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3HFM.pdb
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HEADER COMPLEX(ANTIBODY-ANTIGEN) 11-AUG-88 3HFM
TITLE STRUCTURE OF AN ANTIBODY-ANTIGEN COMPLEX. CRYSTAL STRUCTURE
TITLE 2 OF THE HY/HEL-10 FAB-LYSOZYME COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYHEL-10 IGG1 FAB (LIGHT CHAIN);
COMPND 3 CHAIN: L;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HYHEL-10 IGG1 FAB (HEAVY CHAIN);
COMPND 7 CHAIN: H;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HEN EGG WHITE LYSOZYME;
COMPND 11 CHAIN: Y;
COMPND 12 EC: 3.2.1.17;
COMPND 13 ENGINEERED: 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: GALLUS GALLUS;
SOURCE 11 ORGANISM_COMMON: CHICKEN;
SOURCE 12 ORGANISM_TAXID: 9031
KEYWDS COMPLEX(ANTIBODY-ANTIGEN)
EXPDTA X-RAY DIFFRACTION
AUTHOR E.A.PADLAN,D.R.DAVIES
REVDAT 4 24-FEB-09 3HFM 1 VERSN
REVDAT 3 01-APR-03 3HFM 1 JRNL
REVDAT 2 15-JAN-90 3HFM 1 JRNL
REVDAT 1 12-JUL-89 3HFM 0
JRNL AUTH E.A.PADLAN,E.W.SILVERTON,S.SHERIFF,G.H.COHEN,
JRNL AUTH 2 S.J.SMITH-GILL,D.R.DAVIES
JRNL TITL STRUCTURE OF AN ANTIBODY-ANTIGEN COMPLEX: CRYSTAL
JRNL TITL 2 STRUCTURE OF THE HYHEL-10 FAB-LYSOZYME COMPLEX.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 86 5938 1989
JRNL REFN ISSN 0027-8424
JRNL PMID 2762305
JRNL DOI 10.1073/PNAS.86.15.5938
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.J.SMITH-GILL,C.MAINHART,T.B.LAVOIE,R.J.FELDMANN,
REMARK 1 AUTH 2 W.DROHAN,B.R.BROOKS
REMARK 1 TITL A THREE-DIMENSIONAL MODEL OF AN ANTI-LYSOZYME
REMARK 1 TITL 2 ANTIBODY
REMARK 1 REF J.MOL.BIOL. V. 194 713 1987
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.W.SILVERTON,E.A.PADLAN,D.R.DAVIES,S.SMITH-GILL,
REMARK 1 AUTH 2 M.POTTER
REMARK 1 TITL CRYSTALLINE MONOCLONAL ANTIBODY FABS COMPLEXED TO
REMARK 1 TITL 2 HEN EGG WHITE LYSOZYME
REMARK 1 REF J.MOL.BIOL. V. 180 761 1984
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.246
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4296
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 1
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.012 ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3HFM 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 : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 28.73400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.83900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.36700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.83900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.73400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.36700
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 APPLY THE FOLLOWING TO CHAINS: L, H, Y
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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O TYR L 186 OH TYR L 192 1.91
REMARK 500 N ASP L 151 O SER L 191 1.95
REMARK 500 NH1 ARG Y 5 O TRP Y 123 2.09
REMARK 500 O PRO H 147 NE2 HIS H 199 2.13
REMARK 500 O SER H 156 N SER H 158 2.16
REMARK 500 O ILE H 29 N SER H 31 2.18
REMARK 500 ND2 ASN Y 46 OD1 ASP Y 52 2.19
REMARK 500 OG SER Y 36 O ILE Y 55 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 ARG L 24 CD - NE - CZ ANGL. DEV. = 10.5 DEGREES
REMARK 500 ARG L 45 CD - NE - CZ ANGL. DEV. = 28.2 DEGREES
REMARK 500 TYR L 50 CA - CB - CG ANGL. DEV. = -12.9 DEGREES
REMARK 500 ASN L 145 CA - CB - CG ANGL. DEV. = 18.1 DEGREES
REMARK 500 ARG L 155 CD - NE - CZ ANGL. DEV. = 11.4 DEGREES
REMARK 500 ARG L 155 NE - CZ - NH1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASN L 212 CA - CB - CG ANGL. DEV. = 17.7 DEGREES
REMARK 500 GLU L 213 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 ARG H 38 CA - CB - CG ANGL. DEV. = 13.6 DEGREES
REMARK 500 ARG H 38 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG H 38 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG H 44 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 TYR H 94 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500 ASN H 133 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 GLY H 162 N - CA - C ANGL. DEV. = 26.3 DEGREES
REMARK 500 TYR H 175 N - CA - C ANGL. DEV. = 16.2 DEGREES
REMARK 500 LYS H 209 C - N - CA ANGL. DEV. = 17.8 DEGREES
REMARK 500 VAL H 211 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 ARG Y 5 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG Y 14 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 TYR Y 20 N - CA - CB ANGL. DEV. = 11.2 DEGREES
REMARK 500 ARG Y 21 CD - NE - CZ ANGL. DEV. = -8.6 DEGREES
REMARK 500 ARG Y 45 CD - NE - CZ ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG Y 45 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ASN Y 46 CB - CA - C ANGL. DEV. = 12.7 DEGREES
REMARK 500 ASP Y 101 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG Y 114 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG Y 128 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 15 107.74 -26.68
REMARK 500 GLN L 27 159.66 172.31
REMARK 500 ILE L 29 63.16 8.94
REMARK 500 ASN L 31 -15.24 85.38
REMARK 500 ASN L 32 72.32 -104.69
REMARK 500 SER L 40 115.02 -6.36
REMARK 500 HIS L 41 33.97 81.25
REMARK 500 PRO L 44 -177.90 -50.55
REMARK 500 LEU L 47 -66.30 -104.05
REMARK 500 TYR L 50 -72.15 29.73
REMARK 500 ALA L 51 -41.41 -158.14
REMARK 500 SER L 67 140.72 163.42
REMARK 500 SER L 77 60.99 65.73
REMARK 500 SER L 91 15.59 -145.04
REMARK 500 ARG L 108 -157.72 -86.86
REMARK 500 SER L 122 -70.04 -47.62
REMARK 500 ALA L 130 93.61 168.27
REMARK 500 LEU L 136 66.66 -116.94
REMARK 500 TYR L 140 135.37 175.71
REMARK 500 LYS L 142 -40.97 -25.00
REMARK 500 ILE L 144 124.99 160.87
REMARK 500 ASP L 151 -135.55 71.15
REMARK 500 GLU L 154 155.65 -26.90
REMARK 500 ARG L 155 -106.70 -112.33
REMARK 500 GLN L 156 -114.03 172.74
REMARK 500 LEU L 160 84.18 -157.12
REMARK 500 SER L 162 102.29 179.59
REMARK 500 GLN L 166 154.71 -46.30
REMARK 500 SER L 168 18.74 -67.09
REMARK 500 LYS L 169 -91.13 -114.82
REMARK 500 SER L 171 21.49 45.05
REMARK 500 TYR L 173 -137.83 -105.41
REMARK 500 SER L 174 133.75 143.14
REMARK 500 SER L 177 113.27 179.19
REMARK 500 GLU L 187 45.13 -95.69
REMARK 500 ASN L 190 -30.44 -155.76
REMARK 500 CYS L 194 78.58 -114.45
REMARK 500 ARG L 211 98.40 -64.24
REMARK 500 GLU L 213 -160.45 48.94
REMARK 500 GLN H 16 -148.43 -106.91
REMARK 500 THR H 30 -32.80 -12.34
REMARK 500 SER H 31 -24.92 -164.41
REMARK 500 MET H 48 -94.59 -89.89
REMARK 500 SER H 54 -70.47 115.19
REMARK 500 LYS H 64 -114.61 -13.22
REMARK 500 SER H 65 24.04 -142.47
REMARK 500 SER H 68 85.57 177.36
REMARK 500 ASN H 76 -1.60 39.69
REMARK 500 SER H 84 73.69 31.49
REMARK 500 ASP H 89 0.28 -61.75
REMARK 500 ALA H 91 -169.78 -170.20
REMARK 500 ALA H 96 -159.86 -130.32
REMARK 500 TRP H 98 -90.67 32.24
REMARK 500 ASP H 99 -80.66 -71.08
REMARK 500 ALA H 130 -166.14 -79.27
REMARK 500 THR H 132 53.52 -97.44
REMARK 500 ASN H 133 124.20 137.75
REMARK 500 SER H 134 86.17 -66.68
REMARK 500 ASN H 155 77.47 26.82
REMARK 500 SER H 156 100.80 18.12
REMARK 500 SER H 161 97.72 -56.64
REMARK 500 SER H 172 69.90 21.74
REMARK 500 ASP H 173 16.35 99.37
REMARK 500 LEU H 174 121.49 -176.34
REMARK 500 SER H 185 101.23 -59.47
REMARK 500 SER H 186 78.32 47.13
REMARK 500 PRO H 187 43.57 9.71
REMARK 500 ARG H 188 -77.96 -116.32
REMARK 500 GLU H 191 -31.44 -155.43
REMARK 500 THR H 192 120.07 47.94
REMARK 500 ALA H 198 117.77 -177.99
REMARK 500 SER H 203 61.10 73.57
REMARK 500 ILE H 210 74.56 -161.46
REMARK 500 PRO H 212 86.79 -47.67
REMARK 500 ARG Y 5 -73.25 -0.90
REMARK 500 GLU Y 7 -78.83 -41.73
REMARK 500 LYS Y 13 -38.77 -37.57
REMARK 500 LYS Y 33 -80.97 -59.35
REMARK 500 SER Y 36 -0.64 -167.99
REMARK 500 ALA Y 42 147.41 -34.59
REMARK 500 ASP Y 48 12.72 -58.84
REMARK 500 GLN Y 57 78.57 42.71
REMARK 500 ARG Y 61 -86.16 -87.77
REMARK 500 ARG Y 68 6.07 -154.23
REMARK 500 SER Y 72 111.01 -1.50
REMARK 500 ASN Y 77 18.47 36.26
REMARK 500 ALA Y 82 -24.91 -31.38
REMARK 500 SER Y 85 167.92 -34.49
REMARK 500 LYS Y 96 -31.91 -35.96
REMARK 500 VAL Y 99 -4.80 -46.85
REMARK 500 CYS Y 115 -67.75 -90.68
REMARK 500 LYS Y 116 134.18 -23.47
REMARK 500 TRP Y 123 -37.19 -39.23
REMARK 500 ARG Y 128 66.93 -109.83
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3HFM Y 1 129 UNP P00698 LYSC_CHICK 19 147
DBREF 3HFM L 1 214 PDB 3HFM 3HFM 1 214
DBREF 3HFM H 1 215 PDB 3HFM 3HFM 1 215
SEQRES 1 L 214 ASP ILE VAL LEU THR GLN SER PRO ALA THR LEU SER VAL
SEQRES 2 L 214 THR PRO GLY ASN SER VAL SER LEU SER CYS ARG ALA SER
SEQRES 3 L 214 GLN SER ILE GLY ASN ASN LEU HIS TRP TYR GLN GLN LYS
SEQRES 4 L 214 SER HIS GLU SER PRO ARG LEU LEU ILE LYS TYR ALA SER
SEQRES 5 L 214 GLN SER ILE SER GLY ILE PRO SER ARG PHE SER GLY SER
SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU SER ILE ASN SER VAL
SEQRES 7 L 214 GLU THR GLU ASP PHE GLY MET TYR PHE CYS GLN GLN SER
SEQRES 8 L 214 ASN SER TRP PRO TYR THR PHE GLY GLY GLY THR LYS LEU
SEQRES 9 L 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS
SEQRES 1 H 215 ASP VAL GLN LEU GLN GLU SER GLY PRO SER LEU VAL LYS
SEQRES 2 H 215 PRO SER GLN THR LEU SER LEU THR CYS SER VAL THR GLY
SEQRES 3 H 215 ASP SER ILE THR SER ASP TYR TRP SER TRP ILE ARG LYS
SEQRES 4 H 215 PHE PRO GLY ASN ARG LEU GLU TYR MET GLY TYR VAL SER
SEQRES 5 H 215 TYR SER GLY SER THR TYR TYR ASN PRO SER LEU LYS SER
SEQRES 6 H 215 ARG ILE SER ILE THR ARG ASP THR SER LYS ASN GLN TYR
SEQRES 7 H 215 TYR LEU ASP LEU ASN SER VAL THR THR GLU ASP THR ALA
SEQRES 8 H 215 THR TYR TYR CYS ALA ASN TRP ASP GLY ASP TYR TRP GLY
SEQRES 9 H 215 GLN GLY THR LEU VAL THR VAL SER ALA ALA LYS THR THR
SEQRES 10 H 215 PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SER ALA ALA
SEQRES 11 H 215 GLN THR ASN SER MET VAL THR LEU GLY CYS LEU VAL LYS
SEQRES 12 H 215 GLY TYR PHE PRO GLU PRO VAL THR VAL THR TRP ASN SER
SEQRES 13 H 215 GLY SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL
SEQRES 14 H 215 LEU GLN SER ASP LEU TYR THR LEU SER SER SER VAL THR
SEQRES 15 H 215 VAL PRO SER SER PRO ARG PRO SER GLU THR VAL THR CYS
SEQRES 16 H 215 ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS
SEQRES 17 H 215 LYS ILE VAL PRO ARG ASP CYS
SEQRES 1 Y 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 Y 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 Y 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 Y 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 Y 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 Y 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 Y 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 Y 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 Y 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 Y 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
FORMUL 4 HOH *(H2 O)
HELIX 1 1 GLU L 79 PHE L 83 5 5
HELIX 2 2 SER L 121 GLY L 128 1 8
HELIX 3 3 THR L 182 TYR L 186 5 5
HELIX 4 4 THR H 86 THR H 90 5 5
HELIX 5 5 ARG Y 5 ARG Y 14 1 10
HELIX 6 6 LEU Y 25 ASN Y 37 1 13
HELIX 7 7 CYS Y 80 SER Y 85 1 6
HELIX 8 8 ILE Y 88 VAL Y 99 1 12
HELIX 9 9 ASN Y 103 ALA Y 107 5 5
HELIX 10 10 TRP Y 108 ARG Y 114 1 7
HELIX 11 11 ASP Y 119 ARG Y 125 5 7
SHEET 1 A 4 LEU L 4 SER L 7 0
SHEET 2 A 4 LEU L 21 ALA L 25 -1 N SER L 22 O SER L 7
SHEET 3 A 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23
SHEET 4 A 4 PHE L 62 GLY L 66 -1 O SER L 63 N SER L 74
SHEET 1 B 6 THR L 10 VAL L 13 0
SHEET 2 B 6 LYS L 103 ILE L 106 1 O LYS L 103 N LEU L 11
SHEET 3 B 6 GLY L 84 GLN L 90 -1 O GLY L 84 N LEU L 104
SHEET 4 B 6 LEU L 33 GLN L 38 -1 N HIS L 34 O GLN L 89
SHEET 5 B 6 ARG L 45 LYS L 49 -1 O ARG L 45 N GLN L 37
SHEET 6 B 6 GLN L 53 SER L 54 -1 O GLN L 53 N LYS L 49
SHEET 1 C 4 THR L 114 PHE L 118 0
SHEET 2 C 4 SER L 131 ASN L 137 -1 N VAL L 133 O PHE L 118
SHEET 3 C 4 SER L 174 THR L 180 -1 O MET L 175 N LEU L 136
SHEET 4 C 4 VAL L 159 TRP L 163 -1 O LEU L 160 N THR L 178
SHEET 1 D 3 ASN L 145 ILE L 150 0
SHEET 2 D 3 SER L 191 THR L 197 -1 N THR L 193 O LYS L 149
SHEET 3 D 3 ILE L 205 ASN L 210 -1 N ILE L 205 O ALA L 196
SHEET 1 E 4 GLN H 3 SER H 7 0
SHEET 2 E 4 LEU H 18 THR H 25 -1 O THR H 21 N SER H 7
SHEET 3 E 4 GLN H 77 LEU H 82 -1 O TYR H 78 N CYS H 22
SHEET 4 E 4 THR H 70 ASP H 72 -1 O THR H 70 N TYR H 79
SHEET 1 F 6 LEU H 11 VAL H 12 0
SHEET 2 F 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12
SHEET 3 F 6 ALA H 91 ASN H 97 -1 O ALA H 91 N VAL H 109
SHEET 4 F 6 TRP H 34 LYS H 39 -1 N SER H 35 O ALA H 96
SHEET 5 F 6 LEU H 45 SER H 52 -1 O GLU H 46 N ARG H 38
SHEET 6 F 6 SER H 56 TYR H 59 -1 O SER H 56 N SER H 52
SHEET 1 G 4 SER H 120 LEU H 124 0
SHEET 2 G 4 MET H 135 TYR H 145 -1 O GLY H 139 N LEU H 124
SHEET 3 G 4 TYR H 175 PRO H 184 -1 O TYR H 175 N TYR H 145
SHEET 4 G 4 VAL H 163 THR H 165 -1 N HIS H 164 O SER H 180
SHEET 1 H 4 SER H 120 LEU H 124 0
SHEET 2 H 4 MET H 135 TYR H 145 -1 O GLY H 139 N LEU H 124
SHEET 3 H 4 TYR H 175 PRO H 184 -1 O TYR H 175 N TYR H 145
SHEET 4 H 4 VAL H 169 LEU H 170 -1 N VAL H 169 O THR H 176
SHEET 1 I 3 THR H 153 TRP H 154 0
SHEET 2 I 3 VAL H 193 ASN H 196 -1 N ASN H 196 O THR H 153
SHEET 3 I 3 ASP H 207 ILE H 210 -1 N LYS H 208 O CYS H 195
SHEET 1 J 3 ARG Y 45 ASN Y 46 0
SHEET 2 J 3 SER Y 50 TYR Y 53 -1 O SER Y 50 N ASN Y 46
SHEET 3 J 3 ILE Y 58 ASN Y 59 -1 N ILE Y 58 O TYR Y 53
SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.03
SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.01
SSBOND 3 CYS H 22 CYS H 95 1555 1555 2.02
SSBOND 4 CYS H 140 CYS H 195 1555 1555 2.03
SSBOND 5 CYS Y 6 CYS Y 127 1555 1555 2.04
SSBOND 6 CYS Y 30 CYS Y 115 1555 1555 2.02
SSBOND 7 CYS Y 64 CYS Y 80 1555 1555 2.05
SSBOND 8 CYS Y 76 CYS Y 94 1555 1555 2.02
SSBOND 9 CYS L 214 CYS H 215 1555 1555 2.06
CISPEP 1 SER L 7 PRO L 8 0 -0.39
CISPEP 2 TRP L 94 PRO L 95 0 0.95
CISPEP 3 TYR L 140 PRO L 141 0 1.33
CISPEP 4 PHE H 146 PRO H 147 0 -1.19
CISPEP 5 GLU H 148 PRO H 149 0 -1.27
CISPEP 6 SER H 186 PRO H 187 0 0.64
CRYST1 57.468 118.734 137.678 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 0.017401 0.000000 0.000000 0.00000
ORIGX2 0.000000 0.008422 0.000000 0.00000
ORIGX3 0.000000 0.000000 0.007263 0.00000
SCALE1 0.017401 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008422 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007263 0.00000
ATOM 1 N ASP L 1 9.718 19.693 42.129 1.00 17.12 N
ATOM 2 CA ASP L 1 9.822 19.540 43.611 1.00 17.22 C
ATOM 3 C ASP L 1 8.785 20.459 44.250 1.00 17.48 C
ATOM 4 O ASP L 1 7.582 20.251 43.934 1.00 17.85 O
ATOM 5 CB ASP L 1 11.270 19.694 43.974 1.00 16.97 C
ATOM 6 CG ASP L 1 12.090 20.763 43.302 1.00 17.07 C
ATOM 7 OD1 ASP L 1 11.684 21.923 43.122 1.00 16.76 O
ATOM 8 OD2 ASP L 1 13.242 20.408 42.935 1.00 16.88 O
ATOM 9 N ILE L 2 9.156 21.411 45.084 1.00 17.23 N
ATOM 10 CA ILE L 2 8.185 22.322 45.717 1.00 16.97 C
ATOM 11 C ILE L 2 8.644 23.772 45.576 1.00 16.85 C
ATOM 12 O ILE L 2 9.803 24.075 45.917 1.00 17.12 O
ATOM 13 CB ILE L 2 7.917 21.969 47.222 1.00 16.96 C
ATOM 14 CG1 ILE L 2 6.989 23.059 47.818 1.00 16.46 C
ATOM 15 CG2 ILE L 2 9.221 21.781 48.040 1.00 17.24 C
ATOM 16 CD1 ILE L 2 7.191 23.372 49.312 1.00 15.57 C
ATOM 17 N VAL L 3 7.750 24.625 45.101 1.00 16.35 N
ATOM 18 CA VAL L 3 8.059 26.040 44.900 1.00 15.78 C
ATOM 19 C VAL L 3 7.499 27.010 45.927 1.00 15.40 C
ATOM 20 O VAL L 3 6.475 26.814 46.568 1.00 15.49 O
ATOM 21 CB VAL L 3 7.585 26.454 43.483 1.00 16.01 C
ATOM 22 CG1 VAL L 3 8.194 25.566 42.412 1.00 16.28 C
ATOM 23 CG2 VAL L 3 6.071 26.512 43.404 1.00 15.88 C
ATOM 24 N LEU L 4 8.255 28.084 46.020 1.00 14.92 N
ATOM 25 CA LEU L 4 8.071 29.244 46.882 1.00 14.36 C
ATOM 26 C LEU L 4 8.083 30.473 45.968 1.00 14.17 C
ATOM 27 O LEU L 4 9.064 30.624 45.223 1.00 14.17 O
ATOM 28 CB LEU L 4 9.189 29.239 47.911 1.00 13.58 C
ATOM 29 CG LEU L 4 9.177 28.338 49.117 1.00 13.24 C
ATOM 30 CD1 LEU L 4 8.679 26.932 48.834 1.00 13.20 C
ATOM 31 CD2 LEU L 4 10.621 28.215 49.632 1.00 13.26 C
ATOM 32 N THR L 5 7.052 31.277 46.044 1.00 14.18 N
ATOM 33 CA THR L 5 6.917 32.484 45.220 1.00 14.26 C
ATOM 34 C THR L 5 7.073 33.831 45.895 1.00 14.26 C
ATOM 35 O THR L 5 6.110 34.442 46.406 1.00 14.30 O
ATOM 36 CB THR L 5 5.507 32.382 44.477 1.00 14.25 C
ATOM 37 OG1 THR L 5 5.673 31.284 43.528 1.00 14.19 O
ATOM 38 CG2 THR L 5 5.038 33.667 43.806 1.00 14.46 C
ATOM 39 N GLN L 6 8.301 34.327 45.883 1.00 14.20 N
ATOM 40 CA GLN L 6 8.659 35.602 46.481 1.00 14.40 C
ATOM 41 C GLN L 6 8.197 36.838 45.719 1.00 14.68 C
ATOM 42 O GLN L 6 8.581 37.125 44.588 1.00 14.72 O
ATOM 43 CB GLN L 6 10.170 35.732 46.714 1.00 14.77 C
ATOM 44 CG GLN L 6 10.510 35.687 48.201 1.00 15.61 C
ATOM 45 CD GLN L 6 12.016 35.643 48.372 1.00 16.33 C
ATOM 46 OE1 GLN L 6 12.729 35.302 47.427 1.00 16.39 O
ATOM 47 NE2 GLN L 6 12.477 35.988 49.568 1.00 16.80 N
ATOM 48 N SER L 7 7.366 37.562 46.426 1.00 14.93 N
ATOM 49 CA SER L 7 6.718 38.811 46.071 1.00 15.10 C
ATOM 50 C SER L 7 7.041 39.815 47.189 1.00 15.25 C
ATOM 51 O SER L 7 6.958 39.420 48.370 1.00 15.17 O
ATOM 52 CB SER L 7 5.212 38.660 45.956 1.00 15.41 C
ATOM 53 OG SER L 7 4.542 39.777 46.530 1.00 16.00 O
ATOM 54 N PRO L 8 7.386 41.038 46.856 1.00 15.34 N
ATOM 55 CA PRO L 8 7.520 41.604 45.518 1.00 15.32 C
ATOM 56 C PRO L 8 8.932 41.399 44.992 1.00 15.33 C
ATOM 57 O PRO L 8 9.824 41.014 45.775 1.00 15.22 O
ATOM 58 CB PRO L 8 7.166 43.067 45.744 1.00 15.31 C
ATOM 59 CG PRO L 8 7.709 43.363 47.113 1.00 15.32 C
ATOM 60 CD PRO L 8 7.705 42.050 47.879 1.00 15.36 C
ATOM 61 N ALA L 9 9.106 41.653 43.707 1.00 15.37 N
ATOM 62 CA ALA L 9 10.411 41.496 43.034 1.00 15.34 C
ATOM 63 C ALA L 9 11.450 42.412 43.670 1.00 15.30 C
ATOM 64 O ALA L 9 12.433 41.868 44.228 1.00 15.47 O
ATOM 65 CB ALA L 9 10.276 41.683 41.533 1.00 15.34 C
ATOM 66 N THR L 10 11.245 43.717 43.593 1.00 14.92 N
ATOM 67 CA THR L 10 12.176 44.677 44.185 1.00 14.74 C
ATOM 68 C THR L 10 11.397 45.582 45.153 1.00 14.77 C
ATOM 69 O THR L 10 10.160 45.597 45.171 1.00 14.91 O
ATOM 70 CB THR L 10 12.991 45.587 43.202 1.00 14.61 C
ATOM 71 OG1 THR L 10 12.038 46.033 42.186 1.00 15.00 O
ATOM 72 CG2 THR L 10 14.231 44.934 42.595 1.00 14.74 C
ATOM 73 N LEU L 11 12.182 46.303 45.920 1.00 14.70 N
ATOM 74 CA LEU L 11 11.693 47.245 46.917 1.00 14.79 C
ATOM 75 C LEU L 11 12.765 48.310 47.151 1.00 15.06 C
ATOM 76 O LEU L 11 13.884 47.997 47.569 1.00 15.16 O
ATOM 77 CB LEU L 11 11.281 46.519 48.194 1.00 14.36 C
ATOM 78 CG LEU L 11 9.835 46.045 48.229 1.00 14.18 C
ATOM 79 CD1 LEU L 11 9.413 45.638 49.627 1.00 14.14 C
ATOM 80 CD2 LEU L 11 8.964 47.192 47.726 1.00 14.60 C
ATOM 81 N SER L 12 12.344 49.518 46.853 1.00 15.25 N
ATOM 82 CA SER L 12 13.219 50.704 47.017 1.00 15.41 C
ATOM 83 C SER L 12 12.660 51.395 48.263 1.00 15.33 C
ATOM 84 O SER L 12 11.548 51.953 48.123 1.00 15.42 O
ATOM 85 CB SER L 12 13.191 51.552 45.771 1.00 15.96 C
ATOM 86 OG SER L 12 14.462 51.861 45.222 1.00 16.15 O
ATOM 87 N VAL L 13 13.342 51.358 49.404 1.00 15.20 N
ATOM 88 CA VAL L 13 12.773 52.030 50.588 1.00 15.14 C
ATOM 89 C VAL L 13 13.733 52.955 51.346 1.00 14.84 C
ATOM 90 O VAL L 13 14.929 52.850 51.549 1.00 14.89 O
ATOM 91 CB VAL L 13 12.064 51.057 51.562 1.00 15.28 C
ATOM 92 CG1 VAL L 13 10.874 50.368 50.900 1.00 15.34 C
ATOM 93 CG2 VAL L 13 13.015 50.078 52.210 1.00 15.22 C
ATOM 94 N THR L 14 13.057 53.972 51.807 1.00 14.43 N
ATOM 95 CA THR L 14 13.392 55.144 52.560 1.00 14.16 C
ATOM 96 C THR L 14 13.711 54.981 54.030 1.00 13.70 C
ATOM 97 O THR L 14 12.854 54.861 54.924 1.00 13.48 O
ATOM 98 CB THR L 14 12.140 56.120 52.316 1.00 14.58 C
ATOM 99 OG1 THR L 14 12.195 57.138 53.335 1.00 15.14 O
ATOM 100 CG2 THR L 14 10.825 55.325 52.269 1.00 14.27 C
ATOM 101 N PRO L 15 15.011 54.990 54.293 1.00 13.43 N
ATOM 102 CA PRO L 15 15.562 54.846 55.634 1.00 13.51 C
ATOM 103 C PRO L 15 14.652 55.303 56.749 1.00 13.91 C
ATOM 104 O PRO L 15 14.418 56.497 56.982 1.00 14.06 O
ATOM 105 CB PRO L 15 16.876 55.613 55.531 1.00 13.39 C
ATOM 106 CG PRO L 15 17.361 55.265 54.146 1.00 13.31 C
ATOM 107 CD PRO L 15 16.102 55.125 53.308 1.00 13.36 C
ATOM 108 N GLY L 16 14.138 54.310 57.464 1.00 14.26 N
ATOM 109 CA GLY L 16 13.248 54.462 58.601 1.00 14.59 C
ATOM 110 C GLY L 16 11.853 53.903 58.410 1.00 14.85 C
ATOM 111 O GLY L 16 11.079 53.771 59.381 1.00 14.96 O
ATOM 112 N ASN L 17 11.538 53.582 57.178 1.00 15.01 N
ATOM 113 CA ASN L 17 10.222 53.024 56.809 1.00 15.31 C
ATOM 114 C ASN L 17 10.207 51.528 57.123 1.00 15.56 C
ATOM 115 O ASN L 17 11.253 50.888 57.343 1.00 15.55 O
ATOM 116 CB ASN L 17 9.996 53.357 55.338 1.00 15.75 C
ATOM 117 CG ASN L 17 8.733 54.107 55.005 1.00 16.10 C
ATOM 118 OD1 ASN L 17 8.489 54.426 53.824 1.00 16.49 O
ATOM 119 ND2 ASN L 17 7.913 54.409 56.009 1.00 16.24 N
ATOM 120 N SER L 18 9.010 50.971 57.142 1.00 15.73 N
ATOM 121 CA SER L 18 8.829 49.535 57.413 1.00 15.87 C
ATOM 122 C SER L 18 8.383 48.909 56.087 1.00 15.95 C
ATOM 123 O SER L 18 7.587 49.516 55.370 1.00 16.09 O
ATOM 124 CB SER L 18 7.888 49.197 58.534 1.00 16.02 C
ATOM 125 OG SER L 18 8.616 48.764 59.674 1.00 16.17 O
ATOM 126 N VAL L 19 8.931 47.744 55.866 1.00 15.95 N
ATOM 127 CA VAL L 19 8.677 46.944 54.651 1.00 15.75 C
ATOM 128 C VAL L 19 8.231 45.555 55.060 1.00 15.47 C
ATOM 129 O VAL L 19 8.136 45.304 56.279 1.00 15.41 O
ATOM 130 CB VAL L 19 9.999 47.052 53.855 1.00 16.02 C
ATOM 131 CG1 VAL L 19 10.953 45.899 54.152 1.00 16.16 C
ATOM 132 CG2 VAL L 19 9.759 47.249 52.378 1.00 16.17 C
ATOM 133 N SER L 20 7.964 44.695 54.099 1.00 15.34 N
ATOM 134 CA SER L 20 7.528 43.312 54.383 1.00 15.38 C
ATOM 135 C SER L 20 7.564 42.501 53.082 1.00 15.27 C
ATOM 136 O SER L 20 6.964 42.871 52.064 1.00 15.29 O
ATOM 137 CB SER L 20 6.170 43.245 55.044 1.00 15.59 C
ATOM 138 OG SER L 20 5.137 43.280 54.070 1.00 16.74 O
ATOM 139 N LEU L 21 8.290 41.405 53.175 1.00 15.05 N
ATOM 140 CA LEU L 21 8.475 40.482 52.042 1.00 15.14 C
ATOM 141 C LEU L 21 7.643 39.236 52.287 1.00 15.53 C
ATOM 142 O LEU L 21 7.551 38.793 53.453 1.00 15.72 O
ATOM 143 CB LEU L 21 9.991 40.285 51.947 1.00 14.53 C
ATOM 144 CG LEU L 21 10.823 41.423 52.527 1.00 14.24 C
ATOM 145 CD1 LEU L 21 12.256 40.999 52.794 1.00 14.02 C
ATOM 146 CD2 LEU L 21 10.806 42.585 51.536 1.00 14.23 C
ATOM 147 N SER L 22 7.066 38.707 51.220 1.00 15.70 N
ATOM 148 CA SER L 22 6.222 37.496 51.295 1.00 15.72 C
ATOM 149 C SER L 22 6.915 36.348 50.559 1.00 15.70 C
ATOM 150 O SER L 22 7.805 36.614 49.728 1.00 16.03 O
ATOM 151 CB SER L 22 4.843 37.729 50.718 1.00 15.94 C
ATOM 152 OG SER L 22 4.372 39.037 51.004 1.00 16.80 O
ATOM 153 N CYS L 23 6.493 35.142 50.879 1.00 15.27 N
ATOM 154 CA CYS L 23 7.043 33.906 50.284 1.00 14.92 C
ATOM 155 C CYS L 23 5.988 32.807 50.368 1.00 15.02 C
ATOM 156 O CYS L 23 5.743 32.293 51.472 1.00 15.07 O
ATOM 157 CB CYS L 23 8.324 33.547 51.007 1.00 13.95 C
ATOM 158 SG CYS L 23 9.014 31.905 50.740 1.00 12.78 S
ATOM 159 N ARG L 24 5.399 32.482 49.231 1.00 15.25 N
ATOM 160 CA ARG L 24 4.356 31.470 49.125 1.00 15.41 C
ATOM 161 C ARG L 24 4.769 30.130 48.541 1.00 15.15 C
ATOM 162 O ARG L 24 5.027 29.953 47.343 1.00 15.03 O
ATOM 163 CB ARG L 24 3.139 31.983 48.297 1.00 16.89 C
ATOM 164 CG ARG L 24 2.226 30.870 47.822 1.00 18.35 C
ATOM 165 CD ARG L 24 0.793 31.203 47.565 1.00 19.23 C
ATOM 166 NE ARG L 24 0.074 30.025 47.098 1.00 20.14 N
ATOM 167 CZ ARG L 24 -1.132 29.822 46.603 1.00 20.28 C
ATOM 168 NH1 ARG L 24 -1.485 28.604 46.154 1.00 20.24 N
ATOM 169 NH2 ARG L 24 -2.048 30.791 46.523 1.00 20.15 N
ATOM 170 N ALA L 25 4.793 29.193 49.470 1.00 15.01 N
ATOM 171 CA ALA L 25 5.149 27.800 49.157 1.00 15.17 C
ATOM 172 C ALA L 25 3.872 27.113 48.665 1.00 15.29 C
ATOM 173 O ALA L 25 2.799 27.292 49.265 1.00 15.23 O
ATOM 174 CB ALA L 25 5.763 27.145 50.368 1.00 15.10 C
ATOM 175 N SER L 26 4.015 26.363 47.594 1.00 15.44 N
ATOM 176 CA SER L 26 2.923 25.609 46.962 1.00 15.64 C
ATOM 177 C SER L 26 2.902 24.260 47.689 1.00 15.97 C
ATOM 178 O SER L 26 3.179 23.228 47.068 1.00 16.18 O
ATOM 179 CB SER L 26 3.153 25.357 45.490 1.00 15.55 C
ATOM 180 OG SER L 26 4.362 24.644 45.270 1.00 15.41 O
ATOM 181 N GLN L 27 2.597 24.337 48.958 1.00 16.13 N
ATOM 182 CA GLN L 27 2.545 23.183 49.845 1.00 16.25 C
ATOM 183 C GLN L 27 2.346 23.679 51.285 1.00 16.04 C
ATOM 184 O GLN L 27 2.630 24.826 51.631 1.00 15.92 O
ATOM 185 CB GLN L 27 3.830 22.360 49.831 1.00 17.26 C
ATOM 186 CG GLN L 27 3.981 21.316 48.764 1.00 18.26 C
ATOM 187 CD GLN L 27 2.828 20.342 48.705 1.00 18.72 C
ATOM 188 OE1 GLN L 27 1.746 20.618 48.197 1.00 18.79 O
ATOM 189 NE2 GLN L 27 3.115 19.160 49.257 1.00 19.32 N
ATOM 190 N SER L 28 1.869 22.739 52.071 1.00 15.89 N
ATOM 191 CA SER L 28 1.605 23.030 53.482 1.00 15.74 C
ATOM 192 C SER L 28 2.901 23.351 54.198 1.00 15.60 C
ATOM 193 O SER L 28 2.877 24.241 55.068 1.00 15.75 O
ATOM 194 CB SER L 28 0.835 21.871 54.095 1.00 16.17 C
ATOM 195 OG SER L 28 -0.274 22.335 54.851 1.00 16.69 O
ATOM 196 N ILE L 29 3.977 22.672 53.865 1.00 15.32 N
ATOM 197 CA ILE L 29 5.286 22.885 54.505 1.00 15.00 C
ATOM 198 C ILE L 29 5.170 23.807 55.716 1.00 14.64 C
ATOM 199 O ILE L 29 5.757 24.900 55.718 1.00 14.80 O
ATOM 200 CB ILE L 29 6.359 23.407 53.492 1.00 14.80 C
ATOM 201 CG1 ILE L 29 5.969 24.821 52.994 1.00 14.46 C
ATOM 202 CG2 ILE L 29 6.579 22.410 52.329 1.00 14.90 C
ATOM 203 CD1 ILE L 29 7.129 25.845 53.203 1.00 14.20 C
ATOM 204 N GLY L 30 4.441 23.391 56.726 1.00 14.17 N
ATOM 205 CA GLY L 30 4.200 24.126 57.931 1.00 13.95 C
ATOM 206 C GLY L 30 5.299 24.503 58.870 1.00 13.88 C
ATOM 207 O GLY L 30 5.834 23.636 59.590 1.00 14.13 O
ATOM 208 N ASN L 31 5.662 25.781 58.906 1.00 13.65 N
ATOM 209 CA ASN L 31 6.713 26.227 59.838 1.00 13.54 C
ATOM 210 C ASN L 31 8.156 26.129 59.451 1.00 13.48 C
ATOM 211 O ASN L 31 8.949 26.788 60.169 1.00 13.43 O
ATOM 212 CB ASN L 31 6.396 25.388 61.110 1.00 14.18 C
ATOM 213 CG ASN L 31 7.521 25.185 62.075 1.00 14.80 C
ATOM 214 OD1 ASN L 31 8.508 24.477 61.811 1.00 15.84 O
ATOM 215 ND2 ASN L 31 7.424 25.797 63.256 1.00 15.30 N
ATOM 216 N ASN L 32 8.541 25.394 58.436 1.00 13.50 N
ATOM 217 CA ASN L 32 9.970 25.292 58.073 1.00 13.57 C
ATOM 218 C ASN L 32 10.264 26.123 56.828 1.00 13.42 C
ATOM 219 O ASN L 32 10.486 25.541 55.755 1.00 13.79 O
ATOM 220 CB ASN L 32 10.390 23.830 57.895 1.00 14.27 C
ATOM 221 CG ASN L 32 9.382 22.866 58.494 1.00 15.09 C
ATOM 222 OD1 ASN L 32 8.276 22.742 57.927 1.00 15.74 O
ATOM 223 ND2 ASN L 32 9.735 22.204 59.593 1.00 14.91 N
ATOM 224 N LEU L 33 10.253 27.411 57.017 1.00 12.74 N
ATOM 225 CA LEU L 33 10.526 28.401 55.947 1.00 12.29 C
ATOM 226 C LEU L 33 11.590 29.260 56.624 1.00 12.12 C
ATOM 227 O LEU L 33 11.257 29.816 57.683 1.00 12.16 O
ATOM 228 CB LEU L 33 9.226 29.032 55.530 1.00 11.86 C
ATOM 229 CG LEU L 33 9.218 30.242 54.625 1.00 11.73 C
ATOM 230 CD1 LEU L 33 9.643 31.495 55.382 1.00 11.86 C
ATOM 231 CD2 LEU L 33 10.171 30.010 53.458 1.00 11.58 C
ATOM 232 N HIS L 34 12.780 29.326 56.069 1.00 12.00 N
ATOM 233 CA HIS L 34 13.814 30.143 56.743 1.00 11.82 C
ATOM 234 C HIS L 34 14.326 31.125 55.689 1.00 11.53 C
ATOM 235 O HIS L 34 14.399 30.790 54.507 1.00 11.48 O
ATOM 236 CB HIS L 34 14.971 29.422 57.417 1.00 12.54 C
ATOM 237 CG HIS L 34 14.849 27.945 57.570 1.00 13.16 C
ATOM 238 ND1 HIS L 34 15.876 27.164 58.062 1.00 13.58 N
ATOM 239 CD2 HIS L 34 13.845 27.084 57.291 1.00 13.07 C
ATOM 240 CE1 HIS L 34 15.493 25.899 58.078 1.00 13.55 C
ATOM 241 NE2 HIS L 34 14.265 25.832 57.611 1.00 13.29 N
ATOM 242 N TRP L 35 14.633 32.277 56.230 1.00 11.21 N
ATOM 243 CA TRP L 35 15.128 33.424 55.520 1.00 11.11 C
ATOM 244 C TRP L 35 16.611 33.709 55.654 1.00 11.36 C
ATOM 245 O TRP L 35 17.165 33.635 56.755 1.00 11.52 O
ATOM 246 CB TRP L 35 14.436 34.674 56.113 1.00 10.68 C
ATOM 247 CG TRP L 35 12.963 34.685 55.988 1.00 10.28 C
ATOM 248 CD1 TRP L 35 12.017 34.312 56.893 1.00 10.12 C
ATOM 249 CD2 TRP L 35 12.250 35.119 54.819 1.00 10.24 C
ATOM 250 NE1 TRP L 35 10.759 34.482 56.368 1.00 10.00 N
ATOM 251 CE2 TRP L 35 10.876 34.973 55.101 1.00 10.24 C
ATOM 252 CE3 TRP L 35 12.662 35.607 53.587 1.00 10.28 C
ATOM 253 CZ2 TRP L 35 9.899 35.307 54.178 1.00 10.66 C
ATOM 254 CZ3 TRP L 35 11.695 35.936 52.670 1.00 10.84 C
ATOM 255 CH2 TRP L 35 10.338 35.791 52.955 1.00 11.01 C
ATOM 256 N TYR L 36 17.190 34.056 54.530 1.00 11.76 N
ATOM 257 CA TYR L 36 18.623 34.391 54.493 1.00 12.27 C
ATOM 258 C TYR L 36 18.693 35.799 53.872 1.00 12.64 C
ATOM 259 O TYR L 36 17.673 36.316 53.409 1.00 12.59 O
ATOM 260 CB TYR L 36 19.471 33.402 53.751 1.00 12.34 C
ATOM 261 CG TYR L 36 19.508 31.941 54.045 1.00 12.18 C
ATOM 262 CD1 TYR L 36 18.413 31.113 53.774 1.00 12.30 C
ATOM 263 CD2 TYR L 36 20.647 31.342 54.588 1.00 12.31 C
ATOM 264 CE1 TYR L 36 18.440 29.748 54.034 1.00 12.11 C
ATOM 265 CE2 TYR L 36 20.697 29.976 54.858 1.00 12.41 C
ATOM 266 CZ TYR L 36 19.592 29.182 54.581 1.00 12.30 C
ATOM 267 OH TYR L 36 19.662 27.847 54.850 1.00 11.74 O
ATOM 268 N GLN L 37 19.879 36.337 53.898 1.00 13.13 N
ATOM 269 CA GLN L 37 20.176 37.670 53.350 1.00 13.78 C
ATOM 270 C GLN L 37 21.510 37.505 52.612 1.00 14.19 C
ATOM 271 O GLN L 37 22.414 36.868 53.186 1.00 14.28 O
ATOM 272 CB GLN L 37 20.217 38.752 54.398 1.00 14.26 C
ATOM 273 CG GLN L 37 20.988 40.026 54.062 1.00 14.97 C
ATOM 274 CD GLN L 37 21.183 40.809 55.347 1.00 15.69 C
ATOM 275 OE1 GLN L 37 20.513 40.472 56.327 1.00 16.86 O
ATOM 276 NE2 GLN L 37 22.044 41.807 55.399 1.00 15.98 N
ATOM 277 N GLN L 38 21.576 38.051 51.417 1.00 14.45 N
ATOM 278 CA GLN L 38 22.814 37.964 50.619 1.00 14.69 C
ATOM 279 C GLN L 38 23.164 39.384 50.155 1.00 14.98 C
ATOM 280 O GLN L 38 22.679 39.855 49.118 1.00 14.98 O
ATOM 281 CB GLN L 38 22.752 36.984 49.457 1.00 14.41 C
ATOM 282 CG GLN L 38 24.111 36.790 48.799 1.00 14.07 C
ATOM 283 CD GLN L 38 24.087 35.828 47.641 1.00 14.15 C
ATOM 284 OE1 GLN L 38 23.043 35.520 47.072 1.00 14.07 O
ATOM 285 NE2 GLN L 38 25.269 35.332 47.277 1.00 14.13 N
ATOM 286 N LYS L 39 24.004 40.024 50.944 1.00 15.37 N
ATOM 287 CA LYS L 39 24.464 41.386 50.682 1.00 16.06 C
ATOM 288 C LYS L 39 25.658 41.487 49.746 1.00 16.76 C
ATOM 289 O LYS L 39 26.755 40.996 50.045 1.00 16.87 O
ATOM 290 CB LYS L 39 24.852 42.079 51.994 1.00 15.72 C
ATOM 291 CG LYS L 39 24.972 43.598 51.856 1.00 15.25 C
ATOM 292 CD LYS L 39 24.431 44.271 53.109 1.00 15.13 C
ATOM 293 CE LYS L 39 25.254 43.986 54.337 1.00 15.51 C
ATOM 294 NZ LYS L 39 24.542 44.385 55.581 1.00 15.79 N
ATOM 295 N SER L 40 25.442 42.138 48.628 1.00 17.51 N
ATOM 296 CA SER L 40 26.389 42.398 47.548 1.00 18.17 C
ATOM 297 C SER L 40 27.822 41.962 47.855 1.00 18.55 C
ATOM 298 O SER L 40 28.478 42.516 48.761 1.00 18.57 O
ATOM 299 CB SER L 40 26.403 43.877 47.135 1.00 18.50 C
ATOM 300 OG SER L 40 27.240 44.691 47.926 1.00 18.09 O
ATOM 301 N HIS L 41 28.271 40.975 47.073 1.00 18.83 N
ATOM 302 CA HIS L 41 29.627 40.468 47.243 1.00 19.08 C
ATOM 303 C HIS L 41 29.849 39.468 48.350 1.00 19.16 C
ATOM 304 O HIS L 41 30.964 39.549 48.938 1.00 19.16 O
ATOM 305 CB HIS L 41 30.584 41.638 47.714 1.00 19.67 C
ATOM 306 CG HIS L 41 31.717 41.691 46.740 1.00 20.46 C
ATOM 307 ND1 HIS L 41 31.634 41.029 45.531 1.00 20.73 N
ATOM 308 CD2 HIS L 41 32.909 42.311 46.776 1.00 20.91 C
ATOM 309 CE1 HIS L 41 32.753 41.242 44.857 1.00 21.10 C
ATOM 310 NE2 HIS L 41 33.537 42.012 45.587 1.00 21.65 N
ATOM 311 N GLU L 42 28.881 38.624 48.628 1.00 19.09 N
ATOM 312 CA GLU L 42 29.081 37.658 49.703 1.00 19.00 C
ATOM 313 C GLU L 42 28.087 36.500 49.649 1.00 18.71 C
ATOM 314 O GLU L 42 27.115 36.439 48.895 1.00 18.76 O
ATOM 315 CB GLU L 42 28.900 38.244 51.098 1.00 19.54 C
ATOM 316 CG GLU L 42 29.428 39.626 51.412 1.00 20.72 C
ATOM 317 CD GLU L 42 29.161 40.100 52.815 1.00 21.57 C
ATOM 318 OE1 GLU L 42 28.958 39.345 53.754 1.00 21.91 O
ATOM 319 OE2 GLU L 42 29.181 41.353 52.845 1.00 22.23 O
ATOM 320 N SER L 43 28.455 35.598 50.546 1.00 18.09 N
ATOM 321 CA SER L 43 27.711 34.365 50.774 1.00 17.51 C
ATOM 322 C SER L 43 26.603 34.751 51.752 1.00 16.86 C
ATOM 323 O SER L 43 26.904 35.554 52.659 1.00 17.07 O
ATOM 324 CB SER L 43 28.600 33.313 51.414 1.00 18.21 C
ATOM 325 OG SER L 43 27.920 32.742 52.532 1.00 18.91 O
ATOM 326 N PRO L 44 25.438 34.193 51.549 1.00 15.99 N
ATOM 327 CA PRO L 44 24.306 34.486 52.431 1.00 15.69 C
ATOM 328 C PRO L 44 24.654 34.324 53.901 1.00 15.49 C
ATOM 329 O PRO L 44 25.780 34.015 54.342 1.00 15.51 O
ATOM 330 CB PRO L 44 23.229 33.523 51.936 1.00 15.58 C
ATOM 331 CG PRO L 44 23.564 33.287 50.487 1.00 15.46 C
ATOM 332 CD PRO L 44 25.090 33.253 50.480 1.00 15.63 C
ATOM 333 N ARG L 45 23.628 34.543 54.705 1.00 15.14 N
ATOM 334 CA ARG L 45 23.660 34.445 56.173 1.00 14.68 C
ATOM 335 C ARG L 45 22.216 34.156 56.593 1.00 14.22 C
ATOM 336 O ARG L 45 21.304 34.655 55.917 1.00 14.25 O
ATOM 337 CB ARG L 45 24.234 35.646 56.867 1.00 14.94 C
ATOM 338 CG ARG L 45 23.565 36.992 56.741 1.00 15.29 C
ATOM 339 CD ARG L 45 24.426 38.079 57.253 1.00 16.01 C
ATOM 340 NE ARG L 45 24.210 38.676 58.488 1.00 16.91 N
ATOM 341 CZ ARG L 45 23.776 38.650 59.710 1.00 17.73 C
ATOM 342 NH1 ARG L 45 23.969 39.688 60.555 1.00 17.89 N
ATOM 343 NH2 ARG L 45 23.105 37.599 60.209 1.00 18.15 N
ATOM 344 N LEU L 46 22.051 33.384 57.640 1.00 13.74 N
ATOM 345 CA LEU L 46 20.691 33.058 58.113 1.00 13.41 C
ATOM 346 C LEU L 46 20.200 34.233 58.954 1.00 13.32 C
ATOM 347 O LEU L 46 20.981 34.787 59.754 1.00 13.50 O
ATOM 348 CB LEU L 46 20.737 31.727 58.849 1.00 12.98 C
ATOM 349 CG LEU L 46 19.438 31.098 59.312 1.00 12.70 C
ATOM 350 CD1 LEU L 46 18.617 30.595 58.126 1.00 12.45 C
ATOM 351 CD2 LEU L 46 19.757 29.938 60.251 1.00 12.31 C
ATOM 352 N LEU L 47 18.945 34.591 58.762 1.00 13.10 N
ATOM 353 CA LEU L 47 18.360 35.703 59.529 1.00 12.98 C
ATOM 354 C LEU L 47 17.461 35.063 60.596 1.00 12.90 C
ATOM 355 O LEU L 47 17.740 35.149 61.798 1.00 13.08 O
ATOM 356 CB LEU L 47 17.669 36.699 58.632 1.00 13.14 C
ATOM 357 CG LEU L 47 18.448 37.728 57.837 1.00 13.21 C
ATOM 358 CD1 LEU L 47 17.496 38.779 57.278 1.00 13.13 C
ATOM 359 CD2 LEU L 47 19.489 38.422 58.713 1.00 13.26 C
ATOM 360 N ILE L 48 16.417 34.436 60.105 1.00 12.59 N
ATOM 361 CA ILE L 48 15.405 33.757 60.903 1.00 12.47 C
ATOM 362 C ILE L 48 15.239 32.289 60.602 1.00 12.54 C
ATOM 363 O ILE L 48 15.146 31.982 59.398 1.00 12.69 O
ATOM 364 CB ILE L 48 14.051 34.518 60.593 1.00 12.29 C
ATOM 365 CG1 ILE L 48 14.260 36.018 60.909 1.00 12.26 C
ATOM 366 CG2 ILE L 48 12.833 33.904 61.307 1.00 12.42 C
ATOM 367 CD1 ILE L 48 14.753 36.312 62.346 1.00 11.85 C
ATOM 368 N LYS L 49 15.189 31.428 61.600 1.00 12.60 N
ATOM 369 CA LYS L 49 15.020 29.978 61.409 1.00 12.65 C
ATOM 370 C LYS L 49 13.526 29.635 61.450 1.00 12.68 C
ATOM 371 O LYS L 49 12.672 30.496 61.659 1.00 12.71 O
ATOM 372 CB LYS L 49 15.693 29.116 62.441 1.00 12.86 C
ATOM 373 CG LYS L 49 17.129 28.666 62.254 1.00 13.02 C
ATOM 374 CD LYS L 49 17.490 27.625 63.308 1.00 13.25 C
ATOM 375 CE LYS L 49 18.875 27.715 63.883 1.00 12.86 C
ATOM 376 NZ LYS L 49 19.921 27.255 62.941 1.00 12.68 N
ATOM 377 N TYR L 50 13.240 28.377 61.265 1.00 12.85 N
ATOM 378 CA TYR L 50 11.871 27.821 61.250 1.00 13.23 C
ATOM 379 C TYR L 50 10.878 28.839 60.760 1.00 13.49 C
ATOM 380 O TYR L 50 10.447 28.596 59.583 1.00 13.79 O
ATOM 381 CB TYR L 50 11.585 27.019 62.553 1.00 13.47 C
ATOM 382 CG TYR L 50 12.500 25.796 62.338 1.00 13.66 C
ATOM 383 CD1 TYR L 50 12.173 24.827 61.388 1.00 13.47 C
ATOM 384 CD2 TYR L 50 13.679 25.669 63.054 1.00 13.73 C
ATOM 385 CE1 TYR L 50 13.012 23.735 61.176 1.00 13.25 C
ATOM 386 CE2 TYR L 50 14.519 24.579 62.849 1.00 13.64 C
ATOM 387 CZ TYR L 50 14.185 23.613 61.908 1.00 13.26 C
ATOM 388 OH TYR L 50 15.053 22.573 61.758 1.00 13.23 O
ATOM 389 N ALA L 51 10.473 29.890 61.418 1.00 13.44 N
ATOM 390 CA ALA L 51 9.487 30.802 60.774 1.00 13.54 C
ATOM 391 C ALA L 51 9.518 32.189 61.386 1.00 13.84 C
ATOM 392 O ALA L 51 9.448 33.221 60.704 1.00 13.81 O
ATOM 393 CB ALA L 51 8.131 30.131 60.852 1.00 13.84 C
ATOM 394 N SER L 52 9.629 32.182 62.697 1.00 14.06 N
ATOM 395 CA SER L 52 9.689 33.307 63.599 1.00 13.97 C
ATOM 396 C SER L 52 10.805 33.162 64.633 1.00 14.03 C
ATOM 397 O SER L 52 10.846 33.994 65.557 1.00 14.26 O
ATOM 398 CB SER L 52 8.384 33.401 64.409 1.00 13.99 C
ATOM 399 OG SER L 52 8.405 32.372 65.389 1.00 13.49 O
ATOM 400 N GLN L 53 11.637 32.156 64.490 1.00 14.00 N
ATOM 401 CA GLN L 53 12.748 31.923 65.423 1.00 14.09 C
ATOM 402 C GLN L 53 13.931 32.784 64.928 1.00 14.15 C
ATOM 403 O GLN L 53 14.596 32.367 63.958 1.00 14.40 O
ATOM 404 CB GLN L 53 13.223 30.496 65.561 1.00 14.00 C
ATOM 405 CG GLN L 53 12.257 29.384 65.258 1.00 14.47 C
ATOM 406 CD GLN L 53 12.671 28.081 65.911 1.00 14.52 C
ATOM 407 OE1 GLN L 53 13.748 27.940 66.481 1.00 14.31 O
ATOM 408 NE2 GLN L 53 11.765 27.109 65.818 1.00 14.78 N
ATOM 409 N SER L 54 14.157 33.902 65.575 1.00 13.94 N
ATOM 410 CA SER L 54 15.255 34.791 65.182 1.00 14.10 C
ATOM 411 C SER L 54 16.621 34.235 65.550 1.00 14.07 C
ATOM 412 O SER L 54 16.784 33.791 66.698 1.00 14.14 O
ATOM 413 CB SER L 54 15.055 36.160 65.829 1.00 15.14 C
ATOM 414 OG SER L 54 15.314 36.156 67.223 1.00 15.74 O
ATOM 415 N ILE L 55 17.563 34.270 64.619 1.00 14.04 N
ATOM 416 CA ILE L 55 18.935 33.777 64.888 1.00 14.18 C
ATOM 417 C ILE L 55 19.545 34.781 65.871 1.00 14.34 C
ATOM 418 O ILE L 55 18.927 35.861 66.021 1.00 14.50 O
ATOM 419 CB ILE L 55 19.784 33.576 63.606 1.00 14.27 C
ATOM 420 CG1 ILE L 55 19.159 32.398 62.803 1.00 14.55 C
ATOM 421 CG2 ILE L 55 21.285 33.304 63.859 1.00 14.08 C
ATOM 422 CD1 ILE L 55 18.763 31.232 63.761 1.00 15.11 C
ATOM 423 N SER L 56 20.663 34.474 66.507 1.00 14.16 N
ATOM 424 CA SER L 56 21.248 35.433 67.465 1.00 13.89 C
ATOM 425 C SER L 56 22.347 36.245 66.788 1.00 13.81 C
ATOM 426 O SER L 56 23.202 35.742 66.062 1.00 13.78 O
ATOM 427 CB SER L 56 21.776 34.791 68.727 1.00 14.14 C
ATOM 428 OG SER L 56 23.181 34.871 68.849 1.00 13.89 O
ATOM 429 N GLY L 57 22.265 37.528 67.079 1.00 13.91 N
ATOM 430 CA GLY L 57 23.205 38.522 66.554 1.00 13.88 C
ATOM 431 C GLY L 57 22.614 39.185 65.316 1.00 13.79 C
ATOM 432 O GLY L 57 23.393 39.671 64.488 1.00 13.82 O
ATOM 433 N ILE L 58 21.298 39.172 65.236 1.00 13.79 N
ATOM 434 CA ILE L 58 20.586 39.781 64.104 1.00 14.02 C
ATOM 435 C ILE L 58 19.606 40.797 64.698 1.00 14.30 C
ATOM 436 O ILE L 58 19.013 40.485 65.737 1.00 14.37 O
ATOM 437 CB ILE L 58 19.912 38.779 63.138 1.00 14.08 C
ATOM 438 CG1 ILE L 58 18.605 39.426 62.591 1.00 14.15 C
ATOM 439 CG2 ILE L 58 19.619 37.391 63.741 1.00 14.37 C
ATOM 440 CD1 ILE L 58 17.874 38.507 61.581 1.00 14.96 C
ATOM 441 N PRO L 59 19.506 41.934 64.023 1.00 14.47 N
ATOM 442 CA PRO L 59 18.642 43.035 64.428 1.00 14.62 C
ATOM 443 C PRO L 59 17.241 42.664 64.874 1.00 14.96 C
ATOM 444 O PRO L 59 16.624 41.693 64.398 1.00 15.26 O
ATOM 445 CB PRO L 59 18.612 43.954 63.201 1.00 14.40 C
ATOM 446 CG PRO L 59 19.937 43.715 62.543 1.00 14.32 C
ATOM 447 CD PRO L 59 20.249 42.256 62.787 1.00 14.37 C
ATOM 448 N SER L 60 16.745 43.471 65.800 1.00 14.99 N
ATOM 449 CA SER L 60 15.398 43.277 66.366 1.00 15.31 C
ATOM 450 C SER L 60 14.351 43.873 65.431 1.00 15.28 C
ATOM 451 O SER L 60 13.146 43.891 65.722 1.00 15.29 O
ATOM 452 CB SER L 60 15.336 43.837 67.773 1.00 16.47 C
ATOM 453 OG SER L 60 16.305 43.191 68.601 1.00 17.63 O
ATOM 454 N ARG L 61 14.864 44.348 64.315 1.00 15.04 N