ATOM 2336 C PRO A 409 -15.610 19.771 23.193 1.00 44.36 C +ATOM 2337 O PRO A 409 -15.910 18.844 22.443 1.00 55.39 O +ATOM 2338 CB PRO A 409 -14.819 21.170 21.250 1.00 41.24 C +ATOM 2339 CG PRO A 409 -13.728 22.183 21.277 1.00 61.62 C +ATOM 2340 CD PRO A 409 -13.276 22.301 22.692 1.00 51.69 C +ATOM 2341 N PHE A 410 -15.418 19.619 24.502 1.00 51.53 N +ATOM 2342 CA PHE A 410 -15.534 18.324 25.162 1.00 51.06 C +ATOM 2343 C PHE A 410 -15.413 18.508 26.672 1.00 52.16 C +ATOM 2344 O PHE A 410 -15.307 19.632 27.168 1.00 55.17 O +ATOM 2345 CB PHE A 410 -14.416 17.394 24.684 1.00 49.76 C +ATOM 2346 CG PHE A 410 -13.038 17.874 25.056 1.00 62.85 C +ATOM 2347 CD1 PHE A 410 -12.392 18.838 24.289 1.00 61.48 C +ATOM 2348 CD2 PHE A 410 -12.406 17.401 26.202 1.00 73.01 C +ATOM 2349 CE1 PHE A 410 -11.144 19.329 24.658 1.00 59.87 C +ATOM 2350 CE2 PHE A 410 -11.154 17.887 26.581 1.00 55.37 C +ATOM 2351 CZ PHE A 410 -10.523 18.852 25.806 1.00 56.26 C +ATOM 2352 N SER A 411 -15.426 17.392 27.394 1.00 41.42 N +ATOM 2353 CA SER A 411 -15.296 17.399 28.847 1.00 44.89 C +ATOM 2354 C SER A 411 -14.493 16.157 29.218 1.00 46.80 C +ATOM 2355 O SER A 411 -14.660 15.106 28.602 1.00 38.91 O +ATOM 2356 CB SER A 411 -16.679 17.360 29.504 1.00 60.81 C +ATOM 2357 OG SER A 411 -17.288 18.640 29.496 1.00 83.94 O +ATOM 2358 N VAL A 412 -13.621 16.279 30.212 1.00 47.12 N +ATOM 2359 CA VAL A 412 -12.787 15.156 30.630 1.00 41.50 C +ATOM 2360 C VAL A 412 -13.286 14.466 31.896 1.00 40.55 C +ATOM 2361 O VAL A 412 -14.032 15.047 32.682 1.00 43.56 O +ATOM 2362 CB VAL A 412 -11.340 15.621 30.847 1.00 37.58 C +ATOM 2363 CG1 VAL A 412 -10.751 16.076 29.524 1.00 29.68 C +ATOM 2364 CG2 VAL A 412 -11.302 16.759 31.851 1.00 32.03 C +ATOM 2365 N ARG A 413 -12.871 13.216 32.081 1.00 46.03 N +ATOM 2366 CA ARG A 413 -13.276 12.425 33.242 1.00 36.71 C +ATOM 2367 C ARG A 413 -12.185 11.422 33.600 1.00 33.03 C +ATOM 2368 O ARG A 413 -11.858 10.544 32.805 1.00 37.61 O +ATOM 2369 CB ARG A 413 -14.583 11.688 32.933 1.00 43.97 C +ATOM 2370 CG ARG A 413 -14.815 10.425 33.742 1.00 51.36 C +ATOM 2371 CD ARG A 413 -16.295 10.078 33.797 1.00 61.85 C +ATOM 2372 NE ARG A 413 -16.766 9.499 32.539 1.00 59.90 N +ATOM 2373 CZ ARG A 413 -17.907 8.832 32.403 1.00 60.50 C +ATOM 2374 NH1 ARG A 413 -18.698 8.649 33.452 1.00 52.53 N +ATOM 2375 NH2 ARG A 413 -18.257 8.344 31.219 1.00 23.98 N +ATOM 2376 N TYR A 414 -11.623 11.551 34.798 1.00 32.09 N +ATOM 2377 CA TYR A 414 -10.562 10.643 35.220 1.00 32.39 C +ATOM 2378 C TYR A 414 -11.057 9.365 35.901 1.00 31.53 C +ATOM 2379 O TYR A 414 -12.000 9.386 36.695 1.00 65.12 O +ATOM 2380 CB TYR A 414 -9.573 11.359 36.149 1.00 14.01 C +ATOM 2381 CG TYR A 414 -8.312 10.559 36.381 1.00 25.23 C +ATOM 2382 CD1 TYR A 414 -7.456 10.258 35.322 1.00 39.31 C +ATOM 2383 CD2 TYR A 414 -8.008 10.038 37.637 1.00 19.41 C +ATOM 2384 CE1 TYR A 414 -6.332 9.454 35.502 1.00 52.90 C +ATOM 2385 CE2 TYR A 414 -6.884 9.232 37.828 1.00 45.56 C +ATOM 2386 CZ TYR A 414 -6.052 8.941 36.754 1.00 48.02 C +ATOM 2387 OH TYR A 414 -4.955 8.123 36.920 1.00 55.29 O +ATOM 2388 N ASP A 415 -10.409 8.251 35.571 1.00 44.74 N +ATOM 2389 CA ASP A 415 -10.736 6.943 36.136 1.00 45.65 C +ATOM 2390 C ASP A 415 -9.522 6.431 36.920 1.00 54.50 C +ATOM 2391 O ASP A 415 -8.570 5.900 36.342 1.00 62.76 O +ATOM 2392 CB ASP A 415 -11.085 5.954 35.021 1.00 52.89 C +ATOM 2393 CG ASP A 415 -11.463 4.582 35.546 1.00 39.17 C +ATOM 2394 OD1 ASP A 415 -11.495 3.622 34.749 1.00 52.80 O +ATOM 2395 OD2 ASP A 415 -11.735 4.465 36.759 1.00 41.70 O +ATOM 2396 N PRO A 416 -9.545 6.583 38.254 1.00 40.81 N +ATOM 2397 CA PRO A 416 -8.432 6.130 39.093 1.00 19.09 C +ATOM 2398 C PRO A 416 -8.224 4.619 39.064 1.00 20.61 C +ATOM 2399 O PRO A 416 -7.143 4.131 39.383 1.00 40.06 O +ATOM 2400 CB PRO A 416 -8.801 6.639 40.486 1.00 18.39 C +ATOM 2401 CG PRO A 416 -10.275 6.820 40.450 1.00 36.47 C +ATOM 2402 CD PRO A 416 -10.634 7.179 39.046 1.00 39.25 C +ATOM 2403 N TYR A 417 -9.263 3.884 38.677 1.00 23.31 N +ATOM 2404 CA TYR A 417 -9.202 2.428 38.606 1.00 18.04 C +ATOM 2405 C TYR A 417 -8.345 1.944 37.437 1.00 26.33 C +ATOM 2406 O TYR A 417 -7.694 0.905 37.531 1.00 42.27 O +ATOM 2407 CB TYR A 417 -10.613 1.860 38.496 1.00 34.20 C +ATOM 2408 CG TYR A 417 -11.441 2.080 39.740 1.00 31.39 C +ATOM 2409 CD1 TYR A 417 -12.343 3.137 39.826 1.00 44.97 C +ATOM 2410 CD2 TYR A 417 -11.321 1.232 40.838 1.00 43.77 C +ATOM 2411 CE1 TYR A 417 -13.103 3.344 40.979 1.00 60.75 C +ATOM 2412 CE2 TYR A 417 -12.077 1.431 41.994 1.00 47.93 C +ATOM 2413 CZ TYR A 417 -12.965 2.487 42.057 1.00 46.98 C +ATOM 2414 OH TYR A 417 -13.712 2.688 43.193 1.00 34.47 O +ATOM 2415 N THR A 418 -8.350 2.694 36.336 1.00 29.23 N +ATOM 2416 CA THR A 418 -7.551 2.346 35.158 1.00 22.36 C +ATOM 2417 C THR A 418 -6.510 3.419 34.858 1.00 20.46 C +ATOM 2418 O THR A 418 -5.811 3.341 33.847 1.00 20.80 O +ATOM 2419 CB THR A 418 -8.420 2.174 33.899 1.00 18.97 C +ATOM 2420 OG1 THR A 418 -9.083 3.408 33.603 1.00 50.92 O +ATOM 2421 CG2 THR A 418 -9.448 1.084 34.110 1.00 37.66 C +ATOM 2422 N GLN A 419 -6.409 4.407 35.749 1.00 37.04 N +ATOM 2423 CA GLN A 419 -5.459 5.508 35.593 1.00 38.68 C +ATOM 2424 C GLN A 419 -5.572 6.013 34.167 1.00 41.44 C +ATOM 2425 O GLN A 419 -4.578 6.120 33.449 1.00 53.88 O +ATOM 2426 CB GLN A 419 -4.030 5.028 35.836 1.00 39.99 C +ATOM 2427 CG GLN A 419 -3.746 4.561 37.248 1.00 43.23 C +ATOM 2428 CD GLN A 419 -2.366 3.952 37.373 1.00 55.23 C +ATOM 2429 OE1 GLN A 419 -2.072 2.921 36.766 1.00 66.54 O +ATOM 2430 NE2 GLN A 419 -1.509 4.587 38.160 1.00 65.41 N +ATOM 2431 N ARG A 420 -6.794 6.321 33.759 1.00 36.00 N +ATOM 2432 CA ARG A 420 -7.035 6.780 32.405 1.00 36.42 C +ATOM 2433 C ARG A 420 -8.029 7.928 32.360 1.00 28.89 C +ATOM 2434 O ARG A 420 -8.985 7.966 33.130 1.00 38.54 O +ATOM 2435 CB ARG A 420 -7.560 5.615 31.568 1.00 43.32 C +ATOM 2436 CG ARG A 420 -7.004 5.546 30.162 1.00 46.86 C +ATOM 2437 CD ARG A 420 -7.553 4.328 29.428 1.00 65.16 C +ATOM 2438 NE ARG A 420 -7.693 3.176 30.318 1.00 68.48 N +ATOM 2439 CZ ARG A 420 -7.499 1.911 29.951 1.00 71.50 C +ATOM 2440 NH1 ARG A 420 -7.151 1.621 28.703 1.00 63.28 N +ATOM 2441 NH2 ARG A 420 -7.647 0.936 30.839 1.00 60.10 N +ATOM 2442 N ILE A 421 -7.791 8.864 31.451 1.00 5.09 N +ATOM 2443 CA ILE A 421 -8.679 10.001 31.288 1.00 22.29 C +ATOM 2444 C ILE A 421 -9.675 9.629 30.191 1.00 35.36 C +ATOM 2445 O ILE A 421 -9.301 8.971 29.215 1.00 37.76 O +ATOM 2446 CB ILE A 421 -7.899 11.274 30.842 1.00 17.55 C +ATOM 2447 CG1 ILE A 421 -7.312 11.990 32.058 1.00 11.22 C +ATOM 2448 CG2 ILE A 421 -8.821 12.219 30.077 1.00 27.04 C +ATOM 2449 CD1 ILE A 421 -8.337 12.695 32.912 1.00 30.57 C +ATOM 2450 N GLU A 422 -10.938 10.029 30.357 1.00 44.17 N +ATOM 2451 CA GLU A 422 -11.960 9.765 29.345 1.00 42.82 C +ATOM 2452 C GLU A 422 -12.428 11.103 28.792 1.00 56.06 C +ATOM 2453 O GLU A 422 -12.695 12.035 29.548 1.00 70.09 O +ATOM 2454 CB GLU A 422 -13.153 9.002 29.927 1.00 49.23 C +ATOM 2455 CG GLU A 422 -14.105 8.493 28.846 1.00 66.49 C +ATOM 2456 CD GLU A 422 -15.322 7.775 29.402 1.00 83.44 C +ATOM 2457 OE1 GLU A 422 -16.271 7.529 28.626 1.00 61.26 O +ATOM 2458 OE2 GLU A 422 -15.328 7.455 30.610 1.00 86.85 O +ATOM 2459 N VAL A 423 -12.510 11.202 27.469 1.00 57.84 N +ATOM 2460 CA VAL A 423 -12.938 12.438 26.819 1.00 50.66 C +ATOM 2461 C VAL A 423 -14.405 12.351 26.404 1.00 41.37 C +ATOM 2462 O VAL A 423 -14.783 11.512 25.594 1.00 26.86 O +ATOM 2463 CB VAL A 423 -12.059 12.736 25.584 1.00 38.04 C +ATOM 2464 CG1 VAL A 423 -12.374 14.119 25.045 1.00 46.38 C +ATOM 2465 CG2 VAL A 423 -10.589 12.641 25.964 1.00 40.98 C +ATOM 2466 N LEU A 424 -15.228 13.224 26.971 1.00 46.86 N +ATOM 2467 CA LEU A 424 -16.648 13.218 26.673 1.00 44.59 C +ATOM 2468 C LEU A 424 -17.093 14.362 25.773 1.00 54.91 C +ATOM 2469 O LEU A 424 -16.446 15.408 25.694 1.00 59.89 O +ATOM 2470 CB LEU A 424 -17.454 13.255 27.973 1.00 35.66 C +ATOM 2471 CG LEU A 424 -17.354 12.020 28.864 1.00 33.05 C +ATOM 2472 CD1 LEU A 424 -17.910 12.327 30.240 1.00 38.05 C +ATOM 2473 CD2 LEU A 424 -18.113 10.882 28.222 1.00 20.80 C +ATOM 2474 N ASP A 425 -18.217 14.143 25.097 1.00 42.91 N +ATOM 2475 CA ASP A 425 -18.808 15.122 24.198 1.00 36.38 C +ATOM 2476 C ASP A 425 -19.887 15.885 24.962 1.00 36.99 C +ATOM 2477 O ASP A 425 -20.897 15.312 25.366 1.00 45.17 O +ATOM 2478 CB ASP A 425 -19.425 14.403 22.990 1.00 42.98 C +ATOM 2479 CG ASP A 425 -20.631 15.131 22.431 1.00 50.49 C +ATOM 2480 OD1 ASP A 425 -21.714 14.514 22.364 1.00 50.76 O +ATOM 2481 OD2 ASP A 425 -20.481 16.313 22.063 1.00 60.47 O +ATOM 2482 N ASN A 426 -19.658 17.180 25.163 1.00 36.35 N +ATOM 2483 CA ASN A 426 -20.573 18.059 25.880 1.00 56.38 C +ATOM 2484 C ASN A 426 -22.018 17.551 26.000 1.00 54.47 C +ATOM 2485 O ASN A 426 -22.624 17.646 27.062 1.00 64.32 O +ATOM 2486 CB ASN A 426 -20.567 19.440 25.223 1.00 67.66 C +ATOM 2487 CG ASN A 426 -19.712 19.477 23.967 1.00 86.65 C +ATOM 2488 OD1 ASN A 426 -18.492 19.607 24.043 1.00 84.18 O +ATOM 2489 ND2 ASN A 426 -20.349 19.364 22.810 1.00 95.28 N +ATOM 2490 N THR A 427 -22.564 17.034 24.904 1.00 52.24 N +ATOM 2491 CA THR A 427 -23.931 16.512 24.875 1.00 49.39 C +ATOM 2492 C THR A 427 -24.119 15.287 25.758 1.00 44.74 C +ATOM 2493 O THR A 427 -25.042 15.229 26.565 1.00 42.41 O +ATOM 2494 CB THR A 427 -24.331 16.139 23.443 1.00 60.18 C +ATOM 2495 OG1 THR A 427 -24.295 17.311 22.617 1.00 80.03 O +ATOM 2496 CG2 THR A 427 -25.726 15.511 23.424 1.00 47.23 C +ATOM 2497 N GLN A 428 -23.243 14.306 25.583 1.00 47.04 N +ATOM 2498 CA GLN A 428 -23.288 13.080 26.365 1.00 41.76 C +ATOM 2499 C GLN A 428 -22.836 13.407 27.775 1.00 37.71 C +ATOM 2500 O GLN A 428 -23.197 12.723 28.727 1.00 37.38 O +ATOM 2501 CB GLN A 428 -22.372 12.021 25.759 1.00 57.95 C +ATOM 2502 CG GLN A 428 -20.903 12.400 25.756 1.00 71.47 C +ATOM 2503 CD GLN A 428 -20.130 11.687 24.663 1.00 77.03 C +ATOM 2504 OE1 GLN A 428 -18.945 11.382 24.817 1.00 80.85 O +ATOM 2505 NE2 GLN A 428 -20.794 11.426 23.551 1.00 78.75 N +ATOM 2506 N GLN A 429 -22.031 14.458 27.899 1.00 32.32 N +ATOM 2507 CA GLN A 429 -21.548 14.895 29.201 1.00 44.95 C +ATOM 2508 C GLN A 429 -22.763 15.429 29.964 1.00 53.81 C +ATOM 2509 O GLN A 429 -22.913 15.210 31.169 1.00 51.75 O +ATOM 2510 CB GLN A 429 -20.512 16.008 29.040 1.00 41.33 C +ATOM 2511 CG GLN A 429 -19.548 16.133 30.205 1.00 62.27 C +ATOM 2512 CD GLN A 429 -20.039 17.080 31.279 1.00 54.21 C +ATOM 2513 OE1 GLN A 429 -20.175 16.700 32.442 1.00 48.76 O +ATOM 2514 NE2 GLN A 429 -20.302 18.323 30.896 1.00 50.57 N +ATOM 2515 N LEU A 430 -23.621 16.134 29.227 1.00 64.83 N +ATOM 2516 CA LEU A 430 -24.860 16.721 29.739 1.00 44.71 C +ATOM 2517 C LEU A 430 -25.696 15.589 30.318 1.00 33.89 C +ATOM 2518 O LEU A 430 -26.067 15.607 31.489 1.00 32.98 O +ATOM 2519 CB LEU A 430 -25.628 17.384 28.583 1.00 25.78 C +ATOM 2520 CG LEU A 430 -26.466 18.661 28.737 1.00 39.27 C +ATOM 2521 CD1 LEU A 430 -25.905 19.576 29.817 1.00 34.15 C +ATOM 2522 CD2 LEU A 430 -26.491 19.381 27.394 1.00 18.50 C +ATOM 2523 N LYS A 431 -25.981 14.609 29.466 1.00 27.52 N +ATOM 2524 CA LYS A 431 -26.760 13.440 29.838 1.00 42.32 C +ATOM 2525 C LYS A 431 -26.161 12.743 31.053 1.00 52.75 C +ATOM 2526 O LYS A 431 -26.887 12.280 31.932 1.00 62.72 O +ATOM 2527 CB LYS A 431 -26.813 12.459 28.669 1.00 52.80 C +ATOM 2528 CG LYS A 431 -27.510 13.000 27.440 1.00 68.93 C +ATOM 2529 CD LYS A 431 -27.812 11.887 26.455 1.00 86.73 C +ATOM 2530 CE LYS A 431 -28.484 12.418 25.201 1.00 89.43 C +ATOM 2531 NZ LYS A 431 -28.905 11.304 24.311 1.00 85.66 N +ATOM 2532 N ILE A 432 -24.834 12.665 31.095 1.00 54.13 N +ATOM 2533 CA ILE A 432 -24.143 12.019 32.206 1.00 49.64 C +ATOM 2534 C ILE A 432 -24.449 12.738 33.516 1.00 50.77 C +ATOM 2535 O ILE A 432 -24.717 12.103 34.534 1.00 46.54 O +ATOM 2536 CB ILE A 432 -22.615 11.991 31.973 1.00 48.67 C +ATOM 2537 CG1 ILE A 432 -22.277 10.987 30.867 1.00 39.82 C +ATOM 2538 CG2 ILE A 432 -21.892 11.613 33.254 1.00 52.52 C +ATOM 2539 CD1 ILE A 432 -23.153 9.746 30.857 1.00 39.19 C +ATOM 2540 N LEU A 433 -24.409 14.064 33.486 1.00 38.29 N +ATOM 2541 CA LEU A 433 -24.706 14.852 34.673 1.00 37.40 C +ATOM 2542 C LEU A 433 -26.137 14.569 35.130 1.00 47.88 C +ATOM 2543 O LEU A 433 -26.391 14.315 36.309 1.00 44.20 O +ATOM 2544 CB LEU A 433 -24.558 16.340 34.364 1.00 17.60 C +ATOM 2545 CG LEU A 433 -23.146 16.815 34.048 1.00 38.38 C +ATOM 2546 CD1 LEU A 433 -23.193 17.827 32.920 1.00 51.77 C +ATOM 2547 CD2 LEU A 433 -22.533 17.418 35.297 1.00 44.05 C +ATOM 2548 N ALA A 434 -27.070 14.622 34.184 1.00 40.82 N +ATOM 2549 CA ALA A 434 -28.476 14.376 34.471 1.00 31.10 C +ATOM 2550 C ALA A 434 -28.665 13.096 35.284 1.00 45.92 C +ATOM 2551 O ALA A 434 -29.240 13.117 36.374 1.00 57.70 O +ATOM 2552 CB ALA A 434 -29.262 14.287 33.165 1.00 50.70 C +ATOM 2553 N ASP A 435 -28.186 11.981 34.740 1.00 39.05 N +ATOM 2554 CA ASP A 435 -28.303 10.691 35.407 1.00 44.06 C +ATOM 2555 C ASP A 435 -27.677 10.753 36.792 1.00 51.97 C +ATOM 2556 O ASP A 435 -28.266 10.293 37.768 1.00 49.25 O +ATOM 2557 CB ASP A 435 -27.609 9.602 34.581 1.00 65.86 C +ATOM 2558 CG ASP A 435 -28.199 9.457 33.191 1.00 82.38 C +ATOM 2559 OD1 ASP A 435 -29.439 9.528 33.062 1.00 85.74 O +ATOM 2560 OD2 ASP A 435 -27.424 9.273 32.228 1.00100.00 O +ATOM 2561 N SER A 436 -26.480 11.328 36.871 1.00 46.23 N +ATOM 2562 CA SER A 436 -25.772 11.448 38.142 1.00 40.37 C +ATOM 2563 C SER A 436 -26.622 12.153 39.184 1.00 35.36 C +ATOM 2564 O SER A 436 -26.746 11.684 40.313 1.00 27.25 O +ATOM 2565 CB SER A 436 -24.465 12.220 37.965 1.00 40.94 C +ATOM 2566 OG SER A 436 -23.842 12.443 39.220 1.00 18.64 O +ATOM 2567 N ILE A 437 -27.192 13.291 38.805 1.00 43.24 N +ATOM 2568 CA ILE A 437 -28.036 14.055 39.716 1.00 35.72 C +ATOM 2569 C ILE A 437 -29.258 13.228 40.083 1.00 25.60 C +ATOM 2570 O ILE A 437 -29.517 12.957 41.255 1.00 31.76 O +ATOM 2571 CB ILE A 437 -28.518 15.378 39.068 1.00 45.25 C +ATOM 2572 CG1 ILE A 437 -27.340 16.100 38.410 1.00 47.42 C +ATOM 2573 CG2 ILE A 437 -29.160 16.281 40.125 1.00 52.02 C +ATOM 2574 CD1 ILE A 437 -27.715 17.391 37.730 1.00 59.40 C +ATOM 2575 N ASN A 438 -30.003 12.831 39.059 1.00 25.65 N +ATOM 2576 CA ASN A 438 -31.209 12.036 39.228 1.00 29.75 C +ATOM 2577 C ASN A 438 -31.000 10.878 40.203 1.00 29.52 C +ATOM 2578 O ASN A 438 -31.900 10.527 40.965 1.00 40.32 O +ATOM 2579 CB ASN A 438 -31.663 11.506 37.866 1.00 22.20 C +ATOM 2580 CG ASN A 438 -33.010 10.821 37.925 1.00 43.18 C +ATOM 2581 OD1 ASN A 438 -34.052 11.474 37.973 1.00 53.60 O +ATOM 2582 ND2 ASN A 438 -32.996 9.495 37.919 1.00 75.69 N +ATOM 2583 N SER A 439 -29.807 10.294 40.177 1.00 26.55 N +ATOM 2584 CA SER A 439 -29.490 9.173 41.052 1.00 30.20 C +ATOM 2585 C SER A 439 -29.284 9.615 42.496 1.00 33.18 C +ATOM 2586 O SER A 439 -29.983 9.167 43.402 1.00 40.71 O +ATOM 2587 CB SER A 439 -28.228 8.467 40.555 1.00 42.46 C +ATOM 2588 OG SER A 439 -28.020 7.241 41.236 1.00 54.88 O +ATOM 2589 N GLU A 440 -28.310 10.496 42.693 1.00 44.97 N +ATOM 2590 CA GLU A 440 -27.961 11.018 44.008 1.00 53.35 C +ATOM 2591 C GLU A 440 -29.156 11.492 44.827 1.00 58.79 C +ATOM 2592 O GLU A 440 -29.221 11.265 46.036 1.00 53.68 O +ATOM 2593 CB GLU A 440 -26.962 12.161 43.843 1.00 60.44 C +ATOM 2594 CG GLU A 440 -25.561 11.696 43.508 1.00 64.52 C +ATOM 2595 CD GLU A 440 -24.684 11.613 44.737 1.00 89.45 C +ATOM 2596 OE1 GLU A 440 -25.219 11.779 45.855 1.00100.00 O +ATOM 2597 OE2 GLU A 440 -23.462 11.388 44.589 1.00 88.09 O +ATOM 2598 N ILE A 441 -30.096 12.154 44.163 1.00 59.70 N +ATOM 2599 CA ILE A 441 -31.285 12.669 44.829 1.00 60.50 C +ATOM 2600 C ILE A 441 -32.195 11.572 45.377 1.00 64.02 C +ATOM 2601 O ILE A 441 -32.649 11.657 46.519 1.00 77.13 O +ATOM 2602 CB ILE A 441 -32.113 13.569 43.887 1.00 58.83 C +ATOM 2603 CG1 ILE A 441 -33.235 14.239 44.678 1.00 47.01 C +ATOM 2604 CG2 ILE A 441 -32.693 12.754 42.742 1.00 65.37 C +ATOM 2605 CD1 ILE A 441 -32.745 15.244 45.685 1.00 35.89 C +ATOM 2606 N GLY A 442 -32.466 10.553 44.564 1.00 49.58 N +ATOM 2607 CA GLY A 442 -33.320 9.466 45.011 1.00 55.28 C +ATOM 2608 C GLY A 442 -32.771 8.817 46.268 1.00 54.37 C +ATOM 2609 O GLY A 442 -33.520 8.425 47.165 1.00 52.70 O +ATOM 2610 N ILE A 443 -31.450 8.695 46.323 1.00 54.90 N +ATOM 2611 CA ILE A 443 -30.779 8.105 47.470 1.00 51.18 C +ATOM 2612 C ILE A 443 -30.938 9.061 48.644 1.00 53.49 C +ATOM 2613 O ILE A 443 -31.126 8.635 49.782 1.00 50.05 O +ATOM 2614 CB ILE A 443 -29.280 7.884 47.177 1.00 48.17 C +ATOM 2615 CG1 ILE A 443 -29.097 6.615 46.337 1.00 49.81 C +ATOM 2616 CG2 ILE A 443 -28.501 7.768 48.476 1.00 55.24 C +ATOM 2617 CD1 ILE A 443 -29.910 6.589 45.049 1.00 50.65 C +ATOM 2618 N LEU A 444 -30.855 10.357 48.347 1.00 43.20 N +ATOM 2619 CA LEU A 444 -31.015 11.403 49.349 1.00 32.45 C +ATOM 2620 C LEU A 444 -32.441 11.290 49.872 1.00 45.17 C +ATOM 2621 O LEU A 444 -32.731 11.657 51.010 1.00 49.34 O +ATOM 2622 CB LEU A 444 -30.792 12.780 48.715 1.00 26.20 C +ATOM 2623 CG LEU A 444 -30.720 14.018 49.618 1.00 15.20 C +ATOM 2624 CD1 LEU A 444 -32.111 14.532 49.897 1.00 28.50 C +ATOM 2625 CD2 LEU A 444 -30.005 13.683 50.906 1.00 24.79 C +ATOM 2626 N CYS A 445 -33.321 10.763 49.024 1.00 37.67 N +ATOM 2627 CA CYS A 445 -34.720 10.563 49.375 1.00 47.14 C +ATOM 2628 C CYS A 445 -34.822 9.374 50.323 1.00 58.91 C +ATOM 2629 O CYS A 445 -35.435 9.462 51.388 1.00 68.68 O +ATOM 2630 CB CYS A 445 -35.550 10.287 48.121 1.00 36.14 C +ATOM 2631 SG CYS A 445 -36.340 11.745 47.423 1.00 51.83 S +ATOM 2632 N SER A 446 -34.209 8.263 49.931 1.00 55.38 N +ATOM 2633 CA SER A 446 -34.228 7.054 50.744 1.00 49.49 C +ATOM 2634 C SER A 446 -33.547 7.297 52.084 1.00 48.41 C +ATOM 2635 O SER A 446 -34.015 6.829 53.124 1.00 41.89 O +ATOM 2636 CB SER A 446 -33.523 5.921 50.005 1.00 31.22 C +ATOM 2637 OG SER A 446 -34.113 5.706 48.735 1.00 49.48 O +ATOM 2638 N ALA A 447 -32.433 8.022 52.051 1.00 46.09 N +ATOM 2639 CA ALA A 447 -31.685 8.342 53.263 1.00 42.91 C +ATOM 2640 C ALA A 447 -32.595 9.023 54.287 1.00 51.10 C +ATOM 2641 O ALA A 447 -32.578 8.694 55.473 1.00 44.02 O +ATOM 2642 CB ALA A 447 -30.510 9.252 52.923 1.00 48.36 C +ATOM 2643 N LEU A 448 -33.397 9.969 53.814 1.00 57.01 N +ATOM 2644 CA LEU A 448 -34.313 10.701 54.678 1.00 52.65 C +ATOM 2645 C LEU A 448 -35.341 9.775 55.316 1.00 52.29 C +ATOM 2646 O LEU A 448 -35.625 9.879 56.508 1.00 54.42 O +ATOM 2647 CB LEU A 448 -35.036 11.788 53.878 1.00 43.89 C +ATOM 2648 CG LEU A 448 -34.202 12.996 53.440 1.00 37.47 C +ATOM 2649 CD1 LEU A 448 -35.054 13.898 52.578 1.00 28.39 C +ATOM 2650 CD2 LEU A 448 -33.692 13.753 54.647 1.00 21.10 C +ATOM 2651 N GLN A 449 -35.893 8.872 54.515 1.00 60.96 N +ATOM 2652 CA GLN A 449 -36.909 7.937 54.987 1.00 82.15 C +ATOM 2653 C GLN A 449 -36.542 7.132 56.238 1.00 92.63 C +ATOM 2654 O GLN A 449 -37.324 7.056 57.185 1.00 94.93 O +ATOM 2655 CB GLN A 449 -37.286 6.979 53.856 1.00 83.67 C +ATOM 2656 CG GLN A 449 -37.907 7.671 52.661 1.00 92.30 C +ATOM 2657 CD GLN A 449 -38.992 8.647 53.067 1.00100.00 C +ATOM 2658 OE1 GLN A 449 -39.961 8.270 53.724 1.00100.00 O +ATOM 2659 NE2 GLN A 449 -38.831 9.910 52.686 1.00 96.42 N +ATOM 2660 N LYS A 450 -35.359 6.525 56.240 1.00 91.95 N +ATOM 2661 CA LYS A 450 -34.929 5.718 57.379 1.00 93.47 C +ATOM 2662 C LYS A 450 -34.544 6.559 58.595 1.00 93.85 C +ATOM 2663 O LYS A 450 -34.690 6.114 59.736 1.00 94.86 O +ATOM 2664 CB LYS A 450 -33.755 4.823 56.976 1.00 90.11 C +ATOM 2665 CG LYS A 450 -32.663 5.538 56.209 1.00100.00 C +ATOM 2666 CD LYS A 450 -31.726 4.546 55.539 1.00100.00 C +ATOM 2667 CE LYS A 450 -30.753 5.266 54.623 1.00100.00 C +ATOM 2668 NZ LYS A 450 -29.790 4.346 53.968 1.00 93.35 N +ATOM 2669 N ILE A 451 -34.056 7.771 58.352 1.00 95.00 N +ATOM 2670 CA ILE A 451 -33.662 8.662 59.434 1.00 89.19 C +ATOM 2671 C ILE A 451 -34.899 9.342 60.029 1.00 90.74 C +ATOM 2672 O ILE A 451 -34.813 10.414 60.629 1.00 83.74 O +ATOM 2673 CB ILE A 451 -32.639 9.730 58.937 1.00 86.00 C +ATOM 2674 CG1 ILE A 451 -31.788 10.220 60.111 1.00 82.61 C +ATOM 2675 CG2 ILE A 451 -33.361 10.887 58.262 1.00 67.45 C +ATOM 2676 CD1 ILE A 451 -30.458 10.809 59.692 1.00 62.56 C +ATOM 2677 N LYS A 452 -36.051 8.701 59.852 1.00 92.93 N +ATOM 2678 CA LYS A 452 -37.329 9.192 60.367 1.00 99.91 C +ATOM 2679 C LYS A 452 -37.757 10.585 59.890 1.00100.00 C +ATOM 2680 O LYS A 452 -38.932 10.941 60.140 1.00100.00 O +ATOM 2681 CB LYS A 452 -37.311 9.161 61.897 1.00 94.91 C +ATOM 2682 CG LYS A 452 -37.685 7.815 62.482 1.00 87.47 C +ATOM 2683 CD LYS A 452 -39.163 7.524 62.282 1.00100.00 C +ATOM 2684 CE LYS A 452 -39.509 6.114 62.732 1.00 99.94 C +ATOM 2685 NZ LYS A 452 -39.007 5.096 61.768 1.00100.00 N +ATOM 2686 OXT LYS A 452 -36.930 11.299 59.282 1.00100.00 O +TER 2687 LYS A 452 +ATOM 2688 N VAL B 118 -36.614 36.412 66.929 1.00 64.02 N +ATOM 2689 CA VAL B 118 -36.683 36.375 65.439 1.00 64.44 C +ATOM 2690 C VAL B 118 -37.879 37.172 64.918 1.00 65.24 C +ATOM 2691 O VAL B 118 -39.025 36.909 65.293 1.00 63.74 O +ATOM 2692 CB VAL B 118 -36.803 34.928 64.931 1.00 65.74 C +ATOM 2693 CG1 VAL B 118 -36.946 34.919 63.419 1.00 65.62 C +ATOM 2694 CG2 VAL B 118 -35.583 34.137 65.352 1.00 53.75 C +ATOM 2695 N PRO B 119 -37.626 38.140 64.017 1.00 55.61 N +ATOM 2696 CA PRO B 119 -38.696 38.972 63.454 1.00 61.71 C +ATOM 2697 C PRO B 119 -39.839 38.152 62.887 1.00 64.92 C +ATOM 2698 O PRO B 119 -39.633 37.043 62.402 1.00 81.22 O +ATOM 2699 CB PRO B 119 -37.995 39.787 62.370 1.00 49.01 C +ATOM 2700 CG PRO B 119 -36.563 39.771 62.741 1.00 55.79 C +ATOM 2701 CD PRO B 119 -36.310 38.478 63.453 1.00 51.02 C +ATOM 2702 N TRP B 120 -41.044 38.708 62.940 1.00 64.84 N +ATOM 2703 CA TRP B 120 -42.219 38.024 62.413 1.00 62.46 C +ATOM 2704 C TRP B 120 -42.288 38.207 60.901 1.00 69.96 C +ATOM 2705 O TRP B 120 -41.996 39.285 60.382 1.00 76.89 O +ATOM 2706 CB TRP B 120 -43.497 38.580 63.050 1.00 59.09 C +ATOM 2707 CG TRP B 120 -44.761 38.047 62.432 1.00 48.35 C +ATOM 2708 CD1 TRP B 120 -45.516 37.005 62.883 1.00 34.32 C +ATOM 2709 CD2 TRP B 120 -45.403 38.520 61.240 1.00 46.82 C +ATOM 2710 NE1 TRP B 120 -46.592 36.803 62.051 1.00 51.44 N +ATOM 2711 CE2 TRP B 120 -46.546 37.719 61.033 1.00 51.56 C +ATOM 2712 CE3 TRP B 120 -45.128 39.552 60.330 1.00 33.47 C +ATOM 2713 CZ2 TRP B 120 -47.416 37.913 59.953 1.00 52.85 C +ATOM 2714 CZ3 TRP B 120 -45.989 39.742 59.252 1.00 52.35 C +ATOM 2715 CH2 TRP B 120 -47.118 38.924 59.073 1.00 61.87 C +ATOM 2716 N PHE B 121 -42.671 37.143 60.203 1.00 63.41 N +ATOM 2717 CA PHE B 121 -42.801 37.182 58.752 1.00 55.67 C +ATOM 2718 C PHE B 121 -44.044 36.412 58.299 1.00 55.41 C +ATOM 2719 O PHE B 121 -44.474 35.453 58.951 1.00 47.46 O +ATOM 2720 CB PHE B 121 -41.544 36.607 58.083 1.00 69.65 C +ATOM 2721 CG PHE B 121 -41.293 35.159 58.391 1.00 69.25 C +ATOM 2722 CD1 PHE B 121 -41.925 34.160 57.658 1.00 68.38 C +ATOM 2723 CD2 PHE B 121 -40.413 34.794 59.403 1.00 67.23 C +ATOM 2724 CE1 PHE B 121 -41.687 32.818 57.927 1.00 65.36 C +ATOM 2725 CE2 PHE B 121 -40.168 33.454 59.681 1.00 80.74 C +ATOM 2726 CZ PHE B 121 -40.807 32.463 58.941 1.00 63.51 C +ATOM 2727 N PRO B 122 -44.642 36.832 57.170 1.00 45.57 N +ATOM 2728 CA PRO B 122 -45.843 36.181 56.627 1.00 40.03 C +ATOM 2729 C PRO B 122 -45.626 34.738 56.170 1.00 48.47 C +ATOM 2730 O PRO B 122 -44.685 34.438 55.434 1.00 63.33 O +ATOM 2731 CB PRO B 122 -46.256 37.093 55.471 1.00 34.57 C +ATOM 2732 CG PRO B 122 -45.005 37.797 55.088 1.00 38.44 C +ATOM 2733 CD PRO B 122 -44.204 37.963 56.336 1.00 36.86 C +ATOM 2734 N ARG B 123 -46.502 33.848 56.620 1.00 46.91 N +ATOM 2735 CA ARG B 123 -46.426 32.444 56.245 1.00 55.38 C +ATOM 2736 C ARG B 123 -47.319 32.221 55.031 1.00 60.11 C +ATOM 2737 O ARG B 123 -47.008 31.409 54.163 1.00 74.63 O +ATOM 2738 CB ARG B 123 -46.893 31.558 57.403 1.00 82.66 C +ATOM 2739 CG ARG B 123 -46.173 31.816 58.718 1.00 92.03 C +ATOM 2740 CD ARG B 123 -44.746 31.300 58.673 1.00 83.78 C +ATOM 2741 NE ARG B 123 -44.225 31.035 60.009 1.00 86.12 N +ATOM 2742 CZ ARG B 123 -44.307 29.859 60.624 1.00100.00 C +ATOM 2743 NH1 ARG B 123 -44.893 28.830 60.025 1.00 90.04 N +ATOM 2744 NH2 ARG B 123 -43.805 29.714 61.844 1.00100.00 N +ATOM 2745 N THR B 124 -48.430 32.952 54.980 1.00 58.91 N +ATOM 2746 CA THR B 124 -49.378 32.847 53.873 1.00 55.42 C +ATOM 2747 C THR B 124 -49.408 34.137 53.074 1.00 55.81 C +ATOM 2748 O THR B 124 -49.051 35.204 53.576 1.00 56.63 O +ATOM 2749 CB THR B 124 -50.814 32.576 54.357 1.00 49.31 C +ATOM 2750 OG1 THR B 124 -50.805 31.528 55.330 1.00 60.93 O +ATOM 2751 CG2 THR B 124 -51.693 32.157 53.191 1.00 53.17 C +ATOM 2752 N ILE B 125 -49.851 34.024 51.827 1.00 55.49 N +ATOM 2753 CA ILE B 125 -49.943 35.159 50.921 1.00 57.08 C +ATOM 2754 C ILE B 125 -50.985 36.161 51.412 1.00 63.27 C +ATOM 2755 O ILE B 125 -50.861 37.365 51.181 1.00 54.52 O +ATOM 2756 CB ILE B 125 -50.322 34.688 49.498 1.00 50.66 C +ATOM 2757 CG1 ILE B 125 -50.192 35.844 48.506 1.00 33.10 C +ATOM 2758 CG2 ILE B 125 -51.742 34.137 49.496 1.00 37.48 C +ATOM 2759 CD1 ILE B 125 -49.939 35.399 47.075 1.00 60.02 C +ATOM 2760 N GLN B 126 -52.008 35.654 52.095 1.00 61.65 N +ATOM 2761 CA GLN B 126 -53.078 36.498 52.614 1.00 67.34 C +ATOM 2762 C GLN B 126 -52.652 37.218 53.887 1.00 61.48 C +ATOM 2763 O GLN B 126 -53.331 38.133 54.349 1.00 71.35 O +ATOM 2764 CB GLN B 126 -54.319 35.651 52.897 1.00 70.45 C +ATOM 2765 CG GLN B 126 -54.785 34.826 51.713 1.00 85.51 C +ATOM 2766 CD GLN B 126 -54.438 33.359 51.854 1.00 92.67 C +ATOM 2767 OE1 GLN B 126 -54.557 32.781 52.934 1.00100.00 O +ATOM 2768 NE2 GLN B 126 -54.011 32.745 50.758 1.00 88.41 N +ATOM 2769 N GLU B 127 -51.526 36.794 54.451 1.00 55.05 N +ATOM 2770 CA GLU B 127 -51.008 37.389 55.677 1.00 54.75 C +ATOM 2771 C GLU B 127 -50.348 38.739 55.434 1.00 57.03 C +ATOM 2772 O GLU B 127 -49.892 39.393 56.372 1.00 52.57 O +ATOM 2773 CB GLU B 127 -50.005 36.446 56.332 1.00 56.80 C +ATOM 2774 CG GLU B 127 -50.618 35.145 56.811 1.00 59.86 C +ATOM 2775 CD GLU B 127 -49.856 34.547 57.975 1.00 72.86 C +ATOM 2776 OE1 GLU B 127 -48.714 34.996 58.223 1.00 78.50 O +ATOM 2777 OE2 GLU B 127 -50.400 33.636 58.640 1.00 70.93 O +ATOM 2778 N LEU B 128 -50.294 39.144 54.169 1.00 57.23 N +ATOM 2779 CA LEU B 128 -49.698 40.419 53.797 1.00 65.38 C +ATOM 2780 C LEU B 128 -50.710 41.527 54.082 1.00 76.67 C +ATOM 2781 O LEU B 128 -50.436 42.715 53.873 1.00 82.72 O +ATOM 2782 CB LEU B 128 -49.333 40.422 52.309 1.00 61.86 C +ATOM 2783 CG LEU B 128 -48.313 39.383 51.832 1.00 74.01 C +ATOM 2784 CD1 LEU B 128 -48.101 39.521 50.335 1.00 63.92 C +ATOM 2785 CD2 LEU B 128 -47.002 39.571 52.570 1.00 76.84 C +ATOM 2786 N ASP B 129 -51.882 41.124 54.566 1.00 73.58 N +ATOM 2787 CA ASP B 129 -52.945 42.064 54.884 1.00 72.89 C +ATOM 2788 C ASP B 129 -52.602 42.919 56.100 1.00 77.94 C +ATOM 2789 O ASP B 129 -53.401 43.745 56.531 1.00 91.15 O +ATOM 2790 CB ASP B 129 -54.255 41.312 55.128 1.00 66.61 C +ATOM 2791 CG ASP B 129 -54.823 40.704 53.860 1.00 77.18 C +ATOM 2792 OD1 ASP B 129 -54.396 41.108 52.756 1.00 70.03 O +ATOM 2793 OD2 ASP B 129 -55.697 39.822 53.972 1.00 78.15 O +ATOM 2794 N ARG B 130 -51.402 42.748 56.638 1.00 77.77 N +ATOM 2795 CA ARG B 130 -50.997 43.522 57.800 1.00 77.83 C +ATOM 2796 C ARG B 130 -50.283 44.811 57.406 1.00 89.16 C +ATOM 2797 O ARG B 130 -50.054 45.024 56.196 1.00 93.49 O +ATOM 2798 CB ARG B 130 -50.092 42.680 58.697 1.00 79.04 C +ATOM 2799 CG ARG B 130 -50.452 41.203 58.733 1.00 92.88 C +ATOM 2800 CD ARG B 130 -51.939 40.986 58.965 1.00 93.62 C +ATOM 2801 NE ARG B 130 -52.345 41.366 60.316 1.00100.00 N +ATOM 2802 CZ ARG B 130 -52.151 40.616 61.397 1.00100.00 C +ATOM 2803 NH1 ARG B 130 -51.557 39.435 61.289 1.00100.00 N +ATOM 2804 NH2 ARG B 130 -52.554 41.046 62.586 1.00 96.27 N +ATOM 2805 N ALA B 144 -43.683 69.602 53.885 1.00 87.98 N +ATOM 2806 CA ALA B 144 -44.210 70.629 52.943 1.00 85.44 C +ATOM 2807 C ALA B 144 -43.355 70.716 51.686 1.00 93.15 C +ATOM 2808 O ALA B 144 -43.809 71.203 50.650 1.00100.00 O +ATOM 2809 CB ALA B 144 -44.261 71.989 53.627 1.00 82.44 C +ATOM 2810 N ASP B 145 -42.115 70.243 51.776 1.00 96.64 N +ATOM 2811 CA ASP B 145 -41.212 70.275 50.628 1.00 97.12 C +ATOM 2812 C ASP B 145 -41.808 69.497 49.456 1.00 91.65 C +ATOM 2813 O ASP B 145 -41.375 69.645 48.311 1.00 74.72 O +ATOM 2814 CB ASP B 145 -39.854 69.678 51.004 1.00 97.58 C +ATOM 2815 CG ASP B 145 -39.949 68.214 51.385 1.00100.00 C +ATOM 2816 OD1 ASP B 145 -40.641 67.900 52.375 1.00 89.65 O +ATOM 2817 OD2 ASP B 145 -39.328 67.376 50.697 1.00100.00 O +ATOM 2818 N HIS B 146 -42.807 68.672 49.752 1.00 93.74 N +ATOM 2819 CA HIS B 146 -43.469 67.860 48.739 1.00 95.79 C +ATOM 2820 C HIS B 146 -44.316 68.717 47.803 1.00 87.42 C +ATOM 2821 O HIS B 146 -45.200 69.453 48.245 1.00 88.11 O +ATOM 2822 CB HIS B 146 -44.352 66.798 49.411 1.00100.00 C +ATOM 2823 CG HIS B 146 -45.083 65.911 48.448 1.00100.00 C +ATOM 2824 ND1 HIS B 146 -46.090 66.370 47.626 1.00100.00 N +ATOM 2825 CD2 HIS B 146 -44.963 64.586 48.187 1.00100.00 C +ATOM 2826 CE1 HIS B 146 -46.560 65.369 46.903 1.00100.00 C +ATOM 2827 NE2 HIS B 146 -45.891 64.275 47.225 1.00100.00 N +ATOM 2828 N PRO B 147 -44.052 68.629 46.489 1.00 74.48 N +ATOM 2829 CA PRO B 147 -44.819 69.415 45.516 1.00 79.69 C +ATOM 2830 C PRO B 147 -46.277 68.964 45.494 1.00 84.11 C +ATOM 2831 O PRO B 147 -46.574 67.798 45.239 1.00 92.23 O +ATOM 2832 CB PRO B 147 -44.106 69.149 44.191 1.00 77.32 C +ATOM 2833 CG PRO B 147 -43.387 67.857 44.399 1.00 77.89 C +ATOM 2834 CD PRO B 147 -43.030 67.787 45.847 1.00 70.78 C +ATOM 2835 N GLY B 148 -47.182 69.896 45.772 1.00 85.27 N +ATOM 2836 CA GLY B 148 -48.597 69.570 45.797 1.00 79.76 C +ATOM 2837 C GLY B 148 -49.124 69.508 47.219 1.00 76.37 C +ATOM 2838 O GLY B 148 -50.289 69.181 47.448 1.00 76.12 O +ATOM 2839 N PHE B 149 -48.255 69.817 48.178 1.00 77.29 N +ATOM 2840 CA PHE B 149 -48.622 69.808 49.590 1.00 85.57 C +ATOM 2841 C PHE B 149 -49.673 70.880 49.860 1.00 87.09 C +ATOM 2842 O PHE B 149 -50.528 70.725 50.735 1.00 81.98 O +ATOM 2843 CB PHE B 149 -47.379 70.069 50.449 1.00 93.71 C +ATOM 2844 CG PHE B 149 -47.668 70.231 51.919 1.00100.00 C +ATOM 2845 CD1 PHE B 149 -47.973 69.126 52.709 1.00100.00 C +ATOM 2846 CD2 PHE B 149 -47.608 71.485 52.520 1.00100.00 C +ATOM 2847 CE1 PHE B 149 -48.211 69.268 54.078 1.00100.00 C +ATOM 2848 CE2 PHE B 149 -47.845 71.635 53.889 1.00 97.35 C +ATOM 2849 CZ PHE B 149 -48.147 70.524 54.666 1.00 95.24 C +ATOM 2850 N LYS B 150 -49.608 71.963 49.092 1.00 81.00 N +ATOM 2851 CA LYS B 150 -50.543 73.070 49.245 1.00 78.43 C +ATOM 2852 C LYS B 150 -51.815 72.865 48.421 1.00 85.73 C +ATOM 2853 O LYS B 150 -52.762 73.643 48.532 1.00 79.74 O +ATOM 2854 CB LYS B 150 -49.858 74.372 48.837 1.00 66.54 C +ATOM 2855 CG LYS B 150 -48.435 74.477 49.361 1.00 77.60 C +ATOM 2856 CD LYS B 150 -47.802 75.820 49.043 1.00 96.50 C +ATOM 2857 CE LYS B 150 -46.537 76.027 49.871 1.00100.00 C +ATOM 2858 NZ LYS B 150 -45.926 77.369 49.658 1.00100.00 N +ATOM 2859 N ASP B 151 -51.840 71.810 47.609 1.00 91.48 N +ATOM 2860 CA ASP B 151 -53.002 71.523 46.776 1.00 95.17 C +ATOM 2861 C ASP B 151 -54.036 70.678 47.507 1.00 93.27 C +ATOM 2862 O ASP B 151 -53.836 69.484 47.716 1.00 93.13 O +ATOM 2863 CB ASP B 151 -52.579 70.808 45.492 1.00 99.66 C +ATOM 2864 CG ASP B 151 -53.707 70.720 44.479 1.00 98.38 C +ATOM 2865 OD1 ASP B 151 -54.866 70.478 44.888 1.00 75.71 O +ATOM 2866 OD2 ASP B 151 -53.440 70.888 43.272 1.00 94.60 O +ATOM 2867 N PRO B 152 -55.168 71.293 47.891 1.00 98.40 N +ATOM 2868 CA PRO B 152 -56.246 70.603 48.607 1.00100.00 C +ATOM 2869 C PRO B 152 -56.891 69.466 47.818 1.00100.00 C +ATOM 2870 O PRO B 152 -57.368 68.493 48.405 1.00 97.06 O +ATOM 2871 CB PRO B 152 -57.251 71.715 48.926 1.00 97.64 C +ATOM 2872 CG PRO B 152 -56.524 72.994 48.678 1.00 96.38 C +ATOM 2873 CD PRO B 152 -55.492 72.704 47.641 1.00 97.39 C +ATOM 2874 N VAL B 153 -56.912 69.591 46.493 1.00 97.45 N +ATOM 2875 CA VAL B 153 -57.506 68.556 45.647 1.00 97.98 C +ATOM 2876 C VAL B 153 -56.565 67.359 45.566 1.00 97.63 C +ATOM 2877 O VAL B 153 -56.851 66.294 46.117 1.00100.00 O +ATOM 2878 CB VAL B 153 -57.787 69.080 44.209 1.00 97.27 C +ATOM 2879 CG1 VAL B 153 -58.065 67.910 43.261 1.00 77.64 C +ATOM 2880 CG2 VAL B 153 -58.980 70.026 44.225 1.00100.00 C +ATOM 2881 N TYR B 154 -55.444 67.549 44.873 1.00 91.74 N +ATOM 2882 CA TYR B 154 -54.436 66.507 44.710 1.00 80.82 C +ATOM 2883 C TYR B 154 -54.205 65.804 46.043 1.00 62.59 C +ATOM 2884 O TYR B 154 -54.020 64.589 46.103 1.00 57.90 O +ATOM 2885 CB TYR B 154 -53.133 67.135 44.198 1.00 87.47 C +ATOM 2886 CG TYR B 154 -51.918 66.237 44.263 1.00100.00 C +ATOM 2887 CD1 TYR B 154 -51.844 65.071 43.499 1.00100.00 C +ATOM 2888 CD2 TYR B 154 -50.829 66.566 45.071 1.00100.00 C +ATOM 2889 CE1 TYR B 154 -50.712 64.256 43.538 1.00 98.74 C +ATOM 2890 CE2 TYR B 154 -49.695 65.759 45.116 1.00100.00 C +ATOM 2891 CZ TYR B 154 -49.643 64.610 44.348 1.00 98.20 C +ATOM 2892 OH TYR B 154 -48.516 63.825 44.383 1.00 94.15 O +ATOM 2893 N ARG B 155 -54.224 66.590 47.110 1.00 51.43 N +ATOM 2894 CA ARG B 155 -54.037 66.075 48.453 1.00 48.13 C +ATOM 2895 C ARG B 155 -55.101 65.023 48.747 1.00 51.81 C +ATOM 2896 O ARG B 155 -54.787 63.853 48.971 1.00 73.68 O +ATOM 2897 CB ARG B 155 -54.152 67.220 49.455 1.00 63.48 C +ATOM 2898 CG ARG B 155 -53.527 66.952 50.802 1.00 82.88 C +ATOM 2899 CD ARG B 155 -53.716 68.157 51.704 1.00 99.89 C +ATOM 2900 NE ARG B 155 -53.214 67.930 53.055 1.00100.00 N +ATOM 2901 CZ ARG B 155 -52.190 68.588 53.586 1.00100.00 C +ATOM 2902 NH1 ARG B 155 -51.556 69.515 52.879 1.00 90.91 N +ATOM 2903 NH2 ARG B 155 -51.807 68.327 54.829 1.00100.00 N +ATOM 2904 N ALA B 156 -56.362 65.450 48.744 1.00 55.36 N +ATOM 2905 CA ALA B 156 -57.484 64.560 49.021 1.00 66.74 C +ATOM 2906 C ALA B 156 -57.583 63.466 47.969 1.00 63.72 C +ATOM 2907 O ALA B 156 -58.215 62.432 48.185 1.00 67.32 O +ATOM 2908 CB ALA B 156 -58.776 65.356 49.070 1.00 81.61 C +ATOM 2909 N ARG B 157 -56.966 63.708 46.821 1.00 57.55 N +ATOM 2910 CA ARG B 157 -56.974 62.728 45.745 1.00 59.91 C +ATOM 2911 C ARG B 157 -56.040 61.588 46.141 1.00 62.43 C +ATOM 2912 O ARG B 157 -56.393 60.409 46.042 1.00 38.28 O +ATOM 2913 CB ARG B 157 -56.486 63.371 44.443 1.00 50.90 C +ATOM 2914 CG ARG B 157 -56.250 62.392 43.310 1.00 55.69 C +ATOM 2915 CD ARG B 157 -57.549 62.063 42.600 1.00 44.80 C +ATOM 2916 NE ARG B 157 -57.321 61.498 41.275 1.00 43.79 N +ATOM 2917 CZ ARG B 157 -58.212 60.764 40.616 1.00 54.54 C +ATOM 2918 NH1 ARG B 157 -59.400 60.504 41.157 1.00 34.07 N +ATOM 2919 NH2 ARG B 157 -57.912 60.288 39.413 1.00 46.44 N +ATOM 2920 N ARG B 158 -54.848 61.955 46.604 1.00 59.50 N +ATOM 2921 CA ARG B 158 -53.848 60.979 47.019 1.00 62.03 C +ATOM 2922 C ARG B 158 -54.275 60.227 48.278 1.00 55.94 C +ATOM 2923 O ARG B 158 -53.712 59.181 48.606 1.00 66.56 O +ATOM 2924 CB ARG B 158 -52.504 61.669 47.257 1.00 71.07 C +ATOM 2925 CG ARG B 158 -51.331 60.703 47.377 1.00 80.09 C +ATOM 2926 CD ARG B 158 -50.000 61.403 47.139 1.00 64.88 C +ATOM 2927 NE ARG B 158 -48.891 60.676 47.748 1.00 60.68 N +ATOM 2928 CZ ARG B 158 -47.609 60.917 47.497 1.00 64.02 C +ATOM 2929 NH1 ARG B 158 -47.267 61.867 46.638 1.00 58.33 N +ATOM 2930 NH2 ARG B 158 -46.668 60.198 48.092 1.00 54.60 N +ATOM 2931 N LYS B 159 -55.258 60.774 48.987 1.00 41.95 N +ATOM 2932 CA LYS B 159 -55.779 60.147 50.198 1.00 50.07 C +ATOM 2933 C LYS B 159 -56.865 59.183 49.745 1.00 37.82 C +ATOM 2934 O LYS B 159 -57.219 58.231 50.439 1.00 49.51 O +ATOM 2935 CB LYS B 159 -56.375 61.204 51.129 1.00 67.92 C +ATOM 2936 CG LYS B 159 -57.110 60.630 52.327 1.00 85.85 C +ATOM 2937 CD LYS B 159 -57.559 61.732 53.271 1.00 93.61 C +ATOM 2938 CE LYS B 159 -58.123 61.164 54.563 1.00 92.11 C +ATOM 2939 NZ LYS B 159 -58.401 62.237 55.559 1.00 97.37 N +ATOM 2940 N GLN B 160 -57.382 59.460 48.556 1.00 29.47 N +ATOM 2941 CA GLN B 160 -58.414 58.655 47.934 1.00 49.18 C +ATOM 2942 C GLN B 160 -57.770 57.350 47.496 1.00 57.94 C +ATOM 2943 O GLN B 160 -58.314 56.261 47.695 1.00 57.37 O +ATOM 2944 CB GLN B 160 -58.944 59.401 46.721 1.00 39.15 C +ATOM 2945 CG GLN B 160 -60.240 58.896 46.178 1.00 58.25 C +ATOM 2946 CD GLN B 160 -60.829 59.863 45.183 1.00 68.54 C +ATOM 2947 OE1 GLN B 160 -60.154 60.785 44.721 1.00 38.86 O +ATOM 2948 NE2 GLN B 160 -62.096 59.666 44.849 1.00 77.60 N +ATOM 2949 N PHE B 161 -56.597 57.481 46.889 1.00 66.93 N +ATOM 2950 CA PHE B 161 -55.843 56.334 46.416 1.00 64.47 C +ATOM 2951 C PHE B 161 -55.436 55.470 47.608 1.00 64.32 C +ATOM 2952 O PHE B 161 -55.665 54.261 47.608 1.00 69.20 O +ATOM 2953 CB PHE B 161 -54.596 56.803 45.659 1.00 65.94 C +ATOM 2954 CG PHE B 161 -54.882 57.343 44.282 1.00 57.74 C +ATOM 2955 CD1 PHE B 161 -54.476 58.627 43.928 1.00 56.22 C +ATOM 2956 CD2 PHE B 161 -55.549 56.570 43.337 1.00 55.99 C +ATOM 2957 CE1 PHE B 161 -54.729 59.135 42.655 1.00 59.72 C +ATOM 2958 CE2 PHE B 161 -55.808 57.070 42.059 1.00 60.29 C +ATOM 2959 CZ PHE B 161 -55.396 58.354 41.720 1.00 65.58 C +ATOM 2960 N ALA B 162 -54.842 56.095 48.623 1.00 50.76 N +ATOM 2961 CA ALA B 162 -54.402 55.381 49.822 1.00 60.51 C +ATOM 2962 C ALA B 162 -55.524 54.551 50.444 1.00 68.51 C +ATOM 2963 O ALA B 162 -55.316 53.395 50.823 1.00 77.70 O +ATOM 2964 CB ALA B 162 -53.859 56.366 50.849 1.00 42.85 C +ATOM 2965 N ASP B 163 -56.709 55.146 50.551 1.00 62.79 N +ATOM 2966 CA ASP B 163 -57.864 54.465 51.128 1.00 74.08 C +ATOM 2967 C ASP B 163 -58.154 53.193 50.344 1.00 72.43 C +ATOM 2968 O ASP B 163 -58.538 52.171 50.918 1.00 82.91 O +ATOM 2969 CB ASP B 163 -59.091 55.380 51.103 1.00 86.21 C +ATOM 2970 CG ASP B 163 -59.213 56.237 52.353 1.00100.00 C +ATOM 2971 OD1 ASP B 163 -59.670 55.720 53.396 1.00100.00 O +ATOM 2972 OD2 ASP B 163 -58.856 57.432 52.291 1.00100.00 O +ATOM 2973 N ILE B 164 -57.981 53.260 49.028 1.00 63.62 N +ATOM 2974 CA ILE B 164 -58.213 52.094 48.188 1.00 57.19 C +ATOM 2975 C ILE B 164 -57.329 50.972 48.720 1.00 63.56 C +ATOM 2976 O ILE B 164 -57.780 49.839 48.887 1.00 51.27 O +ATOM 2977 CB ILE B 164 -57.828 52.360 46.718 1.00 54.96 C +ATOM 2978 CG1 ILE B 164 -58.778 53.383 46.093 1.00 57.18 C +ATOM 2979 CG2 ILE B 164 -57.884 51.069 45.927 1.00 45.83 C +ATOM 2980 CD1 ILE B 164 -58.337 53.885 44.730 1.00 71.75 C +ATOM 2981 N ALA B 165 -56.069 51.315 48.990 1.00 54.17 N +ATOM 2982 CA ALA B 165 -55.078 50.373 49.506 1.00 56.78 C +ATOM 2983 C ALA B 165 -55.517 49.765 50.831 1.00 62.38 C +ATOM 2984 O ALA B 165 -55.558 48.546 50.987 1.00 74.61 O +ATOM 2985 CB ALA B 165 -53.730 51.074 49.678 1.00 46.33 C +ATOM 2986 N TYR B 166 -55.846 50.627 51.784 1.00 57.01 N +ATOM 2987 CA TYR B 166 -56.280 50.182 53.100 1.00 54.60 C +ATOM 2988 C TYR B 166 -57.479 49.241 53.039 1.00 54.08 C +ATOM 2989 O TYR B 166 -57.658 48.395 53.911 1.00 56.28 O +ATOM 2990 CB TYR B 166 -56.627 51.392 53.965 1.00 52.61 C +ATOM 2991 CG TYR B 166 -55.454 52.302 54.230 1.00 67.21 C +ATOM 2992 CD1 TYR B 166 -55.543 53.673 53.996 1.00 76.45 C +ATOM 2993 CD2 TYR B 166 -54.258 51.798 54.730 1.00 79.48 C +ATOM 2994 CE1 TYR B 166 -54.471 54.522 54.258 1.00 72.28 C +ATOM 2995 CE2 TYR B 166 -53.179 52.636 54.995 1.00 79.73 C +ATOM 2996 CZ TYR B 166 -53.292 53.996 54.757 1.00 73.81 C +ATOM 2997 OH TYR B 166 -52.233 54.831 55.033 1.00 73.00 O +ATOM 2998 N ASN B 167 -58.297 49.390 52.005 1.00 50.52 N +ATOM 2999 CA ASN B 167 -59.483 48.556 51.858 1.00 72.73 C +ATOM 3000 C ASN B 167 -59.237 47.320 51.015 1.00 75.36 C +ATOM 3001 O ASN B 167 -60.066 46.411 50.974 1.00 80.40 O +ATOM 3002 CB ASN B 167 -60.618 49.360 51.227 1.00 88.50 C +ATOM 3003 CG ASN B 167 -61.044 50.531 52.082 1.00100.00 C +ATOM 3004 OD1 ASN B 167 -61.402 50.364 53.249 1.00100.00 O +ATOM 3005 ND2 ASN B 167 -61.008 51.727 51.506 1.00100.00 N +ATOM 3006 N TYR B 168 -58.097 47.283 50.338 1.00 66.74 N +ATOM 3007 CA TYR B 168 -57.781 46.148 49.485 1.00 64.80 C +ATOM 3008 C TYR B 168 -57.318 44.903 50.227 1.00 54.51 C +ATOM 3009 O TYR B 168 -56.361 44.940 51.002 1.00 61.97 O +ATOM 3010 CB TYR B 168 -56.717 46.528 48.455 1.00 79.84 C +ATOM 3011 CG TYR B 168 -56.423 45.404 47.493 1.00 86.88 C +ATOM 3012 CD1 TYR B 168 -57.311 45.098 46.462 1.00 90.58 C +ATOM 3013 CD2 TYR B 168 -55.290 44.608 47.646 1.00 83.02 C +ATOM 3014 CE1 TYR B 168 -57.086 44.026 45.615 1.00 75.51 C +ATOM 3015 CE2 TYR B 168 -55.054 43.530 46.803 1.00 82.80 C +ATOM 3016 CZ TYR B 168 -55.957 43.245 45.791 1.00 84.21 C +ATOM 3017 OH TYR B 168 -55.740 42.172 44.959 1.00100.00 O +ATOM 3018 N ARG B 169 -58.007 43.798 49.971 1.00 41.53 N +ATOM 3019 CA ARG B 169 -57.665 42.525 50.577 1.00 61.97 C +ATOM 3020 C ARG B 169 -57.327 41.565 49.444 1.00 62.04 C +ATOM 3021 O ARG B 169 -57.967 41.582 48.393 1.00 60.29 O +ATOM 3022 CB ARG B 169 -58.841 41.992 51.396 1.00 69.44 C +ATOM 3023 CG ARG B 169 -58.740 42.291 52.884 1.00 73.47 C +ATOM 3024 CD ARG B 169 -58.968 43.764 53.171 1.00 61.39 C +ATOM 3025 NE ARG B 169 -58.907 44.054 54.600 1.00 77.33 N +ATOM 3026 CZ ARG B 169 -57.972 44.809 55.169 1.00 89.00 C +ATOM 3027 NH1 ARG B 169 -57.015 45.354 54.431 1.00 92.77 N +ATOM 3028 NH2 ARG B 169 -57.991 45.015 56.478 1.00 99.94 N +ATOM 3029 N HIS B 170 -56.310 40.738 49.659 1.00 68.52 N +ATOM 3030 CA HIS B 170 -55.876 39.781 48.651 1.00 74.68 C +ATOM 3031 C HIS B 170 -57.032 38.941 48.115 1.00 73.45 C +ATOM 3032 O HIS B 170 -58.009 38.678 48.817 1.00 60.55 O +ATOM 3033 CB HIS B 170 -54.789 38.867 49.234 1.00 74.49 C +ATOM 3034 CG HIS B 170 -54.401 37.734 48.335 1.00 80.04 C +ATOM 3035 ND1 HIS B 170 -53.412 37.846 47.378 1.00 79.81 N +ATOM 3036 CD2 HIS B 170 -54.861 36.464 48.250 1.00 81.19 C +ATOM 3037 CE1 HIS B 170 -53.285 36.694 46.745 1.00 90.42 C +ATOM 3038 NE2 HIS B 170 -54.152 35.839 47.254 1.00 85.48 N +ATOM 3039 N GLY B 171 -56.911 38.531 46.856 1.00 76.84 N +ATOM 3040 CA GLY B 171 -57.941 37.715 46.240 1.00 81.18 C +ATOM 3041 C GLY B 171 -58.910 38.474 45.356 1.00 81.66 C +ATOM 3042 O GLY B 171 -59.334 37.965 44.315 1.00 58.86 O +ATOM 3043 N GLN B 172 -59.268 39.687 45.769 1.00 85.56 N +ATOM 3044 CA GLN B 172 -60.198 40.510 45.007 1.00 76.95 C +ATOM 3045 C GLN B 172 -59.452 41.357 43.991 1.00 70.70 C +ATOM 3046 O GLN B 172 -58.316 41.764 44.222 1.00 64.21 O +ATOM 3047 CB GLN B 172 -60.990 41.417 45.944 1.00 73.18 C +ATOM 3048 CG GLN B 172 -60.135 42.427 46.672 1.00 89.81 C +ATOM 3049 CD GLN B 172 -60.712 42.795 48.019 1.00 98.74 C +ATOM 3050 OE1 GLN B 172 -60.700 43.959 48.414 1.00100.00 O +ATOM 3051 NE2 GLN B 172 -61.220 41.800 48.736 1.00100.00 N +ATOM 3052 N PRO B 173 -60.090 41.640 42.847 1.00 73.82 N +ATOM 3053 CA PRO B 173 -59.447 42.450 41.806 1.00 66.22 C +ATOM 3054 C PRO B 173 -59.145 43.874 42.263 1.00 59.56 C +ATOM 3055 O PRO B 173 -59.913 44.477 43.012 1.00 40.19 O +ATOM 3056 CB PRO B 173 -60.440 42.399 40.640 1.00 54.59 C +ATOM 3057 CG PRO B 173 -61.748 42.047 41.261 1.00 72.86 C +ATOM 3058 CD PRO B 173 -61.450 41.218 42.470 1.00 76.58 C +ATOM 3059 N ILE B 174 -58.007 44.397 41.816 1.00 62.65 N +ATOM 3060 CA ILE B 174 -57.602 45.749 42.169 1.00 60.69 C +ATOM 3061 C ILE B 174 -58.601 46.732 41.570 1.00 67.23 C +ATOM 3062 O ILE B 174 -58.821 46.750 40.360 1.00 73.73 O +ATOM 3063 CB ILE B 174 -56.191 46.072 41.626 1.00 55.07 C +ATOM 3064 CG1 ILE B 174 -55.239 44.910 41.908 1.00 58.47 C +ATOM 3065 CG2 ILE B 174 -55.674 47.360 42.252 1.00 60.31 C +ATOM 3066 CD1 ILE B 174 -53.902 45.031 41.211 1.00 68.31 C +ATOM 3067 N PRO B 175 -59.230 47.558 42.417 1.00 64.96 N +ATOM 3068 CA PRO B 175 -60.209 48.534 41.920 1.00 70.00 C +ATOM 3069 C PRO B 175 -59.649 49.457 40.840 1.00 74.14 C +ATOM 3070 O PRO B 175 -58.503 49.894 40.921 1.00 73.56 O +ATOM 3071 CB PRO B 175 -60.632 49.302 43.177 1.00 61.64 C +ATOM 3072 CG PRO B 175 -59.589 48.980 44.204 1.00 67.53 C +ATOM 3073 CD PRO B 175 -59.066 47.629 43.877 1.00 61.93 C +ATOM 3074 N ARG B 176 -60.464 49.750 39.829 1.00 66.46 N +ATOM 3075 CA ARG B 176 -60.037 50.627 38.746 1.00 61.16 C +ATOM 3076 C ARG B 176 -60.332 52.077 39.113 1.00 59.92 C +ATOM 3077 O ARG B 176 -61.205 52.352 39.930 1.00 57.89 O +ATOM 3078 CB ARG B 176 -60.754 50.260 37.444 1.00 50.10 C +ATOM 3079 CG ARG B 176 -60.523 48.826 37.001 1.00 58.89 C +ATOM 3080 CD ARG B 176 -61.349 48.479 35.777 1.00 72.01 C +ATOM 3081 NE ARG B 176 -60.631 47.568 34.895 1.00 70.85 N +ATOM 3082 CZ ARG B 176 -59.918 47.957 33.845 1.00 83.18 C +ATOM 3083 NH1 ARG B 176 -59.825 49.245 33.542 1.00 84.71 N +ATOM 3084 NH2 ARG B 176 -59.295 47.057 33.099 1.00 91.27 N +ATOM 3085 N VAL B 177 -59.597 53.001 38.505 1.00 64.04 N +ATOM 3086 CA VAL B 177 -59.777 54.419 38.788 1.00 60.14 C +ATOM 3087 C VAL B 177 -59.834 55.251 37.512 1.00 65.82 C +ATOM 3088 O VAL B 177 -59.168 54.945 36.524 1.00 63.14 O +ATOM 3089 CB VAL B 177 -58.631 54.951 39.678 1.00 56.50 C +ATOM 3090 CG1 VAL B 177 -58.734 56.454 39.824 1.00 57.11 C +ATOM 3091 CG2 VAL B 177 -58.680 54.288 41.039 1.00 61.23 C +ATOM 3092 N GLU B 178 -60.639 56.307 37.548 1.00 67.94 N +ATOM 3093 CA GLU B 178 -60.795 57.208 36.415 1.00 66.12 C +ATOM 3094 C GLU B 178 -59.830 58.385 36.581 1.00 66.76 C +ATOM 3095 O GLU B 178 -60.185 59.411 37.156 1.00 74.54 O +ATOM 3096 CB GLU B 178 -62.238 57.719 36.355 1.00 63.93 C +ATOM 3097 CG GLU B 178 -62.767 57.963 34.953 1.00 81.95 C +ATOM 3098 CD GLU B 178 -64.274 58.168 34.925 1.00 99.54 C +ATOM 3099 OE1 GLU B 178 -64.737 59.259 35.329 1.00100.00 O +ATOM 3100 OE2 GLU B 178 -64.995 57.238 34.501 1.00 90.80 O +ATOM 3101 N TYR B 179 -58.609 58.230 36.079 1.00 62.63 N +ATOM 3102 CA TYR B 179 -57.594 59.275 36.186 1.00 60.17 C +ATOM 3103 C TYR B 179 -58.006 60.559 35.480 1.00 53.94 C +ATOM 3104 O TYR B 179 -58.723 60.521 34.483 1.00 65.06 O +ATOM 3105 CB TYR B 179 -56.267 58.766 35.623 1.00 57.21 C +ATOM 3106 CG TYR B 179 -55.668 57.658 36.454 1.00 53.03 C +ATOM 3107 CD1 TYR B 179 -54.604 57.908 37.321 1.00 62.41 C +ATOM 3108 CD2 TYR B 179 -56.181 56.364 36.395 1.00 55.44 C +ATOM 3109 CE1 TYR B 179 -54.065 56.898 38.109 1.00 61.06 C +ATOM 3110 CE2 TYR B 179 -55.649 55.345 37.179 1.00 67.16 C +ATOM 3111 CZ TYR B 179 -54.591 55.620 38.034 1.00 71.98 C +ATOM 3112 OH TYR B 179 -54.048 54.617 38.807 1.00 75.67 O +ATOM 3113 N MET B 180 -57.549 61.694 36.004 1.00 44.48 N +ATOM 3114 CA MET B 180 -57.883 62.998 35.434 1.00 51.59 C +ATOM 3115 C MET B 180 -56.842 63.481 34.433 1.00 50.91 C +ATOM 3116 O MET B 180 -55.690 63.051 34.465 1.00 43.45 O +ATOM 3117 CB MET B 180 -58.041 64.035 36.551 1.00 69.37 C +ATOM 3118 CG MET B 180 -58.992 63.605 37.664 1.00 76.18 C +ATOM 3119 SD MET B 180 -59.119 64.774 39.038 1.00 78.79 S +ATOM 3120 CE MET B 180 -57.390 65.309 39.234 1.00 79.39 C +ATOM 3121 N GLU B 181 -57.263 64.385 33.553 1.00 55.45 N +ATOM 3122 CA GLU B 181 -56.390 64.930 32.518 1.00 65.48 C +ATOM 3123 C GLU B 181 -55.148 65.607 33.069 1.00 59.13 C +ATOM 3124 O GLU B 181 -54.062 65.471 32.511 1.00 57.90 O +ATOM 3125 CB GLU B 181 -57.158 65.924 31.645 1.00 73.55 C +ATOM 3126 CG GLU B 181 -57.675 65.332 30.350 1.00 74.18 C +ATOM 3127 CD GLU B 181 -58.807 64.355 30.585 1.00 84.60 C +ATOM 3128 OE1 GLU B 181 -59.431 64.425 31.666 1.00 80.82 O +ATOM 3129 OE2 GLU B 181 -59.070 63.518 29.694 1.00 77.62 O +ATOM 3130 N GLU B 182 -55.311 66.356 34.153 1.00 60.69 N +ATOM 3131 CA GLU B 182 -54.173 67.037 34.754 1.00 72.25 C +ATOM 3132 C GLU B 182 -53.154 65.964 35.122 1.00 76.67 C +ATOM 3133 O GLU B 182 -51.955 66.228 35.216 1.00 82.42 O +ATOM 3134 CB GLU B 182 -54.609 67.810 36.001 1.00 75.93 C +ATOM 3135 CG GLU B 182 -55.565 68.966 35.718 1.00 89.10 C +ATOM 3136 CD GLU B 182 -56.965 68.497 35.351 1.00100.00 C +ATOM 3137 OE1 GLU B 182 -57.657 69.213 34.595 1.00100.00 O +ATOM 3138 OE2 GLU B 182 -57.373 67.412 35.817 1.00100.00 O +ATOM 3139 N GLU B 183 -53.654 64.747 35.319 1.00 69.07 N +ATOM 3140 CA GLU B 183 -52.816 63.605 35.662 1.00 65.03 C +ATOM 3141 C GLU B 183 -52.343 62.924 34.380 1.00 71.81 C +ATOM 3142 O GLU B 183 -51.150 62.675 34.200 1.00 72.45 O +ATOM 3143 CB GLU B 183 -53.605 62.613 36.525 1.00 56.35 C +ATOM 3144 CG GLU B 183 -54.175 63.240 37.789 1.00 66.75 C +ATOM 3145 CD GLU B 183 -55.011 62.277 38.612 1.00 66.56 C +ATOM 3146 OE1 GLU B 183 -55.884 61.595 38.036 1.00 37.84 O +ATOM 3147 OE2 GLU B 183 -54.796 62.208 39.841 1.00 72.41 O +ATOM 3148 N LYS B 184 -53.289 62.633 33.491 1.00 71.29 N +ATOM 3149 CA LYS B 184 -52.982 61.986 32.221 1.00 59.63 C +ATOM 3150 C LYS B 184 -51.944 62.782 31.433 1.00 64.36 C +ATOM 3151 O LYS B 184 -51.228 62.230 30.602 1.00 65.37 O +ATOM 3152 CB LYS B 184 -54.255 61.830 31.388 1.00 52.43 C +ATOM 3153 CG LYS B 184 -55.182 60.725 31.869 1.00 52.57 C +ATOM 3154 CD LYS B 184 -56.373 60.557 30.934 1.00 54.98 C +ATOM 3155 CE LYS B 184 -57.288 59.434 31.398 1.00 56.14 C +ATOM 3156 NZ LYS B 184 -58.481 59.279 30.521 1.00 60.61 N +ATOM 3157 N LYS B 185 -51.870 64.083 31.692 1.00 70.38 N +ATOM 3158 CA LYS B 185 -50.902 64.929 31.007 1.00 70.07 C +ATOM 3159 C LYS B 185 -49.524 64.621 31.564 1.00 64.92 C +ATOM 3160 O LYS B 185 -48.561 64.449 30.816 1.00 65.78 O +ATOM 3161 CB LYS B 185 -51.222 66.407 31.231 1.00 79.66 C +ATOM 3162 CG LYS B 185 -50.220 67.347 30.585 1.00 97.13 C +ATOM 3163 CD LYS B 185 -50.411 68.780 31.052 1.00 95.14 C +ATOM 3164 CE LYS B 185 -49.622 69.752 30.185 1.00 92.79 C +ATOM 3165 NZ LYS B 185 -48.155 69.670 30.436 1.00100.00 N +ATOM 3166 N THR B 186 -49.441 64.552 32.887 1.00 70.70 N +ATOM 3167 CA THR B 186 -48.186 64.259 33.561 1.00 81.19 C +ATOM 3168 C THR B 186 -47.702 62.866 33.174 1.00 82.75 C +ATOM 3169 O THR B 186 -46.502 62.616 33.076 1.00 80.57 O +ATOM 3170 CB THR B 186 -48.352 64.325 35.090 1.00 79.41 C +ATOM 3171 OG1 THR B 186 -49.118 65.484 35.437 1.00 69.39 O +ATOM 3172 CG2 THR B 186 -46.998 64.399 35.769 1.00 88.62 C +ATOM 3173 N TRP B 187 -48.644 61.956 32.961 1.00 82.99 N +ATOM 3174 CA TRP B 187 -48.298 60.596 32.577 1.00 84.80 C +ATOM 3175 C TRP B 187 -47.634 60.624 31.205 1.00 81.96 C +ATOM 3176 O TRP B 187 -46.548 60.075 31.019 1.00 67.97 O +ATOM 3177 CB TRP B 187 -49.559 59.724 32.539 1.00 92.87 C +ATOM 3178 CG TRP B 187 -49.391 58.431 31.799 1.00 91.79 C +ATOM 3179 CD1 TRP B 187 -49.854 58.140 30.548 1.00 84.37 C +ATOM 3180 CD2 TRP B 187 -48.739 57.241 32.271 1.00 98.80 C +ATOM 3181 NE1 TRP B 187 -49.531 56.848 30.212 1.00 99.49 N +ATOM 3182 CE2 TRP B 187 -48.847 56.275 31.248 1.00100.00 C +ATOM 3183 CE3 TRP B 187 -48.073 56.903 33.458 1.00 99.80 C +ATOM 3184 CZ2 TRP B 187 -48.313 54.986 31.378 1.00100.00 C +ATOM 3185 CZ3 TRP B 187 -47.541 55.618 33.585 1.00 89.30 C +ATOM 3186 CH2 TRP B 187 -47.668 54.677 32.550 1.00 96.22 C +ATOM 3187 N GLY B 188 -48.294 61.280 30.255 1.00 83.69 N +ATOM 3188 CA GLY B 188 -47.767 61.379 28.906 1.00 81.98 C +ATOM 3189 C GLY B 188 -46.492 62.198 28.806 1.00 84.97 C +ATOM 3190 O GLY B 188 -45.698 62.009 27.885 1.00 84.72 O +ATOM 3191 N THR B 189 -46.290 63.113 29.748 1.00 82.41 N +ATOM 3192 CA THR B 189 -45.092 63.943 29.742 1.00 86.07 C +ATOM 3193 C THR B 189 -43.887 63.085 30.120 1.00 92.27 C +ATOM 3194 O THR B 189 -42.758 63.363 29.711 1.00100.00 O +ATOM 3195 CB THR B 189 -45.216 65.116 30.739 1.00 93.08 C +ATOM 3196 OG1 THR B 189 -46.256 66.001 30.306 1.00 87.08 O +ATOM 3197 CG2 THR B 189 -43.908 65.893 30.823 1.00 99.21 C +ATOM 3198 N VAL B 190 -44.139 62.040 30.904 1.00 94.30 N +ATOM 3199 CA VAL B 190 -43.084 61.127 31.335 1.00 94.99 C +ATOM 3200 C VAL B 190 -42.996 59.950 30.367 1.00100.00 C +ATOM 3201 O VAL B 190 -41.918 59.410 30.118 1.00100.00 O +ATOM 3202 CB VAL B 190 -43.356 60.581 32.750 1.00 96.95 C +ATOM 3203 CG1 VAL B 190 -42.119 59.871 33.275 1.00100.00 C +ATOM 3204 CG2 VAL B 190 -43.757 61.710 33.676 1.00 93.72 C +ATOM 3205 N PHE B 191 -44.147 59.560 29.826 1.00100.00 N +ATOM 3206 CA PHE B 191 -44.230 58.457 28.875 1.00 93.04 C +ATOM 3207 C PHE B 191 -43.579 58.838 27.546 1.00 97.34 C +ATOM 3208 O PHE B 191 -43.198 57.974 26.760 1.00100.00 O +ATOM 3209 CB PHE B 191 -45.693 58.087 28.639 1.00 89.23 C +ATOM 3210 CG PHE B 191 -45.883 56.848 27.815 1.00 95.04 C +ATOM 3211 CD1 PHE B 191 -46.034 55.607 28.427 1.00100.00 C +ATOM 3212 CD2 PHE B 191 -45.930 56.921 26.425 1.00 91.88 C +ATOM 3213 CE1 PHE B 191 -46.233 54.453 27.666 1.00100.00 C +ATOM 3214 CE2 PHE B 191 -46.128 55.776 25.654 1.00 95.25 C +ATOM 3215 CZ PHE B 191 -46.280 54.539 26.276 1.00 95.85 C +ATOM 3216 N LYS B 192 -43.463 60.137 27.295 1.00 99.92 N +ATOM 3217 CA LYS B 192 -42.850 60.620 26.063 1.00 91.40 C +ATOM 3218 C LYS B 192 -41.360 60.847 26.269 1.00 88.92 C +ATOM 3219 O LYS B 192 -40.537 60.420 25.460 1.00 90.84 O +ATOM 3220 CB LYS B 192 -43.502 61.930 25.622 1.00 89.87 C +ATOM 3221 CG LYS B 192 -42.948 62.483 24.322 1.00 89.83 C +ATOM 3222 CD LYS B 192 -43.617 63.793 23.944 1.00 95.97 C +ATOM 3223 CE LYS B 192 -44.966 63.552 23.284 1.00100.00 C +ATOM 3224 NZ LYS B 192 -44.828 63.083 21.877 1.00 92.77 N +ATOM 3225 N THR B 193 -41.025 61.524 27.363 1.00 81.15 N +ATOM 3226 CA THR B 193 -39.640 61.830 27.698 1.00 85.66 C +ATOM 3227 C THR B 193 -38.766 60.586 27.848 1.00 94.76 C +ATOM 3228 O THR B 193 -37.586 60.607 27.500 1.00100.00 O +ATOM 3229 CB THR B 193 -39.551 62.629 29.011 1.00 78.24 C +ATOM 3230 OG1 THR B 193 -38.175 62.821 29.363 1.00 84.32 O +ATOM 3231 CG2 THR B 193 -40.244 61.883 30.127 1.00 86.03 C +ATOM 3232 N LEU B 194 -39.348 59.505 28.361 1.00100.00 N +ATOM 3233 CA LEU B 194 -38.602 58.265 28.573 1.00100.00 C +ATOM 3234 C LEU B 194 -38.678 57.253 27.426 1.00 93.70 C +ATOM 3235 O LEU B 194 -37.737 56.488 27.204 1.00 82.21 O +ATOM 3236 CB LEU B 194 -39.066 57.597 29.872 1.00 91.86 C +ATOM 3237 CG LEU B 194 -38.785 58.369 31.166 1.00 86.06 C +ATOM 3238 CD1 LEU B 194 -39.424 57.643 32.339 1.00 79.72 C +ATOM 3239 CD2 LEU B 194 -37.287 58.507 31.375 1.00 72.84 C +ATOM 3240 N LYS B 195 -39.792 57.245 26.703 1.00 90.86 N +ATOM 3241 CA LYS B 195 -39.966 56.314 25.594 1.00 93.04 C +ATOM 3242 C LYS B 195 -38.857 56.433 24.554 1.00 98.88 C +ATOM 3243 O LYS B 195 -38.557 55.476 23.835 1.00 99.95 O +ATOM 3244 CB LYS B 195 -41.314 56.541 24.914 1.00 91.45 C +ATOM 3245 CG LYS B 195 -41.628 55.517 23.837 1.00 94.15 C +ATOM 3246 CD LYS B 195 -43.096 55.548 23.452 1.00 98.91 C +ATOM 3247 CE LYS B 195 -43.339 54.760 22.173 1.00100.00 C +ATOM 3248 NZ LYS B 195 -42.958 53.326 22.314 1.00100.00 N +ATOM 3249 N SER B 196 -38.254 57.613 24.473 1.00100.00 N +ATOM 3250 CA SER B 196 -37.185 57.854 23.514 1.00100.00 C +ATOM 3251 C SER B 196 -35.855 57.233 23.940 1.00100.00 C +ATOM 3252 O SER B 196 -35.123 56.691 23.111 1.00100.00 O +ATOM 3253 CB SER B 196 -36.998 59.360 23.308 1.00100.00 C +ATOM 3254 OG SER B 196 -36.493 59.977 24.484 1.00100.00 O +ATOM 3255 N LEU B 197 -35.554 57.304 25.235 1.00100.00 N +ATOM 3256 CA LEU B 197 -34.298 56.776 25.764 1.00 98.58 C +ATOM 3257 C LEU B 197 -34.289 55.302 26.163 1.00 98.97 C +ATOM 3258 O LEU B 197 -33.298 54.820 26.710 1.00 92.55 O +ATOM 3259 CB LEU B 197 -33.853 57.598 26.977 1.00 95.15 C +ATOM 3260 CG LEU B 197 -33.921 59.126 26.908 1.00 86.60 C +ATOM 3261 CD1 LEU B 197 -33.402 59.698 28.215 1.00 88.71 C +ATOM 3262 CD2 LEU B 197 -33.098 59.641 25.740 1.00 83.91 C +ATOM 3263 N TYR B 198 -35.371 54.580 25.894 1.00100.00 N +ATOM 3264 CA TYR B 198 -35.414 53.171 26.273 1.00100.00 C +ATOM 3265 C TYR B 198 -34.663 52.246 25.322 1.00100.00 C +ATOM 3266 O TYR B 198 -33.847 51.434 25.759 1.00 98.32 O +ATOM 3267 CB TYR B 198 -36.862 52.709 26.428 1.00100.00 C +ATOM 3268 CG TYR B 198 -37.453 53.058 27.773 1.00100.00 C +ATOM 3269 CD1 TYR B 198 -36.640 53.178 28.904 1.00100.00 C +ATOM 3270 CD2 TYR B 198 -38.820 53.301 27.914 1.00 95.80 C +ATOM 3271 CE1 TYR B 198 -37.172 53.533 30.140 1.00100.00 C +ATOM 3272 CE2 TYR B 198 -39.363 53.656 29.145 1.00 99.81 C +ATOM 3273 CZ TYR B 198 -38.533 53.772 30.253 1.00100.00 C +ATOM 3274 OH TYR B 198 -39.064 54.120 31.476 1.00100.00 O +ATOM 3275 N LYS B 199 -34.938 52.355 24.028 1.00100.00 N +ATOM 3276 CA LYS B 199 -34.246 51.514 23.055 1.00100.00 C +ATOM 3277 C LYS B 199 -32.763 51.847 23.107 1.00 98.56 C +ATOM 3278 O LYS B 199 -31.910 51.053 22.702 1.00100.00 O +ATOM 3279 CB LYS B 199 -34.780 51.771 21.647 1.00100.00 C +ATOM 3280 CG LYS B 199 -34.889 53.241 21.288 1.00 95.60 C +ATOM 3281 CD LYS B 199 -35.785 53.433 20.077 1.00100.00 C +ATOM 3282 CE LYS B 199 -37.207 52.982 20.376 1.00100.00 C +ATOM 3283 NZ LYS B 199 -37.774 53.690 21.559 1.00 97.17 N +ATOM 3284 N THR B 200 -32.468 53.034 23.617 1.00 91.15 N +ATOM 3285 CA THR B 200 -31.097 53.492 23.726 1.00 95.96 C +ATOM 3286 C THR B 200 -30.414 53.014 25.002 1.00100.00 C +ATOM 3287 O THR B 200 -29.512 52.175 24.960 1.00100.00 O +ATOM 3288 CB THR B 200 -31.030 55.027 23.691 1.00 89.26 C +ATOM 3289 OG1 THR B 200 -31.846 55.512 22.621 1.00100.00 O +ATOM 3290 CG2 THR B 200 -29.595 55.495 23.486 1.00 84.09 C +ATOM 3291 N HIS B 201 -30.858 53.552 26.134 1.00100.00 N +ATOM 3292 CA HIS B 201 -30.272 53.227 27.432 1.00100.00 C +ATOM 3293 C HIS B 201 -30.853 52.025 28.187 1.00100.00 C +ATOM 3294 O HIS B 201 -30.129 51.347 28.921 1.00100.00 O +ATOM 3295 CB HIS B 201 -30.327 54.467 28.334 1.00 98.58 C +ATOM 3296 CG HIS B 201 -29.696 55.685 27.729 1.00100.00 C +ATOM 3297 ND1 HIS B 201 -28.465 55.654 27.108 1.00100.00 N +ATOM 3298 CD2 HIS B 201 -30.123 56.967 27.655 1.00 94.96 C +ATOM 3299 CE1 HIS B 201 -28.161 56.867 26.679 1.00100.00 C +ATOM 3300 NE2 HIS B 201 -29.150 57.682 26.998 1.00 95.85 N +ATOM 3301 N ALA B 202 -32.143 51.755 28.016 1.00 99.68 N +ATOM 3302 CA ALA B 202 -32.779 50.636 28.713 1.00100.00 C +ATOM 3303 C ALA B 202 -32.249 49.277 28.262 1.00100.00 C +ATOM 3304 O ALA B 202 -31.786 49.123 27.132 1.00100.00 O +ATOM 3305 CB ALA B 202 -34.286 50.693 28.525 1.00100.00 C +ATOM 3306 N CYS B 203 -32.325 48.294 29.158 1.00100.00 N +ATOM 3307 CA CYS B 203 -31.852 46.942 28.869 1.00100.00 C +ATOM 3308 C CYS B 203 -32.794 46.178 27.945 1.00100.00 C +ATOM 3309 O CYS B 203 -33.970 46.520 27.808 1.00 96.91 O +ATOM 3310 CB CYS B 203 -31.654 46.161 30.172 1.00 98.58 C +ATOM 3311 SG CYS B 203 -33.178 45.661 31.002 1.00100.00 S +ATOM 3312 N TYR B 204 -32.258 45.134 27.322 1.00 96.51 N +ATOM 3313 CA TYR B 204 -33.006 44.308 26.384 1.00100.00 C +ATOM 3314 C TYR B 204 -34.351 43.802 26.903 1.00100.00 C +ATOM 3315 O TYR B 204 -35.390 44.052 26.292 1.00 90.91 O +ATOM 3316 CB TYR B 204 -32.141 43.120 25.945 1.00100.00 C +ATOM 3317 CG TYR B 204 -32.922 41.955 25.379 1.00100.00 C +ATOM 3318 CD1 TYR B 204 -33.793 42.131 24.303 1.00100.00 C +ATOM 3319 CD2 TYR B 204 -32.796 40.676 25.924 1.00100.00 C +ATOM 3320 CE1 TYR B 204 -34.519 41.063 23.782 1.00100.00 C +ATOM 3321 CE2 TYR B 204 -33.517 39.600 25.411 1.00100.00 C +ATOM 3322 CZ TYR B 204 -34.376 39.802 24.340 1.00100.00 C +ATOM 3323 OH TYR B 204 -35.084 38.746 23.817 1.00100.00 O +ATOM 3324 N GLU B 205 -34.328 43.083 28.021 1.00 97.10 N +ATOM 3325 CA GLU B 205 -35.553 42.530 28.597 1.00 92.62 C +ATOM 3326 C GLU B 205 -36.654 43.579 28.684 1.00 92.80 C +ATOM 3327 O GLU B 205 -37.841 43.255 28.672 1.00 84.27 O +ATOM 3328 CB GLU B 205 -35.272 41.955 29.986 1.00 90.09 C +ATOM 3329 CG GLU B 205 -34.184 40.892 30.008 1.00 94.04 C +ATOM 3330 CD GLU B 205 -32.797 41.475 29.805 1.00100.00 C +ATOM 3331 OE1 GLU B 205 -31.881 40.718 29.418 1.00100.00 O +ATOM 3332 OE2 GLU B 205 -32.623 42.693 30.035 1.00100.00 O +ATOM 3333 N TYR B 206 -36.245 44.840 28.766 1.00 96.17 N +ATOM 3334 CA TYR B 206 -37.179 45.955 28.847 1.00 95.19 C +ATOM 3335 C TYR B 206 -37.727 46.260 27.461 1.00 89.60 C +ATOM 3336 O TYR B 206 -38.939 46.291 27.248 1.00 82.02 O +ATOM 3337 CB TYR B 206 -36.468 47.196 29.398 1.00 96.64 C +ATOM 3338 CG TYR B 206 -37.394 48.297 29.869 1.00100.00 C +ATOM 3339 CD1 TYR B 206 -37.405 48.698 31.205 1.00 96.40 C +ATOM 3340 CD2 TYR B 206 -38.247 48.952 28.977 1.00100.00 C +ATOM 3341 CE1 TYR B 206 -38.238 49.723 31.640 1.00 92.61 C +ATOM 3342 CE2 TYR B 206 -39.084 49.980 29.403 1.00 88.45 C +ATOM 3343 CZ TYR B 206 -39.073 50.358 30.734 1.00 92.44 C +ATOM 3344 OH TYR B 206 -39.897 51.370 31.161 1.00100.00 O +ATOM 3345 N ASN B 207 -36.812 46.487 26.524 1.00 89.21 N +ATOM 3346 CA ASN B 207 -37.168 46.801 25.149 1.00 83.61 C +ATOM 3347 C ASN B 207 -37.959 45.678 24.494 1.00 81.92 C +ATOM 3348 O ASN B 207 -38.674 45.907 23.519 1.00 87.79 O +ATOM 3349 CB ASN B 207 -35.902 47.084 24.337 1.00 84.88 C +ATOM 3350 CG ASN B 207 -35.139 48.295 24.845 1.00 85.25 C +ATOM 3351 OD1 ASN B 207 -35.662 49.409 24.853 1.00 93.52 O +ATOM 3352 ND2 ASN B 207 -33.899 48.083 25.273 1.00 56.40 N +ATOM 3353 N HIS B 208 -37.833 44.468 25.032 1.00 79.44 N +ATOM 3354 CA HIS B 208 -38.541 43.318 24.481 1.00 79.24 C +ATOM 3355 C HIS B 208 -39.998 43.281 24.925 1.00 82.31 C +ATOM 3356 O HIS B 208 -40.906 43.124 24.110 1.00 88.47 O +ATOM 3357 CB HIS B 208 -37.857 42.014 24.900 1.00 71.64 C +ATOM 3358 CG HIS B 208 -38.719 40.800 24.725 1.00 94.11 C +ATOM 3359 ND1 HIS B 208 -39.030 39.951 25.765 1.00100.00 N +ATOM 3360 CD2 HIS B 208 -39.352 40.307 23.635 1.00 97.39 C +ATOM 3361 CE1 HIS B 208 -39.817 38.986 25.323 1.00100.00 C +ATOM 3362 NE2 HIS B 208 -40.029 39.178 24.033 1.00 97.55 N +ATOM 3363 N ILE B 209 -40.212 43.433 26.224 1.00 87.23 N +ATOM 3364 CA ILE B 209 -41.552 43.386 26.789 1.00 88.32 C +ATOM 3365 C ILE B 209 -42.419 44.618 26.548 1.00 88.65 C +ATOM 3366 O ILE B 209 -43.648 44.517 26.506 1.00 79.81 O +ATOM 3367 CB ILE B 209 -41.487 43.134 28.311 1.00 92.64 C +ATOM 3368 CG1 ILE B 209 -42.887 42.823 28.844 1.00100.00 C +ATOM 3369 CG2 ILE B 209 -40.884 44.345 29.015 1.00 84.88 C +ATOM 3370 CD1 ILE B 209 -43.500 41.575 28.247 1.00100.00 C +ATOM 3371 N PHE B 210 -41.786 45.777 26.387 1.00 92.19 N +ATOM 3372 CA PHE B 210 -42.529 47.018 26.187 1.00 91.92 C +ATOM 3373 C PHE B 210 -43.615 46.943 25.123 1.00 96.44 C +ATOM 3374 O PHE B 210 -44.789 47.157 25.419 1.00100.00 O +ATOM 3375 CB PHE B 210 -41.583 48.175 25.864 1.00 89.40 C +ATOM 3376 CG PHE B 210 -41.924 49.453 26.582 1.00 97.33 C +ATOM 3377 CD1 PHE B 210 -42.113 50.638 25.877 1.00 98.81 C +ATOM 3378 CD2 PHE B 210 -42.055 49.471 27.966 1.00 97.14 C +ATOM 3379 CE1 PHE B 210 -42.428 51.822 26.546 1.00100.00 C +ATOM 3380 CE2 PHE B 210 -42.369 50.649 28.643 1.00 86.56 C +ATOM 3381 CZ PHE B 210 -42.555 51.826 27.930 1.00 85.39 C +ATOM 3382 N PRO B 211 -43.242 46.628 23.871 1.00 93.67 N +ATOM 3383 CA PRO B 211 -44.285 46.560 22.841 1.00 92.30 C +ATOM 3384 C PRO B 211 -45.448 45.640 23.215 1.00 94.73 C +ATOM 3385 O PRO B 211 -46.543 45.758 22.660 1.00 82.46 O +ATOM 3386 CB PRO B 211 -43.533 46.083 21.600 1.00 98.76 C +ATOM 3387 CG PRO B 211 -42.102 46.420 21.860 1.00100.00 C +ATOM 3388 CD PRO B 211 -41.909 46.306 23.340 1.00 92.28 C +ATOM 3389 N LEU B 212 -45.208 44.729 24.159 1.00 99.82 N +ATOM 3390 CA LEU B 212 -46.246 43.802 24.615 1.00 97.01 C +ATOM 3391 C LEU B 212 -47.076 44.486 25.697 1.00 97.71 C +ATOM 3392 O LEU B 212 -48.273 44.235 25.832 1.00 97.78 O +ATOM 3393 CB LEU B 212 -45.618 42.527 25.186 1.00 82.77 C +ATOM 3394 CG LEU B 212 -44.915 41.595 24.197 1.00 72.26 C +ATOM 3395 CD1 LEU B 212 -43.927 40.716 24.946 1.00 59.90 C +ATOM 3396 CD2 LEU B 212 -45.943 40.756 23.456 1.00 57.54 C +ATOM 3397 N LEU B 213 -46.421 45.345 26.474 1.00 96.22 N +ATOM 3398 CA LEU B 213 -47.088 46.091 27.533 1.00 93.39 C +ATOM 3399 C LEU B 213 -47.961 47.145 26.864 1.00 93.86 C +ATOM 3400 O LEU B 213 -49.097 47.381 27.274 1.00 84.52 O +ATOM 3401 CB LEU B 213 -46.057 46.780 28.430 1.00 82.97 C +ATOM 3402 CG LEU B 213 -45.335 45.925 29.472 1.00 75.57 C +ATOM 3403 CD1 LEU B 213 -44.108 46.673 29.983 1.00 65.93 C +ATOM 3404 CD2 LEU B 213 -46.291 45.595 30.608 1.00 63.30 C +ATOM 3405 N GLU B 214 -47.410 47.775 25.830 1.00 97.38 N +ATOM 3406 CA GLU B 214 -48.115 48.806 25.084 1.00 94.83 C +ATOM 3407 C GLU B 214 -49.301 48.194 24.358 1.00 95.60 C +ATOM 3408 O GLU B 214 -50.414 48.716 24.417 1.00100.00 O +ATOM 3409 CB GLU B 214 -47.170 49.466 24.073 1.00 96.63 C +ATOM 3410 CG GLU B 214 -45.891 50.020 24.688 1.00100.00 C +ATOM 3411 CD GLU B 214 -44.930 50.587 23.650 1.00100.00 C +ATOM 3412 OE1 GLU B 214 -43.874 49.960 23.406 1.00 99.52 O +ATOM 3413 OE2 GLU B 214 -45.230 51.660 23.079 1.00100.00 O +ATOM 3414 N LYS B 215 -49.056 47.080 23.677 1.00 84.05 N +ATOM 3415 CA LYS B 215 -50.100 46.398 22.926 1.00 96.51 C +ATOM 3416 C LYS B 215 -51.109 45.654 23.799 1.00100.00 C +ATOM 3417 O LYS B 215 -52.183 45.276 23.325 1.00100.00 O +ATOM 3418 CB LYS B 215 -49.474 45.408 21.940 1.00 90.98 C +ATOM 3419 CG LYS B 215 -50.489 44.764 21.005 1.00100.00 C +ATOM 3420 CD LYS B 215 -49.831 43.802 20.030 1.00100.00 C +ATOM 3421 CE LYS B 215 -49.099 44.550 18.924 1.00100.00 C +ATOM 3422 NZ LYS B 215 -50.022 45.378 18.094 1.00100.00 N +ATOM 3423 N TYR B 216 -50.779 45.448 25.071 1.00100.00 N +ATOM 3424 CA TYR B 216 -51.682 44.709 25.945 1.00100.00 C +ATOM 3425 C TYR B 216 -52.264 45.431 27.157 1.00100.00 C +ATOM 3426 O TYR B 216 -53.485 45.526 27.296 1.00100.00 O +ATOM 3427 CB TYR B 216 -50.998 43.413 26.388 1.00 92.17 C +ATOM 3428 CG TYR B 216 -50.873 42.412 25.266 1.00100.00 C +ATOM 3429 CD1 TYR B 216 -49.658 42.219 24.603 1.00100.00 C +ATOM 3430 CD2 TYR B 216 -51.980 41.682 24.837 1.00100.00 C +ATOM 3431 CE1 TYR B 216 -49.551 41.323 23.541 1.00100.00 C +ATOM 3432 CE2 TYR B 216 -51.886 40.786 23.779 1.00100.00 C +ATOM 3433 CZ TYR B 216 -50.671 40.611 23.132 1.00100.00 C +ATOM 3434 OH TYR B 216 -50.578 39.727 22.077 1.00100.00 O +ATOM 3435 N CYS B 217 -51.404 45.942 28.030 1.00 93.36 N +ATOM 3436 CA CYS B 217 -51.883 46.621 29.230 1.00100.00 C +ATOM 3437 C CYS B 217 -52.194 48.107 29.050 1.00 99.81 C +ATOM 3438 O CYS B 217 -52.236 48.867 30.020 1.00100.00 O +ATOM 3439 CB CYS B 217 -50.873 46.434 30.363 1.00100.00 C +ATOM 3440 SG CYS B 217 -50.793 44.744 31.003 1.00 99.81 S +ATOM 3441 N GLY B 218 -52.418 48.514 27.807 1.00 96.48 N +ATOM 3442 CA GLY B 218 -52.733 49.903 27.532 1.00100.00 C +ATOM 3443 C GLY B 218 -51.628 50.890 27.859 1.00100.00 C +ATOM 3444 O GLY B 218 -51.888 51.962 28.411 1.00100.00 O +ATOM 3445 N PHE B 219 -50.394 50.535 27.516 1.00 91.88 N +ATOM 3446 CA PHE B 219 -49.259 51.413 27.774 1.00 85.18 C +ATOM 3447 C PHE B 219 -49.121 52.424 26.638 1.00 81.64 C +ATOM 3448 O PHE B 219 -48.424 52.183 25.654 1.00 74.36 O +ATOM 3449 CB PHE B 219 -47.973 50.591 27.920 1.00 73.24 C +ATOM 3450 CG PHE B 219 -47.648 50.217 29.345 1.00 69.87 C +ATOM 3451 CD1 PHE B 219 -48.500 49.389 30.071 1.00 60.24 C +ATOM 3452 CD2 PHE B 219 -46.496 50.699 29.965 1.00 66.24 C +ATOM 3453 CE1 PHE B 219 -48.210 49.040 31.391 1.00 52.33 C +ATOM 3454 CE2 PHE B 219 -46.197 50.356 31.286 1.00 54.70 C +ATOM 3455 CZ PHE B 219 -47.058 49.527 31.999 1.00 60.48 C +ATOM 3456 N HIS B 220 -49.807 53.555 26.786 1.00 87.91 N +ATOM 3457 CA HIS B 220 -49.788 54.630 25.799 1.00 89.49 C +ATOM 3458 C HIS B 220 -49.810 55.967 26.538 1.00 91.78 C +ATOM 3459 O HIS B 220 -50.430 56.085 27.595 1.00100.00 O +ATOM 3460 CB HIS B 220 -51.011 54.519 24.887 1.00 91.70 C +ATOM 3461 CG HIS B 220 -50.961 55.426 23.700 1.00 99.12 C +ATOM 3462 ND1 HIS B 220 -52.098 55.885 23.067 1.00100.00 N +ATOM 3463 CD2 HIS B 220 -49.915 55.956 23.025 1.00 98.33 C +ATOM 3464 CE1 HIS B 220 -51.752 56.657 22.054 1.00100.00 C +ATOM 3465 NE2 HIS B 220 -50.434 56.718 22.004 1.00100.00 N +ATOM 3466 N GLU B 221 -49.142 56.972 25.983 1.00 82.47 N +ATOM 3467 CA GLU B 221 -49.091 58.282 26.624 1.00 87.65 C +ATOM 3468 C GLU B 221 -50.453 58.933 26.820 1.00 84.85 C +ATOM 3469 O GLU B 221 -50.577 59.890 27.585 1.00 90.10 O +ATOM 3470 CB GLU B 221 -48.195 59.228 25.827 1.00 94.21 C +ATOM 3471 CG GLU B 221 -48.565 59.340 24.363 1.00 96.06 C +ATOM 3472 CD GLU B 221 -47.697 60.344 23.630 1.00100.00 C +ATOM 3473 OE1 GLU B 221 -48.044 60.709 22.485 1.00100.00 O +ATOM 3474 OE2 GLU B 221 -46.669 60.768 24.203 1.00100.00 O +ATOM 3475 N ASP B 222 -51.472 58.415 26.140 1.00 81.47 N +ATOM 3476 CA ASP B 222 -52.811 58.986 26.249 1.00 89.80 C +ATOM 3477 C ASP B 222 -53.705 58.340 27.301 1.00 83.18 C +ATOM 3478 O ASP B 222 -54.786 58.854 27.605 1.00 81.72 O +ATOM 3479 CB ASP B 222 -53.502 58.943 24.888 1.00 99.15 C +ATOM 3480 CG ASP B 222 -52.897 59.924 23.903 1.00100.00 C +ATOM 3481 OD1 ASP B 222 -51.778 59.654 23.418 1.00100.00 O +ATOM 3482 OD2 ASP B 222 -53.532 60.964 23.618 1.00 95.35 O +ATOM 3483 N ASN B 223 -53.264 57.219 27.862 1.00 71.97 N +ATOM 3484 CA ASN B 223 -54.054 56.540 28.880 1.00 72.54 C +ATOM 3485 C ASN B 223 -53.190 55.895 29.955 1.00 72.39 C +ATOM 3486 O ASN B 223 -52.209 55.214 29.650 1.00 73.04 O +ATOM 3487 CB ASN B 223 -54.945 55.470 28.246 1.00 83.69 C +ATOM 3488 CG ASN B 223 -55.626 54.594 29.283 1.00 99.58 C +ATOM 3489 OD1 ASN B 223 -55.320 53.406 29.409 1.00100.00 O +ATOM 3490 ND2 ASN B 223 -56.553 55.180 30.036 1.00 88.17 N +ATOM 3491 N ILE B 224 -53.557 56.115 31.214 1.00 67.74 N +ATOM 3492 CA ILE B 224 -52.821 55.538 32.334 1.00 61.97 C +ATOM 3493 C ILE B 224 -53.280 54.093 32.536 1.00 66.83 C +ATOM 3494 O ILE B 224 -54.469 53.830 32.727 1.00 69.52 O +ATOM 3495 CB ILE B 224 -53.058 56.341 33.628 1.00 58.97 C +ATOM 3496 CG1 ILE B 224 -52.377 57.710 33.518 1.00 50.83 C +ATOM 3497 CG2 ILE B 224 -52.507 55.575 34.818 1.00 64.90 C +ATOM 3498 CD1 ILE B 224 -52.521 58.571 34.755 1.00 53.55 C +ATOM 3499 N PRO B 225 -52.334 53.140 32.503 1.00 65.18 N +ATOM 3500 CA PRO B 225 -52.638 51.715 32.674 1.00 59.04 C +ATOM 3501 C PRO B 225 -53.261 51.344 34.014 1.00 58.77 C +ATOM 3502 O PRO B 225 -52.815 51.802 35.067 1.00 54.44 O +ATOM 3503 CB PRO B 225 -51.290 51.024 32.473 1.00 54.60 C +ATOM 3504 CG PRO B 225 -50.396 52.056 31.868 1.00 49.68 C +ATOM 3505 CD PRO B 225 -50.893 53.376 32.331 1.00 55.63 C +ATOM 3506 N GLN B 226 -54.282 50.490 33.961 1.00 53.98 N +ATOM 3507 CA GLN B 226 -54.979 50.035 35.161 1.00 63.11 C +ATOM 3508 C GLN B 226 -54.264 48.848 35.804 1.00 59.81 C +ATOM 3509 O GLN B 226 -53.986 47.843 35.146 1.00 65.82 O +ATOM 3510 CB GLN B 226 -56.424 49.650 34.825 1.00 71.64 C +ATOM 3511 CG GLN B 226 -57.325 50.835 34.505 1.00 76.63 C +ATOM 3512 CD GLN B 226 -57.642 51.697 35.719 1.00 82.35 C +ATOM 3513 OE1 GLN B 226 -58.736 52.252 35.828 1.00 90.41 O +ATOM 3514 NE2 GLN B 226 -56.686 51.812 36.636 1.00 88.22 N +ATOM 3515 N LEU B 227 -53.987 48.977 37.099 1.00 63.21 N +ATOM 3516 CA LEU B 227 -53.287 47.952 37.864 1.00 61.31 C +ATOM 3517 C LEU B 227 -53.841 46.539 37.718 1.00 53.70 C +ATOM 3518 O LEU B 227 -53.076 45.582 37.593 1.00 46.00 O +ATOM 3519 CB LEU B 227 -53.253 48.339 39.348 1.00 47.53 C +ATOM 3520 CG LEU B 227 -52.548 49.650 39.727 1.00 49.37 C +ATOM 3521 CD1 LEU B 227 -52.004 49.538 41.141 1.00 50.49 C +ATOM 3522 CD2 LEU B 227 -51.418 49.951 38.753 1.00 52.51 C +ATOM 3523 N GLU B 228 -55.162 46.398 37.740 1.00 37.21 N +ATOM 3524 CA GLU B 228 -55.759 45.073 37.609 1.00 44.29 C +ATOM 3525 C GLU B 228 -55.299 44.411 36.314 1.00 59.82 C +ATOM 3526 O GLU B 228 -55.149 43.190 36.244 1.00 57.37 O +ATOM 3527 CB GLU B 228 -57.283 45.167 37.621 1.00 42.37 C +ATOM 3528 CG GLU B 228 -57.962 44.210 38.590 1.00 58.34 C +ATOM 3529 CD GLU B 228 -57.339 42.830 38.602 1.00 49.22 C +ATOM 3530 OE1 GLU B 228 -56.340 42.636 39.324 1.00 76.04 O +ATOM 3531 OE2 GLU B 228 -57.848 41.935 37.896 1.00 42.09 O +ATOM 3532 N ASP B 229 -55.074 45.230 35.292 1.00 63.59 N +ATOM 3533 CA ASP B 229 -54.630 44.742 33.994 1.00 54.71 C +ATOM 3534 C ASP B 229 -53.171 44.326 34.075 1.00 42.14 C +ATOM 3535 O ASP B 229 -52.814 43.197 33.743 1.00 47.78 O +ATOM 3536 CB ASP B 229 -54.802 45.837 32.942 1.00 56.30 C +ATOM 3537 CG ASP B 229 -56.256 46.215 32.727 1.00 59.21 C +ATOM 3538 OD1 ASP B 229 -57.129 45.344 32.928 1.00 47.22 O +ATOM 3539 OD2 ASP B 229 -56.525 47.377 32.358 1.00 48.29 O +ATOM 3540 N VAL B 230 -52.330 45.252 34.518 1.00 24.14 N +ATOM 3541 CA VAL B 230 -50.903 44.986 34.658 1.00 28.23 C +ATOM 3542 C VAL B 230 -50.677 43.766 35.552 1.00 25.59 C +ATOM 3543 O VAL B 230 -49.920 42.860 35.205 1.00 24.96 O +ATOM 3544 CB VAL B 230 -50.171 46.193 35.274 1.00 19.93 C +ATOM 3545 CG1 VAL B 230 -48.666 46.012 35.166 1.00 36.37 C +ATOM 3546 CG2 VAL B 230 -50.609 47.457 34.587 1.00 31.35 C +ATOM 3547 N SER B 231 -51.332 43.748 36.707 1.00 22.23 N +ATOM 3548 CA SER B 231 -51.197 42.632 37.630 1.00 28.79 C +ATOM 3549 C SER B 231 -51.616 41.352 36.911 1.00 37.48 C +ATOM 3550 O SER B 231 -50.844 40.400 36.818 1.00 45.95 O +ATOM 3551 CB SER B 231 -52.075 42.859 38.864 1.00 36.95 C +ATOM 3552 OG SER B 231 -52.123 41.705 39.682 1.00 42.47 O +ATOM 3553 N GLN B 232 -52.846 41.345 36.399 1.00 41.53 N +ATOM 3554 CA GLN B 232 -53.362 40.187 35.682 1.00 36.18 C +ATOM 3555 C GLN B 232 -52.392 39.736 34.597 1.00 48.10 C +ATOM 3556 O GLN B 232 -52.249 38.551 34.327 1.00 63.22 O +ATOM 3557 CB GLN B 232 -54.732 40.498 35.076 1.00 36.85 C +ATOM 3558 CG GLN B 232 -55.712 39.337 35.128 1.00 54.29 C +ATOM 3559 CD GLN B 232 -55.817 38.725 36.510 1.00 65.82 C +ATOM 3560 OE1 GLN B 232 -55.427 37.577 36.723 1.00 83.67 O +ATOM 3561 NE2 GLN B 232 -56.310 39.310 37.597 1.00 20.00 N +ATOM 3562 N PHE B 233 -51.721 40.714 33.990 1.00 50.16 N +ATOM 3563 CA PHE B 233 -50.756 40.444 32.931 1.00 48.93 C +ATOM 3564 C PHE B 233 -49.500 39.800 33.494 1.00 44.11 C +ATOM 3565 O PHE B 233 -49.171 38.661 33.167 1.00 40.81 O +ATOM 3566 CB PHE B 233 -50.381 41.742 32.214 1.00 58.23 C +ATOM 3567 CG PHE B 233 -49.363 41.562 31.121 1.00 63.87 C +ATOM 3568 CD1 PHE B 233 -49.425 40.469 30.261 1.00 57.86 C +ATOM 3569 CD2 PHE B 233 -48.346 42.493 30.947 1.00 69.54 C +ATOM 3570 CE1 PHE B 233 -48.484 40.305 29.245 1.00 55.36 C +ATOM 3571 CE2 PHE B 233 -47.400 42.339 29.935 1.00 66.99 C +ATOM 3572 CZ PHE B 233 -47.470 41.243 29.082 1.00 58.00 C +ATOM 3573 N LEU B 234 -48.800 40.551 34.337 1.00 45.08 N +ATOM 3574 CA LEU B 234 -47.571 40.082 34.970 1.00 51.99 C +ATOM 3575 C LEU B 234 -47.713 38.662 35.509 1.00 54.51 C +ATOM 3576 O LEU B 234 -46.764 37.878 35.482 1.00 67.55 O +ATOM 3577 CB LEU B 234 -47.179 41.020 36.117 1.00 26.78 C +ATOM 3578 CG LEU B 234 -46.432 42.298 35.728 1.00 47.52 C +ATOM 3579 CD1 LEU B 234 -46.381 43.245 36.911 1.00 47.80 C +ATOM 3580 CD2 LEU B 234 -45.030 41.951 35.268 1.00 66.07 C +ATOM 3581 N GLN B 235 -48.901 38.333 35.996 1.00 37.39 N +ATOM 3582 CA GLN B 235 -49.141 37.013 36.549 1.00 39.18 C +ATOM 3583 C GLN B 235 -48.933 35.894 35.536 1.00 49.42 C +ATOM 3584 O GLN B 235 -48.373 34.848 35.870 1.00 66.03 O +ATOM 3585 CB GLN B 235 -50.552 36.952 37.133 1.00 42.47 C +ATOM 3586 CG GLN B 235 -50.714 37.807 38.371 1.00 41.61 C +ATOM 3587 CD GLN B 235 -52.106 37.724 38.962 1.00 51.52 C +ATOM 3588 OE1 GLN B 235 -52.604 36.638 39.251 1.00 50.65 O +ATOM 3589 NE2 GLN B 235 -52.743 38.876 39.145 1.00 69.18 N +ATOM 3590 N THR B 236 -49.376 36.110 34.301 1.00 55.42 N +ATOM 3591 CA THR B 236 -49.227 35.095 33.257 1.00 57.64 C +ATOM 3592 C THR B 236 -47.795 35.000 32.742 1.00 42.79 C +ATOM 3593 O THR B 236 -47.411 33.993 32.145 1.00 40.67 O +ATOM 3594 CB THR B 236 -50.148 35.387 32.064 1.00 57.79 C +ATOM 3595 OG1 THR B 236 -50.062 36.777 31.730 1.00 54.71 O +ATOM 3596 CG2 THR B 236 -51.583 35.028 32.407 1.00 55.37 C +ATOM 3597 N CYS B 237 -47.010 36.049 32.975 1.00 24.06 N +ATOM 3598 CA CYS B 237 -45.616 36.072 32.537 1.00 50.52 C +ATOM 3599 C CYS B 237 -44.703 35.342 33.519 1.00 60.62 C +ATOM 3600 O CYS B 237 -43.974 34.419 33.143 1.00 60.80 O +ATOM 3601 CB CYS B 237 -45.119 37.511 32.386 1.00 39.35 C +ATOM 3602 SG CYS B 237 -46.187 38.564 31.401 1.00 63.59 S +ATOM 3603 N THR B 238 -44.755 35.756 34.783 1.00 56.56 N +ATOM 3604 CA THR B 238 -43.916 35.160 35.815 1.00 48.50 C +ATOM 3605 C THR B 238 -44.710 34.700 37.035 1.00 51.09 C +ATOM 3606 O THR B 238 -44.273 33.821 37.779 1.00 66.44 O +ATOM 3607 CB THR B 238 -42.844 36.159 36.272 1.00 48.09 C +ATOM 3608 OG1 THR B 238 -43.480 37.325 36.804 1.00 63.68 O +ATOM 3609 CG2 THR B 238 -41.971 36.572 35.097 1.00 54.75 C +ATOM 3610 N GLY B 239 -45.883 35.287 37.229 1.00 45.86 N +ATOM 3611 CA GLY B 239 -46.698 34.919 38.370 1.00 37.78 C +ATOM 3612 C GLY B 239 -46.763 36.054 39.370 1.00 36.96 C +ATOM 3613 O GLY B 239 -47.435 35.955 40.394 1.00 40.13 O +ATOM 3614 N PHE B 240 -46.058 37.137 39.064 1.00 37.98 N +ATOM 3615 CA PHE B 240 -46.026 38.309 39.926 1.00 39.99 C +ATOM 3616 C PHE B 240 -47.352 39.051 39.876 1.00 51.84 C +ATOM 3617 O PHE B 240 -47.814 39.448 38.803 1.00 61.74 O +ATOM 3618 CB PHE B 240 -44.906 39.254 39.494 1.00 38.03 C +ATOM 3619 CG PHE B 240 -43.769 39.327 40.465 1.00 45.56 C +ATOM 3620 CD1 PHE B 240 -42.767 38.368 40.450 1.00 44.86 C +ATOM 3621 CD2 PHE B 240 -43.704 40.347 41.403 1.00 59.18 C +ATOM 3622 CE1 PHE B 240 -41.717 38.425 41.354 1.00 59.62 C +ATOM 3623 CE2 PHE B 240 -42.656 40.411 42.312 1.00 63.73 C +ATOM 3624 CZ PHE B 240 -41.661 39.449 42.288 1.00 53.74 C +ATOM 3625 N ARG B 241 -47.962 39.233 41.042 1.00 48.36 N +ATOM 3626 CA ARG B 241 -49.227 39.940 41.126 1.00 38.46 C +ATOM 3627 C ARG B 241 -48.958 41.276 41.777 1.00 30.49 C +ATOM 3628 O ARG B 241 -48.049 41.398 42.589 1.00 40.37 O +ATOM 3629 CB ARG B 241 -50.225 39.153 41.966 1.00 27.27 C +ATOM 3630 CG ARG B 241 -49.584 38.273 43.013 1.00 42.48 C +ATOM 3631 CD ARG B 241 -50.587 37.280 43.539 1.00 38.82 C +ATOM 3632 NE ARG B 241 -50.999 36.343 42.502 1.00 53.54 N +ATOM 3633 CZ ARG B 241 -51.817 35.319 42.715 1.00 67.48 C +ATOM 3634 NH1 ARG B 241 -52.305 35.111 43.929 1.00 50.15 N +ATOM 3635 NH2 ARG B 241 -52.140 34.499 41.721 1.00 83.13 N +ATOM 3636 N LEU B 242 -49.742 42.281 41.417 1.00 31.80 N +ATOM 3637 CA LEU B 242 -49.560 43.596 41.999 1.00 30.17 C +ATOM 3638 C LEU B 242 -50.465 43.753 43.212 1.00 43.05 C +ATOM 3639 O LEU B 242 -51.471 43.059 43.342 1.00 25.42 O +ATOM 3640 CB LEU B 242 -49.882 44.675 40.967 1.00 29.30 C +ATOM 3641 CG LEU B 242 -48.821 44.923 39.891 1.00 49.41 C +ATOM 3642 CD1 LEU B 242 -49.293 46.032 38.961 1.00 57.07 C +ATOM 3643 CD2 LEU B 242 -47.495 45.305 40.535 1.00 25.53 C +ATOM 3644 N ARG B 243 -50.078 44.651 44.111 1.00 51.99 N +ATOM 3645 CA ARG B 243 -50.855 44.939 45.311 1.00 51.87 C +ATOM 3646 C ARG B 243 -50.732 46.426 45.613 1.00 58.50 C +ATOM 3647 O ARG B 243 -49.633 46.937 45.828 1.00 66.87 O +ATOM 3648 CB ARG B 243 -50.356 44.132 46.511 1.00 49.19 C +ATOM 3649 CG ARG B 243 -51.373 44.078 47.636 1.00 47.76 C +ATOM 3650 CD ARG B 243 -50.796 43.518 48.921 1.00 53.15 C +ATOM 3651 NE ARG B 243 -51.715 43.734 50.035 1.00 66.41 N +ATOM 3652 CZ ARG B 243 -52.489 42.791 50.563 1.00 58.98 C +ATOM 3653 NH1 ARG B 243 -52.463 41.556 50.078 1.00 72.19 N +ATOM 3654 NH2 ARG B 243 -53.300 43.082 51.570 1.00 47.51 N +ATOM 3655 N PRO B 244 -51.869 47.140 45.637 1.00 56.82 N +ATOM 3656 CA PRO B 244 -51.855 48.581 45.914 1.00 41.81 C +ATOM 3657 C PRO B 244 -51.452 48.912 47.348 1.00 45.42 C +ATOM 3658 O PRO B 244 -52.141 48.551 48.299 1.00 45.79 O +ATOM 3659 CB PRO B 244 -53.284 49.019 45.593 1.00 22.99 C +ATOM 3660 CG PRO B 244 -54.103 47.791 45.788 1.00 23.84 C +ATOM 3661 CD PRO B 244 -53.233 46.629 45.415 1.00 33.55 C +ATOM 3662 N VAL B 245 -50.326 49.603 47.495 1.00 46.64 N +ATOM 3663 CA VAL B 245 -49.831 49.989 48.811 1.00 57.89 C +ATOM 3664 C VAL B 245 -50.239 51.429 49.097 1.00 73.52 C +ATOM 3665 O VAL B 245 -50.192 52.279 48.206 1.00 78.88 O +ATOM 3666 CB VAL B 245 -48.286 49.877 48.885 1.00 58.34 C +ATOM 3667 CG1 VAL B 245 -47.636 51.023 48.126 1.00 67.35 C +ATOM 3668 CG2 VAL B 245 -47.833 49.873 50.335 1.00 52.31 C +ATOM 3669 N ALA B 246 -50.639 51.699 50.337 1.00 85.17 N +ATOM 3670 CA ALA B 246 -51.050 53.045 50.732 1.00 80.94 C +ATOM 3671 C ALA B 246 -50.049 54.085 50.223 1.00 78.81 C +ATOM 3672 O ALA B 246 -50.377 54.917 49.373 1.00 72.96 O +ATOM 3673 CB ALA B 246 -51.166 53.128 52.251 1.00 83.46 C +ATOM 3674 N GLY B 247 -48.828 54.030 50.747 1.00 73.30 N +ATOM 3675 CA GLY B 247 -47.796 54.961 50.332 1.00 72.06 C +ATOM 3676 C GLY B 247 -46.437 54.292 50.317 1.00 70.96 C +ATOM 3677 O GLY B 247 -45.890 54.002 49.256 1.00 65.10 O +ATOM 3678 N LEU B 248 -45.895 54.045 51.505 1.00 82.56 N +ATOM 3679 CA LEU B 248 -44.588 53.411 51.644 1.00 87.46 C +ATOM 3680 C LEU B 248 -44.627 52.395 52.780 1.00 80.78 C +ATOM 3681 O LEU B 248 -45.562 52.387 53.579 1.00 85.05 O +ATOM 3682 CB LEU B 248 -43.517 54.471 51.936 1.00 91.70 C +ATOM 3683 CG LEU B 248 -43.373 54.956 53.384 1.00100.00 C +ATOM 3684 CD1 LEU B 248 -42.105 55.781 53.520 1.00 95.76 C +ATOM 3685 CD2 LEU B 248 -44.595 55.768 53.781 1.00100.00 C +ATOM 3686 N LEU B 249 -43.616 51.535 52.842 1.00 67.02 N +ATOM 3687 CA LEU B 249 -43.534 50.532 53.895 1.00 63.13 C +ATOM 3688 C LEU B 249 -42.101 50.081 54.136 1.00 65.19 C +ATOM 3689 O LEU B 249 -41.228 50.267 53.293 1.00 49.32 O +ATOM 3690 CB LEU B 249 -44.407 49.320 53.566 1.00 59.40 C +ATOM 3691 CG LEU B 249 -44.772 49.008 52.117 1.00 57.14 C +ATOM 3692 CD1 LEU B 249 -43.519 48.858 51.276 1.00 59.86 C +ATOM 3693 CD2 LEU B 249 -45.598 47.734 52.093 1.00 68.38 C +ATOM 3694 N SER B 250 -41.869 49.495 55.304 1.00 64.35 N +ATOM 3695 CA SER B 250 -40.545 49.022 55.685 1.00 62.49 C +ATOM 3696 C SER B 250 -39.915 48.126 54.625 1.00 70.64 C +ATOM 3697 O SER B 250 -40.619 47.521 53.818 1.00 78.71 O +ATOM 3698 CB SER B 250 -40.635 48.260 57.004 1.00 45.86 C +ATOM 3699 OG SER B 250 -39.420 47.598 57.290 1.00 69.61 O +ATOM 3700 N SER B 251 -38.586 48.050 54.628 1.00 81.86 N +ATOM 3701 CA SER B 251 -37.871 47.210 53.674 1.00 82.78 C +ATOM 3702 C SER B 251 -38.236 45.762 53.955 1.00 77.72 C +ATOM 3703 O SER B 251 -38.366 44.947 53.039 1.00 65.78 O +ATOM 3704 CB SER B 251 -36.359 47.383 53.825 1.00 73.43 C +ATOM 3705 OG SER B 251 -36.021 48.738 54.049 1.00 90.84 O +ATOM 3706 N ARG B 252 -38.394 45.451 55.238 1.00 62.78 N +ATOM 3707 CA ARG B 252 -38.750 44.107 55.656 1.00 58.79 C +ATOM 3708 C ARG B 252 -40.112 43.729 55.086 1.00 63.08 C +ATOM 3709 O ARG B 252 -40.316 42.601 54.642 1.00 78.89 O +ATOM 3710 CB ARG B 252 -38.783 44.025 57.181 1.00 60.93 C +ATOM 3711 CG ARG B 252 -39.238 42.677 57.719 1.00 79.31 C +ATOM 3712 CD ARG B 252 -39.269 42.683 59.234 1.00 94.81 C +ATOM 3713 NE ARG B 252 -37.958 42.987 59.801 1.00 99.40 N +ATOM 3714 CZ ARG B 252 -36.929 42.145 59.797 1.00 85.17 C +ATOM 3715 NH1 ARG B 252 -37.058 40.943 59.253 1.00 76.66 N +ATOM 3716 NH2 ARG B 252 -35.775 42.503 60.344 1.00 73.12 N +ATOM 3717 N ASP B 253 -41.041 44.681 55.100 1.00 62.76 N +ATOM 3718 CA ASP B 253 -42.392 44.448 54.593 1.00 57.99 C +ATOM 3719 C ASP B 253 -42.413 44.387 53.075 1.00 60.84 C +ATOM 3720 O ASP B 253 -43.062 43.521 52.484 1.00 47.13 O +ATOM 3721 CB ASP B 253 -43.325 45.558 55.063 1.00 62.86 C +ATOM 3722 CG ASP B 253 -43.441 45.617 56.562 1.00 82.05 C +ATOM 3723 OD1 ASP B 253 -42.508 46.147 57.205 1.00 84.11 O +ATOM 3724 OD2 ASP B 253 -44.463 45.131 57.095 1.00 82.41 O +ATOM 3725 N PHE B 254 -41.713 45.323 52.447 1.00 71.62 N +ATOM 3726 CA PHE B 254 -41.639 45.370 50.995 1.00 81.25 C +ATOM 3727 C PHE B 254 -41.059 44.048 50.500 1.00 77.02 C +ATOM 3728 O PHE B 254 -41.704 43.313 49.748 1.00 80.30 O +ATOM 3729 CB PHE B 254 -40.743 46.534 50.559 1.00 85.08 C +ATOM 3730 CG PHE B 254 -40.869 46.898 49.105 1.00 92.74 C +ATOM 3731 CD1 PHE B 254 -41.713 46.185 48.257 1.00100.00 C +ATOM 3732 CD2 PHE B 254 -40.139 47.963 48.585 1.00100.00 C +ATOM 3733 CE1 PHE B 254 -41.824 46.527 46.912 1.00100.00 C +ATOM 3734 CE2 PHE B 254 -40.244 48.313 47.240 1.00100.00 C +ATOM 3735 CZ PHE B 254 -41.087 47.595 46.404 1.00100.00 C +ATOM 3736 N LEU B 255 -39.838 43.755 50.936 1.00 65.08 N +ATOM 3737 CA LEU B 255 -39.150 42.530 50.552 1.00 52.40 C +ATOM 3738 C LEU B 255 -39.988 41.289 50.850 1.00 49.55 C +ATOM 3739 O LEU B 255 -39.991 40.331 50.080 1.00 58.75 O +ATOM 3740 CB LEU B 255 -37.806 42.441 51.279 1.00 42.75 C +ATOM 3741 CG LEU B 255 -36.633 43.180 50.622 1.00 49.61 C +ATOM 3742 CD1 LEU B 255 -37.130 44.391 49.853 1.00 39.36 C +ATOM 3743 CD2 LEU B 255 -35.638 43.590 51.692 1.00 52.31 C +ATOM 3744 N GLY B 256 -40.700 41.308 51.971 1.00 48.37 N +ATOM 3745 CA GLY B 256 -41.526 40.169 52.330 1.00 51.48 C +ATOM 3746 C GLY B 256 -42.554 39.836 51.262 1.00 56.98 C +ATOM 3747 O GLY B 256 -42.925 38.675 51.081 1.00 43.96 O +ATOM 3748 N GLY B 257 -43.023 40.856 50.552 1.00 63.18 N +ATOM 3749 CA GLY B 257 -44.003 40.626 49.510 1.00 66.05 C +ATOM 3750 C GLY B 257 -43.383 39.868 48.355 1.00 56.41 C +ATOM 3751 O GLY B 257 -44.022 39.017 47.742 1.00 59.16 O +ATOM 3752 N LEU B 258 -42.123 40.176 48.067 1.00 37.56 N +ATOM 3753 CA LEU B 258 -41.396 39.543 46.973 1.00 32.65 C +ATOM 3754 C LEU B 258 -41.315 38.027 47.127 1.00 32.75 C +ATOM 3755 O LEU B 258 -41.258 37.299 46.137 1.00 42.08 O +ATOM 3756 CB LEU B 258 -39.985 40.140 46.871 1.00 17.19 C +ATOM 3757 CG LEU B 258 -39.918 41.665 46.736 1.00 48.83 C +ATOM 3758 CD1 LEU B 258 -38.495 42.148 47.004 1.00 28.30 C +ATOM 3759 CD2 LEU B 258 -40.392 42.072 45.347 1.00 48.32 C +ATOM 3760 N ALA B 259 -41.310 37.557 48.370 1.00 32.23 N +ATOM 3761 CA ALA B 259 -41.233 36.127 48.658 1.00 28.79 C +ATOM 3762 C ALA B 259 -42.428 35.387 48.086 1.00 30.15 C +ATOM 3763 O ALA B 259 -42.395 34.166 47.937 1.00 34.54 O +ATOM 3764 CB ALA B 259 -41.163 35.899 50.160 1.00 38.29 C +ATOM 3765 N PHE B 260 -43.491 36.129 47.781 1.00 38.35 N +ATOM 3766 CA PHE B 260 -44.709 35.544 47.224 1.00 28.17 C +ATOM 3767 C PHE B 260 -44.920 36.036 45.810 1.00 32.46 C +ATOM 3768 O PHE B 260 -45.983 35.822 45.225 1.00 29.36 O +ATOM 3769 CB PHE B 260 -45.922 35.926 48.068 1.00 23.46 C +ATOM 3770 CG PHE B 260 -45.761 35.628 49.521 1.00 23.16 C +ATOM 3771 CD1 PHE B 260 -44.996 36.455 50.331 1.00 21.32 C +ATOM 3772 CD2 PHE B 260 -46.362 34.507 50.083 1.00 30.85 C +ATOM 3773 CE1 PHE B 260 -44.832 36.167 51.684 1.00 42.56 C +ATOM 3774 CE2 PHE B 260 -46.204 34.209 51.436 1.00 18.09 C +ATOM 3775 CZ PHE B 260 -45.440 35.039 52.237 1.00 14.90 C +ATOM 3776 N ARG B 261 -43.901 36.699 45.268 1.00 43.21 N +ATOM 3777 CA ARG B 261 -43.965 37.245 43.920 1.00 52.93 C +ATOM 3778 C ARG B 261 -45.102 38.263 43.874 1.00 61.31 C +ATOM 3779 O ARG B 261 -45.873 38.327 42.911 1.00 65.05 O +ATOM 3780 CB ARG B 261 -44.200 36.128 42.902 1.00 58.77 C +ATOM 3781 CG ARG B 261 -43.047 35.151 42.812 1.00 65.11 C +ATOM 3782 CD ARG B 261 -42.894 34.573 41.419 1.00 72.90 C +ATOM 3783 NE ARG B 261 -41.849 33.556 41.401 1.00 66.80 N +ATOM 3784 CZ ARG B 261 -41.228 33.131 40.309 1.00 62.18 C +ATOM 3785 NH1 ARG B 261 -41.533 33.639 39.124 1.00 64.89 N +ATOM 3786 NH2 ARG B 261 -40.283 32.206 40.408 1.00 78.44 N +ATOM 3787 N VAL B 262 -45.191 39.045 44.948 1.00 47.17 N +ATOM 3788 CA VAL B 262 -46.195 40.089 45.089 1.00 38.17 C +ATOM 3789 C VAL B 262 -45.486 41.444 45.175 1.00 38.46 C +ATOM 3790 O VAL B 262 -44.604 41.640 46.015 1.00 35.95 O +ATOM 3791 CB VAL B 262 -47.040 39.881 46.367 1.00 16.94 C +ATOM 3792 CG1 VAL B 262 -47.867 41.120 46.652 1.00 15.75 C +ATOM 3793 CG2 VAL B 262 -47.948 38.668 46.200 1.00 13.76 C +ATOM 3794 N PHE B 263 -45.870 42.371 44.303 1.00 44.65 N +ATOM 3795 CA PHE B 263 -45.265 43.695 44.289 1.00 56.23 C +ATOM 3796 C PHE B 263 -46.218 44.747 44.843 1.00 64.47 C +ATOM 3797 O PHE B 263 -47.352 44.875 44.384 1.00 75.10 O +ATOM 3798 CB PHE B 263 -44.863 44.075 42.863 1.00 45.33 C +ATOM 3799 CG PHE B 263 -44.028 45.324 42.779 1.00 54.31 C +ATOM 3800 CD1 PHE B 263 -42.919 45.494 43.601 1.00 58.96 C +ATOM 3801 CD2 PHE B 263 -44.347 46.331 41.871 1.00 60.80 C +ATOM 3802 CE1 PHE B 263 -42.138 46.649 43.516 1.00 62.13 C +ATOM 3803 CE2 PHE B 263 -43.571 47.490 41.780 1.00 62.38 C +ATOM 3804 CZ PHE B 263 -42.467 47.649 42.603 1.00 62.30 C +ATOM 3805 N HIS B 264 -45.754 45.499 45.836 1.00 56.84 N +ATOM 3806 CA HIS B 264 -46.572 46.544 46.438 1.00 50.73 C +ATOM 3807 C HIS B 264 -46.416 47.813 45.610 1.00 52.79 C +ATOM 3808 O HIS B 264 -45.410 48.518 45.693 1.00 42.06 O +ATOM 3809 CB HIS B 264 -46.148 46.764 47.895 1.00 60.26 C +ATOM 3810 CG HIS B 264 -46.536 45.640 48.802 1.00 66.12 C +ATOM 3811 ND1 HIS B 264 -47.659 45.679 49.601 1.00 64.49 N +ATOM 3812 CD2 HIS B 264 -45.978 44.420 48.998 1.00 62.27 C +ATOM 3813 CE1 HIS B 264 -47.775 44.531 50.250 1.00 54.65 C +ATOM 3814 NE2 HIS B 264 -46.769 43.755 49.900 1.00 65.71 N +ATOM 3815 N CYS B 265 -47.436 48.089 44.805 1.00 70.90 N +ATOM 3816 CA CYS B 265 -47.435 49.237 43.909 1.00 78.16 C +ATOM 3817 C CYS B 265 -48.309 50.406 44.355 1.00 78.58 C +ATOM 3818 O CYS B 265 -49.303 50.231 45.063 1.00 77.71 O +ATOM 3819 CB CYS B 265 -47.867 48.774 42.515 1.00 71.85 C +ATOM 3820 SG CYS B 265 -47.906 50.055 41.257 1.00 92.69 S +ATOM 3821 N THR B 266 -47.912 51.601 43.928 1.00 70.23 N +ATOM 3822 CA THR B 266 -48.629 52.833 44.233 1.00 59.70 C +ATOM 3823 C THR B 266 -49.603 53.135 43.092 1.00 54.47 C +ATOM 3824 O THR B 266 -49.217 53.145 41.923 1.00 54.63 O +ATOM 3825 CB THR B 266 -47.653 54.019 44.380 1.00 55.29 C +ATOM 3826 OG1 THR B 266 -47.137 54.381 43.093 1.00 37.72 O +ATOM 3827 CG2 THR B 266 -46.496 53.642 45.286 1.00 59.90 C +ATOM 3828 N GLN B 267 -50.865 53.378 43.433 1.00 44.15 N +ATOM 3829 CA GLN B 267 -51.881 53.671 42.428 1.00 43.60 C +ATOM 3830 C GLN B 267 -51.917 55.148 42.057 1.00 41.75 C +ATOM 3831 O GLN B 267 -52.416 55.512 40.993 1.00 28.69 O +ATOM 3832 CB GLN B 267 -53.259 53.246 42.936 1.00 45.29 C +ATOM 3833 CG GLN B 267 -54.383 53.474 41.944 1.00 34.06 C +ATOM 3834 CD GLN B 267 -55.212 52.224 41.703 1.00 59.87 C +ATOM 3835 OE1 GLN B 267 -55.741 51.619 42.642 1.00 57.98 O +ATOM 3836 NE2 GLN B 267 -55.335 51.833 40.436 1.00 68.10 N +ATOM 3837 N TYR B 268 -51.378 55.991 42.934 1.00 50.13 N +ATOM 3838 CA TYR B 268 -51.364 57.432 42.706 1.00 55.50 C +ATOM 3839 C TYR B 268 -50.285 57.930 41.743 1.00 57.92 C +ATOM 3840 O TYR B 268 -49.548 57.141 41.150 1.00 50.68 O +ATOM 3841 CB TYR B 268 -51.261 58.174 44.046 1.00 64.16 C +ATOM 3842 CG TYR B 268 -49.999 57.914 44.841 1.00 65.73 C +ATOM 3843 CD1 TYR B 268 -48.819 58.605 44.559 1.00 64.71 C +ATOM 3844 CD2 TYR B 268 -49.996 57.011 45.907 1.00 79.87 C +ATOM 3845 CE1 TYR B 268 -47.669 58.411 45.321 1.00 76.68 C +ATOM 3846 CE2 TYR B 268 -48.850 56.809 46.677 1.00 90.35 C +ATOM 3847 CZ TYR B 268 -47.689 57.512 46.380 1.00 89.09 C +ATOM 3848 OH TYR B 268 -46.557 57.328 47.149 1.00 82.46 O +ATOM 3849 N ILE B 269 -50.201 59.251 41.599 1.00 62.65 N +ATOM 3850 CA ILE B 269 -49.236 59.876 40.698 1.00 61.05 C +ATOM 3851 C ILE B 269 -48.692 61.198 41.232 1.00 56.59 C +ATOM 3852 O ILE B 269 -49.374 61.906 41.971 1.00 53.39 O +ATOM 3853 CB ILE B 269 -49.871 60.159 39.327 1.00 70.67 C +ATOM 3854 CG1 ILE B 269 -48.848 60.823 38.404 1.00 68.86 C +ATOM 3855 CG2 ILE B 269 -51.088 61.059 39.502 1.00 74.10 C +ATOM 3856 CD1 ILE B 269 -49.304 60.939 36.972 1.00 82.60 C +ATOM 3857 N ARG B 270 -47.467 61.530 40.836 1.00 64.18 N +ATOM 3858 CA ARG B 270 -46.820 62.764 41.259 1.00 70.10 C +ATOM 3859 C ARG B 270 -47.694 63.956 40.893 1.00 79.83 C +ATOM 3860 O ARG B 270 -48.646 63.824 40.126 1.00 80.48 O +ATOM 3861 CB ARG B 270 -45.464 62.900 40.570 1.00 65.85 C +ATOM 3862 CG ARG B 270 -45.550 62.888 39.054 1.00 66.82 C +ATOM 3863 CD ARG B 270 -44.172 62.910 38.429 1.00 81.52 C +ATOM 3864 NE ARG B 270 -43.675 61.562 38.172 1.00 87.21 N +ATOM 3865 CZ ARG B 270 -42.731 61.273 37.284 1.00 88.22 C +ATOM 3866 NH1 ARG B 270 -42.178 62.238 36.562 1.00 90.32 N +ATOM 3867 NH2 ARG B 270 -42.338 60.019 37.118 1.00 75.36 N +ATOM 3868 N HIS B 271 -47.373 65.121 41.446 1.00 86.18 N +ATOM 3869 CA HIS B 271 -48.139 66.324 41.149 1.00 90.54 C +ATOM 3870 C HIS B 271 -47.652 66.930 39.841 1.00 85.85 C +ATOM 3871 O HIS B 271 -46.453 66.954 39.564 1.00 64.73 O +ATOM 3872 CB HIS B 271 -48.003 67.355 42.272 1.00 95.52 C +ATOM 3873 CG HIS B 271 -48.968 68.493 42.156 1.00 89.69 C +ATOM 3874 ND1 HIS B 271 -48.561 69.798 41.981 1.00 76.85 N +ATOM 3875 CD2 HIS B 271 -50.322 68.519 42.161 1.00 91.52 C +ATOM 3876 CE1 HIS B 271 -49.624 70.578 41.882 1.00 88.56 C +ATOM 3877 NE2 HIS B 271 -50.704 69.825 41.988 1.00 92.65 N +ATOM 3878 N GLY B 272 -48.593 67.426 39.047 1.00 87.30 N +ATOM 3879 CA GLY B 272 -48.253 68.016 37.766 1.00 95.34 C +ATOM 3880 C GLY B 272 -47.317 69.212 37.789 1.00 97.82 C +ATOM 3881 O GLY B 272 -46.806 69.603 36.740 1.00 89.23 O +ATOM 3882 N SER B 273 -47.087 69.801 38.960 1.00 99.95 N +ATOM 3883 CA SER B 273 -46.199 70.960 39.055 1.00 94.57 C +ATOM 3884 C SER B 273 -44.850 70.649 38.420 1.00 82.28 C +ATOM 3885 O SER B 273 -44.390 71.368 37.534 1.00 87.61 O +ATOM 3886 CB SER B 273 -46.007 71.382 40.519 1.00100.00 C +ATOM 3887 OG SER B 273 -45.427 70.348 41.293 1.00 92.20 O +ATOM 3888 N LYS B 274 -44.225 69.570 38.877 1.00 77.90 N +ATOM 3889 CA LYS B 274 -42.938 69.148 38.341 1.00 89.43 C +ATOM 3890 C LYS B 274 -43.052 67.708 37.846 1.00 94.52 C +ATOM 3891 O LYS B 274 -42.761 66.758 38.575 1.00 86.19 O +ATOM 3892 CB LYS B 274 -41.853 69.272 39.414 1.00 89.55 C +ATOM 3893 CG LYS B 274 -41.369 70.704 39.616 1.00 92.41 C +ATOM 3894 CD LYS B 274 -40.805 71.285 38.324 1.00 99.23 C +ATOM 3895 CE LYS B 274 -40.452 72.758 38.479 1.00 99.82 C +ATOM 3896 NZ LYS B 274 -40.050 73.381 37.185 1.00100.00 N +ATOM 3897 N PRO B 275 -43.491 67.538 36.586 1.00100.00 N +ATOM 3898 CA PRO B 275 -43.669 66.230 35.944 1.00100.00 C +ATOM 3899 C PRO B 275 -42.367 65.507 35.607 1.00 92.42 C +ATOM 3900 O PRO B 275 -42.377 64.474 34.934 1.00 86.52 O +ATOM 3901 CB PRO B 275 -44.487 66.554 34.695 1.00100.00 C +ATOM 3902 CG PRO B 275 -44.133 67.963 34.375 1.00100.00 C +ATOM 3903 CD PRO B 275 -43.848 68.647 35.681 1.00 98.17 C +ATOM 3904 N MET B 276 -41.249 66.049 36.081 1.00 81.69 N +ATOM 3905 CA MET B 276 -39.947 65.444 35.826 1.00 91.13 C +ATOM 3906 C MET B 276 -39.250 65.096 37.138 1.00 93.32 C +ATOM 3907 O MET B 276 -38.050 64.821 37.165 1.00100.00 O +ATOM 3908 CB MET B 276 -39.074 66.404 35.012 1.00100.00 C +ATOM 3909 CG MET B 276 -38.520 65.815 33.721 1.00100.00 C +ATOM 3910 SD MET B 276 -39.786 65.096 32.646 1.00100.00 S +ATOM 3911 CE MET B 276 -39.536 63.354 32.966 1.00100.00 C +ATOM 3912 N TYR B 277 -40.013 65.103 38.225 1.00 90.51 N +ATOM 3913 CA TYR B 277 -39.458 64.791 39.531 1.00 93.75 C +ATOM 3914 C TYR B 277 -40.507 64.265 40.503 1.00 95.85 C +ATOM 3915 O TYR B 277 -41.626 64.780 40.570 1.00 94.33 O +ATOM 3916 CB TYR B 277 -38.790 66.032 40.123 1.00100.00 C +ATOM 3917 CG TYR B 277 -38.720 66.023 41.631 1.00 98.17 C +ATOM 3918 CD1 TYR B 277 -37.804 65.212 42.297 1.00100.00 C +ATOM 3919 CD2 TYR B 277 -39.574 66.819 42.393 1.00 88.77 C +ATOM 3920 CE1 TYR B 277 -37.740 65.193 43.684 1.00100.00 C +ATOM 3921 CE2 TYR B 277 -39.519 66.807 43.780 1.00 94.70 C +ATOM 3922 CZ TYR B 277 -38.599 65.993 44.420 1.00100.00 C +ATOM 3923 OH TYR B 277 -38.534 65.987 45.795 1.00100.00 O +ATOM 3924 N THR B 278 -40.128 63.236 41.253 1.00 95.17 N +ATOM 3925 CA THR B 278 -41.008 62.633 42.248 1.00 98.21 C +ATOM 3926 C THR B 278 -40.183 62.325 43.493 1.00 93.52 C +ATOM 3927 O THR B 278 -39.116 61.717 43.410 1.00 89.12 O +ATOM 3928 CB THR B 278 -41.651 61.331 41.726 1.00100.00 C +ATOM 3929 OG1 THR B 278 -41.895 61.454 40.319 1.00100.00 O +ATOM 3930 CG2 THR B 278 -42.968 61.078 42.438 1.00 97.39 C +ATOM 3931 N PRO B 279 -40.672 62.739 44.672 1.00 96.39 N +ATOM 3932 CA PRO B 279 -39.940 62.489 45.918 1.00 95.92 C +ATOM 3933 C PRO B 279 -40.085 61.053 46.409 1.00 87.33 C +ATOM 3934 O PRO B 279 -39.436 60.638 47.366 1.00 85.43 O +ATOM 3935 CB PRO B 279 -40.547 63.494 46.891 1.00 99.85 C +ATOM 3936 CG PRO B 279 -41.942 63.711 46.390 1.00 93.17 C +ATOM 3937 CD PRO B 279 -41.950 63.432 44.908 1.00 96.89 C +ATOM 3938 N GLU B 280 -40.935 60.292 45.727 1.00 77.03 N +ATOM 3939 CA GLU B 280 -41.181 58.905 46.088 1.00 74.74 C +ATOM 3940 C GLU B 280 -41.876 58.169 44.944 1.00 78.36 C +ATOM 3941 O GLU B 280 -42.347 58.786 43.991 1.00 70.27 O +ATOM 3942 CB GLU B 280 -42.037 58.851 47.355 1.00 68.54 C +ATOM 3943 CG GLU B 280 -43.525 58.950 47.083 1.00 83.22 C +ATOM 3944 CD GLU B 280 -44.013 60.384 47.074 1.00 90.41 C +ATOM 3945 OE1 GLU B 280 -44.071 61.002 48.156 1.00 86.76 O +ATOM 3946 OE2 GLU B 280 -44.341 60.897 45.986 1.00 98.96 O +ATOM 3947 N PRO B 281 -41.981 56.834 45.048 1.00 79.29 N +ATOM 3948 CA PRO B 281 -42.623 56.037 43.996 1.00 81.83 C +ATOM 3949 C PRO B 281 -44.057 56.416 43.641 1.00 72.28 C +ATOM 3950 O PRO B 281 -44.912 56.539 44.515 1.00 76.26 O +ATOM 3951 CB PRO B 281 -42.533 54.602 44.517 1.00 86.01 C +ATOM 3952 CG PRO B 281 -41.529 54.635 45.610 1.00 95.32 C +ATOM 3953 CD PRO B 281 -41.555 56.005 46.188 1.00 84.71 C +ATOM 3954 N ASP B 282 -44.303 56.591 42.345 1.00 57.88 N +ATOM 3955 CA ASP B 282 -45.625 56.924 41.814 1.00 52.74 C +ATOM 3956 C ASP B 282 -45.931 55.914 40.710 1.00 54.70 C +ATOM 3957 O ASP B 282 -45.044 55.168 40.297 1.00 58.09 O +ATOM 3958 CB ASP B 282 -45.633 58.341 41.240 1.00 66.43 C +ATOM 3959 CG ASP B 282 -44.863 58.449 39.939 1.00 78.92 C +ATOM 3960 OD1 ASP B 282 -45.340 59.148 39.023 1.00 87.37 O +ATOM 3961 OD2 ASP B 282 -43.782 57.838 39.832 1.00 86.33 O +ATOM 3962 N ILE B 283 -47.166 55.889 40.222 1.00 66.28 N +ATOM 3963 CA ILE B 283 -47.542 54.932 39.180 1.00 71.93 C +ATOM 3964 C ILE B 283 -46.640 54.941 37.942 1.00 74.24 C +ATOM 3965 O ILE B 283 -46.714 54.043 37.103 1.00 73.66 O +ATOM 3966 CB ILE B 283 -49.000 55.144 38.717 1.00 62.68 C +ATOM 3967 CG1 ILE B 283 -49.479 53.911 37.941 1.00 54.55 C +ATOM 3968 CG2 ILE B 283 -49.097 56.393 37.856 1.00 68.03 C +ATOM 3969 CD1 ILE B 283 -50.987 53.760 37.881 1.00 69.59 C +ATOM 3970 N CYS B 284 -45.790 55.954 37.823 1.00 73.07 N +ATOM 3971 CA CYS B 284 -44.882 56.037 36.689 1.00 79.04 C +ATOM 3972 C CYS B 284 -43.635 55.222 37.000 1.00 74.38 C +ATOM 3973 O CYS B 284 -43.191 54.411 36.189 1.00 83.07 O +ATOM 3974 CB CYS B 284 -44.493 57.493 36.423 1.00 87.12 C +ATOM 3975 SG CYS B 284 -45.886 58.633 36.313 1.00100.00 S +ATOM 3976 N HIS B 285 -43.074 55.445 38.183 1.00 63.84 N +ATOM 3977 CA HIS B 285 -41.878 54.729 38.610 1.00 71.00 C +ATOM 3978 C HIS B 285 -42.148 53.226 38.658 1.00 74.30 C +ATOM 3979 O HIS B 285 -41.334 52.419 38.198 1.00 64.25 O +ATOM 3980 CB HIS B 285 -41.437 55.234 39.989 1.00 70.96 C +ATOM 3981 CG HIS B 285 -40.495 54.315 40.704 1.00 80.88 C +ATOM 3982 ND1 HIS B 285 -39.134 54.320 40.478 1.00 86.16 N +ATOM 3983 CD2 HIS B 285 -40.715 53.386 41.664 1.00 81.95 C +ATOM 3984 CE1 HIS B 285 -38.557 53.434 41.271 1.00 92.15 C +ATOM 3985 NE2 HIS B 285 -39.492 52.853 42.002 1.00 94.55 N +ATOM 3986 N GLU B 286 -43.306 52.861 39.197 1.00 72.70 N +ATOM 3987 CA GLU B 286 -43.688 51.463 39.321 1.00 68.31 C +ATOM 3988 C GLU B 286 -43.988 50.795 37.985 1.00 66.37 C +ATOM 3989 O GLU B 286 -43.587 49.656 37.756 1.00 83.61 O +ATOM 3990 CB GLU B 286 -44.910 51.336 40.236 1.00 70.61 C +ATOM 3991 CG GLU B 286 -44.863 52.224 41.468 1.00 90.67 C +ATOM 3992 CD GLU B 286 -44.128 51.584 42.632 1.00 93.74 C +ATOM 3993 OE1 GLU B 286 -44.787 50.956 43.484 1.00 87.42 O +ATOM 3994 OE2 GLU B 286 -42.890 51.714 42.705 1.00 87.70 O +ATOM 3995 N LEU B 287 -44.687 51.507 37.106 1.00 61.19 N +ATOM 3996 CA LEU B 287 -45.062 50.963 35.802 1.00 51.14 C +ATOM 3997 C LEU B 287 -44.002 51.109 34.712 1.00 55.43 C +ATOM 3998 O LEU B 287 -43.787 50.187 33.928 1.00 52.39 O +ATOM 3999 CB LEU B 287 -46.365 51.608 35.328 1.00 52.01 C +ATOM 4000 CG LEU B 287 -47.683 51.118 35.939 1.00 56.75 C +ATOM 4001 CD1 LEU B 287 -48.849 51.689 35.139 1.00 51.84 C +ATOM 4002 CD2 LEU B 287 -47.735 49.597 35.942 1.00 26.43 C +ATOM 4003 N LEU B 288 -43.350 52.266 34.654 1.00 63.30 N +ATOM 4004 CA LEU B 288 -42.316 52.514 33.650 1.00 63.83 C +ATOM 4005 C LEU B 288 -40.926 52.325 34.246 1.00 72.88 C +ATOM 4006 O LEU B 288 -39.964 52.971 33.824 1.00 76.97 O +ATOM 4007 CB LEU B 288 -42.440 53.938 33.094 1.00 59.92 C +ATOM 4008 CG LEU B 288 -43.815 54.376 32.581 1.00 61.12 C +ATOM 4009 CD1 LEU B 288 -43.798 55.868 32.298 1.00 71.68 C +ATOM 4010 CD2 LEU B 288 -44.174 53.598 31.328 1.00 63.71 C +ATOM 4011 N GLY B 289 -40.826 51.440 35.233 1.00 76.38 N +ATOM 4012 CA GLY B 289 -39.545 51.193 35.866 1.00 79.16 C +ATOM 4013 C GLY B 289 -39.412 49.797 36.439 1.00 75.97 C +ATOM 4014 O GLY B 289 -38.494 49.057 36.079 1.00 79.25 O +ATOM 4015 N HIS B 290 -40.330 49.438 37.332 1.00 67.22 N +ATOM 4016 CA HIS B 290 -40.308 48.125 37.971 1.00 70.99 C +ATOM 4017 C HIS B 290 -40.985 47.031 37.143 1.00 67.43 C +ATOM 4018 O HIS B 290 -40.361 46.033 36.780 1.00 77.17 O +ATOM 4019 CB HIS B 290 -40.976 48.202 39.350 1.00 67.02 C +ATOM 4020 CG HIS B 290 -40.089 48.757 40.422 1.00 67.51 C +ATOM 4021 ND1 HIS B 290 -39.238 47.972 41.167 1.00 73.03 N +ATOM 4022 CD2 HIS B 290 -39.924 50.024 40.873 1.00 69.16 C +ATOM 4023 CE1 HIS B 290 -38.584 48.728 42.031 1.00 74.93 C +ATOM 4024 NE2 HIS B 290 -38.982 49.978 41.873 1.00 78.02 N +ATOM 4025 N VAL B 291 -42.266 47.233 36.851 1.00 66.78 N +ATOM 4026 CA VAL B 291 -43.073 46.277 36.096 1.00 71.14 C +ATOM 4027 C VAL B 291 -42.396 45.541 34.935 1.00 72.81 C +ATOM 4028 O VAL B 291 -42.426 44.309 34.882 1.00 57.34 O +ATOM 4029 CB VAL B 291 -44.356 46.958 35.561 1.00 69.21 C +ATOM 4030 CG1 VAL B 291 -45.138 45.998 34.674 1.00 59.39 C +ATOM 4031 CG2 VAL B 291 -45.221 47.413 36.721 1.00 62.18 C +ATOM 4032 N PRO B 292 -41.778 46.282 33.992 1.00 73.61 N +ATOM 4033 CA PRO B 292 -41.130 45.603 32.861 1.00 71.67 C +ATOM 4034 C PRO B 292 -40.092 44.563 33.254 1.00 72.48 C +ATOM 4035 O PRO B 292 -39.877 43.596 32.529 1.00 79.75 O +ATOM 4036 CB PRO B 292 -40.516 46.742 32.043 1.00 62.64 C +ATOM 4037 CG PRO B 292 -41.202 47.969 32.497 1.00 69.22 C +ATOM 4038 CD PRO B 292 -41.622 47.743 33.918 1.00 66.49 C +ATOM 4039 N LEU B 293 -39.444 44.763 34.399 1.00 57.88 N +ATOM 4040 CA LEU B 293 -38.434 43.822 34.859 1.00 51.03 C +ATOM 4041 C LEU B 293 -39.085 42.605 35.500 1.00 51.98 C +ATOM 4042 O LEU B 293 -38.580 41.489 35.392 1.00 55.82 O +ATOM 4043 CB LEU B 293 -37.500 44.498 35.863 1.00 52.91 C +ATOM 4044 CG LEU B 293 -36.324 45.285 35.276 1.00 71.66 C +ATOM 4045 CD1 LEU B 293 -35.552 44.418 34.289 1.00 78.03 C +ATOM 4046 CD2 LEU B 293 -36.843 46.533 34.592 1.00 61.55 C +ATOM 4047 N PHE B 294 -40.215 42.830 36.164 1.00 56.22 N +ATOM 4048 CA PHE B 294 -40.942 41.752 36.825 1.00 54.22 C +ATOM 4049 C PHE B 294 -41.658 40.863 35.810 1.00 53.13 C +ATOM 4050 O PHE B 294 -42.345 39.913 36.182 1.00 51.22 O +ATOM 4051 CB PHE B 294 -41.962 42.328 37.817 1.00 55.75 C +ATOM 4052 CG PHE B 294 -41.345 42.894 39.061 1.00 54.18 C +ATOM 4053 CD1 PHE B 294 -40.886 42.056 40.074 1.00 42.65 C +ATOM 4054 CD2 PHE B 294 -41.209 44.269 39.214 1.00 62.02 C +ATOM 4055 CE1 PHE B 294 -40.297 42.581 41.223 1.00 44.22 C +ATOM 4056 CE2 PHE B 294 -40.622 44.805 40.358 1.00 61.59 C +ATOM 4057 CZ PHE B 294 -40.165 43.959 41.364 1.00 63.94 C +ATOM 4058 N SER B 295 -41.506 41.178 34.528 1.00 42.33 N +ATOM 4059 CA SER B 295 -42.134 40.380 33.485 1.00 57.34 C +ATOM 4060 C SER B 295 -41.125 39.350 32.990 1.00 67.54 C +ATOM 4061 O SER B 295 -41.484 38.402 32.290 1.00 70.27 O +ATOM 4062 CB SER B 295 -42.578 41.271 32.328 1.00 57.63 C +ATOM 4063 OG SER B 295 -41.485 41.995 31.798 1.00 81.53 O +ATOM 4064 N ASP B 296 -39.864 39.540 33.377 1.00 69.04 N +ATOM 4065 CA ASP B 296 -38.781 38.648 32.974 1.00 69.72 C +ATOM 4066 C ASP B 296 -38.601 37.480 33.939 1.00 73.53 C +ATOM 4067 O ASP B 296 -38.401 37.668 35.139 1.00 79.47 O +ATOM 4068 CB ASP B 296 -37.471 39.426 32.861 1.00 73.34 C +ATOM 4069 CG ASP B 296 -36.278 38.523 32.636 1.00 87.96 C +ATOM 4070 OD1 ASP B 296 -36.218 37.877 31.568 1.00 93.45 O +ATOM 4071 OD2 ASP B 296 -35.406 38.460 33.528 1.00 87.02 O +ATOM 4072 N ARG B 297 -38.665 36.274 33.384 1.00 66.35 N +ATOM 4073 CA ARG B 297 -38.534 35.031 34.136 1.00 61.68 C +ATOM 4074 C ARG B 297 -37.387 34.994 35.141 1.00 59.82 C +ATOM 4075 O ARG B 297 -37.589 34.683 36.314 1.00 49.35 O +ATOM 4076 CB ARG B 297 -38.376 33.866 33.159 1.00 74.84 C +ATOM 4077 CG ARG B 297 -38.056 32.547 33.820 1.00 80.99 C +ATOM 4078 CD ARG B 297 -39.312 31.917 34.373 1.00 94.19 C +ATOM 4079 NE ARG B 297 -39.033 30.645 35.031 1.00100.00 N +ATOM 4080 CZ ARG B 297 -38.772 29.509 34.391 1.00100.00 C +ATOM 4081 NH1 ARG B 297 -38.749 29.480 33.064 1.00100.00 N +ATOM 4082 NH2 ARG B 297 -38.534 28.401 35.082 1.00100.00 N +ATOM 4083 N SER B 298 -36.182 35.295 34.675 1.00 62.25 N +ATOM 4084 CA SER B 298 -35.008 35.270 35.537 1.00 74.66 C +ATOM 4085 C SER B 298 -35.052 36.317 36.644 1.00 74.28 C +ATOM 4086 O SER B 298 -34.607 36.060 37.764 1.00 69.21 O +ATOM 4087 CB SER B 298 -33.739 35.461 34.699 1.00 88.66 C +ATOM 4088 OG SER B 298 -33.660 34.503 33.655 1.00 96.26 O +ATOM 4089 N PHE B 299 -35.588 37.495 36.334 1.00 69.97 N +ATOM 4090 CA PHE B 299 -35.665 38.572 37.317 1.00 68.19 C +ATOM 4091 C PHE B 299 -36.595 38.245 38.482 1.00 72.62 C +ATOM 4092 O PHE B 299 -36.286 38.551 39.634 1.00 71.20 O +ATOM 4093 CB PHE B 299 -36.122 39.874 36.653 1.00 62.01 C +ATOM 4094 CG PHE B 299 -36.043 41.071 37.560 1.00 80.44 C +ATOM 4095 CD1 PHE B 299 -34.970 41.954 37.481 1.00 85.38 C +ATOM 4096 CD2 PHE B 299 -37.038 41.313 38.502 1.00 94.09 C +ATOM 4097 CE1 PHE B 299 -34.888 43.060 38.330 1.00 86.12 C +ATOM 4098 CE2 PHE B 299 -36.966 42.415 39.354 1.00 93.02 C +ATOM 4099 CZ PHE B 299 -35.890 43.290 39.267 1.00 91.75 C +ATOM 4100 N ALA B 300 -37.733 37.630 38.181 1.00 74.86 N +ATOM 4101 CA ALA B 300 -38.706 37.270 39.209 1.00 72.38 C +ATOM 4102 C ALA B 300 -38.104 36.367 40.287 1.00 73.94 C +ATOM 4103 O ALA B 300 -38.161 36.694 41.474 1.00 79.90 O +ATOM 4104 CB ALA B 300 -39.915 36.592 38.573 1.00 64.49 C +ATOM 4105 N GLN B 301 -37.535 35.234 39.880 1.00 60.82 N +ATOM 4106 CA GLN B 301 -36.927 34.308 40.834 1.00 59.12 C +ATOM 4107 C GLN B 301 -35.908 35.070 41.668 1.00 52.85 C +ATOM 4108 O GLN B 301 -35.829 34.906 42.886 1.00 42.05 O +ATOM 4109 CB GLN B 301 -36.232 33.165 40.096 1.00 75.11 C +ATOM 4110 CG GLN B 301 -37.136 32.383 39.169 1.00 97.35 C +ATOM 4111 CD GLN B 301 -36.359 31.421 38.296 1.00100.00 C +ATOM 4112 OE1 GLN B 301 -35.207 31.680 37.945 1.00100.00 O +ATOM 4113 NE2 GLN B 301 -36.982 30.303 37.943 1.00 97.11 N +ATOM 4114 N PHE B 302 -35.130 35.906 40.988 1.00 49.60 N +ATOM 4115 CA PHE B 302 -34.107 36.725 41.629 1.00 54.69 C +ATOM 4116 C PHE B 302 -34.740 37.556 42.748 1.00 59.93 C +ATOM 4117 O PHE B 302 -34.316 37.492 43.905 1.00 61.04 O +ATOM 4118 CB PHE B 302 -33.449 37.631 40.574 1.00 46.54 C +ATOM 4119 CG PHE B 302 -32.724 38.822 41.142 1.00 61.15 C +ATOM 4120 CD1 PHE B 302 -31.975 38.721 42.311 1.00 59.47 C +ATOM 4121 CD2 PHE B 302 -32.783 40.050 40.492 1.00 66.45 C +ATOM 4122 CE1 PHE B 302 -31.301 39.826 42.818 1.00 59.27 C +ATOM 4123 CE2 PHE B 302 -32.112 41.156 40.992 1.00 72.43 C +ATOM 4124 CZ PHE B 302 -31.369 41.044 42.157 1.00 66.68 C +ATOM 4125 N SER B 303 -35.757 38.335 42.394 1.00 60.89 N +ATOM 4126 CA SER B 303 -36.458 39.170 43.359 1.00 54.20 C +ATOM 4127 C SER B 303 -36.943 38.297 44.511 1.00 47.38 C +ATOM 4128 O SER B 303 -36.668 38.571 45.678 1.00 54.63 O +ATOM 4129 CB SER B 303 -37.660 39.856 42.692 1.00 45.16 C +ATOM 4130 OG SER B 303 -37.253 40.686 41.618 1.00 39.85 O +ATOM 4131 N GLN B 304 -37.664 37.237 44.167 1.00 22.00 N +ATOM 4132 CA GLN B 304 -38.206 36.320 45.157 1.00 25.19 C +ATOM 4133 C GLN B 304 -37.154 35.833 46.142 1.00 38.37 C +ATOM 4134 O GLN B 304 -37.442 35.651 47.326 1.00 53.20 O +ATOM 4135 CB GLN B 304 -38.841 35.120 44.466 1.00 7.89 C +ATOM 4136 CG GLN B 304 -39.624 34.225 45.398 1.00 5.59 C +ATOM 4137 CD GLN B 304 -40.481 33.238 44.646 1.00 17.21 C +ATOM 4138 OE1 GLN B 304 -40.334 33.073 43.437 1.00 27.54 O +ATOM 4139 NE2 GLN B 304 -41.388 32.576 45.354 1.00 18.31 N +ATOM 4140 N GLU B 305 -35.940 35.604 45.649 1.00 43.72 N +ATOM 4141 CA GLU B 305 -34.851 35.143 46.503 1.00 61.99 C +ATOM 4142 C GLU B 305 -34.678 36.116 47.664 1.00 69.94 C +ATOM 4143 O GLU B 305 -34.644 35.712 48.828 1.00 75.09 O +ATOM 4144 CB GLU B 305 -33.550 35.059 45.704 1.00 71.67 C +ATOM 4145 CG GLU B 305 -33.516 33.930 44.690 1.00 74.16 C +ATOM 4146 CD GLU B 305 -33.855 32.582 45.298 1.00 80.11 C +ATOM 4147 OE1 GLU B 305 -34.687 31.861 44.711 1.00 94.32 O +ATOM 4148 OE2 GLU B 305 -33.293 32.243 46.359 1.00 74.94 O +ATOM 4149 N ILE B 306 -34.565 37.400 47.338 1.00 56.48 N +ATOM 4150 CA ILE B 306 -34.408 38.434 48.352 1.00 52.28 C +ATOM 4151 C ILE B 306 -35.565 38.370 49.345 1.00 57.18 C +ATOM 4152 O ILE B 306 -35.371 38.503 50.556 1.00 64.85 O +ATOM 4153 CB ILE B 306 -34.389 39.839 47.719 1.00 55.36 C +ATOM 4154 CG1 ILE B 306 -33.547 39.826 46.439 1.00 60.79 C +ATOM 4155 CG2 ILE B 306 -33.842 40.848 48.716 1.00 49.22 C +ATOM 4156 CD1 ILE B 306 -33.549 41.138 45.685 1.00 62.48 C +ATOM 4157 N GLY B 307 -36.771 38.164 48.821 1.00 48.52 N +ATOM 4158 CA GLY B 307 -37.943 38.087 49.671 1.00 57.63 C +ATOM 4159 C GLY B 307 -37.827 36.946 50.656 1.00 60.82 C +ATOM 4160 O GLY B 307 -38.082 37.109 51.850 1.00 57.71 O +ATOM 4161 N LEU B 308 -37.423 35.787 50.145 1.00 64.07 N +ATOM 4162 CA LEU B 308 -37.262 34.596 50.967 1.00 55.82 C +ATOM 4163 C LEU B 308 -36.110 34.797 51.946 1.00 53.47 C +ATOM 4164 O LEU B 308 -36.105 34.235 53.041 1.00 46.25 O +ATOM 4165 CB LEU B 308 -37.010 33.387 50.068 1.00 42.02 C +ATOM 4166 CG LEU B 308 -38.229 33.049 49.205 1.00 47.91 C +ATOM 4167 CD1 LEU B 308 -37.787 32.678 47.808 1.00 40.23 C +ATOM 4168 CD2 LEU B 308 -39.014 31.919 49.854 1.00 45.13 C +ATOM 4169 N ALA B 309 -35.137 35.607 51.539 1.00 49.57 N +ATOM 4170 CA ALA B 309 -33.983 35.906 52.378 1.00 42.49 C +ATOM 4171 C ALA B 309 -34.414 36.753 53.572 1.00 41.22 C +ATOM 4172 O ALA B 309 -34.182 36.395 54.727 1.00 46.77 O +ATOM 4173 CB ALA B 309 -32.934 36.651 51.568 1.00 31.59 C +ATOM 4174 N SER B 310 -35.054 37.876 53.272 1.00 33.82 N +ATOM 4175 CA SER B 310 -35.522 38.811 54.283 1.00 40.75 C +ATOM 4176 C SER B 310 -36.486 38.221 55.311 1.00 39.25 C +ATOM 4177 O SER B 310 -36.659 38.782 56.393 1.00 51.49 O +ATOM 4178 CB SER B 310 -36.184 40.011 53.597 1.00 60.17 C +ATOM 4179 OG SER B 310 -37.361 39.622 52.908 1.00 62.03 O +ATOM 4180 N LEU B 311 -37.114 37.099 54.980 1.00 12.02 N +ATOM 4181 CA LEU B 311 -38.071 36.489 55.899 1.00 47.55 C +ATOM 4182 C LEU B 311 -37.464 36.123 57.256 1.00 48.33 C +ATOM 4183 O LEU B 311 -36.754 35.126 57.386 1.00 59.22 O +ATOM 4184 CB LEU B 311 -38.706 35.251 55.259 1.00 52.66 C +ATOM 4185 CG LEU B 311 -39.624 35.509 54.059 1.00 42.32 C +ATOM 4186 CD1 LEU B 311 -40.166 34.194 53.529 1.00 54.87 C +ATOM 4187 CD2 LEU B 311 -40.766 36.413 54.471 1.00 61.47 C +ATOM 4188 N GLY B 312 -37.755 36.942 58.264 1.00 48.49 N +ATOM 4189 CA GLY B 312 -37.242 36.689 59.598 1.00 55.95 C +ATOM 4190 C GLY B 312 -35.790 37.088 59.784 1.00 58.83 C +ATOM 4191 O GLY B 312 -35.192 36.781 60.814 1.00 54.63 O +ATOM 4192 N ALA B 313 -35.221 37.772 58.796 1.00 59.26 N +ATOM 4193 CA ALA B 313 -33.824 38.204 58.866 1.00 79.51 C +ATOM 4194 C ALA B 313 -33.637 39.361 59.848 1.00 91.68 C +ATOM 4195 O ALA B 313 -34.514 40.217 59.993 1.00100.00 O +ATOM 4196 CB ALA B 313 -33.335 38.612 57.484 1.00 78.37 C +ATOM 4197 N PRO B 314 -32.478 39.410 60.528 1.00 87.52 N +ATOM 4198 CA PRO B 314 -32.241 40.495 61.487 1.00 80.10 C +ATOM 4199 C PRO B 314 -32.055 41.836 60.783 1.00 78.70 C +ATOM 4200 O PRO B 314 -31.518 41.900 59.674 1.00 56.63 O +ATOM 4201 CB PRO B 314 -30.994 40.046 62.248 1.00 63.86 C +ATOM 4202 CG PRO B 314 -30.290 39.128 61.313 1.00 49.98 C +ATOM 4203 CD PRO B 314 -31.330 38.491 60.428 1.00 71.57 C +ATOM 4204 N ASP B 315 -32.506 42.897 61.446 1.00 73.05 N +ATOM 4205 CA ASP B 315 -32.432 44.253 60.913 1.00 73.98 C +ATOM 4206 C ASP B 315 -31.186 44.571 60.088 1.00 78.88 C +ATOM 4207 O ASP B 315 -31.294 45.020 58.945 1.00 76.97 O +ATOM 4208 CB ASP B 315 -32.566 45.261 62.056 1.00 71.53 C +ATOM 4209 CG ASP B 315 -33.834 45.060 62.859 1.00 79.25 C +ATOM 4210 OD1 ASP B 315 -33.845 44.180 63.743 1.00 75.19 O +ATOM 4211 OD2 ASP B 315 -34.820 45.782 62.604 1.00 85.56 O +ATOM 4212 N GLU B 316 -30.007 44.347 60.661 1.00 78.88 N +ATOM 4213 CA GLU B 316 -28.755 44.632 59.960 1.00 79.73 C +ATOM 4214 C GLU B 316 -28.744 44.075 58.549 1.00 72.76 C +ATOM 4215 O GLU B 316 -28.324 44.751 57.613 1.00 65.25 O +ATOM 4216 CB GLU B 316 -27.564 44.053 60.721 1.00 79.80 C +ATOM 4217 CG GLU B 316 -27.721 42.598 61.086 1.00 99.07 C +ATOM 4218 CD GLU B 316 -28.252 42.420 62.490 1.00100.00 C +ATOM 4219 OE1 GLU B 316 -27.984 41.359 63.094 1.00100.00 O +ATOM 4220 OE2 GLU B 316 -28.935 43.344 62.986 1.00100.00 O +ATOM 4221 N TYR B 317 -29.196 42.835 58.401 1.00 72.58 N +ATOM 4222 CA TYR B 317 -29.220 42.195 57.096 1.00 79.65 C +ATOM 4223 C TYR B 317 -30.387 42.677 56.255 1.00 80.27 C +ATOM 4224 O TYR B 317 -30.301 42.720 55.029 1.00 69.59 O +ATOM 4225 CB TYR B 317 -29.274 40.678 57.258 1.00 93.84 C +ATOM 4226 CG TYR B 317 -27.928 40.089 57.577 1.00 96.59 C +ATOM 4227 CD1 TYR B 317 -27.534 39.895 58.899 1.00 96.42 C +ATOM 4228 CD2 TYR B 317 -27.025 39.774 56.562 1.00 84.40 C +ATOM 4229 CE1 TYR B 317 -26.271 39.399 59.206 1.00 99.21 C +ATOM 4230 CE2 TYR B 317 -25.759 39.277 56.854 1.00 95.13 C +ATOM 4231 CZ TYR B 317 -25.387 39.095 58.178 1.00100.00 C +ATOM 4232 OH TYR B 317 -24.133 38.603 58.467 1.00100.00 O +ATOM 4233 N ILE B 318 -31.484 43.022 56.918 1.00 81.29 N +ATOM 4234 CA ILE B 318 -32.655 43.525 56.216 1.00 79.03 C +ATOM 4235 C ILE B 318 -32.227 44.796 55.486 1.00 85.15 C +ATOM 4236 O ILE B 318 -32.490 44.970 54.296 1.00 77.47 O +ATOM 4237 CB ILE B 318 -33.788 43.877 57.202 1.00 74.45 C +ATOM 4238 CG1 ILE B 318 -34.489 42.602 57.670 1.00 56.83 C +ATOM 4239 CG2 ILE B 318 -34.782 44.824 56.541 1.00 78.83 C +ATOM 4240 CD1 ILE B 318 -35.292 41.913 56.589 1.00 79.43 C +ATOM 4241 N GLU B 319 -31.560 45.678 56.224 1.00 88.63 N +ATOM 4242 CA GLU B 319 -31.074 46.941 55.685 1.00 92.74 C +ATOM 4243 C GLU B 319 -30.050 46.689 54.582 1.00 86.10 C +ATOM 4244 O GLU B 319 -30.008 47.406 53.581 1.00 76.49 O +ATOM 4245 CB GLU B 319 -30.447 47.773 56.806 1.00 96.66 C +ATOM 4246 CG GLU B 319 -29.969 49.142 56.372 1.00100.00 C +ATOM 4247 CD GLU B 319 -28.500 49.363 56.677 1.00100.00 C +ATOM 4248 OE1 GLU B 319 -28.197 50.127 57.619 1.00100.00 O +ATOM 4249 OE2 GLU B 319 -27.650 48.770 55.975 1.00 99.05 O +ATOM 4250 N LYS B 320 -29.224 45.666 54.781 1.00 87.10 N +ATOM 4251 CA LYS B 320 -28.202 45.292 53.809 1.00 92.68 C +ATOM 4252 C LYS B 320 -28.864 44.866 52.500 1.00 88.40 C +ATOM 4253 O LYS B 320 -28.428 45.258 51.418 1.00 70.36 O +ATOM 4254 CB LYS B 320 -27.354 44.138 54.348 1.00100.00 C +ATOM 4255 CG LYS B 320 -26.291 44.550 55.355 1.00100.00 C +ATOM 4256 CD LYS B 320 -25.489 43.340 55.815 1.00100.00 C +ATOM 4257 CE LYS B 320 -24.377 43.729 56.778 1.00 96.33 C +ATOM 4258 NZ LYS B 320 -23.638 42.536 57.283 1.00 59.54 N +ATOM 4259 N LEU B 321 -29.919 44.061 52.606 1.00 85.57 N +ATOM 4260 CA LEU B 321 -30.646 43.590 51.430 1.00 79.11 C +ATOM 4261 C LEU B 321 -31.269 44.784 50.711 1.00 77.76 C +ATOM 4262 O LEU B 321 -31.179 44.896 49.487 1.00 54.13 O +ATOM 4263 CB LEU B 321 -31.744 42.602 51.836 1.00 75.56 C +ATOM 4264 CG LEU B 321 -31.280 41.207 52.257 1.00 69.23 C +ATOM 4265 CD1 LEU B 321 -32.328 40.581 53.162 1.00 72.14 C +ATOM 4266 CD2 LEU B 321 -31.037 40.348 51.026 1.00 32.48 C +ATOM 4267 N ALA B 322 -31.907 45.668 51.477 1.00 72.88 N +ATOM 4268 CA ALA B 322 -32.525 46.859 50.905 1.00 68.29 C +ATOM 4269 C ALA B 322 -31.470 47.572 50.075 1.00 70.79 C +ATOM 4270 O ALA B 322 -31.694 47.902 48.912 1.00 76.89 O +ATOM 4271 CB ALA B 322 -33.030 47.779 52.009 1.00 56.42 C +ATOM 4272 N THR B 323 -30.307 47.791 50.681 1.00 76.29 N +ATOM 4273 CA THR B 323 -29.206 48.460 50.002 1.00 94.13 C +ATOM 4274 C THR B 323 -28.848 47.734 48.702 1.00 96.35 C +ATOM 4275 O THR B 323 -28.527 48.369 47.692 1.00 98.99 O +ATOM 4276 CB THR B 323 -27.961 48.528 50.907 1.00100.00 C +ATOM 4277 OG1 THR B 323 -28.347 48.948 52.224 1.00100.00 O +ATOM 4278 CG2 THR B 323 -26.949 49.513 50.342 1.00100.00 C +ATOM 4279 N ILE B 324 -28.892 46.405 48.734 1.00 91.07 N +ATOM 4280 CA ILE B 324 -28.592 45.611 47.547 1.00 86.66 C +ATOM 4281 C ILE B 324 -29.711 45.849 46.544 1.00 84.53 C +ATOM 4282 O ILE B 324 -29.464 46.127 45.374 1.00 75.58 O +ATOM 4283 CB ILE B 324 -28.541 44.105 47.871 1.00 88.67 C +ATOM 4284 CG1 ILE B 324 -27.476 43.832 48.935 1.00 74.72 C +ATOM 4285 CG2 ILE B 324 -28.251 43.310 46.602 1.00 81.43 C +ATOM 4286 CD1 ILE B 324 -26.072 44.207 48.507 1.00 59.98 C +ATOM 4287 N TYR B 325 -30.943 45.734 47.030 1.00 84.30 N +ATOM 4288 CA TYR B 325 -32.140 45.944 46.221 1.00 87.69 C +ATOM 4289 C TYR B 325 -32.006 47.251 45.441 1.00 84.03 C +ATOM 4290 O TYR B 325 -32.486 47.377 44.314 1.00 63.33 O +ATOM 4291 CB TYR B 325 -33.362 45.997 47.147 1.00 94.13 C +ATOM 4292 CG TYR B 325 -34.686 46.270 46.468 1.00100.00 C +ATOM 4293 CD1 TYR B 325 -35.173 47.574 46.342 1.00100.00 C +ATOM 4294 CD2 TYR B 325 -35.480 45.220 46.001 1.00100.00 C +ATOM 4295 CE1 TYR B 325 -36.422 47.826 45.773 1.00100.00 C +ATOM 4296 CE2 TYR B 325 -36.729 45.459 45.431 1.00100.00 C +ATOM 4297 CZ TYR B 325 -37.194 46.763 45.322 1.00100.00 C +ATOM 4298 OH TYR B 325 -38.435 46.999 44.777 1.00100.00 O +ATOM 4299 N TRP B 326 -31.344 48.221 46.060 1.00 84.11 N +ATOM 4300 CA TRP B 326 -31.126 49.519 45.449 1.00 86.01 C +ATOM 4301 C TRP B 326 -30.174 49.407 44.268 1.00 87.90 C +ATOM 4302 O TRP B 326 -30.566 49.617 43.125 1.00 85.81 O +ATOM 4303 CB TRP B 326 -30.545 50.485 46.486 1.00 85.17 C +ATOM 4304 CG TRP B 326 -30.574 51.927 46.068 1.00 99.70 C +ATOM 4305 CD1 TRP B 326 -29.592 52.613 45.409 1.00100.00 C +ATOM 4306 CD2 TRP B 326 -31.624 52.874 46.316 1.00100.00 C +ATOM 4307 NE1 TRP B 326 -29.961 53.927 45.237 1.00100.00 N +ATOM 4308 CE2 TRP B 326 -31.202 54.114 45.786 1.00100.00 C +ATOM 4309 CE3 TRP B 326 -32.876 52.793 46.940 1.00100.00 C +ATOM 4310 CZ2 TRP B 326 -31.990 55.266 45.856 1.00 98.96 C +ATOM 4311 CZ3 TRP B 326 -33.659 53.942 47.011 1.00100.00 C +ATOM 4312 CH2 TRP B 326 -33.211 55.162 46.471 1.00100.00 C +ATOM 4313 N PHE B 327 -28.919 49.067 44.555 1.00 88.82 N +ATOM 4314 CA PHE B 327 -27.885 48.942 43.525 1.00 93.56 C +ATOM 4315 C PHE B 327 -28.148 47.816 42.534 1.00 89.91 C +ATOM 4316 O PHE B 327 -27.256 47.405 41.788 1.00 89.17 O +ATOM 4317 CB PHE B 327 -26.519 48.742 44.182 1.00 96.80 C +ATOM 4318 CG PHE B 327 -26.029 49.950 44.931 1.00100.00 C +ATOM 4319 CD1 PHE B 327 -25.649 51.105 44.249 1.00100.00 C +ATOM 4320 CD2 PHE B 327 -25.949 49.937 46.322 1.00100.00 C +ATOM 4321 CE1 PHE B 327 -25.198 52.229 44.942 1.00100.00 C +ATOM 4322 CE2 PHE B 327 -25.499 51.056 47.023 1.00100.00 C +ATOM 4323 CZ PHE B 327 -25.125 52.206 46.331 1.00100.00 C +ATOM 4324 N THR B 328 -29.376 47.320 42.530 1.00 89.94 N +ATOM 4325 CA THR B 328 -29.755 46.252 41.621 1.00 88.60 C +ATOM 4326 C THR B 328 -31.089 46.585 40.962 1.00 92.98 C +ATOM 4327 O THR B 328 -31.130 47.050 39.825 1.00 71.65 O +ATOM 4328 CB THR B 328 -29.880 44.894 42.367 1.00 88.37 C +ATOM 4329 OG1 THR B 328 -30.752 45.037 43.496 1.00 87.10 O +ATOM 4330 CG2 THR B 328 -28.519 44.418 42.849 1.00 78.14 C +ATOM 4331 N VAL B 329 -32.170 46.368 41.702 1.00100.00 N +ATOM 4332 CA VAL B 329 -33.524 46.623 41.221 1.00100.00 C +ATOM 4333 C VAL B 329 -33.808 48.103 40.967 1.00 99.41 C +ATOM 4334 O VAL B 329 -34.377 48.473 39.941 1.00 94.57 O +ATOM 4335 CB VAL B 329 -34.577 46.072 42.223 1.00100.00 C +ATOM 4336 CG1 VAL B 329 -35.979 46.280 41.675 1.00100.00 C +ATOM 4337 CG2 VAL B 329 -34.332 44.595 42.464 1.00 89.69 C +ATOM 4338 N GLU B 330 -33.406 48.947 41.907 1.00 98.51 N +ATOM 4339 CA GLU B 330 -33.633 50.381 41.793 1.00 98.85 C +ATOM 4340 C GLU B 330 -32.655 51.100 40.872 1.00100.00 C +ATOM 4341 O GLU B 330 -33.064 51.734 39.904 1.00 98.41 O +ATOM 4342 CB GLU B 330 -33.601 51.010 43.184 1.00 99.44 C +ATOM 4343 CG GLU B 330 -34.797 50.639 44.031 1.00100.00 C +ATOM 4344 CD GLU B 330 -36.060 51.342 43.580 1.00100.00 C +ATOM 4345 OE1 GLU B 330 -37.081 51.230 44.290 1.00100.00 O +ATOM 4346 OE2 GLU B 330 -36.030 52.010 42.523 1.00100.00 O +ATOM 4347 N PHE B 331 -31.364 50.997 41.174 1.00100.00 N +ATOM 4348 CA PHE B 331 -30.333 51.653 40.371 1.00100.00 C +ATOM 4349 C PHE B 331 -29.212 50.711 39.941 1.00100.00 C +ATOM 4350 O PHE B 331 -28.036 50.961 40.217 1.00100.00 O +ATOM 4351 CB PHE B 331 -29.738 52.831 41.144 1.00 99.38 C +ATOM 4352 CG PHE B 331 -30.709 53.948 41.375 1.00 99.09 C +ATOM 4353 CD1 PHE B 331 -31.624 53.886 42.422 1.00 92.66 C +ATOM 4354 CD2 PHE B 331 -30.721 55.060 40.540 1.00100.00 C +ATOM 4355 CE1 PHE B 331 -32.537 54.915 42.633 1.00 94.76 C +ATOM 4356 CE2 PHE B 331 -31.631 56.096 40.742 1.00100.00 C +ATOM 4357 CZ PHE B 331 -32.540 56.022 41.792 1.00100.00 C +ATOM 4358 N GLY B 332 -29.581 49.630 39.261 1.00100.00 N +ATOM 4359 CA GLY B 332 -28.587 48.677 38.809 1.00100.00 C +ATOM 4360 C GLY B 332 -28.355 48.756 37.314 1.00100.00 C +ATOM 4361 O GLY B 332 -29.209 49.240 36.564 1.00100.00 O +ATOM 4362 N LEU B 333 -27.190 48.280 36.884 1.00100.00 N +ATOM 4363 CA LEU B 333 -26.824 48.268 35.473 1.00100.00 C +ATOM 4364 C LEU B 333 -26.417 46.847 35.111 1.00100.00 C +ATOM 4365 O LEU B 333 -25.650 46.214 35.834 1.00100.00 O +ATOM 4366 CB LEU B 333 -25.664 49.233 35.212 1.00100.00 C +ATOM 4367 CG LEU B 333 -25.995 50.727 35.334 1.00100.00 C +ATOM 4368 CD1 LEU B 333 -24.735 51.545 35.112 1.00100.00 C +ATOM 4369 CD2 LEU B 333 -27.061 51.117 34.323 1.00 84.61 C +ATOM 4370 N CYS B 334 -26.926 46.348 33.989 1.00100.00 N +ATOM 4371 CA CYS B 334 -26.620 44.986 33.564 1.00100.00 C +ATOM 4372 C CYS B 334 -25.609 44.888 32.427 1.00100.00 C +ATOM 4373 O CYS B 334 -25.142 45.896 31.892 1.00 93.62 O +ATOM 4374 CB CYS B 334 -27.905 44.265 33.153 1.00100.00 C +ATOM 4375 SG CYS B 334 -28.666 44.917 31.638 1.00100.00 S +ATOM 4376 N LYS B 335 -25.292 43.649 32.066 1.00100.00 N +ATOM 4377 CA LYS B 335 -24.339 43.357 31.002 1.00100.00 C +ATOM 4378 C LYS B 335 -25.026 42.823 29.747 1.00100.00 C +ATOM 4379 O LYS B 335 -25.701 41.791 29.787 1.00 97.61 O +ATOM 4380 CB LYS B 335 -23.321 42.329 31.494 1.00100.00 C +ATOM 4381 CG LYS B 335 -22.360 42.868 32.528 1.00100.00 C +ATOM 4382 CD LYS B 335 -20.937 42.832 32.003 1.00100.00 C +ATOM 4383 CE LYS B 335 -20.589 44.115 31.257 1.00100.00 C +ATOM 4384 NZ LYS B 335 -21.324 44.259 29.967 1.00100.00 N +ATOM 4385 N GLN B 336 -24.842 43.523 28.633 1.00 95.53 N +ATOM 4386 CA GLN B 336 -25.443 43.109 27.370 1.00 99.94 C +ATOM 4387 C GLN B 336 -24.378 42.927 26.290 1.00100.00 C +ATOM 4388 O GLN B 336 -24.341 43.667 25.308 1.00100.00 O +ATOM 4389 CB GLN B 336 -26.473 44.146 26.917 1.00 97.51 C +ATOM 4390 CG GLN B 336 -27.642 44.306 27.879 1.00100.00 C +ATOM 4391 CD GLN B 336 -28.710 43.242 27.684 1.00100.00 C +ATOM 4392 OE1 GLN B 336 -28.713 42.519 26.685 1.00100.00 O +ATOM 4393 NE2 GLN B 336 -29.628 43.145 28.642 1.00100.00 N +ATOM 4394 N GLY B 337 -23.518 41.930 26.481 1.00100.00 N +ATOM 4395 CA GLY B 337 -22.454 41.662 25.529 1.00 93.95 C +ATOM 4396 C GLY B 337 -21.164 42.327 25.969 1.00 97.49 C +ATOM 4397 O GLY B 337 -20.369 41.742 26.702 1.00 94.10 O +ATOM 4398 N ASP B 338 -20.957 43.559 25.518 1.00100.00 N +ATOM 4399 CA ASP B 338 -19.764 44.318 25.879 1.00100.00 C +ATOM 4400 C ASP B 338 -20.222 45.594 26.566 1.00100.00 C +ATOM 4401 O ASP B 338 -19.634 46.045 27.551 1.00100.00 O +ATOM 4402 CB ASP B 338 -18.961 44.686 24.629 1.00100.00 C +ATOM 4403 CG ASP B 338 -18.370 43.475 23.938 1.00100.00 C +ATOM 4404 OD1 ASP B 338 -17.615 42.728 24.596 1.00100.00 O +ATOM 4405 OD2 ASP B 338 -18.660 43.272 22.738 1.00 98.72 O +ATOM 4406 N SER B 339 -21.293 46.160 26.024 1.00100.00 N +ATOM 4407 CA SER B 339 -21.873 47.391 26.536 1.00100.00 C +ATOM 4408 C SER B 339 -22.663 47.188 27.822 1.00100.00 C +ATOM 4409 O SER B 339 -22.945 46.057 28.228 1.00100.00 O +ATOM 4410 CB SER B 339 -22.786 48.010 25.475 1.00100.00 C +ATOM 4411 OG SER B 339 -23.727 47.060 24.999 1.00100.00 O +ATOM 4412 N ILE B 340 -23.019 48.305 28.449 1.00100.00 N +ATOM 4413 CA ILE B 340 -23.785 48.296 29.686 1.00100.00 C +ATOM 4414 C ILE B 340 -25.127 48.991 29.479 1.00100.00 C +ATOM 4415 O ILE B 340 -25.204 50.061 28.864 1.00 99.68 O +ATOM 4416 CB ILE B 340 -23.012 49.006 30.832 1.00 97.56 C +ATOM 4417 CG1 ILE B 340 -22.320 47.958 31.706 1.00 77.79 C +ATOM 4418 CG2 ILE B 340 -23.959 49.863 31.669 1.00 89.25 C +ATOM 4419 CD1 ILE B 340 -21.116 47.316 31.049 1.00 45.99 C +ATOM 4420 N LYS B 341 -26.179 48.371 30.001 1.00100.00 N +ATOM 4421 CA LYS B 341 -27.525 48.917 29.896 1.00100.00 C +ATOM 4422 C LYS B 341 -28.089 49.186 31.289 1.00100.00 C +ATOM 4423 O LYS B 341 -27.562 48.694 32.292 1.00100.00 O +ATOM 4424 CB LYS B 341 -28.435 47.941 29.147 1.00 99.30 C +ATOM 4425 CG LYS B 341 -28.138 47.838 27.663 1.00 92.41 C +ATOM 4426 CD LYS B 341 -28.521 49.112 26.935 1.00 94.05 C +ATOM 4427 CE LYS B 341 -28.442 48.933 25.430 1.00 96.81 C +ATOM 4428 NZ LYS B 341 -27.106 48.426 25.012 1.00100.00 N +ATOM 4429 N ALA B 342 -29.157 49.975 31.345 1.00100.00 N +ATOM 4430 CA ALA B 342 -29.796 50.306 32.612 1.00100.00 C +ATOM 4431 C ALA B 342 -31.028 49.433 32.820 1.00100.00 C +ATOM 4432 O ALA B 342 -31.896 49.349 31.952 1.00100.00 O +ATOM 4433 CB ALA B 342 -30.187 51.782 32.632 1.00100.00 C +ATOM 4434 N TYR B 343 -31.091 48.770 33.969 1.00100.00 N +ATOM 4435 CA TYR B 343 -32.225 47.909 34.288 1.00100.00 C +ATOM 4436 C TYR B 343 -32.834 48.333 35.617 1.00100.00 C +ATOM 4437 O TYR B 343 -33.850 47.788 36.051 1.00100.00 O +ATOM 4438 CB TYR B 343 -31.784 46.438 34.339 1.00100.00 C +ATOM 4439 CG TYR B 343 -31.074 46.031 35.612 1.00100.00 C +ATOM 4440 CD1 TYR B 343 -29.693 46.176 35.741 1.00 97.49 C +ATOM 4441 CD2 TYR B 343 -31.783 45.495 36.686 1.00100.00 C +ATOM 4442 CE1 TYR B 343 -29.036 45.797 36.910 1.00 92.68 C +ATOM 4443 CE2 TYR B 343 -31.136 45.114 37.857 1.00100.00 C +ATOM 4444 CZ TYR B 343 -29.763 45.270 37.962 1.00 99.50 C +ATOM 4445 OH TYR B 343 -29.120 44.908 39.122 1.00100.00 O +ATOM 4446 N GLY B 344 -32.202 49.313 36.255 1.00100.00 N +ATOM 4447 CA GLY B 344 -32.695 49.812 37.524 1.00 96.04 C +ATOM 4448 C GLY B 344 -34.029 50.508 37.342 1.00100.00 C +ATOM 4449 O GLY B 344 -34.221 51.267 36.389 1.00 91.72 O +ATOM 4450 N ALA B 345 -34.954 50.248 38.260 1.00100.00 N +ATOM 4451 CA ALA B 345 -36.286 50.839 38.204 1.00 94.41 C +ATOM 4452 C ALA B 345 -36.234 52.341 38.441 1.00 95.61 C +ATOM 4453 O ALA B 345 -36.970 53.105 37.815 1.00 95.17 O +ATOM 4454 CB ALA B 345 -37.183 50.178 39.229 1.00 80.87 C +ATOM 4455 N GLY B 346 -35.362 52.762 39.350 1.00 94.40 N +ATOM 4456 CA GLY B 346 -35.228 54.176 39.636 1.00 95.70 C +ATOM 4457 C GLY B 346 -34.596 54.903 38.463 1.00 96.08 C +ATOM 4458 O GLY B 346 -34.825 56.095 38.265 1.00100.00 O +ATOM 4459 N LEU B 347 -33.795 54.181 37.686 1.00 90.98 N +ATOM 4460 CA LEU B 347 -33.125 54.752 36.522 1.00 93.82 C +ATOM 4461 C LEU B 347 -34.092 54.934 35.358 1.00 98.26 C +ATOM 4462 O LEU B 347 -34.172 56.007 34.764 1.00100.00 O +ATOM 4463 CB LEU B 347 -31.982 53.843 36.063 1.00 96.72 C +ATOM 4464 CG LEU B 347 -30.817 53.599 37.024 1.00100.00 C +ATOM 4465 CD1 LEU B 347 -29.974 52.442 36.503 1.00 96.93 C +ATOM 4466 CD2 LEU B 347 -29.981 54.864 37.158 1.00100.00 C +ATOM 4467 N LEU B 348 -34.816 53.866 35.039 1.00100.00 N +ATOM 4468 CA LEU B 348 -35.768 53.864 33.935 1.00 97.50 C +ATOM 4469 C LEU B 348 -36.913 54.860 34.069 1.00 88.35 C +ATOM 4470 O LEU B 348 -37.398 55.384 33.067 1.00 81.45 O +ATOM 4471 CB LEU B 348 -36.332 52.454 33.746 1.00100.00 C +ATOM 4472 CG LEU B 348 -35.267 51.414 33.384 1.00 95.13 C +ATOM 4473 CD1 LEU B 348 -35.729 50.031 33.803 1.00 82.59 C +ATOM 4474 CD2 LEU B 348 -34.987 51.475 31.892 1.00100.00 C +ATOM 4475 N SER B 349 -37.352 55.114 35.297 1.00 85.54 N +ATOM 4476 CA SER B 349 -38.444 56.053 35.523 1.00 93.03 C +ATOM 4477 C SER B 349 -37.941 57.489 35.642 1.00100.00 C +ATOM 4478 O SER B 349 -38.727 58.436 35.573 1.00100.00 O +ATOM 4479 CB SER B 349 -39.218 55.671 36.786 1.00 89.12 C +ATOM 4480 OG SER B 349 -38.435 55.854 37.952 1.00 84.89 O +ATOM 4481 N SER B 350 -36.629 57.647 35.813 1.00100.00 N +ATOM 4482 CA SER B 350 -36.025 58.972 35.946 1.00 94.48 C +ATOM 4483 C SER B 350 -35.258 59.366 34.690 1.00 88.87 C +ATOM 4484 O SER B 350 -34.260 58.740 34.333 1.00 80.63 O +ATOM 4485 CB SER B 350 -35.085 59.007 37.149 1.00 96.72 C +ATOM 4486 OG SER B 350 -34.109 60.021 36.998 1.00 82.26 O +ATOM 4487 N PHE B 351 -35.731 60.421 34.034 1.00 91.05 N +ATOM 4488 CA PHE B 351 -35.124 60.914 32.801 1.00100.00 C +ATOM 4489 C PHE B 351 -33.689 61.427 32.942 1.00100.00 C +ATOM 4490 O PHE B 351 -32.827 61.116 32.120 1.00100.00 O +ATOM 4491 CB PHE B 351 -35.987 62.027 32.199 1.00100.00 C +ATOM 4492 CG PHE B 351 -35.323 62.758 31.066 1.00100.00 C +ATOM 4493 CD1 PHE B 351 -35.195 62.155 29.819 1.00100.00 C +ATOM 4494 CD2 PHE B 351 -34.811 64.040 31.247 1.00100.00 C +ATOM 4495 CE1 PHE B 351 -34.566 62.815 28.769 1.00100.00 C +ATOM 4496 CE2 PHE B 351 -34.179 64.711 30.203 1.00100.00 C +ATOM 4497 CZ PHE B 351 -34.056 64.097 28.961 1.00100.00 C +ATOM 4498 N GLY B 352 -33.444 62.220 33.980 1.00100.00 N +ATOM 4499 CA GLY B 352 -32.122 62.784 34.192 1.00 97.48 C +ATOM 4500 C GLY B 352 -31.017 61.793 34.504 1.00 95.87 C +ATOM 4501 O GLY B 352 -29.868 61.996 34.109 1.00 86.00 O +ATOM 4502 N GLU B 353 -31.353 60.721 35.215 1.00 93.46 N +ATOM 4503 CA GLU B 353 -30.356 59.719 35.573 1.00 93.61 C +ATOM 4504 C GLU B 353 -30.228 58.607 34.541 1.00 92.61 C +ATOM 4505 O GLU B 353 -29.250 57.858 34.540 1.00 89.20 O +ATOM 4506 CB GLU B 353 -30.680 59.113 36.935 1.00 91.82 C +ATOM 4507 CG GLU B 353 -29.449 58.705 37.722 1.00 80.75 C +ATOM 4508 CD GLU B 353 -29.690 58.730 39.215 1.00 83.70 C +ATOM 4509 OE1 GLU B 353 -28.797 58.294 39.970 1.00 78.05 O +ATOM 4510 OE2 GLU B 353 -30.775 59.190 39.632 1.00 90.12 O +ATOM 4511 N LEU B 354 -31.223 58.496 33.672 1.00 94.32 N +ATOM 4512 CA LEU B 354 -31.206 57.474 32.638 1.00100.00 C +ATOM 4513 C LEU B 354 -30.037 57.724 31.686 1.00100.00 C +ATOM 4514 O LEU B 354 -29.366 56.788 31.243 1.00100.00 O +ATOM 4515 CB LEU B 354 -32.529 57.493 31.870 1.00100.00 C +ATOM 4516 CG LEU B 354 -32.731 56.463 30.755 1.00100.00 C +ATOM 4517 CD1 LEU B 354 -32.472 55.051 31.272 1.00100.00 C +ATOM 4518 CD2 LEU B 354 -34.153 56.591 30.229 1.00100.00 C +ATOM 4519 N GLN B 355 -29.797 58.995 31.381 1.00100.00 N +ATOM 4520 CA GLN B 355 -28.709 59.372 30.488 1.00100.00 C +ATOM 4521 C GLN B 355 -27.395 59.543 31.251 1.00100.00 C +ATOM 4522 O GLN B 355 -26.312 59.445 30.669 1.00100.00 O +ATOM 4523 CB GLN B 355 -29.056 60.673 29.768 1.00100.00 C +ATOM 4524 CG GLN B 355 -29.909 61.625 30.592 1.00100.00 C +ATOM 4525 CD GLN B 355 -30.520 62.725 29.748 1.00100.00 C +ATOM 4526 OE1 GLN B 355 -30.344 63.914 30.024 1.00100.00 O +ATOM 4527 NE2 GLN B 355 -31.245 62.332 28.709 1.00 98.92 N +ATOM 4528 N TYR B 356 -27.495 59.789 32.555 1.00100.00 N +ATOM 4529 CA TYR B 356 -26.309 59.978 33.385 1.00100.00 C +ATOM 4530 C TYR B 356 -25.576 58.675 33.710 1.00100.00 C +ATOM 4531 O TYR B 356 -24.347 58.611 33.650 1.00100.00 O +ATOM 4532 CB TYR B 356 -26.677 60.667 34.698 1.00100.00 C +ATOM 4533 CG TYR B 356 -25.622 60.495 35.771 1.00100.00 C +ATOM 4534 CD1 TYR B 356 -24.336 61.008 35.594 1.00100.00 C +ATOM 4535 CD2 TYR B 356 -25.902 59.815 36.957 1.00100.00 C +ATOM 4536 CE1 TYR B 356 -23.356 60.854 36.570 1.00100.00 C +ATOM 4537 CE2 TYR B 356 -24.927 59.654 37.942 1.00100.00 C +ATOM 4538 CZ TYR B 356 -23.657 60.178 37.742 1.00100.00 C +ATOM 4539 OH TYR B 356 -22.696 60.041 38.719 1.00100.00 O +ATOM 4540 N CYS B 357 -26.337 57.648 34.070 1.00 98.65 N +ATOM 4541 CA CYS B 357 -25.765 56.353 34.421 1.00100.00 C +ATOM 4542 C CYS B 357 -25.103 55.664 33.229 1.00100.00 C +ATOM 4543 O CYS B 357 -24.252 54.788 33.405 1.00100.00 O +ATOM 4544 CB CYS B 357 -26.853 55.442 34.990 1.00100.00 C +ATOM 4545 SG CYS B 357 -28.183 55.062 33.819 1.00100.00 S +ATOM 4546 N LEU B 358 -25.490 56.069 32.021 1.00100.00 N +ATOM 4547 CA LEU B 358 -24.953 55.481 30.798 1.00100.00 C +ATOM 4548 C LEU B 358 -23.689 56.179 30.295 1.00100.00 C +ATOM 4549 O LEU B 358 -23.009 55.679 29.396 1.00100.00 O +ATOM 4550 CB LEU B 358 -26.027 55.500 29.705 1.00 96.86 C +ATOM 4551 CG LEU B 358 -26.470 54.148 29.129 1.00 99.60 C +ATOM 4552 CD1 LEU B 358 -25.356 53.571 28.268 1.00100.00 C +ATOM 4553 CD2 LEU B 358 -26.837 53.195 30.257 1.00 97.83 C +ATOM 4554 N SER B 359 -23.370 57.327 30.884 1.00100.00 N +ATOM 4555 CA SER B 359 -22.190 58.082 30.480 1.00100.00 C +ATOM 4556 C SER B 359 -20.915 57.598 31.168 1.00100.00 C +ATOM 4557 O SER B 359 -20.940 56.646 31.954 1.00 96.18 O +ATOM 4558 CB SER B 359 -22.398 59.576 30.759 1.00100.00 C +ATOM 4559 OG SER B 359 -22.612 59.818 32.138 1.00 96.44 O +ATOM 4560 N GLU B 360 -19.804 58.265 30.864 1.00100.00 N +ATOM 4561 CA GLU B 360 -18.503 57.923 31.435 1.00100.00 C +ATOM 4562 C GLU B 360 -18.099 58.867 32.564 1.00100.00 C +ATOM 4563 O GLU B 360 -16.949 59.306 32.642 1.00100.00 O +ATOM 4564 CB GLU B 360 -17.429 57.943 30.348 1.00100.00 C +ATOM 4565 CG GLU B 360 -17.462 56.733 29.434 1.00100.00 C +ATOM 4566 CD GLU B 360 -16.837 57.010 28.081 1.00100.00 C +ATOM 4567 OE1 GLU B 360 -15.660 57.430 28.051 1.00100.00 O +ATOM 4568 OE2 GLU B 360 -17.522 56.814 27.050 1.00100.00 O +ATOM 4569 N LYS B 361 -19.055 59.176 33.434 1.00100.00 N +ATOM 4570 CA LYS B 361 -18.804 60.058 34.564 1.00100.00 C +ATOM 4571 C LYS B 361 -18.758 59.261 35.872 1.00100.00 C +ATOM 4572 O LYS B 361 -17.870 59.469 36.704 1.00100.00 O +ATOM 4573 CB LYS B 361 -19.885 61.146 34.638 1.00100.00 C +ATOM 4574 CG LYS B 361 -19.947 62.024 33.396 1.00 94.40 C +ATOM 4575 CD LYS B 361 -20.954 63.155 33.538 1.00 96.23 C +ATOM 4576 CE LYS B 361 -20.918 64.059 32.312 1.00100.00 C +ATOM 4577 NZ LYS B 361 -21.851 65.214 32.421 1.00100.00 N +ATOM 4578 N PRO B 362 -19.700 58.312 36.058 1.00100.00 N +ATOM 4579 CA PRO B 362 -19.736 57.503 37.282 1.00100.00 C +ATOM 4580 C PRO B 362 -18.673 56.411 37.267 1.00100.00 C +ATOM 4581 O PRO B 362 -18.290 55.930 36.201 1.00100.00 O +ATOM 4582 CB PRO B 362 -21.151 56.934 37.287 1.00100.00 C +ATOM 4583 CG PRO B 362 -21.505 56.828 35.836 1.00100.00 C +ATOM 4584 CD PRO B 362 -20.763 57.918 35.113 1.00100.00 C +ATOM 4585 N LYS B 363 -18.197 56.026 38.449 1.00100.00 N +ATOM 4586 CA LYS B 363 -17.175 54.984 38.554 1.00100.00 C +ATOM 4587 C LYS B 363 -17.827 53.624 38.798 1.00100.00 C +ATOM 4588 O LYS B 363 -18.153 53.265 39.933 1.00 97.58 O +ATOM 4589 CB LYS B 363 -16.187 55.316 39.681 1.00100.00 C +ATOM 4590 CG LYS B 363 -16.827 55.722 41.004 1.00 99.68 C +ATOM 4591 CD LYS B 363 -16.303 57.071 41.489 1.00100.00 C +ATOM 4592 CE LYS B 363 -14.775 57.139 41.440 1.00100.00 C +ATOM 4593 NZ LYS B 363 -14.140 56.378 42.549 1.00 93.91 N +ATOM 4594 N LEU B 364 -18.012 52.877 37.712 1.00100.00 N +ATOM 4595 CA LEU B 364 -18.638 51.559 37.755 1.00100.00 C +ATOM 4596 C LEU B 364 -17.831 50.526 38.524 1.00100.00 C +ATOM 4597 O LEU B 364 -16.601 50.594 38.587 1.00100.00 O +ATOM 4598 CB LEU B 364 -18.870 51.037 36.332 1.00100.00 C +ATOM 4599 CG LEU B 364 -19.783 51.828 35.390 1.00100.00 C +ATOM 4600 CD1 LEU B 364 -21.047 52.231 36.132 1.00100.00 C +ATOM 4601 CD2 LEU B 364 -19.052 53.047 34.850 1.00100.00 C +ATOM 4602 N LEU B 365 -18.547 49.564 39.097 1.00100.00 N +ATOM 4603 CA LEU B 365 -17.934 48.480 39.855 1.00100.00 C +ATOM 4604 C LEU B 365 -18.729 47.191 39.623 1.00100.00 C +ATOM 4605 O LEU B 365 -19.873 47.229 39.163 1.00 97.98 O +ATOM 4606 CB LEU B 365 -17.892 48.828 41.347 1.00 91.41 C +ATOM 4607 CG LEU B 365 -16.962 49.983 41.732 1.00 87.27 C +ATOM 4608 CD1 LEU B 365 -17.157 50.297 43.201 1.00 88.25 C +ATOM 4609 CD2 LEU B 365 -15.510 49.622 41.437 1.00 67.33 C +ATOM 4610 N PRO B 366 -18.130 46.030 39.945 1.00100.00 N +ATOM 4611 CA PRO B 366 -18.821 44.752 39.748 1.00100.00 C +ATOM 4612 C PRO B 366 -19.833 44.443 40.842 1.00100.00 C +ATOM 4613 O PRO B 366 -19.627 44.772 42.012 1.00100.00 O +ATOM 4614 CB PRO B 366 -17.682 43.737 39.713 1.00100.00 C +ATOM 4615 CG PRO B 366 -16.635 44.337 40.597 1.00100.00 C +ATOM 4616 CD PRO B 366 -16.790 45.841 40.532 1.00100.00 C +ATOM 4617 N LEU B 367 -20.935 43.813 40.455 1.00100.00 N +ATOM 4618 CA LEU B 367 -21.959 43.458 41.420 1.00 98.44 C +ATOM 4619 C LEU B 367 -21.377 42.419 42.375 1.00100.00 C +ATOM 4620 O LEU B 367 -21.341 41.224 42.070 1.00100.00 O +ATOM 4621 CB LEU B 367 -23.197 42.897 40.710 1.00 98.95 C +ATOM 4622 CG LEU B 367 -24.342 42.544 41.666 1.00100.00 C +ATOM 4623 CD1 LEU B 367 -24.873 43.813 42.318 1.00100.00 C +ATOM 4624 CD2 LEU B 367 -25.443 41.823 40.916 1.00100.00 C +ATOM 4625 N GLU B 368 -20.909 42.891 43.526 1.00100.00 N +ATOM 4626 CA GLU B 368 -20.324 42.030 44.550 1.00100.00 C +ATOM 4627 C GLU B 368 -21.059 42.285 45.858 1.00100.00 C +ATOM 4628 O GLU B 368 -20.647 43.121 46.663 1.00100.00 O +ATOM 4629 CB GLU B 368 -18.838 42.347 44.724 1.00100.00 C +ATOM 4630 CG GLU B 368 -18.014 41.217 45.318 1.00100.00 C +ATOM 4631 CD GLU B 368 -16.525 41.520 45.305 1.00100.00 C +ATOM 4632 OE1 GLU B 368 -15.875 41.385 46.367 1.00100.00 O +ATOM 4633 OE2 GLU B 368 -16.005 41.899 44.231 1.00100.00 O +ATOM 4634 N LEU B 369 -22.152 41.556 46.058 1.00100.00 N +ATOM 4635 CA LEU B 369 -22.987 41.698 47.250 1.00100.00 C +ATOM 4636 C LEU B 369 -22.245 41.812 48.581 1.00 97.87 C +ATOM 4637 O LEU B 369 -22.792 42.335 49.555 1.00 87.33 O +ATOM 4638 CB LEU B 369 -23.991 40.542 47.322 1.00100.00 C +ATOM 4639 CG LEU B 369 -25.182 40.672 46.364 1.00100.00 C +ATOM 4640 CD1 LEU B 369 -24.703 40.517 44.930 1.00100.00 C +ATOM 4641 CD2 LEU B 369 -26.232 39.633 46.702 1.00 96.69 C +ATOM 4642 N GLU B 370 -21.010 41.323 48.629 1.00100.00 N +ATOM 4643 CA GLU B 370 -20.232 41.388 49.859 1.00100.00 C +ATOM 4644 C GLU B 370 -19.931 42.834 50.237 1.00100.00 C +ATOM 4645 O GLU B 370 -20.244 43.278 51.344 1.00 98.83 O +ATOM 4646 CB GLU B 370 -18.921 40.614 49.709 1.00 88.24 C +ATOM 4647 CG GLU B 370 -18.566 39.781 50.932 1.00 93.23 C +ATOM 4648 CD GLU B 370 -18.512 40.602 52.209 1.00100.00 C +ATOM 4649 OE1 GLU B 370 -17.436 41.161 52.512 1.00100.00 O +ATOM 4650 OE2 GLU B 370 -19.545 40.686 52.910 1.00100.00 O +ATOM 4651 N LYS B 371 -19.326 43.563 49.305 1.00100.00 N +ATOM 4652 CA LYS B 371 -18.962 44.955 49.532 1.00100.00 C +ATOM 4653 C LYS B 371 -20.014 45.934 49.021 1.00 95.01 C +ATOM 4654 O LYS B 371 -19.826 47.150 49.082 1.00 91.53 O +ATOM 4655 CB LYS B 371 -17.613 45.241 48.870 1.00100.00 C +ATOM 4656 CG LYS B 371 -16.496 44.322 49.345 1.00100.00 C +ATOM 4657 CD LYS B 371 -16.262 44.471 50.845 1.00100.00 C +ATOM 4658 CE LYS B 371 -15.181 43.525 51.337 1.00100.00 C +ATOM 4659 NZ LYS B 371 -15.008 43.612 52.811 1.00 84.96 N +ATOM 4660 N THR B 372 -21.124 45.404 48.518 1.00 98.20 N +ATOM 4661 CA THR B 372 -22.194 46.254 48.007 1.00100.00 C +ATOM 4662 C THR B 372 -23.169 46.641 49.115 1.00100.00 C +ATOM 4663 O THR B 372 -23.771 47.715 49.077 1.00 97.61 O +ATOM 4664 CB THR B 372 -22.994 45.556 46.890 1.00100.00 C +ATOM 4665 OG1 THR B 372 -22.115 45.193 45.818 1.00100.00 O +ATOM 4666 CG2 THR B 372 -24.077 46.485 46.359 1.00100.00 C +ATOM 4667 N ALA B 373 -23.320 45.754 50.096 1.00100.00 N +ATOM 4668 CA ALA B 373 -24.222 45.985 51.221 1.00 97.69 C +ATOM 4669 C ALA B 373 -23.672 47.034 52.181 1.00 94.98 C +ATOM 4670 O ALA B 373 -24.431 47.716 52.874 1.00 84.20 O +ATOM 4671 CB ALA B 373 -24.468 44.678 51.965 1.00 91.73 C +ATOM 4672 N ILE B 374 -22.350 47.155 52.222 1.00100.00 N +ATOM 4673 CA ILE B 374 -21.699 48.120 53.099 1.00100.00 C +ATOM 4674 C ILE B 374 -21.835 49.526 52.537 1.00 98.56 C +ATOM 4675 O ILE B 374 -22.001 50.496 53.278 1.00100.00 O +ATOM 4676 CB ILE B 374 -20.199 47.802 53.256 1.00100.00 C +ATOM 4677 CG1 ILE B 374 -20.021 46.349 53.708 1.00100.00 C +ATOM 4678 CG2 ILE B 374 -19.563 48.762 54.252 1.00100.00 C +ATOM 4679 CD1 ILE B 374 -18.670 45.759 53.368 1.00100.00 C +ATOM 4680 N GLN B 375 -21.768 49.616 51.214 1.00 94.60 N +ATOM 4681 CA GLN B 375 -21.868 50.879 50.493 1.00 99.42 C +ATOM 4682 C GLN B 375 -23.003 51.801 50.940 1.00100.00 C +ATOM 4683 O GLN B 375 -24.168 51.407 50.950 1.00100.00 O +ATOM 4684 CB GLN B 375 -22.019 50.594 49.002 1.00100.00 C +ATOM 4685 CG GLN B 375 -22.489 51.785 48.203 1.00100.00 C +ATOM 4686 CD GLN B 375 -21.395 52.801 47.993 1.00100.00 C +ATOM 4687 OE1 GLN B 375 -20.276 52.635 48.481 1.00100.00 O +ATOM 4688 NE2 GLN B 375 -21.708 53.863 47.260 1.00 95.80 N +ATOM 4689 N ASN B 376 -22.649 53.039 51.280 1.00100.00 N +ATOM 4690 CA ASN B 376 -23.615 54.047 51.716 1.00100.00 C +ATOM 4691 C ASN B 376 -23.991 54.943 50.531 1.00100.00 C +ATOM 4692 O ASN B 376 -23.123 55.362 49.763 1.00100.00 O +ATOM 4693 CB ASN B 376 -23.011 54.898 52.840 1.00100.00 C +ATOM 4694 CG ASN B 376 -24.056 55.400 53.820 1.00100.00 C +ATOM 4695 OD1 ASN B 376 -24.270 56.606 53.953 1.00100.00 O +ATOM 4696 ND2 ASN B 376 -24.713 54.475 54.514 1.00100.00 N +ATOM 4697 N TYR B 377 -25.281 55.240 50.387 1.00100.00 N +ATOM 4698 CA TYR B 377 -25.750 56.074 49.278 1.00100.00 C +ATOM 4699 C TYR B 377 -26.676 57.224 49.685 1.00100.00 C +ATOM 4700 O TYR B 377 -27.248 57.230 50.781 1.00100.00 O +ATOM 4701 CB TYR B 377 -26.467 55.201 48.242 1.00100.00 C +ATOM 4702 CG TYR B 377 -27.708 54.521 48.776 1.00100.00 C +ATOM 4703 CD1 TYR B 377 -28.962 55.129 48.670 1.00100.00 C +ATOM 4704 CD2 TYR B 377 -27.630 53.273 49.392 1.00 99.54 C +ATOM 4705 CE1 TYR B 377 -30.108 54.509 49.165 1.00100.00 C +ATOM 4706 CE2 TYR B 377 -28.769 52.644 49.891 1.00100.00 C +ATOM 4707 CZ TYR B 377 -30.006 53.267 49.773 1.00100.00 C +ATOM 4708 OH TYR B 377 -31.140 52.649 50.250 1.00 96.80 O +ATOM 4709 N THR B 378 -26.816 58.192 48.780 1.00100.00 N +ATOM 4710 CA THR B 378 -27.675 59.353 49.000 1.00100.00 C +ATOM 4711 C THR B 378 -29.063 59.039 48.458 1.00100.00 C +ATOM 4712 O THR B 378 -29.207 58.243 47.527 1.00100.00 O +ATOM 4713 CB THR B 378 -27.144 60.608 48.271 1.00100.00 C +ATOM 4714 OG1 THR B 378 -28.039 61.706 48.498 1.00 98.57 O +ATOM 4715 CG2 THR B 378 -27.041 60.352 46.770 1.00100.00 C +ATOM 4716 N VAL B 379 -30.080 59.673 49.029 1.00100.00 N +ATOM 4717 CA VAL B 379 -31.453 59.434 48.603 1.00100.00 C +ATOM 4718 C VAL B 379 -31.970 60.457 47.591 1.00100.00 C +ATOM 4719 O VAL B 379 -32.625 60.095 46.611 1.00100.00 O +ATOM 4720 CB VAL B 379 -32.409 59.428 49.817 1.00100.00 C +ATOM 4721 CG1 VAL B 379 -32.293 60.746 50.580 1.00 97.45 C +ATOM 4722 CG2 VAL B 379 -33.840 59.195 49.350 1.00 85.15 C +ATOM 4723 N THR B 380 -31.663 61.730 47.825 1.00100.00 N +ATOM 4724 CA THR B 380 -32.134 62.807 46.959 1.00100.00 C +ATOM 4725 C THR B 380 -31.364 63.043 45.661 1.00100.00 C +ATOM 4726 O THR B 380 -31.858 63.737 44.770 1.00 89.12 O +ATOM 4727 CB THR B 380 -32.173 64.149 47.723 1.00 99.55 C +ATOM 4728 OG1 THR B 380 -30.865 64.453 48.223 1.00 96.22 O +ATOM 4729 CG2 THR B 380 -33.154 64.076 48.879 1.00 82.80 C +ATOM 4730 N GLU B 381 -30.169 62.477 45.538 1.00100.00 N +ATOM 4731 CA GLU B 381 -29.400 62.707 44.326 1.00100.00 C +ATOM 4732 C GLU B 381 -28.788 61.484 43.657 1.00100.00 C +ATOM 4733 O GLU B 381 -28.987 60.350 44.094 1.00100.00 O +ATOM 4734 CB GLU B 381 -28.318 63.750 44.604 1.00100.00 C +ATOM 4735 CG GLU B 381 -28.871 65.159 44.762 1.00100.00 C +ATOM 4736 CD GLU B 381 -27.800 66.161 45.127 1.00100.00 C +ATOM 4737 OE1 GLU B 381 -28.081 67.067 45.942 1.00100.00 O +ATOM 4738 OE2 GLU B 381 -26.676 66.041 44.598 1.00100.00 O +ATOM 4739 N PHE B 382 -28.045 61.743 42.582 1.00100.00 N +ATOM 4740 CA PHE B 382 -27.394 60.707 41.781 1.00100.00 C +ATOM 4741 C PHE B 382 -26.262 59.980 42.499 1.00 99.99 C +ATOM 4742 O PHE B 382 -25.509 60.579 43.271 1.00 94.86 O +ATOM 4743 CB PHE B 382 -26.848 61.313 40.482 1.00 98.66 C +ATOM 4744 CG PHE B 382 -27.906 61.893 39.571 1.00100.00 C +ATOM 4745 CD1 PHE B 382 -29.209 62.097 40.018 1.00100.00 C +ATOM 4746 CD2 PHE B 382 -27.588 62.249 38.263 1.00100.00 C +ATOM 4747 CE1 PHE B 382 -30.175 62.649 39.177 1.00100.00 C +ATOM 4748 CE2 PHE B 382 -28.546 62.801 37.415 1.00100.00 C +ATOM 4749 CZ PHE B 382 -29.842 63.001 37.872 1.00100.00 C +ATOM 4750 N GLN B 383 -26.139 58.685 42.215 1.00100.00 N +ATOM 4751 CA GLN B 383 -25.109 57.844 42.818 1.00100.00 C +ATOM 4752 C GLN B 383 -23.933 57.623 41.868 1.00100.00 C +ATOM 4753 O GLN B 383 -24.109 57.147 40.746 1.00 98.41 O +ATOM 4754 CB GLN B 383 -25.706 56.490 43.214 1.00 99.99 C +ATOM 4755 CG GLN B 383 -26.752 56.570 44.321 1.00100.00 C +ATOM 4756 CD GLN B 383 -28.109 57.018 43.811 1.00100.00 C +ATOM 4757 OE1 GLN B 383 -28.874 57.674 44.524 1.00100.00 O +ATOM 4758 NE2 GLN B 383 -28.416 56.665 42.568 1.00100.00 N +ATOM 4759 N PRO B 384 -22.708 57.951 42.318 1.00100.00 N +ATOM 4760 CA PRO B 384 -21.526 57.769 41.465 1.00100.00 C +ATOM 4761 C PRO B 384 -21.255 56.288 41.239 1.00100.00 C +ATOM 4762 O PRO B 384 -20.595 55.902 40.273 1.00 91.07 O +ATOM 4763 CB PRO B 384 -20.406 58.450 42.248 1.00100.00 C +ATOM 4764 CG PRO B 384 -20.860 58.391 43.672 1.00100.00 C +ATOM 4765 CD PRO B 384 -22.360 58.469 43.651 1.00100.00 C +ATOM 4766 N LEU B 385 -21.794 55.471 42.139 1.00100.00 N +ATOM 4767 CA LEU B 385 -21.630 54.026 42.075 1.00100.00 C +ATOM 4768 C LEU B 385 -22.867 53.327 41.518 1.00100.00 C +ATOM 4769 O LEU B 385 -23.995 53.578 41.958 1.00100.00 O +ATOM 4770 CB LEU B 385 -21.319 53.467 43.470 1.00100.00 C +ATOM 4771 CG LEU B 385 -19.878 53.537 43.991 1.00100.00 C +ATOM 4772 CD1 LEU B 385 -19.696 52.454 45.040 1.00 93.37 C +ATOM 4773 CD2 LEU B 385 -18.867 53.350 42.860 1.00 98.70 C +ATOM 4774 N TYR B 386 -22.634 52.459 40.536 1.00100.00 N +ATOM 4775 CA TYR B 386 -23.679 51.667 39.889 1.00100.00 C +ATOM 4776 C TYR B 386 -23.063 50.289 39.635 1.00100.00 C +ATOM 4777 O TYR B 386 -22.306 50.107 38.679 1.00 87.69 O +ATOM 4778 CB TYR B 386 -24.094 52.288 38.546 1.00100.00 C +ATOM 4779 CG TYR B 386 -24.846 53.603 38.634 1.00100.00 C +ATOM 4780 CD1 TYR B 386 -24.363 54.739 37.984 1.00100.00 C +ATOM 4781 CD2 TYR B 386 -26.059 53.705 39.329 1.00100.00 C +ATOM 4782 CE1 TYR B 386 -25.063 55.942 38.017 1.00100.00 C +ATOM 4783 CE2 TYR B 386 -26.769 54.908 39.367 1.00 99.27 C +ATOM 4784 CZ TYR B 386 -26.264 56.020 38.706 1.00100.00 C +ATOM 4785 OH TYR B 386 -26.963 57.204 38.724 1.00 89.53 O +ATOM 4786 N TYR B 387 -23.381 49.326 40.496 1.00100.00 N +ATOM 4787 CA TYR B 387 -22.841 47.975 40.361 1.00100.00 C +ATOM 4788 C TYR B 387 -23.339 47.253 39.115 1.00100.00 C +ATOM 4789 O TYR B 387 -24.541 47.049 38.935 1.00100.00 O +ATOM 4790 CB TYR B 387 -23.168 47.150 41.608 1.00100.00 C +ATOM 4791 CG TYR B 387 -22.478 47.678 42.837 1.00 98.77 C +ATOM 4792 CD1 TYR B 387 -22.939 48.831 43.472 1.00100.00 C +ATOM 4793 CD2 TYR B 387 -21.340 47.055 43.344 1.00100.00 C +ATOM 4794 CE1 TYR B 387 -22.281 49.356 44.579 1.00100.00 C +ATOM 4795 CE2 TYR B 387 -20.674 47.571 44.453 1.00100.00 C +ATOM 4796 CZ TYR B 387 -21.150 48.723 45.065 1.00100.00 C +ATOM 4797 OH TYR B 387 -20.498 49.252 46.158 1.00100.00 O +ATOM 4798 N VAL B 388 -22.392 46.859 38.266 1.00100.00 N +ATOM 4799 CA VAL B 388 -22.698 46.170 37.016 1.00100.00 C +ATOM 4800 C VAL B 388 -22.828 44.655 37.165 1.00100.00 C +ATOM 4801 O VAL B 388 -21.831 43.953 37.350 1.00100.00 O +ATOM 4802 CB VAL B 388 -21.614 46.463 35.957 1.00100.00 C +ATOM 4803 CG1 VAL B 388 -21.993 45.821 34.630 1.00100.00 C +ATOM 4804 CG2 VAL B 388 -21.437 47.967 35.801 1.00 96.31 C +ATOM 4805 N ALA B 389 -24.061 44.160 37.077 1.00100.00 N +ATOM 4806 CA ALA B 389 -24.330 42.729 37.185 1.00100.00 C +ATOM 4807 C ALA B 389 -24.231 42.069 35.813 1.00100.00 C +ATOM 4808 O ALA B 389 -24.646 42.643 34.802 1.00100.00 O +ATOM 4809 CB ALA B 389 -25.718 42.498 37.764 1.00100.00 C +ATOM 4810 N GLU B 390 -23.670 40.866 35.780 1.00100.00 N +ATOM 4811 CA GLU B 390 -23.536 40.137 34.527 1.00100.00 C +ATOM 4812 C GLU B 390 -24.935 39.874 33.987 1.00100.00 C +ATOM 4813 O GLU B 390 -25.251 40.212 32.846 1.00100.00 O +ATOM 4814 CB GLU B 390 -22.810 38.811 34.763 1.00100.00 C +ATOM 4815 CG GLU B 390 -21.389 38.972 35.270 1.00100.00 C +ATOM 4816 CD GLU B 390 -20.652 37.647 35.374 1.00100.00 C +ATOM 4817 OE1 GLU B 390 -21.275 36.594 35.115 1.00 90.81 O +ATOM 4818 OE2 GLU B 390 -19.448 37.661 35.716 1.00100.00 O +ATOM 4819 N SER B 391 -25.771 39.276 34.829 1.00 90.63 N +ATOM 4820 CA SER B 391 -27.141 38.960 34.458 1.00 94.47 C +ATOM 4821 C SER B 391 -27.980 38.802 35.718 1.00 99.76 C +ATOM 4822 O SER B 391 -27.444 38.736 36.824 1.00100.00 O +ATOM 4823 CB SER B 391 -27.179 37.665 33.642 1.00 93.37 C +ATOM 4824 OG SER B 391 -28.460 37.454 33.071 1.00100.00 O +ATOM 4825 N PHE B 392 -29.297 38.755 35.546 1.00 99.74 N +ATOM 4826 CA PHE B 392 -30.208 38.592 36.673 1.00 93.22 C +ATOM 4827 C PHE B 392 -30.104 37.152 37.151 1.00 96.10 C +ATOM 4828 O PHE B 392 -30.234 36.870 38.340 1.00100.00 O +ATOM 4829 CB PHE B 392 -31.636 38.913 36.239 1.00 82.66 C +ATOM 4830 CG PHE B 392 -31.727 40.079 35.298 1.00 93.42 C +ATOM 4831 CD1 PHE B 392 -32.138 39.898 33.982 1.00100.00 C +ATOM 4832 CD2 PHE B 392 -31.384 41.359 35.723 1.00 84.08 C +ATOM 4833 CE1 PHE B 392 -32.207 40.977 33.102 1.00 96.84 C +ATOM 4834 CE2 PHE B 392 -31.449 42.443 34.853 1.00 78.21 C +ATOM 4835 CZ PHE B 392 -31.860 42.253 33.540 1.00 87.99 C +ATOM 4836 N ASN B 393 -29.861 36.249 36.206 1.00 99.16 N +ATOM 4837 CA ASN B 393 -29.706 34.829 36.501 1.00100.00 C +ATOM 4838 C ASN B 393 -28.422 34.676 37.308 1.00100.00 C +ATOM 4839 O ASN B 393 -28.301 33.810 38.181 1.00 95.97 O +ATOM 4840 CB ASN B 393 -29.574 34.046 35.193 1.00100.00 C +ATOM 4841 CG ASN B 393 -29.818 32.563 35.374 1.00100.00 C +ATOM 4842 OD1 ASN B 393 -29.332 31.949 36.326 1.00100.00 O +ATOM 4843 ND2 ASN B 393 -30.578 31.976 34.454 1.00100.00 N +ATOM 4844 N ASP B 394 -27.474 35.555 36.985 1.00100.00 N +ATOM 4845 CA ASP B 394 -26.154 35.608 37.599 1.00100.00 C +ATOM 4846 C ASP B 394 -26.165 36.363 38.930 1.00 98.41 C +ATOM 4847 O ASP B 394 -25.612 35.884 39.925 1.00 76.46 O +ATOM 4848 CB ASP B 394 -25.181 36.266 36.615 1.00100.00 C +ATOM 4849 CG ASP B 394 -24.139 37.121 37.303 1.00100.00 C +ATOM 4850 OD1 ASP B 394 -23.088 36.566 37.686 1.00100.00 O +ATOM 4851 OD2 ASP B 394 -24.369 38.341 37.458 1.00 94.84 O +ATOM 4852 N ALA B 395 -26.777 37.545 38.947 1.00 96.60 N +ATOM 4853 CA ALA B 395 -26.866 38.331 40.176 1.00 93.92 C +ATOM 4854 C ALA B 395 -27.545 37.430 41.202 1.00 99.31 C +ATOM 4855 O ALA B 395 -27.199 37.420 42.385 1.00 99.13 O +ATOM 4856 CB ALA B 395 -27.701 39.591 39.946 1.00 72.96 C +ATOM 4857 N LYS B 396 -28.504 36.656 40.708 1.00100.00 N +ATOM 4858 CA LYS B 396 -29.276 35.721 41.515 1.00100.00 C +ATOM 4859 C LYS B 396 -28.398 34.840 42.395 1.00 96.15 C +ATOM 4860 O LYS B 396 -28.729 34.582 43.553 1.00 96.56 O +ATOM 4861 CB LYS B 396 -30.118 34.838 40.591 1.00 96.26 C +ATOM 4862 CG LYS B 396 -30.888 33.736 41.284 1.00100.00 C +ATOM 4863 CD LYS B 396 -31.774 33.014 40.286 1.00 95.00 C +ATOM 4864 CE LYS B 396 -32.632 31.972 40.969 1.00100.00 C +ATOM 4865 NZ LYS B 396 -31.803 30.870 41.524 1.00100.00 N +ATOM 4866 N GLU B 397 -27.282 34.383 41.839 1.00 90.43 N +ATOM 4867 CA GLU B 397 -26.368 33.513 42.569 1.00 99.60 C +ATOM 4868 C GLU B 397 -25.544 34.204 43.655 1.00100.00 C +ATOM 4869 O GLU B 397 -25.231 33.598 44.680 1.00100.00 O +ATOM 4870 CB GLU B 397 -25.455 32.798 41.578 1.00 93.35 C +ATOM 4871 CG GLU B 397 -26.223 31.976 40.551 1.00100.00 C +ATOM 4872 CD GLU B 397 -27.115 30.924 41.195 1.00100.00 C +ATOM 4873 OE1 GLU B 397 -26.661 30.270 42.158 1.00100.00 O +ATOM 4874 OE2 GLU B 397 -28.265 30.745 40.739 1.00 94.05 O +ATOM 4875 N LYS B 398 -25.173 35.460 43.432 1.00100.00 N +ATOM 4876 CA LYS B 398 -24.419 36.186 44.452 1.00 95.06 C +ATOM 4877 C LYS B 398 -25.435 36.580 45.527 1.00 87.87 C +ATOM 4878 O LYS B 398 -25.099 36.776 46.700 1.00 73.44 O +ATOM 4879 CB LYS B 398 -23.753 37.440 43.865 1.00 83.62 C +ATOM 4880 CG LYS B 398 -24.212 37.836 42.465 1.00 72.13 C +ATOM 4881 CD LYS B 398 -23.214 38.802 41.842 1.00 71.94 C +ATOM 4882 CE LYS B 398 -23.507 39.044 40.373 1.00 67.41 C +ATOM 4883 NZ LYS B 398 -22.359 39.677 39.656 1.00 66.81 N +ATOM 4884 N VAL B 399 -26.689 36.684 45.103 1.00 79.57 N +ATOM 4885 CA VAL B 399 -27.787 37.028 45.993 1.00 80.28 C +ATOM 4886 C VAL B 399 -28.052 35.830 46.887 1.00 82.73 C +ATOM 4887 O VAL B 399 -28.169 35.958 48.104 1.00 82.05 O +ATOM 4888 CB VAL B 399 -29.052 37.354 45.185 1.00 85.05 C +ATOM 4889 CG1 VAL B 399 -30.286 37.345 46.083 1.00 72.36 C +ATOM 4890 CG2 VAL B 399 -28.885 38.699 44.526 1.00 95.57 C +ATOM 4891 N ARG B 400 -28.160 34.664 46.262 1.00 92.20 N +ATOM 4892 CA ARG B 400 -28.385 33.430 46.995 1.00 96.00 C +ATOM 4893 C ARG B 400 -27.243 33.317 47.986 1.00 94.18 C +ATOM 4894 O ARG B 400 -27.433 32.929 49.138 1.00 93.17 O +ATOM 4895 CB ARG B 400 -28.362 32.233 46.041 1.00100.00 C +ATOM 4896 CG ARG B 400 -29.705 31.924 45.399 1.00100.00 C +ATOM 4897 CD ARG B 400 -29.788 30.477 44.949 1.00100.00 C +ATOM 4898 NE ARG B 400 -29.609 29.557 46.069 1.00100.00 N +ATOM 4899 CZ ARG B 400 -30.592 28.861 46.627 1.00100.00 C +ATOM 4900 NH1 ARG B 400 -31.836 28.981 46.177 1.00 93.15 N +ATOM 4901 NH2 ARG B 400 -30.332 28.046 47.640 1.00100.00 N +ATOM 4902 N ASN B 401 -26.048 33.659 47.513 1.00 93.64 N +ATOM 4903 CA ASN B 401 -24.851 33.624 48.338 1.00100.00 C +ATOM 4904 C ASN B 401 -25.051 34.576 49.506 1.00100.00 C +ATOM 4905 O ASN B 401 -24.904 34.192 50.668 1.00100.00 O +ATOM 4906 CB ASN B 401 -23.631 34.053 47.522 1.00100.00 C +ATOM 4907 CG ASN B 401 -22.785 32.878 47.081 1.00100.00 C +ATOM 4908 OD1 ASN B 401 -21.574 33.002 46.900 1.00100.00 O +ATOM 4909 ND2 ASN B 401 -23.422 31.723 46.909 1.00100.00 N +ATOM 4910 N PHE B 402 -25.382 35.824 49.184 1.00 93.04 N +ATOM 4911 CA PHE B 402 -25.625 36.836 50.204 1.00 91.07 C +ATOM 4912 C PHE B 402 -26.781 36.348 51.064 1.00 92.04 C +ATOM 4913 O PHE B 402 -26.919 36.732 52.227 1.00 74.85 O +ATOM 4914 CB PHE B 402 -25.997 38.168 49.557 1.00 86.42 C +ATOM 4915 CG PHE B 402 -25.881 39.344 50.481 1.00 94.63 C +ATOM 4916 CD1 PHE B 402 -24.634 39.795 50.893 1.00 96.48 C +ATOM 4917 CD2 PHE B 402 -27.016 40.004 50.939 1.00 98.63 C +ATOM 4918 CE1 PHE B 402 -24.517 40.889 51.746 1.00 97.75 C +ATOM 4919 CE2 PHE B 402 -26.910 41.099 51.793 1.00 98.92 C +ATOM 4920 CZ PHE B 402 -25.659 41.541 52.197 1.00 93.38 C +ATOM 4921 N ALA B 403 -27.613 35.501 50.467 1.00 91.11 N +ATOM 4922 CA ALA B 403 -28.760 34.928 51.151 1.00 78.32 C +ATOM 4923 C ALA B 403 -28.242 33.843 52.081 1.00 75.97 C +ATOM 4924 O ALA B 403 -28.704 33.709 53.213 1.00 91.47 O +ATOM 4925 CB ALA B 403 -29.733 34.335 50.141 1.00 59.20 C +ATOM 4926 N ALA B 404 -27.277 33.068 51.595 1.00 56.75 N +ATOM 4927 CA ALA B 404 -26.691 32.002 52.395 1.00 62.82 C +ATOM 4928 C ALA B 404 -25.909 32.653 53.522 1.00 68.19 C +ATOM 4929 O ALA B 404 -25.646 32.036 54.556 1.00 76.83 O +ATOM 4930 CB ALA B 404 -25.772 31.147 51.544 1.00 78.44 C +ATOM 4931 N THR B 405 -25.539 33.912 53.309 1.00 62.58 N +ATOM 4932 CA THR B 405 -24.802 34.671 54.314 1.00 75.32 C +ATOM 4933 C THR B 405 -25.749 35.002 55.471 1.00 72.06 C +ATOM 4934 O THR B 405 -25.349 35.016 56.637 1.00 73.32 O +ATOM 4935 CB THR B 405 -24.254 35.989 53.728 1.00 73.78 C +ATOM 4936 OG1 THR B 405 -23.637 35.728 52.463 1.00 95.88 O +ATOM 4937 CG2 THR B 405 -23.230 36.602 54.673 1.00 67.17 C +ATOM 4938 N ILE B 406 -27.006 35.265 55.128 1.00 57.19 N +ATOM 4939 CA ILE B 406 -28.027 35.596 56.113 1.00 54.50 C +ATOM 4940 C ILE B 406 -28.164 34.500 57.160 1.00 55.94 C +ATOM 4941 O ILE B 406 -28.687 33.415 56.883 1.00 57.55 O +ATOM 4942 CB ILE B 406 -29.407 35.802 55.447 1.00 71.06 C +ATOM 4943 CG1 ILE B 406 -29.247 36.639 54.173 1.00 65.50 C +ATOM 4944 CG2 ILE B 406 -30.365 36.464 56.435 1.00 59.64 C +ATOM 4945 CD1 ILE B 406 -28.596 37.991 54.386 1.00 69.61 C +ATOM 4946 N PRO B 407 -27.716 34.779 58.391 1.00 54.54 N +ATOM 4947 CA PRO B 407 -27.789 33.812 59.489 1.00 49.13 C +ATOM 4948 C PRO B 407 -29.197 33.673 60.073 1.00 47.38 C +ATOM 4949 O PRO B 407 -29.612 34.476 60.907 1.00 52.30 O +ATOM 4950 CB PRO B 407 -26.785 34.353 60.514 1.00 50.96 C +ATOM 4951 CG PRO B 407 -26.207 35.625 59.904 1.00 61.37 C +ATOM 4952 CD PRO B 407 -27.131 36.052 58.827 1.00 58.57 C +ATOM 4953 N ARG B 408 -29.919 32.648 59.621 1.00 48.85 N +ATOM 4954 CA ARG B 408 -31.278 32.349 60.083 1.00 56.74 C +ATOM 4955 C ARG B 408 -31.277 30.963 60.727 1.00 59.82 C +ATOM 4956 O ARG B 408 -30.673 30.032 60.194 1.00 73.93 O +ATOM 4957 CB ARG B 408 -32.258 32.353 58.902 1.00 79.31 C +ATOM 4958 CG ARG B 408 -32.643 33.733 58.386 1.00 96.41 C +ATOM 4959 CD ARG B 408 -34.139 33.826 58.093 1.00 89.26 C +ATOM 4960 NE ARG B 408 -34.576 32.865 57.083 1.00 61.83 N +ATOM 4961 CZ ARG B 408 -34.211 32.901 55.807 1.00 62.62 C +ATOM 4962 NH1 ARG B 408 -33.399 33.852 55.370 1.00 55.94 N +ATOM 4963 NH2 ARG B 408 -34.658 31.983 54.965 1.00 79.75 N +ATOM 4964 N PRO B 409 -31.982 30.798 61.862 1.00 50.99 N +ATOM 4965 CA PRO B 409 -32.009 29.489 62.531 1.00 53.84 C +ATOM 4966 C PRO B 409 -32.743 28.393 61.765 1.00 64.96 C +ATOM 4967 O PRO B 409 -33.130 27.372 62.337 1.00 66.01 O +ATOM 4968 CB PRO B 409 -32.665 29.778 63.884 1.00 59.30 C +ATOM 4969 CG PRO B 409 -32.847 31.274 63.948 1.00 71.67 C +ATOM 4970 CD PRO B 409 -32.834 31.779 62.546 1.00 64.79 C +ATOM 4971 N PHE B 410 -32.926 28.607 60.465 1.00 74.36 N +ATOM 4972 CA PHE B 410 -33.626 27.641 59.621 1.00 68.36 C +ATOM 4973 C PHE B 410 -33.606 28.045 58.147 1.00 66.39 C +ATOM 4974 O PHE B 410 -32.862 28.942 57.732 1.00 56.30 O +ATOM 4975 CB PHE B 410 -35.087 27.514 60.078 1.00 63.35 C +ATOM 4976 CG PHE B 410 -35.779 28.845 60.269 1.00 67.61 C +ATOM 4977 CD1 PHE B 410 -35.455 29.934 59.460 1.00 68.04 C +ATOM 4978 CD2 PHE B 410 -36.733 29.021 61.269 1.00 71.61 C +ATOM 4979 CE1 PHE B 410 -36.065 31.171 59.642 1.00 63.36 C +ATOM 4980 CE2 PHE B 410 -37.353 30.259 61.460 1.00 60.66 C +ATOM 4981 CZ PHE B 410 -37.014 31.335 60.643 1.00 62.48 C +ATOM 4982 N SER B 411 -34.454 27.371 57.376 1.00 54.52 N +ATOM 4983 CA SER B 411 -34.597 27.616 55.949 1.00 39.07 C +ATOM 4984 C SER B 411 -36.081 27.573 55.602 1.00 37.27 C +ATOM 4985 O SER B 411 -36.830 26.781 56.176 1.00 36.77 O +ATOM 4986 CB SER B 411 -33.851 26.545 55.156 1.00 30.32 C +ATOM 4987 OG SER B 411 -32.618 27.052 54.680 1.00 50.98 O +ATOM 4988 N VAL B 412 -36.505 28.421 54.670 1.00 35.39 N +ATOM 4989 CA VAL B 412 -37.907 28.462 54.269 1.00 24.54 C +ATOM 4990 C VAL B 412 -38.051 28.197 52.782 1.00 32.26 C +ATOM 4991 O VAL B 412 -37.167 28.533 51.995 1.00 24.52 O +ATOM 4992 CB VAL B 412 -38.545 29.834 54.579 1.00 24.31 C +ATOM 4993 CG1 VAL B 412 -38.834 29.952 56.065 1.00 23.33 C +ATOM 4994 CG2 VAL B 412 -37.624 30.951 54.124 1.00 32.01 C +ATOM 4995 N ARG B 413 -39.172 27.589 52.408 1.00 37.85 N +ATOM 4996 CA ARG B 413 -39.451 27.279 51.011 1.00 54.90 C +ATOM 4997 C ARG B 413 -40.881 27.665 50.672 1.00 60.27 C +ATOM 4998 O ARG B 413 -41.797 27.404 51.446 1.00 52.18 O +ATOM 4999 CB ARG B 413 -39.251 25.786 50.742 1.00 57.85 C +ATOM 5000 CG ARG B 413 -39.631 25.353 49.331 1.00 60.82 C +ATOM 5001 CD ARG B 413 -40.979 24.642 49.292 1.00 66.38 C +ATOM 5002 NE ARG B 413 -41.160 23.735 50.424 1.00 70.92 N +ATOM 5003 CZ ARG B 413 -42.153 22.857 50.529 1.00 72.59 C +ATOM 5004 NH1 ARG B 413 -43.062 22.763 49.567 1.00 65.24 N +ATOM 5005 NH2 ARG B 413 -42.236 22.069 51.593 1.00 55.86 N +ATOM 5006 N TYR B 414 -41.066 28.295 49.515 1.00 56.80 N +ATOM 5007 CA TYR B 414 -42.394 28.715 49.083 1.00 55.62 C +ATOM 5008 C TYR B 414 -43.104 27.626 48.279 1.00 53.33 C +ATOM 5009 O TYR B 414 -42.519 27.028 47.374 1.00 80.67 O +ATOM 5010 CB TYR B 414 -42.296 29.994 48.242 1.00 57.36 C +ATOM 5011 CG TYR B 414 -43.637 30.549 47.814 1.00 71.59 C +ATOM 5012 CD1 TYR B 414 -44.657 30.758 48.742 1.00 81.20 C +ATOM 5013 CD2 TYR B 414 -43.891 30.858 46.480 1.00 62.03 C +ATOM 5014 CE1 TYR B 414 -45.897 31.259 48.353 1.00 83.10 C +ATOM 5015 CE2 TYR B 414 -45.127 31.359 46.079 1.00 84.22 C +ATOM 5016 CZ TYR B 414 -46.126 31.558 47.020 1.00 89.09 C +ATOM 5017 OH TYR B 414 -47.349 32.057 46.630 1.00 94.04 O +ATOM 5018 N ASP B 415 -44.367 27.373 48.620 1.00 46.78 N +ATOM 5019 CA ASP B 415 -45.180 26.370 47.931 1.00 45.75 C +ATOM 5020 C ASP B 415 -46.236 27.085 47.094 1.00 37.93 C +ATOM 5021 O ASP B 415 -47.249 27.540 47.615 1.00 42.42 O +ATOM 5022 CB ASP B 415 -45.859 25.437 48.942 1.00 53.54 C +ATOM 5023 CG ASP B 415 -46.218 24.085 48.344 1.00 72.49 C +ATOM 5024 OD1 ASP B 415 -46.902 24.059 47.300 1.00 81.43 O +ATOM 5025 OD2 ASP B 415 -45.814 23.049 48.914 1.00 68.23 O +ATOM 5026 N PRO B 416 -46.001 27.195 45.779 1.00 34.92 N +ATOM 5027 CA PRO B 416 -46.923 27.860 44.856 1.00 40.44 C +ATOM 5028 C PRO B 416 -48.309 27.243 44.755 1.00 37.13 C +ATOM 5029 O PRO B 416 -49.238 27.895 44.287 1.00 52.25 O +ATOM 5030 CB PRO B 416 -46.191 27.825 43.511 1.00 44.31 C +ATOM 5031 CG PRO B 416 -44.790 27.484 43.823 1.00 49.92 C +ATOM 5032 CD PRO B 416 -44.810 26.686 45.086 1.00 50.32 C +ATOM 5033 N TYR B 417 -48.455 25.994 45.186 1.00 28.69 N +ATOM 5034 CA TYR B 417 -49.752 25.320 45.117 1.00 38.77 C +ATOM 5035 C TYR B 417 -50.640 25.709 46.288 1.00 41.07 C +ATOM 5036 O TYR B 417 -51.817 26.021 46.110 1.00 53.69 O +ATOM 5037 CB TYR B 417 -49.567 23.797 45.091 1.00 36.92 C +ATOM 5038 CG TYR B 417 -49.060 23.262 43.766 1.00 59.52 C +ATOM 5039 CD1 TYR B 417 -47.699 23.266 43.468 1.00 74.44 C +ATOM 5040 CD2 TYR B 417 -49.940 22.764 42.803 1.00 63.68 C +ATOM 5041 CE1 TYR B 417 -47.228 22.794 42.244 1.00 65.02 C +ATOM 5042 CE2 TYR B 417 -49.474 22.289 41.574 1.00 54.57 C +ATOM 5043 CZ TYR B 417 -48.120 22.307 41.305 1.00 51.94 C +ATOM 5044 OH TYR B 417 -47.658 21.844 40.097 1.00 52.98 O +ATOM 5045 N THR B 418 -50.070 25.681 47.487 1.00 46.91 N +ATOM 5046 CA THR B 418 -50.803 26.039 48.695 1.00 55.02 C +ATOM 5047 C THR B 418 -50.545 27.502 49.022 1.00 52.04 C +ATOM 5048 O THR B 418 -51.076 28.034 49.997 1.00 69.95 O +ATOM 5049 CB THR B 418 -50.358 25.185 49.897 1.00 57.50 C +ATOM 5050 OG1 THR B 418 -48.956 25.374 50.127 1.00 56.66 O +ATOM 5051 CG2 THR B 418 -50.623 23.725 49.629 1.00 61.75 C +ATOM 5052 N GLN B 419 -49.729 28.148 48.195 1.00 45.36 N +ATOM 5053 CA GLN B 419 -49.376 29.551 48.384 1.00 52.53 C +ATOM 5054 C GLN B 419 -49.104 29.867 49.854 1.00 48.40 C +ATOM 5055 O GLN B 419 -49.516 30.899 50.384 1.00 53.82 O +ATOM 5056 CB GLN B 419 -50.471 30.447 47.806 1.00 62.30 C +ATOM 5057 CG GLN B 419 -50.455 30.436 46.279 1.00 92.40 C +ATOM 5058 CD GLN B 419 -51.487 31.347 45.650 1.00100.00 C +ATOM 5059 OE1 GLN B 419 -52.414 31.815 46.313 1.00100.00 O +ATOM 5060 NE2 GLN B 419 -51.331 31.601 44.353 1.00100.00 N +ATOM 5061 N ARG B 420 -48.386 28.945 50.490 1.00 52.67 N +ATOM 5062 CA ARG B 420 -47.991 29.041 51.889 1.00 48.06 C +ATOM 5063 C ARG B 420 -46.469 29.147 51.897 1.00 44.16 C +ATOM 5064 O ARG B 420 -45.822 28.907 50.879 1.00 52.33 O +ATOM 5065 CB ARG B 420 -48.362 27.764 52.637 1.00 52.96 C +ATOM 5066 CG ARG B 420 -49.732 27.712 53.262 1.00 53.84 C +ATOM 5067 CD ARG B 420 -49.979 26.280 53.697 1.00 76.17 C +ATOM 5068 NE ARG B 420 -51.049 26.141 54.677 1.00 99.80 N +ATOM 5069 CZ ARG B 420 -51.632 24.984 54.976 1.00100.00 C +ATOM 5070 NH1 ARG B 420 -51.249 23.871 54.362 1.00 88.44 N +ATOM 5071 NH2 ARG B 420 -52.604 24.940 55.878 1.00100.00 N +ATOM 5072 N ILE B 421 -45.903 29.499 53.045 1.00 26.85 N +ATOM 5073 CA ILE B 421 -44.456 29.582 53.188 1.00 12.67 C +ATOM 5074 C ILE B 421 -44.092 28.423 54.108 1.00 36.59 C +ATOM 5075 O ILE B 421 -44.552 28.368 55.249 1.00 29.54 O +ATOM 5076 CB ILE B 421 -44.007 30.895 53.845 1.00 12.33 C +ATOM 5077 CG1 ILE B 421 -43.703 31.935 52.766 1.00 18.57 C +ATOM 5078 CG2 ILE B 421 -42.772 30.652 54.702 1.00 5.84 C +ATOM 5079 CD1 ILE B 421 -42.415 31.683 52.017 1.00 21.32 C +ATOM 5080 N GLU B 422 -43.270 27.502 53.608 1.00 59.38 N +ATOM 5081 CA GLU B 422 -42.865 26.322 54.368 1.00 60.87 C +ATOM 5082 C GLU B 422 -41.584 26.500 55.163 1.00 59.70 C +ATOM 5083 O GLU B 422 -40.531 26.814 54.606 1.00 65.41 O +ATOM 5084 CB GLU B 422 -42.691 25.123 53.430 1.00 67.51 C +ATOM 5085 CG GLU B 422 -43.987 24.598 52.828 1.00 76.03 C +ATOM 5086 CD GLU B 422 -44.869 23.902 53.848 1.00 84.53 C +ATOM 5087 OE1 GLU B 422 -44.861 22.653 53.888 1.00 97.45 O +ATOM 5088 OE2 GLU B 422 -45.571 24.605 54.606 1.00 81.73 O +ATOM 5089 N VAL B 423 -41.682 26.282 56.471 1.00 61.14 N +ATOM 5090 CA VAL B 423 -40.528 26.389 57.351 1.00 66.29 C +ATOM 5091 C VAL B 423 -39.871 25.013 57.410 1.00 63.63 C +ATOM 5092 O VAL B 423 -40.459 24.047 57.903 1.00 60.26 O +ATOM 5093 CB VAL B 423 -40.929 26.814 58.789 1.00 64.16 C +ATOM 5094 CG1 VAL B 423 -39.685 27.189 59.579 1.00 54.84 C +ATOM 5095 CG2 VAL B 423 -41.898 27.979 58.747 1.00 70.94 C +ATOM 5096 N LEU B 424 -38.654 24.925 56.889 1.00 63.78 N +ATOM 5097 CA LEU B 424 -37.928 23.668 56.888 1.00 55.00 C +ATOM 5098 C LEU B 424 -37.094 23.572 58.152 1.00 62.60 C +ATOM 5099 O LEU B 424 -36.039 24.200 58.263 1.00 69.94 O +ATOM 5100 CB LEU B 424 -37.033 23.578 55.647 1.00 55.01 C +ATOM 5101 CG LEU B 424 -37.729 23.888 54.318 1.00 47.53 C +ATOM 5102 CD1 LEU B 424 -36.681 24.167 53.261 1.00 44.35 C +ATOM 5103 CD2 LEU B 424 -38.630 22.731 53.910 1.00 31.73 C +ATOM 5104 N ASP B 425 -37.585 22.788 59.107 1.00 68.96 N +ATOM 5105 CA ASP B 425 -36.904 22.586 60.378 1.00 76.54 C +ATOM 5106 C ASP B 425 -37.063 21.133 60.805 1.00 80.36 C +ATOM 5107 O ASP B 425 -36.247 20.607 61.560 1.00 92.65 O +ATOM 5108 CB ASP B 425 -37.497 23.502 61.452 1.00 75.64 C +ATOM 5109 CG ASP B 425 -39.004 23.353 61.578 1.00 84.75 C +ATOM 5110 OD1 ASP B 425 -39.722 23.768 60.647 1.00 93.24 O +ATOM 5111 OD2 ASP B 425 -39.474 22.821 62.606 1.00 91.90 O +ATOM 5112 N ASN B 426 -38.119 20.489 60.315 1.00 76.24 N +ATOM 5113 CA ASN B 426 -38.377 19.098 60.650 1.00 71.04 C +ATOM 5114 C ASN B 426 -37.817 18.152 59.598 1.00 75.63 C +ATOM 5115 O ASN B 426 -37.666 18.521 58.434 1.00 83.46 O +ATOM 5116 CB ASN B 426 -39.875 18.853 60.803 1.00 80.23 C +ATOM 5117 CG ASN B 426 -40.174 17.523 61.457 1.00100.00 C +ATOM 5118 OD1 ASN B 426 -41.212 16.912 61.209 1.00100.00 O +ATOM 5119 ND2 ASN B 426 -39.257 17.064 62.304 1.00100.00 N +ATOM 5120 N THR B 427 -37.520 16.925 60.017 1.00 81.33 N +ATOM 5121 CA THR B 427 -36.971 15.920 59.115 1.00 80.19 C +ATOM 5122 C THR B 427 -37.966 15.469 58.053 1.00 70.69 C +ATOM 5123 O THR B 427 -37.566 14.986 56.996 1.00 79.70 O +ATOM 5124 CB THR B 427 -36.492 14.675 59.887 1.00 83.76 C +ATOM 5125 OG1 THR B 427 -37.585 14.122 60.628 1.00 87.74 O +ATOM 5126 CG2 THR B 427 -35.366 15.041 60.837 1.00 76.68 C +ATOM 5127 N GLN B 428 -39.258 15.618 58.329 1.00 49.69 N +ATOM 5128 CA GLN B 428 -40.274 15.222 57.358 1.00 52.53 C +ATOM 5129 C GLN B 428 -40.512 16.362 56.377 1.00 51.11 C +ATOM 5130 O GLN B 428 -40.998 16.152 55.266 1.00 41.08 O +ATOM 5131 CB GLN B 428 -41.583 14.849 58.059 1.00 66.13 C +ATOM 5132 CG GLN B 428 -41.884 13.350 58.049 1.00 90.15 C +ATOM 5133 CD GLN B 428 -42.820 12.933 56.919 1.00 86.66 C +ATOM 5134 OE1 GLN B 428 -43.249 13.758 56.110 1.00 83.00 O +ATOM 5135 NE2 GLN B 428 -43.141 11.644 56.863 1.00 61.40 N +ATOM 5136 N GLN B 429 -40.159 17.570 56.801 1.00 58.96 N +ATOM 5137 CA GLN B 429 -40.306 18.749 55.964 1.00 63.52 C +ATOM 5138 C GLN B 429 -39.372 18.618 54.765 1.00 54.99 C +ATOM 5139 O GLN B 429 -39.667 19.103 53.674 1.00 69.70 O +ATOM 5140 CB GLN B 429 -39.948 20.008 56.761 1.00 79.59 C +ATOM 5141 CG GLN B 429 -41.129 20.664 57.460 1.00 81.71 C +ATOM 5142 CD GLN B 429 -42.184 21.154 56.489 1.00 78.96 C +ATOM 5143 OE1 GLN B 429 -42.078 22.250 55.942 1.00 84.65 O +ATOM 5144 NE2 GLN B 429 -43.208 20.339 56.265 1.00 58.71 N +ATOM 5145 N LEU B 430 -38.242 17.953 54.983 1.00 40.34 N +ATOM 5146 CA LEU B 430 -37.248 17.758 53.936 1.00 44.53 C +ATOM 5147 C LEU B 430 -37.571 16.560 53.047 1.00 49.41 C +ATOM 5148 O LEU B 430 -37.144 16.501 51.895 1.00 49.82 O +ATOM 5149 CB LEU B 430 -35.865 17.598 54.567 1.00 49.27 C +ATOM 5150 CG LEU B 430 -35.478 18.807 55.429 1.00 46.92 C +ATOM 5151 CD1 LEU B 430 -34.289 18.477 56.314 1.00 39.85 C +ATOM 5152 CD2 LEU B 430 -35.166 19.983 54.524 1.00 60.57 C +ATOM 5153 N LYS B 431 -38.325 15.608 53.590 1.00 50.79 N +ATOM 5154 CA LYS B 431 -38.714 14.420 52.841 1.00 49.15 C +ATOM 5155 C LYS B 431 -39.484 14.846 51.597 1.00 44.82 C +ATOM 5156 O LYS B 431 -39.309 14.287 50.513 1.00 55.90 O +ATOM 5157 CB LYS B 431 -39.616 13.528 53.697 1.00 56.53 C +ATOM 5158 CG LYS B 431 -38.895 12.614 54.665 1.00 62.29 C +ATOM 5159 CD LYS B 431 -39.851 11.565 55.223 1.00 61.91 C +ATOM 5160 CE LYS B 431 -39.242 10.789 56.381 1.00 75.65 C +ATOM 5161 NZ LYS B 431 -40.178 9.751 56.894 1.00 72.22 N +ATOM 5162 N ILE B 432 -40.332 15.853 51.773 1.00 45.17 N +ATOM 5163 CA ILE B 432 -41.174 16.367 50.697 1.00 66.00 C +ATOM 5164 C ILE B 432 -40.487 17.306 49.711 1.00 58.78 C +ATOM 5165 O ILE B 432 -40.816 17.309 48.528 1.00 60.28 O +ATOM 5166 CB ILE B 432 -42.422 17.066 51.269 1.00 80.32 C +ATOM 5167 CG1 ILE B 432 -42.156 17.510 52.712 1.00 88.13 C +ATOM 5168 CG2 ILE B 432 -43.620 16.126 51.185 1.00 94.34 C +ATOM 5169 CD1 ILE B 432 -43.408 17.664 53.567 1.00100.00 C +ATOM 5170 N LEU B 433 -39.556 18.120 50.189 1.00 48.19 N +ATOM 5171 CA LEU B 433 -38.847 19.015 49.284 1.00 46.48 C +ATOM 5172 C LEU B 433 -37.998 18.106 48.397 1.00 50.62 C +ATOM 5173 O LEU B 433 -37.876 18.321 47.185 1.00 29.72 O +ATOM 5174 CB LEU B 433 -37.955 19.989 50.070 1.00 22.61 C +ATOM 5175 CG LEU B 433 -36.949 20.838 49.276 1.00 25.63 C +ATOM 5176 CD1 LEU B 433 -37.657 21.582 48.169 1.00 23.52 C +ATOM 5177 CD2 LEU B 433 -36.252 21.815 50.205 1.00 21.65 C +ATOM 5178 N ALA B 434 -37.426 17.077 49.020 1.00 47.79 N +ATOM 5179 CA ALA B 434 -36.602 16.112 48.311 1.00 41.30 C +ATOM 5180 C ALA B 434 -37.425 15.524 47.179 1.00 40.66 C +ATOM 5181 O ALA B 434 -36.962 15.417 46.046 1.00 51.69 O +ATOM 5182 CB ALA B 434 -36.155 15.008 49.258 1.00 47.23 C +ATOM 5183 N ASP B 435 -38.655 15.142 47.500 1.00 30.86 N +ATOM 5184 CA ASP B 435 -39.565 14.560 46.522 1.00 32.91 C +ATOM 5185 C ASP B 435 -39.855 15.528 45.379 1.00 38.97 C +ATOM 5186 O ASP B 435 -39.901 15.130 44.216 1.00 34.99 O +ATOM 5187 CB ASP B 435 -40.871 14.161 47.202 1.00 43.61 C +ATOM 5188 CG ASP B 435 -40.810 12.776 47.800 1.00 66.74 C +ATOM 5189 OD1 ASP B 435 -40.589 11.814 47.036 1.00 84.71 O +ATOM 5190 OD2 ASP B 435 -40.981 12.651 49.032 1.00 83.09 O +ATOM 5191 N SER B 436 -40.046 16.799 45.715 1.00 34.82 N +ATOM 5192 CA SER B 436 -40.329 17.809 44.707 1.00 43.47 C +ATOM 5193 C SER B 436 -39.190 17.826 43.701 1.00 53.51 C +ATOM 5194 O SER B 436 -39.404 17.737 42.489 1.00 63.67 O +ATOM 5195 CB SER B 436 -40.465 19.189 45.355 1.00 46.54 C +ATOM 5196 OG SER B 436 -41.375 19.151 46.437 1.00 76.55 O +ATOM 5197 N ILE B 437 -37.971 17.931 44.214 1.00 48.32 N +ATOM 5198 CA ILE B 437 -36.797 17.959 43.359 1.00 45.93 C +ATOM 5199 C ILE B 437 -36.667 16.668 42.560 1.00 39.76 C +ATOM 5200 O ILE B 437 -36.589 16.693 41.333 1.00 48.97 O +ATOM 5201 CB ILE B 437 -35.533 18.176 44.198 1.00 43.57 C +ATOM 5202 CG1 ILE B 437 -35.731 19.409 45.081 1.00 42.04 C +ATOM 5203 CG2 ILE B 437 -34.316 18.344 43.294 1.00 48.96 C +ATOM 5204 CD1 ILE B 437 -34.519 19.806 45.894 1.00 39.26 C +ATOM 5205 N ASN B 438 -36.656 15.543 43.264 1.00 33.67 N +ATOM 5206 CA ASN B 438 -36.529 14.237 42.630 1.00 30.51 C +ATOM 5207 C ASN B 438 -37.346 14.111 41.349 1.00 39.75 C +ATOM 5208 O ASN B 438 -36.847 13.653 40.323 1.00 40.63 O +ATOM 5209 CB ASN B 438 -36.947 13.138 43.607 1.00 30.24 C +ATOM 5210 CG ASN B 438 -36.557 11.754 43.128 1.00 36.18 C +ATOM 5211 OD1 ASN B 438 -35.462 11.548 42.609 1.00 54.57 O +ATOM 5212 ND2 ASN B 438 -37.457 10.794 43.304 1.00 48.83 N +ATOM 5213 N SER B 439 -38.608 14.516 41.415 1.00 51.34 N +ATOM 5214 CA SER B 439 -39.494 14.435 40.259 1.00 57.68 C +ATOM 5215 C SER B 439 -39.127 15.435 39.173 1.00 54.76 C +ATOM 5216 O SER B 439 -39.203 15.128 37.984 1.00 62.90 O +ATOM 5217 CB SER B 439 -40.943 14.675 40.687 1.00 56.79 C +ATOM 5218 OG SER B 439 -41.148 16.038 41.019 1.00 65.36 O +ATOM 5219 N GLU B 440 -38.733 16.634 39.589 1.00 51.44 N +ATOM 5220 CA GLU B 440 -38.371 17.692 38.651 1.00 62.89 C +ATOM 5221 C GLU B 440 -37.122 17.366 37.837 1.00 62.26 C +ATOM 5222 O GLU B 440 -37.033 17.718 36.658 1.00 64.31 O +ATOM 5223 CB GLU B 440 -38.189 19.011 39.402 1.00 63.42 C +ATOM 5224 CG GLU B 440 -39.501 19.692 39.771 1.00 61.16 C +ATOM 5225 CD GLU B 440 -39.426 21.200 39.640 1.00 64.23 C +ATOM 5226 OE1 GLU B 440 -38.774 21.837 40.494 1.00 63.45 O +ATOM 5227 OE2 GLU B 440 -40.014 21.749 38.684 1.00 72.09 O +ATOM 5228 N ILE B 441 -36.156 16.699 38.462 1.00 55.97 N +ATOM 5229 CA ILE B 441 -34.945 16.322 37.749 1.00 43.28 C +ATOM 5230 C ILE B 441 -35.323 15.196 36.811 1.00 38.75 C +ATOM 5231 O ILE B 441 -34.890 15.164 35.660 1.00 43.38 O +ATOM 5232 CB ILE B 441 -33.846 15.805 38.690 1.00 32.29 C +ATOM 5233 CG1 ILE B 441 -33.820 16.632 39.974 1.00 44.61 C +ATOM 5234 CG2 ILE B 441 -32.495 15.879 37.989 1.00 31.94 C +ATOM 5235 CD1 ILE B 441 -33.009 16.004 41.084 1.00 55.07 C +ATOM 5236 N GLY B 442 -36.138 14.276 37.319 1.00 34.13 N +ATOM 5237 CA GLY B 442 -36.581 13.151 36.517 1.00 41.01 C +ATOM 5238 C GLY B 442 -37.110 13.663 35.192 1.00 42.69 C +ATOM 5239 O GLY B 442 -37.046 12.983 34.165 1.00 47.02 O +ATOM 5240 N ILE B 443 -37.639 14.880 35.223 1.00 24.56 N +ATOM 5241 CA ILE B 443 -38.163 15.516 34.026 1.00 33.86 C +ATOM 5242 C ILE B 443 -36.970 16.035 33.231 1.00 24.72 C +ATOM 5243 O ILE B 443 -36.845 15.784 32.035 1.00 26.74 O +ATOM 5244 CB ILE B 443 -39.085 16.689 34.399 1.00 33.65 C +ATOM 5245 CG1 ILE B 443 -40.372 16.143 35.020 1.00 18.45 C +ATOM 5246 CG2 ILE B 443 -39.386 17.535 33.174 1.00 31.90 C +ATOM 5247 CD1 ILE B 443 -41.346 17.198 35.466 1.00 28.89 C +ATOM 5248 N LEU B 444 -36.093 16.752 33.928 1.00 24.82 N +ATOM 5249 CA LEU B 444 -34.885 17.326 33.348 1.00 19.51 C +ATOM 5250 C LEU B 444 -34.037 16.268 32.642 1.00 24.69 C +ATOM 5251 O LEU B 444 -33.402 16.549 31.622 1.00 14.93 O +ATOM 5252 CB LEU B 444 -34.068 18.008 34.451 1.00 17.16 C +ATOM 5253 CG LEU B 444 -32.841 18.845 34.070 1.00 13.22 C +ATOM 5254 CD1 LEU B 444 -32.948 19.380 32.654 1.00 5.57 C +ATOM 5255 CD2 LEU B 444 -32.719 19.986 35.052 1.00 25.10 C +ATOM 5256 N CYS B 445 -34.033 15.058 33.195 1.00 16.52 N +ATOM 5257 CA CYS B 445 -33.288 13.942 32.626 1.00 23.91 C +ATOM 5258 C CYS B 445 -33.978 13.425 31.367 1.00 35.90 C +ATOM 5259 O CYS B 445 -33.385 13.413 30.291 1.00 52.53 O +ATOM 5260 CB CYS B 445 -33.177 12.806 33.636 1.00 21.95 C +ATOM 5261 SG CYS B 445 -31.986 13.104 34.932 1.00 40.86 S +ATOM 5262 N SER B 446 -35.231 12.996 31.509 1.00 36.20 N +ATOM 5263 CA SER B 446 -36.011 12.475 30.384 1.00 35.38 C +ATOM 5264 C SER B 446 -35.928 13.433 29.200 1.00 32.96 C +ATOM 5265 O SER B 446 -35.768 13.011 28.054 1.00 47.99 O +ATOM 5266 CB SER B 446 -37.474 12.291 30.797 1.00 52.34 C +ATOM 5267 OG SER B 446 -37.602 11.335 31.836 1.00 95.09 O +ATOM 5268 N ALA B 447 -36.041 14.726 29.491 1.00 22.50 N +ATOM 5269 CA ALA B 447 -35.963 15.759 28.468 1.00 19.89 C +ATOM 5270 C ALA B 447 -34.593 15.672 27.811 1.00 39.54 C +ATOM 5271 O ALA B 447 -34.479 15.496 26.596 1.00 45.35 O +ATOM 5272 CB ALA B 447 -36.155 17.138 29.093 1.00 21.10 C +ATOM 5273 N LEU B 448 -33.553 15.788 28.631 1.00 52.94 N +ATOM 5274 CA LEU B 448 -32.177 15.724 28.153 1.00 46.98 C +ATOM 5275 C LEU B 448 -31.920 14.453 27.357 1.00 43.58 C +ATOM 5276 O LEU B 448 -31.272 14.489 26.315 1.00 57.61 O +ATOM 5277 CB LEU B 448 -31.207 15.793 29.332 1.00 21.33 C +ATOM 5278 CG LEU B 448 -30.956 17.199 29.876 1.00 30.43 C +ATOM 5279 CD1 LEU B 448 -30.039 17.117 31.079 1.00 22.31 C +ATOM 5280 CD2 LEU B 448 -30.343 18.070 28.792 1.00 19.85 C +ATOM 5281 N GLN B 449 -32.423 13.331 27.857 1.00 31.83 N +ATOM 5282 CA GLN B 449 -32.240 12.050 27.188 1.00 51.09 C +ATOM 5283 C GLN B 449 -32.799 12.068 25.771 1.00 57.60 C +ATOM 5284 O GLN B 449 -32.375 11.291 24.912 1.00 84.67 O +ATOM 5285 CB GLN B 449 -32.931 10.931 27.977 1.00 60.51 C +ATOM 5286 CG GLN B 449 -32.390 10.716 29.379 1.00 85.66 C +ATOM 5287 CD GLN B 449 -30.877 10.749 29.438 1.00 87.05 C +ATOM 5288 OE1 GLN B 449 -30.292 11.439 30.274 1.00 92.85 O +ATOM 5289 NE2 GLN B 449 -30.233 10.001 28.549 1.00 86.96 N +ATOM 5290 N LYS B 450 -33.753 12.958 25.529 1.00 51.88 N +ATOM 5291 CA LYS B 450 -34.376 13.044 24.220 1.00 58.83 C +ATOM 5292 C LYS B 450 -33.770 14.112 23.319 1.00 53.86 C +ATOM 5293 O LYS B 450 -34.303 14.392 22.245 1.00 60.53 O +ATOM 5294 CB LYS B 450 -35.873 13.299 24.388 1.00 52.01 C +ATOM 5295 CG LYS B 450 -36.623 12.113 24.955 1.00 48.95 C +ATOM 5296 CD LYS B 450 -38.073 12.453 25.219 1.00 31.16 C +ATOM 5297 CE LYS B 450 -38.803 11.265 25.814 1.00 42.41 C +ATOM 5298 NZ LYS B 450 -38.154 10.823 27.075 1.00 60.56 N +ATOM 5299 N ILE B 451 -32.655 14.699 23.747 1.00 54.92 N +ATOM 5300 CA ILE B 451 -32.010 15.740 22.954 1.00 69.53 C +ATOM 5301 C ILE B 451 -30.631 15.361 22.425 1.00 70.22 C +ATOM 5302 O ILE B 451 -29.628 16.005 22.734 1.00 50.03 O +ATOM 5303 CB ILE B 451 -31.906 17.071 23.746 1.00 76.55 C +ATOM 5304 CG1 ILE B 451 -31.476 18.198 22.800 1.00 81.46 C +ATOM 5305 CG2 ILE B 451 -30.936 16.924 24.910 1.00 52.00 C +ATOM 5306 CD1 ILE B 451 -32.445 18.456 21.660 1.00 67.09 C +ATOM 5307 N LYS B 452 -30.594 14.309 21.615 1.00 88.57 N +ATOM 5308 CA LYS B 452 -29.349 13.850 21.024 1.00 99.23 C +ATOM 5309 C LYS B 452 -29.173 14.512 19.652 1.00100.00 C +ATOM 5310 O LYS B 452 -28.190 15.265 19.474 1.00100.00 O +ATOM 5311 CB LYS B 452 -29.371 12.324 20.877 1.00 91.96 C +ATOM 5312 CG LYS B 452 -28.133 11.748 20.217 1.00 84.44 C +ATOM 5313 CD LYS B 452 -28.153 10.228 20.240 1.00 72.11 C +ATOM 5314 CE LYS B 452 -29.142 9.672 19.230 1.00 71.82 C +ATOM 5315 NZ LYS B 452 -28.710 9.937 17.832 1.00 70.50 N +ATOM 5316 OXT LYS B 452 -30.029 14.278 18.772 1.00100.00 O +TER 5317 LYS B 452 +HETATM 5318 FE FE A 453 6.443 25.284 42.925 1.00 84.26 FE +HETATM 5319 FE FE B 454 -39.037 51.235 43.684 1.00 91.31 FE +CONECT 1355 5318 +CONECT 1394 5318 +CONECT 1715 5318 +CONECT 3985 5319 +CONECT 4024 5319 +CONECT 4345 5319 +CONECT 5318 1355 1394 1715 +CONECT 5319 3985 4024 4345 +MASTER 324 0 2 32 12 0 4 6 5317 2 8 52 +END \ No newline at end of file diff --git a/tests/SIFTS/2pah.xml b/tests/testdata/sifts/2pah.xml similarity index 92% rename from tests/SIFTS/2pah.xml rename to tests/testdata/sifts/2pah.xml index f981257..5404a75 100644 --- a/tests/SIFTS/2pah.xml +++ b/tests/testdata/sifts/2pah.xml @@ -1,23 +1,23 @@ - + Copyright notice: (c) 2004-2013, EMBL-EBI, PDBe-UniProt - Jose M. Dana, Paul Gane, Jie Luo, Glen van Ginkel, Claire O'Donovan, Maria J. Martin, Sameer Velankar. + Jose M. Dana, Paul Gane, Jie Luo, Glen van Ginkel, Claire O'Donovan, Maria J. Martin, Sameer Velankar. The information included is supplied as-is, under the terms and conditions of the licence agreement. - - - - - + + + + + - - + + @@ -29,11 +29,10 @@ - + - - + T loop @@ -45,12 +44,11 @@ - + - - - + + T loop @@ -62,12 +60,11 @@ - + - - - + + T loop @@ -79,12 +76,11 @@ - + - - - + + T loop @@ -96,12 +92,11 @@ - + - - - + + T loop @@ -113,12 +108,11 @@ - + - - - + + T loop @@ -130,12 +124,11 @@ - + - - - + + T loop @@ -147,12 +140,11 @@ - + - - - + + H helix @@ -164,12 +156,11 @@ - + - - - + + H helix @@ -181,12 +172,11 @@ - + - - - + + H helix @@ -198,12 +188,11 @@ - + - - - + + H helix @@ -215,12 +204,11 @@ - + - - - + + H helix @@ -232,12 +220,11 @@ - + - - - + + H helix @@ -249,12 +236,11 @@ - + - - - + + H helix @@ -266,12 +252,11 @@ - + - - - + + T loop @@ -283,12 +268,11 @@ - + - - - + + T loop @@ -300,12 +284,11 @@ - + - - - + + T loop @@ -317,12 +300,11 @@ - + - - - + + T loop @@ -334,12 +316,11 @@ - + - - - + + T loop @@ -351,12 +332,11 @@ - + - - - + + T loop Not_Observed @@ -369,12 +349,11 @@ - + - - - + + T loop Not_Observed @@ -387,12 +366,11 @@ - + - - - + + T loop Not_Observed @@ -405,12 +383,11 @@ - + - - - + + T loop Not_Observed @@ -423,12 +400,11 @@ - + - - - + + T loop Not_Observed @@ -441,12 +417,11 @@ - + - - - + + T loop Not_Observed @@ -459,12 +434,11 @@ - + - - - + + T loop @@ -476,12 +450,11 @@ - + - - - + + T loop @@ -493,12 +466,11 @@ - + - - - + + T loop @@ -510,12 +482,11 @@ - + - - - + + T loop @@ -527,13 +498,12 @@ - + - - - + + T loop @@ -545,13 +515,12 @@ - + - - - + + T loop @@ -563,13 +532,12 @@ - + - - - + + T loop @@ -581,13 +549,12 @@ - + - - - + + T loop @@ -599,13 +566,12 @@ - + - - - + + H helix @@ -617,13 +583,12 @@ - + - - - + + H helix @@ -635,13 +600,12 @@ - + - - - + + H helix @@ -653,14 +617,13 @@ - + - - - - H + + + H helix @@ -671,13 +634,12 @@ - + - - - + + H helix @@ -689,13 +651,12 @@ - + - - - + + H helix @@ -707,13 +668,12 @@ - + - - - + + H helix @@ -725,13 +685,12 @@ - + - - - + + H helix @@ -743,13 +702,12 @@ - + - - - + + H helix @@ -761,13 +719,12 @@ - + - - - + + H helix @@ -779,13 +736,12 @@ - + - - - + + H helix @@ -797,13 +753,12 @@ - + - - - + + H helix @@ -815,13 +770,12 @@ - + - - - + + H helix @@ -833,13 +787,12 @@ - + - - - + + H helix @@ -851,13 +804,12 @@ - + - - - + + H helix @@ -869,13 +821,12 @@ - + - - - + + H helix @@ -887,12 +838,11 @@ - + - - - + + H helix @@ -904,12 +854,11 @@ - + - - - + + H helix @@ -921,12 +870,11 @@ - + - - - + + T loop @@ -938,12 +886,11 @@ - + - - - + + T loop @@ -955,12 +902,11 @@ - + - - - + + T loop @@ -972,12 +918,11 @@ - + - - - + + T loop @@ -989,12 +934,11 @@ - + - - - + + T loop @@ -1006,12 +950,11 @@ - + - - - + + T loop @@ -1023,12 +966,11 @@ - + - - - + + T loop @@ -1040,12 +982,11 @@ - + - - - + + T loop @@ -1057,12 +998,11 @@ - + - - - + + T loop @@ -1074,12 +1014,11 @@ - + - - - + + T loop @@ -1091,12 +1030,11 @@ - + - - - + + T loop @@ -1108,12 +1046,11 @@ - + - - - + + H helix @@ -1125,12 +1062,11 @@ - + - - - + + H helix @@ -1142,12 +1078,11 @@ - + - - - + + H helix @@ -1159,12 +1094,11 @@ - + - - - + + H helix @@ -1176,12 +1110,11 @@ - + - - - + + H helix @@ -1193,12 +1126,11 @@ - + - - - + + H helix @@ -1210,12 +1142,11 @@ - + - - - + + H helix @@ -1227,12 +1158,11 @@ - + - - - + + H helix @@ -1244,12 +1174,11 @@ - + - - - + + H helix @@ -1261,12 +1190,11 @@ - + - - - + + H helix @@ -1278,12 +1206,11 @@ - + - - - + + H helix @@ -1295,12 +1222,11 @@ - + - - - + + H helix @@ -1312,12 +1238,11 @@ - + - - - + + H helix @@ -1329,12 +1254,11 @@ - + - - - + + H helix @@ -1346,12 +1270,11 @@ - + - - - + + H helix @@ -1363,12 +1286,11 @@ - + - - - + + H helix @@ -1380,12 +1302,11 @@ - + - - - + + H helix @@ -1397,12 +1318,11 @@ - + - - - + + H helix @@ -1414,12 +1334,11 @@ - + - - - + + H helix @@ -1431,12 +1350,11 @@ - + - - - + + H helix @@ -1448,12 +1366,11 @@ - + - - - + + H helix @@ -1465,12 +1382,11 @@ - + - - - + + H helix @@ -1482,12 +1398,11 @@ - + - - - + + H helix @@ -1499,12 +1414,11 @@ - + - - - + + H helix @@ -1516,12 +1430,11 @@ - + - - - + + H helix @@ -1533,12 +1446,11 @@ - + - - - + + H helix @@ -1550,12 +1462,11 @@ - + - - - + + H helix @@ -1567,12 +1478,11 @@ - + - - - + + H helix @@ -1584,12 +1494,11 @@ - + - - - + + H helix @@ -1601,12 +1510,11 @@ - + - - - + + H helix @@ -1618,12 +1526,11 @@ - + - - - + + H helix @@ -1635,12 +1542,11 @@ - + - - - + + H helix @@ -1652,12 +1558,11 @@ - + - - - + + H helix @@ -1669,12 +1574,11 @@ - + - - - + + H helix @@ -1686,12 +1590,11 @@ - + - - - + + H helix @@ -1703,12 +1606,11 @@ - + - - - + + H helix @@ -1720,12 +1622,11 @@ - + - - - + + H helix @@ -1737,12 +1638,11 @@ - + - - - + + H helix @@ -1754,12 +1654,11 @@ - + - - - + + T loop @@ -1771,12 +1670,11 @@ - + - - - + + T loop @@ -1788,12 +1686,11 @@ - + - - - + + T loop @@ -1805,12 +1702,11 @@ - + - - - + + T loop @@ -1822,12 +1718,11 @@ - + - - - + + T loop @@ -1839,12 +1734,11 @@ - + - - - + + T loop @@ -1856,12 +1750,11 @@ - + - - - + + T loop @@ -1873,12 +1766,11 @@ - + - - - + + T loop @@ -1890,12 +1782,11 @@ - + - - - + + H helix @@ -1907,12 +1798,11 @@ - + - - - + + H helix @@ -1924,12 +1814,11 @@ - + - - - + + H helix @@ -1941,12 +1830,11 @@ - + - - - + + H helix @@ -1958,12 +1846,11 @@ - + - - - + + H helix @@ -1975,12 +1862,11 @@ - + - - - + + H helix @@ -1992,12 +1878,11 @@ - + - - - + + H helix @@ -2009,12 +1894,11 @@ - + - - - + + H helix @@ -2026,12 +1910,11 @@ - + - - - + + H helix @@ -2043,12 +1926,11 @@ - + - - - + + H helix @@ -2060,12 +1942,11 @@ - + - - - + + H helix @@ -2077,12 +1958,11 @@ - + - - - + + H helix @@ -2093,14 +1973,13 @@ + - + - - - - + + H helix @@ -2111,14 +1990,13 @@ + - + - - - - + + T loop @@ -2129,14 +2007,13 @@ + - + - - - - + + T loop @@ -2147,14 +2024,13 @@ + - + - - - - + + E strand @@ -2165,14 +2041,13 @@ + - + - - - - + + E strand @@ -2183,14 +2058,13 @@ + - + - - - - + + E strand @@ -2201,14 +2075,13 @@ + - + - - - - + + E strand @@ -2219,14 +2092,13 @@ + - + - - - - + + T loop @@ -2237,14 +2109,13 @@ + - + - - - - + + T loop @@ -2255,14 +2126,13 @@ + - + - - - - + + T loop @@ -2273,14 +2143,13 @@ + - + - - - - + + T loop @@ -2291,14 +2160,13 @@ + - + - - - - + + T loop @@ -2309,14 +2177,13 @@ + - + - - - - + + H helix @@ -2327,14 +2194,13 @@ + - + - - - - + + H helix @@ -2345,14 +2211,13 @@ + - + - - - - + + H helix @@ -2363,14 +2228,13 @@ + - + - - - - + + H helix @@ -2381,14 +2245,13 @@ + - + - - - - + + H helix @@ -2399,14 +2262,13 @@ + - + - - - - + + H helix @@ -2417,14 +2279,13 @@ + - + - - - - + + H helix @@ -2435,14 +2296,13 @@ + - + - - - - + + H helix @@ -2453,14 +2313,13 @@ + - + - - - - + + H helix @@ -2471,14 +2330,13 @@ + - + - - - - + + H helix @@ -2489,14 +2347,13 @@ + - + - - - - + + T loop @@ -2508,12 +2365,11 @@ - + - - - + + T loop @@ -2525,12 +2381,11 @@ - + - - - + + E strand @@ -2542,12 +2397,11 @@ - + - - - + + E strand @@ -2559,12 +2413,11 @@ - + - - - + + E strand @@ -2576,12 +2429,11 @@ - + - - - + + E strand @@ -2593,12 +2445,11 @@ - + - - - + + T loop @@ -2610,12 +2461,11 @@ - + - - - + + T loop @@ -2627,12 +2477,11 @@ - + - - - + + T loop @@ -2644,12 +2493,11 @@ - + - - - + + T loop @@ -2661,12 +2509,11 @@ - + - - - + + T loop @@ -2678,12 +2525,11 @@ - + - - - + + T loop @@ -2695,12 +2541,11 @@ - + - - - + + T loop @@ -2712,12 +2557,11 @@ - + - - - + + T loop @@ -2729,12 +2573,11 @@ - + - - - + + T loop @@ -2746,12 +2589,11 @@ - + - - - + + T loop @@ -2763,12 +2605,11 @@ - + - - - + + T loop @@ -2780,12 +2621,11 @@ - + - - - + + T loop @@ -2797,12 +2637,11 @@ - + - - - + + T loop @@ -2814,12 +2653,11 @@ - + - - - + + T loop @@ -2831,12 +2669,11 @@ - + - - - + + T loop @@ -2848,13 +2685,12 @@ - + + - - - + T loop @@ -2866,13 +2702,12 @@ - + + - - - + H helix @@ -2884,13 +2719,12 @@ - + + - - - + H helix @@ -2902,13 +2736,12 @@ - + + - - - + H helix @@ -2920,13 +2753,12 @@ - + + - - - + H helix @@ -2938,13 +2770,12 @@ - + + - - - + H helix @@ -2956,13 +2787,12 @@ - + + - - - + H helix @@ -2974,13 +2804,12 @@ - + + - - - + H helix @@ -2992,13 +2821,12 @@ - + + - - - + T loop @@ -3010,13 +2838,12 @@ - + + - - - + T loop @@ -3028,13 +2855,12 @@ - + + - - - + T loop @@ -3046,13 +2872,12 @@ - + + - - - + T loop @@ -3064,12 +2889,11 @@ - + - - - + + T loop @@ -3081,12 +2905,11 @@ - + - - - + + T loop @@ -3098,12 +2921,11 @@ - + - - - + + T loop @@ -3115,12 +2937,11 @@ - + - - - + + H helix @@ -3132,12 +2953,11 @@ - + - - - + + H helix @@ -3149,12 +2969,11 @@ - + - - - + + H helix @@ -3166,12 +2985,11 @@ - + - - - + + H helix @@ -3183,12 +3001,11 @@ - + - - - + + H helix @@ -3200,12 +3017,11 @@ - + - - - + + H helix @@ -3217,12 +3033,11 @@ - + - - - + + H helix @@ -3235,12 +3050,11 @@ - + - - - + + H helix @@ -3253,12 +3067,11 @@ - + - - - + + H helix @@ -3271,12 +3084,11 @@ - + - - - + + H helix @@ -3289,12 +3101,11 @@ - + - - - + + H helix @@ -3307,12 +3118,11 @@ - + - - - + + H helix @@ -3325,12 +3135,11 @@ - + - - - + + H helix @@ -3343,12 +3152,11 @@ - + - - - + + H helix @@ -3361,12 +3169,11 @@ - + - - - + + H helix @@ -3379,12 +3186,11 @@ - + - - - + + H helix @@ -3397,12 +3203,11 @@ - + - - - + + T loop @@ -3415,12 +3220,11 @@ - + - - - + + T loop @@ -3433,12 +3237,11 @@ - + - - - + + H helix @@ -3451,12 +3254,11 @@ - + - - - + + H helix @@ -3469,12 +3271,11 @@ - + - - - + + H helix @@ -3487,12 +3288,11 @@ - + - - - + + H helix @@ -3505,12 +3305,11 @@ - + - - - + + H helix @@ -3523,12 +3322,11 @@ - + - - - + + H helix @@ -3541,12 +3339,11 @@ - + - - - + + H helix @@ -3559,12 +3356,11 @@ - + - - - + + H helix @@ -3577,12 +3373,11 @@ - + - - - + + H helix @@ -3594,12 +3389,11 @@ - + - - - + + H helix @@ -3611,12 +3405,11 @@ - + - - - + + H helix @@ -3628,12 +3421,11 @@ - + - - - + + H helix @@ -3645,12 +3437,11 @@ - + - - - + + H helix @@ -3662,12 +3453,11 @@ - + - - - + + H helix @@ -3679,12 +3469,11 @@ - + - - - + + T loop @@ -3696,12 +3485,11 @@ - + - - - + + T loop @@ -3713,13 +3501,12 @@ - + - - - - T + + + T loop @@ -3730,12 +3517,11 @@ - + - - - + + T loop @@ -3747,12 +3533,11 @@ - + - - - + + T loop @@ -3764,12 +3549,11 @@ - + - - - + + E strand @@ -3781,12 +3565,11 @@ - + - - - + + E strand @@ -3798,12 +3581,11 @@ - + - - - + + E strand @@ -3815,12 +3597,11 @@ - + - - - + + E strand @@ -3832,12 +3613,11 @@ - + - - - + + T loop @@ -3849,12 +3629,11 @@ - + - - - + + T loop @@ -3866,12 +3645,11 @@ - + - - - + + E strand @@ -3883,12 +3661,11 @@ - + - - - + + E strand @@ -3900,12 +3677,11 @@ - + - - - + + E strand @@ -3917,13 +3693,12 @@ - + - - + + - E strand @@ -3935,13 +3710,12 @@ - + - - + + - T loop @@ -3953,13 +3727,12 @@ - + - - + + - H helix @@ -3971,13 +3744,12 @@ - + - - + + - H helix @@ -3989,13 +3761,12 @@ - + - - + + - H helix @@ -4007,13 +3778,12 @@ - + - - + + - H helix @@ -4025,13 +3795,12 @@ - + - - + + - H helix @@ -4043,13 +3812,12 @@ - + - - + + - H helix @@ -4061,13 +3829,12 @@ - + - - + + - H helix @@ -4079,13 +3846,12 @@ - + - - + + - H helix @@ -4097,13 +3863,12 @@ - + - - + + - H helix @@ -4115,13 +3880,12 @@ - + - - + + - H helix @@ -4133,13 +3897,12 @@ - + - - + + - H helix @@ -4151,13 +3914,12 @@ - + - - + + - H helix @@ -4169,13 +3931,12 @@ - + - - + + - H helix @@ -4187,13 +3948,12 @@ - + - - + + - H helix @@ -4205,13 +3965,12 @@ - + - - + + - T loop @@ -4223,13 +3982,12 @@ - + - - + + - T loop @@ -4241,13 +3999,12 @@ - + - - + + - T loop @@ -4259,12 +4016,11 @@ - + - - - + + T loop @@ -4276,12 +4032,11 @@ - + - - - + + T loop @@ -4293,12 +4048,11 @@ - + - - - + + T loop @@ -4310,12 +4064,11 @@ - + - - - + + T loop @@ -4327,12 +4080,11 @@ - + - - - + + E strand @@ -4344,12 +4096,11 @@ - + - - - + + E strand @@ -4361,12 +4112,11 @@ - + - - - + + T loop @@ -4378,12 +4128,11 @@ - + - - - + + H helix @@ -4395,12 +4144,11 @@ - + - - - + + H helix @@ -4412,12 +4160,11 @@ - + - - - + + H helix @@ -4429,12 +4176,11 @@ - + - - - + + H helix @@ -4446,12 +4192,11 @@ - + - - - + + H helix @@ -4462,14 +4207,13 @@ + - + - - - - + + H helix @@ -4480,14 +4224,13 @@ + - + - - - - + + T loop @@ -4498,14 +4241,13 @@ + - + - - - - + + T loop @@ -4516,14 +4258,13 @@ + - + - - - - + + T loop @@ -4534,14 +4275,13 @@ + - + - - - - + + T loop @@ -4552,14 +4292,13 @@ + - + - - - - + + T loop @@ -4570,14 +4309,13 @@ + - + - - - - + + T loop @@ -4588,14 +4326,13 @@ + - + - - - - + + T loop @@ -4606,14 +4343,13 @@ + - + - - - - + + T loop @@ -4624,14 +4360,13 @@ + - + - - - - + + T loop @@ -4642,14 +4377,13 @@ + - + - - - - + + T loop @@ -4660,14 +4394,13 @@ + - + - - - - + + T loop @@ -4678,14 +4411,13 @@ + - + - - - - + + T loop @@ -4696,14 +4428,13 @@ + - + - - - - + + T loop @@ -4714,14 +4445,13 @@ + - + - - - - + + E strand @@ -4732,14 +4462,13 @@ + - + - - - - + + E strand @@ -4750,14 +4479,13 @@ + - + - - - - + + E strand @@ -4768,14 +4496,13 @@ + - + - - - - + + T loop @@ -4786,14 +4513,13 @@ + - + - - - - + + H helix @@ -4804,14 +4530,13 @@ + - + - - - - + + H helix @@ -4823,12 +4548,11 @@ - + - - - + + H helix @@ -4840,12 +4564,11 @@ - + - - - + + H helix @@ -4857,12 +4580,11 @@ - + - - - + + H helix @@ -4874,12 +4596,11 @@ - + - - - + + H helix @@ -4891,12 +4612,11 @@ - + - - - + + H helix @@ -4908,12 +4628,11 @@ - + - - - + + H helix @@ -4925,12 +4644,11 @@ - + - - - + + H helix @@ -4942,12 +4660,11 @@ - + - - - + + H helix @@ -4959,12 +4676,11 @@ - + - - - + + H helix @@ -4976,12 +4692,11 @@ - + - - - + + H helix @@ -4993,12 +4708,11 @@ - + - - - + + H helix @@ -5010,12 +4724,11 @@ - + - - - + + H helix @@ -5027,12 +4740,11 @@ - + - - - + + H helix @@ -5044,12 +4756,11 @@ - + - - - + + T loop @@ -5061,12 +4772,11 @@ - + - - - + + T loop @@ -5078,13 +4788,12 @@ - + - + - - + T loop @@ -5096,13 +4805,12 @@ - + - + - - + T loop @@ -5114,13 +4822,12 @@ - + - + - - + T loop @@ -5132,13 +4839,12 @@ - + - + - - + E strand @@ -5150,13 +4856,12 @@ - + - + - - + E strand @@ -5168,13 +4873,12 @@ - + - + - - + E strand @@ -5186,13 +4890,12 @@ - + - + - - + E strand @@ -5204,13 +4907,12 @@ - + - + - - + E strand @@ -5222,13 +4924,12 @@ - + - + - - + T loop @@ -5240,13 +4941,12 @@ - + - + - - + T loop @@ -5258,13 +4958,12 @@ - + - + - - + T loop @@ -5276,13 +4975,12 @@ - + - + - - + T loop @@ -5294,13 +4992,12 @@ - + - + - - + E strand @@ -5312,13 +5009,12 @@ - + - + - - + E strand @@ -5330,13 +5026,12 @@ - + - + - - + E strand @@ -5348,13 +5043,12 @@ - + - + - - + E strand @@ -5366,13 +5060,12 @@ - + - + - - + E strand @@ -5384,13 +5077,12 @@ - + - + - - + H helix @@ -5402,13 +5094,12 @@ - + - + - - + H helix @@ -5420,12 +5111,11 @@ - + - - - + + H helix @@ -5437,12 +5127,11 @@ - + - - - + + H helix @@ -5454,11 +5143,11 @@ + - - - + + H helix @@ -5470,11 +5159,10 @@ + - - - + H helix @@ -5486,11 +5174,10 @@ + - - - + H helix @@ -5502,11 +5189,10 @@ + - - - + H helix @@ -5518,11 +5204,10 @@ + - - - + H helix @@ -5534,11 +5219,10 @@ + - - - + H helix @@ -5550,11 +5234,10 @@ + - - - + H helix @@ -5566,11 +5249,10 @@ + - - - + H helix @@ -5582,11 +5264,10 @@ + - - - + H helix @@ -5598,11 +5279,10 @@ + - - - + H helix @@ -5614,11 +5294,10 @@ + - - - + H helix @@ -5630,11 +5309,10 @@ + - - - + H helix @@ -5646,11 +5324,10 @@ + - - - + H helix @@ -5662,11 +5339,10 @@ + - - - + H helix @@ -5678,11 +5354,10 @@ + - - - + H helix @@ -5694,11 +5369,10 @@ + - - - + H helix @@ -5710,11 +5384,10 @@ + - - - + H helix @@ -5726,11 +5399,10 @@ + - - - + H helix @@ -5742,11 +5414,10 @@ + - - - + H helix @@ -5758,11 +5429,10 @@ + - - - + H helix @@ -5774,27 +5444,23 @@ + - - - + H helix - + - - - H helix @@ -5805,10 +5471,9 @@ + - - H helix @@ -5821,7 +5486,6 @@ - T loop @@ -5835,96 +5499,81 @@ PH4H_HUMAN - + - - - - + - + - + - + - - - - + - + - + - - + + - - + + - - - + + + + + + - - - - - + + - - - - - - - - - - + @@ -5939,12 +5588,11 @@ + - - - + T loop @@ -5955,13 +5603,12 @@ - + - - - + + T loop @@ -5972,13 +5619,12 @@ - + - - - + + T loop @@ -5989,13 +5635,12 @@ - + - - - + + T loop @@ -6006,13 +5651,12 @@ - + - - - + + T loop @@ -6023,13 +5667,12 @@ - + - - - + + T loop @@ -6040,13 +5683,12 @@ - + - - - + + T loop @@ -6057,13 +5699,12 @@ - + - - - + + H helix @@ -6074,13 +5715,12 @@ - + - - - + + H helix @@ -6091,13 +5731,12 @@ - + - - - + + H helix @@ -6108,13 +5747,12 @@ - + - - - + + H helix @@ -6125,13 +5763,12 @@ - + - - - + + H helix @@ -6142,13 +5779,12 @@ - + - - - + + H helix @@ -6159,13 +5795,12 @@ - + - - - + + Not_Observed @@ -6175,13 +5810,12 @@ - + - - - + + Not_Observed @@ -6191,13 +5825,12 @@ - + - - - + + Not_Observed @@ -6207,13 +5840,12 @@ - + - - - + + Not_Observed @@ -6223,13 +5855,12 @@ - + - - - + + Not_Observed @@ -6239,13 +5870,12 @@ - + - - - + + Not_Observed @@ -6255,13 +5885,12 @@ - + - - - + + Not_Observed @@ -6271,13 +5900,12 @@ - + - - - + + Not_Observed @@ -6287,13 +5915,12 @@ - + - - - + + Not_Observed @@ -6303,13 +5930,12 @@ - + - - - + + Not_Observed @@ -6319,13 +5945,12 @@ - + - - - + + Not_Observed @@ -6335,13 +5960,12 @@ - + - - - + + Not_Observed @@ -6351,13 +5975,12 @@ - + - - - + + Not_Observed @@ -6367,13 +5990,12 @@ - + - - - + + T loop @@ -6384,13 +6006,12 @@ - + - - - + + T loop @@ -6401,13 +6022,12 @@ - + - - - + + T loop @@ -6418,14 +6038,13 @@ - - + - - - + + + T loop @@ -6436,14 +6055,13 @@ - - + - - - + + + T loop @@ -6454,14 +6072,13 @@ - - + - - - + + + T loop @@ -6472,14 +6089,13 @@ - - + - - - + + + T loop @@ -6490,14 +6106,13 @@ - - + - - - + + + H helix @@ -6508,14 +6123,13 @@ - - + - - - + + + H helix @@ -6526,14 +6140,13 @@ - - + - - - + + + H helix @@ -6544,14 +6157,13 @@ - - + - - - + + + H helix @@ -6562,14 +6174,13 @@ - - + - - - + + + H helix @@ -6580,14 +6191,13 @@ - - + - - - + + + H helix @@ -6598,14 +6208,13 @@ - - + - - - + + + H helix @@ -6616,14 +6225,13 @@ - - + - - - + + + H helix @@ -6634,14 +6242,13 @@ - - + - - - + + + H helix @@ -6652,14 +6259,13 @@ - - + - - - + + + H helix @@ -6670,14 +6276,13 @@ - - + - - - + + + H helix @@ -6688,14 +6293,13 @@ - - + - - - + + + H helix @@ -6706,14 +6310,13 @@ - - + - - - + + + H helix @@ -6724,14 +6327,13 @@ - - + - - - + + + H helix @@ -6742,14 +6344,13 @@ - - + - - - + + + H helix @@ -6760,14 +6361,13 @@ - - + - - - + + + H helix @@ -6778,13 +6378,12 @@ - + - - - + + H helix @@ -6795,13 +6394,12 @@ - + - - - + + H helix @@ -6812,13 +6410,12 @@ - + - - - + + T loop @@ -6829,13 +6426,12 @@ - + - - - + + T loop @@ -6846,13 +6442,12 @@ - + - - - + + T loop @@ -6863,13 +6458,12 @@ - + - - - + + T loop @@ -6880,13 +6474,12 @@ - + - - - + + T loop @@ -6897,13 +6490,12 @@ - + - - - + + T loop @@ -6914,13 +6506,12 @@ - + - - - + + T loop @@ -6931,13 +6522,12 @@ - + - - - + + T loop @@ -6948,13 +6538,12 @@ - + - - - + + T loop @@ -6965,13 +6554,12 @@ - + - - - + + T loop @@ -6982,13 +6570,12 @@ - + - - - + + T loop @@ -6999,13 +6586,12 @@ - + - - - + + H helix @@ -7016,13 +6602,12 @@ - + - - - + + H helix @@ -7033,13 +6618,12 @@ - + - - - + + H helix @@ -7050,13 +6634,12 @@ - + - - - + + H helix @@ -7067,13 +6650,12 @@ - + - - - + + H helix @@ -7084,13 +6666,12 @@ - + - - - + + H helix @@ -7101,13 +6682,12 @@ - + - - - + + H helix @@ -7118,13 +6698,12 @@ - + - - - + + H helix @@ -7135,13 +6714,12 @@ - + - - - + + H helix @@ -7152,13 +6730,12 @@ - + - - - + + H helix @@ -7169,13 +6746,12 @@ - + - - - + + H helix @@ -7186,13 +6762,12 @@ - + - - - + + H helix @@ -7203,13 +6778,12 @@ - + - - - + + H helix @@ -7220,13 +6794,12 @@ - + - - - + + H helix @@ -7237,13 +6810,12 @@ - + - - - + + H helix @@ -7254,13 +6826,12 @@ - + - - - + + H helix @@ -7271,13 +6842,12 @@ - + - - - + + H helix @@ -7288,13 +6858,12 @@ - + - - - + + H helix @@ -7305,13 +6874,12 @@ - + - - - + + H helix @@ -7322,13 +6890,12 @@ - + - - - + + H helix @@ -7339,13 +6906,12 @@ - + - - - + + H helix @@ -7356,13 +6922,12 @@ - + - - - + + H helix @@ -7373,13 +6938,12 @@ - + - - - + + H helix @@ -7390,13 +6954,12 @@ - + - - - + + H helix @@ -7407,13 +6970,12 @@ - + - - - + + H helix @@ -7424,13 +6986,12 @@ - + - - - + + H helix @@ -7441,13 +7002,12 @@ - + - - - + + H helix @@ -7458,13 +7018,12 @@ - + - - - + + H helix @@ -7475,13 +7034,12 @@ - + - - - + + H helix @@ -7492,13 +7050,12 @@ - + - - - + + H helix @@ -7509,13 +7066,12 @@ - + - - - + + H helix @@ -7526,13 +7082,12 @@ - + - - - + + H helix @@ -7543,13 +7098,12 @@ - + - - - + + H helix @@ -7560,13 +7114,12 @@ - + - - - + + H helix @@ -7577,13 +7130,12 @@ - + - - - + + H helix @@ -7594,13 +7146,12 @@ - + - - - + + H helix @@ -7611,13 +7162,12 @@ - + - - - + + H helix @@ -7628,13 +7178,12 @@ - + - - - + + H helix @@ -7645,13 +7194,12 @@ - + - - - + + T loop @@ -7662,13 +7210,12 @@ - + - - - + + T loop @@ -7679,13 +7226,12 @@ - + - - - + + T loop @@ -7696,13 +7242,12 @@ - + - - - + + T loop @@ -7713,13 +7258,12 @@ - + - - - + + T loop @@ -7730,13 +7274,12 @@ - + - - - + + T loop @@ -7747,13 +7290,12 @@ - + - - - + + T loop @@ -7764,13 +7306,12 @@ - + - - - + + T loop @@ -7781,13 +7322,12 @@ - + - - - + + H helix @@ -7798,13 +7338,12 @@ - + - - - + + H helix @@ -7815,13 +7354,12 @@ - + - - - + + H helix @@ -7832,13 +7370,12 @@ - + - - - + + H helix @@ -7849,13 +7386,12 @@ - + - - - + + H helix @@ -7866,13 +7402,12 @@ - + - - - + + H helix @@ -7883,13 +7418,12 @@ - + - - - + + H helix @@ -7900,13 +7434,12 @@ - + - - - + + H helix @@ -7917,13 +7450,12 @@ - + - - - + + H helix @@ -7934,13 +7466,12 @@ - + - - - + + H helix @@ -7951,13 +7482,12 @@ - + - - - + + H helix @@ -7968,13 +7498,12 @@ - + - - - + + H helix @@ -7985,14 +7514,13 @@ - + - - - - + + + H helix @@ -8003,14 +7531,13 @@ - + - - - - + + + T loop @@ -8021,14 +7548,13 @@ - + - - - - + + + T loop @@ -8039,14 +7565,13 @@ - + - - - - + + + E strand @@ -8057,14 +7582,13 @@ - + - - - - + + + E strand @@ -8075,14 +7599,13 @@ - + - - - - + + + E strand @@ -8093,14 +7616,13 @@ - + - - - - + + + E strand @@ -8111,14 +7633,13 @@ - + - - - - + + + T loop @@ -8129,14 +7650,13 @@ - + - - - - + + + T loop @@ -8147,14 +7667,13 @@ - + - - - - + + + T loop @@ -8165,14 +7684,13 @@ - + - - - - + + + T loop @@ -8183,14 +7701,13 @@ - + - - - - + + + T loop @@ -8201,14 +7718,13 @@ - + - - - - + + + H helix @@ -8219,14 +7735,13 @@ - + - - - - + + + H helix @@ -8237,14 +7752,13 @@ - + - - - - + + + H helix @@ -8255,14 +7769,13 @@ - + - - - - + + + H helix @@ -8273,14 +7786,13 @@ - + - - - - + + + H helix @@ -8291,14 +7803,13 @@ - + - - - - + + + H helix @@ -8309,14 +7820,13 @@ - + - - - - + + + H helix @@ -8327,14 +7837,13 @@ - + - - - - + + + H helix @@ -8345,14 +7854,13 @@ - + - - - - + + + H helix @@ -8363,14 +7871,13 @@ - + - - - - + + + H helix @@ -8381,14 +7888,13 @@ - + - - - - + + + T loop @@ -8399,13 +7905,12 @@ - + - - - + + T loop @@ -8416,13 +7921,12 @@ - + - - - + + E strand @@ -8433,13 +7937,12 @@ - + - - - + + E strand @@ -8450,13 +7953,12 @@ - + - - - + + E strand @@ -8467,13 +7969,12 @@ - + - - - + + E strand @@ -8484,13 +7985,12 @@ - + - - - + + T loop @@ -8501,13 +8001,12 @@ - + - - - + + T loop @@ -8518,13 +8017,12 @@ - + - - - + + T loop @@ -8535,13 +8033,12 @@ - + - - - + + T loop @@ -8552,13 +8049,12 @@ - + - - - + + T loop @@ -8569,13 +8065,12 @@ - + - - - + + T loop @@ -8586,13 +8081,12 @@ - + - - - + + T loop @@ -8603,13 +8097,12 @@ - + - - - + + T loop @@ -8620,13 +8113,12 @@ - + - - - + + T loop @@ -8637,13 +8129,12 @@ - + - - - + + T loop @@ -8654,13 +8145,12 @@ - + - - - + + T loop @@ -8671,13 +8161,12 @@ - + - - - + + T loop @@ -8688,13 +8177,12 @@ - + - - - + + T loop @@ -8705,13 +8193,12 @@ - + - - - + + T loop @@ -8722,13 +8209,12 @@ - + - - - + + T loop @@ -8739,14 +8225,13 @@ - - + - - - + + + T loop @@ -8757,14 +8242,13 @@ - - + - - - + + + H helix @@ -8775,14 +8259,13 @@ - - + - - - + + + H helix @@ -8793,14 +8276,13 @@ - - + - - - + + + H helix @@ -8811,14 +8293,13 @@ - - + - - - + + + H helix @@ -8829,14 +8310,13 @@ - - + - - - + + + H helix @@ -8847,14 +8327,13 @@ - - + - - - + + + H helix @@ -8865,14 +8344,13 @@ - - + - - - + + + H helix @@ -8883,14 +8361,13 @@ - - + - - - + + + T loop @@ -8901,14 +8378,13 @@ - - + - - - + + + T loop @@ -8919,14 +8395,13 @@ - - + - - - + + + T loop @@ -8937,14 +8412,13 @@ - - + - - - + + + T loop @@ -8955,13 +8429,12 @@ - + - - - + + T loop @@ -8972,13 +8445,12 @@ - + - - - + + T loop @@ -8989,13 +8461,12 @@ - + - - - + + T loop @@ -9006,13 +8477,12 @@ - + - - - + + H helix @@ -9023,13 +8493,12 @@ - + - - - + + H helix @@ -9040,13 +8509,12 @@ - + - - - + + H helix @@ -9057,13 +8525,12 @@ - + - - - + + H helix @@ -9074,13 +8541,12 @@ - + - - - + + H helix @@ -9091,13 +8557,12 @@ - + - - - + + H helix @@ -9108,14 +8573,13 @@ - + - - - - + + + H helix @@ -9126,14 +8590,13 @@ - + - - - - + + + H helix @@ -9144,14 +8607,13 @@ - + - - - - + + + H helix @@ -9162,14 +8624,13 @@ - + - - - - + + + H helix @@ -9180,14 +8641,13 @@ - + - - - - + + + H helix @@ -9198,14 +8658,13 @@ - + - - - - + + + H helix @@ -9216,14 +8675,13 @@ - + - - - - + + + H helix @@ -9234,14 +8692,13 @@ - + - - - - + + + H helix @@ -9252,14 +8709,13 @@ - + - - - - + + + H helix @@ -9270,14 +8726,13 @@ - + - - - - + + + H helix @@ -9288,14 +8743,13 @@ - + - - - - + + + T loop @@ -9306,14 +8760,13 @@ - + - - - - + + + T loop @@ -9324,14 +8777,13 @@ - + - - - - + + + H helix @@ -9342,14 +8794,13 @@ - + - - - - + + + H helix @@ -9360,14 +8811,13 @@ - + - - - - + + + H helix @@ -9378,14 +8828,13 @@ - + - - - - + + + H helix @@ -9396,14 +8845,13 @@ - + - - - - + + + H helix @@ -9414,14 +8862,13 @@ - + - - - - + + + H helix @@ -9432,14 +8879,13 @@ - + - - - - + + + H helix @@ -9450,14 +8896,13 @@ - + - - - - + + + H helix @@ -9468,13 +8913,12 @@ - + - - - + + H helix @@ -9485,13 +8929,12 @@ - + - - - + + H helix @@ -9502,13 +8945,12 @@ - + - - - + + H helix @@ -9519,13 +8961,12 @@ - + - - - + + H helix @@ -9536,13 +8977,12 @@ - + - - - + + H helix @@ -9553,13 +8993,12 @@ - + - - - + + H helix @@ -9570,13 +9009,12 @@ - + - - - + + T loop @@ -9587,13 +9025,12 @@ - + - - - + + T loop @@ -9604,13 +9041,12 @@ - + - - - + + T loop @@ -9621,13 +9057,12 @@ - + - - - + + T loop @@ -9638,13 +9073,12 @@ - + - - - + + T loop @@ -9655,13 +9089,12 @@ - + - - - + + E strand @@ -9672,13 +9105,12 @@ - + - - - + + E strand @@ -9689,13 +9121,12 @@ - + - - - + + E strand @@ -9706,13 +9137,12 @@ - + - - - + + E strand @@ -9723,13 +9153,12 @@ - + - - - + + T loop @@ -9740,13 +9169,12 @@ - + - - - + + T loop @@ -9757,13 +9185,12 @@ - + - - - + + E strand @@ -9774,13 +9201,12 @@ - + - - - + + E strand @@ -9791,13 +9217,12 @@ - + - - - + + E strand @@ -9808,14 +9233,13 @@ - + - - - - + + + E strand @@ -9826,14 +9250,13 @@ - + - - - - + + + T loop @@ -9844,14 +9267,13 @@ - + - - - - + + + H helix @@ -9862,14 +9284,13 @@ - + - - - - + + + H helix @@ -9880,14 +9301,13 @@ - + - - - - + + + H helix @@ -9898,14 +9318,13 @@ - + - - - - + + + H helix @@ -9916,14 +9335,13 @@ - + - - - - + + + H helix @@ -9934,14 +9352,13 @@ - + - - - - + + + H helix @@ -9952,14 +9369,13 @@ - + - - - - + + + H helix @@ -9970,14 +9386,13 @@ - + - - - - + + + H helix @@ -9988,14 +9403,13 @@ - + - - - - + + + H helix @@ -10006,14 +9420,13 @@ - + - - - - + + + H helix @@ -10024,14 +9437,13 @@ - + - - - - + + + H helix @@ -10042,14 +9454,13 @@ - + - - - - + + + H helix @@ -10060,14 +9471,13 @@ - + - - - - + + + H helix @@ -10078,14 +9488,13 @@ - + - - - - + + + H helix @@ -10096,14 +9505,13 @@ - + - - - - + + + T loop @@ -10114,14 +9522,13 @@ - + - - - - + + + T loop @@ -10132,14 +9539,13 @@ - + - - - - + + + T loop @@ -10150,13 +9556,12 @@ - + - - - + + T loop @@ -10167,13 +9572,12 @@ - + - - - + + T loop @@ -10184,13 +9588,12 @@ - + - - - + + T loop @@ -10201,13 +9604,12 @@ - + - - - + + T loop @@ -10218,13 +9620,12 @@ - + - - - + + E strand @@ -10235,13 +9636,12 @@ - + - - - + + E strand @@ -10252,13 +9652,12 @@ - + - - - + + T loop @@ -10269,13 +9668,12 @@ - + - - - + + H helix @@ -10286,13 +9684,12 @@ - + - - - + + H helix @@ -10303,13 +9700,12 @@ - + - - - + + H helix @@ -10320,13 +9716,12 @@ - + - - - + + H helix @@ -10337,13 +9732,12 @@ - + - - - + + H helix @@ -10354,14 +9748,13 @@ - + - - - - + + + H helix @@ -10372,14 +9765,13 @@ - + - - - - + + + T loop @@ -10390,14 +9782,13 @@ - + - - - - + + + T loop @@ -10408,14 +9799,13 @@ - + - - - - + + + T loop @@ -10426,14 +9816,13 @@ - + - - - - + + + T loop @@ -10444,14 +9833,13 @@ - + - - - - + + + T loop @@ -10462,14 +9850,13 @@ - + - - - - + + + T loop @@ -10480,14 +9867,13 @@ - + - - - - + + + T loop @@ -10498,14 +9884,13 @@ - + - - - - + + + T loop @@ -10516,14 +9901,13 @@ - + - - - - + + + T loop @@ -10534,14 +9918,13 @@ - + - - - - + + + T loop @@ -10552,14 +9935,13 @@ - + - - - - + + + T loop @@ -10570,14 +9952,13 @@ - + - - - - + + + T loop @@ -10588,14 +9969,13 @@ - + - - - - + + + T loop @@ -10606,14 +9986,13 @@ - + - - - - + + + E strand @@ -10624,14 +10003,13 @@ - + - - - - + + + E strand @@ -10642,14 +10020,13 @@ - + - - - - + + + E strand @@ -10660,14 +10037,13 @@ - + - - - - + + + T loop @@ -10678,14 +10054,13 @@ - + - - - - + + + H helix @@ -10696,14 +10071,13 @@ - + - - - - + + + H helix @@ -10714,13 +10088,12 @@ - + - - - + + H helix @@ -10731,13 +10104,12 @@ - + - - - + + H helix @@ -10748,13 +10120,12 @@ - + - - - + + H helix @@ -10765,13 +10136,12 @@ - + - - - + + H helix @@ -10782,13 +10152,12 @@ - + - - - + + H helix @@ -10799,13 +10168,12 @@ - + - - - + + H helix @@ -10816,13 +10184,12 @@ - + - - - + + H helix @@ -10833,13 +10200,12 @@ - + - - - + + H helix @@ -10850,13 +10216,12 @@ - + - - - + + H helix @@ -10867,13 +10232,12 @@ - + - - - + + H helix @@ -10884,13 +10248,12 @@ - + - - - + + H helix @@ -10901,13 +10264,12 @@ - + - - - + + H helix @@ -10918,13 +10280,12 @@ - + - - - + + H helix @@ -10935,13 +10296,12 @@ - + - - - + + H helix @@ -10952,13 +10312,12 @@ - + - - - + + T loop @@ -10969,14 +10328,13 @@ - + - - - + + T loop @@ -10987,14 +10345,13 @@ - + - - - + + T loop @@ -11005,14 +10362,13 @@ - + - - - + + T loop @@ -11023,14 +10379,13 @@ - + - - - + + E strand @@ -11041,14 +10396,13 @@ - + - - - + + E strand @@ -11059,14 +10413,13 @@ - + - - - + + E strand @@ -11077,14 +10430,13 @@ - + - - - + + E strand @@ -11095,14 +10447,13 @@ - + - - - + + E strand @@ -11113,14 +10464,13 @@ - + - - - + + T loop @@ -11131,14 +10481,13 @@ - + - - - + + T loop @@ -11149,14 +10498,13 @@ - + - - - + + T loop @@ -11167,14 +10515,13 @@ - + - - - + + T loop @@ -11185,14 +10532,13 @@ - + - - - + + E strand @@ -11203,14 +10549,13 @@ - + - - - + + E strand @@ -11221,14 +10566,13 @@ - + - - - + + E strand @@ -11239,14 +10583,13 @@ - + - - - + + E strand @@ -11257,14 +10600,13 @@ - + - - - + + E strand @@ -11275,14 +10617,13 @@ - + - - - + + T loop @@ -11293,14 +10634,13 @@ - + - - - + + H helix @@ -11311,13 +10651,12 @@ - + - - - + + H helix @@ -11328,13 +10667,12 @@ - + - - - + + H helix @@ -11345,12 +10683,12 @@ - + - - + + H helix @@ -11361,12 +10699,11 @@ - + - - + H helix @@ -11377,12 +10714,11 @@ - + - - + H helix @@ -11393,12 +10729,11 @@ - + - - + H helix @@ -11409,12 +10744,11 @@ - + - - + H helix @@ -11425,12 +10759,11 @@ - + - - + H helix @@ -11441,12 +10774,11 @@ - + - - + H helix @@ -11457,12 +10789,11 @@ - + - - + H helix @@ -11473,12 +10804,11 @@ - + - - + H helix @@ -11489,12 +10819,11 @@ - + - - + H helix @@ -11505,12 +10834,11 @@ - + - - + H helix @@ -11521,12 +10849,11 @@ - + - - + H helix @@ -11537,12 +10864,11 @@ - + - - + H helix @@ -11553,12 +10879,11 @@ - + - - + H helix @@ -11569,12 +10894,11 @@ - + - - + H helix @@ -11585,12 +10909,11 @@ - + - - + H helix @@ -11601,12 +10924,11 @@ - + - - + H helix @@ -11617,12 +10939,11 @@ - + - - + H helix @@ -11633,12 +10954,11 @@ - + - - + H helix @@ -11649,12 +10969,11 @@ - + - - + H helix @@ -11665,28 +10984,24 @@ - + - - + H helix - - + - - H helix @@ -11696,11 +11011,10 @@ + - - T loop @@ -11710,10 +11024,9 @@ + - - T loop @@ -11727,51 +11040,48 @@ PH4H_HUMAN - + - + - + - + - + - + - + - + - + - - + + - - + + - - - - + - + @@ -11780,35 +11090,23 @@ - + - - - - - - - - - - - - - - + + @@ -11816,7 +11114,7 @@ - + diff --git a/tests/SIFTS/2pm7.xml b/tests/testdata/sifts/2pm7.xml similarity index 100% rename from tests/SIFTS/2pm7.xml rename to tests/testdata/sifts/2pm7.xml diff --git a/tests/SIFTS/2w4o.xml b/tests/testdata/sifts/2w4o.xml similarity index 100% rename from tests/SIFTS/2w4o.xml rename to tests/testdata/sifts/2w4o.xml diff --git a/tests/SIFTS/3ehk.xml b/tests/testdata/sifts/3ehk.xml similarity index 100% rename from tests/SIFTS/3ehk.xml rename to tests/testdata/sifts/3ehk.xml diff --git a/tests/SIFTS/3fqd.xml b/tests/testdata/sifts/3fqd.xml similarity index 100% rename from tests/SIFTS/3fqd.xml rename to tests/testdata/sifts/3fqd.xml diff --git a/tests/SIFTS/3mn5.xml b/tests/testdata/sifts/3mn5.xml similarity index 100% rename from tests/SIFTS/3mn5.xml rename to tests/testdata/sifts/3mn5.xml diff --git a/tests/SIFTS/4abo.xml b/tests/testdata/sifts/4abo.xml similarity index 100% rename from tests/SIFTS/4abo.xml rename to tests/testdata/sifts/4abo.xml diff --git a/tests/SIFTS/4ibw.xml b/tests/testdata/sifts/4ibw.xml similarity index 100% rename from tests/SIFTS/4ibw.xml rename to tests/testdata/sifts/4ibw.xml diff --git a/tests/SIFTS/4v9d.xml b/tests/testdata/sifts/4v9d.xml similarity index 100% rename from tests/SIFTS/4v9d.xml rename to tests/testdata/sifts/4v9d.xml diff --git a/tests/SIFTS/4why.xml b/tests/testdata/sifts/4why.xml similarity index 100% rename from tests/SIFTS/4why.xml rename to tests/testdata/sifts/4why.xml diff --git a/tests/VALIDATION/2pah_validation.xml b/tests/testdata/validation/2pah_validation.xml similarity index 100% rename from tests/VALIDATION/2pah_validation.xml rename to tests/testdata/validation/2pah_validation.xml diff --git a/tests/VARIATION/ensembl_variation_rs557625940.csv b/tests/testdata/variation/ensembl_variation_rs557625940.csv similarity index 100% rename from tests/VARIATION/ensembl_variation_rs557625940.csv rename to tests/testdata/variation/ensembl_variation_rs557625940.csv diff --git a/tests/VARIATION/icgc_ENST00000308677.json b/tests/testdata/variation/icgc_ENST00000308677.json similarity index 100% rename from tests/VARIATION/icgc_ENST00000308677.json rename to tests/testdata/variation/icgc_ENST00000308677.json diff --git a/tests/VARIATION/somatic_variation_ENSP00000326864.csv b/tests/testdata/variation/somatic_variation_ENSP00000326864.csv similarity index 100% rename from tests/VARIATION/somatic_variation_ENSP00000326864.csv rename to tests/testdata/variation/somatic_variation_ENSP00000326864.csv diff --git a/tests/VARIATION/transcript_variation_ENSP00000326864.csv b/tests/testdata/variation/transcript_variation_ENSP00000326864.csv similarity index 100% rename from tests/VARIATION/transcript_variation_ENSP00000326864.csv rename to tests/testdata/variation/transcript_variation_ENSP00000326864.csv diff --git a/tests/VARIATION/uniprot_variants_O96013.csv b/tests/testdata/variation/uniprot_variants_O96013.csv similarity index 100% rename from tests/VARIATION/uniprot_variants_O96013.csv rename to tests/testdata/variation/uniprot_variants_O96013.csv