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1JRH.pdb
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HEADER COMPLEX (ANTIBODY/ANTIGEN) 23-SEP-97 1JRH
TITLE COMPLEX (ANTIBODY/ANTIGEN)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIBODY A6;
COMPND 3 CHAIN: L;
COMPND 4 FRAGMENT: FAB FRAGMENT;PEPSIN DIGESTION OF INTACT ANTIBODY;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ANTIBODY A6;
COMPND 7 CHAIN: H;
COMPND 8 FRAGMENT: FAB FRAGMENT;PEPSIN DIGESTION OF INTACT ANTIBODY;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: INTERFERON-GAMMA RECEPTOR ALPHA CHAIN;
COMPND 11 CHAIN: I;
COMPND 12 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: CDNA;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 OTHER_DETAILS: ESCHERICHIA COLI HIOREDOXIN GENE FUSION
SOURCE 17 EXPRESSION SYSTEM, BOVINE ENTEROKINASE CLEAVAGE
KEYWDS CYTOKINE RECEPTOR, COMPLEX (ANTIBODY/ANTIGEN),
KEYWDS 2 TRANSMEMBRANE, GLYCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR F.K.WINKLER,S.SOGABE
REVDAT 2 24-FEB-09 1JRH 1 VERSN
REVDAT 1 25-MAR-98 1JRH 0
JRNL AUTH S.SOGABE,F.STUART,C.HENKE,A.BRIDGES,G.WILLIAMS,
JRNL AUTH 2 A.BIRCH,F.K.WINKLER,J.A.ROBINSON
JRNL TITL NEUTRALIZING EPITOPES ON THE EXTRACELLULAR
JRNL TITL 2 INTERFERON GAMMA RECEPTOR (IFNGAMMAR) ALPHA-CHAIN
JRNL TITL 3 CHARACTERIZED BY HOMOLOG SCANNING MUTAGENESIS AND
JRNL TITL 4 X-RAY CRYSTAL STRUCTURE OF THE A6
JRNL TITL 5 FAB-IFNGAMMAR1-108 COMPLEX.
JRNL REF J.MOL.BIOL. V. 273 882 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9367779
JRNL DOI 10.1006/JMBI.1997.1336
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.WILLIAMS,N.RUEGG,A.BIRCH,C.WEBER,K.HOFSTADTER,
REMARK 1 AUTH 2 J.A.ROBINSON,M.AGUET,G.GAROTTA,D.SCHLATTER,W.HUBER
REMARK 1 TITL DISSECTION OF THE EXTRACELLULAR HUMAN INTERFERON
REMARK 1 TITL 2 GAMMA RECEPTOR ALPHA-CHAIN INTO TWO
REMARK 1 TITL 3 IMMUNOGLOBULIN-LIKE DOMAINS. PRODUCTION IN AN
REMARK 1 TITL 4 ESCHERICHIA COLI THIOREDOXIN GENE FUSION
REMARK 1 TITL 5 EXPRESSION SYSTEM AND RECOGNITION BY NEUTRALIZING
REMARK 1 TITL 6 ANTIBODIES
REMARK 1 REF BIOCHEMISTRY V. 34 1787 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.BRIDGES,A.BIRCH,G.WILLIAMS,M.AGUET,D.SCHLATTER,
REMARK 1 AUTH 2 W.HUBER,G.GAROTTA,J.A.ROBINSON
REMARK 1 TITL VARIABLE REGION CDNA SEQUENCES AND
REMARK 1 TITL 2 CHARACTERIZATION OF MURINE ANTI-HUMAN INTERFERON
REMARK 1 TITL 3 GAMMA RECEPTOR MONOCLONAL ANTIBODIES THAT INHIBIT
REMARK 1 TITL 4 RECEPTOR BINDING BY INTERFERON GAMMA
REMARK 1 REF MOL.IMMUNOL. V. 32 1329 1995
REMARK 1 REFN ISSN 0161-5890
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 19997
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.314
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 954
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.90
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1793
REMARK 3 BIN R VALUE (WORKING SET) : 0.3220
REMARK 3 BIN FREE R VALUE : 0.3990
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 99
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 : 3454
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 30
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 58.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.10
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) : 0.40
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) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.85
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) : 2.000 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.000 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.500 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 20.000; 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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ATOMS WITH B-FACTORS > 80 A**2 MUST
REMARK 3 BE CONSIDERED DISORDERED.
REMARK 4
REMARK 4 1JRH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : FEB-96
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ENRAF-NONIUS FR591
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MARXDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19997
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 (%) : 98.8
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.28800
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRIES 1BBJ, 1BBC, AND 2HFL
REMARK 200
REMARK 200 REMARK: FOR FV_HEAVY AND FV_LIGHT, 1BBJ AND 1BBC, RESPECTIVELY.
REMARK 200 FOR FC, 2HFL. THESE ARE COMBINED AND OPTIMIZED. <I/SIGMA(I)&
REMARK 200 GT FOR THE DATA SET : 29.7 <I/SIGMA(I)> FOR SHELL : 5.9
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10%(W/V) PEG ME 5000, 0.5M NACL,
REMARK 280 50MM BIS/TRIS, PH 5.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 42.87000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.79000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.40000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.79000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.87000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.40000
REMARK 290 SMTRY3 4 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, I
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 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 PRO L 120
REMARK 465 SER L 121
REMARK 465 SER L 122
REMARK 465 GLU L 123
REMARK 465 GLN L 124
REMARK 465 LEU L 125
REMARK 465 THR L 126
REMARK 465 SER L 127
REMARK 465 GLY L 128
REMARK 465 GLY L 129
REMARK 465 ALA L 130
REMARK 465 SER L 131
REMARK 465 VAL L 132
REMARK 465 VAL L 133
REMARK 465 TRP L 148
REMARK 465 LYS L 149
REMARK 465 ILE L 150
REMARK 465 ASP L 151
REMARK 465 GLY L 152
REMARK 465 SER L 153
REMARK 465 GLU L 154
REMARK 465 ARG L 155
REMARK 465 GLN L 156
REMARK 465 ASN L 157
REMARK 465 THR L 178
REMARK 465 LEU L 179
REMARK 465 THR L 180
REMARK 465 LEU L 181
REMARK 465 THR L 182
REMARK 465 LYS L 183
REMARK 465 ASP L 184
REMARK 465 GLU L 185
REMARK 465 TYR L 186
REMARK 465 GLU L 187
REMARK 465 ARG L 188
REMARK 465 HIS L 189
REMARK 465 ASN L 190
REMARK 465 SER L 191
REMARK 465 TYR L 192
REMARK 465 SER L 208
REMARK 465 PHE L 209
REMARK 465 ASN L 210
REMARK 465 ARG L 211
REMARK 465 ASN L 212
REMARK 465 GLU L 213
REMARK 465 CYS L 214
REMARK 465 PRO H 121
REMARK 465 SER H 122
REMARK 465 VAL H 123
REMARK 465 TYR H 124
REMARK 465 PRO H 125
REMARK 465 LEU H 126
REMARK 465 ALA H 127
REMARK 465 PRO H 128
REMARK 465 GLY H 129
REMARK 465 SER H 130
REMARK 465 ALA H 131
REMARK 465 ALA H 132
REMARK 465 GLN H 133
REMARK 465 THR H 134
REMARK 465 ASN H 135
REMARK 465 SER H 136
REMARK 465 MET H 137
REMARK 465 VAL H 138
REMARK 465 THR H 139
REMARK 465 LEU H 140
REMARK 465 GLY H 141
REMARK 465 LYS H 145
REMARK 465 GLY H 146
REMARK 465 SER H 164
REMARK 465 LEU H 165
REMARK 465 VAL H 196
REMARK 465 PRO H 197
REMARK 465 SER H 198
REMARK 465 SER H 199
REMARK 465 PRO H 200
REMARK 465 ARG H 201
REMARK 465 PRO H 202
REMARK 465 SER H 203
REMARK 465 GLU H 204
REMARK 465 THR H 205
REMARK 465 VAL H 206
REMARK 465 THR H 207
REMARK 465 LYS H 222
REMARK 465 ILE H 223
REMARK 465 GLU I 1
REMARK 465 MET I 2
REMARK 465 GLY I 3
REMARK 465 THR I 4
REMARK 465 ALA I 5
REMARK 465 ASP I 6
REMARK 465 LEU I 7
REMARK 465 GLY I 8
REMARK 465 PRO I 9
REMARK 465 SER I 10
REMARK 465 ARG I 106
REMARK 465 ASP I 107
REMARK 465 GLY I 108
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 SER I 11 OG
REMARK 480 VAL I 89 CG1 CG2
REMARK 480 GLN I 91 CG CD OE1 NE2
REMARK 480 LYS I 92 CG CD CE NZ
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 PRO L 8 -155.39 -104.35
REMARK 500 TYR L 30 53.24 34.68
REMARK 500 ASN L 31 16.84 58.82
REMARK 500 ALA L 51 -39.02 62.75
REMARK 500 GLU L 57 -22.05 85.87
REMARK 500 SER L 67 165.37 178.88
REMARK 500 THR L 94 -137.47 54.27
REMARK 500 PRO L 141 -172.03 -65.72
REMARK 500 ILE L 144 146.12 -172.08
REMARK 500 SER L 171 62.31 -50.56
REMARK 500 LYS L 199 9.45 -65.99
REMARK 500 SER L 201 -159.43 -156.97
REMARK 500 THR L 202 -34.79 -143.82
REMARK 500 SER H 15 -9.61 67.06
REMARK 500 GLN H 16 -164.92 -75.65
REMARK 500 LEU H 48 -70.68 -97.83
REMARK 500 SER H 82B 46.73 39.62
REMARK 500 ALA H 88 -172.68 -171.84
REMARK 500 PRO H 97 35.73 -65.59
REMARK 500 ALA H 114 -147.07 -137.84
REMARK 500 LYS H 115 143.23 -170.59
REMARK 500 THR H 116 75.77 -49.15
REMARK 500 PHE H 148 142.67 -174.09
REMARK 500 SER H 162 24.89 49.50
REMARK 500 GLN H 179 -127.92 -80.96
REMARK 500 HIS H 212 77.78 -169.16
REMARK 500 SER H 216 28.13 38.78
REMARK 500 LYS H 218 67.84 -159.02
REMARK 500 ASP H 220 28.43 -79.54
REMARK 500 SER I 22 92.21 -161.27
REMARK 500 ASN I 24 -165.28 70.90
REMARK 500 MET I 25 52.16 -98.83
REMARK 500 ASN I 53 73.95 -154.05
REMARK 500 ASN I 62 76.75 26.05
REMARK 500 HIS I 66 45.84 -91.68
REMARK 500 CYS I 68 117.68 -161.09
REMARK 500 ASP I 76 92.27 68.84
REMARK 500 ALA I 103 -75.83 -114.53
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JRH L 4 214 PIR S01320 S01320 24 234
DBREF 1JRH I 1 108 UNP P15260 INGR1_HUMAN 18 125
DBREF 1JRH H 1 223 PDB 1JRH 1JRH 1 223
SEQADV 1JRH SER L 9 PIR S01320 ALA 29 CONFLICT
SEQADV 1JRH PHE L 11 PIR S01320 LEU 31 CONFLICT
SEQADV 1JRH LEU L 15 PIR S01320 VAL 35 CONFLICT
SEQADV 1JRH ASP L 17 PIR S01320 GLU 37 CONFLICT
SEQADV 1JRH ARG L 18 PIR S01320 SER 38 CONFLICT
SEQADV 1JRH LYS L 24 PIR S01320 ARG 44 CONFLICT
SEQADV 1JRH ASP L 28 PIR S01320 ASN 48 CONFLICT
SEQADV 1JRH ASN L 31 PIR S01320 SER 51 CONFLICT
SEQADV 1JRH ARG L 32 PIR S01320 ASN 52 CONFLICT
SEQADV 1JRH PRO L 40 PIR S01320 GLN 60 CONFLICT
SEQADV 1JRH ASN L 42 PIR S01320 LYS 62 CONFLICT
SEQADV 1JRH ALA L 43 PIR S01320 SER 63 CONFLICT
SEQADV 1JRH ARG L 45 PIR S01320 GLN 65 CONFLICT
SEQADV 1JRH ILE L 48 PIR S01320 VAL 68 CONFLICT
SEQADV 1JRH SER L 49 PIR S01320 TYR 69 CONFLICT
SEQADV 1JRH GLY L 50 PIR S01320 VAL 70 CONFLICT
SEQADV 1JRH SER L 53 PIR S01320 LYS 73 CONFLICT
SEQADV 1JRH GLU L 55 PIR S01320 VAL 75 CONFLICT
SEQADV 1JRH THR L 56 PIR S01320 ASP 76 CONFLICT
SEQADV 1JRH GLU L 57 PIR S01320 GLY 77 CONFLICT
SEQADV 1JRH LYS L 69 PIR S01320 THR 89 CONFLICT
SEQADV 1JRH ASP L 70 PIR S01320 GLN 90 CONFLICT
SEQADV 1JRH THR L 72 PIR S01320 SER 92 CONFLICT
SEQADV 1JRH SER L 74 PIR S01320 LYS 94 CONFLICT
SEQADV 1JRH THR L 76 PIR S01320 ASN 96 CONFLICT
SEQADV 1JRH THR L 80 PIR S01320 SER 100 CONFLICT
SEQADV 1JRH VAL L 83 PIR S01320 PHE 103 CONFLICT
SEQADV 1JRH ALA L 84 PIR S01320 GLY 104 CONFLICT
SEQADV 1JRH THR L 85 PIR S01320 SER 105 CONFLICT
SEQADV 1JRH GLN L 90 PIR S01320 HIS 110 CONFLICT
SEQADV 1JRH TYR L 91 PIR S01320 PHE 111 CONFLICT
SEQADV 1JRH SER L 93 PIR S01320 ASP 113 CONFLICT
SEQADV 1JRH L PIR S01320 PRO 115 DELETION
SEQADV 1JRH TRP L 96 PIR S01320 PHE 116 CONFLICT
SEQADV 1JRH GLY L 100 PIR S01320 SER 120 CONFLICT
SEQADV 1JRH ILE L 106 PIR S01320 MET 126 CONFLICT
SEQADV 1JRH SER I 105 UNP P15260 CYS 122 ENGINEERED
SEQRES 1 L 213 SER VAL GLU MET THR GLN SER PRO SER SER PHE SER VAL
SEQRES 2 L 213 SER LEU GLY ASP ARG VAL THR ILE THR CYS LYS ALA SER
SEQRES 3 L 213 GLU ASP ILE TYR ASN ARG LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 L 213 PRO GLY ASN ALA PRO ARG LEU LEU ILE SER GLY ALA THR
SEQRES 5 L 213 SER LEU GLU THR GLU VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 L 213 GLY SER GLY LYS ASP TYR THR LEU SER ILE THR SER LEU
SEQRES 7 L 213 GLN THR GLU ASP VAL ALA THR TYR TYR CYS GLN GLN TYR
SEQRES 8 L 213 TRP SER THR TRP THR PHE GLY GLY GLY THR LYS LEU GLU
SEQRES 9 L 213 ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE
SEQRES 10 L 213 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER
SEQRES 11 L 213 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE
SEQRES 12 L 213 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN
SEQRES 13 L 213 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP
SEQRES 14 L 213 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS
SEQRES 15 L 213 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA
SEQRES 16 L 213 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE
SEQRES 17 L 213 ASN ARG ASN GLU CYS
SEQRES 1 H 219 ALA VAL LYS LEU GLN GLU SER GLY PRO GLY ILE LEU LYS
SEQRES 2 H 219 PRO SER GLN THR LEU SER LEU THR CYS SER PHE SER GLY
SEQRES 3 H 219 PHE SER LEU THR THR TYR GLY MET GLY VAL GLY TRP ILE
SEQRES 4 H 219 ARG GLN SER SER GLY LYS GLY LEU GLU TRP LEU ALA HIS
SEQRES 5 H 219 ILE TRP TRP ASP ASP ASP LYS TYR TYR ASN PRO SER LEU
SEQRES 6 H 219 LYS SER ARG LEU THR ILE SER LYS ASP THR SER ARG ASN
SEQRES 7 H 219 GLN VAL PHE LEU LYS ILE THR SER VAL ALA THR ALA ASP
SEQRES 8 H 219 THR ALA THR TYR TYR CYS ALA ARG ARG ALA PRO PHE TYR
SEQRES 9 H 219 GLY ASN HIS ALA MET ASP TYR TRP GLY GLN GLY THR THR
SEQRES 10 H 219 VAL THR VAL SER SER ALA LYS THR THR PRO PRO SER VAL
SEQRES 11 H 219 TYR PRO LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER
SEQRES 12 H 219 MET VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO
SEQRES 13 H 219 GLU PRO VAL THR VAL THR TRP ASN SER GLY SER LEU SER
SEQRES 14 H 219 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP
SEQRES 15 H 219 LEU TYR THR LEU SER SER SER VAL THR VAL PRO SER SER
SEQRES 16 H 219 PRO ARG PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS
SEQRES 17 H 219 PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE
SEQRES 1 I 108 GLU MET GLY THR ALA ASP LEU GLY PRO SER SER VAL PRO
SEQRES 2 I 108 THR PRO THR ASN VAL THR ILE GLU SER TYR ASN MET ASN
SEQRES 3 I 108 PRO ILE VAL TYR TRP GLU TYR GLN ILE MET PRO GLN VAL
SEQRES 4 I 108 PRO VAL PHE THR VAL GLU VAL LYS ASN TYR GLY VAL LYS
SEQRES 5 I 108 ASN SER GLU TRP ILE ASP ALA CYS ILE ASN ILE SER HIS
SEQRES 6 I 108 HIS TYR CYS ASN ILE SER ASP HIS VAL GLY ASP PRO SER
SEQRES 7 I 108 ASN SER LEU TRP VAL ARG VAL LYS ALA ARG VAL GLY GLN
SEQRES 8 I 108 LYS GLU SER ALA TYR ALA LYS SER GLU GLU PHE ALA VAL
SEQRES 9 I 108 SER ARG ASP GLY
FORMUL 4 HOH *30(H2 O)
HELIX 1 1 THR L 80 ASP L 82 5 3
HELIX 2 2 LYS H 64 ARG H 66 5 3
HELIX 3 3 THR H 84 ASP H 86 5 3
HELIX 4 4 PRO H 213 SER H 215 5 3
HELIX 5 5 SER I 71 HIS I 73 5 3
SHEET 1 E 4 MET L 4 SER L 7 0
SHEET 2 E 4 VAL L 19 ALA L 25 -1 N LYS L 24 O THR L 5
SHEET 3 E 4 ASP L 70 ILE L 75 -1 N ILE L 75 O VAL L 19
SHEET 4 E 4 PHE L 62 SER L 67 -1 N SER L 67 O ASP L 70
SHEET 1 F 2 SER L 10 VAL L 13 0
SHEET 2 F 2 LYS L 103 ILE L 106 1 N LYS L 103 O PHE L 11
SHEET 1 G 3 THR L 85 GLN L 90 0
SHEET 2 G 3 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85
SHEET 3 G 3 ARG L 45 ILE L 48 -1 N ILE L 48 O TRP L 35
SHEET 1 H 3 THR L 114 SER L 116 0
SHEET 2 H 3 CYS L 134 ASN L 137 -1 N ASN L 137 O THR L 114
SHEET 3 H 3 MET L 175 SER L 177 -1 N SER L 177 O CYS L 134
SHEET 1 I 2 ASN L 145 LYS L 147 0
SHEET 2 I 2 GLU L 195 THR L 197 -1 N THR L 197 O ASN L 145
SHEET 1 A 4 LYS H 3 SER H 7 0
SHEET 2 A 4 LEU H 18 SER H 25 -1 N SER H 25 O LYS H 3
SHEET 3 A 4 GLN H 77 ILE H 82 -1 N ILE H 82 O LEU H 18
SHEET 4 A 4 LEU H 67 ASP H 72 -1 N ASP H 72 O GLN H 77
SHEET 1 B 5 THR H 107 VAL H 109 0
SHEET 2 B 5 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107
SHEET 3 B 5 GLY H 35 GLN H 39 -1 N GLN H 39 O THR H 89
SHEET 4 B 5 ALA H 49 TRP H 52 -1 N ILE H 51 O VAL H 35A
SHEET 5 B 5 LYS H 57 TYR H 59 -1 N TYR H 58 O HIS H 50
SHEET 1 C 3 THR H 153 THR H 156 0
SHEET 2 C 3 ASN H 209 HIS H 212 -1 N ALA H 211 O THR H 153
SHEET 3 C 3 THR H 217 VAL H 219 -1 N VAL H 219 O VAL H 210
SHEET 1 D 2 VAL H 171 THR H 173 0
SHEET 2 D 2 SER H 189 VAL H 191 -1 N SER H 190 O HIS H 172
SHEET 1 J 3 THR I 19 GLU I 21 0
SHEET 2 J 3 ILE I 28 TYR I 30 -1 N TYR I 30 O THR I 19
SHEET 3 J 3 TYR I 67 ASN I 69 -1 N CYS I 68 O VAL I 29
SHEET 1 K 3 SER I 80 ARG I 88 0
SHEET 2 K 3 VAL I 41 TYR I 49 -1 N TYR I 49 O SER I 80
SHEET 3 K 3 ILE I 57 CYS I 60 -1 N CYS I 60 O VAL I 44
SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.02
SSBOND 2 CYS H 142 CYS H 208 1555 1555 2.05
SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.03
SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.04
SSBOND 5 CYS I 60 CYS I 68 1555 1555 2.03
CISPEP 1 SER L 7 PRO L 8 0 -3.10
CISPEP 2 TYR L 140 PRO L 141 0 -0.15
CISPEP 3 PHE H 148 PRO H 149 0 -2.98
CISPEP 4 GLU H 150 PRO H 151 0 4.13
CRYST1 85.740 90.800 101.580 90.00 90.00 90.00 P 21 21 21 4
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 0.011663 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011013 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009844 0.00000
ATOM 1 N SER L 1 6.148 49.671 41.513 1.00 70.56 N
ATOM 2 CA SER L 1 5.612 48.312 41.825 1.00 68.33 C
ATOM 3 C SER L 1 4.086 48.383 41.994 1.00 65.84 C
ATOM 4 O SER L 1 3.539 49.475 42.181 1.00 70.69 O
ATOM 5 CB SER L 1 6.278 47.802 43.104 1.00 67.05 C
ATOM 6 OG SER L 1 7.691 47.839 42.965 1.00 57.96 O
ATOM 7 N VAL L 2 3.404 47.240 41.910 1.00 58.05 N
ATOM 8 CA VAL L 2 1.941 47.183 42.086 1.00 52.04 C
ATOM 9 C VAL L 2 1.683 46.616 43.509 1.00 53.67 C
ATOM 10 O VAL L 2 2.407 45.725 43.946 1.00 57.19 O
ATOM 11 CB VAL L 2 1.268 46.237 41.033 1.00 43.18 C
ATOM 12 CG1 VAL L 2 -0.236 46.238 41.215 1.00 31.28 C
ATOM 13 CG2 VAL L 2 1.641 46.628 39.593 1.00 20.18 C
ATOM 14 N GLU L 3 0.687 47.120 44.241 1.00 53.79 N
ATOM 15 CA GLU L 3 0.404 46.587 45.586 1.00 52.52 C
ATOM 16 C GLU L 3 -0.953 45.889 45.546 1.00 56.95 C
ATOM 17 O GLU L 3 -1.838 46.255 44.746 1.00 55.15 O
ATOM 18 CB GLU L 3 0.383 47.669 46.679 1.00 49.96 C
ATOM 19 CG GLU L 3 1.682 48.437 46.908 1.00 53.58 C
ATOM 20 CD GLU L 3 1.839 49.605 45.940 1.00 74.42 C
ATOM 21 OE1 GLU L 3 0.837 50.314 45.686 1.00 71.54 O
ATOM 22 OE2 GLU L 3 2.959 49.817 45.428 1.00 87.49 O
ATOM 23 N MET L 4 -1.107 44.883 46.405 1.00 55.77 N
ATOM 24 CA MET L 4 -2.335 44.105 46.469 1.00 52.64 C
ATOM 25 C MET L 4 -2.774 44.027 47.905 1.00 53.97 C
ATOM 26 O MET L 4 -2.101 43.410 48.731 1.00 53.40 O
ATOM 27 CB MET L 4 -2.088 42.688 45.958 1.00 49.91 C
ATOM 28 CG MET L 4 -1.532 42.602 44.561 1.00 26.55 C
ATOM 29 SD MET L 4 -2.688 43.150 43.362 1.00 45.85 S
ATOM 30 CE MET L 4 -3.602 41.681 43.133 1.00 49.03 C
ATOM 31 N THR L 5 -3.900 44.647 48.211 1.00 56.41 N
ATOM 32 CA THR L 5 -4.394 44.626 49.561 1.00 58.41 C
ATOM 33 C THR L 5 -5.525 43.653 49.755 1.00 60.61 C
ATOM 34 O THR L 5 -6.562 43.712 49.083 1.00 59.73 O
ATOM 35 CB THR L 5 -4.824 46.015 50.007 1.00 63.22 C
ATOM 36 OG1 THR L 5 -3.659 46.839 50.137 1.00 74.76 O
ATOM 37 CG2 THR L 5 -5.553 45.948 51.352 1.00 72.47 C
ATOM 38 N GLN L 6 -5.296 42.745 50.688 1.00 60.84 N
ATOM 39 CA GLN L 6 -6.270 41.746 51.049 1.00 63.90 C
ATOM 40 C GLN L 6 -6.673 42.079 52.459 1.00 72.52 C
ATOM 41 O GLN L 6 -5.843 42.037 53.377 1.00 79.20 O
ATOM 42 CB GLN L 6 -5.640 40.369 51.081 1.00 56.21 C
ATOM 43 CG GLN L 6 -5.699 39.605 49.810 1.00 43.66 C
ATOM 44 CD GLN L 6 -5.264 38.173 50.013 1.00 58.63 C
ATOM 45 OE1 GLN L 6 -4.294 37.721 49.406 1.00 80.18 O
ATOM 46 NE2 GLN L 6 -5.978 37.446 50.874 1.00 39.03 N
ATOM 47 N SER L 7 -7.930 42.420 52.657 1.00 77.28 N
ATOM 48 CA SER L 7 -8.356 42.694 54.008 1.00 83.23 C
ATOM 49 C SER L 7 -9.460 41.712 54.398 1.00 85.88 C
ATOM 50 O SER L 7 -10.395 41.464 53.624 1.00 90.48 O
ATOM 51 CB SER L 7 -8.804 44.149 54.143 1.00 81.05 C
ATOM 52 OG SER L 7 -7.711 45.011 53.865 1.00 82.46 O
ATOM 53 N PRO L 8 -9.341 41.115 55.594 1.00 83.23 N
ATOM 54 CA PRO L 8 -8.187 41.329 56.460 1.00 80.78 C
ATOM 55 C PRO L 8 -7.266 40.117 56.413 1.00 75.91 C
ATOM 56 O PRO L 8 -7.257 39.351 55.443 1.00 69.60 O
ATOM 57 CB PRO L 8 -8.832 41.495 57.842 1.00 86.50 C
ATOM 58 CG PRO L 8 -10.195 40.735 57.725 1.00 87.27 C
ATOM 59 CD PRO L 8 -10.309 40.243 56.274 1.00 81.35 C
ATOM 60 N SER L 9 -6.500 39.957 57.480 1.00 73.83 N
ATOM 61 CA SER L 9 -5.583 38.846 57.601 1.00 77.89 C
ATOM 62 C SER L 9 -6.354 37.567 57.927 1.00 75.73 C
ATOM 63 O SER L 9 -5.891 36.461 57.639 1.00 76.38 O
ATOM 64 CB SER L 9 -4.554 39.139 58.700 1.00 85.10 C
ATOM 65 OG SER L 9 -3.930 40.393 58.469 1.00114.21 O
ATOM 66 N SER L 10 -7.529 37.718 58.527 1.00 71.45 N
ATOM 67 CA SER L 10 -8.347 36.568 58.887 1.00 67.49 C
ATOM 68 C SER L 10 -9.815 36.940 58.755 1.00 64.88 C
ATOM 69 O SER L 10 -10.142 38.111 58.570 1.00 66.70 O
ATOM 70 CB SER L 10 -8.043 36.108 60.315 1.00 62.04 C
ATOM 71 OG SER L 10 -8.595 37.001 61.260 1.00 62.87 O
ATOM 72 N PHE L 11 -10.691 35.944 58.857 1.00 64.17 N
ATOM 73 CA PHE L 11 -12.130 36.143 58.724 1.00 60.32 C
ATOM 74 C PHE L 11 -12.813 34.980 59.443 1.00 56.35 C
ATOM 75 O PHE L 11 -12.630 33.821 59.077 1.00 55.11 O
ATOM 76 CB PHE L 11 -12.519 36.166 57.228 1.00 62.76 C
ATOM 77 CG PHE L 11 -13.867 36.792 56.946 1.00 87.08 C
ATOM 78 CD1 PHE L 11 -14.597 37.420 57.965 1.00110.41 C
ATOM 79 CD2 PHE L 11 -14.405 36.757 55.654 1.00 84.40 C
ATOM 80 CE1 PHE L 11 -15.843 38.002 57.705 1.00109.21 C
ATOM 81 CE2 PHE L 11 -15.649 37.335 55.379 1.00 93.66 C
ATOM 82 CZ PHE L 11 -16.370 37.958 56.407 1.00107.02 C
ATOM 83 N SER L 12 -13.580 35.301 60.479 1.00 55.64 N
ATOM 84 CA SER L 12 -14.315 34.307 61.248 1.00 50.91 C
ATOM 85 C SER L 12 -15.535 33.897 60.426 1.00 51.16 C
ATOM 86 O SER L 12 -16.371 34.729 60.045 1.00 51.40 O
ATOM 87 CB SER L 12 -14.734 34.920 62.573 1.00 52.62 C
ATOM 88 OG SER L 12 -13.606 35.513 63.199 1.00 71.38 O
ATOM 89 N VAL L 13 -15.634 32.608 60.147 1.00 46.28 N
ATOM 90 CA VAL L 13 -16.718 32.083 59.338 1.00 48.13 C
ATOM 91 C VAL L 13 -17.167 30.743 59.903 1.00 48.99 C
ATOM 92 O VAL L 13 -16.486 30.191 60.756 1.00 49.59 O
ATOM 93 CB VAL L 13 -16.260 31.889 57.869 1.00 45.59 C
ATOM 94 CG1 VAL L 13 -15.885 33.241 57.250 1.00 41.58 C
ATOM 95 CG2 VAL L 13 -15.098 30.908 57.805 1.00 33.64 C
ATOM 96 N SER L 14 -18.313 30.237 59.442 1.00 47.20 N
ATOM 97 CA SER L 14 -18.847 28.940 59.882 1.00 41.95 C
ATOM 98 C SER L 14 -18.995 28.064 58.648 1.00 39.45 C
ATOM 99 O SER L 14 -19.144 28.588 57.547 1.00 36.19 O
ATOM 100 CB SER L 14 -20.215 29.104 60.555 1.00 42.81 C
ATOM 101 OG SER L 14 -20.182 30.045 61.612 1.00 52.43 O
ATOM 102 N LEU L 15 -18.964 26.742 58.801 1.00 40.93 N
ATOM 103 CA LEU L 15 -19.085 25.880 57.615 1.00 42.52 C
ATOM 104 C LEU L 15 -20.473 26.043 57.079 1.00 38.59 C
ATOM 105 O LEU L 15 -21.392 26.334 57.826 1.00 43.08 O
ATOM 106 CB LEU L 15 -18.867 24.400 57.912 1.00 43.75 C
ATOM 107 CG LEU L 15 -17.831 23.973 58.929 1.00 42.11 C
ATOM 108 CD1 LEU L 15 -18.475 24.135 60.314 1.00 54.45 C
ATOM 109 CD2 LEU L 15 -17.405 22.530 58.664 1.00 34.48 C
ATOM 110 N GLY L 16 -20.620 25.849 55.785 1.00 34.76 N
ATOM 111 CA GLY L 16 -21.916 26.011 55.182 1.00 37.40 C
ATOM 112 C GLY L 16 -22.141 27.433 54.701 1.00 38.63 C
ATOM 113 O GLY L 16 -22.964 27.671 53.815 1.00 44.80 O
ATOM 114 N ASP L 17 -21.426 28.391 55.273 1.00 35.28 N
ATOM 115 CA ASP L 17 -21.583 29.769 54.834 1.00 36.81 C
ATOM 116 C ASP L 17 -21.007 29.911 53.441 1.00 39.10 C
ATOM 117 O ASP L 17 -20.352 28.992 52.923 1.00 35.29 O
ATOM 118 CB ASP L 17 -20.827 30.734 55.751 1.00 40.80 C
ATOM 119 CG ASP L 17 -21.323 30.711 57.191 1.00 56.90 C
ATOM 120 OD1 ASP L 17 -22.343 30.031 57.486 1.00 56.55 O
ATOM 121 OD2 ASP L 17 -20.674 31.388 58.029 1.00 48.89 O
ATOM 122 N ARG L 18 -21.281 31.063 52.832 1.00 47.21 N
ATOM 123 CA ARG L 18 -20.724 31.401 51.527 1.00 48.62 C
ATOM 124 C ARG L 18 -19.707 32.399 51.992 1.00 47.68 C
ATOM 125 O ARG L 18 -19.998 33.228 52.860 1.00 48.63 O
ATOM 126 CB ARG L 18 -21.714 32.094 50.580 1.00 50.88 C
ATOM 127 CG ARG L 18 -21.207 32.119 49.123 1.00 70.62 C
ATOM 128 CD ARG L 18 -22.102 32.880 48.162 1.00 77.79 C
ATOM 129 NE ARG L 18 -22.234 34.274 48.571 1.00 99.43 N
ATOM 130 CZ ARG L 18 -23.347 34.802 49.075 1.00129.32 C
ATOM 131 NH1 ARG L 18 -24.439 34.052 49.218 1.00131.53 N
ATOM 132 NH2 ARG L 18 -23.367 36.081 49.442 1.00134.49 N
ATOM 133 N VAL L 19 -18.510 32.318 51.437 1.00 49.10 N
ATOM 134 CA VAL L 19 -17.469 33.222 51.851 1.00 45.55 C
ATOM 135 C VAL L 19 -16.896 33.933 50.658 1.00 46.31 C
ATOM 136 O VAL L 19 -16.627 33.319 49.612 1.00 41.70 O
ATOM 137 CB VAL L 19 -16.342 32.488 52.586 1.00 42.21 C
ATOM 138 CG1 VAL L 19 -15.430 33.507 53.243 1.00 53.56 C
ATOM 139 CG2 VAL L 19 -16.917 31.510 53.630 1.00 24.39 C
ATOM 140 N THR L 20 -16.737 35.238 50.822 1.00 47.69 N
ATOM 141 CA THR L 20 -16.153 36.056 49.792 1.00 48.82 C
ATOM 142 C THR L 20 -14.941 36.703 50.422 1.00 53.03 C
ATOM 143 O THR L 20 -15.015 37.220 51.551 1.00 56.03 O
ATOM 144 CB THR L 20 -17.100 37.137 49.316 1.00 45.70 C
ATOM 145 OG1 THR L 20 -18.341 36.537 48.930 1.00 47.52 O
ATOM 146 CG2 THR L 20 -16.492 37.849 48.107 1.00 41.63 C
ATOM 147 N ILE L 21 -13.824 36.638 49.696 1.00 54.85 N
ATOM 148 CA ILE L 21 -12.563 37.237 50.125 1.00 53.00 C
ATOM 149 C ILE L 21 -12.278 38.346 49.126 1.00 52.15 C
ATOM 150 O ILE L 21 -12.439 38.166 47.910 1.00 48.08 O
ATOM 151 CB ILE L 21 -11.392 36.227 50.129 1.00 49.84 C
ATOM 152 CG1 ILE L 21 -11.686 35.099 51.109 1.00 42.07 C
ATOM 153 CG2 ILE L 21 -10.109 36.901 50.617 1.00 43.74 C
ATOM 154 CD1 ILE L 21 -10.654 34.017 51.101 1.00 34.98 C
ATOM 155 N THR L 22 -11.858 39.488 49.650 1.00 52.56 N
ATOM 156 CA THR L 22 -11.589 40.634 48.820 1.00 56.89 C
ATOM 157 C THR L 22 -10.101 40.928 48.611 1.00 58.31 C
ATOM 158 O THR L 22 -9.285 40.849 49.543 1.00 60.77 O
ATOM 159 CB THR L 22 -12.390 41.842 49.365 1.00 59.26 C
ATOM 160 OG1 THR L 22 -13.726 41.776 48.837 1.00 50.55 O
ATOM 161 CG2 THR L 22 -11.740 43.178 48.997 1.00 67.15 C
ATOM 162 N CYS L 23 -9.778 41.260 47.361 1.00 59.56 N
ATOM 163 CA CYS L 23 -8.420 41.572 46.914 1.00 62.11 C
ATOM 164 C CYS L 23 -8.461 42.848 46.051 1.00 62.27 C
ATOM 165 O CYS L 23 -9.166 42.888 45.031 1.00 63.19 O
ATOM 166 CB CYS L 23 -7.884 40.386 46.084 1.00 62.64 C
ATOM 167 SG CYS L 23 -6.228 40.559 45.330 1.00 60.11 S
ATOM 168 N LYS L 24 -7.719 43.882 46.449 1.00 59.39 N
ATOM 169 CA LYS L 24 -7.704 45.122 45.678 1.00 60.52 C
ATOM 170 C LYS L 24 -6.279 45.466 45.227 1.00 61.51 C
ATOM 171 O LYS L 24 -5.347 45.476 46.050 1.00 61.80 O
ATOM 172 CB LYS L 24 -8.297 46.256 46.519 1.00 66.08 C
ATOM 173 CG LYS L 24 -8.927 47.410 45.722 1.00 86.11 C
ATOM 174 CD LYS L 24 -7.945 48.558 45.470 1.00102.32 C
ATOM 175 CE LYS L 24 -8.514 49.596 44.505 1.00 86.45 C
ATOM 176 NZ LYS L 24 -7.477 50.596 44.119 1.00 85.39 N
ATOM 177 N ALA L 25 -6.131 45.745 43.925 1.00 56.94 N
ATOM 178 CA ALA L 25 -4.848 46.090 43.287 1.00 55.60 C
ATOM 179 C ALA L 25 -4.690 47.614 43.100 1.00 59.01 C
ATOM 180 O ALA L 25 -5.662 48.305 42.773 1.00 62.80 O
ATOM 181 CB ALA L 25 -4.754 45.392 41.941 1.00 51.46 C
ATOM 182 N SER L 26 -3.477 48.136 43.295 1.00 55.03 N
ATOM 183 CA SER L 26 -3.218 49.575 43.175 1.00 51.82 C
ATOM 184 C SER L 26 -3.485 50.209 41.801 1.00 52.85 C
ATOM 185 O SER L 26 -3.672 51.424 41.694 1.00 57.49 O
ATOM 186 CB SER L 26 -1.784 49.880 43.610 1.00 45.96 C
ATOM 187 OG SER L 26 -0.848 49.238 42.767 1.00 53.09 O
ATOM 188 N GLU L 27 -3.505 49.399 40.752 1.00 54.06 N
ATOM 189 CA GLU L 27 -3.751 49.897 39.398 1.00 57.96 C
ATOM 190 C GLU L 27 -4.333 48.754 38.568 1.00 59.05 C
ATOM 191 O GLU L 27 -4.196 47.586 38.941 1.00 59.01 O
ATOM 192 CB GLU L 27 -2.444 50.396 38.769 1.00 58.09 C
ATOM 193 CG GLU L 27 -1.373 49.322 38.653 1.00 62.41 C
ATOM 194 CD GLU L 27 -0.088 49.796 37.977 1.00 62.96 C
ATOM 195 OE1 GLU L 27 -0.016 49.722 36.723 1.00 46.60 O
ATOM 196 OE2 GLU L 27 0.846 50.234 38.698 1.00 47.71 O
ATOM 197 N ASP L 28 -4.978 49.078 37.450 1.00 57.07 N
ATOM 198 CA ASP L 28 -5.576 48.049 36.604 1.00 56.29 C
ATOM 199 C ASP L 28 -4.554 46.948 36.245 1.00 59.62 C
ATOM 200 O ASP L 28 -3.550 47.222 35.567 1.00 58.66 O
ATOM 201 CB ASP L 28 -6.136 48.687 35.329 1.00 55.69 C
ATOM 202 CG ASP L 28 -7.236 47.833 34.653 1.00 73.83 C
ATOM 203 OD1 ASP L 28 -7.309 46.595 34.873 1.00 68.37 O
ATOM 204 OD2 ASP L 28 -8.040 48.417 33.888 1.00 85.83 O
ATOM 205 N ILE L 29 -4.812 45.718 36.715 1.00 56.96 N
ATOM 206 CA ILE L 29 -3.940 44.564 36.441 1.00 52.20 C
ATOM 207 C ILE L 29 -4.552 43.644 35.392 1.00 52.40 C
ATOM 208 O ILE L 29 -4.218 42.460 35.304 1.00 50.34 O
ATOM 209 CB ILE L 29 -3.610 43.727 37.709 1.00 43.69 C
ATOM 210 CG1 ILE L 29 -4.886 43.213 38.360 1.00 37.32 C
ATOM 211 CG2 ILE L 29 -2.811 44.546 38.683 1.00 33.59 C
ATOM 212 CD1 ILE L 29 -4.632 42.431 39.619 1.00 31.71 C
ATOM 213 N TYR L 30 -5.462 44.216 34.611 1.00 54.57 N
ATOM 214 CA TYR L 30 -6.145 43.553 33.503 1.00 57.53 C
ATOM 215 C TYR L 30 -6.471 42.062 33.648 1.00 56.89 C
ATOM 216 O TYR L 30 -6.116 41.260 32.787 1.00 61.00 O
ATOM 217 CB TYR L 30 -5.353 43.811 32.203 1.00 57.32 C
ATOM 218 CG TYR L 30 -5.212 45.289 31.885 1.00 60.36 C
ATOM 219 CD1 TYR L 30 -4.347 46.099 32.624 1.00 61.98 C
ATOM 220 CD2 TYR L 30 -5.977 45.890 30.883 1.00 74.47 C
ATOM 221 CE1 TYR L 30 -4.248 47.472 32.383 1.00 85.33 C
ATOM 222 CE2 TYR L 30 -5.886 47.271 30.630 1.00 88.17 C
ATOM 223 CZ TYR L 30 -5.019 48.054 31.390 1.00 94.89 C
ATOM 224 OH TYR L 30 -4.935 49.418 31.188 1.00100.15 O
ATOM 225 N ASN L 31 -7.144 41.699 34.738 1.00 55.83 N
ATOM 226 CA ASN L 31 -7.559 40.314 35.000 1.00 54.57 C
ATOM 227 C ASN L 31 -6.468 39.245 35.076 1.00 51.89 C
ATOM 228 O ASN L 31 -6.762 38.055 34.981 1.00 49.90 O
ATOM 229 CB ASN L 31 -8.645 39.873 34.004 1.00 58.69 C
ATOM 230 CG ASN L 31 -10.047 40.343 34.403 1.00 69.44 C
ATOM 231 OD1 ASN L 31 -10.219 41.362 35.083 1.00 80.53 O
ATOM 232 ND2 ASN L 31 -11.057 39.594 33.975 1.00 81.89 N
ATOM 233 N ARG L 32 -5.213 39.660 35.245 1.00 50.77 N
ATOM 234 CA ARG L 32 -4.100 38.718 35.380 1.00 44.62 C
ATOM 235 C ARG L 32 -3.968 38.467 36.880 1.00 45.17 C
ATOM 236 O ARG L 32 -3.017 38.916 37.537 1.00 43.20 O
ATOM 237 CB ARG L 32 -2.821 39.326 34.815 1.00 44.01 C
ATOM 238 CG ARG L 32 -2.963 39.775 33.380 1.00 38.56 C
ATOM 239 CD ARG L 32 -3.578 38.688 32.557 1.00 27.51 C
ATOM 240 NE ARG L 32 -3.766 39.104 31.173 1.00 61.61 N
ATOM 241 CZ ARG L 32 -4.544 38.469 30.296 1.00 79.87 C
ATOM 242 NH1 ARG L 32 -5.227 37.372 30.653 1.00 50.68 N
ATOM 243 NH2 ARG L 32 -4.633 38.933 29.052 1.00 85.48 N
ATOM 244 N LEU L 33 -4.942 37.740 37.413 1.00 43.87 N
ATOM 245 CA LEU L 33 -5.000 37.474 38.837 1.00 41.30 C
ATOM 246 C LEU L 33 -5.043 36.005 39.106 1.00 37.08 C
ATOM 247 O LEU L 33 -5.705 35.267 38.385 1.00 39.42 O
ATOM 248 CB LEU L 33 -6.259 38.093 39.422 1.00 37.28 C
ATOM 249 CG LEU L 33 -6.292 37.957 40.926 1.00 39.52 C
ATOM 250 CD1 LEU L 33 -5.520 39.124 41.501 1.00 17.79 C
ATOM 251 CD2 LEU L 33 -7.710 37.938 41.412 1.00 51.54 C
ATOM 252 N ALA L 34 -4.350 35.580 40.147 1.00 28.65 N
ATOM 253 CA ALA L 34 -4.345 34.186 40.498 1.00 31.83 C
ATOM 254 C ALA L 34 -4.788 34.137 41.924 1.00 32.42 C
ATOM 255 O ALA L 34 -4.692 35.135 42.640 1.00 32.02 O
ATOM 256 CB ALA L 34 -2.962 33.587 40.357 1.00 29.14 C
ATOM 257 N TRP L 35 -5.283 32.977 42.327 1.00 28.78 N
ATOM 258 CA TRP L 35 -5.730 32.754 43.683 1.00 31.36 C
ATOM 259 C TRP L 35 -5.085 31.452 44.116 1.00 33.06 C
ATOM 260 O TRP L 35 -5.091 30.480 43.353 1.00 27.90 O
ATOM 261 CB TRP L 35 -7.247 32.612 43.751 1.00 35.25 C
ATOM 262 CG TRP L 35 -8.015 33.893 43.620 1.00 36.33 C
ATOM 263 CD1 TRP L 35 -8.627 34.355 42.502 1.00 46.79 C
ATOM 264 CD2 TRP L 35 -8.277 34.864 44.654 1.00 51.03 C
ATOM 265 NE1 TRP L 35 -9.254 35.553 42.760 1.00 62.20 N
ATOM 266 CE2 TRP L 35 -9.058 35.891 44.071 1.00 47.37 C
ATOM 267 CE3 TRP L 35 -7.925 34.968 46.010 1.00 44.29 C
ATOM 268 CZ2 TRP L 35 -9.498 37.015 44.795 1.00 31.65 C
ATOM 269 CZ3 TRP L 35 -8.364 36.088 46.737 1.00 21.12 C
ATOM 270 CH2 TRP L 35 -9.143 37.094 46.121 1.00 34.84 C
ATOM 271 N TYR L 36 -4.547 31.454 45.339 1.00 32.61 N
ATOM 272 CA TYR L 36 -3.851 30.319 45.942 1.00 33.99 C
ATOM 273 C TYR L 36 -4.366 29.991 47.352 1.00 35.86 C
ATOM 274 O TYR L 36 -4.638 30.889 48.156 1.00 39.41 O
ATOM 275 CB TYR L 36 -2.345 30.623 46.073 1.00 36.66 C
ATOM 276 CG TYR L 36 -1.629 30.961 44.786 1.00 32.84 C
ATOM 277 CD1 TYR L 36 -1.677 32.250 44.266 1.00 32.02 C
ATOM 278 CD2 TYR L 36 -0.938 29.983 44.069 1.00 32.96 C
ATOM 279 CE1 TYR L 36 -1.068 32.562 43.056 1.00 39.78 C
ATOM 280 CE2 TYR L 36 -0.325 30.280 42.862 1.00 37.04 C
ATOM 281 CZ TYR L 36 -0.398 31.575 42.357 1.00 47.47 C
ATOM 282 OH TYR L 36 0.161 31.877 41.134 1.00 36.47 O
ATOM 283 N GLN L 37 -4.482 28.704 47.657 1.00 32.31 N
ATOM 284 CA GLN L 37 -4.934 28.266 48.968 1.00 34.24 C
ATOM 285 C GLN L 37 -3.763 27.608 49.659 1.00 32.55 C
ATOM 286 O GLN L 37 -2.987 26.904 49.025 1.00 37.03 O
ATOM 287 CB GLN L 37 -6.062 27.251 48.817 1.00 39.01 C
ATOM 288 CG GLN L 37 -6.439 26.548 50.101 1.00 37.78 C
ATOM 289 CD GLN L 37 -7.196 25.281 49.819 1.00 39.62 C
ATOM 290 OE1 GLN L 37 -6.604 24.256 49.472 1.00 50.89 O
ATOM 291 NE2 GLN L 37 -8.510 25.336 49.963 1.00 58.70 N
ATOM 292 N GLN L 38 -3.620 27.806 50.955 1.00 30.56 N
ATOM 293 CA GLN L 38 -2.492 27.190 51.613 1.00 31.22 C
ATOM 294 C GLN L 38 -2.786 26.733 53.024 1.00 33.26 C
ATOM 295 O GLN L 38 -3.061 27.542 53.917 1.00 34.31 O
ATOM 296 CB GLN L 38 -1.327 28.159 51.610 1.00 34.96 C
ATOM 297 CG GLN L 38 -0.032 27.562 52.106 1.00 52.44 C
ATOM 298 CD GLN L 38 0.917 28.616 52.633 1.00 52.32 C
ATOM 299 OE1 GLN L 38 2.101 28.607 52.323 1.00 45.40 O
ATOM 300 NE2 GLN L 38 0.396 29.536 53.439 1.00 49.71 N
ATOM 301 N LYS L 39 -2.735 25.423 53.218 1.00 35.95 N
ATOM 302 CA LYS L 39 -2.974 24.829 54.526 1.00 39.96 C
ATOM 303 C LYS L 39 -1.616 24.806 55.235 1.00 41.96 C
ATOM 304 O LYS L 39 -0.582 24.638 54.595 1.00 40.83 O
ATOM 305 CB LYS L 39 -3.528 23.403 54.359 1.00 39.99 C
ATOM 306 CG LYS L 39 -4.888 23.310 53.639 1.00 27.04 C
ATOM 307 CD LYS L 39 -5.180 21.870 53.208 1.00 53.31 C
ATOM 308 CE LYS L 39 -6.412 21.769 52.325 1.00 38.02 C
ATOM 309 NZ LYS L 39 -7.582 22.038 53.161 1.00 39.33 N
ATOM 310 N PRO L 40 -1.596 24.984 56.558 1.00 43.75 N
ATOM 311 CA PRO L 40 -0.343 24.979 57.317 1.00 49.00 C
ATOM 312 C PRO L 40 0.718 23.921 56.938 1.00 54.30 C
ATOM 313 O PRO L 40 0.397 22.739 56.765 1.00 55.43 O
ATOM 314 CB PRO L 40 -0.834 24.815 58.749 1.00 52.28 C
ATOM 315 CG PRO L 40 -2.076 25.646 58.746 1.00 64.49 C
ATOM 316 CD PRO L 40 -2.747 25.211 57.449 1.00 53.18 C
ATOM 317 N GLY L 41 1.977 24.367 56.816 1.00 56.69 N
ATOM 318 CA GLY L 41 3.096 23.486 56.490 1.00 48.51 C
ATOM 319 C GLY L 41 2.965 22.771 55.168 1.00 43.70 C
ATOM 320 O GLY L 41 3.236 21.588 55.068 1.00 45.80 O
ATOM 321 N ASN L 42 2.561 23.504 54.146 1.00 45.37 N
ATOM 322 CA ASN L 42 2.350 22.949 52.812 1.00 41.79 C
ATOM 323 C ASN L 42 2.551 24.065 51.812 1.00 42.91 C
ATOM 324 O ASN L 42 2.341 25.238 52.124 1.00 41.55 O
ATOM 325 CB ASN L 42 0.902 22.501 52.637 1.00 45.83 C
ATOM 326 CG ASN L 42 0.672 21.078 53.011 1.00 45.71 C
ATOM 327 OD1 ASN L 42 0.706 20.192 52.154 1.00 51.20 O
ATOM 328 ND2 ASN L 42 0.425 20.834 54.294 1.00 61.71 N
ATOM 329 N ALA L 43 2.942 23.705 50.601 1.00 45.94 N
ATOM 330 CA ALA L 43 3.115 24.699 49.554 1.00 44.57 C
ATOM 331 C ALA L 43 1.712 25.184 49.100 1.00 43.37 C
ATOM 332 O ALA L 43 0.716 24.441 49.192 1.00 42.37 O
ATOM 333 CB ALA L 43 3.876 24.069 48.381 1.00 45.26 C
ATOM 334 N PRO L 44 1.604 26.441 48.643 1.00 40.17 N
ATOM 335 CA PRO L 44 0.317 26.986 48.172 1.00 40.78 C
ATOM 336 C PRO L 44 -0.199 26.177 46.990 1.00 38.30 C
ATOM 337 O PRO L 44 0.586 25.658 46.209 1.00 41.24 O
ATOM 338 CB PRO L 44 0.675 28.399 47.719 1.00 34.07 C
ATOM 339 CG PRO L 44 1.851 28.737 48.591 1.00 41.03 C
ATOM 340 CD PRO L 44 2.659 27.462 48.577 1.00 40.11 C
ATOM 341 N ARG L 45 -1.515 26.071 46.863 1.00 39.10 N
ATOM 342 CA ARG L 45 -2.137 25.333 45.777 1.00 35.15 C
ATOM 343 C ARG L 45 -2.785 26.423 44.938 1.00 36.51 C
ATOM 344 O ARG L 45 -3.485 27.276 45.481 1.00 41.39 O
ATOM 345 CB ARG L 45 -3.188 24.378 46.334 1.00 35.03 C
ATOM 346 CG ARG L 45 -3.807 23.430 45.317 1.00 57.64 C
ATOM 347 CD ARG L 45 -4.977 22.681 45.959 1.00 85.11 C
ATOM 348 NE ARG L 45 -5.873 22.069 44.973 1.00102.92 N
ATOM 349 CZ ARG L 45 -7.119 21.662 45.226 1.00103.14 C
ATOM 350 NH1 ARG L 45 -7.646 21.799 46.445 1.00 90.02 N
ATOM 351 NH2 ARG L 45 -7.848 21.119 44.252 1.00102.07 N
ATOM 352 N LEU L 46 -2.543 26.404 43.628 1.00 36.87 N
ATOM 353 CA LEU L 46 -3.110 27.394 42.716 1.00 34.25 C
ATOM 354 C LEU L 46 -4.548 26.961 42.519 1.00 35.47 C
ATOM 355 O LEU L 46 -4.807 25.809 42.183 1.00 34.02 O
ATOM 356 CB LEU L 46 -2.408 27.368 41.354 1.00 34.99 C
ATOM 357 CG LEU L 46 -2.529 28.521 40.343 1.00 29.19 C
ATOM 358 CD1 LEU L 46 -2.514 27.890 38.966 1.00 16.45 C
ATOM 359 CD2 LEU L 46 -3.761 29.385 40.526 1.00 38.66 C
ATOM 360 N LEU L 47 -5.475 27.887 42.743 1.00 39.73 N
ATOM 361 CA LEU L 47 -6.903 27.637 42.589 1.00 36.19 C
ATOM 362 C LEU L 47 -7.429 28.286 41.326 1.00 38.45 C
ATOM 363 O LEU L 47 -7.985 27.618 40.445 1.00 37.71 O
ATOM 364 CB LEU L 47 -7.677 28.196 43.784 1.00 28.35 C
ATOM 365 CG LEU L 47 -7.391 27.454 45.088 1.00 31.96 C
ATOM 366 CD1 LEU L 47 -8.226 28.034 46.196 1.00 27.87 C
ATOM 367 CD2 LEU L 47 -7.687 25.981 44.941 1.00 14.87 C
ATOM 368 N ILE L 48 -7.238 29.593 41.232 1.00 35.87 N
ATOM 369 CA ILE L 48 -7.757 30.321 40.096 1.00 38.68 C
ATOM 370 C ILE L 48 -6.705 31.132 39.415 1.00 40.15 C
ATOM 371 O ILE L 48 -5.824 31.694 40.072 1.00 44.78 O
ATOM 372 CB ILE L 48 -8.869 31.286 40.538 1.00 38.48 C
ATOM 373 CG1 ILE L 48 -10.031 30.485 41.139 1.00 34.05 C
ATOM 374 CG2 ILE L 48 -9.289 32.175 39.377 1.00 23.40 C
ATOM 375 CD1 ILE L 48 -11.142 31.324 41.691 1.00 38.73 C
ATOM 376 N SER L 49 -6.819 31.198 38.098 1.00 35.67 N
ATOM 377 CA SER L 49 -5.913 31.967 37.280 1.00 35.19 C
ATOM 378 C SER L 49 -6.792 32.831 36.400 1.00 36.53 C
ATOM 379 O SER L 49 -7.975 32.538 36.202 1.00 33.58 O
ATOM 380 CB SER L 49 -5.021 31.060 36.421 1.00 35.03 C
ATOM 381 OG SER L 49 -5.724 30.445 35.352 1.00 35.48 O
ATOM 382 N GLY L 50 -6.209 33.906 35.889 1.00 40.79 N
ATOM 383 CA GLY L 50 -6.929 34.811 35.020 1.00 41.52 C
ATOM 384 C GLY L 50 -8.198 35.291 35.671 1.00 41.89 C
ATOM 385 O GLY L 50 -9.225 35.387 35.010 1.00 46.73 O
ATOM 386 N ALA L 51 -8.121 35.570 36.969 1.00 36.89 N
ATOM 387 CA ALA L 51 -9.247 36.053 37.758 1.00 37.02 C
ATOM 388 C ALA L 51 -10.442 35.109 37.880 1.00 39.47 C
ATOM 389 O ALA L 51 -11.046 35.004 38.954 1.00 38.51 O
ATOM 390 CB ALA L 51 -9.702 37.397 37.250 1.00 35.67 C
ATOM 391 N THR L 52 -10.789 34.410 36.807 1.00 41.91 N
ATOM 392 CA THR L 52 -11.941 33.520 36.839 1.00 45.41 C
ATOM 393 C THR L 52 -11.736 32.087 36.393 1.00 48.17 C
ATOM 394 O THR L 52 -12.691 31.318 36.439 1.00 51.50 O
ATOM 395 CB THR L 52 -13.066 34.045 35.954 1.00 45.27 C
ATOM 396 OG1 THR L 52 -12.683 33.888 34.579 1.00 38.25 O
ATOM 397 CG2 THR L 52 -13.351 35.522 36.252 1.00 43.00 C
ATOM 398 N SER L 53 -10.542 31.710 35.941 1.00 50.62 N
ATOM 399 CA SER L 53 -10.342 30.329 35.500 1.00 49.86 C
ATOM 400 C SER L 53 -9.879 29.386 36.608 1.00 49.52 C
ATOM 401 O SER L 53 -8.778 29.523 37.154 1.00 54.34 O
ATOM 402 CB SER L 53 -9.379 30.270 34.312 1.00 51.56 C
ATOM 403 OG SER L 53 -9.863 31.035 33.218 1.00 58.26 O
ATOM 404 N LEU L 54 -10.741 28.430 36.938 1.00 46.19 N
ATOM 405 CA LEU L 54 -10.454 27.436 37.963 1.00 45.60 C
ATOM 406 C LEU L 54 -9.453 26.442 37.443 1.00 45.31 C
ATOM 407 O LEU L 54 -9.426 26.127 36.254 1.00 42.72 O
ATOM 408 CB LEU L 54 -11.705 26.637 38.342 1.00 44.53 C
ATOM 409 CG LEU L 54 -12.797 27.127 39.291 1.00 32.64 C