HEADER    TRANSPORT PROTEIN                       02-FEB-18   6FMY              
TITLE     IMISX-EP OF S-PEPTST                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DI-OR TRIPEPTIDE:H+ SYMPORTER;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS THERMOPHILUS (STRAIN ATCC BAA-250 
SOURCE   3 / LMG 18311);                                                        
SOURCE   4 ORGANISM_TAXID: 264199;                                              
SOURCE   5 STRAIN: ATCC BAA-250 / LMG 18311;                                    
SOURCE   6 GENE: DTPT, STU0970;                                                 
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SERIAL CRYSTALLOGRAPHY, EXPERIMENTAL PHASING, IN MESO                 
KEYWDS   2 CRYSTALLIZATION, IN SITU DIFFRACTION DATA COLLECTION, MEMBRANE       
KEYWDS   3 PROTEIN STRUCTURE., MEMBRANE PROTEIN, TRANSPORT PROTEIN              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.-Y.HUANG,V.OLIERIC,N.HOWE,R.WARSHAMANAGE,T.WEINERT,E.PANEPUCCI,     
AUTHOR   2 L.VOGELEY,S.BASU,K.DIEDERICHS,M.CAFFREY,M.WANG                       
REVDAT   2   10-OCT-18 6FMY    1       COMPND JRNL                              
REVDAT   1   05-SEP-18 6FMY    0                                                
JRNL        AUTH   C.Y.HUANG,V.OLIERIC,N.HOWE,R.WARSHAMANAGE,T.WEINERT,         
JRNL        AUTH 2 E.PANEPUCCI,L.VOGELEY,S.BASU,K.DIEDERICHS,M.CAFFREY,M.WANG   
JRNL        TITL   IN SITU SERIAL CRYSTALLOGRAPHY FOR RAPID DE NOVO MEMBRANE    
JRNL        TITL 2 PROTEIN STRUCTURE DETERMINATION.                             
JRNL        REF    COMMUN BIOL                   V.   1   124 2018              
JRNL        REFN                   ESSN 2399-3642                               
JRNL        PMID   30272004                                                     
JRNL        DOI    10.1038/S42003-018-0123-6                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.29                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.430                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 33068                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1661                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.4032 -  6.1776    0.99     2603   144  0.1999 0.2140        
REMARK   3     2  6.1776 -  4.9048    1.00     2615   143  0.2207 0.2501        
REMARK   3     3  4.9048 -  4.2852    1.00     2643   129  0.1862 0.2165        
REMARK   3     4  4.2852 -  3.8936    1.00     2616   147  0.1881 0.2174        
REMARK   3     5  3.8936 -  3.6146    1.00     2597   140  0.2074 0.2110        
REMARK   3     6  3.6146 -  3.4015    1.00     2634   121  0.2101 0.2902        
REMARK   3     7  3.4015 -  3.2312    1.00     2598   161  0.2159 0.2920        
REMARK   3     8  3.2312 -  3.0906    1.00     2655   127  0.2228 0.2231        
REMARK   3     9  3.0906 -  2.9716    1.00     2592   132  0.2345 0.3085        
REMARK   3    10  2.9716 -  2.8691    1.00     2634   124  0.2368 0.2881        
REMARK   3    11  2.8691 -  2.7794    1.00     2603   141  0.2264 0.3208        
REMARK   3    12  2.7794 -  2.6999    1.00     2617   152  0.2327 0.3205        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.240           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           3853                                  
REMARK   3   ANGLE     :  0.705           5166                                  
REMARK   3   CHIRALITY :  0.040            581                                  
REMARK   3   PLANARITY :  0.004            612                                  
REMARK   3   DIHEDRAL  : 13.643           2169                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6FMY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200008381.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-AUG-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 2.0664                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33070                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.290                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 423.6                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 40.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 378.0                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXCD, SHELXDE                                      
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22 %(V/V) PEG- 400, 325 MM AMMONIUM      
REMARK 280  DIHYDROGEN PHOSPHATE, 100 MM HEPES, PH 7.0, LIPIDIC CUBIC PHASE,    
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.73500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.73500            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       50.61000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.10000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       50.61000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.10000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       55.73500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       50.61000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       55.10000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       55.73500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       50.61000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       55.10000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 480 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 21190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     SER A   271                                                      
REMARK 465     VAL A   272                                                      
REMARK 465     LYS A   273                                                      
REMARK 465     VAL A   274                                                      
REMARK 465     THR A   275                                                      
REMARK 465     SER A   276                                                      
REMARK 465     TRP A   346                                                      
REMARK 465     LYS A   347                                                      
REMARK 465     LYS A   348                                                      
REMARK 465     ASN A   349                                                      
REMARK 465     THR A   412                                                      
REMARK 465     LYS A   413                                                      
REMARK 465     LEU A   414                                                      
REMARK 465     ALA A   415                                                      
REMARK 465     PRO A   416                                                      
REMARK 465     LYS A   417                                                      
REMARK 465     ALA A   418                                                      
REMARK 465     PHE A   419                                                      
REMARK 465     ASN A   420                                                      
REMARK 465     SER A   421                                                      
REMARK 465     GLN A   422                                                      
REMARK 465     MET A   423                                                      
REMARK 465     MET A   424                                                      
REMARK 465     GLN A   476                                                      
REMARK 465     GLY A   477                                                      
REMARK 465     LEU A   478                                                      
REMARK 465     MET A   479                                                      
REMARK 465     GLN A   480                                                      
REMARK 465     GLY A   481                                                      
REMARK 465     VAL A   482                                                      
REMARK 465     GLU A   483                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 281    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 448    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A   6     -134.33     43.09                                   
REMARK 500    ALA A 173     -165.89   -101.45                                   
REMARK 500    TRP A 243       45.25    -96.23                                   
REMARK 500    VAL A 304      -78.22   -115.91                                   
REMARK 500    SER A 316       75.07   -114.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     78M A  501                                                       
REMARK 610     78M A  505                                                       
REMARK 610     78M A  510                                                       
REMARK 610     78M A  511                                                       
REMARK 610     78M A  512                                                       
REMARK 610     78M A  513                                                       
REMARK 610     78M A  514                                                       
REMARK 610     PE5 A  517                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 78M A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 78M A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 78M A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 78M A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 78M A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 78M A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 78M A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 78M A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 78M A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 78M A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 78M A 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 78M A 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 78M A 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 78M A 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 78M A 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 78M A 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PE5 A 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 518                 
DBREF  6FMY A    1   483  UNP    Q5M4H8   Q5M4H8_STRT2     1    483             
SEQRES   1 A  483  MET GLU ASP LYS GLY LYS THR PHE PHE GLY GLN PRO LEU          
SEQRES   2 A  483  GLY LEU SER THR LEU PHE MET THR GLU MET TRP GLU ARG          
SEQRES   3 A  483  PHE SER TYR TYR GLY MET ARG ALA ILE LEU LEU TYR TYR          
SEQRES   4 A  483  MET TRP PHE LEU ILE SER THR GLY ASP LEU HIS ILE THR          
SEQRES   5 A  483  ARG ALA THR ALA ALA SER ILE MET ALA ILE TYR ALA SER          
SEQRES   6 A  483  MET VAL TYR LEU SER GLY THR ILE GLY GLY PHE VAL ALA          
SEQRES   7 A  483  ASP ARG ILE ILE GLY ALA ARG PRO ALA VAL PHE TRP GLY          
SEQRES   8 A  483  GLY VAL LEU ILE MET LEU GLY HIS ILE VAL LEU ALA LEU          
SEQRES   9 A  483  PRO PHE GLY ALA SER ALA LEU PHE GLY SER ILE ILE LEU          
SEQRES  10 A  483  ILE ILE ILE GLY THR GLY PHE LEU LYS PRO ASN VAL SER          
SEQRES  11 A  483  THR LEU VAL GLY THR LEU TYR ASP GLU HIS ASP ARG ARG          
SEQRES  12 A  483  ARG ASP ALA GLY PHE SER ILE PHE VAL PHE GLY ILE ASN          
SEQRES  13 A  483  LEU GLY ALA PHE ILE ALA PRO LEU ILE VAL GLY ALA ALA          
SEQRES  14 A  483  GLN GLU ALA ALA GLY TYR HIS VAL ALA PHE SER LEU ALA          
SEQRES  15 A  483  ALA ILE GLY MET PHE ILE GLY LEU LEU VAL TYR TYR PHE          
SEQRES  16 A  483  GLY GLY LYS LYS THR LEU ASP PRO HIS TYR LEU ARG PRO          
SEQRES  17 A  483  THR ASP PRO LEU ALA PRO GLU GLU VAL LYS PRO LEU LEU          
SEQRES  18 A  483  VAL LYS VAL SER LEU ALA VAL ALA GLY PHE ILE ALA ILE          
SEQRES  19 A  483  ILE VAL VAL MET ASN LEU VAL GLY TRP ASN SER LEU PRO          
SEQRES  20 A  483  ALA TYR ILE ASN LEU LEU THR ILE VAL ALA ILE ALA ILE          
SEQRES  21 A  483  PRO VAL PHE TYR PHE ALA TRP MET ILE SER SER VAL LYS          
SEQRES  22 A  483  VAL THR SER THR GLU HIS LEU ARG VAL VAL SER TYR ILE          
SEQRES  23 A  483  PRO LEU PHE ILE ALA ALA VAL LEU PHE TRP ALA ILE GLU          
SEQRES  24 A  483  GLU GLN GLY SER VAL VAL LEU ALA THR PHE ALA ALA GLU          
SEQRES  25 A  483  ARG VAL ASP SER SER TRP PHE PRO VAL SER TRP PHE GLN          
SEQRES  26 A  483  SER LEU ASN PRO LEU PHE ILE MET LEU TYR THR PRO PHE          
SEQRES  27 A  483  PHE ALA TRP LEU TRP THR ALA TRP LYS LYS ASN GLN PRO          
SEQRES  28 A  483  SER SER PRO THR LYS PHE ALA VAL GLY LEU MET PHE ALA          
SEQRES  29 A  483  GLY LEU SER PHE LEU LEU MET ALA ILE PRO GLY ALA LEU          
SEQRES  30 A  483  TYR GLY THR SER GLY LYS VAL SER PRO LEU TRP LEU VAL          
SEQRES  31 A  483  GLY SER TRP ALA LEU VAL ILE LEU GLY GLU MET LEU ILE          
SEQRES  32 A  483  SER PRO VAL GLY LEU SER VAL THR THR LYS LEU ALA PRO          
SEQRES  33 A  483  LYS ALA PHE ASN SER GLN MET MET SER MET TRP PHE LEU          
SEQRES  34 A  483  SER SER SER VAL GLY SER ALA LEU ASN ALA GLN LEU VAL          
SEQRES  35 A  483  THR LEU TYR ASN ALA LYS SER GLU VAL ALA TYR PHE SER          
SEQRES  36 A  483  TYR PHE GLY LEU GLY SER VAL VAL LEU GLY ILE VAL LEU          
SEQRES  37 A  483  VAL PHE LEU SER LYS ARG ILE GLN GLY LEU MET GLN GLY          
SEQRES  38 A  483  VAL GLU                                                      
HET    78M  A 501      17                                                       
HET    78M  A 502      22                                                       
HET    78M  A 503      22                                                       
HET    78M  A 504      22                                                       
HET    78M  A 505      20                                                       
HET    78M  A 506      22                                                       
HET    78M  A 507      22                                                       
HET    78M  A 508      22                                                       
HET    78M  A 509      22                                                       
HET    78M  A 510      16                                                       
HET    78M  A 511      16                                                       
HET    78M  A 512      12                                                       
HET    78M  A 513      14                                                       
HET    78M  A 514      12                                                       
HET    78M  A 515      22                                                       
HET    78M  A 516      22                                                       
HET    PE5  A 517      10                                                       
HET    PO4  A 518       5                                                       
HETNAM     78M (2S)-2,3-DIHYDROXYPROPYL(7Z)-PENTADEC-7-ENOATE                   
HETNAM     PE5 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     78M 7.8 MONOACYLGLYCEROL                                             
HETSYN     PE5 2-(2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-           
HETSYN   2 PE5  ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL, POLYETHYLENE           
HETSYN   3 PE5  GLYCOL PEG400                                                   
FORMUL   2  78M    16(C18 H34 O4)                                               
FORMUL  18  PE5    C18 H38 O9                                                   
FORMUL  19  PO4    O4 P 3-                                                      
FORMUL  20  HOH   *10(H2 O)                                                     
HELIX    1 AA1 LEU A   13  THR A   46  1                                  34    
HELIX    2 AA2 THR A   52  ILE A   81  1                                  30    
HELIX    3 AA3 GLY A   83  LEU A  104  1                                  22    
HELIX    4 AA4 ALA A  108  THR A  135  1                                  28    
HELIX    5 AA5 ARG A  142  ALA A  173  1                                  32    
HELIX    6 AA6 GLY A  174  LEU A  201  1                                  28    
HELIX    7 AA7 ASP A  202  ARG A  207  5                                   6    
HELIX    8 AA8 ALA A  213  GLU A  215  5                                   3    
HELIX    9 AA9 GLU A  216  GLY A  242  1                                  27    
HELIX   10 AB1 SER A  245  ILE A  269  1                                  25    
HELIX   11 AB2 HIS A  279  GLN A  301  1                                  23    
HELIX   12 AB3 VAL A  304  VAL A  314  1                                  11    
HELIX   13 AB4 PRO A  320  GLN A  325  5                                   6    
HELIX   14 AB5 SER A  326  ALA A  345  1                                  20    
HELIX   15 AB6 SER A  352  GLY A  379  1                                  28    
HELIX   16 AB7 PRO A  386  THR A  411  1                                  26    
HELIX   17 AB8 TRP A  427  VAL A  442  1                                  16    
HELIX   18 AB9 THR A  443  TYR A  445  5                                   3    
HELIX   19 AC1 SER A  449  SER A  472  1                                  24    
SITE     1 AC1  5 MET A 238  TRP A 243  SER A 245  ALA A 248                    
SITE     2 AC1  5 ASN A 251                                                     
SITE     1 AC2  8 PRO A 211  LEU A 212  LEU A 221  ALA A 376                    
SITE     2 AC2  8 78M A 503  78M A 504  78M A 510  HOH A 601                    
SITE     1 AC3  6 LEU A 369  ILE A 373  ALA A 376  VAL A 451                    
SITE     2 AC3  6 78M A 502  HOH A 601                                          
SITE     1 AC4  3 LEU A 212  VAL A 217  78M A 502                               
SITE     1 AC5  2 VAL A 177  PHE A 195                                          
SITE     1 AC6  7 LEU A 370  TYR A 378  LYS A 383  VAL A 384                    
SITE     2 AC6  7 SER A 385  TRP A 388  78M A 509                               
SITE     1 AC7  3 GLN A 440  THR A 443  LEU A 444                               
SITE     1 AC8  7 VAL A 101  PHE A 106  SER A 109  GLY A 113                    
SITE     2 AC8  7 VAL A 469  PHE A 470  LYS A 473                               
SITE     1 AC9  5 ASP A 315  PHE A 319  SER A 385  PRO A 386                    
SITE     2 AC9  5 78M A 506                                                     
SITE     1 AD1  6 LEU A 221  SER A 225  TYR A 378  TRP A 388                    
SITE     2 AD1  6 78M A 502  78M A 512                                          
SITE     1 AD2  7 ARG A  85  PRO A  86  PHE A  89  TYR A 193                    
SITE     2 AD2  7 TYR A 194  LYS A 198  78M A 514                               
SITE     1 AD3  1 78M A 510                                                     
SITE     1 AD4  4 PHE A 112  ASN A 244  TYR A 249  78M A 516                    
SITE     1 AD5  7 MET A  96  PHE A 187  LEU A 190  LEU A 191                    
SITE     2 AD5  7 TYR A 194  PHE A 195  78M A 511                               
SITE     1 AD6  5 SER A  70  THR A  72  ILE A  73  PHE A  76                    
SITE     2 AD6  5 78M A 516                                                     
SITE     1 AD7 11 ILE A  59  ILE A  62  MET A  66  PHE A 112                    
SITE     2 AD7 11 ILE A 115  ILE A 116  PHE A 231  LEU A 246                    
SITE     3 AD7 11 LEU A 253  78M A 513  78M A 515                               
SITE     1 AD8  1 GLN A 170                                                     
SITE     1 AD9  5 ASP A  48  PHE A 106  GLY A 107  ALA A 108                    
SITE     2 AD9  5 SER A 109                                                     
CRYST1  101.220  110.200  111.470  90.00  90.00  90.00 C 2 2 21      8          
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      0.009879  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009074  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008971        0.00000                         
ATOM      1  N   GLY A   5      23.752  -6.226  20.407  1.00 81.19           N  
ATOM      2  CA  GLY A   5      25.058  -6.792  20.703  1.00 77.51           C  
ATOM      3  C   GLY A   5      25.875  -5.968  21.680  1.00 71.50           C  
ATOM      4  O   GLY A   5      27.069  -5.749  21.466  1.00 82.73           O  
ATOM      5  N   LYS A   6      25.226  -5.551  22.770  1.00 75.50           N  
ATOM      6  CA  LYS A   6      25.733  -4.537  23.692  1.00 77.06           C  
ATOM      7  C   LYS A   6      26.337  -3.382  22.886  1.00 74.70           C  
ATOM      8  O   LYS A   6      25.706  -2.952  21.919  1.00 86.13           O  
ATOM      9  CB  LYS A   6      26.672  -5.178  24.727  1.00 75.12           C  
ATOM     10  CG  LYS A   6      25.861  -5.744  25.925  1.00 77.69           C  
ATOM     11  CD  LYS A   6      26.181  -7.195  26.334  1.00 91.88           C  
ATOM     12  CE  LYS A   6      24.968  -7.832  27.038  1.00 94.12           C  
ATOM     13  NZ  LYS A   6      25.273  -8.974  27.957  1.00106.36           N  
ATOM     14  N   THR A   7      27.520  -2.866  23.222  1.00 46.90           N  
ATOM     15  CA  THR A   7      27.953  -1.605  22.613  1.00 50.75           C  
ATOM     16  C   THR A   7      27.962  -1.662  21.082  1.00 56.65           C  
ATOM     17  O   THR A   7      28.119  -2.723  20.473  1.00 56.50           O  
ATOM     18  CB  THR A   7      29.348  -1.205  23.102  1.00 48.78           C  
ATOM     19  OG1 THR A   7      30.320  -2.151  22.635  1.00 58.80           O  
ATOM     20  CG2 THR A   7      29.393  -1.112  24.619  1.00 49.74           C  
ATOM     21  N   PHE A   8      27.767  -0.493  20.463  1.00 48.25           N  
ATOM     22  CA  PHE A   8      27.905  -0.295  19.020  1.00 45.90           C  
ATOM     23  C   PHE A   8      29.199   0.481  18.801  1.00 46.00           C  
ATOM     24  O   PHE A   8      29.229   1.704  18.963  1.00 39.80           O  
ATOM     25  CB  PHE A   8      26.702   0.450  18.441  1.00 40.82           C  
ATOM     26  CG  PHE A   8      26.791   0.699  16.951  1.00 41.32           C  
ATOM     27  CD1 PHE A   8      26.478  -0.304  16.047  1.00 44.26           C  
ATOM     28  CD2 PHE A   8      27.170   1.941  16.458  1.00 41.76           C  
ATOM     29  CE1 PHE A   8      26.550  -0.081  14.680  1.00 37.48           C  
ATOM     30  CE2 PHE A   8      27.245   2.171  15.089  1.00 41.34           C  
ATOM     31  CZ  PHE A   8      26.935   1.158  14.201  1.00 38.68           C  
ATOM     32  N   PHE A   9      30.265  -0.235  18.436  1.00 51.16           N  
ATOM     33  CA  PHE A   9      31.605   0.348  18.329  1.00 43.76           C  
ATOM     34  C   PHE A   9      32.018   1.013  19.639  1.00 45.55           C  
ATOM     35  O   PHE A   9      32.570   2.115  19.652  1.00 48.60           O  
ATOM     36  CB  PHE A   9      31.692   1.336  17.163  1.00 43.34           C  
ATOM     37  CG  PHE A   9      31.767   0.677  15.818  1.00 51.67           C  
ATOM     38  CD1 PHE A   9      32.987   0.515  15.184  1.00 52.11           C  
ATOM     39  CD2 PHE A   9      30.623   0.211  15.190  1.00 54.43           C  
ATOM     40  CE1 PHE A   9      33.067  -0.091  13.944  1.00 55.10           C  
ATOM     41  CE2 PHE A   9      30.697  -0.400  13.947  1.00 55.11           C  
ATOM     42  CZ  PHE A   9      31.922  -0.552  13.325  1.00 54.30           C  
ATOM     43  N   GLY A  10      31.746   0.335  20.754  1.00 42.85           N  
ATOM     44  CA  GLY A  10      31.997   0.880  22.067  1.00 41.19           C  
ATOM     45  C   GLY A  10      30.961   1.863  22.559  1.00 50.01           C  
ATOM     46  O   GLY A  10      30.931   2.159  23.759  1.00 51.23           O  
ATOM     47  N   GLN A  11      30.105   2.366  21.679  1.00 57.53           N  
ATOM     48  CA  GLN A  11      29.126   3.394  22.004  1.00 45.55           C  
ATOM     49  C   GLN A  11      27.810   2.757  22.420  1.00 41.50           C  
ATOM     50  O   GLN A  11      27.586   1.565  22.202  1.00 44.32           O  
ATOM     51  CB  GLN A  11      28.947   4.316  20.799  1.00 40.28           C  
ATOM     52  CG  GLN A  11      30.251   4.854  20.253  1.00 41.68           C  
ATOM     53  CD  GLN A  11      31.091   5.518  21.324  1.00 46.28           C  
ATOM     54  OE1 GLN A  11      30.564   6.097  22.273  1.00 50.74           O  
ATOM     55  NE2 GLN A  11      32.406   5.431  21.182  1.00 49.72           N  
ATOM     56  N   PRO A  12      26.910   3.524  23.044  1.00 45.68           N  
ATOM     57  CA  PRO A  12      25.622   2.951  23.454  1.00 39.20           C  
ATOM     58  C   PRO A  12      24.845   2.395  22.270  1.00 43.04           C  
ATOM     59  O   PRO A  12      24.988   2.850  21.133  1.00 41.59           O  
ATOM     60  CB  PRO A  12      24.888   4.136  24.093  1.00 28.44           C  
ATOM     61  CG  PRO A  12      25.953   5.067  24.508  1.00 34.00           C  
ATOM     62  CD  PRO A  12      27.061   4.913  23.511  1.00 42.53           C  
ATOM     63  N   LEU A  13      23.997   1.405  22.564  1.00 43.79           N  
ATOM     64  CA  LEU A  13      23.299   0.665  21.518  1.00 35.20           C  
ATOM     65  C   LEU A  13      22.476   1.569  20.620  1.00 47.70           C  
ATOM     66  O   LEU A  13      22.262   1.246  19.445  1.00 53.61           O  
ATOM     67  CB  LEU A  13      22.400  -0.396  22.144  1.00 53.20           C  
ATOM     68  CG  LEU A  13      22.976  -1.796  21.983  1.00 69.63           C  
ATOM     69  CD1 LEU A  13      22.212  -2.844  22.784  1.00 69.18           C  
ATOM     70  CD2 LEU A  13      23.039  -2.161  20.503  1.00 71.86           C  
ATOM     71  N   GLY A  14      21.992   2.688  21.147  1.00 50.04           N  
ATOM     72  CA  GLY A  14      21.140   3.544  20.349  1.00 39.94           C  
ATOM     73  C   GLY A  14      21.851   4.347  19.303  1.00 41.76           C  
ATOM     74  O   GLY A  14      21.183   5.007  18.500  1.00 41.76           O  
ATOM     75  N   LEU A  15      23.183   4.341  19.299  1.00 39.48           N  
ATOM     76  CA  LEU A  15      23.885   4.968  18.186  1.00 40.44           C  
ATOM     77  C   LEU A  15      23.563   4.258  16.880  1.00 40.53           C  
ATOM     78  O   LEU A  15      23.435   4.907  15.840  1.00 40.63           O  
ATOM     79  CB  LEU A  15      25.388   4.981  18.448  1.00 38.14           C  
ATOM     80  CG  LEU A  15      26.116   6.014  17.583  1.00 33.62           C  
ATOM     81  CD1 LEU A  15      25.485   7.383  17.762  1.00 41.38           C  
ATOM     82  CD2 LEU A  15      27.593   6.055  17.908  1.00 36.67           C  
ATOM     83  N   SER A  16      23.368   2.936  16.933  1.00 33.61           N  
ATOM     84  CA  SER A  16      23.078   2.169  15.724  1.00 41.72           C  
ATOM     85  C   SER A  16      21.811   2.667  15.041  1.00 35.17           C  
ATOM     86  O   SER A  16      21.795   2.884  13.825  1.00 37.46           O  
ATOM     87  CB  SER A  16      22.959   0.681  16.060  1.00 35.81           C  
ATOM     88  OG  SER A  16      21.980   0.465  17.061  1.00 49.75           O  
ATOM     89  N   THR A  17      20.733   2.851  15.807  1.00 32.32           N  
ATOM     90  CA  THR A  17      19.502   3.371  15.219  1.00 36.64           C  
ATOM     91  C   THR A  17      19.739   4.740  14.593  1.00 31.66           C  
ATOM     92  O   THR A  17      19.401   4.969  13.427  1.00 33.39           O  
ATOM     93  CB  THR A  17      18.388   3.441  16.270  1.00 32.62           C  
ATOM     94  OG1 THR A  17      18.745   4.380  17.288  1.00 55.09           O  
ATOM     95  CG2 THR A  17      18.168   2.086  16.917  1.00 31.16           C  
ATOM     96  N   LEU A  18      20.353   5.656  15.347  1.00 32.65           N  
ATOM     97  CA  LEU A  18      20.576   7.007  14.838  1.00 34.62           C  
ATOM     98  C   LEU A  18      21.597   7.017  13.708  1.00 33.73           C  
ATOM     99  O   LEU A  18      21.429   7.741  12.721  1.00 34.84           O  
ATOM    100  CB  LEU A  18      21.017   7.926  15.972  1.00 37.09           C  
ATOM    101  CG  LEU A  18      19.969   8.218  17.044  1.00 33.61           C  
ATOM    102  CD1 LEU A  18      20.579   9.049  18.153  1.00 37.63           C  
ATOM    103  CD2 LEU A  18      18.763   8.925  16.447  1.00 32.12           C  
ATOM    104  N   PHE A  19      22.666   6.229  13.845  1.00 38.67           N  
ATOM    105  CA  PHE A  19      23.623   6.033  12.760  1.00 28.02           C  
ATOM    106  C   PHE A  19      22.912   5.662  11.465  1.00 31.39           C  
ATOM    107  O   PHE A  19      23.200   6.220  10.402  1.00 33.66           O  
ATOM    108  CB  PHE A  19      24.623   4.945  13.166  1.00 30.04           C  
ATOM    109  CG  PHE A  19      25.637   4.586  12.116  1.00 30.46           C  
ATOM    110  CD1 PHE A  19      25.299   3.769  11.045  1.00 30.00           C  
ATOM    111  CD2 PHE A  19      26.952   5.002  12.242  1.00 32.24           C  
ATOM    112  CE1 PHE A  19      26.237   3.421  10.097  1.00 26.40           C  
ATOM    113  CE2 PHE A  19      27.899   4.647  11.296  1.00 32.65           C  
ATOM    114  CZ  PHE A  19      27.539   3.854  10.225  1.00 29.47           C  
ATOM    115  N   MET A  20      21.985   4.708  11.532  1.00 29.69           N  
ATOM    116  CA  MET A  20      21.345   4.245  10.311  1.00 28.46           C  
ATOM    117  C   MET A  20      20.223   5.167   9.865  1.00 38.15           C  
ATOM    118  O   MET A  20      19.970   5.284   8.659  1.00 39.39           O  
ATOM    119  CB  MET A  20      20.813   2.827  10.495  1.00 31.86           C  
ATOM    120  CG  MET A  20      21.898   1.799  10.673  1.00 36.64           C  
ATOM    121  SD  MET A  20      21.204   0.151  10.536  1.00 68.04           S  
ATOM    122  CE  MET A  20      20.666   0.179   8.828  1.00 34.42           C  
ATOM    123  N   THR A  21      19.528   5.803  10.811  1.00 46.06           N  
ATOM    124  CA  THR A  21      18.514   6.789  10.456  1.00 31.24           C  
ATOM    125  C   THR A  21      19.092   7.833   9.515  1.00 30.56           C  
ATOM    126  O   THR A  21      18.564   8.073   8.423  1.00 29.91           O  
ATOM    127  CB  THR A  21      17.967   7.458  11.717  1.00 32.29           C  
ATOM    128  OG1 THR A  21      17.419   6.464  12.588  1.00 27.36           O  
ATOM    129  CG2 THR A  21      16.888   8.469  11.357  1.00 31.61           C  
ATOM    130  N   GLU A  22      20.208   8.437   9.912  1.00 28.62           N  
ATOM    131  CA  GLU A  22      20.791   9.509   9.122  1.00 31.26           C  
ATOM    132  C   GLU A  22      21.547   8.984   7.907  1.00 28.64           C  
ATOM    133  O   GLU A  22      21.621   9.680   6.888  1.00 29.99           O  
ATOM    134  CB  GLU A  22      21.691  10.364  10.014  1.00 30.03           C  
ATOM    135  CG  GLU A  22      22.406  11.504   9.308  1.00 39.66           C  
ATOM    136  CD  GLU A  22      21.489  12.609   8.794  1.00 40.18           C  
ATOM    137  OE1 GLU A  22      20.248  12.454   8.813  1.00 40.79           O  
ATOM    138  OE2 GLU A  22      22.029  13.650   8.363  1.00 53.22           O  
ATOM    139  N   MET A  23      22.094   7.765   7.978  1.00 33.57           N  
ATOM    140  CA  MET A  23      22.706   7.172   6.794  1.00 27.07           C  
ATOM    141  C   MET A  23      21.710   7.090   5.645  1.00 33.05           C  
ATOM    142  O   MET A  23      22.066   7.310   4.480  1.00 31.99           O  
ATOM    143  CB  MET A  23      23.255   5.776   7.110  1.00 28.91           C  
ATOM    144  CG  MET A  23      23.847   5.076   5.875  1.00 28.73           C  
ATOM    145  SD  MET A  23      24.463   3.390   6.110  1.00 39.58           S  
ATOM    146  CE  MET A  23      22.943   2.442   6.115  1.00 30.98           C  
ATOM    147  N   TRP A  24      20.454   6.782   5.955  1.00 29.51           N  
ATOM    148  CA  TRP A  24      19.436   6.645   4.925  1.00 28.87           C  
ATOM    149  C   TRP A  24      18.793   7.967   4.540  1.00 31.46           C  
ATOM    150  O   TRP A  24      18.341   8.113   3.398  1.00 35.39           O  
ATOM    151  CB  TRP A  24      18.375   5.644   5.379  1.00 32.28           C  
ATOM    152  CG  TRP A  24      18.864   4.254   5.262  1.00 28.04           C  
ATOM    153  CD1 TRP A  24      19.184   3.405   6.280  1.00 33.59           C  
ATOM    154  CD2 TRP A  24      19.134   3.548   4.048  1.00 40.20           C  
ATOM    155  NE1 TRP A  24      19.619   2.203   5.773  1.00 36.13           N  
ATOM    156  CE2 TRP A  24      19.598   2.267   4.404  1.00 43.52           C  
ATOM    157  CE3 TRP A  24      19.018   3.873   2.692  1.00 31.59           C  
ATOM    158  CZ2 TRP A  24      19.945   1.309   3.453  1.00 35.78           C  
ATOM    159  CZ3 TRP A  24      19.362   2.924   1.751  1.00 25.88           C  
ATOM    160  CH2 TRP A  24      19.822   1.657   2.135  1.00 32.21           C  
ATOM    161  N   GLU A  25      18.742   8.933   5.457  1.00 24.87           N  
ATOM    162  CA  GLU A  25      18.371  10.289   5.068  1.00 26.65           C  
ATOM    163  C   GLU A  25      19.376  10.853   4.076  1.00 30.79           C  
ATOM    164  O   GLU A  25      18.999  11.384   3.024  1.00 34.21           O  
ATOM    165  CB  GLU A  25      18.264  11.193   6.300  1.00 36.71           C  
ATOM    166  CG  GLU A  25      17.761  12.621   6.024  1.00 26.97           C  
ATOM    167  CD  GLU A  25      18.846  13.570   5.558  1.00 33.76           C  
ATOM    168  OE1 GLU A  25      19.991  13.443   6.039  1.00 39.82           O  
ATOM    169  OE2 GLU A  25      18.553  14.441   4.709  1.00 43.66           O  
ATOM    170  N   ARG A  26      20.666  10.741   4.397  1.00 28.02           N  
ATOM    171  CA  ARG A  26      21.701  11.224   3.493  1.00 29.25           C  
ATOM    172  C   ARG A  26      21.711  10.442   2.187  1.00 27.99           C  
ATOM    173  O   ARG A  26      22.033  11.002   1.134  1.00 34.23           O  
ATOM    174  CB  ARG A  26      23.069  11.154   4.174  1.00 25.34           C  
ATOM    175  CG  ARG A  26      23.205  12.035   5.414  1.00 28.43           C  
ATOM    176  CD  ARG A  26      23.438  13.499   5.060  1.00 27.64           C  
ATOM    177  NE  ARG A  26      22.197  14.252   4.899  1.00 29.79           N  
ATOM    178  CZ  ARG A  26      22.145  15.553   4.629  1.00 30.73           C  
ATOM    179  NH1 ARG A  26      23.265  16.249   4.485  1.00 31.80           N  
ATOM    180  NH2 ARG A  26      20.974  16.159   4.500  1.00 32.60           N  
ATOM    181  N   PHE A  27      21.362   9.155   2.230  1.00 25.58           N  
ATOM    182  CA  PHE A  27      21.195   8.394   0.996  1.00 25.33           C  
ATOM    183  C   PHE A  27      20.107   9.009   0.124  1.00 34.32           C  
ATOM    184  O   PHE A  27      20.298   9.208  -1.081  1.00 32.74           O  
ATOM    185  CB  PHE A  27      20.871   6.930   1.319  1.00 27.42           C  
ATOM    186  CG  PHE A  27      20.469   6.104   0.115  1.00 24.71           C  
ATOM    187  CD1 PHE A  27      19.151   6.076  -0.317  1.00 28.68           C  
ATOM    188  CD2 PHE A  27      21.402   5.335  -0.561  1.00 24.89           C  
ATOM    189  CE1 PHE A  27      18.776   5.320  -1.410  1.00 30.42           C  
ATOM    190  CE2 PHE A  27      21.032   4.571  -1.653  1.00 30.23           C  
ATOM    191  CZ  PHE A  27      19.716   4.564  -2.078  1.00 32.65           C  
ATOM    192  N   SER A  28      18.951   9.314   0.720  1.00 33.67           N  
ATOM    193  CA  SER A  28      17.844   9.879  -0.047  1.00 34.31           C  
ATOM    194  C   SER A  28      18.166  11.284  -0.536  1.00 30.05           C  
ATOM    195  O   SER A  28      17.877  11.630  -1.688  1.00 32.92           O  
ATOM    196  CB  SER A  28      16.579   9.895   0.802  1.00 27.30           C  
ATOM    197  OG  SER A  28      16.741  10.754   1.915  1.00 28.09           O  
ATOM    198  N   TYR A  29      18.760  12.108   0.329  1.00 29.46           N  
ATOM    199  CA  TYR A  29      19.074  13.483  -0.045  1.00 36.86           C  
ATOM    200  C   TYR A  29      20.123  13.533  -1.149  1.00 33.68           C  
ATOM    201  O   TYR A  29      19.903  14.146  -2.200  1.00 26.68           O  
ATOM    202  CB  TYR A  29      19.541  14.269   1.182  1.00 26.77           C  
ATOM    203  CG  TYR A  29      19.967  15.688   0.871  1.00 21.94           C  
ATOM    204  CD1 TYR A  29      19.025  16.700   0.713  1.00 22.04           C  
ATOM    205  CD2 TYR A  29      21.310  16.016   0.736  1.00 24.41           C  
ATOM    206  CE1 TYR A  29      19.413  17.999   0.426  1.00 26.97           C  
ATOM    207  CE2 TYR A  29      21.706  17.308   0.449  1.00 19.68           C  
ATOM    208  CZ  TYR A  29      20.756  18.295   0.295  1.00 24.89           C  
ATOM    209  OH  TYR A  29      21.157  19.579   0.009  1.00 34.85           O  
ATOM    210  N   TYR A  30      21.272  12.890  -0.933  1.00 29.31           N  
ATOM    211  CA  TYR A  30      22.374  13.024  -1.880  1.00 29.08           C  
ATOM    212  C   TYR A  30      22.173  12.186  -3.136  1.00 31.19           C  
ATOM    213  O   TYR A  30      22.723  12.525  -4.188  1.00 31.60           O  
ATOM    214  CB  TYR A  30      23.698  12.674  -1.198  1.00 22.87           C  
ATOM    215  CG  TYR A  30      24.218  13.811  -0.352  1.00 25.85           C  
ATOM    216  CD1 TYR A  30      24.517  15.039  -0.931  1.00 24.25           C  
ATOM    217  CD2 TYR A  30      24.395  13.670   1.021  1.00 24.41           C  
ATOM    218  CE1 TYR A  30      24.981  16.090  -0.176  1.00 22.63           C  
ATOM    219  CE2 TYR A  30      24.865  14.722   1.790  1.00 28.32           C  
ATOM    220  CZ  TYR A  30      25.155  15.931   1.182  1.00 23.56           C  
ATOM    221  OH  TYR A  30      25.621  16.990   1.924  1.00 31.87           O  
ATOM    222  N   GLY A  31      21.392  11.107  -3.057  1.00 31.18           N  
ATOM    223  CA  GLY A  31      21.058  10.368  -4.265  1.00 22.88           C  
ATOM    224  C   GLY A  31      20.226  11.201  -5.220  1.00 33.89           C  
ATOM    225  O   GLY A  31      20.498  11.257  -6.423  1.00 31.41           O  
ATOM    226  N   MET A  32      19.192  11.859  -4.693  1.00 31.18           N  
ATOM    227  CA  MET A  32      18.459  12.845  -5.478  1.00 30.04           C  
ATOM    228  C   MET A  32      19.379  13.973  -5.925  1.00 31.67           C  
ATOM    229  O   MET A  32      19.292  14.447  -7.064  1.00 33.07           O  
ATOM    230  CB  MET A  32      17.285  13.379  -4.652  1.00 29.34           C  
ATOM    231  CG  MET A  32      16.617  14.639  -5.191  1.00 35.11           C  
ATOM    232  SD  MET A  32      17.409  16.182  -4.670  1.00 42.10           S  
ATOM    233  CE  MET A  32      17.308  16.032  -2.887  1.00 31.73           C  
ATOM    234  N   ARG A  33      20.281  14.404  -5.041  1.00 32.93           N  
ATOM    235  CA  ARG A  33      21.182  15.509  -5.355  1.00 31.18           C  
ATOM    236  C   ARG A  33      22.074  15.197  -6.551  1.00 30.75           C  
ATOM    237  O   ARG A  33      22.484  16.112  -7.274  1.00 29.35           O  
ATOM    238  CB  ARG A  33      22.030  15.833  -4.125  1.00 35.83           C  
ATOM    239  CG  ARG A  33      22.757  17.149  -4.184  1.00 38.78           C  
ATOM    240  CD  ARG A  33      21.820  18.310  -3.929  1.00 33.90           C  
ATOM    241  NE  ARG A  33      22.524  19.568  -4.147  1.00 32.62           N  
ATOM    242  CZ  ARG A  33      21.935  20.726  -4.410  1.00 27.24           C  
ATOM    243  NH1 ARG A  33      20.614  20.800  -4.492  1.00 34.38           N  
ATOM    244  NH2 ARG A  33      22.673  21.810  -4.598  1.00 38.93           N  
ATOM    245  N   ALA A  34      22.374  13.918  -6.784  1.00 24.78           N  
ATOM    246  CA  ALA A  34      23.292  13.539  -7.851  1.00 26.31           C  
ATOM    247  C   ALA A  34      22.647  13.519  -9.230  1.00 28.86           C  
ATOM    248  O   ALA A  34      23.366  13.581 -10.231  1.00 29.89           O  
ATOM    249  CB  ALA A  34      23.899  12.167  -7.554  1.00 30.44           C  
ATOM    250  N   ILE A  35      21.322  13.442  -9.314  1.00 28.73           N  
ATOM    251  CA  ILE A  35      20.635  13.326 -10.593  1.00 32.76           C  
ATOM    252  C   ILE A  35      19.620  14.431 -10.814  1.00 35.11           C  
ATOM    253  O   ILE A  35      18.984  14.463 -11.872  1.00 34.44           O  
ATOM    254  CB  ILE A  35      19.951  11.953 -10.750  1.00 31.09           C  
ATOM    255  CG1 ILE A  35      18.994  11.710  -9.583  1.00 34.58           C  
ATOM    256  CG2 ILE A  35      20.982  10.843 -10.846  1.00 26.71           C  
ATOM    257  CD1 ILE A  35      18.029  10.572  -9.802  1.00 37.56           C  
ATOM    258  N   LEU A  36      19.441  15.338  -9.853  1.00 30.53           N  
ATOM    259  CA  LEU A  36      18.417  16.364 -10.013  1.00 28.00           C  
ATOM    260  C   LEU A  36      18.796  17.368 -11.093  1.00 32.23           C  
ATOM    261  O   LEU A  36      17.939  17.799 -11.873  1.00 33.63           O  
ATOM    262  CB  LEU A  36      18.164  17.078  -8.687  1.00 28.95           C  
ATOM    263  CG  LEU A  36      17.001  18.068  -8.760  1.00 28.41           C  
ATOM    264  CD1 LEU A  36      15.700  17.348  -9.079  1.00 27.91           C  
ATOM    265  CD2 LEU A  36      16.875  18.858  -7.475  1.00 29.13           C  
ATOM    266  N   LEU A  37      20.070  17.756 -11.154  1.00 26.91           N  
ATOM    267  CA  LEU A  37      20.491  18.713 -12.172  1.00 27.12           C  
ATOM    268  C   LEU A  37      20.315  18.127 -13.569  1.00 32.59           C  
ATOM    269  O   LEU A  37      19.770  18.779 -14.468  1.00 30.38           O  
ATOM    270  CB  LEU A  37      21.943  19.138 -11.930  1.00 32.17           C  
ATOM    271  CG  LEU A  37      22.537  20.190 -12.869  1.00 29.55           C  
ATOM    272  CD1 LEU A  37      21.625  21.408 -12.980  1.00 26.33           C  
ATOM    273  CD2 LEU A  37      23.931  20.602 -12.408  1.00 29.43           C  
ATOM    274  N   TYR A  38      20.751  16.881 -13.761  1.00 35.25           N  
ATOM    275  CA  TYR A  38      20.525  16.209 -15.035  1.00 30.23           C  
ATOM    276  C   TYR A  38      19.042  16.033 -15.310  1.00 38.40           C  
ATOM    277  O   TYR A  38      18.612  16.089 -16.469  1.00 39.59           O  
ATOM    278  CB  TYR A  38      21.228  14.853 -15.048  1.00 24.09           C  
ATOM    279  CG  TYR A  38      22.699  14.930 -14.701  1.00 26.90           C  
ATOM    280  CD1 TYR A  38      23.461  16.032 -15.074  1.00 24.82           C  
ATOM    281  CD2 TYR A  38      23.321  13.909 -13.994  1.00 21.81           C  
ATOM    282  CE1 TYR A  38      24.798  16.110 -14.758  1.00 27.85           C  
ATOM    283  CE2 TYR A  38      24.658  13.978 -13.673  1.00 23.07           C  
ATOM    284  CZ  TYR A  38      25.392  15.081 -14.059  1.00 28.05           C  
ATOM    285  OH  TYR A  38      26.726  15.154 -13.741  1.00 30.56           O  
ATOM    286  N   TYR A  39      18.245  15.837 -14.259  1.00 37.93           N  
ATOM    287  CA  TYR A  39      16.804  15.729 -14.443  1.00 32.22           C  
ATOM    288  C   TYR A  39      16.230  17.013 -15.027  1.00 30.72           C  
ATOM    289  O   TYR A  39      15.414  16.969 -15.954  1.00 36.05           O  
ATOM    290  CB  TYR A  39      16.130  15.377 -13.120  1.00 29.61           C  
ATOM    291  CG  TYR A  39      14.649  15.128 -13.256  1.00 32.57           C  
ATOM    292  CD1 TYR A  39      14.169  14.198 -14.170  1.00 35.61           C  
ATOM    293  CD2 TYR A  39      13.732  15.822 -12.480  1.00 26.91           C  
ATOM    294  CE1 TYR A  39      12.818  13.967 -14.308  1.00 39.81           C  
ATOM    295  CE2 TYR A  39      12.377  15.597 -12.610  1.00 39.88           C  
ATOM    296  CZ  TYR A  39      11.926  14.668 -13.526  1.00 42.50           C  
ATOM    297  OH  TYR A  39      10.577  14.437 -13.662  1.00 45.84           O  
ATOM    298  N   MET A  40      16.654  18.170 -14.512  1.00 35.43           N  
ATOM    299  CA  MET A  40      16.159  19.430 -15.056  1.00 36.31           C  
ATOM    300  C   MET A  40      16.655  19.647 -16.477  1.00 36.69           C  
ATOM    301  O   MET A  40      15.890  20.088 -17.342  1.00 36.35           O  
ATOM    302  CB  MET A  40      16.567  20.591 -14.159  1.00 26.98           C  
ATOM    303  CG  MET A  40      16.084  20.448 -12.738  1.00 27.60           C  
ATOM    304  SD  MET A  40      16.589  21.837 -11.714  1.00 41.01           S  
ATOM    305  CE  MET A  40      15.082  22.788 -11.741  1.00 35.66           C  
ATOM    306  N   TRP A  41      17.934  19.354 -16.734  1.00 29.59           N  
ATOM    307  CA  TRP A  41      18.442  19.376 -18.102  1.00 28.94           C  
ATOM    308  C   TRP A  41      17.559  18.543 -19.015  1.00 36.76           C  
ATOM    309  O   TRP A  41      17.225  18.956 -20.129  1.00 39.61           O  
ATOM    310  CB  TRP A  41      19.869  18.834 -18.155  1.00 27.57           C  
ATOM    311  CG  TRP A  41      20.909  19.716 -17.580  1.00 38.89           C  
ATOM    312  CD1 TRP A  41      20.727  20.908 -16.939  1.00 33.75           C  
ATOM    313  CD2 TRP A  41      22.315  19.472 -17.591  1.00 32.69           C  
ATOM    314  NE1 TRP A  41      21.942  21.418 -16.546  1.00 33.78           N  
ATOM    315  CE2 TRP A  41      22.931  20.554 -16.938  1.00 27.58           C  
ATOM    316  CE3 TRP A  41      23.114  18.438 -18.089  1.00 33.57           C  
ATOM    317  CZ2 TRP A  41      24.306  20.633 -16.773  1.00 28.26           C  
ATOM    318  CZ3 TRP A  41      24.480  18.519 -17.923  1.00 36.01           C  
ATOM    319  CH2 TRP A  41      25.063  19.609 -17.270  1.00 38.08           C  
ATOM    320  N   PHE A  42      17.198  17.343 -18.559  1.00 33.37           N  
ATOM    321  CA  PHE A  42      16.345  16.468 -19.351  1.00 37.09           C  
ATOM    322  C   PHE A  42      14.972  17.095 -19.568  1.00 43.90           C  
ATOM    323  O   PHE A  42      14.443  17.087 -20.687  1.00 41.59           O  
ATOM    324  CB  PHE A  42      16.233  15.108 -18.658  1.00 34.24           C  
ATOM    325  CG  PHE A  42      15.124  14.250 -19.177  1.00 44.00           C  
ATOM    326  CD1 PHE A  42      15.252  13.583 -20.383  1.00 55.85           C  
ATOM    327  CD2 PHE A  42      13.956  14.093 -18.447  1.00 48.07           C  
ATOM    328  CE1 PHE A  42      14.231  12.781 -20.859  1.00 48.95           C  
ATOM    329  CE2 PHE A  42      12.932  13.295 -18.916  1.00 40.88           C  
ATOM    330  CZ  PHE A  42      13.069  12.637 -20.123  1.00 44.95           C  
ATOM    331  N   LEU A  43      14.383  17.651 -18.504  1.00 35.07           N  
ATOM    332  CA  LEU A  43      13.093  18.324 -18.633  1.00 40.54           C  
ATOM    333  C   LEU A  43      13.194  19.538 -19.549  1.00 47.85           C  
ATOM    334  O   LEU A  43      12.275  19.818 -20.331  1.00 47.17           O  
ATOM    335  CB  LEU A  43      12.569  18.730 -17.253  1.00 40.89           C  
ATOM    336  CG  LEU A  43      12.169  17.596 -16.303  1.00 45.75           C  
ATOM    337  CD1 LEU A  43      11.575  18.141 -15.006  1.00 38.15           C  
ATOM    338  CD2 LEU A  43      11.196  16.645 -16.984  1.00 32.70           C  
ATOM    339  N   ILE A  44      14.303  20.274 -19.466  1.00 45.88           N  
ATOM    340  CA  ILE A  44      14.555  21.341 -20.429  1.00 33.85           C  
ATOM    341  C   ILE A  44      14.712  20.761 -21.826  1.00 40.16           C  
ATOM    342  O   ILE A  44      14.220  21.326 -22.810  1.00 42.71           O  
ATOM    343  CB  ILE A  44      15.799  22.149 -20.016  1.00 32.58           C  
ATOM    344  CG1 ILE A  44      15.565  22.867 -18.692  1.00 32.35           C  
ATOM    345  CG2 ILE A  44      16.167  23.155 -21.092  1.00 31.36           C  
ATOM    346  CD1 ILE A  44      16.831  23.417 -18.085  1.00 27.53           C  
ATOM    347  N   SER A  45      15.392  19.616 -21.934  1.00 46.00           N  
ATOM    348  CA  SER A  45      15.730  19.074 -23.246  1.00 34.47           C  
ATOM    349  C   SER A  45      14.491  18.658 -24.027  1.00 42.97           C  
ATOM    350  O   SER A  45      14.463  18.787 -25.256  1.00 52.45           O  
ATOM    351  CB  SER A  45      16.687  17.893 -23.094  1.00 41.41           C  
ATOM    352  OG  SER A  45      16.708  17.099 -24.266  1.00 62.91           O  
ATOM    353  N   THR A  46      13.462  18.168 -23.346  1.00 39.14           N  
ATOM    354  CA  THR A  46      12.228  17.768 -24.007  1.00 36.25           C  
ATOM    355  C   THR A  46      11.224  18.908 -24.126  1.00 42.25           C  
ATOM    356  O   THR A  46      10.097  18.677 -24.575  1.00 43.07           O  
ATOM    357  CB  THR A  46      11.588  16.599 -23.256  1.00 40.71           C  
ATOM    358  OG1 THR A  46      10.987  17.079 -22.047  1.00 48.50           O  
ATOM    359  CG2 THR A  46      12.647  15.564 -22.902  1.00 38.56           C  
ATOM    360  N   GLY A  47      11.601  20.123 -23.735  1.00 47.68           N  
ATOM    361  CA  GLY A  47      10.705  21.256 -23.768  1.00 37.21           C  
ATOM    362  C   GLY A  47       9.753  21.362 -22.597  1.00 45.07           C  
ATOM    363  O   GLY A  47       8.946  22.299 -22.564  1.00 49.31           O  
ATOM    364  N   ASP A  48       9.824  20.444 -21.629  1.00 48.33           N  
ATOM    365  CA  ASP A  48       8.857  20.448 -20.535  1.00 50.60           C  
ATOM    366  C   ASP A  48       9.142  21.566 -19.537  1.00 48.17           C  
ATOM    367  O   ASP A  48       8.211  22.191 -19.016  1.00 54.79           O  
ATOM    368  CB  ASP A  48       8.851  19.089 -19.836  1.00 47.18           C  
ATOM    369  CG  ASP A  48       7.613  18.878 -18.990  1.00 52.21           C  
ATOM    370  OD1 ASP A  48       6.506  18.845 -19.565  1.00 74.97           O  
ATOM    371  OD2 ASP A  48       7.745  18.739 -17.755  1.00 59.35           O  
ATOM    372  N   LEU A  49      10.413  21.830 -19.257  1.00 42.98           N  
ATOM    373  CA  LEU A  49      10.826  22.863 -18.313  1.00 42.31           C  
ATOM    374  C   LEU A  49      11.442  24.024 -19.084  1.00 42.57           C  
ATOM    375  O   LEU A  49      12.491  23.865 -19.713  1.00 49.81           O  
ATOM    376  CB  LEU A  49      11.819  22.297 -17.299  1.00 45.68           C  
ATOM    377  CG  LEU A  49      12.418  23.256 -16.278  1.00 40.48           C  
ATOM    378  CD1 LEU A  49      11.328  23.928 -15.461  1.00 35.65           C  
ATOM    379  CD2 LEU A  49      13.374  22.494 -15.380  1.00 46.98           C  
ATOM    380  N   HIS A  50      10.797  25.187 -19.033  1.00 46.29           N  
ATOM    381  CA  HIS A  50      11.228  26.336 -19.830  1.00 43.43           C  
ATOM    382  C   HIS A  50      12.098  27.272 -18.991  1.00 41.04           C  
ATOM    383  O   HIS A  50      11.697  28.371 -18.604  1.00 40.83           O  
ATOM    384  CB  HIS A  50      10.020  27.068 -20.407  1.00 54.52           C  
ATOM    385  CG  HIS A  50       9.212  26.246 -21.360  1.00 55.47           C  
ATOM    386  ND1 HIS A  50       8.037  25.627 -20.994  1.00 56.24           N  
ATOM    387  CD2 HIS A  50       9.423  25.920 -22.657  1.00 57.44           C  
ATOM    388  CE1 HIS A  50       7.552  24.963 -22.028  1.00 68.26           C  
ATOM    389  NE2 HIS A  50       8.375  25.124 -23.048  1.00 69.45           N  
ATOM    390  N   ILE A  51      13.310  26.797 -18.701  1.00 40.87           N  
ATOM    391  CA  ILE A  51      14.348  27.598 -18.067  1.00 30.76           C  
ATOM    392  C   ILE A  51      15.664  27.296 -18.768  1.00 38.78           C  
ATOM    393  O   ILE A  51      15.809  26.283 -19.454  1.00 37.35           O  
ATOM    394  CB  ILE A  51      14.489  27.327 -16.551  1.00 41.68           C  
ATOM    395  CG1 ILE A  51      14.906  25.872 -16.310  1.00 37.21           C  
ATOM    396  CG2 ILE A  51      13.199  27.663 -15.813  1.00 36.44           C  
ATOM    397  CD1 ILE A  51      15.246  25.561 -14.873  1.00 31.37           C  
ATOM    398  N   THR A  52      16.631  28.192 -18.589  1.00 34.80           N  
ATOM    399  CA  THR A  52      17.971  27.949 -19.098  1.00 36.05           C  
ATOM    400  C   THR A  52      18.713  26.980 -18.180  1.00 47.13           C  
ATOM    401  O   THR A  52      18.363  26.804 -17.010  1.00 40.95           O  
ATOM    402  CB  THR A  52      18.756  29.256 -19.210  1.00 34.27           C  
ATOM    403  OG1 THR A  52      19.025  29.763 -17.896  1.00 41.88           O  
ATOM    404  CG2 THR A  52      17.959  30.285 -19.987  1.00 37.03           C  
ATOM    405  N   ARG A  53      19.752  26.342 -18.726  1.00 40.98           N  
ATOM    406  CA  ARG A  53      20.609  25.522 -17.878  1.00 34.14           C  
ATOM    407  C   ARG A  53      21.293  26.366 -16.814  1.00 40.45           C  
ATOM    408  O   ARG A  53      21.576  25.871 -15.716  1.00 35.36           O  
ATOM    409  CB  ARG A  53      21.646  24.776 -18.719  1.00 31.39           C  
ATOM    410  CG  ARG A  53      21.061  23.660 -19.555  1.00 30.03           C  
ATOM    411  CD  ARG A  53      22.129  22.670 -19.977  1.00 31.74           C  
ATOM    412  NE  ARG A  53      21.542  21.538 -20.686  1.00 41.02           N  
ATOM    413  CZ  ARG A  53      22.226  20.485 -21.121  1.00 32.52           C  
ATOM    414  NH1 ARG A  53      23.535  20.408 -20.922  1.00 27.44           N  
ATOM    415  NH2 ARG A  53      21.595  19.507 -21.755  1.00 38.26           N  
ATOM    416  N   ALA A  54      21.560  27.640 -17.115  1.00 34.64           N  
ATOM    417  CA  ALA A  54      22.073  28.539 -16.089  1.00 35.06           C  
ATOM    418  C   ALA A  54      21.078  28.678 -14.947  1.00 37.33           C  
ATOM    419  O   ALA A  54      21.466  28.678 -13.773  1.00 41.87           O  
ATOM    420  CB  ALA A  54      22.394  29.905 -16.692  1.00 32.05           C  
ATOM    421  N   THR A  55      19.788  28.786 -15.270  1.00 38.41           N  
ATOM    422  CA  THR A  55      18.777  28.841 -14.222  1.00 37.50           C  
ATOM    423  C   THR A  55      18.645  27.497 -13.517  1.00 34.45           C  
ATOM    424  O   THR A  55      18.449  27.451 -12.296  1.00 32.69           O  
ATOM    425  CB  THR A  55      17.433  29.275 -14.806  1.00 37.33           C  
ATOM    426  OG1 THR A  55      17.579  30.569 -15.404  1.00 42.06           O  
ATOM    427  CG2 THR A  55      16.374  29.350 -13.710  1.00 31.90           C  
ATOM    428  N   ALA A  56      18.756  26.393 -14.266  1.00 34.00           N  
ATOM    429  CA  ALA A  56      18.710  25.079 -13.635  1.00 32.20           C  
ATOM    430  C   ALA A  56      19.863  24.914 -12.653  1.00 36.75           C  
ATOM    431  O   ALA A  56      19.706  24.303 -11.590  1.00 37.84           O  
ATOM    432  CB  ALA A  56      18.732  23.974 -14.697  1.00 32.79           C  
ATOM    433  N   ALA A  57      21.023  25.481 -12.979  1.00 36.82           N  
ATOM    434  CA  ALA A  57      22.145  25.432 -12.052  1.00 29.79           C  
ATOM    435  C   ALA A  57      21.916  26.326 -10.837  1.00 37.89           C  
ATOM    436  O   ALA A  57      22.349  25.984  -9.729  1.00 37.23           O  
ATOM    437  CB  ALA A  57      23.436  25.821 -12.773  1.00 33.59           C  
ATOM    438  N   SER A  58      21.243  27.467 -11.015  1.00 35.84           N  
ATOM    439  CA  SER A  58      20.990  28.353  -9.883  1.00 35.81           C  
ATOM    440  C   SER A  58      19.959  27.768  -8.929  1.00 39.40           C  
ATOM    441  O   SER A  58      19.980  28.073  -7.730  1.00 34.68           O  
ATOM    442  CB  SER A  58      20.524  29.719 -10.374  1.00 38.49           C  
ATOM    443  OG  SER A  58      19.256  29.609 -10.995  1.00 59.82           O  
ATOM    444  N   ILE A  59      19.054  26.930  -9.438  1.00 40.75           N  
ATOM    445  CA  ILE A  59      18.064  26.296  -8.574  1.00 37.42           C  
ATOM    446  C   ILE A  59      18.735  25.302  -7.637  1.00 28.46           C  
ATOM    447  O   ILE A  59      18.405  25.233  -6.449  1.00 30.69           O  
ATOM    448  CB  ILE A  59      16.958  25.637  -9.419  1.00 32.07           C  
ATOM    449  CG1 ILE A  59      16.032  26.714  -9.985  1.00 34.99           C  
ATOM    450  CG2 ILE A  59      16.163  24.643  -8.590  1.00 29.01           C  
ATOM    451  CD1 ILE A  59      15.101  26.219 -11.045  1.00 41.69           C  
ATOM    452  N   MET A  60      19.702  24.535  -8.148  1.00 33.23           N  
ATOM    453  CA  MET A  60      20.445  23.608  -7.299  1.00 35.06           C  
ATOM    454  C   MET A  60      21.080  24.330  -6.117  1.00 31.99           C  
ATOM    455  O   MET A  60      21.009  23.851  -4.980  1.00 33.41           O  
ATOM    456  CB  MET A  60      21.510  22.883  -8.123  1.00 35.43           C  
ATOM    457  CG  MET A  60      20.950  21.993  -9.231  1.00 29.20           C  
ATOM    458  SD  MET A  60      20.109  20.524  -8.608  1.00 34.82           S  
ATOM    459  CE  MET A  60      21.503  19.543  -8.065  1.00 25.72           C  
ATOM    460  N   ALA A  61      21.675  25.500  -6.361  1.00 34.27           N  
ATOM    461  CA  ALA A  61      22.365  26.220  -5.296  1.00 29.56           C  
ATOM    462  C   ALA A  61      21.383  26.772  -4.270  1.00 33.11           C  
ATOM    463  O   ALA A  61      21.581  26.613  -3.060  1.00 30.45           O  
ATOM    464  CB  ALA A  61      23.212  27.345  -5.887  1.00 34.68           C  
ATOM    465  N   ILE A  62      20.316  27.428  -4.734  1.00 29.00           N  
ATOM    466  CA  ILE A  62      19.373  28.040  -3.805  1.00 30.09           C  
ATOM    467  C   ILE A  62      18.523  26.975  -3.119  1.00 33.38           C  
ATOM    468  O   ILE A  62      18.045  27.182  -1.996  1.00 33.00           O  
ATOM    469  CB  ILE A  62      18.513  29.091  -4.533  1.00 38.80           C  
ATOM    470  CG1 ILE A  62      17.977  30.128  -3.540  1.00 36.85           C  
ATOM    471  CG2 ILE A  62      17.388  28.426  -5.322  1.00 25.75           C  
ATOM    472  CD1 ILE A  62      19.064  30.959  -2.874  1.00 29.63           C  
ATOM    473  N   TYR A  63      18.321  25.826  -3.771  1.00 33.89           N  
ATOM    474  CA  TYR A  63      17.698  24.686  -3.104  1.00 30.70           C  
ATOM    475  C   TYR A  63      18.523  24.267  -1.894  1.00 36.04           C  
ATOM    476  O   TYR A  63      17.996  24.130  -0.783  1.00 29.74           O  
ATOM    477  CB  TYR A  63      17.548  23.530  -4.101  1.00 31.21           C  
ATOM    478  CG  TYR A  63      16.799  22.290  -3.640  1.00 34.06           C  
ATOM    479  CD1 TYR A  63      16.221  22.204  -2.375  1.00 32.37           C  
ATOM    480  CD2 TYR A  63      16.679  21.193  -4.488  1.00 36.95           C  
ATOM    481  CE1 TYR A  63      15.546  21.059  -1.974  1.00 32.58           C  
ATOM    482  CE2 TYR A  63      16.009  20.050  -4.098  1.00 34.11           C  
ATOM    483  CZ  TYR A  63      15.444  19.987  -2.842  1.00 36.19           C  
ATOM    484  OH  TYR A  63      14.777  18.844  -2.464  1.00 31.65           O  
ATOM    485  N   ALA A  64      19.829  24.076  -2.091  1.00 32.22           N  
ATOM    486  CA  ALA A  64      20.705  23.744  -0.975  1.00 33.56           C  
ATOM    487  C   ALA A  64      20.646  24.819   0.102  1.00 34.01           C  
ATOM    488  O   ALA A  64      20.514  24.513   1.291  1.00 35.69           O  
ATOM    489  CB  ALA A  64      22.137  23.554  -1.476  1.00 27.71           C  
ATOM    490  N   SER A  65      20.709  26.091  -0.306  1.00 31.11           N  
ATOM    491  CA  SER A  65      20.757  27.193   0.650  1.00 29.43           C  
ATOM    492  C   SER A  65      19.549  27.187   1.581  1.00 34.63           C  
ATOM    493  O   SER A  65      19.686  27.414   2.789  1.00 35.38           O  
ATOM    494  CB  SER A  65      20.851  28.522  -0.100  1.00 29.05           C  
ATOM    495  OG  SER A  65      20.961  29.615   0.789  1.00 30.53           O  
ATOM    496  N   MET A  66      18.356  26.929   1.041  1.00 29.47           N  
ATOM    497  CA  MET A  66      17.168  26.898   1.886  1.00 31.59           C  
ATOM    498  C   MET A  66      17.162  25.688   2.812  1.00 39.03           C  
ATOM    499  O   MET A  66      16.632  25.768   3.924  1.00 36.38           O  
ATOM    500  CB  MET A  66      15.909  26.917   1.021  1.00 32.68           C  
ATOM    501  CG  MET A  66      15.752  28.160   0.156  1.00 34.92           C  
ATOM    502  SD  MET A  66      15.542  29.684   1.101  1.00 55.58           S  
ATOM    503  CE  MET A  66      17.198  30.368   1.066  1.00 27.64           C  
ATOM    504  N   VAL A  67      17.747  24.571   2.377  1.00 34.66           N  
ATOM    505  CA  VAL A  67      17.797  23.373   3.213  1.00 34.06           C  
ATOM    506  C   VAL A  67      18.631  23.628   4.466  1.00 38.38           C  
ATOM    507  O   VAL A  67      18.223  23.283   5.582  1.00 37.93           O  
ATOM    508  CB  VAL A  67      18.328  22.178   2.398  1.00 34.25           C  
ATOM    509  CG1 VAL A  67      18.705  21.027   3.306  1.00 24.12           C  
ATOM    510  CG2 VAL A  67      17.282  21.731   1.383  1.00 33.45           C  
ATOM    511  N   TYR A  68      19.804  24.248   4.305  1.00 34.18           N  
ATOM    512  CA  TYR A  68      20.605  24.613   5.471  1.00 34.92           C  
ATOM    513  C   TYR A  68      19.916  25.696   6.296  1.00 42.71           C  
ATOM    514  O   TYR A  68      19.910  25.634   7.532  1.00 45.00           O  
ATOM    515  CB  TYR A  68      21.999  25.070   5.035  1.00 42.21           C  
ATOM    516  CG  TYR A  68      22.767  24.052   4.215  1.00 48.55           C  
ATOM    517  CD1 TYR A  68      23.358  22.947   4.813  1.00 54.70           C  
ATOM    518  CD2 TYR A  68      22.918  24.209   2.844  1.00 53.80           C  
ATOM    519  CE1 TYR A  68      24.062  22.019   4.064  1.00 57.30           C  
ATOM    520  CE2 TYR A  68      23.615  23.287   2.086  1.00 55.54           C  
ATOM    521  CZ  TYR A  68      24.187  22.196   2.701  1.00 60.00           C  
ATOM    522  OH  TYR A  68      24.886  21.279   1.951  1.00 73.40           O  
ATOM    523  N   LEU A  69      19.324  26.693   5.633  1.00 38.78           N  
ATOM    524  CA  LEU A  69      18.558  27.711   6.342  1.00 39.89           C  
ATOM    525  C   LEU A  69      17.298  27.142   6.979  1.00 41.88           C  
ATOM    526  O   LEU A  69      16.775  27.733   7.926  1.00 43.14           O  
ATOM    527  CB  LEU A  69      18.187  28.850   5.394  1.00 38.80           C  
ATOM    528  CG  LEU A  69      17.350  29.992   5.974  1.00 34.28           C  
ATOM    529  CD1 LEU A  69      18.079  30.662   7.130  1.00 33.23           C  
ATOM    530  CD2 LEU A  69      16.997  31.000   4.897  1.00 38.68           C  
ATOM    531  N   SER A  70      16.784  26.023   6.476  1.00 41.45           N  
ATOM    532  CA  SER A  70      15.686  25.379   7.178  1.00 37.65           C  
ATOM    533  C   SER A  70      16.185  24.708   8.448  1.00 44.94           C  
ATOM    534  O   SER A  70      15.425  24.560   9.413  1.00 38.50           O  
ATOM    535  CB  SER A  70      14.981  24.374   6.265  1.00 30.35           C  
ATOM    536  OG  SER A  70      13.864  23.792   6.914  1.00 42.85           O  
ATOM    537  N   GLY A  71      17.459  24.320   8.468  1.00 44.55           N  
ATOM    538  CA  GLY A  71      18.057  23.628   9.590  1.00 34.34           C  
ATOM    539  C   GLY A  71      18.403  24.484  10.787  1.00 38.14           C  
ATOM    540  O   GLY A  71      18.696  23.931  11.851  1.00 49.52           O  
ATOM    541  N   THR A  72      18.388  25.810  10.652  1.00 45.88           N  
ATOM    542  CA  THR A  72      18.624  26.647  11.824  1.00 38.34           C  
ATOM    543  C   THR A  72      17.389  26.746  12.709  1.00 44.35           C  
ATOM    544  O   THR A  72      17.515  26.966  13.919  1.00 49.36           O  
ATOM    545  CB  THR A  72      19.084  28.045  11.410  1.00 49.03           C  
ATOM    546  OG1 THR A  72      19.159  28.879  12.574  1.00 83.24           O  
ATOM    547  CG2 THR A  72      18.119  28.664  10.413  1.00 38.88           C  
ATOM    548  N   ILE A  73      16.201  26.573  12.133  1.00 38.60           N  
ATOM    549  CA  ILE A  73      14.969  26.644  12.907  1.00 40.17           C  
ATOM    550  C   ILE A  73      14.556  25.293  13.482  1.00 38.37           C  
ATOM    551  O   ILE A  73      13.883  25.254  14.522  1.00 37.04           O  
ATOM    552  CB  ILE A  73      13.837  27.223  12.038  1.00 41.67           C  
ATOM    553  CG1 ILE A  73      14.204  28.620  11.548  1.00 47.59           C  
ATOM    554  CG2 ILE A  73      12.544  27.296  12.806  1.00 61.11           C  
ATOM    555  CD1 ILE A  73      14.486  28.690  10.073  1.00 57.42           C  
ATOM    556  N   GLY A  74      14.964  24.187  12.856  1.00 37.40           N  
ATOM    557  CA  GLY A  74      14.446  22.887  13.251  1.00 38.60           C  
ATOM    558  C   GLY A  74      14.709  22.545  14.705  1.00 37.40           C  
ATOM    559  O   GLY A  74      13.862  21.948  15.374  1.00 30.53           O  
ATOM    560  N   GLY A  75      15.889  22.902  15.213  1.00 34.86           N  
ATOM    561  CA  GLY A  75      16.177  22.652  16.615  1.00 31.78           C  
ATOM    562  C   GLY A  75      15.248  23.415  17.539  1.00 36.60           C  
ATOM    563  O   GLY A  75      14.774  22.878  18.543  1.00 35.05           O  
ATOM    564  N   PHE A  76      14.968  24.676  17.205  1.00 39.56           N  
ATOM    565  CA  PHE A  76      14.031  25.473  17.991  1.00 31.58           C  
ATOM    566  C   PHE A  76      12.654  24.826  18.027  1.00 36.24           C  
ATOM    567  O   PHE A  76      12.040  24.702  19.093  1.00 37.50           O  
ATOM    568  CB  PHE A  76      13.944  26.885  17.410  1.00 38.52           C  
ATOM    569  CG  PHE A  76      12.873  27.740  18.030  1.00 43.22           C  
ATOM    570  CD1 PHE A  76      11.590  27.767  17.501  1.00 45.23           C  
ATOM    571  CD2 PHE A  76      13.155  28.538  19.125  1.00 44.31           C  
ATOM    572  CE1 PHE A  76      10.607  28.556  18.064  1.00 41.36           C  
ATOM    573  CE2 PHE A  76      12.177  29.335  19.688  1.00 40.65           C  
ATOM    574  CZ  PHE A  76      10.900  29.340  19.159  1.00 38.68           C  
ATOM    575  N   VAL A  77      12.142  24.428  16.862  1.00 38.49           N  
ATOM    576  CA  VAL A  77      10.796  23.867  16.804  1.00 42.15           C  
ATOM    577  C   VAL A  77      10.701  22.616  17.667  1.00 35.25           C  
ATOM    578  O   VAL A  77       9.711  22.411  18.380  1.00 41.07           O  
ATOM    579  CB  VAL A  77      10.390  23.598  15.342  1.00 42.36           C  
ATOM    580  CG1 VAL A  77       9.018  22.958  15.288  1.00 35.91           C  
ATOM    581  CG2 VAL A  77      10.402  24.897  14.547  1.00 35.28           C  
ATOM    582  N   ALA A  78      11.745  21.784  17.653  1.00 36.72           N  
ATOM    583  CA  ALA A  78      11.729  20.561  18.450  1.00 32.65           C  
ATOM    584  C   ALA A  78      12.048  20.810  19.918  1.00 35.51           C  
ATOM    585  O   ALA A  78      11.615  20.038  20.776  1.00 40.27           O  
ATOM    586  CB  ALA A  78      12.718  19.551  17.880  1.00 32.69           C  
ATOM    587  N   ASP A  79      12.804  21.859  20.237  1.00 37.23           N  
ATOM    588  CA  ASP A  79      13.113  22.108  21.639  1.00 33.05           C  
ATOM    589  C   ASP A  79      11.980  22.813  22.366  1.00 39.19           C  
ATOM    590  O   ASP A  79      11.928  22.753  23.598  1.00 39.36           O  
ATOM    591  CB  ASP A  79      14.398  22.928  21.767  1.00 39.20           C  
ATOM    592  CG  ASP A  79      15.635  22.143  21.372  1.00 43.30           C  
ATOM    593  OD1 ASP A  79      15.631  20.907  21.554  1.00 51.09           O  
ATOM    594  OD2 ASP A  79      16.603  22.760  20.874  1.00 49.51           O  
ATOM    595  N   ARG A  80      11.057  23.448  21.638  1.00 31.36           N  
ATOM    596  CA  ARG A  80      10.032  24.267  22.269  1.00 28.66           C  
ATOM    597  C   ARG A  80       8.599  23.950  21.863  1.00 35.37           C  
ATOM    598  O   ARG A  80       7.686  24.316  22.609  1.00 29.11           O  
ATOM    599  CB  ARG A  80      10.302  25.756  21.995  1.00 36.35           C  
ATOM    600  CG  ARG A  80      11.647  26.188  22.565  1.00 41.20           C  
ATOM    601  CD  ARG A  80      11.890  27.689  22.615  1.00 39.02           C  
ATOM    602  NE  ARG A  80      10.942  28.454  23.426  1.00 43.24           N  
ATOM    603  CZ  ARG A  80      10.771  28.318  24.738  1.00 35.14           C  
ATOM    604  NH1 ARG A  80      11.453  27.414  25.413  1.00 40.36           N  
ATOM    605  NH2 ARG A  80       9.897  29.078  25.378  1.00 49.84           N  
ATOM    606  N   ILE A  81       8.357  23.287  20.734  1.00 35.29           N  
ATOM    607  CA  ILE A  81       6.983  23.127  20.274  1.00 35.38           C  
ATOM    608  C   ILE A  81       6.605  21.655  20.186  1.00 33.66           C  
ATOM    609  O   ILE A  81       5.656  21.210  20.841  1.00 41.37           O  
ATOM    610  CB  ILE A  81       6.753  23.836  18.928  1.00 30.57           C  
ATOM    611  CG1 ILE A  81       6.891  25.356  19.091  1.00 26.36           C  
ATOM    612  CG2 ILE A  81       5.383  23.495  18.380  1.00 28.61           C  
ATOM    613  CD1 ILE A  81       6.614  26.132  17.831  1.00 41.89           C  
ATOM    614  N   ILE A  82       7.332  20.893  19.374  1.00 39.63           N  
ATOM    615  CA  ILE A  82       7.143  19.449  19.272  1.00 36.53           C  
ATOM    616  C   ILE A  82       8.338  18.801  19.953  1.00 41.97           C  
ATOM    617  O   ILE A  82       9.168  19.497  20.541  1.00 52.79           O  
ATOM    618  CB  ILE A  82       6.995  19.001  17.807  1.00 35.32           C  
ATOM    619  CG1 ILE A  82       8.264  19.313  17.010  1.00 28.85           C  
ATOM    620  CG2 ILE A  82       5.797  19.688  17.164  1.00 25.04           C  
ATOM    621  CD1 ILE A  82       8.147  18.979  15.533  1.00 28.46           C  
ATOM    622  N   GLY A  83       8.435  17.484  19.907  1.00 28.40           N  
ATOM    623  CA  GLY A  83       9.581  16.842  20.511  1.00 38.09           C  
ATOM    624  C   GLY A  83      10.770  16.785  19.572  1.00 32.50           C  
ATOM    625  O   GLY A  83      10.676  17.064  18.380  1.00 38.38           O  
ATOM    626  N   ALA A  84      11.921  16.409  20.125  1.00 32.61           N  
ATOM    627  CA  ALA A  84      13.070  16.148  19.265  1.00 28.13           C  
ATOM    628  C   ALA A  84      12.853  14.890  18.438  1.00 39.10           C  
ATOM    629  O   ALA A  84      13.172  14.855  17.243  1.00 40.47           O  
ATOM    630  CB  ALA A  84      14.342  16.016  20.100  1.00 29.95           C  
ATOM    631  N   ARG A  85      12.321  13.844  19.057  1.00 40.72           N  
ATOM    632  CA  ARG A  85      12.058  12.594  18.347  1.00 40.67           C  
ATOM    633  C   ARG A  85      10.911  12.738  17.348  1.00 35.56           C  
ATOM    634  O   ARG A  85      10.992  12.173  16.241  1.00 34.64           O  
ATOM    635  CB  ARG A  85      11.776  11.455  19.340  1.00 39.48           C  
ATOM    636  CG  ARG A  85      13.035  10.800  19.902  1.00 36.32           C  
ATOM    637  CD  ARG A  85      12.734   9.951  21.129  1.00 42.38           C  
ATOM    638  NE  ARG A  85      11.924   8.773  20.826  1.00 44.82           N  
ATOM    639  CZ  ARG A  85      11.514   7.905  21.746  1.00 47.59           C  
ATOM    640  NH1 ARG A  85      11.837   8.091  23.018  1.00 46.10           N  
ATOM    641  NH2 ARG A  85      10.778   6.859  21.398  1.00 46.69           N  
ATOM    642  N   PRO A  86       9.822  13.443  17.680  1.00 34.81           N  
ATOM    643  CA  PRO A  86       8.811  13.711  16.640  1.00 29.49           C  
ATOM    644  C   PRO A  86       9.312  14.560  15.483  1.00 30.89           C  
ATOM    645  O   PRO A  86       8.859  14.358  14.351  1.00 29.39           O  
ATOM    646  CB  PRO A  86       7.697  14.427  17.420  1.00 28.37           C  
ATOM    647  CG  PRO A  86       7.837  13.906  18.795  1.00 31.14           C  
ATOM    648  CD  PRO A  86       9.298  13.734  19.030  1.00 30.38           C  
ATOM    649  N   ALA A  87      10.232  15.501  15.720  1.00 31.19           N  
ATOM    650  CA  ALA A  87      10.729  16.321  14.618  1.00 27.63           C  
ATOM    651  C   ALA A  87      11.492  15.476  13.608  1.00 34.28           C  
ATOM    652  O   ALA A  87      11.358  15.670  12.394  1.00 36.63           O  
ATOM    653  CB  ALA A  87      11.617  17.447  15.145  1.00 25.75           C  
ATOM    654  N   VAL A  88      12.298  14.535  14.095  1.00 34.10           N  
ATOM    655  CA  VAL A  88      13.057  13.661  13.208  1.00 33.83           C  
ATOM    656  C   VAL A  88      12.116  12.771  12.406  1.00 34.13           C  
ATOM    657  O   VAL A  88      12.250  12.644  11.184  1.00 32.23           O  
ATOM    658  CB  VAL A  88      14.072  12.837  14.020  1.00 31.65           C  
ATOM    659  CG1 VAL A  88      14.700  11.753  13.157  1.00 35.69           C  
ATOM    660  CG2 VAL A  88      15.141  13.752  14.598  1.00 34.59           C  
ATOM    661  N   PHE A  89      11.143  12.152  13.080  1.00 36.59           N  
ATOM    662  CA  PHE A  89      10.202  11.268  12.398  1.00 33.45           C  
ATOM    663  C   PHE A  89       9.398  12.019  11.343  1.00 34.62           C  
ATOM    664  O   PHE A  89       9.413  11.662  10.160  1.00 32.39           O  
ATOM    665  CB  PHE A  89       9.262  10.607  13.409  1.00 31.47           C  
ATOM    666  CG  PHE A  89       8.187   9.769  12.769  1.00 36.32           C  
ATOM    667  CD1 PHE A  89       8.441   8.457  12.405  1.00 30.07           C  
ATOM    668  CD2 PHE A  89       6.929  10.296  12.519  1.00 33.68           C  
ATOM    669  CE1 PHE A  89       7.463   7.687  11.810  1.00 31.08           C  
ATOM    670  CE2 PHE A  89       5.949   9.531  11.921  1.00 32.81           C  
ATOM    671  CZ  PHE A  89       6.215   8.223  11.569  1.00 27.13           C  
ATOM    672  N   TRP A  90       8.670  13.060  11.761  1.00 32.79           N  
ATOM    673  CA  TRP A  90       7.819  13.777  10.817  1.00 29.20           C  
ATOM    674  C   TRP A  90       8.637  14.531   9.779  1.00 37.19           C  
ATOM    675  O   TRP A  90       8.162  14.748   8.659  1.00 42.29           O  
ATOM    676  CB  TRP A  90       6.881  14.725  11.559  1.00 29.43           C  
ATOM    677  CG  TRP A  90       5.762  13.999  12.217  1.00 32.12           C  
ATOM    678  CD1 TRP A  90       5.500  13.935  13.552  1.00 22.91           C  
ATOM    679  CD2 TRP A  90       4.764  13.198  11.571  1.00 37.31           C  
ATOM    680  NE1 TRP A  90       4.392  13.156  13.778  1.00 33.65           N  
ATOM    681  CE2 TRP A  90       3.922  12.691  12.577  1.00 29.87           C  
ATOM    682  CE3 TRP A  90       4.498  12.868  10.237  1.00 34.31           C  
ATOM    683  CZ2 TRP A  90       2.833  11.870  12.295  1.00 31.91           C  
ATOM    684  CZ3 TRP A  90       3.417  12.052   9.958  1.00 33.54           C  
ATOM    685  CH2 TRP A  90       2.598  11.563  10.983  1.00 38.91           C  
ATOM    686  N   GLY A  91       9.859  14.932  10.123  1.00 31.84           N  
ATOM    687  CA  GLY A  91      10.760  15.437   9.103  1.00 32.57           C  
ATOM    688  C   GLY A  91      11.077  14.382   8.060  1.00 34.57           C  
ATOM    689  O   GLY A  91      11.114  14.670   6.862  1.00 32.42           O  
ATOM    690  N   GLY A  92      11.291  13.140   8.502  1.00 32.26           N  
ATOM    691  CA  GLY A  92      11.559  12.064   7.562  1.00 25.82           C  
ATOM    692  C   GLY A  92      10.377  11.775   6.660  1.00 30.47           C  
ATOM    693  O   GLY A  92      10.545  11.479   5.475  1.00 31.18           O  
ATOM    694  N   VAL A  93       9.164  11.855   7.210  1.00 27.91           N  
ATOM    695  CA  VAL A  93       7.961  11.694   6.396  1.00 31.99           C  
ATOM    696  C   VAL A  93       7.933  12.733   5.282  1.00 38.10           C  
ATOM    697  O   VAL A  93       7.599  12.424   4.132  1.00 34.28           O  
ATOM    698  CB  VAL A  93       6.703  11.771   7.283  1.00 34.57           C  
ATOM    699  CG1 VAL A  93       5.451  11.912   6.434  1.00 34.87           C  
ATOM    700  CG2 VAL A  93       6.611  10.538   8.168  1.00 30.71           C  
ATOM    701  N   LEU A  94       8.312  13.975   5.596  1.00 35.10           N  
ATOM    702  CA  LEU A  94       8.298  15.024   4.581  1.00 35.33           C  
ATOM    703  C   LEU A  94       9.390  14.808   3.539  1.00 38.49           C  
ATOM    704  O   LEU A  94       9.171  15.058   2.347  1.00 38.83           O  
ATOM    705  CB  LEU A  94       8.438  16.391   5.246  1.00 33.53           C  
ATOM    706  CG  LEU A  94       7.276  16.760   6.170  1.00 36.12           C  
ATOM    707  CD1 LEU A  94       7.579  18.029   6.950  1.00 32.42           C  
ATOM    708  CD2 LEU A  94       5.991  16.910   5.368  1.00 33.65           C  
ATOM    709  N   ILE A  95      10.570  14.344   3.960  1.00 29.06           N  
ATOM    710  CA  ILE A  95      11.629  14.072   2.992  1.00 31.42           C  
ATOM    711  C   ILE A  95      11.240  12.904   2.093  1.00 33.71           C  
ATOM    712  O   ILE A  95      11.492  12.924   0.882  1.00 37.66           O  
ATOM    713  CB  ILE A  95      12.971  13.817   3.703  1.00 29.39           C  
ATOM    714  CG1 ILE A  95      13.323  14.962   4.652  1.00 31.61           C  
ATOM    715  CG2 ILE A  95      14.085  13.647   2.683  1.00 31.92           C  
ATOM    716  CD1 ILE A  95      14.516  14.654   5.540  1.00 30.91           C  
ATOM    717  N   MET A  96      10.621  11.868   2.668  1.00 30.22           N  
ATOM    718  CA  MET A  96      10.141  10.750   1.860  1.00 29.76           C  
ATOM    719  C   MET A  96       9.078  11.204   0.869  1.00 36.58           C  
ATOM    720  O   MET A  96       9.110  10.823  -0.307  1.00 33.14           O  
ATOM    721  CB  MET A  96       9.592   9.645   2.761  1.00 28.74           C  
ATOM    722  CG  MET A  96       9.171   8.384   2.027  1.00 34.86           C  
ATOM    723  SD  MET A  96       8.376   7.173   3.103  1.00 38.75           S  
ATOM    724  CE  MET A  96       6.938   8.097   3.643  1.00 37.24           C  
ATOM    725  N   LEU A  97       8.130  12.026   1.325  1.00 39.11           N  
ATOM    726  CA  LEU A  97       7.085  12.516   0.432  1.00 34.80           C  
ATOM    727  C   LEU A  97       7.668  13.387  -0.673  1.00 36.75           C  
ATOM    728  O   LEU A  97       7.210  13.333  -1.820  1.00 31.59           O  
ATOM    729  CB  LEU A  97       6.033  13.284   1.229  1.00 29.29           C  
ATOM    730  CG  LEU A  97       5.130  12.407   2.099  1.00 36.24           C  
ATOM    731  CD1 LEU A  97       4.320  13.253   3.068  1.00 26.74           C  
ATOM    732  CD2 LEU A  97       4.217  11.556   1.229  1.00 25.58           C  
ATOM    733  N   GLY A  98       8.689  14.183  -0.352  1.00 33.10           N  
ATOM    734  CA  GLY A  98       9.322  15.001  -1.372  1.00 30.10           C  
ATOM    735  C   GLY A  98       9.903  14.178  -2.507  1.00 39.81           C  
ATOM    736  O   GLY A  98       9.848  14.581  -3.672  1.00 43.80           O  
ATOM    737  N   HIS A  99      10.458  13.008  -2.188  1.00 36.10           N  
ATOM    738  CA  HIS A  99      11.038  12.167  -3.230  1.00 27.90           C  
ATOM    739  C   HIS A  99       9.970  11.361  -3.958  1.00 31.07           C  
ATOM    740  O   HIS A  99      10.087  11.115  -5.164  1.00 31.88           O  
ATOM    741  CB  HIS A  99      12.096  11.246  -2.628  1.00 28.52           C  
ATOM    742  CG  HIS A  99      13.327  11.964  -2.169  1.00 30.31           C  
ATOM    743  ND1 HIS A  99      13.787  11.896  -0.873  1.00 32.60           N  
ATOM    744  CD2 HIS A  99      14.198  12.758  -2.836  1.00 34.38           C  
ATOM    745  CE1 HIS A  99      14.887  12.619  -0.759  1.00 36.76           C  
ATOM    746  NE2 HIS A  99      15.158  13.152  -1.936  1.00 36.93           N  
ATOM    747  N   ILE A 100       8.925  10.938  -3.244  1.00 33.49           N  
ATOM    748  CA  ILE A 100       7.794  10.290  -3.900  1.00 33.35           C  
ATOM    749  C   ILE A 100       7.201  11.209  -4.962  1.00 34.28           C  
ATOM    750  O   ILE A 100       6.808  10.759  -6.044  1.00 39.50           O  
ATOM    751  CB  ILE A 100       6.746   9.862  -2.852  1.00 38.11           C  
ATOM    752  CG1 ILE A 100       7.301   8.734  -1.980  1.00 32.19           C  
ATOM    753  CG2 ILE A 100       5.452   9.430  -3.520  1.00 32.29           C  
ATOM    754  CD1 ILE A 100       6.408   8.352  -0.815  1.00 25.95           C  
ATOM    755  N   VAL A 101       7.159  12.514  -4.683  1.00 34.60           N  
ATOM    756  CA  VAL A 101       6.591  13.471  -5.630  1.00 38.23           C  
ATOM    757  C   VAL A 101       7.321  13.408  -6.967  1.00 40.85           C  
ATOM    758  O   VAL A 101       6.696  13.435  -8.035  1.00 43.02           O  
ATOM    759  CB  VAL A 101       6.613  14.889  -5.025  1.00 39.16           C  
ATOM    760  CG1 VAL A 101       6.388  15.939  -6.095  1.00 34.20           C  
ATOM    761  CG2 VAL A 101       5.548  15.012  -3.945  1.00 40.08           C  
ATOM    762  N   LEU A 102       8.651  13.298  -6.934  1.00 40.22           N  
ATOM    763  CA  LEU A 102       9.419  13.225  -8.173  1.00 36.01           C  
ATOM    764  C   LEU A 102       9.320  11.861  -8.842  1.00 39.06           C  
ATOM    765  O   LEU A 102       9.503  11.763 -10.061  1.00 39.69           O  
ATOM    766  CB  LEU A 102      10.885  13.564  -7.909  1.00 32.77           C  
ATOM    767  CG  LEU A 102      11.189  15.038  -7.649  1.00 26.83           C  
ATOM    768  CD1 LEU A 102      12.674  15.235  -7.436  1.00 29.05           C  
ATOM    769  CD2 LEU A 102      10.690  15.903  -8.796  1.00 29.21           C  
ATOM    770  N   ALA A 103       9.041  10.804  -8.076  1.00 33.06           N  
ATOM    771  CA  ALA A 103       8.913   9.481  -8.680  1.00 38.85           C  
ATOM    772  C   ALA A 103       7.604   9.338  -9.446  1.00 45.37           C  
ATOM    773  O   ALA A 103       7.517   8.524 -10.371  1.00 45.57           O  
ATOM    774  CB  ALA A 103       9.026   8.396  -7.610  1.00 30.56           C  
ATOM    775  N   LEU A 104       6.585  10.115  -9.080  1.00 43.47           N  
ATOM    776  CA  LEU A 104       5.313  10.093  -9.778  1.00 44.43           C  
ATOM    777  C   LEU A 104       5.483  10.587 -11.216  1.00 54.60           C  
ATOM    778  O   LEU A 104       6.450  11.277 -11.535  1.00 54.62           O  
ATOM    779  CB  LEU A 104       4.298  10.956  -9.034  1.00 49.90           C  
ATOM    780  CG  LEU A 104       4.018  10.548  -7.588  1.00 49.75           C  
ATOM    781  CD1 LEU A 104       3.102  11.551  -6.911  1.00 46.38           C  
ATOM    782  CD2 LEU A 104       3.425   9.149  -7.529  1.00 45.82           C  
ATOM    783  N   PRO A 105       4.550  10.222 -12.118  1.00 58.28           N  
ATOM    784  CA  PRO A 105       4.676  10.637 -13.534  1.00 49.90           C  
ATOM    785  C   PRO A 105       4.326  12.100 -13.761  1.00 56.32           C  
ATOM    786  O   PRO A 105       3.331  12.444 -14.400  1.00 64.47           O  
ATOM    787  CB  PRO A 105       3.692   9.699 -14.242  1.00 43.69           C  
ATOM    788  CG  PRO A 105       2.668   9.379 -13.223  1.00 49.46           C  
ATOM    789  CD  PRO A 105       3.394   9.320 -11.912  1.00 54.34           C  
ATOM    790  N   PHE A 106       5.159  12.979 -13.223  1.00 56.35           N  
ATOM    791  CA  PHE A 106       5.055  14.404 -13.476  1.00 48.10           C  
ATOM    792  C   PHE A 106       6.318  14.871 -14.195  1.00 50.21           C  
ATOM    793  O   PHE A 106       7.180  14.073 -14.582  1.00 48.11           O  
ATOM    794  CB  PHE A 106       4.859  15.186 -12.178  1.00 56.19           C  
ATOM    795  CG  PHE A 106       3.644  14.792 -11.395  1.00 61.19           C  
ATOM    796  CD1 PHE A 106       2.378  14.930 -11.929  1.00 72.50           C  
ATOM    797  CD2 PHE A 106       3.769  14.318 -10.101  1.00 62.96           C  
ATOM    798  CE1 PHE A 106       1.263  14.580 -11.193  1.00 73.46           C  
ATOM    799  CE2 PHE A 106       2.654  13.970  -9.363  1.00 68.39           C  
ATOM    800  CZ  PHE A 106       1.401  14.099  -9.910  1.00 72.18           C  
ATOM    801  N   GLY A 107       6.421  16.183 -14.361  1.00 51.99           N  
ATOM    802  CA  GLY A 107       7.614  16.803 -14.887  1.00 34.39           C  
ATOM    803  C   GLY A 107       8.002  18.016 -14.069  1.00 46.33           C  
ATOM    804  O   GLY A 107       8.326  17.895 -12.884  1.00 63.00           O  
ATOM    805  N   ALA A 108       7.956  19.198 -14.686  1.00 45.60           N  
ATOM    806  CA  ALA A 108       8.364  20.411 -13.984  1.00 47.93           C  
ATOM    807  C   ALA A 108       7.363  20.815 -12.908  1.00 51.22           C  
ATOM    808  O   ALA A 108       7.746  21.453 -11.920  1.00 56.88           O  
ATOM    809  CB  ALA A 108       8.555  21.551 -14.982  1.00 50.49           C  
ATOM    810  N   SER A 109       6.087  20.457 -13.081  1.00 49.98           N  
ATOM    811  CA  SER A 109       5.056  20.877 -12.136  1.00 47.47           C  
ATOM    812  C   SER A 109       5.336  20.354 -10.732  1.00 43.39           C  
ATOM    813  O   SER A 109       5.119  21.063  -9.742  1.00 46.03           O  
ATOM    814  CB  SER A 109       3.682  20.416 -12.627  1.00 50.57           C  
ATOM    815  OG  SER A 109       3.699  19.042 -12.975  1.00 47.13           O  
ATOM    816  N   ALA A 110       5.840  19.123 -10.629  1.00 43.47           N  
ATOM    817  CA  ALA A 110       6.155  18.525  -9.338  1.00 43.41           C  
ATOM    818  C   ALA A 110       7.410  19.100  -8.698  1.00 44.34           C  
ATOM    819  O   ALA A 110       7.623  18.880  -7.501  1.00 41.26           O  
ATOM    820  CB  ALA A 110       6.315  17.012  -9.495  1.00 31.20           C  
ATOM    821  N   LEU A 111       8.232  19.835  -9.452  1.00 38.19           N  
ATOM    822  CA  LEU A 111       9.548  20.228  -8.956  1.00 36.61           C  
ATOM    823  C   LEU A 111       9.453  21.119  -7.725  1.00 36.74           C  
ATOM    824  O   LEU A 111      10.215  20.941  -6.768  1.00 40.28           O  
ATOM    825  CB  LEU A 111      10.338  20.933 -10.057  1.00 43.33           C  
ATOM    826  CG  LEU A 111      11.034  20.026 -11.066  1.00 49.84           C  
ATOM    827  CD1 LEU A 111      11.703  20.851 -12.153  1.00 48.77           C  
ATOM    828  CD2 LEU A 111      12.049  19.145 -10.359  1.00 53.30           C  
ATOM    829  N   PHE A 112       8.546  22.096  -7.734  1.00 45.35           N  
ATOM    830  CA  PHE A 112       8.453  23.012  -6.601  1.00 37.68           C  
ATOM    831  C   PHE A 112       7.945  22.303  -5.352  1.00 43.51           C  
ATOM    832  O   PHE A 112       8.435  22.556  -4.244  1.00 38.93           O  
ATOM    833  CB  PHE A 112       7.548  24.197  -6.944  1.00 43.56           C  
ATOM    834  CG  PHE A 112       7.497  25.248  -5.871  1.00 54.65           C  
ATOM    835  CD1 PHE A 112       6.359  25.420  -5.099  1.00 45.57           C  
ATOM    836  CD2 PHE A 112       8.595  26.054  -5.627  1.00 51.97           C  
ATOM    837  CE1 PHE A 112       6.318  26.386  -4.112  1.00 50.49           C  
ATOM    838  CE2 PHE A 112       8.560  27.019  -4.643  1.00 44.47           C  
ATOM    839  CZ  PHE A 112       7.421  27.186  -3.884  1.00 58.54           C  
ATOM    840  N   GLY A 113       6.959  21.420  -5.507  1.00 37.02           N  
ATOM    841  CA  GLY A 113       6.435  20.705  -4.356  1.00 32.65           C  
ATOM    842  C   GLY A 113       7.459  19.778  -3.732  1.00 35.19           C  
ATOM    843  O   GLY A 113       7.519  19.637  -2.507  1.00 35.19           O  
ATOM    844  N   SER A 114       8.280  19.134  -4.563  1.00 40.69           N  
ATOM    845  CA  SER A 114       9.334  18.273  -4.038  1.00 32.23           C  
ATOM    846  C   SER A 114      10.388  19.086  -3.301  1.00 29.07           C  
ATOM    847  O   SER A 114      10.835  18.695  -2.217  1.00 34.98           O  
ATOM    848  CB  SER A 114       9.966  17.475  -5.174  1.00 29.38           C  
ATOM    849  OG  SER A 114      10.930  16.569  -4.678  1.00 46.82           O  
ATOM    850  N   ILE A 115      10.780  20.230  -3.864  1.00 28.57           N  
ATOM    851  CA  ILE A 115      11.790  21.072  -3.230  1.00 31.38           C  
ATOM    852  C   ILE A 115      11.283  21.605  -1.897  1.00 36.84           C  
ATOM    853  O   ILE A 115      12.006  21.597  -0.893  1.00 37.06           O  
ATOM    854  CB  ILE A 115      12.203  22.206  -4.185  1.00 34.15           C  
ATOM    855  CG1 ILE A 115      12.992  21.637  -5.366  1.00 31.25           C  
ATOM    856  CG2 ILE A 115      13.009  23.268  -3.456  1.00 31.18           C  
ATOM    857  CD1 ILE A 115      13.376  22.665  -6.395  1.00 33.51           C  
ATOM    858  N   ILE A 116      10.029  22.056  -1.854  1.00 41.24           N  
ATOM    859  CA  ILE A 116       9.524  22.652  -0.623  1.00 42.02           C  
ATOM    860  C   ILE A 116       9.319  21.591   0.456  1.00 40.05           C  
ATOM    861  O   ILE A 116       9.532  21.860   1.645  1.00 35.93           O  
ATOM    862  CB  ILE A 116       8.239  23.454  -0.906  1.00 42.35           C  
ATOM    863  CG1 ILE A 116       7.890  24.322   0.298  1.00 47.13           C  
ATOM    864  CG2 ILE A 116       7.078  22.541  -1.283  1.00 49.29           C  
ATOM    865  CD1 ILE A 116       8.956  25.337   0.619  1.00 49.14           C  
ATOM    866  N   LEU A 117       8.928  20.373   0.071  1.00 37.24           N  
ATOM    867  CA  LEU A 117       8.731  19.311   1.054  1.00 40.42           C  
ATOM    868  C   LEU A 117      10.049  18.912   1.708  1.00 40.30           C  
ATOM    869  O   LEU A 117      10.118  18.730   2.930  1.00 34.29           O  
ATOM    870  CB  LEU A 117       8.071  18.096   0.392  1.00 35.62           C  
ATOM    871  CG  LEU A 117       6.544  18.043   0.286  1.00 44.68           C  
ATOM    872  CD1 LEU A 117       6.110  16.919  -0.644  1.00 36.06           C  
ATOM    873  CD2 LEU A 117       5.911  17.869   1.661  1.00 39.32           C  
ATOM    874  N   ILE A 118      11.106  18.784   0.911  1.00 31.98           N  
ATOM    875  CA  ILE A 118      12.397  18.361   1.437  1.00 31.93           C  
ATOM    876  C   ILE A 118      13.051  19.475   2.251  1.00 30.74           C  
ATOM    877  O   ILE A 118      13.683  19.210   3.280  1.00 36.14           O  
ATOM    878  CB  ILE A 118      13.283  17.871   0.277  1.00 36.21           C  
ATOM    879  CG1 ILE A 118      12.820  16.477  -0.160  1.00 31.95           C  
ATOM    880  CG2 ILE A 118      14.755  17.866   0.659  1.00 32.00           C  
ATOM    881  CD1 ILE A 118      13.424  15.993  -1.446  1.00 33.30           C  
ATOM    882  N   ILE A 119      12.884  20.734   1.831  1.00 36.16           N  
ATOM    883  CA  ILE A 119      13.407  21.858   2.612  1.00 30.13           C  
ATOM    884  C   ILE A 119      12.851  21.821   4.033  1.00 32.60           C  
ATOM    885  O   ILE A 119      13.604  21.831   5.015  1.00 37.51           O  
ATOM    886  CB  ILE A 119      13.092  23.197   1.917  1.00 36.93           C  
ATOM    887  CG1 ILE A 119      14.011  23.414   0.709  1.00 34.66           C  
ATOM    888  CG2 ILE A 119      13.220  24.360   2.901  1.00 32.17           C  
ATOM    889  CD1 ILE A 119      13.581  24.562  -0.186  1.00 30.52           C  
ATOM    890  N   ILE A 120      11.524  21.752   4.161  1.00 35.80           N  
ATOM    891  CA  ILE A 120      10.890  21.730   5.477  1.00 38.13           C  
ATOM    892  C   ILE A 120      11.285  20.470   6.243  1.00 37.08           C  
ATOM    893  O   ILE A 120      11.716  20.539   7.401  1.00 40.36           O  
ATOM    894  CB  ILE A 120       9.362  21.859   5.328  1.00 36.67           C  
ATOM    895  CG1 ILE A 120       9.006  23.235   4.755  1.00 30.86           C  
ATOM    896  CG2 ILE A 120       8.656  21.617   6.659  1.00 29.51           C  
ATOM    897  CD1 ILE A 120       7.659  23.293   4.072  1.00 34.28           C  
ATOM    898  N   GLY A 121      11.164  19.303   5.601  1.00 33.79           N  
ATOM    899  CA  GLY A 121      11.430  18.052   6.298  1.00 35.54           C  
ATOM    900  C   GLY A 121      12.862  17.927   6.784  1.00 37.89           C  
ATOM    901  O   GLY A 121      13.110  17.514   7.921  1.00 34.86           O  
ATOM    902  N   THR A 122      13.825  18.273   5.929  1.00 36.05           N  
ATOM    903  CA  THR A 122      15.224  18.243   6.346  1.00 39.26           C  
ATOM    904  C   THR A 122      15.472  19.215   7.495  1.00 36.09           C  
ATOM    905  O   THR A 122      16.280  18.941   8.389  1.00 38.02           O  
ATOM    906  CB  THR A 122      16.134  18.560   5.156  1.00 37.78           C  
ATOM    907  OG1 THR A 122      15.844  17.651   4.086  1.00 43.97           O  
ATOM    908  CG2 THR A 122      17.594  18.415   5.536  1.00 41.55           C  
ATOM    909  N   GLY A 123      14.767  20.348   7.500  1.00 40.02           N  
ATOM    910  CA  GLY A 123      14.915  21.295   8.593  1.00 33.39           C  
ATOM    911  C   GLY A 123      14.476  20.721   9.927  1.00 37.53           C  
ATOM    912  O   GLY A 123      15.102  20.974  10.958  1.00 33.26           O  
ATOM    913  N   PHE A 124      13.395  19.936   9.923  1.00 34.74           N  
ATOM    914  CA  PHE A 124      12.955  19.278  11.150  1.00 40.63           C  
ATOM    915  C   PHE A 124      13.908  18.160  11.559  1.00 40.64           C  
ATOM    916  O   PHE A 124      14.239  18.021  12.742  1.00 37.84           O  
ATOM    917  CB  PHE A 124      11.536  18.727  10.974  1.00 38.88           C  
ATOM    918  CG  PHE A 124      10.453  19.764  11.102  1.00 47.36           C  
ATOM    919  CD1 PHE A 124      10.593  20.830  11.974  1.00 48.88           C  
ATOM    920  CD2 PHE A 124       9.290  19.667  10.351  1.00 52.96           C  
ATOM    921  CE1 PHE A 124       9.596  21.781  12.092  1.00 50.11           C  
ATOM    922  CE2 PHE A 124       8.290  20.617  10.467  1.00 49.34           C  
ATOM    923  CZ  PHE A 124       8.444  21.674  11.339  1.00 47.99           C  
ATOM    924  N   LEU A 125      14.365  17.357  10.597  1.00 34.53           N  
ATOM    925  CA  LEU A 125      15.093  16.136  10.929  1.00 32.40           C  
ATOM    926  C   LEU A 125      16.566  16.408  11.219  1.00 36.19           C  
ATOM    927  O   LEU A 125      17.099  15.947  12.234  1.00 35.15           O  
ATOM    928  CB  LEU A 125      14.943  15.118   9.792  1.00 26.65           C  
ATOM    929  CG  LEU A 125      15.517  13.702   9.926  1.00 27.00           C  
ATOM    930  CD1 LEU A 125      14.724  12.754   9.062  1.00 30.77           C  
ATOM    931  CD2 LEU A 125      16.988  13.632   9.533  1.00 30.79           C  
ATOM    932  N   LYS A 126      17.234  17.156  10.340  1.00 37.57           N  
ATOM    933  CA  LYS A 126      18.697  17.185  10.340  1.00 38.96           C  
ATOM    934  C   LYS A 126      19.303  17.731  11.629  1.00 35.37           C  
ATOM    935  O   LYS A 126      20.213  17.083  12.176  1.00 41.95           O  
ATOM    936  CB  LYS A 126      19.194  17.956   9.116  1.00 35.18           C  
ATOM    937  CG  LYS A 126      20.705  18.071   9.030  1.00 56.85           C  
ATOM    938  CD  LYS A 126      21.376  16.706   9.073  1.00 56.74           C  
ATOM    939  CE  LYS A 126      22.891  16.850   9.104  1.00 55.66           C  
ATOM    940  NZ  LYS A 126      23.581  15.600   9.516  1.00 67.44           N  
ATOM    941  N   PRO A 127      18.878  18.878  12.170  1.00 33.87           N  
ATOM    942  CA  PRO A 127      19.475  19.302  13.447  1.00 28.88           C  
ATOM    943  C   PRO A 127      19.115  18.388  14.605  1.00 35.60           C  
ATOM    944  O   PRO A 127      19.943  18.178  15.500  1.00 36.78           O  
ATOM    945  CB  PRO A 127      18.925  20.723  13.641  1.00 28.95           C  
ATOM    946  CG  PRO A 127      17.673  20.757  12.848  1.00 32.56           C  
ATOM    947  CD  PRO A 127      17.931  19.885  11.654  1.00 37.15           C  
ATOM    948  N   ASN A 128      17.910  17.815  14.608  1.00 34.77           N  
ATOM    949  CA  ASN A 128      17.445  17.081  15.778  1.00 36.12           C  
ATOM    950  C   ASN A 128      17.914  15.633  15.808  1.00 39.41           C  
ATOM    951  O   ASN A 128      17.890  15.015  16.878  1.00 36.50           O  
ATOM    952  CB  ASN A 128      15.921  17.134  15.863  1.00 32.22           C  
ATOM    953  CG  ASN A 128      15.402  18.548  16.003  1.00 34.52           C  
ATOM    954  OD1 ASN A 128      15.671  19.222  16.996  1.00 30.53           O  
ATOM    955  ND2 ASN A 128      14.652  19.007  15.003  1.00 29.93           N  
ATOM    956  N   VAL A 129      18.335  15.073  14.674  1.00 36.24           N  
ATOM    957  CA  VAL A 129      18.976  13.765  14.737  1.00 35.97           C  
ATOM    958  C   VAL A 129      20.341  13.889  15.406  1.00 38.67           C  
ATOM    959  O   VAL A 129      20.751  12.997  16.159  1.00 36.14           O  
ATOM    960  CB  VAL A 129      19.055  13.126  13.334  1.00 34.23           C  
ATOM    961  CG1 VAL A 129      19.944  13.942  12.403  1.00 45.58           C  
ATOM    962  CG2 VAL A 129      19.525  11.683  13.423  1.00 30.07           C  
ATOM    963  N   SER A 130      21.048  15.003  15.189  1.00 37.36           N  
ATOM    964  CA  SER A 130      22.300  15.226  15.908  1.00 37.90           C  
ATOM    965  C   SER A 130      22.041  15.466  17.389  1.00 45.84           C  
ATOM    966  O   SER A 130      22.823  15.033  18.244  1.00 47.07           O  
ATOM    967  CB  SER A 130      23.064  16.401  15.296  1.00 32.01           C  
ATOM    968  OG  SER A 130      23.392  16.154  13.937  1.00 61.75           O  
ATOM    969  N   THR A 131      20.941  16.153  17.707  1.00 42.60           N  
ATOM    970  CA  THR A 131      20.547  16.346  19.098  1.00 32.69           C  
ATOM    971  C   THR A 131      20.340  15.013  19.806  1.00 40.46           C  
ATOM    972  O   THR A 131      20.816  14.819  20.930  1.00 44.86           O  
ATOM    973  CB  THR A 131      19.276  17.195  19.161  1.00 32.92           C  
ATOM    974  OG1 THR A 131      19.577  18.542  18.777  1.00 35.35           O  
ATOM    975  CG2 THR A 131      18.681  17.189  20.555  1.00 28.56           C  
ATOM    976  N   LEU A 132      19.653  14.071  19.152  1.00 44.99           N  
ATOM    977  CA  LEU A 132      19.364  12.788  19.785  1.00 35.83           C  
ATOM    978  C   LEU A 132      20.627  11.983  20.045  1.00 37.20           C  
ATOM    979  O   LEU A 132      20.654  11.166  20.969  1.00 37.02           O  
ATOM    980  CB  LEU A 132      18.398  11.983  18.921  1.00 35.62           C  
ATOM    981  CG  LEU A 132      16.988  12.560  18.817  1.00 33.11           C  
ATOM    982  CD1 LEU A 132      16.157  11.783  17.810  1.00 35.99           C  
ATOM    983  CD2 LEU A 132      16.321  12.558  20.182  1.00 37.75           C  
ATOM    984  N   VAL A 133      21.672  12.184  19.239  1.00 39.01           N  
ATOM    985  CA  VAL A 133      22.938  11.504  19.496  1.00 38.35           C  
ATOM    986  C   VAL A 133      23.502  11.935  20.841  1.00 39.36           C  
ATOM    987  O   VAL A 133      24.013  11.112  21.611  1.00 41.66           O  
ATOM    988  CB  VAL A 133      23.936  11.768  18.353  1.00 36.08           C  
ATOM    989  CG1 VAL A 133      25.259  11.075  18.632  1.00 28.88           C  
ATOM    990  CG2 VAL A 133      23.353  11.304  17.030  1.00 36.80           C  
ATOM    991  N   GLY A 134      23.408  13.229  21.150  1.00 34.83           N  
ATOM    992  CA  GLY A 134      23.885  13.710  22.433  1.00 37.12           C  
ATOM    993  C   GLY A 134      23.128  13.122  23.606  1.00 39.59           C  
ATOM    994  O   GLY A 134      23.708  12.893  24.669  1.00 46.18           O  
ATOM    995  N   THR A 135      21.833  12.855  23.429  1.00 38.07           N  
ATOM    996  CA  THR A 135      21.027  12.282  24.499  1.00 44.87           C  
ATOM    997  C   THR A 135      21.434  10.856  24.851  1.00 46.66           C  
ATOM    998  O   THR A 135      20.999  10.347  25.889  1.00 46.15           O  
ATOM    999  CB  THR A 135      19.545  12.319  24.116  1.00 46.65           C  
ATOM   1000  OG1 THR A 135      19.258  11.284  23.165  1.00 45.59           O  
ATOM   1001  CG2 THR A 135      19.193  13.665  23.501  1.00 40.95           C  
ATOM   1002  N   LEU A 136      22.253  10.203  24.021  1.00 47.65           N  
ATOM   1003  CA  LEU A 136      22.749   8.874  24.363  1.00 45.97           C  
ATOM   1004  C   LEU A 136      23.799   8.951  25.463  1.00 51.18           C  
ATOM   1005  O   LEU A 136      23.867   8.072  26.330  1.00 50.58           O  
ATOM   1006  CB  LEU A 136      23.325   8.196  23.122  1.00 42.03           C  
ATOM   1007  CG  LEU A 136      22.391   8.129  21.917  1.00 41.32           C  
ATOM   1008  CD1 LEU A 136      23.161   7.690  20.685  1.00 38.58           C  
ATOM   1009  CD2 LEU A 136      21.234   7.188  22.200  1.00 40.22           C  
ATOM   1010  N   TYR A 137      24.625   9.993  25.437  1.00 52.13           N  
ATOM   1011  CA  TYR A 137      25.657  10.235  26.443  1.00 55.63           C  
ATOM   1012  C   TYR A 137      25.094  11.251  27.426  1.00 75.69           C  
ATOM   1013  O   TYR A 137      25.045  12.449  27.134  1.00 73.41           O  
ATOM   1014  CB  TYR A 137      26.940  10.729  25.786  1.00 54.83           C  
ATOM   1015  CG  TYR A 137      27.326   9.895  24.597  1.00 61.37           C  
ATOM   1016  CD1 TYR A 137      28.046   8.724  24.760  1.00 46.52           C  
ATOM   1017  CD2 TYR A 137      26.951  10.266  23.311  1.00 55.13           C  
ATOM   1018  CE1 TYR A 137      28.393   7.956  23.685  1.00 46.04           C  
ATOM   1019  CE2 TYR A 137      27.292   9.497  22.225  1.00 47.13           C  
ATOM   1020  CZ  TYR A 137      28.014   8.341  22.420  1.00 49.77           C  
ATOM   1021  OH  TYR A 137      28.366   7.556  21.351  1.00 51.55           O  
ATOM   1022  N   ASP A 138      24.677  10.763  28.596  1.00 72.72           N  
ATOM   1023  CA  ASP A 138      23.895  11.578  29.520  1.00 85.95           C  
ATOM   1024  C   ASP A 138      24.627  12.866  29.894  1.00 98.96           C  
ATOM   1025  O   ASP A 138      24.105  13.967  29.688  1.00113.26           O  
ATOM   1026  CB  ASP A 138      23.531  10.756  30.759  1.00 95.72           C  
ATOM   1027  CG  ASP A 138      22.168  10.077  30.631  1.00 87.00           C  
ATOM   1028  OD1 ASP A 138      21.141  10.759  30.833  1.00 79.85           O  
ATOM   1029  OD2 ASP A 138      22.122   8.868  30.316  1.00 82.65           O  
ATOM   1030  N   GLU A 139      25.846  12.755  30.423  1.00 92.19           N  
ATOM   1031  CA  GLU A 139      26.593  13.969  30.733  1.00 97.56           C  
ATOM   1032  C   GLU A 139      28.048  13.634  31.026  1.00 97.79           C  
ATOM   1033  O   GLU A 139      28.353  12.594  31.616  1.00102.12           O  
ATOM   1034  CB  GLU A 139      25.987  14.720  31.927  1.00102.29           C  
ATOM   1035  CG  GLU A 139      26.454  16.163  32.039  1.00104.47           C  
ATOM   1036  CD  GLU A 139      25.857  16.888  33.230  1.00103.24           C  
ATOM   1037  OE1 GLU A 139      24.882  16.371  33.815  1.00103.03           O  
ATOM   1038  OE2 GLU A 139      26.364  17.974  33.583  1.00112.06           O  
ATOM   1039  N   HIS A 140      28.933  14.547  30.618  1.00 90.43           N  
ATOM   1040  CA  HIS A 140      30.353  14.514  30.974  1.00 89.74           C  
ATOM   1041  C   HIS A 140      30.994  13.179  30.594  1.00 89.02           C  
ATOM   1042  O   HIS A 140      31.723  12.560  31.373  1.00 84.21           O  
ATOM   1043  CB  HIS A 140      30.547  14.815  32.463  1.00 96.84           C  
ATOM   1044  CG  HIS A 140      30.042  16.163  32.882  1.00104.94           C  
ATOM   1045  ND1 HIS A 140      30.332  17.317  32.185  1.00104.02           N  
ATOM   1046  CD2 HIS A 140      29.276  16.541  33.933  1.00101.36           C  
ATOM   1047  CE1 HIS A 140      29.762  18.347  32.786  1.00102.13           C  
ATOM   1048  NE2 HIS A 140      29.115  17.903  33.849  1.00101.78           N  
ATOM   1049  N   ASP A 141      30.714  12.734  29.372  1.00 86.67           N  
ATOM   1050  CA  ASP A 141      31.171  11.443  28.878  1.00 65.41           C  
ATOM   1051  C   ASP A 141      32.307  11.648  27.885  1.00 63.26           C  
ATOM   1052  O   ASP A 141      32.192  12.461  26.963  1.00 68.00           O  
ATOM   1053  CB  ASP A 141      30.016  10.676  28.225  1.00 61.30           C  
ATOM   1054  CG  ASP A 141      30.176   9.167  28.328  1.00 64.42           C  
ATOM   1055  OD1 ASP A 141      31.311   8.670  28.171  1.00 63.10           O  
ATOM   1056  OD2 ASP A 141      29.159   8.478  28.567  1.00 44.80           O  
ATOM   1057  N   ARG A 142      33.405  10.915  28.082  1.00 62.70           N  
ATOM   1058  CA  ARG A 142      34.490  10.939  27.106  1.00 68.81           C  
ATOM   1059  C   ARG A 142      34.058  10.327  25.777  1.00 63.32           C  
ATOM   1060  O   ARG A 142      34.570  10.715  24.720  1.00 61.55           O  
ATOM   1061  CB  ARG A 142      35.715  10.207  27.668  1.00 74.35           C  
ATOM   1062  CG  ARG A 142      36.888  10.088  26.701  1.00 83.88           C  
ATOM   1063  CD  ARG A 142      37.955   9.119  27.204  1.00 93.31           C  
ATOM   1064  NE  ARG A 142      38.220   8.048  26.242  1.00 97.79           N  
ATOM   1065  CZ  ARG A 142      39.057   8.152  25.214  1.00 89.94           C  
ATOM   1066  NH1 ARG A 142      39.714   9.283  25.003  1.00 83.28           N  
ATOM   1067  NH2 ARG A 142      39.234   7.125  24.391  1.00 92.04           N  
ATOM   1068  N   ARG A 143      33.101   9.392  25.807  1.00 55.68           N  
ATOM   1069  CA  ARG A 143      32.671   8.709  24.590  1.00 60.42           C  
ATOM   1070  C   ARG A 143      32.014   9.644  23.584  1.00 61.93           C  
ATOM   1071  O   ARG A 143      31.911   9.283  22.407  1.00 61.86           O  
ATOM   1072  CB  ARG A 143      31.694   7.582  24.926  1.00 53.47           C  
ATOM   1073  CG  ARG A 143      32.306   6.390  25.623  1.00 43.26           C  
ATOM   1074  CD  ARG A 143      31.341   5.846  26.654  1.00 51.24           C  
ATOM   1075  NE  ARG A 143      30.482   4.788  26.137  1.00 39.71           N  
ATOM   1076  CZ  ARG A 143      29.281   4.504  26.631  1.00 46.87           C  
ATOM   1077  NH1 ARG A 143      28.793   5.220  27.635  1.00 34.75           N  
ATOM   1078  NH2 ARG A 143      28.562   3.515  26.117  1.00 54.64           N  
ATOM   1079  N   ARG A 144      31.576  10.829  24.017  1.00 59.74           N  
ATOM   1080  CA  ARG A 144      30.784  11.709  23.161  1.00 55.44           C  
ATOM   1081  C   ARG A 144      31.487  11.998  21.837  1.00 57.34           C  
ATOM   1082  O   ARG A 144      30.883  11.890  20.763  1.00 56.35           O  
ATOM   1083  CB  ARG A 144      30.481  13.012  23.902  1.00 57.44           C  
ATOM   1084  CG  ARG A 144      29.344  13.820  23.304  1.00 66.71           C  
ATOM   1085  CD  ARG A 144      29.291  15.219  23.903  1.00 69.94           C  
ATOM   1086  NE  ARG A 144      27.981  15.840  23.723  1.00 69.52           N  
ATOM   1087  CZ  ARG A 144      26.954  15.656  24.547  1.00 70.42           C  
ATOM   1088  NH1 ARG A 144      27.088  14.868  25.606  1.00 59.40           N  
ATOM   1089  NH2 ARG A 144      25.792  16.254  24.315  1.00 73.35           N  
ATOM   1090  N   ASP A 145      32.769  12.367  21.896  1.00 62.06           N  
ATOM   1091  CA  ASP A 145      33.499  12.693  20.673  1.00 63.83           C  
ATOM   1092  C   ASP A 145      33.574  11.494  19.733  1.00 58.04           C  
ATOM   1093  O   ASP A 145      33.419  11.642  18.515  1.00 55.71           O  
ATOM   1094  CB  ASP A 145      34.901  13.207  21.016  1.00 65.76           C  
ATOM   1095  CG  ASP A 145      34.949  14.721  21.188  1.00 69.54           C  
ATOM   1096  OD1 ASP A 145      34.038  15.286  21.831  1.00 70.07           O  
ATOM   1097  OD2 ASP A 145      35.911  15.345  20.689  1.00 85.54           O  
ATOM   1098  N   ALA A 146      33.794  10.296  20.279  1.00 56.51           N  
ATOM   1099  CA  ALA A 146      33.848   9.105  19.436  1.00 51.73           C  
ATOM   1100  C   ALA A 146      32.495   8.826  18.793  1.00 48.19           C  
ATOM   1101  O   ALA A 146      32.410   8.576  17.585  1.00 46.13           O  
ATOM   1102  CB  ALA A 146      34.317   7.902  20.253  1.00 40.73           C  
ATOM   1103  N   GLY A 147      31.421   8.888  19.585  1.00 39.34           N  
ATOM   1104  CA  GLY A 147      30.103   8.562  19.068  1.00 40.03           C  
ATOM   1105  C   GLY A 147      29.642   9.481  17.957  1.00 45.92           C  
ATOM   1106  O   GLY A 147      28.930   9.050  17.044  1.00 38.49           O  
ATOM   1107  N   PHE A 148      30.031  10.757  18.015  1.00 47.34           N  
ATOM   1108  CA  PHE A 148      29.718  11.661  16.916  1.00 37.47           C  
ATOM   1109  C   PHE A 148      30.545  11.341  15.677  1.00 41.64           C  
ATOM   1110  O   PHE A 148      30.085  11.573  14.554  1.00 45.96           O  
ATOM   1111  CB  PHE A 148      29.925  13.110  17.350  1.00 46.52           C  
ATOM   1112  CG  PHE A 148      28.742  13.698  18.064  1.00 44.45           C  
ATOM   1113  CD1 PHE A 148      27.724  14.315  17.352  1.00 55.93           C  
ATOM   1114  CD2 PHE A 148      28.641  13.627  19.442  1.00 43.78           C  
ATOM   1115  CE1 PHE A 148      26.629  14.856  18.004  1.00 61.48           C  
ATOM   1116  CE2 PHE A 148      27.549  14.166  20.102  1.00 51.52           C  
ATOM   1117  CZ  PHE A 148      26.542  14.782  19.382  1.00 49.68           C  
ATOM   1118  N   SER A 149      31.757  10.805  15.854  1.00 41.07           N  
ATOM   1119  CA  SER A 149      32.533  10.362  14.700  1.00 38.57           C  
ATOM   1120  C   SER A 149      31.874   9.167  14.028  1.00 39.55           C  
ATOM   1121  O   SER A 149      31.841   9.080  12.795  1.00 46.80           O  
ATOM   1122  CB  SER A 149      33.959  10.013  15.122  1.00 35.09           C  
ATOM   1123  OG  SER A 149      34.468  10.971  16.029  1.00 46.05           O  
ATOM   1124  N   ILE A 150      31.353   8.230  14.824  1.00 34.76           N  
ATOM   1125  CA  ILE A 150      30.593   7.116  14.267  1.00 36.98           C  
ATOM   1126  C   ILE A 150      29.373   7.642  13.522  1.00 38.40           C  
ATOM   1127  O   ILE A 150      29.102   7.252  12.380  1.00 36.77           O  
ATOM   1128  CB  ILE A 150      30.195   6.131  15.383  1.00 39.76           C  
ATOM   1129  CG1 ILE A 150      31.373   5.860  16.326  1.00 40.10           C  
ATOM   1130  CG2 ILE A 150      29.657   4.834  14.790  1.00 41.74           C  
ATOM   1131  CD1 ILE A 150      32.339   4.809  15.843  1.00 38.12           C  
ATOM   1132  N   PHE A 151      28.634   8.555  14.156  1.00 36.05           N  
ATOM   1133  CA  PHE A 151      27.437   9.128  13.546  1.00 36.48           C  
ATOM   1134  C   PHE A 151      27.764   9.800  12.218  1.00 37.89           C  
ATOM   1135  O   PHE A 151      27.088   9.570  11.209  1.00 36.95           O  
ATOM   1136  CB  PHE A 151      26.791  10.118  14.520  1.00 42.80           C  
ATOM   1137  CG  PHE A 151      25.530  10.757  14.007  1.00 42.95           C  
ATOM   1138  CD1 PHE A 151      24.357  10.025  13.909  1.00 37.12           C  
ATOM   1139  CD2 PHE A 151      25.510  12.098  13.655  1.00 36.45           C  
ATOM   1140  CE1 PHE A 151      23.191  10.616  13.452  1.00 34.01           C  
ATOM   1141  CE2 PHE A 151      24.349  12.695  13.199  1.00 35.69           C  
ATOM   1142  CZ  PHE A 151      23.187  11.953  13.097  1.00 33.83           C  
ATOM   1143  N   VAL A 152      28.812  10.626  12.198  1.00 32.59           N  
ATOM   1144  CA  VAL A 152      29.231  11.274  10.959  1.00 37.41           C  
ATOM   1145  C   VAL A 152      29.686  10.246   9.934  1.00 35.39           C  
ATOM   1146  O   VAL A 152      29.493  10.436   8.727  1.00 29.12           O  
ATOM   1147  CB  VAL A 152      30.325  12.317  11.257  1.00 40.93           C  
ATOM   1148  CG1 VAL A 152      30.989  12.803   9.978  1.00 35.51           C  
ATOM   1149  CG2 VAL A 152      29.729  13.493  12.015  1.00 31.71           C  
ATOM   1150  N   PHE A 153      30.272   9.134  10.384  1.00 41.93           N  
ATOM   1151  CA  PHE A 153      30.693   8.112   9.431  1.00 37.90           C  
ATOM   1152  C   PHE A 153      29.495   7.519   8.701  1.00 36.88           C  
ATOM   1153  O   PHE A 153      29.558   7.278   7.490  1.00 37.29           O  
ATOM   1154  CB  PHE A 153      31.501   7.022  10.133  1.00 33.51           C  
ATOM   1155  CG  PHE A 153      31.933   5.913   9.216  1.00 38.08           C  
ATOM   1156  CD1 PHE A 153      32.662   6.189   8.071  1.00 37.27           C  
ATOM   1157  CD2 PHE A 153      31.604   4.597   9.495  1.00 47.32           C  
ATOM   1158  CE1 PHE A 153      33.055   5.171   7.220  1.00 49.71           C  
ATOM   1159  CE2 PHE A 153      31.995   3.575   8.651  1.00 40.22           C  
ATOM   1160  CZ  PHE A 153      32.721   3.862   7.513  1.00 44.80           C  
ATOM   1161  N   GLY A 154      28.388   7.296   9.413  1.00 34.02           N  
ATOM   1162  CA  GLY A 154      27.159   6.884   8.753  1.00 28.88           C  
ATOM   1163  C   GLY A 154      26.582   7.952   7.846  1.00 30.68           C  
ATOM   1164  O   GLY A 154      25.889   7.638   6.874  1.00 33.32           O  
ATOM   1165  N   ILE A 155      26.851   9.224   8.150  1.00 30.78           N  
ATOM   1166  CA  ILE A 155      26.436  10.315   7.270  1.00 27.74           C  
ATOM   1167  C   ILE A 155      27.167  10.213   5.938  1.00 30.13           C  
ATOM   1168  O   ILE A 155      26.551  10.177   4.867  1.00 33.20           O  
ATOM   1169  CB  ILE A 155      26.689  11.676   7.944  1.00 33.78           C  
ATOM   1170  CG1 ILE A 155      25.823  11.825   9.194  1.00 31.08           C  
ATOM   1171  CG2 ILE A 155      26.456  12.821   6.968  1.00 24.02           C  
ATOM   1172  CD1 ILE A 155      25.820  13.215   9.776  1.00 35.39           C  
ATOM   1173  N   ASN A 156      28.500  10.160   5.995  1.00 27.66           N  
ATOM   1174  CA  ASN A 156      29.300  10.096   4.776  1.00 31.53           C  
ATOM   1175  C   ASN A 156      29.049   8.802   4.016  1.00 33.57           C  
ATOM   1176  O   ASN A 156      29.042   8.789   2.779  1.00 35.43           O  
ATOM   1177  CB  ASN A 156      30.782  10.233   5.121  1.00 32.28           C  
ATOM   1178  CG  ASN A 156      31.065  11.424   6.009  1.00 37.17           C  
ATOM   1179  OD1 ASN A 156      30.479  12.493   5.841  1.00 42.32           O  
ATOM   1180  ND2 ASN A 156      31.967  11.245   6.968  1.00 49.51           N  
ATOM   1181  N   LEU A 157      28.844   7.701   4.741  1.00 30.14           N  
ATOM   1182  CA  LEU A 157      28.602   6.415   4.095  1.00 29.33           C  
ATOM   1183  C   LEU A 157      27.344   6.456   3.234  1.00 32.89           C  
ATOM   1184  O   LEU A 157      27.348   5.982   2.091  1.00 30.38           O  
ATOM   1185  CB  LEU A 157      28.503   5.324   5.157  1.00 26.88           C  
ATOM   1186  CG  LEU A 157      28.766   3.882   4.744  1.00 42.12           C  
ATOM   1187  CD1 LEU A 157      30.094   3.767   4.013  1.00 36.50           C  
ATOM   1188  CD2 LEU A 157      28.759   3.016   5.986  1.00 46.74           C  
ATOM   1189  N   GLY A 158      26.264   7.040   3.758  1.00 28.06           N  
ATOM   1190  CA  GLY A 158      25.048   7.172   2.976  1.00 24.06           C  
ATOM   1191  C   GLY A 158      25.190   8.129   1.812  1.00 32.48           C  
ATOM   1192  O   GLY A 158      24.589   7.915   0.757  1.00 31.11           O  
ATOM   1193  N   ALA A 159      25.983   9.191   1.982  1.00 31.86           N  
ATOM   1194  CA  ALA A 159      26.257  10.091   0.868  1.00 26.25           C  
ATOM   1195  C   ALA A 159      27.138   9.433  -0.184  1.00 31.24           C  
ATOM   1196  O   ALA A 159      27.130   9.852  -1.346  1.00 37.06           O  
ATOM   1197  CB  ALA A 159      26.919  11.368   1.378  1.00 28.95           C  
ATOM   1198  N   PHE A 160      27.900   8.408   0.199  1.00 29.61           N  
ATOM   1199  CA  PHE A 160      28.839   7.790  -0.731  1.00 32.69           C  
ATOM   1200  C   PHE A 160      28.147   6.786  -1.643  1.00 33.11           C  
ATOM   1201  O   PHE A 160      28.372   6.784  -2.858  1.00 32.59           O  
ATOM   1202  CB  PHE A 160      29.980   7.129   0.051  1.00 39.92           C  
ATOM   1203  CG  PHE A 160      30.746   6.098  -0.732  1.00 37.09           C  
ATOM   1204  CD1 PHE A 160      31.668   6.476  -1.698  1.00 32.21           C  
ATOM   1205  CD2 PHE A 160      30.552   4.745  -0.488  1.00 34.63           C  
ATOM   1206  CE1 PHE A 160      32.376   5.523  -2.414  1.00 32.43           C  
ATOM   1207  CE2 PHE A 160      31.256   3.788  -1.199  1.00 28.28           C  
ATOM   1208  CZ  PHE A 160      32.168   4.176  -2.162  1.00 31.55           C  
ATOM   1209  N   ILE A 161      27.291   5.934  -1.078  1.00 27.10           N  
ATOM   1210  CA  ILE A 161      26.648   4.900  -1.882  1.00 32.31           C  
ATOM   1211  C   ILE A 161      25.465   5.425  -2.687  1.00 33.47           C  
ATOM   1212  O   ILE A 161      25.069   4.790  -3.674  1.00 30.97           O  
ATOM   1213  CB  ILE A 161      26.181   3.732  -0.999  1.00 27.87           C  
ATOM   1214  CG1 ILE A 161      25.145   4.224   0.013  1.00 28.44           C  
ATOM   1215  CG2 ILE A 161      27.369   3.085  -0.297  1.00 24.50           C  
ATOM   1216  CD1 ILE A 161      24.352   3.117   0.659  1.00 23.81           C  
ATOM   1217  N   ALA A 162      24.894   6.566  -2.302  1.00 31.39           N  
ATOM   1218  CA  ALA A 162      23.661   7.024  -2.941  1.00 25.13           C  
ATOM   1219  C   ALA A 162      23.842   7.371  -4.414  1.00 29.36           C  
ATOM   1220  O   ALA A 162      23.040   6.891  -5.233  1.00 30.97           O  
ATOM   1221  CB  ALA A 162      23.071   8.198  -2.152  1.00 25.39           C  
ATOM   1222  N   PRO A 163      24.828   8.179  -4.830  1.00 31.68           N  
ATOM   1223  CA  PRO A 163      24.992   8.400  -6.276  1.00 30.51           C  
ATOM   1224  C   PRO A 163      25.323   7.130  -7.039  1.00 29.21           C  
ATOM   1225  O   PRO A 163      24.939   7.002  -8.207  1.00 29.26           O  
ATOM   1226  CB  PRO A 163      26.136   9.423  -6.355  1.00 29.91           C  
ATOM   1227  CG  PRO A 163      26.149  10.079  -5.026  1.00 27.66           C  
ATOM   1228  CD  PRO A 163      25.774   9.002  -4.057  1.00 27.10           C  
ATOM   1229  N   LEU A 164      26.020   6.181  -6.414  1.00 32.10           N  
ATOM   1230  CA  LEU A 164      26.283   4.907  -7.072  1.00 29.09           C  
ATOM   1231  C   LEU A 164      24.979   4.175  -7.364  1.00 29.06           C  
ATOM   1232  O   LEU A 164      24.660   3.882  -8.521  1.00 34.22           O  
ATOM   1233  CB  LEU A 164      27.208   4.052  -6.202  1.00 28.06           C  
ATOM   1234  CG  LEU A 164      28.521   4.711  -5.765  1.00 35.49           C  
ATOM   1235  CD1 LEU A 164      29.333   3.792  -4.857  1.00 25.64           C  
ATOM   1236  CD2 LEU A 164      29.342   5.131  -6.975  1.00 34.56           C  
ATOM   1237  N   ILE A 165      24.197   3.897  -6.319  1.00 32.33           N  
ATOM   1238  CA  ILE A 165      22.979   3.107  -6.479  1.00 26.73           C  
ATOM   1239  C   ILE A 165      21.925   3.890  -7.255  1.00 32.76           C  
ATOM   1240  O   ILE A 165      21.355   3.393  -8.233  1.00 32.54           O  
ATOM   1241  CB  ILE A 165      22.459   2.654  -5.103  1.00 24.11           C  
ATOM   1242  CG1 ILE A 165      23.464   1.698  -4.453  1.00 25.10           C  
ATOM   1243  CG2 ILE A 165      21.095   1.996  -5.231  1.00 32.10           C  
ATOM   1244  CD1 ILE A 165      23.090   1.262  -3.049  1.00 21.66           C  
ATOM   1245  N   VAL A 166      21.652   5.127  -6.838  1.00 29.73           N  
ATOM   1246  CA  VAL A 166      20.591   5.896  -7.480  1.00 25.35           C  
ATOM   1247  C   VAL A 166      20.993   6.292  -8.896  1.00 32.47           C  
ATOM   1248  O   VAL A 166      20.172   6.254  -9.821  1.00 35.78           O  
ATOM   1249  CB  VAL A 166      20.224   7.117  -6.619  1.00 24.16           C  
ATOM   1250  CG1 VAL A 166      19.127   7.933  -7.285  1.00 23.97           C  
ATOM   1251  CG2 VAL A 166      19.783   6.658  -5.234  1.00 31.41           C  
ATOM   1252  N   GLY A 167      22.261   6.653  -9.097  1.00 28.49           N  
ATOM   1253  CA  GLY A 167      22.709   7.035 -10.428  1.00 27.66           C  
ATOM   1254  C   GLY A 167      22.671   5.882 -11.414  1.00 34.39           C  
ATOM   1255  O   GLY A 167      22.269   6.053 -12.569  1.00 32.61           O  
ATOM   1256  N   ALA A 168      23.092   4.693 -10.978  1.00 28.66           N  
ATOM   1257  CA  ALA A 168      23.002   3.526 -11.846  1.00 36.33           C  
ATOM   1258  C   ALA A 168      21.549   3.165 -12.127  1.00 42.69           C  
ATOM   1259  O   ALA A 168      21.211   2.750 -13.242  1.00 40.30           O  
ATOM   1260  CB  ALA A 168      23.745   2.345 -11.222  1.00 28.89           C  
ATOM   1261  N   ALA A 169      20.673   3.329 -11.133  1.00 39.75           N  
ATOM   1262  CA  ALA A 169      19.257   3.045 -11.344  1.00 36.41           C  
ATOM   1263  C   ALA A 169      18.638   4.019 -12.336  1.00 41.78           C  
ATOM   1264  O   ALA A 169      17.795   3.628 -13.151  1.00 39.20           O  
ATOM   1265  CB  ALA A 169      18.507   3.088 -10.016  1.00 32.13           C  
ATOM   1266  N   GLN A 170      19.032   5.296 -12.273  1.00 39.75           N  
ATOM   1267  CA  GLN A 170      18.605   6.248 -13.294  1.00 38.09           C  
ATOM   1268  C   GLN A 170      19.087   5.816 -14.670  1.00 43.75           C  
ATOM   1269  O   GLN A 170      18.407   6.043 -15.676  1.00 43.00           O  
ATOM   1270  CB  GLN A 170      19.124   7.649 -12.964  1.00 37.03           C  
ATOM   1271  CG  GLN A 170      18.567   8.766 -13.849  1.00 42.92           C  
ATOM   1272  CD  GLN A 170      19.149   8.787 -15.256  1.00 43.62           C  
ATOM   1273  OE1 GLN A 170      20.330   8.505 -15.458  1.00 51.21           O  
ATOM   1274  NE2 GLN A 170      18.309   9.092 -16.239  1.00 39.55           N  
ATOM   1275  N   GLU A 171      20.273   5.217 -14.740  1.00 45.41           N  
ATOM   1276  CA  GLU A 171      20.761   4.733 -16.022  1.00 46.50           C  
ATOM   1277  C   GLU A 171      19.972   3.512 -16.475  1.00 48.04           C  
ATOM   1278  O   GLU A 171      19.617   3.393 -17.653  1.00 44.41           O  
ATOM   1279  CB  GLU A 171      22.249   4.408 -15.921  1.00 52.11           C  
ATOM   1280  CG  GLU A 171      22.996   4.574 -17.221  1.00 55.23           C  
ATOM   1281  CD  GLU A 171      24.195   3.663 -17.309  1.00 57.65           C  
ATOM   1282  OE1 GLU A 171      24.405   2.869 -16.369  1.00 64.58           O  
ATOM   1283  OE2 GLU A 171      24.924   3.734 -18.318  1.00 79.55           O  
ATOM   1284  N   ALA A 172      19.675   2.607 -15.543  1.00 48.58           N  
ATOM   1285  CA  ALA A 172      18.953   1.383 -15.870  1.00 41.52           C  
ATOM   1286  C   ALA A 172      17.498   1.678 -16.222  1.00 49.28           C  
ATOM   1287  O   ALA A 172      17.072   1.495 -17.368  1.00 49.82           O  
ATOM   1288  CB  ALA A 172      19.049   0.406 -14.696  1.00 37.69           C  
ATOM   1289  N   ALA A 173      16.718   2.131 -15.245  1.00 44.85           N  
ATOM   1290  CA  ALA A 173      15.326   2.498 -15.451  1.00 43.76           C  
ATOM   1291  C   ALA A 173      15.218   4.022 -15.545  1.00 53.86           C  
ATOM   1292  O   ALA A 173      16.218   4.722 -15.711  1.00 49.89           O  
ATOM   1293  CB  ALA A 173      14.463   1.909 -14.335  1.00 37.63           C  
ATOM   1294  N   GLY A 174      14.006   4.554 -15.445  1.00 39.94           N  
ATOM   1295  CA  GLY A 174      13.803   5.975 -15.648  1.00 54.80           C  
ATOM   1296  C   GLY A 174      14.434   6.848 -14.568  1.00 45.42           C  
ATOM   1297  O   GLY A 174      15.014   6.382 -13.586  1.00 41.61           O  
ATOM   1298  N   TYR A 175      14.331   8.165 -14.785  1.00 40.77           N  
ATOM   1299  CA  TYR A 175      14.549   9.116 -13.696  1.00 32.51           C  
ATOM   1300  C   TYR A 175      13.564   8.868 -12.561  1.00 36.61           C  
ATOM   1301  O   TYR A 175      13.923   8.959 -11.381  1.00 36.23           O  
ATOM   1302  CB  TYR A 175      14.406  10.557 -14.201  1.00 36.16           C  
ATOM   1303  CG  TYR A 175      15.643  11.154 -14.842  1.00 39.51           C  
ATOM   1304  CD1 TYR A 175      16.714  11.585 -14.066  1.00 40.48           C  
ATOM   1305  CD2 TYR A 175      15.729  11.310 -16.221  1.00 42.26           C  
ATOM   1306  CE1 TYR A 175      17.846  12.131 -14.648  1.00 40.61           C  
ATOM   1307  CE2 TYR A 175      16.853  11.859 -16.810  1.00 39.78           C  
ATOM   1308  CZ  TYR A 175      17.907  12.266 -16.020  1.00 34.12           C  
ATOM   1309  OH  TYR A 175      19.028  12.809 -16.603  1.00 41.32           O  
ATOM   1310  N   HIS A 176      12.310   8.556 -12.902  1.00 35.10           N  
ATOM   1311  CA  HIS A 176      11.280   8.375 -11.884  1.00 38.70           C  
ATOM   1312  C   HIS A 176      11.561   7.155 -11.020  1.00 38.90           C  
ATOM   1313  O   HIS A 176      11.304   7.169  -9.811  1.00 38.05           O  
ATOM   1314  CB  HIS A 176       9.907   8.250 -12.542  1.00 42.36           C  
ATOM   1315  CG  HIS A 176       9.401   9.526 -13.134  1.00 38.56           C  
ATOM   1316  ND1 HIS A 176       9.863  10.764 -12.742  1.00 56.41           N  
ATOM   1317  CD2 HIS A 176       8.467   9.756 -14.085  1.00 41.43           C  
ATOM   1318  CE1 HIS A 176       9.236  11.702 -13.428  1.00 51.82           C  
ATOM   1319  NE2 HIS A 176       8.384  11.117 -14.250  1.00 45.94           N  
ATOM   1320  N   VAL A 177      12.083   6.086 -11.621  1.00 33.35           N  
ATOM   1321  CA  VAL A 177      12.466   4.919 -10.837  1.00 29.78           C  
ATOM   1322  C   VAL A 177      13.622   5.262  -9.905  1.00 38.16           C  
ATOM   1323  O   VAL A 177      13.672   4.799  -8.758  1.00 38.69           O  
ATOM   1324  CB  VAL A 177      12.808   3.746 -11.770  1.00 35.26           C  
ATOM   1325  CG1 VAL A 177      13.079   2.490 -10.971  1.00 31.18           C  
ATOM   1326  CG2 VAL A 177      11.674   3.524 -12.764  1.00 48.59           C  
ATOM   1327  N   ALA A 178      14.556   6.095 -10.368  1.00 35.86           N  
ATOM   1328  CA  ALA A 178      15.669   6.487  -9.512  1.00 30.04           C  
ATOM   1329  C   ALA A 178      15.190   7.316  -8.327  1.00 37.14           C  
ATOM   1330  O   ALA A 178      15.664   7.129  -7.199  1.00 35.60           O  
ATOM   1331  CB  ALA A 178      16.711   7.255 -10.321  1.00 32.17           C  
ATOM   1332  N   PHE A 179      14.250   8.238  -8.559  1.00 27.65           N  
ATOM   1333  CA  PHE A 179      13.746   9.057  -7.461  1.00 31.04           C  
ATOM   1334  C   PHE A 179      12.956   8.231  -6.454  1.00 32.54           C  
ATOM   1335  O   PHE A 179      12.958   8.548  -5.259  1.00 28.36           O  
ATOM   1336  CB  PHE A 179      12.890  10.205  -7.997  1.00 37.06           C  
ATOM   1337  CG  PHE A 179      13.688  11.324  -8.605  1.00 33.53           C  
ATOM   1338  CD1 PHE A 179      14.609  12.027  -7.845  1.00 32.50           C  
ATOM   1339  CD2 PHE A 179      13.509  11.680  -9.931  1.00 33.63           C  
ATOM   1340  CE1 PHE A 179      15.343  13.054  -8.399  1.00 33.00           C  
ATOM   1341  CE2 PHE A 179      14.238  12.709 -10.491  1.00 29.35           C  
ATOM   1342  CZ  PHE A 179      15.157  13.397  -9.725  1.00 32.67           C  
ATOM   1343  N   SER A 180      12.279   7.174  -6.908  1.00 36.01           N  
ATOM   1344  CA  SER A 180      11.606   6.281  -5.971  1.00 34.58           C  
ATOM   1345  C   SER A 180      12.605   5.551  -5.086  1.00 33.51           C  
ATOM   1346  O   SER A 180      12.310   5.279  -3.917  1.00 36.95           O  
ATOM   1347  CB  SER A 180      10.732   5.283  -6.728  1.00 28.42           C  
ATOM   1348  OG  SER A 180      11.502   4.511  -7.628  1.00 43.39           O  
ATOM   1349  N   LEU A 181      13.791   5.242  -5.614  1.00 37.43           N  
ATOM   1350  CA  LEU A 181      14.819   4.618  -4.789  1.00 31.27           C  
ATOM   1351  C   LEU A 181      15.248   5.541  -3.661  1.00 34.54           C  
ATOM   1352  O   LEU A 181      15.477   5.089  -2.532  1.00 31.87           O  
ATOM   1353  CB  LEU A 181      16.027   4.230  -5.639  1.00 29.34           C  
ATOM   1354  CG  LEU A 181      15.859   3.119  -6.673  1.00 39.97           C  
ATOM   1355  CD1 LEU A 181      17.182   2.406  -6.871  1.00 38.59           C  
ATOM   1356  CD2 LEU A 181      14.775   2.135  -6.263  1.00 41.14           C  
ATOM   1357  N   ALA A 182      15.381   6.837  -3.950  1.00 31.14           N  
ATOM   1358  CA  ALA A 182      15.674   7.791  -2.888  1.00 31.14           C  
ATOM   1359  C   ALA A 182      14.556   7.805  -1.856  1.00 31.63           C  
ATOM   1360  O   ALA A 182      14.816   7.818  -0.648  1.00 30.94           O  
ATOM   1361  CB  ALA A 182      15.894   9.187  -3.472  1.00 25.73           C  
ATOM   1362  N   ALA A 183      13.303   7.777  -2.315  1.00 30.34           N  
ATOM   1363  CA  ALA A 183      12.180   7.743  -1.385  1.00 33.65           C  
ATOM   1364  C   ALA A 183      12.226   6.495  -0.512  1.00 27.76           C  
ATOM   1365  O   ALA A 183      11.895   6.548   0.678  1.00 26.41           O  
ATOM   1366  CB  ALA A 183      10.861   7.815  -2.152  1.00 29.50           C  
ATOM   1367  N   ILE A 184      12.646   5.367  -1.085  1.00 27.05           N  
ATOM   1368  CA  ILE A 184      12.688   4.112  -0.340  1.00 29.46           C  
ATOM   1369  C   ILE A 184      13.772   4.155   0.733  1.00 26.53           C  
ATOM   1370  O   ILE A 184      13.592   3.631   1.840  1.00 29.15           O  
ATOM   1371  CB  ILE A 184      12.883   2.934  -1.314  1.00 33.34           C  
ATOM   1372  CG1 ILE A 184      11.619   2.718  -2.151  1.00 35.33           C  
ATOM   1373  CG2 ILE A 184      13.247   1.669  -0.573  1.00 22.26           C  
ATOM   1374  CD1 ILE A 184      11.724   1.568  -3.143  1.00 33.18           C  
ATOM   1375  N   GLY A 185      14.911   4.779   0.427  1.00 23.90           N  
ATOM   1376  CA  GLY A 185      15.950   4.926   1.433  1.00 29.31           C  
ATOM   1377  C   GLY A 185      15.461   5.666   2.662  1.00 31.29           C  
ATOM   1378  O   GLY A 185      15.702   5.245   3.796  1.00 32.80           O  
ATOM   1379  N   MET A 186      14.756   6.781   2.451  1.00 29.75           N  
ATOM   1380  CA  MET A 186      14.177   7.512   3.573  1.00 28.56           C  
ATOM   1381  C   MET A 186      13.171   6.648   4.327  1.00 36.18           C  
ATOM   1382  O   MET A 186      13.105   6.689   5.562  1.00 26.96           O  
ATOM   1383  CB  MET A 186      13.524   8.800   3.071  1.00 26.81           C  
ATOM   1384  CG  MET A 186      12.804   9.576   4.150  1.00 32.29           C  
ATOM   1385  SD  MET A 186      13.844   9.839   5.593  1.00 38.52           S  
ATOM   1386  CE  MET A 186      14.948  11.049   4.924  1.00 32.61           C  
ATOM   1387  N   PHE A 187      12.393   5.844   3.595  1.00 35.66           N  
ATOM   1388  CA  PHE A 187      11.464   4.911   4.226  1.00 31.56           C  
ATOM   1389  C   PHE A 187      12.205   3.913   5.113  1.00 36.70           C  
ATOM   1390  O   PHE A 187      11.801   3.661   6.255  1.00 35.98           O  
ATOM   1391  CB  PHE A 187      10.647   4.190   3.150  1.00 31.21           C  
ATOM   1392  CG  PHE A 187       9.619   3.246   3.700  1.00 33.46           C  
ATOM   1393  CD1 PHE A 187       8.535   3.725   4.414  1.00 30.69           C  
ATOM   1394  CD2 PHE A 187       9.726   1.882   3.489  1.00 34.03           C  
ATOM   1395  CE1 PHE A 187       7.586   2.860   4.917  1.00 44.12           C  
ATOM   1396  CE2 PHE A 187       8.778   1.012   3.990  1.00 32.12           C  
ATOM   1397  CZ  PHE A 187       7.706   1.503   4.705  1.00 34.21           C  
ATOM   1398  N   ILE A 188      13.299   3.337   4.602  1.00 26.49           N  
ATOM   1399  CA  ILE A 188      14.109   2.427   5.409  1.00 24.39           C  
ATOM   1400  C   ILE A 188      14.593   3.125   6.673  1.00 32.20           C  
ATOM   1401  O   ILE A 188      14.540   2.559   7.772  1.00 29.23           O  
ATOM   1402  CB  ILE A 188      15.284   1.878   4.578  1.00 33.90           C  
ATOM   1403  CG1 ILE A 188      14.771   1.001   3.434  1.00 36.53           C  
ATOM   1404  CG2 ILE A 188      16.256   1.110   5.467  1.00 35.67           C  
ATOM   1405  CD1 ILE A 188      15.866   0.440   2.545  1.00 34.02           C  
ATOM   1406  N   GLY A 189      15.063   4.367   6.538  1.00 31.01           N  
ATOM   1407  CA  GLY A 189      15.500   5.111   7.706  1.00 23.25           C  
ATOM   1408  C   GLY A 189      14.386   5.313   8.713  1.00 25.43           C  
ATOM   1409  O   GLY A 189      14.615   5.277   9.922  1.00 29.59           O  
ATOM   1410  N   LEU A 190      13.160   5.514   8.228  1.00 30.56           N  
ATOM   1411  CA  LEU A 190      12.026   5.695   9.130  1.00 33.04           C  
ATOM   1412  C   LEU A 190      11.700   4.410   9.881  1.00 37.01           C  
ATOM   1413  O   LEU A 190      11.447   4.439  11.091  1.00 34.52           O  
ATOM   1414  CB  LEU A 190      10.809   6.187   8.352  1.00 31.75           C  
ATOM   1415  CG  LEU A 190      10.752   7.695   8.140  1.00 35.96           C  
ATOM   1416  CD1 LEU A 190       9.582   8.045   7.241  1.00 39.64           C  
ATOM   1417  CD2 LEU A 190      10.643   8.397   9.482  1.00 25.53           C  
ATOM   1418  N   LEU A 191      11.688   3.274   9.176  1.00 34.01           N  
ATOM   1419  CA  LEU A 191      11.445   1.988   9.826  1.00 36.34           C  
ATOM   1420  C   LEU A 191      12.444   1.744  10.947  1.00 36.60           C  
ATOM   1421  O   LEU A 191      12.066   1.454  12.087  1.00 32.17           O  
ATOM   1422  CB  LEU A 191      11.523   0.849   8.805  1.00 37.90           C  
ATOM   1423  CG  LEU A 191      10.376   0.638   7.817  1.00 42.46           C  
ATOM   1424  CD1 LEU A 191      10.736  -0.440   6.803  1.00 38.91           C  
ATOM   1425  CD2 LEU A 191       9.101   0.272   8.554  1.00 43.65           C  
ATOM   1426  N   VAL A 192      13.735   1.856  10.631  1.00 34.12           N  
ATOM   1427  CA  VAL A 192      14.766   1.642  11.639  1.00 33.34           C  
ATOM   1428  C   VAL A 192      14.659   2.689  12.740  1.00 31.57           C  
ATOM   1429  O   VAL A 192      14.819   2.378  13.926  1.00 38.11           O  
ATOM   1430  CB  VAL A 192      16.158   1.643  10.982  1.00 28.93           C  
ATOM   1431  CG1 VAL A 192      17.231   1.368  12.017  1.00 33.05           C  
ATOM   1432  CG2 VAL A 192      16.209   0.614   9.866  1.00 31.80           C  
ATOM   1433  N   TYR A 193      14.367   3.938  12.372  1.00 34.10           N  
ATOM   1434  CA  TYR A 193      14.279   4.998  13.373  1.00 37.61           C  
ATOM   1435  C   TYR A 193      13.093   4.781  14.303  1.00 39.44           C  
ATOM   1436  O   TYR A 193      13.226   4.870  15.529  1.00 45.56           O  
ATOM   1437  CB  TYR A 193      14.182   6.365  12.697  1.00 31.50           C  
ATOM   1438  CG  TYR A 193      13.810   7.467  13.652  1.00 36.04           C  
ATOM   1439  CD1 TYR A 193      14.720   7.929  14.594  1.00 36.21           C  
ATOM   1440  CD2 TYR A 193      12.544   8.039  13.622  1.00 34.09           C  
ATOM   1441  CE1 TYR A 193      14.385   8.932  15.475  1.00 39.24           C  
ATOM   1442  CE2 TYR A 193      12.199   9.045  14.500  1.00 35.90           C  
ATOM   1443  CZ  TYR A 193      13.125   9.486  15.423  1.00 41.78           C  
ATOM   1444  OH  TYR A 193      12.799  10.485  16.302  1.00 39.34           O  
ATOM   1445  N   TYR A 194      11.917   4.506  13.735  1.00 31.12           N  
ATOM   1446  CA  TYR A 194      10.729   4.319  14.557  1.00 34.37           C  
ATOM   1447  C   TYR A 194      10.891   3.124  15.491  1.00 43.33           C  
ATOM   1448  O   TYR A 194      10.946   3.276  16.718  1.00 46.16           O  
ATOM   1449  CB  TYR A 194       9.493   4.155  13.672  1.00 36.54           C  
ATOM   1450  CG  TYR A 194       8.214   4.057  14.468  1.00 48.99           C  
ATOM   1451  CD1 TYR A 194       7.490   5.196  14.802  1.00 44.31           C  
ATOM   1452  CD2 TYR A 194       7.739   2.826  14.901  1.00 46.46           C  
ATOM   1453  CE1 TYR A 194       6.320   5.106  15.538  1.00 52.72           C  
ATOM   1454  CE2 TYR A 194       6.580   2.727  15.640  1.00 47.27           C  
ATOM   1455  CZ  TYR A 194       5.870   3.867  15.954  1.00 52.83           C  
ATOM   1456  OH  TYR A 194       4.710   3.764  16.687  1.00 59.18           O  
ATOM   1457  N   PHE A 195      10.977   1.919  14.925  1.00 41.33           N  
ATOM   1458  CA  PHE A 195      11.020   0.725  15.760  1.00 33.98           C  
ATOM   1459  C   PHE A 195      12.294   0.658  16.593  1.00 41.45           C  
ATOM   1460  O   PHE A 195      12.264   0.166  17.726  1.00 57.05           O  
ATOM   1461  CB  PHE A 195      10.866  -0.524  14.893  1.00 29.13           C  
ATOM   1462  CG  PHE A 195       9.566  -0.573  14.143  1.00 36.58           C  
ATOM   1463  CD1 PHE A 195       8.395  -0.943  14.782  1.00 33.30           C  
ATOM   1464  CD2 PHE A 195       9.513  -0.232  12.802  1.00 36.17           C  
ATOM   1465  CE1 PHE A 195       7.197  -0.979  14.097  1.00 37.45           C  
ATOM   1466  CE2 PHE A 195       8.319  -0.266  12.112  1.00 41.92           C  
ATOM   1467  CZ  PHE A 195       7.159  -0.639  12.759  1.00 39.71           C  
ATOM   1468  N   GLY A 196      13.412   1.164  16.070  1.00 40.25           N  
ATOM   1469  CA  GLY A 196      14.638   1.173  16.848  1.00 38.12           C  
ATOM   1470  C   GLY A 196      14.639   2.217  17.945  1.00 42.03           C  
ATOM   1471  O   GLY A 196      15.221   2.001  19.013  1.00 41.88           O  
ATOM   1472  N   GLY A 197      13.990   3.357  17.704  1.00 45.00           N  
ATOM   1473  CA  GLY A 197      13.936   4.396  18.719  1.00 43.70           C  
ATOM   1474  C   GLY A 197      13.099   4.003  19.922  1.00 43.77           C  
ATOM   1475  O   GLY A 197      13.485   4.264  21.065  1.00 45.20           O  
ATOM   1476  N   LYS A 198      11.941   3.378  19.682  1.00 45.91           N  
ATOM   1477  CA  LYS A 198      11.103   2.898  20.780  1.00 47.14           C  
ATOM   1478  C   LYS A 198      11.902   2.057  21.763  1.00 47.33           C  
ATOM   1479  O   LYS A 198      11.718   2.163  22.981  1.00 51.61           O  
ATOM   1480  CB  LYS A 198       9.938   2.071  20.236  1.00 51.05           C  
ATOM   1481  CG  LYS A 198       8.731   2.854  19.765  1.00 58.05           C  
ATOM   1482  CD  LYS A 198       7.720   1.895  19.153  1.00 61.69           C  
ATOM   1483  CE  LYS A 198       6.298   2.406  19.283  1.00 71.02           C  
ATOM   1484  NZ  LYS A 198       5.306   1.374  18.868  1.00 71.59           N  
ATOM   1485  N   LYS A 199      12.796   1.213  21.251  1.00 53.01           N  
ATOM   1486  CA  LYS A 199      13.538   0.310  22.121  1.00 65.92           C  
ATOM   1487  C   LYS A 199      14.634   1.036  22.885  1.00 59.47           C  
ATOM   1488  O   LYS A 199      14.850   0.763  24.070  1.00 58.57           O  
ATOM   1489  CB  LYS A 199      14.126  -0.841  21.304  1.00 59.07           C  
ATOM   1490  CG  LYS A 199      13.158  -1.463  20.312  1.00 50.06           C  
ATOM   1491  CD  LYS A 199      13.617  -2.854  19.906  1.00 70.70           C  
ATOM   1492  CE  LYS A 199      15.095  -2.867  19.536  1.00 59.49           C  
ATOM   1493  NZ  LYS A 199      15.634  -4.252  19.426  1.00 53.49           N  
ATOM   1494  N   THR A 200      15.327   1.967  22.235  1.00 63.86           N  
ATOM   1495  CA  THR A 200      16.478   2.615  22.850  1.00 58.36           C  
ATOM   1496  C   THR A 200      16.178   3.991  23.429  1.00 56.18           C  
ATOM   1497  O   THR A 200      16.491   4.252  24.593  1.00 67.30           O  
ATOM   1498  CB  THR A 200      17.619   2.772  21.846  1.00 56.60           C  
ATOM   1499  OG1 THR A 200      17.968   1.501  21.285  1.00 61.59           O  
ATOM   1500  CG2 THR A 200      18.801   3.364  22.570  1.00 57.71           C  
ATOM   1501  N   LEU A 201      15.610   4.885  22.628  1.00 52.81           N  
ATOM   1502  CA  LEU A 201      15.666   6.308  22.922  1.00 42.09           C  
ATOM   1503  C   LEU A 201      14.906   6.655  24.198  1.00 42.54           C  
ATOM   1504  O   LEU A 201      14.006   5.939  24.642  1.00 44.65           O  
ATOM   1505  CB  LEU A 201      15.118   7.116  21.747  1.00 41.05           C  
ATOM   1506  CG  LEU A 201      15.996   7.063  20.500  1.00 39.21           C  
ATOM   1507  CD1 LEU A 201      15.330   7.788  19.352  1.00 33.14           C  
ATOM   1508  CD2 LEU A 201      17.357   7.665  20.801  1.00 39.38           C  
ATOM   1509  N   ASP A 202      15.297   7.776  24.786  1.00 56.27           N  
ATOM   1510  CA  ASP A 202      14.661   8.256  26.005  1.00 49.83           C  
ATOM   1511  C   ASP A 202      13.273   8.796  25.677  1.00 54.48           C  
ATOM   1512  O   ASP A 202      13.138   9.617  24.760  1.00 50.26           O  
ATOM   1513  CB  ASP A 202      15.526   9.344  26.637  1.00 47.89           C  
ATOM   1514  CG  ASP A 202      15.155   9.633  28.077  1.00 58.93           C  
ATOM   1515  OD1 ASP A 202      13.950   9.711  28.394  1.00 60.35           O  
ATOM   1516  OD2 ASP A 202      16.085   9.787  28.895  1.00 57.45           O  
ATOM   1517  N   PRO A 203      12.221   8.366  26.383  1.00 51.87           N  
ATOM   1518  CA  PRO A 203      10.889   8.931  26.119  1.00 50.77           C  
ATOM   1519  C   PRO A 203      10.770  10.398  26.496  1.00 50.33           C  
ATOM   1520  O   PRO A 203       9.735  11.011  26.204  1.00 51.04           O  
ATOM   1521  CB  PRO A 203       9.955   8.060  26.971  1.00 48.17           C  
ATOM   1522  CG  PRO A 203      10.744   6.829  27.272  1.00 56.96           C  
ATOM   1523  CD  PRO A 203      12.165   7.286  27.378  1.00 56.16           C  
ATOM   1524  N   HIS A 204      11.792  10.973  27.135  1.00 50.64           N  
ATOM   1525  CA  HIS A 204      11.770  12.395  27.461  1.00 49.66           C  
ATOM   1526  C   HIS A 204      11.714  13.255  26.205  1.00 47.91           C  
ATOM   1527  O   HIS A 204      11.124  14.342  26.220  1.00 37.90           O  
ATOM   1528  CB  HIS A 204      12.999  12.746  28.298  1.00 48.83           C  
ATOM   1529  CG  HIS A 204      12.925  14.084  28.962  1.00 53.36           C  
ATOM   1530  ND1 HIS A 204      14.003  14.940  29.030  1.00 63.71           N  
ATOM   1531  CD2 HIS A 204      11.909  14.705  29.606  1.00 58.72           C  
ATOM   1532  CE1 HIS A 204      13.652  16.037  29.677  1.00 63.41           C  
ATOM   1533  NE2 HIS A 204      12.386  15.920  30.037  1.00 74.26           N  
ATOM   1534  N   TYR A 205      12.300  12.780  25.108  1.00 43.31           N  
ATOM   1535  CA  TYR A 205      12.385  13.536  23.868  1.00 38.71           C  
ATOM   1536  C   TYR A 205      11.242  13.235  22.909  1.00 36.89           C  
ATOM   1537  O   TYR A 205      11.287  13.667  21.752  1.00 34.65           O  
ATOM   1538  CB  TYR A 205      13.740  13.280  23.214  1.00 40.71           C  
ATOM   1539  CG  TYR A 205      14.846  13.483  24.215  1.00 36.47           C  
ATOM   1540  CD1 TYR A 205      15.228  14.762  24.598  1.00 38.91           C  
ATOM   1541  CD2 TYR A 205      15.476  12.403  24.815  1.00 41.31           C  
ATOM   1542  CE1 TYR A 205      16.225  14.961  25.531  1.00 42.95           C  
ATOM   1543  CE2 TYR A 205      16.475  12.592  25.750  1.00 48.57           C  
ATOM   1544  CZ  TYR A 205      16.845  13.874  26.104  1.00 42.98           C  
ATOM   1545  OH  TYR A 205      17.840  14.075  27.032  1.00 51.99           O  
ATOM   1546  N   LEU A 206      10.221  12.506  23.367  1.00 40.45           N  
ATOM   1547  CA  LEU A 206       8.932  12.487  22.689  1.00 37.66           C  
ATOM   1548  C   LEU A 206       8.174  13.796  22.864  1.00 37.96           C  
ATOM   1549  O   LEU A 206       7.112  13.969  22.256  1.00 45.24           O  
ATOM   1550  CB  LEU A 206       8.077  11.330  23.213  1.00 43.13           C  
ATOM   1551  CG  LEU A 206       8.543   9.901  22.925  1.00 46.19           C  
ATOM   1552  CD1 LEU A 206       7.617   8.899  23.591  1.00 45.69           C  
ATOM   1553  CD2 LEU A 206       8.607   9.653  21.427  1.00 37.81           C  
ATOM   1554  N   ARG A 207       8.701  14.712  23.667  1.00 46.74           N  
ATOM   1555  CA  ARG A 207       8.046  15.935  24.097  1.00 51.83           C  
ATOM   1556  C   ARG A 207       9.106  17.027  24.142  1.00 39.14           C  
ATOM   1557  O   ARG A 207      10.283  16.732  24.379  1.00 36.65           O  
ATOM   1558  CB  ARG A 207       7.387  15.725  25.476  1.00 47.42           C  
ATOM   1559  CG  ARG A 207       6.609  16.895  26.075  1.00 72.82           C  
ATOM   1560  CD  ARG A 207       5.368  17.277  25.273  1.00 82.66           C  
ATOM   1561  NE  ARG A 207       4.349  16.237  25.210  1.00 93.58           N  
ATOM   1562  CZ  ARG A 207       3.311  16.278  24.379  1.00103.04           C  
ATOM   1563  NH1 ARG A 207       2.419  15.297  24.379  1.00115.68           N  
ATOM   1564  NH2 ARG A 207       3.171  17.298  23.540  1.00 96.54           N  
ATOM   1565  N   PRO A 208       8.739  18.278  23.850  1.00 37.30           N  
ATOM   1566  CA  PRO A 208       9.707  19.376  23.983  1.00 32.26           C  
ATOM   1567  C   PRO A 208      10.335  19.427  25.368  1.00 36.13           C  
ATOM   1568  O   PRO A 208       9.666  19.252  26.388  1.00 30.10           O  
ATOM   1569  CB  PRO A 208       8.865  20.629  23.699  1.00 33.91           C  
ATOM   1570  CG  PRO A 208       7.432  20.155  23.628  1.00 38.08           C  
ATOM   1571  CD  PRO A 208       7.514  18.735  23.182  1.00 35.51           C  
ATOM   1572  N   THR A 209      11.646  19.676  25.390  1.00 37.19           N  
ATOM   1573  CA  THR A 209      12.406  19.779  26.634  1.00 33.41           C  
ATOM   1574  C   THR A 209      12.314  21.157  27.277  1.00 41.54           C  
ATOM   1575  O   THR A 209      12.377  21.263  28.507  1.00 38.15           O  
ATOM   1576  CB  THR A 209      13.878  19.437  26.383  1.00 23.38           C  
ATOM   1577  OG1 THR A 209      14.380  20.262  25.321  1.00 32.43           O  
ATOM   1578  CG2 THR A 209      14.027  17.974  25.988  1.00 27.76           C  
ATOM   1579  N   ASP A 210      12.180  22.213  26.474  1.00 30.79           N  
ATOM   1580  CA  ASP A 210      11.971  23.576  26.958  1.00 32.16           C  
ATOM   1581  C   ASP A 210      10.651  24.084  26.385  1.00 37.63           C  
ATOM   1582  O   ASP A 210      10.640  24.918  25.469  1.00 40.76           O  
ATOM   1583  CB  ASP A 210      13.129  24.497  26.570  1.00 32.62           C  
ATOM   1584  CG  ASP A 210      13.039  25.869  27.231  1.00 38.70           C  
ATOM   1585  OD1 ASP A 210      12.367  25.991  28.280  1.00 48.82           O  
ATOM   1586  OD2 ASP A 210      13.615  26.839  26.687  1.00 34.91           O  
ATOM   1587  N   PRO A 211       9.521  23.598  26.897  1.00 38.83           N  
ATOM   1588  CA  PRO A 211       8.232  23.962  26.299  1.00 38.05           C  
ATOM   1589  C   PRO A 211       7.942  25.448  26.434  1.00 36.56           C  
ATOM   1590  O   PRO A 211       8.423  26.118  27.348  1.00 39.07           O  
ATOM   1591  CB  PRO A 211       7.220  23.122  27.095  1.00 35.21           C  
ATOM   1592  CG  PRO A 211       8.019  22.100  27.816  1.00 34.10           C  
ATOM   1593  CD  PRO A 211       9.358  22.709  28.059  1.00 30.74           C  
ATOM   1594  N   LEU A 212       7.138  25.959  25.506  1.00 44.85           N  
ATOM   1595  CA  LEU A 212       6.705  27.345  25.595  1.00 34.75           C  
ATOM   1596  C   LEU A 212       5.939  27.572  26.890  1.00 44.47           C  
ATOM   1597  O   LEU A 212       5.102  26.758  27.285  1.00 48.38           O  
ATOM   1598  CB  LEU A 212       5.826  27.715  24.401  1.00 41.46           C  
ATOM   1599  CG  LEU A 212       6.476  27.825  23.027  1.00 37.71           C  
ATOM   1600  CD1 LEU A 212       5.447  28.315  22.032  1.00 34.61           C  
ATOM   1601  CD2 LEU A 212       7.664  28.763  23.072  1.00 36.36           C  
ATOM   1602  N   ALA A 213       6.252  28.673  27.564  1.00 40.93           N  
ATOM   1603  CA  ALA A 213       5.490  29.098  28.724  1.00 31.57           C  
ATOM   1604  C   ALA A 213       4.224  29.815  28.263  1.00 35.24           C  
ATOM   1605  O   ALA A 213       4.138  30.251  27.113  1.00 35.38           O  
ATOM   1606  CB  ALA A 213       6.346  30.001  29.606  1.00 33.91           C  
ATOM   1607  N   PRO A 214       3.206  29.924  29.129  1.00 36.63           N  
ATOM   1608  CA  PRO A 214       1.941  30.538  28.683  1.00 35.10           C  
ATOM   1609  C   PRO A 214       2.104  31.910  28.053  1.00 32.07           C  
ATOM   1610  O   PRO A 214       1.427  32.218  27.065  1.00 41.32           O  
ATOM   1611  CB  PRO A 214       1.118  30.610  29.975  1.00 30.01           C  
ATOM   1612  CG  PRO A 214       1.621  29.489  30.794  1.00 35.16           C  
ATOM   1613  CD  PRO A 214       3.099  29.400  30.504  1.00 36.42           C  
ATOM   1614  N   GLU A 215       2.993  32.741  28.593  1.00 34.26           N  
ATOM   1615  CA  GLU A 215       3.151  34.097  28.089  1.00 28.32           C  
ATOM   1616  C   GLU A 215       3.982  34.173  26.819  1.00 26.87           C  
ATOM   1617  O   GLU A 215       3.974  35.216  26.159  1.00 36.28           O  
ATOM   1618  CB  GLU A 215       3.782  34.987  29.161  1.00 26.45           C  
ATOM   1619  CG  GLU A 215       2.870  35.257  30.344  1.00 35.68           C  
ATOM   1620  CD  GLU A 215       1.614  36.011  29.948  1.00 33.64           C  
ATOM   1621  OE1 GLU A 215       1.729  37.197  29.579  1.00 39.80           O  
ATOM   1622  OE2 GLU A 215       0.515  35.417  29.992  1.00 45.66           O  
ATOM   1623  N   GLU A 216       4.695  33.109  26.455  1.00 27.84           N  
ATOM   1624  CA  GLU A 216       5.584  33.166  25.302  1.00 26.82           C  
ATOM   1625  C   GLU A 216       4.902  32.825  23.989  1.00 26.66           C  
ATOM   1626  O   GLU A 216       5.496  33.040  22.930  1.00 38.88           O  
ATOM   1627  CB  GLU A 216       6.772  32.221  25.489  1.00 32.30           C  
ATOM   1628  CG  GLU A 216       7.478  32.354  26.813  1.00 27.22           C  
ATOM   1629  CD  GLU A 216       8.705  31.478  26.889  1.00 35.20           C  
ATOM   1630  OE1 GLU A 216       9.785  31.919  26.441  1.00 44.68           O  
ATOM   1631  OE2 GLU A 216       8.586  30.336  27.379  1.00 30.75           O  
ATOM   1632  N   VAL A 217       3.680  32.303  24.028  1.00 30.34           N  
ATOM   1633  CA  VAL A 217       3.042  31.838  22.802  1.00 29.74           C  
ATOM   1634  C   VAL A 217       2.684  33.016  21.904  1.00 32.50           C  
ATOM   1635  O   VAL A 217       2.990  33.016  20.705  1.00 34.03           O  
ATOM   1636  CB  VAL A 217       1.811  30.974  23.132  1.00 33.74           C  
ATOM   1637  CG1 VAL A 217       1.214  30.403  21.861  1.00 35.02           C  
ATOM   1638  CG2 VAL A 217       2.204  29.862  24.096  1.00 28.77           C  
ATOM   1639  N   LYS A 218       2.053  34.045  22.473  1.00 34.67           N  
ATOM   1640  CA  LYS A 218       1.622  35.186  21.666  1.00 34.75           C  
ATOM   1641  C   LYS A 218       2.782  35.939  21.022  1.00 29.33           C  
ATOM   1642  O   LYS A 218       2.713  36.208  19.809  1.00 25.72           O  
ATOM   1643  CB  LYS A 218       0.750  36.120  22.513  1.00 34.64           C  
ATOM   1644  CG  LYS A 218       0.116  37.243  21.714  1.00 41.79           C  
ATOM   1645  CD  LYS A 218      -0.847  38.052  22.558  1.00 45.09           C  
ATOM   1646  CE  LYS A 218      -0.189  39.297  23.117  1.00 50.55           C  
ATOM   1647  NZ  LYS A 218      -1.154  40.117  23.903  1.00 59.30           N  
ATOM   1648  N   PRO A 219       3.852  36.311  21.735  1.00 30.75           N  
ATOM   1649  CA  PRO A 219       4.968  36.974  21.039  1.00 29.55           C  
ATOM   1650  C   PRO A 219       5.554  36.139  19.917  1.00 32.34           C  
ATOM   1651  O   PRO A 219       5.865  36.680  18.848  1.00 38.59           O  
ATOM   1652  CB  PRO A 219       5.986  37.218  22.163  1.00 24.92           C  
ATOM   1653  CG  PRO A 219       5.171  37.275  23.393  1.00 26.36           C  
ATOM   1654  CD  PRO A 219       4.081  36.267  23.191  1.00 32.43           C  
ATOM   1655  N   LEU A 220       5.706  34.828  20.124  1.00 33.60           N  
ATOM   1656  CA  LEU A 220       6.211  33.975  19.054  1.00 35.50           C  
ATOM   1657  C   LEU A 220       5.265  33.977  17.863  1.00 36.36           C  
ATOM   1658  O   LEU A 220       5.706  34.007  16.709  1.00 34.96           O  
ATOM   1659  CB  LEU A 220       6.426  32.552  19.567  1.00 34.03           C  
ATOM   1660  CG  LEU A 220       7.005  31.580  18.539  1.00 33.53           C  
ATOM   1661  CD1 LEU A 220       8.328  32.104  17.992  1.00 29.47           C  
ATOM   1662  CD2 LEU A 220       7.180  30.202  19.154  1.00 46.13           C  
ATOM   1663  N   LEU A 221       3.957  33.957  18.129  1.00 35.74           N  
ATOM   1664  CA  LEU A 221       2.973  34.040  17.056  1.00 39.88           C  
ATOM   1665  C   LEU A 221       3.104  35.349  16.288  1.00 39.15           C  
ATOM   1666  O   LEU A 221       3.101  35.361  15.052  1.00 37.24           O  
ATOM   1667  CB  LEU A 221       1.563  33.897  17.628  1.00 42.72           C  
ATOM   1668  CG  LEU A 221       0.496  33.709  16.555  1.00 53.58           C  
ATOM   1669  CD1 LEU A 221       0.854  32.491  15.736  1.00 52.22           C  
ATOM   1670  CD2 LEU A 221      -0.889  33.568  17.163  1.00 55.10           C  
ATOM   1671  N   VAL A 222       3.204  36.467  17.008  1.00 36.03           N  
ATOM   1672  CA  VAL A 222       3.371  37.764  16.356  1.00 38.79           C  
ATOM   1673  C   VAL A 222       4.643  37.773  15.519  1.00 33.24           C  
ATOM   1674  O   VAL A 222       4.653  38.231  14.370  1.00 42.66           O  
ATOM   1675  CB  VAL A 222       3.374  38.894  17.403  1.00 31.43           C  
ATOM   1676  CG1 VAL A 222       3.761  40.215  16.763  1.00 30.94           C  
ATOM   1677  CG2 VAL A 222       2.010  39.006  18.069  1.00 28.21           C  
ATOM   1678  N   LYS A 223       5.731  37.242  16.081  1.00 33.92           N  
ATOM   1679  CA  LYS A 223       7.023  37.252  15.400  1.00 33.16           C  
ATOM   1680  C   LYS A 223       6.964  36.489  14.082  1.00 28.81           C  
ATOM   1681  O   LYS A 223       7.360  37.008  13.033  1.00 32.37           O  
ATOM   1682  CB  LYS A 223       8.086  36.661  16.329  1.00 36.20           C  
ATOM   1683  CG  LYS A 223       9.513  36.762  15.832  1.00 39.51           C  
ATOM   1684  CD  LYS A 223      10.485  36.494  16.971  1.00 45.83           C  
ATOM   1685  CE  LYS A 223      10.270  37.481  18.112  1.00 52.04           C  
ATOM   1686  NZ  LYS A 223      10.217  36.821  19.448  1.00 64.06           N  
ATOM   1687  N   VAL A 224       6.467  35.252  14.118  1.00 30.81           N  
ATOM   1688  CA  VAL A 224       6.374  34.448  12.904  1.00 32.22           C  
ATOM   1689  C   VAL A 224       5.386  35.060  11.918  1.00 41.87           C  
ATOM   1690  O   VAL A 224       5.584  34.980  10.700  1.00 42.39           O  
ATOM   1691  CB  VAL A 224       5.996  32.998  13.264  1.00 31.44           C  
ATOM   1692  CG1 VAL A 224       5.907  32.137  12.011  1.00 47.13           C  
ATOM   1693  CG2 VAL A 224       7.003  32.416  14.243  1.00 30.02           C  
ATOM   1694  N   SER A 225       4.321  35.692  12.418  1.00 35.96           N  
ATOM   1695  CA  SER A 225       3.313  36.266  11.531  1.00 35.26           C  
ATOM   1696  C   SER A 225       3.820  37.537  10.862  1.00 39.13           C  
ATOM   1697  O   SER A 225       3.536  37.781   9.683  1.00 33.64           O  
ATOM   1698  CB  SER A 225       2.027  36.548  12.308  1.00 42.87           C  
ATOM   1699  OG  SER A 225       1.599  35.398  13.016  1.00 47.38           O  
ATOM   1700  N   LEU A 226       4.562  38.364  11.601  1.00 34.63           N  
ATOM   1701  CA  LEU A 226       5.148  39.557  11.000  1.00 34.13           C  
ATOM   1702  C   LEU A 226       6.166  39.190   9.930  1.00 36.54           C  
ATOM   1703  O   LEU A 226       6.301  39.893   8.921  1.00 42.07           O  
ATOM   1704  CB  LEU A 226       5.798  40.428  12.074  1.00 30.41           C  
ATOM   1705  CG  LEU A 226       4.850  41.223  12.966  1.00 41.79           C  
ATOM   1706  CD1 LEU A 226       5.645  41.964  14.021  1.00 31.90           C  
ATOM   1707  CD2 LEU A 226       4.009  42.188  12.139  1.00 37.63           C  
ATOM   1708  N   ALA A 227       6.890  38.089  10.129  1.00 39.32           N  
ATOM   1709  CA  ALA A 227       7.877  37.677   9.139  1.00 39.79           C  
ATOM   1710  C   ALA A 227       7.208  37.207   7.855  1.00 36.45           C  
ATOM   1711  O   ALA A 227       7.672  37.525   6.756  1.00 34.74           O  
ATOM   1712  CB  ALA A 227       8.774  36.583   9.718  1.00 29.30           C  
ATOM   1713  N   VAL A 228       6.112  36.459   7.971  1.00 32.14           N  
ATOM   1714  CA  VAL A 228       5.443  35.944   6.782  1.00 39.33           C  
ATOM   1715  C   VAL A 228       4.745  37.070   6.029  1.00 48.94           C  
ATOM   1716  O   VAL A 228       4.804  37.139   4.795  1.00 49.76           O  
ATOM   1717  CB  VAL A 228       4.466  34.818   7.167  1.00 39.65           C  
ATOM   1718  CG1 VAL A 228       3.662  34.377   5.961  1.00 37.89           C  
ATOM   1719  CG2 VAL A 228       5.228  33.642   7.762  1.00 32.88           C  
ATOM   1720  N   ALA A 229       4.086  37.976   6.757  1.00 46.98           N  
ATOM   1721  CA  ALA A 229       3.368  39.070   6.110  1.00 44.83           C  
ATOM   1722  C   ALA A 229       4.318  39.948   5.305  1.00 41.65           C  
ATOM   1723  O   ALA A 229       4.071  40.234   4.128  1.00 40.72           O  
ATOM   1724  CB  ALA A 229       2.617  39.899   7.154  1.00 27.26           C  
ATOM   1725  N   GLY A 230       5.420  40.375   5.924  1.00 42.77           N  
ATOM   1726  CA  GLY A 230       6.402  41.166   5.200  1.00 45.17           C  
ATOM   1727  C   GLY A 230       7.002  40.416   4.027  1.00 50.34           C  
ATOM   1728  O   GLY A 230       7.215  40.987   2.955  1.00 50.15           O  
ATOM   1729  N   PHE A 231       7.279  39.122   4.212  1.00 48.80           N  
ATOM   1730  CA  PHE A 231       7.782  38.307   3.111  1.00 42.75           C  
ATOM   1731  C   PHE A 231       6.738  38.175   2.013  1.00 42.37           C  
ATOM   1732  O   PHE A 231       7.067  38.225   0.823  1.00 45.44           O  
ATOM   1733  CB  PHE A 231       8.205  36.930   3.626  1.00 47.50           C  
ATOM   1734  CG  PHE A 231       8.726  36.007   2.556  1.00 46.22           C  
ATOM   1735  CD1 PHE A 231       9.962  36.229   1.972  1.00 49.40           C  
ATOM   1736  CD2 PHE A 231       7.989  34.904   2.151  1.00 47.47           C  
ATOM   1737  CE1 PHE A 231      10.448  35.378   0.995  1.00 50.53           C  
ATOM   1738  CE2 PHE A 231       8.469  34.048   1.177  1.00 43.50           C  
ATOM   1739  CZ  PHE A 231       9.700  34.287   0.597  1.00 51.12           C  
ATOM   1740  N   ILE A 232       5.471  38.006   2.395  1.00 40.35           N  
ATOM   1741  CA  ILE A 232       4.402  37.996   1.405  1.00 43.46           C  
ATOM   1742  C   ILE A 232       4.222  39.384   0.802  1.00 45.73           C  
ATOM   1743  O   ILE A 232       3.962  39.516  -0.399  1.00 48.87           O  
ATOM   1744  CB  ILE A 232       3.103  37.454   2.034  1.00 50.00           C  
ATOM   1745  CG1 ILE A 232       3.115  35.919   2.038  1.00 43.79           C  
ATOM   1746  CG2 ILE A 232       1.871  37.995   1.320  1.00 38.46           C  
ATOM   1747  CD1 ILE A 232       1.811  35.286   2.482  1.00 45.63           C  
ATOM   1748  N   ALA A 233       4.398  40.440   1.602  1.00 40.44           N  
ATOM   1749  CA  ALA A 233       4.291  41.796   1.071  1.00 37.74           C  
ATOM   1750  C   ALA A 233       5.370  42.073   0.032  1.00 44.06           C  
ATOM   1751  O   ALA A 233       5.102  42.707  -0.996  1.00 45.86           O  
ATOM   1752  CB  ALA A 233       4.370  42.817   2.204  1.00 41.69           C  
ATOM   1753  N   ILE A 234       6.598  41.606   0.280  1.00 39.65           N  
ATOM   1754  CA  ILE A 234       7.666  41.769  -0.704  1.00 45.49           C  
ATOM   1755  C   ILE A 234       7.284  41.091  -2.014  1.00 46.22           C  
ATOM   1756  O   ILE A 234       7.451  41.656  -3.101  1.00 42.19           O  
ATOM   1757  CB  ILE A 234       8.996  41.220  -0.155  1.00 40.57           C  
ATOM   1758  CG1 ILE A 234       9.478  42.051   1.034  1.00 37.15           C  
ATOM   1759  CG2 ILE A 234      10.060  41.210  -1.240  1.00 45.01           C  
ATOM   1760  CD1 ILE A 234      10.766  41.538   1.644  1.00 34.25           C  
ATOM   1761  N   ILE A 235       6.739  39.877  -1.925  1.00 44.68           N  
ATOM   1762  CA  ILE A 235       6.477  39.077  -3.119  1.00 43.04           C  
ATOM   1763  C   ILE A 235       5.420  39.739  -4.000  1.00 56.80           C  
ATOM   1764  O   ILE A 235       5.505  39.693  -5.234  1.00 55.80           O  
ATOM   1765  CB  ILE A 235       6.081  37.644  -2.714  1.00 47.19           C  
ATOM   1766  CG1 ILE A 235       7.291  36.915  -2.125  1.00 48.78           C  
ATOM   1767  CG2 ILE A 235       5.511  36.877  -3.900  1.00 45.77           C  
ATOM   1768  CD1 ILE A 235       6.993  35.510  -1.661  1.00 48.81           C  
ATOM   1769  N   VAL A 236       4.417  40.380  -3.392  1.00 56.91           N  
ATOM   1770  CA  VAL A 236       3.391  41.020  -4.214  1.00 54.85           C  
ATOM   1771  C   VAL A 236       3.932  42.296  -4.847  1.00 51.61           C  
ATOM   1772  O   VAL A 236       3.572  42.632  -5.983  1.00 52.70           O  
ATOM   1773  CB  VAL A 236       2.108  41.277  -3.398  1.00 52.85           C  
ATOM   1774  CG1 VAL A 236       1.711  40.018  -2.624  1.00 42.46           C  
ATOM   1775  CG2 VAL A 236       2.261  42.461  -2.455  1.00 42.30           C  
ATOM   1776  N   VAL A 237       4.822  43.011  -4.153  1.00 46.87           N  
ATOM   1777  CA  VAL A 237       5.415  44.207  -4.742  1.00 42.40           C  
ATOM   1778  C   VAL A 237       6.293  43.833  -5.926  1.00 47.23           C  
ATOM   1779  O   VAL A 237       6.306  44.530  -6.946  1.00 55.37           O  
ATOM   1780  CB  VAL A 237       6.190  45.007  -3.681  1.00 46.74           C  
ATOM   1781  CG1 VAL A 237       7.019  46.105  -4.333  1.00 35.15           C  
ATOM   1782  CG2 VAL A 237       5.227  45.606  -2.673  1.00 50.69           C  
ATOM   1783  N   MET A 238       7.026  42.724  -5.821  1.00 48.71           N  
ATOM   1784  CA  MET A 238       7.795  42.231  -6.957  1.00 40.92           C  
ATOM   1785  C   MET A 238       6.923  42.102  -8.196  1.00 53.96           C  
ATOM   1786  O   MET A 238       7.217  42.683  -9.246  1.00 57.93           O  
ATOM   1787  CB  MET A 238       8.416  40.883  -6.623  1.00 53.83           C  
ATOM   1788  CG  MET A 238       9.374  40.926  -5.489  1.00 56.67           C  
ATOM   1789  SD  MET A 238      10.188  39.343  -5.365  1.00 54.50           S  
ATOM   1790  CE  MET A 238      11.697  39.901  -4.619  1.00 53.86           C  
ATOM   1791  N   ASN A 239       5.836  41.334  -8.083  1.00 53.84           N  
ATOM   1792  CA  ASN A 239       4.989  41.073  -9.241  1.00 56.66           C  
ATOM   1793  C   ASN A 239       4.330  42.346  -9.752  1.00 58.43           C  
ATOM   1794  O   ASN A 239       4.078  42.470 -10.956  1.00 62.87           O  
ATOM   1795  CB  ASN A 239       3.936  40.024  -8.890  1.00 47.07           C  
ATOM   1796  CG  ASN A 239       4.550  38.690  -8.486  1.00 51.62           C  
ATOM   1797  OD1 ASN A 239       4.484  37.714  -9.230  1.00 60.28           O  
ATOM   1798  ND2 ASN A 239       5.142  38.643  -7.298  1.00 54.91           N  
ATOM   1799  N   LEU A 240       4.053  43.300  -8.862  1.00 55.08           N  
ATOM   1800  CA  LEU A 240       3.521  44.585  -9.303  1.00 61.62           C  
ATOM   1801  C   LEU A 240       4.508  45.300 -10.216  1.00 56.67           C  
ATOM   1802  O   LEU A 240       4.142  45.773 -11.298  1.00 68.33           O  
ATOM   1803  CB  LEU A 240       3.185  45.462  -8.096  1.00 49.60           C  
ATOM   1804  CG  LEU A 240       1.959  45.075  -7.274  1.00 51.64           C  
ATOM   1805  CD1 LEU A 240       1.470  46.278  -6.487  1.00 43.07           C  
ATOM   1806  CD2 LEU A 240       0.860  44.510  -8.163  1.00 42.40           C  
ATOM   1807  N   VAL A 241       5.774  45.385  -9.793  1.00 54.73           N  
ATOM   1808  CA  VAL A 241       6.809  46.065 -10.571  1.00 54.37           C  
ATOM   1809  C   VAL A 241       7.331  45.209 -11.715  1.00 56.71           C  
ATOM   1810  O   VAL A 241       8.182  45.668 -12.488  1.00 53.55           O  
ATOM   1811  CB  VAL A 241       7.922  46.509  -9.595  1.00 46.83           C  
ATOM   1812  CG1 VAL A 241       8.919  47.451 -10.259  1.00 63.24           C  
ATOM   1813  CG2 VAL A 241       7.304  47.191  -8.388  1.00 49.45           C  
ATOM   1814  N   GLY A 242       6.833  43.986 -11.869  1.00 62.42           N  
ATOM   1815  CA  GLY A 242       7.222  43.151 -12.986  1.00 61.24           C  
ATOM   1816  C   GLY A 242       8.437  42.283 -12.756  1.00 64.07           C  
ATOM   1817  O   GLY A 242       9.026  41.803 -13.731  1.00 66.69           O  
ATOM   1818  N   TRP A 243       8.827  42.064 -11.503  1.00 67.73           N  
ATOM   1819  CA  TRP A 243       9.953  41.207 -11.145  1.00 65.18           C  
ATOM   1820  C   TRP A 243       9.497  39.804 -10.783  1.00 58.89           C  
ATOM   1821  O   TRP A 243       9.950  39.231  -9.791  1.00 56.99           O  
ATOM   1822  CB  TRP A 243      10.744  41.830  -9.996  1.00 58.31           C  
ATOM   1823  CG  TRP A 243      11.495  43.063 -10.403  1.00 60.34           C  
ATOM   1824  CD1 TRP A 243      11.838  43.434 -11.675  1.00 63.37           C  
ATOM   1825  CD2 TRP A 243      11.997  44.093  -9.539  1.00 63.55           C  
ATOM   1826  NE1 TRP A 243      12.527  44.624 -11.653  1.00 59.79           N  
ATOM   1827  CE2 TRP A 243      12.638  45.050 -10.355  1.00 68.58           C  
ATOM   1828  CE3 TRP A 243      11.970  44.299  -8.156  1.00 66.04           C  
ATOM   1829  CZ2 TRP A 243      13.245  46.194  -9.832  1.00 67.38           C  
ATOM   1830  CZ3 TRP A 243      12.574  45.436  -7.641  1.00 64.95           C  
ATOM   1831  CH2 TRP A 243      13.202  46.367  -8.477  1.00 64.70           C  
ATOM   1832  N   ASN A 244       8.603  39.224 -11.577  1.00 57.77           N  
ATOM   1833  CA  ASN A 244       7.966  37.957 -11.253  1.00 54.29           C  
ATOM   1834  C   ASN A 244       8.615  36.772 -11.959  1.00 52.54           C  
ATOM   1835  O   ASN A 244       8.000  35.707 -12.059  1.00 58.32           O  
ATOM   1836  CB  ASN A 244       6.477  38.024 -11.591  1.00 63.30           C  
ATOM   1837  CG  ASN A 244       6.212  38.744 -12.898  1.00 77.06           C  
ATOM   1838  OD1 ASN A 244       6.624  38.293 -13.967  1.00 83.71           O  
ATOM   1839  ND2 ASN A 244       5.508  39.870 -12.819  1.00 78.33           N  
ATOM   1840  N   SER A 245       9.837  36.928 -12.454  1.00 48.80           N  
ATOM   1841  CA  SER A 245      10.520  35.821 -13.110  1.00 47.53           C  
ATOM   1842  C   SER A 245      11.139  34.894 -12.076  1.00 57.02           C  
ATOM   1843  O   SER A 245      11.430  35.298 -10.946  1.00 55.55           O  
ATOM   1844  CB  SER A 245      11.602  36.333 -14.062  1.00 45.00           C  
ATOM   1845  OG  SER A 245      12.698  36.867 -13.347  1.00 45.01           O  
ATOM   1846  N   LEU A 246      11.327  33.633 -12.468  1.00 49.46           N  
ATOM   1847  CA  LEU A 246      11.991  32.682 -11.580  1.00 47.22           C  
ATOM   1848  C   LEU A 246      13.380  33.144 -11.158  1.00 41.45           C  
ATOM   1849  O   LEU A 246      13.701  33.037  -9.963  1.00 50.23           O  
ATOM   1850  CB  LEU A 246      12.035  31.295 -12.240  1.00 52.88           C  
ATOM   1851  CG  LEU A 246      12.844  30.237 -11.484  1.00 51.14           C  
ATOM   1852  CD1 LEU A 246      12.215  29.933 -10.131  1.00 54.06           C  
ATOM   1853  CD2 LEU A 246      12.979  28.974 -12.317  1.00 48.99           C  
ATOM   1854  N   PRO A 247      14.244  33.649 -12.046  1.00 40.67           N  
ATOM   1855  CA  PRO A 247      15.529  34.188 -11.569  1.00 38.73           C  
ATOM   1856  C   PRO A 247      15.382  35.321 -10.568  1.00 44.78           C  
ATOM   1857  O   PRO A 247      16.301  35.554  -9.773  1.00 46.99           O  
ATOM   1858  CB  PRO A 247      16.207  34.664 -12.861  1.00 32.68           C  
ATOM   1859  CG  PRO A 247      15.621  33.809 -13.921  1.00 34.10           C  
ATOM   1860  CD  PRO A 247      14.193  33.603 -13.520  1.00 42.74           C  
ATOM   1861  N   ALA A 248      14.257  36.039 -10.582  1.00 44.11           N  
ATOM   1862  CA  ALA A 248      14.058  37.120  -9.624  1.00 35.01           C  
ATOM   1863  C   ALA A 248      13.683  36.582  -8.248  1.00 45.44           C  
ATOM   1864  O   ALA A 248      14.110  37.133  -7.226  1.00 38.36           O  
ATOM   1865  CB  ALA A 248      12.989  38.089 -10.132  1.00 34.13           C  
ATOM   1866  N   TYR A 249      12.882  35.513  -8.201  1.00 42.21           N  
ATOM   1867  CA  TYR A 249      12.559  34.887  -6.922  1.00 44.51           C  
ATOM   1868  C   TYR A 249      13.804  34.303  -6.263  1.00 48.35           C  
ATOM   1869  O   TYR A 249      13.965  34.381  -5.038  1.00 36.47           O  
ATOM   1870  CB  TYR A 249      11.503  33.800  -7.114  1.00 38.81           C  
ATOM   1871  CG  TYR A 249      10.099  34.326  -7.298  1.00 47.72           C  
ATOM   1872  CD1 TYR A 249       9.452  35.006  -6.274  1.00 41.85           C  
ATOM   1873  CD2 TYR A 249       9.413  34.127  -8.489  1.00 49.29           C  
ATOM   1874  CE1 TYR A 249       8.168  35.481  -6.434  1.00 45.61           C  
ATOM   1875  CE2 TYR A 249       8.128  34.598  -8.658  1.00 54.87           C  
ATOM   1876  CZ  TYR A 249       7.509  35.275  -7.627  1.00 48.67           C  
ATOM   1877  OH  TYR A 249       6.225  35.745  -7.794  1.00 55.08           O  
ATOM   1878  N   ILE A 250      14.694  33.711  -7.062  1.00 45.71           N  
ATOM   1879  CA  ILE A 250      15.950  33.203  -6.522  1.00 44.91           C  
ATOM   1880  C   ILE A 250      16.756  34.339  -5.908  1.00 39.68           C  
ATOM   1881  O   ILE A 250      17.386  34.176  -4.856  1.00 41.16           O  
ATOM   1882  CB  ILE A 250      16.737  32.460  -7.619  1.00 37.88           C  
ATOM   1883  CG1 ILE A 250      15.987  31.191  -8.032  1.00 32.79           C  
ATOM   1884  CG2 ILE A 250      18.144  32.128  -7.148  1.00 40.33           C  
ATOM   1885  CD1 ILE A 250      16.762  30.293  -8.965  1.00 31.66           C  
ATOM   1886  N   ASN A 251      16.721  35.516  -6.535  1.00 43.62           N  
ATOM   1887  CA  ASN A 251      17.424  36.665  -5.977  1.00 43.05           C  
ATOM   1888  C   ASN A 251      16.820  37.088  -4.646  1.00 42.43           C  
ATOM   1889  O   ASN A 251      17.549  37.481  -3.729  1.00 45.62           O  
ATOM   1890  CB  ASN A 251      17.410  37.825  -6.971  1.00 43.85           C  
ATOM   1891  CG  ASN A 251      18.232  37.536  -8.210  1.00 45.26           C  
ATOM   1892  OD1 ASN A 251      19.019  36.591  -8.240  1.00 48.02           O  
ATOM   1893  ND2 ASN A 251      18.059  38.354  -9.240  1.00 50.05           N  
ATOM   1894  N   LEU A 252      15.493  37.015  -4.522  1.00 35.48           N  
ATOM   1895  CA  LEU A 252      14.851  37.306  -3.243  1.00 41.80           C  
ATOM   1896  C   LEU A 252      15.408  36.416  -2.137  1.00 39.34           C  
ATOM   1897  O   LEU A 252      15.806  36.902  -1.073  1.00 41.44           O  
ATOM   1898  CB  LEU A 252      13.337  37.129  -3.362  1.00 44.65           C  
ATOM   1899  CG  LEU A 252      12.516  37.194  -2.073  1.00 42.77           C  
ATOM   1900  CD1 LEU A 252      12.649  38.552  -1.392  1.00 41.71           C  
ATOM   1901  CD2 LEU A 252      11.058  36.870  -2.356  1.00 41.56           C  
ATOM   1902  N   LEU A 253      15.453  35.104  -2.380  1.00 42.34           N  
ATOM   1903  CA  LEU A 253      15.994  34.186  -1.383  1.00 40.94           C  
ATOM   1904  C   LEU A 253      17.477  34.438  -1.149  1.00 43.90           C  
ATOM   1905  O   LEU A 253      17.957  34.332  -0.015  1.00 42.18           O  
ATOM   1906  CB  LEU A 253      15.759  32.744  -1.819  1.00 36.78           C  
ATOM   1907  CG  LEU A 253      14.307  32.406  -2.138  1.00 38.62           C  
ATOM   1908  CD1 LEU A 253      14.217  30.984  -2.625  1.00 44.97           C  
ATOM   1909  CD2 LEU A 253      13.427  32.617  -0.918  1.00 47.75           C  
ATOM   1910  N   THR A 254      18.218  34.764  -2.211  1.00 40.35           N  
ATOM   1911  CA  THR A 254      19.622  35.132  -2.060  1.00 36.39           C  
ATOM   1912  C   THR A 254      19.769  36.298  -1.090  1.00 40.66           C  
ATOM   1913  O   THR A 254      20.518  36.220  -0.109  1.00 42.32           O  
ATOM   1914  CB  THR A 254      20.220  35.484  -3.425  1.00 41.84           C  
ATOM   1915  OG1 THR A 254      19.957  34.422  -4.351  1.00 42.13           O  
ATOM   1916  CG2 THR A 254      21.719  35.689  -3.322  1.00 23.91           C  
ATOM   1917  N   ILE A 255      19.032  37.384  -1.343  1.00 39.47           N  
ATOM   1918  CA  ILE A 255      19.064  38.548  -0.460  1.00 37.67           C  
ATOM   1919  C   ILE A 255      18.622  38.159   0.944  1.00 44.17           C  
ATOM   1920  O   ILE A 255      19.252  38.534   1.939  1.00 42.97           O  
ATOM   1921  CB  ILE A 255      18.190  39.677  -1.038  1.00 37.26           C  
ATOM   1922  CG1 ILE A 255      18.793  40.204  -2.342  1.00 29.39           C  
ATOM   1923  CG2 ILE A 255      18.020  40.795  -0.026  1.00 39.84           C  
ATOM   1924  CD1 ILE A 255      17.763  40.686  -3.342  1.00 37.06           C  
ATOM   1925  N   VAL A 256      17.535  37.390   1.044  1.00 41.67           N  
ATOM   1926  CA  VAL A 256      17.054  36.937   2.347  1.00 36.82           C  
ATOM   1927  C   VAL A 256      18.122  36.109   3.053  1.00 40.66           C  
ATOM   1928  O   VAL A 256      18.373  36.283   4.252  1.00 42.09           O  
ATOM   1929  CB  VAL A 256      15.735  36.153   2.189  1.00 42.27           C  
ATOM   1930  CG1 VAL A 256      15.439  35.336   3.442  1.00 47.42           C  
ATOM   1931  CG2 VAL A 256      14.579  37.102   1.889  1.00 43.01           C  
ATOM   1932  N   ALA A 257      18.789  35.218   2.316  1.00 35.34           N  
ATOM   1933  CA  ALA A 257      19.759  34.317   2.934  1.00 38.62           C  
ATOM   1934  C   ALA A 257      21.014  35.046   3.393  1.00 42.75           C  
ATOM   1935  O   ALA A 257      21.611  34.663   4.403  1.00 52.66           O  
ATOM   1936  CB  ALA A 257      20.134  33.200   1.965  1.00 35.94           C  
ATOM   1937  N   ILE A 258      21.434  36.081   2.668  1.00 42.14           N  
ATOM   1938  CA  ILE A 258      22.627  36.816   3.069  1.00 43.72           C  
ATOM   1939  C   ILE A 258      22.286  37.894   4.099  1.00 41.89           C  
ATOM   1940  O   ILE A 258      23.109  38.205   4.964  1.00 50.96           O  
ATOM   1941  CB  ILE A 258      23.326  37.397   1.826  1.00 44.67           C  
ATOM   1942  CG1 ILE A 258      23.898  36.259   0.974  1.00 42.87           C  
ATOM   1943  CG2 ILE A 258      24.438  38.372   2.211  1.00 38.18           C  
ATOM   1944  CD1 ILE A 258      23.804  36.497  -0.510  1.00 34.91           C  
ATOM   1945  N   ALA A 259      21.076  38.455   4.052  1.00 46.58           N  
ATOM   1946  CA  ALA A 259      20.735  39.516   4.986  1.00 48.99           C  
ATOM   1947  C   ALA A 259      20.607  38.990   6.414  1.00 54.16           C  
ATOM   1948  O   ALA A 259      20.930  39.715   7.368  1.00 64.34           O  
ATOM   1949  CB  ALA A 259      19.446  40.213   4.543  1.00 45.53           C  
ATOM   1950  N   ILE A 260      20.159  37.735   6.582  1.00 49.14           N  
ATOM   1951  CA  ILE A 260      20.035  37.168   7.929  1.00 54.20           C  
ATOM   1952  C   ILE A 260      21.353  37.224   8.688  1.00 61.01           C  
ATOM   1953  O   ILE A 260      21.374  37.775   9.804  1.00 67.16           O  
ATOM   1954  CB  ILE A 260      19.444  35.746   7.856  1.00 47.89           C  
ATOM   1955  CG1 ILE A 260      17.993  35.792   7.381  1.00 41.34           C  
ATOM   1956  CG2 ILE A 260      19.492  35.069   9.220  1.00 56.02           C  
ATOM   1957  CD1 ILE A 260      17.371  34.437   7.271  1.00 45.49           C  
ATOM   1958  N   PRO A 261      22.478  36.719   8.166  1.00 62.99           N  
ATOM   1959  CA  PRO A 261      23.727  36.881   8.922  1.00 63.88           C  
ATOM   1960  C   PRO A 261      24.111  38.341   9.104  1.00 61.60           C  
ATOM   1961  O   PRO A 261      24.343  38.767  10.240  1.00 66.65           O  
ATOM   1962  CB  PRO A 261      24.758  36.113   8.073  1.00 57.88           C  
ATOM   1963  CG  PRO A 261      23.977  35.168   7.267  1.00 54.08           C  
ATOM   1964  CD  PRO A 261      22.687  35.885   6.969  1.00 49.19           C  
ATOM   1965  N   VAL A 262      24.153  39.116   8.011  1.00 61.00           N  
ATOM   1966  CA  VAL A 262      24.514  40.531   8.082  1.00 61.86           C  
ATOM   1967  C   VAL A 262      23.749  41.231   9.202  1.00 66.20           C  
ATOM   1968  O   VAL A 262      24.328  41.985   9.996  1.00 72.06           O  
ATOM   1969  CB  VAL A 262      24.285  41.210   6.720  1.00 54.93           C  
ATOM   1970  CG1 VAL A 262      24.452  42.728   6.836  1.00 58.41           C  
ATOM   1971  CG2 VAL A 262      25.258  40.643   5.697  1.00 52.52           C  
ATOM   1972  N   PHE A 263      22.450  40.946   9.324  1.00 68.70           N  
ATOM   1973  CA  PHE A 263      21.653  41.604  10.355  1.00 71.19           C  
ATOM   1974  C   PHE A 263      22.026  41.122  11.751  1.00 73.91           C  
ATOM   1975  O   PHE A 263      22.085  41.925  12.689  1.00 81.95           O  
ATOM   1976  CB  PHE A 263      20.161  41.406  10.090  1.00 61.88           C  
ATOM   1977  CG  PHE A 263      19.568  42.462   9.194  1.00 73.25           C  
ATOM   1978  CD1 PHE A 263      20.168  43.706   9.080  1.00 77.68           C  
ATOM   1979  CD2 PHE A 263      18.417  42.211   8.462  1.00 79.55           C  
ATOM   1980  CE1 PHE A 263      19.636  44.680   8.259  1.00 83.18           C  
ATOM   1981  CE2 PHE A 263      17.879  43.182   7.637  1.00 77.55           C  
ATOM   1982  CZ  PHE A 263      18.489  44.418   7.535  1.00 81.49           C  
ATOM   1983  N   TYR A 264      22.281  39.821  11.911  1.00 73.85           N  
ATOM   1984  CA  TYR A 264      22.803  39.317  13.179  1.00 74.42           C  
ATOM   1985  C   TYR A 264      24.152  39.948  13.509  1.00 75.55           C  
ATOM   1986  O   TYR A 264      24.398  40.340  14.656  1.00 73.10           O  
ATOM   1987  CB  TYR A 264      22.936  37.795  13.135  1.00 70.19           C  
ATOM   1988  CG  TYR A 264      21.639  37.005  13.136  1.00 80.14           C  
ATOM   1989  CD1 TYR A 264      21.655  35.623  13.279  1.00 84.49           C  
ATOM   1990  CD2 TYR A 264      20.406  37.628  12.990  1.00 90.37           C  
ATOM   1991  CE1 TYR A 264      20.478  34.882  13.284  1.00 92.47           C  
ATOM   1992  CE2 TYR A 264      19.225  36.894  12.992  1.00 95.03           C  
ATOM   1993  CZ  TYR A 264      19.266  35.522  13.140  1.00 96.39           C  
ATOM   1994  OH  TYR A 264      18.095  34.791  13.143  1.00 85.26           O  
ATOM   1995  N   PHE A 265      25.042  40.047  12.518  1.00 84.31           N  
ATOM   1996  CA  PHE A 265      26.349  40.656  12.756  1.00 86.73           C  
ATOM   1997  C   PHE A 265      26.210  42.123  13.146  1.00 86.73           C  
ATOM   1998  O   PHE A 265      26.739  42.552  14.176  1.00 89.77           O  
ATOM   1999  CB  PHE A 265      27.247  40.514  11.524  1.00 80.14           C  
ATOM   2000  CG  PHE A 265      27.729  39.107  11.273  1.00 87.82           C  
ATOM   2001  CD1 PHE A 265      28.649  38.499  12.116  1.00 86.00           C  
ATOM   2002  CD2 PHE A 265      27.267  38.398  10.181  1.00 90.38           C  
ATOM   2003  CE1 PHE A 265      29.086  37.202  11.869  1.00 84.24           C  
ATOM   2004  CE2 PHE A 265      27.694  37.108   9.936  1.00 91.78           C  
ATOM   2005  CZ  PHE A 265      28.606  36.511  10.780  1.00 86.36           C  
ATOM   2006  N   ALA A 266      25.508  42.913  12.326  1.00 82.89           N  
ATOM   2007  CA  ALA A 266      25.271  44.309  12.682  1.00 82.34           C  
ATOM   2008  C   ALA A 266      24.534  44.431  14.009  1.00 85.22           C  
ATOM   2009  O   ALA A 266      24.710  45.418  14.730  1.00 89.76           O  
ATOM   2010  CB  ALA A 266      24.489  45.014  11.574  1.00 65.40           C  
ATOM   2011  N   TRP A 267      23.715  43.435  14.349  1.00 87.07           N  
ATOM   2012  CA  TRP A 267      23.022  43.417  15.635  1.00 93.63           C  
ATOM   2013  C   TRP A 267      24.014  43.353  16.792  1.00 96.85           C  
ATOM   2014  O   TRP A 267      24.010  44.210  17.685  1.00 94.55           O  
ATOM   2015  CB  TRP A 267      22.058  42.224  15.658  1.00 96.19           C  
ATOM   2016  CG  TRP A 267      21.218  41.984  16.883  1.00 96.87           C  
ATOM   2017  CD1 TRP A 267      21.465  42.389  18.165  1.00 93.82           C  
ATOM   2018  CD2 TRP A 267      19.991  41.244  16.928  1.00104.55           C  
ATOM   2019  NE1 TRP A 267      20.462  41.951  19.001  1.00 94.25           N  
ATOM   2020  CE2 TRP A 267      19.545  41.247  18.264  1.00101.71           C  
ATOM   2021  CE3 TRP A 267      19.222  40.583  15.963  1.00101.85           C  
ATOM   2022  CZ2 TRP A 267      18.363  40.614  18.660  1.00100.94           C  
ATOM   2023  CZ3 TRP A 267      18.050  39.955  16.358  1.00 92.67           C  
ATOM   2024  CH2 TRP A 267      17.633  39.975  17.692  1.00 94.37           C  
ATOM   2025  N   MET A 268      24.872  42.327  16.795  1.00 99.56           N  
ATOM   2026  CA  MET A 268      25.809  42.116  17.895  1.00 97.18           C  
ATOM   2027  C   MET A 268      26.868  43.209  17.988  1.00 95.96           C  
ATOM   2028  O   MET A 268      27.519  43.334  19.031  1.00 92.52           O  
ATOM   2029  CB  MET A 268      26.484  40.745  17.762  1.00 99.08           C  
ATOM   2030  CG  MET A 268      25.571  39.554  18.057  1.00105.73           C  
ATOM   2031  SD  MET A 268      26.457  37.989  18.207  1.00203.58           S  
ATOM   2032  CE  MET A 268      27.470  38.293  19.646  1.00101.41           C  
ATOM   2033  N   ILE A 269      27.057  44.002  16.934  1.00 95.93           N  
ATOM   2034  CA  ILE A 269      27.929  45.170  17.000  1.00 96.37           C  
ATOM   2035  C   ILE A 269      27.086  46.351  17.472  1.00100.01           C  
ATOM   2036  O   ILE A 269      27.363  47.510  17.140  1.00 99.33           O  
ATOM   2037  CB  ILE A 269      28.611  45.442  15.643  1.00 94.48           C  
ATOM   2038  CG1 ILE A 269      29.191  44.146  15.086  1.00 91.46           C  
ATOM   2039  CG2 ILE A 269      29.776  46.418  15.784  1.00 92.18           C  
ATOM   2040  CD1 ILE A 269      30.293  43.563  15.945  1.00 96.58           C  
ATOM   2041  N   SER A 270      26.046  46.061  18.251  1.00101.03           N  
ATOM   2042  CA  SER A 270      25.194  47.093  18.837  1.00 92.53           C  
ATOM   2043  C   SER A 270      24.378  46.548  20.010  1.00 92.10           C  
ATOM   2044  O   SER A 270      24.917  45.936  20.931  1.00 79.39           O  
ATOM   2045  CB  SER A 270      24.264  47.679  17.774  1.00 93.06           C  
ATOM   2046  OG  SER A 270      25.006  48.376  16.790  1.00 94.16           O  
ATOM   2047  N   THR A 277      32.074  46.209  24.857  1.00105.90           N  
ATOM   2048  CA  THR A 277      32.245  45.231  25.923  1.00100.74           C  
ATOM   2049  C   THR A 277      33.200  44.140  25.465  1.00101.30           C  
ATOM   2050  O   THR A 277      32.857  42.957  25.492  1.00 99.68           O  
ATOM   2051  CB  THR A 277      30.901  44.591  26.338  1.00 92.80           C  
ATOM   2052  OG1 THR A 277      30.431  43.723  25.300  1.00 90.74           O  
ATOM   2053  CG2 THR A 277      29.845  45.657  26.616  1.00106.47           C  
ATOM   2054  N   GLU A 278      34.410  44.545  25.073  1.00104.24           N  
ATOM   2055  CA  GLU A 278      35.311  43.698  24.289  1.00101.91           C  
ATOM   2056  C   GLU A 278      34.586  43.177  23.052  1.00103.00           C  
ATOM   2057  O   GLU A 278      34.606  41.987  22.730  1.00 96.70           O  
ATOM   2058  CB  GLU A 278      35.893  42.561  25.123  1.00 92.34           C  
ATOM   2059  CG  GLU A 278      36.797  43.056  26.237  1.00 93.80           C  
ATOM   2060  CD  GLU A 278      37.823  44.064  25.747  1.00 97.85           C  
ATOM   2061  OE1 GLU A 278      38.484  43.790  24.727  1.00 94.19           O  
ATOM   2062  OE2 GLU A 278      37.957  45.138  26.370  1.00 99.48           O  
ATOM   2063  N   HIS A 279      33.925  44.111  22.364  1.00104.76           N  
ATOM   2064  CA  HIS A 279      33.149  43.788  21.172  1.00 93.83           C  
ATOM   2065  C   HIS A 279      34.001  43.149  20.086  1.00 97.37           C  
ATOM   2066  O   HIS A 279      33.488  42.359  19.285  1.00 93.41           O  
ATOM   2067  CB  HIS A 279      32.496  45.058  20.629  1.00 92.59           C  
ATOM   2068  CG  HIS A 279      33.485  46.071  20.152  1.00112.28           C  
ATOM   2069  ND1 HIS A 279      34.099  45.986  18.920  1.00105.98           N  
ATOM   2070  CD2 HIS A 279      33.995  47.172  20.751  1.00124.05           C  
ATOM   2071  CE1 HIS A 279      34.934  46.998  18.773  1.00106.69           C  
ATOM   2072  NE2 HIS A 279      34.889  47.734  19.869  1.00119.58           N  
ATOM   2073  N   LEU A 280      35.294  43.477  20.034  1.00102.32           N  
ATOM   2074  CA  LEU A 280      36.134  43.041  18.923  1.00103.08           C  
ATOM   2075  C   LEU A 280      36.280  41.526  18.834  1.00 99.24           C  
ATOM   2076  O   LEU A 280      36.797  41.041  17.825  1.00102.70           O  
ATOM   2077  CB  LEU A 280      37.520  43.707  19.002  1.00101.45           C  
ATOM   2078  CG  LEU A 280      38.389  43.552  20.257  1.00 95.58           C  
ATOM   2079  CD1 LEU A 280      39.221  42.274  20.220  1.00 96.33           C  
ATOM   2080  CD2 LEU A 280      39.284  44.772  20.481  1.00 97.44           C  
ATOM   2081  N   ARG A 281      35.847  40.770  19.844  1.00 92.94           N  
ATOM   2082  CA  ARG A 281      35.769  39.324  19.675  1.00 89.52           C  
ATOM   2083  C   ARG A 281      34.776  38.976  18.575  1.00 93.77           C  
ATOM   2084  O   ARG A 281      35.040  38.106  17.736  1.00 94.61           O  
ATOM   2085  CB  ARG A 281      35.399  38.652  21.000  1.00 77.04           C  
ATOM   2086  N   VAL A 282      33.648  39.690  18.535  1.00 89.39           N  
ATOM   2087  CA  VAL A 282      32.685  39.527  17.445  1.00 86.04           C  
ATOM   2088  C   VAL A 282      33.316  39.942  16.123  1.00 83.59           C  
ATOM   2089  O   VAL A 282      33.388  39.159  15.167  1.00 86.51           O  
ATOM   2090  CB  VAL A 282      31.405  40.335  17.720  1.00 86.79           C  
ATOM   2091  CG1 VAL A 282      30.324  39.945  16.710  1.00 87.03           C  
ATOM   2092  CG2 VAL A 282      30.928  40.123  19.133  1.00 85.17           C  
ATOM   2093  N   VAL A 283      33.816  41.174  16.076  1.00 87.85           N  
ATOM   2094  CA  VAL A 283      34.476  41.750  14.911  1.00 92.92           C  
ATOM   2095  C   VAL A 283      35.500  40.776  14.333  1.00 89.50           C  
ATOM   2096  O   VAL A 283      35.674  40.698  13.110  1.00 80.73           O  
ATOM   2097  CB  VAL A 283      35.122  43.104  15.286  1.00 89.25           C  
ATOM   2098  CG1 VAL A 283      36.511  43.267  14.654  1.00 90.01           C  
ATOM   2099  CG2 VAL A 283      34.211  44.258  14.883  1.00 81.11           C  
ATOM   2100  N   SER A 284      36.173  40.019  15.207  1.00 89.24           N  
ATOM   2101  CA  SER A 284      37.111  38.991  14.759  1.00 94.71           C  
ATOM   2102  C   SER A 284      36.441  37.951  13.862  1.00 81.80           C  
ATOM   2103  O   SER A 284      37.078  37.416  12.949  1.00 73.13           O  
ATOM   2104  CB  SER A 284      37.735  38.297  15.968  1.00 92.71           C  
ATOM   2105  OG  SER A 284      38.242  39.235  16.903  1.00110.24           O  
ATOM   2106  N   TYR A 285      35.167  37.654  14.107  1.00 76.60           N  
ATOM   2107  CA  TYR A 285      34.491  36.583  13.410  1.00 77.04           C  
ATOM   2108  C   TYR A 285      34.135  36.937  11.974  1.00 70.83           C  
ATOM   2109  O   TYR A 285      33.902  36.016  11.172  1.00 67.39           O  
ATOM   2110  CB  TYR A 285      33.223  36.198  14.175  1.00 70.55           C  
ATOM   2111  CG  TYR A 285      32.627  34.885  13.743  1.00 74.78           C  
ATOM   2112  CD1 TYR A 285      31.390  34.833  13.120  1.00 78.37           C  
ATOM   2113  CD2 TYR A 285      33.315  33.691  13.940  1.00 83.88           C  
ATOM   2114  CE1 TYR A 285      30.849  33.636  12.714  1.00 93.61           C  
ATOM   2115  CE2 TYR A 285      32.779  32.487  13.534  1.00 82.98           C  
ATOM   2116  CZ  TYR A 285      31.546  32.468  12.922  1.00 88.58           C  
ATOM   2117  OH  TYR A 285      30.996  31.280  12.512  1.00 90.16           O  
ATOM   2118  N   ILE A 286      34.092  38.229  11.623  1.00 62.30           N  
ATOM   2119  CA  ILE A 286      33.722  38.609  10.257  1.00 62.01           C  
ATOM   2120  C   ILE A 286      34.642  37.956   9.233  1.00 66.17           C  
ATOM   2121  O   ILE A 286      34.135  37.279   8.320  1.00 60.27           O  
ATOM   2122  CB  ILE A 286      33.662  40.137  10.127  1.00 68.05           C  
ATOM   2123  CG1 ILE A 286      32.743  40.727  11.214  1.00 69.72           C  
ATOM   2124  CG2 ILE A 286      33.207  40.552   8.726  1.00 62.77           C  
ATOM   2125  CD1 ILE A 286      31.261  40.400  11.041  1.00 62.23           C  
ATOM   2126  N   PRO A 287      35.974  38.077   9.321  1.00 69.13           N  
ATOM   2127  CA  PRO A 287      36.799  37.344   8.353  1.00 68.64           C  
ATOM   2128  C   PRO A 287      36.620  35.839   8.445  1.00 62.68           C  
ATOM   2129  O   PRO A 287      36.608  35.159   7.411  1.00 64.27           O  
ATOM   2130  CB  PRO A 287      38.235  37.774   8.706  1.00 62.02           C  
ATOM   2131  CG  PRO A 287      38.096  39.059   9.418  1.00 63.25           C  
ATOM   2132  CD  PRO A 287      36.816  38.909  10.204  1.00 65.77           C  
ATOM   2133  N   LEU A 288      36.462  35.302   9.658  1.00 56.83           N  
ATOM   2134  CA  LEU A 288      36.231  33.870   9.812  1.00 62.02           C  
ATOM   2135  C   LEU A 288      34.923  33.443   9.156  1.00 65.74           C  
ATOM   2136  O   LEU A 288      34.855  32.385   8.519  1.00 62.06           O  
ATOM   2137  CB  LEU A 288      36.234  33.496  11.295  1.00 64.26           C  
ATOM   2138  CG  LEU A 288      37.577  33.607  12.021  1.00 66.87           C  
ATOM   2139  CD1 LEU A 288      37.570  32.773  13.297  1.00 64.72           C  
ATOM   2140  CD2 LEU A 288      38.726  33.197  11.109  1.00 65.50           C  
ATOM   2141  N   PHE A 289      33.872  34.252   9.298  1.00 64.81           N  
ATOM   2142  CA  PHE A 289      32.597  33.916   8.674  1.00 58.29           C  
ATOM   2143  C   PHE A 289      32.682  34.037   7.158  1.00 56.90           C  
ATOM   2144  O   PHE A 289      32.244  33.139   6.429  1.00 52.24           O  
ATOM   2145  CB  PHE A 289      31.484  34.807   9.226  1.00 53.85           C  
ATOM   2146  CG  PHE A 289      30.106  34.359   8.835  1.00 57.29           C  
ATOM   2147  CD1 PHE A 289      29.460  33.362   9.551  1.00 55.70           C  
ATOM   2148  CD2 PHE A 289      29.452  34.934   7.757  1.00 48.33           C  
ATOM   2149  CE1 PHE A 289      28.190  32.948   9.199  1.00 52.98           C  
ATOM   2150  CE2 PHE A 289      28.182  34.525   7.400  1.00 38.60           C  
ATOM   2151  CZ  PHE A 289      27.550  33.532   8.120  1.00 50.92           C  
ATOM   2152  N   ILE A 290      33.239  35.147   6.666  1.00 55.06           N  
ATOM   2153  CA  ILE A 290      33.390  35.327   5.225  1.00 56.44           C  
ATOM   2154  C   ILE A 290      34.212  34.191   4.632  1.00 56.20           C  
ATOM   2155  O   ILE A 290      33.922  33.703   3.533  1.00 49.08           O  
ATOM   2156  CB  ILE A 290      34.010  36.704   4.917  1.00 60.83           C  
ATOM   2157  CG1 ILE A 290      33.085  37.824   5.393  1.00 56.59           C  
ATOM   2158  CG2 ILE A 290      34.275  36.856   3.426  1.00 53.78           C  
ATOM   2159  CD1 ILE A 290      33.714  39.192   5.330  1.00 58.04           C  
ATOM   2160  N   ALA A 291      35.234  33.734   5.361  1.00 52.82           N  
ATOM   2161  CA  ALA A 291      36.034  32.612   4.881  1.00 44.47           C  
ATOM   2162  C   ALA A 291      35.199  31.346   4.777  1.00 52.25           C  
ATOM   2163  O   ALA A 291      35.345  30.573   3.822  1.00 57.14           O  
ATOM   2164  CB  ALA A 291      37.229  32.380   5.801  1.00 50.56           C  
ATOM   2165  N   ALA A 292      34.317  31.114   5.751  1.00 51.56           N  
ATOM   2166  CA  ALA A 292      33.480  29.920   5.716  1.00 48.08           C  
ATOM   2167  C   ALA A 292      32.483  29.981   4.566  1.00 45.43           C  
ATOM   2168  O   ALA A 292      32.222  28.966   3.910  1.00 41.41           O  
ATOM   2169  CB  ALA A 292      32.759  29.748   7.052  1.00 46.64           C  
ATOM   2170  N   VAL A 293      31.929  31.166   4.298  1.00 45.21           N  
ATOM   2171  CA  VAL A 293      30.954  31.314   3.221  1.00 40.55           C  
ATOM   2172  C   VAL A 293      31.587  31.000   1.870  1.00 43.20           C  
ATOM   2173  O   VAL A 293      31.002  30.288   1.045  1.00 39.43           O  
ATOM   2174  CB  VAL A 293      30.341  32.726   3.254  1.00 33.50           C  
ATOM   2175  CG1 VAL A 293      29.642  33.042   1.944  1.00 34.14           C  
ATOM   2176  CG2 VAL A 293      29.370  32.849   4.418  1.00 41.24           C  
ATOM   2177  N   LEU A 294      32.792  31.513   1.620  1.00 46.09           N  
ATOM   2178  CA  LEU A 294      33.415  31.283   0.321  1.00 45.78           C  
ATOM   2179  C   LEU A 294      33.854  29.834   0.163  1.00 45.01           C  
ATOM   2180  O   LEU A 294      33.816  29.290  -0.948  1.00 39.55           O  
ATOM   2181  CB  LEU A 294      34.597  32.228   0.123  1.00 49.07           C  
ATOM   2182  CG  LEU A 294      34.221  33.705   0.223  1.00 49.41           C  
ATOM   2183  CD1 LEU A 294      35.457  34.576   0.182  1.00 53.16           C  
ATOM   2184  CD2 LEU A 294      33.247  34.088  -0.878  1.00 41.33           C  
ATOM   2185  N   PHE A 295      34.279  29.193   1.253  1.00 40.61           N  
ATOM   2186  CA  PHE A 295      34.641  27.784   1.158  1.00 41.33           C  
ATOM   2187  C   PHE A 295      33.426  26.937   0.814  1.00 39.46           C  
ATOM   2188  O   PHE A 295      33.462  26.119  -0.115  1.00 32.47           O  
ATOM   2189  CB  PHE A 295      35.270  27.280   2.456  1.00 50.39           C  
ATOM   2190  CG  PHE A 295      35.421  25.788   2.483  1.00 49.21           C  
ATOM   2191  CD1 PHE A 295      36.511  25.186   1.884  1.00 41.06           C  
ATOM   2192  CD2 PHE A 295      34.449  24.985   3.062  1.00 45.01           C  
ATOM   2193  CE1 PHE A 295      36.643  23.819   1.878  1.00 45.70           C  
ATOM   2194  CE2 PHE A 295      34.576  23.616   3.055  1.00 41.58           C  
ATOM   2195  CZ  PHE A 295      35.672  23.035   2.460  1.00 44.58           C  
ATOM   2196  N   TRP A 296      32.343  27.104   1.576  1.00 35.96           N  
ATOM   2197  CA  TRP A 296      31.128  26.348   1.309  1.00 40.04           C  
ATOM   2198  C   TRP A 296      30.586  26.636  -0.082  1.00 36.07           C  
ATOM   2199  O   TRP A 296      30.024  25.742  -0.720  1.00 39.20           O  
ATOM   2200  CB  TRP A 296      30.077  26.649   2.377  1.00 38.75           C  
ATOM   2201  CG  TRP A 296      30.402  26.051   3.717  1.00 46.84           C  
ATOM   2202  CD1 TRP A 296      30.583  26.718   4.894  1.00 46.76           C  
ATOM   2203  CD2 TRP A 296      30.592  24.663   4.011  1.00 49.19           C  
ATOM   2204  NE1 TRP A 296      30.869  25.832   5.902  1.00 48.81           N  
ATOM   2205  CE2 TRP A 296      30.881  24.563   5.386  1.00 46.93           C  
ATOM   2206  CE3 TRP A 296      30.543  23.493   3.245  1.00 46.26           C  
ATOM   2207  CZ2 TRP A 296      31.122  23.341   6.011  1.00 49.20           C  
ATOM   2208  CZ3 TRP A 296      30.782  22.281   3.867  1.00 51.28           C  
ATOM   2209  CH2 TRP A 296      31.067  22.214   5.236  1.00 47.40           C  
ATOM   2210  N   ALA A 297      30.768  27.862  -0.578  1.00 33.24           N  
ATOM   2211  CA  ALA A 297      30.375  28.164  -1.948  1.00 32.11           C  
ATOM   2212  C   ALA A 297      31.080  27.237  -2.930  1.00 36.43           C  
ATOM   2213  O   ALA A 297      30.437  26.606  -3.777  1.00 35.37           O  
ATOM   2214  CB  ALA A 297      30.674  29.627  -2.269  1.00 23.26           C  
ATOM   2215  N   ILE A 298      32.403  27.118  -2.810  1.00 36.46           N  
ATOM   2216  CA  ILE A 298      33.160  26.260  -3.718  1.00 35.40           C  
ATOM   2217  C   ILE A 298      32.785  24.797  -3.509  1.00 36.20           C  
ATOM   2218  O   ILE A 298      32.573  24.049  -4.472  1.00 42.62           O  
ATOM   2219  CB  ILE A 298      34.671  26.487  -3.533  1.00 36.60           C  
ATOM   2220  CG1 ILE A 298      35.042  27.914  -3.930  1.00 36.84           C  
ATOM   2221  CG2 ILE A 298      35.470  25.482  -4.351  1.00 31.96           C  
ATOM   2222  CD1 ILE A 298      36.469  28.265  -3.611  1.00 38.59           C  
ATOM   2223  N   GLU A 299      32.694  24.369  -2.248  1.00 31.87           N  
ATOM   2224  CA  GLU A 299      32.405  22.968  -1.958  1.00 34.11           C  
ATOM   2225  C   GLU A 299      31.000  22.579  -2.400  1.00 32.44           C  
ATOM   2226  O   GLU A 299      30.780  21.442  -2.836  1.00 36.73           O  
ATOM   2227  CB  GLU A 299      32.600  22.697  -0.462  1.00 37.69           C  
ATOM   2228  CG  GLU A 299      32.452  21.241  -0.038  1.00 40.05           C  
ATOM   2229  CD  GLU A 299      31.006  20.834   0.188  1.00 42.61           C  
ATOM   2230  OE1 GLU A 299      30.210  21.685   0.636  1.00 43.58           O  
ATOM   2231  OE2 GLU A 299      30.664  19.667  -0.093  1.00 43.10           O  
ATOM   2232  N   GLU A 300      30.039  23.496  -2.296  1.00 42.31           N  
ATOM   2233  CA  GLU A 300      28.681  23.199  -2.730  1.00 36.73           C  
ATOM   2234  C   GLU A 300      28.482  23.370  -4.231  1.00 31.35           C  
ATOM   2235  O   GLU A 300      27.428  22.980  -4.745  1.00 28.79           O  
ATOM   2236  CB  GLU A 300      27.678  24.066  -1.963  1.00 33.41           C  
ATOM   2237  CG  GLU A 300      27.100  23.372  -0.739  1.00 44.19           C  
ATOM   2238  CD  GLU A 300      26.263  22.160  -1.111  1.00 56.00           C  
ATOM   2239  OE1 GLU A 300      25.363  22.301  -1.967  1.00 60.60           O  
ATOM   2240  OE2 GLU A 300      26.510  21.066  -0.561  1.00 54.64           O  
ATOM   2241  N   GLN A 301      29.462  23.924  -4.947  1.00 34.13           N  
ATOM   2242  CA  GLN A 301      29.390  23.971  -6.401  1.00 36.12           C  
ATOM   2243  C   GLN A 301      29.747  22.644  -7.057  1.00 36.18           C  
ATOM   2244  O   GLN A 301      29.553  22.500  -8.270  1.00 31.59           O  
ATOM   2245  CB  GLN A 301      30.296  25.077  -6.941  1.00 27.94           C  
ATOM   2246  CG  GLN A 301      29.594  26.412  -7.017  1.00 37.74           C  
ATOM   2247  CD  GLN A 301      30.546  27.567  -7.207  1.00 36.63           C  
ATOM   2248  OE1 GLN A 301      31.751  27.378  -7.317  1.00 53.15           O  
ATOM   2249  NE2 GLN A 301      30.007  28.777  -7.235  1.00 32.36           N  
ATOM   2250  N   GLY A 302      30.260  21.676  -6.293  1.00 25.72           N  
ATOM   2251  CA  GLY A 302      30.511  20.362  -6.855  1.00 25.50           C  
ATOM   2252  C   GLY A 302      29.240  19.671  -7.304  1.00 33.89           C  
ATOM   2253  O   GLY A 302      29.248  18.915  -8.279  1.00 33.44           O  
ATOM   2254  N   SER A 303      28.131  19.924  -6.604  1.00 34.79           N  
ATOM   2255  CA  SER A 303      26.839  19.398  -7.022  1.00 27.52           C  
ATOM   2256  C   SER A 303      26.308  20.105  -8.258  1.00 32.09           C  
ATOM   2257  O   SER A 303      25.397  19.585  -8.912  1.00 28.42           O  
ATOM   2258  CB  SER A 303      25.824  19.533  -5.887  1.00 28.10           C  
ATOM   2259  OG  SER A 303      26.319  18.990  -4.676  1.00 70.32           O  
ATOM   2260  N   VAL A 304      26.856  21.275  -8.587  1.00 29.04           N  
ATOM   2261  CA  VAL A 304      26.328  22.128  -9.645  1.00 28.64           C  
ATOM   2262  C   VAL A 304      27.355  22.248 -10.763  1.00 34.92           C  
ATOM   2263  O   VAL A 304      27.241  21.582 -11.796  1.00 35.30           O  
ATOM   2264  CB  VAL A 304      25.945  23.515  -9.092  1.00 35.92           C  
ATOM   2265  CG1 VAL A 304      25.132  24.292 -10.109  1.00 33.24           C  
ATOM   2266  CG2 VAL A 304      25.182  23.383  -7.781  1.00 27.00           C  
ATOM   2267  N   VAL A 305      28.371  23.086 -10.554  1.00 29.15           N  
ATOM   2268  CA  VAL A 305      29.346  23.371 -11.605  1.00 28.42           C  
ATOM   2269  C   VAL A 305      30.159  22.126 -11.947  1.00 33.41           C  
ATOM   2270  O   VAL A 305      30.349  21.794 -13.123  1.00 36.09           O  
ATOM   2271  CB  VAL A 305      30.251  24.545 -11.187  1.00 28.84           C  
ATOM   2272  CG1 VAL A 305      31.484  24.619 -12.079  1.00 28.23           C  
ATOM   2273  CG2 VAL A 305      29.472  25.850 -11.237  1.00 30.39           C  
ATOM   2274  N   LEU A 306      30.661  21.423 -10.933  1.00 34.39           N  
ATOM   2275  CA  LEU A 306      31.447  20.226 -11.219  1.00 36.55           C  
ATOM   2276  C   LEU A 306      30.582  19.111 -11.799  1.00 34.74           C  
ATOM   2277  O   LEU A 306      31.070  18.302 -12.599  1.00 32.72           O  
ATOM   2278  CB  LEU A 306      32.173  19.754  -9.959  1.00 34.75           C  
ATOM   2279  CG  LEU A 306      33.625  20.203  -9.767  1.00 28.55           C  
ATOM   2280  CD1 LEU A 306      33.804  21.678 -10.080  1.00 28.76           C  
ATOM   2281  CD2 LEU A 306      34.093  19.891  -8.351  1.00 21.97           C  
ATOM   2282  N   ALA A 307      29.302  19.058 -11.424  1.00 26.26           N  
ATOM   2283  CA  ALA A 307      28.396  18.092 -12.039  1.00 28.97           C  
ATOM   2284  C   ALA A 307      28.177  18.400 -13.514  1.00 31.47           C  
ATOM   2285  O   ALA A 307      28.108  17.482 -14.340  1.00 28.36           O  
ATOM   2286  CB  ALA A 307      27.062  18.069 -11.295  1.00 22.51           C  
ATOM   2287  N   THR A 308      28.053  19.683 -13.862  1.00 30.66           N  
ATOM   2288  CA  THR A 308      27.939  20.063 -15.266  1.00 30.00           C  
ATOM   2289  C   THR A 308      29.192  19.667 -16.035  1.00 33.19           C  
ATOM   2290  O   THR A 308      29.113  19.113 -17.137  1.00 34.32           O  
ATOM   2291  CB  THR A 308      27.695  21.569 -15.403  1.00 31.01           C  
ATOM   2292  OG1 THR A 308      28.805  22.281 -14.851  1.00 57.32           O  
ATOM   2293  CG2 THR A 308      26.449  21.996 -14.669  1.00 32.91           C  
ATOM   2294  N   PHE A 309      30.363  19.956 -15.464  1.00 30.14           N  
ATOM   2295  CA  PHE A 309      31.619  19.608 -16.118  1.00 30.28           C  
ATOM   2296  C   PHE A 309      31.703  18.110 -16.381  1.00 32.76           C  
ATOM   2297  O   PHE A 309      32.093  17.685 -17.474  1.00 32.66           O  
ATOM   2298  CB  PHE A 309      32.792  20.082 -15.259  1.00 31.78           C  
ATOM   2299  CG  PHE A 309      34.139  19.914 -15.908  1.00 32.56           C  
ATOM   2300  CD1 PHE A 309      34.805  18.700 -15.851  1.00 32.49           C  
ATOM   2301  CD2 PHE A 309      34.748  20.977 -16.554  1.00 31.67           C  
ATOM   2302  CE1 PHE A 309      36.040  18.545 -16.441  1.00 36.02           C  
ATOM   2303  CE2 PHE A 309      35.987  20.831 -17.140  1.00 28.53           C  
ATOM   2304  CZ  PHE A 309      36.634  19.611 -17.087  1.00 33.30           C  
ATOM   2305  N   ALA A 310      31.326  17.294 -15.395  1.00 35.73           N  
ATOM   2306  CA  ALA A 310      31.397  15.847 -15.566  1.00 35.43           C  
ATOM   2307  C   ALA A 310      30.534  15.380 -16.733  1.00 31.77           C  
ATOM   2308  O   ALA A 310      30.945  14.508 -17.509  1.00 30.31           O  
ATOM   2309  CB  ALA A 310      30.982  15.152 -14.271  1.00 24.75           C  
ATOM   2310  N   ALA A 311      29.341  15.962 -16.885  1.00 30.07           N  
ATOM   2311  CA  ALA A 311      28.424  15.525 -17.934  1.00 30.95           C  
ATOM   2312  C   ALA A 311      28.824  16.057 -19.305  1.00 31.52           C  
ATOM   2313  O   ALA A 311      28.771  15.324 -20.298  1.00 39.10           O  
ATOM   2314  CB  ALA A 311      27.000  15.961 -17.597  1.00 25.95           C  
ATOM   2315  N   GLU A 312      29.235  17.319 -19.383  1.00 30.55           N  
ATOM   2316  CA  GLU A 312      29.494  17.948 -20.671  1.00 30.29           C  
ATOM   2317  C   GLU A 312      30.924  17.772 -21.154  1.00 35.82           C  
ATOM   2318  O   GLU A 312      31.170  17.869 -22.358  1.00 36.69           O  
ATOM   2319  CB  GLU A 312      29.197  19.448 -20.601  1.00 26.71           C  
ATOM   2320  CG  GLU A 312      27.724  19.831 -20.502  1.00 35.56           C  
ATOM   2321  CD  GLU A 312      27.538  21.332 -20.324  1.00 52.49           C  
ATOM   2322  OE1 GLU A 312      28.483  21.992 -19.837  1.00 51.59           O  
ATOM   2323  OE2 GLU A 312      26.458  21.855 -20.675  1.00 60.68           O  
ATOM   2324  N   ARG A 313      31.862  17.497 -20.256  1.00 37.09           N  
ATOM   2325  CA  ARG A 313      33.262  17.776 -20.520  1.00 32.99           C  
ATOM   2326  C   ARG A 313      34.202  16.630 -20.161  1.00 37.96           C  
ATOM   2327  O   ARG A 313      35.391  16.703 -20.480  1.00 32.05           O  
ATOM   2328  CB  ARG A 313      33.656  19.059 -19.765  1.00 33.66           C  
ATOM   2329  CG  ARG A 313      34.996  19.641 -20.100  1.00 46.10           C  
ATOM   2330  CD  ARG A 313      34.957  20.761 -21.121  1.00 41.01           C  
ATOM   2331  NE  ARG A 313      36.252  21.434 -21.106  1.00 40.87           N  
ATOM   2332  CZ  ARG A 313      37.361  20.918 -21.624  1.00 38.04           C  
ATOM   2333  NH1 ARG A 313      37.331  19.733 -22.222  1.00 41.03           N  
ATOM   2334  NH2 ARG A 313      38.501  21.586 -21.550  1.00 45.88           N  
ATOM   2335  N   VAL A 314      33.708  15.572 -19.527  1.00 42.86           N  
ATOM   2336  CA  VAL A 314      34.510  14.402 -19.189  1.00 43.38           C  
ATOM   2337  C   VAL A 314      34.049  13.245 -20.064  1.00 39.92           C  
ATOM   2338  O   VAL A 314      32.842  13.014 -20.207  1.00 49.17           O  
ATOM   2339  CB  VAL A 314      34.398  14.057 -17.693  1.00 41.99           C  
ATOM   2340  CG1 VAL A 314      34.842  12.625 -17.423  1.00 33.94           C  
ATOM   2341  CG2 VAL A 314      35.227  15.031 -16.877  1.00 40.62           C  
ATOM   2342  N   ASP A 315      35.004  12.537 -20.672  1.00 42.95           N  
ATOM   2343  CA  ASP A 315      34.681  11.345 -21.458  1.00 62.15           C  
ATOM   2344  C   ASP A 315      34.420  10.200 -20.482  1.00 63.57           C  
ATOM   2345  O   ASP A 315      35.259   9.332 -20.230  1.00 65.76           O  
ATOM   2346  CB  ASP A 315      35.777  11.023 -22.472  1.00 69.47           C  
ATOM   2347  CG  ASP A 315      37.176  11.061 -21.879  1.00 63.72           C  
ATOM   2348  OD1 ASP A 315      37.317  11.042 -20.639  1.00 61.41           O  
ATOM   2349  OD2 ASP A 315      38.150  11.111 -22.665  1.00 64.95           O  
ATOM   2350  N   SER A 316      33.222  10.226 -19.907  1.00 55.26           N  
ATOM   2351  CA  SER A 316      32.717   9.214 -18.982  1.00 59.56           C  
ATOM   2352  C   SER A 316      31.542   8.526 -19.667  1.00 59.18           C  
ATOM   2353  O   SER A 316      30.379   8.774 -19.344  1.00 59.32           O  
ATOM   2354  CB  SER A 316      32.305   9.842 -17.657  1.00 60.94           C  
ATOM   2355  OG  SER A 316      31.204  10.717 -17.835  1.00 63.38           O  
ATOM   2356  N   SER A 317      31.852   7.665 -20.633  1.00 53.11           N  
ATOM   2357  CA  SER A 317      30.827   6.936 -21.364  1.00 50.51           C  
ATOM   2358  C   SER A 317      30.677   5.494 -20.900  1.00 50.37           C  
ATOM   2359  O   SER A 317      29.748   4.813 -21.346  1.00 54.62           O  
ATOM   2360  CB  SER A 317      31.126   6.966 -22.869  1.00 48.83           C  
ATOM   2361  OG  SER A 317      32.514   6.827 -23.117  1.00 50.34           O  
ATOM   2362  N   TRP A 318      31.552   5.018 -20.016  1.00 49.15           N  
ATOM   2363  CA  TRP A 318      31.467   3.666 -19.484  1.00 45.51           C  
ATOM   2364  C   TRP A 318      30.861   3.602 -18.085  1.00 50.29           C  
ATOM   2365  O   TRP A 318      30.797   2.512 -17.509  1.00 52.89           O  
ATOM   2366  CB  TRP A 318      32.855   3.006 -19.484  1.00 48.57           C  
ATOM   2367  CG  TRP A 318      33.941   3.768 -18.750  1.00 49.62           C  
ATOM   2368  CD1 TRP A 318      34.765   4.728 -19.268  1.00 46.11           C  
ATOM   2369  CD2 TRP A 318      34.334   3.604 -17.379  1.00 57.11           C  
ATOM   2370  NE1 TRP A 318      35.635   5.178 -18.302  1.00 60.04           N  
ATOM   2371  CE2 TRP A 318      35.391   4.505 -17.134  1.00 62.32           C  
ATOM   2372  CE3 TRP A 318      33.889   2.789 -16.333  1.00 62.12           C  
ATOM   2373  CZ2 TRP A 318      36.007   4.614 -15.888  1.00 65.16           C  
ATOM   2374  CZ3 TRP A 318      34.504   2.899 -15.097  1.00 64.33           C  
ATOM   2375  CH2 TRP A 318      35.550   3.804 -14.885  1.00 66.45           C  
ATOM   2376  N   PHE A 319      30.411   4.724 -17.524  1.00 45.15           N  
ATOM   2377  CA  PHE A 319      29.808   4.713 -16.196  1.00 42.79           C  
ATOM   2378  C   PHE A 319      28.934   5.952 -16.042  1.00 37.79           C  
ATOM   2379  O   PHE A 319      29.152   6.960 -16.725  1.00 44.49           O  
ATOM   2380  CB  PHE A 319      30.879   4.658 -15.092  1.00 39.34           C  
ATOM   2381  CG  PHE A 319      31.642   5.938 -14.913  1.00 50.00           C  
ATOM   2382  CD1 PHE A 319      32.715   6.242 -15.735  1.00 60.07           C  
ATOM   2383  CD2 PHE A 319      31.300   6.829 -13.908  1.00 44.66           C  
ATOM   2384  CE1 PHE A 319      33.425   7.415 -15.564  1.00 54.61           C  
ATOM   2385  CE2 PHE A 319      32.001   8.007 -13.737  1.00 48.65           C  
ATOM   2386  CZ  PHE A 319      33.067   8.300 -14.565  1.00 56.63           C  
ATOM   2387  N   PRO A 320      27.938   5.906 -15.151  1.00 39.67           N  
ATOM   2388  CA  PRO A 320      27.059   7.068 -14.955  1.00 31.53           C  
ATOM   2389  C   PRO A 320      27.806   8.280 -14.416  1.00 34.33           C  
ATOM   2390  O   PRO A 320      28.593   8.188 -13.472  1.00 33.09           O  
ATOM   2391  CB  PRO A 320      26.022   6.558 -13.947  1.00 32.24           C  
ATOM   2392  CG  PRO A 320      26.030   5.085 -14.108  1.00 32.85           C  
ATOM   2393  CD  PRO A 320      27.453   4.725 -14.415  1.00 36.93           C  
ATOM   2394  N   VAL A 321      27.514   9.435 -15.014  1.00 41.41           N  
ATOM   2395  CA  VAL A 321      28.204  10.675 -14.677  1.00 31.73           C  
ATOM   2396  C   VAL A 321      27.902  11.114 -13.248  1.00 35.28           C  
ATOM   2397  O   VAL A 321      28.732  11.768 -12.601  1.00 33.25           O  
ATOM   2398  CB  VAL A 321      27.813  11.757 -15.698  1.00 30.78           C  
ATOM   2399  CG1 VAL A 321      28.462  13.059 -15.358  1.00 41.04           C  
ATOM   2400  CG2 VAL A 321      28.205  11.326 -17.097  1.00 52.78           C  
ATOM   2401  N   SER A 322      26.725  10.765 -12.726  1.00 28.74           N  
ATOM   2402  CA  SER A 322      26.367  11.172 -11.373  1.00 21.25           C  
ATOM   2403  C   SER A 322      27.273  10.550 -10.319  1.00 29.81           C  
ATOM   2404  O   SER A 322      27.304  11.036  -9.182  1.00 27.42           O  
ATOM   2405  CB  SER A 322      24.908  10.813 -11.091  1.00 27.78           C  
ATOM   2406  OG  SER A 322      24.576   9.572 -11.684  1.00 36.00           O  
ATOM   2407  N   TRP A 323      28.019   9.498 -10.675  1.00 31.55           N  
ATOM   2408  CA  TRP A 323      28.896   8.834  -9.715  1.00 27.20           C  
ATOM   2409  C   TRP A 323      30.000   9.745  -9.197  1.00 31.34           C  
ATOM   2410  O   TRP A 323      30.570   9.461  -8.138  1.00 30.42           O  
ATOM   2411  CB  TRP A 323      29.518   7.583 -10.335  1.00 33.75           C  
ATOM   2412  CG  TRP A 323      28.556   6.446 -10.478  1.00 38.07           C  
ATOM   2413  CD1 TRP A 323      27.219   6.465 -10.210  1.00 33.57           C  
ATOM   2414  CD2 TRP A 323      28.857   5.117 -10.922  1.00 33.05           C  
ATOM   2415  NE1 TRP A 323      26.667   5.234 -10.462  1.00 36.46           N  
ATOM   2416  CE2 TRP A 323      27.652   4.388 -10.899  1.00 36.64           C  
ATOM   2417  CE3 TRP A 323      30.027   4.474 -11.336  1.00 31.01           C  
ATOM   2418  CZ2 TRP A 323      27.583   3.048 -11.275  1.00 36.90           C  
ATOM   2419  CZ3 TRP A 323      29.958   3.145 -11.708  1.00 31.76           C  
ATOM   2420  CH2 TRP A 323      28.745   2.446 -11.676  1.00 30.98           C  
ATOM   2421  N   PHE A 324      30.319  10.829  -9.913  1.00 28.46           N  
ATOM   2422  CA  PHE A 324      31.330  11.763  -9.427  1.00 33.64           C  
ATOM   2423  C   PHE A 324      30.934  12.399  -8.101  1.00 35.49           C  
ATOM   2424  O   PHE A 324      31.812  12.840  -7.351  1.00 32.09           O  
ATOM   2425  CB  PHE A 324      31.593  12.859 -10.460  1.00 35.65           C  
ATOM   2426  CG  PHE A 324      32.433  12.414 -11.620  1.00 31.73           C  
ATOM   2427  CD1 PHE A 324      33.812  12.334 -11.505  1.00 29.63           C  
ATOM   2428  CD2 PHE A 324      31.846  12.097 -12.830  1.00 30.04           C  
ATOM   2429  CE1 PHE A 324      34.583  11.933 -12.574  1.00 31.39           C  
ATOM   2430  CE2 PHE A 324      32.609  11.699 -13.900  1.00 29.82           C  
ATOM   2431  CZ  PHE A 324      33.980  11.615 -13.773  1.00 31.93           C  
ATOM   2432  N   GLN A 325      29.637  12.450  -7.791  1.00 30.62           N  
ATOM   2433  CA  GLN A 325      29.204  12.999  -6.512  1.00 29.55           C  
ATOM   2434  C   GLN A 325      29.650  12.143  -5.336  1.00 37.18           C  
ATOM   2435  O   GLN A 325      29.670  12.635  -4.202  1.00 35.63           O  
ATOM   2436  CB  GLN A 325      27.687  13.157  -6.497  1.00 24.71           C  
ATOM   2437  CG  GLN A 325      27.178  14.155  -7.516  1.00 22.20           C  
ATOM   2438  CD  GLN A 325      27.779  15.533  -7.324  1.00 27.28           C  
ATOM   2439  OE1 GLN A 325      27.649  16.139  -6.258  1.00 40.28           O  
ATOM   2440  NE2 GLN A 325      28.448  16.035  -8.355  1.00 22.23           N  
ATOM   2441  N   SER A 326      30.014  10.880  -5.578  1.00 33.53           N  
ATOM   2442  CA  SER A 326      30.493  10.029  -4.496  1.00 33.49           C  
ATOM   2443  C   SER A 326      31.898  10.399  -4.046  1.00 33.13           C  
ATOM   2444  O   SER A 326      32.324   9.963  -2.972  1.00 35.32           O  
ATOM   2445  CB  SER A 326      30.462   8.559  -4.918  1.00 26.72           C  
ATOM   2446  OG  SER A 326      29.143   8.051  -4.877  1.00 33.84           O  
ATOM   2447  N   LEU A 327      32.625  11.189  -4.839  1.00 36.78           N  
ATOM   2448  CA  LEU A 327      33.996  11.539  -4.481  1.00 31.01           C  
ATOM   2449  C   LEU A 327      34.046  12.450  -3.262  1.00 33.72           C  
ATOM   2450  O   LEU A 327      34.997  12.377  -2.473  1.00 34.22           O  
ATOM   2451  CB  LEU A 327      34.697  12.201  -5.669  1.00 22.07           C  
ATOM   2452  CG  LEU A 327      35.073  11.281  -6.831  1.00 33.60           C  
ATOM   2453  CD1 LEU A 327      35.306  12.079  -8.105  1.00 33.87           C  
ATOM   2454  CD2 LEU A 327      36.310  10.476  -6.474  1.00 36.37           C  
ATOM   2455  N   ASN A 328      33.039  13.311  -3.093  1.00 32.45           N  
ATOM   2456  CA  ASN A 328      33.012  14.199  -1.932  1.00 35.72           C  
ATOM   2457  C   ASN A 328      32.970  13.414  -0.623  1.00 32.39           C  
ATOM   2458  O   ASN A 328      33.869  13.601   0.215  1.00 34.66           O  
ATOM   2459  CB  ASN A 328      31.857  15.198  -2.088  1.00 35.14           C  
ATOM   2460  CG  ASN A 328      31.936  16.350  -1.102  1.00 35.62           C  
ATOM   2461  OD1 ASN A 328      32.043  16.147   0.108  1.00 39.03           O  
ATOM   2462  ND2 ASN A 328      31.882  17.572  -1.619  1.00 44.82           N  
ATOM   2463  N   PRO A 329      32.011  12.508  -0.390  1.00 36.41           N  
ATOM   2464  CA  PRO A 329      32.051  11.747   0.871  1.00 36.26           C  
ATOM   2465  C   PRO A 329      33.161  10.711   0.923  1.00 37.85           C  
ATOM   2466  O   PRO A 329      33.654  10.410   2.018  1.00 43.25           O  
ATOM   2467  CB  PRO A 329      30.667  11.093   0.927  1.00 35.73           C  
ATOM   2468  CG  PRO A 329      30.292  10.937  -0.489  1.00 36.95           C  
ATOM   2469  CD  PRO A 329      30.827  12.145  -1.193  1.00 36.53           C  
ATOM   2470  N   LEU A 330      33.565  10.152  -0.221  1.00 34.86           N  
ATOM   2471  CA  LEU A 330      34.679   9.209  -0.231  1.00 39.36           C  
ATOM   2472  C   LEU A 330      35.945   9.850   0.325  1.00 36.61           C  
ATOM   2473  O   LEU A 330      36.613   9.277   1.194  1.00 40.74           O  
ATOM   2474  CB  LEU A 330      34.922   8.690  -1.647  1.00 32.33           C  
ATOM   2475  CG  LEU A 330      36.201   7.866  -1.791  1.00 28.00           C  
ATOM   2476  CD1 LEU A 330      36.062   6.551  -1.046  1.00 24.28           C  
ATOM   2477  CD2 LEU A 330      36.527   7.633  -3.253  1.00 26.28           C  
ATOM   2478  N   PHE A 331      36.293  11.043  -0.166  1.00 36.60           N  
ATOM   2479  CA  PHE A 331      37.489  11.709   0.339  1.00 38.83           C  
ATOM   2480  C   PHE A 331      37.330  12.124   1.793  1.00 38.88           C  
ATOM   2481  O   PHE A 331      38.315  12.128   2.539  1.00 41.11           O  
ATOM   2482  CB  PHE A 331      37.841  12.912  -0.533  1.00 39.44           C  
ATOM   2483  CG  PHE A 331      38.677  12.557  -1.732  1.00 40.89           C  
ATOM   2484  CD1 PHE A 331      39.962  12.055  -1.573  1.00 45.95           C  
ATOM   2485  CD2 PHE A 331      38.183  12.722  -3.013  1.00 33.65           C  
ATOM   2486  CE1 PHE A 331      40.734  11.722  -2.671  1.00 39.88           C  
ATOM   2487  CE2 PHE A 331      38.948  12.393  -4.112  1.00 42.44           C  
ATOM   2488  CZ  PHE A 331      40.226  11.888  -3.942  1.00 31.50           C  
ATOM   2489  N   ILE A 332      36.111  12.459   2.220  1.00 36.91           N  
ATOM   2490  CA  ILE A 332      35.890  12.725   3.638  1.00 46.66           C  
ATOM   2491  C   ILE A 332      36.214  11.487   4.462  1.00 46.39           C  
ATOM   2492  O   ILE A 332      36.887  11.571   5.494  1.00 49.25           O  
ATOM   2493  CB  ILE A 332      34.450  13.209   3.895  1.00 42.34           C  
ATOM   2494  CG1 ILE A 332      34.238  14.608   3.313  1.00 43.25           C  
ATOM   2495  CG2 ILE A 332      34.152  13.217   5.387  1.00 30.46           C  
ATOM   2496  CD1 ILE A 332      32.893  15.215   3.657  1.00 30.48           C  
ATOM   2497  N   MET A 333      35.760  10.317   4.010  1.00 38.48           N  
ATOM   2498  CA  MET A 333      35.989   9.094   4.769  1.00 33.95           C  
ATOM   2499  C   MET A 333      37.453   8.668   4.750  1.00 45.03           C  
ATOM   2500  O   MET A 333      37.938   8.102   5.734  1.00 54.29           O  
ATOM   2501  CB  MET A 333      35.105   7.974   4.230  1.00 36.90           C  
ATOM   2502  CG  MET A 333      33.631   8.215   4.477  1.00 34.16           C  
ATOM   2503  SD  MET A 333      32.575   6.828   4.020  1.00 42.64           S  
ATOM   2504  CE  MET A 333      32.848   6.756   2.254  1.00 33.08           C  
ATOM   2505  N   LEU A 334      38.166   8.913   3.650  1.00 47.01           N  
ATOM   2506  CA  LEU A 334      39.583   8.568   3.614  1.00 42.51           C  
ATOM   2507  C   LEU A 334      40.407   9.553   4.432  1.00 43.92           C  
ATOM   2508  O   LEU A 334      41.323   9.153   5.159  1.00 52.11           O  
ATOM   2509  CB  LEU A 334      40.087   8.525   2.171  1.00 44.27           C  
ATOM   2510  CG  LEU A 334      39.457   7.552   1.172  1.00 44.76           C  
ATOM   2511  CD1 LEU A 334      40.014   7.851  -0.204  1.00 47.96           C  
ATOM   2512  CD2 LEU A 334      39.715   6.101   1.548  1.00 43.01           C  
ATOM   2513  N   TYR A 335      40.091  10.846   4.327  1.00 39.85           N  
ATOM   2514  CA  TYR A 335      40.825  11.859   5.079  1.00 46.10           C  
ATOM   2515  C   TYR A 335      40.523  11.805   6.574  1.00 54.66           C  
ATOM   2516  O   TYR A 335      41.393  12.135   7.388  1.00 51.62           O  
ATOM   2517  CB  TYR A 335      40.493  13.257   4.551  1.00 44.93           C  
ATOM   2518  CG  TYR A 335      41.016  13.599   3.166  1.00 39.58           C  
ATOM   2519  CD1 TYR A 335      42.124  12.954   2.630  1.00 48.65           C  
ATOM   2520  CD2 TYR A 335      40.407  14.588   2.405  1.00 46.34           C  
ATOM   2521  CE1 TYR A 335      42.601  13.283   1.369  1.00 55.94           C  
ATOM   2522  CE2 TYR A 335      40.875  14.923   1.150  1.00 52.20           C  
ATOM   2523  CZ  TYR A 335      41.971  14.269   0.635  1.00 49.44           C  
ATOM   2524  OH  TYR A 335      42.432  14.608  -0.618  1.00 46.47           O  
ATOM   2525  N   THR A 336      39.309  11.391   6.961  1.00 54.39           N  
ATOM   2526  CA  THR A 336      38.851  11.618   8.334  1.00 62.22           C  
ATOM   2527  C   THR A 336      39.616  10.830   9.401  1.00 65.70           C  
ATOM   2528  O   THR A 336      39.834  11.383  10.486  1.00 67.73           O  
ATOM   2529  CB  THR A 336      37.332  11.373   8.465  1.00 52.90           C  
ATOM   2530  OG1 THR A 336      36.872  11.844   9.741  1.00 69.11           O  
ATOM   2531  CG2 THR A 336      36.946   9.908   8.305  1.00 61.24           C  
ATOM   2532  N   PRO A 337      40.060   9.582   9.188  1.00 64.40           N  
ATOM   2533  CA  PRO A 337      40.862   8.953  10.250  1.00 68.21           C  
ATOM   2534  C   PRO A 337      42.242   9.569  10.360  1.00 69.87           C  
ATOM   2535  O   PRO A 337      42.791   9.662  11.465  1.00 77.50           O  
ATOM   2536  CB  PRO A 337      40.921   7.485   9.813  1.00 71.48           C  
ATOM   2537  CG  PRO A 337      40.928   7.564   8.343  1.00 62.23           C  
ATOM   2538  CD  PRO A 337      40.032   8.724   7.985  1.00 66.82           C  
ATOM   2539  N   PHE A 338      42.796  10.025   9.235  1.00 66.19           N  
ATOM   2540  CA  PHE A 338      44.100  10.677   9.225  1.00 68.87           C  
ATOM   2541  C   PHE A 338      44.098  11.922  10.107  1.00 71.90           C  
ATOM   2542  O   PHE A 338      44.890  12.034  11.049  1.00 76.15           O  
ATOM   2543  CB  PHE A 338      44.473  11.023   7.781  1.00 57.91           C  
ATOM   2544  CG  PHE A 338      45.835  11.639   7.624  1.00 57.20           C  
ATOM   2545  CD1 PHE A 338      46.909  10.873   7.201  1.00 61.90           C  
ATOM   2546  CD2 PHE A 338      46.037  12.989   7.870  1.00 68.78           C  
ATOM   2547  CE1 PHE A 338      48.159  11.438   7.044  1.00 73.28           C  
ATOM   2548  CE2 PHE A 338      47.284  13.557   7.719  1.00 74.55           C  
ATOM   2549  CZ  PHE A 338      48.346  12.782   7.305  1.00 68.95           C  
ATOM   2550  N   PHE A 339      43.211  12.876   9.808  1.00 65.53           N  
ATOM   2551  CA  PHE A 339      43.203  14.146  10.527  1.00 64.94           C  
ATOM   2552  C   PHE A 339      42.879  13.981  12.006  1.00 72.76           C  
ATOM   2553  O   PHE A 339      43.243  14.848  12.808  1.00 76.96           O  
ATOM   2554  CB  PHE A 339      42.216  15.113   9.874  1.00 56.28           C  
ATOM   2555  CG  PHE A 339      42.733  15.735   8.612  1.00 51.32           C  
ATOM   2556  CD1 PHE A 339      42.681  15.046   7.413  1.00 51.63           C  
ATOM   2557  CD2 PHE A 339      43.283  17.004   8.626  1.00 57.89           C  
ATOM   2558  CE1 PHE A 339      43.163  15.612   6.251  1.00 46.32           C  
ATOM   2559  CE2 PHE A 339      43.765  17.577   7.469  1.00 61.50           C  
ATOM   2560  CZ  PHE A 339      43.705  16.880   6.278  1.00 59.42           C  
ATOM   2561  N   ALA A 340      42.205  12.895  12.388  1.00 76.55           N  
ATOM   2562  CA  ALA A 340      42.048  12.592  13.806  1.00 79.51           C  
ATOM   2563  C   ALA A 340      43.397  12.265  14.434  1.00 84.34           C  
ATOM   2564  O   ALA A 340      43.763  12.816  15.479  1.00 81.93           O  
ATOM   2565  CB  ALA A 340      41.067  11.435  13.989  1.00 75.08           C  
ATOM   2566  N   TRP A 341      44.151  11.363  13.799  1.00 81.89           N  
ATOM   2567  CA  TRP A 341      45.523  11.084  14.213  1.00 86.41           C  
ATOM   2568  C   TRP A 341      46.373  12.348  14.176  1.00 88.34           C  
ATOM   2569  O   TRP A 341      47.127  12.631  15.114  1.00 87.52           O  
ATOM   2570  CB  TRP A 341      46.099   9.980  13.312  1.00 85.88           C  
ATOM   2571  CG  TRP A 341      47.621   9.836  13.182  1.00 94.47           C  
ATOM   2572  CD1 TRP A 341      48.559  10.832  13.073  1.00 93.23           C  
ATOM   2573  CD2 TRP A 341      48.350   8.603  13.101  1.00111.70           C  
ATOM   2574  NE1 TRP A 341      49.815  10.294  12.954  1.00105.00           N  
ATOM   2575  CE2 TRP A 341      49.715   8.928  12.965  1.00113.11           C  
ATOM   2576  CE3 TRP A 341      47.979   7.255  13.139  1.00107.66           C  
ATOM   2577  CZ2 TRP A 341      50.709   7.955  12.869  1.00111.53           C  
ATOM   2578  CZ3 TRP A 341      48.967   6.291  13.043  1.00105.45           C  
ATOM   2579  CH2 TRP A 341      50.315   6.646  12.909  1.00108.43           C  
ATOM   2580  N   LEU A 342      46.270  13.115  13.088  1.00 86.28           N  
ATOM   2581  CA  LEU A 342      47.155  14.259  12.892  1.00 79.95           C  
ATOM   2582  C   LEU A 342      47.051  15.256  14.039  1.00 84.55           C  
ATOM   2583  O   LEU A 342      48.071  15.742  14.541  1.00 95.82           O  
ATOM   2584  CB  LEU A 342      46.838  14.941  11.564  1.00 76.44           C  
ATOM   2585  CG  LEU A 342      47.623  16.229  11.309  1.00 80.24           C  
ATOM   2586  CD1 LEU A 342      49.070  15.920  10.947  1.00 89.08           C  
ATOM   2587  CD2 LEU A 342      46.958  17.077  10.240  1.00 68.51           C  
ATOM   2588  N   TRP A 343      45.833  15.561  14.481  1.00 78.36           N  
ATOM   2589  CA  TRP A 343      45.637  16.642  15.438  1.00 78.28           C  
ATOM   2590  C   TRP A 343      45.836  16.217  16.886  1.00 83.83           C  
ATOM   2591  O   TRP A 343      45.954  17.088  17.754  1.00 80.80           O  
ATOM   2592  CB  TRP A 343      44.252  17.257  15.240  1.00 75.85           C  
ATOM   2593  CG  TRP A 343      44.246  18.208  14.091  1.00 82.38           C  
ATOM   2594  CD1 TRP A 343      45.220  19.112  13.780  1.00 84.67           C  
ATOM   2595  CD2 TRP A 343      43.247  18.330  13.075  1.00 76.53           C  
ATOM   2596  NE1 TRP A 343      44.882  19.802  12.644  1.00 71.27           N  
ATOM   2597  CE2 TRP A 343      43.676  19.341  12.190  1.00 76.04           C  
ATOM   2598  CE3 TRP A 343      42.028  17.691  12.830  1.00 75.05           C  
ATOM   2599  CZ2 TRP A 343      42.932  19.724  11.084  1.00 75.23           C  
ATOM   2600  CZ3 TRP A 343      41.292  18.074  11.730  1.00 78.73           C  
ATOM   2601  CH2 TRP A 343      41.746  19.081  10.872  1.00 81.25           C  
ATOM   2602  N   THR A 344      45.890  14.916  17.171  1.00 85.60           N  
ATOM   2603  CA  THR A 344      46.325  14.462  18.485  1.00 88.13           C  
ATOM   2604  C   THR A 344      47.839  14.512  18.644  1.00 95.16           C  
ATOM   2605  O   THR A 344      48.335  14.327  19.761  1.00 98.18           O  
ATOM   2606  CB  THR A 344      45.833  13.036  18.756  1.00 86.04           C  
ATOM   2607  OG1 THR A 344      46.378  12.141  17.779  1.00 95.78           O  
ATOM   2608  CG2 THR A 344      44.310  12.968  18.707  1.00 79.15           C  
ATOM   2609  N   ALA A 345      48.575  14.764  17.563  1.00 99.52           N  
ATOM   2610  CA  ALA A 345      50.032  14.863  17.614  1.00 80.05           C  
ATOM   2611  C   ALA A 345      50.503  16.304  17.421  1.00 81.79           C  
ATOM   2612  O   ALA A 345      49.720  17.188  17.073  1.00 81.86           O  
ATOM   2613  CB  ALA A 345      50.664  13.955  16.564  1.00 67.30           C  
ATOM   2614  N   GLN A 350      50.544  22.544  16.427  1.00 67.11           N  
ATOM   2615  CA  GLN A 350      49.170  22.599  15.948  1.00 81.11           C  
ATOM   2616  C   GLN A 350      48.740  24.045  15.764  1.00 78.67           C  
ATOM   2617  O   GLN A 350      48.869  24.860  16.678  1.00 78.39           O  
ATOM   2618  CB  GLN A 350      48.225  21.872  16.906  1.00 85.68           C  
ATOM   2619  CG  GLN A 350      46.760  21.967  16.517  1.00 81.06           C  
ATOM   2620  CD  GLN A 350      45.903  20.951  17.239  1.00 84.41           C  
ATOM   2621  OE1 GLN A 350      44.996  21.304  17.990  1.00 90.26           O  
ATOM   2622  NE2 GLN A 350      46.187  19.674  17.011  1.00 84.03           N  
ATOM   2623  N   PRO A 351      48.228  24.359  14.581  1.00 79.30           N  
ATOM   2624  CA  PRO A 351      47.959  25.754  14.229  1.00 81.13           C  
ATOM   2625  C   PRO A 351      46.626  26.260  14.769  1.00 78.21           C  
ATOM   2626  O   PRO A 351      45.762  25.507  15.223  1.00 67.42           O  
ATOM   2627  CB  PRO A 351      47.967  25.730  12.696  1.00 76.20           C  
ATOM   2628  CG  PRO A 351      47.517  24.358  12.356  1.00 82.64           C  
ATOM   2629  CD  PRO A 351      48.058  23.453  13.431  1.00 79.49           C  
ATOM   2630  N   SER A 352      46.479  27.581  14.679  1.00 82.70           N  
ATOM   2631  CA  SER A 352      45.342  28.304  15.220  1.00 73.28           C  
ATOM   2632  C   SER A 352      44.083  28.040  14.409  1.00 77.62           C  
ATOM   2633  O   SER A 352      44.113  27.500  13.299  1.00 76.89           O  
ATOM   2634  CB  SER A 352      45.615  29.807  15.227  1.00 72.63           C  
ATOM   2635  OG  SER A 352      46.853  30.100  15.843  1.00100.64           O  
ATOM   2636  N   SER A 353      42.962  28.470  14.981  1.00 74.51           N  
ATOM   2637  CA  SER A 353      41.693  28.388  14.264  1.00 72.19           C  
ATOM   2638  C   SER A 353      41.637  29.333  13.069  1.00 71.60           C  
ATOM   2639  O   SER A 353      41.225  28.888  11.985  1.00 74.39           O  
ATOM   2640  CB  SER A 353      40.543  28.624  15.246  1.00 79.64           C  
ATOM   2641  OG  SER A 353      40.487  27.575  16.202  1.00 85.98           O  
ATOM   2642  N   PRO A 354      42.003  30.618  13.176  1.00 71.38           N  
ATOM   2643  CA  PRO A 354      41.986  31.460  11.964  1.00 74.40           C  
ATOM   2644  C   PRO A 354      42.897  30.942  10.864  1.00 71.40           C  
ATOM   2645  O   PRO A 354      42.463  30.814   9.712  1.00 68.50           O  
ATOM   2646  CB  PRO A 354      42.431  32.836  12.485  1.00 68.29           C  
ATOM   2647  CG  PRO A 354      43.114  32.563  13.781  1.00 77.61           C  
ATOM   2648  CD  PRO A 354      42.375  31.403  14.367  1.00 71.68           C  
ATOM   2649  N   THR A 355      44.153  30.626  11.189  1.00 81.16           N  
ATOM   2650  CA  THR A 355      45.075  30.143  10.167  1.00 72.37           C  
ATOM   2651  C   THR A 355      44.604  28.819   9.570  1.00 65.34           C  
ATOM   2652  O   THR A 355      44.930  28.509   8.419  1.00 56.90           O  
ATOM   2653  CB  THR A 355      46.488  30.025  10.751  1.00 71.59           C  
ATOM   2654  OG1 THR A 355      47.431  29.760   9.704  1.00 77.29           O  
ATOM   2655  CG2 THR A 355      46.562  28.920  11.782  1.00 77.73           C  
ATOM   2656  N   LYS A 356      43.814  28.042  10.317  1.00 65.29           N  
ATOM   2657  CA  LYS A 356      43.196  26.852   9.735  1.00 62.82           C  
ATOM   2658  C   LYS A 356      42.162  27.228   8.681  1.00 58.37           C  
ATOM   2659  O   LYS A 356      42.052  26.561   7.645  1.00 56.12           O  
ATOM   2660  CB  LYS A 356      42.548  26.000  10.825  1.00 66.60           C  
ATOM   2661  CG  LYS A 356      43.483  25.020  11.508  1.00 66.90           C  
ATOM   2662  CD  LYS A 356      42.895  24.592  12.837  1.00 76.97           C  
ATOM   2663  CE  LYS A 356      43.728  23.529  13.522  1.00 78.64           C  
ATOM   2664  NZ  LYS A 356      43.285  23.374  14.934  1.00 84.54           N  
ATOM   2665  N   PHE A 357      41.395  28.291   8.932  1.00 56.91           N  
ATOM   2666  CA  PHE A 357      40.383  28.733   7.978  1.00 56.03           C  
ATOM   2667  C   PHE A 357      41.018  29.195   6.672  1.00 61.46           C  
ATOM   2668  O   PHE A 357      40.561  28.831   5.582  1.00 61.92           O  
ATOM   2669  CB  PHE A 357      39.548  29.858   8.591  1.00 62.83           C  
ATOM   2670  CG  PHE A 357      38.364  29.378   9.384  1.00 67.89           C  
ATOM   2671  CD1 PHE A 357      38.503  28.380  10.335  1.00 69.48           C  
ATOM   2672  CD2 PHE A 357      37.113  29.942   9.189  1.00 62.32           C  
ATOM   2673  CE1 PHE A 357      37.413  27.943  11.067  1.00 69.94           C  
ATOM   2674  CE2 PHE A 357      36.021  29.513   9.916  1.00 62.99           C  
ATOM   2675  CZ  PHE A 357      36.171  28.511  10.857  1.00 72.22           C  
ATOM   2676  N   ALA A 358      42.069  30.014   6.767  1.00 64.99           N  
ATOM   2677  CA  ALA A 358      42.725  30.537   5.573  1.00 65.70           C  
ATOM   2678  C   ALA A 358      43.240  29.410   4.685  1.00 56.52           C  
ATOM   2679  O   ALA A 358      43.004  29.402   3.472  1.00 57.22           O  
ATOM   2680  CB  ALA A 358      43.867  31.472   5.974  1.00 53.17           C  
ATOM   2681  N   VAL A 359      43.939  28.440   5.281  1.00 55.91           N  
ATOM   2682  CA  VAL A 359      44.463  27.313   4.514  1.00 59.09           C  
ATOM   2683  C   VAL A 359      43.324  26.526   3.882  1.00 54.95           C  
ATOM   2684  O   VAL A 359      43.435  26.043   2.748  1.00 51.42           O  
ATOM   2685  CB  VAL A 359      45.343  26.420   5.410  1.00 58.13           C  
ATOM   2686  CG1 VAL A 359      45.856  25.218   4.632  1.00 47.33           C  
ATOM   2687  CG2 VAL A 359      46.503  27.224   5.978  1.00 49.92           C  
ATOM   2688  N   GLY A 360      42.209  26.388   4.603  1.00 55.55           N  
ATOM   2689  CA  GLY A 360      41.049  25.723   4.036  1.00 51.98           C  
ATOM   2690  C   GLY A 360      40.523  26.425   2.800  1.00 48.86           C  
ATOM   2691  O   GLY A 360      40.169  25.781   1.810  1.00 51.64           O  
ATOM   2692  N   LEU A 361      40.473  27.758   2.835  1.00 48.31           N  
ATOM   2693  CA  LEU A 361      40.053  28.500   1.652  1.00 53.04           C  
ATOM   2694  C   LEU A 361      41.107  28.437   0.554  1.00 54.26           C  
ATOM   2695  O   LEU A 361      40.765  28.476  -0.634  1.00 52.13           O  
ATOM   2696  CB  LEU A 361      39.749  29.951   2.020  1.00 48.89           C  
ATOM   2697  CG  LEU A 361      38.946  30.750   0.992  1.00 53.26           C  
ATOM   2698  CD1 LEU A 361      37.513  30.247   0.913  1.00 46.08           C  
ATOM   2699  CD2 LEU A 361      38.983  32.233   1.320  1.00 51.58           C  
ATOM   2700  N   MET A 362      42.385  28.341   0.930  1.00 54.55           N  
ATOM   2701  CA  MET A 362      43.449  28.205  -0.061  1.00 49.83           C  
ATOM   2702  C   MET A 362      43.309  26.896  -0.829  1.00 54.74           C  
ATOM   2703  O   MET A 362      43.338  26.881  -2.065  1.00 54.49           O  
ATOM   2704  CB  MET A 362      44.823  28.291   0.619  1.00 54.64           C  
ATOM   2705  CG  MET A 362      45.189  29.677   1.175  1.00 62.73           C  
ATOM   2706  SD  MET A 362      46.797  29.748   2.011  1.00 56.90           S  
ATOM   2707  CE  MET A 362      47.831  30.510   0.759  1.00 57.41           C  
ATOM   2708  N   PHE A 363      43.148  25.782  -0.108  1.00 55.16           N  
ATOM   2709  CA  PHE A 363      42.932  24.493  -0.759  1.00 46.59           C  
ATOM   2710  C   PHE A 363      41.666  24.513  -1.609  1.00 49.04           C  
ATOM   2711  O   PHE A 363      41.669  24.050  -2.756  1.00 44.30           O  
ATOM   2712  CB  PHE A 363      42.868  23.383   0.291  1.00 40.92           C  
ATOM   2713  CG  PHE A 363      44.214  22.839   0.682  1.00 56.40           C  
ATOM   2714  CD1 PHE A 363      45.102  22.398  -0.286  1.00 55.60           C  
ATOM   2715  CD2 PHE A 363      44.597  22.774   2.013  1.00 56.78           C  
ATOM   2716  CE1 PHE A 363      46.339  21.895   0.064  1.00 43.31           C  
ATOM   2717  CE2 PHE A 363      45.836  22.274   2.367  1.00 48.97           C  
ATOM   2718  CZ  PHE A 363      46.707  21.835   1.391  1.00 45.24           C  
ATOM   2719  N   ALA A 364      40.571  25.049  -1.062  1.00 44.42           N  
ATOM   2720  CA  ALA A 364      39.347  25.199  -1.843  1.00 41.02           C  
ATOM   2721  C   ALA A 364      39.613  25.978  -3.125  1.00 44.36           C  
ATOM   2722  O   ALA A 364      39.151  25.599  -4.208  1.00 41.02           O  
ATOM   2723  CB  ALA A 364      38.270  25.892  -1.006  1.00 33.59           C  
ATOM   2724  N   GLY A 365      40.378  27.065  -3.022  1.00 42.73           N  
ATOM   2725  CA  GLY A 365      40.749  27.811  -4.210  1.00 39.66           C  
ATOM   2726  C   GLY A 365      41.681  27.042  -5.123  1.00 45.43           C  
ATOM   2727  O   GLY A 365      41.615  27.190  -6.348  1.00 42.73           O  
ATOM   2728  N   LEU A 366      42.561  26.217  -4.546  1.00 48.54           N  
ATOM   2729  CA  LEU A 366      43.432  25.372  -5.358  1.00 46.60           C  
ATOM   2730  C   LEU A 366      42.632  24.360  -6.166  1.00 43.89           C  
ATOM   2731  O   LEU A 366      43.041  23.985  -7.270  1.00 45.57           O  
ATOM   2732  CB  LEU A 366      44.450  24.649  -4.472  1.00 42.75           C  
ATOM   2733  CG  LEU A 366      45.595  25.465  -3.867  1.00 51.96           C  
ATOM   2734  CD1 LEU A 366      46.516  24.577  -3.042  1.00 43.77           C  
ATOM   2735  CD2 LEU A 366      46.377  26.184  -4.955  1.00 50.11           C  
ATOM   2736  N   SER A 367      41.493  23.910  -5.635  1.00 42.13           N  
ATOM   2737  CA  SER A 367      40.667  22.947  -6.357  1.00 37.73           C  
ATOM   2738  C   SER A 367      40.058  23.563  -7.610  1.00 38.46           C  
ATOM   2739  O   SER A 367      39.884  22.876  -8.624  1.00 36.64           O  
ATOM   2740  CB  SER A 367      39.569  22.408  -5.443  1.00 38.34           C  
ATOM   2741  OG  SER A 367      38.663  23.436  -5.082  1.00 39.77           O  
ATOM   2742  N   PHE A 368      39.714  24.852  -7.560  1.00 39.45           N  
ATOM   2743  CA  PHE A 368      39.184  25.516  -8.746  1.00 37.98           C  
ATOM   2744  C   PHE A 368      40.289  25.938  -9.702  1.00 41.13           C  
ATOM   2745  O   PHE A 368      40.077  25.952 -10.920  1.00 40.78           O  
ATOM   2746  CB  PHE A 368      38.335  26.723  -8.347  1.00 33.76           C  
ATOM   2747  CG  PHE A 368      36.858  26.450  -8.348  1.00 39.24           C  
ATOM   2748  CD1 PHE A 368      36.364  25.236  -7.896  1.00 39.81           C  
ATOM   2749  CD2 PHE A 368      35.962  27.410  -8.793  1.00 39.36           C  
ATOM   2750  CE1 PHE A 368      35.006  24.980  -7.895  1.00 30.21           C  
ATOM   2751  CE2 PHE A 368      34.601  27.159  -8.793  1.00 31.81           C  
ATOM   2752  CZ  PHE A 368      34.126  25.941  -8.345  1.00 30.33           C  
ATOM   2753  N   LEU A 369      41.466  26.284  -9.178  1.00 41.32           N  
ATOM   2754  CA  LEU A 369      42.599  26.580 -10.047  1.00 46.26           C  
ATOM   2755  C   LEU A 369      43.013  25.354 -10.847  1.00 45.41           C  
ATOM   2756  O   LEU A 369      43.336  25.462 -12.037  1.00 38.76           O  
ATOM   2757  CB  LEU A 369      43.774  27.101  -9.224  1.00 46.59           C  
ATOM   2758  CG  LEU A 369      43.648  28.539  -8.734  1.00 43.58           C  
ATOM   2759  CD1 LEU A 369      44.827  28.898  -7.848  1.00 45.01           C  
ATOM   2760  CD2 LEU A 369      43.553  29.485  -9.921  1.00 39.22           C  
ATOM   2761  N   LEU A 370      43.003  24.179 -10.212  1.00 34.34           N  
ATOM   2762  CA  LEU A 370      43.344  22.951 -10.920  1.00 42.64           C  
ATOM   2763  C   LEU A 370      42.420  22.728 -12.110  1.00 43.24           C  
ATOM   2764  O   LEU A 370      42.866  22.303 -13.181  1.00 37.02           O  
ATOM   2765  CB  LEU A 370      43.283  21.765  -9.959  1.00 44.14           C  
ATOM   2766  CG  LEU A 370      43.709  20.382 -10.451  1.00 46.81           C  
ATOM   2767  CD1 LEU A 370      44.389  19.660  -9.316  1.00 65.09           C  
ATOM   2768  CD2 LEU A 370      42.522  19.567 -10.942  1.00 49.90           C  
ATOM   2769  N   MET A 371      41.129  23.023 -11.943  1.00 38.37           N  
ATOM   2770  CA  MET A 371      40.160  22.774 -13.003  1.00 33.89           C  
ATOM   2771  C   MET A 371      40.310  23.730 -14.176  1.00 35.54           C  
ATOM   2772  O   MET A 371      39.781  23.448 -15.256  1.00 34.91           O  
ATOM   2773  CB  MET A 371      38.743  22.856 -12.443  1.00 35.13           C  
ATOM   2774  CG  MET A 371      38.386  21.694 -11.538  1.00 42.66           C  
ATOM   2775  SD  MET A 371      38.407  20.121 -12.421  1.00 39.19           S  
ATOM   2776  CE  MET A 371      37.241  20.469 -13.735  1.00 27.25           C  
ATOM   2777  N   ALA A 372      41.004  24.853 -13.993  1.00 38.55           N  
ATOM   2778  CA  ALA A 372      41.222  25.762 -15.109  1.00 35.51           C  
ATOM   2779  C   ALA A 372      42.274  25.238 -16.076  1.00 36.53           C  
ATOM   2780  O   ALA A 372      42.295  25.655 -17.237  1.00 37.19           O  
ATOM   2781  CB  ALA A 372      41.621  27.142 -14.590  1.00 33.70           C  
ATOM   2782  N   ILE A 373      43.123  24.317 -15.632  1.00 32.95           N  
ATOM   2783  CA  ILE A 373      44.255  23.818 -16.415  1.00 40.55           C  
ATOM   2784  C   ILE A 373      43.814  23.053 -17.664  1.00 46.23           C  
ATOM   2785  O   ILE A 373      44.324  23.347 -18.756  1.00 49.58           O  
ATOM   2786  CB  ILE A 373      45.182  22.945 -15.549  1.00 38.74           C  
ATOM   2787  CG1 ILE A 373      45.723  23.745 -14.361  1.00 30.50           C  
ATOM   2788  CG2 ILE A 373      46.315  22.390 -16.389  1.00 39.35           C  
ATOM   2789  CD1 ILE A 373      46.694  22.971 -13.489  1.00 28.81           C  
ATOM   2790  N   PRO A 374      42.905  22.066 -17.579  1.00 39.89           N  
ATOM   2791  CA  PRO A 374      42.601  21.275 -18.789  1.00 33.60           C  
ATOM   2792  C   PRO A 374      42.057  22.093 -19.950  1.00 45.79           C  
ATOM   2793  O   PRO A 374      42.434  21.845 -21.102  1.00 42.76           O  
ATOM   2794  CB  PRO A 374      41.573  20.252 -18.285  1.00 37.83           C  
ATOM   2795  CG  PRO A 374      41.002  20.856 -17.059  1.00 38.23           C  
ATOM   2796  CD  PRO A 374      42.143  21.568 -16.419  1.00 39.19           C  
ATOM   2797  N   GLY A 375      41.173  23.057 -19.686  1.00 41.91           N  
ATOM   2798  CA  GLY A 375      40.669  23.893 -20.763  1.00 33.16           C  
ATOM   2799  C   GLY A 375      41.741  24.788 -21.355  1.00 44.52           C  
ATOM   2800  O   GLY A 375      41.802  24.979 -22.573  1.00 37.44           O  
ATOM   2801  N   ALA A 376      42.601  25.349 -20.502  1.00 42.64           N  
ATOM   2802  CA  ALA A 376      43.695  26.182 -20.989  1.00 38.70           C  
ATOM   2803  C   ALA A 376      44.661  25.378 -21.846  1.00 39.63           C  
ATOM   2804  O   ALA A 376      45.150  25.867 -22.870  1.00 44.32           O  
ATOM   2805  CB  ALA A 376      44.427  26.816 -19.811  1.00 35.63           C  
ATOM   2806  N   LEU A 377      44.932  24.134 -21.458  1.00 37.95           N  
ATOM   2807  CA  LEU A 377      45.931  23.344 -22.166  1.00 36.83           C  
ATOM   2808  C   LEU A 377      45.344  22.675 -23.402  1.00 38.80           C  
ATOM   2809  O   LEU A 377      45.899  22.785 -24.499  1.00 35.89           O  
ATOM   2810  CB  LEU A 377      46.531  22.300 -21.224  1.00 38.72           C  
ATOM   2811  CG  LEU A 377      47.692  21.468 -21.764  1.00 38.00           C  
ATOM   2812  CD1 LEU A 377      48.887  22.356 -22.083  1.00 35.64           C  
ATOM   2813  CD2 LEU A 377      48.069  20.386 -20.763  1.00 40.01           C  
ATOM   2814  N   TYR A 378      44.218  21.981 -23.241  1.00 37.99           N  
ATOM   2815  CA  TYR A 378      43.666  21.131 -24.287  1.00 36.26           C  
ATOM   2816  C   TYR A 378      42.568  21.798 -25.102  1.00 41.04           C  
ATOM   2817  O   TYR A 378      42.203  21.276 -26.160  1.00 35.85           O  
ATOM   2818  CB  TYR A 378      43.104  19.839 -23.678  1.00 30.44           C  
ATOM   2819  CG  TYR A 378      44.135  18.890 -23.107  1.00 35.26           C  
ATOM   2820  CD1 TYR A 378      44.974  18.165 -23.942  1.00 29.63           C  
ATOM   2821  CD2 TYR A 378      44.247  18.694 -21.733  1.00 38.44           C  
ATOM   2822  CE1 TYR A 378      45.909  17.283 -23.427  1.00 43.75           C  
ATOM   2823  CE2 TYR A 378      45.180  17.813 -21.209  1.00 37.44           C  
ATOM   2824  CZ  TYR A 378      46.008  17.110 -22.061  1.00 38.82           C  
ATOM   2825  OH  TYR A 378      46.935  16.233 -21.548  1.00 52.14           O  
ATOM   2826  N   GLY A 379      42.032  22.921 -24.642  1.00 38.94           N  
ATOM   2827  CA  GLY A 379      40.844  23.494 -25.235  1.00 33.14           C  
ATOM   2828  C   GLY A 379      39.583  23.062 -24.504  1.00 31.47           C  
ATOM   2829  O   GLY A 379      39.591  22.201 -23.622  1.00 43.23           O  
ATOM   2830  N   THR A 380      38.467  23.669 -24.902  1.00 36.34           N  
ATOM   2831  CA  THR A 380      37.188  23.475 -24.231  1.00 30.82           C  
ATOM   2832  C   THR A 380      36.198  22.634 -25.035  1.00 35.84           C  
ATOM   2833  O   THR A 380      35.190  22.184 -24.476  1.00 46.92           O  
ATOM   2834  CB  THR A 380      36.588  24.857 -23.896  1.00 36.98           C  
ATOM   2835  OG1 THR A 380      37.488  25.560 -23.033  1.00 48.87           O  
ATOM   2836  CG2 THR A 380      35.251  24.761 -23.187  1.00 60.22           C  
ATOM   2837  N   SER A 381      36.470  22.370 -26.311  1.00 34.58           N  
ATOM   2838  CA  SER A 381      35.531  21.651 -27.161  1.00 40.19           C  
ATOM   2839  C   SER A 381      35.692  20.135 -27.084  1.00 49.05           C  
ATOM   2840  O   SER A 381      34.989  19.418 -27.807  1.00 59.17           O  
ATOM   2841  CB  SER A 381      35.683  22.112 -28.615  1.00 34.78           C  
ATOM   2842  OG  SER A 381      37.045  22.146 -29.000  1.00 53.72           O  
ATOM   2843  N   GLY A 382      36.588  19.627 -26.235  1.00 43.49           N  
ATOM   2844  CA  GLY A 382      36.823  18.222 -26.123  1.00 29.75           C  
ATOM   2845  C   GLY A 382      36.424  17.676 -24.765  1.00 41.32           C  
ATOM   2846  O   GLY A 382      35.652  18.286 -24.010  1.00 42.66           O  
ATOM   2847  N   LYS A 383      36.966  16.501 -24.445  1.00 33.47           N  
ATOM   2848  CA  LYS A 383      36.706  15.822 -23.190  1.00 40.53           C  
ATOM   2849  C   LYS A 383      38.034  15.470 -22.536  1.00 34.71           C  
ATOM   2850  O   LYS A 383      38.996  15.112 -23.218  1.00 40.47           O  
ATOM   2851  CB  LYS A 383      35.860  14.554 -23.397  1.00 42.61           C  
ATOM   2852  CG  LYS A 383      34.703  14.754 -24.354  1.00 39.89           C  
ATOM   2853  CD  LYS A 383      33.393  14.285 -23.759  1.00 42.79           C  
ATOM   2854  CE  LYS A 383      32.211  14.772 -24.576  1.00 31.04           C  
ATOM   2855  NZ  LYS A 383      30.908  14.551 -23.887  1.00 53.52           N  
ATOM   2856  N   VAL A 384      38.093  15.594 -21.210  1.00 44.86           N  
ATOM   2857  CA  VAL A 384      39.336  15.392 -20.474  1.00 43.06           C  
ATOM   2858  C   VAL A 384      39.223  14.165 -19.582  1.00 42.24           C  
ATOM   2859  O   VAL A 384      38.157  13.548 -19.488  1.00 35.76           O  
ATOM   2860  CB  VAL A 384      39.699  16.632 -19.642  1.00 37.12           C  
ATOM   2861  CG1 VAL A 384      40.082  17.787 -20.561  1.00 34.96           C  
ATOM   2862  CG2 VAL A 384      38.529  17.025 -18.757  1.00 36.68           C  
ATOM   2863  N   SER A 385      40.324  13.806 -18.923  1.00 48.45           N  
ATOM   2864  CA  SER A 385      40.321  12.661 -18.026  1.00 42.77           C  
ATOM   2865  C   SER A 385      39.379  12.913 -16.854  1.00 45.29           C  
ATOM   2866  O   SER A 385      39.307  14.036 -16.339  1.00 45.17           O  
ATOM   2867  CB  SER A 385      41.729  12.382 -17.503  1.00 44.11           C  
ATOM   2868  OG  SER A 385      41.716  11.348 -16.540  1.00 48.39           O  
ATOM   2869  N   PRO A 386      38.654  11.892 -16.398  1.00 35.58           N  
ATOM   2870  CA  PRO A 386      37.917  12.021 -15.134  1.00 36.88           C  
ATOM   2871  C   PRO A 386      38.816  12.249 -13.929  1.00 37.40           C  
ATOM   2872  O   PRO A 386      38.305  12.602 -12.859  1.00 41.51           O  
ATOM   2873  CB  PRO A 386      37.166  10.687 -15.026  1.00 47.85           C  
ATOM   2874  CG  PRO A 386      37.858   9.769 -15.958  1.00 47.33           C  
ATOM   2875  CD  PRO A 386      38.408  10.604 -17.062  1.00 37.18           C  
ATOM   2876  N   LEU A 387      40.132  12.068 -14.073  1.00 44.54           N  
ATOM   2877  CA  LEU A 387      41.047  12.260 -12.952  1.00 37.99           C  
ATOM   2878  C   LEU A 387      41.156  13.723 -12.544  1.00 39.32           C  
ATOM   2879  O   LEU A 387      41.480  14.015 -11.387  1.00 37.21           O  
ATOM   2880  CB  LEU A 387      42.422  11.703 -13.307  1.00 28.11           C  
ATOM   2881  CG  LEU A 387      42.499  10.179 -13.266  1.00 31.93           C  
ATOM   2882  CD1 LEU A 387      43.740   9.683 -13.984  1.00 35.45           C  
ATOM   2883  CD2 LEU A 387      42.484   9.709 -11.822  1.00 26.26           C  
ATOM   2884  N   TRP A 388      40.903  14.649 -13.472  1.00 39.81           N  
ATOM   2885  CA  TRP A 388      40.873  16.065 -13.120  1.00 42.30           C  
ATOM   2886  C   TRP A 388      39.846  16.335 -12.027  1.00 39.20           C  
ATOM   2887  O   TRP A 388      40.144  17.002 -11.029  1.00 38.27           O  
ATOM   2888  CB  TRP A 388      40.569  16.914 -14.357  1.00 37.59           C  
ATOM   2889  CG  TRP A 388      41.669  16.943 -15.377  1.00 47.19           C  
ATOM   2890  CD1 TRP A 388      41.706  16.267 -16.561  1.00 41.57           C  
ATOM   2891  CD2 TRP A 388      42.890  17.694 -15.306  1.00 48.33           C  
ATOM   2892  NE1 TRP A 388      42.871  16.549 -17.232  1.00 46.44           N  
ATOM   2893  CE2 TRP A 388      43.615  17.422 -16.484  1.00 44.00           C  
ATOM   2894  CE3 TRP A 388      43.439  18.568 -14.362  1.00 41.07           C  
ATOM   2895  CZ2 TRP A 388      44.861  17.992 -16.742  1.00 47.41           C  
ATOM   2896  CZ3 TRP A 388      44.676  19.133 -14.621  1.00 40.41           C  
ATOM   2897  CH2 TRP A 388      45.373  18.842 -15.801  1.00 48.67           C  
ATOM   2898  N   LEU A 389      38.624  15.822 -12.201  1.00 33.33           N  
ATOM   2899  CA  LEU A 389      37.607  15.984 -11.168  1.00 32.46           C  
ATOM   2900  C   LEU A 389      37.988  15.235  -9.901  1.00 35.36           C  
ATOM   2901  O   LEU A 389      37.686  15.685  -8.790  1.00 33.58           O  
ATOM   2902  CB  LEU A 389      36.248  15.512 -11.683  1.00 26.14           C  
ATOM   2903  CG  LEU A 389      35.537  16.483 -12.625  1.00 39.74           C  
ATOM   2904  CD1 LEU A 389      34.258  15.873 -13.161  1.00 37.68           C  
ATOM   2905  CD2 LEU A 389      35.257  17.799 -11.921  1.00 24.15           C  
ATOM   2906  N   VAL A 390      38.647  14.084 -10.048  1.00 29.99           N  
ATOM   2907  CA  VAL A 390      39.095  13.338  -8.878  1.00 34.85           C  
ATOM   2908  C   VAL A 390      40.093  14.164  -8.076  1.00 41.21           C  
ATOM   2909  O   VAL A 390      40.017  14.235  -6.843  1.00 40.37           O  
ATOM   2910  CB  VAL A 390      39.684  11.978  -9.299  1.00 41.52           C  
ATOM   2911  CG1 VAL A 390      40.197  11.226  -8.081  1.00 34.93           C  
ATOM   2912  CG2 VAL A 390      38.634  11.151 -10.029  1.00 32.27           C  
ATOM   2913  N   GLY A 391      41.031  14.821  -8.760  1.00 41.22           N  
ATOM   2914  CA  GLY A 391      41.970  15.682  -8.062  1.00 33.47           C  
ATOM   2915  C   GLY A 391      41.326  16.930  -7.491  1.00 41.00           C  
ATOM   2916  O   GLY A 391      41.738  17.418  -6.434  1.00 41.59           O  
ATOM   2917  N   SER A 392      40.311  17.463  -8.174  1.00 44.50           N  
ATOM   2918  CA  SER A 392      39.631  18.659  -7.686  1.00 39.67           C  
ATOM   2919  C   SER A 392      38.941  18.391  -6.354  1.00 33.77           C  
ATOM   2920  O   SER A 392      39.095  19.157  -5.396  1.00 32.76           O  
ATOM   2921  CB  SER A 392      38.626  19.151  -8.730  1.00 33.38           C  
ATOM   2922  OG  SER A 392      38.075  20.405  -8.369  1.00 37.79           O  
ATOM   2923  N   TRP A 393      38.181  17.296  -6.273  1.00 30.72           N  
ATOM   2924  CA  TRP A 393      37.517  16.955  -5.021  1.00 32.52           C  
ATOM   2925  C   TRP A 393      38.526  16.613  -3.929  1.00 40.66           C  
ATOM   2926  O   TRP A 393      38.303  16.926  -2.754  1.00 39.42           O  
ATOM   2927  CB  TRP A 393      36.539  15.802  -5.237  1.00 28.78           C  
ATOM   2928  CG  TRP A 393      35.135  16.264  -5.469  1.00 31.93           C  
ATOM   2929  CD1 TRP A 393      34.326  16.902  -4.575  1.00 26.55           C  
ATOM   2930  CD2 TRP A 393      34.369  16.123  -6.672  1.00 35.70           C  
ATOM   2931  NE1 TRP A 393      33.108  17.172  -5.146  1.00 25.47           N  
ATOM   2932  CE2 TRP A 393      33.107  16.703  -6.433  1.00 28.92           C  
ATOM   2933  CE3 TRP A 393      34.630  15.567  -7.929  1.00 22.13           C  
ATOM   2934  CZ2 TRP A 393      32.108  16.742  -7.402  1.00 30.00           C  
ATOM   2935  CZ3 TRP A 393      33.638  15.608  -8.889  1.00 27.83           C  
ATOM   2936  CH2 TRP A 393      32.392  16.190  -8.621  1.00 30.47           C  
ATOM   2937  N   ALA A 394      39.643  15.976  -4.292  1.00 38.12           N  
ATOM   2938  CA  ALA A 394      40.676  15.699  -3.300  1.00 35.39           C  
ATOM   2939  C   ALA A 394      41.175  16.986  -2.659  1.00 40.12           C  
ATOM   2940  O   ALA A 394      41.450  17.023  -1.454  1.00 41.57           O  
ATOM   2941  CB  ALA A 394      41.836  14.936  -3.937  1.00 27.83           C  
ATOM   2942  N   LEU A 395      41.278  18.059  -3.445  1.00 36.39           N  
ATOM   2943  CA  LEU A 395      41.780  19.321  -2.911  1.00 36.12           C  
ATOM   2944  C   LEU A 395      40.753  19.996  -2.012  1.00 41.38           C  
ATOM   2945  O   LEU A 395      41.081  20.447  -0.908  1.00 43.05           O  
ATOM   2946  CB  LEU A 395      42.180  20.248  -4.055  1.00 32.05           C  
ATOM   2947  CG  LEU A 395      43.517  19.902  -4.699  1.00 37.20           C  
ATOM   2948  CD1 LEU A 395      43.726  20.758  -5.931  1.00 37.92           C  
ATOM   2949  CD2 LEU A 395      44.644  20.097  -3.693  1.00 25.22           C  
ATOM   2950  N   VAL A 396      39.503  20.087  -2.469  1.00 35.65           N  
ATOM   2951  CA  VAL A 396      38.514  20.855  -1.720  1.00 34.14           C  
ATOM   2952  C   VAL A 396      38.149  20.140  -0.421  1.00 42.40           C  
ATOM   2953  O   VAL A 396      37.948  20.782   0.617  1.00 40.83           O  
ATOM   2954  CB  VAL A 396      37.279  21.149  -2.597  1.00 35.78           C  
ATOM   2955  CG1 VAL A 396      36.434  19.895  -2.820  1.00 32.37           C  
ATOM   2956  CG2 VAL A 396      36.451  22.277  -1.999  1.00 28.89           C  
ATOM   2957  N   ILE A 397      38.089  18.805  -0.444  1.00 41.58           N  
ATOM   2958  CA  ILE A 397      37.770  18.071   0.775  1.00 39.11           C  
ATOM   2959  C   ILE A 397      38.921  18.176   1.763  1.00 42.38           C  
ATOM   2960  O   ILE A 397      38.703  18.232   2.980  1.00 44.06           O  
ATOM   2961  CB  ILE A 397      37.416  16.608   0.451  1.00 46.92           C  
ATOM   2962  CG1 ILE A 397      36.181  16.547  -0.455  1.00 42.23           C  
ATOM   2963  CG2 ILE A 397      37.195  15.816   1.732  1.00 36.01           C  
ATOM   2964  CD1 ILE A 397      35.052  17.465  -0.018  1.00 34.59           C  
ATOM   2965  N   LEU A 398      40.157  18.218   1.263  1.00 44.58           N  
ATOM   2966  CA  LEU A 398      41.291  18.561   2.113  1.00 41.15           C  
ATOM   2967  C   LEU A 398      41.000  19.835   2.897  1.00 48.59           C  
ATOM   2968  O   LEU A 398      41.122  19.863   4.124  1.00 54.49           O  
ATOM   2969  CB  LEU A 398      42.547  18.717   1.261  1.00 45.99           C  
ATOM   2970  CG  LEU A 398      43.901  18.583   1.949  1.00 49.02           C  
ATOM   2971  CD1 LEU A 398      44.029  17.238   2.650  1.00 50.96           C  
ATOM   2972  CD2 LEU A 398      44.990  18.746   0.916  1.00 54.65           C  
ATOM   2973  N   GLY A 399      40.545  20.884   2.203  1.00 43.05           N  
ATOM   2974  CA  GLY A 399      40.197  22.119   2.883  1.00 47.63           C  
ATOM   2975  C   GLY A 399      39.033  21.977   3.844  1.00 46.48           C  
ATOM   2976  O   GLY A 399      38.934  22.728   4.818  1.00 46.97           O  
ATOM   2977  N   GLU A 400      38.136  21.020   3.590  1.00 39.04           N  
ATOM   2978  CA  GLU A 400      37.035  20.792   4.520  1.00 41.49           C  
ATOM   2979  C   GLU A 400      37.527  20.218   5.840  1.00 49.97           C  
ATOM   2980  O   GLU A 400      36.966  20.528   6.895  1.00 46.69           O  
ATOM   2981  CB  GLU A 400      35.986  19.870   3.895  1.00 41.87           C  
ATOM   2982  CG  GLU A 400      34.702  19.775   4.716  1.00 52.81           C  
ATOM   2983  CD  GLU A 400      33.638  18.897   4.084  1.00 51.28           C  
ATOM   2984  OE1 GLU A 400      33.741  18.606   2.876  1.00 52.79           O  
ATOM   2985  OE2 GLU A 400      32.695  18.498   4.801  1.00 57.61           O  
ATOM   2986  N   MET A 401      38.578  19.399   5.806  1.00 51.31           N  
ATOM   2987  CA  MET A 401      39.102  18.831   7.042  1.00 50.02           C  
ATOM   2988  C   MET A 401      39.626  19.917   7.970  1.00 51.35           C  
ATOM   2989  O   MET A 401      39.479  19.818   9.191  1.00 62.25           O  
ATOM   2990  CB  MET A 401      40.195  17.815   6.725  1.00 46.76           C  
ATOM   2991  CG  MET A 401      39.688  16.607   5.970  1.00 49.69           C  
ATOM   2992  SD  MET A 401      38.606  15.584   6.989  1.00 46.84           S  
ATOM   2993  CE  MET A 401      37.220  15.354   5.881  1.00 46.34           C  
ATOM   2994  N   LEU A 402      40.234  20.966   7.415  1.00 54.54           N  
ATOM   2995  CA  LEU A 402      40.739  22.042   8.263  1.00 61.79           C  
ATOM   2996  C   LEU A 402      39.616  22.942   8.762  1.00 63.99           C  
ATOM   2997  O   LEU A 402      39.617  23.355   9.927  1.00 72.14           O  
ATOM   2998  CB  LEU A 402      41.778  22.879   7.515  1.00 53.17           C  
ATOM   2999  CG  LEU A 402      43.036  22.200   6.976  1.00 49.75           C  
ATOM   3000  CD1 LEU A 402      42.869  21.893   5.510  1.00 64.39           C  
ATOM   3001  CD2 LEU A 402      44.242  23.088   7.185  1.00 63.81           C  
ATOM   3002  N   ILE A 403      38.650  23.247   7.900  1.00 59.67           N  
ATOM   3003  CA  ILE A 403      37.633  24.234   8.244  1.00 61.13           C  
ATOM   3004  C   ILE A 403      36.534  23.619   9.100  1.00 67.00           C  
ATOM   3005  O   ILE A 403      36.121  24.202  10.108  1.00 68.67           O  
ATOM   3006  CB  ILE A 403      37.063  24.885   6.970  1.00 55.00           C  
ATOM   3007  CG1 ILE A 403      38.113  25.793   6.332  1.00 62.53           C  
ATOM   3008  CG2 ILE A 403      35.792  25.655   7.288  1.00 65.80           C  
ATOM   3009  CD1 ILE A 403      37.655  26.457   5.060  1.00 67.17           C  
ATOM   3010  N   SER A 404      36.048  22.436   8.730  1.00 67.74           N  
ATOM   3011  CA  SER A 404      34.799  21.952   9.327  1.00 76.22           C  
ATOM   3012  C   SER A 404      34.982  21.541  10.786  1.00 80.04           C  
ATOM   3013  O   SER A 404      34.386  22.185  11.655  1.00 82.80           O  
ATOM   3014  CB  SER A 404      34.203  20.808   8.493  1.00 77.29           C  
ATOM   3015  OG  SER A 404      32.934  20.430   9.001  1.00 78.19           O  
ATOM   3016  N   PRO A 405      35.791  20.520  11.120  1.00 79.19           N  
ATOM   3017  CA  PRO A 405      35.866  20.108  12.541  1.00 86.48           C  
ATOM   3018  C   PRO A 405      36.305  21.225  13.473  1.00 85.44           C  
ATOM   3019  O   PRO A 405      35.816  21.315  14.605  1.00 82.07           O  
ATOM   3020  CB  PRO A 405      36.873  18.952  12.515  1.00 83.45           C  
ATOM   3021  CG  PRO A 405      36.848  18.452  11.113  1.00 80.12           C  
ATOM   3022  CD  PRO A 405      36.660  19.679  10.280  1.00 65.71           C  
ATOM   3023  N   VAL A 406      37.210  22.091  13.013  1.00 87.31           N  
ATOM   3024  CA  VAL A 406      37.631  23.230  13.821  1.00 87.48           C  
ATOM   3025  C   VAL A 406      36.551  24.307  13.847  1.00 82.41           C  
ATOM   3026  O   VAL A 406      36.335  24.951  14.879  1.00 81.48           O  
ATOM   3027  CB  VAL A 406      38.971  23.777  13.288  1.00 85.12           C  
ATOM   3028  CG1 VAL A 406      39.492  24.914  14.161  1.00 82.34           C  
ATOM   3029  CG2 VAL A 406      39.990  22.653  13.191  1.00 81.96           C  
ATOM   3030  N   GLY A 407      35.823  24.481  12.739  1.00 83.05           N  
ATOM   3031  CA  GLY A 407      34.998  25.670  12.570  1.00 84.02           C  
ATOM   3032  C   GLY A 407      33.898  25.828  13.604  1.00 87.88           C  
ATOM   3033  O   GLY A 407      33.626  26.943  14.059  1.00 86.84           O  
ATOM   3034  N   LEU A 408      33.232  24.727  13.971  1.00 91.05           N  
ATOM   3035  CA  LEU A 408      32.181  24.817  14.982  1.00 90.71           C  
ATOM   3036  C   LEU A 408      32.738  25.290  16.321  1.00 93.41           C  
ATOM   3037  O   LEU A 408      32.050  25.998  17.066  1.00 88.53           O  
ATOM   3038  CB  LEU A 408      31.467  23.467  15.152  1.00 91.18           C  
ATOM   3039  CG  LEU A 408      30.936  22.689  13.937  1.00 91.46           C  
ATOM   3040  CD1 LEU A 408      31.968  21.696  13.444  1.00 89.03           C  
ATOM   3041  CD2 LEU A 408      29.618  21.965  14.219  1.00 78.26           C  
ATOM   3042  N   SER A 409      33.984  24.926  16.634  1.00 94.50           N  
ATOM   3043  CA  SER A 409      34.595  25.347  17.892  1.00 87.26           C  
ATOM   3044  C   SER A 409      34.887  26.845  17.903  1.00 95.70           C  
ATOM   3045  O   SER A 409      34.611  27.528  18.896  1.00100.90           O  
ATOM   3046  CB  SER A 409      35.871  24.540  18.139  1.00 86.33           C  
ATOM   3047  OG  SER A 409      36.729  25.174  19.070  1.00 92.03           O  
ATOM   3048  N   VAL A 410      35.419  27.381  16.800  1.00 97.02           N  
ATOM   3049  CA  VAL A 410      35.835  28.781  16.755  1.00 89.00           C  
ATOM   3050  C   VAL A 410      34.660  29.744  16.875  1.00 90.93           C  
ATOM   3051  O   VAL A 410      34.862  30.926  17.175  1.00 96.21           O  
ATOM   3052  CB  VAL A 410      36.618  29.062  15.458  1.00 93.48           C  
ATOM   3053  CG1 VAL A 410      37.306  27.807  14.987  1.00 95.03           C  
ATOM   3054  CG2 VAL A 410      35.695  29.584  14.372  1.00 95.92           C  
ATOM   3055  N   THR A 411      33.437  29.272  16.654  1.00 95.12           N  
ATOM   3056  CA  THR A 411      32.265  30.137  16.676  1.00 95.72           C  
ATOM   3057  C   THR A 411      31.848  30.470  18.106  1.00 91.14           C  
ATOM   3058  O   THR A 411      31.614  31.631  18.445  1.00 97.15           O  
ATOM   3059  CB  THR A 411      31.077  29.492  15.938  1.00 94.15           C  
ATOM   3060  OG1 THR A 411      31.545  28.809  14.770  1.00 97.86           O  
ATOM   3061  CG2 THR A 411      30.059  30.552  15.531  1.00 88.60           C  
ATOM   3062  N   SER A 425      23.025  26.948  14.556  1.00 84.83           N  
ATOM   3063  CA  SER A 425      24.110  27.840  14.953  1.00105.02           C  
ATOM   3064  C   SER A 425      24.272  28.989  13.962  1.00 98.85           C  
ATOM   3065  O   SER A 425      23.714  28.956  12.868  1.00 92.82           O  
ATOM   3066  CB  SER A 425      25.426  27.067  15.060  1.00 94.33           C  
ATOM   3067  OG  SER A 425      25.286  25.913  15.864  1.00 94.42           O  
ATOM   3068  N   MET A 426      25.042  30.010  14.349  1.00 87.96           N  
ATOM   3069  CA  MET A 426      25.476  31.003  13.374  1.00 78.17           C  
ATOM   3070  C   MET A 426      26.447  30.406  12.363  1.00 88.43           C  
ATOM   3071  O   MET A 426      26.611  30.954  11.264  1.00 85.08           O  
ATOM   3072  CB  MET A 426      26.111  32.194  14.089  1.00 91.29           C  
ATOM   3073  CG  MET A 426      26.611  33.272  13.160  1.00 82.52           C  
ATOM   3074  SD  MET A 426      26.806  34.858  13.969  1.00133.56           S  
ATOM   3075  CE  MET A 426      25.825  35.866  12.864  1.00 72.45           C  
ATOM   3076  N   TRP A 427      27.088  29.291  12.712  1.00 92.53           N  
ATOM   3077  CA  TRP A 427      27.963  28.577  11.791  1.00 79.84           C  
ATOM   3078  C   TRP A 427      27.191  27.654  10.860  1.00 68.07           C  
ATOM   3079  O   TRP A 427      27.632  27.414   9.729  1.00 75.22           O  
ATOM   3080  CB  TRP A 427      29.007  27.775  12.573  1.00 82.86           C  
ATOM   3081  CG  TRP A 427      30.299  27.639  11.843  1.00 92.29           C  
ATOM   3082  CD1 TRP A 427      31.252  28.597  11.690  1.00 93.35           C  
ATOM   3083  CD2 TRP A 427      30.784  26.479  11.156  1.00 92.85           C  
ATOM   3084  NE1 TRP A 427      32.303  28.113  10.951  1.00 97.43           N  
ATOM   3085  CE2 TRP A 427      32.041  26.813  10.611  1.00 86.08           C  
ATOM   3086  CE3 TRP A 427      30.280  25.192  10.949  1.00 85.46           C  
ATOM   3087  CZ2 TRP A 427      32.798  25.908   9.872  1.00 79.64           C  
ATOM   3088  CZ3 TRP A 427      31.035  24.295  10.216  1.00 87.94           C  
ATOM   3089  CH2 TRP A 427      32.280  24.657   9.688  1.00 85.29           C  
ATOM   3090  N   PHE A 428      26.047  27.135  11.315  1.00 72.41           N  
ATOM   3091  CA  PHE A 428      25.116  26.444  10.428  1.00 71.57           C  
ATOM   3092  C   PHE A 428      24.740  27.325   9.239  1.00 70.72           C  
ATOM   3093  O   PHE A 428      24.488  26.818   8.139  1.00 69.52           O  
ATOM   3094  CB  PHE A 428      23.872  26.045  11.235  1.00 85.29           C  
ATOM   3095  CG  PHE A 428      23.184  24.784  10.759  1.00 80.35           C  
ATOM   3096  CD1 PHE A 428      22.810  24.625   9.435  1.00 62.61           C  
ATOM   3097  CD2 PHE A 428      22.885  23.767  11.657  1.00 76.50           C  
ATOM   3098  CE1 PHE A 428      22.161  23.468   9.009  1.00 57.33           C  
ATOM   3099  CE2 PHE A 428      22.240  22.608  11.240  1.00 67.72           C  
ATOM   3100  CZ  PHE A 428      21.878  22.459   9.913  1.00 69.08           C  
ATOM   3101  N   LEU A 429      24.724  28.647   9.440  1.00 60.17           N  
ATOM   3102  CA  LEU A 429      24.314  29.597   8.413  1.00 52.18           C  
ATOM   3103  C   LEU A 429      25.382  29.858   7.360  1.00 49.57           C  
ATOM   3104  O   LEU A 429      25.039  30.294   6.255  1.00 43.67           O  
ATOM   3105  CB  LEU A 429      23.917  30.925   9.057  1.00 56.70           C  
ATOM   3106  CG  LEU A 429      22.425  31.139   9.301  1.00 59.08           C  
ATOM   3107  CD1 LEU A 429      22.227  32.416  10.082  1.00 58.03           C  
ATOM   3108  CD2 LEU A 429      21.677  31.192   7.978  1.00 51.28           C  
ATOM   3109  N   SER A 430      26.658  29.620   7.671  1.00 54.38           N  
ATOM   3110  CA  SER A 430      27.701  29.804   6.668  1.00 42.53           C  
ATOM   3111  C   SER A 430      27.454  28.944   5.435  1.00 42.84           C  
ATOM   3112  O   SER A 430      27.807  29.345   4.322  1.00 42.56           O  
ATOM   3113  CB  SER A 430      29.073  29.491   7.266  1.00 43.61           C  
ATOM   3114  OG  SER A 430      29.120  28.183   7.813  1.00 48.68           O  
ATOM   3115  N   SER A 431      26.839  27.772   5.606  1.00 45.45           N  
ATOM   3116  CA  SER A 431      26.573  26.908   4.462  1.00 32.80           C  
ATOM   3117  C   SER A 431      25.430  27.445   3.615  1.00 42.88           C  
ATOM   3118  O   SER A 431      25.420  27.270   2.391  1.00 39.87           O  
ATOM   3119  CB  SER A 431      26.255  25.486   4.927  1.00 42.03           C  
ATOM   3120  OG  SER A 431      27.322  24.957   5.692  1.00 64.12           O  
ATOM   3121  N   SER A 432      24.446  28.082   4.247  1.00 38.25           N  
ATOM   3122  CA  SER A 432      23.328  28.621   3.483  1.00 34.22           C  
ATOM   3123  C   SER A 432      23.753  29.842   2.674  1.00 40.62           C  
ATOM   3124  O   SER A 432      23.313  30.027   1.531  1.00 38.74           O  
ATOM   3125  CB  SER A 432      22.175  28.963   4.424  1.00 37.08           C  
ATOM   3126  OG  SER A 432      20.992  29.220   3.692  1.00 39.61           O  
ATOM   3127  N   VAL A 433      24.630  30.671   3.238  1.00 37.19           N  
ATOM   3128  CA  VAL A 433      25.077  31.867   2.534  1.00 39.88           C  
ATOM   3129  C   VAL A 433      25.986  31.499   1.369  1.00 37.80           C  
ATOM   3130  O   VAL A 433      25.895  32.090   0.286  1.00 35.18           O  
ATOM   3131  CB  VAL A 433      25.763  32.829   3.520  1.00 46.11           C  
ATOM   3132  CG1 VAL A 433      26.225  34.086   2.810  1.00 46.45           C  
ATOM   3133  CG2 VAL A 433      24.810  33.175   4.633  1.00 38.74           C  
ATOM   3134  N   GLY A 434      26.870  30.518   1.566  1.00 34.26           N  
ATOM   3135  CA  GLY A 434      27.712  30.065   0.471  1.00 34.56           C  
ATOM   3136  C   GLY A 434      26.907  29.553  -0.710  1.00 37.70           C  
ATOM   3137  O   GLY A 434      27.236  29.830  -1.866  1.00 37.42           O  
ATOM   3138  N   SER A 435      25.836  28.807  -0.435  1.00 35.34           N  
ATOM   3139  CA  SER A 435      24.978  28.331  -1.514  1.00 32.26           C  
ATOM   3140  C   SER A 435      24.126  29.455  -2.082  1.00 37.46           C  
ATOM   3141  O   SER A 435      23.759  29.414  -3.262  1.00 36.33           O  
ATOM   3142  CB  SER A 435      24.091  27.189  -1.018  1.00 36.93           C  
ATOM   3143  OG  SER A 435      24.855  26.182  -0.376  1.00 52.78           O  
ATOM   3144  N   ALA A 436      23.790  30.452  -1.259  1.00 43.88           N  
ATOM   3145  CA  ALA A 436      23.075  31.622  -1.758  1.00 33.13           C  
ATOM   3146  C   ALA A 436      23.943  32.404  -2.730  1.00 28.15           C  
ATOM   3147  O   ALA A 436      23.506  32.746  -3.834  1.00 34.50           O  
ATOM   3148  CB  ALA A 436      22.632  32.510  -0.596  1.00 37.20           C  
ATOM   3149  N   LEU A 437      25.183  32.694  -2.331  1.00 34.63           N  
ATOM   3150  CA  LEU A 437      26.147  33.263  -3.264  1.00 31.76           C  
ATOM   3151  C   LEU A 437      26.281  32.390  -4.503  1.00 33.20           C  
ATOM   3152  O   LEU A 437      26.382  32.902  -5.623  1.00 38.52           O  
ATOM   3153  CB  LEU A 437      27.500  33.440  -2.574  1.00 34.35           C  
ATOM   3154  CG  LEU A 437      28.692  33.922  -3.406  1.00 46.06           C  
ATOM   3155  CD1 LEU A 437      28.430  35.282  -4.047  1.00 36.29           C  
ATOM   3156  CD2 LEU A 437      29.940  33.969  -2.542  1.00 41.62           C  
ATOM   3157  N   ASN A 438      26.251  31.066  -4.326  1.00 37.24           N  
ATOM   3158  CA  ASN A 438      26.359  30.171  -5.473  1.00 34.80           C  
ATOM   3159  C   ASN A 438      25.211  30.375  -6.452  1.00 35.62           C  
ATOM   3160  O   ASN A 438      25.408  30.296  -7.668  1.00 37.29           O  
ATOM   3161  CB  ASN A 438      26.409  28.717  -5.012  1.00 31.91           C  
ATOM   3162  CG  ASN A 438      27.809  28.267  -4.679  1.00 34.62           C  
ATOM   3163  OD1 ASN A 438      28.780  28.956  -4.992  1.00 34.59           O  
ATOM   3164  ND2 ASN A 438      27.927  27.101  -4.050  1.00 34.67           N  
ATOM   3165  N   ALA A 439      24.005  30.640  -5.942  1.00 36.12           N  
ATOM   3166  CA  ALA A 439      22.851  30.841  -6.811  1.00 32.59           C  
ATOM   3167  C   ALA A 439      23.070  31.972  -7.808  1.00 35.29           C  
ATOM   3168  O   ALA A 439      22.430  31.992  -8.865  1.00 31.50           O  
ATOM   3169  CB  ALA A 439      21.604  31.110  -5.967  1.00 27.52           C  
ATOM   3170  N   GLN A 440      23.970  32.904  -7.501  1.00 35.13           N  
ATOM   3171  CA  GLN A 440      24.325  33.969  -8.428  1.00 40.94           C  
ATOM   3172  C   GLN A 440      25.511  33.597  -9.308  1.00 39.02           C  
ATOM   3173  O   GLN A 440      25.504  33.882 -10.509  1.00 43.49           O  
ATOM   3174  CB  GLN A 440      24.641  35.250  -7.652  1.00 45.74           C  
ATOM   3175  CG  GLN A 440      23.590  35.619  -6.624  1.00 38.07           C  
ATOM   3176  CD  GLN A 440      22.277  35.999  -7.264  1.00 49.40           C  
ATOM   3177  OE1 GLN A 440      22.243  36.805  -8.191  1.00 47.30           O  
ATOM   3178  NE2 GLN A 440      21.187  35.406  -6.787  1.00 46.93           N  
ATOM   3179  N   LEU A 441      26.526  32.946  -8.736  1.00 35.24           N  
ATOM   3180  CA  LEU A 441      27.773  32.725  -9.461  1.00 27.39           C  
ATOM   3181  C   LEU A 441      27.654  31.625 -10.509  1.00 40.04           C  
ATOM   3182  O   LEU A 441      28.186  31.771 -11.615  1.00 38.51           O  
ATOM   3183  CB  LEU A 441      28.894  32.396  -8.480  1.00 32.78           C  
ATOM   3184  CG  LEU A 441      29.169  33.422  -7.380  1.00 39.01           C  
ATOM   3185  CD1 LEU A 441      30.406  33.023  -6.599  1.00 32.66           C  
ATOM   3186  CD2 LEU A 441      29.320  34.826  -7.952  1.00 38.67           C  
ATOM   3187  N   VAL A 442      26.965  30.523 -10.190  1.00 36.65           N  
ATOM   3188  CA  VAL A 442      26.959  29.364 -11.080  1.00 32.57           C  
ATOM   3189  C   VAL A 442      26.303  29.676 -12.416  1.00 36.94           C  
ATOM   3190  O   VAL A 442      26.539  28.965 -13.400  1.00 39.70           O  
ATOM   3191  CB  VAL A 442      26.273  28.148 -10.414  1.00 29.26           C  
ATOM   3192  CG1 VAL A 442      26.949  27.804  -9.101  1.00 27.25           C  
ATOM   3193  CG2 VAL A 442      24.785  28.393 -10.228  1.00 25.31           C  
ATOM   3194  N   THR A 443      25.474  30.720 -12.480  1.00 41.02           N  
ATOM   3195  CA  THR A 443      24.931  31.162 -13.758  1.00 42.27           C  
ATOM   3196  C   THR A 443      26.000  31.746 -14.677  1.00 38.36           C  
ATOM   3197  O   THR A 443      25.747  31.895 -15.878  1.00 45.12           O  
ATOM   3198  CB  THR A 443      23.813  32.189 -13.533  1.00 47.40           C  
ATOM   3199  OG1 THR A 443      24.312  33.295 -12.771  1.00 41.29           O  
ATOM   3200  CG2 THR A 443      22.648  31.555 -12.783  1.00 38.90           C  
ATOM   3201  N   LEU A 444      27.182  32.075 -14.151  1.00 38.19           N  
ATOM   3202  CA  LEU A 444      28.285  32.538 -14.984  1.00 35.29           C  
ATOM   3203  C   LEU A 444      29.079  31.402 -15.608  1.00 42.30           C  
ATOM   3204  O   LEU A 444      29.998  31.670 -16.391  1.00 38.04           O  
ATOM   3205  CB  LEU A 444      29.248  33.405 -14.177  1.00 33.98           C  
ATOM   3206  CG  LEU A 444      28.674  34.606 -13.439  1.00 35.49           C  
ATOM   3207  CD1 LEU A 444      29.796  35.312 -12.714  1.00 32.90           C  
ATOM   3208  CD2 LEU A 444      27.986  35.533 -14.418  1.00 41.30           C  
ATOM   3209  N   TYR A 445      28.770  30.152 -15.276  1.00 45.63           N  
ATOM   3210  CA  TYR A 445      29.534  29.022 -15.783  1.00 36.23           C  
ATOM   3211  C   TYR A 445      28.894  28.467 -17.047  1.00 33.84           C  
ATOM   3212  O   TYR A 445      27.691  28.196 -17.076  1.00 37.67           O  
ATOM   3213  CB  TYR A 445      29.652  27.911 -14.738  1.00 31.94           C  
ATOM   3214  CG  TYR A 445      30.444  26.731 -15.253  1.00 41.16           C  
ATOM   3215  CD1 TYR A 445      31.832  26.731 -15.193  1.00 36.49           C  
ATOM   3216  CD2 TYR A 445      29.810  25.630 -15.826  1.00 39.96           C  
ATOM   3217  CE1 TYR A 445      32.568  25.668 -15.675  1.00 33.52           C  
ATOM   3218  CE2 TYR A 445      30.540  24.561 -16.314  1.00 39.82           C  
ATOM   3219  CZ  TYR A 445      31.920  24.587 -16.233  1.00 33.77           C  
ATOM   3220  OH  TYR A 445      32.659  23.532 -16.709  1.00 37.07           O  
ATOM   3221  N   ASN A 446      29.709  28.302 -18.082  1.00 35.12           N  
ATOM   3222  CA  ASN A 446      29.364  27.550 -19.284  1.00 43.55           C  
ATOM   3223  C   ASN A 446      30.669  27.211 -19.996  1.00 39.35           C  
ATOM   3224  O   ASN A 446      31.759  27.462 -19.472  1.00 38.87           O  
ATOM   3225  CB  ASN A 446      28.394  28.329 -20.178  1.00 28.72           C  
ATOM   3226  CG  ASN A 446      28.785  29.777 -20.332  1.00 40.07           C  
ATOM   3227  OD1 ASN A 446      29.804  30.094 -20.947  1.00 43.29           O  
ATOM   3228  ND2 ASN A 446      27.977  30.669 -19.777  1.00 43.03           N  
ATOM   3229  N   ALA A 447      30.562  26.637 -21.196  1.00 43.65           N  
ATOM   3230  CA  ALA A 447      31.760  26.205 -21.910  1.00 44.88           C  
ATOM   3231  C   ALA A 447      32.640  27.392 -22.283  1.00 52.60           C  
ATOM   3232  O   ALA A 447      33.862  27.355 -22.099  1.00 58.70           O  
ATOM   3233  CB  ALA A 447      31.370  25.403 -23.152  1.00 60.00           C  
ATOM   3234  N   LYS A 448      32.036  28.465 -22.797  1.00 54.49           N  
ATOM   3235  CA  LYS A 448      32.829  29.628 -23.183  1.00 46.47           C  
ATOM   3236  C   LYS A 448      33.475  30.287 -21.969  1.00 43.71           C  
ATOM   3237  O   LYS A 448      34.606  30.781 -22.052  1.00 48.28           O  
ATOM   3238  CB  LYS A 448      31.961  30.629 -23.945  1.00 46.88           C  
ATOM   3239  N   SER A 449      32.785  30.292 -20.830  1.00 40.07           N  
ATOM   3240  CA  SER A 449      33.285  30.942 -19.624  1.00 32.78           C  
ATOM   3241  C   SER A 449      34.054  29.996 -18.708  1.00 45.29           C  
ATOM   3242  O   SER A 449      34.440  30.404 -17.607  1.00 42.32           O  
ATOM   3243  CB  SER A 449      32.128  31.584 -18.849  1.00 39.56           C  
ATOM   3244  OG  SER A 449      31.532  30.668 -17.943  1.00 33.75           O  
ATOM   3245  N   GLU A 450      34.307  28.759 -19.148  1.00 44.32           N  
ATOM   3246  CA  GLU A 450      34.829  27.725 -18.257  1.00 35.69           C  
ATOM   3247  C   GLU A 450      36.150  28.133 -17.614  1.00 38.48           C  
ATOM   3248  O   GLU A 450      36.258  28.220 -16.386  1.00 45.87           O  
ATOM   3249  CB  GLU A 450      35.007  26.410 -19.016  1.00 38.97           C  
ATOM   3250  CG  GLU A 450      35.829  25.394 -18.230  1.00 37.28           C  
ATOM   3251  CD  GLU A 450      36.093  24.126 -19.006  1.00 39.60           C  
ATOM   3252  OE1 GLU A 450      35.192  23.694 -19.752  1.00 46.11           O  
ATOM   3253  OE2 GLU A 450      37.200  23.562 -18.873  1.00 42.11           O  
ATOM   3254  N   VAL A 451      37.180  28.358 -18.432  1.00 37.34           N  
ATOM   3255  CA  VAL A 451      38.516  28.574 -17.885  1.00 41.02           C  
ATOM   3256  C   VAL A 451      38.572  29.856 -17.066  1.00 36.89           C  
ATOM   3257  O   VAL A 451      39.281  29.923 -16.056  1.00 35.11           O  
ATOM   3258  CB  VAL A 451      39.564  28.568 -19.014  1.00 37.69           C  
ATOM   3259  CG1 VAL A 451      40.962  28.739 -18.450  1.00 33.07           C  
ATOM   3260  CG2 VAL A 451      39.468  27.276 -19.818  1.00 40.14           C  
ATOM   3261  N   ALA A 452      37.823  30.884 -17.465  1.00 36.43           N  
ATOM   3262  CA  ALA A 452      37.813  32.120 -16.691  1.00 40.01           C  
ATOM   3263  C   ALA A 452      37.117  31.925 -15.351  1.00 45.02           C  
ATOM   3264  O   ALA A 452      37.617  32.377 -14.316  1.00 34.29           O  
ATOM   3265  CB  ALA A 452      37.144  33.237 -17.491  1.00 43.51           C  
ATOM   3266  N   TYR A 453      35.969  31.247 -15.355  1.00 36.31           N  
ATOM   3267  CA  TYR A 453      35.228  31.002 -14.122  1.00 38.00           C  
ATOM   3268  C   TYR A 453      36.099  30.296 -13.086  1.00 41.85           C  
ATOM   3269  O   TYR A 453      36.274  30.786 -11.964  1.00 34.96           O  
ATOM   3270  CB  TYR A 453      33.969  30.188 -14.439  1.00 36.47           C  
ATOM   3271  CG  TYR A 453      33.094  29.843 -13.254  1.00 37.31           C  
ATOM   3272  CD1 TYR A 453      33.379  28.742 -12.457  1.00 36.40           C  
ATOM   3273  CD2 TYR A 453      31.961  30.594 -12.954  1.00 38.33           C  
ATOM   3274  CE1 TYR A 453      32.580  28.410 -11.381  1.00 43.30           C  
ATOM   3275  CE2 TYR A 453      31.151  30.265 -11.877  1.00 39.92           C  
ATOM   3276  CZ  TYR A 453      31.468  29.170 -11.095  1.00 36.37           C  
ATOM   3277  OH  TYR A 453      30.678  28.826 -10.021  1.00 37.03           O  
ATOM   3278  N   PHE A 454      36.664  29.140 -13.450  1.00 45.56           N  
ATOM   3279  CA  PHE A 454      37.512  28.402 -12.517  1.00 42.47           C  
ATOM   3280  C   PHE A 454      38.706  29.236 -12.074  1.00 42.67           C  
ATOM   3281  O   PHE A 454      38.985  29.359 -10.876  1.00 43.48           O  
ATOM   3282  CB  PHE A 454      37.997  27.097 -13.150  1.00 38.19           C  
ATOM   3283  CG  PHE A 454      36.951  26.030 -13.227  1.00 40.60           C  
ATOM   3284  CD1 PHE A 454      36.299  25.591 -12.085  1.00 39.27           C  
ATOM   3285  CD2 PHE A 454      36.637  25.445 -14.442  1.00 34.77           C  
ATOM   3286  CE1 PHE A 454      35.337  24.597 -12.159  1.00 42.83           C  
ATOM   3287  CE2 PHE A 454      35.681  24.452 -14.524  1.00 35.54           C  
ATOM   3288  CZ  PHE A 454      35.029  24.027 -13.384  1.00 38.12           C  
ATOM   3289  N   SER A 455      39.427  29.815 -13.033  1.00 38.24           N  
ATOM   3290  CA  SER A 455      40.675  30.499 -12.711  1.00 39.88           C  
ATOM   3291  C   SER A 455      40.426  31.730 -11.845  1.00 41.41           C  
ATOM   3292  O   SER A 455      41.080  31.921 -10.812  1.00 36.93           O  
ATOM   3293  CB  SER A 455      41.403  30.866 -14.006  1.00 34.56           C  
ATOM   3294  OG  SER A 455      42.470  31.761 -13.768  1.00 67.09           O  
ATOM   3295  N   TYR A 456      39.467  32.567 -12.242  1.00 38.77           N  
ATOM   3296  CA  TYR A 456      39.207  33.818 -11.532  1.00 48.13           C  
ATOM   3297  C   TYR A 456      38.713  33.562 -10.109  1.00 52.72           C  
ATOM   3298  O   TYR A 456      39.310  34.039  -9.135  1.00 48.03           O  
ATOM   3299  CB  TYR A 456      38.204  34.651 -12.336  1.00 41.51           C  
ATOM   3300  CG  TYR A 456      37.592  35.819 -11.610  1.00 49.75           C  
ATOM   3301  CD1 TYR A 456      38.254  37.036 -11.523  1.00 65.95           C  
ATOM   3302  CD2 TYR A 456      36.331  35.716 -11.041  1.00 57.80           C  
ATOM   3303  CE1 TYR A 456      37.683  38.114 -10.868  1.00 64.50           C  
ATOM   3304  CE2 TYR A 456      35.753  36.782 -10.385  1.00 64.80           C  
ATOM   3305  CZ  TYR A 456      36.431  37.980 -10.301  1.00 62.50           C  
ATOM   3306  OH  TYR A 456      35.849  39.040  -9.645  1.00 67.33           O  
ATOM   3307  N   PHE A 457      37.626  32.797  -9.968  1.00 53.41           N  
ATOM   3308  CA  PHE A 457      37.096  32.510  -8.637  1.00 51.40           C  
ATOM   3309  C   PHE A 457      38.043  31.629  -7.830  1.00 55.20           C  
ATOM   3310  O   PHE A 457      38.100  31.748  -6.600  1.00 49.20           O  
ATOM   3311  CB  PHE A 457      35.713  31.860  -8.744  1.00 40.43           C  
ATOM   3312  CG  PHE A 457      34.639  32.799  -9.225  1.00 53.69           C  
ATOM   3313  CD1 PHE A 457      34.107  33.758  -8.375  1.00 50.32           C  
ATOM   3314  CD2 PHE A 457      34.160  32.725 -10.526  1.00 49.53           C  
ATOM   3315  CE1 PHE A 457      33.120  34.628  -8.812  1.00 49.55           C  
ATOM   3316  CE2 PHE A 457      33.173  33.593 -10.969  1.00 50.74           C  
ATOM   3317  CZ  PHE A 457      32.652  34.544 -10.110  1.00 45.22           C  
ATOM   3318  N   GLY A 458      38.791  30.749  -8.495  1.00 47.19           N  
ATOM   3319  CA  GLY A 458      39.770  29.946  -7.783  1.00 45.70           C  
ATOM   3320  C   GLY A 458      40.902  30.783  -7.224  1.00 47.94           C  
ATOM   3321  O   GLY A 458      41.320  30.595  -6.078  1.00 50.79           O  
ATOM   3322  N   LEU A 459      41.408  31.727  -8.018  1.00 46.19           N  
ATOM   3323  CA  LEU A 459      42.453  32.615  -7.522  1.00 46.35           C  
ATOM   3324  C   LEU A 459      41.925  33.532  -6.428  1.00 53.92           C  
ATOM   3325  O   LEU A 459      42.610  33.765  -5.425  1.00 57.80           O  
ATOM   3326  CB  LEU A 459      43.034  33.438  -8.665  1.00 53.40           C  
ATOM   3327  CG  LEU A 459      44.001  34.533  -8.221  1.00 53.05           C  
ATOM   3328  CD1 LEU A 459      45.217  33.920  -7.544  1.00 51.12           C  
ATOM   3329  CD2 LEU A 459      44.407  35.397  -9.400  1.00 52.76           C  
ATOM   3330  N   GLY A 460      40.709  34.057  -6.601  1.00 49.83           N  
ATOM   3331  CA  GLY A 460      40.145  34.940  -5.594  1.00 45.30           C  
ATOM   3332  C   GLY A 460      40.069  34.295  -4.224  1.00 50.15           C  
ATOM   3333  O   GLY A 460      40.273  34.956  -3.204  1.00 60.27           O  
ATOM   3334  N   SER A 461      39.787  32.991  -4.182  1.00 53.44           N  
ATOM   3335  CA  SER A 461      39.708  32.286  -2.905  1.00 55.09           C  
ATOM   3336  C   SER A 461      41.084  32.158  -2.261  1.00 53.02           C  
ATOM   3337  O   SER A 461      41.239  32.387  -1.056  1.00 52.94           O  
ATOM   3338  CB  SER A 461      39.081  30.909  -3.111  1.00 50.10           C  
ATOM   3339  OG  SER A 461      37.906  31.007  -3.893  1.00 54.03           O  
ATOM   3340  N   VAL A 462      42.095  31.787  -3.051  1.00 55.63           N  
ATOM   3341  CA  VAL A 462      43.446  31.632  -2.515  1.00 57.27           C  
ATOM   3342  C   VAL A 462      43.966  32.966  -1.991  1.00 55.20           C  
ATOM   3343  O   VAL A 462      44.533  33.046  -0.896  1.00 57.98           O  
ATOM   3344  CB  VAL A 462      44.383  31.045  -3.587  1.00 52.45           C  
ATOM   3345  CG1 VAL A 462      45.828  31.063  -3.107  1.00 47.82           C  
ATOM   3346  CG2 VAL A 462      43.951  29.632  -3.949  1.00 46.26           C  
ATOM   3347  N   VAL A 463      43.773  34.034  -2.767  1.00 52.01           N  
ATOM   3348  CA  VAL A 463      44.234  35.358  -2.354  1.00 55.97           C  
ATOM   3349  C   VAL A 463      43.554  35.779  -1.055  1.00 57.79           C  
ATOM   3350  O   VAL A 463      44.208  36.245  -0.115  1.00 54.83           O  
ATOM   3351  CB  VAL A 463      44.000  36.378  -3.484  1.00 52.86           C  
ATOM   3352  CG1 VAL A 463      44.098  37.799  -2.961  1.00 38.15           C  
ATOM   3353  CG2 VAL A 463      45.002  36.148  -4.605  1.00 49.40           C  
ATOM   3354  N   LEU A 464      42.231  35.608  -0.978  1.00 51.19           N  
ATOM   3355  CA  LEU A 464      41.522  35.904   0.264  1.00 49.72           C  
ATOM   3356  C   LEU A 464      42.031  35.046   1.415  1.00 54.11           C  
ATOM   3357  O   LEU A 464      41.964  35.463   2.578  1.00 56.33           O  
ATOM   3358  CB  LEU A 464      40.018  35.714   0.064  1.00 48.05           C  
ATOM   3359  CG  LEU A 464      39.360  36.858  -0.712  1.00 52.75           C  
ATOM   3360  CD1 LEU A 464      38.022  36.450  -1.293  1.00 49.48           C  
ATOM   3361  CD2 LEU A 464      39.202  38.074   0.185  1.00 55.82           C  
ATOM   3362  N   GLY A 465      42.552  33.856   1.115  1.00 55.84           N  
ATOM   3363  CA  GLY A 465      43.203  33.066   2.143  1.00 63.25           C  
ATOM   3364  C   GLY A 465      44.522  33.660   2.589  1.00 65.41           C  
ATOM   3365  O   GLY A 465      44.918  33.500   3.747  1.00 59.56           O  
ATOM   3366  N   ILE A 466      45.222  34.349   1.685  1.00 62.89           N  
ATOM   3367  CA  ILE A 466      46.447  35.044   2.070  1.00 70.04           C  
ATOM   3368  C   ILE A 466      46.126  36.181   3.032  1.00 71.94           C  
ATOM   3369  O   ILE A 466      46.779  36.343   4.069  1.00 72.82           O  
ATOM   3370  CB  ILE A 466      47.194  35.555   0.823  1.00 70.74           C  
ATOM   3371  CG1 ILE A 466      47.737  34.384   0.001  1.00 63.57           C  
ATOM   3372  CG2 ILE A 466      48.324  36.497   1.221  1.00 60.72           C  
ATOM   3373  CD1 ILE A 466      49.084  33.877   0.479  1.00 71.06           C  
ATOM   3374  N   VAL A 467      45.107  36.981   2.704  1.00 61.83           N  
ATOM   3375  CA  VAL A 467      44.701  38.082   3.575  1.00 62.19           C  
ATOM   3376  C   VAL A 467      44.351  37.566   4.964  1.00 66.30           C  
ATOM   3377  O   VAL A 467      44.676  38.196   5.977  1.00 71.68           O  
ATOM   3378  CB  VAL A 467      43.529  38.858   2.944  1.00 51.42           C  
ATOM   3379  CG1 VAL A 467      42.968  39.875   3.925  1.00 46.88           C  
ATOM   3380  CG2 VAL A 467      43.980  39.544   1.665  1.00 54.78           C  
ATOM   3381  N   LEU A 468      43.706  36.403   5.038  1.00 60.21           N  
ATOM   3382  CA  LEU A 468      43.361  35.855   6.344  1.00 66.00           C  
ATOM   3383  C   LEU A 468      44.607  35.423   7.107  1.00 67.27           C  
ATOM   3384  O   LEU A 468      44.663  35.557   8.334  1.00 70.56           O  
ATOM   3385  CB  LEU A 468      42.382  34.695   6.182  1.00 68.86           C  
ATOM   3386  CG  LEU A 468      41.482  34.378   7.375  1.00 63.76           C  
ATOM   3387  CD1 LEU A 468      40.331  33.533   6.911  1.00 78.80           C  
ATOM   3388  CD2 LEU A 468      42.230  33.651   8.473  1.00 78.19           C  
ATOM   3389  N   VAL A 469      45.618  34.905   6.406  1.00 70.21           N  
ATOM   3390  CA  VAL A 469      46.876  34.574   7.073  1.00 77.03           C  
ATOM   3391  C   VAL A 469      47.502  35.831   7.668  1.00 71.48           C  
ATOM   3392  O   VAL A 469      48.047  35.808   8.779  1.00 70.14           O  
ATOM   3393  CB  VAL A 469      47.839  33.867   6.099  1.00 72.84           C  
ATOM   3394  CG1 VAL A 469      49.200  33.653   6.749  1.00 75.76           C  
ATOM   3395  CG2 VAL A 469      47.269  32.539   5.651  1.00 70.89           C  
ATOM   3396  N   PHE A 470      47.438  36.946   6.934  1.00 74.04           N  
ATOM   3397  CA  PHE A 470      47.855  38.230   7.488  1.00 72.67           C  
ATOM   3398  C   PHE A 470      47.013  38.593   8.702  1.00 76.84           C  
ATOM   3399  O   PHE A 470      47.540  39.018   9.737  1.00 79.75           O  
ATOM   3400  CB  PHE A 470      47.749  39.327   6.424  1.00 73.30           C  
ATOM   3401  CG  PHE A 470      48.961  39.449   5.559  1.00 77.33           C  
ATOM   3402  CD1 PHE A 470      50.227  39.287   6.092  1.00 78.18           C  
ATOM   3403  CD2 PHE A 470      48.835  39.720   4.208  1.00 81.22           C  
ATOM   3404  CE1 PHE A 470      51.348  39.399   5.293  1.00 78.60           C  
ATOM   3405  CE2 PHE A 470      49.950  39.830   3.404  1.00 82.17           C  
ATOM   3406  CZ  PHE A 470      51.208  39.668   3.945  1.00 83.23           C  
ATOM   3407  N   LEU A 471      45.697  38.428   8.590  1.00 73.89           N  
ATOM   3408  CA  LEU A 471      44.767  38.726   9.671  1.00 69.99           C  
ATOM   3409  C   LEU A 471      44.769  37.666  10.768  1.00 77.00           C  
ATOM   3410  O   LEU A 471      44.188  37.903  11.834  1.00 75.00           O  
ATOM   3411  CB  LEU A 471      43.354  38.900   9.098  1.00 61.83           C  
ATOM   3412  CG  LEU A 471      42.932  40.276   8.556  1.00 61.31           C  
ATOM   3413  CD1 LEU A 471      43.932  40.872   7.568  1.00 66.92           C  
ATOM   3414  CD2 LEU A 471      41.555  40.186   7.918  1.00 59.96           C  
ATOM   3415  N   SER A 472      45.412  36.515  10.542  1.00 81.54           N  
ATOM   3416  CA  SER A 472      45.518  35.498  11.584  1.00 79.14           C  
ATOM   3417  C   SER A 472      46.302  35.987  12.791  1.00 85.89           C  
ATOM   3418  O   SER A 472      46.193  35.389  13.866  1.00 84.94           O  
ATOM   3419  CB  SER A 472      46.174  34.235  11.025  1.00 79.46           C  
ATOM   3420  OG  SER A 472      47.551  34.449  10.767  1.00 89.88           O  
ATOM   3421  N   LYS A 473      47.084  37.058  12.640  1.00 91.58           N  
ATOM   3422  CA  LYS A 473      47.814  37.607  13.780  1.00 96.58           C  
ATOM   3423  C   LYS A 473      46.857  38.106  14.854  1.00101.10           C  
ATOM   3424  O   LYS A 473      47.039  37.827  16.045  1.00101.16           O  
ATOM   3425  CB  LYS A 473      48.746  38.737  13.324  1.00 97.95           C  
ATOM   3426  CG  LYS A 473      48.037  39.895  12.617  1.00 86.84           C  
ATOM   3427  CD  LYS A 473      48.909  41.133  12.502  1.00 90.39           C  
ATOM   3428  CE  LYS A 473      48.369  42.107  11.466  1.00 96.22           C  
ATOM   3429  NZ  LYS A 473      47.184  42.854  11.956  1.00108.45           N  
ATOM   3430  N   ARG A 474      45.822  38.842  14.446  1.00 93.64           N  
ATOM   3431  CA  ARG A 474      44.983  39.560  15.394  1.00 83.86           C  
ATOM   3432  C   ARG A 474      44.149  38.626  16.262  1.00 89.00           C  
ATOM   3433  O   ARG A 474      43.720  39.026  17.349  1.00 88.83           O  
ATOM   3434  CB  ARG A 474      44.093  40.542  14.627  1.00 80.78           C  
ATOM   3435  CG  ARG A 474      43.197  41.412  15.483  1.00 88.76           C  
ATOM   3436  CD  ARG A 474      43.974  42.099  16.598  1.00 98.75           C  
ATOM   3437  NE  ARG A 474      43.070  42.784  17.516  1.00106.75           N  
ATOM   3438  CZ  ARG A 474      43.405  43.179  18.740  1.00 98.72           C  
ATOM   3439  NH1 ARG A 474      44.626  42.948  19.206  1.00 85.54           N  
ATOM   3440  NH2 ARG A 474      42.517  43.797  19.506  1.00103.11           N  
ATOM   3441  N   ILE A 475      43.930  37.391  15.826  1.00 93.89           N  
ATOM   3442  CA  ILE A 475      43.159  36.430  16.609  1.00 89.29           C  
ATOM   3443  C   ILE A 475      43.858  35.075  16.663  1.00 82.71           C  
ATOM   3444  O   ILE A 475      43.555  34.243  17.520  1.00 74.22           O  
ATOM   3445  CB  ILE A 475      41.734  36.287  16.049  1.00 84.69           C  
ATOM   3446  CG1 ILE A 475      41.766  35.833  14.588  1.00 95.11           C  
ATOM   3447  CG2 ILE A 475      41.012  37.598  16.150  1.00 87.76           C  
ATOM   3448  CD1 ILE A 475      40.388  35.619  13.983  1.00 83.67           C  
TER    3449      ILE A 475                                                      
HETATM 3450  O21 78M A 501      13.999  39.749 -15.068  0.99 81.94           O  
HETATM 3451  C20 78M A 501      15.087  39.940 -14.206  0.99 70.36           C  
HETATM 3452  C18 78M A 501      14.576  40.225 -12.795  0.99 60.49           C  
HETATM 3453  O19 78M A 501      13.667  41.289 -12.817  0.99 62.03           O  
HETATM 3454  C17 78M A 501      15.744  40.589 -11.884  0.99 61.72           C  
HETATM 3455  O2  78M A 501      15.402  40.226 -10.578  0.99 66.73           O  
HETATM 3456  C1  78M A 501      15.365  41.296  -9.681  0.99 62.19           C  
HETATM 3457  O1  78M A 501      15.933  42.301  -9.950  0.99 70.35           O  
HETATM 3458  C2  78M A 501      14.593  41.171  -8.366  0.99 55.98           C  
HETATM 3459  C3  78M A 501      15.578  41.159  -7.198  0.99 53.10           C  
HETATM 3460  C4  78M A 501      14.831  40.935  -5.885  0.99 50.68           C  
HETATM 3461  C5  78M A 501      14.279  42.264  -5.375  0.99 63.70           C  
HETATM 3462  C6  78M A 501      14.190  42.236  -3.851  0.99 49.52           C  
HETATM 3463  C7  78M A 501      15.097  43.327  -3.294  0.99 63.65           C  
HETATM 3464  C8  78M A 501      15.093  43.615  -2.008  0.99 81.28           C  
HETATM 3465  C9  78M A 501      14.182  42.868  -1.036  0.99 61.32           C  
HETATM 3466  C10 78M A 501      14.125  43.634   0.284  0.99 63.57           C  
HETATM 3467  O21 78M A 502      46.122  31.599 -26.719  0.98 72.05           O  
HETATM 3468  C20 78M A 502      47.441  31.267 -26.382  0.98 74.98           C  
HETATM 3469  C18 78M A 502      47.501  29.808 -25.932  0.98 69.61           C  
HETATM 3470  O19 78M A 502      46.233  29.399 -25.502  0.98 60.03           O  
HETATM 3471  C17 78M A 502      48.495  29.673 -24.780  0.98 66.41           C  
HETATM 3472  O2  78M A 502      47.809  29.692 -23.560  0.98 64.79           O  
HETATM 3473  C1  78M A 502      48.502  29.062 -22.524  0.98 67.41           C  
HETATM 3474  O1  78M A 502      49.678  29.045 -22.540  0.98 78.36           O  
HETATM 3475  C2  78M A 502      47.781  28.379 -21.370  0.98 51.19           C  
HETATM 3476  C3  78M A 502      48.671  27.238 -20.893  0.98 45.23           C  
HETATM 3477  C4  78M A 502      48.028  26.598 -19.672  0.98 49.68           C  
HETATM 3478  C5  78M A 502      48.888  25.443 -19.177  0.98 49.48           C  
HETATM 3479  C6  78M A 502      48.737  25.340 -17.661  0.98 49.28           C  
HETATM 3480  C7  78M A 502      49.106  26.679 -17.028  0.98 51.16           C  
HETATM 3481  C8  78M A 502      49.473  26.746 -15.764  0.98 53.80           C  
HETATM 3482  C9  78M A 502      49.545  25.490 -14.899  0.98 52.23           C  
HETATM 3483  C10 78M A 502      50.043  25.868 -13.506  0.98 62.91           C  
HETATM 3484  C11 78M A 502      51.197  24.956 -13.095  0.98 65.31           C  
HETATM 3485  C12 78M A 502      50.747  24.022 -11.974  0.98 54.52           C  
HETATM 3486  C13 78M A 502      51.922  23.137 -11.566  0.98 50.07           C  
HETATM 3487  C15 78M A 502      51.452  23.611  -9.179  0.98 71.11           C  
HETATM 3488  C14 78M A 502      51.626  22.502 -10.212  0.98 52.56           C  
HETATM 3489  O21 78M A 503      44.144  29.173 -23.473  1.00 61.08           O  
HETATM 3490  C20 78M A 503      44.885  29.943 -22.572  1.00 63.36           C  
HETATM 3491  C18 78M A 503      44.065  30.165 -21.312  1.00 54.53           C  
HETATM 3492  O19 78M A 503      42.785  30.596 -21.670  1.00 73.03           O  
HETATM 3493  C17 78M A 503      44.751  31.233 -20.471  1.00 59.80           C  
HETATM 3494  O2  78M A 503      44.242  31.164 -19.174  1.00 61.69           O  
HETATM 3495  C1  78M A 503      45.039  30.416 -18.303  1.00 61.31           C  
HETATM 3496  O1  78M A 503      46.217  30.550 -18.310  1.00 74.67           O  
HETATM 3497  C2  78M A 503      44.391  29.423 -17.344  1.00 47.69           C  
HETATM 3498  C3  78M A 503      44.993  29.603 -15.955  1.00 42.85           C  
HETATM 3499  C4  78M A 503      45.380  28.247 -15.371  1.00 37.03           C  
HETATM 3500  C5  78M A 503      45.658  28.448 -13.885  1.00 45.96           C  
HETATM 3501  C6  78M A 503      46.332  27.221 -13.277  1.00 47.19           C  
HETATM 3502  C7  78M A 503      47.280  27.708 -12.183  1.00 56.31           C  
HETATM 3503  C8  78M A 503      47.548  26.989 -11.111  1.00 52.91           C  
HETATM 3504  C9  78M A 503      46.928  25.613 -10.887  1.00 51.61           C  
HETATM 3505  C10 78M A 503      47.477  25.072  -9.568  1.00 57.27           C  
HETATM 3506  C11 78M A 503      46.822  23.741  -9.205  1.00 51.05           C  
HETATM 3507  C12 78M A 503      47.889  22.827  -8.606  1.00 62.17           C  
HETATM 3508  C13 78M A 503      47.416  22.285  -7.260  1.00 52.82           C  
HETATM 3509  C15 78M A 503      48.832  21.698  -5.295  1.00 65.85           C  
HETATM 3510  C14 78M A 503      48.459  21.308  -6.722  1.00 65.46           C  
HETATM 3511  O21 78M A 504       3.778  24.735  25.075  1.00 66.01           O  
HETATM 3512  C20 78M A 504       2.777  24.883  26.043  1.00 64.63           C  
HETATM 3513  C18 78M A 504       2.154  26.263  25.870  1.00 69.03           C  
HETATM 3514  O19 78M A 504       1.320  26.562  26.957  1.00 68.43           O  
HETATM 3515  C17 78M A 504       1.343  26.242  24.579  1.00 64.58           C  
HETATM 3516  O2  78M A 504       2.120  26.686  23.501  1.00 84.22           O  
HETATM 3517  C1  78M A 504       1.983  25.931  22.327  1.00 72.76           C  
HETATM 3518  O1  78M A 504       2.040  24.748  22.373  1.00 64.59           O  
HETATM 3519  C2  78M A 504       1.744  26.642  20.994  1.00 55.85           C  
HETATM 3520  C3  78M A 504       2.711  26.125  19.933  1.00 44.84           C  
HETATM 3521  C4  78M A 504       2.507  26.918  18.644  1.00 53.25           C  
HETATM 3522  C5  78M A 504       3.223  28.265  18.724  1.00 53.85           C  
HETATM 3523  C6  78M A 504       2.631  29.181  17.651  1.00 59.67           C  
HETATM 3524  C7  78M A 504       3.698  30.039  16.966  1.00 54.68           C  
HETATM 3525  C8  78M A 504       4.405  29.595  15.941  1.00 53.50           C  
HETATM 3526  C9  78M A 504       4.199  28.184  15.392  1.00 68.43           C  
HETATM 3527  C10 78M A 504       4.094  28.201  13.868  1.00 79.98           C  
HETATM 3528  C11 78M A 504       3.022  27.199  13.438  1.00 85.64           C  
HETATM 3529  C12 78M A 504       3.085  26.979  11.927  1.00 87.77           C  
HETATM 3530  C13 78M A 504       1.675  27.051  11.341  1.00 71.42           C  
HETATM 3531  C15 78M A 504       1.653  24.590  11.000  1.00 63.26           C  
HETATM 3532  C14 78M A 504       0.925  25.759  11.656  1.00 67.41           C  
HETATM 3533  O21 78M A 505      10.145   3.484 -18.009  1.00 75.46           O  
HETATM 3534  C20 78M A 505       9.630   4.624 -17.373  1.00 73.37           C  
HETATM 3535  C18 78M A 505       8.499   4.237 -16.418  1.00 58.73           C  
HETATM 3536  O19 78M A 505       7.321   3.967 -17.127  1.00 71.68           O  
HETATM 3537  C17 78M A 505       8.244   5.387 -15.449  1.00 53.76           C  
HETATM 3538  O2  78M A 505       8.589   4.956 -14.165  1.00 57.70           O  
HETATM 3539  C1  78M A 505       7.571   5.093 -13.214  1.00 60.03           C  
HETATM 3540  O1  78M A 505       6.812   6.003 -13.280  1.00 68.08           O  
HETATM 3541  C2  78M A 505       7.434   4.068 -12.089  1.00 41.12           C  
HETATM 3542  C3  78M A 505       8.561   4.245 -11.075  1.00 65.45           C  
HETATM 3543  C4  78M A 505       7.993   4.818  -9.779  1.00 54.80           C  
HETATM 3544  C5  78M A 505       7.018   3.814  -9.167  1.00 64.77           C  
HETATM 3545  C6  78M A 505       6.912   4.032  -7.657  1.00 58.27           C  
HETATM 3546  C7  78M A 505       7.546   2.845  -6.930  1.00 53.57           C  
HETATM 3547  C8  78M A 505       7.835   2.907  -5.644  1.00 58.62           C  
HETATM 3548  C9  78M A 505       7.555   4.166  -4.825  1.00 51.54           C  
HETATM 3549  C10 78M A 505       7.296   3.760  -3.376  1.00 49.83           C  
HETATM 3550  C11 78M A 505       8.065   4.670  -2.421  1.00 49.73           C  
HETATM 3551  C12 78M A 505       8.270   3.920  -1.107  1.00 46.78           C  
HETATM 3552  C13 78M A 505       7.936   4.833   0.069  1.00 42.17           C  
HETATM 3553  O21 78M A 506      43.318  14.459 -26.347  1.00 75.76           O  
HETATM 3554  C20 78M A 506      43.226  15.097 -25.102  1.00 69.28           C  
HETATM 3555  C18 78M A 506      43.122  14.040 -24.003  1.00 70.73           C  
HETATM 3556  O19 78M A 506      41.901  13.367 -24.136  1.00 65.18           O  
HETATM 3557  C17 78M A 506      43.200  14.698 -22.624  1.00 63.75           C  
HETATM 3558  O2  78M A 506      43.260  13.712 -21.629  1.00 74.90           O  
HETATM 3559  C1  78M A 506      43.654  14.187 -20.373  1.00 55.16           C  
HETATM 3560  O1  78M A 506      42.912  14.859 -19.741  1.00 66.15           O  
HETATM 3561  C2  78M A 506      45.037  13.845 -19.818  1.00 63.50           C  
HETATM 3562  C3  78M A 506      44.991  12.493 -19.106  1.00 75.82           C  
HETATM 3563  C4  78M A 506      46.196  12.371 -18.172  1.00 71.37           C  
HETATM 3564  C5  78M A 506      45.775  11.693 -16.869  1.00 55.79           C  
HETATM 3565  C6  78M A 506      46.064  12.626 -15.695  1.00 56.16           C  
HETATM 3566  C7  78M A 506      45.365  13.963 -15.935  1.00 56.05           C  
HETATM 3567  C8  78M A 506      45.172  14.822 -14.953  1.00 47.19           C  
HETATM 3568  C9  78M A 506      45.634  14.520 -13.528  1.00 46.20           C  
HETATM 3569  C10 78M A 506      45.808  15.830 -12.761  1.00 52.21           C  
HETATM 3570  C11 78M A 506      45.142  15.720 -11.391  1.00 47.88           C  
HETATM 3571  C12 78M A 506      46.198  15.543 -10.302  1.00 60.86           C  
HETATM 3572  C13 78M A 506      45.904  16.516  -9.163  1.00 64.28           C  
HETATM 3573  C15 78M A 506      45.850  16.824  -6.688  1.00 44.35           C  
HETATM 3574  C14 78M A 506      46.281  15.894  -7.820  1.00 62.20           C  
HETATM 3575  O21 78M A 507      21.979  35.933 -11.985  1.00 67.05           O  
HETATM 3576  C20 78M A 507      22.579  36.990 -11.285  1.00 62.66           C  
HETATM 3577  C18 78M A 507      23.917  37.361 -11.927  1.00 62.61           C  
HETATM 3578  O19 78M A 507      24.153  36.537 -13.034  1.00 65.97           O  
HETATM 3579  C17 78M A 507      25.061  37.192 -10.926  1.00 62.24           C  
HETATM 3580  O2  78M A 507      26.285  37.258 -11.606  1.00 68.95           O  
HETATM 3581  C1  78M A 507      27.339  37.822 -10.873  1.00 78.95           C  
HETATM 3582  O1  78M A 507      27.321  37.789  -9.688  1.00 78.42           O  
HETATM 3583  C2  78M A 507      28.508  38.486 -11.603  1.00 71.85           C  
HETATM 3584  C3  78M A 507      29.443  39.162 -10.599  1.00 70.80           C  
HETATM 3585  C4  78M A 507      30.669  38.282 -10.364  1.00 62.21           C  
HETATM 3586  C5  78M A 507      31.712  39.069  -9.574  1.00 53.92           C  
HETATM 3587  C6  78M A 507      32.187  38.243  -8.380  1.00 63.23           C  
HETATM 3588  C7  78M A 507      31.326  38.573  -7.163  1.00 59.94           C  
HETATM 3589  C8  78M A 507      31.640  38.151  -5.954  1.00 54.44           C  
HETATM 3590  C9  78M A 507      32.882  37.302  -5.681  1.00 61.02           C  
HETATM 3591  C10 78M A 507      33.176  37.320  -4.180  1.00 66.04           C  
HETATM 3592  C11 78M A 507      31.866  37.217  -3.397  1.00 64.17           C  
HETATM 3593  C12 78M A 507      31.985  37.760  -1.970  1.00 66.98           C  
HETATM 3594  C13 78M A 507      33.440  37.924  -1.532  1.00 68.68           C  
HETATM 3595  C15 78M A 507      34.621  39.507  -0.008  1.00 70.15           C  
HETATM 3596  C14 78M A 507      33.473  38.506  -0.120  1.00 69.60           C  
HETATM 3597  O21 78M A 508      50.544  36.517  12.056  0.98 88.27           O  
HETATM 3598  C20 78M A 508      51.531  37.014  11.198  0.98 78.45           C  
HETATM 3599  C18 78M A 508      51.399  36.326   9.844  0.98 77.98           C  
HETATM 3600  O19 78M A 508      51.330  34.939  10.024  0.98 77.00           O  
HETATM 3601  C17 78M A 508      52.618  36.659   8.992  0.98 68.91           C  
HETATM 3602  O2  78M A 508      52.472  36.042   7.746  0.98 78.87           O  
HETATM 3603  C1  78M A 508      53.117  36.727   6.715  0.98 68.62           C  
HETATM 3604  O1  78M A 508      53.807  37.657   6.961  0.98 74.62           O  
HETATM 3605  C2  78M A 508      52.932  36.286   5.270  0.98 64.99           C  
HETATM 3606  C3  78M A 508      53.795  37.177   4.382  0.98 62.55           C  
HETATM 3607  C4  78M A 508      53.690  36.686   2.945  0.98 66.98           C  
HETATM 3608  C5  78M A 508      53.885  35.174   2.956  0.98 61.84           C  
HETATM 3609  C6  78M A 508      54.516  34.756   1.638  0.98 64.83           C  
HETATM 3610  C7  78M A 508      53.494  35.021   0.542  0.98 67.01           C  
HETATM 3611  C8  78M A 508      53.471  34.230  -0.504  0.98 70.52           C  
HETATM 3612  C9  78M A 508      54.472  33.082  -0.589  0.98 70.32           C  
HETATM 3613  C10 78M A 508      55.300  33.271  -1.853  0.98 63.38           C  
HETATM 3614  C11 78M A 508      54.331  33.365  -3.026  0.98 56.60           C  
HETATM 3615  C12 78M A 508      54.864  34.360  -4.050  0.98 55.55           C  
HETATM 3616  C13 78M A 508      54.817  33.699  -5.424  0.98 52.12           C  
HETATM 3617  C15 78M A 508      53.433  35.650  -6.134  0.98 66.41           C  
HETATM 3618  C14 78M A 508      54.613  34.755  -6.506  0.98 50.65           C  
HETATM 3619  O21 78M A 509      42.053  10.813 -20.723  1.00 79.16           O  
HETATM 3620  C20 78M A 509      41.707   9.629 -20.055  1.00 75.79           C  
HETATM 3621  C18 78M A 509      40.520   8.996 -20.774  1.00 77.00           C  
HETATM 3622  O19 78M A 509      39.819  10.014 -21.425  1.00 74.58           O  
HETATM 3623  C17 78M A 509      39.604   8.296 -19.772  1.00 80.28           C  
HETATM 3624  O2  78M A 509      40.395   7.656 -18.813  1.00 93.94           O  
HETATM 3625  C1  78M A 509      39.845   6.482 -18.286  1.00 91.93           C  
HETATM 3626  O1  78M A 509      39.699   5.531 -18.980  1.00 95.26           O  
HETATM 3627  C2  78M A 509      39.429   6.424 -16.817  1.00 76.09           C  
HETATM 3628  C3  78M A 509      40.646   6.504 -15.894  1.00 69.70           C  
HETATM 3629  C4  78M A 509      40.196   6.236 -14.456  1.00 66.92           C  
HETATM 3630  C5  78M A 509      38.917   7.026 -14.185  1.00 71.17           C  
HETATM 3631  C6  78M A 509      38.267   6.672 -12.849  1.00 62.76           C  
HETATM 3632  C7  78M A 509      37.841   7.977 -12.178  1.00 60.12           C  
HETATM 3633  C8  78M A 509      36.644   8.166 -11.653  1.00 56.95           C  
HETATM 3634  C9  78M A 509      35.556   7.093 -11.658  1.00 64.20           C  
HETATM 3635  C10 78M A 509      34.256   7.692 -11.114  1.00 61.80           C  
HETATM 3636  C11 78M A 509      34.386   8.023  -9.627  1.00 50.93           C  
HETATM 3637  C12 78M A 509      33.631   6.980  -8.800  1.00 55.99           C  
HETATM 3638  C13 78M A 509      33.849   7.229  -7.307  1.00 43.94           C  
HETATM 3639  C15 78M A 509      34.509   5.191  -6.014  1.00 43.21           C  
HETATM 3640  C14 78M A 509      33.334   6.033  -6.510  1.00 38.75           C  
HETATM 3641  O21 78M A 510      49.087  14.718 -19.158  0.96 67.17           O  
HETATM 3642  C20 78M A 510      49.021  15.168 -17.832  0.96 58.24           C  
HETATM 3643  C18 78M A 510      48.246  16.478 -17.801  0.96 50.91           C  
HETATM 3644  O19 78M A 510      47.618  16.641 -19.040  0.96 57.79           O  
HETATM 3645  C17 78M A 510      49.223  17.625 -17.543  0.96 52.76           C  
HETATM 3646  O2  78M A 510      48.733  18.460 -16.531  0.96 58.23           O  
HETATM 3647  C1  78M A 510      49.104  18.108 -15.226  0.96 52.63           C  
HETATM 3648  O1  78M A 510      49.536  17.032 -14.983  0.96 58.30           O  
HETATM 3649  C2  78M A 510      48.952  19.118 -14.096  0.96 51.33           C  
HETATM 3650  C3  78M A 510      48.541  18.381 -12.825  0.96 47.20           C  
HETATM 3651  C4  78M A 510      47.954  19.389 -11.842  0.96 55.78           C  
HETATM 3652  C5  78M A 510      49.056  19.902 -10.918  0.96 59.00           C  
HETATM 3653  C6  78M A 510      49.353  18.844  -9.855  0.96 67.44           C  
HETATM 3654  C7  78M A 510      50.608  19.229  -9.074  0.96 60.24           C  
HETATM 3655  C8  78M A 510      50.852  18.696  -7.893  0.96 56.08           C  
HETATM 3656  C9  78M A 510      49.887  17.685  -7.277  0.96 57.50           C  
HETATM 3657  O21 78M A 511       9.729   6.245  19.401  0.93 60.38           O  
HETATM 3658  C20 78M A 511       9.192   6.607  18.161  0.93 47.57           C  
HETATM 3659  C18 78M A 511      10.172   7.500  17.400  0.93 51.93           C  
HETATM 3660  O19 78M A 511      11.406   7.565  18.063  0.93 51.69           O  
HETATM 3661  C17 78M A 511       9.561   8.894  17.283  0.93 34.08           C  
HETATM 3662  O2  78M A 511       8.328   8.799  16.624  0.93 35.46           O  
HETATM 3663  C1  78M A 511       7.506   9.909  16.832  0.93 42.44           C  
HETATM 3664  O1  78M A 511       7.837  10.735  17.609  0.93 42.33           O  
HETATM 3665  C2  78M A 511       6.194  10.075  16.070  0.93 26.03           C  
HETATM 3666  C3  78M A 511       5.696   8.717  15.588  0.93 26.11           C  
HETATM 3667  C4  78M A 511       4.274   8.865  15.054  0.93 27.95           C  
HETATM 3668  C5  78M A 511       3.869   7.580  14.335  0.93 38.03           C  
HETATM 3669  C6  78M A 511       2.557   7.816  13.589  0.93 30.71           C  
HETATM 3670  C7  78M A 511       2.116   6.528  12.897  0.93 46.55           C  
HETATM 3671  C8  78M A 511       2.069   6.449  11.582  0.93 51.92           C  
HETATM 3672  C9  78M A 511       2.453   7.643  10.709  0.93 48.91           C  
HETATM 3673  O21 78M A 512      51.141  10.062 -18.012  0.85 60.53           O  
HETATM 3674  C20 78M A 512      51.387  10.456 -16.689  0.85 65.99           C  
HETATM 3675  C18 78M A 512      50.615  11.743 -16.416  0.85 65.19           C  
HETATM 3676  O19 78M A 512      50.609  12.500 -17.593  0.85 58.59           O  
HETATM 3677  C17 78M A 512      51.280  12.530 -15.285  0.85 60.14           C  
HETATM 3678  O2  78M A 512      50.404  13.523 -14.824  0.85 56.73           O  
HETATM 3679  C1  78M A 512      50.794  14.156 -13.636  0.85 55.58           C  
HETATM 3680  O1  78M A 512      51.689  14.934 -13.647  0.85 50.05           O  
HETATM 3681  C2  78M A 512      50.065  13.849 -12.327  0.85 59.90           C  
HETATM 3682  C3  78M A 512      50.693  14.641 -11.180  0.85 47.22           C  
HETATM 3683  C4  78M A 512      50.904  13.728  -9.973  0.85 49.15           C  
HETATM 3684  C5  78M A 512      49.655  13.716  -9.095  0.85 54.88           C  
HETATM 3685  O21 78M A 513       7.391  32.345 -12.638  0.82 54.80           O  
HETATM 3686  C20 78M A 513       6.903  31.532 -11.608  0.82 56.48           C  
HETATM 3687  C18 78M A 513       8.076  30.915 -10.846  0.82 68.28           C  
HETATM 3688  O19 78M A 513       8.209  29.565 -11.189  0.82 68.26           O  
HETATM 3689  C17 78M A 513       7.815  31.011  -9.347  0.82 68.42           C  
HETATM 3690  O2  78M A 513       8.748  30.218  -8.670  0.82 63.79           O  
HETATM 3691  C1  78M A 513       8.627  30.290  -7.277  0.82 64.57           C  
HETATM 3692  O1  78M A 513       7.605  30.653  -6.798  0.82 69.20           O  
HETATM 3693  C2  78M A 513       9.801  29.901  -6.380  0.82 48.40           C  
HETATM 3694  C3  78M A 513      10.071  30.990  -5.341  0.82 51.10           C  
HETATM 3695  C4  78M A 513       9.239  30.759  -4.081  0.82 54.35           C  
HETATM 3696  C5  78M A 513       9.520  31.870  -3.070  0.82 50.42           C  
HETATM 3697  C6  78M A 513       8.352  31.966  -2.091  0.82 57.67           C  
HETATM 3698  C7  78M A 513       8.019  30.571  -1.567  0.82 59.78           C  
HETATM 3699  O21 78M A 514       3.486   1.982  14.057  0.76 67.95           O  
HETATM 3700  C20 78M A 514       4.398   1.701  13.029  0.76 59.60           C  
HETATM 3701  C18 78M A 514       5.046   2.994  12.533  0.76 50.29           C  
HETATM 3702  O19 78M A 514       4.050   3.916  12.191  0.76 50.65           O  
HETATM 3703  C17 78M A 514       5.919   2.687  11.317  0.76 49.61           C  
HETATM 3704  O2  78M A 514       6.247   3.867  10.639  0.76 53.89           O  
HETATM 3705  C1  78M A 514       7.368   3.736   9.811  0.76 51.79           C  
HETATM 3706  O1  78M A 514       8.382   3.319  10.261  0.76 52.01           O  
HETATM 3707  C2  78M A 514       7.292   4.125   8.335  0.76 38.16           C  
HETATM 3708  C3  78M A 514       6.658   5.508   8.208  0.76 42.73           C  
HETATM 3709  C4  78M A 514       5.328   5.405   7.464  0.76 49.70           C  
HETATM 3710  C5  78M A 514       5.564   5.577   5.966  0.76 46.03           C  
HETATM 3711  O21 78M A 515      17.497  30.040  17.358  1.00 76.68           O  
HETATM 3712  C20 78M A 515      16.396  30.891  17.185  1.00 80.21           C  
HETATM 3713  C18 78M A 515      15.257  30.113  16.529  1.00 66.66           C  
HETATM 3714  O19 78M A 515      15.786  29.265  15.549  1.00 77.48           O  
HETATM 3715  C17 78M A 515      14.257  31.078  15.892  1.00 71.57           C  
HETATM 3716  O2  78M A 515      13.437  30.390  14.986  1.00 70.30           O  
HETATM 3717  C1  78M A 515      12.094  30.793  14.995  1.00 67.18           C  
HETATM 3718  O1  78M A 515      11.701  31.526  15.839  1.00 73.34           O  
HETATM 3719  C2  78M A 515      11.135  30.295  13.911  1.00 66.52           C  
HETATM 3720  C3  78M A 515       9.798  29.878  14.524  1.00 61.80           C  
HETATM 3721  C4  78M A 515       9.320  28.558  13.909  1.00 60.83           C  
HETATM 3722  C5  78M A 515       8.631  28.790  12.561  1.00 70.95           C  
HETATM 3723  C6  78M A 515       9.393  28.087  11.435  1.00 66.84           C  
HETATM 3724  C7  78M A 515       8.528  27.004  10.787  1.00 70.14           C  
HETATM 3725  C8  78M A 515       9.081  25.922  10.268  1.00 76.19           C  
HETATM 3726  C9  78M A 515      10.597  25.727  10.310  1.00 71.13           C  
HETATM 3727  C10 78M A 515      11.054  24.666   9.308  1.00 64.45           C  
HETATM 3728  C11 78M A 515      10.865  25.170   7.874  1.00 66.46           C  
HETATM 3729  C12 78M A 515      11.357  26.614   7.751  1.00 74.83           C  
HETATM 3730  C13 78M A 515      11.877  26.896   6.341  1.00 82.51           C  
HETATM 3731  C15 78M A 515      13.581  28.302   5.170  1.00 62.08           C  
HETATM 3732  C14 78M A 515      12.576  28.257   6.320  1.00 62.53           C  
HETATM 3733  O21 78M A 516       9.291  25.660 -12.366  0.84 62.83           O  
HETATM 3734  C20 78M A 516       9.339  25.447 -10.982  0.84 64.06           C  
HETATM 3735  C18 78M A 516      10.733  25.808 -10.478  0.84 60.33           C  
HETATM 3736  O19 78M A 516      11.677  25.136 -11.259  0.84 65.41           O  
HETATM 3737  C17 78M A 516      10.885  25.396  -9.016  0.84 59.97           C  
HETATM 3738  O2  78M A 516      12.216  25.568  -8.617  0.84 61.76           O  
HETATM 3739  C1  78M A 516      12.422  26.676  -7.786  0.84 56.17           C  
HETATM 3740  O1  78M A 516      11.694  27.605  -7.848  0.84 61.81           O  
HETATM 3741  C2  78M A 516      13.575  26.696  -6.787  0.84 52.41           C  
HETATM 3742  C3  78M A 516      13.125  27.435  -5.530  0.84 43.40           C  
HETATM 3743  C4  78M A 516      14.164  27.222  -4.432  0.84 49.80           C  
HETATM 3744  C5  78M A 516      13.472  26.910  -3.109  0.84 46.17           C  
HETATM 3745  C6  78M A 516      12.479  28.021  -2.786  0.84 52.75           C  
HETATM 3746  C7  78M A 516      11.214  27.433  -2.173  0.84 59.08           C  
HETATM 3747  C8  78M A 516      10.806  27.814  -0.980  0.84 66.56           C  
HETATM 3748  C9  78M A 516      11.576  28.847  -0.161  0.84 63.39           C  
HETATM 3749  C10 78M A 516      11.090  28.764   1.284  0.84 76.27           C  
HETATM 3750  C11 78M A 516      12.016  29.560   2.199  0.84 77.57           C  
HETATM 3751  C12 78M A 516      11.850  31.050   1.915  0.84 74.43           C  
HETATM 3752  C13 78M A 516      12.364  31.873   3.095  0.84 52.92           C  
HETATM 3753  C15 78M A 516      11.166  33.669   4.349  0.84 63.59           C  
HETATM 3754  C14 78M A 516      11.198  32.175   4.031  0.84 61.81           C  
HETATM 3755  O1  PE5 A 517      17.864   8.699 -18.794  1.00 70.32           O  
HETATM 3756  C1  PE5 A 517      17.679   9.560 -19.884  1.00 68.38           C  
HETATM 3757  C2  PE5 A 517      18.832  10.562 -19.954  1.00 64.13           C  
HETATM 3758  O2  PE5 A 517      20.037   9.907 -19.678  1.00 67.97           O  
HETATM 3759  C3  PE5 A 517      21.132  10.761 -19.495  1.00 75.19           C  
HETATM 3760  C4  PE5 A 517      21.957  10.258 -18.310  1.00 67.65           C  
HETATM 3761  O3  PE5 A 517      22.550  11.337 -17.644  1.00 53.19           O  
HETATM 3762  C5  PE5 A 517      23.796  11.704 -18.171  1.00 73.10           C  
HETATM 3763  C6  PE5 A 517      24.061  13.188 -17.912  1.00 52.06           C  
HETATM 3764  O4  PE5 A 517      23.641  13.946 -19.011  1.00 58.55           O  
HETATM 3765  P   PO4 A 518       4.409  18.530 -16.274  1.00 56.43           P  
HETATM 3766  O1  PO4 A 518       4.493  18.950 -17.719  1.00 78.10           O  
HETATM 3767  O2  PO4 A 518       5.556  19.143 -15.512  1.00 69.87           O  
HETATM 3768  O3  PO4 A 518       4.476  17.024 -16.194  1.00 74.09           O  
HETATM 3769  O4  PO4 A 518       3.106  19.008 -15.683  1.00 91.76           O  
HETATM 3770  O   HOH A 601      43.795  28.427 -25.459  0.90 60.16           O  
HETATM 3771  O   HOH A 602      39.368  24.101 -17.786  1.00 36.40           O  
HETATM 3772  O   HOH A 603      31.422  22.805 -19.056  1.00 40.12           O  
HETATM 3773  O   HOH A 604      33.285   9.472 -23.679  1.00 54.72           O  
HETATM 3774  O   HOH A 605      13.404   8.559 -17.601  1.00 41.50           O  
HETATM 3775  O   HOH A 606       7.763  14.206 -10.975  1.00 45.57           O  
HETATM 3776  O   HOH A 607       5.565  12.880 -17.118  1.00 51.96           O  
HETATM 3777  O   HOH A 608      14.622  31.403 -16.737  1.00 29.74           O  
HETATM 3778  O   HOH A 609      50.516  29.572   8.344  1.00 44.79           O  
HETATM 3779  O   HOH A 610       4.886  34.744 -11.010  1.00 55.77           O  
CONECT 3450 3451                                                                
CONECT 3451 3450 3452                                                           
CONECT 3452 3451 3453 3454                                                      
CONECT 3453 3452                                                                
CONECT 3454 3452 3455                                                           
CONECT 3455 3454 3456                                                           
CONECT 3456 3455 3457 3458                                                      
CONECT 3457 3456                                                                
CONECT 3458 3456 3459                                                           
CONECT 3459 3458 3460                                                           
CONECT 3460 3459 3461                                                           
CONECT 3461 3460 3462                                                           
CONECT 3462 3461 3463                                                           
CONECT 3463 3462 3464                                                           
CONECT 3464 3463 3465                                                           
CONECT 3465 3464 3466                                                           
CONECT 3466 3465                                                                
CONECT 3467 3468                                                                
CONECT 3468 3467 3469                                                           
CONECT 3469 3468 3470 3471                                                      
CONECT 3470 3469                                                                
CONECT 3471 3469 3472                                                           
CONECT 3472 3471 3473                                                           
CONECT 3473 3472 3474 3475                                                      
CONECT 3474 3473                                                                
CONECT 3475 3473 3476                                                           
CONECT 3476 3475 3477                                                           
CONECT 3477 3476 3478                                                           
CONECT 3478 3477 3479                                                           
CONECT 3479 3478 3480                                                           
CONECT 3480 3479 3481                                                           
CONECT 3481 3480 3482                                                           
CONECT 3482 3481 3483                                                           
CONECT 3483 3482 3484                                                           
CONECT 3484 3483 3485                                                           
CONECT 3485 3484 3486                                                           
CONECT 3486 3485 3488                                                           
CONECT 3487 3488                                                                
CONECT 3488 3486 3487                                                           
CONECT 3489 3490                                                                
CONECT 3490 3489 3491                                                           
CONECT 3491 3490 3492 3493                                                      
CONECT 3492 3491                                                                
CONECT 3493 3491 3494                                                           
CONECT 3494 3493 3495                                                           
CONECT 3495 3494 3496 3497                                                      
CONECT 3496 3495                                                                
CONECT 3497 3495 3498                                                           
CONECT 3498 3497 3499                                                           
CONECT 3499 3498 3500                                                           
CONECT 3500 3499 3501                                                           
CONECT 3501 3500 3502                                                           
CONECT 3502 3501 3503                                                           
CONECT 3503 3502 3504                                                           
CONECT 3504 3503 3505                                                           
CONECT 3505 3504 3506                                                           
CONECT 3506 3505 3507                                                           
CONECT 3507 3506 3508                                                           
CONECT 3508 3507 3510                                                           
CONECT 3509 3510                                                                
CONECT 3510 3508 3509                                                           
CONECT 3511 3512                                                                
CONECT 3512 3511 3513                                                           
CONECT 3513 3512 3514 3515                                                      
CONECT 3514 3513                                                                
CONECT 3515 3513 3516                                                           
CONECT 3516 3515 3517                                                           
CONECT 3517 3516 3518 3519                                                      
CONECT 3518 3517                                                                
CONECT 3519 3517 3520                                                           
CONECT 3520 3519 3521                                                           
CONECT 3521 3520 3522                                                           
CONECT 3522 3521 3523                                                           
CONECT 3523 3522 3524                                                           
CONECT 3524 3523 3525                                                           
CONECT 3525 3524 3526                                                           
CONECT 3526 3525 3527                                                           
CONECT 3527 3526 3528                                                           
CONECT 3528 3527 3529                                                           
CONECT 3529 3528 3530                                                           
CONECT 3530 3529 3532                                                           
CONECT 3531 3532                                                                
CONECT 3532 3530 3531                                                           
CONECT 3533 3534                                                                
CONECT 3534 3533 3535                                                           
CONECT 3535 3534 3536 3537                                                      
CONECT 3536 3535                                                                
CONECT 3537 3535 3538                                                           
CONECT 3538 3537 3539                                                           
CONECT 3539 3538 3540 3541                                                      
CONECT 3540 3539                                                                
CONECT 3541 3539 3542                                                           
CONECT 3542 3541 3543                                                           
CONECT 3543 3542 3544                                                           
CONECT 3544 3543 3545                                                           
CONECT 3545 3544 3546                                                           
CONECT 3546 3545 3547                                                           
CONECT 3547 3546 3548                                                           
CONECT 3548 3547 3549                                                           
CONECT 3549 3548 3550                                                           
CONECT 3550 3549 3551                                                           
CONECT 3551 3550 3552                                                           
CONECT 3552 3551                                                                
CONECT 3553 3554                                                                
CONECT 3554 3553 3555                                                           
CONECT 3555 3554 3556 3557                                                      
CONECT 3556 3555                                                                
CONECT 3557 3555 3558                                                           
CONECT 3558 3557 3559                                                           
CONECT 3559 3558 3560 3561                                                      
CONECT 3560 3559                                                                
CONECT 3561 3559 3562                                                           
CONECT 3562 3561 3563                                                           
CONECT 3563 3562 3564                                                           
CONECT 3564 3563 3565                                                           
CONECT 3565 3564 3566                                                           
CONECT 3566 3565 3567                                                           
CONECT 3567 3566 3568                                                           
CONECT 3568 3567 3569                                                           
CONECT 3569 3568 3570                                                           
CONECT 3570 3569 3571                                                           
CONECT 3571 3570 3572                                                           
CONECT 3572 3571 3574                                                           
CONECT 3573 3574                                                                
CONECT 3574 3572 3573                                                           
CONECT 3575 3576                                                                
CONECT 3576 3575 3577                                                           
CONECT 3577 3576 3578 3579                                                      
CONECT 3578 3577                                                                
CONECT 3579 3577 3580                                                           
CONECT 3580 3579 3581                                                           
CONECT 3581 3580 3582 3583                                                      
CONECT 3582 3581                                                                
CONECT 3583 3581 3584                                                           
CONECT 3584 3583 3585                                                           
CONECT 3585 3584 3586                                                           
CONECT 3586 3585 3587                                                           
CONECT 3587 3586 3588                                                           
CONECT 3588 3587 3589                                                           
CONECT 3589 3588 3590                                                           
CONECT 3590 3589 3591                                                           
CONECT 3591 3590 3592                                                           
CONECT 3592 3591 3593                                                           
CONECT 3593 3592 3594                                                           
CONECT 3594 3593 3596                                                           
CONECT 3595 3596                                                                
CONECT 3596 3594 3595                                                           
CONECT 3597 3598                                                                
CONECT 3598 3597 3599                                                           
CONECT 3599 3598 3600 3601                                                      
CONECT 3600 3599                                                                
CONECT 3601 3599 3602                                                           
CONECT 3602 3601 3603                                                           
CONECT 3603 3602 3604 3605                                                      
CONECT 3604 3603                                                                
CONECT 3605 3603 3606                                                           
CONECT 3606 3605 3607                                                           
CONECT 3607 3606 3608                                                           
CONECT 3608 3607 3609                                                           
CONECT 3609 3608 3610                                                           
CONECT 3610 3609 3611                                                           
CONECT 3611 3610 3612                                                           
CONECT 3612 3611 3613                                                           
CONECT 3613 3612 3614                                                           
CONECT 3614 3613 3615                                                           
CONECT 3615 3614 3616                                                           
CONECT 3616 3615 3618                                                           
CONECT 3617 3618                                                                
CONECT 3618 3616 3617                                                           
CONECT 3619 3620                                                                
CONECT 3620 3619 3621                                                           
CONECT 3621 3620 3622 3623                                                      
CONECT 3622 3621                                                                
CONECT 3623 3621 3624                                                           
CONECT 3624 3623 3625                                                           
CONECT 3625 3624 3626 3627                                                      
CONECT 3626 3625                                                                
CONECT 3627 3625 3628                                                           
CONECT 3628 3627 3629                                                           
CONECT 3629 3628 3630                                                           
CONECT 3630 3629 3631                                                           
CONECT 3631 3630 3632                                                           
CONECT 3632 3631 3633                                                           
CONECT 3633 3632 3634                                                           
CONECT 3634 3633 3635                                                           
CONECT 3635 3634 3636                                                           
CONECT 3636 3635 3637                                                           
CONECT 3637 3636 3638                                                           
CONECT 3638 3637 3640                                                           
CONECT 3639 3640                                                                
CONECT 3640 3638 3639                                                           
CONECT 3641 3642                                                                
CONECT 3642 3641 3643                                                           
CONECT 3643 3642 3644 3645                                                      
CONECT 3644 3643                                                                
CONECT 3645 3643 3646                                                           
CONECT 3646 3645 3647                                                           
CONECT 3647 3646 3648 3649                                                      
CONECT 3648 3647                                                                
CONECT 3649 3647 3650                                                           
CONECT 3650 3649 3651                                                           
CONECT 3651 3650 3652                                                           
CONECT 3652 3651 3653                                                           
CONECT 3653 3652 3654                                                           
CONECT 3654 3653 3655                                                           
CONECT 3655 3654 3656                                                           
CONECT 3656 3655                                                                
CONECT 3657 3658                                                                
CONECT 3658 3657 3659                                                           
CONECT 3659 3658 3660 3661                                                      
CONECT 3660 3659                                                                
CONECT 3661 3659 3662                                                           
CONECT 3662 3661 3663                                                           
CONECT 3663 3662 3664 3665                                                      
CONECT 3664 3663                                                                
CONECT 3665 3663 3666                                                           
CONECT 3666 3665 3667                                                           
CONECT 3667 3666 3668                                                           
CONECT 3668 3667 3669                                                           
CONECT 3669 3668 3670                                                           
CONECT 3670 3669 3671                                                           
CONECT 3671 3670 3672                                                           
CONECT 3672 3671                                                                
CONECT 3673 3674                                                                
CONECT 3674 3673 3675                                                           
CONECT 3675 3674 3676 3677                                                      
CONECT 3676 3675                                                                
CONECT 3677 3675 3678                                                           
CONECT 3678 3677 3679                                                           
CONECT 3679 3678 3680 3681                                                      
CONECT 3680 3679                                                                
CONECT 3681 3679 3682                                                           
CONECT 3682 3681 3683                                                           
CONECT 3683 3682 3684                                                           
CONECT 3684 3683                                                                
CONECT 3685 3686                                                                
CONECT 3686 3685 3687                                                           
CONECT 3687 3686 3688 3689                                                      
CONECT 3688 3687                                                                
CONECT 3689 3687 3690                                                           
CONECT 3690 3689 3691                                                           
CONECT 3691 3690 3692 3693                                                      
CONECT 3692 3691                                                                
CONECT 3693 3691 3694                                                           
CONECT 3694 3693 3695                                                           
CONECT 3695 3694 3696                                                           
CONECT 3696 3695 3697                                                           
CONECT 3697 3696 3698                                                           
CONECT 3698 3697                                                                
CONECT 3699 3700                                                                
CONECT 3700 3699 3701                                                           
CONECT 3701 3700 3702 3703                                                      
CONECT 3702 3701                                                                
CONECT 3703 3701 3704                                                           
CONECT 3704 3703 3705                                                           
CONECT 3705 3704 3706 3707                                                      
CONECT 3706 3705                                                                
CONECT 3707 3705 3708                                                           
CONECT 3708 3707 3709                                                           
CONECT 3709 3708 3710                                                           
CONECT 3710 3709                                                                
CONECT 3711 3712                                                                
CONECT 3712 3711 3713                                                           
CONECT 3713 3712 3714 3715                                                      
CONECT 3714 3713                                                                
CONECT 3715 3713 3716                                                           
CONECT 3716 3715 3717                                                           
CONECT 3717 3716 3718 3719                                                      
CONECT 3718 3717                                                                
CONECT 3719 3717 3720                                                           
CONECT 3720 3719 3721                                                           
CONECT 3721 3720 3722                                                           
CONECT 3722 3721 3723                                                           
CONECT 3723 3722 3724                                                           
CONECT 3724 3723 3725                                                           
CONECT 3725 3724 3726                                                           
CONECT 3726 3725 3727                                                           
CONECT 3727 3726 3728                                                           
CONECT 3728 3727 3729                                                           
CONECT 3729 3728 3730                                                           
CONECT 3730 3729 3732                                                           
CONECT 3731 3732                                                                
CONECT 3732 3730 3731                                                           
CONECT 3733 3734                                                                
CONECT 3734 3733 3735                                                           
CONECT 3735 3734 3736 3737                                                      
CONECT 3736 3735                                                                
CONECT 3737 3735 3738                                                           
CONECT 3738 3737 3739                                                           
CONECT 3739 3738 3740 3741                                                      
CONECT 3740 3739                                                                
CONECT 3741 3739 3742                                                           
CONECT 3742 3741 3743                                                           
CONECT 3743 3742 3744                                                           
CONECT 3744 3743 3745                                                           
CONECT 3745 3744 3746                                                           
CONECT 3746 3745 3747                                                           
CONECT 3747 3746 3748                                                           
CONECT 3748 3747 3749                                                           
CONECT 3749 3748 3750                                                           
CONECT 3750 3749 3751                                                           
CONECT 3751 3750 3752                                                           
CONECT 3752 3751 3754                                                           
CONECT 3753 3754                                                                
CONECT 3754 3752 3753                                                           
CONECT 3755 3756                                                                
CONECT 3756 3755 3757                                                           
CONECT 3757 3756 3758                                                           
CONECT 3758 3757 3759                                                           
CONECT 3759 3758 3760                                                           
CONECT 3760 3759 3761                                                           
CONECT 3761 3760 3762                                                           
CONECT 3762 3761 3763                                                           
CONECT 3763 3762 3764                                                           
CONECT 3764 3763                                                                
CONECT 3765 3766 3767 3768 3769                                                 
CONECT 3766 3765                                                                
CONECT 3767 3765                                                                
CONECT 3768 3765                                                                
CONECT 3769 3765                                                                
MASTER      379    0   18   19    0    0   31    6 3778    1  320   38          
END                                                                             
