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HEADER    COMPLEX (MYRISTYLATION/TRANSFERASE)     23-SEP-97   1AVZ              
TITLE     V-1 NEF PROTEIN IN COMPLEX WITH WILD TYPE FYN SH3 DOMAIN              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEGATIVE FACTOR;                                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CONSERVED CORE DOMAIN;                                     
COMPND   5 SYNONYM: NEF, F-PROTEIN;                                             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: FYN TYROSINE KINASE;                                       
COMPND  10 CHAIN: C;                                                            
COMPND  11 FRAGMENT: SRC-HOMOLOGY 3 DOMAIN;                                     
COMPND  12 SYNONYM: SH3 DOMAIN;                                                 
COMPND  13 EC: 2.7.1.112;                                                       
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE   3 ORGANISM_TAXID: 11676;                                               
SOURCE   4 VARIANT: LAI ISOLATE;                                                
SOURCE   5 CELL_LINE: BL21;                                                     
SOURCE   6 GENE: HIV-1 NEF;                                                     
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 CELL_LINE: BL21;                                                     
SOURCE  16 GENE: FYN TYROSINE KINASE;                                           
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PGEX-2T                                   
KEYWDS    COMPLEX (MYRISTYLATION-TRANSFERASE), GTP-BINDING, HIV-1,              
KEYWDS   2 PHOSPHORYLATION, NEF, SH3 DOMAIN, FYN, TYROSINE KINASE, COMPLEX      
KEYWDS   3 (MYRISTYLATION-TRANSFERASE) COMPLEX                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.AROLD,P.FRANKEN,C.DUMAS                                             
REVDAT   4   11-APR-18 1AVZ    1       REMARK                                   
REVDAT   3   04-APR-18 1AVZ    1       REMARK                                   
REVDAT   2   24-FEB-09 1AVZ    1       VERSN                                    
REVDAT   1   25-MAR-98 1AVZ    0                                                
JRNL        AUTH   S.AROLD,P.FRANKEN,M.P.STRUB,F.HOH,S.BENICHOU,R.BENAROUS,     
JRNL        AUTH 2 C.DUMAS                                                      
JRNL        TITL   THE CRYSTAL STRUCTURE OF HIV-1 NEF PROTEIN BOUND TO THE FYN  
JRNL        TITL 2 KINASE SH3 DOMAIN SUGGESTS A ROLE FOR THIS COMPLEX IN        
JRNL        TITL 3 ALTERED T CELL RECEPTOR SIGNALING.                           
JRNL        REF    STRUCTURE                     V.   5  1361 1997              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   9351809                                                      
JRNL        DOI    10.1016/S0969-2126(97)00286-4                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.H.LEE,K.SAKSELA,U.A.MIRZA,B.T.CHAIT,J.KURIYAN              
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE CONSERVED CORE OF HIV-1 NEF         
REMARK   1  TITL 2 COMPLEXED WITH A SRC FAMILY SH3 DOMAIN                       
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V.  85   931 1996              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   S.GRZESIEK,A.BAX,G.M.CLORE,A.M.GRONENBORN,J.S.HU,J.KAUFMAN,  
REMARK   1  AUTH 2 I.PALMER,S.J.STAHL,P.T.WINGFIELD                             
REMARK   1  TITL   THE SOLUTION STRUCTURE OF HIV-1 NEF REVEALS AN UNEXPECTED    
REMARK   1  TITL 2 FOLD AND PERMITS DELINEATION OF THE BINDING SURFACE FOR THE  
REMARK   1  TITL 3 SH3 DOMAIN OF HCK TYROSINE PROTEIN KINASE                    
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   3   340 1996              
REMARK   1  REFN                   ISSN 1072-8368                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 75.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 11662                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2186                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.210                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1AVZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000171324.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-OCT-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM02                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0373                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : TWO BENT MIRRORS                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : PRINCETON 2K                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14778                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.06700                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.8                                            
REMARK 200 STARTING MODEL: PDB ENTRIES 1EFN AND 1SHF                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.9                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      149.13333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       74.56667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      111.85000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       37.28333            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      186.41667            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      149.13333            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       74.56667            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       37.28333            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      111.85000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      186.41667            
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: A, B, C                               
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     GLY A    56                                                      
REMARK 465     SER A    57                                                      
REMARK 465     LEU A    58                                                      
REMARK 465     GLU A    59                                                      
REMARK 465     ALA A    60                                                      
REMARK 465     GLN A    61                                                      
REMARK 465     GLU A    62                                                      
REMARK 465     GLU A    63                                                      
REMARK 465     GLU A    64                                                      
REMARK 465     GLU A    65                                                      
REMARK 465     VAL A    66                                                      
REMARK 465     GLY A    67                                                      
REMARK 465     PHE A    68                                                      
REMARK 465     PRO A    69                                                      
REMARK 465     VAL A    70                                                      
REMARK 465     THR A    71                                                      
REMARK 465     PRO A    72                                                      
REMARK 465     GLN A    73                                                      
REMARK 465     GLU A   149                                                      
REMARK 465     PRO A   150                                                      
REMARK 465     ASP A   151                                                      
REMARK 465     LYS A   152                                                      
REMARK 465     VAL A   153                                                      
REMARK 465     GLU A   154                                                      
REMARK 465     GLU A   155                                                      
REMARK 465     ALA A   156                                                      
REMARK 465     ASN A   157                                                      
REMARK 465     LYS A   158                                                      
REMARK 465     GLY A   159                                                      
REMARK 465     GLU A   160                                                      
REMARK 465     ASN A   161                                                      
REMARK 465     THR A   162                                                      
REMARK 465     SER A   163                                                      
REMARK 465     LEU A   164                                                      
REMARK 465     LEU A   165                                                      
REMARK 465     HIS A   166                                                      
REMARK 465     PRO A   167                                                      
REMARK 465     VAL A   168                                                      
REMARK 465     SER A   169                                                      
REMARK 465     LEU A   170                                                      
REMARK 465     HIS A   171                                                      
REMARK 465     GLY A   172                                                      
REMARK 465     MET A   173                                                      
REMARK 465     ASP A   174                                                      
REMARK 465     ASP A   175                                                      
REMARK 465     PRO A   176                                                      
REMARK 465     GLU A   177                                                      
REMARK 465     ARG A   178                                                      
REMARK 465     LYS A   204                                                      
REMARK 465     ASN A   205                                                      
REMARK 465     CYS A   206                                                      
REMARK 465     GLY B    56                                                      
REMARK 465     SER B    57                                                      
REMARK 465     LEU B    58                                                      
REMARK 465     GLU B    59                                                      
REMARK 465     ALA B    60                                                      
REMARK 465     GLN B    61                                                      
REMARK 465     GLU B    62                                                      
REMARK 465     GLU B    63                                                      
REMARK 465     GLU B    64                                                      
REMARK 465     GLU B    65                                                      
REMARK 465     VAL B    66                                                      
REMARK 465     GLY B    67                                                      
REMARK 465     PHE B    68                                                      
REMARK 465     PRO B    69                                                      
REMARK 465     VAL B    70                                                      
REMARK 465     GLU B   149                                                      
REMARK 465     PRO B   150                                                      
REMARK 465     ASP B   151                                                      
REMARK 465     LYS B   152                                                      
REMARK 465     VAL B   153                                                      
REMARK 465     GLU B   154                                                      
REMARK 465     GLU B   155                                                      
REMARK 465     ALA B   156                                                      
REMARK 465     ASN B   157                                                      
REMARK 465     LYS B   158                                                      
REMARK 465     GLY B   159                                                      
REMARK 465     GLU B   160                                                      
REMARK 465     ASN B   161                                                      
REMARK 465     THR B   162                                                      
REMARK 465     SER B   163                                                      
REMARK 465     LEU B   164                                                      
REMARK 465     LEU B   165                                                      
REMARK 465     HIS B   166                                                      
REMARK 465     PRO B   167                                                      
REMARK 465     VAL B   168                                                      
REMARK 465     SER B   169                                                      
REMARK 465     LEU B   170                                                      
REMARK 465     HIS B   171                                                      
REMARK 465     GLY B   172                                                      
REMARK 465     MET B   173                                                      
REMARK 465     ASP B   174                                                      
REMARK 465     ASP B   175                                                      
REMARK 465     PRO B   176                                                      
REMARK 465     GLU B   177                                                      
REMARK 465     ARG B   178                                                      
REMARK 465     LYS B   204                                                      
REMARK 465     ASN B   205                                                      
REMARK 465     CYS B   206                                                      
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    PRO A 122   C   -  N   -  CA  ANGL. DEV. =  11.7 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    MET A  79       97.24    -68.12                                   
REMARK 500    PRO A 122       44.29    -54.06                                   
REMARK 500    CYS A 142       36.00    -87.92                                   
REMARK 500    ALA A 195       10.08    -68.93                                   
REMARK 500    ARG A 196      -30.99   -132.38                                   
REMARK 500    HIS A 199       68.55   -117.88                                   
REMARK 500    TYR A 202        0.82    -63.12                                   
REMARK 500    PRO B  75      162.08    -49.28                                   
REMARK 500    LEU B 110      -73.62    -61.53                                   
REMARK 500    PRO B 122       51.69    -60.22                                   
REMARK 500    CYS B 142       25.50    -76.01                                   
REMARK 500    LEU B 198      -70.49    -91.00                                   
REMARK 500    TYR B 202       -0.77    -55.49                                   
REMARK 500    LYS C 105      102.46    -30.50                                   
REMARK 500    GLN C 110      112.76   -169.51                                   
REMARK 500    ASN C 113       94.47   -161.26                                   
REMARK 500    SER C 115       67.56    -67.73                                   
REMARK 500    GLU C 116       -3.33   -170.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1AVZ A   58   206  UNP    P03406   NEF_HV1BR       58    206             
DBREF  1AVZ B   58   206  UNP    P03406   NEF_HV1BR       58    206             
DBREF  1AVZ C   85   141  UNP    P06241   FYN_HUMAN       84    140             
SEQRES   1 A  151  GLY SER LEU GLU ALA GLN GLU GLU GLU GLU VAL GLY PHE          
SEQRES   2 A  151  PRO VAL THR PRO GLN VAL PRO LEU ARG PRO MET THR TYR          
SEQRES   3 A  151  LYS ALA ALA VAL ASP LEU SER HIS PHE LEU LYS GLU LYS          
SEQRES   4 A  151  GLY GLY LEU GLU GLY LEU ILE HIS SER GLN ARG ARG GLN          
SEQRES   5 A  151  ASP ILE LEU ASP LEU TRP ILE TYR HIS THR GLN GLY TYR          
SEQRES   6 A  151  PHE PRO ASP TRP GLN ASN TYR THR PRO GLY PRO GLY VAL          
SEQRES   7 A  151  ARG TYR PRO LEU THR PHE GLY TRP CYS TYR LYS LEU VAL          
SEQRES   8 A  151  PRO VAL GLU PRO ASP LYS VAL GLU GLU ALA ASN LYS GLY          
SEQRES   9 A  151  GLU ASN THR SER LEU LEU HIS PRO VAL SER LEU HIS GLY          
SEQRES  10 A  151  MET ASP ASP PRO GLU ARG GLU VAL LEU GLU TRP ARG PHE          
SEQRES  11 A  151  ASP SER ARG LEU ALA PHE HIS HIS VAL ALA ARG GLU LEU          
SEQRES  12 A  151  HIS PRO GLU TYR PHE LYS ASN CYS                              
SEQRES   1 B  151  GLY SER LEU GLU ALA GLN GLU GLU GLU GLU VAL GLY PHE          
SEQRES   2 B  151  PRO VAL THR PRO GLN VAL PRO LEU ARG PRO MET THR TYR          
SEQRES   3 B  151  LYS ALA ALA VAL ASP LEU SER HIS PHE LEU LYS GLU LYS          
SEQRES   4 B  151  GLY GLY LEU GLU GLY LEU ILE HIS SER GLN ARG ARG GLN          
SEQRES   5 B  151  ASP ILE LEU ASP LEU TRP ILE TYR HIS THR GLN GLY TYR          
SEQRES   6 B  151  PHE PRO ASP TRP GLN ASN TYR THR PRO GLY PRO GLY VAL          
SEQRES   7 B  151  ARG TYR PRO LEU THR PHE GLY TRP CYS TYR LYS LEU VAL          
SEQRES   8 B  151  PRO VAL GLU PRO ASP LYS VAL GLU GLU ALA ASN LYS GLY          
SEQRES   9 B  151  GLU ASN THR SER LEU LEU HIS PRO VAL SER LEU HIS GLY          
SEQRES  10 B  151  MET ASP ASP PRO GLU ARG GLU VAL LEU GLU TRP ARG PHE          
SEQRES  11 B  151  ASP SER ARG LEU ALA PHE HIS HIS VAL ALA ARG GLU LEU          
SEQRES  12 B  151  HIS PRO GLU TYR PHE LYS ASN CYS                              
SEQRES   1 C   57  THR LEU PHE VAL ALA LEU TYR ASP TYR GLU ALA ARG THR          
SEQRES   2 C   57  GLU ASP ASP LEU SER PHE HIS LYS GLY GLU LYS PHE GLN          
SEQRES   3 C   57  ILE LEU ASN SER SER GLU GLY ASP TRP TRP GLU ALA ARG          
SEQRES   4 C   57  SER LEU THR THR GLY GLU THR GLY TYR ILE PRO SER ASN          
SEQRES   5 C   57  TYR VAL ALA PRO VAL                                          
HELIX    1   1 TYR A   81  LYS A   94  1                                  14    
HELIX    2   2 GLN A  104  THR A  117  1                                  14    
HELIX    3   3 SER A  187  ALA A  190  5                                   4    
HELIX    4   4 VAL A  194  GLU A  197  1                                   4    
HELIX    5   5 TYR B   81  LYS B   94  1                                  14    
HELIX    6   6 GLN B  104  THR B  117  1                                  14    
HELIX    7   7 SER B  187  ALA B  190  5                                   4    
HELIX    8   8 VAL B  194  GLU B  197  1                                   4    
HELIX    9   9 SER C  135  TYR C  137  5                                   3    
SHEET    1   A 2 TYR A 143  PRO A 147  0                                        
SHEET    2   A 2 LEU A 181  PHE A 185 -1  N  ARG A 184   O  LYS A 144           
SHEET    1   B 2 TYR B 143  PRO B 147  0                                        
SHEET    2   B 2 LEU B 181  PHE B 185 -1  N  ARG B 184   O  LYS B 144           
SHEET    1   C 2 TRP C 119  ARG C 123  0                                        
SHEET    2   C 2 THR C 130  PRO C 134 -1  N  ILE C 133   O  TRP C 120           
CISPEP   1 GLY A  130    PRO A  131          0         0.11                     
CISPEP   2 GLY B  130    PRO B  131          0        -0.35                     
CRYST1  108.200  108.200  223.700  90.00  90.00 120.00 P 65 2 2     24          
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      0.009242  0.005336  0.000000        0.00000                         
SCALE2      0.000000  0.010672  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004470        0.00000                         
ATOM      1  N   VAL A  74      12.296  31.204  98.961  1.00 59.03           N  
ATOM      2  CA  VAL A  74      12.647  32.157 100.060  1.00 59.03           C  
ATOM      3  C   VAL A  74      11.987  31.856 101.422  1.00 59.03           C  
ATOM      4  O   VAL A  74      11.495  32.773 102.085  1.00 59.03           O  
ATOM      5  CB  VAL A  74      12.328  33.622  99.633  1.00 67.05           C  
ATOM      6  CG1 VAL A  74      13.242  34.036  98.497  1.00 67.05           C  
ATOM      7  CG2 VAL A  74      10.862  33.759  99.197  1.00 67.05           C  
ATOM      8  N   PRO A  75      12.066  30.590 101.905  1.00 53.68           N  
ATOM      9  CA  PRO A  75      11.472  30.162 103.193  1.00 53.68           C  
ATOM     10  C   PRO A  75      11.608  31.145 104.376  1.00 53.68           C  
ATOM     11  O   PRO A  75      12.657  31.777 104.561  1.00 53.68           O  
ATOM     12  CB  PRO A  75      12.180  28.831 103.469  1.00 53.68           C  
ATOM     13  CG  PRO A  75      12.365  28.273 102.070  1.00 53.68           C  
ATOM     14  CD  PRO A  75      12.859  29.493 101.309  1.00 53.68           C  
ATOM     15  N   LEU A  76      10.541  31.241 105.173  1.00 64.11           N  
ATOM     16  CA  LEU A  76      10.481  32.151 106.323  1.00 64.11           C  
ATOM     17  C   LEU A  76      11.465  31.833 107.464  1.00 64.11           C  
ATOM     18  O   LEU A  76      11.305  30.837 108.173  1.00 64.11           O  
ATOM     19  CB  LEU A  76       9.054  32.211 106.878  1.00 47.04           C  
ATOM     20  CG  LEU A  76       8.646  33.553 107.489  1.00 47.04           C  
ATOM     21  CD1 LEU A  76       8.152  34.461 106.382  1.00 47.04           C  
ATOM     22  CD2 LEU A  76       7.563  33.367 108.533  1.00 47.04           C  
ATOM     23  N   ARG A  77      12.436  32.729 107.670  1.00 49.64           N  
ATOM     24  CA  ARG A  77      13.467  32.584 108.700  1.00 49.64           C  
ATOM     25  C   ARG A  77      13.396  33.624 109.824  1.00 49.64           C  
ATOM     26  O   ARG A  77      12.775  34.687 109.668  1.00 49.64           O  
ATOM     27  CB  ARG A  77      14.855  32.590 108.056  1.00 53.89           C  
ATOM     28  CG  ARG A  77      14.970  33.521 106.882  1.00 53.89           C  
ATOM     29  CD  ARG A  77      15.687  32.850 105.739  1.00 53.89           C  
ATOM     30  NE  ARG A  77      17.108  33.176 105.728  1.00 53.89           N  
ATOM     31  CZ  ARG A  77      17.677  34.030 104.878  1.00 53.89           C  
ATOM     32  NH1 ARG A  77      16.943  34.654 103.960  1.00 53.89           N  
ATOM     33  NH2 ARG A  77      18.986  34.253 104.930  1.00 53.89           N  
ATOM     34  N   PRO A  78      13.967  33.286 111.009  1.00 49.48           N  
ATOM     35  CA  PRO A  78      13.991  34.165 112.190  1.00 49.48           C  
ATOM     36  C   PRO A  78      15.133  35.174 112.142  1.00 49.48           C  
ATOM     37  O   PRO A  78      16.290  34.800 111.936  1.00 49.48           O  
ATOM     38  CB  PRO A  78      14.171  33.175 113.340  1.00 50.86           C  
ATOM     39  CG  PRO A  78      15.049  32.123 112.739  1.00 50.86           C  
ATOM     40  CD  PRO A  78      14.437  31.925 111.367  1.00 50.86           C  
ATOM     41  N   MET A  79      14.810  36.450 112.319  1.00 40.55           N  
ATOM     42  CA  MET A  79      15.829  37.501 112.292  1.00 40.55           C  
ATOM     43  C   MET A  79      16.789  37.428 113.489  1.00 40.55           C  
ATOM     44  O   MET A  79      16.462  37.876 114.595  1.00 40.55           O  
ATOM     45  CB  MET A  79      15.158  38.876 112.218  1.00 40.47           C  
ATOM     46  CG  MET A  79      16.097  40.074 112.323  1.00 40.47           C  
ATOM     47  SD  MET A  79      17.200  40.250 110.941  1.00 40.47           S  
ATOM     48  CE  MET A  79      16.178  41.050 109.716  1.00 40.47           C  
ATOM     49  N   THR A  80      17.952  36.807 113.277  1.00 27.91           N  
ATOM     50  CA  THR A  80      18.958  36.690 114.326  1.00 27.91           C  
ATOM     51  C   THR A  80      20.022  37.758 114.150  1.00 27.91           C  
ATOM     52  O   THR A  80      20.040  38.465 113.139  1.00 27.91           O  
ATOM     53  CB  THR A  80      19.627  35.316 114.341  1.00 29.52           C  
ATOM     54  OG1 THR A  80      20.131  35.006 113.038  1.00 29.52           O  
ATOM     55  CG2 THR A  80      18.639  34.257 114.798  1.00 29.52           C  
ATOM     56  N   TYR A  81      20.899  37.876 115.148  1.00 31.86           N  
ATOM     57  CA  TYR A  81      21.981  38.857 115.140  1.00 31.86           C  
ATOM     58  C   TYR A  81      22.846  38.708 113.890  1.00 31.86           C  
ATOM     59  O   TYR A  81      23.120  39.698 113.215  1.00 31.86           O  
ATOM     60  CB  TYR A  81      22.815  38.704 116.417  1.00 24.82           C  
ATOM     61  CG  TYR A  81      24.088  39.521 116.462  1.00 24.82           C  
ATOM     62  CD1 TYR A  81      24.079  40.825 116.915  1.00 24.82           C  
ATOM     63  CD2 TYR A  81      25.312  38.979 116.049  1.00 24.82           C  
ATOM     64  CE1 TYR A  81      25.253  41.587 116.958  1.00 24.82           C  
ATOM     65  CE2 TYR A  81      26.498  39.735 116.082  1.00 24.82           C  
ATOM     66  CZ  TYR A  81      26.462  41.043 116.539  1.00 24.82           C  
ATOM     67  OH  TYR A  81      27.613  41.812 116.555  1.00 24.82           O  
ATOM     68  N   LYS A  82      23.222  37.470 113.563  1.00 33.68           N  
ATOM     69  CA  LYS A  82      24.050  37.199 112.393  1.00 33.68           C  
ATOM     70  C   LYS A  82      23.339  37.607 111.122  1.00 33.68           C  
ATOM     71  O   LYS A  82      23.948  38.186 110.221  1.00 33.68           O  
ATOM     72  CB  LYS A  82      24.460  35.726 112.319  1.00 68.51           C  
ATOM     73  CG  LYS A  82      23.316  34.716 112.420  1.00 68.51           C  
ATOM     74  CD  LYS A  82      23.831  33.275 112.264  1.00 68.51           C  
ATOM     75  CE  LYS A  82      22.791  32.242 112.703  1.00 68.51           C  
ATOM     76  NZ  LYS A  82      23.392  30.880 112.798  1.00 68.51           N  
ATOM     77  N   ALA A  83      22.043  37.318 111.060  1.00 28.50           N  
ATOM     78  CA  ALA A  83      21.225  37.672 109.906  1.00 28.50           C  
ATOM     79  C   ALA A  83      21.085  39.197 109.800  1.00 28.50           C  
ATOM     80  O   ALA A  83      21.150  39.745 108.705  1.00 28.50           O  
ATOM     81  CB  ALA A  83      19.868  37.021 110.027  1.00 25.37           C  
ATOM     82  N   ALA A  84      20.938  39.871 110.942  1.00 24.55           N  
ATOM     83  CA  ALA A  84      20.805  41.325 110.977  1.00 24.55           C  
ATOM     84  C   ALA A  84      22.066  41.961 110.421  1.00 24.55           C  
ATOM     85  O   ALA A  84      22.013  42.861 109.567  1.00 24.55           O  
ATOM     86  CB  ALA A  84      20.582  41.793 112.398  1.00 17.58           C  
ATOM     87  N   VAL A  85      23.206  41.470 110.907  1.00 31.61           N  
ATOM     88  CA  VAL A  85      24.507  41.969 110.488  1.00 31.61           C  
ATOM     89  C   VAL A  85      24.724  41.760 108.997  1.00 31.61           C  
ATOM     90  O   VAL A  85      24.951  42.719 108.271  1.00 31.61           O  
ATOM     91  CB  VAL A  85      25.638  41.319 111.305  1.00 25.19           C  
ATOM     92  CG1 VAL A  85      26.969  41.579 110.658  1.00 25.19           C  
ATOM     93  CG2 VAL A  85      25.632  41.884 112.711  1.00 25.19           C  
ATOM     94  N   ASP A  86      24.576  40.525 108.530  1.00 23.55           N  
ATOM     95  CA  ASP A  86      24.773  40.225 107.124  1.00 23.55           C  
ATOM     96  C   ASP A  86      23.954  41.112 106.215  1.00 23.55           C  
ATOM     97  O   ASP A  86      24.435  41.567 105.167  1.00 23.55           O  
ATOM     98  CB  ASP A  86      24.454  38.772 106.873  1.00 20.26           C  
ATOM     99  CG  ASP A  86      25.447  37.853 107.528  1.00 20.26           C  
ATOM    100  OD1 ASP A  86      26.469  38.336 108.091  1.00 20.26           O  
ATOM    101  OD2 ASP A  86      25.214  36.631 107.462  1.00 20.26           O  
ATOM    102  N   LEU A  87      22.744  41.406 106.680  1.00 25.89           N  
ATOM    103  CA  LEU A  87      21.786  42.244 105.983  1.00 25.89           C  
ATOM    104  C   LEU A  87      22.263  43.686 105.925  1.00 25.89           C  
ATOM    105  O   LEU A  87      22.216  44.311 104.865  1.00 25.89           O  
ATOM    106  CB  LEU A  87      20.439  42.164 106.703  1.00 22.13           C  
ATOM    107  CG  LEU A  87      19.253  43.009 106.233  1.00 22.13           C  
ATOM    108  CD1 LEU A  87      19.038  42.871 104.698  1.00 22.13           C  
ATOM    109  CD2 LEU A  87      18.032  42.560 107.025  1.00 22.13           C  
ATOM    110  N   SER A  88      22.711  44.210 107.066  1.00 25.15           N  
ATOM    111  CA  SER A  88      23.198  45.587 107.156  1.00 25.15           C  
ATOM    112  C   SER A  88      24.389  45.794 106.229  1.00 25.15           C  
ATOM    113  O   SER A  88      24.565  46.869 105.663  1.00 25.15           O  
ATOM    114  CB  SER A  88      23.611  45.907 108.588  1.00 17.58           C  
ATOM    115  OG  SER A  88      22.616  45.503 109.504  1.00 17.58           O  
ATOM    116  N   HIS A  89      25.205  44.753 106.090  1.00 39.97           N  
ATOM    117  CA  HIS A  89      26.386  44.782 105.235  1.00 39.97           C  
ATOM    118  C   HIS A  89      25.951  44.857 103.782  1.00 39.97           C  
ATOM    119  O   HIS A  89      26.507  45.615 102.984  1.00 39.97           O  
ATOM    120  CB  HIS A  89      27.238  43.521 105.465  1.00 28.99           C  
ATOM    121  CG  HIS A  89      28.066  43.570 106.715  1.00 28.99           C  
ATOM    122  ND1 HIS A  89      28.625  42.444 107.283  1.00 28.99           N  
ATOM    123  CD2 HIS A  89      28.406  44.609 107.519  1.00 28.99           C  
ATOM    124  CE1 HIS A  89      29.266  42.788 108.386  1.00 28.99           C  
ATOM    125  NE2 HIS A  89      29.147  44.096 108.552  1.00 28.99           N  
ATOM    126  N   PHE A  90      24.932  44.067 103.469  1.00 42.70           N  
ATOM    127  CA  PHE A  90      24.346  43.980 102.145  1.00 42.70           C  
ATOM    128  C   PHE A  90      23.873  45.367 101.680  1.00 42.70           C  
ATOM    129  O   PHE A  90      24.446  45.952 100.751  1.00 42.70           O  
ATOM    130  CB  PHE A  90      23.188  42.988 102.230  1.00 55.88           C  
ATOM    131  CG  PHE A  90      22.494  42.755 100.948  1.00 55.88           C  
ATOM    132  CD1 PHE A  90      23.209  42.463  99.802  1.00 55.88           C  
ATOM    133  CD2 PHE A  90      21.116  42.827 100.882  1.00 55.88           C  
ATOM    134  CE1 PHE A  90      22.553  42.245  98.597  1.00 55.88           C  
ATOM    135  CE2 PHE A  90      20.453  42.612  99.692  1.00 55.88           C  
ATOM    136  CZ  PHE A  90      21.170  42.319  98.543  1.00 55.88           C  
ATOM    137  N   LEU A  91      22.908  45.919 102.416  1.00 44.02           N  
ATOM    138  CA  LEU A  91      22.296  47.231 102.154  1.00 44.02           C  
ATOM    139  C   LEU A  91      23.271  48.414 102.220  1.00 44.02           C  
ATOM    140  O   LEU A  91      22.919  49.557 101.892  1.00 44.02           O  
ATOM    141  CB  LEU A  91      21.159  47.467 103.156  1.00 26.77           C  
ATOM    142  CG  LEU A  91      20.218  46.273 103.320  1.00 26.77           C  
ATOM    143  CD1 LEU A  91      19.144  46.614 104.326  1.00 26.77           C  
ATOM    144  CD2 LEU A  91      19.628  45.888 101.963  1.00 26.77           C  
ATOM    145  N   LYS A  92      24.465  48.156 102.738  1.00 52.16           N  
ATOM    146  CA  LYS A  92      25.478  49.190 102.826  1.00 52.16           C  
ATOM    147  C   LYS A  92      26.329  49.071 101.564  1.00 52.16           C  
ATOM    148  O   LYS A  92      26.726  50.079 100.976  1.00 52.16           O  
ATOM    149  CB  LYS A  92      26.320  49.003 104.092  1.00 41.46           C  
ATOM    150  CG  LYS A  92      27.462  50.005 104.263  1.00 41.46           C  
ATOM    151  CD  LYS A  92      26.963  51.442 104.382  1.00 41.46           C  
ATOM    152  CE  LYS A  92      28.128  52.399 104.597  1.00 41.46           C  
ATOM    153  NZ  LYS A  92      27.728  53.829 104.450  1.00 41.46           N  
ATOM    154  N   GLU A  93      26.584  47.834 101.137  1.00 62.86           N  
ATOM    155  CA  GLU A  93      27.371  47.583  99.934  1.00 62.86           C  
ATOM    156  C   GLU A  93      26.600  48.126  98.754  1.00 62.86           C  
ATOM    157  O   GLU A  93      27.138  48.891  97.947  1.00 62.86           O  
ATOM    158  CB  GLU A  93      27.596  46.090  99.749  1.00 68.58           C  
ATOM    159  CG  GLU A  93      28.638  45.527 100.687  1.00 68.58           C  
ATOM    160  CD  GLU A  93      28.493  44.031 100.873  1.00 68.58           C  
ATOM    161  OE1 GLU A  93      28.363  43.309  99.855  1.00 68.58           O  
ATOM    162  OE2 GLU A  93      28.500  43.579 102.041  1.00 68.58           O  
ATOM    163  N   LYS A  94      25.323  47.756  98.695  1.00 47.93           N  
ATOM    164  CA  LYS A  94      24.427  48.194  97.634  1.00 47.93           C  
ATOM    165  C   LYS A  94      24.249  49.716  97.596  1.00 47.93           C  
ATOM    166  O   LYS A  94      24.188  50.308  96.520  1.00 47.93           O  
ATOM    167  CB  LYS A  94      23.065  47.523  97.795  1.00 55.52           C  
ATOM    168  CG  LYS A  94      22.055  47.889  96.714  1.00 55.52           C  
ATOM    169  CD  LYS A  94      20.720  47.169  96.907  1.00 55.52           C  
ATOM    170  CE  LYS A  94      20.916  45.659  96.987  1.00 55.52           C  
ATOM    171  NZ  LYS A  94      21.736  45.103  95.860  1.00 55.52           N  
ATOM    172  N   GLY A  95      24.172  50.340  98.772  1.00 40.17           N  
ATOM    173  CA  GLY A  95      23.986  51.783  98.865  1.00 40.17           C  
ATOM    174  C   GLY A  95      22.525  52.185  98.742  1.00 40.17           C  
ATOM    175  O   GLY A  95      21.671  51.351  98.456  1.00 40.17           O  
ATOM    176  N   GLY A  96      22.217  53.453  98.984  1.00 51.22           N  
ATOM    177  CA  GLY A  96      20.835  53.885  98.862  1.00 51.22           C  
ATOM    178  C   GLY A  96      20.144  54.164 100.177  1.00 51.22           C  
ATOM    179  O   GLY A  96      19.745  55.296 100.435  1.00 51.22           O  
ATOM    180  N   LEU A  97      19.994  53.142 101.013  1.00 51.74           N  
ATOM    181  CA  LEU A  97      19.339  53.327 102.302  1.00 51.74           C  
ATOM    182  C   LEU A  97      20.131  54.334 103.120  1.00 51.74           C  
ATOM    183  O   LEU A  97      19.566  55.110 103.885  1.00 51.74           O  
ATOM    184  CB  LEU A  97      19.215  51.998 103.055  1.00 44.94           C  
ATOM    185  CG  LEU A  97      18.456  52.053 104.385  1.00 44.94           C  
ATOM    186  CD1 LEU A  97      17.030  52.454 104.145  1.00 44.94           C  
ATOM    187  CD2 LEU A  97      18.497  50.703 105.065  1.00 44.94           C  
ATOM    188  N   GLU A  98      21.445  54.338 102.922  1.00 41.69           N  
ATOM    189  CA  GLU A  98      22.332  55.260 103.630  1.00 41.69           C  
ATOM    190  C   GLU A  98      22.050  56.689 103.157  1.00 41.69           C  
ATOM    191  O   GLU A  98      22.171  56.989 101.972  1.00 41.69           O  
ATOM    192  CB  GLU A  98      23.793  54.859 103.366  1.00 36.83           C  
ATOM    193  CG  GLU A  98      24.844  55.896 103.757  1.00 36.83           C  
ATOM    194  CD  GLU A  98      24.997  56.079 105.252  1.00 36.83           C  
ATOM    195  OE1 GLU A  98      24.970  55.061 105.964  1.00 36.83           O  
ATOM    196  OE2 GLU A  98      25.165  57.235 105.710  1.00 36.83           O  
ATOM    197  N   GLY A  99      21.626  57.550 104.071  1.00 40.48           N  
ATOM    198  CA  GLY A  99      21.330  58.921 103.698  1.00 40.48           C  
ATOM    199  C   GLY A  99      19.866  59.204 103.367  1.00 40.48           C  
ATOM    200  O   GLY A  99      19.431  60.358 103.438  1.00 40.48           O  
ATOM    201  N   LEU A 100      19.109  58.161 103.013  1.00 42.81           N  
ATOM    202  CA  LEU A 100      17.682  58.262 102.665  1.00 42.81           C  
ATOM    203  C   LEU A 100      16.834  58.835 103.803  1.00 42.81           C  
ATOM    204  O   LEU A 100      16.996  58.428 104.959  1.00 42.81           O  
ATOM    205  CB  LEU A 100      17.155  56.869 102.327  1.00 28.97           C  
ATOM    206  CG  LEU A 100      15.815  56.701 101.613  1.00 28.97           C  
ATOM    207  CD1 LEU A 100      15.957  57.225 100.197  1.00 28.97           C  
ATOM    208  CD2 LEU A 100      15.419  55.229 101.584  1.00 28.97           C  
ATOM    209  N   ILE A 101      15.910  59.743 103.463  1.00 32.84           N  
ATOM    210  CA  ILE A 101      15.004  60.399 104.428  1.00 32.84           C  
ATOM    211  C   ILE A 101      13.991  59.364 104.935  1.00 32.84           C  
ATOM    212  O   ILE A 101      13.591  58.478 104.190  1.00 32.84           O  
ATOM    213  CB  ILE A 101      14.236  61.606 103.784  1.00 29.97           C  
ATOM    214  CG1 ILE A 101      15.104  62.326 102.731  1.00 29.97           C  
ATOM    215  CG2 ILE A 101      13.852  62.624 104.845  1.00 29.97           C  
ATOM    216  CD1 ILE A 101      15.162  61.628 101.316  1.00 29.97           C  
ATOM    217  N   HIS A 102      13.581  59.477 106.195  1.00 47.06           N  
ATOM    218  CA  HIS A 102      12.648  58.523 106.803  1.00 47.06           C  
ATOM    219  C   HIS A 102      11.157  58.881 106.774  1.00 47.06           C  
ATOM    220  O   HIS A 102      10.764  60.039 106.932  1.00 47.06           O  
ATOM    221  CB  HIS A 102      13.085  58.237 108.252  1.00 37.99           C  
ATOM    222  CG  HIS A 102      12.211  57.257 108.985  1.00 37.99           C  
ATOM    223  ND1 HIS A 102      11.177  57.653 109.804  1.00 37.99           N  
ATOM    224  CD2 HIS A 102      12.243  55.905 109.047  1.00 37.99           C  
ATOM    225  CE1 HIS A 102      10.611  56.587 110.340  1.00 37.99           C  
ATOM    226  NE2 HIS A 102      11.239  55.514 109.900  1.00 37.99           N  
ATOM    227  N   SER A 103      10.343  57.841 106.621  1.00 47.08           N  
ATOM    228  CA  SER A 103       8.888  57.934 106.597  1.00 47.08           C  
ATOM    229  C   SER A 103       8.380  56.535 106.933  1.00 47.08           C  
ATOM    230  O   SER A 103       8.983  55.539 106.503  1.00 47.08           O  
ATOM    231  CB  SER A 103       8.382  58.339 105.210  1.00 39.16           C  
ATOM    232  OG  SER A 103       8.467  57.277 104.268  1.00 39.16           O  
ATOM    233  N   GLN A 104       7.285  56.453 107.692  1.00 33.42           N  
ATOM    234  CA  GLN A 104       6.729  55.160 108.076  1.00 33.42           C  
ATOM    235  C   GLN A 104       6.465  54.267 106.882  1.00 33.42           C  
ATOM    236  O   GLN A 104       6.792  53.083 106.909  1.00 33.42           O  
ATOM    237  CB  GLN A 104       5.454  55.341 108.887  1.00 38.00           C  
ATOM    238  CG  GLN A 104       5.663  55.270 110.399  1.00 38.00           C  
ATOM    239  CD  GLN A 104       6.067  53.876 110.886  1.00 38.00           C  
ATOM    240  OE1 GLN A 104       6.565  53.715 112.003  1.00 38.00           O  
ATOM    241  NE2 GLN A 104       5.853  52.868 110.048  1.00 38.00           N  
ATOM    242  N   ARG A 105       5.924  54.862 105.823  1.00 33.56           N  
ATOM    243  CA  ARG A 105       5.604  54.167 104.581  1.00 33.56           C  
ATOM    244  C   ARG A 105       6.867  53.540 103.966  1.00 33.56           C  
ATOM    245  O   ARG A 105       6.809  52.475 103.353  1.00 33.56           O  
ATOM    246  CB  ARG A 105       4.917  55.165 103.639  1.00 40.97           C  
ATOM    247  CG  ARG A 105       5.112  54.972 102.160  1.00 40.97           C  
ATOM    248  CD  ARG A 105       4.467  53.723 101.662  1.00 40.97           C  
ATOM    249  NE  ARG A 105       3.035  53.724 101.900  1.00 40.97           N  
ATOM    250  CZ  ARG A 105       2.140  53.296 101.016  1.00 40.97           C  
ATOM    251  NH1 ARG A 105       2.539  52.841  99.829  1.00 40.97           N  
ATOM    252  NH2 ARG A 105       0.848  53.284 101.333  1.00 40.97           N  
ATOM    253  N   ARG A 106       8.013  54.192 104.157  1.00 44.05           N  
ATOM    254  CA  ARG A 106       9.277  53.677 103.636  1.00 44.05           C  
ATOM    255  C   ARG A 106       9.793  52.568 104.529  1.00 44.05           C  
ATOM    256  O   ARG A 106      10.194  51.502 104.048  1.00 44.05           O  
ATOM    257  CB  ARG A 106      10.304  54.790 103.525  1.00 42.66           C  
ATOM    258  CG  ARG A 106      10.170  55.572 102.251  1.00 42.66           C  
ATOM    259  CD  ARG A 106      10.976  56.843 102.333  1.00 42.66           C  
ATOM    260  NE  ARG A 106      11.308  57.328 101.004  1.00 42.66           N  
ATOM    261  CZ  ARG A 106      11.910  58.480 100.750  1.00 42.66           C  
ATOM    262  NH1 ARG A 106      12.257  59.297 101.733  1.00 42.66           N  
ATOM    263  NH2 ARG A 106      12.189  58.796  99.500  1.00 42.66           N  
ATOM    264  N   GLN A 107       9.770  52.824 105.834  1.00 43.13           N  
ATOM    265  CA  GLN A 107      10.202  51.837 106.813  1.00 43.13           C  
ATOM    266  C   GLN A 107       9.371  50.588 106.578  1.00 43.13           C  
ATOM    267  O   GLN A 107       9.869  49.488 106.734  1.00 43.13           O  
ATOM    268  CB  GLN A 107       9.983  52.364 108.232  1.00 23.07           C  
ATOM    269  CG  GLN A 107      10.381  51.412 109.366  1.00 23.07           C  
ATOM    270  CD  GLN A 107      10.199  52.026 110.759  1.00 23.07           C  
ATOM    271  OE1 GLN A 107      10.192  53.252 110.932  1.00 23.07           O  
ATOM    272  NE2 GLN A 107      10.074  51.166 111.762  1.00 23.07           N  
ATOM    273  N   ASP A 108       8.127  50.773 106.131  1.00 44.41           N  
ATOM    274  CA  ASP A 108       7.229  49.666 105.854  1.00 44.41           C  
ATOM    275  C   ASP A 108       7.607  48.981 104.552  1.00 44.41           C  
ATOM    276  O   ASP A 108       7.630  47.756 104.481  1.00 44.41           O  
ATOM    277  CB  ASP A 108       5.778  50.151 105.831  1.00 58.66           C  
ATOM    278  CG  ASP A 108       5.285  50.596 107.209  1.00 58.66           C  
ATOM    279  OD1 ASP A 108       6.086  50.616 108.166  1.00 58.66           O  
ATOM    280  OD2 ASP A 108       4.089  50.932 107.345  1.00 58.66           O  
ATOM    281  N   ILE A 109       7.942  49.772 103.537  1.00 41.01           N  
ATOM    282  CA  ILE A 109       8.349  49.237 102.234  1.00 41.01           C  
ATOM    283  C   ILE A 109       9.622  48.382 102.381  1.00 41.01           C  
ATOM    284  O   ILE A 109       9.791  47.362 101.700  1.00 41.01           O  
ATOM    285  CB  ILE A 109       8.568  50.396 101.211  1.00 26.16           C  
ATOM    286  CG1 ILE A 109       7.217  51.042 100.881  1.00 26.16           C  
ATOM    287  CG2 ILE A 109       9.272  49.896  99.934  1.00 26.16           C  
ATOM    288  CD1 ILE A 109       7.332  52.399 100.208  1.00 26.16           C  
ATOM    289  N   LEU A 110      10.491  48.790 103.304  1.00 41.84           N  
ATOM    290  CA  LEU A 110      11.729  48.075 103.578  1.00 41.84           C  
ATOM    291  C   LEU A 110      11.394  46.741 104.262  1.00 41.84           C  
ATOM    292  O   LEU A 110      11.896  45.692 103.858  1.00 41.84           O  
ATOM    293  CB  LEU A 110      12.635  48.926 104.477  1.00 31.59           C  
ATOM    294  CG  LEU A 110      14.161  48.824 104.333  1.00 31.59           C  
ATOM    295  CD1 LEU A 110      14.826  49.681 105.402  1.00 31.59           C  
ATOM    296  CD2 LEU A 110      14.639  47.386 104.444  1.00 31.59           C  
ATOM    297  N   ASP A 111      10.531  46.791 105.278  1.00 41.58           N  
ATOM    298  CA  ASP A 111      10.112  45.601 106.019  1.00 41.58           C  
ATOM    299  C   ASP A 111       9.540  44.547 105.089  1.00 41.58           C  
ATOM    300  O   ASP A 111       9.849  43.359 105.211  1.00 41.58           O  
ATOM    301  CB  ASP A 111       9.082  45.963 107.079  1.00 31.73           C  
ATOM    302  CG  ASP A 111       9.722  46.479 108.339  1.00 31.73           C  
ATOM    303  OD1 ASP A 111      10.438  47.492 108.267  1.00 31.73           O  
ATOM    304  OD2 ASP A 111       9.554  45.859 109.412  1.00 31.73           O  
ATOM    305  N   LEU A 112       8.728  44.993 104.139  1.00 39.53           N  
ATOM    306  CA  LEU A 112       8.130  44.091 103.178  1.00 39.53           C  
ATOM    307  C   LEU A 112       9.154  43.595 102.162  1.00 39.53           C  
ATOM    308  O   LEU A 112       9.190  42.402 101.892  1.00 39.53           O  
ATOM    309  CB  LEU A 112       6.952  44.768 102.475  1.00 29.56           C  
ATOM    310  CG  LEU A 112       5.711  45.089 103.316  1.00 29.56           C  
ATOM    311  CD1 LEU A 112       4.720  45.842 102.468  1.00 29.56           C  
ATOM    312  CD2 LEU A 112       5.078  43.803 103.832  1.00 29.56           C  
ATOM    313  N   TRP A 113      10.003  44.485 101.633  1.00 40.64           N  
ATOM    314  CA  TRP A 113      11.011  44.086 100.631  1.00 40.64           C  
ATOM    315  C   TRP A 113      11.921  42.953 101.121  1.00 40.64           C  
ATOM    316  O   TRP A 113      12.189  41.982 100.392  1.00 40.64           O  
ATOM    317  CB  TRP A 113      11.866  45.283 100.155  1.00 55.74           C  
ATOM    318  CG  TRP A 113      12.791  44.927  98.989  1.00 55.74           C  
ATOM    319  CD1 TRP A 113      12.421  44.409  97.771  1.00 55.74           C  
ATOM    320  CD2 TRP A 113      14.224  44.995  98.970  1.00 55.74           C  
ATOM    321  NE1 TRP A 113      13.531  44.139  97.007  1.00 55.74           N  
ATOM    322  CE2 TRP A 113      14.654  44.485  97.717  1.00 55.74           C  
ATOM    323  CE3 TRP A 113      15.196  45.424  99.891  1.00 55.74           C  
ATOM    324  CZ2 TRP A 113      16.019  44.404  97.360  1.00 55.74           C  
ATOM    325  CZ3 TRP A 113      16.556  45.340  99.533  1.00 55.74           C  
ATOM    326  CH2 TRP A 113      16.949  44.830  98.280  1.00 55.74           C  
ATOM    327  N   ILE A 114      12.376  43.082 102.365  1.00 41.38           N  
ATOM    328  CA  ILE A 114      13.237  42.090 102.984  1.00 41.38           C  
ATOM    329  C   ILE A 114      12.420  40.819 103.230  1.00 41.38           C  
ATOM    330  O   ILE A 114      12.908  39.712 103.008  1.00 41.38           O  
ATOM    331  CB  ILE A 114      13.818  42.630 104.311  1.00 27.03           C  
ATOM    332  CG1 ILE A 114      14.582  43.933 104.063  1.00 27.03           C  
ATOM    333  CG2 ILE A 114      14.730  41.602 104.962  1.00 27.03           C  
ATOM    334  CD1 ILE A 114      15.743  43.806 103.107  1.00 27.03           C  
ATOM    335  N   TYR A 115      11.159  40.997 103.628  1.00 38.86           N  
ATOM    336  CA  TYR A 115      10.243  39.883 103.904  1.00 38.86           C  
ATOM    337  C   TYR A 115       9.954  39.043 102.662  1.00 38.86           C  
ATOM    338  O   TYR A 115       9.809  37.815 102.736  1.00 38.86           O  
ATOM    339  CB  TYR A 115       8.938  40.415 104.501  1.00 36.00           C  
ATOM    340  CG  TYR A 115       7.775  39.445 104.455  1.00 36.00           C  
ATOM    341  CD1 TYR A 115       7.698  38.365 105.335  1.00 36.00           C  
ATOM    342  CD2 TYR A 115       6.734  39.617 103.533  1.00 36.00           C  
ATOM    343  CE1 TYR A 115       6.612  37.479 105.305  1.00 36.00           C  
ATOM    344  CE2 TYR A 115       5.644  38.739 103.495  1.00 36.00           C  
ATOM    345  CZ  TYR A 115       5.596  37.677 104.386  1.00 36.00           C  
ATOM    346  OH  TYR A 115       4.520  36.827 104.359  1.00 36.00           O  
ATOM    347  N   HIS A 116       9.877  39.711 101.520  1.00 53.50           N  
ATOM    348  CA  HIS A 116       9.617  39.031 100.272  1.00 53.50           C  
ATOM    349  C   HIS A 116      10.839  38.284  99.756  1.00 53.50           C  
ATOM    350  O   HIS A 116      10.748  37.098  99.428  1.00 53.50           O  
ATOM    351  CB  HIS A 116       9.087  40.025  99.248  1.00 51.55           C  
ATOM    352  CG  HIS A 116       7.612  40.244  99.356  1.00 51.55           C  
ATOM    353  ND1 HIS A 116       6.716  39.202  99.444  1.00 51.55           N  
ATOM    354  CD2 HIS A 116       6.873  41.379  99.393  1.00 51.55           C  
ATOM    355  CE1 HIS A 116       5.489  39.682  99.531  1.00 51.55           C  
ATOM    356  NE2 HIS A 116       5.557  41.001  99.502  1.00 51.55           N  
ATOM    357  N   THR A 117      11.990  38.959  99.774  1.00 51.52           N  
ATOM    358  CA  THR A 117      13.253  38.380  99.307  1.00 51.52           C  
ATOM    359  C   THR A 117      14.004  37.491 100.311  1.00 51.52           C  
ATOM    360  O   THR A 117      14.512  36.431  99.941  1.00 51.52           O  
ATOM    361  CB  THR A 117      14.224  39.474  98.832  1.00 57.91           C  
ATOM    362  OG1 THR A 117      14.672  40.241  99.953  1.00 57.91           O  
ATOM    363  CG2 THR A 117      13.542  40.400  97.863  1.00 57.91           C  
ATOM    364  N   GLN A 118      14.091  37.915 101.569  1.00 45.62           N  
ATOM    365  CA  GLN A 118      14.813  37.135 102.574  1.00 45.62           C  
ATOM    366  C   GLN A 118      13.920  36.183 103.337  1.00 45.62           C  
ATOM    367  O   GLN A 118      14.286  35.034 103.566  1.00 45.62           O  
ATOM    368  CB  GLN A 118      15.514  38.056 103.561  1.00 62.10           C  
ATOM    369  CG  GLN A 118      16.208  39.250 102.919  1.00 62.10           C  
ATOM    370  CD  GLN A 118      17.486  38.901 102.185  1.00 62.10           C  
ATOM    371  OE1 GLN A 118      18.264  39.786 101.849  1.00 62.10           O  
ATOM    372  NE2 GLN A 118      17.715  37.613 101.943  1.00 62.10           N  
ATOM    373  N   GLY A 119      12.749  36.668 103.732  1.00 43.26           N  
ATOM    374  CA  GLY A 119      11.819  35.838 104.471  1.00 43.26           C  
ATOM    375  C   GLY A 119      11.824  36.162 105.948  1.00 43.26           C  
ATOM    376  O   GLY A 119      11.416  35.337 106.757  1.00 43.26           O  
ATOM    377  N   TYR A 120      12.296  37.353 106.309  1.00 33.09           N  
ATOM    378  CA  TYR A 120      12.321  37.757 107.709  1.00 33.09           C  
ATOM    379  C   TYR A 120      10.991  38.391 108.133  1.00 33.09           C  
ATOM    380  O   TYR A 120      10.588  39.446 107.615  1.00 33.09           O  
ATOM    381  CB  TYR A 120      13.501  38.703 107.970  1.00 42.23           C  
ATOM    382  CG  TYR A 120      14.852  38.023 107.866  1.00 42.23           C  
ATOM    383  CD1 TYR A 120      15.120  36.861 108.588  1.00 42.23           C  
ATOM    384  CD2 TYR A 120      15.846  38.508 107.011  1.00 42.23           C  
ATOM    385  CE1 TYR A 120      16.329  36.192 108.452  1.00 42.23           C  
ATOM    386  CE2 TYR A 120      17.059  37.840 106.870  1.00 42.23           C  
ATOM    387  CZ  TYR A 120      17.284  36.686 107.594  1.00 42.23           C  
ATOM    388  OH  TYR A 120      18.447  35.986 107.449  1.00 42.23           O  
ATOM    389  N   PHE A 121      10.314  37.741 109.077  1.00 34.10           N  
ATOM    390  CA  PHE A 121       9.029  38.231 109.561  1.00 34.10           C  
ATOM    391  C   PHE A 121       9.216  39.693 109.976  1.00 34.10           C  
ATOM    392  O   PHE A 121      10.167  40.020 110.686  1.00 34.10           O  
ATOM    393  CB  PHE A 121       8.513  37.362 110.724  1.00 42.67           C  
ATOM    394  CG  PHE A 121       7.079  37.657 111.125  1.00 42.67           C  
ATOM    395  CD1 PHE A 121       6.010  37.109 110.422  1.00 42.67           C  
ATOM    396  CD2 PHE A 121       6.804  38.501 112.202  1.00 42.67           C  
ATOM    397  CE1 PHE A 121       4.706  37.400 110.791  1.00 42.67           C  
ATOM    398  CE2 PHE A 121       5.502  38.789 112.569  1.00 42.67           C  
ATOM    399  CZ  PHE A 121       4.457  38.240 111.861  1.00 42.67           C  
ATOM    400  N   PRO A 122       8.354  40.592 109.459  1.00 30.46           N  
ATOM    401  CA  PRO A 122       8.257  42.049 109.639  1.00 30.46           C  
ATOM    402  C   PRO A 122       8.166  42.624 111.053  1.00 30.46           C  
ATOM    403  O   PRO A 122       7.399  43.553 111.294  1.00 30.46           O  
ATOM    404  CB  PRO A 122       7.016  42.405 108.818  1.00 29.53           C  
ATOM    405  CG  PRO A 122       7.052  41.406 107.719  1.00 29.53           C  
ATOM    406  CD  PRO A 122       7.356  40.138 108.475  1.00 29.53           C  
ATOM    407  N   ASP A 123       8.985  42.127 111.974  1.00 33.63           N  
ATOM    408  CA  ASP A 123       8.961  42.643 113.340  1.00 33.63           C  
ATOM    409  C   ASP A 123      10.361  42.908 113.893  1.00 33.63           C  
ATOM    410  O   ASP A 123      10.558  42.909 115.110  1.00 33.63           O  
ATOM    411  CB  ASP A 123       8.193  41.685 114.263  1.00 42.36           C  
ATOM    412  CG  ASP A 123       8.905  40.342 114.466  1.00 42.36           C  
ATOM    413  OD1 ASP A 123       9.879  40.027 113.737  1.00 42.36           O  
ATOM    414  OD2 ASP A 123       8.461  39.590 115.366  1.00 42.36           O  
ATOM    415  N   TRP A 124      11.311  43.195 113.000  1.00 25.07           N  
ATOM    416  CA  TRP A 124      12.695  43.435 113.408  1.00 25.07           C  
ATOM    417  C   TRP A 124      13.238  44.861 113.222  1.00 25.07           C  
ATOM    418  O   TRP A 124      14.266  45.206 113.800  1.00 25.07           O  
ATOM    419  CB  TRP A 124      13.602  42.453 112.685  1.00 27.69           C  
ATOM    420  CG  TRP A 124      13.578  42.688 111.229  1.00 27.69           C  
ATOM    421  CD1 TRP A 124      12.796  42.059 110.312  1.00 27.69           C  
ATOM    422  CD2 TRP A 124      14.302  43.700 110.513  1.00 27.69           C  
ATOM    423  NE1 TRP A 124      12.971  42.625 109.068  1.00 27.69           N  
ATOM    424  CE2 TRP A 124      13.890  43.636 109.170  1.00 27.69           C  
ATOM    425  CE3 TRP A 124      15.258  44.661 110.885  1.00 27.69           C  
ATOM    426  CZ2 TRP A 124      14.395  44.491 108.199  1.00 27.69           C  
ATOM    427  CZ3 TRP A 124      15.755  45.508 109.922  1.00 27.69           C  
ATOM    428  CH2 TRP A 124      15.322  45.420 108.594  1.00 27.69           C  
ATOM    429  N   GLN A 125      12.615  45.669 112.370  1.00 17.58           N  
ATOM    430  CA  GLN A 125      13.105  47.033 112.160  1.00 17.58           C  
ATOM    431  C   GLN A 125      12.435  48.076 113.064  1.00 17.58           C  
ATOM    432  O   GLN A 125      11.746  48.973 112.583  1.00 17.58           O  
ATOM    433  CB  GLN A 125      12.958  47.431 110.694  1.00 18.67           C  
ATOM    434  CG  GLN A 125      13.540  48.780 110.390  1.00 18.67           C  
ATOM    435  CD  GLN A 125      13.384  49.167 108.955  1.00 18.67           C  
ATOM    436  OE1 GLN A 125      13.566  50.333 108.591  1.00 18.67           O  
ATOM    437  NE2 GLN A 125      13.057  48.192 108.113  1.00 18.67           N  
ATOM    438  N   ASN A 126      12.699  48.004 114.362  1.00 27.52           N  
ATOM    439  CA  ASN A 126      12.092  48.929 115.308  1.00 27.52           C  
ATOM    440  C   ASN A 126      13.071  49.885 115.977  1.00 27.52           C  
ATOM    441  O   ASN A 126      13.811  49.483 116.857  1.00 27.52           O  
ATOM    442  CB  ASN A 126      11.387  48.136 116.407  1.00 46.16           C  
ATOM    443  CG  ASN A 126      10.298  47.243 115.869  1.00 46.16           C  
ATOM    444  OD1 ASN A 126      10.223  46.060 116.214  1.00 46.16           O  
ATOM    445  ND2 ASN A 126       9.432  47.807 115.023  1.00 46.16           N  
ATOM    446  N   TYR A 127      13.027  51.163 115.626  1.00 28.57           N  
ATOM    447  CA  TYR A 127      13.907  52.150 116.247  1.00 28.57           C  
ATOM    448  C   TYR A 127      13.370  52.576 117.617  1.00 28.57           C  
ATOM    449  O   TYR A 127      12.501  51.910 118.147  1.00 28.57           O  
ATOM    450  CB  TYR A 127      14.089  53.301 115.290  1.00 18.93           C  
ATOM    451  CG  TYR A 127      14.542  52.776 113.948  1.00 18.93           C  
ATOM    452  CD1 TYR A 127      15.865  52.416 113.731  1.00 18.93           C  
ATOM    453  CD2 TYR A 127      13.641  52.574 112.925  1.00 18.93           C  
ATOM    454  CE1 TYR A 127      16.276  51.864 112.529  1.00 18.93           C  
ATOM    455  CE2 TYR A 127      14.035  52.025 111.722  1.00 18.93           C  
ATOM    456  CZ  TYR A 127      15.356  51.675 111.528  1.00 18.93           C  
ATOM    457  OH  TYR A 127      15.750  51.152 110.319  1.00 18.93           O  
ATOM    458  N   THR A 128      13.948  53.595 118.245  1.00 23.63           N  
ATOM    459  CA  THR A 128      13.478  54.015 119.571  1.00 23.63           C  
ATOM    460  C   THR A 128      12.737  55.344 119.466  1.00 23.63           C  
ATOM    461  O   THR A 128      12.995  56.118 118.546  1.00 23.63           O  
ATOM    462  CB  THR A 128      14.646  54.159 120.603  1.00 17.58           C  
ATOM    463  OG1 THR A 128      15.561  55.181 120.184  1.00 17.58           O  
ATOM    464  CG2 THR A 128      15.411  52.876 120.747  1.00 17.58           C  
ATOM    465  N   PRO A 129      11.820  55.639 120.412  1.00 31.51           N  
ATOM    466  CA  PRO A 129      11.063  56.893 120.384  1.00 31.51           C  
ATOM    467  C   PRO A 129      11.995  58.067 120.519  1.00 31.51           C  
ATOM    468  O   PRO A 129      12.884  58.045 121.361  1.00 31.51           O  
ATOM    469  CB  PRO A 129      10.184  56.781 121.628  1.00 26.93           C  
ATOM    470  CG  PRO A 129      11.034  56.048 122.569  1.00 26.93           C  
ATOM    471  CD  PRO A 129      11.548  54.927 121.672  1.00 26.93           C  
ATOM    472  N   GLY A 130      11.796  59.088 119.694  1.00 42.88           N  
ATOM    473  CA  GLY A 130      12.642  60.261 119.780  1.00 42.88           C  
ATOM    474  C   GLY A 130      12.341  61.053 121.040  1.00 42.88           C  
ATOM    475  O   GLY A 130      11.924  60.488 122.060  1.00 42.88           O  
ATOM    476  N   PRO A 131      12.626  62.361 121.027  1.00 40.62           N  
ATOM    477  CA  PRO A 131      13.202  63.018 119.855  1.00 40.62           C  
ATOM    478  C   PRO A 131      14.704  62.710 119.831  1.00 40.62           C  
ATOM    479  O   PRO A 131      15.256  62.199 120.813  1.00 40.62           O  
ATOM    480  CB  PRO A 131      12.933  64.487 120.143  1.00 45.58           C  
ATOM    481  CG  PRO A 131      13.113  64.549 121.646  1.00 45.58           C  
ATOM    482  CD  PRO A 131      12.361  63.328 122.109  1.00 45.58           C  
ATOM    483  N   GLY A 132      15.359  63.033 118.720  1.00 40.13           N  
ATOM    484  CA  GLY A 132      16.779  62.772 118.599  1.00 40.13           C  
ATOM    485  C   GLY A 132      17.052  61.537 117.763  1.00 40.13           C  
ATOM    486  O   GLY A 132      16.230  61.117 116.954  1.00 40.13           O  
ATOM    487  N   VAL A 133      18.197  60.919 117.995  1.00 42.73           N  
ATOM    488  CA  VAL A 133      18.577  59.739 117.241  1.00 42.73           C  
ATOM    489  C   VAL A 133      17.731  58.506 117.586  1.00 42.73           C  
ATOM    490  O   VAL A 133      17.440  58.233 118.761  1.00 42.73           O  
ATOM    491  CB  VAL A 133      20.062  59.443 117.463  1.00 29.98           C  
ATOM    492  CG1 VAL A 133      20.617  58.592 116.339  1.00 29.98           C  
ATOM    493  CG2 VAL A 133      20.827  60.740 117.601  1.00 29.98           C  
ATOM    494  N   ARG A 134      17.328  57.773 116.553  1.00 31.36           N  
ATOM    495  CA  ARG A 134      16.513  56.566 116.720  1.00 31.36           C  
ATOM    496  C   ARG A 134      17.355  55.298 116.590  1.00 31.36           C  
ATOM    497  O   ARG A 134      17.568  54.792 115.488  1.00 31.36           O  
ATOM    498  CB  ARG A 134      15.404  56.531 115.665  1.00 60.87           C  
ATOM    499  CG  ARG A 134      14.092  57.164 116.067  1.00 60.87           C  
ATOM    500  CD  ARG A 134      14.219  58.647 116.307  1.00 60.87           C  
ATOM    501  NE  ARG A 134      12.943  59.209 116.736  1.00 60.87           N  
ATOM    502  CZ  ARG A 134      12.541  60.449 116.481  1.00 60.87           C  
ATOM    503  NH1 ARG A 134      13.315  61.278 115.792  1.00 60.87           N  
ATOM    504  NH2 ARG A 134      11.358  60.861 116.913  1.00 60.87           N  
ATOM    505  N   TYR A 135      17.800  54.760 117.715  1.00 17.58           N  
ATOM    506  CA  TYR A 135      18.625  53.563 117.696  1.00 17.58           C  
ATOM    507  C   TYR A 135      17.752  52.343 117.485  1.00 17.58           C  
ATOM    508  O   TYR A 135      16.711  52.223 118.117  1.00 17.58           O  
ATOM    509  CB  TYR A 135      19.404  53.458 119.009  1.00 17.58           C  
ATOM    510  CG  TYR A 135      20.222  54.699 119.288  1.00 17.58           C  
ATOM    511  CD1 TYR A 135      21.297  55.061 118.469  1.00 17.58           C  
ATOM    512  CD2 TYR A 135      19.878  55.554 120.323  1.00 17.58           C  
ATOM    513  CE1 TYR A 135      21.988  56.247 118.678  1.00 17.58           C  
ATOM    514  CE2 TYR A 135      20.567  56.733 120.531  1.00 17.58           C  
ATOM    515  CZ  TYR A 135      21.612  57.069 119.710  1.00 17.58           C  
ATOM    516  OH  TYR A 135      22.264  58.254 119.937  1.00 17.58           O  
ATOM    517  N   PRO A 136      18.176  51.408 116.613  1.00 17.58           N  
ATOM    518  CA  PRO A 136      17.456  50.170 116.288  1.00 17.58           C  
ATOM    519  C   PRO A 136      17.389  49.272 117.496  1.00 17.58           C  
ATOM    520  O   PRO A 136      18.324  49.245 118.285  1.00 17.58           O  
ATOM    521  CB  PRO A 136      18.316  49.559 115.193  1.00 17.58           C  
ATOM    522  CG  PRO A 136      19.657  50.005 115.550  1.00 17.58           C  
ATOM    523  CD  PRO A 136      19.469  51.439 115.921  1.00 17.58           C  
ATOM    524  N   LEU A 137      16.286  48.549 117.659  1.00 17.58           N  
ATOM    525  CA  LEU A 137      16.156  47.695 118.833  1.00 17.58           C  
ATOM    526  C   LEU A 137      16.801  46.362 118.562  1.00 17.58           C  
ATOM    527  O   LEU A 137      17.237  45.681 119.493  1.00 17.58           O  
ATOM    528  CB  LEU A 137      14.696  47.504 119.270  1.00 17.58           C  
ATOM    529  CG  LEU A 137      13.708  48.656 119.472  1.00 17.58           C  
ATOM    530  CD1 LEU A 137      12.630  48.171 120.388  1.00 17.58           C  
ATOM    531  CD2 LEU A 137      14.353  49.880 120.059  1.00 17.58           C  
ATOM    532  N   THR A 138      16.893  45.999 117.288  1.00 21.47           N  
ATOM    533  CA  THR A 138      17.516  44.735 116.923  1.00 21.47           C  
ATOM    534  C   THR A 138      19.048  44.805 116.912  1.00 21.47           C  
ATOM    535  O   THR A 138      19.655  45.493 116.078  1.00 21.47           O  
ATOM    536  CB  THR A 138      16.971  44.238 115.581  1.00 25.79           C  
ATOM    537  OG1 THR A 138      15.633  43.775 115.787  1.00 25.79           O  
ATOM    538  CG2 THR A 138      17.824  43.110 115.000  1.00 25.79           C  
ATOM    539  N   PHE A 139      19.665  44.152 117.891  1.00 23.08           N  
ATOM    540  CA  PHE A 139      21.122  44.125 117.978  1.00 23.08           C  
ATOM    541  C   PHE A 139      21.618  43.460 116.708  1.00 23.08           C  
ATOM    542  O   PHE A 139      21.274  42.302 116.442  1.00 23.08           O  
ATOM    543  CB  PHE A 139      21.553  43.270 119.166  1.00 18.21           C  
ATOM    544  CG  PHE A 139      23.003  43.402 119.536  1.00 18.21           C  
ATOM    545  CD1 PHE A 139      23.627  44.640 119.553  1.00 18.21           C  
ATOM    546  CD2 PHE A 139      23.706  42.303 119.991  1.00 18.21           C  
ATOM    547  CE1 PHE A 139      24.917  44.784 120.038  1.00 18.21           C  
ATOM    548  CE2 PHE A 139      24.994  42.442 120.475  1.00 18.21           C  
ATOM    549  CZ  PHE A 139      25.595  43.688 120.497  1.00 18.21           C  
ATOM    550  N   GLY A 140      22.391  44.190 115.914  1.00 17.58           N  
ATOM    551  CA  GLY A 140      22.901  43.617 114.689  1.00 17.58           C  
ATOM    552  C   GLY A 140      22.438  44.380 113.476  1.00 17.58           C  
ATOM    553  O   GLY A 140      23.007  44.207 112.414  1.00 17.58           O  
ATOM    554  N   TRP A 141      21.345  45.133 113.593  1.00 17.58           N  
ATOM    555  CA  TRP A 141      20.838  45.954 112.485  1.00 17.58           C  
ATOM    556  C   TRP A 141      21.691  47.197 112.687  1.00 17.58           C  
ATOM    557  O   TRP A 141      21.540  47.902 113.695  1.00 17.58           O  
ATOM    558  CB  TRP A 141      19.343  46.251 112.693  1.00 17.58           C  
ATOM    559  CG  TRP A 141      18.698  47.191 111.700  1.00 17.58           C  
ATOM    560  CD1 TRP A 141      17.970  48.315 112.001  1.00 17.58           C  
ATOM    561  CD2 TRP A 141      18.775  47.142 110.266  1.00 17.58           C  
ATOM    562  NE1 TRP A 141      17.611  48.973 110.847  1.00 17.58           N  
ATOM    563  CE2 TRP A 141      18.096  48.278 109.770  1.00 17.58           C  
ATOM    564  CE3 TRP A 141      19.363  46.262 109.356  1.00 17.58           C  
ATOM    565  CZ2 TRP A 141      17.996  48.559 108.409  1.00 17.58           C  
ATOM    566  CZ3 TRP A 141      19.263  46.541 107.997  1.00 17.58           C  
ATOM    567  CH2 TRP A 141      18.586  47.680 107.540  1.00 17.58           C  
ATOM    568  N   CYS A 142      22.635  47.434 111.786  1.00 21.05           N  
ATOM    569  CA  CYS A 142      23.522  48.558 111.994  1.00 21.05           C  
ATOM    570  C   CYS A 142      23.026  49.885 111.434  1.00 21.05           C  
ATOM    571  O   CYS A 142      23.826  50.699 110.974  1.00 21.05           O  
ATOM    572  CB  CYS A 142      24.961  48.227 111.515  1.00 19.68           C  
ATOM    573  SG  CYS A 142      25.723  46.604 112.062  1.00 19.68           S  
ATOM    574  N   TYR A 143      21.717  50.128 111.495  1.00 17.58           N  
ATOM    575  CA  TYR A 143      21.153  51.395 111.005  1.00 17.58           C  
ATOM    576  C   TYR A 143      20.404  52.117 112.098  1.00 17.58           C  
ATOM    577  O   TYR A 143      19.866  51.488 112.989  1.00 17.58           O  
ATOM    578  CB  TYR A 143      20.226  51.179 109.823  1.00 17.58           C  
ATOM    579  CG  TYR A 143      20.952  50.937 108.528  1.00 17.58           C  
ATOM    580  CD1 TYR A 143      21.497  51.989 107.812  1.00 17.58           C  
ATOM    581  CD2 TYR A 143      21.076  49.662 108.007  1.00 17.58           C  
ATOM    582  CE1 TYR A 143      22.144  51.776 106.607  1.00 17.58           C  
ATOM    583  CE2 TYR A 143      21.715  49.432 106.812  1.00 17.58           C  
ATOM    584  CZ  TYR A 143      22.248  50.491 106.112  1.00 17.58           C  
ATOM    585  OH  TYR A 143      22.897  50.251 104.916  1.00 17.58           O  
ATOM    586  N   LYS A 144      20.419  53.443 112.051  1.00 17.77           N  
ATOM    587  CA  LYS A 144      19.741  54.263 113.036  1.00 17.77           C  
ATOM    588  C   LYS A 144      19.175  55.440 112.283  1.00 17.77           C  
ATOM    589  O   LYS A 144      19.587  55.679 111.164  1.00 17.77           O  
ATOM    590  CB  LYS A 144      20.729  54.761 114.075  1.00 17.58           C  
ATOM    591  CG  LYS A 144      21.838  55.637 113.532  1.00 17.58           C  
ATOM    592  CD  LYS A 144      22.736  56.123 114.670  1.00 17.58           C  
ATOM    593  CE  LYS A 144      23.971  56.850 114.139  1.00 17.58           C  
ATOM    594  NZ  LYS A 144      24.912  57.212 115.231  1.00 17.58           N  
ATOM    595  N   LEU A 145      18.220  56.167 112.860  1.00 28.73           N  
ATOM    596  CA  LEU A 145      17.646  57.326 112.172  1.00 28.73           C  
ATOM    597  C   LEU A 145      18.190  58.574 112.820  1.00 28.73           C  
ATOM    598  O   LEU A 145      18.025  58.785 114.022  1.00 28.73           O  
ATOM    599  CB  LEU A 145      16.129  57.308 112.248  1.00 17.58           C  
ATOM    600  CG  LEU A 145      15.543  55.988 111.761  1.00 17.58           C  
ATOM    601  CD1 LEU A 145      14.061  55.953 112.046  1.00 17.58           C  
ATOM    602  CD2 LEU A 145      15.856  55.812 110.290  1.00 17.58           C  
ATOM    603  N   VAL A 146      18.862  59.387 112.010  1.00 31.82           N  
ATOM    604  CA  VAL A 146      19.499  60.620 112.475  1.00 31.82           C  
ATOM    605  C   VAL A 146      18.776  61.872 111.978  1.00 31.82           C  
ATOM    606  O   VAL A 146      18.495  61.996 110.775  1.00 31.82           O  
ATOM    607  CB  VAL A 146      21.007  60.680 111.989  1.00 30.24           C  
ATOM    608  CG1 VAL A 146      21.671  61.983 112.411  1.00 30.24           C  
ATOM    609  CG2 VAL A 146      21.809  59.503 112.533  1.00 30.24           C  
ATOM    610  N   PRO A 147      18.402  62.779 112.903  1.00 32.21           N  
ATOM    611  CA  PRO A 147      17.720  64.016 112.521  1.00 32.21           C  
ATOM    612  C   PRO A 147      18.668  64.948 111.769  1.00 32.21           C  
ATOM    613  O   PRO A 147      19.807  65.181 112.198  1.00 32.21           O  
ATOM    614  CB  PRO A 147      17.293  64.613 113.868  1.00 27.89           C  
ATOM    615  CG  PRO A 147      18.268  64.054 114.832  1.00 27.89           C  
ATOM    616  CD  PRO A 147      18.380  62.620 114.365  1.00 27.89           C  
ATOM    617  N   VAL A 148      18.227  65.371 110.585  1.00 48.26           N  
ATOM    618  CA  VAL A 148      18.962  66.283 109.699  1.00 48.26           C  
ATOM    619  C   VAL A 148      18.009  66.681 108.581  1.00 48.26           C  
ATOM    620  O   VAL A 148      17.904  65.941 107.563  1.00 48.26           O  
ATOM    621  CB  VAL A 148      20.269  65.671 109.061  1.00 35.36           C  
ATOM    622  CG1 VAL A 148      21.517  66.471 109.525  1.00 35.36           C  
ATOM    623  CG2 VAL A 148      20.411  64.161 109.368  1.00 35.36           C  
ATOM    624  N   GLU A 179      10.738  66.838 112.849  1.00 60.52           N  
ATOM    625  CA  GLU A 179      12.140  66.379 113.022  1.00 60.52           C  
ATOM    626  C   GLU A 179      12.495  65.425 111.887  1.00 60.52           C  
ATOM    627  O   GLU A 179      12.525  64.213 112.084  1.00 60.52           O  
ATOM    628  CB  GLU A 179      12.296  65.669 114.375  1.00 49.12           C  
ATOM    629  CG  GLU A 179      13.753  65.418 114.800  1.00 49.12           C  
ATOM    630  CD  GLU A 179      13.904  65.013 116.269  1.00 49.12           C  
ATOM    631  OE1 GLU A 179      13.313  63.987 116.672  1.00 49.12           O  
ATOM    632  OE2 GLU A 179      14.618  65.725 117.020  1.00 49.12           O  
ATOM    633  N   VAL A 180      12.752  65.972 110.699  1.00 56.21           N  
ATOM    634  CA  VAL A 180      13.090  65.168 109.516  1.00 56.21           C  
ATOM    635  C   VAL A 180      14.254  64.203 109.782  1.00 56.21           C  
ATOM    636  O   VAL A 180      15.353  64.639 110.118  1.00 56.21           O  
ATOM    637  CB  VAL A 180      13.455  66.076 108.326  1.00 54.83           C  
ATOM    638  CG1 VAL A 180      13.457  65.265 107.037  1.00 54.83           C  
ATOM    639  CG2 VAL A 180      12.490  67.261 108.240  1.00 54.83           C  
ATOM    640  N   LEU A 181      14.016  62.903 109.616  1.00 50.48           N  
ATOM    641  CA  LEU A 181      15.053  61.898 109.876  1.00 50.48           C  
ATOM    642  C   LEU A 181      15.567  61.196 108.637  1.00 50.48           C  
ATOM    643  O   LEU A 181      14.870  61.142 107.629  1.00 50.48           O  
ATOM    644  CB  LEU A 181      14.522  60.805 110.804  1.00 48.36           C  
ATOM    645  CG  LEU A 181      13.866  61.141 112.138  1.00 48.36           C  
ATOM    646  CD1 LEU A 181      13.609  59.847 112.880  1.00 48.36           C  
ATOM    647  CD2 LEU A 181      14.748  62.050 112.960  1.00 48.36           C  
ATOM    648  N   GLU A 182      16.776  60.635 108.727  1.00 31.13           N  
ATOM    649  CA  GLU A 182      17.350  59.873 107.613  1.00 31.13           C  
ATOM    650  C   GLU A 182      18.178  58.680 108.069  1.00 31.13           C  
ATOM    651  O   GLU A 182      18.855  58.748 109.090  1.00 31.13           O  
ATOM    652  CB  GLU A 182      18.156  60.754 106.658  1.00 49.80           C  
ATOM    653  CG  GLU A 182      19.335  61.486 107.251  1.00 49.80           C  
ATOM    654  CD  GLU A 182      20.230  62.067 106.165  1.00 49.80           C  
ATOM    655  OE1 GLU A 182      21.136  61.339 105.706  1.00 49.80           O  
ATOM    656  OE2 GLU A 182      20.019  63.231 105.756  1.00 49.80           O  
ATOM    657  N   TRP A 183      18.063  57.567 107.354  1.00 25.06           N  
ATOM    658  CA  TRP A 183      18.817  56.365 107.699  1.00 25.06           C  
ATOM    659  C   TRP A 183      20.327  56.620 107.670  1.00 25.06           C  
ATOM    660  O   TRP A 183      20.825  57.329 106.786  1.00 25.06           O  
ATOM    661  CB  TRP A 183      18.478  55.220 106.738  1.00 34.30           C  
ATOM    662  CG  TRP A 183      17.254  54.429 107.127  1.00 34.30           C  
ATOM    663  CD1 TRP A 183      17.174  53.473 108.100  1.00 34.30           C  
ATOM    664  CD2 TRP A 183      15.932  54.518 106.547  1.00 34.30           C  
ATOM    665  NE1 TRP A 183      15.894  52.964 108.166  1.00 34.30           N  
ATOM    666  CE2 TRP A 183      15.116  53.586 107.224  1.00 34.30           C  
ATOM    667  CE3 TRP A 183      15.363  55.295 105.525  1.00 34.30           C  
ATOM    668  CZ2 TRP A 183      13.769  53.409 106.910  1.00 34.30           C  
ATOM    669  CZ3 TRP A 183      14.024  55.111 105.218  1.00 34.30           C  
ATOM    670  CH2 TRP A 183      13.247  54.178 105.908  1.00 34.30           C  
ATOM    671  N   ARG A 184      21.050  56.038 108.632  1.00 34.18           N  
ATOM    672  CA  ARG A 184      22.508  56.181 108.739  1.00 34.18           C  
ATOM    673  C   ARG A 184      23.145  54.924 109.308  1.00 34.18           C  
ATOM    674  O   ARG A 184      22.846  54.528 110.437  1.00 34.18           O  
ATOM    675  CB  ARG A 184      22.884  57.359 109.642  1.00 51.92           C  
ATOM    676  CG  ARG A 184      22.604  58.722 109.066  1.00 51.92           C  
ATOM    677  CD  ARG A 184      23.623  59.173 108.023  1.00 51.92           C  
ATOM    678  NE  ARG A 184      23.333  60.532 107.553  1.00 51.92           N  
ATOM    679  CZ  ARG A 184      23.246  61.614 108.337  1.00 51.92           C  
ATOM    680  NH1 ARG A 184      23.433  61.527 109.651  1.00 51.92           N  
ATOM    681  NH2 ARG A 184      22.929  62.793 107.811  1.00 51.92           N  
ATOM    682  N   PHE A 185      24.036  54.320 108.527  1.00 20.23           N  
ATOM    683  CA  PHE A 185      24.773  53.112 108.922  1.00 20.23           C  
ATOM    684  C   PHE A 185      25.872  53.484 109.906  1.00 20.23           C  
ATOM    685  O   PHE A 185      26.621  54.434 109.671  1.00 20.23           O  
ATOM    686  CB  PHE A 185      25.399  52.461 107.688  1.00 16.50           C  
ATOM    687  CG  PHE A 185      26.249  51.260 107.986  1.00 16.50           C  
ATOM    688  CD1 PHE A 185      27.517  51.404 108.522  1.00 16.50           C  
ATOM    689  CD2 PHE A 185      25.807  49.977 107.667  1.00 16.50           C  
ATOM    690  CE1 PHE A 185      28.331  50.293 108.738  1.00 16.50           C  
ATOM    691  CE2 PHE A 185      26.623  48.861 107.880  1.00 16.50           C  
ATOM    692  CZ  PHE A 185      27.882  49.023 108.409  1.00 16.50           C  
ATOM    693  N   ASP A 186      25.955  52.733 111.001  1.00 18.39           N  
ATOM    694  CA  ASP A 186      26.966  52.938 112.043  1.00 18.39           C  
ATOM    695  C   ASP A 186      27.218  51.546 112.608  1.00 18.39           C  
ATOM    696  O   ASP A 186      26.444  51.063 113.412  1.00 18.39           O  
ATOM    697  CB  ASP A 186      26.423  53.887 113.116  1.00 28.29           C  
ATOM    698  CG  ASP A 186      27.364  54.066 114.317  1.00 28.29           C  
ATOM    699  OD1 ASP A 186      28.402  53.375 114.410  1.00 28.29           O  
ATOM    700  OD2 ASP A 186      27.038  54.900 115.201  1.00 28.29           O  
ATOM    701  N   SER A 187      28.280  50.896 112.135  1.00 16.50           N  
ATOM    702  CA  SER A 187      28.651  49.548 112.557  1.00 16.50           C  
ATOM    703  C   SER A 187      28.913  49.367 114.055  1.00 16.50           C  
ATOM    704  O   SER A 187      28.983  48.239 114.535  1.00 16.50           O  
ATOM    705  CB  SER A 187      29.849  49.065 111.752  1.00 22.45           C  
ATOM    706  OG  SER A 187      30.988  49.856 112.033  1.00 22.45           O  
ATOM    707  N   ARG A 188      29.064  50.461 114.796  1.00 16.50           N  
ATOM    708  CA  ARG A 188      29.271  50.354 116.238  1.00 16.50           C  
ATOM    709  C   ARG A 188      28.083  49.687 116.913  1.00 16.50           C  
ATOM    710  O   ARG A 188      28.227  49.028 117.932  1.00 16.50           O  
ATOM    711  CB  ARG A 188      29.511  51.722 116.852  1.00 19.87           C  
ATOM    712  CG  ARG A 188      30.889  52.223 116.564  1.00 19.87           C  
ATOM    713  CD  ARG A 188      31.100  53.559 117.155  1.00 19.87           C  
ATOM    714  NE  ARG A 188      30.253  54.530 116.492  1.00 19.87           N  
ATOM    715  CZ  ARG A 188      30.011  55.737 116.991  1.00 19.87           C  
ATOM    716  NH1 ARG A 188      30.569  56.077 118.149  1.00 19.87           N  
ATOM    717  NH2 ARG A 188      29.197  56.587 116.362  1.00 19.87           N  
ATOM    718  N   LEU A 189      26.909  49.852 116.307  1.00 34.51           N  
ATOM    719  CA  LEU A 189      25.648  49.297 116.799  1.00 34.51           C  
ATOM    720  C   LEU A 189      25.681  47.766 116.912  1.00 34.51           C  
ATOM    721  O   LEU A 189      24.889  47.189 117.664  1.00 34.51           O  
ATOM    722  CB  LEU A 189      24.478  49.769 115.915  1.00 21.63           C  
ATOM    723  CG  LEU A 189      24.298  51.278 115.700  1.00 21.63           C  
ATOM    724  CD1 LEU A 189      23.387  51.558 114.535  1.00 21.63           C  
ATOM    725  CD2 LEU A 189      23.768  51.928 116.927  1.00 21.63           C  
ATOM    726  N   ALA A 190      26.591  47.118 116.173  1.00 23.36           N  
ATOM    727  CA  ALA A 190      26.752  45.652 116.238  1.00 23.36           C  
ATOM    728  C   ALA A 190      27.595  45.245 117.439  1.00 23.36           C  
ATOM    729  O   ALA A 190      27.735  44.052 117.728  1.00 23.36           O  
ATOM    730  CB  ALA A 190      27.396  45.119 115.001  1.00 18.40           C  
ATOM    731  N   PHE A 191      28.143  46.253 118.129  1.00 18.47           N  
ATOM    732  CA  PHE A 191      28.987  46.079 119.309  1.00 18.47           C  
ATOM    733  C   PHE A 191      28.372  46.681 120.578  1.00 18.47           C  
ATOM    734  O   PHE A 191      28.559  46.148 121.665  1.00 18.47           O  
ATOM    735  CB  PHE A 191      30.399  46.622 119.024  1.00 16.50           C  
ATOM    736  CG  PHE A 191      31.121  45.834 117.971  1.00 16.50           C  
ATOM    737  CD1 PHE A 191      31.409  44.487 118.181  1.00 16.50           C  
ATOM    738  CD2 PHE A 191      31.393  46.376 116.726  1.00 16.50           C  
ATOM    739  CE1 PHE A 191      31.930  43.705 117.176  1.00 16.50           C  
ATOM    740  CE2 PHE A 191      31.920  45.581 115.705  1.00 16.50           C  
ATOM    741  CZ  PHE A 191      32.184  44.253 115.939  1.00 16.50           C  
ATOM    742  N   HIS A 192      27.630  47.777 120.453  1.00 28.58           N  
ATOM    743  CA  HIS A 192      26.970  48.383 121.604  1.00 28.58           C  
ATOM    744  C   HIS A 192      25.463  48.377 121.331  1.00 28.58           C  
ATOM    745  O   HIS A 192      25.033  48.769 120.256  1.00 28.58           O  
ATOM    746  CB  HIS A 192      27.476  49.810 121.818  1.00 60.45           C  
ATOM    747  CG  HIS A 192      28.944  49.894 122.126  1.00 60.45           C  
ATOM    748  ND1 HIS A 192      29.920  49.847 121.150  1.00 60.45           N  
ATOM    749  CD2 HIS A 192      29.600  50.061 123.300  1.00 60.45           C  
ATOM    750  CE1 HIS A 192      31.108  49.989 121.705  1.00 60.45           C  
ATOM    751  NE2 HIS A 192      30.946  50.121 123.009  1.00 60.45           N  
ATOM    752  N   HIS A 193      24.671  47.826 122.246  1.00 20.91           N  
ATOM    753  CA  HIS A 193      23.208  47.797 122.077  1.00 20.91           C  
ATOM    754  C   HIS A 193      22.673  49.075 122.736  1.00 20.91           C  
ATOM    755  O   HIS A 193      22.019  49.027 123.776  1.00 20.91           O  
ATOM    756  CB  HIS A 193      22.629  46.569 122.770  1.00 20.57           C  
ATOM    757  CG  HIS A 193      21.275  46.162 122.291  1.00 20.57           C  
ATOM    758  ND1 HIS A 193      20.831  44.862 122.368  1.00 20.57           N  
ATOM    759  CD2 HIS A 193      20.255  46.870 121.758  1.00 20.57           C  
ATOM    760  CE1 HIS A 193      19.598  44.785 121.906  1.00 20.57           C  
ATOM    761  NE2 HIS A 193      19.224  45.991 121.530  1.00 20.57           N  
ATOM    762  N   VAL A 194      22.991  50.216 122.131  1.00 26.70           N  
ATOM    763  CA  VAL A 194      22.594  51.516 122.646  1.00 26.70           C  
ATOM    764  C   VAL A 194      21.098  51.677 122.861  1.00 26.70           C  
ATOM    765  O   VAL A 194      20.673  52.324 123.822  1.00 26.70           O  
ATOM    766  CB  VAL A 194      23.184  52.641 121.769  1.00 16.50           C  
ATOM    767  CG1 VAL A 194      22.835  52.425 120.342  1.00 16.50           C  
ATOM    768  CG2 VAL A 194      22.722  53.991 122.245  1.00 16.50           C  
ATOM    769  N   ALA A 195      20.305  51.034 122.006  1.00 32.34           N  
ATOM    770  CA  ALA A 195      18.842  51.073 122.100  1.00 32.34           C  
ATOM    771  C   ALA A 195      18.338  50.328 123.319  1.00 32.34           C  
ATOM    772  O   ALA A 195      17.151  50.102 123.448  1.00 32.34           O  
ATOM    773  CB  ALA A 195      18.221  50.459 120.867  1.00 26.13           C  
ATOM    774  N   ARG A 196      19.238  49.945 124.205  1.00 21.51           N  
ATOM    775  CA  ARG A 196      18.875  49.201 125.386  1.00 21.51           C  
ATOM    776  C   ARG A 196      19.547  49.840 126.589  1.00 21.51           C  
ATOM    777  O   ARG A 196      19.040  49.786 127.718  1.00 21.51           O  
ATOM    778  CB  ARG A 196      19.315  47.761 125.203  1.00 16.94           C  
ATOM    779  CG  ARG A 196      19.321  46.915 126.443  1.00 16.94           C  
ATOM    780  CD  ARG A 196      19.271  45.445 126.043  1.00 16.94           C  
ATOM    781  NE  ARG A 196      19.501  44.549 127.173  1.00 16.94           N  
ATOM    782  CZ  ARG A 196      19.273  43.239 127.152  1.00 16.94           C  
ATOM    783  NH1 ARG A 196      18.801  42.668 126.055  1.00 16.94           N  
ATOM    784  NH2 ARG A 196      19.497  42.502 128.235  1.00 16.94           N  
ATOM    785  N   GLU A 197      20.720  50.424 126.359  1.00 38.52           N  
ATOM    786  CA  GLU A 197      21.434  51.111 127.427  1.00 38.52           C  
ATOM    787  C   GLU A 197      20.480  52.256 127.724  1.00 38.52           C  
ATOM    788  O   GLU A 197      20.150  52.528 128.877  1.00 38.52           O  
ATOM    789  CB  GLU A 197      22.781  51.651 126.911  1.00 62.76           C  
ATOM    790  CG  GLU A 197      23.860  50.578 126.665  1.00 62.76           C  
ATOM    791  CD  GLU A 197      25.035  51.067 125.797  1.00 62.76           C  
ATOM    792  OE1 GLU A 197      25.242  52.300 125.670  1.00 62.76           O  
ATOM    793  OE2 GLU A 197      25.747  50.208 125.225  1.00 62.76           O  
ATOM    794  N   LEU A 198      19.917  52.781 126.633  1.00 31.28           N  
ATOM    795  CA  LEU A 198      18.976  53.903 126.618  1.00 31.28           C  
ATOM    796  C   LEU A 198      17.508  53.618 126.918  1.00 31.28           C  
ATOM    797  O   LEU A 198      16.946  54.266 127.784  1.00 31.28           O  
ATOM    798  CB  LEU A 198      19.075  54.635 125.275  1.00 28.63           C  
ATOM    799  CG  LEU A 198      20.068  55.792 125.136  1.00 28.63           C  
ATOM    800  CD1 LEU A 198      21.391  55.525 125.825  1.00 28.63           C  
ATOM    801  CD2 LEU A 198      20.254  56.065 123.667  1.00 28.63           C  
ATOM    802  N   HIS A 199      16.878  52.701 126.181  1.00 16.50           N  
ATOM    803  CA  HIS A 199      15.460  52.381 126.390  1.00 16.50           C  
ATOM    804  C   HIS A 199      15.239  50.933 126.808  1.00 16.50           C  
ATOM    805  O   HIS A 199      14.530  50.191 126.125  1.00 16.50           O  
ATOM    806  CB  HIS A 199      14.670  52.650 125.109  1.00 32.87           C  
ATOM    807  CG  HIS A 199      14.722  54.072 124.657  1.00 32.87           C  
ATOM    808  ND1 HIS A 199      13.948  55.060 125.227  1.00 32.87           N  
ATOM    809  CD2 HIS A 199      15.497  54.683 123.730  1.00 32.87           C  
ATOM    810  CE1 HIS A 199      14.251  56.220 124.671  1.00 32.87           C  
ATOM    811  NE2 HIS A 199      15.187  56.018 123.760  1.00 32.87           N  
ATOM    812  N   PRO A 200      15.671  50.572 128.027  1.00 26.86           N  
ATOM    813  CA  PRO A 200      15.524  49.194 128.505  1.00 26.86           C  
ATOM    814  C   PRO A 200      14.147  48.566 128.523  1.00 26.86           C  
ATOM    815  O   PRO A 200      14.058  47.337 128.541  1.00 26.86           O  
ATOM    816  CB  PRO A 200      16.141  49.253 129.894  1.00 18.02           C  
ATOM    817  CG  PRO A 200      15.782  50.624 130.345  1.00 18.02           C  
ATOM    818  CD  PRO A 200      16.085  51.461 129.131  1.00 18.02           C  
ATOM    819  N   GLU A 201      13.087  49.380 128.454  1.00 36.80           N  
ATOM    820  CA  GLU A 201      11.708  48.862 128.499  1.00 36.80           C  
ATOM    821  C   GLU A 201      11.420  47.829 127.428  1.00 36.80           C  
ATOM    822  O   GLU A 201      10.834  46.781 127.712  1.00 36.80           O  
ATOM    823  CB  GLU A 201      10.673  49.972 128.355  1.00 43.68           C  
ATOM    824  CG  GLU A 201      11.023  51.247 129.052  1.00 43.68           C  
ATOM    825  CD  GLU A 201      11.881  52.139 128.191  1.00 43.68           C  
ATOM    826  OE1 GLU A 201      11.375  52.643 127.158  1.00 43.68           O  
ATOM    827  OE2 GLU A 201      13.062  52.330 128.554  1.00 43.68           O  
ATOM    828  N   TYR A 202      11.831  48.131 126.197  1.00 25.65           N  
ATOM    829  CA  TYR A 202      11.607  47.232 125.083  1.00 25.65           C  
ATOM    830  C   TYR A 202      12.334  45.910 125.275  1.00 25.65           C  
ATOM    831  O   TYR A 202      12.257  45.045 124.415  1.00 25.65           O  
ATOM    832  CB  TYR A 202      12.043  47.895 123.777  1.00 33.94           C  
ATOM    833  CG  TYR A 202      11.465  49.280 123.596  1.00 33.94           C  
ATOM    834  CD1 TYR A 202      10.142  49.450 123.214  1.00 33.94           C  
ATOM    835  CD2 TYR A 202      12.216  50.419 123.882  1.00 33.94           C  
ATOM    836  CE1 TYR A 202       9.567  50.719 123.136  1.00 33.94           C  
ATOM    837  CE2 TYR A 202      11.650  51.697 123.808  1.00 33.94           C  
ATOM    838  CZ  TYR A 202      10.323  51.836 123.437  1.00 33.94           C  
ATOM    839  OH  TYR A 202       9.726  53.076 123.414  1.00 33.94           O  
ATOM    840  N   PHE A 203      13.039  45.738 126.394  1.00 38.86           N  
ATOM    841  CA  PHE A 203      13.777  44.489 126.642  1.00 38.86           C  
ATOM    842  C   PHE A 203      13.570  44.019 128.083  1.00 38.86           C  
ATOM    843  O   PHE A 203      14.535  44.153 128.877  1.00 23.55           O  
ATOM    844  CB  PHE A 203      15.294  44.656 126.340  1.00 23.55           C  
ATOM    845  CG  PHE A 203      15.593  45.505 125.120  1.00 23.55           C  
ATOM    846  CD1 PHE A 203      15.701  46.891 125.233  1.00 23.55           C  
ATOM    847  CD2 PHE A 203      15.733  44.931 123.865  1.00 23.55           C  
ATOM    848  CE1 PHE A 203      15.934  47.679 124.131  1.00 23.55           C  
ATOM    849  CE2 PHE A 203      15.970  45.725 122.752  1.00 23.55           C  
ATOM    850  CZ  PHE A 203      16.070  47.099 122.888  1.00 23.55           C  
TER     851      PHE A 203                                                      
ATOM    852  N   THR B  71       0.256  31.290  92.390  1.00 58.97           N  
ATOM    853  CA  THR B  71      -0.553  32.530  92.617  1.00 58.97           C  
ATOM    854  C   THR B  71       0.304  33.744  93.002  1.00 58.97           C  
ATOM    855  O   THR B  71       0.896  33.775  94.082  1.00 58.97           O  
ATOM    856  CB  THR B  71      -1.670  32.282  93.695  1.00 58.97           C  
ATOM    857  OG1 THR B  71      -2.855  31.796  93.052  1.00 58.97           O  
ATOM    858  CG2 THR B  71      -2.022  33.554  94.479  1.00 58.97           C  
ATOM    859  N   PRO B  72       0.407  34.745  92.100  1.00 53.04           N  
ATOM    860  CA  PRO B  72       1.188  35.966  92.348  1.00 53.04           C  
ATOM    861  C   PRO B  72       0.605  36.759  93.508  1.00 53.04           C  
ATOM    862  O   PRO B  72      -0.501  36.487  93.984  1.00 53.04           O  
ATOM    863  CB  PRO B  72       1.017  36.759  91.050  1.00 49.04           C  
ATOM    864  CG  PRO B  72       0.859  35.709  90.035  1.00 49.04           C  
ATOM    865  CD  PRO B  72      -0.076  34.723  90.709  1.00 49.04           C  
ATOM    866  N   GLN B  73       1.344  37.763  93.947  1.00 49.45           N  
ATOM    867  CA  GLN B  73       0.881  38.594  95.042  1.00 49.45           C  
ATOM    868  C   GLN B  73       0.336  39.897  94.449  1.00 49.45           C  
ATOM    869  O   GLN B  73       1.081  40.664  93.824  1.00 49.45           O  
ATOM    870  CB  GLN B  73       2.029  38.849  96.030  1.00 49.61           C  
ATOM    871  CG  GLN B  73       1.586  39.351  97.400  1.00 49.61           C  
ATOM    872  CD  GLN B  73       1.718  40.858  97.560  1.00 49.61           C  
ATOM    873  OE1 GLN B  73       2.057  41.344  98.635  1.00 49.61           O  
ATOM    874  NE2 GLN B  73       1.465  41.600  96.491  1.00 49.61           N  
ATOM    875  N   VAL B  74      -0.965  40.129  94.641  1.00 31.60           N  
ATOM    876  CA  VAL B  74      -1.654  41.322  94.125  1.00 31.60           C  
ATOM    877  C   VAL B  74      -1.067  42.695  94.486  1.00 31.60           C  
ATOM    878  O   VAL B  74      -0.460  42.887  95.549  1.00 31.60           O  
ATOM    879  CB  VAL B  74      -3.160  41.310  94.486  1.00 21.87           C  
ATOM    880  CG1 VAL B  74      -3.832  40.148  93.811  1.00 21.87           C  
ATOM    881  CG2 VAL B  74      -3.356  41.243  95.989  1.00 21.87           C  
ATOM    882  N   PRO B  75      -1.260  43.677  93.593  1.00 27.95           N  
ATOM    883  CA  PRO B  75      -0.788  45.049  93.737  1.00 27.95           C  
ATOM    884  C   PRO B  75      -1.128  45.670  95.085  1.00 27.95           C  
ATOM    885  O   PRO B  75      -1.944  45.148  95.823  1.00 27.95           O  
ATOM    886  CB  PRO B  75      -1.521  45.750  92.613  1.00 27.95           C  
ATOM    887  CG  PRO B  75      -1.495  44.730  91.552  1.00 27.95           C  
ATOM    888  CD  PRO B  75      -1.933  43.513  92.295  1.00 27.95           C  
ATOM    889  N   LEU B  76      -0.445  46.741  95.438  1.00 28.42           N  
ATOM    890  CA  LEU B  76      -0.718  47.403  96.681  1.00 28.42           C  
ATOM    891  C   LEU B  76      -1.860  48.372  96.440  1.00 28.42           C  
ATOM    892  O   LEU B  76      -2.023  48.897  95.324  1.00 28.42           O  
ATOM    893  CB  LEU B  76       0.507  48.175  97.184  1.00 28.42           C  
ATOM    894  CG  LEU B  76       1.439  47.525  98.209  1.00 28.42           C  
ATOM    895  CD1 LEU B  76       2.040  46.209  97.687  1.00 28.42           C  
ATOM    896  CD2 LEU B  76       2.537  48.511  98.517  1.00 28.42           C  
ATOM    897  N   ARG B  77      -2.630  48.626  97.486  1.00 19.00           N  
ATOM    898  CA  ARG B  77      -3.793  49.549  97.447  1.00 19.00           C  
ATOM    899  C   ARG B  77      -4.133  49.893  98.883  1.00 19.00           C  
ATOM    900  O   ARG B  77      -4.054  49.039  99.794  1.00 19.00           O  
ATOM    901  CB  ARG B  77      -4.990  48.860  96.753  1.00 13.55           C  
ATOM    902  CG  ARG B  77      -5.229  47.403  97.086  1.00 13.55           C  
ATOM    903  CD  ARG B  77      -6.611  47.074  96.625  1.00 13.55           C  
ATOM    904  NE  ARG B  77      -6.862  45.643  96.484  1.00 13.55           N  
ATOM    905  CZ  ARG B  77      -8.074  45.095  96.441  1.00 13.55           C  
ATOM    906  NH1 ARG B  77      -9.165  45.845  96.553  1.00 13.55           N  
ATOM    907  NH2 ARG B  77      -8.196  43.812  96.147  1.00 13.55           N  
ATOM    908  N   PRO B  78      -4.525  51.148  99.169  1.00 23.69           N  
ATOM    909  CA  PRO B  78      -4.834  51.536 100.536  1.00 23.69           C  
ATOM    910  C   PRO B  78      -6.148  50.953 101.058  1.00 23.69           C  
ATOM    911  O   PRO B  78      -7.082  50.768 100.278  1.00 23.69           O  
ATOM    912  CB  PRO B  78      -4.896  53.060 100.461  1.00 17.75           C  
ATOM    913  CG  PRO B  78      -5.357  53.320  99.092  1.00 17.75           C  
ATOM    914  CD  PRO B  78      -4.576  52.327  98.288  1.00 17.75           C  
ATOM    915  N   MET B  79      -6.216  50.691 102.344  1.00 23.13           N  
ATOM    916  CA  MET B  79      -7.440  50.175 102.955  1.00 23.13           C  
ATOM    917  C   MET B  79      -8.430  51.333 102.861  1.00 23.13           C  
ATOM    918  O   MET B  79      -8.026  52.499 102.822  1.00 23.13           O  
ATOM    919  CB  MET B  79      -7.169  49.823 104.411  1.00 17.75           C  
ATOM    920  CG  MET B  79      -8.371  49.440 105.238  1.00 17.75           C  
ATOM    921  SD  MET B  79      -9.219  48.037 104.554  1.00 17.75           S  
ATOM    922  CE  MET B  79      -8.232  46.683 105.071  1.00 17.75           C  
ATOM    923  N   THR B  80      -9.713  51.012 102.742  1.00 19.84           N  
ATOM    924  CA  THR B  80     -10.768  52.022 102.651  1.00 19.84           C  
ATOM    925  C   THR B  80     -11.961  51.573 103.492  1.00 19.84           C  
ATOM    926  O   THR B  80     -12.104  50.375 103.772  1.00 19.84           O  
ATOM    927  CB  THR B  80     -11.209  52.209 101.200  1.00 17.75           C  
ATOM    928  OG1 THR B  80     -11.775  50.995 100.694  1.00 17.75           O  
ATOM    929  CG2 THR B  80     -10.012  52.556 100.351  1.00 17.75           C  
ATOM    930  N   TYR B  81     -12.794  52.532 103.913  1.00 17.75           N  
ATOM    931  CA  TYR B  81     -13.991  52.247 104.720  1.00 17.75           C  
ATOM    932  C   TYR B  81     -14.776  51.060 104.131  1.00 17.75           C  
ATOM    933  O   TYR B  81     -14.896  50.019 104.767  1.00 17.75           O  
ATOM    934  CB  TYR B  81     -14.901  53.493 104.821  1.00 17.75           C  
ATOM    935  CG  TYR B  81     -16.150  53.284 105.646  1.00 17.75           C  
ATOM    936  CD1 TYR B  81     -17.295  52.726 105.083  1.00 17.75           C  
ATOM    937  CD2 TYR B  81     -16.172  53.590 107.000  1.00 17.75           C  
ATOM    938  CE1 TYR B  81     -18.433  52.469 105.845  1.00 17.75           C  
ATOM    939  CE2 TYR B  81     -17.307  53.341 107.782  1.00 17.75           C  
ATOM    940  CZ  TYR B  81     -18.434  52.776 107.197  1.00 17.75           C  
ATOM    941  OH  TYR B  81     -19.545  52.516 107.965  1.00 17.75           O  
ATOM    942  N   LYS B  82     -15.254  51.190 102.897  1.00 17.75           N  
ATOM    943  CA  LYS B  82     -15.994  50.097 102.322  1.00 17.75           C  
ATOM    944  C   LYS B  82     -15.190  48.807 102.313  1.00 17.75           C  
ATOM    945  O   LYS B  82     -15.735  47.742 102.641  1.00 17.75           O  
ATOM    946  CB  LYS B  82     -16.566  50.440 100.937  1.00 30.85           C  
ATOM    947  CG  LYS B  82     -15.616  51.014  99.914  1.00 30.85           C  
ATOM    948  CD  LYS B  82     -16.374  51.418  98.623  1.00 30.85           C  
ATOM    949  CE  LYS B  82     -15.428  52.014  97.542  1.00 30.85           C  
ATOM    950  NZ  LYS B  82     -16.119  52.544  96.316  1.00 30.85           N  
ATOM    951  N   ALA B  83     -13.885  48.896 102.040  1.00 17.75           N  
ATOM    952  CA  ALA B  83     -13.029  47.694 101.998  1.00 17.75           C  
ATOM    953  C   ALA B  83     -12.898  47.096 103.376  1.00 17.75           C  
ATOM    954  O   ALA B  83     -12.897  45.880 103.542  1.00 17.75           O  
ATOM    955  CB  ALA B  83     -11.657  48.029 101.452  1.00 18.56           C  
ATOM    956  N   ALA B  84     -12.793  47.984 104.354  1.00 17.75           N  
ATOM    957  CA  ALA B  84     -12.658  47.617 105.751  1.00 17.75           C  
ATOM    958  C   ALA B  84     -13.910  46.902 106.243  1.00 17.75           C  
ATOM    959  O   ALA B  84     -13.817  45.860 106.894  1.00 17.75           O  
ATOM    960  CB  ALA B  84     -12.381  48.870 106.593  1.00 17.75           C  
ATOM    961  N   VAL B  85     -15.077  47.458 105.912  1.00 19.85           N  
ATOM    962  CA  VAL B  85     -16.363  46.893 106.327  1.00 19.85           C  
ATOM    963  C   VAL B  85     -16.570  45.500 105.757  1.00 19.85           C  
ATOM    964  O   VAL B  85     -16.763  44.564 106.524  1.00 19.85           O  
ATOM    965  CB  VAL B  85     -17.572  47.785 105.923  1.00 17.75           C  
ATOM    966  CG1 VAL B  85     -18.850  47.136 106.349  1.00 17.75           C  
ATOM    967  CG2 VAL B  85     -17.466  49.163 106.541  1.00 17.75           C  
ATOM    968  N   ASP B  86     -16.516  45.358 104.427  1.00 19.11           N  
ATOM    969  CA  ASP B  86     -16.702  44.052 103.774  1.00 19.11           C  
ATOM    970  C   ASP B  86     -15.776  43.001 104.392  1.00 19.11           C  
ATOM    971  O   ASP B  86     -16.169  41.865 104.633  1.00 19.11           O  
ATOM    972  CB  ASP B  86     -16.394  44.133 102.276  1.00 37.42           C  
ATOM    973  CG  ASP B  86     -17.292  45.095 101.522  1.00 37.42           C  
ATOM    974  OD1 ASP B  86     -18.367  45.512 102.031  1.00 37.42           O  
ATOM    975  OD2 ASP B  86     -16.919  45.416 100.377  1.00 37.42           O  
ATOM    976  N   LEU B  87     -14.544  43.415 104.666  1.00 32.19           N  
ATOM    977  CA  LEU B  87     -13.505  42.569 105.236  1.00 32.19           C  
ATOM    978  C   LEU B  87     -13.828  42.117 106.655  1.00 32.19           C  
ATOM    979  O   LEU B  87     -13.533  40.985 107.027  1.00 32.19           O  
ATOM    980  CB  LEU B  87     -12.183  43.327 105.176  1.00 46.51           C  
ATOM    981  CG  LEU B  87     -10.890  42.685 105.649  1.00 46.51           C  
ATOM    982  CD1 LEU B  87     -10.662  41.349 104.964  1.00 46.51           C  
ATOM    983  CD2 LEU B  87      -9.757  43.650 105.338  1.00 46.51           C  
ATOM    984  N   SER B  88     -14.438  43.004 107.437  1.00 17.75           N  
ATOM    985  CA  SER B  88     -14.823  42.692 108.807  1.00 17.75           C  
ATOM    986  C   SER B  88     -15.926  41.646 108.770  1.00 17.75           C  
ATOM    987  O   SER B  88     -15.810  40.604 109.419  1.00 17.75           O  
ATOM    988  CB  SER B  88     -15.319  43.939 109.537  1.00 17.75           C  
ATOM    989  OG  SER B  88     -14.288  44.891 109.681  1.00 17.75           O  
ATOM    990  N   HIS B  89     -16.983  41.904 107.998  1.00 27.44           N  
ATOM    991  CA  HIS B  89     -18.069  40.935 107.895  1.00 27.44           C  
ATOM    992  C   HIS B  89     -17.484  39.599 107.447  1.00 27.44           C  
ATOM    993  O   HIS B  89     -17.941  38.549 107.879  1.00 27.44           O  
ATOM    994  CB  HIS B  89     -19.153  41.371 106.897  1.00 24.22           C  
ATOM    995  CG  HIS B  89     -19.929  42.582 107.323  1.00 24.22           C  
ATOM    996  ND1 HIS B  89     -20.512  43.437 106.414  1.00 24.22           N  
ATOM    997  CD2 HIS B  89     -20.179  43.096 108.547  1.00 24.22           C  
ATOM    998  CE1 HIS B  89     -21.084  44.436 107.067  1.00 24.22           C  
ATOM    999  NE2 HIS B  89     -20.896  44.260 108.358  1.00 24.22           N  
ATOM   1000  N   PHE B  90     -16.451  39.647 106.611  1.00 42.37           N  
ATOM   1001  CA  PHE B  90     -15.803  38.437 106.114  1.00 42.37           C  
ATOM   1002  C   PHE B  90     -15.142  37.619 107.208  1.00 42.37           C  
ATOM   1003  O   PHE B  90     -15.284  36.403 107.244  1.00 42.37           O  
ATOM   1004  CB  PHE B  90     -14.744  38.776 105.071  1.00 30.21           C  
ATOM   1005  CG  PHE B  90     -14.012  37.574 104.545  1.00 30.21           C  
ATOM   1006  CD1 PHE B  90     -14.711  36.493 104.020  1.00 30.21           C  
ATOM   1007  CD2 PHE B  90     -12.627  37.524 104.549  1.00 30.21           C  
ATOM   1008  CE1 PHE B  90     -14.045  35.385 103.503  1.00 30.21           C  
ATOM   1009  CE2 PHE B  90     -11.946  36.403 104.027  1.00 30.21           C  
ATOM   1010  CZ  PHE B  90     -12.666  35.336 103.506  1.00 30.21           C  
ATOM   1011  N   LEU B  91     -14.363  38.280 108.052  1.00 38.25           N  
ATOM   1012  CA  LEU B  91     -13.669  37.587 109.129  1.00 38.25           C  
ATOM   1013  C   LEU B  91     -14.625  37.229 110.269  1.00 38.25           C  
ATOM   1014  O   LEU B  91     -14.279  36.447 111.162  1.00 38.25           O  
ATOM   1015  CB  LEU B  91     -12.503  38.441 109.652  1.00 43.69           C  
ATOM   1016  CG  LEU B  91     -11.476  38.977 108.642  1.00 43.69           C  
ATOM   1017  CD1 LEU B  91     -10.435  39.776 109.393  1.00 43.69           C  
ATOM   1018  CD2 LEU B  91     -10.823  37.862 107.844  1.00 43.69           C  
ATOM   1019  N   LYS B  92     -15.810  37.843 110.253  1.00 24.53           N  
ATOM   1020  CA  LYS B  92     -16.847  37.598 111.265  1.00 24.53           C  
ATOM   1021  C   LYS B  92     -17.651  36.380 110.798  1.00 24.53           C  
ATOM   1022  O   LYS B  92     -17.919  35.466 111.567  1.00 24.53           O  
ATOM   1023  CB  LYS B  92     -17.727  38.851 111.407  1.00 47.29           C  
ATOM   1024  CG  LYS B  92     -18.875  38.747 112.385  1.00 47.29           C  
ATOM   1025  CD  LYS B  92     -18.405  38.405 113.777  1.00 47.29           C  
ATOM   1026  CE  LYS B  92     -19.598  38.248 114.718  1.00 47.29           C  
ATOM   1027  NZ  LYS B  92     -19.201  37.733 116.071  1.00 47.29           N  
ATOM   1028  N   GLU B  93     -17.984  36.366 109.512  1.00 48.79           N  
ATOM   1029  CA  GLU B  93     -18.711  35.267 108.906  1.00 48.79           C  
ATOM   1030  C   GLU B  93     -17.859  34.015 109.076  1.00 48.79           C  
ATOM   1031  O   GLU B  93     -18.356  32.963 109.466  1.00 48.79           O  
ATOM   1032  CB  GLU B  93     -18.921  35.540 107.414  1.00 68.75           C  
ATOM   1033  CG  GLU B  93     -19.950  36.639 107.097  1.00 68.75           C  
ATOM   1034  CD  GLU B  93     -19.865  37.171 105.652  1.00 68.75           C  
ATOM   1035  OE1 GLU B  93     -19.798  36.358 104.700  1.00 68.75           O  
ATOM   1036  OE2 GLU B  93     -19.884  38.408 105.462  1.00 68.75           O  
ATOM   1037  N   LYS B  94     -16.559  34.161 108.838  1.00 46.78           N  
ATOM   1038  CA  LYS B  94     -15.622  33.049 108.942  1.00 46.78           C  
ATOM   1039  C   LYS B  94     -15.419  32.591 110.384  1.00 46.78           C  
ATOM   1040  O   LYS B  94     -15.295  31.394 110.633  1.00 46.78           O  
ATOM   1041  CB  LYS B  94     -14.286  33.417 108.300  1.00 58.58           C  
ATOM   1042  CG  LYS B  94     -13.364  32.234 108.105  1.00 58.58           C  
ATOM   1043  CD  LYS B  94     -11.997  32.661 107.577  1.00 58.58           C  
ATOM   1044  CE  LYS B  94     -12.073  33.215 106.155  1.00 58.58           C  
ATOM   1045  NZ  LYS B  94     -12.600  32.215 105.177  1.00 58.58           N  
ATOM   1046  N   GLY B  95     -15.433  33.531 111.331  1.00 35.32           N  
ATOM   1047  CA  GLY B  95     -15.245  33.199 112.740  1.00 35.32           C  
ATOM   1048  C   GLY B  95     -13.813  32.815 113.080  1.00 35.32           C  
ATOM   1049  O   GLY B  95     -13.106  32.239 112.253  1.00 35.32           O  
ATOM   1050  N   GLY B  96     -13.374  33.115 114.297  1.00 41.76           N  
ATOM   1051  CA  GLY B  96     -12.011  32.775 114.678  1.00 41.76           C  
ATOM   1052  C   GLY B  96     -11.279  33.973 115.253  1.00 41.76           C  
ATOM   1053  O   GLY B  96     -10.730  33.908 116.353  1.00 41.76           O  
ATOM   1054  N   LEU B  97     -11.258  35.073 114.504  1.00 33.84           N  
ATOM   1055  CA  LEU B  97     -10.606  36.283 114.981  1.00 33.84           C  
ATOM   1056  C   LEU B  97     -11.402  36.810 116.164  1.00 33.84           C  
ATOM   1057  O   LEU B  97     -10.864  37.513 117.019  1.00 33.84           O  
ATOM   1058  CB  LEU B  97     -10.550  37.344 113.887  1.00 35.50           C  
ATOM   1059  CG  LEU B  97      -9.797  38.614 114.290  1.00 35.50           C  
ATOM   1060  CD1 LEU B  97      -8.322  38.296 114.519  1.00 35.50           C  
ATOM   1061  CD2 LEU B  97      -9.958  39.668 113.203  1.00 35.50           C  
ATOM   1062  N   GLU B  98     -12.699  36.492 116.189  1.00 52.53           N  
ATOM   1063  CA  GLU B  98     -13.581  36.918 117.276  1.00 52.53           C  
ATOM   1064  C   GLU B  98     -13.259  36.093 118.520  1.00 52.53           C  
ATOM   1065  O   GLU B  98     -13.323  34.859 118.488  1.00 52.53           O  
ATOM   1066  CB  GLU B  98     -15.059  36.757 116.871  1.00 50.25           C  
ATOM   1067  CG  GLU B  98     -16.097  36.852 118.029  1.00 50.25           C  
ATOM   1068  CD  GLU B  98     -16.308  38.256 118.602  1.00 50.25           C  
ATOM   1069  OE1 GLU B  98     -16.506  39.196 117.813  1.00 50.25           O  
ATOM   1070  OE2 GLU B  98     -16.327  38.416 119.846  1.00 50.25           O  
ATOM   1071  N   GLY B  99     -12.860  36.784 119.587  1.00 58.49           N  
ATOM   1072  CA  GLY B  99     -12.520  36.121 120.833  1.00 58.49           C  
ATOM   1073  C   GLY B  99     -11.051  35.744 120.986  1.00 58.49           C  
ATOM   1074  O   GLY B  99     -10.582  35.501 122.104  1.00 58.49           O  
ATOM   1075  N   LEU B 100     -10.323  35.713 119.867  1.00 45.82           N  
ATOM   1076  CA  LEU B 100      -8.898  35.363 119.833  1.00 45.82           C  
ATOM   1077  C   LEU B 100      -8.076  36.297 120.710  1.00 45.82           C  
ATOM   1078  O   LEU B 100      -8.313  37.500 120.728  1.00 45.82           O  
ATOM   1079  CB  LEU B 100      -8.389  35.449 118.397  1.00 40.31           C  
ATOM   1080  CG  LEU B 100      -7.054  34.799 118.068  1.00 40.31           C  
ATOM   1081  CD1 LEU B 100      -7.202  33.288 118.111  1.00 40.31           C  
ATOM   1082  CD2 LEU B 100      -6.601  35.243 116.692  1.00 40.31           C  
ATOM   1083  N   ILE B 101      -7.114  35.743 121.441  1.00 40.16           N  
ATOM   1084  CA  ILE B 101      -6.258  36.557 122.315  1.00 40.16           C  
ATOM   1085  C   ILE B 101      -5.230  37.348 121.465  1.00 40.16           C  
ATOM   1086  O   ILE B 101      -4.606  36.806 120.547  1.00 40.16           O  
ATOM   1087  CB  ILE B 101      -5.531  35.687 123.420  1.00 34.01           C  
ATOM   1088  CG1 ILE B 101      -6.382  34.467 123.834  1.00 34.01           C  
ATOM   1089  CG2 ILE B 101      -5.292  36.528 124.660  1.00 34.01           C  
ATOM   1090  CD1 ILE B 101      -6.311  33.259 122.874  1.00 34.01           C  
ATOM   1091  N   HIS B 102      -5.075  38.633 121.771  1.00 48.02           N  
ATOM   1092  CA  HIS B 102      -4.170  39.520 121.036  1.00 48.02           C  
ATOM   1093  C   HIS B 102      -2.682  39.409 121.352  1.00 48.02           C  
ATOM   1094  O   HIS B 102      -2.286  39.186 122.505  1.00 48.02           O  
ATOM   1095  CB  HIS B 102      -4.600  40.984 121.243  1.00 61.19           C  
ATOM   1096  CG  HIS B 102      -3.796  41.982 120.455  1.00 61.19           C  
ATOM   1097  ND1 HIS B 102      -2.711  42.653 120.980  1.00 61.19           N  
ATOM   1098  CD2 HIS B 102      -3.936  42.432 119.187  1.00 61.19           C  
ATOM   1099  CE1 HIS B 102      -2.219  43.473 120.071  1.00 61.19           C  
ATOM   1100  NE2 HIS B 102      -2.944  43.359 118.973  1.00 61.19           N  
ATOM   1101  N   SER B 103      -1.875  39.627 120.310  1.00 42.42           N  
ATOM   1102  CA  SER B 103      -0.402  39.640 120.378  1.00 42.42           C  
ATOM   1103  C   SER B 103       0.091  40.313 119.098  1.00 42.42           C  
ATOM   1104  O   SER B 103      -0.531  40.156 118.042  1.00 42.42           O  
ATOM   1105  CB  SER B 103       0.203  38.223 120.489  1.00 38.35           C  
ATOM   1106  OG  SER B 103       0.266  37.547 119.242  1.00 38.35           O  
ATOM   1107  N   GLN B 104       1.175  41.083 119.190  1.00 25.60           N  
ATOM   1108  CA  GLN B 104       1.735  41.750 118.007  1.00 25.60           C  
ATOM   1109  C   GLN B 104       2.023  40.746 116.881  1.00 25.60           C  
ATOM   1110  O   GLN B 104       1.782  41.029 115.711  1.00 25.60           O  
ATOM   1111  CB  GLN B 104       3.015  42.520 118.359  1.00 35.69           C  
ATOM   1112  CG  GLN B 104       2.791  43.969 118.744  1.00 35.69           C  
ATOM   1113  CD  GLN B 104       2.454  44.834 117.556  1.00 35.69           C  
ATOM   1114  OE1 GLN B 104       1.973  45.963 117.714  1.00 35.69           O  
ATOM   1115  NE2 GLN B 104       2.717  44.321 116.350  1.00 35.69           N  
ATOM   1116  N   ARG B 105       2.488  39.557 117.256  1.00 29.71           N  
ATOM   1117  CA  ARG B 105       2.802  38.489 116.307  1.00 29.71           C  
ATOM   1118  C   ARG B 105       1.567  38.078 115.509  1.00 29.71           C  
ATOM   1119  O   ARG B 105       1.671  37.673 114.352  1.00 29.71           O  
ATOM   1120  CB  ARG B 105       3.402  37.297 117.063  1.00 28.79           C  
ATOM   1121  CG  ARG B 105       3.328  35.917 116.399  1.00 28.79           C  
ATOM   1122  CD  ARG B 105       4.036  35.807 115.043  1.00 28.79           C  
ATOM   1123  NE  ARG B 105       5.429  36.240 115.051  1.00 28.79           N  
ATOM   1124  CZ  ARG B 105       6.412  35.627 114.391  1.00 28.79           C  
ATOM   1125  NH1 ARG B 105       6.168  34.537 113.665  1.00 28.79           N  
ATOM   1126  NH2 ARG B 105       7.650  36.113 114.453  1.00 28.79           N  
ATOM   1127  N   ARG B 106       0.392  38.206 116.127  1.00 34.53           N  
ATOM   1128  CA  ARG B 106      -0.888  37.874 115.487  1.00 34.53           C  
ATOM   1129  C   ARG B 106      -1.421  39.049 114.674  1.00 34.53           C  
ATOM   1130  O   ARG B 106      -1.840  38.874 113.523  1.00 34.53           O  
ATOM   1131  CB  ARG B 106      -1.893  37.464 116.546  1.00 34.07           C  
ATOM   1132  CG  ARG B 106      -1.573  36.120 117.114  1.00 34.07           C  
ATOM   1133  CD  ARG B 106      -2.457  35.803 118.281  1.00 34.07           C  
ATOM   1134  NE  ARG B 106      -2.532  34.360 118.426  1.00 34.07           N  
ATOM   1135  CZ  ARG B 106      -3.213  33.726 119.372  1.00 34.07           C  
ATOM   1136  NH1 ARG B 106      -3.901  34.402 120.291  1.00 34.07           N  
ATOM   1137  NH2 ARG B 106      -3.191  32.397 119.397  1.00 34.07           N  
ATOM   1138  N   GLN B 107      -1.390  40.238 115.282  1.00 25.73           N  
ATOM   1139  CA  GLN B 107      -1.818  41.477 114.631  1.00 25.73           C  
ATOM   1140  C   GLN B 107      -1.064  41.547 113.315  1.00 25.73           C  
ATOM   1141  O   GLN B 107      -1.669  41.752 112.265  1.00 25.73           O  
ATOM   1142  CB  GLN B 107      -1.477  42.693 115.509  1.00 19.18           C  
ATOM   1143  CG  GLN B 107      -1.853  44.041 114.908  1.00 19.18           C  
ATOM   1144  CD  GLN B 107      -2.028  45.141 115.958  1.00 19.18           C  
ATOM   1145  OE1 GLN B 107      -2.294  44.858 117.115  1.00 19.18           O  
ATOM   1146  NE2 GLN B 107      -1.908  46.398 115.544  1.00 19.18           N  
ATOM   1147  N   ASP B 108       0.232  41.222 113.395  1.00 35.64           N  
ATOM   1148  CA  ASP B 108       1.177  41.201 112.270  1.00 35.64           C  
ATOM   1149  C   ASP B 108       0.950  40.090 111.241  1.00 35.64           C  
ATOM   1150  O   ASP B 108       1.242  40.273 110.053  1.00 35.64           O  
ATOM   1151  CB  ASP B 108       2.615  41.100 112.789  1.00 44.47           C  
ATOM   1152  CG  ASP B 108       3.146  42.414 113.332  1.00 44.47           C  
ATOM   1153  OD1 ASP B 108       2.332  43.322 113.652  1.00 44.47           O  
ATOM   1154  OD2 ASP B 108       4.393  42.516 113.447  1.00 44.47           O  
ATOM   1155  N   ILE B 109       0.543  38.912 111.711  1.00 34.25           N  
ATOM   1156  CA  ILE B 109       0.258  37.804 110.798  1.00 34.25           C  
ATOM   1157  C   ILE B 109      -1.008  38.191 110.065  1.00 34.25           C  
ATOM   1158  O   ILE B 109      -1.167  37.843 108.894  1.00 34.25           O  
ATOM   1159  CB  ILE B 109       0.016  36.465 111.523  1.00 33.63           C  
ATOM   1160  CG1 ILE B 109       1.316  35.960 112.138  1.00 33.63           C  
ATOM   1161  CG2 ILE B 109      -0.523  35.419 110.543  1.00 33.63           C  
ATOM   1162  CD1 ILE B 109       1.149  34.698 112.965  1.00 33.63           C  
ATOM   1163  N   LEU B 110      -1.901  38.906 110.767  1.00 25.23           N  
ATOM   1164  CA  LEU B 110      -3.149  39.379 110.177  1.00 25.23           C  
ATOM   1165  C   LEU B 110      -2.765  40.316 109.023  1.00 25.23           C  
ATOM   1166  O   LEU B 110      -2.848  39.911 107.862  1.00 25.23           O  
ATOM   1167  CB  LEU B 110      -4.016  40.119 111.208  1.00 17.75           C  
ATOM   1168  CG  LEU B 110      -5.555  39.936 111.132  1.00 17.75           C  
ATOM   1169  CD1 LEU B 110      -6.252  40.781 112.168  1.00 17.75           C  
ATOM   1170  CD2 LEU B 110      -6.111  40.290 109.775  1.00 17.75           C  
ATOM   1171  N   ASP B 111      -2.291  41.524 109.349  1.00 21.60           N  
ATOM   1172  CA  ASP B 111      -1.864  42.513 108.350  1.00 21.60           C  
ATOM   1173  C   ASP B 111      -1.250  41.876 107.104  1.00 21.60           C  
ATOM   1174  O   ASP B 111      -1.539  42.289 105.982  1.00 21.60           O  
ATOM   1175  CB  ASP B 111      -0.844  43.504 108.939  1.00 21.23           C  
ATOM   1176  CG  ASP B 111      -1.465  44.480 109.924  1.00 21.23           C  
ATOM   1177  OD1 ASP B 111      -2.252  44.028 110.773  1.00 21.23           O  
ATOM   1178  OD2 ASP B 111      -1.183  45.699 109.861  1.00 21.23           O  
ATOM   1179  N   LEU B 112      -0.419  40.857 107.302  1.00 31.35           N  
ATOM   1180  CA  LEU B 112       0.240  40.170 106.194  1.00 31.35           C  
ATOM   1181  C   LEU B 112      -0.674  39.231 105.403  1.00 31.35           C  
ATOM   1182  O   LEU B 112      -0.524  39.112 104.186  1.00 31.35           O  
ATOM   1183  CB  LEU B 112       1.470  39.406 106.693  1.00 34.27           C  
ATOM   1184  CG  LEU B 112       2.688  40.201 107.166  1.00 34.27           C  
ATOM   1185  CD1 LEU B 112       3.675  39.267 107.843  1.00 34.27           C  
ATOM   1186  CD2 LEU B 112       3.340  40.896 105.981  1.00 34.27           C  
ATOM   1187  N   TRP B 113      -1.575  38.533 106.097  1.00 41.49           N  
ATOM   1188  CA  TRP B 113      -2.505  37.617 105.435  1.00 41.49           C  
ATOM   1189  C   TRP B 113      -3.455  38.405 104.539  1.00 41.49           C  
ATOM   1190  O   TRP B 113      -3.760  37.980 103.424  1.00 41.49           O  
ATOM   1191  CB  TRP B 113      -3.314  36.805 106.452  1.00 66.82           C  
ATOM   1192  CG  TRP B 113      -4.177  35.749 105.795  1.00 66.82           C  
ATOM   1193  CD1 TRP B 113      -3.761  34.757 104.947  1.00 66.82           C  
ATOM   1194  CD2 TRP B 113      -5.605  35.620 105.891  1.00 66.82           C  
ATOM   1195  NE1 TRP B 113      -4.838  34.026 104.502  1.00 66.82           N  
ATOM   1196  CE2 TRP B 113      -5.985  34.532 105.063  1.00 66.82           C  
ATOM   1197  CE3 TRP B 113      -6.609  36.319 106.586  1.00 66.82           C  
ATOM   1198  CZ2 TRP B 113      -7.326  34.126 104.918  1.00 66.82           C  
ATOM   1199  CZ3 TRP B 113      -7.946  35.911 106.441  1.00 66.82           C  
ATOM   1200  CH2 TRP B 113      -8.286  34.827 105.611  1.00 66.82           C  
ATOM   1201  N   ILE B 114      -3.941  39.538 105.055  1.00 42.95           N  
ATOM   1202  CA  ILE B 114      -4.841  40.424 104.314  1.00 42.95           C  
ATOM   1203  C   ILE B 114      -4.053  40.986 103.138  1.00 42.95           C  
ATOM   1204  O   ILE B 114      -4.511  40.946 102.009  1.00 42.95           O  
ATOM   1205  CB  ILE B 114      -5.356  41.609 105.194  1.00 35.79           C  
ATOM   1206  CG1 ILE B 114      -6.179  41.096 106.383  1.00 35.79           C  
ATOM   1207  CG2 ILE B 114      -6.150  42.598 104.353  1.00 35.79           C  
ATOM   1208  CD1 ILE B 114      -7.214  40.054 106.020  1.00 35.79           C  
ATOM   1209  N   TYR B 115      -2.843  41.462 103.418  1.00 43.36           N  
ATOM   1210  CA  TYR B 115      -1.946  42.023 102.410  1.00 43.36           C  
ATOM   1211  C   TYR B 115      -1.627  41.032 101.283  1.00 43.36           C  
ATOM   1212  O   TYR B 115      -1.621  41.404 100.119  1.00 43.36           O  
ATOM   1213  CB  TYR B 115      -0.657  42.490 103.097  1.00 45.17           C  
ATOM   1214  CG  TYR B 115       0.534  42.719 102.189  1.00 45.17           C  
ATOM   1215  CD1 TYR B 115       0.643  43.885 101.433  1.00 45.17           C  
ATOM   1216  CD2 TYR B 115       1.577  41.791 102.127  1.00 45.17           C  
ATOM   1217  CE1 TYR B 115       1.763  44.126 100.643  1.00 45.17           C  
ATOM   1218  CE2 TYR B 115       2.700  42.021 101.342  1.00 45.17           C  
ATOM   1219  CZ  TYR B 115       2.789  43.189 100.604  1.00 45.17           C  
ATOM   1220  OH  TYR B 115       3.902  43.424  99.828  1.00 45.17           O  
ATOM   1221  N   HIS B 116      -1.367  39.776 101.633  1.00 47.95           N  
ATOM   1222  CA  HIS B 116      -1.050  38.769 100.631  1.00 47.95           C  
ATOM   1223  C   HIS B 116      -2.236  38.504  99.749  1.00 47.95           C  
ATOM   1224  O   HIS B 116      -2.150  38.638  98.531  1.00 47.95           O  
ATOM   1225  CB  HIS B 116      -0.584  37.464 101.282  1.00 60.46           C  
ATOM   1226  CG  HIS B 116       0.891  37.419 101.528  1.00 60.46           C  
ATOM   1227  ND1 HIS B 116       1.814  37.628 100.526  1.00 60.46           N  
ATOM   1228  CD2 HIS B 116       1.602  37.245 102.666  1.00 60.46           C  
ATOM   1229  CE1 HIS B 116       3.031  37.591 101.037  1.00 60.46           C  
ATOM   1230  NE2 HIS B 116       2.929  37.360 102.334  1.00 60.46           N  
ATOM   1231  N   THR B 117      -3.360  38.183 100.380  1.00 35.74           N  
ATOM   1232  CA  THR B 117      -4.584  37.876  99.666  1.00 35.74           C  
ATOM   1233  C   THR B 117      -5.239  39.082  98.970  1.00 35.74           C  
ATOM   1234  O   THR B 117      -5.385  39.072  97.755  1.00 35.74           O  
ATOM   1235  CB  THR B 117      -5.598  37.133 100.585  1.00 19.28           C  
ATOM   1236  OG1 THR B 117      -5.978  37.972 101.676  1.00 19.28           O  
ATOM   1237  CG2 THR B 117      -4.978  35.857 101.170  1.00 19.28           C  
ATOM   1238  N   GLN B 118      -5.541  40.146  99.720  1.00 40.08           N  
ATOM   1239  CA  GLN B 118      -6.206  41.350  99.185  1.00 40.08           C  
ATOM   1240  C   GLN B 118      -5.289  42.415  98.588  1.00 40.08           C  
ATOM   1241  O   GLN B 118      -5.666  43.096  97.632  1.00 40.08           O  
ATOM   1242  CB  GLN B 118      -7.046  42.050 100.261  1.00 45.34           C  
ATOM   1243  CG  GLN B 118      -7.660  41.175 101.336  1.00 45.34           C  
ATOM   1244  CD  GLN B 118      -8.808  40.346 100.844  1.00 45.34           C  
ATOM   1245  OE1 GLN B 118      -9.494  39.706 101.646  1.00 45.34           O  
ATOM   1246  NE2 GLN B 118      -9.037  40.348  99.524  1.00 45.34           N  
ATOM   1247  N   GLY B 119      -4.140  42.643  99.215  1.00 22.90           N  
ATOM   1248  CA  GLY B 119      -3.213  43.655  98.717  1.00 22.90           C  
ATOM   1249  C   GLY B 119      -3.221  44.968  99.488  1.00 22.90           C  
ATOM   1250  O   GLY B 119      -2.488  45.898  99.159  1.00 22.90           O  
ATOM   1251  N   TYR B 120      -4.043  45.058 100.524  1.00 31.93           N  
ATOM   1252  CA  TYR B 120      -4.112  46.277 101.306  1.00 31.93           C  
ATOM   1253  C   TYR B 120      -2.823  46.562 102.035  1.00 31.93           C  
ATOM   1254  O   TYR B 120      -2.408  45.772 102.885  1.00 31.93           O  
ATOM   1255  CB  TYR B 120      -5.256  46.190 102.305  1.00 35.32           C  
ATOM   1256  CG  TYR B 120      -6.572  46.210 101.608  1.00 35.32           C  
ATOM   1257  CD1 TYR B 120      -6.915  47.274 100.777  1.00 35.32           C  
ATOM   1258  CD2 TYR B 120      -7.427  45.124 101.675  1.00 35.32           C  
ATOM   1259  CE1 TYR B 120      -8.062  47.243 100.023  1.00 35.32           C  
ATOM   1260  CE2 TYR B 120      -8.582  45.086 100.920  1.00 35.32           C  
ATOM   1261  CZ  TYR B 120      -8.891  46.145 100.102  1.00 35.32           C  
ATOM   1262  OH  TYR B 120     -10.044  46.103  99.375  1.00 35.32           O  
ATOM   1263  N   PHE B 121      -2.187  47.685 101.713  1.00 30.98           N  
ATOM   1264  CA  PHE B 121      -0.939  48.075 102.368  1.00 30.98           C  
ATOM   1265  C   PHE B 121      -1.104  47.983 103.892  1.00 30.98           C  
ATOM   1266  O   PHE B 121      -2.000  48.616 104.438  1.00 30.98           O  
ATOM   1267  CB  PHE B 121      -0.578  49.510 101.989  1.00 29.49           C  
ATOM   1268  CG  PHE B 121       0.823  49.901 102.371  1.00 29.49           C  
ATOM   1269  CD1 PHE B 121       1.905  49.524 101.575  1.00 29.49           C  
ATOM   1270  CD2 PHE B 121       1.072  50.609 103.538  1.00 29.49           C  
ATOM   1271  CE1 PHE B 121       3.201  49.841 101.932  1.00 29.49           C  
ATOM   1272  CE2 PHE B 121       2.367  50.931 103.901  1.00 29.49           C  
ATOM   1273  CZ  PHE B 121       3.432  50.542 103.095  1.00 29.49           C  
ATOM   1274  N   PRO B 122      -0.200  47.249 104.593  1.00 31.33           N  
ATOM   1275  CA  PRO B 122      -0.164  47.010 106.045  1.00 31.33           C  
ATOM   1276  C   PRO B 122      -0.033  48.199 107.000  1.00 31.33           C  
ATOM   1277  O   PRO B 122       0.789  48.164 107.898  1.00 31.33           O  
ATOM   1278  CB  PRO B 122       1.053  46.100 106.204  1.00 28.13           C  
ATOM   1279  CG  PRO B 122       1.209  45.460 104.898  1.00 28.13           C  
ATOM   1280  CD  PRO B 122       0.953  46.586 103.959  1.00 28.13           C  
ATOM   1281  N   ASP B 123      -0.868  49.215 106.873  1.00 36.24           N  
ATOM   1282  CA  ASP B 123      -0.766  50.374 107.759  1.00 36.24           C  
ATOM   1283  C   ASP B 123      -2.151  50.851 108.163  1.00 36.24           C  
ATOM   1284  O   ASP B 123      -2.365  52.038 108.443  1.00 36.24           O  
ATOM   1285  CB  ASP B 123       0.002  51.505 107.057  1.00 59.32           C  
ATOM   1286  CG  ASP B 123      -0.699  52.028 105.795  1.00 59.32           C  
ATOM   1287  OD1 ASP B 123      -1.653  51.388 105.284  1.00 59.32           O  
ATOM   1288  OD2 ASP B 123      -0.265  53.093 105.298  1.00 59.32           O  
ATOM   1289  N   TRP B 124      -3.059  49.885 108.283  1.00 26.60           N  
ATOM   1290  CA  TRP B 124      -4.465  50.137 108.586  1.00 26.60           C  
ATOM   1291  C   TRP B 124      -5.003  49.572 109.917  1.00 26.60           C  
ATOM   1292  O   TRP B 124      -5.983  50.095 110.478  1.00 26.60           O  
ATOM   1293  CB  TRP B 124      -5.307  49.585 107.411  1.00 17.75           C  
ATOM   1294  CG  TRP B 124      -5.184  48.069 107.199  1.00 17.75           C  
ATOM   1295  CD1 TRP B 124      -4.298  47.409 106.386  1.00 17.75           C  
ATOM   1296  CD2 TRP B 124      -5.956  47.054 107.846  1.00 17.75           C  
ATOM   1297  NE1 TRP B 124      -4.470  46.044 106.492  1.00 17.75           N  
ATOM   1298  CE2 TRP B 124      -5.482  45.802 107.382  1.00 17.75           C  
ATOM   1299  CE3 TRP B 124      -7.000  47.079 108.774  1.00 17.75           C  
ATOM   1300  CZ2 TRP B 124      -6.021  44.595 107.818  1.00 17.75           C  
ATOM   1301  CZ3 TRP B 124      -7.534  45.875 109.205  1.00 17.75           C  
ATOM   1302  CH2 TRP B 124      -7.043  44.651 108.726  1.00 17.75           C  
ATOM   1303  N   GLN B 125      -4.404  48.474 110.381  1.00 26.52           N  
ATOM   1304  CA  GLN B 125      -4.844  47.811 111.605  1.00 26.52           C  
ATOM   1305  C   GLN B 125      -4.247  48.416 112.862  1.00 26.52           C  
ATOM   1306  O   GLN B 125      -3.608  47.729 113.647  1.00 26.52           O  
ATOM   1307  CB  GLN B 125      -4.547  46.304 111.547  1.00 30.46           C  
ATOM   1308  CG  GLN B 125      -5.132  45.572 112.738  1.00 30.46           C  
ATOM   1309  CD  GLN B 125      -4.932  44.086 112.720  1.00 30.46           C  
ATOM   1310  OE1 GLN B 125      -5.190  43.418 113.719  1.00 30.46           O  
ATOM   1311  NE2 GLN B 125      -4.506  43.547 111.586  1.00 30.46           N  
ATOM   1312  N   ASN B 126      -4.466  49.703 113.064  1.00 35.85           N  
ATOM   1313  CA  ASN B 126      -3.928  50.344 114.241  1.00 35.85           C  
ATOM   1314  C   ASN B 126      -5.022  50.694 115.220  1.00 35.85           C  
ATOM   1315  O   ASN B 126      -5.989  51.377 114.878  1.00 35.85           O  
ATOM   1316  CB  ASN B 126      -3.130  51.591 113.864  1.00 48.29           C  
ATOM   1317  CG  ASN B 126      -2.017  51.293 112.879  1.00 48.29           C  
ATOM   1318  OD1 ASN B 126      -2.050  51.765 111.740  1.00 48.29           O  
ATOM   1319  ND2 ASN B 126      -1.038  50.487 113.297  1.00 48.29           N  
ATOM   1320  N   TYR B 127      -4.899  50.149 116.422  1.00 30.29           N  
ATOM   1321  CA  TYR B 127      -5.851  50.429 117.471  1.00 30.29           C  
ATOM   1322  C   TYR B 127      -5.284  51.586 118.287  1.00 30.29           C  
ATOM   1323  O   TYR B 127      -4.241  52.133 117.937  1.00 30.29           O  
ATOM   1324  CB  TYR B 127      -6.075  49.183 118.306  1.00 17.75           C  
ATOM   1325  CG  TYR B 127      -6.417  47.994 117.450  1.00 17.75           C  
ATOM   1326  CD1 TYR B 127      -7.728  47.714 117.111  1.00 17.75           C  
ATOM   1327  CD2 TYR B 127      -5.423  47.168 116.947  1.00 17.75           C  
ATOM   1328  CE1 TYR B 127      -8.048  46.635 116.284  1.00 17.75           C  
ATOM   1329  CE2 TYR B 127      -5.729  46.092 116.123  1.00 17.75           C  
ATOM   1330  CZ  TYR B 127      -7.047  45.832 115.795  1.00 17.75           C  
ATOM   1331  OH  TYR B 127      -7.359  44.769 114.978  1.00 17.75           O  
ATOM   1332  N   THR B 128      -5.997  52.011 119.321  1.00 49.42           N  
ATOM   1333  CA  THR B 128      -5.534  53.120 120.141  1.00 49.42           C  
ATOM   1334  C   THR B 128      -4.687  52.660 121.324  1.00 49.42           C  
ATOM   1335  O   THR B 128      -4.564  51.457 121.589  1.00 49.42           O  
ATOM   1336  CB  THR B 128      -6.720  53.936 120.674  1.00 60.78           C  
ATOM   1337  OG1 THR B 128      -7.628  53.069 121.362  1.00 60.78           O  
ATOM   1338  CG2 THR B 128      -7.430  54.621 119.546  1.00 60.78           C  
ATOM   1339  N   PRO B 129      -4.041  53.619 122.020  1.00 56.81           N  
ATOM   1340  CA  PRO B 129      -3.207  53.280 123.182  1.00 56.81           C  
ATOM   1341  C   PRO B 129      -4.074  53.028 124.427  1.00 56.81           C  
ATOM   1342  O   PRO B 129      -5.036  53.762 124.679  1.00 56.81           O  
ATOM   1343  CB  PRO B 129      -2.332  54.524 123.338  1.00 51.58           C  
ATOM   1344  CG  PRO B 129      -3.261  55.634 122.891  1.00 51.58           C  
ATOM   1345  CD  PRO B 129      -3.894  55.047 121.661  1.00 51.58           C  
ATOM   1346  N   GLY B 130      -3.755  51.970 125.174  1.00 62.65           N  
ATOM   1347  CA  GLY B 130      -4.503  51.648 126.382  1.00 62.65           C  
ATOM   1348  C   GLY B 130      -4.238  52.594 127.550  1.00 62.65           C  
ATOM   1349  O   GLY B 130      -3.810  53.736 127.344  1.00 62.65           O  
ATOM   1350  N   PRO B 131      -4.541  52.178 128.791  1.00 55.64           N  
ATOM   1351  CA  PRO B 131      -5.121  50.881 129.155  1.00 55.64           C  
ATOM   1352  C   PRO B 131      -6.633  50.815 128.888  1.00 55.64           C  
ATOM   1353  O   PRO B 131      -7.315  51.845 128.818  1.00 55.64           O  
ATOM   1354  CB  PRO B 131      -4.816  50.794 130.649  1.00 48.34           C  
ATOM   1355  CG  PRO B 131      -4.942  52.224 131.081  1.00 48.34           C  
ATOM   1356  CD  PRO B 131      -4.207  52.963 129.993  1.00 48.34           C  
ATOM   1357  N   GLY B 132      -7.146  49.600 128.736  1.00 63.20           N  
ATOM   1358  CA  GLY B 132      -8.568  49.429 128.491  1.00 63.20           C  
ATOM   1359  C   GLY B 132      -8.917  48.851 127.133  1.00 63.20           C  
ATOM   1360  O   GLY B 132      -8.265  47.911 126.667  1.00 63.20           O  
ATOM   1361  N   VAL B 133      -9.971  49.393 126.519  1.00 64.86           N  
ATOM   1362  CA  VAL B 133     -10.426  48.946 125.204  1.00 64.86           C  
ATOM   1363  C   VAL B 133      -9.596  49.620 124.115  1.00 64.86           C  
ATOM   1364  O   VAL B 133      -9.301  50.817 124.194  1.00 64.86           O  
ATOM   1365  CB  VAL B 133     -11.910  49.292 124.953  1.00 55.05           C  
ATOM   1366  CG1 VAL B 133     -12.454  48.462 123.799  1.00 55.05           C  
ATOM   1367  CG2 VAL B 133     -12.724  49.098 126.212  1.00 55.05           C  
ATOM   1368  N   ARG B 134      -9.194  48.835 123.118  1.00 55.98           N  
ATOM   1369  CA  ARG B 134      -8.410  49.346 122.003  1.00 55.98           C  
ATOM   1370  C   ARG B 134      -9.306  49.518 120.783  1.00 55.98           C  
ATOM   1371  O   ARG B 134      -9.702  48.541 120.150  1.00 55.98           O  
ATOM   1372  CB  ARG B 134      -7.253  48.404 121.698  1.00 68.75           C  
ATOM   1373  CG  ARG B 134      -5.938  48.775 122.376  1.00 68.75           C  
ATOM   1374  CD  ARG B 134      -6.009  48.762 123.904  1.00 68.75           C  
ATOM   1375  NE  ARG B 134      -4.707  49.060 124.516  1.00 68.75           N  
ATOM   1376  CZ  ARG B 134      -4.226  48.462 125.604  1.00 68.75           C  
ATOM   1377  NH1 ARG B 134      -4.927  47.521 126.222  1.00 68.75           N  
ATOM   1378  NH2 ARG B 134      -3.043  48.814 126.086  1.00 68.75           N  
ATOM   1379  N   TYR B 135      -9.667  50.768 120.504  1.00 44.15           N  
ATOM   1380  CA  TYR B 135     -10.531  51.094 119.374  1.00 44.15           C  
ATOM   1381  C   TYR B 135      -9.690  51.284 118.133  1.00 44.15           C  
ATOM   1382  O   TYR B 135      -8.654  51.947 118.165  1.00 44.15           O  
ATOM   1383  CB  TYR B 135     -11.357  52.353 119.643  1.00 54.35           C  
ATOM   1384  CG  TYR B 135     -12.204  52.248 120.881  1.00 54.35           C  
ATOM   1385  CD1 TYR B 135     -13.134  51.216 121.033  1.00 54.35           C  
ATOM   1386  CD2 TYR B 135     -12.038  53.144 121.928  1.00 54.35           C  
ATOM   1387  CE1 TYR B 135     -13.864  51.079 122.204  1.00 54.35           C  
ATOM   1388  CE2 TYR B 135     -12.762  53.015 123.097  1.00 54.35           C  
ATOM   1389  CZ  TYR B 135     -13.670  51.985 123.229  1.00 54.35           C  
ATOM   1390  OH  TYR B 135     -14.367  51.848 124.405  1.00 54.35           O  
ATOM   1391  N   PRO B 136     -10.143  50.716 117.007  1.00 36.43           N  
ATOM   1392  CA  PRO B 136      -9.444  50.799 115.720  1.00 36.43           C  
ATOM   1393  C   PRO B 136      -9.423  52.213 115.146  1.00 36.43           C  
ATOM   1394  O   PRO B 136     -10.395  52.961 115.297  1.00 36.43           O  
ATOM   1395  CB  PRO B 136     -10.236  49.828 114.852  1.00 37.81           C  
ATOM   1396  CG  PRO B 136     -11.623  49.921 115.429  1.00 37.81           C  
ATOM   1397  CD  PRO B 136     -11.397  49.945 116.895  1.00 37.81           C  
ATOM   1398  N   LEU B 137      -8.301  52.599 114.540  1.00 32.16           N  
ATOM   1399  CA  LEU B 137      -8.185  53.943 113.957  1.00 32.16           C  
ATOM   1400  C   LEU B 137      -8.847  54.019 112.587  1.00 32.16           C  
ATOM   1401  O   LEU B 137      -9.280  55.086 112.150  1.00 32.16           O  
ATOM   1402  CB  LEU B 137      -6.720  54.381 113.815  1.00 39.17           C  
ATOM   1403  CG  LEU B 137      -5.784  54.469 115.022  1.00 39.17           C  
ATOM   1404  CD1 LEU B 137      -4.680  55.449 114.676  1.00 39.17           C  
ATOM   1405  CD2 LEU B 137      -6.520  54.935 116.265  1.00 39.17           C  
ATOM   1406  N   THR B 138      -8.874  52.890 111.895  1.00 26.58           N  
ATOM   1407  CA  THR B 138      -9.475  52.841 110.586  1.00 26.58           C  
ATOM   1408  C   THR B 138     -10.986  52.707 110.704  1.00 26.58           C  
ATOM   1409  O   THR B 138     -11.482  51.648 111.098  1.00 26.58           O  
ATOM   1410  CB  THR B 138      -8.913  51.666 109.762  1.00 17.75           C  
ATOM   1411  OG1 THR B 138      -7.557  51.936 109.389  1.00 17.75           O  
ATOM   1412  CG2 THR B 138      -9.715  51.462 108.504  1.00 17.75           C  
ATOM   1413  N   PHE B 139     -11.705  53.802 110.428  1.00 29.82           N  
ATOM   1414  CA  PHE B 139     -13.179  53.821 110.454  1.00 29.82           C  
ATOM   1415  C   PHE B 139     -13.585  52.732 109.463  1.00 29.82           C  
ATOM   1416  O   PHE B 139     -13.089  52.722 108.336  1.00 29.82           O  
ATOM   1417  CB  PHE B 139     -13.677  55.183 109.932  1.00 17.75           C  
ATOM   1418  CG  PHE B 139     -15.167  55.444 110.119  1.00 17.75           C  
ATOM   1419  CD1 PHE B 139     -15.849  55.010 111.242  1.00 17.75           C  
ATOM   1420  CD2 PHE B 139     -15.850  56.258 109.214  1.00 17.75           C  
ATOM   1421  CE1 PHE B 139     -17.166  55.404 111.453  1.00 17.75           C  
ATOM   1422  CE2 PHE B 139     -17.160  56.646 109.430  1.00 17.75           C  
ATOM   1423  CZ  PHE B 139     -17.812  56.226 110.542  1.00 17.75           C  
ATOM   1424  N   GLY B 140     -14.411  51.781 109.895  1.00 17.75           N  
ATOM   1425  CA  GLY B 140     -14.844  50.714 109.003  1.00 17.75           C  
ATOM   1426  C   GLY B 140     -14.298  49.349 109.371  1.00 17.75           C  
ATOM   1427  O   GLY B 140     -14.689  48.354 108.775  1.00 17.75           O  
ATOM   1428  N   TRP B 141     -13.290  49.312 110.239  1.00 28.66           N  
ATOM   1429  CA  TRP B 141     -12.716  48.051 110.713  1.00 28.66           C  
ATOM   1430  C   TRP B 141     -13.487  47.906 112.008  1.00 28.66           C  
ATOM   1431  O   TRP B 141     -13.272  48.661 112.971  1.00 28.66           O  
ATOM   1432  CB  TRP B 141     -11.211  48.170 110.973  1.00 17.75           C  
ATOM   1433  CG  TRP B 141     -10.586  46.974 111.648  1.00 17.75           C  
ATOM   1434  CD1 TRP B 141      -9.950  46.968 112.860  1.00 17.75           C  
ATOM   1435  CD2 TRP B 141     -10.526  45.617 111.163  1.00 17.75           C  
ATOM   1436  NE1 TRP B 141      -9.503  45.696 113.157  1.00 17.75           N  
ATOM   1437  CE2 TRP B 141      -9.850  44.853 112.135  1.00 17.75           C  
ATOM   1438  CE3 TRP B 141     -10.986  44.978 110.012  1.00 17.75           C  
ATOM   1439  CZ2 TRP B 141      -9.619  43.490 111.984  1.00 17.75           C  
ATOM   1440  CZ3 TRP B 141     -10.751  43.607 109.866  1.00 17.75           C  
ATOM   1441  CH2 TRP B 141     -10.081  42.886 110.849  1.00 17.75           C  
ATOM   1442  N   CYS B 142     -14.475  47.015 111.940  1.00 37.13           N  
ATOM   1443  CA  CYS B 142     -15.418  46.724 113.011  1.00 37.13           C  
ATOM   1444  C   CYS B 142     -14.887  45.869 114.168  1.00 37.13           C  
ATOM   1445  O   CYS B 142     -15.663  45.212 114.861  1.00 37.13           O  
ATOM   1446  CB  CYS B 142     -16.694  46.101 112.400  1.00 36.06           C  
ATOM   1447  SG  CYS B 142     -17.607  47.108 111.147  1.00 36.06           S  
ATOM   1448  N   TYR B 143     -13.574  45.898 114.391  1.00 28.81           N  
ATOM   1449  CA  TYR B 143     -12.955  45.139 115.491  1.00 28.81           C  
ATOM   1450  C   TYR B 143     -12.180  45.992 116.471  1.00 28.81           C  
ATOM   1451  O   TYR B 143     -11.454  46.903 116.084  1.00 28.81           O  
ATOM   1452  CB  TYR B 143     -12.008  44.086 114.973  1.00 18.31           C  
ATOM   1453  CG  TYR B 143     -12.697  42.892 114.434  1.00 18.31           C  
ATOM   1454  CD1 TYR B 143     -13.045  41.852 115.265  1.00 18.31           C  
ATOM   1455  CD2 TYR B 143     -12.968  42.777 113.082  1.00 18.31           C  
ATOM   1456  CE1 TYR B 143     -13.639  40.725 114.772  1.00 18.31           C  
ATOM   1457  CE2 TYR B 143     -13.563  41.645 112.573  1.00 18.31           C  
ATOM   1458  CZ  TYR B 143     -13.893  40.627 113.428  1.00 18.31           C  
ATOM   1459  OH  TYR B 143     -14.473  39.494 112.947  1.00 18.31           O  
ATOM   1460  N   LYS B 144     -12.306  45.663 117.746  1.00 35.27           N  
ATOM   1461  CA  LYS B 144     -11.602  46.400 118.771  1.00 35.27           C  
ATOM   1462  C   LYS B 144     -10.846  45.413 119.649  1.00 35.27           C  
ATOM   1463  O   LYS B 144     -10.917  44.202 119.414  1.00 35.27           O  
ATOM   1464  CB  LYS B 144     -12.592  47.227 119.588  1.00 34.87           C  
ATOM   1465  CG  LYS B 144     -13.748  46.435 120.199  1.00 34.87           C  
ATOM   1466  CD  LYS B 144     -14.687  47.356 120.974  1.00 34.87           C  
ATOM   1467  CE  LYS B 144     -15.800  46.591 121.690  1.00 34.87           C  
ATOM   1468  NZ  LYS B 144     -16.731  47.491 122.467  1.00 34.87           N  
ATOM   1469  N   LEU B 145     -10.027  45.922 120.572  1.00 45.66           N  
ATOM   1470  CA  LEU B 145      -9.286  45.045 121.484  1.00 45.66           C  
ATOM   1471  C   LEU B 145      -9.820  45.302 122.886  1.00 45.66           C  
ATOM   1472  O   LEU B 145      -9.856  46.443 123.354  1.00 45.66           O  
ATOM   1473  CB  LEU B 145      -7.758  45.258 121.405  1.00 26.85           C  
ATOM   1474  CG  LEU B 145      -7.045  44.923 120.084  1.00 26.85           C  
ATOM   1475  CD1 LEU B 145      -5.566  45.135 120.206  1.00 26.85           C  
ATOM   1476  CD2 LEU B 145      -7.314  43.503 119.677  1.00 26.85           C  
ATOM   1477  N   VAL B 146     -10.341  44.239 123.497  1.00 46.01           N  
ATOM   1478  CA  VAL B 146     -10.911  44.311 124.839  1.00 46.01           C  
ATOM   1479  C   VAL B 146     -10.173  43.420 125.831  1.00 46.01           C  
ATOM   1480  O   VAL B 146      -9.935  42.231 125.571  1.00 46.01           O  
ATOM   1481  CB  VAL B 146     -12.407  43.916 124.844  1.00 33.03           C  
ATOM   1482  CG1 VAL B 146     -12.940  43.896 126.259  1.00 33.03           C  
ATOM   1483  CG2 VAL B 146     -13.208  44.898 124.005  1.00 33.03           C  
ATOM   1484  N   PRO B 147      -9.770  44.004 126.971  1.00 52.05           N  
ATOM   1485  CA  PRO B 147      -9.057  43.301 128.038  1.00 52.05           C  
ATOM   1486  C   PRO B 147      -9.994  42.337 128.738  1.00 52.05           C  
ATOM   1487  O   PRO B 147     -10.995  42.741 129.327  1.00 52.05           O  
ATOM   1488  CB  PRO B 147      -8.629  44.437 128.965  1.00 55.18           C  
ATOM   1489  CG  PRO B 147      -9.727  45.466 128.786  1.00 55.18           C  
ATOM   1490  CD  PRO B 147      -9.927  45.437 127.289  1.00 55.18           C  
ATOM   1491  N   VAL B 148      -9.701  41.051 128.619  1.00 68.65           N  
ATOM   1492  CA  VAL B 148     -10.522  40.030 129.254  1.00 68.65           C  
ATOM   1493  C   VAL B 148      -9.636  38.904 129.766  1.00 68.65           C  
ATOM   1494  O   VAL B 148      -8.858  38.367 128.941  1.00 68.65           O  
ATOM   1495  CB  VAL B 148     -11.599  39.458 128.276  1.00 61.97           C  
ATOM   1496  CG1 VAL B 148     -12.289  38.227 128.884  1.00 61.97           C  
ATOM   1497  CG2 VAL B 148     -12.650  40.524 127.967  1.00 61.97           C  
ATOM   1498  N   GLU B 179      -2.082  44.929 129.619  1.00 53.85           N  
ATOM   1499  CA  GLU B 179      -3.055  43.892 130.068  1.00 53.85           C  
ATOM   1500  C   GLU B 179      -3.330  42.903 128.955  1.00 53.85           C  
ATOM   1501  O   GLU B 179      -2.998  43.155 127.801  1.00 53.85           O  
ATOM   1502  CB  GLU B 179      -4.358  44.552 130.514  1.00 44.88           C  
ATOM   1503  CG  GLU B 179      -4.991  45.427 129.446  1.00 44.88           C  
ATOM   1504  CD  GLU B 179      -5.657  46.683 130.000  1.00 44.88           C  
ATOM   1505  OE1 GLU B 179      -6.581  46.572 130.837  1.00 44.88           O  
ATOM   1506  OE2 GLU B 179      -5.266  47.791 129.581  1.00 44.88           O  
ATOM   1507  N   VAL B 180      -3.909  41.763 129.316  1.00 58.12           N  
ATOM   1508  CA  VAL B 180      -4.233  40.716 128.348  1.00 58.12           C  
ATOM   1509  C   VAL B 180      -5.470  41.121 127.575  1.00 58.12           C  
ATOM   1510  O   VAL B 180      -6.562  41.216 128.138  1.00 58.12           O  
ATOM   1511  CB  VAL B 180      -4.528  39.370 129.029  1.00 53.39           C  
ATOM   1512  CG1 VAL B 180      -4.595  38.261 127.984  1.00 53.39           C  
ATOM   1513  CG2 VAL B 180      -3.481  39.075 130.085  1.00 53.39           C  
ATOM   1514  N   LEU B 181      -5.293  41.335 126.277  1.00 57.00           N  
ATOM   1515  CA  LEU B 181      -6.388  41.742 125.418  1.00 57.00           C  
ATOM   1516  C   LEU B 181      -6.817  40.643 124.455  1.00 57.00           C  
ATOM   1517  O   LEU B 181      -6.130  39.619 124.302  1.00 57.00           O  
ATOM   1518  CB  LEU B 181      -5.981  42.960 124.599  1.00 24.73           C  
ATOM   1519  CG  LEU B 181      -5.489  44.214 125.301  1.00 24.73           C  
ATOM   1520  CD1 LEU B 181      -5.295  45.297 124.261  1.00 24.73           C  
ATOM   1521  CD2 LEU B 181      -6.471  44.653 126.332  1.00 24.73           C  
ATOM   1522  N   GLU B 182      -7.967  40.880 123.818  1.00 47.13           N  
ATOM   1523  CA  GLU B 182      -8.532  39.978 122.818  1.00 47.13           C  
ATOM   1524  C   GLU B 182      -9.456  40.695 121.813  1.00 47.13           C  
ATOM   1525  O   GLU B 182     -10.144  41.671 122.149  1.00 47.13           O  
ATOM   1526  CB  GLU B 182      -9.243  38.797 123.473  1.00 68.63           C  
ATOM   1527  CG  GLU B 182     -10.378  39.158 124.392  1.00 68.63           C  
ATOM   1528  CD  GLU B 182     -11.267  37.963 124.655  1.00 68.63           C  
ATOM   1529  OE1 GLU B 182     -12.182  37.735 123.837  1.00 68.63           O  
ATOM   1530  OE2 GLU B 182     -11.040  37.242 125.654  1.00 68.63           O  
ATOM   1531  N   TRP B 183      -9.417  40.229 120.564  1.00 47.95           N  
ATOM   1532  CA  TRP B 183     -10.222  40.792 119.483  1.00 47.95           C  
ATOM   1533  C   TRP B 183     -11.709  40.599 119.680  1.00 47.95           C  
ATOM   1534  O   TRP B 183     -12.178  39.498 119.975  1.00 47.95           O  
ATOM   1535  CB  TRP B 183      -9.814  40.204 118.132  1.00 39.03           C  
ATOM   1536  CG  TRP B 183      -8.659  40.897 117.490  1.00 39.03           C  
ATOM   1537  CD1 TRP B 183      -8.668  42.125 116.885  1.00 39.03           C  
ATOM   1538  CD2 TRP B 183      -7.331  40.383 117.330  1.00 39.03           C  
ATOM   1539  NE1 TRP B 183      -7.434  42.400 116.350  1.00 39.03           N  
ATOM   1540  CE2 TRP B 183      -6.595  41.345 116.606  1.00 39.03           C  
ATOM   1541  CE3 TRP B 183      -6.696  39.187 117.717  1.00 39.03           C  
ATOM   1542  CZ2 TRP B 183      -5.246  41.156 116.260  1.00 39.03           C  
ATOM   1543  CZ3 TRP B 183      -5.353  38.999 117.371  1.00 39.03           C  
ATOM   1544  CH2 TRP B 183      -4.648  39.979 116.647  1.00 39.03           C  
ATOM   1545  N   ARG B 184     -12.442  41.686 119.472  1.00 53.80           N  
ATOM   1546  CA  ARG B 184     -13.888  41.709 119.616  1.00 53.80           C  
ATOM   1547  C   ARG B 184     -14.546  42.513 118.507  1.00 53.80           C  
ATOM   1548  O   ARG B 184     -14.179  43.662 118.262  1.00 53.80           O  
ATOM   1549  CB  ARG B 184     -14.269  42.316 120.964  1.00 68.63           C  
ATOM   1550  CG  ARG B 184     -13.930  41.445 122.141  1.00 68.63           C  
ATOM   1551  CD  ARG B 184     -14.944  40.331 122.317  1.00 68.63           C  
ATOM   1552  NE  ARG B 184     -14.620  39.527 123.492  1.00 68.63           N  
ATOM   1553  CZ  ARG B 184     -14.517  40.009 124.733  1.00 68.63           C  
ATOM   1554  NH1 ARG B 184     -14.723  41.300 124.977  1.00 68.63           N  
ATOM   1555  NH2 ARG B 184     -14.179  39.201 125.730  1.00 68.63           N  
ATOM   1556  N   PHE B 185     -15.514  41.884 117.844  1.00 30.26           N  
ATOM   1557  CA  PHE B 185     -16.287  42.491 116.766  1.00 30.26           C  
ATOM   1558  C   PHE B 185     -17.344  43.380 117.408  1.00 30.26           C  
ATOM   1559  O   PHE B 185     -17.914  43.006 118.424  1.00 30.26           O  
ATOM   1560  CB  PHE B 185     -16.965  41.385 115.959  1.00 21.14           C  
ATOM   1561  CG  PHE B 185     -17.852  41.881 114.865  1.00 21.14           C  
ATOM   1562  CD1 PHE B 185     -19.106  42.379 115.150  1.00 21.14           C  
ATOM   1563  CD2 PHE B 185     -17.447  41.815 113.541  1.00 21.14           C  
ATOM   1564  CE1 PHE B 185     -19.940  42.801 114.148  1.00 21.14           C  
ATOM   1565  CE2 PHE B 185     -18.287  42.241 112.526  1.00 21.14           C  
ATOM   1566  CZ  PHE B 185     -19.538  42.735 112.835  1.00 21.14           C  
ATOM   1567  N   ASP B 186     -17.589  44.553 116.837  1.00 27.80           N  
ATOM   1568  CA  ASP B 186     -18.601  45.499 117.344  1.00 27.80           C  
ATOM   1569  C   ASP B 186     -18.982  46.421 116.179  1.00 27.80           C  
ATOM   1570  O   ASP B 186     -18.319  47.430 115.941  1.00 27.80           O  
ATOM   1571  CB  ASP B 186     -18.045  46.331 118.514  1.00 27.55           C  
ATOM   1572  CG  ASP B 186     -19.066  47.323 119.094  1.00 27.55           C  
ATOM   1573  OD1 ASP B 186     -20.104  47.591 118.469  1.00 27.55           O  
ATOM   1574  OD2 ASP B 186     -18.844  47.866 120.192  1.00 27.55           O  
ATOM   1575  N   SER B 187     -20.087  46.111 115.504  1.00 19.72           N  
ATOM   1576  CA  SER B 187     -20.523  46.892 114.348  1.00 19.72           C  
ATOM   1577  C   SER B 187     -20.774  48.367 114.572  1.00 19.72           C  
ATOM   1578  O   SER B 187     -20.909  49.114 113.613  1.00 19.72           O  
ATOM   1579  CB  SER B 187     -21.737  46.258 113.678  1.00 29.39           C  
ATOM   1580  OG  SER B 187     -22.869  46.366 114.513  1.00 29.39           O  
ATOM   1581  N   ARG B 188     -20.821  48.808 115.817  1.00 19.87           N  
ATOM   1582  CA  ARG B 188     -21.039  50.225 116.064  1.00 19.87           C  
ATOM   1583  C   ARG B 188     -19.825  51.056 115.625  1.00 19.87           C  
ATOM   1584  O   ARG B 188     -19.924  52.269 115.396  1.00 19.87           O  
ATOM   1585  CB  ARG B 188     -21.353  50.461 117.537  1.00 25.40           C  
ATOM   1586  CG  ARG B 188     -22.669  49.856 117.964  1.00 25.40           C  
ATOM   1587  CD  ARG B 188     -22.884  50.049 119.432  1.00 25.40           C  
ATOM   1588  NE  ARG B 188     -21.834  49.377 120.170  1.00 25.40           N  
ATOM   1589  CZ  ARG B 188     -21.622  49.529 121.471  1.00 25.40           C  
ATOM   1590  NH1 ARG B 188     -22.399  50.343 122.186  1.00 25.40           N  
ATOM   1591  NH2 ARG B 188     -20.613  48.883 122.052  1.00 25.40           N  
ATOM   1592  N   LEU B 189     -18.681  50.388 115.512  1.00 25.13           N  
ATOM   1593  CA  LEU B 189     -17.448  51.042 115.100  1.00 25.13           C  
ATOM   1594  C   LEU B 189     -17.587  51.508 113.651  1.00 25.13           C  
ATOM   1595  O   LEU B 189     -16.871  52.423 113.204  1.00 25.13           O  
ATOM   1596  CB  LEU B 189     -16.260  50.084 115.231  1.00 17.63           C  
ATOM   1597  CG  LEU B 189     -15.941  49.470 116.594  1.00 17.63           C  
ATOM   1598  CD1 LEU B 189     -14.809  48.464 116.431  1.00 17.63           C  
ATOM   1599  CD2 LEU B 189     -15.585  50.545 117.611  1.00 17.63           C  
ATOM   1600  N   ALA B 190     -18.499  50.858 112.926  1.00 17.63           N  
ATOM   1601  CA  ALA B 190     -18.778  51.191 111.537  1.00 17.63           C  
ATOM   1602  C   ALA B 190     -19.646  52.441 111.431  1.00 17.63           C  
ATOM   1603  O   ALA B 190     -19.807  52.999 110.348  1.00 17.63           O  
ATOM   1604  CB  ALA B 190     -19.459  50.035 110.861  1.00 17.63           C  
ATOM   1605  N   PHE B 191     -20.147  52.911 112.572  1.00 19.74           N  
ATOM   1606  CA  PHE B 191     -21.010  54.085 112.611  1.00 19.74           C  
ATOM   1607  C   PHE B 191     -20.513  55.159 113.565  1.00 19.74           C  
ATOM   1608  O   PHE B 191     -21.025  56.280 113.572  1.00 19.74           O  
ATOM   1609  CB  PHE B 191     -22.449  53.676 112.968  1.00 17.63           C  
ATOM   1610  CG  PHE B 191     -23.086  52.790 111.944  1.00 17.63           C  
ATOM   1611  CD1 PHE B 191     -23.619  53.325 110.781  1.00 17.63           C  
ATOM   1612  CD2 PHE B 191     -23.093  51.410 112.109  1.00 17.63           C  
ATOM   1613  CE1 PHE B 191     -24.139  52.497 109.795  1.00 17.63           C  
ATOM   1614  CE2 PHE B 191     -23.611  50.576 111.126  1.00 17.63           C  
ATOM   1615  CZ  PHE B 191     -24.135  51.126 109.968  1.00 17.63           C  
ATOM   1616  N   HIS B 192     -19.547  54.805 114.401  1.00 33.22           N  
ATOM   1617  CA  HIS B 192     -18.969  55.760 115.337  1.00 33.22           C  
ATOM   1618  C   HIS B 192     -17.445  55.697 115.274  1.00 33.22           C  
ATOM   1619  O   HIS B 192     -16.859  54.622 115.460  1.00 33.22           O  
ATOM   1620  CB  HIS B 192     -19.447  55.477 116.761  1.00 29.80           C  
ATOM   1621  CG  HIS B 192     -20.916  55.712 116.965  1.00 29.80           C  
ATOM   1622  ND1 HIS B 192     -21.870  54.736 116.733  1.00 29.80           N  
ATOM   1623  CD2 HIS B 192     -21.594  56.804 117.397  1.00 29.80           C  
ATOM   1624  CE1 HIS B 192     -23.069  55.220 117.012  1.00 29.80           C  
ATOM   1625  NE2 HIS B 192     -22.929  56.472 117.418  1.00 29.80           N  
ATOM   1626  N   HIS B 193     -16.815  56.821 114.925  1.00 25.76           N  
ATOM   1627  CA  HIS B 193     -15.352  56.886 114.875  1.00 25.76           C  
ATOM   1628  C   HIS B 193     -14.878  57.161 116.301  1.00 25.76           C  
ATOM   1629  O   HIS B 193     -14.346  58.232 116.599  1.00 25.76           O  
ATOM   1630  CB  HIS B 193     -14.856  58.014 113.956  1.00 22.96           C  
ATOM   1631  CG  HIS B 193     -13.522  57.734 113.330  1.00 22.96           C  
ATOM   1632  ND1 HIS B 193     -13.170  58.215 112.086  1.00 22.96           N  
ATOM   1633  CD2 HIS B 193     -12.506  56.930 113.722  1.00 22.96           C  
ATOM   1634  CE1 HIS B 193     -12.003  57.706 111.734  1.00 22.96           C  
ATOM   1635  NE2 HIS B 193     -11.579  56.923 112.710  1.00 22.96           N  
ATOM   1636  N   VAL B 194     -15.110  56.197 117.187  1.00 27.98           N  
ATOM   1637  CA  VAL B 194     -14.731  56.329 118.580  1.00 27.98           C  
ATOM   1638  C   VAL B 194     -13.234  56.575 118.742  1.00 27.98           C  
ATOM   1639  O   VAL B 194     -12.829  57.386 119.592  1.00 27.98           O  
ATOM   1640  CB  VAL B 194     -15.207  55.118 119.421  1.00 27.84           C  
ATOM   1641  CG1 VAL B 194     -14.853  53.829 118.738  1.00 27.84           C  
ATOM   1642  CG2 VAL B 194     -14.592  55.158 120.814  1.00 27.84           C  
ATOM   1643  N   ALA B 195     -12.415  55.941 117.902  1.00 45.91           N  
ATOM   1644  CA  ALA B 195     -10.964  56.139 117.985  1.00 45.91           C  
ATOM   1645  C   ALA B 195     -10.522  57.507 117.486  1.00 45.91           C  
ATOM   1646  O   ALA B 195      -9.342  57.714 117.225  1.00 45.91           O  
ATOM   1647  CB  ALA B 195     -10.224  55.055 117.235  1.00 37.51           C  
ATOM   1648  N   ARG B 196     -11.473  58.424 117.348  1.00 47.00           N  
ATOM   1649  CA  ARG B 196     -11.201  59.784 116.911  1.00 47.00           C  
ATOM   1650  C   ARG B 196     -11.984  60.724 117.803  1.00 47.00           C  
ATOM   1651  O   ARG B 196     -11.653  61.898 117.918  1.00 47.00           O  
ATOM   1652  CB  ARG B 196     -11.591  59.969 115.459  1.00 37.44           C  
ATOM   1653  CG  ARG B 196     -11.493  61.384 114.932  1.00 37.44           C  
ATOM   1654  CD  ARG B 196     -11.703  61.343 113.433  1.00 37.44           C  
ATOM   1655  NE  ARG B 196     -12.121  62.616 112.858  1.00 37.44           N  
ATOM   1656  CZ  ARG B 196     -11.926  62.954 111.587  1.00 37.44           C  
ATOM   1657  NH1 ARG B 196     -11.312  62.122 110.761  1.00 37.44           N  
ATOM   1658  NH2 ARG B 196     -12.379  64.108 111.127  1.00 37.44           N  
ATOM   1659  N   GLU B 197     -13.055  60.213 118.405  1.00 60.25           N  
ATOM   1660  CA  GLU B 197     -13.842  61.003 119.344  1.00 60.25           C  
ATOM   1661  C   GLU B 197     -12.950  61.077 120.583  1.00 60.25           C  
ATOM   1662  O   GLU B 197     -12.996  62.042 121.339  1.00 60.25           O  
ATOM   1663  CB  GLU B 197     -15.164  60.298 119.691  1.00 68.63           C  
ATOM   1664  CG  GLU B 197     -16.241  60.338 118.590  1.00 68.63           C  
ATOM   1665  CD  GLU B 197     -17.409  59.357 118.819  1.00 68.63           C  
ATOM   1666  OE1 GLU B 197     -17.705  59.004 119.986  1.00 68.63           O  
ATOM   1667  OE2 GLU B 197     -18.030  58.936 117.815  1.00 68.63           O  
ATOM   1668  N   LEU B 198     -12.112  60.050 120.747  1.00 53.06           N  
ATOM   1669  CA  LEU B 198     -11.168  59.932 121.863  1.00 53.06           C  
ATOM   1670  C   LEU B 198      -9.801  60.547 121.532  1.00 53.06           C  
ATOM   1671  O   LEU B 198      -9.451  61.602 122.063  1.00 53.06           O  
ATOM   1672  CB  LEU B 198     -11.002  58.456 122.269  1.00 41.87           C  
ATOM   1673  CG  LEU B 198     -11.990  57.871 123.281  1.00 41.87           C  
ATOM   1674  CD1 LEU B 198     -13.416  58.369 123.038  1.00 41.87           C  
ATOM   1675  CD2 LEU B 198     -11.933  56.365 123.237  1.00 41.87           C  
ATOM   1676  N   HIS B 199      -9.049  59.902 120.644  1.00 47.72           N  
ATOM   1677  CA  HIS B 199      -7.724  60.375 120.250  1.00 47.72           C  
ATOM   1678  C   HIS B 199      -7.724  61.099 118.883  1.00 47.72           C  
ATOM   1679  O   HIS B 199      -7.396  60.493 117.861  1.00 47.72           O  
ATOM   1680  CB  HIS B 199      -6.749  59.191 120.189  1.00 61.71           C  
ATOM   1681  CG  HIS B 199      -6.715  58.353 121.428  1.00 61.71           C  
ATOM   1682  ND1 HIS B 199      -5.923  58.663 122.514  1.00 61.71           N  
ATOM   1683  CD2 HIS B 199      -7.334  57.192 121.740  1.00 61.71           C  
ATOM   1684  CE1 HIS B 199      -6.057  57.728 123.438  1.00 61.71           C  
ATOM   1685  NE2 HIS B 199      -6.909  56.823 122.993  1.00 61.71           N  
ATOM   1686  N   PRO B 200      -8.109  62.393 118.840  1.00 40.94           N  
ATOM   1687  CA  PRO B 200      -8.126  63.129 117.566  1.00 40.94           C  
ATOM   1688  C   PRO B 200      -6.755  63.445 116.968  1.00 40.94           C  
ATOM   1689  O   PRO B 200      -6.661  63.838 115.795  1.00 40.94           O  
ATOM   1690  CB  PRO B 200      -8.912  64.407 117.901  1.00 39.14           C  
ATOM   1691  CG  PRO B 200      -8.653  64.597 119.355  1.00 39.14           C  
ATOM   1692  CD  PRO B 200      -8.766  63.183 119.893  1.00 39.14           C  
ATOM   1693  N   GLU B 201      -5.698  63.285 117.764  1.00 56.71           N  
ATOM   1694  CA  GLU B 201      -4.344  63.551 117.285  1.00 56.71           C  
ATOM   1695  C   GLU B 201      -4.095  62.781 115.988  1.00 56.71           C  
ATOM   1696  O   GLU B 201      -3.835  63.390 114.956  1.00 56.71           O  
ATOM   1697  CB  GLU B 201      -3.305  63.119 118.320  1.00 64.25           C  
ATOM   1698  CG  GLU B 201      -3.642  63.481 119.755  1.00 64.25           C  
ATOM   1699  CD  GLU B 201      -4.419  62.396 120.481  1.00 64.25           C  
ATOM   1700  OE1 GLU B 201      -3.967  61.224 120.501  1.00 64.25           O  
ATOM   1701  OE2 GLU B 201      -5.481  62.729 121.043  1.00 64.25           O  
ATOM   1702  N   TYR B 202      -4.295  61.458 116.041  1.00 42.89           N  
ATOM   1703  CA  TYR B 202      -4.073  60.537 114.925  1.00 42.89           C  
ATOM   1704  C   TYR B 202      -4.804  60.843 113.638  1.00 42.89           C  
ATOM   1705  O   TYR B 202      -4.661  60.097 112.658  1.00 42.89           O  
ATOM   1706  CB  TYR B 202      -4.433  59.113 115.327  1.00 59.88           C  
ATOM   1707  CG  TYR B 202      -3.779  58.631 116.590  1.00 59.88           C  
ATOM   1708  CD1 TYR B 202      -2.480  58.124 116.582  1.00 59.88           C  
ATOM   1709  CD2 TYR B 202      -4.473  58.645 117.794  1.00 59.88           C  
ATOM   1710  CE1 TYR B 202      -1.889  57.639 117.755  1.00 59.88           C  
ATOM   1711  CE2 TYR B 202      -3.898  58.167 118.963  1.00 59.88           C  
ATOM   1712  CZ  TYR B 202      -2.613  57.666 118.939  1.00 59.88           C  
ATOM   1713  OH  TYR B 202      -2.066  57.207 120.110  1.00 59.88           O  
ATOM   1714  N   PHE B 203      -5.599  61.914 113.634  1.00 52.00           N  
ATOM   1715  CA  PHE B 203      -6.379  62.283 112.447  1.00 52.00           C  
ATOM   1716  C   PHE B 203      -6.249  63.746 112.044  1.00 52.00           C  
ATOM   1717  O   PHE B 203      -6.525  64.035 110.858  1.00 34.29           O  
ATOM   1718  CB  PHE B 203      -7.851  61.898 112.662  1.00 34.29           C  
ATOM   1719  CG  PHE B 203      -8.018  60.482 113.114  1.00 34.29           C  
ATOM   1720  CD1 PHE B 203      -7.917  59.432 112.192  1.00 34.29           C  
ATOM   1721  CD2 PHE B 203      -8.136  60.182 114.465  1.00 34.29           C  
ATOM   1722  CE1 PHE B 203      -7.919  58.108 112.603  1.00 34.29           C  
ATOM   1723  CE2 PHE B 203      -8.138  58.863 114.884  1.00 34.29           C  
ATOM   1724  CZ  PHE B 203      -8.028  57.818 113.944  1.00 34.29           C  
TER    1725      PHE B 203                                                      
ATOM   1726  N   THR C  85      -7.878  44.744  72.200  1.00 62.70           N  
ATOM   1727  CA  THR C  85      -7.428  45.371  73.486  1.00 62.70           C  
ATOM   1728  C   THR C  85      -8.266  44.821  74.677  1.00 62.70           C  
ATOM   1729  O   THR C  85      -8.766  45.577  75.535  1.00 62.70           O  
ATOM   1730  CB  THR C  85      -7.549  46.941  73.434  1.00 52.99           C  
ATOM   1731  OG1 THR C  85      -7.161  47.435  72.145  1.00 52.99           O  
ATOM   1732  CG2 THR C  85      -6.666  47.589  74.505  1.00 52.99           C  
ATOM   1733  N   LEU C  86      -8.414  43.500  74.727  1.00 54.52           N  
ATOM   1734  CA  LEU C  86      -9.189  42.865  75.788  1.00 54.52           C  
ATOM   1735  C   LEU C  86      -8.449  41.661  76.385  1.00 54.52           C  
ATOM   1736  O   LEU C  86      -8.299  40.615  75.751  1.00 54.52           O  
ATOM   1737  CB  LEU C  86     -10.598  42.506  75.282  1.00 38.78           C  
ATOM   1738  CG  LEU C  86     -10.880  41.404  74.258  1.00 38.78           C  
ATOM   1739  CD1 LEU C  86     -12.329  41.557  73.795  1.00 38.78           C  
ATOM   1740  CD2 LEU C  86      -9.927  41.490  73.078  1.00 38.78           C  
ATOM   1741  N   PHE C  87      -8.042  41.834  77.640  1.00 51.17           N  
ATOM   1742  CA  PHE C  87      -7.264  40.872  78.421  1.00 51.17           C  
ATOM   1743  C   PHE C  87      -7.933  39.545  78.842  1.00 51.17           C  
ATOM   1744  O   PHE C  87      -9.161  39.414  78.839  1.00 51.17           O  
ATOM   1745  CB  PHE C  87      -6.676  41.583  79.658  1.00 54.59           C  
ATOM   1746  CG  PHE C  87      -5.888  42.844  79.336  1.00 54.59           C  
ATOM   1747  CD1 PHE C  87      -6.430  43.856  78.535  1.00 54.59           C  
ATOM   1748  CD2 PHE C  87      -4.610  43.027  79.851  1.00 54.59           C  
ATOM   1749  CE1 PHE C  87      -5.712  45.016  78.249  1.00 54.59           C  
ATOM   1750  CE2 PHE C  87      -3.888  44.185  79.569  1.00 54.59           C  
ATOM   1751  CZ  PHE C  87      -4.446  45.180  78.768  1.00 54.59           C  
ATOM   1752  N   VAL C  88      -7.086  38.580  79.225  1.00 47.11           N  
ATOM   1753  CA  VAL C  88      -7.487  37.237  79.664  1.00 47.11           C  
ATOM   1754  C   VAL C  88      -6.822  36.904  81.010  1.00 47.11           C  
ATOM   1755  O   VAL C  88      -5.697  37.333  81.270  1.00 47.11           O  
ATOM   1756  CB  VAL C  88      -7.053  36.168  78.624  1.00 44.02           C  
ATOM   1757  CG1 VAL C  88      -5.533  36.136  78.500  1.00 44.02           C  
ATOM   1758  CG2 VAL C  88      -7.587  34.786  79.010  1.00 44.02           C  
ATOM   1759  N   ALA C  89      -7.497  36.108  81.838  1.00 46.23           N  
ATOM   1760  CA  ALA C  89      -6.965  35.735  83.150  1.00 46.23           C  
ATOM   1761  C   ALA C  89      -5.859  34.662  83.128  1.00 46.23           C  
ATOM   1762  O   ALA C  89      -5.989  33.624  82.465  1.00 46.23           O  
ATOM   1763  CB  ALA C  89      -8.106  35.304  84.068  1.00 41.11           C  
ATOM   1764  N   LEU C  90      -4.767  34.928  83.849  1.00 47.66           N  
ATOM   1765  CA  LEU C  90      -3.640  33.995  83.938  1.00 47.66           C  
ATOM   1766  C   LEU C  90      -3.826  33.037  85.116  1.00 47.66           C  
ATOM   1767  O   LEU C  90      -3.438  31.867  85.044  1.00 47.66           O  
ATOM   1768  CB  LEU C  90      -2.300  34.728  84.141  1.00 39.36           C  
ATOM   1769  CG  LEU C  90      -1.729  35.801  83.204  1.00 39.36           C  
ATOM   1770  CD1 LEU C  90      -0.329  36.147  83.661  1.00 39.36           C  
ATOM   1771  CD2 LEU C  90      -1.694  35.345  81.756  1.00 39.36           C  
ATOM   1772  N   TYR C  91      -4.365  33.559  86.218  1.00 43.28           N  
ATOM   1773  CA  TYR C  91      -4.598  32.779  87.436  1.00 43.28           C  
ATOM   1774  C   TYR C  91      -6.001  33.051  87.972  1.00 43.28           C  
ATOM   1775  O   TYR C  91      -6.607  34.066  87.645  1.00 43.28           O  
ATOM   1776  CB  TYR C  91      -3.591  33.173  88.519  1.00 64.35           C  
ATOM   1777  CG  TYR C  91      -2.203  33.444  88.010  1.00 64.35           C  
ATOM   1778  CD1 TYR C  91      -1.332  32.402  87.743  1.00 64.35           C  
ATOM   1779  CD2 TYR C  91      -1.771  34.745  87.774  1.00 64.35           C  
ATOM   1780  CE1 TYR C  91      -0.064  32.641  87.249  1.00 64.35           C  
ATOM   1781  CE2 TYR C  91      -0.505  35.000  87.275  1.00 64.35           C  
ATOM   1782  CZ  TYR C  91       0.348  33.941  87.015  1.00 64.35           C  
ATOM   1783  OH  TYR C  91       1.610  34.167  86.514  1.00 64.35           O  
ATOM   1784  N   ASP C  92      -6.510  32.146  88.801  1.00 45.55           N  
ATOM   1785  CA  ASP C  92      -7.837  32.301  89.402  1.00 45.55           C  
ATOM   1786  C   ASP C  92      -7.724  33.320  90.528  1.00 45.55           C  
ATOM   1787  O   ASP C  92      -6.643  33.509  91.076  1.00 45.55           O  
ATOM   1788  CB  ASP C  92      -8.341  30.955  89.941  1.00 66.17           C  
ATOM   1789  CG  ASP C  92      -8.400  29.884  88.863  1.00 66.17           C  
ATOM   1790  OD1 ASP C  92      -7.339  29.319  88.514  1.00 66.17           O  
ATOM   1791  OD2 ASP C  92      -9.504  29.622  88.344  1.00 66.17           O  
ATOM   1792  N   TYR C  93      -8.832  33.962  90.882  1.00 42.70           N  
ATOM   1793  CA  TYR C  93      -8.818  34.980  91.933  1.00 42.70           C  
ATOM   1794  C   TYR C  93     -10.185  35.161  92.588  1.00 42.70           C  
ATOM   1795  O   TYR C  93     -11.146  35.498  91.904  1.00 42.70           O  
ATOM   1796  CB  TYR C  93      -8.361  36.316  91.330  1.00 35.71           C  
ATOM   1797  CG  TYR C  93      -8.553  37.512  92.228  1.00 35.71           C  
ATOM   1798  CD1 TYR C  93      -7.592  37.858  93.181  1.00 35.71           C  
ATOM   1799  CD2 TYR C  93      -9.698  38.291  92.136  1.00 35.71           C  
ATOM   1800  CE1 TYR C  93      -7.773  38.946  94.023  1.00 35.71           C  
ATOM   1801  CE2 TYR C  93      -9.889  39.381  92.971  1.00 35.71           C  
ATOM   1802  CZ  TYR C  93      -8.928  39.702  93.913  1.00 35.71           C  
ATOM   1803  OH  TYR C  93      -9.152  40.754  94.770  1.00 35.71           O  
ATOM   1804  N   GLU C  94     -10.277  34.926  93.899  1.00 51.63           N  
ATOM   1805  CA  GLU C  94     -11.538  35.103  94.628  1.00 51.63           C  
ATOM   1806  C   GLU C  94     -11.484  36.437  95.363  1.00 51.63           C  
ATOM   1807  O   GLU C  94     -10.634  36.656  96.231  1.00 51.63           O  
ATOM   1808  CB  GLU C  94     -11.776  33.976  95.637  1.00 70.20           C  
ATOM   1809  CG  GLU C  94     -13.060  34.144  96.465  1.00 70.20           C  
ATOM   1810  CD  GLU C  94     -12.995  33.454  97.832  1.00 70.20           C  
ATOM   1811  OE1 GLU C  94     -12.699  32.238  97.876  1.00 70.20           O  
ATOM   1812  OE2 GLU C  94     -13.240  34.125  98.866  1.00 70.20           O  
ATOM   1813  N   ALA C  95     -12.403  37.320  94.994  1.00 49.04           N  
ATOM   1814  CA  ALA C  95     -12.512  38.654  95.561  1.00 49.04           C  
ATOM   1815  C   ALA C  95     -13.048  38.584  96.971  1.00 49.04           C  
ATOM   1816  O   ALA C  95     -13.741  37.627  97.312  1.00 49.04           O  
ATOM   1817  CB  ALA C  95     -13.449  39.463  94.710  1.00 45.96           C  
ATOM   1818  N   ARG C  96     -12.710  39.569  97.804  1.00 51.69           N  
ATOM   1819  CA  ARG C  96     -13.235  39.588  99.172  1.00 51.69           C  
ATOM   1820  C   ARG C  96     -13.809  40.927  99.627  1.00 51.69           C  
ATOM   1821  O   ARG C  96     -13.954  41.184 100.819  1.00 51.69           O  
ATOM   1822  CB  ARG C  96     -12.259  39.002 100.199  1.00 58.94           C  
ATOM   1823  CG  ARG C  96     -12.530  37.530 100.518  1.00 58.94           C  
ATOM   1824  CD  ARG C  96     -11.572  36.605  99.784  1.00 58.94           C  
ATOM   1825  NE  ARG C  96     -10.499  36.115 100.650  1.00 58.94           N  
ATOM   1826  CZ  ARG C  96      -9.309  35.673 100.227  1.00 58.94           C  
ATOM   1827  NH1 ARG C  96      -9.009  35.656  98.930  1.00 58.94           N  
ATOM   1828  NH2 ARG C  96      -8.420  35.217 101.111  1.00 58.94           N  
ATOM   1829  N   THR C  97     -14.125  41.773  98.652  1.00 45.43           N  
ATOM   1830  CA  THR C  97     -14.764  43.070  98.871  1.00 45.43           C  
ATOM   1831  C   THR C  97     -15.805  43.145  97.750  1.00 45.43           C  
ATOM   1832  O   THR C  97     -15.605  42.580  96.665  1.00 45.43           O  
ATOM   1833  CB  THR C  97     -13.781  44.282  98.797  1.00 51.91           C  
ATOM   1834  OG1 THR C  97     -13.076  44.280  97.549  1.00 51.91           O  
ATOM   1835  CG2 THR C  97     -12.787  44.251  99.956  1.00 51.91           C  
ATOM   1836  N   GLU C  98     -16.923  43.813  98.004  1.00 40.75           N  
ATOM   1837  CA  GLU C  98     -17.978  43.889  97.001  1.00 40.75           C  
ATOM   1838  C   GLU C  98     -17.577  44.493  95.668  1.00 40.75           C  
ATOM   1839  O   GLU C  98     -18.186  44.180  94.649  1.00 40.75           O  
ATOM   1840  CB  GLU C  98     -19.207  44.610  97.556  1.00 30.17           C  
ATOM   1841  CG  GLU C  98     -19.780  44.010  98.846  1.00 30.17           C  
ATOM   1842  CD  GLU C  98     -19.986  42.502  98.786  1.00 30.17           C  
ATOM   1843  OE1 GLU C  98     -20.730  42.034  97.884  1.00 30.17           O  
ATOM   1844  OE2 GLU C  98     -19.414  41.798  99.661  1.00 30.17           O  
ATOM   1845  N   ASP C  99     -16.521  45.303  95.669  1.00 26.54           N  
ATOM   1846  CA  ASP C  99     -16.055  45.963  94.448  1.00 26.54           C  
ATOM   1847  C   ASP C  99     -15.016  45.253  93.596  1.00 26.54           C  
ATOM   1848  O   ASP C  99     -14.693  45.728  92.518  1.00 26.54           O  
ATOM   1849  CB  ASP C  99     -15.616  47.395  94.738  1.00 28.21           C  
ATOM   1850  CG  ASP C  99     -16.769  48.271  95.166  1.00 28.21           C  
ATOM   1851  OD1 ASP C  99     -17.894  47.742  95.325  1.00 28.21           O  
ATOM   1852  OD2 ASP C  99     -16.556  49.492  95.342  1.00 28.21           O  
ATOM   1853  N   ASP C 100     -14.482  44.130  94.060  1.00 22.52           N  
ATOM   1854  CA  ASP C 100     -13.521  43.422  93.233  1.00 22.52           C  
ATOM   1855  C   ASP C 100     -14.312  42.469  92.357  1.00 22.52           C  
ATOM   1856  O   ASP C 100     -15.519  42.253  92.573  1.00 22.52           O  
ATOM   1857  CB  ASP C 100     -12.519  42.633  94.068  1.00 40.94           C  
ATOM   1858  CG  ASP C 100     -11.585  43.510  94.858  1.00 40.94           C  
ATOM   1859  OD1 ASP C 100     -11.609  44.755  94.707  1.00 40.94           O  
ATOM   1860  OD2 ASP C 100     -10.807  42.931  95.649  1.00 40.94           O  
ATOM   1861  N   LEU C 101     -13.632  41.884  91.381  1.00 25.96           N  
ATOM   1862  CA  LEU C 101     -14.271  40.951  90.480  1.00 25.96           C  
ATOM   1863  C   LEU C 101     -13.551  39.607  90.591  1.00 25.96           C  
ATOM   1864  O   LEU C 101     -12.320  39.556  90.517  1.00 25.96           O  
ATOM   1865  CB  LEU C 101     -14.197  41.492  89.052  1.00 35.95           C  
ATOM   1866  CG  LEU C 101     -15.309  41.121  88.075  1.00 35.95           C  
ATOM   1867  CD1 LEU C 101     -15.218  42.029  86.891  1.00 35.95           C  
ATOM   1868  CD2 LEU C 101     -15.224  39.668  87.628  1.00 35.95           C  
ATOM   1869  N   SER C 102     -14.322  38.538  90.803  1.00 31.24           N  
ATOM   1870  CA  SER C 102     -13.790  37.180  90.901  1.00 31.24           C  
ATOM   1871  C   SER C 102     -13.740  36.568  89.506  1.00 31.24           C  
ATOM   1872  O   SER C 102     -14.555  36.919  88.658  1.00 31.24           O  
ATOM   1873  CB  SER C 102     -14.671  36.337  91.809  1.00 44.24           C  
ATOM   1874  OG  SER C 102     -14.784  36.952  93.079  1.00 44.24           O  
ATOM   1875  N   PHE C 103     -12.782  35.672  89.260  1.00 35.19           N  
ATOM   1876  CA  PHE C 103     -12.633  35.052  87.937  1.00 35.19           C  
ATOM   1877  C   PHE C 103     -11.797  33.781  87.914  1.00 35.19           C  
ATOM   1878  O   PHE C 103     -10.924  33.594  88.760  1.00 35.19           O  
ATOM   1879  CB  PHE C 103     -12.057  36.056  86.930  1.00 24.84           C  
ATOM   1880  CG  PHE C 103     -10.848  36.804  87.426  1.00 24.84           C  
ATOM   1881  CD1 PHE C 103      -9.574  36.285  87.262  1.00 24.84           C  
ATOM   1882  CD2 PHE C 103     -10.987  38.032  88.067  1.00 24.84           C  
ATOM   1883  CE1 PHE C 103      -8.454  36.973  87.735  1.00 24.84           C  
ATOM   1884  CE2 PHE C 103      -9.874  38.725  88.542  1.00 24.84           C  
ATOM   1885  CZ  PHE C 103      -8.606  38.191  88.375  1.00 24.84           C  
ATOM   1886  N   HIS C 104     -12.055  32.930  86.917  1.00 62.67           N  
ATOM   1887  CA  HIS C 104     -11.352  31.658  86.750  1.00 62.67           C  
ATOM   1888  C   HIS C 104     -10.408  31.684  85.553  1.00 62.67           C  
ATOM   1889  O   HIS C 104     -10.833  32.013  84.443  1.00 62.67           O  
ATOM   1890  CB  HIS C 104     -12.356  30.509  86.575  1.00 70.20           C  
ATOM   1891  CG  HIS C 104     -13.116  30.166  87.824  1.00 70.20           C  
ATOM   1892  ND1 HIS C 104     -12.552  29.473  88.876  1.00 70.20           N  
ATOM   1893  CD2 HIS C 104     -14.400  30.416  88.186  1.00 70.20           C  
ATOM   1894  CE1 HIS C 104     -13.454  29.314  89.832  1.00 70.20           C  
ATOM   1895  NE2 HIS C 104     -14.581  29.877  89.437  1.00 70.20           N  
ATOM   1896  N   LYS C 105      -9.155  31.272  85.783  1.00 66.61           N  
ATOM   1897  CA  LYS C 105      -8.096  31.233  84.760  1.00 66.61           C  
ATOM   1898  C   LYS C 105      -8.619  30.981  83.358  1.00 66.61           C  
ATOM   1899  O   LYS C 105      -8.934  29.851  82.997  1.00 66.61           O  
ATOM   1900  CB  LYS C 105      -7.042  30.164  85.088  1.00 70.20           C  
ATOM   1901  CG  LYS C 105      -5.994  29.976  83.966  1.00 70.20           C  
ATOM   1902  CD  LYS C 105      -5.101  28.738  84.151  1.00 70.20           C  
ATOM   1903  CE  LYS C 105      -4.116  28.881  85.318  1.00 70.20           C  
ATOM   1904  NZ  LYS C 105      -3.112  27.765  85.391  1.00 70.20           N  
ATOM   1905  N   GLY C 106      -8.695  32.040  82.566  1.00 67.28           N  
ATOM   1906  CA  GLY C 106      -9.195  31.897  81.213  1.00 67.28           C  
ATOM   1907  C   GLY C 106     -10.365  32.818  80.933  1.00 67.28           C  
ATOM   1908  O   GLY C 106     -10.709  33.047  79.772  1.00 67.28           O  
ATOM   1909  N   GLU C 107     -10.995  33.323  81.995  1.00 58.50           N  
ATOM   1910  CA  GLU C 107     -12.119  34.242  81.858  1.00 58.50           C  
ATOM   1911  C   GLU C 107     -11.583  35.489  81.158  1.00 58.50           C  
ATOM   1912  O   GLU C 107     -10.562  36.048  81.562  1.00 58.50           O  
ATOM   1913  CB  GLU C 107     -12.697  34.594  83.237  1.00 62.86           C  
ATOM   1914  CG  GLU C 107     -14.029  35.356  83.208  1.00 62.86           C  
ATOM   1915  CD  GLU C 107     -14.666  35.493  84.587  1.00 62.86           C  
ATOM   1916  OE1 GLU C 107     -14.730  34.481  85.320  1.00 62.86           O  
ATOM   1917  OE2 GLU C 107     -15.104  36.614  84.941  1.00 62.86           O  
ATOM   1918  N   LYS C 108     -12.231  35.862  80.058  1.00 51.62           N  
ATOM   1919  CA  LYS C 108     -11.828  37.020  79.267  1.00 51.62           C  
ATOM   1920  C   LYS C 108     -12.426  38.290  79.873  1.00 51.62           C  
ATOM   1921  O   LYS C 108     -13.462  38.234  80.540  1.00 51.62           O  
ATOM   1922  CB  LYS C 108     -12.315  36.850  77.822  1.00 60.32           C  
ATOM   1923  CG  LYS C 108     -12.129  35.449  77.238  1.00 60.32           C  
ATOM   1924  CD  LYS C 108     -10.686  35.185  76.817  1.00 60.32           C  
ATOM   1925  CE  LYS C 108     -10.466  35.478  75.340  1.00 60.32           C  
ATOM   1926  NZ  LYS C 108     -11.274  34.554  74.498  1.00 60.32           N  
ATOM   1927  N   PHE C 109     -11.772  39.427  79.635  1.00 39.80           N  
ATOM   1928  CA  PHE C 109     -12.223  40.723  80.151  1.00 39.80           C  
ATOM   1929  C   PHE C 109     -12.202  41.820  79.100  1.00 39.80           C  
ATOM   1930  O   PHE C 109     -12.166  41.561  77.903  1.00 39.80           O  
ATOM   1931  CB  PHE C 109     -11.334  41.170  81.308  1.00 40.03           C  
ATOM   1932  CG  PHE C 109     -11.464  40.325  82.523  1.00 40.03           C  
ATOM   1933  CD1 PHE C 109     -12.560  40.469  83.363  1.00 40.03           C  
ATOM   1934  CD2 PHE C 109     -10.507  39.375  82.827  1.00 40.03           C  
ATOM   1935  CE1 PHE C 109     -12.702  39.678  84.489  1.00 40.03           C  
ATOM   1936  CE2 PHE C 109     -10.638  38.578  83.953  1.00 40.03           C  
ATOM   1937  CZ  PHE C 109     -11.742  38.733  84.782  1.00 40.03           C  
ATOM   1938  N   GLN C 110     -12.260  43.054  79.579  1.00 30.56           N  
ATOM   1939  CA  GLN C 110     -12.213  44.243  78.744  1.00 30.56           C  
ATOM   1940  C   GLN C 110     -12.043  45.362  79.728  1.00 30.56           C  
ATOM   1941  O   GLN C 110     -12.942  45.635  80.513  1.00 30.56           O  
ATOM   1942  CB  GLN C 110     -13.504  44.450  77.974  1.00 25.06           C  
ATOM   1943  CG  GLN C 110     -13.527  45.760  77.196  1.00 25.06           C  
ATOM   1944  CD  GLN C 110     -14.760  45.889  76.331  1.00 25.06           C  
ATOM   1945  OE1 GLN C 110     -15.828  45.373  76.679  1.00 25.06           O  
ATOM   1946  NE2 GLN C 110     -14.624  46.563  75.190  1.00 25.06           N  
ATOM   1947  N   ILE C 111     -10.881  46.004  79.686  1.00 19.20           N  
ATOM   1948  CA  ILE C 111     -10.558  47.068  80.626  1.00 19.20           C  
ATOM   1949  C   ILE C 111     -11.334  48.355  80.401  1.00 19.20           C  
ATOM   1950  O   ILE C 111     -11.375  48.886  79.304  1.00 19.20           O  
ATOM   1951  CB  ILE C 111      -9.041  47.360  80.633  1.00 20.92           C  
ATOM   1952  CG1 ILE C 111      -8.238  46.043  80.674  1.00 20.92           C  
ATOM   1953  CG2 ILE C 111      -8.666  48.224  81.826  1.00 20.92           C  
ATOM   1954  CD1 ILE C 111      -8.435  45.157  81.906  1.00 20.92           C  
ATOM   1955  N   LEU C 112     -11.988  48.830  81.450  1.00 18.45           N  
ATOM   1956  CA  LEU C 112     -12.755  50.059  81.366  1.00 18.45           C  
ATOM   1957  C   LEU C 112     -11.918  51.216  81.921  1.00 18.45           C  
ATOM   1958  O   LEU C 112     -12.139  52.391  81.577  1.00 19.98           O  
ATOM   1959  CB  LEU C 112     -14.042  49.939  82.165  1.00 19.98           C  
ATOM   1960  CG  LEU C 112     -14.901  48.724  81.899  1.00 19.98           C  
ATOM   1961  CD1 LEU C 112     -16.169  48.901  82.654  1.00 19.98           C  
ATOM   1962  CD2 LEU C 112     -15.174  48.604  80.435  1.00 19.98           C  
ATOM   1963  N   ASN C 113     -10.973  50.894  82.806  1.00 25.73           N  
ATOM   1964  CA  ASN C 113     -10.114  51.924  83.364  1.00 25.73           C  
ATOM   1965  C   ASN C 113      -8.821  51.421  83.993  1.00 25.73           C  
ATOM   1966  O   ASN C 113      -8.790  51.052  85.177  1.00 58.49           O  
ATOM   1967  CB  ASN C 113     -10.886  52.801  84.347  1.00 58.49           C  
ATOM   1968  CG  ASN C 113     -10.019  53.862  84.958  1.00 58.49           C  
ATOM   1969  OD1 ASN C 113      -9.272  54.551  84.255  1.00 58.49           O  
ATOM   1970  ND2 ASN C 113     -10.073  53.975  86.280  1.00 58.49           N  
ATOM   1971  N   SER C 114      -7.752  51.429  83.191  1.00 47.35           N  
ATOM   1972  CA  SER C 114      -6.434  51.013  83.658  1.00 47.35           C  
ATOM   1973  C   SER C 114      -5.671  52.186  84.277  1.00 47.35           C  
ATOM   1974  O   SER C 114      -4.963  52.016  85.267  1.00 37.69           O  
ATOM   1975  CB  SER C 114      -5.608  50.351  82.540  1.00 37.69           C  
ATOM   1976  OG  SER C 114      -6.059  50.684  81.240  1.00 37.69           O  
ATOM   1977  N   SER C 115      -5.924  53.386  83.761  1.00 35.69           N  
ATOM   1978  CA  SER C 115      -5.289  54.632  84.216  1.00 35.69           C  
ATOM   1979  C   SER C 115      -5.654  55.116  85.633  1.00 35.69           C  
ATOM   1980  O   SER C 115      -6.256  56.188  85.793  1.00 53.09           O  
ATOM   1981  CB  SER C 115      -5.590  55.753  83.204  1.00 53.09           C  
ATOM   1982  OG  SER C 115      -6.996  55.946  83.037  1.00 53.09           O  
ATOM   1983  N   GLU C 116      -5.234  54.372  86.656  1.00 46.18           N  
ATOM   1984  CA  GLU C 116      -5.539  54.752  88.036  1.00 46.18           C  
ATOM   1985  C   GLU C 116      -4.790  53.912  89.073  1.00 46.18           C  
ATOM   1986  O   GLU C 116      -4.893  54.146  90.277  1.00 70.37           O  
ATOM   1987  CB  GLU C 116      -7.037  54.626  88.271  1.00 70.37           C  
ATOM   1988  CG  GLU C 116      -7.492  55.095  89.625  1.00 70.37           C  
ATOM   1989  CD  GLU C 116      -8.840  54.555  89.960  1.00 70.37           C  
ATOM   1990  OE1 GLU C 116      -8.925  53.347  90.286  1.00 70.37           O  
ATOM   1991  OE2 GLU C 116      -9.811  55.332  89.855  1.00 70.37           O  
ATOM   1992  N   GLY C 117      -4.041  52.934  88.583  1.00 25.25           N  
ATOM   1993  CA  GLY C 117      -3.284  52.055  89.447  1.00 25.25           C  
ATOM   1994  C   GLY C 117      -3.100  50.674  88.844  1.00 25.25           C  
ATOM   1995  O   GLY C 117      -3.419  50.433  87.668  1.00 57.94           O  
ATOM   1996  N   ASP C 118      -2.553  49.764  89.649  1.00 43.01           N  
ATOM   1997  CA  ASP C 118      -2.323  48.380  89.219  1.00 43.01           C  
ATOM   1998  C   ASP C 118      -3.577  47.526  89.464  1.00 43.01           C  
ATOM   1999  O   ASP C 118      -3.564  46.300  89.311  1.00 57.77           O  
ATOM   2000  CB  ASP C 118      -1.105  47.793  89.927  1.00 57.77           C  
ATOM   2001  CG  ASP C 118       0.169  48.575  89.655  1.00 57.77           C  
ATOM   2002  OD1 ASP C 118       0.225  49.289  88.618  1.00 57.77           O  
ATOM   2003  OD2 ASP C 118       1.114  48.465  90.472  1.00 57.77           O  
ATOM   2004  N   TRP C 119      -4.653  48.195  89.888  1.00 35.75           N  
ATOM   2005  CA  TRP C 119      -5.957  47.565  90.112  1.00 35.75           C  
ATOM   2006  C   TRP C 119      -6.848  48.139  89.044  1.00 35.75           C  
ATOM   2007  O   TRP C 119      -7.235  49.304  89.108  1.00 35.75           O  
ATOM   2008  CB  TRP C 119      -6.498  47.860  91.505  1.00 22.65           C  
ATOM   2009  CG  TRP C 119      -5.924  46.905  92.501  1.00 22.65           C  
ATOM   2010  CD1 TRP C 119      -4.842  47.106  93.304  1.00 22.65           C  
ATOM   2011  CD2 TRP C 119      -6.386  45.579  92.769  1.00 22.65           C  
ATOM   2012  NE1 TRP C 119      -4.604  45.989  94.059  1.00 22.65           N  
ATOM   2013  CE2 TRP C 119      -5.536  45.035  93.753  1.00 22.65           C  
ATOM   2014  CE3 TRP C 119      -7.441  44.797  92.277  1.00 22.65           C  
ATOM   2015  CZ2 TRP C 119      -5.703  43.740  94.258  1.00 22.65           C  
ATOM   2016  CZ3 TRP C 119      -7.608  43.516  92.776  1.00 22.65           C  
ATOM   2017  CH2 TRP C 119      -6.742  42.999  93.761  1.00 22.65           C  
ATOM   2018  N   TRP C 120      -7.095  47.336  88.017  1.00 25.43           N  
ATOM   2019  CA  TRP C 120      -7.903  47.780  86.900  1.00 25.43           C  
ATOM   2020  C   TRP C 120      -9.387  47.494  87.032  1.00 25.43           C  
ATOM   2021  O   TRP C 120      -9.788  46.448  87.533  1.00 25.43           O  
ATOM   2022  CB  TRP C 120      -7.376  47.173  85.599  1.00 31.23           C  
ATOM   2023  CG  TRP C 120      -5.954  47.576  85.250  1.00 31.23           C  
ATOM   2024  CD1 TRP C 120      -5.177  48.530  85.869  1.00 31.23           C  
ATOM   2025  CD2 TRP C 120      -5.163  47.055  84.179  1.00 31.23           C  
ATOM   2026  NE1 TRP C 120      -3.957  48.632  85.235  1.00 31.23           N  
ATOM   2027  CE2 TRP C 120      -3.926  47.740  84.195  1.00 31.23           C  
ATOM   2028  CE3 TRP C 120      -5.382  46.085  83.202  1.00 31.23           C  
ATOM   2029  CZ2 TRP C 120      -2.921  47.475  83.278  1.00 31.23           C  
ATOM   2030  CZ3 TRP C 120      -4.385  45.825  82.293  1.00 31.23           C  
ATOM   2031  CH2 TRP C 120      -3.169  46.518  82.333  1.00 31.23           C  
ATOM   2032  N   GLU C 121     -10.199  48.461  86.629  1.00 27.96           N  
ATOM   2033  CA  GLU C 121     -11.629  48.296  86.658  1.00 27.96           C  
ATOM   2034  C   GLU C 121     -11.889  47.613  85.329  1.00 27.96           C  
ATOM   2035  O   GLU C 121     -11.627  48.177  84.281  1.00 27.96           O  
ATOM   2036  CB  GLU C 121     -12.298  49.654  86.706  1.00 55.61           C  
ATOM   2037  CG  GLU C 121     -13.781  49.576  86.819  1.00 55.61           C  
ATOM   2038  CD  GLU C 121     -14.407  50.932  86.902  1.00 55.61           C  
ATOM   2039  OE1 GLU C 121     -14.478  51.464  88.033  1.00 55.61           O  
ATOM   2040  OE2 GLU C 121     -14.807  51.465  85.837  1.00 55.61           O  
ATOM   2041  N   ALA C 122     -12.331  46.369  85.364  1.00 28.43           N  
ATOM   2042  CA  ALA C 122     -12.569  45.649  84.133  1.00 28.43           C  
ATOM   2043  C   ALA C 122     -13.974  45.078  84.048  1.00 28.43           C  
ATOM   2044  O   ALA C 122     -14.710  45.074  85.035  1.00 28.43           O  
ATOM   2045  CB  ALA C 122     -11.556  44.561  83.983  1.00 19.20           C  
ATOM   2046  N   ARG C 123     -14.341  44.620  82.853  1.00 38.26           N  
ATOM   2047  CA  ARG C 123     -15.648  44.033  82.606  1.00 38.26           C  
ATOM   2048  C   ARG C 123     -15.549  42.623  82.052  1.00 38.26           C  
ATOM   2049  O   ARG C 123     -15.018  42.403  80.958  1.00 38.26           O  
ATOM   2050  CB  ARG C 123     -16.444  44.894  81.643  1.00 21.64           C  
ATOM   2051  CG  ARG C 123     -17.695  44.220  81.129  1.00 21.64           C  
ATOM   2052  CD  ARG C 123     -18.614  45.206  80.439  1.00 21.64           C  
ATOM   2053  NE  ARG C 123     -18.006  45.872  79.288  1.00 21.64           N  
ATOM   2054  CZ  ARG C 123     -18.279  47.125  78.937  1.00 21.64           C  
ATOM   2055  NH1 ARG C 123     -19.149  47.827  79.654  1.00 21.64           N  
ATOM   2056  NH2 ARG C 123     -17.669  47.683  77.903  1.00 21.64           N  
ATOM   2057  N   SER C 124     -16.091  41.678  82.814  1.00 34.81           N  
ATOM   2058  CA  SER C 124     -16.096  40.271  82.452  1.00 34.81           C  
ATOM   2059  C   SER C 124     -16.844  40.037  81.156  1.00 34.81           C  
ATOM   2060  O   SER C 124     -17.985  40.456  81.020  1.00 34.81           O  
ATOM   2061  CB  SER C 124     -16.753  39.465  83.570  1.00 42.94           C  
ATOM   2062  OG  SER C 124     -16.969  38.124  83.183  1.00 42.94           O  
ATOM   2063  N   LEU C 125     -16.197  39.376  80.202  1.00 28.71           N  
ATOM   2064  CA  LEU C 125     -16.825  39.068  78.916  1.00 28.71           C  
ATOM   2065  C   LEU C 125     -17.874  37.954  79.085  1.00 28.71           C  
ATOM   2066  O   LEU C 125     -18.866  37.875  78.350  1.00 28.71           O  
ATOM   2067  CB  LEU C 125     -15.756  38.667  77.887  1.00 23.27           C  
ATOM   2068  CG  LEU C 125     -14.891  39.792  77.307  1.00 23.27           C  
ATOM   2069  CD1 LEU C 125     -13.860  39.244  76.346  1.00 23.27           C  
ATOM   2070  CD2 LEU C 125     -15.772  40.807  76.595  1.00 23.27           C  
ATOM   2071  N   THR C 126     -17.648  37.126  80.100  1.00 30.01           N  
ATOM   2072  CA  THR C 126     -18.506  35.999  80.457  1.00 30.01           C  
ATOM   2073  C   THR C 126     -19.831  36.447  81.106  1.00 30.01           C  
ATOM   2074  O   THR C 126     -20.896  36.242  80.525  1.00 30.01           O  
ATOM   2075  CB  THR C 126     -17.727  35.028  81.403  1.00 29.24           C  
ATOM   2076  OG1 THR C 126     -16.786  34.256  80.644  1.00 29.24           O  
ATOM   2077  CG2 THR C 126     -18.661  34.118  82.165  1.00 29.24           C  
ATOM   2078  N   THR C 127     -19.758  37.076  82.285  1.00 33.01           N  
ATOM   2079  CA  THR C 127     -20.951  37.543  83.011  1.00 33.01           C  
ATOM   2080  C   THR C 127     -21.495  38.959  82.704  1.00 33.01           C  
ATOM   2081  O   THR C 127     -22.705  39.188  82.756  1.00 33.01           O  
ATOM   2082  CB  THR C 127     -20.749  37.431  84.540  1.00 39.75           C  
ATOM   2083  OG1 THR C 127     -19.509  38.043  84.912  1.00 39.75           O  
ATOM   2084  CG2 THR C 127     -20.742  35.981  84.977  1.00 39.75           C  
ATOM   2085  N   GLY C 128     -20.608  39.896  82.382  1.00 22.66           N  
ATOM   2086  CA  GLY C 128     -21.017  41.263  82.104  1.00 22.66           C  
ATOM   2087  C   GLY C 128     -20.811  42.138  83.328  1.00 22.66           C  
ATOM   2088  O   GLY C 128     -21.052  43.341  83.316  1.00 22.66           O  
ATOM   2089  N   GLU C 129     -20.346  41.503  84.394  1.00 25.35           N  
ATOM   2090  CA  GLU C 129     -20.081  42.146  85.669  1.00 25.35           C  
ATOM   2091  C   GLU C 129     -18.780  42.953  85.617  1.00 25.35           C  
ATOM   2092  O   GLU C 129     -17.782  42.508  85.049  1.00 25.35           O  
ATOM   2093  CB  GLU C 129     -19.962  41.053  86.726  1.00 32.65           C  
ATOM   2094  CG  GLU C 129     -19.983  41.516  88.159  1.00 32.65           C  
ATOM   2095  CD  GLU C 129     -19.688  40.377  89.112  1.00 32.65           C  
ATOM   2096  OE1 GLU C 129     -19.469  39.249  88.622  1.00 32.65           O  
ATOM   2097  OE2 GLU C 129     -19.665  40.601  90.344  1.00 32.65           O  
ATOM   2098  N   THR C 130     -18.803  44.141  86.214  1.00 19.20           N  
ATOM   2099  CA  THR C 130     -17.636  45.013  86.272  1.00 19.20           C  
ATOM   2100  C   THR C 130     -17.094  45.069  87.703  1.00 19.20           C  
ATOM   2101  O   THR C 130     -17.832  44.875  88.680  1.00 19.20           O  
ATOM   2102  CB  THR C 130     -17.986  46.444  85.891  1.00 19.20           C  
ATOM   2103  OG1 THR C 130     -19.112  46.857  86.662  1.00 19.20           O  
ATOM   2104  CG2 THR C 130     -18.305  46.567  84.422  1.00 19.20           C  
ATOM   2105  N   GLY C 131     -15.812  45.406  87.823  1.00 19.20           N  
ATOM   2106  CA  GLY C 131     -15.194  45.502  89.131  1.00 19.20           C  
ATOM   2107  C   GLY C 131     -13.697  45.486  88.992  1.00 19.20           C  
ATOM   2108  O   GLY C 131     -13.184  45.142  87.933  1.00 19.20           O  
ATOM   2109  N   TYR C 132     -12.999  45.806  90.076  1.00 21.20           N  
ATOM   2110  CA  TYR C 132     -11.540  45.858  90.085  1.00 21.20           C  
ATOM   2111  C   TYR C 132     -10.848  44.512  90.130  1.00 21.20           C  
ATOM   2112  O   TYR C 132     -11.176  43.666  90.961  1.00 21.20           O  
ATOM   2113  CB  TYR C 132     -11.058  46.697  91.266  1.00 38.42           C  
ATOM   2114  CG  TYR C 132     -11.426  48.139  91.137  1.00 38.42           C  
ATOM   2115  CD1 TYR C 132     -11.034  48.874  90.023  1.00 38.42           C  
ATOM   2116  CD2 TYR C 132     -12.206  48.762  92.098  1.00 38.42           C  
ATOM   2117  CE1 TYR C 132     -11.415  50.200  89.861  1.00 38.42           C  
ATOM   2118  CE2 TYR C 132     -12.596  50.088  91.951  1.00 38.42           C  
ATOM   2119  CZ  TYR C 132     -12.198  50.807  90.824  1.00 38.42           C  
ATOM   2120  OH  TYR C 132     -12.589  52.128  90.667  1.00 38.42           O  
ATOM   2121  N   ILE C 133      -9.875  44.331  89.246  1.00 32.15           N  
ATOM   2122  CA  ILE C 133      -9.086  43.113  89.186  1.00 32.15           C  
ATOM   2123  C   ILE C 133      -7.619  43.538  89.303  1.00 32.15           C  
ATOM   2124  O   ILE C 133      -7.265  44.667  88.941  1.00 32.15           O  
ATOM   2125  CB  ILE C 133      -9.315  42.357  87.865  1.00 36.85           C  
ATOM   2126  CG1 ILE C 133      -8.960  43.246  86.672  1.00 36.85           C  
ATOM   2127  CG2 ILE C 133     -10.758  41.885  87.776  1.00 36.85           C  
ATOM   2128  CD1 ILE C 133      -8.982  42.516  85.327  1.00 36.85           C  
ATOM   2129  N   PRO C 134      -6.750  42.657  89.841  1.00 25.74           N  
ATOM   2130  CA  PRO C 134      -5.320  42.954  90.004  1.00 25.74           C  
ATOM   2131  C   PRO C 134      -4.620  42.792  88.668  1.00 25.74           C  
ATOM   2132  O   PRO C 134      -4.439  41.672  88.212  1.00 25.74           O  
ATOM   2133  CB  PRO C 134      -4.874  41.890  90.998  1.00 27.01           C  
ATOM   2134  CG  PRO C 134      -5.679  40.720  90.605  1.00 27.01           C  
ATOM   2135  CD  PRO C 134      -7.057  41.299  90.323  1.00 27.01           C  
ATOM   2136  N   SER C 135      -4.239  43.903  88.039  1.00 19.30           N  
ATOM   2137  CA  SER C 135      -3.607  43.855  86.723  1.00 19.30           C  
ATOM   2138  C   SER C 135      -2.469  42.839  86.544  1.00 19.30           C  
ATOM   2139  O   SER C 135      -2.273  42.322  85.434  1.00 19.30           O  
ATOM   2140  CB  SER C 135      -3.146  45.245  86.306  1.00 28.64           C  
ATOM   2141  OG  SER C 135      -2.230  45.775  87.244  1.00 28.64           O  
ATOM   2142  N   ASN C 136      -1.732  42.543  87.623  1.00 28.61           N  
ATOM   2143  CA  ASN C 136      -0.628  41.575  87.563  1.00 28.61           C  
ATOM   2144  C   ASN C 136      -1.134  40.140  87.354  1.00 28.61           C  
ATOM   2145  O   ASN C 136      -0.353  39.226  87.065  1.00 28.61           O  
ATOM   2146  CB  ASN C 136       0.295  41.669  88.794  1.00 52.57           C  
ATOM   2147  CG  ASN C 136      -0.358  41.185  90.075  1.00 52.57           C  
ATOM   2148  OD1 ASN C 136      -1.579  41.125  90.181  1.00 52.57           O  
ATOM   2149  ND2 ASN C 136       0.463  40.853  91.068  1.00 52.57           N  
ATOM   2150  N   TYR C 137      -2.455  39.972  87.435  1.00 35.67           N  
ATOM   2151  CA  TYR C 137      -3.112  38.681  87.250  1.00 35.67           C  
ATOM   2152  C   TYR C 137      -3.649  38.484  85.847  1.00 35.67           C  
ATOM   2153  O   TYR C 137      -4.231  37.446  85.578  1.00 35.67           O  
ATOM   2154  CB  TYR C 137      -4.281  38.534  88.213  1.00 39.70           C  
ATOM   2155  CG  TYR C 137      -3.971  37.841  89.506  1.00 39.70           C  
ATOM   2156  CD1 TYR C 137      -2.885  38.224  90.293  1.00 39.70           C  
ATOM   2157  CD2 TYR C 137      -4.801  36.827  89.969  1.00 39.70           C  
ATOM   2158  CE1 TYR C 137      -2.637  37.614  91.511  1.00 39.70           C  
ATOM   2159  CE2 TYR C 137      -4.566  36.210  91.181  1.00 39.70           C  
ATOM   2160  CZ  TYR C 137      -3.483  36.608  91.952  1.00 39.70           C  
ATOM   2161  OH  TYR C 137      -3.262  36.001  93.171  1.00 39.70           O  
ATOM   2162  N   VAL C 138      -3.518  39.480  84.974  1.00 48.59           N  
ATOM   2163  CA  VAL C 138      -4.008  39.339  83.600  1.00 48.59           C  
ATOM   2164  C   VAL C 138      -2.970  39.729  82.545  1.00 48.59           C  
ATOM   2165  O   VAL C 138      -1.913  40.285  82.867  1.00 48.59           O  
ATOM   2166  CB  VAL C 138      -5.307  40.154  83.341  1.00 35.86           C  
ATOM   2167  CG1 VAL C 138      -6.419  39.723  84.309  1.00 35.86           C  
ATOM   2168  CG2 VAL C 138      -5.027  41.671  83.413  1.00 35.86           C  
ATOM   2169  N   ALA C 139      -3.298  39.439  81.286  1.00 39.48           N  
ATOM   2170  CA  ALA C 139      -2.438  39.730  80.137  1.00 39.48           C  
ATOM   2171  C   ALA C 139      -3.300  39.752  78.872  1.00 39.48           C  
ATOM   2172  O   ALA C 139      -4.299  39.036  78.794  1.00 39.48           O  
ATOM   2173  CB  ALA C 139      -1.355  38.669  80.020  1.00 54.95           C  
ATOM   2174  N   PRO C 140      -2.919  40.566  77.865  1.00 39.28           N  
ATOM   2175  CA  PRO C 140      -3.627  40.717  76.583  1.00 39.28           C  
ATOM   2176  C   PRO C 140      -3.879  39.385  75.885  1.00 39.28           C  
ATOM   2177  O   PRO C 140      -3.148  38.434  76.115  1.00 39.28           O  
ATOM   2178  CB  PRO C 140      -2.668  41.588  75.770  1.00 31.12           C  
ATOM   2179  CG  PRO C 140      -2.026  42.440  76.810  1.00 31.12           C  
ATOM   2180  CD  PRO C 140      -1.725  41.431  77.897  1.00 31.12           C  
ATOM   2181  N   VAL C 141      -4.900  39.306  75.034  1.00 48.13           N  
ATOM   2182  CA  VAL C 141      -5.181  38.048  74.336  1.00 48.13           C  
ATOM   2183  C   VAL C 141      -4.063  37.609  73.381  1.00 48.13           C  
ATOM   2184  O   VAL C 141      -3.413  38.487  72.748  1.00 46.82           O  
ATOM   2185  CB  VAL C 141      -6.540  38.070  73.567  1.00 46.82           C  
ATOM   2186  CG1 VAL C 141      -7.692  37.950  74.544  1.00 46.82           C  
ATOM   2187  CG2 VAL C 141      -6.679  39.337  72.715  1.00 46.82           C  
ATOM   2188  OXT VAL C 141      -3.850  36.374  73.296  1.00 46.82           O  
TER    2189      VAL C 141                                                      
MASTER      405    0    0    9    6    0    0    6 2186    3    0   29          
END

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Related entries of code: 1avz

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
1azg	RCSB PDB PDBbind	67aa, >1AZG_2\|Chain... *
1efn	RCSB PDB PDBbind	59aa, >1EFN_1\|Chains... at 96%
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
No complexes with the same small molecule ligand are found!

Entry Information

PDB ID	1avz
Complex Type	Protein-Protein
PDBbind Subset	general set
Protein Name	HIV-1 Nef protein
Ligand Name	Fyn kinase SH3 domain
EC.Number	E.C.2.7.1.112
Resolution	3(Å)
Affinity (Kd/Ki/IC50)	Kd=15.8uM
Release Year	1998
Protein/NA Sequence	Check fasta file
Primary Reference	Biochemistry. 1998 Oct 20; 37(42):14683-91

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): P03406 P06241
Entrez Gene ID	NCBI Entrez Gene ID: 2534
ASD	Information of known allosteric effects of PDB entries

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