CNRS Nantes University US2B US2B
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***  TRANSPORT PROTEIN 14-DEC-17 6BWB  ***

elNémo ID: 2307251753061188334

Job options:

ID        	=	 2307251753061188334
JOBID     	=	 TRANSPORT PROTEIN 14-DEC-17 6BWB
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSPORT PROTEIN                       14-DEC-17   6BWB              
TITLE     HENDRA VIRUS W PROTEIN C-TERMINUS IN COMPLEX WITH IMPORTIN ALPHA 3    
TITLE    2 CRYSTAL FORM 3                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IMPORTIN SUBUNIT ALPHA-3;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: IMPORTIN ALPHA Q1,QIP1,KARYOPHERIN SUBUNIT ALPHA-4;         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PROTEIN W;                                                 
COMPND   8 CHAIN: B;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KPNA4, QIP1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HENDRA VIRUS;                                   
SOURCE  11 ORGANISM_COMMON: ISOLATE HORSE/AUTRALIA/HENDRA/1994;                 
SOURCE  12 ORGANISM_TAXID: 928303;                                              
SOURCE  13 GENE: P/V/C;                                                         
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    COMPLEX, HENDRA VIRUS, IMPORTIN, KARYOPHERIN, PHOSPHOPROTEIN, W,      
KEYWDS   2 TRANSPORT PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.TSIMBALYUK,K.M.SMITH,M.R.EDWARDS,D.ARAGAO,E.M.CROSS,C.F.BASLER,     
AUTHOR   2 J.K.FORWOOD                                                          
REVDAT   5   29-MAR-23 6BWB    1       AUTHOR                                   
REVDAT   4   01-JAN-20 6BWB    1       REMARK                                   
REVDAT   3   20-FEB-19 6BWB    1       REMARK                                   
REVDAT   2   16-JAN-19 6BWB    1       JRNL                                     
REVDAT   1   04-JUL-18 6BWB    0                                                
JRNL        AUTH   K.M.SMITH,S.TSIMBALYUK,M.R.EDWARDS,E.M.CROSS,J.BATRA,        
JRNL        AUTH 2 T.P.SOARES DA COSTA,D.ARAGAO,C.F.BASLER,J.K.FORWOOD          
JRNL        TITL   STRUCTURAL BASIS FOR IMPORTIN ALPHA 3 SPECIFICITY OF W       
JRNL        TITL 2 PROTEINS IN HENDRA AND NIPAH VIRUSES.                        
JRNL        REF    NAT COMMUN                    V.   9  3703 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   30209309                                                     
JRNL        DOI    10.1038/S41467-018-05928-5                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 22194                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1119                            
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 29.4974 -  4.5949    1.00     2800   155  0.1668 0.1843        
REMARK   3     2  4.5949 -  3.6493    1.00     2660   130  0.1526 0.1866        
REMARK   3     3  3.6493 -  3.1886    1.00     2664   126  0.1874 0.2121        
REMARK   3     4  3.1886 -  2.8974    1.00     2606   156  0.1894 0.2509        
REMARK   3     5  2.8974 -  2.6899    1.00     2583   135  0.1852 0.2358        
REMARK   3     6  2.6899 -  2.5314    1.00     2599   146  0.1922 0.2569        
REMARK   3     7  2.5314 -  2.4046    1.00     2597   121  0.1964 0.2344        
REMARK   3     8  2.4046 -  2.3000    1.00     2566   150  0.1914 0.2563        
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)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.110           
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      :  0.006           3483                                  
REMARK   3   ANGLE     :  0.710           4754                                  
REMARK   3   CHIRALITY :  0.043            571                                  
REMARK   3   PLANARITY :  0.006            618                                  
REMARK   3   DIHEDRAL  : 21.478           1281                                  
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 6BWB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000231666.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22252                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.495                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 12.90                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.10                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 8.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CHLORIDE, 0.1M MES PH6.5,    
REMARK 280  10% W/V PEG 4000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.08000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       84.64450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.49500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       84.64450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.08000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       29.49500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    63                                                      
REMARK 465     GLY A    64                                                      
REMARK 465     ASP A    65                                                      
REMARK 465     TYR A    66                                                      
REMARK 465     ARG A    67                                                      
REMARK 465     VAL A    68                                                      
REMARK 465     GLN A    69                                                      
REMARK 465     ASN A    70                                                      
REMARK 465     THR A    71                                                      
REMARK 465     ASP A   488                                                      
REMARK 465     ASP A   489                                                      
REMARK 465     ILE A   490                                                      
REMARK 465     ASP A   491                                                      
REMARK 465     GLU A   492                                                      
REMARK 465     ASP A   493                                                      
REMARK 465     PRO A   494                                                      
REMARK 465     SER A   495                                                      
REMARK 465     LEU A   496                                                      
REMARK 465     VAL A   497                                                      
REMARK 465     PRO A   498                                                      
REMARK 465     GLU A   499                                                      
REMARK 465     ALA A   500                                                      
REMARK 465     ILE A   501                                                      
REMARK 465     GLN A   502                                                      
REMARK 465     GLY A   503                                                      
REMARK 465     GLY A   504                                                      
REMARK 465     THR A   505                                                      
REMARK 465     PHE A   506                                                      
REMARK 465     GLY A   507                                                      
REMARK 465     PHE A   508                                                      
REMARK 465     ASN A   509                                                      
REMARK 465     SER A   510                                                      
REMARK 465     SER A   511                                                      
REMARK 465     ALA A   512                                                      
REMARK 465     ASN A   513                                                      
REMARK 465     VAL A   514                                                      
REMARK 465     PRO A   515                                                      
REMARK 465     THR A   516                                                      
REMARK 465     GLU A   517                                                      
REMARK 465     GLY A   518                                                      
REMARK 465     PHE A   519                                                      
REMARK 465     GLN A   520                                                      
REMARK 465     PHE A   521                                                      
REMARK 465     SER B   408                                                      
REMARK 465     ARG B   409                                                      
REMARK 465     SER B   410                                                      
REMARK 465     LEU B   411                                                      
REMARK 465     ASN B   412                                                      
REMARK 465     MET B   413                                                      
REMARK 465     LEU B   414                                                      
REMARK 465     GLY B   415                                                      
REMARK 465     ARG B   416                                                      
REMARK 465     LYS B   417                                                      
REMARK 465     THR B   418                                                      
REMARK 465     ARG B   445                                                      
REMARK 465     MET B   446                                                      
REMARK 465     SER B   447                                                      
REMARK 465     ASN B   448                                                      
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    GLU A 445        0.78    -68.12                                   
REMARK 500    ASP B 432       52.67    -92.78                                   
REMARK 500    LEU B 443        9.78     83.31                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6BVZ   RELATED DB: PDB                                   
REMARK 900 6BVZ CONTAINS IMPORTIN ALPHA 3 IN CARGO FREE STATE                   
REMARK 900 RELATED ID: 6BVV   RELATED DB: PDB                                   
REMARK 900 6BVV CONTAINS NIPAH VIRUS W PROTEIN C-TERMINUS IN COMPLEX WITH       
REMARK 900 IMPORTIN ALPHA 3                                                     
REMARK 900 RELATED ID: 6BVT   RELATED DB: PDB                                   
REMARK 900 6BVT CONTAINS IMPORTIN ALPHA 1 IN CARGO FREE STATE                   
REMARK 900 RELATED ID: 6BW0   RELATED DB: PDB                                   
REMARK 900 6BW0 CONTAINS NIPAH VIRUS W PROTEIN C-TERMINUS IN COMPLEX WITH       
REMARK 900 IMPORTIN ALPHA 1                                                     
REMARK 900 RELATED ID: 6BW1   RELATED DB: PDB                                   
REMARK 900 6BW1 CONTAINS HENDRA VIRUS W PROTEIN C-TERMINUS IN COMPLEX WITH      
REMARK 900 IMPORTIN ALPHA 1                                                     
REMARK 900 RELATED ID: 6BW9   RELATED DB: PDB                                   
REMARK 900 6BW9 CONTAINS HENDRA VIRUS W PROTEIN C-TERMINUS IN COMPLEX WITH      
REMARK 900 IMPORTIN ALPHA 3 CRYSTAL FORM 1                                      
REMARK 900 RELATED ID: 6BWA   RELATED DB: PDB                                   
REMARK 900 6BWA CONTAINS HENDRA VIRUS W PROTEIN C-TERMINUS IN COMPLEX WITH      
REMARK 900 IMPORTIN ALPHA 3 CRYSTAL FORM 2                                      
DBREF  6BWB A   64   521  UNP    O00629   IMA3_HUMAN      64    521             
DBREF  6BWB B  409   448  UNP    P0C1C6   W_HENDH        409    448             
SEQADV 6BWB SER A   63  UNP  O00629              EXPRESSION TAG                 
SEQADV 6BWB SER B  408  UNP  P0C1C6              EXPRESSION TAG                 
SEQRES   1 A  459  SER GLY ASP TYR ARG VAL GLN ASN THR SER LEU GLU ALA          
SEQRES   2 A  459  ILE VAL GLN ASN ALA SER SER ASP ASN GLN GLY ILE GLN          
SEQRES   3 A  459  LEU SER ALA VAL GLN ALA ALA ARG LYS LEU LEU SER SER          
SEQRES   4 A  459  ASP ARG ASN PRO PRO ILE ASP ASP LEU ILE LYS SER GLY          
SEQRES   5 A  459  ILE LEU PRO ILE LEU VAL HIS CYS LEU GLU ARG ASP ASP          
SEQRES   6 A  459  ASN PRO SER LEU GLN PHE GLU ALA ALA TRP ALA LEU THR          
SEQRES   7 A  459  ASN ILE ALA SER GLY THR SER GLU GLN THR GLN ALA VAL          
SEQRES   8 A  459  VAL GLN SER ASN ALA VAL PRO LEU PHE LEU ARG LEU LEU          
SEQRES   9 A  459  HIS SER PRO HIS GLN ASN VAL CYS GLU GLN ALA VAL TRP          
SEQRES  10 A  459  ALA LEU GLY ASN ILE ILE GLY ASP GLY PRO GLN CYS ARG          
SEQRES  11 A  459  ASP TYR VAL ILE SER LEU GLY VAL VAL LYS PRO LEU LEU          
SEQRES  12 A  459  SER PHE ILE SER PRO SER ILE PRO ILE THR PHE LEU ARG          
SEQRES  13 A  459  ASN VAL THR TRP VAL MET VAL ASN LEU CYS ARG HIS LYS          
SEQRES  14 A  459  ASP PRO PRO PRO PRO MET GLU THR ILE GLN GLU ILE LEU          
SEQRES  15 A  459  PRO ALA LEU CYS VAL LEU ILE HIS HIS THR ASP VAL ASN          
SEQRES  16 A  459  ILE LEU VAL ASP THR VAL TRP ALA LEU SER TYR LEU THR          
SEQRES  17 A  459  ASP ALA GLY ASN GLU GLN ILE GLN MET VAL ILE ASP SER          
SEQRES  18 A  459  GLY ILE VAL PRO HIS LEU VAL PRO LEU LEU SER HIS GLN          
SEQRES  19 A  459  GLU VAL LYS VAL GLN THR ALA ALA LEU ARG ALA VAL GLY          
SEQRES  20 A  459  ASN ILE VAL THR GLY THR ASP GLU GLN THR GLN VAL VAL          
SEQRES  21 A  459  LEU ASN CYS ASP ALA LEU SER HIS PHE PRO ALA LEU LEU          
SEQRES  22 A  459  THR HIS PRO LYS GLU LYS ILE ASN LYS GLU ALA VAL TRP          
SEQRES  23 A  459  PHE LEU SER ASN ILE THR ALA GLY ASN GLN GLN GLN VAL          
SEQRES  24 A  459  GLN ALA VAL ILE ASP ALA ASN LEU VAL PRO MET ILE ILE          
SEQRES  25 A  459  HIS LEU LEU ASP LYS GLY ASP PHE GLY THR GLN LYS GLU          
SEQRES  26 A  459  ALA ALA TRP ALA ILE SER ASN LEU THR ILE SER GLY ARG          
SEQRES  27 A  459  LYS ASP GLN VAL ALA TYR LEU ILE GLN GLN ASN VAL ILE          
SEQRES  28 A  459  PRO PRO PHE CYS ASN LEU LEU THR VAL LYS ASP ALA GLN          
SEQRES  29 A  459  VAL VAL GLN VAL VAL LEU ASP GLY LEU SER ASN ILE LEU          
SEQRES  30 A  459  LYS MET ALA GLU ASP GLU ALA GLU THR ILE GLY ASN LEU          
SEQRES  31 A  459  ILE GLU GLU CYS GLY GLY LEU GLU LYS ILE GLU GLN LEU          
SEQRES  32 A  459  GLN ASN HIS GLU ASN GLU ASP ILE TYR LYS LEU ALA TYR          
SEQRES  33 A  459  GLU ILE ILE ASP GLN PHE PHE SER SER ASP ASP ILE ASP          
SEQRES  34 A  459  GLU ASP PRO SER LEU VAL PRO GLU ALA ILE GLN GLY GLY          
SEQRES  35 A  459  THR PHE GLY PHE ASN SER SER ALA ASN VAL PRO THR GLU          
SEQRES  36 A  459  GLY PHE GLN PHE                                              
SEQRES   1 B   41  SER ARG SER LEU ASN MET LEU GLY ARG LYS THR CYS LEU          
SEQRES   2 B   41  GLY ARG ARG VAL VAL GLN PRO GLY MET PHE ALA ASP TYR          
SEQRES   3 B   41  PRO PRO THR LYS LYS ALA ARG VAL LEU LEU ARG ARG MET          
SEQRES   4 B   41  SER ASN                                                      
FORMUL   3  HOH   *205(H2 O)                                                    
HELIX    1 AA1 SER A   72  SER A   82  1                                  11    
HELIX    2 AA2 ASN A   84  SER A  101  1                                  18    
HELIX    3 AA3 PRO A  106  SER A  113  1                                   8    
HELIX    4 AA4 ILE A  115  LEU A  123  1                                   9    
HELIX    5 AA5 ASN A  128  SER A  144  1                                  17    
HELIX    6 AA6 THR A  146  SER A  156  1                                  11    
HELIX    7 AA7 ASN A  157  LEU A  166  1                                  10    
HELIX    8 AA8 HIS A  170  ASP A  187  1                                  18    
HELIX    9 AA9 GLY A  188  LEU A  198  1                                  11    
HELIX   10 AB1 VAL A  200  PHE A  207  1                                   8    
HELIX   11 AB2 PRO A  213  HIS A  230  1                                  18    
HELIX   12 AB3 PRO A  236  ILE A  251  1                                  16    
HELIX   13 AB4 ASP A  255  ASP A  271  1                                  17    
HELIX   14 AB5 GLY A  273  SER A  283  1                                  11    
HELIX   15 AB6 ILE A  285  VAL A  290  1                                   6    
HELIX   16 AB7 PRO A  291  HIS A  295  5                                   5    
HELIX   17 AB8 GLU A  297  THR A  313  1                                  17    
HELIX   18 AB9 THR A  315  ASN A  324  1                                  10    
HELIX   19 AC1 CYS A  325  HIS A  330  5                                   6    
HELIX   20 AC2 PHE A  331  THR A  336  1                                   6    
HELIX   21 AC3 LYS A  339  ALA A  355  1                                  17    
HELIX   22 AC4 ASN A  357  ALA A  367  1                                  11    
HELIX   23 AC5 LEU A  369  GLY A  380  1                                  12    
HELIX   24 AC6 ASP A  381  THR A  396  1                                  16    
HELIX   25 AC7 ARG A  400  GLN A  410  1                                  11    
HELIX   26 AC8 VAL A  412  LEU A  419  1                                   8    
HELIX   27 AC9 LEU A  420  VAL A  422  5                                   3    
HELIX   28 AD1 ASP A  424  ALA A  442  1                                  19    
HELIX   29 AD2 GLU A  445  CYS A  456  1                                  12    
HELIX   30 AD3 GLY A  457  GLN A  466  1                                  10    
HELIX   31 AD4 ASN A  470  PHE A  485  1                                  16    
CISPEP   1 ASP A  232    PRO A  233          0         1.89                     
CRYST1   48.160   58.990  169.289  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020764  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016952  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005907        0.00000                         
ATOM      1  N   SER A  72      18.377 -14.273 -33.588  1.00 70.71           N  
ATOM      2  CA  SER A  72      18.696 -13.947 -32.207  1.00 59.79           C  
ATOM      3  C   SER A  72      19.355 -12.578 -32.109  1.00 60.81           C  
ATOM      4  O   SER A  72      19.943 -12.093 -33.078  1.00 52.33           O  
ATOM      5  CB  SER A  72      19.624 -15.000 -31.600  1.00 70.78           C  
ATOM      6  OG  SER A  72      20.976 -14.726 -31.929  1.00 67.19           O  
ATOM      7  N   LEU A  73      19.279 -11.975 -30.919  1.00 51.84           N  
ATOM      8  CA  LEU A  73      19.821 -10.632 -30.727  1.00 48.19           C  
ATOM      9  C   LEU A  73      21.324 -10.591 -30.975  1.00 55.97           C  
ATOM     10  O   LEU A  73      21.836  -9.622 -31.555  1.00 43.77           O  
ATOM     11  CB  LEU A  73      19.505 -10.139 -29.317  1.00 62.42           C  
ATOM     12  CG  LEU A  73      18.137  -9.488 -29.087  1.00 54.17           C  
ATOM     13  CD1 LEU A  73      17.012 -10.459 -29.372  1.00 57.75           C  
ATOM     14  CD2 LEU A  73      18.041  -8.961 -27.662  1.00 45.86           C  
ATOM     15  N   GLU A  74      22.052 -11.616 -30.521  1.00 63.01           N  
ATOM     16  CA  GLU A  74      23.496 -11.668 -30.747  1.00 59.86           C  
ATOM     17  C   GLU A  74      23.818 -11.610 -32.233  1.00 56.96           C  
ATOM     18  O   GLU A  74      24.634 -10.790 -32.678  1.00 52.16           O  
ATOM     19  CB  GLU A  74      24.079 -12.943 -30.138  1.00 68.76           C  
ATOM     20  CG  GLU A  74      24.708 -12.766 -28.766  1.00 82.75           C  
ATOM     21  CD  GLU A  74      25.310 -14.058 -28.229  1.00 83.03           C  
ATOM     22  OE1 GLU A  74      26.124 -14.683 -28.943  1.00 76.09           O  
ATOM     23  OE2 GLU A  74      24.960 -14.456 -27.097  1.00 95.98           O  
ATOM     24  N   ALA A  75      23.191 -12.493 -33.014  1.00 51.08           N  
ATOM     25  CA  ALA A  75      23.431 -12.505 -34.451  1.00 52.66           C  
ATOM     26  C   ALA A  75      23.029 -11.179 -35.077  1.00 48.56           C  
ATOM     27  O   ALA A  75      23.731 -10.659 -35.951  1.00 41.52           O  
ATOM     28  CB  ALA A  75      22.670 -13.660 -35.099  1.00 54.32           C  
ATOM     29  N   ILE A  76      21.900 -10.616 -34.640  1.00 53.46           N  
ATOM     30  CA  ILE A  76      21.428  -9.356 -35.203  1.00 35.93           C  
ATOM     31  C   ILE A  76      22.462  -8.261 -34.991  1.00 44.51           C  
ATOM     32  O   ILE A  76      22.803  -7.521 -35.918  1.00 42.27           O  
ATOM     33  CB  ILE A  76      20.068  -8.983 -34.591  1.00 34.83           C  
ATOM     34  CG1 ILE A  76      18.970  -9.816 -35.257  1.00 37.07           C  
ATOM     35  CG2 ILE A  76      19.790  -7.491 -34.747  1.00 34.67           C  
ATOM     36  CD1 ILE A  76      17.659  -9.821 -34.515  1.00 43.15           C  
ATOM     37  N   VAL A  77      22.971  -8.141 -33.763  1.00 47.93           N  
ATOM     38  CA  VAL A  77      23.980  -7.128 -33.461  1.00 51.08           C  
ATOM     39  C   VAL A  77      25.226  -7.355 -34.309  1.00 48.85           C  
ATOM     40  O   VAL A  77      25.779  -6.420 -34.911  1.00 49.85           O  
ATOM     41  CB  VAL A  77      24.307  -7.143 -31.956  1.00 50.87           C  
ATOM     42  CG1 VAL A  77      25.608  -6.392 -31.650  1.00 46.68           C  
ATOM     43  CG2 VAL A  77      23.161  -6.544 -31.173  1.00 45.39           C  
ATOM     44  N   GLN A  78      25.694  -8.602 -34.357  1.00 55.28           N  
ATOM     45  CA  GLN A  78      26.878  -8.916 -35.149  1.00 57.53           C  
ATOM     46  C   GLN A  78      26.694  -8.493 -36.603  1.00 53.04           C  
ATOM     47  O   GLN A  78      27.520  -7.757 -37.159  1.00 48.84           O  
ATOM     48  CB  GLN A  78      27.177 -10.411 -35.051  1.00 53.78           C  
ATOM     49  CG  GLN A  78      28.355 -10.851 -35.894  1.00 67.50           C  
ATOM     50  CD  GLN A  78      29.236 -11.832 -35.166  1.00 65.63           C  
ATOM     51  OE1 GLN A  78      30.462 -11.700 -35.164  1.00 67.35           O  
ATOM     52  NE2 GLN A  78      28.618 -12.825 -34.536  1.00 65.47           N  
ATOM     53  N   ASN A  79      25.600  -8.936 -37.227  1.00 47.80           N  
ATOM     54  CA  ASN A  79      25.345  -8.645 -38.635  1.00 42.91           C  
ATOM     55  C   ASN A  79      25.085  -7.164 -38.878  1.00 44.95           C  
ATOM     56  O   ASN A  79      25.355  -6.666 -39.977  1.00 40.74           O  
ATOM     57  CB  ASN A  79      24.158  -9.470 -39.127  1.00 39.35           C  
ATOM     58  CG  ASN A  79      24.456 -10.959 -39.151  1.00 39.97           C  
ATOM     59  OD1 ASN A  79      25.605 -11.371 -39.327  1.00 42.23           O  
ATOM     60  ND2 ASN A  79      23.419 -11.774 -38.983  1.00 36.03           N  
ATOM     61  N   ALA A  80      24.569  -6.442 -37.878  1.00 41.95           N  
ATOM     62  CA  ALA A  80      24.349  -5.012 -38.036  1.00 33.87           C  
ATOM     63  C   ALA A  80      25.650  -4.229 -37.957  1.00 34.33           C  
ATOM     64  O   ALA A  80      25.746  -3.143 -38.536  1.00 40.34           O  
ATOM     65  CB  ALA A  80      23.369  -4.507 -36.978  1.00 39.06           C  
ATOM     66  N   SER A  81      26.654  -4.745 -37.244  1.00 51.68           N  
ATOM     67  CA  SER A  81      27.957  -4.082 -37.245  1.00 52.85           C  
ATOM     68  C   SER A  81      28.716  -4.271 -38.556  1.00 50.61           C  
ATOM     69  O   SER A  81      29.694  -3.556 -38.790  1.00 52.38           O  
ATOM     70  CB  SER A  81      28.800  -4.602 -36.083  1.00 55.99           C  
ATOM     71  OG  SER A  81      28.984  -6.004 -36.191  1.00 75.50           O  
ATOM     72  N   SER A  82      28.273  -5.194 -39.410  1.00 53.51           N  
ATOM     73  CA  SER A  82      28.991  -5.568 -40.622  1.00 47.51           C  
ATOM     74  C   SER A  82      29.243  -4.370 -41.530  1.00 47.59           C  
ATOM     75  O   SER A  82      28.496  -3.386 -41.541  1.00 45.33           O  
ATOM     76  CB  SER A  82      28.201  -6.609 -41.412  1.00 44.98           C  
ATOM     77  OG  SER A  82      27.762  -7.653 -40.567  1.00 50.64           O  
ATOM     78  N   ASP A  83      30.305  -4.486 -42.331  1.00 48.48           N  
ATOM     79  CA  ASP A  83      30.622  -3.498 -43.356  1.00 50.65           C  
ATOM     80  C   ASP A  83      29.845  -3.711 -44.651  1.00 45.96           C  
ATOM     81  O   ASP A  83      29.902  -2.849 -45.535  1.00 48.35           O  
ATOM     82  CB  ASP A  83      32.119  -3.529 -43.672  1.00 56.21           C  
ATOM     83  CG  ASP A  83      32.977  -3.132 -42.488  1.00 65.76           C  
ATOM     84  OD1 ASP A  83      33.301  -4.015 -41.664  1.00 61.69           O  
ATOM     85  OD2 ASP A  83      33.328  -1.934 -42.384  1.00 71.52           O  
ATOM     86  N   ASN A  84      29.155  -4.842 -44.801  1.00 29.46           N  
ATOM     87  CA  ASN A  84      28.328  -5.102 -45.976  1.00 38.79           C  
ATOM     88  C   ASN A  84      26.913  -4.599 -45.705  1.00 33.66           C  
ATOM     89  O   ASN A  84      26.198  -5.154 -44.863  1.00 25.72           O  
ATOM     90  CB  ASN A  84      28.331  -6.591 -46.304  1.00 36.04           C  
ATOM     91  CG  ASN A  84      27.541  -6.912 -47.561  1.00 35.18           C  
ATOM     92  OD1 ASN A  84      26.312  -6.910 -47.549  1.00 30.84           O  
ATOM     93  ND2 ASN A  84      28.249  -7.191 -48.652  1.00 28.24           N  
ATOM     94  N   GLN A  85      26.492  -3.561 -46.426  1.00 25.06           N  
ATOM     95  CA  GLN A  85      25.280  -2.875 -46.004  1.00 36.87           C  
ATOM     96  C   GLN A  85      24.005  -3.623 -46.387  1.00 32.43           C  
ATOM     97  O   GLN A  85      22.950  -3.326 -45.824  1.00 27.42           O  
ATOM     98  CB  GLN A  85      25.263  -1.432 -46.528  1.00 35.18           C  
ATOM     99  CG  GLN A  85      25.254  -1.249 -48.008  1.00 49.21           C  
ATOM    100  CD  GLN A  85      25.490   0.210 -48.389  1.00 51.65           C  
ATOM    101  OE1 GLN A  85      26.304   0.900 -47.769  1.00 41.33           O  
ATOM    102  NE2 GLN A  85      24.770   0.689 -49.399  1.00 47.60           N  
ATOM    103  N   GLY A  86      24.068  -4.619 -47.272  1.00 30.83           N  
ATOM    104  CA  GLY A  86      22.916  -5.493 -47.464  1.00 34.29           C  
ATOM    105  C   GLY A  86      22.616  -6.337 -46.232  1.00 31.50           C  
ATOM    106  O   GLY A  86      21.461  -6.449 -45.794  1.00 36.10           O  
ATOM    107  N   ILE A  87      23.663  -6.925 -45.643  1.00 32.66           N  
ATOM    108  CA  ILE A  87      23.531  -7.680 -44.394  1.00 32.47           C  
ATOM    109  C   ILE A  87      23.144  -6.755 -43.245  1.00 27.09           C  
ATOM    110  O   ILE A  87      22.284  -7.096 -42.420  1.00 25.00           O  
ATOM    111  CB  ILE A  87      24.843  -8.440 -44.100  1.00 27.86           C  
ATOM    112  CG1 ILE A  87      25.008  -9.584 -45.097  1.00 32.73           C  
ATOM    113  CG2 ILE A  87      24.872  -8.994 -42.678  1.00 24.71           C  
ATOM    114  CD1 ILE A  87      26.412  -9.730 -45.634  1.00 31.62           C  
ATOM    115  N   GLN A  88      23.793  -5.587 -43.156  1.00 20.31           N  
ATOM    116  CA  GLN A  88      23.394  -4.574 -42.184  1.00 28.06           C  
ATOM    117  C   GLN A  88      21.903  -4.298 -42.279  1.00 29.76           C  
ATOM    118  O   GLN A  88      21.199  -4.272 -41.268  1.00 21.68           O  
ATOM    119  CB  GLN A  88      24.161  -3.270 -42.417  1.00 29.52           C  
ATOM    120  CG  GLN A  88      25.383  -3.057 -41.582  1.00 47.72           C  
ATOM    121  CD  GLN A  88      25.541  -1.599 -41.176  1.00 43.11           C  
ATOM    122  OE1 GLN A  88      25.789  -0.729 -42.012  1.00 37.04           O  
ATOM    123  NE2 GLN A  88      25.392  -1.328 -39.886  1.00 44.93           N  
ATOM    124  N   LEU A  89      21.412  -4.044 -43.491  1.00 22.23           N  
ATOM    125  CA  LEU A  89      20.016  -3.659 -43.635  1.00 22.77           C  
ATOM    126  C   LEU A  89      19.109  -4.787 -43.181  1.00 21.79           C  
ATOM    127  O   LEU A  89      18.151  -4.553 -42.443  1.00 17.65           O  
ATOM    128  CB  LEU A  89      19.727  -3.263 -45.081  1.00 22.40           C  
ATOM    129  CG  LEU A  89      18.312  -2.810 -45.408  1.00 24.58           C  
ATOM    130  CD1 LEU A  89      17.928  -1.607 -44.561  1.00 23.15           C  
ATOM    131  CD2 LEU A  89      18.222  -2.478 -46.891  1.00 21.89           C  
ATOM    132  N   SER A  90      19.407  -6.025 -43.591  1.00 27.66           N  
ATOM    133  CA  SER A  90      18.585  -7.154 -43.153  1.00 26.07           C  
ATOM    134  C   SER A  90      18.532  -7.242 -41.628  1.00 24.44           C  
ATOM    135  O   SER A  90      17.465  -7.451 -41.035  1.00 22.55           O  
ATOM    136  CB  SER A  90      19.133  -8.453 -43.740  1.00 30.18           C  
ATOM    137  OG  SER A  90      18.999  -8.463 -45.142  1.00 53.18           O  
ATOM    138  N   ALA A  91      19.682  -7.077 -40.974  1.00 17.66           N  
ATOM    139  CA  ALA A  91      19.733  -7.182 -39.517  1.00 21.73           C  
ATOM    140  C   ALA A  91      19.011  -6.021 -38.840  1.00 13.67           C  
ATOM    141  O   ALA A  91      18.299  -6.211 -37.848  1.00 18.27           O  
ATOM    142  CB  ALA A  91      21.191  -7.242 -39.053  1.00 22.47           C  
ATOM    143  N   VAL A  92      19.198  -4.805 -39.341  1.00 17.26           N  
ATOM    144  CA  VAL A  92      18.478  -3.665 -38.783  1.00 21.27           C  
ATOM    145  C   VAL A  92      16.980  -3.865 -38.943  1.00 15.34           C  
ATOM    146  O   VAL A  92      16.202  -3.559 -38.036  1.00 18.01           O  
ATOM    147  CB  VAL A  92      18.959  -2.353 -39.434  1.00 15.67           C  
ATOM    148  CG1 VAL A  92      18.110  -1.177 -38.975  1.00 23.80           C  
ATOM    149  CG2 VAL A  92      20.410  -2.098 -39.079  1.00 24.62           C  
ATOM    150  N   GLN A  93      16.547  -4.390 -40.089  1.00 15.56           N  
ATOM    151  CA  GLN A  93      15.128  -4.651 -40.280  1.00 17.52           C  
ATOM    152  C   GLN A  93      14.621  -5.710 -39.307  1.00 24.11           C  
ATOM    153  O   GLN A  93      13.479  -5.628 -38.840  1.00 19.28           O  
ATOM    154  CB  GLN A  93      14.868  -5.064 -41.723  1.00 22.77           C  
ATOM    155  CG  GLN A  93      14.971  -3.903 -42.700  1.00 26.47           C  
ATOM    156  CD  GLN A  93      14.644  -4.293 -44.137  1.00 29.70           C  
ATOM    157  OE1 GLN A  93      14.776  -5.455 -44.525  1.00 36.91           O  
ATOM    158  NE2 GLN A  93      14.213  -3.317 -44.931  1.00 25.37           N  
ATOM    159  N   ALA A  94      15.453  -6.707 -38.984  1.00 22.07           N  
ATOM    160  CA  ALA A  94      15.047  -7.719 -38.004  1.00 23.40           C  
ATOM    161  C   ALA A  94      14.882  -7.112 -36.610  1.00 23.21           C  
ATOM    162  O   ALA A  94      13.957  -7.470 -35.860  1.00 22.42           O  
ATOM    163  CB  ALA A  94      16.072  -8.851 -37.969  1.00 20.13           C  
ATOM    164  N   ALA A  95      15.782  -6.199 -36.242  1.00 19.23           N  
ATOM    165  CA  ALA A  95      15.643  -5.488 -34.973  1.00 22.79           C  
ATOM    166  C   ALA A  95      14.376  -4.642 -34.968  1.00 15.89           C  
ATOM    167  O   ALA A  95      13.615  -4.630 -33.991  1.00 21.00           O  
ATOM    168  CB  ALA A  95      16.875  -4.615 -34.727  1.00 13.71           C  
ATOM    169  N   ARG A  96      14.136  -3.924 -36.064  1.00 16.08           N  
ATOM    170  CA  ARG A  96      12.920  -3.135 -36.183  1.00 18.35           C  
ATOM    171  C   ARG A  96      11.686  -4.011 -36.030  1.00 17.71           C  
ATOM    172  O   ARG A  96      10.741  -3.641 -35.330  1.00 17.43           O  
ATOM    173  CB  ARG A  96      12.905  -2.406 -37.524  1.00 13.90           C  
ATOM    174  CG  ARG A  96      11.637  -1.560 -37.759  1.00 15.51           C  
ATOM    175  CD  ARG A  96      10.587  -2.308 -38.593  1.00 10.92           C  
ATOM    176  NE  ARG A  96      10.993  -2.413 -39.993  1.00 16.34           N  
ATOM    177  CZ  ARG A  96      10.323  -3.077 -40.936  1.00 22.57           C  
ATOM    178  NH1 ARG A  96       9.194  -3.719 -40.647  1.00 19.32           N  
ATOM    179  NH2 ARG A  96      10.784  -3.096 -42.182  1.00 17.92           N  
ATOM    180  N   LYS A  97      11.676  -5.177 -36.681  1.00 22.05           N  
ATOM    181  CA  LYS A  97      10.550  -6.093 -36.539  1.00 25.62           C  
ATOM    182  C   LYS A  97      10.333  -6.464 -35.080  1.00 25.46           C  
ATOM    183  O   LYS A  97       9.198  -6.440 -34.585  1.00 20.39           O  
ATOM    184  CB  LYS A  97      10.762  -7.344 -37.393  1.00 26.06           C  
ATOM    185  CG  LYS A  97      10.065  -8.592 -36.840  1.00 37.58           C  
ATOM    186  CD  LYS A  97       9.715  -9.602 -37.929  1.00 42.04           C  
ATOM    187  CE  LYS A  97      10.076 -11.045 -37.550  1.00 56.70           C  
ATOM    188  NZ  LYS A  97       9.626 -11.474 -36.183  1.00 60.82           N  
ATOM    189  N   LEU A  98      11.406  -6.823 -34.365  1.00 21.65           N  
ATOM    190  CA  LEU A  98      11.229  -7.116 -32.947  1.00 17.50           C  
ATOM    191  C   LEU A  98      10.616  -5.933 -32.213  1.00 19.97           C  
ATOM    192  O   LEU A  98       9.851  -6.113 -31.261  1.00 18.86           O  
ATOM    193  CB  LEU A  98      12.563  -7.490 -32.307  1.00 23.29           C  
ATOM    194  CG  LEU A  98      13.132  -8.864 -32.658  1.00 33.11           C  
ATOM    195  CD1 LEU A  98      14.483  -9.030 -31.972  1.00 34.58           C  
ATOM    196  CD2 LEU A  98      12.179  -9.975 -32.263  1.00 33.27           C  
ATOM    197  N   LEU A  99      10.932  -4.720 -32.641  1.00 23.09           N  
ATOM    198  CA  LEU A  99      10.501  -3.538 -31.910  1.00 19.74           C  
ATOM    199  C   LEU A  99       9.128  -3.028 -32.324  1.00 18.57           C  
ATOM    200  O   LEU A  99       8.564  -2.192 -31.616  1.00 17.06           O  
ATOM    201  CB  LEU A  99      11.527  -2.412 -32.090  1.00 21.21           C  
ATOM    202  CG  LEU A  99      12.854  -2.626 -31.376  1.00 13.81           C  
ATOM    203  CD1 LEU A  99      13.895  -1.674 -31.918  1.00 21.43           C  
ATOM    204  CD2 LEU A  99      12.678  -2.430 -29.871  1.00 22.56           C  
ATOM    205  N   SER A 100       8.565  -3.508 -33.437  1.00 18.02           N  
ATOM    206  CA  SER A 100       7.357  -2.889 -33.975  1.00 24.53           C  
ATOM    207  C   SER A 100       6.264  -3.890 -34.335  1.00 20.60           C  
ATOM    208  O   SER A 100       5.367  -3.550 -35.110  1.00 25.40           O  
ATOM    209  CB  SER A 100       7.704  -2.050 -35.208  1.00 27.14           C  
ATOM    210  OG  SER A 100       8.253  -2.875 -36.219  1.00 32.27           O  
ATOM    211  N   SER A 101       6.295  -5.099 -33.779  1.00 28.90           N  
ATOM    212  CA  SER A 101       5.294  -6.108 -34.118  1.00 33.43           C  
ATOM    213  C   SER A 101       4.096  -6.065 -33.188  1.00 41.64           C  
ATOM    214  O   SER A 101       2.963  -6.301 -33.621  1.00 43.21           O  
ATOM    215  CB  SER A 101       5.914  -7.504 -34.075  1.00 32.75           C  
ATOM    216  OG  SER A 101       6.886  -7.644 -35.093  1.00 41.83           O  
ATOM    217  N   ASP A 102       4.334  -5.781 -31.914  1.00 39.36           N  
ATOM    218  CA  ASP A 102       3.271  -5.716 -30.923  1.00 49.54           C  
ATOM    219  C   ASP A 102       3.459  -4.470 -30.069  1.00 57.54           C  
ATOM    220  O   ASP A 102       4.306  -3.620 -30.373  1.00 43.89           O  
ATOM    221  CB  ASP A 102       3.287  -6.974 -30.059  1.00 52.15           C  
ATOM    222  CG  ASP A 102       4.678  -7.295 -29.553  1.00 57.35           C  
ATOM    223  OD1 ASP A 102       5.149  -6.588 -28.637  1.00 47.45           O  
ATOM    224  OD2 ASP A 102       5.315  -8.222 -30.097  1.00 64.04           O  
ATOM    225  N   ARG A 103       2.686  -4.363 -28.992  1.00 54.50           N  
ATOM    226  CA  ARG A 103       2.771  -3.240 -28.072  1.00 45.46           C  
ATOM    227  C   ARG A 103       3.572  -3.580 -26.817  1.00 48.61           C  
ATOM    228  O   ARG A 103       3.433  -2.901 -25.796  1.00 61.93           O  
ATOM    229  CB  ARG A 103       1.361  -2.763 -27.715  1.00 56.22           C  
ATOM    230  CG  ARG A 103       0.665  -2.057 -28.879  1.00 63.16           C  
ATOM    231  CD  ARG A 103      -0.861  -2.043 -28.766  1.00 88.11           C  
ATOM    232  NE  ARG A 103      -1.365  -0.979 -27.888  1.00 91.81           N  
ATOM    233  CZ  ARG A 103      -1.995  -1.160 -26.729  1.00 92.18           C  
ATOM    234  NH1 ARG A 103      -2.410  -0.110 -26.027  1.00 86.83           N  
ATOM    235  NH2 ARG A 103      -2.230  -2.381 -26.258  1.00 96.31           N  
ATOM    236  N   ASN A 104       4.416  -4.615 -26.878  1.00 49.71           N  
ATOM    237  CA  ASN A 104       5.290  -4.991 -25.762  1.00 47.79           C  
ATOM    238  C   ASN A 104       6.680  -5.328 -26.293  1.00 41.23           C  
ATOM    239  O   ASN A 104       7.199  -6.429 -26.085  1.00 44.24           O  
ATOM    240  CB  ASN A 104       4.692  -6.161 -24.980  1.00 51.20           C  
ATOM    241  CG  ASN A 104       3.815  -5.702 -23.824  1.00 71.50           C  
ATOM    242  OD1 ASN A 104       4.298  -5.507 -22.708  1.00 69.79           O  
ATOM    243  ND2 ASN A 104       2.524  -5.517 -24.090  1.00 70.42           N  
ATOM    244  N   PRO A 105       7.323  -4.380 -26.976  1.00 28.49           N  
ATOM    245  CA  PRO A 105       8.609  -4.690 -27.592  1.00 33.58           C  
ATOM    246  C   PRO A 105       9.665  -4.930 -26.556  1.00 27.98           C  
ATOM    247  O   PRO A 105       9.634  -4.348 -25.450  1.00 35.36           O  
ATOM    248  CB  PRO A 105       8.909  -3.424 -28.421  1.00 31.81           C  
ATOM    249  CG  PRO A 105       8.139  -2.344 -27.749  1.00 33.38           C  
ATOM    250  CD  PRO A 105       6.898  -2.996 -27.234  1.00 33.10           C  
ATOM    251  N   PRO A 106      10.656  -5.770 -26.837  1.00 29.92           N  
ATOM    252  CA  PRO A 106      11.732  -6.037 -25.870  1.00 29.40           C  
ATOM    253  C   PRO A 106      12.815  -4.964 -25.909  1.00 26.43           C  
ATOM    254  O   PRO A 106      13.959  -5.186 -26.312  1.00 30.30           O  
ATOM    255  CB  PRO A 106      12.237  -7.408 -26.320  1.00 24.14           C  
ATOM    256  CG  PRO A 106      12.065  -7.378 -27.798  1.00 28.59           C  
ATOM    257  CD  PRO A 106      10.794  -6.596 -28.054  1.00 25.85           C  
ATOM    258  N   ILE A 107      12.455  -3.754 -25.473  1.00 25.95           N  
ATOM    259  CA  ILE A 107      13.385  -2.632 -25.566  1.00 25.82           C  
ATOM    260  C   ILE A 107      14.608  -2.874 -24.688  1.00 24.81           C  
ATOM    261  O   ILE A 107      15.746  -2.619 -25.102  1.00 32.65           O  
ATOM    262  CB  ILE A 107      12.673  -1.310 -25.207  1.00 25.91           C  
ATOM    263  CG1 ILE A 107      11.557  -1.028 -26.220  1.00 24.50           C  
ATOM    264  CG2 ILE A 107      13.676  -0.140 -25.178  1.00 23.69           C  
ATOM    265  CD1 ILE A 107      10.686   0.185 -25.897  1.00 22.85           C  
ATOM    266  N   ASP A 108      14.402  -3.371 -23.468  1.00 22.49           N  
ATOM    267  CA  ASP A 108      15.533  -3.564 -22.566  1.00 25.10           C  
ATOM    268  C   ASP A 108      16.524  -4.577 -23.127  1.00 21.78           C  
ATOM    269  O   ASP A 108      17.743  -4.368 -23.059  1.00 20.54           O  
ATOM    270  CB  ASP A 108      15.036  -3.993 -21.187  1.00 24.94           C  
ATOM    271  CG  ASP A 108      14.487  -2.824 -20.373  1.00 42.95           C  
ATOM    272  OD1 ASP A 108      14.900  -1.665 -20.620  1.00 32.34           O  
ATOM    273  OD2 ASP A 108      13.643  -3.062 -19.480  1.00 51.40           O  
ATOM    274  N   ASP A 109      16.023  -5.671 -23.708  1.00 26.68           N  
ATOM    275  CA  ASP A 109      16.922  -6.661 -24.296  1.00 30.20           C  
ATOM    276  C   ASP A 109      17.731  -6.062 -25.441  1.00 28.24           C  
ATOM    277  O   ASP A 109      18.942  -6.290 -25.545  1.00 28.88           O  
ATOM    278  CB  ASP A 109      16.130  -7.876 -24.781  1.00 28.81           C  
ATOM    279  CG  ASP A 109      15.609  -8.726 -23.638  1.00 41.36           C  
ATOM    280  OD1 ASP A 109      14.640  -9.483 -23.855  1.00 45.81           O  
ATOM    281  OD2 ASP A 109      16.157  -8.620 -22.518  1.00 48.87           O  
ATOM    282  N   LEU A 110      17.091  -5.282 -26.307  1.00 25.65           N  
ATOM    283  CA  LEU A 110      17.835  -4.729 -27.432  1.00 33.22           C  
ATOM    284  C   LEU A 110      18.845  -3.685 -26.975  1.00 25.30           C  
ATOM    285  O   LEU A 110      19.931  -3.586 -27.560  1.00 26.11           O  
ATOM    286  CB  LEU A 110      16.875  -4.149 -28.472  1.00 34.42           C  
ATOM    287  CG  LEU A 110      16.357  -5.183 -29.479  1.00 22.55           C  
ATOM    288  CD1 LEU A 110      14.855  -5.309 -29.414  1.00 32.57           C  
ATOM    289  CD2 LEU A 110      16.777  -4.807 -30.864  1.00 25.75           C  
ATOM    290  N   ILE A 111      18.532  -2.919 -25.927  1.00 20.76           N  
ATOM    291  CA  ILE A 111      19.516  -1.984 -25.383  1.00 21.98           C  
ATOM    292  C   ILE A 111      20.702  -2.737 -24.802  1.00 24.97           C  
ATOM    293  O   ILE A 111      21.862  -2.373 -25.027  1.00 28.35           O  
ATOM    294  CB  ILE A 111      18.879  -1.075 -24.323  1.00 25.35           C  
ATOM    295  CG1 ILE A 111      17.895  -0.117 -24.977  1.00 23.24           C  
ATOM    296  CG2 ILE A 111      19.971  -0.294 -23.569  1.00 23.47           C  
ATOM    297  CD1 ILE A 111      17.094   0.727 -23.983  1.00 31.71           C  
ATOM    298  N   LYS A 112      20.426  -3.771 -24.002  1.00 28.77           N  
ATOM    299  CA  LYS A 112      21.498  -4.543 -23.381  1.00 34.48           C  
ATOM    300  C   LYS A 112      22.388  -5.222 -24.417  1.00 27.52           C  
ATOM    301  O   LYS A 112      23.587  -5.390 -24.186  1.00 28.46           O  
ATOM    302  CB  LYS A 112      20.904  -5.577 -22.425  1.00 34.00           C  
ATOM    303  CG  LYS A 112      20.528  -4.995 -21.066  1.00 51.73           C  
ATOM    304  CD  LYS A 112      19.335  -5.702 -20.407  1.00 58.91           C  
ATOM    305  CE  LYS A 112      18.701  -4.794 -19.347  1.00 58.40           C  
ATOM    306  NZ  LYS A 112      18.081  -5.534 -18.215  1.00 61.15           N  
ATOM    307  N   SER A 113      21.834  -5.605 -25.564  1.00 31.00           N  
ATOM    308  CA  SER A 113      22.634  -6.276 -26.582  1.00 30.28           C  
ATOM    309  C   SER A 113      23.657  -5.361 -27.233  1.00 28.10           C  
ATOM    310  O   SER A 113      24.504  -5.851 -27.988  1.00 27.85           O  
ATOM    311  CB  SER A 113      21.728  -6.857 -27.663  1.00 37.90           C  
ATOM    312  OG  SER A 113      21.055  -5.826 -28.371  1.00 33.89           O  
ATOM    313  N   GLY A 114      23.602  -4.057 -26.968  1.00 33.57           N  
ATOM    314  CA  GLY A 114      24.557  -3.139 -27.554  1.00 23.11           C  
ATOM    315  C   GLY A 114      24.252  -2.701 -28.968  1.00 30.04           C  
ATOM    316  O   GLY A 114      25.177  -2.437 -29.741  1.00 29.42           O  
ATOM    317  N   ILE A 115      22.975  -2.582 -29.326  1.00 39.06           N  
ATOM    318  CA  ILE A 115      22.618  -2.205 -30.688  1.00 31.98           C  
ATOM    319  C   ILE A 115      22.526  -0.693 -30.867  1.00 20.06           C  
ATOM    320  O   ILE A 115      22.640  -0.207 -32.002  1.00 21.52           O  
ATOM    321  CB  ILE A 115      21.294  -2.881 -31.094  1.00 27.10           C  
ATOM    322  CG1 ILE A 115      21.202  -2.999 -32.614  1.00 28.46           C  
ATOM    323  CG2 ILE A 115      20.099  -2.126 -30.502  1.00 25.51           C  
ATOM    324  CD1 ILE A 115      19.983  -3.728 -33.098  1.00 33.32           C  
ATOM    325  N   LEU A 116      22.354   0.066 -29.786  1.00 21.41           N  
ATOM    326  CA  LEU A 116      22.147   1.508 -29.929  1.00 20.55           C  
ATOM    327  C   LEU A 116      23.257   2.187 -30.710  1.00 20.55           C  
ATOM    328  O   LEU A 116      22.946   2.933 -31.656  1.00 18.75           O  
ATOM    329  CB  LEU A 116      21.985   2.152 -28.550  1.00 23.39           C  
ATOM    330  CG  LEU A 116      20.667   1.894 -27.823  1.00 26.30           C  
ATOM    331  CD1 LEU A 116      20.708   2.579 -26.471  1.00 23.58           C  
ATOM    332  CD2 LEU A 116      19.479   2.379 -28.623  1.00 20.95           C  
ATOM    333  N   PRO A 117      24.539   2.014 -30.372  1.00 27.12           N  
ATOM    334  CA  PRO A 117      25.586   2.659 -31.180  1.00 26.70           C  
ATOM    335  C   PRO A 117      25.552   2.243 -32.633  1.00 25.67           C  
ATOM    336  O   PRO A 117      25.856   3.057 -33.511  1.00 21.72           O  
ATOM    337  CB  PRO A 117      26.890   2.216 -30.494  1.00 31.25           C  
ATOM    338  CG  PRO A 117      26.512   1.104 -29.561  1.00 26.41           C  
ATOM    339  CD  PRO A 117      25.093   1.352 -29.178  1.00 25.63           C  
ATOM    340  N   ILE A 118      25.165   1.001 -32.917  1.00 28.57           N  
ATOM    341  CA  ILE A 118      25.098   0.545 -34.299  1.00 22.15           C  
ATOM    342  C   ILE A 118      23.982   1.270 -35.044  1.00 19.60           C  
ATOM    343  O   ILE A 118      24.182   1.758 -36.159  1.00 14.39           O  
ATOM    344  CB  ILE A 118      24.923  -0.983 -34.345  1.00 26.99           C  
ATOM    345  CG1 ILE A 118      26.154  -1.672 -33.736  1.00 32.26           C  
ATOM    346  CG2 ILE A 118      24.710  -1.462 -35.777  1.00 24.72           C  
ATOM    347  CD1 ILE A 118      25.925  -3.113 -33.360  1.00 33.73           C  
ATOM    348  N   LEU A 119      22.790   1.351 -34.443  1.00 17.65           N  
ATOM    349  CA  LEU A 119      21.688   2.076 -35.076  1.00 16.87           C  
ATOM    350  C   LEU A 119      22.056   3.533 -35.315  1.00 15.73           C  
ATOM    351  O   LEU A 119      21.795   4.090 -36.394  1.00 12.93           O  
ATOM    352  CB  LEU A 119      20.440   1.981 -34.203  1.00 17.15           C  
ATOM    353  CG  LEU A 119      19.906   0.568 -34.006  1.00 18.25           C  
ATOM    354  CD1 LEU A 119      18.768   0.571 -33.009  1.00 21.59           C  
ATOM    355  CD2 LEU A 119      19.438  -0.032 -35.333  1.00 23.92           C  
ATOM    356  N   VAL A 120      22.689   4.162 -34.325  1.00 15.15           N  
ATOM    357  CA  VAL A 120      23.090   5.555 -34.482  1.00 16.72           C  
ATOM    358  C   VAL A 120      24.072   5.692 -35.638  1.00 20.72           C  
ATOM    359  O   VAL A 120      23.950   6.603 -36.466  1.00 18.12           O  
ATOM    360  CB  VAL A 120      23.666   6.088 -33.159  1.00 19.87           C  
ATOM    361  CG1 VAL A 120      24.182   7.492 -33.327  1.00 22.87           C  
ATOM    362  CG2 VAL A 120      22.583   6.087 -32.090  1.00 20.14           C  
ATOM    363  N   HIS A 121      25.044   4.778 -35.728  1.00 20.56           N  
ATOM    364  CA  HIS A 121      25.973   4.793 -36.857  1.00 22.37           C  
ATOM    365  C   HIS A 121      25.232   4.639 -38.180  1.00 19.85           C  
ATOM    366  O   HIS A 121      25.553   5.316 -39.165  1.00 19.13           O  
ATOM    367  CB  HIS A 121      27.014   3.680 -36.706  1.00 33.50           C  
ATOM    368  CG  HIS A 121      28.022   3.928 -35.625  1.00 63.12           C  
ATOM    369  ND1 HIS A 121      28.212   5.167 -35.049  1.00 72.33           N  
ATOM    370  CD2 HIS A 121      28.895   3.091 -35.013  1.00 69.78           C  
ATOM    371  CE1 HIS A 121      29.158   5.082 -34.130  1.00 80.76           C  
ATOM    372  NE2 HIS A 121      29.589   3.834 -34.088  1.00 75.72           N  
ATOM    373  N   CYS A 122      24.241   3.747 -38.222  1.00 18.15           N  
ATOM    374  CA  CYS A 122      23.434   3.566 -39.429  1.00 20.14           C  
ATOM    375  C   CYS A 122      22.752   4.859 -39.842  1.00 17.13           C  
ATOM    376  O   CYS A 122      22.496   5.079 -41.029  1.00 17.44           O  
ATOM    377  CB  CYS A 122      22.382   2.483 -39.200  1.00 18.13           C  
ATOM    378  SG  CYS A 122      23.004   0.811 -39.233  1.00 22.33           S  
ATOM    379  N   LEU A 123      22.420   5.709 -38.874  1.00 23.11           N  
ATOM    380  CA  LEU A 123      21.807   6.992 -39.212  1.00 18.81           C  
ATOM    381  C   LEU A 123      22.711   7.871 -40.070  1.00 21.89           C  
ATOM    382  O   LEU A 123      22.213   8.811 -40.706  1.00 18.29           O  
ATOM    383  CB  LEU A 123      21.436   7.759 -37.948  1.00 21.02           C  
ATOM    384  CG  LEU A 123      20.384   7.143 -37.038  1.00 15.00           C  
ATOM    385  CD1 LEU A 123      20.158   8.086 -35.882  1.00 16.48           C  
ATOM    386  CD2 LEU A 123      19.077   6.871 -37.787  1.00 12.85           C  
ATOM    387  N   GLU A 124      24.018   7.598 -40.106  1.00 20.97           N  
ATOM    388  CA  GLU A 124      24.950   8.423 -40.873  1.00 23.37           C  
ATOM    389  C   GLU A 124      25.047   8.030 -42.340  1.00 23.94           C  
ATOM    390  O   GLU A 124      25.763   8.698 -43.091  1.00 31.50           O  
ATOM    391  CB  GLU A 124      26.357   8.353 -40.276  1.00 16.98           C  
ATOM    392  CG  GLU A 124      26.440   8.594 -38.788  1.00 32.73           C  
ATOM    393  CD  GLU A 124      27.867   8.514 -38.268  1.00 41.18           C  
ATOM    394  OE1 GLU A 124      28.786   8.304 -39.087  1.00 49.18           O  
ATOM    395  OE2 GLU A 124      28.067   8.647 -37.040  1.00 42.58           O  
ATOM    396  N   ARG A 125      24.358   6.976 -42.772  1.00 24.25           N  
ATOM    397  CA  ARG A 125      24.590   6.389 -44.095  1.00 21.28           C  
ATOM    398  C   ARG A 125      23.711   7.076 -45.139  1.00 22.78           C  
ATOM    399  O   ARG A 125      22.659   6.580 -45.547  1.00 18.24           O  
ATOM    400  CB  ARG A 125      24.338   4.891 -44.045  1.00 25.95           C  
ATOM    401  CG  ARG A 125      25.068   4.199 -42.895  1.00 33.40           C  
ATOM    402  CD  ARG A 125      26.566   4.338 -43.020  1.00 34.83           C  
ATOM    403  NE  ARG A 125      27.028   3.924 -44.338  1.00 38.86           N  
ATOM    404  CZ  ARG A 125      27.192   2.659 -44.714  1.00 47.02           C  
ATOM    405  NH1 ARG A 125      26.926   1.664 -43.874  1.00 28.83           N  
ATOM    406  NH2 ARG A 125      27.619   2.391 -45.941  1.00 67.93           N  
ATOM    407  N   ASP A 126      24.169   8.247 -45.584  1.00 19.95           N  
ATOM    408  CA  ASP A 126      23.457   8.979 -46.627  1.00 22.01           C  
ATOM    409  C   ASP A 126      23.391   8.189 -47.927  1.00 23.98           C  
ATOM    410  O   ASP A 126      22.500   8.419 -48.748  1.00 23.10           O  
ATOM    411  CB  ASP A 126      24.134  10.326 -46.871  1.00 37.06           C  
ATOM    412  CG  ASP A 126      24.282  11.141 -45.602  1.00 41.91           C  
ATOM    413  OD1 ASP A 126      25.406  11.201 -45.057  1.00 53.02           O  
ATOM    414  OD2 ASP A 126      23.268  11.701 -45.135  1.00 44.65           O  
ATOM    415  N   ASP A 127      24.326   7.267 -48.138  1.00 27.80           N  
ATOM    416  CA  ASP A 127      24.320   6.424 -49.324  1.00 26.32           C  
ATOM    417  C   ASP A 127      23.293   5.303 -49.253  1.00 25.94           C  
ATOM    418  O   ASP A 127      23.095   4.607 -50.254  1.00 24.49           O  
ATOM    419  CB  ASP A 127      25.706   5.813 -49.530  1.00 31.17           C  
ATOM    420  CG  ASP A 127      26.220   5.118 -48.285  1.00 34.83           C  
ATOM    421  OD1 ASP A 127      25.986   5.642 -47.176  1.00 29.44           O  
ATOM    422  OD2 ASP A 127      26.849   4.047 -48.411  1.00 49.25           O  
ATOM    423  N   ASN A 128      22.657   5.090 -48.102  1.00 26.32           N  
ATOM    424  CA  ASN A 128      21.676   4.020 -47.937  1.00 24.43           C  
ATOM    425  C   ASN A 128      20.488   4.542 -47.149  1.00 19.36           C  
ATOM    426  O   ASN A 128      20.327   4.248 -45.959  1.00 19.75           O  
ATOM    427  CB  ASN A 128      22.298   2.803 -47.257  1.00 22.14           C  
ATOM    428  CG  ASN A 128      21.499   1.552 -47.508  1.00 17.94           C  
ATOM    429  OD1 ASN A 128      20.278   1.605 -47.613  1.00 25.28           O  
ATOM    430  ND2 ASN A 128      22.178   0.423 -47.625  1.00 32.12           N  
ATOM    431  N   PRO A 129      19.626   5.328 -47.790  1.00 19.62           N  
ATOM    432  CA  PRO A 129      18.420   5.825 -47.112  1.00 23.71           C  
ATOM    433  C   PRO A 129      17.573   4.741 -46.456  1.00 22.48           C  
ATOM    434  O   PRO A 129      16.940   5.017 -45.431  1.00 14.39           O  
ATOM    435  CB  PRO A 129      17.653   6.518 -48.246  1.00 30.96           C  
ATOM    436  CG  PRO A 129      18.675   6.873 -49.235  1.00 27.52           C  
ATOM    437  CD  PRO A 129      19.728   5.823 -49.169  1.00 18.03           C  
ATOM    438  N   SER A 130      17.516   3.529 -47.021  1.00 18.89           N  
ATOM    439  CA  SER A 130      16.748   2.454 -46.390  1.00 24.62           C  
ATOM    440  C   SER A 130      17.293   2.135 -45.011  1.00 19.78           C  
ATOM    441  O   SER A 130      16.531   1.903 -44.067  1.00 19.47           O  
ATOM    442  CB  SER A 130      16.777   1.193 -47.253  1.00 18.26           C  
ATOM    443  OG  SER A 130      16.093   1.398 -48.463  1.00 34.99           O  
ATOM    444  N   LEU A 131      18.614   2.100 -44.886  1.00 16.55           N  
ATOM    445  CA  LEU A 131      19.225   1.811 -43.599  1.00 19.28           C  
ATOM    446  C   LEU A 131      18.956   2.933 -42.606  1.00 19.65           C  
ATOM    447  O   LEU A 131      18.636   2.672 -41.443  1.00 16.57           O  
ATOM    448  CB  LEU A 131      20.727   1.593 -43.786  1.00 18.03           C  
ATOM    449  CG  LEU A 131      21.495   1.021 -42.600  1.00 24.17           C  
ATOM    450  CD1 LEU A 131      21.037  -0.390 -42.253  1.00 24.76           C  
ATOM    451  CD2 LEU A 131      22.983   1.044 -42.902  1.00 30.55           C  
ATOM    452  N   GLN A 132      19.059   4.190 -43.055  1.00 18.78           N  
ATOM    453  CA  GLN A 132      18.716   5.322 -42.198  1.00 17.49           C  
ATOM    454  C   GLN A 132      17.276   5.218 -41.719  1.00 14.70           C  
ATOM    455  O   GLN A 132      16.989   5.384 -40.534  1.00 13.75           O  
ATOM    456  CB  GLN A 132      18.926   6.639 -42.951  1.00 16.01           C  
ATOM    457  CG  GLN A 132      20.338   6.895 -43.437  1.00 21.64           C  
ATOM    458  CD  GLN A 132      20.464   8.231 -44.159  1.00 18.70           C  
ATOM    459  OE1 GLN A 132      19.771   8.491 -45.143  1.00 17.90           O  
ATOM    460  NE2 GLN A 132      21.332   9.093 -43.654  1.00 15.61           N  
ATOM    461  N   PHE A 133      16.356   4.942 -42.635  1.00 13.82           N  
ATOM    462  CA  PHE A 133      14.944   4.869 -42.286  1.00 15.94           C  
ATOM    463  C   PHE A 133      14.686   3.750 -41.283  1.00 14.21           C  
ATOM    464  O   PHE A 133      14.024   3.963 -40.259  1.00 13.49           O  
ATOM    465  CB  PHE A 133      14.116   4.680 -43.563  1.00 18.26           C  
ATOM    466  CG  PHE A 133      12.725   4.186 -43.319  1.00 16.04           C  
ATOM    467  CD1 PHE A 133      11.745   5.043 -42.849  1.00 16.05           C  
ATOM    468  CD2 PHE A 133      12.396   2.863 -43.561  1.00 16.12           C  
ATOM    469  CE1 PHE A 133      10.463   4.591 -42.613  1.00 15.75           C  
ATOM    470  CE2 PHE A 133      11.110   2.400 -43.332  1.00 17.26           C  
ATOM    471  CZ  PHE A 133      10.142   3.263 -42.857  1.00 20.11           C  
ATOM    472  N   GLU A 134      15.219   2.550 -41.541  1.00 13.90           N  
ATOM    473  CA  GLU A 134      14.964   1.432 -40.634  1.00 11.71           C  
ATOM    474  C   GLU A 134      15.602   1.667 -39.267  1.00 10.64           C  
ATOM    475  O   GLU A 134      15.008   1.350 -38.232  1.00 10.70           O  
ATOM    476  CB  GLU A 134      15.481   0.127 -41.237  1.00 14.30           C  
ATOM    477  CG  GLU A 134      14.802  -0.296 -42.533  1.00 19.75           C  
ATOM    478  CD  GLU A 134      13.367  -0.814 -42.362  1.00 24.10           C  
ATOM    479  OE1 GLU A 134      12.867  -0.921 -41.220  1.00 23.24           O  
ATOM    480  OE2 GLU A 134      12.738  -1.128 -43.391  1.00 25.19           O  
ATOM    481  N   ALA A 135      16.819   2.207 -39.242  1.00 14.59           N  
ATOM    482  CA  ALA A 135      17.454   2.526 -37.974  1.00 13.51           C  
ATOM    483  C   ALA A 135      16.669   3.592 -37.226  1.00 11.31           C  
ATOM    484  O   ALA A 135      16.485   3.500 -36.008  1.00 10.76           O  
ATOM    485  CB  ALA A 135      18.888   2.983 -38.228  1.00 12.17           C  
ATOM    486  N   ALA A 136      16.204   4.619 -37.936  1.00 16.27           N  
ATOM    487  CA  ALA A 136      15.376   5.643 -37.312  1.00 13.34           C  
ATOM    488  C   ALA A 136      14.102   5.046 -36.740  1.00  8.26           C  
ATOM    489  O   ALA A 136      13.641   5.468 -35.686  1.00 12.67           O  
ATOM    490  CB  ALA A 136      15.042   6.737 -38.326  1.00 14.65           C  
ATOM    491  N   TRP A 137      13.522   4.060 -37.420  1.00 14.41           N  
ATOM    492  CA  TRP A 137      12.299   3.424 -36.938  1.00  8.04           C  
ATOM    493  C   TRP A 137      12.570   2.623 -35.668  1.00  9.54           C  
ATOM    494  O   TRP A 137      11.820   2.709 -34.678  1.00  8.93           O  
ATOM    495  CB  TRP A 137      11.744   2.539 -38.053  1.00 14.03           C  
ATOM    496  CG  TRP A 137      10.446   1.843 -37.792  1.00 13.80           C  
ATOM    497  CD1 TRP A 137       9.802   1.686 -36.595  1.00 17.83           C  
ATOM    498  CD2 TRP A 137       9.630   1.195 -38.770  1.00 13.55           C  
ATOM    499  NE1 TRP A 137       8.647   0.976 -36.770  1.00  9.83           N  
ATOM    500  CE2 TRP A 137       8.512   0.667 -38.098  1.00 12.83           C  
ATOM    501  CE3 TRP A 137       9.732   1.017 -40.153  1.00 18.32           C  
ATOM    502  CZ2 TRP A 137       7.500  -0.031 -38.764  1.00 16.08           C  
ATOM    503  CZ3 TRP A 137       8.720   0.321 -40.813  1.00 19.42           C  
ATOM    504  CH2 TRP A 137       7.620  -0.190 -40.111  1.00 14.48           C  
ATOM    505  N   ALA A 138      13.645   1.836 -35.682  1.00 11.07           N  
ATOM    506  CA  ALA A 138      14.046   1.100 -34.488  1.00 12.20           C  
ATOM    507  C   ALA A 138      14.289   2.052 -33.320  1.00 11.32           C  
ATOM    508  O   ALA A 138      13.817   1.817 -32.201  1.00 12.43           O  
ATOM    509  CB  ALA A 138      15.297   0.279 -34.789  1.00 12.42           C  
ATOM    510  N   LEU A 139      15.015   3.145 -33.569  1.00 11.28           N  
ATOM    511  CA  LEU A 139      15.313   4.100 -32.506  1.00 11.92           C  
ATOM    512  C   LEU A 139      14.052   4.820 -32.047  1.00 12.74           C  
ATOM    513  O   LEU A 139      13.882   5.072 -30.851  1.00 14.53           O  
ATOM    514  CB  LEU A 139      16.374   5.103 -32.978  1.00  9.37           C  
ATOM    515  CG  LEU A 139      17.816   4.572 -33.069  1.00  9.23           C  
ATOM    516  CD1 LEU A 139      18.724   5.579 -33.748  1.00 11.27           C  
ATOM    517  CD2 LEU A 139      18.358   4.238 -31.706  1.00 12.33           C  
ATOM    518  N   THR A 140      13.146   5.138 -32.976  1.00  7.97           N  
ATOM    519  CA  THR A 140      11.848   5.688 -32.612  1.00  9.10           C  
ATOM    520  C   THR A 140      11.179   4.818 -31.568  1.00  7.50           C  
ATOM    521  O   THR A 140      10.719   5.308 -30.530  1.00  9.17           O  
ATOM    522  CB  THR A 140      10.946   5.807 -33.849  1.00  8.75           C  
ATOM    523  OG1 THR A 140      11.478   6.776 -34.762  1.00 11.35           O  
ATOM    524  CG2 THR A 140       9.545   6.241 -33.454  1.00  9.35           C  
ATOM    525  N   ASN A 141      11.113   3.514 -31.831  1.00  9.26           N  
ATOM    526  CA  ASN A 141      10.376   2.640 -30.926  1.00  8.02           C  
ATOM    527  C   ASN A 141      11.108   2.430 -29.607  1.00 13.35           C  
ATOM    528  O   ASN A 141      10.461   2.311 -28.557  1.00 14.73           O  
ATOM    529  CB  ASN A 141      10.075   1.317 -31.617  1.00 13.05           C  
ATOM    530  CG  ASN A 141       8.930   1.442 -32.601  1.00 11.98           C  
ATOM    531  OD1 ASN A 141       8.561   2.551 -32.990  1.00  9.60           O  
ATOM    532  ND2 ASN A 141       8.356   0.318 -32.999  1.00 16.21           N  
ATOM    533  N   ILE A 142      12.442   2.391 -29.626  1.00 12.59           N  
ATOM    534  CA  ILE A 142      13.184   2.361 -28.368  1.00 11.15           C  
ATOM    535  C   ILE A 142      12.898   3.619 -27.552  1.00 14.58           C  
ATOM    536  O   ILE A 142      12.717   3.561 -26.330  1.00 14.61           O  
ATOM    537  CB  ILE A 142      14.690   2.200 -28.636  1.00 12.53           C  
ATOM    538  CG1 ILE A 142      14.981   0.799 -29.175  1.00 14.55           C  
ATOM    539  CG2 ILE A 142      15.497   2.466 -27.356  1.00 14.42           C  
ATOM    540  CD1 ILE A 142      16.344   0.646 -29.758  1.00 20.39           C  
ATOM    541  N   ALA A 143      12.882   4.776 -28.213  1.00 10.15           N  
ATOM    542  CA  ALA A 143      12.641   6.053 -27.555  1.00  9.07           C  
ATOM    543  C   ALA A 143      11.193   6.235 -27.112  1.00 12.67           C  
ATOM    544  O   ALA A 143      10.915   7.159 -26.342  1.00  9.61           O  
ATOM    545  CB  ALA A 143      13.025   7.199 -28.490  1.00  8.15           C  
ATOM    546  N   SER A 144      10.266   5.399 -27.582  1.00 10.37           N  
ATOM    547  CA  SER A 144       8.867   5.505 -27.180  1.00 17.86           C  
ATOM    548  C   SER A 144       8.594   4.885 -25.819  1.00 15.23           C  
ATOM    549  O   SER A 144       7.444   4.896 -25.373  1.00 14.64           O  
ATOM    550  CB  SER A 144       7.968   4.827 -28.210  1.00 14.94           C  
ATOM    551  OG  SER A 144       8.182   3.424 -28.187  1.00 15.39           O  
ATOM    552  N   GLY A 145       9.609   4.348 -25.159  1.00 17.36           N  
ATOM    553  CA  GLY A 145       9.444   3.665 -23.896  1.00 19.68           C  
ATOM    554  C   GLY A 145       9.645   4.585 -22.715  1.00 15.00           C  
ATOM    555  O   GLY A 145       9.321   5.776 -22.764  1.00 13.96           O  
ATOM    556  N   THR A 146      10.196   4.023 -21.640  1.00 14.51           N  
ATOM    557  CA  THR A 146      10.359   4.756 -20.391  1.00 20.93           C  
ATOM    558  C   THR A 146      11.447   5.820 -20.517  1.00 16.89           C  
ATOM    559  O   THR A 146      12.227   5.848 -21.475  1.00 17.09           O  
ATOM    560  CB  THR A 146      10.723   3.811 -19.250  1.00 23.57           C  
ATOM    561  OG1 THR A 146      12.042   3.288 -19.472  1.00 22.26           O  
ATOM    562  CG2 THR A 146       9.720   2.675 -19.156  1.00 19.95           C  
ATOM    563  N   SER A 147      11.519   6.688 -19.503  1.00 14.84           N  
ATOM    564  CA  SER A 147      12.530   7.736 -19.516  1.00 18.73           C  
ATOM    565  C   SER A 147      13.925   7.146 -19.663  1.00 15.38           C  
ATOM    566  O   SER A 147      14.734   7.651 -20.440  1.00 21.66           O  
ATOM    567  CB  SER A 147      12.435   8.591 -18.254  1.00 18.25           C  
ATOM    568  OG  SER A 147      11.275   9.410 -18.286  1.00 36.41           O  
ATOM    569  N   GLU A 148      14.220   6.064 -18.945  1.00 17.50           N  
ATOM    570  CA  GLU A 148      15.544   5.448 -19.037  1.00 18.99           C  
ATOM    571  C   GLU A 148      15.854   4.981 -20.461  1.00 16.92           C  
ATOM    572  O   GLU A 148      16.989   5.109 -20.936  1.00 16.56           O  
ATOM    573  CB  GLU A 148      15.633   4.283 -18.048  1.00 24.86           C  
ATOM    574  CG  GLU A 148      16.531   3.137 -18.479  1.00 41.53           C  
ATOM    575  CD  GLU A 148      16.587   2.021 -17.441  1.00 58.88           C  
ATOM    576  OE1 GLU A 148      16.966   2.307 -16.281  1.00 77.75           O  
ATOM    577  OE2 GLU A 148      16.230   0.868 -17.776  1.00 57.89           O  
ATOM    578  N   GLN A 149      14.856   4.454 -21.169  1.00 18.75           N  
ATOM    579  CA  GLN A 149      15.090   3.967 -22.528  1.00 19.34           C  
ATOM    580  C   GLN A 149      15.256   5.126 -23.513  1.00 11.07           C  
ATOM    581  O   GLN A 149      16.164   5.120 -24.364  1.00 15.27           O  
ATOM    582  CB  GLN A 149      13.938   3.051 -22.936  1.00 13.15           C  
ATOM    583  CG  GLN A 149      13.842   1.824 -22.051  1.00 18.17           C  
ATOM    584  CD  GLN A 149      12.506   1.092 -22.151  1.00 17.38           C  
ATOM    585  OE1 GLN A 149      11.507   1.643 -22.600  1.00 23.28           O  
ATOM    586  NE2 GLN A 149      12.489  -0.160 -21.727  1.00 23.76           N  
ATOM    587  N   THR A 150      14.399   6.141 -23.405  1.00  9.14           N  
ATOM    588  CA  THR A 150      14.589   7.344 -24.215  1.00 14.90           C  
ATOM    589  C   THR A 150      15.964   7.950 -23.964  1.00 11.33           C  
ATOM    590  O   THR A 150      16.661   8.350 -24.905  1.00 14.60           O  
ATOM    591  CB  THR A 150      13.508   8.382 -23.913  1.00 15.06           C  
ATOM    592  OG1 THR A 150      12.209   7.778 -23.993  1.00 14.14           O  
ATOM    593  CG2 THR A 150      13.589   9.523 -24.913  1.00  9.74           C  
ATOM    594  N   GLN A 151      16.368   8.019 -22.699  1.00 16.28           N  
ATOM    595  CA  GLN A 151      17.664   8.580 -22.347  1.00 17.16           C  
ATOM    596  C   GLN A 151      18.804   7.745 -22.894  1.00 17.64           C  
ATOM    597  O   GLN A 151      19.846   8.295 -23.237  1.00 16.87           O  
ATOM    598  CB  GLN A 151      17.808   8.704 -20.826  1.00 16.40           C  
ATOM    599  CG  GLN A 151      17.020   9.843 -20.208  1.00 25.41           C  
ATOM    600  CD  GLN A 151      17.129  11.102 -21.025  1.00 32.71           C  
ATOM    601  OE1 GLN A 151      18.212  11.654 -21.202  1.00 38.22           O  
ATOM    602  NE2 GLN A 151      16.006  11.537 -21.577  1.00 38.89           N  
ATOM    603  N   ALA A 152      18.651   6.423 -22.958  1.00 13.25           N  
ATOM    604  CA  ALA A 152      19.677   5.608 -23.601  1.00 19.40           C  
ATOM    605  C   ALA A 152      19.852   6.035 -25.052  1.00 13.51           C  
ATOM    606  O   ALA A 152      20.978   6.180 -25.553  1.00 20.54           O  
ATOM    607  CB  ALA A 152      19.291   4.131 -23.511  1.00 14.38           C  
ATOM    608  N   VAL A 153      18.742   6.303 -25.729  1.00 16.42           N  
ATOM    609  CA  VAL A 153      18.820   6.767 -27.107  1.00 12.78           C  
ATOM    610  C   VAL A 153      19.553   8.116 -27.204  1.00 12.55           C  
ATOM    611  O   VAL A 153      20.437   8.268 -28.041  1.00 10.97           O  
ATOM    612  CB  VAL A 153      17.417   6.927 -27.714  1.00 10.00           C  
ATOM    613  CG1 VAL A 153      17.498   7.611 -29.068  1.00 12.84           C  
ATOM    614  CG2 VAL A 153      16.725   5.579 -27.824  1.00 11.96           C  
ATOM    615  N   VAL A 154      19.229   9.042 -26.307  1.00 15.08           N  
ATOM    616  CA  VAL A 154      19.888  10.342 -26.263  1.00 13.49           C  
ATOM    617  C   VAL A 154      21.380  10.231 -25.919  1.00 14.94           C  
ATOM    618  O   VAL A 154      22.204  10.918 -26.512  1.00 13.15           O  
ATOM    619  CB  VAL A 154      19.220  11.270 -25.231  1.00 17.40           C  
ATOM    620  CG1 VAL A 154      19.921  12.616 -25.192  1.00 18.68           C  
ATOM    621  CG2 VAL A 154      17.740  11.438 -25.540  1.00 16.70           C  
ATOM    622  N   GLN A 155      21.719   9.372 -24.958  1.00 16.49           N  
ATOM    623  CA  GLN A 155      23.090   9.172 -24.533  1.00 20.06           C  
ATOM    624  C   GLN A 155      23.933   8.648 -25.684  1.00 20.74           C  
ATOM    625  O   GLN A 155      25.122   8.937 -25.740  1.00 18.48           O  
ATOM    626  CB  GLN A 155      23.171   8.222 -23.336  1.00 21.61           C  
ATOM    627  CG  GLN A 155      22.762   8.850 -22.013  1.00 25.33           C  
ATOM    628  CD  GLN A 155      23.647  10.016 -21.610  1.00 43.99           C  
ATOM    629  OE1 GLN A 155      24.847  10.030 -21.883  1.00 34.67           O  
ATOM    630  NE2 GLN A 155      23.056  10.999 -20.943  1.00 33.88           N  
ATOM    631  N   SER A 156      23.353   7.857 -26.585  1.00 16.16           N  
ATOM    632  CA  SER A 156      24.167   7.347 -27.679  1.00 20.52           C  
ATOM    633  C   SER A 156      24.332   8.358 -28.820  1.00 19.49           C  
ATOM    634  O   SER A 156      24.739   7.976 -29.924  1.00 17.24           O  
ATOM    635  CB  SER A 156      23.587   6.035 -28.192  1.00 14.83           C  
ATOM    636  OG  SER A 156      22.263   6.213 -28.624  1.00 29.03           O  
ATOM    637  N   ASN A 157      24.054   9.640 -28.561  1.00 15.09           N  
ATOM    638  CA  ASN A 157      24.266  10.734 -29.516  1.00 14.65           C  
ATOM    639  C   ASN A 157      23.310  10.663 -30.706  1.00 11.84           C  
ATOM    640  O   ASN A 157      23.644  11.122 -31.797  1.00 12.40           O  
ATOM    641  CB  ASN A 157      25.717  10.780 -30.023  1.00 14.56           C  
ATOM    642  CG  ASN A 157      26.071  12.113 -30.688  1.00 13.45           C  
ATOM    643  OD1 ASN A 157      25.774  13.185 -30.157  1.00  9.18           O  
ATOM    644  ND2 ASN A 157      26.701  12.046 -31.861  1.00 19.07           N  
ATOM    645  N   ALA A 158      22.095  10.143 -30.510  1.00 16.44           N  
ATOM    646  CA  ALA A 158      21.169  10.027 -31.634  1.00 16.44           C  
ATOM    647  C   ALA A 158      20.638  11.386 -32.093  1.00 10.30           C  
ATOM    648  O   ALA A 158      20.270  11.534 -33.267  1.00 12.63           O  
ATOM    649  CB  ALA A 158      20.011   9.108 -31.260  1.00 11.93           C  
ATOM    650  N   VAL A 159      20.597  12.386 -31.215  1.00  8.24           N  
ATOM    651  CA  VAL A 159      19.832  13.600 -31.503  1.00  8.63           C  
ATOM    652  C   VAL A 159      20.466  14.402 -32.639  1.00 11.02           C  
ATOM    653  O   VAL A 159      19.754  14.801 -33.573  1.00 11.38           O  
ATOM    654  CB  VAL A 159      19.653  14.450 -30.235  1.00 10.83           C  
ATOM    655  CG1 VAL A 159      19.126  15.865 -30.556  1.00 11.10           C  
ATOM    656  CG2 VAL A 159      18.684  13.767 -29.295  1.00 15.05           C  
ATOM    657  N   PRO A 160      21.767  14.687 -32.611  1.00 10.83           N  
ATOM    658  CA  PRO A 160      22.355  15.451 -33.724  1.00 13.35           C  
ATOM    659  C   PRO A 160      22.215  14.744 -35.061  1.00 12.33           C  
ATOM    660  O   PRO A 160      22.057  15.399 -36.100  1.00 13.74           O  
ATOM    661  CB  PRO A 160      23.825  15.610 -33.302  1.00 12.56           C  
ATOM    662  CG  PRO A 160      23.830  15.372 -31.842  1.00 12.10           C  
ATOM    663  CD  PRO A 160      22.771  14.349 -31.599  1.00 10.28           C  
ATOM    664  N   LEU A 161      22.210  13.413 -35.063  1.00 11.63           N  
ATOM    665  CA  LEU A 161      22.042  12.694 -36.318  1.00 14.60           C  
ATOM    666  C   LEU A 161      20.602  12.745 -36.809  1.00 12.40           C  
ATOM    667  O   LEU A 161      20.355  12.848 -38.017  1.00 17.65           O  
ATOM    668  CB  LEU A 161      22.522  11.257 -36.147  1.00 17.52           C  
ATOM    669  CG  LEU A 161      24.038  11.209 -35.917  1.00 13.40           C  
ATOM    670  CD1 LEU A 161      24.446   9.869 -35.436  1.00 31.14           C  
ATOM    671  CD2 LEU A 161      24.770  11.549 -37.190  1.00 23.88           C  
ATOM    672  N   PHE A 162      19.630  12.692 -35.899  1.00 14.76           N  
ATOM    673  CA  PHE A 162      18.251  12.918 -36.323  1.00 14.80           C  
ATOM    674  C   PHE A 162      18.083  14.322 -36.902  1.00 12.43           C  
ATOM    675  O   PHE A 162      17.409  14.516 -37.926  1.00 16.41           O  
ATOM    676  CB  PHE A 162      17.301  12.703 -35.145  1.00 13.32           C  
ATOM    677  CG  PHE A 162      17.062  11.259 -34.806  1.00 10.64           C  
ATOM    678  CD1 PHE A 162      16.725  10.343 -35.789  1.00 12.24           C  
ATOM    679  CD2 PHE A 162      17.143  10.827 -33.499  1.00  9.25           C  
ATOM    680  CE1 PHE A 162      16.491   9.017 -35.469  1.00 10.32           C  
ATOM    681  CE2 PHE A 162      16.907   9.509 -33.171  1.00 12.91           C  
ATOM    682  CZ  PHE A 162      16.581   8.602 -34.161  1.00 15.58           C  
ATOM    683  N   LEU A 163      18.689  15.316 -36.256  1.00 11.81           N  
ATOM    684  CA  LEU A 163      18.622  16.678 -36.774  1.00 16.03           C  
ATOM    685  C   LEU A 163      19.230  16.757 -38.166  1.00 13.87           C  
ATOM    686  O   LEU A 163      18.717  17.470 -39.034  1.00 19.80           O  
ATOM    687  CB  LEU A 163      19.324  17.647 -35.815  1.00 12.15           C  
ATOM    688  CG  LEU A 163      18.635  17.883 -34.469  1.00 14.41           C  
ATOM    689  CD1 LEU A 163      19.479  18.777 -33.571  1.00 15.92           C  
ATOM    690  CD2 LEU A 163      17.245  18.493 -34.645  1.00 18.10           C  
ATOM    691  N   ARG A 164      20.321  16.023 -38.397  1.00 10.84           N  
ATOM    692  CA  ARG A 164      20.877  15.926 -39.743  1.00 17.77           C  
ATOM    693  C   ARG A 164      19.870  15.316 -40.714  1.00 16.95           C  
ATOM    694  O   ARG A 164      19.724  15.784 -41.848  1.00 19.83           O  
ATOM    695  CB  ARG A 164      22.165  15.097 -39.734  1.00 20.76           C  
ATOM    696  CG  ARG A 164      23.419  15.827 -39.214  1.00 32.41           C  
ATOM    697  CD  ARG A 164      24.708  15.277 -39.859  1.00 34.93           C  
ATOM    698  NE  ARG A 164      24.680  15.430 -41.321  1.00 63.47           N  
ATOM    699  CZ  ARG A 164      24.569  14.438 -42.208  1.00 66.95           C  
ATOM    700  NH1 ARG A 164      24.503  13.166 -41.819  1.00 64.56           N  
ATOM    701  NH2 ARG A 164      24.539  14.718 -43.509  1.00 47.72           N  
ATOM    702  N   LEU A 165      19.194  14.246 -40.302  1.00 14.74           N  
ATOM    703  CA  LEU A 165      18.255  13.581 -41.202  1.00 18.12           C  
ATOM    704  C   LEU A 165      17.059  14.453 -41.532  1.00 17.80           C  
ATOM    705  O   LEU A 165      16.343  14.168 -42.499  1.00 15.83           O  
ATOM    706  CB  LEU A 165      17.773  12.267 -40.595  1.00 17.33           C  
ATOM    707  CG  LEU A 165      18.864  11.198 -40.448  1.00 16.93           C  
ATOM    708  CD1 LEU A 165      18.282   9.940 -39.861  1.00 22.49           C  
ATOM    709  CD2 LEU A 165      19.528  10.887 -41.778  1.00 18.93           C  
ATOM    710  N   LEU A 166      16.821  15.500 -40.746  1.00 13.68           N  
ATOM    711  CA  LEU A 166      15.721  16.408 -41.057  1.00 15.54           C  
ATOM    712  C   LEU A 166      15.905  17.110 -42.396  1.00 18.21           C  
ATOM    713  O   LEU A 166      14.936  17.643 -42.942  1.00 23.56           O  
ATOM    714  CB  LEU A 166      15.559  17.455 -39.953  1.00 14.81           C  
ATOM    715  CG  LEU A 166      15.063  16.955 -38.602  1.00 12.04           C  
ATOM    716  CD1 LEU A 166      14.874  18.129 -37.674  1.00 15.34           C  
ATOM    717  CD2 LEU A 166      13.770  16.179 -38.743  1.00 17.53           C  
ATOM    718  N   HIS A 167      17.120  17.119 -42.941  1.00 22.81           N  
ATOM    719  CA  HIS A 167      17.389  17.738 -44.233  1.00 21.43           C  
ATOM    720  C   HIS A 167      17.717  16.693 -45.288  1.00 22.18           C  
ATOM    721  O   HIS A 167      18.340  17.000 -46.304  1.00 30.61           O  
ATOM    722  CB  HIS A 167      18.508  18.772 -44.088  1.00 24.67           C  
ATOM    723  CG  HIS A 167      18.360  19.631 -42.868  1.00 31.19           C  
ATOM    724  ND1 HIS A 167      17.379  20.594 -42.751  1.00 33.83           N  
ATOM    725  CD2 HIS A 167      19.034  19.636 -41.692  1.00 27.98           C  
ATOM    726  CE1 HIS A 167      17.466  21.168 -41.565  1.00 33.62           C  
ATOM    727  NE2 HIS A 167      18.470  20.614 -40.908  1.00 42.83           N  
ATOM    728  N   SER A 168      17.294  15.461 -45.063  1.00 22.79           N  
ATOM    729  CA  SER A 168      17.496  14.426 -46.047  1.00 24.55           C  
ATOM    730  C   SER A 168      16.606  14.673 -47.266  1.00 27.03           C  
ATOM    731  O   SER A 168      15.506  15.220 -47.146  1.00 27.18           O  
ATOM    732  CB  SER A 168      17.194  13.070 -45.431  1.00 23.93           C  
ATOM    733  OG  SER A 168      16.854  12.109 -46.397  1.00 21.77           O  
ATOM    734  N   PRO A 169      17.071  14.303 -48.460  1.00 26.65           N  
ATOM    735  CA  PRO A 169      16.211  14.429 -49.648  1.00 37.53           C  
ATOM    736  C   PRO A 169      15.083  13.419 -49.690  1.00 33.11           C  
ATOM    737  O   PRO A 169      14.136  13.612 -50.461  1.00 32.00           O  
ATOM    738  CB  PRO A 169      17.187  14.217 -50.817  1.00 31.84           C  
ATOM    739  CG  PRO A 169      18.328  13.468 -50.235  1.00 31.42           C  
ATOM    740  CD  PRO A 169      18.438  13.864 -48.800  1.00 32.01           C  
ATOM    741  N   HIS A 170      15.148  12.357 -48.890  1.00 23.83           N  
ATOM    742  CA  HIS A 170      14.154  11.293 -48.906  1.00 26.50           C  
ATOM    743  C   HIS A 170      13.119  11.543 -47.820  1.00 27.87           C  
ATOM    744  O   HIS A 170      13.446  11.542 -46.628  1.00 23.96           O  
ATOM    745  CB  HIS A 170      14.823   9.937 -48.714  1.00 23.70           C  
ATOM    746  CG  HIS A 170      16.056   9.763 -49.540  1.00 32.58           C  
ATOM    747  ND1 HIS A 170      16.028   9.273 -50.827  1.00 40.33           N  
ATOM    748  CD2 HIS A 170      17.354  10.036 -49.271  1.00 39.06           C  
ATOM    749  CE1 HIS A 170      17.257   9.238 -51.310  1.00 39.31           C  
ATOM    750  NE2 HIS A 170      18.081   9.697 -50.385  1.00 38.71           N  
ATOM    751  N   GLN A 171      11.868  11.723 -48.243  1.00 21.52           N  
ATOM    752  CA  GLN A 171      10.793  12.127 -47.343  1.00 26.88           C  
ATOM    753  C   GLN A 171      10.678  11.194 -46.137  1.00 24.01           C  
ATOM    754  O   GLN A 171      10.523  11.650 -45.002  1.00 17.73           O  
ATOM    755  CB  GLN A 171       9.474  12.167 -48.127  1.00 35.53           C  
ATOM    756  CG  GLN A 171       8.280  12.712 -47.359  1.00 47.23           C  
ATOM    757  CD  GLN A 171       8.066  14.181 -47.604  1.00 55.33           C  
ATOM    758  OE1 GLN A 171       8.772  15.021 -47.049  1.00 59.98           O  
ATOM    759  NE2 GLN A 171       7.089  14.504 -48.447  1.00 57.55           N  
ATOM    760  N   ASN A 172      10.731   9.880 -46.370  1.00 18.90           N  
ATOM    761  CA  ASN A 172      10.449   8.913 -45.308  1.00 19.37           C  
ATOM    762  C   ASN A 172      11.519   8.942 -44.219  1.00 17.53           C  
ATOM    763  O   ASN A 172      11.215   8.754 -43.032  1.00 16.47           O  
ATOM    764  CB  ASN A 172      10.322   7.512 -45.908  1.00 20.10           C  
ATOM    765  CG  ASN A 172      11.552   7.096 -46.698  1.00 27.17           C  
ATOM    766  OD1 ASN A 172      11.875   7.681 -47.736  1.00 32.22           O  
ATOM    767  ND2 ASN A 172      12.237   6.068 -46.217  1.00 31.61           N  
ATOM    768  N   VAL A 173      12.772   9.190 -44.605  1.00 18.79           N  
ATOM    769  CA  VAL A 173      13.843   9.399 -43.634  1.00 13.01           C  
ATOM    770  C   VAL A 173      13.536  10.611 -42.760  1.00 12.22           C  
ATOM    771  O   VAL A 173      13.649  10.562 -41.527  1.00 10.74           O  
ATOM    772  CB  VAL A 173      15.188   9.557 -44.364  1.00 14.06           C  
ATOM    773  CG1 VAL A 173      16.275   9.986 -43.406  1.00 17.98           C  
ATOM    774  CG2 VAL A 173      15.559   8.255 -45.037  1.00 21.38           C  
ATOM    775  N   CYS A 174      13.145  11.717 -43.397  1.00 13.57           N  
ATOM    776  CA  CYS A 174      12.802  12.941 -42.672  1.00 16.95           C  
ATOM    777  C   CYS A 174      11.669  12.693 -41.686  1.00 15.41           C  
ATOM    778  O   CYS A 174      11.735  13.097 -40.519  1.00 15.90           O  
ATOM    779  CB  CYS A 174      12.379  14.052 -43.644  1.00 16.63           C  
ATOM    780  SG  CYS A 174      13.595  14.710 -44.778  1.00 23.96           S  
ATOM    781  N   GLU A 175      10.595  12.056 -42.157  1.00 13.85           N  
ATOM    782  CA  GLU A 175       9.435  11.802 -41.308  1.00 15.75           C  
ATOM    783  C   GLU A 175       9.813  10.968 -40.100  1.00 11.26           C  
ATOM    784  O   GLU A 175       9.368  11.240 -38.978  1.00 13.86           O  
ATOM    785  CB  GLU A 175       8.345  11.064 -42.081  1.00 19.07           C  
ATOM    786  CG  GLU A 175       7.643  11.879 -43.115  1.00 31.13           C  
ATOM    787  CD  GLU A 175       6.281  11.308 -43.473  1.00 36.10           C  
ATOM    788  OE1 GLU A 175       5.519  10.915 -42.551  1.00 35.22           O  
ATOM    789  OE2 GLU A 175       5.987  11.249 -44.683  1.00 40.09           O  
ATOM    790  N   GLN A 176      10.589   9.907 -40.316  1.00 10.51           N  
ATOM    791  CA  GLN A 176      10.885   9.036 -39.190  1.00  9.77           C  
ATOM    792  C   GLN A 176      11.786   9.743 -38.193  1.00  9.62           C  
ATOM    793  O   GLN A 176      11.639   9.548 -36.983  1.00 11.63           O  
ATOM    794  CB  GLN A 176      11.505   7.719 -39.678  1.00  8.66           C  
ATOM    795  CG  GLN A 176      11.349   6.565 -38.698  1.00 14.16           C  
ATOM    796  CD  GLN A 176       9.901   6.352 -38.298  1.00 14.95           C  
ATOM    797  OE1 GLN A 176       9.041   6.126 -39.143  1.00 16.47           O  
ATOM    798  NE2 GLN A 176       9.622   6.453 -37.008  1.00 14.07           N  
ATOM    799  N   ALA A 177      12.696  10.596 -38.679  1.00 12.87           N  
ATOM    800  CA  ALA A 177      13.503  11.413 -37.776  1.00 11.43           C  
ATOM    801  C   ALA A 177      12.637  12.380 -36.974  1.00 10.73           C  
ATOM    802  O   ALA A 177      12.870  12.588 -35.779  1.00  9.88           O  
ATOM    803  CB  ALA A 177      14.553  12.181 -38.573  1.00 12.75           C  
ATOM    804  N   VAL A 178      11.645  12.998 -37.618  1.00 10.73           N  
ATOM    805  CA  VAL A 178      10.714  13.852 -36.882  1.00 13.81           C  
ATOM    806  C   VAL A 178      10.027  13.056 -35.778  1.00 12.26           C  
ATOM    807  O   VAL A 178       9.933  13.508 -34.634  1.00 12.65           O  
ATOM    808  CB  VAL A 178       9.702  14.492 -37.851  1.00 14.96           C  
ATOM    809  CG1 VAL A 178       8.515  15.089 -37.098  1.00 17.73           C  
ATOM    810  CG2 VAL A 178      10.388  15.563 -38.665  1.00 11.30           C  
ATOM    811  N   TRP A 179       9.543  11.862 -36.101  1.00  8.15           N  
ATOM    812  CA  TRP A 179       8.869  11.025 -35.112  1.00 11.88           C  
ATOM    813  C   TRP A 179       9.789  10.715 -33.921  1.00  9.31           C  
ATOM    814  O   TRP A 179       9.408  10.883 -32.746  1.00  7.05           O  
ATOM    815  CB  TRP A 179       8.399   9.745 -35.818  1.00  9.09           C  
ATOM    816  CG  TRP A 179       7.402   8.914 -35.110  1.00  9.38           C  
ATOM    817  CD1 TRP A 179       7.247   8.784 -33.770  1.00  7.26           C  
ATOM    818  CD2 TRP A 179       6.423   8.061 -35.714  1.00  8.75           C  
ATOM    819  NE1 TRP A 179       6.232   7.909 -33.492  1.00 11.62           N  
ATOM    820  CE2 TRP A 179       5.706   7.451 -34.671  1.00 14.26           C  
ATOM    821  CE3 TRP A 179       6.084   7.755 -37.034  1.00  9.11           C  
ATOM    822  CZ2 TRP A 179       4.662   6.558 -34.904  1.00 13.18           C  
ATOM    823  CZ3 TRP A 179       5.042   6.877 -37.271  1.00  9.58           C  
ATOM    824  CH2 TRP A 179       4.335   6.292 -36.210  1.00 12.22           C  
ATOM    825  N   ALA A 180      11.006  10.250 -34.215  1.00  9.18           N  
ATOM    826  CA  ALA A 180      11.960   9.915 -33.158  1.00 10.86           C  
ATOM    827  C   ALA A 180      12.232  11.119 -32.268  1.00  9.18           C  
ATOM    828  O   ALA A 180      12.265  11.012 -31.030  1.00 11.04           O  
ATOM    829  CB  ALA A 180      13.263   9.406 -33.771  1.00  8.85           C  
ATOM    830  N   LEU A 181      12.449  12.281 -32.885  1.00  9.11           N  
ATOM    831  CA  LEU A 181      12.651  13.482 -32.099  1.00  6.86           C  
ATOM    832  C   LEU A 181      11.418  13.802 -31.277  1.00  9.84           C  
ATOM    833  O   LEU A 181      11.534  14.330 -30.169  1.00 11.19           O  
ATOM    834  CB  LEU A 181      13.023  14.639 -33.021  1.00 11.77           C  
ATOM    835  CG  LEU A 181      14.431  14.528 -33.636  1.00 10.12           C  
ATOM    836  CD1 LEU A 181      14.632  15.550 -34.734  1.00 15.83           C  
ATOM    837  CD2 LEU A 181      15.481  14.703 -32.570  1.00  7.94           C  
ATOM    838  N   GLY A 182      10.230  13.483 -31.787  1.00 10.23           N  
ATOM    839  CA  GLY A 182       9.030  13.731 -31.009  1.00  9.21           C  
ATOM    840  C   GLY A 182       9.031  12.945 -29.715  1.00 10.87           C  
ATOM    841  O   GLY A 182       8.688  13.472 -28.658  1.00  9.10           O  
ATOM    842  N   ASN A 183       9.442  11.676 -29.782  1.00  9.09           N  
ATOM    843  CA  ASN A 183       9.523  10.853 -28.571  1.00  9.17           C  
ATOM    844  C   ASN A 183      10.564  11.395 -27.594  1.00 12.85           C  
ATOM    845  O   ASN A 183      10.334  11.469 -26.368  1.00 13.26           O  
ATOM    846  CB  ASN A 183       9.845   9.410 -28.945  1.00 10.63           C  
ATOM    847  CG  ASN A 183       8.638   8.675 -29.482  1.00 13.11           C  
ATOM    848  OD1 ASN A 183       7.501   9.082 -29.251  1.00 15.98           O  
ATOM    849  ND2 ASN A 183       8.876   7.578 -30.191  1.00 13.71           N  
ATOM    850  N   ILE A 184      11.724  11.777 -28.123  1.00 10.23           N  
ATOM    851  CA  ILE A 184      12.768  12.334 -27.272  1.00 13.32           C  
ATOM    852  C   ILE A 184      12.271  13.604 -26.588  1.00 12.34           C  
ATOM    853  O   ILE A 184      12.374  13.758 -25.365  1.00 11.49           O  
ATOM    854  CB  ILE A 184      14.045  12.586 -28.095  1.00 14.55           C  
ATOM    855  CG1 ILE A 184      14.647  11.252 -28.528  1.00 13.24           C  
ATOM    856  CG2 ILE A 184      15.068  13.383 -27.285  1.00 13.65           C  
ATOM    857  CD1 ILE A 184      15.731  11.388 -29.570  1.00 15.18           C  
ATOM    858  N   ILE A 185      11.714  14.527 -27.368  1.00 12.61           N  
ATOM    859  CA  ILE A 185      11.207  15.774 -26.813  1.00 11.02           C  
ATOM    860  C   ILE A 185      10.121  15.488 -25.790  1.00 12.39           C  
ATOM    861  O   ILE A 185      10.015  16.173 -24.768  1.00 15.52           O  
ATOM    862  CB  ILE A 185      10.691  16.683 -27.942  1.00 11.60           C  
ATOM    863  CG1 ILE A 185      11.854  17.134 -28.817  1.00 11.61           C  
ATOM    864  CG2 ILE A 185       9.920  17.887 -27.368  1.00 12.40           C  
ATOM    865  CD1 ILE A 185      11.439  17.674 -30.173  1.00  9.02           C  
ATOM    866  N   GLY A 186       9.293  14.476 -26.047  1.00 13.36           N  
ATOM    867  CA  GLY A 186       8.214  14.161 -25.136  1.00 14.45           C  
ATOM    868  C   GLY A 186       8.675  13.634 -23.801  1.00 13.83           C  
ATOM    869  O   GLY A 186       7.898  13.663 -22.840  1.00 16.71           O  
ATOM    870  N   ASP A 187       9.915  13.142 -23.716  1.00 14.78           N  
ATOM    871  CA  ASP A 187      10.366  12.584 -22.442  1.00 10.20           C  
ATOM    872  C   ASP A 187      10.330  13.606 -21.306  1.00 16.41           C  
ATOM    873  O   ASP A 187      10.082  13.244 -20.150  1.00 20.62           O  
ATOM    874  CB  ASP A 187      11.768  12.019 -22.565  1.00 15.48           C  
ATOM    875  CG  ASP A 187      12.151  11.198 -21.351  1.00 15.86           C  
ATOM    876  OD1 ASP A 187      11.315  10.375 -20.924  1.00 17.99           O  
ATOM    877  OD2 ASP A 187      13.270  11.362 -20.827  1.00 28.89           O  
ATOM    878  N   GLY A 188      10.610  14.874 -21.590  1.00 21.22           N  
ATOM    879  CA  GLY A 188      10.626  15.864 -20.536  1.00 19.06           C  
ATOM    880  C   GLY A 188      11.310  17.168 -20.902  1.00 19.31           C  
ATOM    881  O   GLY A 188      11.911  17.311 -21.971  1.00 22.18           O  
ATOM    882  N   PRO A 189      11.250  18.145 -19.991  1.00 18.38           N  
ATOM    883  CA  PRO A 189      11.734  19.494 -20.338  1.00 21.34           C  
ATOM    884  C   PRO A 189      13.234  19.582 -20.557  1.00 20.17           C  
ATOM    885  O   PRO A 189      13.677  20.391 -21.380  1.00 17.58           O  
ATOM    886  CB  PRO A 189      11.291  20.347 -19.142  1.00 23.44           C  
ATOM    887  CG  PRO A 189      11.161  19.370 -18.006  1.00 24.01           C  
ATOM    888  CD  PRO A 189      10.684  18.087 -18.634  1.00 16.85           C  
ATOM    889  N   GLN A 190      14.038  18.787 -19.852  1.00 20.38           N  
ATOM    890  CA  GLN A 190      15.482  18.856 -20.067  1.00 20.53           C  
ATOM    891  C   GLN A 190      15.875  18.258 -21.415  1.00 20.75           C  
ATOM    892  O   GLN A 190      16.696  18.839 -22.137  1.00 24.73           O  
ATOM    893  CB  GLN A 190      16.222  18.164 -18.918  1.00 23.08           C  
ATOM    894  CG  GLN A 190      16.653  19.135 -17.810  1.00 22.21           C  
ATOM    895  CD  GLN A 190      15.475  19.761 -17.068  1.00 29.42           C  
ATOM    896  OE1 GLN A 190      14.589  19.062 -16.579  1.00 32.83           O  
ATOM    897  NE2 GLN A 190      15.468  21.083 -16.982  1.00 31.27           N  
ATOM    898  N   CYS A 191      15.304  17.104 -21.778  1.00 20.27           N  
ATOM    899  CA  CYS A 191      15.488  16.579 -23.132  1.00 21.52           C  
ATOM    900  C   CYS A 191      15.025  17.588 -24.172  1.00 17.50           C  
ATOM    901  O   CYS A 191      15.722  17.854 -25.160  1.00 20.28           O  
ATOM    902  CB  CYS A 191      14.702  15.288 -23.316  1.00 25.82           C  
ATOM    903  SG  CYS A 191      15.501  13.807 -22.845  1.00 39.80           S  
ATOM    904  N   ARG A 192      13.811  18.111 -23.992  1.00 15.10           N  
ATOM    905  CA  ARG A 192      13.278  19.113 -24.904  1.00 17.98           C  
ATOM    906  C   ARG A 192      14.282  20.233 -25.094  1.00 15.17           C  
ATOM    907  O   ARG A 192      14.584  20.618 -26.223  1.00 14.05           O  
ATOM    908  CB  ARG A 192      11.947  19.652 -24.363  1.00 19.33           C  
ATOM    909  CG  ARG A 192      11.382  20.862 -25.103  1.00 18.43           C  
ATOM    910  CD  ARG A 192      10.438  21.641 -24.206  1.00 18.18           C  
ATOM    911  NE  ARG A 192      11.170  22.292 -23.129  1.00 19.93           N  
ATOM    912  CZ  ARG A 192      10.629  22.716 -21.994  1.00 18.81           C  
ATOM    913  NH1 ARG A 192       9.338  22.557 -21.765  1.00 17.09           N  
ATOM    914  NH2 ARG A 192      11.392  23.292 -21.075  1.00 23.98           N  
ATOM    915  N   ASP A 193      14.829  20.748 -23.991  1.00 20.65           N  
ATOM    916  CA  ASP A 193      15.714  21.904 -24.067  1.00 15.89           C  
ATOM    917  C   ASP A 193      17.047  21.546 -24.704  1.00 14.22           C  
ATOM    918  O   ASP A 193      17.643  22.386 -25.384  1.00 14.05           O  
ATOM    919  CB  ASP A 193      15.930  22.498 -22.674  1.00 20.58           C  
ATOM    920  CG  ASP A 193      14.694  23.227 -22.149  1.00 23.50           C  
ATOM    921  OD1 ASP A 193      13.840  23.632 -22.972  1.00 24.33           O  
ATOM    922  OD2 ASP A 193      14.573  23.399 -20.916  1.00 28.89           O  
ATOM    923  N   TYR A 194      17.531  20.316 -24.514  1.00 15.86           N  
ATOM    924  CA  TYR A 194      18.682  19.871 -25.296  1.00 11.95           C  
ATOM    925  C   TYR A 194      18.367  19.939 -26.787  1.00 15.21           C  
ATOM    926  O   TYR A 194      19.106  20.555 -27.564  1.00 13.59           O  
ATOM    927  CB  TYR A 194      19.113  18.456 -24.892  1.00 12.80           C  
ATOM    928  CG  TYR A 194      20.319  17.951 -25.690  1.00 10.98           C  
ATOM    929  CD1 TYR A 194      21.468  18.725 -25.815  1.00 13.92           C  
ATOM    930  CD2 TYR A 194      20.297  16.717 -26.326  1.00 13.69           C  
ATOM    931  CE1 TYR A 194      22.565  18.282 -26.536  1.00 16.47           C  
ATOM    932  CE2 TYR A 194      21.386  16.263 -27.067  1.00 12.32           C  
ATOM    933  CZ  TYR A 194      22.525  17.052 -27.162  1.00 15.28           C  
ATOM    934  OH  TYR A 194      23.628  16.633 -27.888  1.00  9.73           O  
ATOM    935  N   VAL A 195      17.245  19.344 -27.200  1.00 12.48           N  
ATOM    936  CA  VAL A 195      16.913  19.311 -28.624  1.00 12.22           C  
ATOM    937  C   VAL A 195      16.711  20.727 -29.169  1.00  9.99           C  
ATOM    938  O   VAL A 195      17.150  21.052 -30.280  1.00 11.99           O  
ATOM    939  CB  VAL A 195      15.680  18.420 -28.862  1.00  9.32           C  
ATOM    940  CG1 VAL A 195      15.379  18.307 -30.344  1.00  7.68           C  
ATOM    941  CG2 VAL A 195      15.908  17.032 -28.270  1.00 11.01           C  
ATOM    942  N   ILE A 196      16.056  21.591 -28.395  1.00 11.93           N  
ATOM    943  CA  ILE A 196      15.843  22.978 -28.806  1.00 14.16           C  
ATOM    944  C   ILE A 196      17.177  23.689 -28.985  1.00 11.17           C  
ATOM    945  O   ILE A 196      17.404  24.380 -29.981  1.00 14.80           O  
ATOM    946  CB  ILE A 196      14.959  23.714 -27.781  1.00 17.38           C  
ATOM    947  CG1 ILE A 196      13.514  23.236 -27.890  1.00 14.31           C  
ATOM    948  CG2 ILE A 196      15.064  25.249 -27.975  1.00 15.35           C  
ATOM    949  CD1 ILE A 196      12.605  23.789 -26.825  1.00 12.33           C  
ATOM    950  N   SER A 197      18.073  23.549 -28.004  1.00 13.82           N  
ATOM    951  CA  SER A 197      19.356  24.239 -28.057  1.00 10.46           C  
ATOM    952  C   SER A 197      20.148  23.876 -29.305  1.00 11.64           C  
ATOM    953  O   SER A 197      20.981  24.665 -29.754  1.00 21.99           O  
ATOM    954  CB  SER A 197      20.174  23.916 -26.800  1.00 19.05           C  
ATOM    955  OG  SER A 197      20.746  22.611 -26.865  1.00 18.16           O  
ATOM    956  N   LEU A 198      19.919  22.688 -29.870  1.00 20.39           N  
ATOM    957  CA  LEU A 198      20.606  22.283 -31.088  1.00 15.36           C  
ATOM    958  C   LEU A 198      19.889  22.732 -32.355  1.00 17.46           C  
ATOM    959  O   LEU A 198      20.422  22.527 -33.452  1.00 19.31           O  
ATOM    960  CB  LEU A 198      20.786  20.759 -31.119  1.00 11.70           C  
ATOM    961  CG  LEU A 198      21.655  20.103 -30.033  1.00 17.36           C  
ATOM    962  CD1 LEU A 198      21.821  18.612 -30.304  1.00 12.87           C  
ATOM    963  CD2 LEU A 198      23.028  20.763 -29.929  1.00 19.82           C  
ATOM    964  N   GLY A 199      18.697  23.318 -32.239  1.00 19.11           N  
ATOM    965  CA  GLY A 199      18.048  23.938 -33.379  1.00 21.05           C  
ATOM    966  C   GLY A 199      17.077  23.043 -34.118  1.00 12.68           C  
ATOM    967  O   GLY A 199      17.241  22.793 -35.312  1.00 27.32           O  
ATOM    968  N   VAL A 200      16.037  22.581 -33.437  1.00 15.02           N  
ATOM    969  CA  VAL A 200      15.083  21.674 -34.062  1.00 15.29           C  
ATOM    970  C   VAL A 200      13.884  22.437 -34.604  1.00  9.93           C  
ATOM    971  O   VAL A 200      13.247  22.001 -35.568  1.00 18.34           O  
ATOM    972  CB  VAL A 200      14.635  20.593 -33.069  1.00 16.00           C  
ATOM    973  CG1 VAL A 200      13.879  21.217 -31.923  1.00 14.18           C  
ATOM    974  CG2 VAL A 200      13.790  19.546 -33.768  1.00 12.70           C  
ATOM    975  N   VAL A 201      13.565  23.577 -33.996  1.00 11.16           N  
ATOM    976  CA  VAL A 201      12.273  24.202 -34.245  1.00 15.77           C  
ATOM    977  C   VAL A 201      12.164  24.669 -35.692  1.00 18.16           C  
ATOM    978  O   VAL A 201      11.194  24.348 -36.386  1.00 16.27           O  
ATOM    979  CB  VAL A 201      12.036  25.355 -33.256  1.00 22.35           C  
ATOM    980  CG1 VAL A 201      10.704  26.040 -33.528  1.00 21.23           C  
ATOM    981  CG2 VAL A 201      12.068  24.826 -31.840  1.00 19.77           C  
ATOM    982  N   LYS A 202      13.127  25.461 -36.159  1.00 18.10           N  
ATOM    983  CA  LYS A 202      13.003  26.017 -37.506  1.00 22.53           C  
ATOM    984  C   LYS A 202      12.951  24.936 -38.570  1.00 20.20           C  
ATOM    985  O   LYS A 202      12.099  25.026 -39.474  1.00 21.27           O  
ATOM    986  CB  LYS A 202      14.147  26.993 -37.785  1.00 27.13           C  
ATOM    987  CG  LYS A 202      14.022  28.327 -37.072  1.00 36.80           C  
ATOM    988  CD  LYS A 202      14.661  29.445 -37.899  1.00 51.19           C  
ATOM    989  CE  LYS A 202      14.862  30.711 -37.089  1.00 43.87           C  
ATOM    990  NZ  LYS A 202      15.734  30.491 -35.899  1.00 59.13           N  
ATOM    991  N   PRO A 203      13.823  23.928 -38.561  1.00 17.87           N  
ATOM    992  CA  PRO A 203      13.649  22.828 -39.518  1.00 15.79           C  
ATOM    993  C   PRO A 203      12.309  22.133 -39.389  1.00 19.05           C  
ATOM    994  O   PRO A 203      11.672  21.840 -40.407  1.00 14.39           O  
ATOM    995  CB  PRO A 203      14.815  21.887 -39.190  1.00 22.14           C  
ATOM    996  CG  PRO A 203      15.437  22.407 -37.932  1.00 19.18           C  
ATOM    997  CD  PRO A 203      15.112  23.847 -37.858  1.00 19.99           C  
ATOM    998  N   LEU A 204      11.857  21.860 -38.165  1.00 16.43           N  
ATOM    999  CA  LEU A 204      10.566  21.206 -37.987  1.00 19.85           C  
ATOM   1000  C   LEU A 204       9.466  22.004 -38.671  1.00 19.38           C  
ATOM   1001  O   LEU A 204       8.691  21.467 -39.474  1.00 15.56           O  
ATOM   1002  CB  LEU A 204      10.282  21.048 -36.494  1.00 19.86           C  
ATOM   1003  CG  LEU A 204       8.930  20.471 -36.096  1.00 19.40           C  
ATOM   1004  CD1 LEU A 204       8.813  19.019 -36.541  1.00 18.50           C  
ATOM   1005  CD2 LEU A 204       8.734  20.592 -34.602  1.00 15.64           C  
ATOM   1006  N   LEU A 205       9.417  23.307 -38.394  1.00 12.76           N  
ATOM   1007  CA  LEU A 205       8.359  24.150 -38.930  1.00 20.55           C  
ATOM   1008  C   LEU A 205       8.481  24.319 -40.434  1.00 20.03           C  
ATOM   1009  O   LEU A 205       7.474  24.552 -41.109  1.00 19.47           O  
ATOM   1010  CB  LEU A 205       8.379  25.513 -38.239  1.00 12.92           C  
ATOM   1011  CG  LEU A 205       8.100  25.536 -36.739  1.00 12.63           C  
ATOM   1012  CD1 LEU A 205       7.893  26.979 -36.284  1.00 23.28           C  
ATOM   1013  CD2 LEU A 205       6.909  24.672 -36.332  1.00 15.68           C  
ATOM   1014  N   SER A 206       9.690  24.174 -40.978  1.00 19.49           N  
ATOM   1015  CA  SER A 206       9.886  24.351 -42.412  1.00 18.93           C  
ATOM   1016  C   SER A 206       9.134  23.319 -43.242  1.00 23.81           C  
ATOM   1017  O   SER A 206       8.967  23.517 -44.451  1.00 25.60           O  
ATOM   1018  CB  SER A 206      11.385  24.285 -42.748  1.00 21.99           C  
ATOM   1019  OG  SER A 206      11.886  22.949 -42.733  1.00 22.33           O  
ATOM   1020  N   PHE A 207       8.695  22.214 -42.639  1.00 27.44           N  
ATOM   1021  CA  PHE A 207       7.981  21.201 -43.406  1.00 22.61           C  
ATOM   1022  C   PHE A 207       6.538  21.594 -43.674  1.00 20.19           C  
ATOM   1023  O   PHE A 207       5.887  20.967 -44.513  1.00 29.06           O  
ATOM   1024  CB  PHE A 207       8.010  19.859 -42.676  1.00 21.57           C  
ATOM   1025  CG  PHE A 207       9.394  19.323 -42.459  1.00 23.59           C  
ATOM   1026  CD1 PHE A 207      10.224  19.082 -43.536  1.00 27.28           C  
ATOM   1027  CD2 PHE A 207       9.864  19.063 -41.185  1.00 17.62           C  
ATOM   1028  CE1 PHE A 207      11.504  18.605 -43.344  1.00 31.53           C  
ATOM   1029  CE2 PHE A 207      11.139  18.570 -40.989  1.00 21.47           C  
ATOM   1030  CZ  PHE A 207      11.961  18.343 -42.066  1.00 21.66           C  
ATOM   1031  N   ILE A 208       6.031  22.611 -42.985  1.00 21.09           N  
ATOM   1032  CA  ILE A 208       4.631  23.012 -43.092  1.00 25.91           C  
ATOM   1033  C   ILE A 208       4.477  23.787 -44.398  1.00 29.47           C  
ATOM   1034  O   ILE A 208       4.812  24.970 -44.474  1.00 28.66           O  
ATOM   1035  CB  ILE A 208       4.181  23.834 -41.884  1.00 15.50           C  
ATOM   1036  CG1 ILE A 208       4.307  22.984 -40.620  1.00 14.48           C  
ATOM   1037  CG2 ILE A 208       2.736  24.310 -42.069  1.00 26.83           C  
ATOM   1038  CD1 ILE A 208       4.136  23.744 -39.367  1.00 20.21           C  
ATOM   1039  N   SER A 209       3.962  23.119 -45.421  1.00 31.60           N  
ATOM   1040  CA  SER A 209       3.723  23.732 -46.719  1.00 24.87           C  
ATOM   1041  C   SER A 209       2.596  22.974 -47.397  1.00 27.18           C  
ATOM   1042  O   SER A 209       2.250  21.859 -46.986  1.00 21.85           O  
ATOM   1043  CB  SER A 209       4.976  23.698 -47.595  1.00 21.41           C  
ATOM   1044  OG  SER A 209       5.076  22.439 -48.234  1.00 36.15           O  
ATOM   1045  N   PRO A 210       2.020  23.537 -48.467  1.00 31.50           N  
ATOM   1046  CA  PRO A 210       0.816  22.924 -49.059  1.00 29.68           C  
ATOM   1047  C   PRO A 210       1.011  21.483 -49.481  1.00 29.11           C  
ATOM   1048  O   PRO A 210       0.052  20.703 -49.462  1.00 25.45           O  
ATOM   1049  CB  PRO A 210       0.522  23.832 -50.263  1.00 31.98           C  
ATOM   1050  CG  PRO A 210       1.126  25.151 -49.898  1.00 28.09           C  
ATOM   1051  CD  PRO A 210       2.362  24.817 -49.110  1.00 33.06           C  
ATOM   1052  N   SER A 211       2.224  21.093 -49.840  1.00 27.24           N  
ATOM   1053  CA  SER A 211       2.448  19.762 -50.378  1.00 24.37           C  
ATOM   1054  C   SER A 211       2.759  18.722 -49.309  1.00 28.06           C  
ATOM   1055  O   SER A 211       2.828  17.532 -49.631  1.00 26.76           O  
ATOM   1056  CB  SER A 211       3.588  19.803 -51.402  1.00 30.08           C  
ATOM   1057  OG  SER A 211       4.767  20.330 -50.818  1.00 47.93           O  
ATOM   1058  N   ILE A 212       2.931  19.124 -48.052  1.00 27.64           N  
ATOM   1059  CA  ILE A 212       3.306  18.139 -47.034  1.00 25.90           C  
ATOM   1060  C   ILE A 212       2.224  17.069 -46.953  1.00 15.99           C  
ATOM   1061  O   ILE A 212       1.028  17.403 -46.895  1.00 20.86           O  
ATOM   1062  CB  ILE A 212       3.513  18.816 -45.668  1.00 26.10           C  
ATOM   1063  CG1 ILE A 212       4.167  17.825 -44.703  1.00 22.24           C  
ATOM   1064  CG2 ILE A 212       2.181  19.355 -45.104  1.00 23.57           C  
ATOM   1065  CD1 ILE A 212       4.278  18.329 -43.261  1.00 24.25           C  
ATOM   1066  N   PRO A 213       2.565  15.783 -46.943  1.00 20.67           N  
ATOM   1067  CA  PRO A 213       1.535  14.753 -46.732  1.00 21.93           C  
ATOM   1068  C   PRO A 213       0.869  14.900 -45.374  1.00 21.12           C  
ATOM   1069  O   PRO A 213       1.483  15.324 -44.394  1.00 15.64           O  
ATOM   1070  CB  PRO A 213       2.311  13.435 -46.829  1.00 27.49           C  
ATOM   1071  CG  PRO A 213       3.578  13.773 -47.558  1.00 24.86           C  
ATOM   1072  CD  PRO A 213       3.885  15.204 -47.238  1.00 22.84           C  
ATOM   1073  N   ILE A 214      -0.401  14.504 -45.315  1.00 20.20           N  
ATOM   1074  CA  ILE A 214      -1.203  14.768 -44.124  1.00 19.96           C  
ATOM   1075  C   ILE A 214      -0.678  13.974 -42.928  1.00 18.01           C  
ATOM   1076  O   ILE A 214      -0.697  14.457 -41.790  1.00 17.46           O  
ATOM   1077  CB  ILE A 214      -2.689  14.472 -44.416  1.00 20.65           C  
ATOM   1078  CG1 ILE A 214      -3.556  15.012 -43.297  1.00 21.06           C  
ATOM   1079  CG2 ILE A 214      -2.923  12.979 -44.611  1.00 31.71           C  
ATOM   1080  CD1 ILE A 214      -3.668  16.532 -43.324  1.00 28.83           C  
ATOM   1081  N   THR A 215      -0.179  12.759 -43.162  1.00 17.33           N  
ATOM   1082  CA  THR A 215       0.365  11.958 -42.067  1.00 17.57           C  
ATOM   1083  C   THR A 215       1.595  12.627 -41.465  1.00 13.12           C  
ATOM   1084  O   THR A 215       1.759  12.693 -40.234  1.00 18.27           O  
ATOM   1085  CB  THR A 215       0.733  10.564 -42.566  1.00 21.06           C  
ATOM   1086  OG1 THR A 215       1.787  10.672 -43.529  1.00 33.87           O  
ATOM   1087  CG2 THR A 215      -0.443   9.884 -43.210  1.00 21.65           C  
ATOM   1088  N   PHE A 216       2.478  13.124 -42.330  1.00 17.38           N  
ATOM   1089  CA  PHE A 216       3.655  13.840 -41.860  1.00 18.24           C  
ATOM   1090  C   PHE A 216       3.244  15.079 -41.080  1.00 12.22           C  
ATOM   1091  O   PHE A 216       3.818  15.373 -40.027  1.00 12.53           O  
ATOM   1092  CB  PHE A 216       4.546  14.206 -43.058  1.00 17.75           C  
ATOM   1093  CG  PHE A 216       5.918  14.733 -42.689  1.00 16.77           C  
ATOM   1094  CD1 PHE A 216       6.381  14.718 -41.383  1.00 13.46           C  
ATOM   1095  CD2 PHE A 216       6.742  15.253 -43.665  1.00 23.49           C  
ATOM   1096  CE1 PHE A 216       7.637  15.203 -41.071  1.00 16.60           C  
ATOM   1097  CE2 PHE A 216       7.996  15.743 -43.352  1.00 20.94           C  
ATOM   1098  CZ  PHE A 216       8.440  15.719 -42.054  1.00 15.39           C  
ATOM   1099  N   LEU A 217       2.256  15.821 -41.583  1.00 15.51           N  
ATOM   1100  CA  LEU A 217       1.830  17.032 -40.898  1.00 14.55           C  
ATOM   1101  C   LEU A 217       1.267  16.712 -39.518  1.00 14.52           C  
ATOM   1102  O   LEU A 217       1.481  17.462 -38.561  1.00 14.98           O  
ATOM   1103  CB  LEU A 217       0.799  17.776 -41.750  1.00 13.00           C  
ATOM   1104  CG  LEU A 217       0.393  19.168 -41.250  1.00 11.45           C  
ATOM   1105  CD1 LEU A 217       1.594  20.059 -40.988  1.00 18.75           C  
ATOM   1106  CD2 LEU A 217      -0.516  19.834 -42.242  1.00 18.68           C  
ATOM   1107  N   ARG A 218       0.555  15.594 -39.390  1.00 15.30           N  
ATOM   1108  CA  ARG A 218       0.079  15.181 -38.074  1.00 18.61           C  
ATOM   1109  C   ARG A 218       1.244  14.920 -37.134  1.00 13.92           C  
ATOM   1110  O   ARG A 218       1.194  15.280 -35.951  1.00 12.32           O  
ATOM   1111  CB  ARG A 218      -0.786  13.926 -38.191  1.00 22.25           C  
ATOM   1112  CG  ARG A 218      -2.150  14.160 -38.778  1.00 17.43           C  
ATOM   1113  CD  ARG A 218      -2.834  12.845 -39.084  1.00 23.12           C  
ATOM   1114  NE  ARG A 218      -4.132  13.051 -39.719  1.00 18.34           N  
ATOM   1115  CZ  ARG A 218      -4.699  12.198 -40.564  1.00 27.04           C  
ATOM   1116  NH1 ARG A 218      -4.084  11.064 -40.880  1.00 29.36           N  
ATOM   1117  NH2 ARG A 218      -5.882  12.486 -41.101  1.00 21.42           N  
ATOM   1118  N   ASN A 219       2.310  14.297 -37.640  1.00 12.23           N  
ATOM   1119  CA  ASN A 219       3.470  14.088 -36.776  1.00 12.06           C  
ATOM   1120  C   ASN A 219       4.123  15.414 -36.386  1.00 13.29           C  
ATOM   1121  O   ASN A 219       4.503  15.607 -35.226  1.00 10.17           O  
ATOM   1122  CB  ASN A 219       4.475  13.155 -37.450  1.00 22.39           C  
ATOM   1123  CG  ASN A 219       4.198  11.691 -37.156  1.00 27.11           C  
ATOM   1124  OD1 ASN A 219       4.189  10.856 -38.061  1.00 38.80           O  
ATOM   1125  ND2 ASN A 219       3.969  11.376 -35.892  1.00 26.46           N  
ATOM   1126  N   VAL A 220       4.260  16.337 -37.338  1.00 11.28           N  
ATOM   1127  CA  VAL A 220       4.842  17.649 -37.048  1.00 10.65           C  
ATOM   1128  C   VAL A 220       4.050  18.365 -35.959  1.00 11.75           C  
ATOM   1129  O   VAL A 220       4.622  18.986 -35.047  1.00 11.70           O  
ATOM   1130  CB  VAL A 220       4.907  18.502 -38.330  1.00 12.13           C  
ATOM   1131  CG1 VAL A 220       5.352  19.913 -38.004  1.00 16.61           C  
ATOM   1132  CG2 VAL A 220       5.829  17.883 -39.332  1.00 10.01           C  
ATOM   1133  N   THR A 221       2.723  18.302 -36.041  1.00 10.57           N  
ATOM   1134  CA  THR A 221       1.901  19.021 -35.078  1.00  8.41           C  
ATOM   1135  C   THR A 221       1.979  18.365 -33.706  1.00  9.03           C  
ATOM   1136  O   THR A 221       2.000  19.057 -32.680  1.00  5.61           O  
ATOM   1137  CB  THR A 221       0.455  19.091 -35.576  1.00 10.30           C  
ATOM   1138  OG1 THR A 221      -0.082  17.767 -35.704  1.00 37.78           O  
ATOM   1139  CG2 THR A 221       0.410  19.736 -36.905  1.00 10.45           C  
ATOM   1140  N   TRP A 222       2.047  17.032 -33.668  1.00 10.20           N  
ATOM   1141  CA  TRP A 222       2.266  16.346 -32.399  1.00  9.94           C  
ATOM   1142  C   TRP A 222       3.613  16.734 -31.788  1.00 10.34           C  
ATOM   1143  O   TRP A 222       3.723  16.949 -30.572  1.00 12.35           O  
ATOM   1144  CB  TRP A 222       2.157  14.835 -32.617  1.00 11.95           C  
ATOM   1145  CG  TRP A 222       2.732  13.991 -31.513  1.00 11.63           C  
ATOM   1146  CD1 TRP A 222       2.248  13.849 -30.248  1.00 11.93           C  
ATOM   1147  CD2 TRP A 222       3.900  13.167 -31.592  1.00 11.08           C  
ATOM   1148  NE1 TRP A 222       3.043  12.984 -29.530  1.00 13.08           N  
ATOM   1149  CE2 TRP A 222       4.069  12.558 -30.334  1.00 13.74           C  
ATOM   1150  CE3 TRP A 222       4.824  12.893 -32.602  1.00 10.85           C  
ATOM   1151  CZ2 TRP A 222       5.123  11.692 -30.063  1.00 14.79           C  
ATOM   1152  CZ3 TRP A 222       5.862  12.032 -32.331  1.00  9.71           C  
ATOM   1153  CH2 TRP A 222       6.005  11.440 -31.074  1.00  8.29           C  
ATOM   1154  N   VAL A 223       4.656  16.834 -32.610  1.00  9.34           N  
ATOM   1155  CA  VAL A 223       5.943  17.270 -32.078  1.00  8.77           C  
ATOM   1156  C   VAL A 223       5.827  18.679 -31.499  1.00  7.41           C  
ATOM   1157  O   VAL A 223       6.428  18.992 -30.464  1.00  9.24           O  
ATOM   1158  CB  VAL A 223       7.032  17.179 -33.163  1.00  7.64           C  
ATOM   1159  CG1 VAL A 223       8.329  17.801 -32.678  1.00 12.55           C  
ATOM   1160  CG2 VAL A 223       7.268  15.733 -33.547  1.00  7.89           C  
ATOM   1161  N   MET A 224       5.055  19.554 -32.153  1.00  7.76           N  
ATOM   1162  CA  MET A 224       4.822  20.891 -31.593  1.00  9.73           C  
ATOM   1163  C   MET A 224       4.114  20.828 -30.240  1.00 10.61           C  
ATOM   1164  O   MET A 224       4.431  21.593 -29.313  1.00 13.58           O  
ATOM   1165  CB  MET A 224       4.015  21.723 -32.579  1.00 11.51           C  
ATOM   1166  CG  MET A 224       4.774  21.985 -33.852  1.00 14.66           C  
ATOM   1167  SD  MET A 224       3.752  22.655 -35.163  1.00 18.04           S  
ATOM   1168  CE  MET A 224       3.441  24.291 -34.520  1.00 22.40           C  
ATOM   1169  N   VAL A 225       3.138  19.934 -30.109  1.00  8.99           N  
ATOM   1170  CA  VAL A 225       2.546  19.690 -28.796  1.00  9.11           C  
ATOM   1171  C   VAL A 225       3.639  19.385 -27.780  1.00  9.44           C  
ATOM   1172  O   VAL A 225       3.675  19.953 -26.683  1.00 10.36           O  
ATOM   1173  CB  VAL A 225       1.526  18.540 -28.866  1.00  9.92           C  
ATOM   1174  CG1 VAL A 225       1.070  18.163 -27.456  1.00 13.32           C  
ATOM   1175  CG2 VAL A 225       0.346  18.922 -29.716  1.00  9.53           C  
ATOM   1176  N   ASN A 226       4.530  18.452 -28.123  1.00 13.40           N  
ATOM   1177  CA  ASN A 226       5.563  18.047 -27.174  1.00  9.85           C  
ATOM   1178  C   ASN A 226       6.522  19.190 -26.868  1.00 10.65           C  
ATOM   1179  O   ASN A 226       7.034  19.290 -25.751  1.00 11.39           O  
ATOM   1180  CB  ASN A 226       6.311  16.826 -27.702  1.00 11.55           C  
ATOM   1181  CG  ASN A 226       5.576  15.531 -27.397  1.00 19.76           C  
ATOM   1182  OD1 ASN A 226       4.591  15.533 -26.657  1.00 11.10           O  
ATOM   1183  ND2 ASN A 226       6.048  14.425 -27.958  1.00 12.69           N  
ATOM   1184  N   LEU A 227       6.766  20.067 -27.834  1.00 11.77           N  
ATOM   1185  CA  LEU A 227       7.599  21.234 -27.580  1.00  8.12           C  
ATOM   1186  C   LEU A 227       6.928  22.231 -26.643  1.00 19.30           C  
ATOM   1187  O   LEU A 227       7.634  22.990 -25.970  1.00 16.13           O  
ATOM   1188  CB  LEU A 227       7.948  21.929 -28.895  1.00  9.06           C  
ATOM   1189  CG  LEU A 227       9.001  21.237 -29.752  1.00 14.34           C  
ATOM   1190  CD1 LEU A 227       8.932  21.754 -31.182  1.00 17.09           C  
ATOM   1191  CD2 LEU A 227      10.395  21.446 -29.183  1.00 11.02           C  
ATOM   1192  N   CYS A 228       5.590  22.247 -26.573  1.00 15.61           N  
ATOM   1193  CA  CYS A 228       4.894  23.241 -25.756  1.00  9.92           C  
ATOM   1194  C   CYS A 228       4.528  22.789 -24.341  1.00 12.67           C  
ATOM   1195  O   CYS A 228       4.253  23.651 -23.503  1.00 18.53           O  
ATOM   1196  CB  CYS A 228       3.601  23.679 -26.450  1.00 11.75           C  
ATOM   1197  SG  CYS A 228       3.837  24.568 -28.006  1.00 16.06           S  
ATOM   1198  N   ARG A 229       4.515  21.487 -24.043  1.00  9.83           N  
ATOM   1199  CA  ARG A 229       3.697  20.972 -22.944  1.00 13.44           C  
ATOM   1200  C   ARG A 229       4.358  20.922 -21.567  1.00 18.23           C  
ATOM   1201  O   ARG A 229       3.637  20.932 -20.557  1.00 20.51           O  
ATOM   1202  CB  ARG A 229       3.206  19.559 -23.275  1.00 21.18           C  
ATOM   1203  CG  ARG A 229       4.279  18.483 -23.252  1.00 21.66           C  
ATOM   1204  CD  ARG A 229       3.789  17.232 -23.976  1.00 19.91           C  
ATOM   1205  NE  ARG A 229       2.545  16.714 -23.434  1.00 20.36           N  
ATOM   1206  CZ  ARG A 229       1.773  15.824 -24.053  1.00 18.91           C  
ATOM   1207  NH1 ARG A 229       0.650  15.419 -23.477  1.00 19.49           N  
ATOM   1208  NH2 ARG A 229       2.114  15.345 -25.245  1.00 17.29           N  
ATOM   1209  N   HIS A 230       5.677  20.813 -21.461  1.00 19.73           N  
ATOM   1210  CA  HIS A 230       6.286  20.630 -20.144  1.00 20.21           C  
ATOM   1211  C   HIS A 230       6.552  21.973 -19.471  1.00 16.33           C  
ATOM   1212  O   HIS A 230       6.874  22.960 -20.131  1.00 19.33           O  
ATOM   1213  CB  HIS A 230       7.583  19.845 -20.263  1.00 21.54           C  
ATOM   1214  CG  HIS A 230       7.392  18.459 -20.791  1.00 24.00           C  
ATOM   1215  ND1 HIS A 230       6.693  17.492 -20.098  1.00 31.35           N  
ATOM   1216  CD2 HIS A 230       7.818  17.873 -21.935  1.00 25.18           C  
ATOM   1217  CE1 HIS A 230       6.686  16.372 -20.798  1.00 24.56           C  
ATOM   1218  NE2 HIS A 230       7.362  16.576 -21.917  1.00 36.50           N  
ATOM   1219  N   LYS A 231       6.430  21.999 -18.138  1.00 26.47           N  
ATOM   1220  CA  LYS A 231       6.372  23.258 -17.394  1.00 32.13           C  
ATOM   1221  C   LYS A 231       7.495  23.478 -16.385  1.00 40.57           C  
ATOM   1222  O   LYS A 231       7.453  24.483 -15.661  1.00 49.76           O  
ATOM   1223  CB  LYS A 231       5.038  23.367 -16.650  1.00 29.53           C  
ATOM   1224  CG  LYS A 231       3.901  23.873 -17.510  1.00 34.62           C  
ATOM   1225  CD  LYS A 231       2.543  23.496 -16.933  1.00 41.92           C  
ATOM   1226  CE  LYS A 231       2.368  23.984 -15.510  1.00 46.13           C  
ATOM   1227  NZ  LYS A 231       1.174  24.856 -15.374  1.00 42.50           N  
ATOM   1228  N   ASP A 232       8.497  22.605 -16.305  1.00 28.56           N  
ATOM   1229  CA  ASP A 232       9.490  22.674 -15.230  1.00 33.17           C  
ATOM   1230  C   ASP A 232      10.905  22.504 -15.775  1.00 20.28           C  
ATOM   1231  O   ASP A 232      11.574  21.506 -15.496  1.00 29.20           O  
ATOM   1232  CB  ASP A 232       9.179  21.617 -14.170  1.00 43.76           C  
ATOM   1233  CG  ASP A 232       9.383  22.128 -12.761  1.00 55.39           C  
ATOM   1234  OD1 ASP A 232      10.515  22.542 -12.430  1.00 58.39           O  
ATOM   1235  OD2 ASP A 232       8.401  22.130 -11.989  1.00 61.85           O  
ATOM   1236  N   PRO A 233      11.412  23.491 -16.523  1.00 17.99           N  
ATOM   1237  CA  PRO A 233      10.794  24.777 -16.878  1.00 26.51           C  
ATOM   1238  C   PRO A 233       9.940  24.735 -18.146  1.00 24.73           C  
ATOM   1239  O   PRO A 233       9.953  23.732 -18.848  1.00 25.10           O  
ATOM   1240  CB  PRO A 233      12.006  25.680 -17.102  1.00 28.65           C  
ATOM   1241  CG  PRO A 233      13.027  24.749 -17.688  1.00 19.24           C  
ATOM   1242  CD  PRO A 233      12.809  23.415 -16.991  1.00 21.54           C  
ATOM   1243  N   PRO A 234       9.214  25.808 -18.441  1.00 29.83           N  
ATOM   1244  CA  PRO A 234       8.491  25.875 -19.714  1.00 26.61           C  
ATOM   1245  C   PRO A 234       9.453  26.141 -20.854  1.00 25.24           C  
ATOM   1246  O   PRO A 234      10.615  26.508 -20.617  1.00 22.19           O  
ATOM   1247  CB  PRO A 234       7.519  27.044 -19.513  1.00 32.06           C  
ATOM   1248  CG  PRO A 234       8.227  27.933 -18.509  1.00 29.93           C  
ATOM   1249  CD  PRO A 234       9.047  27.032 -17.639  1.00 26.33           C  
ATOM   1250  N   PRO A 235       9.019  25.944 -22.097  1.00 22.61           N  
ATOM   1251  CA  PRO A 235       9.922  26.148 -23.219  1.00 24.19           C  
ATOM   1252  C   PRO A 235      10.403  27.582 -23.271  1.00 21.67           C  
ATOM   1253  O   PRO A 235       9.691  28.513 -22.845  1.00 24.59           O  
ATOM   1254  CB  PRO A 235       9.055  25.798 -24.438  1.00 28.87           C  
ATOM   1255  CG  PRO A 235       7.653  25.914 -23.954  1.00 20.87           C  
ATOM   1256  CD  PRO A 235       7.689  25.509 -22.534  1.00 19.97           C  
ATOM   1257  N   PRO A 236      11.595  27.815 -23.811  1.00 28.14           N  
ATOM   1258  CA  PRO A 236      12.094  29.185 -23.950  1.00 22.94           C  
ATOM   1259  C   PRO A 236      11.129  30.084 -24.715  1.00 26.22           C  
ATOM   1260  O   PRO A 236      10.425  29.651 -25.633  1.00 21.56           O  
ATOM   1261  CB  PRO A 236      13.407  29.004 -24.716  1.00 27.26           C  
ATOM   1262  CG  PRO A 236      13.834  27.621 -24.438  1.00 25.01           C  
ATOM   1263  CD  PRO A 236      12.606  26.814 -24.191  1.00 28.43           C  
ATOM   1264  N   MET A 237      11.136  31.364 -24.344  1.00 17.88           N  
ATOM   1265  CA  MET A 237      10.281  32.349 -24.998  1.00 24.62           C  
ATOM   1266  C   MET A 237      10.530  32.410 -26.502  1.00 26.45           C  
ATOM   1267  O   MET A 237       9.585  32.547 -27.285  1.00 23.83           O  
ATOM   1268  CB  MET A 237      10.508  33.727 -24.372  1.00 30.62           C  
ATOM   1269  CG  MET A 237      10.113  33.823 -22.910  1.00 42.23           C  
ATOM   1270  SD  MET A 237       8.325  33.722 -22.648  1.00 58.29           S  
ATOM   1271  CE  MET A 237       8.244  34.080 -20.894  1.00 37.43           C  
ATOM   1272  N   GLU A 238      11.797  32.356 -26.925  1.00 21.28           N  
ATOM   1273  CA  GLU A 238      12.105  32.347 -28.356  1.00 32.97           C  
ATOM   1274  C   GLU A 238      11.403  31.197 -29.065  1.00 27.78           C  
ATOM   1275  O   GLU A 238      10.891  31.359 -30.179  1.00 29.35           O  
ATOM   1276  CB  GLU A 238      13.619  32.248 -28.586  1.00 38.15           C  
ATOM   1277  CG  GLU A 238      13.997  31.836 -30.026  1.00 55.14           C  
ATOM   1278  CD  GLU A 238      15.499  31.854 -30.301  1.00 63.46           C  
ATOM   1279  OE1 GLU A 238      16.214  30.966 -29.782  1.00 62.46           O  
ATOM   1280  OE2 GLU A 238      15.963  32.750 -31.044  1.00 67.79           O  
ATOM   1281  N   THR A 239      11.400  30.016 -28.445  1.00 26.76           N  
ATOM   1282  CA  THR A 239      10.742  28.861 -29.045  1.00 28.79           C  
ATOM   1283  C   THR A 239       9.243  29.084 -29.162  1.00 19.88           C  
ATOM   1284  O   THR A 239       8.639  28.749 -30.182  1.00 17.08           O  
ATOM   1285  CB  THR A 239      11.041  27.616 -28.217  1.00 23.41           C  
ATOM   1286  OG1 THR A 239      12.447  27.375 -28.265  1.00 23.53           O  
ATOM   1287  CG2 THR A 239      10.295  26.396 -28.755  1.00 19.29           C  
ATOM   1288  N   ILE A 240       8.627  29.640 -28.125  1.00 21.90           N  
ATOM   1289  CA  ILE A 240       7.209  29.968 -28.197  1.00 18.09           C  
ATOM   1290  C   ILE A 240       6.949  30.960 -29.320  1.00 18.98           C  
ATOM   1291  O   ILE A 240       5.962  30.841 -30.055  1.00 22.38           O  
ATOM   1292  CB  ILE A 240       6.732  30.507 -26.840  1.00 22.80           C  
ATOM   1293  CG1 ILE A 240       6.836  29.399 -25.789  1.00 20.67           C  
ATOM   1294  CG2 ILE A 240       5.307  31.043 -26.939  1.00 24.38           C  
ATOM   1295  CD1 ILE A 240       6.483  29.868 -24.366  1.00 39.30           C  
ATOM   1296  N   GLN A 241       7.824  31.957 -29.469  1.00 23.39           N  
ATOM   1297  CA  GLN A 241       7.648  32.958 -30.521  1.00 29.02           C  
ATOM   1298  C   GLN A 241       7.777  32.347 -31.909  1.00 22.53           C  
ATOM   1299  O   GLN A 241       7.127  32.806 -32.853  1.00 25.26           O  
ATOM   1300  CB  GLN A 241       8.667  34.088 -30.350  1.00 30.44           C  
ATOM   1301  CG  GLN A 241       8.339  35.060 -29.220  1.00 38.54           C  
ATOM   1302  CD  GLN A 241       9.484  36.012 -28.897  1.00 53.68           C  
ATOM   1303  OE1 GLN A 241      10.418  35.659 -28.170  1.00 49.60           O  
ATOM   1304  NE2 GLN A 241       9.416  37.226 -29.433  1.00 54.89           N  
ATOM   1305  N   GLU A 242       8.624  31.331 -32.055  1.00 23.24           N  
ATOM   1306  CA  GLU A 242       8.718  30.622 -33.328  1.00 23.75           C  
ATOM   1307  C   GLU A 242       7.499  29.731 -33.565  1.00 20.93           C  
ATOM   1308  O   GLU A 242       7.033  29.589 -34.700  1.00 15.23           O  
ATOM   1309  CB  GLU A 242      10.000  29.789 -33.356  1.00 22.53           C  
ATOM   1310  CG  GLU A 242      11.281  30.602 -33.592  1.00 38.69           C  
ATOM   1311  CD  GLU A 242      12.565  29.941 -33.043  1.00 54.32           C  
ATOM   1312  OE1 GLU A 242      12.489  28.859 -32.409  1.00 38.59           O  
ATOM   1313  OE2 GLU A 242      13.664  30.514 -33.242  1.00 56.07           O  
ATOM   1314  N   ILE A 243       6.961  29.132 -32.504  1.00 15.22           N  
ATOM   1315  CA  ILE A 243       5.911  28.133 -32.670  1.00 18.15           C  
ATOM   1316  C   ILE A 243       4.567  28.796 -32.917  1.00 16.84           C  
ATOM   1317  O   ILE A 243       3.750  28.287 -33.689  1.00 15.35           O  
ATOM   1318  CB  ILE A 243       5.851  27.210 -31.438  1.00 15.32           C  
ATOM   1319  CG1 ILE A 243       7.015  26.220 -31.456  1.00 18.42           C  
ATOM   1320  CG2 ILE A 243       4.506  26.454 -31.386  1.00 19.38           C  
ATOM   1321  CD1 ILE A 243       7.120  25.394 -30.189  1.00 23.04           C  
ATOM   1322  N   LEU A 244       4.307  29.920 -32.257  1.00 16.11           N  
ATOM   1323  CA  LEU A 244       2.967  30.494 -32.295  1.00 16.96           C  
ATOM   1324  C   LEU A 244       2.496  30.830 -33.703  1.00 18.83           C  
ATOM   1325  O   LEU A 244       1.324  30.554 -34.011  1.00 18.57           O  
ATOM   1326  CB  LEU A 244       2.919  31.735 -31.405  1.00 13.62           C  
ATOM   1327  CG  LEU A 244       2.270  31.562 -30.045  1.00 28.98           C  
ATOM   1328  CD1 LEU A 244       2.394  32.858 -29.251  1.00 24.01           C  
ATOM   1329  CD2 LEU A 244       0.801  31.160 -30.177  1.00 23.48           C  
ATOM   1330  N   PRO A 245       3.314  31.419 -34.581  1.00 16.80           N  
ATOM   1331  CA  PRO A 245       2.853  31.664 -35.962  1.00  8.48           C  
ATOM   1332  C   PRO A 245       2.457  30.396 -36.688  1.00 15.02           C  
ATOM   1333  O   PRO A 245       1.515  30.392 -37.495  1.00 19.92           O  
ATOM   1334  CB  PRO A 245       4.071  32.327 -36.616  1.00 15.00           C  
ATOM   1335  CG  PRO A 245       4.814  32.958 -35.514  1.00 16.84           C  
ATOM   1336  CD  PRO A 245       4.611  32.060 -34.304  1.00 21.74           C  
ATOM   1337  N   ALA A 246       3.160  29.300 -36.418  1.00 14.48           N  
ATOM   1338  CA  ALA A 246       2.772  28.031 -37.014  1.00 14.28           C  
ATOM   1339  C   ALA A 246       1.415  27.578 -36.490  1.00 12.07           C  
ATOM   1340  O   ALA A 246       0.614  27.008 -37.239  1.00 14.28           O  
ATOM   1341  CB  ALA A 246       3.842  26.972 -36.748  1.00 14.10           C  
ATOM   1342  N   LEU A 247       1.136  27.817 -35.206  1.00 11.04           N  
ATOM   1343  CA  LEU A 247      -0.162  27.437 -34.656  1.00 14.87           C  
ATOM   1344  C   LEU A 247      -1.274  28.305 -35.235  1.00 20.24           C  
ATOM   1345  O   LEU A 247      -2.394  27.825 -35.459  1.00 17.19           O  
ATOM   1346  CB  LEU A 247      -0.147  27.541 -33.129  1.00 16.23           C  
ATOM   1347  CG  LEU A 247       0.794  26.590 -32.378  1.00 18.93           C  
ATOM   1348  CD1 LEU A 247       0.823  26.936 -30.903  1.00 19.12           C  
ATOM   1349  CD2 LEU A 247       0.386  25.135 -32.563  1.00 15.89           C  
ATOM   1350  N   CYS A 248      -0.972  29.584 -35.488  1.00 16.45           N  
ATOM   1351  CA  CYS A 248      -1.918  30.467 -36.165  1.00 17.93           C  
ATOM   1352  C   CYS A 248      -2.209  29.988 -37.574  1.00 13.81           C  
ATOM   1353  O   CYS A 248      -3.324  30.167 -38.078  1.00 21.94           O  
ATOM   1354  CB  CYS A 248      -1.370  31.889 -36.212  1.00 17.09           C  
ATOM   1355  SG  CYS A 248      -1.248  32.631 -34.593  1.00 20.46           S  
ATOM   1356  N   VAL A 249      -1.225  29.391 -38.232  1.00 19.44           N  
ATOM   1357  CA  VAL A 249      -1.504  28.767 -39.520  1.00 19.47           C  
ATOM   1358  C   VAL A 249      -2.375  27.528 -39.334  1.00 21.33           C  
ATOM   1359  O   VAL A 249      -3.410  27.370 -39.993  1.00 21.37           O  
ATOM   1360  CB  VAL A 249      -0.195  28.438 -40.253  1.00 18.29           C  
ATOM   1361  CG1 VAL A 249      -0.455  27.494 -41.434  1.00 17.59           C  
ATOM   1362  CG2 VAL A 249       0.465  29.730 -40.732  1.00 18.83           C  
ATOM   1363  N   LEU A 250      -1.980  26.639 -38.422  1.00 17.51           N  
ATOM   1364  CA  LEU A 250      -2.595  25.318 -38.354  1.00 14.95           C  
ATOM   1365  C   LEU A 250      -3.995  25.337 -37.752  1.00 13.39           C  
ATOM   1366  O   LEU A 250      -4.757  24.398 -37.978  1.00 13.12           O  
ATOM   1367  CB  LEU A 250      -1.700  24.372 -37.558  1.00 11.40           C  
ATOM   1368  CG  LEU A 250      -0.375  24.001 -38.224  1.00 18.73           C  
ATOM   1369  CD1 LEU A 250       0.562  23.400 -37.194  1.00 17.10           C  
ATOM   1370  CD2 LEU A 250      -0.595  23.037 -39.365  1.00 13.37           C  
ATOM   1371  N   ILE A 251      -4.370  26.379 -37.014  1.00 12.99           N  
ATOM   1372  CA  ILE A 251      -5.685  26.376 -36.400  1.00 11.69           C  
ATOM   1373  C   ILE A 251      -6.800  26.408 -37.431  1.00 11.95           C  
ATOM   1374  O   ILE A 251      -7.954  26.149 -37.087  1.00 11.74           O  
ATOM   1375  CB  ILE A 251      -5.824  27.544 -35.399  1.00 10.46           C  
ATOM   1376  CG1 ILE A 251      -6.917  27.195 -34.390  1.00 12.86           C  
ATOM   1377  CG2 ILE A 251      -6.098  28.853 -36.113  1.00 13.26           C  
ATOM   1378  CD1 ILE A 251      -6.937  28.054 -33.186  1.00 13.66           C  
ATOM   1379  N   HIS A 252      -6.476  26.679 -38.692  1.00 17.03           N  
ATOM   1380  CA  HIS A 252      -7.442  26.683 -39.779  1.00 11.56           C  
ATOM   1381  C   HIS A 252      -7.539  25.345 -40.493  1.00 11.01           C  
ATOM   1382  O   HIS A 252      -8.390  25.192 -41.371  1.00 17.66           O  
ATOM   1383  CB  HIS A 252      -7.081  27.775 -40.798  1.00 13.83           C  
ATOM   1384  CG  HIS A 252      -7.126  29.157 -40.232  1.00 11.75           C  
ATOM   1385  ND1 HIS A 252      -6.018  29.974 -40.169  1.00 23.98           N  
ATOM   1386  CD2 HIS A 252      -8.142  29.862 -39.689  1.00 12.48           C  
ATOM   1387  CE1 HIS A 252      -6.352  31.126 -39.615  1.00 15.83           C  
ATOM   1388  NE2 HIS A 252      -7.635  31.082 -39.311  1.00 20.58           N  
ATOM   1389  N   HIS A 253      -6.707  24.369 -40.150  1.00 16.84           N  
ATOM   1390  CA  HIS A 253      -6.810  23.071 -40.796  1.00 15.82           C  
ATOM   1391  C   HIS A 253      -8.116  22.389 -40.405  1.00 13.84           C  
ATOM   1392  O   HIS A 253      -8.629  22.570 -39.298  1.00 14.96           O  
ATOM   1393  CB  HIS A 253      -5.625  22.186 -40.418  1.00 18.54           C  
ATOM   1394  CG  HIS A 253      -5.125  21.339 -41.549  1.00 13.87           C  
ATOM   1395  ND1 HIS A 253      -5.823  20.253 -42.039  1.00 14.86           N  
ATOM   1396  CD2 HIS A 253      -3.995  21.426 -42.290  1.00 18.06           C  
ATOM   1397  CE1 HIS A 253      -5.142  19.711 -43.033  1.00 14.64           C  
ATOM   1398  NE2 HIS A 253      -4.027  20.402 -43.204  1.00 17.87           N  
ATOM   1399  N   THR A 254      -8.657  21.597 -41.332  1.00 13.29           N  
ATOM   1400  CA  THR A 254      -9.896  20.868 -41.092  1.00 19.32           C  
ATOM   1401  C   THR A 254      -9.669  19.401 -40.764  1.00 13.58           C  
ATOM   1402  O   THR A 254     -10.621  18.713 -40.389  1.00 19.22           O  
ATOM   1403  CB  THR A 254     -10.836  20.969 -42.303  1.00 19.01           C  
ATOM   1404  OG1 THR A 254     -10.186  20.478 -43.483  1.00 18.12           O  
ATOM   1405  CG2 THR A 254     -11.255  22.398 -42.522  1.00 23.15           C  
ATOM   1406  N   ASP A 255      -8.446  18.901 -40.894  1.00 23.34           N  
ATOM   1407  CA  ASP A 255      -8.138  17.567 -40.402  1.00 18.45           C  
ATOM   1408  C   ASP A 255      -8.256  17.557 -38.882  1.00 13.45           C  
ATOM   1409  O   ASP A 255      -7.602  18.352 -38.199  1.00 15.86           O  
ATOM   1410  CB  ASP A 255      -6.741  17.155 -40.843  1.00 13.23           C  
ATOM   1411  CG  ASP A 255      -6.344  15.786 -40.320  1.00 16.72           C  
ATOM   1412  OD1 ASP A 255      -6.847  14.771 -40.840  1.00 21.13           O  
ATOM   1413  OD2 ASP A 255      -5.527  15.728 -39.378  1.00 15.15           O  
ATOM   1414  N   VAL A 256      -9.099  16.660 -38.362  1.00 11.09           N  
ATOM   1415  CA  VAL A 256      -9.391  16.625 -36.930  1.00 10.22           C  
ATOM   1416  C   VAL A 256      -8.113  16.450 -36.117  1.00 16.36           C  
ATOM   1417  O   VAL A 256      -7.918  17.110 -35.090  1.00 12.95           O  
ATOM   1418  CB  VAL A 256     -10.403  15.511 -36.616  1.00 16.80           C  
ATOM   1419  CG1 VAL A 256     -10.645  15.407 -35.106  1.00 18.14           C  
ATOM   1420  CG2 VAL A 256     -11.720  15.767 -37.339  1.00 24.31           C  
ATOM   1421  N   ASN A 257      -7.246  15.521 -36.531  1.00 14.46           N  
ATOM   1422  CA  ASN A 257      -6.040  15.240 -35.755  1.00 18.69           C  
ATOM   1423  C   ASN A 257      -5.174  16.489 -35.607  1.00  9.31           C  
ATOM   1424  O   ASN A 257      -4.729  16.831 -34.504  1.00 13.91           O  
ATOM   1425  CB  ASN A 257      -5.255  14.105 -36.411  1.00 18.25           C  
ATOM   1426  CG  ASN A 257      -5.941  12.762 -36.257  1.00 31.45           C  
ATOM   1427  OD1 ASN A 257      -6.231  12.078 -37.236  1.00 45.12           O  
ATOM   1428  ND2 ASN A 257      -6.221  12.388 -35.019  1.00 44.08           N  
ATOM   1429  N   ILE A 258      -4.944  17.194 -36.712  1.00 11.18           N  
ATOM   1430  CA  ILE A 258      -4.104  18.385 -36.685  1.00  9.13           C  
ATOM   1431  C   ILE A 258      -4.744  19.454 -35.817  1.00 14.19           C  
ATOM   1432  O   ILE A 258      -4.065  20.121 -35.034  1.00 13.93           O  
ATOM   1433  CB  ILE A 258      -3.848  18.875 -38.124  1.00 13.23           C  
ATOM   1434  CG1 ILE A 258      -2.856  17.941 -38.817  1.00 13.75           C  
ATOM   1435  CG2 ILE A 258      -3.302  20.313 -38.149  1.00 14.76           C  
ATOM   1436  CD1 ILE A 258      -2.932  17.999 -40.293  1.00 20.01           C  
ATOM   1437  N   LEU A 259      -6.060  19.620 -35.930  1.00 12.04           N  
ATOM   1438  CA  LEU A 259      -6.745  20.674 -35.198  1.00 10.34           C  
ATOM   1439  C   LEU A 259      -6.747  20.402 -33.700  1.00 10.72           C  
ATOM   1440  O   LEU A 259      -6.499  21.308 -32.897  1.00  9.08           O  
ATOM   1441  CB  LEU A 259      -8.176  20.813 -35.729  1.00  8.32           C  
ATOM   1442  CG  LEU A 259      -8.962  22.029 -35.277  1.00 14.40           C  
ATOM   1443  CD1 LEU A 259      -8.197  23.323 -35.564  1.00 15.97           C  
ATOM   1444  CD2 LEU A 259     -10.332  22.038 -35.958  1.00 19.38           C  
ATOM   1445  N   VAL A 260      -7.008  19.158 -33.306  1.00  9.87           N  
ATOM   1446  CA  VAL A 260      -6.981  18.796 -31.895  1.00  7.18           C  
ATOM   1447  C   VAL A 260      -5.587  19.022 -31.325  1.00 11.90           C  
ATOM   1448  O   VAL A 260      -5.426  19.597 -30.243  1.00 12.23           O  
ATOM   1449  CB  VAL A 260      -7.442  17.340 -31.714  1.00 14.37           C  
ATOM   1450  CG1 VAL A 260      -7.203  16.861 -30.318  1.00 12.60           C  
ATOM   1451  CG2 VAL A 260      -8.922  17.184 -32.049  1.00 21.49           C  
ATOM   1452  N   ASP A 261      -4.551  18.589 -32.051  1.00 11.47           N  
ATOM   1453  CA  ASP A 261      -3.197  18.769 -31.535  1.00  9.58           C  
ATOM   1454  C   ASP A 261      -2.798  20.244 -31.510  1.00  9.12           C  
ATOM   1455  O   ASP A 261      -2.125  20.689 -30.574  1.00 10.50           O  
ATOM   1456  CB  ASP A 261      -2.209  17.932 -32.356  1.00 14.16           C  
ATOM   1457  CG  ASP A 261      -2.211  16.447 -31.947  1.00 13.59           C  
ATOM   1458  OD1 ASP A 261      -2.872  16.099 -30.942  1.00 20.38           O  
ATOM   1459  OD2 ASP A 261      -1.551  15.625 -32.621  1.00 24.15           O  
ATOM   1460  N   THR A 262      -3.216  21.024 -32.512  1.00  9.68           N  
ATOM   1461  CA  THR A 262      -2.951  22.462 -32.509  1.00  8.67           C  
ATOM   1462  C   THR A 262      -3.555  23.127 -31.279  1.00 12.06           C  
ATOM   1463  O   THR A 262      -2.880  23.889 -30.570  1.00 11.39           O  
ATOM   1464  CB  THR A 262      -3.511  23.089 -33.785  1.00  9.19           C  
ATOM   1465  OG1 THR A 262      -2.814  22.574 -34.926  1.00  7.69           O  
ATOM   1466  CG2 THR A 262      -3.387  24.606 -33.759  1.00 14.00           C  
ATOM   1467  N   VAL A 263      -4.826  22.828 -30.998  1.00  9.50           N  
ATOM   1468  CA  VAL A 263      -5.509  23.453 -29.871  1.00 10.68           C  
ATOM   1469  C   VAL A 263      -4.925  22.969 -28.554  1.00 10.76           C  
ATOM   1470  O   VAL A 263      -4.855  23.731 -27.584  1.00 12.30           O  
ATOM   1471  CB  VAL A 263      -7.027  23.191 -29.967  1.00 11.25           C  
ATOM   1472  CG1 VAL A 263      -7.767  23.771 -28.779  1.00 10.23           C  
ATOM   1473  CG2 VAL A 263      -7.573  23.790 -31.257  1.00 12.32           C  
ATOM   1474  N   TRP A 264      -4.469  21.719 -28.492  1.00 10.21           N  
ATOM   1475  CA  TRP A 264      -3.825  21.251 -27.269  1.00  9.58           C  
ATOM   1476  C   TRP A 264      -2.493  21.958 -27.037  1.00  9.81           C  
ATOM   1477  O   TRP A 264      -2.172  22.336 -25.904  1.00 15.11           O  
ATOM   1478  CB  TRP A 264      -3.634  19.735 -27.320  1.00 13.55           C  
ATOM   1479  CG  TRP A 264      -4.730  18.997 -26.646  1.00  9.02           C  
ATOM   1480  CD1 TRP A 264      -5.824  18.428 -27.231  1.00 15.50           C  
ATOM   1481  CD2 TRP A 264      -4.846  18.749 -25.249  1.00  9.77           C  
ATOM   1482  NE1 TRP A 264      -6.613  17.837 -26.277  1.00 14.18           N  
ATOM   1483  CE2 TRP A 264      -6.034  18.024 -25.051  1.00 11.65           C  
ATOM   1484  CE3 TRP A 264      -4.057  19.062 -24.145  1.00 13.53           C  
ATOM   1485  CZ2 TRP A 264      -6.450  17.613 -23.794  1.00 16.13           C  
ATOM   1486  CZ3 TRP A 264      -4.473  18.654 -22.905  1.00 14.24           C  
ATOM   1487  CH2 TRP A 264      -5.658  17.943 -22.736  1.00 13.96           C  
ATOM   1488  N   ALA A 265      -1.695  22.143 -28.088  1.00 12.33           N  
ATOM   1489  CA  ALA A 265      -0.459  22.905 -27.933  1.00 13.85           C  
ATOM   1490  C   ALA A 265      -0.761  24.320 -27.461  1.00  8.77           C  
ATOM   1491  O   ALA A 265      -0.080  24.858 -26.578  1.00 14.47           O  
ATOM   1492  CB  ALA A 265       0.314  22.932 -29.254  1.00 11.62           C  
ATOM   1493  N   LEU A 266      -1.790  24.937 -28.031  1.00 12.27           N  
ATOM   1494  CA  LEU A 266      -2.207  26.246 -27.546  1.00 10.24           C  
ATOM   1495  C   LEU A 266      -2.559  26.187 -26.070  1.00 14.30           C  
ATOM   1496  O   LEU A 266      -2.140  27.050 -25.297  1.00 14.88           O  
ATOM   1497  CB  LEU A 266      -3.393  26.764 -28.363  1.00 13.33           C  
ATOM   1498  CG  LEU A 266      -3.089  27.223 -29.787  1.00 13.97           C  
ATOM   1499  CD1 LEU A 266      -4.385  27.571 -30.514  1.00 19.00           C  
ATOM   1500  CD2 LEU A 266      -2.152  28.427 -29.775  1.00 17.62           C  
ATOM   1501  N   SER A 267      -3.305  25.160 -25.652  1.00 12.63           N  
ATOM   1502  CA  SER A 267      -3.709  25.075 -24.256  1.00 13.42           C  
ATOM   1503  C   SER A 267      -2.513  24.910 -23.344  1.00 15.00           C  
ATOM   1504  O   SER A 267      -2.543  25.354 -22.192  1.00 14.64           O  
ATOM   1505  CB  SER A 267      -4.675  23.916 -24.038  1.00 14.38           C  
ATOM   1506  OG  SER A 267      -3.984  22.705 -23.820  1.00 13.03           O  
ATOM   1507  N   TYR A 268      -1.469  24.238 -23.823  1.00 16.81           N  
ATOM   1508  CA  TYR A 268      -0.276  24.093 -23.004  1.00 16.39           C  
ATOM   1509  C   TYR A 268       0.473  25.411 -22.906  1.00 18.41           C  
ATOM   1510  O   TYR A 268       1.141  25.668 -21.899  1.00 18.42           O  
ATOM   1511  CB  TYR A 268       0.627  22.995 -23.569  1.00 16.99           C  
ATOM   1512  CG  TYR A 268       0.166  21.593 -23.229  1.00 11.90           C  
ATOM   1513  CD1 TYR A 268      -0.097  21.231 -21.918  1.00 11.96           C  
ATOM   1514  CD2 TYR A 268      -0.011  20.637 -24.220  1.00  8.78           C  
ATOM   1515  CE1 TYR A 268      -0.506  19.962 -21.601  1.00 13.32           C  
ATOM   1516  CE2 TYR A 268      -0.426  19.372 -23.915  1.00 10.25           C  
ATOM   1517  CZ  TYR A 268      -0.669  19.030 -22.606  1.00 13.35           C  
ATOM   1518  OH  TYR A 268      -1.083  17.756 -22.302  1.00 16.17           O  
ATOM   1519  N   LEU A 269       0.365  26.260 -23.930  1.00 15.03           N  
ATOM   1520  CA  LEU A 269       0.925  27.607 -23.820  1.00  9.63           C  
ATOM   1521  C   LEU A 269       0.089  28.490 -22.894  1.00 18.75           C  
ATOM   1522  O   LEU A 269       0.638  29.252 -22.092  1.00 25.41           O  
ATOM   1523  CB  LEU A 269       1.044  28.238 -25.201  1.00  9.89           C  
ATOM   1524  CG  LEU A 269       1.997  27.556 -26.187  1.00 15.81           C  
ATOM   1525  CD1 LEU A 269       2.026  28.304 -27.523  1.00 16.25           C  
ATOM   1526  CD2 LEU A 269       3.408  27.441 -25.638  1.00 22.27           C  
ATOM   1527  N   THR A 270      -1.240  28.396 -22.966  1.00 16.94           N  
ATOM   1528  CA  THR A 270      -2.080  29.267 -22.147  1.00 16.74           C  
ATOM   1529  C   THR A 270      -2.112  28.842 -20.689  1.00 15.60           C  
ATOM   1530  O   THR A 270      -2.594  29.614 -19.856  1.00 19.28           O  
ATOM   1531  CB  THR A 270      -3.515  29.326 -22.677  1.00 17.07           C  
ATOM   1532  OG1 THR A 270      -4.105  28.019 -22.665  1.00 17.19           O  
ATOM   1533  CG2 THR A 270      -3.557  29.903 -24.082  1.00 15.75           C  
ATOM   1534  N   ASP A 271      -1.629  27.645 -20.366  1.00 18.43           N  
ATOM   1535  CA  ASP A 271      -1.468  27.203 -18.984  1.00 17.05           C  
ATOM   1536  C   ASP A 271      -0.091  27.527 -18.422  1.00 19.93           C  
ATOM   1537  O   ASP A 271       0.196  27.155 -17.281  1.00 24.87           O  
ATOM   1538  CB  ASP A 271      -1.701  25.686 -18.869  1.00 23.51           C  
ATOM   1539  CG  ASP A 271      -1.828  25.204 -17.417  1.00 35.37           C  
ATOM   1540  OD1 ASP A 271      -2.240  26.005 -16.546  1.00 30.47           O  
ATOM   1541  OD2 ASP A 271      -1.513  24.019 -17.141  1.00 35.57           O  
ATOM   1542  N   ALA A 272       0.772  28.183 -19.196  1.00 24.61           N  
ATOM   1543  CA  ALA A 272       2.161  28.379 -18.804  1.00 28.81           C  
ATOM   1544  C   ALA A 272       2.402  29.669 -18.026  1.00 30.13           C  
ATOM   1545  O   ALA A 272       3.501  29.846 -17.492  1.00 41.64           O  
ATOM   1546  CB  ALA A 272       3.058  28.359 -20.044  1.00 26.42           C  
ATOM   1547  N   GLY A 273       1.421  30.566 -17.943  1.00 27.93           N  
ATOM   1548  CA  GLY A 273       1.573  31.781 -17.162  1.00 29.39           C  
ATOM   1549  C   GLY A 273       1.009  33.017 -17.834  1.00 28.70           C  
ATOM   1550  O   GLY A 273       0.705  32.995 -19.029  1.00 26.05           O  
ATOM   1551  N   ASN A 274       0.888  34.113 -17.080  1.00 27.56           N  
ATOM   1552  CA  ASN A 274       0.272  35.320 -17.622  1.00 34.02           C  
ATOM   1553  C   ASN A 274       1.025  35.822 -18.842  1.00 25.47           C  
ATOM   1554  O   ASN A 274       0.414  36.275 -19.813  1.00 26.67           O  
ATOM   1555  CB  ASN A 274       0.210  36.413 -16.551  1.00 30.89           C  
ATOM   1556  CG  ASN A 274      -1.160  36.501 -15.876  1.00 44.64           C  
ATOM   1557  OD1 ASN A 274      -2.054  35.687 -16.129  1.00 33.90           O  
ATOM   1558  ND2 ASN A 274      -1.321  37.489 -15.000  1.00 46.64           N  
ATOM   1559  N   GLU A 275       2.352  35.753 -18.813  1.00 26.27           N  
ATOM   1560  CA  GLU A 275       3.131  36.229 -19.951  1.00 28.85           C  
ATOM   1561  C   GLU A 275       2.880  35.369 -21.183  1.00 28.93           C  
ATOM   1562  O   GLU A 275       2.724  35.890 -22.294  1.00 27.50           O  
ATOM   1563  CB  GLU A 275       4.620  36.245 -19.596  1.00 29.79           C  
ATOM   1564  CG  GLU A 275       5.479  36.961 -20.629  1.00 50.67           C  
ATOM   1565  CD  GLU A 275       6.904  37.179 -20.169  1.00 46.17           C  
ATOM   1566  OE1 GLU A 275       7.748  37.495 -21.029  1.00 49.20           O  
ATOM   1567  OE2 GLU A 275       7.178  37.038 -18.957  1.00 44.17           O  
ATOM   1568  N   GLN A 276       2.828  34.047 -21.012  1.00 25.34           N  
ATOM   1569  CA  GLN A 276       2.516  33.186 -22.148  1.00 29.29           C  
ATOM   1570  C   GLN A 276       1.095  33.438 -22.643  1.00 20.46           C  
ATOM   1571  O   GLN A 276       0.850  33.457 -23.854  1.00 16.84           O  
ATOM   1572  CB  GLN A 276       2.725  31.719 -21.766  1.00 21.74           C  
ATOM   1573  CG  GLN A 276       4.193  31.325 -21.597  1.00 39.01           C  
ATOM   1574  CD  GLN A 276       4.799  31.760 -20.257  1.00 48.63           C  
ATOM   1575  OE1 GLN A 276       4.220  32.570 -19.529  1.00 37.53           O  
ATOM   1576  NE2 GLN A 276       5.972  31.214 -19.931  1.00 38.47           N  
ATOM   1577  N   ILE A 277       0.149  33.658 -21.725  1.00 17.96           N  
ATOM   1578  CA  ILE A 277      -1.220  33.976 -22.123  1.00 17.68           C  
ATOM   1579  C   ILE A 277      -1.230  35.228 -22.981  1.00 22.87           C  
ATOM   1580  O   ILE A 277      -1.926  35.301 -24.001  1.00 22.17           O  
ATOM   1581  CB  ILE A 277      -2.116  34.148 -20.880  1.00 22.76           C  
ATOM   1582  CG1 ILE A 277      -2.360  32.803 -20.201  1.00 17.79           C  
ATOM   1583  CG2 ILE A 277      -3.443  34.800 -21.258  1.00 21.70           C  
ATOM   1584  CD1 ILE A 277      -2.986  32.917 -18.834  1.00 20.48           C  
ATOM   1585  N   GLN A 278      -0.475  36.244 -22.571  1.00 29.02           N  
ATOM   1586  CA  GLN A 278      -0.452  37.483 -23.331  1.00 19.44           C  
ATOM   1587  C   GLN A 278       0.194  37.279 -24.691  1.00 23.54           C  
ATOM   1588  O   GLN A 278      -0.234  37.882 -25.681  1.00 22.02           O  
ATOM   1589  CB  GLN A 278       0.288  38.566 -22.544  1.00 29.90           C  
ATOM   1590  CG  GLN A 278      -0.036  39.968 -23.015  1.00 24.62           C  
ATOM   1591  CD  GLN A 278      -1.517  40.247 -22.948  1.00 26.08           C  
ATOM   1592  OE1 GLN A 278      -2.172  39.921 -21.957  1.00 28.18           O  
ATOM   1593  NE2 GLN A 278      -2.065  40.824 -24.014  1.00 30.30           N  
ATOM   1594  N   MET A 279       1.228  36.435 -24.762  1.00 26.48           N  
ATOM   1595  CA  MET A 279       1.784  36.081 -26.065  1.00 22.32           C  
ATOM   1596  C   MET A 279       0.717  35.456 -26.955  1.00 20.23           C  
ATOM   1597  O   MET A 279       0.611  35.785 -28.141  1.00 21.30           O  
ATOM   1598  CB  MET A 279       2.965  35.127 -25.897  1.00 29.28           C  
ATOM   1599  CG  MET A 279       4.182  35.747 -25.218  1.00 29.87           C  
ATOM   1600  SD  MET A 279       5.560  34.602 -25.081  1.00 43.54           S  
ATOM   1601  CE  MET A 279       5.949  34.352 -26.809  1.00 34.12           C  
ATOM   1602  N   VAL A 280      -0.085  34.548 -26.398  1.00 24.45           N  
ATOM   1603  CA  VAL A 280      -1.132  33.894 -27.185  1.00 24.10           C  
ATOM   1604  C   VAL A 280      -2.143  34.923 -27.675  1.00 22.86           C  
ATOM   1605  O   VAL A 280      -2.559  34.908 -28.838  1.00 24.08           O  
ATOM   1606  CB  VAL A 280      -1.812  32.785 -26.358  1.00 24.83           C  
ATOM   1607  CG1 VAL A 280      -3.102  32.299 -27.044  1.00 20.34           C  
ATOM   1608  CG2 VAL A 280      -0.851  31.620 -26.134  1.00 19.04           C  
ATOM   1609  N   ILE A 281      -2.569  35.821 -26.783  1.00 21.23           N  
ATOM   1610  CA  ILE A 281      -3.548  36.847 -27.148  1.00 17.52           C  
ATOM   1611  C   ILE A 281      -2.990  37.759 -28.233  1.00 21.89           C  
ATOM   1612  O   ILE A 281      -3.660  38.059 -29.230  1.00 24.53           O  
ATOM   1613  CB  ILE A 281      -3.963  37.651 -25.903  1.00 22.22           C  
ATOM   1614  CG1 ILE A 281      -4.916  36.828 -25.037  1.00 16.67           C  
ATOM   1615  CG2 ILE A 281      -4.600  38.989 -26.301  1.00 19.66           C  
ATOM   1616  CD1 ILE A 281      -5.166  37.407 -23.682  1.00 21.40           C  
ATOM   1617  N   ASP A 282      -1.766  38.250 -28.032  1.00 22.78           N  
ATOM   1618  CA  ASP A 282      -1.152  39.183 -28.967  1.00 29.53           C  
ATOM   1619  C   ASP A 282      -0.995  38.583 -30.355  1.00 26.09           C  
ATOM   1620  O   ASP A 282      -0.916  39.329 -31.337  1.00 28.71           O  
ATOM   1621  CB  ASP A 282       0.220  39.627 -28.436  1.00 33.23           C  
ATOM   1622  CG  ASP A 282       0.118  40.505 -27.188  1.00 31.32           C  
ATOM   1623  OD1 ASP A 282      -0.987  41.009 -26.888  1.00 39.04           O  
ATOM   1624  OD2 ASP A 282       1.148  40.691 -26.506  1.00 42.16           O  
ATOM   1625  N   SER A 283      -0.951  37.256 -30.464  1.00 22.38           N  
ATOM   1626  CA  SER A 283      -0.828  36.638 -31.773  1.00 23.05           C  
ATOM   1627  C   SER A 283      -2.094  36.766 -32.604  1.00 22.17           C  
ATOM   1628  O   SER A 283      -2.053  36.467 -33.802  1.00 26.29           O  
ATOM   1629  CB  SER A 283      -0.468  35.163 -31.624  1.00 22.85           C  
ATOM   1630  OG  SER A 283      -1.614  34.394 -31.278  1.00 23.64           O  
ATOM   1631  N   GLY A 284      -3.203  37.194 -32.003  1.00 17.86           N  
ATOM   1632  CA  GLY A 284      -4.466  37.331 -32.703  1.00 24.91           C  
ATOM   1633  C   GLY A 284      -5.239  36.047 -32.910  1.00 24.28           C  
ATOM   1634  O   GLY A 284      -6.211  36.045 -33.676  1.00 18.72           O  
ATOM   1635  N   ILE A 285      -4.862  34.962 -32.231  1.00 20.56           N  
ATOM   1636  CA  ILE A 285      -5.441  33.656 -32.519  1.00 19.79           C  
ATOM   1637  C   ILE A 285      -6.719  33.384 -31.733  1.00 13.15           C  
ATOM   1638  O   ILE A 285      -7.487  32.499 -32.121  1.00 20.02           O  
ATOM   1639  CB  ILE A 285      -4.410  32.549 -32.240  1.00 12.60           C  
ATOM   1640  CG1 ILE A 285      -4.759  31.285 -33.028  1.00 18.64           C  
ATOM   1641  CG2 ILE A 285      -4.329  32.257 -30.731  1.00 18.48           C  
ATOM   1642  CD1 ILE A 285      -3.717  30.207 -32.946  1.00 20.99           C  
ATOM   1643  N   VAL A 286      -6.963  34.124 -30.644  1.00 18.58           N  
ATOM   1644  CA  VAL A 286      -8.103  33.806 -29.774  1.00 15.17           C  
ATOM   1645  C   VAL A 286      -9.417  33.874 -30.526  1.00 19.89           C  
ATOM   1646  O   VAL A 286     -10.295  33.029 -30.280  1.00 17.70           O  
ATOM   1647  CB  VAL A 286      -8.076  34.713 -28.530  1.00 13.61           C  
ATOM   1648  CG1 VAL A 286      -9.278  34.440 -27.610  1.00 17.45           C  
ATOM   1649  CG2 VAL A 286      -6.781  34.522 -27.770  1.00 19.68           C  
ATOM   1650  N   PRO A 287      -9.655  34.847 -31.411  1.00 18.90           N  
ATOM   1651  CA  PRO A 287     -10.901  34.848 -32.193  1.00 16.76           C  
ATOM   1652  C   PRO A 287     -11.097  33.606 -33.043  1.00 17.05           C  
ATOM   1653  O   PRO A 287     -12.241  33.293 -33.395  1.00 16.98           O  
ATOM   1654  CB  PRO A 287     -10.761  36.102 -33.063  1.00 22.23           C  
ATOM   1655  CG  PRO A 287      -9.851  36.995 -32.286  1.00 19.10           C  
ATOM   1656  CD  PRO A 287      -8.893  36.096 -31.587  1.00 18.02           C  
ATOM   1657  N   HIS A 288     -10.027  32.900 -33.405  1.00 15.95           N  
ATOM   1658  CA  HIS A 288     -10.159  31.651 -34.144  1.00 20.17           C  
ATOM   1659  C   HIS A 288     -10.263  30.444 -33.226  1.00 23.04           C  
ATOM   1660  O   HIS A 288     -10.713  29.377 -33.663  1.00 19.13           O  
ATOM   1661  CB  HIS A 288      -8.968  31.457 -35.087  1.00 16.29           C  
ATOM   1662  CG  HIS A 288      -8.935  32.430 -36.221  1.00 24.19           C  
ATOM   1663  ND1 HIS A 288      -7.959  33.397 -36.344  1.00 27.70           N  
ATOM   1664  CD2 HIS A 288      -9.764  32.592 -37.280  1.00 23.27           C  
ATOM   1665  CE1 HIS A 288      -8.187  34.110 -37.433  1.00 34.14           C  
ATOM   1666  NE2 HIS A 288      -9.275  33.640 -38.020  1.00 30.49           N  
ATOM   1667  N   LEU A 289      -9.869  30.603 -31.967  1.00 15.00           N  
ATOM   1668  CA  LEU A 289      -9.923  29.519 -30.999  1.00 16.54           C  
ATOM   1669  C   LEU A 289     -11.309  29.411 -30.375  1.00 15.96           C  
ATOM   1670  O   LEU A 289     -11.875  28.314 -30.287  1.00 14.12           O  
ATOM   1671  CB  LEU A 289      -8.860  29.759 -29.928  1.00 19.51           C  
ATOM   1672  CG  LEU A 289      -8.693  28.737 -28.823  1.00 31.04           C  
ATOM   1673  CD1 LEU A 289      -8.282  27.409 -29.402  1.00 31.61           C  
ATOM   1674  CD2 LEU A 289      -7.649  29.254 -27.838  1.00 24.65           C  
ATOM   1675  N   VAL A 290     -11.889  30.545 -29.979  1.00 12.55           N  
ATOM   1676  CA  VAL A 290     -13.149  30.516 -29.234  1.00 19.62           C  
ATOM   1677  C   VAL A 290     -14.243  29.770 -29.993  1.00 19.55           C  
ATOM   1678  O   VAL A 290     -14.991  29.009 -29.361  1.00 12.64           O  
ATOM   1679  CB  VAL A 290     -13.579  31.936 -28.858  1.00 17.71           C  
ATOM   1680  CG1 VAL A 290     -14.981  31.939 -28.268  1.00 17.61           C  
ATOM   1681  CG2 VAL A 290     -12.607  32.525 -27.860  1.00 15.96           C  
ATOM   1682  N   PRO A 291     -14.437  29.992 -31.293  1.00 17.05           N  
ATOM   1683  CA  PRO A 291     -15.529  29.288 -31.980  1.00 15.80           C  
ATOM   1684  C   PRO A 291     -15.378  27.780 -31.976  1.00 14.80           C  
ATOM   1685  O   PRO A 291     -16.366  27.082 -32.218  1.00 15.23           O  
ATOM   1686  CB  PRO A 291     -15.478  29.854 -33.408  1.00 20.09           C  
ATOM   1687  CG  PRO A 291     -14.374  30.867 -33.437  1.00 24.50           C  
ATOM   1688  CD  PRO A 291     -13.987  31.178 -32.042  1.00 16.36           C  
ATOM   1689  N   LEU A 292     -14.187  27.245 -31.707  1.00 15.97           N  
ATOM   1690  CA  LEU A 292     -14.032  25.797 -31.683  1.00 12.42           C  
ATOM   1691  C   LEU A 292     -14.762  25.159 -30.505  1.00 10.85           C  
ATOM   1692  O   LEU A 292     -14.904  23.932 -30.469  1.00 10.23           O  
ATOM   1693  CB  LEU A 292     -12.539  25.431 -31.660  1.00 12.15           C  
ATOM   1694  CG  LEU A 292     -11.715  25.899 -32.861  1.00 12.61           C  
ATOM   1695  CD1 LEU A 292     -10.244  25.553 -32.701  1.00 10.18           C  
ATOM   1696  CD2 LEU A 292     -12.256  25.306 -34.148  1.00 19.69           C  
ATOM   1697  N   LEU A 293     -15.240  25.959 -29.556  1.00 12.97           N  
ATOM   1698  CA  LEU A 293     -16.112  25.445 -28.506  1.00 13.07           C  
ATOM   1699  C   LEU A 293     -17.391  24.825 -29.058  1.00 16.33           C  
ATOM   1700  O   LEU A 293     -18.046  24.050 -28.349  1.00 14.67           O  
ATOM   1701  CB  LEU A 293     -16.473  26.572 -27.531  1.00  9.66           C  
ATOM   1702  CG  LEU A 293     -15.329  27.144 -26.701  1.00 14.83           C  
ATOM   1703  CD1 LEU A 293     -15.770  28.387 -25.966  1.00 15.40           C  
ATOM   1704  CD2 LEU A 293     -14.828  26.111 -25.726  1.00 13.09           C  
ATOM   1705  N   SER A 294     -17.774  25.161 -30.292  1.00 12.08           N  
ATOM   1706  CA  SER A 294     -18.947  24.587 -30.938  1.00 20.21           C  
ATOM   1707  C   SER A 294     -18.587  23.754 -32.162  1.00 14.80           C  
ATOM   1708  O   SER A 294     -19.444  23.522 -33.019  1.00 13.98           O  
ATOM   1709  CB  SER A 294     -19.930  25.691 -31.326  1.00 20.50           C  
ATOM   1710  OG  SER A 294     -20.351  26.403 -30.178  1.00 25.21           O  
ATOM   1711  N   HIS A 295     -17.339  23.305 -32.262  1.00 15.22           N  
ATOM   1712  CA  HIS A 295     -16.953  22.377 -33.318  1.00 13.20           C  
ATOM   1713  C   HIS A 295     -17.796  21.104 -33.230  1.00 12.08           C  
ATOM   1714  O   HIS A 295     -18.318  20.752 -32.171  1.00 15.70           O  
ATOM   1715  CB  HIS A 295     -15.464  22.046 -33.198  1.00  8.70           C  
ATOM   1716  CG  HIS A 295     -14.848  21.554 -34.464  1.00 10.12           C  
ATOM   1717  ND1 HIS A 295     -14.802  20.218 -34.803  1.00 10.27           N  
ATOM   1718  CD2 HIS A 295     -14.252  22.223 -35.477  1.00 10.97           C  
ATOM   1719  CE1 HIS A 295     -14.207  20.088 -35.975  1.00 11.04           C  
ATOM   1720  NE2 HIS A 295     -13.865  21.289 -36.405  1.00 12.60           N  
ATOM   1721  N   GLN A 296     -17.948  20.418 -34.365  1.00  8.31           N  
ATOM   1722  CA  GLN A 296     -18.726  19.179 -34.366  1.00 15.78           C  
ATOM   1723  C   GLN A 296     -17.997  18.049 -33.644  1.00 12.65           C  
ATOM   1724  O   GLN A 296     -18.643  17.144 -33.107  1.00 15.66           O  
ATOM   1725  CB  GLN A 296     -19.057  18.755 -35.802  1.00 17.62           C  
ATOM   1726  CG  GLN A 296     -20.047  19.670 -36.517  1.00 47.94           C  
ATOM   1727  CD  GLN A 296     -21.509  19.424 -36.126  1.00 49.82           C  
ATOM   1728  OE1 GLN A 296     -21.964  18.279 -36.030  1.00 58.27           O  
ATOM   1729  NE2 GLN A 296     -22.245  20.503 -35.904  1.00 30.32           N  
ATOM   1730  N   GLU A 297     -16.668  18.086 -33.625  1.00 11.75           N  
ATOM   1731  CA  GLU A 297     -15.850  17.049 -33.010  1.00 12.34           C  
ATOM   1732  C   GLU A 297     -15.656  17.370 -31.533  1.00 14.67           C  
ATOM   1733  O   GLU A 297     -15.061  18.396 -31.182  1.00 13.68           O  
ATOM   1734  CB  GLU A 297     -14.488  16.943 -33.699  1.00 13.89           C  
ATOM   1735  CG  GLU A 297     -14.218  15.619 -34.359  1.00 35.20           C  
ATOM   1736  CD  GLU A 297     -14.548  14.423 -33.489  1.00 38.07           C  
ATOM   1737  OE1 GLU A 297     -15.259  13.543 -34.015  1.00 32.01           O  
ATOM   1738  OE2 GLU A 297     -14.114  14.364 -32.301  1.00 26.42           O  
ATOM   1739  N   VAL A 298     -16.108  16.465 -30.668  1.00 14.03           N  
ATOM   1740  CA  VAL A 298     -16.059  16.736 -29.237  1.00 12.39           C  
ATOM   1741  C   VAL A 298     -14.618  16.849 -28.754  1.00 11.41           C  
ATOM   1742  O   VAL A 298     -14.336  17.578 -27.803  1.00 12.75           O  
ATOM   1743  CB  VAL A 298     -16.848  15.656 -28.471  1.00 10.89           C  
ATOM   1744  CG1 VAL A 298     -16.233  14.278 -28.687  1.00 17.73           C  
ATOM   1745  CG2 VAL A 298     -16.914  15.988 -27.004  1.00 13.24           C  
ATOM   1746  N   LYS A 299     -13.684  16.153 -29.399  1.00 12.02           N  
ATOM   1747  CA  LYS A 299     -12.276  16.270 -29.026  1.00  9.15           C  
ATOM   1748  C   LYS A 299     -11.742  17.678 -29.269  1.00  8.93           C  
ATOM   1749  O   LYS A 299     -10.997  18.222 -28.443  1.00 15.24           O  
ATOM   1750  CB  LYS A 299     -11.461  15.248 -29.804  1.00 13.22           C  
ATOM   1751  CG  LYS A 299     -11.510  13.845 -29.222  1.00 12.97           C  
ATOM   1752  CD  LYS A 299     -11.142  12.807 -30.264  1.00 33.82           C  
ATOM   1753  CE  LYS A 299     -10.659  11.524 -29.618  1.00 41.71           C  
ATOM   1754  NZ  LYS A 299      -9.173  11.389 -29.707  1.00 59.28           N  
ATOM   1755  N   VAL A 300     -12.124  18.290 -30.389  1.00  8.99           N  
ATOM   1756  CA  VAL A 300     -11.826  19.705 -30.614  1.00 11.02           C  
ATOM   1757  C   VAL A 300     -12.507  20.575 -29.559  1.00  9.47           C  
ATOM   1758  O   VAL A 300     -11.892  21.488 -29.001  1.00 11.76           O  
ATOM   1759  CB  VAL A 300     -12.239  20.114 -32.039  1.00 10.92           C  
ATOM   1760  CG1 VAL A 300     -11.903  21.571 -32.298  1.00 15.51           C  
ATOM   1761  CG2 VAL A 300     -11.551  19.244 -33.057  1.00  8.46           C  
ATOM   1762  N   GLN A 301     -13.786  20.317 -29.276  1.00 14.03           N  
ATOM   1763  CA  GLN A 301     -14.514  21.130 -28.301  1.00 10.19           C  
ATOM   1764  C   GLN A 301     -13.821  21.132 -26.948  1.00 13.01           C  
ATOM   1765  O   GLN A 301     -13.683  22.179 -26.308  1.00 11.70           O  
ATOM   1766  CB  GLN A 301     -15.939  20.614 -28.135  1.00 10.71           C  
ATOM   1767  CG  GLN A 301     -16.838  20.809 -29.313  1.00 13.94           C  
ATOM   1768  CD  GLN A 301     -18.221  20.254 -29.048  1.00 15.76           C  
ATOM   1769  OE1 GLN A 301     -18.469  19.056 -29.222  1.00 16.31           O  
ATOM   1770  NE2 GLN A 301     -19.123  21.114 -28.593  1.00 12.44           N  
ATOM   1771  N   THR A 302     -13.415  19.958 -26.478  1.00 11.50           N  
ATOM   1772  CA  THR A 302     -12.797  19.876 -25.161  1.00 13.24           C  
ATOM   1773  C   THR A 302     -11.391  20.469 -25.167  1.00  8.76           C  
ATOM   1774  O   THR A 302     -10.990  21.130 -24.198  1.00  8.00           O  
ATOM   1775  CB  THR A 302     -12.763  18.432 -24.685  1.00  8.24           C  
ATOM   1776  OG1 THR A 302     -11.928  17.668 -25.544  1.00 24.04           O  
ATOM   1777  CG2 THR A 302     -14.156  17.842 -24.688  1.00 13.15           C  
ATOM   1778  N   ALA A 303     -10.629  20.267 -26.250  1.00  9.05           N  
ATOM   1779  CA  ALA A 303      -9.335  20.934 -26.342  1.00 14.18           C  
ATOM   1780  C   ALA A 303      -9.496  22.451 -26.311  1.00  7.83           C  
ATOM   1781  O   ALA A 303      -8.725  23.157 -25.645  1.00 13.72           O  
ATOM   1782  CB  ALA A 303      -8.610  20.495 -27.607  1.00  8.91           C  
ATOM   1783  N   ALA A 304     -10.492  22.971 -27.024  1.00  8.82           N  
ATOM   1784  CA  ALA A 304     -10.722  24.409 -27.029  1.00 13.53           C  
ATOM   1785  C   ALA A 304     -11.150  24.884 -25.654  1.00 14.73           C  
ATOM   1786  O   ALA A 304     -10.723  25.944 -25.190  1.00 12.10           O  
ATOM   1787  CB  ALA A 304     -11.777  24.777 -28.081  1.00 13.59           C  
ATOM   1788  N   LEU A 305     -12.008  24.116 -24.995  1.00 12.75           N  
ATOM   1789  CA  LEU A 305     -12.433  24.472 -23.655  1.00 12.26           C  
ATOM   1790  C   LEU A 305     -11.233  24.611 -22.738  1.00 13.82           C  
ATOM   1791  O   LEU A 305     -11.160  25.548 -21.941  1.00 12.22           O  
ATOM   1792  CB  LEU A 305     -13.409  23.413 -23.137  1.00 10.49           C  
ATOM   1793  CG  LEU A 305     -14.221  23.692 -21.883  1.00 18.04           C  
ATOM   1794  CD1 LEU A 305     -14.918  25.039 -21.940  1.00 14.47           C  
ATOM   1795  CD2 LEU A 305     -15.252  22.591 -21.723  1.00 17.64           C  
ATOM   1796  N   ARG A 306     -10.254  23.712 -22.872  1.00 10.91           N  
ATOM   1797  CA  ARG A 306      -9.053  23.798 -22.040  1.00 11.45           C  
ATOM   1798  C   ARG A 306      -8.218  25.034 -22.380  1.00  9.61           C  
ATOM   1799  O   ARG A 306      -7.767  25.759 -21.483  1.00  8.68           O  
ATOM   1800  CB  ARG A 306      -8.210  22.528 -22.195  1.00 15.37           C  
ATOM   1801  CG  ARG A 306      -7.078  22.413 -21.194  1.00 15.06           C  
ATOM   1802  CD  ARG A 306      -6.167  21.241 -21.521  1.00 19.19           C  
ATOM   1803  NE  ARG A 306      -5.273  20.941 -20.407  1.00 16.55           N  
ATOM   1804  CZ  ARG A 306      -4.073  21.482 -20.232  1.00 18.55           C  
ATOM   1805  NH1 ARG A 306      -3.584  22.350 -21.104  1.00 17.29           N  
ATOM   1806  NH2 ARG A 306      -3.347  21.142 -19.181  1.00 28.34           N  
ATOM   1807  N   ALA A 307      -7.982  25.280 -23.668  1.00 12.89           N  
ATOM   1808  CA  ALA A 307      -7.155  26.421 -24.069  1.00 13.88           C  
ATOM   1809  C   ALA A 307      -7.750  27.756 -23.600  1.00 12.46           C  
ATOM   1810  O   ALA A 307      -7.067  28.581 -22.961  1.00 16.96           O  
ATOM   1811  CB  ALA A 307      -6.979  26.417 -25.584  1.00 13.91           C  
ATOM   1812  N   VAL A 308      -9.030  27.994 -23.910  1.00 15.10           N  
ATOM   1813  CA  VAL A 308      -9.645  29.266 -23.523  1.00 14.99           C  
ATOM   1814  C   VAL A 308      -9.892  29.317 -22.015  1.00 11.90           C  
ATOM   1815  O   VAL A 308      -9.855  30.399 -21.412  1.00 21.65           O  
ATOM   1816  CB  VAL A 308     -10.943  29.527 -24.321  1.00 14.43           C  
ATOM   1817  CG1 VAL A 308     -10.655  29.471 -25.821  1.00 19.58           C  
ATOM   1818  CG2 VAL A 308     -12.011  28.541 -23.955  1.00 32.01           C  
ATOM   1819  N   GLY A 309     -10.138  28.172 -21.369  1.00 11.27           N  
ATOM   1820  CA  GLY A 309     -10.283  28.174 -19.924  1.00 20.41           C  
ATOM   1821  C   GLY A 309      -9.016  28.619 -19.223  1.00 12.64           C  
ATOM   1822  O   GLY A 309      -9.053  29.425 -18.285  1.00 15.42           O  
ATOM   1823  N   ASN A 310      -7.871  28.100 -19.665  1.00 16.17           N  
ATOM   1824  CA  ASN A 310      -6.608  28.588 -19.126  1.00 17.73           C  
ATOM   1825  C   ASN A 310      -6.475  30.086 -19.345  1.00 13.47           C  
ATOM   1826  O   ASN A 310      -6.031  30.811 -18.445  1.00 16.25           O  
ATOM   1827  CB  ASN A 310      -5.426  27.846 -19.750  1.00 16.10           C  
ATOM   1828  CG  ASN A 310      -5.438  26.381 -19.430  1.00 17.66           C  
ATOM   1829  OD1 ASN A 310      -6.007  25.963 -18.429  1.00 15.19           O  
ATOM   1830  ND2 ASN A 310      -4.818  25.584 -20.288  1.00 19.99           N  
ATOM   1831  N   ILE A 311      -6.854  30.582 -20.528  1.00 16.27           N  
ATOM   1832  CA  ILE A 311      -6.798  32.036 -20.718  1.00 16.81           C  
ATOM   1833  C   ILE A 311      -7.583  32.741 -19.612  1.00 19.18           C  
ATOM   1834  O   ILE A 311      -7.081  33.663 -18.956  1.00 20.72           O  
ATOM   1835  CB  ILE A 311      -7.305  32.441 -22.111  1.00 17.26           C  
ATOM   1836  CG1 ILE A 311      -6.388  31.889 -23.202  1.00 14.71           C  
ATOM   1837  CG2 ILE A 311      -7.362  33.969 -22.218  1.00 16.54           C  
ATOM   1838  CD1 ILE A 311      -6.798  32.303 -24.612  1.00 15.16           C  
ATOM   1839  N   VAL A 312      -8.825  32.311 -19.372  1.00 22.47           N  
ATOM   1840  CA  VAL A 312      -9.656  33.020 -18.395  1.00 18.94           C  
ATOM   1841  C   VAL A 312      -9.275  32.715 -16.955  1.00 27.11           C  
ATOM   1842  O   VAL A 312      -9.927  33.233 -16.035  1.00 19.18           O  
ATOM   1843  CB  VAL A 312     -11.159  32.739 -18.598  1.00 19.89           C  
ATOM   1844  CG1 VAL A 312     -11.580  33.131 -20.030  1.00 18.72           C  
ATOM   1845  CG2 VAL A 312     -11.500  31.301 -18.305  1.00 14.79           C  
ATOM   1846  N   THR A 313      -8.245  31.892 -16.712  1.00 22.17           N  
ATOM   1847  CA  THR A 313      -7.674  31.863 -15.361  1.00 31.60           C  
ATOM   1848  C   THR A 313      -6.799  33.076 -15.060  1.00 19.28           C  
ATOM   1849  O   THR A 313      -6.397  33.257 -13.909  1.00 23.66           O  
ATOM   1850  CB  THR A 313      -6.830  30.601 -15.111  1.00 20.79           C  
ATOM   1851  OG1 THR A 313      -5.609  30.672 -15.869  1.00 23.78           O  
ATOM   1852  CG2 THR A 313      -7.607  29.342 -15.465  1.00 20.20           C  
ATOM   1853  N   GLY A 314      -6.491  33.899 -16.052  1.00 24.28           N  
ATOM   1854  CA  GLY A 314      -5.609  35.030 -15.843  1.00 25.61           C  
ATOM   1855  C   GLY A 314      -6.318  36.284 -15.375  1.00 24.26           C  
ATOM   1856  O   GLY A 314      -7.220  36.231 -14.533  1.00 27.14           O  
ATOM   1857  N   THR A 315      -5.918  37.422 -15.925  1.00 24.60           N  
ATOM   1858  CA  THR A 315      -6.430  38.705 -15.480  1.00 27.81           C  
ATOM   1859  C   THR A 315      -7.809  38.989 -16.078  1.00 36.13           C  
ATOM   1860  O   THR A 315      -8.249  38.363 -17.050  1.00 27.06           O  
ATOM   1861  CB  THR A 315      -5.478  39.824 -15.875  1.00 29.13           C  
ATOM   1862  OG1 THR A 315      -5.350  39.839 -17.304  1.00 30.16           O  
ATOM   1863  CG2 THR A 315      -4.109  39.622 -15.232  1.00 33.75           C  
ATOM   1864  N   ASP A 316      -8.481  39.986 -15.492  1.00 29.19           N  
ATOM   1865  CA  ASP A 316      -9.774  40.421 -16.013  1.00 32.73           C  
ATOM   1866  C   ASP A 316      -9.659  40.873 -17.462  1.00 26.22           C  
ATOM   1867  O   ASP A 316     -10.570  40.645 -18.264  1.00 29.23           O  
ATOM   1868  CB  ASP A 316     -10.341  41.549 -15.147  1.00 35.28           C  
ATOM   1869  CG  ASP A 316     -10.903  41.050 -13.831  1.00 25.89           C  
ATOM   1870  OD1 ASP A 316     -10.682  39.872 -13.504  1.00 31.42           O  
ATOM   1871  OD2 ASP A 316     -11.576  41.834 -13.124  1.00 44.02           O  
ATOM   1872  N   GLU A 317      -8.542  41.501 -17.824  1.00 24.96           N  
ATOM   1873  CA  GLU A 317      -8.379  41.999 -19.186  1.00 27.79           C  
ATOM   1874  C   GLU A 317      -8.205  40.855 -20.181  1.00 27.69           C  
ATOM   1875  O   GLU A 317      -8.807  40.865 -21.264  1.00 24.65           O  
ATOM   1876  CB  GLU A 317      -7.188  42.953 -19.253  1.00 26.20           C  
ATOM   1877  CG  GLU A 317      -7.156  44.016 -18.153  1.00 31.02           C  
ATOM   1878  CD  GLU A 317      -6.366  43.580 -16.907  1.00 50.13           C  
ATOM   1879  OE1 GLU A 317      -6.979  43.085 -15.933  1.00 36.89           O  
ATOM   1880  OE2 GLU A 317      -5.119  43.719 -16.906  1.00 65.37           O  
ATOM   1881  N   GLN A 318      -7.392  39.855 -19.832  1.00 22.91           N  
ATOM   1882  CA  GLN A 318      -7.256  38.675 -20.682  1.00 24.50           C  
ATOM   1883  C   GLN A 318      -8.584  37.922 -20.794  1.00 21.25           C  
ATOM   1884  O   GLN A 318      -9.042  37.578 -21.903  1.00 23.65           O  
ATOM   1885  CB  GLN A 318      -6.149  37.788 -20.117  1.00 25.30           C  
ATOM   1886  CG  GLN A 318      -4.773  38.462 -20.159  1.00 26.84           C  
ATOM   1887  CD  GLN A 318      -3.723  37.753 -19.319  1.00 23.73           C  
ATOM   1888  OE1 GLN A 318      -4.030  37.142 -18.300  1.00 23.77           O  
ATOM   1889  NE2 GLN A 318      -2.476  37.832 -19.752  1.00 26.44           N  
ATOM   1890  N   THR A 319      -9.237  37.690 -19.649  1.00 22.93           N  
ATOM   1891  CA  THR A 319     -10.566  37.086 -19.666  1.00 27.30           C  
ATOM   1892  C   THR A 319     -11.494  37.855 -20.595  1.00 23.19           C  
ATOM   1893  O   THR A 319     -12.280  37.255 -21.337  1.00 20.30           O  
ATOM   1894  CB  THR A 319     -11.144  37.037 -18.252  1.00 17.19           C  
ATOM   1895  OG1 THR A 319     -10.354  36.156 -17.449  1.00 23.12           O  
ATOM   1896  CG2 THR A 319     -12.575  36.541 -18.259  1.00 20.84           C  
ATOM   1897  N   GLN A 320     -11.391  39.186 -20.589  1.00 27.53           N  
ATOM   1898  CA  GLN A 320     -12.273  40.015 -21.403  1.00 23.99           C  
ATOM   1899  C   GLN A 320     -11.951  39.875 -22.879  1.00 21.36           C  
ATOM   1900  O   GLN A 320     -12.851  39.962 -23.722  1.00 23.63           O  
ATOM   1901  CB  GLN A 320     -12.158  41.484 -20.978  1.00 26.23           C  
ATOM   1902  CG  GLN A 320     -13.258  42.359 -21.521  1.00 27.19           C  
ATOM   1903  CD  GLN A 320     -14.619  41.911 -21.045  1.00 21.99           C  
ATOM   1904  OE1 GLN A 320     -14.824  41.675 -19.858  1.00 19.71           O  
ATOM   1905  NE2 GLN A 320     -15.552  41.767 -21.974  1.00 26.82           N  
ATOM   1906  N   VAL A 321     -10.679  39.667 -23.215  1.00 20.80           N  
ATOM   1907  CA  VAL A 321     -10.350  39.307 -24.592  1.00 20.90           C  
ATOM   1908  C   VAL A 321     -11.153  38.085 -25.003  1.00 24.71           C  
ATOM   1909  O   VAL A 321     -11.681  38.009 -26.118  1.00 21.13           O  
ATOM   1910  CB  VAL A 321      -8.840  39.051 -24.749  1.00 31.42           C  
ATOM   1911  CG1 VAL A 321      -8.543  38.577 -26.176  1.00 27.74           C  
ATOM   1912  CG2 VAL A 321      -8.039  40.305 -24.411  1.00 24.91           C  
ATOM   1913  N   VAL A 322     -11.249  37.101 -24.106  1.00 27.30           N  
ATOM   1914  CA  VAL A 322     -11.999  35.890 -24.456  1.00 19.37           C  
ATOM   1915  C   VAL A 322     -13.493  36.185 -24.552  1.00 20.34           C  
ATOM   1916  O   VAL A 322     -14.185  35.688 -25.451  1.00 18.17           O  
ATOM   1917  CB  VAL A 322     -11.719  34.759 -23.447  1.00 20.17           C  
ATOM   1918  CG1 VAL A 322     -12.799  33.683 -23.539  1.00 20.59           C  
ATOM   1919  CG2 VAL A 322     -10.349  34.144 -23.705  1.00 17.84           C  
ATOM   1920  N   LEU A 323     -14.024  36.951 -23.605  1.00 21.21           N  
ATOM   1921  CA  LEU A 323     -15.455  37.241 -23.606  1.00 19.13           C  
ATOM   1922  C   LEU A 323     -15.872  38.047 -24.829  1.00 21.46           C  
ATOM   1923  O   LEU A 323     -17.006  37.908 -25.298  1.00 19.42           O  
ATOM   1924  CB  LEU A 323     -15.839  37.986 -22.334  1.00 25.36           C  
ATOM   1925  CG  LEU A 323     -15.803  37.144 -21.063  1.00 19.51           C  
ATOM   1926  CD1 LEU A 323     -15.864  38.045 -19.849  1.00 35.63           C  
ATOM   1927  CD2 LEU A 323     -16.955  36.154 -21.043  1.00 28.21           C  
ATOM   1928  N   ASN A 324     -14.973  38.876 -25.368  1.00 26.46           N  
ATOM   1929  CA  ASN A 324     -15.293  39.713 -26.525  1.00 21.59           C  
ATOM   1930  C   ASN A 324     -15.408  38.918 -27.814  1.00 26.18           C  
ATOM   1931  O   ASN A 324     -15.825  39.482 -28.831  1.00 23.62           O  
ATOM   1932  CB  ASN A 324     -14.231  40.805 -26.718  1.00 25.63           C  
ATOM   1933  CG  ASN A 324     -14.264  41.869 -25.628  1.00 27.23           C  
ATOM   1934  OD1 ASN A 324     -15.270  42.045 -24.937  1.00 24.30           O  
ATOM   1935  ND2 ASN A 324     -13.155  42.588 -25.475  1.00 27.22           N  
ATOM   1936  N   CYS A 325     -15.016  37.643 -27.817  1.00 31.63           N  
ATOM   1937  CA  CYS A 325     -15.251  36.778 -28.964  1.00 27.06           C  
ATOM   1938  C   CYS A 325     -16.551  35.999 -28.840  1.00 23.83           C  
ATOM   1939  O   CYS A 325     -16.731  34.997 -29.541  1.00 30.16           O  
ATOM   1940  CB  CYS A 325     -14.088  35.811 -29.157  1.00 27.69           C  
ATOM   1941  SG  CYS A 325     -12.481  36.591 -29.334  1.00 31.54           S  
ATOM   1942  N   ASP A 326     -17.453  36.433 -27.959  1.00 26.19           N  
ATOM   1943  CA  ASP A 326     -18.756  35.798 -27.787  1.00 29.14           C  
ATOM   1944  C   ASP A 326     -18.608  34.385 -27.224  1.00 20.34           C  
ATOM   1945  O   ASP A 326     -19.316  33.464 -27.624  1.00 22.21           O  
ATOM   1946  CB  ASP A 326     -19.534  35.778 -29.107  1.00 31.39           C  
ATOM   1947  CG  ASP A 326     -21.046  35.818 -28.905  1.00 31.70           C  
ATOM   1948  OD1 ASP A 326     -21.496  36.011 -27.754  1.00 45.27           O  
ATOM   1949  OD2 ASP A 326     -21.782  35.653 -29.900  1.00 39.45           O  
ATOM   1950  N   ALA A 327     -17.680  34.215 -26.286  1.00 24.82           N  
ATOM   1951  CA  ALA A 327     -17.416  32.888 -25.741  1.00 19.06           C  
ATOM   1952  C   ALA A 327     -18.661  32.306 -25.096  1.00 14.84           C  
ATOM   1953  O   ALA A 327     -19.009  31.138 -25.319  1.00 16.37           O  
ATOM   1954  CB  ALA A 327     -16.284  32.958 -24.722  1.00 23.78           C  
ATOM   1955  N   LEU A 328     -19.347  33.105 -24.279  1.00 15.96           N  
ATOM   1956  CA  LEU A 328     -20.451  32.571 -23.492  1.00 20.24           C  
ATOM   1957  C   LEU A 328     -21.578  32.038 -24.360  1.00 13.39           C  
ATOM   1958  O   LEU A 328     -22.361  31.212 -23.888  1.00 16.05           O  
ATOM   1959  CB  LEU A 328     -20.976  33.643 -22.541  1.00 18.38           C  
ATOM   1960  CG  LEU A 328     -19.987  34.099 -21.458  1.00 21.72           C  
ATOM   1961  CD1 LEU A 328     -20.623  35.169 -20.567  1.00 24.99           C  
ATOM   1962  CD2 LEU A 328     -19.500  32.943 -20.598  1.00 30.20           C  
ATOM   1963  N   SER A 329     -21.656  32.474 -25.618  1.00 16.90           N  
ATOM   1964  CA  SER A 329     -22.655  31.974 -26.558  1.00 22.86           C  
ATOM   1965  C   SER A 329     -22.560  30.469 -26.737  1.00 21.09           C  
ATOM   1966  O   SER A 329     -23.556  29.815 -27.058  1.00 16.89           O  
ATOM   1967  CB  SER A 329     -22.472  32.651 -27.921  1.00 24.77           C  
ATOM   1968  OG  SER A 329     -23.133  33.899 -27.960  1.00 53.68           O  
ATOM   1969  N   HIS A 330     -21.369  29.906 -26.572  1.00 23.26           N  
ATOM   1970  CA  HIS A 330     -21.147  28.502 -26.874  1.00 17.02           C  
ATOM   1971  C   HIS A 330     -21.458  27.580 -25.705  1.00 11.98           C  
ATOM   1972  O   HIS A 330     -21.352  26.361 -25.859  1.00 17.39           O  
ATOM   1973  CB  HIS A 330     -19.694  28.302 -27.326  1.00 13.85           C  
ATOM   1974  CG  HIS A 330     -19.321  29.120 -28.518  1.00 13.58           C  
ATOM   1975  ND1 HIS A 330     -19.616  28.732 -29.805  1.00 17.30           N  
ATOM   1976  CD2 HIS A 330     -18.689  30.311 -28.619  1.00 19.10           C  
ATOM   1977  CE1 HIS A 330     -19.175  29.645 -30.650  1.00 16.94           C  
ATOM   1978  NE2 HIS A 330     -18.608  30.613 -29.956  1.00 17.19           N  
ATOM   1979  N   PHE A 331     -21.856  28.118 -24.550  1.00 13.00           N  
ATOM   1980  CA  PHE A 331     -21.900  27.298 -23.342  1.00 13.33           C  
ATOM   1981  C   PHE A 331     -23.219  26.566 -23.084  1.00 17.20           C  
ATOM   1982  O   PHE A 331     -23.197  25.504 -22.443  1.00 16.18           O  
ATOM   1983  CB  PHE A 331     -21.503  28.163 -22.142  1.00 12.04           C  
ATOM   1984  CG  PHE A 331     -20.016  28.229 -21.961  1.00 10.84           C  
ATOM   1985  CD1 PHE A 331     -19.243  29.022 -22.792  1.00 13.83           C  
ATOM   1986  CD2 PHE A 331     -19.383  27.419 -21.034  1.00 11.23           C  
ATOM   1987  CE1 PHE A 331     -17.870  29.045 -22.667  1.00 21.10           C  
ATOM   1988  CE2 PHE A 331     -18.013  27.443 -20.897  1.00 13.68           C  
ATOM   1989  CZ  PHE A 331     -17.252  28.255 -21.722  1.00 16.82           C  
ATOM   1990  N   PRO A 332     -24.373  27.046 -23.559  1.00 15.39           N  
ATOM   1991  CA  PRO A 332     -25.588  26.227 -23.406  1.00 18.74           C  
ATOM   1992  C   PRO A 332     -25.392  24.796 -23.887  1.00 18.18           C  
ATOM   1993  O   PRO A 332     -25.743  23.845 -23.177  1.00 18.30           O  
ATOM   1994  CB  PRO A 332     -26.626  26.993 -24.240  1.00 18.80           C  
ATOM   1995  CG  PRO A 332     -26.174  28.396 -24.200  1.00 13.36           C  
ATOM   1996  CD  PRO A 332     -24.671  28.336 -24.212  1.00 18.97           C  
ATOM   1997  N   ALA A 333     -24.825  24.621 -25.082  1.00 14.30           N  
ATOM   1998  CA  ALA A 333     -24.564  23.295 -25.624  1.00 14.14           C  
ATOM   1999  C   ALA A 333     -23.505  22.527 -24.845  1.00 16.42           C  
ATOM   2000  O   ALA A 333     -23.365  21.319 -25.065  1.00 16.91           O  
ATOM   2001  CB  ALA A 333     -24.130  23.406 -27.079  1.00 18.83           C  
ATOM   2002  N   LEU A 334     -22.749  23.186 -23.963  1.00 11.59           N  
ATOM   2003  CA  LEU A 334     -21.773  22.501 -23.119  1.00 14.96           C  
ATOM   2004  C   LEU A 334     -22.321  22.185 -21.737  1.00 15.97           C  
ATOM   2005  O   LEU A 334     -21.996  21.135 -21.174  1.00 13.79           O  
ATOM   2006  CB  LEU A 334     -20.503  23.342 -22.971  1.00 14.07           C  
ATOM   2007  CG  LEU A 334     -19.806  23.730 -24.277  1.00 14.15           C  
ATOM   2008  CD1 LEU A 334     -18.627  24.641 -24.010  1.00 14.17           C  
ATOM   2009  CD2 LEU A 334     -19.355  22.497 -25.041  1.00 10.52           C  
ATOM   2010  N   LEU A 335     -23.153  23.072 -21.184  1.00 14.65           N  
ATOM   2011  CA  LEU A 335     -23.770  22.807 -19.890  1.00 15.72           C  
ATOM   2012  C   LEU A 335     -24.820  21.706 -19.968  1.00 17.27           C  
ATOM   2013  O   LEU A 335     -25.093  21.046 -18.957  1.00 16.00           O  
ATOM   2014  CB  LEU A 335     -24.397  24.085 -19.346  1.00 13.65           C  
ATOM   2015  CG  LEU A 335     -23.432  25.235 -19.090  1.00 13.57           C  
ATOM   2016  CD1 LEU A 335     -24.178  26.449 -18.579  1.00 20.80           C  
ATOM   2017  CD2 LEU A 335     -22.351  24.841 -18.104  1.00 13.21           C  
ATOM   2018  N   THR A 336     -25.443  21.522 -21.134  1.00 16.24           N  
ATOM   2019  CA  THR A 336     -26.412  20.453 -21.357  1.00 14.29           C  
ATOM   2020  C   THR A 336     -25.809  19.239 -22.043  1.00 20.26           C  
ATOM   2021  O   THR A 336     -26.541  18.294 -22.351  1.00 19.95           O  
ATOM   2022  CB  THR A 336     -27.582  20.946 -22.214  1.00 19.73           C  
ATOM   2023  OG1 THR A 336     -27.082  21.678 -23.339  1.00 18.20           O  
ATOM   2024  CG2 THR A 336     -28.502  21.808 -21.405  1.00 26.48           C  
ATOM   2025  N   HIS A 337     -24.510  19.243 -22.298  1.00 16.30           N  
ATOM   2026  CA  HIS A 337     -23.912  18.127 -23.005  1.00 17.34           C  
ATOM   2027  C   HIS A 337     -24.208  16.838 -22.244  1.00 15.39           C  
ATOM   2028  O   HIS A 337     -24.256  16.850 -21.015  1.00 16.53           O  
ATOM   2029  CB  HIS A 337     -22.405  18.322 -23.134  1.00 14.22           C  
ATOM   2030  CG  HIS A 337     -21.814  17.641 -24.322  1.00 13.84           C  
ATOM   2031  ND1 HIS A 337     -21.591  16.283 -24.370  1.00 11.03           N  
ATOM   2032  CD2 HIS A 337     -21.387  18.137 -25.506  1.00 17.98           C  
ATOM   2033  CE1 HIS A 337     -21.068  15.968 -25.543  1.00 12.58           C  
ATOM   2034  NE2 HIS A 337     -20.930  17.077 -26.249  1.00 15.90           N  
ATOM   2035  N   PRO A 338     -24.430  15.724 -22.942  1.00 19.82           N  
ATOM   2036  CA  PRO A 338     -24.579  14.434 -22.249  1.00 17.45           C  
ATOM   2037  C   PRO A 338     -23.378  14.024 -21.408  1.00 15.95           C  
ATOM   2038  O   PRO A 338     -23.551  13.282 -20.437  1.00 13.19           O  
ATOM   2039  CB  PRO A 338     -24.785  13.449 -23.406  1.00 18.83           C  
ATOM   2040  CG  PRO A 338     -25.265  14.263 -24.531  1.00 19.23           C  
ATOM   2041  CD  PRO A 338     -24.699  15.615 -24.384  1.00 13.48           C  
ATOM   2042  N   LYS A 339     -22.163  14.425 -21.776  1.00 15.36           N  
ATOM   2043  CA  LYS A 339     -20.976  13.994 -21.045  1.00 17.00           C  
ATOM   2044  C   LYS A 339     -20.812  14.844 -19.794  1.00 14.51           C  
ATOM   2045  O   LYS A 339     -20.666  16.068 -19.880  1.00 20.06           O  
ATOM   2046  CB  LYS A 339     -19.727  14.092 -21.916  1.00 17.62           C  
ATOM   2047  CG  LYS A 339     -19.776  13.270 -23.192  1.00 26.44           C  
ATOM   2048  CD  LYS A 339     -19.827  11.778 -22.912  1.00 39.53           C  
ATOM   2049  CE  LYS A 339     -20.194  10.980 -24.170  1.00 50.55           C  
ATOM   2050  NZ  LYS A 339     -21.619  10.518 -24.153  1.00 39.70           N  
ATOM   2051  N   GLU A 340     -20.817  14.189 -18.636  1.00 17.80           N  
ATOM   2052  CA  GLU A 340     -20.676  14.901 -17.370  1.00 20.53           C  
ATOM   2053  C   GLU A 340     -19.327  15.593 -17.266  1.00 17.34           C  
ATOM   2054  O   GLU A 340     -19.222  16.675 -16.680  1.00 16.23           O  
ATOM   2055  CB  GLU A 340     -20.863  13.930 -16.208  1.00 27.35           C  
ATOM   2056  CG  GLU A 340     -22.215  13.254 -16.208  1.00 29.94           C  
ATOM   2057  CD  GLU A 340     -22.472  12.488 -14.937  1.00 39.82           C  
ATOM   2058  OE1 GLU A 340     -21.489  12.010 -14.327  1.00 41.14           O  
ATOM   2059  OE2 GLU A 340     -23.655  12.370 -14.550  1.00 41.52           O  
ATOM   2060  N   LYS A 341     -18.273  14.984 -17.811  1.00 17.67           N  
ATOM   2061  CA  LYS A 341     -16.967  15.633 -17.756  1.00 22.70           C  
ATOM   2062  C   LYS A 341     -17.000  16.978 -18.470  1.00 10.77           C  
ATOM   2063  O   LYS A 341     -16.396  17.949 -18.010  1.00 16.47           O  
ATOM   2064  CB  LYS A 341     -15.888  14.722 -18.349  1.00 23.46           C  
ATOM   2065  CG  LYS A 341     -15.462  13.600 -17.405  1.00 31.13           C  
ATOM   2066  CD  LYS A 341     -14.208  12.869 -17.874  1.00 52.22           C  
ATOM   2067  CE  LYS A 341     -14.491  11.914 -19.038  1.00 62.06           C  
ATOM   2068  NZ  LYS A 341     -13.388  10.915 -19.223  1.00 53.73           N  
ATOM   2069  N   ILE A 342     -17.718  17.063 -19.589  1.00 14.50           N  
ATOM   2070  CA  ILE A 342     -17.837  18.340 -20.283  1.00 12.28           C  
ATOM   2071  C   ILE A 342     -18.603  19.347 -19.431  1.00 13.48           C  
ATOM   2072  O   ILE A 342     -18.230  20.519 -19.366  1.00 13.50           O  
ATOM   2073  CB  ILE A 342     -18.493  18.144 -21.660  1.00 19.55           C  
ATOM   2074  CG1 ILE A 342     -17.486  17.506 -22.603  1.00 22.93           C  
ATOM   2075  CG2 ILE A 342     -19.001  19.477 -22.225  1.00 16.25           C  
ATOM   2076  CD1 ILE A 342     -18.060  17.072 -23.937  1.00 21.81           C  
ATOM   2077  N   ASN A 343     -19.711  18.934 -18.805  1.00 11.19           N  
ATOM   2078  CA  ASN A 343     -20.411  19.861 -17.923  1.00 12.07           C  
ATOM   2079  C   ASN A 343     -19.460  20.407 -16.866  1.00 15.17           C  
ATOM   2080  O   ASN A 343     -19.457  21.608 -16.580  1.00 13.58           O  
ATOM   2081  CB  ASN A 343     -21.600  19.192 -17.227  1.00 18.83           C  
ATOM   2082  CG  ASN A 343     -22.495  18.394 -18.166  1.00 14.25           C  
ATOM   2083  OD1 ASN A 343     -23.087  17.402 -17.742  1.00 18.20           O  
ATOM   2084  ND2 ASN A 343     -22.613  18.816 -19.424  1.00 14.14           N  
ATOM   2085  N   LYS A 344     -18.644  19.527 -16.278  1.00 15.30           N  
ATOM   2086  CA  LYS A 344     -17.744  19.925 -15.202  1.00 14.24           C  
ATOM   2087  C   LYS A 344     -16.715  20.931 -15.697  1.00 13.60           C  
ATOM   2088  O   LYS A 344     -16.445  21.942 -15.036  1.00 13.91           O  
ATOM   2089  CB  LYS A 344     -17.078  18.674 -14.629  1.00 14.57           C  
ATOM   2090  CG  LYS A 344     -15.965  18.913 -13.646  1.00 18.82           C  
ATOM   2091  CD  LYS A 344     -15.538  17.580 -13.032  1.00 26.03           C  
ATOM   2092  CE  LYS A 344     -14.197  17.666 -12.327  1.00 50.55           C  
ATOM   2093  NZ  LYS A 344     -13.951  16.470 -11.462  1.00 48.07           N  
ATOM   2094  N   GLU A 345     -16.167  20.690 -16.886  1.00 11.49           N  
ATOM   2095  CA  GLU A 345     -15.164  21.592 -17.437  1.00 12.41           C  
ATOM   2096  C   GLU A 345     -15.775  22.931 -17.837  1.00 11.00           C  
ATOM   2097  O   GLU A 345     -15.173  23.994 -17.614  1.00 14.73           O  
ATOM   2098  CB  GLU A 345     -14.488  20.900 -18.620  1.00 15.43           C  
ATOM   2099  CG  GLU A 345     -13.597  19.719 -18.183  1.00 20.58           C  
ATOM   2100  CD  GLU A 345     -13.390  18.662 -19.261  1.00 19.25           C  
ATOM   2101  OE1 GLU A 345     -12.791  17.604 -18.953  1.00 19.68           O  
ATOM   2102  OE2 GLU A 345     -13.818  18.888 -20.411  1.00 21.61           O  
ATOM   2103  N   ALA A 346     -16.976  22.908 -18.415  1.00 11.73           N  
ATOM   2104  CA  ALA A 346     -17.667  24.146 -18.747  1.00 11.59           C  
ATOM   2105  C   ALA A 346     -17.967  24.969 -17.500  1.00 10.40           C  
ATOM   2106  O   ALA A 346     -17.795  26.195 -17.499  1.00 12.09           O  
ATOM   2107  CB  ALA A 346     -18.959  23.833 -19.503  1.00 15.47           C  
ATOM   2108  N   VAL A 347     -18.435  24.317 -16.433  1.00  8.11           N  
ATOM   2109  CA  VAL A 347     -18.730  25.038 -15.199  1.00 13.88           C  
ATOM   2110  C   VAL A 347     -17.451  25.565 -14.556  1.00 16.09           C  
ATOM   2111  O   VAL A 347     -17.462  26.618 -13.921  1.00 15.78           O  
ATOM   2112  CB  VAL A 347     -19.518  24.136 -14.238  1.00 17.44           C  
ATOM   2113  CG1 VAL A 347     -19.681  24.800 -12.895  1.00 17.30           C  
ATOM   2114  CG2 VAL A 347     -20.886  23.810 -14.832  1.00 21.91           C  
ATOM   2115  N   TRP A 348     -16.328  24.861 -14.709  1.00 18.04           N  
ATOM   2116  CA  TRP A 348     -15.057  25.409 -14.241  1.00 14.92           C  
ATOM   2117  C   TRP A 348     -14.743  26.714 -14.964  1.00 16.38           C  
ATOM   2118  O   TRP A 348     -14.429  27.739 -14.338  1.00 15.63           O  
ATOM   2119  CB  TRP A 348     -13.949  24.370 -14.444  1.00 14.25           C  
ATOM   2120  CG  TRP A 348     -12.557  24.907 -14.413  1.00 13.13           C  
ATOM   2121  CD1 TRP A 348     -11.854  25.311 -13.314  1.00 10.81           C  
ATOM   2122  CD2 TRP A 348     -11.674  25.062 -15.530  1.00 13.54           C  
ATOM   2123  NE1 TRP A 348     -10.600  25.718 -13.679  1.00 12.31           N  
ATOM   2124  CE2 TRP A 348     -10.463  25.578 -15.032  1.00 12.36           C  
ATOM   2125  CE3 TRP A 348     -11.790  24.818 -16.901  1.00 15.41           C  
ATOM   2126  CZ2 TRP A 348      -9.384  25.863 -15.850  1.00 11.70           C  
ATOM   2127  CZ3 TRP A 348     -10.706  25.104 -17.717  1.00 11.79           C  
ATOM   2128  CH2 TRP A 348      -9.519  25.621 -17.182  1.00 13.98           C  
ATOM   2129  N   PHE A 349     -14.827  26.687 -16.296  1.00 13.77           N  
ATOM   2130  CA  PHE A 349     -14.663  27.904 -17.087  1.00 12.53           C  
ATOM   2131  C   PHE A 349     -15.565  29.017 -16.554  1.00 15.55           C  
ATOM   2132  O   PHE A 349     -15.121  30.142 -16.282  1.00 17.14           O  
ATOM   2133  CB  PHE A 349     -14.979  27.589 -18.556  1.00 13.25           C  
ATOM   2134  CG  PHE A 349     -14.830  28.762 -19.497  1.00 15.97           C  
ATOM   2135  CD1 PHE A 349     -15.757  29.795 -19.499  1.00 18.41           C  
ATOM   2136  CD2 PHE A 349     -13.784  28.809 -20.410  1.00 19.70           C  
ATOM   2137  CE1 PHE A 349     -15.630  30.860 -20.373  1.00 18.57           C  
ATOM   2138  CE2 PHE A 349     -13.655  29.881 -21.280  1.00 26.09           C  
ATOM   2139  CZ  PHE A 349     -14.576  30.898 -21.266  1.00 16.31           C  
ATOM   2140  N   LEU A 350     -16.851  28.718 -16.407  1.00 13.42           N  
ATOM   2141  CA  LEU A 350     -17.786  29.756 -15.994  1.00 18.22           C  
ATOM   2142  C   LEU A 350     -17.469  30.268 -14.595  1.00 15.95           C  
ATOM   2143  O   LEU A 350     -17.638  31.459 -14.332  1.00 17.47           O  
ATOM   2144  CB  LEU A 350     -19.221  29.230 -16.083  1.00 11.69           C  
ATOM   2145  CG  LEU A 350     -19.710  28.947 -17.507  1.00  9.90           C  
ATOM   2146  CD1 LEU A 350     -21.114  28.354 -17.498  1.00 14.10           C  
ATOM   2147  CD2 LEU A 350     -19.682  30.203 -18.371  1.00 20.38           C  
ATOM   2148  N   SER A 351     -16.987  29.401 -13.698  1.00 17.42           N  
ATOM   2149  CA  SER A 351     -16.608  29.851 -12.365  1.00 16.49           C  
ATOM   2150  C   SER A 351     -15.417  30.788 -12.432  1.00 21.40           C  
ATOM   2151  O   SER A 351     -15.275  31.676 -11.586  1.00 22.82           O  
ATOM   2152  CB  SER A 351     -16.293  28.655 -11.462  1.00 16.88           C  
ATOM   2153  OG  SER A 351     -14.982  28.180 -11.678  1.00 15.85           O  
ATOM   2154  N   ASN A 352     -14.548  30.605 -13.426  1.00 18.04           N  
ATOM   2155  CA  ASN A 352     -13.460  31.555 -13.609  1.00 16.72           C  
ATOM   2156  C   ASN A 352     -13.949  32.849 -14.234  1.00 22.30           C  
ATOM   2157  O   ASN A 352     -13.252  33.866 -14.164  1.00 20.56           O  
ATOM   2158  CB  ASN A 352     -12.350  30.948 -14.465  1.00 16.90           C  
ATOM   2159  CG  ASN A 352     -11.467  30.004 -13.681  1.00 19.94           C  
ATOM   2160  OD1 ASN A 352     -11.241  30.206 -12.491  1.00 21.31           O  
ATOM   2161  ND2 ASN A 352     -10.970  28.960 -14.339  1.00 18.38           N  
ATOM   2162  N   ILE A 353     -15.114  32.830 -14.873  1.00 26.62           N  
ATOM   2163  CA  ILE A 353     -15.697  34.091 -15.332  1.00 21.31           C  
ATOM   2164  C   ILE A 353     -16.377  34.824 -14.175  1.00 23.22           C  
ATOM   2165  O   ILE A 353     -16.194  36.033 -13.990  1.00 16.27           O  
ATOM   2166  CB  ILE A 353     -16.672  33.847 -16.496  1.00 18.85           C  
ATOM   2167  CG1 ILE A 353     -15.970  33.124 -17.649  1.00 21.94           C  
ATOM   2168  CG2 ILE A 353     -17.248  35.173 -16.990  1.00 17.70           C  
ATOM   2169  CD1 ILE A 353     -14.806  33.882 -18.270  1.00 17.43           C  
ATOM   2170  N   THR A 354     -17.167  34.111 -13.372  1.00 19.76           N  
ATOM   2171  CA  THR A 354     -17.911  34.770 -12.303  1.00 22.73           C  
ATOM   2172  C   THR A 354     -17.006  35.297 -11.200  1.00 31.54           C  
ATOM   2173  O   THR A 354     -17.488  36.026 -10.326  1.00 19.70           O  
ATOM   2174  CB  THR A 354     -18.941  33.823 -11.689  1.00 21.51           C  
ATOM   2175  OG1 THR A 354     -18.286  32.646 -11.188  1.00 27.83           O  
ATOM   2176  CG2 THR A 354     -20.005  33.442 -12.715  1.00 17.15           C  
ATOM   2177  N   ALA A 355     -15.720  34.943 -11.219  1.00 23.46           N  
ATOM   2178  CA  ALA A 355     -14.755  35.470 -10.265  1.00 26.27           C  
ATOM   2179  C   ALA A 355     -14.165  36.800 -10.705  1.00 19.25           C  
ATOM   2180  O   ALA A 355     -13.297  37.325 -10.009  1.00 28.24           O  
ATOM   2181  CB  ALA A 355     -13.623  34.463 -10.043  1.00 22.03           C  
ATOM   2182  N   GLY A 356     -14.602  37.351 -11.828  1.00 25.32           N  
ATOM   2183  CA  GLY A 356     -14.134  38.637 -12.296  1.00 25.57           C  
ATOM   2184  C   GLY A 356     -15.003  39.776 -11.806  1.00 27.68           C  
ATOM   2185  O   GLY A 356     -15.770  39.648 -10.848  1.00 24.29           O  
ATOM   2186  N   ASN A 357     -14.890  40.906 -12.501  1.00 35.07           N  
ATOM   2187  CA  ASN A 357     -15.551  42.140 -12.102  1.00 33.81           C  
ATOM   2188  C   ASN A 357     -17.051  42.057 -12.385  1.00 30.74           C  
ATOM   2189  O   ASN A 357     -17.558  41.079 -12.944  1.00 36.70           O  
ATOM   2190  CB  ASN A 357     -14.927  43.328 -12.831  1.00 38.08           C  
ATOM   2191  CG  ASN A 357     -15.103  43.252 -14.340  1.00 34.92           C  
ATOM   2192  OD1 ASN A 357     -16.214  43.094 -14.844  1.00 34.53           O  
ATOM   2193  ND2 ASN A 357     -14.000  43.370 -15.068  1.00 34.86           N  
ATOM   2194  N   GLN A 358     -17.761  43.128 -12.012  1.00 37.12           N  
ATOM   2195  CA  GLN A 358     -19.219  43.152 -12.117  1.00 31.24           C  
ATOM   2196  C   GLN A 358     -19.674  42.974 -13.555  1.00 23.88           C  
ATOM   2197  O   GLN A 358     -20.724  42.382 -13.808  1.00 26.34           O  
ATOM   2198  CB  GLN A 358     -19.794  44.471 -11.599  1.00 35.36           C  
ATOM   2199  CG  GLN A 358     -19.184  45.077 -10.369  1.00 50.56           C  
ATOM   2200  CD  GLN A 358     -19.429  46.573 -10.327  1.00 49.71           C  
ATOM   2201  OE1 GLN A 358     -20.495  47.047 -10.723  1.00 42.61           O  
ATOM   2202  NE2 GLN A 358     -18.433  47.326  -9.881  1.00 64.84           N  
ATOM   2203  N   GLN A 359     -18.935  43.544 -14.504  1.00 24.92           N  
ATOM   2204  CA  GLN A 359     -19.319  43.419 -15.905  1.00 31.35           C  
ATOM   2205  C   GLN A 359     -19.237  41.973 -16.369  1.00 27.40           C  
ATOM   2206  O   GLN A 359     -20.050  41.533 -17.185  1.00 27.05           O  
ATOM   2207  CB  GLN A 359     -18.431  44.303 -16.783  1.00 32.58           C  
ATOM   2208  CG  GLN A 359     -18.714  45.791 -16.654  1.00 45.71           C  
ATOM   2209  CD  GLN A 359     -18.377  46.343 -15.281  1.00 49.65           C  
ATOM   2210  OE1 GLN A 359     -17.276  46.127 -14.759  1.00 41.63           O  
ATOM   2211  NE2 GLN A 359     -19.330  47.054 -14.686  1.00 49.56           N  
ATOM   2212  N   GLN A 360     -18.285  41.210 -15.844  1.00 22.92           N  
ATOM   2213  CA  GLN A 360     -18.134  39.831 -16.287  1.00 27.24           C  
ATOM   2214  C   GLN A 360     -19.150  38.922 -15.609  1.00 20.72           C  
ATOM   2215  O   GLN A 360     -19.702  38.010 -16.246  1.00 22.84           O  
ATOM   2216  CB  GLN A 360     -16.698  39.384 -16.030  1.00 25.48           C  
ATOM   2217  CG  GLN A 360     -15.713  40.114 -16.935  1.00 22.49           C  
ATOM   2218  CD  GLN A 360     -14.279  39.881 -16.559  1.00 25.54           C  
ATOM   2219  OE1 GLN A 360     -13.980  39.367 -15.481  1.00 30.67           O  
ATOM   2220  NE2 GLN A 360     -13.374  40.263 -17.443  1.00 22.36           N  
ATOM   2221  N   VAL A 361     -19.436  39.179 -14.330  1.00 20.82           N  
ATOM   2222  CA  VAL A 361     -20.604  38.578 -13.686  1.00 24.99           C  
ATOM   2223  C   VAL A 361     -21.850  38.836 -14.526  1.00 29.69           C  
ATOM   2224  O   VAL A 361     -22.650  37.928 -14.800  1.00 24.88           O  
ATOM   2225  CB  VAL A 361     -20.769  39.134 -12.259  1.00 28.85           C  
ATOM   2226  CG1 VAL A 361     -22.084  38.644 -11.628  1.00 32.79           C  
ATOM   2227  CG2 VAL A 361     -19.578  38.750 -11.387  1.00 25.88           C  
ATOM   2228  N   GLN A 362     -22.033  40.091 -14.944  1.00 29.02           N  
ATOM   2229  CA  GLN A 362     -23.213  40.453 -15.714  1.00 30.69           C  
ATOM   2230  C   GLN A 362     -23.214  39.768 -17.065  1.00 28.39           C  
ATOM   2231  O   GLN A 362     -24.280  39.440 -17.583  1.00 25.09           O  
ATOM   2232  CB  GLN A 362     -23.290  41.971 -15.901  1.00 36.38           C  
ATOM   2233  CG  GLN A 362     -24.668  42.465 -16.303  1.00 23.75           C  
ATOM   2234  CD  GLN A 362     -25.692  42.215 -15.226  1.00 22.84           C  
ATOM   2235  OE1 GLN A 362     -25.410  42.383 -14.039  1.00 34.09           O  
ATOM   2236  NE2 GLN A 362     -26.882  41.793 -15.627  1.00 24.36           N  
ATOM   2237  N   ALA A 363     -22.041  39.574 -17.665  1.00 24.88           N  
ATOM   2238  CA  ALA A 363     -21.969  38.813 -18.905  1.00 23.23           C  
ATOM   2239  C   ALA A 363     -22.533  37.418 -18.698  1.00 19.66           C  
ATOM   2240  O   ALA A 363     -23.346  36.935 -19.491  1.00 21.51           O  
ATOM   2241  CB  ALA A 363     -20.527  38.745 -19.402  1.00 23.91           C  
ATOM   2242  N   VAL A 364     -22.136  36.764 -17.610  1.00 24.28           N  
ATOM   2243  CA  VAL A 364     -22.680  35.438 -17.327  1.00 23.11           C  
ATOM   2244  C   VAL A 364     -24.198  35.505 -17.175  1.00 27.35           C  
ATOM   2245  O   VAL A 364     -24.930  34.646 -17.688  1.00 23.98           O  
ATOM   2246  CB  VAL A 364     -22.008  34.842 -16.079  1.00 18.67           C  
ATOM   2247  CG1 VAL A 364     -22.629  33.484 -15.732  1.00 24.40           C  
ATOM   2248  CG2 VAL A 364     -20.518  34.702 -16.298  1.00 22.66           C  
ATOM   2249  N   ILE A 365     -24.693  36.521 -16.462  1.00 27.51           N  
ATOM   2250  CA  ILE A 365     -26.136  36.641 -16.224  1.00 30.43           C  
ATOM   2251  C   ILE A 365     -26.884  36.877 -17.536  1.00 24.32           C  
ATOM   2252  O   ILE A 365     -27.910  36.246 -17.813  1.00 23.63           O  
ATOM   2253  CB  ILE A 365     -26.418  37.765 -15.209  1.00 32.31           C  
ATOM   2254  CG1 ILE A 365     -25.979  37.347 -13.804  1.00 32.33           C  
ATOM   2255  CG2 ILE A 365     -27.896  38.113 -15.182  1.00 28.31           C  
ATOM   2256  CD1 ILE A 365     -25.911  38.491 -12.815  1.00 31.77           C  
ATOM   2257  N   ASP A 366     -26.391  37.812 -18.349  1.00 24.01           N  
ATOM   2258  CA  ASP A 366     -27.033  38.193 -19.600  1.00 24.83           C  
ATOM   2259  C   ASP A 366     -27.042  37.063 -20.614  1.00 25.93           C  
ATOM   2260  O   ASP A 366     -27.817  37.108 -21.575  1.00 30.44           O  
ATOM   2261  CB  ASP A 366     -26.309  39.402 -20.203  1.00 31.13           C  
ATOM   2262  CG  ASP A 366     -26.510  40.688 -19.394  1.00 34.77           C  
ATOM   2263  OD1 ASP A 366     -27.404  40.726 -18.519  1.00 29.80           O  
ATOM   2264  OD2 ASP A 366     -25.764  41.665 -19.637  1.00 37.44           O  
ATOM   2265  N   ALA A 367     -26.192  36.063 -20.439  1.00 29.48           N  
ATOM   2266  CA  ALA A 367     -26.146  34.940 -21.354  1.00 25.80           C  
ATOM   2267  C   ALA A 367     -27.140  33.852 -20.984  1.00 23.97           C  
ATOM   2268  O   ALA A 367     -27.158  32.804 -21.631  1.00 27.21           O  
ATOM   2269  CB  ALA A 367     -24.733  34.368 -21.400  1.00 27.21           C  
ATOM   2270  N   ASN A 368     -27.967  34.085 -19.968  1.00 20.50           N  
ATOM   2271  CA  ASN A 368     -28.977  33.122 -19.539  1.00 33.25           C  
ATOM   2272  C   ASN A 368     -28.334  31.809 -19.107  1.00 19.90           C  
ATOM   2273  O   ASN A 368     -28.879  30.728 -19.333  1.00 29.13           O  
ATOM   2274  CB  ASN A 368     -30.016  32.881 -20.637  1.00 31.82           C  
ATOM   2275  CG  ASN A 368     -30.755  34.139 -21.026  1.00 38.10           C  
ATOM   2276  OD1 ASN A 368     -31.303  34.841 -20.175  1.00 46.51           O  
ATOM   2277  ND2 ASN A 368     -30.771  34.438 -22.322  1.00 48.03           N  
ATOM   2278  N   LEU A 369     -27.182  31.898 -18.447  1.00 20.30           N  
ATOM   2279  CA  LEU A 369     -26.479  30.698 -18.019  1.00 17.65           C  
ATOM   2280  C   LEU A 369     -26.721  30.348 -16.559  1.00 18.86           C  
ATOM   2281  O   LEU A 369     -26.555  29.181 -16.188  1.00 17.66           O  
ATOM   2282  CB  LEU A 369     -24.974  30.855 -18.258  1.00 20.97           C  
ATOM   2283  CG  LEU A 369     -24.555  31.063 -19.718  1.00 15.94           C  
ATOM   2284  CD1 LEU A 369     -23.064  31.351 -19.816  1.00 18.04           C  
ATOM   2285  CD2 LEU A 369     -24.908  29.855 -20.558  1.00 22.48           C  
ATOM   2286  N   VAL A 370     -27.151  31.306 -15.734  1.00 20.73           N  
ATOM   2287  CA  VAL A 370     -27.259  31.046 -14.297  1.00 20.69           C  
ATOM   2288  C   VAL A 370     -28.249  29.932 -14.001  1.00 18.91           C  
ATOM   2289  O   VAL A 370     -27.958  29.093 -13.139  1.00 23.77           O  
ATOM   2290  CB  VAL A 370     -27.576  32.345 -13.547  1.00 21.90           C  
ATOM   2291  CG1 VAL A 370     -27.975  32.050 -12.107  1.00 25.80           C  
ATOM   2292  CG2 VAL A 370     -26.377  33.258 -13.575  1.00 18.89           C  
ATOM   2293  N   PRO A 371     -29.425  29.869 -14.624  1.00 15.82           N  
ATOM   2294  CA  PRO A 371     -30.336  28.765 -14.293  1.00 17.73           C  
ATOM   2295  C   PRO A 371     -29.740  27.412 -14.606  1.00 17.22           C  
ATOM   2296  O   PRO A 371     -29.962  26.454 -13.859  1.00 21.62           O  
ATOM   2297  CB  PRO A 371     -31.581  29.074 -15.136  1.00 19.31           C  
ATOM   2298  CG  PRO A 371     -31.514  30.565 -15.342  1.00 19.77           C  
ATOM   2299  CD  PRO A 371     -30.062  30.869 -15.494  1.00 21.63           C  
ATOM   2300  N   MET A 372     -28.972  27.311 -15.690  1.00 16.47           N  
ATOM   2301  CA  MET A 372     -28.290  26.061 -16.010  1.00 17.89           C  
ATOM   2302  C   MET A 372     -27.228  25.724 -14.963  1.00 17.83           C  
ATOM   2303  O   MET A 372     -27.085  24.563 -14.562  1.00 17.72           O  
ATOM   2304  CB  MET A 372     -27.650  26.161 -17.394  1.00 22.92           C  
ATOM   2305  CG  MET A 372     -28.580  25.858 -18.560  1.00 24.96           C  
ATOM   2306  SD  MET A 372     -27.994  26.615 -20.112  1.00 32.53           S  
ATOM   2307  CE  MET A 372     -28.237  25.272 -21.243  1.00 37.11           C  
ATOM   2308  N   ILE A 373     -26.459  26.726 -14.528  1.00 13.42           N  
ATOM   2309  CA  ILE A 373     -25.486  26.517 -13.458  1.00 22.65           C  
ATOM   2310  C   ILE A 373     -26.180  26.027 -12.194  1.00 18.49           C  
ATOM   2311  O   ILE A 373     -25.686  25.127 -11.508  1.00 19.23           O  
ATOM   2312  CB  ILE A 373     -24.688  27.812 -13.198  1.00 17.26           C  
ATOM   2313  CG1 ILE A 373     -23.819  28.157 -14.410  1.00 17.84           C  
ATOM   2314  CG2 ILE A 373     -23.817  27.660 -11.968  1.00 20.97           C  
ATOM   2315  CD1 ILE A 373     -23.074  29.484 -14.300  1.00 23.51           C  
ATOM   2316  N   ILE A 374     -27.332  26.614 -11.863  1.00 19.37           N  
ATOM   2317  CA  ILE A 374     -28.037  26.254 -10.636  1.00 18.68           C  
ATOM   2318  C   ILE A 374     -28.645  24.866 -10.758  1.00 18.70           C  
ATOM   2319  O   ILE A 374     -28.701  24.103  -9.784  1.00 20.08           O  
ATOM   2320  CB  ILE A 374     -29.101  27.320 -10.320  1.00 18.07           C  
ATOM   2321  CG1 ILE A 374     -28.410  28.626  -9.919  1.00 19.69           C  
ATOM   2322  CG2 ILE A 374     -30.044  26.831  -9.236  1.00 21.43           C  
ATOM   2323  CD1 ILE A 374     -29.356  29.803  -9.723  1.00 23.13           C  
ATOM   2324  N   HIS A 375     -29.096  24.503 -11.958  1.00 17.23           N  
ATOM   2325  CA  HIS A 375     -29.589  23.149 -12.163  1.00 21.06           C  
ATOM   2326  C   HIS A 375     -28.469  22.132 -12.010  1.00 20.57           C  
ATOM   2327  O   HIS A 375     -28.678  21.053 -11.450  1.00 16.02           O  
ATOM   2328  CB  HIS A 375     -30.238  23.013 -13.537  1.00 17.84           C  
ATOM   2329  CG  HIS A 375     -30.475  21.594 -13.929  1.00 15.83           C  
ATOM   2330  ND1 HIS A 375     -31.585  20.886 -13.528  1.00 17.46           N  
ATOM   2331  CD2 HIS A 375     -29.719  20.734 -14.650  1.00 22.60           C  
ATOM   2332  CE1 HIS A 375     -31.513  19.656 -14.002  1.00 27.52           C  
ATOM   2333  NE2 HIS A 375     -30.388  19.535 -14.683  1.00 23.57           N  
ATOM   2334  N   LEU A 376     -27.275  22.447 -12.516  1.00 19.73           N  
ATOM   2335  CA  LEU A 376     -26.159  21.521 -12.346  1.00 17.77           C  
ATOM   2336  C   LEU A 376     -25.707  21.472 -10.890  1.00 21.71           C  
ATOM   2337  O   LEU A 376     -25.284  20.417 -10.401  1.00 17.76           O  
ATOM   2338  CB  LEU A 376     -25.001  21.916 -13.260  1.00 19.57           C  
ATOM   2339  CG  LEU A 376     -25.232  21.737 -14.763  1.00 19.39           C  
ATOM   2340  CD1 LEU A 376     -24.040  22.274 -15.552  1.00 16.85           C  
ATOM   2341  CD2 LEU A 376     -25.486  20.277 -15.102  1.00 16.64           C  
ATOM   2342  N   LEU A 377     -25.786  22.605 -10.189  1.00 16.42           N  
ATOM   2343  CA  LEU A 377     -25.508  22.629  -8.757  1.00 15.89           C  
ATOM   2344  C   LEU A 377     -26.471  21.724  -8.002  1.00 21.33           C  
ATOM   2345  O   LEU A 377     -26.086  21.078  -7.022  1.00 22.75           O  
ATOM   2346  CB  LEU A 377     -25.609  24.066  -8.239  1.00 16.11           C  
ATOM   2347  CG  LEU A 377     -25.243  24.312  -6.773  1.00 27.94           C  
ATOM   2348  CD1 LEU A 377     -23.739  24.278  -6.587  1.00 23.20           C  
ATOM   2349  CD2 LEU A 377     -25.800  25.644  -6.302  1.00 25.72           C  
ATOM   2350  N   ASP A 378     -27.731  21.665  -8.453  1.00 17.56           N  
ATOM   2351  CA  ASP A 378     -28.763  20.881  -7.772  1.00 16.79           C  
ATOM   2352  C   ASP A 378     -28.676  19.397  -8.129  1.00 27.27           C  
ATOM   2353  O   ASP A 378     -28.605  18.542  -7.237  1.00 27.57           O  
ATOM   2354  CB  ASP A 378     -30.145  21.449  -8.130  1.00 27.79           C  
ATOM   2355  CG  ASP A 378     -31.311  20.748  -7.409  1.00 36.11           C  
ATOM   2356  OD1 ASP A 378     -31.105  20.027  -6.406  1.00 33.92           O  
ATOM   2357  OD2 ASP A 378     -32.460  20.934  -7.869  1.00 38.29           O  
ATOM   2358  N   LYS A 379     -28.655  19.072  -9.427  1.00 23.31           N  
ATOM   2359  CA  LYS A 379     -28.867  17.709  -9.898  1.00 24.67           C  
ATOM   2360  C   LYS A 379     -27.661  17.096 -10.590  1.00 23.94           C  
ATOM   2361  O   LYS A 379     -27.715  15.920 -10.966  1.00 24.61           O  
ATOM   2362  CB  LYS A 379     -30.062  17.669 -10.862  1.00 28.69           C  
ATOM   2363  CG  LYS A 379     -31.412  18.043 -10.234  1.00 36.61           C  
ATOM   2364  CD  LYS A 379     -31.943  16.935  -9.326  1.00 44.15           C  
ATOM   2365  CE  LYS A 379     -33.310  17.275  -8.721  1.00 43.02           C  
ATOM   2366  NZ  LYS A 379     -34.092  18.239  -9.542  1.00 65.91           N  
ATOM   2367  N   GLY A 380     -26.580  17.835 -10.774  1.00 24.26           N  
ATOM   2368  CA  GLY A 380     -25.445  17.297 -11.486  1.00 26.43           C  
ATOM   2369  C   GLY A 380     -24.693  16.257 -10.675  1.00 23.72           C  
ATOM   2370  O   GLY A 380     -24.979  15.991  -9.509  1.00 23.33           O  
ATOM   2371  N   ASP A 381     -23.710  15.644 -11.329  1.00 22.95           N  
ATOM   2372  CA  ASP A 381     -22.771  14.785 -10.627  1.00 29.33           C  
ATOM   2373  C   ASP A 381     -21.958  15.621  -9.647  1.00 21.62           C  
ATOM   2374  O   ASP A 381     -21.874  16.844  -9.767  1.00 26.45           O  
ATOM   2375  CB  ASP A 381     -21.837  14.080 -11.611  1.00 26.39           C  
ATOM   2376  CG  ASP A 381     -21.037  15.059 -12.464  1.00 30.68           C  
ATOM   2377  OD1 ASP A 381     -21.662  15.849 -13.214  1.00 27.16           O  
ATOM   2378  OD2 ASP A 381     -19.785  15.048 -12.376  1.00 25.99           O  
ATOM   2379  N   PHE A 382     -21.337  14.945  -8.674  1.00 23.02           N  
ATOM   2380  CA  PHE A 382     -20.708  15.668  -7.570  1.00 27.18           C  
ATOM   2381  C   PHE A 382     -19.530  16.522  -8.038  1.00 22.16           C  
ATOM   2382  O   PHE A 382     -19.305  17.602  -7.484  1.00 28.67           O  
ATOM   2383  CB  PHE A 382     -20.279  14.697  -6.455  1.00 34.72           C  
ATOM   2384  CG  PHE A 382     -19.108  13.813  -6.812  1.00 52.83           C  
ATOM   2385  CD1 PHE A 382     -17.800  14.218  -6.544  1.00 44.13           C  
ATOM   2386  CD2 PHE A 382     -19.314  12.569  -7.392  1.00 53.12           C  
ATOM   2387  CE1 PHE A 382     -16.727  13.401  -6.870  1.00 43.24           C  
ATOM   2388  CE2 PHE A 382     -18.251  11.750  -7.717  1.00 36.79           C  
ATOM   2389  CZ  PHE A 382     -16.954  12.163  -7.458  1.00 58.36           C  
ATOM   2390  N   GLY A 383     -18.784  16.087  -9.058  1.00 22.26           N  
ATOM   2391  CA  GLY A 383     -17.701  16.920  -9.581  1.00 20.00           C  
ATOM   2392  C   GLY A 383     -18.206  18.208 -10.207  1.00 21.79           C  
ATOM   2393  O   GLY A 383     -17.682  19.306  -9.951  1.00 23.41           O  
ATOM   2394  N   THR A 384     -19.250  18.097 -11.025  1.00 22.60           N  
ATOM   2395  CA  THR A 384     -19.866  19.291 -11.577  1.00 17.45           C  
ATOM   2396  C   THR A 384     -20.479  20.139 -10.476  1.00 12.49           C  
ATOM   2397  O   THR A 384     -20.409  21.367 -10.530  1.00 18.64           O  
ATOM   2398  CB  THR A 384     -20.916  18.905 -12.617  1.00 14.58           C  
ATOM   2399  OG1 THR A 384     -20.321  18.021 -13.573  1.00 16.14           O  
ATOM   2400  CG2 THR A 384     -21.435  20.130 -13.322  1.00 13.48           C  
ATOM   2401  N   GLN A 385     -21.080  19.503  -9.465  1.00 15.44           N  
ATOM   2402  CA  GLN A 385     -21.655  20.258  -8.351  1.00 19.80           C  
ATOM   2403  C   GLN A 385     -20.586  21.070  -7.642  1.00 17.90           C  
ATOM   2404  O   GLN A 385     -20.817  22.217  -7.256  1.00 15.70           O  
ATOM   2405  CB  GLN A 385     -22.337  19.312  -7.361  1.00 20.54           C  
ATOM   2406  CG  GLN A 385     -23.674  18.803  -7.813  1.00 25.74           C  
ATOM   2407  CD  GLN A 385     -24.246  17.781  -6.855  1.00 30.75           C  
ATOM   2408  OE1 GLN A 385     -23.576  16.813  -6.493  1.00 21.12           O  
ATOM   2409  NE2 GLN A 385     -25.489  17.989  -6.438  1.00 29.05           N  
ATOM   2410  N   LYS A 386     -19.407  20.479  -7.461  1.00 19.90           N  
ATOM   2411  CA  LYS A 386     -18.284  21.184  -6.858  1.00 13.64           C  
ATOM   2412  C   LYS A 386     -17.918  22.411  -7.675  1.00 19.81           C  
ATOM   2413  O   LYS A 386     -17.746  23.515  -7.135  1.00 22.88           O  
ATOM   2414  CB  LYS A 386     -17.112  20.220  -6.760  1.00 22.64           C  
ATOM   2415  CG  LYS A 386     -15.799  20.799  -6.227  1.00 36.75           C  
ATOM   2416  CD  LYS A 386     -14.688  19.745  -6.220  1.00 38.43           C  
ATOM   2417  CE  LYS A 386     -15.066  18.465  -5.449  1.00 52.93           C  
ATOM   2418  NZ  LYS A 386     -14.553  17.220  -6.109  1.00 51.93           N  
ATOM   2419  N   GLU A 387     -17.793  22.232  -8.994  1.00 17.04           N  
ATOM   2420  CA  GLU A 387     -17.427  23.366  -9.839  1.00 14.96           C  
ATOM   2421  C   GLU A 387     -18.516  24.431  -9.839  1.00 15.73           C  
ATOM   2422  O   GLU A 387     -18.220  25.630  -9.930  1.00 18.86           O  
ATOM   2423  CB  GLU A 387     -17.141  22.894 -11.262  1.00 15.40           C  
ATOM   2424  CG  GLU A 387     -15.990  21.904 -11.376  1.00 18.42           C  
ATOM   2425  CD  GLU A 387     -14.687  22.439 -10.798  1.00 20.88           C  
ATOM   2426  OE1 GLU A 387     -14.053  21.736  -9.980  1.00 29.68           O  
ATOM   2427  OE2 GLU A 387     -14.300  23.567 -11.159  1.00 20.92           O  
ATOM   2428  N   ALA A 388     -19.780  24.020  -9.724  1.00 15.84           N  
ATOM   2429  CA  ALA A 388     -20.863  24.995  -9.686  1.00 14.69           C  
ATOM   2430  C   ALA A 388     -20.888  25.732  -8.354  1.00 17.81           C  
ATOM   2431  O   ALA A 388     -21.195  26.930  -8.304  1.00 20.39           O  
ATOM   2432  CB  ALA A 388     -22.198  24.307  -9.950  1.00 14.13           C  
ATOM   2433  N   ALA A 389     -20.580  25.035  -7.259  1.00 14.23           N  
ATOM   2434  CA  ALA A 389     -20.418  25.718  -5.980  1.00 24.48           C  
ATOM   2435  C   ALA A 389     -19.348  26.793  -6.083  1.00 15.71           C  
ATOM   2436  O   ALA A 389     -19.535  27.918  -5.600  1.00 24.68           O  
ATOM   2437  CB  ALA A 389     -20.079  24.710  -4.883  1.00 23.71           C  
ATOM   2438  N   TRP A 390     -18.232  26.478  -6.742  1.00 16.61           N  
ATOM   2439  CA  TRP A 390     -17.221  27.504  -6.994  1.00 17.24           C  
ATOM   2440  C   TRP A 390     -17.798  28.668  -7.798  1.00 22.90           C  
ATOM   2441  O   TRP A 390     -17.554  29.833  -7.479  1.00 20.04           O  
ATOM   2442  CB  TRP A 390     -16.010  26.902  -7.716  1.00 18.12           C  
ATOM   2443  CG  TRP A 390     -14.990  26.279  -6.809  1.00 20.98           C  
ATOM   2444  CD1 TRP A 390     -14.804  24.947  -6.568  1.00 19.32           C  
ATOM   2445  CD2 TRP A 390     -14.009  26.966  -6.029  1.00 17.86           C  
ATOM   2446  NE1 TRP A 390     -13.762  24.765  -5.697  1.00 23.62           N  
ATOM   2447  CE2 TRP A 390     -13.259  25.989  -5.346  1.00 17.65           C  
ATOM   2448  CE3 TRP A 390     -13.682  28.315  -5.852  1.00 19.49           C  
ATOM   2449  CZ2 TRP A 390     -12.210  26.319  -4.493  1.00 25.74           C  
ATOM   2450  CZ3 TRP A 390     -12.647  28.640  -5.013  1.00 23.89           C  
ATOM   2451  CH2 TRP A 390     -11.918  27.647  -4.340  1.00 22.58           C  
ATOM   2452  N   ALA A 391     -18.539  28.377  -8.870  1.00 20.17           N  
ATOM   2453  CA  ALA A 391     -19.069  29.456  -9.713  1.00 23.88           C  
ATOM   2454  C   ALA A 391     -19.990  30.390  -8.926  1.00 17.21           C  
ATOM   2455  O   ALA A 391     -19.891  31.626  -9.018  1.00 26.00           O  
ATOM   2456  CB  ALA A 391     -19.814  28.865 -10.909  1.00 20.40           C  
ATOM   2457  N   ILE A 392     -20.903  29.808  -8.151  1.00 16.18           N  
ATOM   2458  CA  ILE A 392     -21.793  30.599  -7.304  1.00 19.06           C  
ATOM   2459  C   ILE A 392     -20.989  31.448  -6.320  1.00 26.26           C  
ATOM   2460  O   ILE A 392     -21.155  32.673  -6.254  1.00 21.75           O  
ATOM   2461  CB  ILE A 392     -22.788  29.686  -6.569  1.00 19.07           C  
ATOM   2462  CG1 ILE A 392     -23.598  28.846  -7.556  1.00 22.60           C  
ATOM   2463  CG2 ILE A 392     -23.729  30.517  -5.698  1.00 21.84           C  
ATOM   2464  CD1 ILE A 392     -24.453  29.654  -8.509  1.00 19.53           C  
ATOM   2465  N   SER A 393     -20.131  30.812  -5.513  1.00 22.86           N  
ATOM   2466  CA  SER A 393     -19.387  31.573  -4.509  1.00 19.04           C  
ATOM   2467  C   SER A 393     -18.504  32.645  -5.148  1.00 24.15           C  
ATOM   2468  O   SER A 393     -18.400  33.760  -4.628  1.00 22.19           O  
ATOM   2469  CB  SER A 393     -18.544  30.640  -3.645  1.00 21.63           C  
ATOM   2470  OG  SER A 393     -19.357  29.871  -2.774  1.00 23.67           O  
ATOM   2471  N   ASN A 394     -17.854  32.333  -6.272  1.00 20.46           N  
ATOM   2472  CA  ASN A 394     -17.008  33.319  -6.933  1.00 21.66           C  
ATOM   2473  C   ASN A 394     -17.814  34.519  -7.389  1.00 24.85           C  
ATOM   2474  O   ASN A 394     -17.279  35.631  -7.465  1.00 24.82           O  
ATOM   2475  CB  ASN A 394     -16.300  32.697  -8.135  1.00 23.15           C  
ATOM   2476  CG  ASN A 394     -15.083  31.892  -7.744  1.00 23.98           C  
ATOM   2477  OD1 ASN A 394     -14.722  31.814  -6.570  1.00 20.80           O  
ATOM   2478  ND2 ASN A 394     -14.451  31.269  -8.729  1.00 25.85           N  
ATOM   2479  N   LEU A 395     -19.093  34.318  -7.718  1.00 21.17           N  
ATOM   2480  CA  LEU A 395     -19.912  35.471  -8.082  1.00 26.54           C  
ATOM   2481  C   LEU A 395     -19.945  36.528  -6.977  1.00 24.58           C  
ATOM   2482  O   LEU A 395     -20.081  37.720  -7.266  1.00 27.34           O  
ATOM   2483  CB  LEU A 395     -21.330  35.022  -8.419  1.00 24.11           C  
ATOM   2484  CG  LEU A 395     -22.075  36.013  -9.318  1.00 39.08           C  
ATOM   2485  CD1 LEU A 395     -23.019  35.288 -10.262  1.00 32.19           C  
ATOM   2486  CD2 LEU A 395     -22.838  37.045  -8.499  1.00 41.89           C  
ATOM   2487  N   THR A 396     -19.824  36.125  -5.715  1.00 23.14           N  
ATOM   2488  CA  THR A 396     -19.959  37.070  -4.612  1.00 30.75           C  
ATOM   2489  C   THR A 396     -18.709  37.905  -4.372  1.00 28.80           C  
ATOM   2490  O   THR A 396     -18.758  38.851  -3.580  1.00 39.89           O  
ATOM   2491  CB  THR A 396     -20.305  36.332  -3.324  1.00 26.96           C  
ATOM   2492  OG1 THR A 396     -19.189  35.534  -2.925  1.00 27.37           O  
ATOM   2493  CG2 THR A 396     -21.526  35.444  -3.525  1.00 26.06           C  
ATOM   2494  N   ILE A 397     -17.594  37.590  -5.024  1.00 26.87           N  
ATOM   2495  CA  ILE A 397     -16.366  38.354  -4.808  1.00 28.28           C  
ATOM   2496  C   ILE A 397     -16.573  39.807  -5.219  1.00 26.93           C  
ATOM   2497  O   ILE A 397     -16.352  40.734  -4.432  1.00 35.63           O  
ATOM   2498  CB  ILE A 397     -15.190  37.711  -5.567  1.00 28.45           C  
ATOM   2499  CG1 ILE A 397     -14.873  36.328  -4.999  1.00 21.66           C  
ATOM   2500  CG2 ILE A 397     -13.950  38.590  -5.481  1.00 30.23           C  
ATOM   2501  CD1 ILE A 397     -13.948  35.515  -5.886  1.00 28.68           C  
ATOM   2502  N   SER A 398     -16.996  40.027  -6.464  1.00 27.19           N  
ATOM   2503  CA  SER A 398     -17.218  41.374  -6.977  1.00 27.06           C  
ATOM   2504  C   SER A 398     -18.654  41.609  -7.426  1.00 24.46           C  
ATOM   2505  O   SER A 398     -18.942  42.651  -8.026  1.00 31.58           O  
ATOM   2506  CB  SER A 398     -16.256  41.652  -8.133  1.00 34.91           C  
ATOM   2507  OG  SER A 398     -14.920  41.678  -7.666  1.00 37.91           O  
ATOM   2508  N   GLY A 399     -19.563  40.680  -7.145  1.00 28.12           N  
ATOM   2509  CA  GLY A 399     -20.933  40.833  -7.597  1.00 40.56           C  
ATOM   2510  C   GLY A 399     -21.678  41.881  -6.788  1.00 42.45           C  
ATOM   2511  O   GLY A 399     -21.521  41.986  -5.571  1.00 46.01           O  
ATOM   2512  N   ARG A 400     -22.498  42.667  -7.482  1.00 39.63           N  
ATOM   2513  CA  ARG A 400     -23.328  43.671  -6.836  1.00 38.70           C  
ATOM   2514  C   ARG A 400     -24.503  43.015  -6.128  1.00 45.88           C  
ATOM   2515  O   ARG A 400     -24.875  41.872  -6.408  1.00 45.69           O  
ATOM   2516  CB  ARG A 400     -23.864  44.678  -7.851  1.00 39.66           C  
ATOM   2517  CG  ARG A 400     -22.801  45.382  -8.667  1.00 50.53           C  
ATOM   2518  CD  ARG A 400     -23.431  46.459  -9.522  1.00 47.60           C  
ATOM   2519  NE  ARG A 400     -24.449  45.915 -10.422  1.00 40.79           N  
ATOM   2520  CZ  ARG A 400     -24.252  45.615 -11.702  1.00 36.36           C  
ATOM   2521  NH1 ARG A 400     -23.067  45.799 -12.269  1.00 37.80           N  
ATOM   2522  NH2 ARG A 400     -25.248  45.128 -12.430  1.00 41.71           N  
ATOM   2523  N   LYS A 401     -25.109  43.771  -5.213  1.00 52.28           N  
ATOM   2524  CA  LYS A 401     -26.248  43.243  -4.474  1.00 44.66           C  
ATOM   2525  C   LYS A 401     -27.358  42.796  -5.414  1.00 33.81           C  
ATOM   2526  O   LYS A 401     -28.039  41.806  -5.133  1.00 37.93           O  
ATOM   2527  CB  LYS A 401     -26.768  44.290  -3.486  1.00 52.15           C  
ATOM   2528  CG  LYS A 401     -28.094  43.923  -2.823  1.00 64.40           C  
ATOM   2529  CD  LYS A 401     -28.410  44.847  -1.653  1.00 82.29           C  
ATOM   2530  CE  LYS A 401     -29.863  44.725  -1.216  1.00 80.28           C  
ATOM   2531  NZ  LYS A 401     -30.418  46.040  -0.791  1.00 71.36           N  
ATOM   2532  N   ASP A 402     -27.552  43.495  -6.538  1.00 37.98           N  
ATOM   2533  CA  ASP A 402     -28.621  43.113  -7.457  1.00 33.73           C  
ATOM   2534  C   ASP A 402     -28.289  41.824  -8.199  1.00 35.12           C  
ATOM   2535  O   ASP A 402     -29.194  41.042  -8.512  1.00 32.71           O  
ATOM   2536  CB  ASP A 402     -28.903  44.233  -8.458  1.00 32.04           C  
ATOM   2537  CG  ASP A 402     -27.686  44.609  -9.279  1.00 36.26           C  
ATOM   2538  OD1 ASP A 402     -26.659  44.965  -8.675  1.00 54.42           O  
ATOM   2539  OD2 ASP A 402     -27.753  44.549 -10.526  1.00 42.10           O  
ATOM   2540  N   GLN A 403     -27.008  41.569  -8.465  1.00 32.61           N  
ATOM   2541  CA  GLN A 403     -26.619  40.313  -9.103  1.00 31.69           C  
ATOM   2542  C   GLN A 403     -26.819  39.126  -8.156  1.00 30.12           C  
ATOM   2543  O   GLN A 403     -27.390  38.090  -8.539  1.00 33.68           O  
ATOM   2544  CB  GLN A 403     -25.174  40.432  -9.577  1.00 24.89           C  
ATOM   2545  CG  GLN A 403     -24.965  41.643 -10.498  1.00 32.73           C  
ATOM   2546  CD  GLN A 403     -23.516  41.868 -10.923  1.00 29.87           C  
ATOM   2547  OE1 GLN A 403     -22.598  41.848 -10.102  1.00 33.14           O  
ATOM   2548  NE2 GLN A 403     -23.311  42.093 -12.213  1.00 24.98           N  
ATOM   2549  N   VAL A 404     -26.393  39.271  -6.899  1.00 32.04           N  
ATOM   2550  CA  VAL A 404     -26.669  38.242  -5.896  1.00 36.03           C  
ATOM   2551  C   VAL A 404     -28.173  38.077  -5.703  1.00 34.48           C  
ATOM   2552  O   VAL A 404     -28.675  36.966  -5.478  1.00 28.12           O  
ATOM   2553  CB  VAL A 404     -25.966  38.591  -4.570  1.00 37.26           C  
ATOM   2554  CG1 VAL A 404     -26.318  37.574  -3.492  1.00 35.02           C  
ATOM   2555  CG2 VAL A 404     -24.472  38.651  -4.757  1.00 36.65           C  
ATOM   2556  N   ALA A 405     -28.915  39.181  -5.773  1.00 34.85           N  
ATOM   2557  CA  ALA A 405     -30.365  39.102  -5.662  1.00 45.66           C  
ATOM   2558  C   ALA A 405     -30.953  38.286  -6.803  1.00 40.21           C  
ATOM   2559  O   ALA A 405     -31.843  37.455  -6.586  1.00 31.42           O  
ATOM   2560  CB  ALA A 405     -30.964  40.510  -5.634  1.00 47.28           C  
ATOM   2561  N   TYR A 406     -30.471  38.511  -8.029  1.00 32.30           N  
ATOM   2562  CA  TYR A 406     -30.876  37.670  -9.149  1.00 39.17           C  
ATOM   2563  C   TYR A 406     -30.659  36.199  -8.812  1.00 35.26           C  
ATOM   2564  O   TYR A 406     -31.563  35.371  -8.973  1.00 32.60           O  
ATOM   2565  CB  TYR A 406     -30.107  38.067 -10.414  1.00 32.09           C  
ATOM   2566  CG  TYR A 406     -30.306  37.108 -11.562  1.00 36.78           C  
ATOM   2567  CD1 TYR A 406     -31.537  36.994 -12.193  1.00 41.11           C  
ATOM   2568  CD2 TYR A 406     -29.261  36.318 -12.020  1.00 41.84           C  
ATOM   2569  CE1 TYR A 406     -31.725  36.108 -13.251  1.00 40.20           C  
ATOM   2570  CE2 TYR A 406     -29.434  35.434 -13.073  1.00 40.85           C  
ATOM   2571  CZ  TYR A 406     -30.666  35.329 -13.683  1.00 43.90           C  
ATOM   2572  OH  TYR A 406     -30.835  34.444 -14.728  1.00 39.84           O  
ATOM   2573  N   LEU A 407     -29.475  35.862  -8.299  1.00 33.17           N  
ATOM   2574  CA  LEU A 407     -29.216  34.471  -7.922  1.00 31.12           C  
ATOM   2575  C   LEU A 407     -30.269  33.971  -6.943  1.00 33.82           C  
ATOM   2576  O   LEU A 407     -30.768  32.845  -7.061  1.00 23.54           O  
ATOM   2577  CB  LEU A 407     -27.820  34.323  -7.304  1.00 40.69           C  
ATOM   2578  CG  LEU A 407     -26.582  34.564  -8.170  1.00 36.61           C  
ATOM   2579  CD1 LEU A 407     -25.373  33.991  -7.450  1.00 32.17           C  
ATOM   2580  CD2 LEU A 407     -26.726  33.963  -9.558  1.00 35.00           C  
ATOM   2581  N   ILE A 408     -30.593  34.792  -5.943  1.00 41.69           N  
ATOM   2582  CA  ILE A 408     -31.600  34.396  -4.959  1.00 40.10           C  
ATOM   2583  C   ILE A 408     -32.927  34.118  -5.653  1.00 31.55           C  
ATOM   2584  O   ILE A 408     -33.589  33.108  -5.391  1.00 27.51           O  
ATOM   2585  CB  ILE A 408     -31.751  35.476  -3.871  1.00 41.34           C  
ATOM   2586  CG1 ILE A 408     -30.447  35.657  -3.093  1.00 30.24           C  
ATOM   2587  CG2 ILE A 408     -32.905  35.125  -2.914  1.00 38.60           C  
ATOM   2588  CD1 ILE A 408     -30.075  34.482  -2.189  1.00 39.54           C  
ATOM   2589  N   GLN A 409     -33.335  35.017  -6.550  1.00 27.79           N  
ATOM   2590  CA  GLN A 409     -34.565  34.815  -7.304  1.00 31.42           C  
ATOM   2591  C   GLN A 409     -34.584  33.459  -7.993  1.00 32.34           C  
ATOM   2592  O   GLN A 409     -35.648  32.843  -8.115  1.00 25.36           O  
ATOM   2593  CB  GLN A 409     -34.728  35.928  -8.340  1.00 47.40           C  
ATOM   2594  CG  GLN A 409     -34.906  37.317  -7.747  1.00 52.44           C  
ATOM   2595  CD  GLN A 409     -34.677  38.433  -8.762  1.00 71.78           C  
ATOM   2596  OE1 GLN A 409     -34.498  38.182  -9.959  1.00 59.92           O  
ATOM   2597  NE2 GLN A 409     -34.678  39.674  -8.282  1.00 69.48           N  
ATOM   2598  N   GLN A 410     -33.425  32.973  -8.441  1.00 30.55           N  
ATOM   2599  CA  GLN A 410     -33.343  31.740  -9.212  1.00 26.72           C  
ATOM   2600  C   GLN A 410     -33.233  30.492  -8.342  1.00 33.50           C  
ATOM   2601  O   GLN A 410     -32.845  29.429  -8.845  1.00 25.19           O  
ATOM   2602  CB  GLN A 410     -32.166  31.814 -10.179  1.00 29.66           C  
ATOM   2603  CG  GLN A 410     -32.254  32.996 -11.142  1.00 32.36           C  
ATOM   2604  CD  GLN A 410     -33.507  32.946 -11.999  1.00 32.91           C  
ATOM   2605  OE1 GLN A 410     -33.949  31.874 -12.404  1.00 32.95           O  
ATOM   2606  NE2 GLN A 410     -34.095  34.108 -12.263  1.00 36.94           N  
ATOM   2607  N   ASN A 411     -33.568  30.595  -7.056  1.00 26.10           N  
ATOM   2608  CA  ASN A 411     -33.623  29.444  -6.158  1.00 28.10           C  
ATOM   2609  C   ASN A 411     -32.239  28.823  -5.970  1.00 21.73           C  
ATOM   2610  O   ASN A 411     -32.071  27.602  -5.975  1.00 27.81           O  
ATOM   2611  CB  ASN A 411     -34.633  28.407  -6.669  1.00 34.33           C  
ATOM   2612  CG  ASN A 411     -35.381  27.695  -5.538  1.00 53.95           C  
ATOM   2613  OD1 ASN A 411     -35.773  28.317  -4.544  1.00 44.37           O  
ATOM   2614  ND2 ASN A 411     -35.579  26.386  -5.686  1.00 51.46           N  
ATOM   2615  N   VAL A 412     -31.238  29.682  -5.770  1.00 21.08           N  
ATOM   2616  CA  VAL A 412     -29.871  29.196  -5.587  1.00 25.24           C  
ATOM   2617  C   VAL A 412     -29.649  28.611  -4.186  1.00 23.23           C  
ATOM   2618  O   VAL A 412     -28.812  27.710  -4.007  1.00 25.74           O  
ATOM   2619  CB  VAL A 412     -28.880  30.336  -5.886  1.00 26.46           C  
ATOM   2620  CG1 VAL A 412     -28.864  31.366  -4.765  1.00 30.41           C  
ATOM   2621  CG2 VAL A 412     -27.481  29.794  -6.142  1.00 31.68           C  
ATOM   2622  N   ILE A 413     -30.390  29.082  -3.188  1.00 26.43           N  
ATOM   2623  CA  ILE A 413     -30.068  28.809  -1.789  1.00 25.99           C  
ATOM   2624  C   ILE A 413     -30.256  27.334  -1.441  1.00 25.16           C  
ATOM   2625  O   ILE A 413     -29.374  26.750  -0.799  1.00 25.60           O  
ATOM   2626  CB  ILE A 413     -30.893  29.709  -0.852  1.00 27.45           C  
ATOM   2627  CG1 ILE A 413     -30.429  31.166  -0.965  1.00 22.09           C  
ATOM   2628  CG2 ILE A 413     -30.805  29.224   0.605  1.00 36.93           C  
ATOM   2629  CD1 ILE A 413     -29.008  31.423  -0.476  1.00 26.96           C  
ATOM   2630  N   PRO A 414     -31.369  26.696  -1.789  1.00 22.95           N  
ATOM   2631  CA  PRO A 414     -31.582  25.292  -1.370  1.00 24.72           C  
ATOM   2632  C   PRO A 414     -30.476  24.364  -1.855  1.00 28.50           C  
ATOM   2633  O   PRO A 414     -29.911  23.611  -1.049  1.00 32.47           O  
ATOM   2634  CB  PRO A 414     -32.946  24.941  -1.987  1.00 23.09           C  
ATOM   2635  CG  PRO A 414     -33.638  26.244  -2.094  1.00 17.47           C  
ATOM   2636  CD  PRO A 414     -32.580  27.271  -2.398  1.00 25.46           C  
ATOM   2637  N   PRO A 415     -30.117  24.369  -3.148  1.00 29.60           N  
ATOM   2638  CA  PRO A 415     -29.026  23.466  -3.580  1.00 30.73           C  
ATOM   2639  C   PRO A 415     -27.650  23.900  -3.095  1.00 20.65           C  
ATOM   2640  O   PRO A 415     -26.811  23.052  -2.722  1.00 30.75           O  
ATOM   2641  CB  PRO A 415     -29.123  23.507  -5.112  1.00 31.03           C  
ATOM   2642  CG  PRO A 415     -29.781  24.783  -5.426  1.00 24.13           C  
ATOM   2643  CD  PRO A 415     -30.728  25.069  -4.298  1.00 32.60           C  
ATOM   2644  N   PHE A 416     -27.393  25.211  -3.091  1.00 25.46           N  
ATOM   2645  CA  PHE A 416     -26.166  25.719  -2.490  1.00 25.81           C  
ATOM   2646  C   PHE A 416     -25.982  25.149  -1.082  1.00 28.25           C  
ATOM   2647  O   PHE A 416     -24.938  24.571  -0.763  1.00 27.78           O  
ATOM   2648  CB  PHE A 416     -26.214  27.253  -2.480  1.00 25.23           C  
ATOM   2649  CG  PHE A 416     -24.871  27.926  -2.351  1.00 25.88           C  
ATOM   2650  CD1 PHE A 416     -23.785  27.500  -3.093  1.00 26.72           C  
ATOM   2651  CD2 PHE A 416     -24.716  29.027  -1.521  1.00 28.65           C  
ATOM   2652  CE1 PHE A 416     -22.571  28.131  -2.989  1.00 22.86           C  
ATOM   2653  CE2 PHE A 416     -23.497  29.665  -1.411  1.00 27.76           C  
ATOM   2654  CZ  PHE A 416     -22.422  29.218  -2.153  1.00 27.78           C  
ATOM   2655  N   CYS A 417     -27.016  25.259  -0.243  1.00 27.47           N  
ATOM   2656  CA  CYS A 417     -26.940  24.773   1.134  1.00 35.28           C  
ATOM   2657  C   CYS A 417     -26.877  23.254   1.191  1.00 36.70           C  
ATOM   2658  O   CYS A 417     -26.215  22.693   2.074  1.00 29.83           O  
ATOM   2659  CB  CYS A 417     -28.146  25.270   1.939  1.00 33.18           C  
ATOM   2660  SG  CYS A 417     -28.120  27.027   2.341  1.00 32.63           S  
ATOM   2661  N   ASN A 418     -27.581  22.567   0.283  1.00 23.75           N  
ATOM   2662  CA  ASN A 418     -27.522  21.112   0.262  1.00 21.58           C  
ATOM   2663  C   ASN A 418     -26.091  20.632   0.123  1.00 30.39           C  
ATOM   2664  O   ASN A 418     -25.752  19.530   0.576  1.00 23.83           O  
ATOM   2665  CB  ASN A 418     -28.372  20.557  -0.881  1.00 30.25           C  
ATOM   2666  CG  ASN A 418     -29.861  20.548  -0.560  1.00 46.49           C  
ATOM   2667  OD1 ASN A 418     -30.265  20.754   0.588  1.00 47.67           O  
ATOM   2668  ND2 ASN A 418     -30.686  20.293  -1.577  1.00 33.59           N  
ATOM   2669  N   LEU A 419     -25.241  21.436  -0.514  1.00 25.12           N  
ATOM   2670  CA  LEU A 419     -23.847  20.998  -0.633  1.00 27.93           C  
ATOM   2671  C   LEU A 419     -23.044  21.103   0.669  1.00 36.26           C  
ATOM   2672  O   LEU A 419     -21.859  20.754   0.666  1.00 33.53           O  
ATOM   2673  CB  LEU A 419     -23.137  21.793  -1.723  1.00 26.54           C  
ATOM   2674  CG  LEU A 419     -23.639  21.509  -3.137  1.00 31.45           C  
ATOM   2675  CD1 LEU A 419     -22.851  22.354  -4.102  1.00 34.47           C  
ATOM   2676  CD2 LEU A 419     -23.509  20.035  -3.489  1.00 28.28           C  
ATOM   2677  N   LEU A 420     -23.635  21.552   1.777  1.00 33.17           N  
ATOM   2678  CA  LEU A 420     -22.869  21.772   2.999  1.00 33.64           C  
ATOM   2679  C   LEU A 420     -22.535  20.492   3.758  1.00 32.73           C  
ATOM   2680  O   LEU A 420     -21.704  20.539   4.670  1.00 29.62           O  
ATOM   2681  CB  LEU A 420     -23.629  22.710   3.936  1.00 24.92           C  
ATOM   2682  CG  LEU A 420     -23.556  24.192   3.578  1.00 30.23           C  
ATOM   2683  CD1 LEU A 420     -24.657  24.958   4.286  1.00 33.40           C  
ATOM   2684  CD2 LEU A 420     -22.191  24.771   3.927  1.00 24.83           C  
ATOM   2685  N   THR A 421     -23.144  19.358   3.419  1.00 29.09           N  
ATOM   2686  CA  THR A 421     -22.910  18.120   4.151  1.00 30.96           C  
ATOM   2687  C   THR A 421     -22.000  17.147   3.416  1.00 33.65           C  
ATOM   2688  O   THR A 421     -21.883  15.993   3.838  1.00 33.55           O  
ATOM   2689  CB  THR A 421     -24.235  17.428   4.456  1.00 36.19           C  
ATOM   2690  OG1 THR A 421     -24.924  17.174   3.226  1.00 35.96           O  
ATOM   2691  CG2 THR A 421     -25.104  18.299   5.360  1.00 31.53           C  
ATOM   2692  N   VAL A 422     -21.350  17.572   2.335  1.00 29.64           N  
ATOM   2693  CA  VAL A 422     -20.509  16.655   1.572  1.00 30.55           C  
ATOM   2694  C   VAL A 422     -19.228  16.396   2.346  1.00 34.45           C  
ATOM   2695  O   VAL A 422     -18.902  17.121   3.292  1.00 33.91           O  
ATOM   2696  CB  VAL A 422     -20.196  17.199   0.165  1.00 34.07           C  
ATOM   2697  CG1 VAL A 422     -21.477  17.392  -0.624  1.00 34.85           C  
ATOM   2698  CG2 VAL A 422     -19.402  18.503   0.249  1.00 29.87           C  
ATOM   2699  N   LYS A 423     -18.489  15.363   1.936  1.00 35.16           N  
ATOM   2700  CA  LYS A 423     -17.227  15.013   2.573  1.00 38.83           C  
ATOM   2701  C   LYS A 423     -16.064  15.892   2.138  1.00 36.38           C  
ATOM   2702  O   LYS A 423     -15.042  15.921   2.831  1.00 46.53           O  
ATOM   2703  CB  LYS A 423     -16.872  13.550   2.282  1.00 44.28           C  
ATOM   2704  CG  LYS A 423     -17.452  12.550   3.275  1.00 58.83           C  
ATOM   2705  CD  LYS A 423     -18.743  11.906   2.783  1.00 67.87           C  
ATOM   2706  CE  LYS A 423     -18.531  10.451   2.357  1.00 65.83           C  
ATOM   2707  NZ  LYS A 423     -17.998  10.324   0.970  1.00 89.42           N  
ATOM   2708  N   ASP A 424     -16.178  16.596   1.014  1.00 31.91           N  
ATOM   2709  CA  ASP A 424     -15.078  17.422   0.519  1.00 35.51           C  
ATOM   2710  C   ASP A 424     -15.050  18.732   1.296  1.00 31.95           C  
ATOM   2711  O   ASP A 424     -15.894  19.607   1.081  1.00 32.49           O  
ATOM   2712  CB  ASP A 424     -15.224  17.680  -0.979  1.00 30.20           C  
ATOM   2713  CG  ASP A 424     -14.019  18.383  -1.575  1.00 31.78           C  
ATOM   2714  OD1 ASP A 424     -13.381  19.200  -0.875  1.00 33.10           O  
ATOM   2715  OD2 ASP A 424     -13.704  18.116  -2.750  1.00 35.56           O  
ATOM   2716  N   ALA A 425     -14.062  18.880   2.178  1.00 33.31           N  
ATOM   2717  CA  ALA A 425     -13.990  20.064   3.026  1.00 23.11           C  
ATOM   2718  C   ALA A 425     -13.859  21.342   2.207  1.00 21.26           C  
ATOM   2719  O   ALA A 425     -14.336  22.403   2.630  1.00 30.38           O  
ATOM   2720  CB  ALA A 425     -12.819  19.929   4.002  1.00 24.48           C  
ATOM   2721  N   GLN A 426     -13.211  21.268   1.042  1.00 31.40           N  
ATOM   2722  CA  GLN A 426     -13.054  22.449   0.198  1.00 28.72           C  
ATOM   2723  C   GLN A 426     -14.403  22.964  -0.307  1.00 29.50           C  
ATOM   2724  O   GLN A 426     -14.631  24.178  -0.379  1.00 25.79           O  
ATOM   2725  CB  GLN A 426     -12.143  22.120  -0.977  1.00 19.83           C  
ATOM   2726  CG  GLN A 426     -11.851  23.316  -1.874  1.00 43.62           C  
ATOM   2727  CD  GLN A 426     -10.994  22.954  -3.080  1.00 58.75           C  
ATOM   2728  OE1 GLN A 426     -11.477  22.348  -4.040  1.00 49.11           O  
ATOM   2729  NE2 GLN A 426      -9.716  23.326  -3.036  1.00 57.25           N  
ATOM   2730  N   VAL A 427     -15.306  22.056  -0.671  1.00 23.59           N  
ATOM   2731  CA  VAL A 427     -16.637  22.462  -1.116  1.00 29.28           C  
ATOM   2732  C   VAL A 427     -17.400  23.111   0.027  1.00 26.16           C  
ATOM   2733  O   VAL A 427     -18.073  24.132  -0.152  1.00 22.96           O  
ATOM   2734  CB  VAL A 427     -17.398  21.247  -1.671  1.00 26.32           C  
ATOM   2735  CG1 VAL A 427     -18.761  21.673  -2.193  1.00 20.76           C  
ATOM   2736  CG2 VAL A 427     -16.581  20.582  -2.749  1.00 25.86           C  
ATOM   2737  N   VAL A 428     -17.335  22.505   1.211  1.00 21.22           N  
ATOM   2738  CA  VAL A 428     -18.000  23.077   2.374  1.00 28.73           C  
ATOM   2739  C   VAL A 428     -17.502  24.493   2.607  1.00 20.01           C  
ATOM   2740  O   VAL A 428     -18.289  25.426   2.804  1.00 25.42           O  
ATOM   2741  CB  VAL A 428     -17.779  22.180   3.608  1.00 30.31           C  
ATOM   2742  CG1 VAL A 428     -18.537  22.727   4.812  1.00 28.17           C  
ATOM   2743  CG2 VAL A 428     -18.227  20.745   3.312  1.00 23.62           C  
ATOM   2744  N   GLN A 429     -16.185  24.676   2.574  1.00 21.92           N  
ATOM   2745  CA  GLN A 429     -15.614  25.997   2.803  1.00 23.09           C  
ATOM   2746  C   GLN A 429     -16.079  26.981   1.744  1.00 27.67           C  
ATOM   2747  O   GLN A 429     -16.424  28.126   2.058  1.00 25.07           O  
ATOM   2748  CB  GLN A 429     -14.084  25.905   2.814  1.00 23.87           C  
ATOM   2749  CG  GLN A 429     -13.383  27.218   3.111  1.00 30.35           C  
ATOM   2750  CD  GLN A 429     -13.676  27.711   4.516  1.00 52.45           C  
ATOM   2751  OE1 GLN A 429     -13.369  27.034   5.498  1.00 51.28           O  
ATOM   2752  NE2 GLN A 429     -14.288  28.888   4.618  1.00 48.47           N  
ATOM   2753  N   VAL A 430     -16.069  26.564   0.478  1.00 25.17           N  
ATOM   2754  CA  VAL A 430     -16.511  27.448  -0.596  1.00 22.09           C  
ATOM   2755  C   VAL A 430     -17.944  27.900  -0.348  1.00 19.24           C  
ATOM   2756  O   VAL A 430     -18.271  29.087  -0.465  1.00 24.28           O  
ATOM   2757  CB  VAL A 430     -16.370  26.738  -1.952  1.00 21.67           C  
ATOM   2758  CG1 VAL A 430     -17.272  27.373  -3.007  1.00 19.68           C  
ATOM   2759  CG2 VAL A 430     -14.933  26.777  -2.398  1.00 24.24           C  
ATOM   2760  N   VAL A 431     -18.823  26.953  -0.023  1.00 15.22           N  
ATOM   2761  CA  VAL A 431     -20.232  27.281   0.189  1.00 22.75           C  
ATOM   2762  C   VAL A 431     -20.391  28.235   1.367  1.00 25.30           C  
ATOM   2763  O   VAL A 431     -21.151  29.209   1.292  1.00 23.81           O  
ATOM   2764  CB  VAL A 431     -21.057  25.992   0.378  1.00 26.90           C  
ATOM   2765  CG1 VAL A 431     -22.515  26.325   0.702  1.00 25.02           C  
ATOM   2766  CG2 VAL A 431     -20.974  25.119  -0.883  1.00 24.31           C  
ATOM   2767  N   LEU A 432     -19.698  27.966   2.479  1.00 23.72           N  
ATOM   2768  CA  LEU A 432     -19.808  28.849   3.638  1.00 26.98           C  
ATOM   2769  C   LEU A 432     -19.294  30.247   3.320  1.00 26.97           C  
ATOM   2770  O   LEU A 432     -19.906  31.238   3.720  1.00 29.00           O  
ATOM   2771  CB  LEU A 432     -19.056  28.260   4.833  1.00 26.60           C  
ATOM   2772  CG  LEU A 432     -19.745  27.138   5.596  1.00 21.47           C  
ATOM   2773  CD1 LEU A 432     -18.867  26.711   6.773  1.00 38.57           C  
ATOM   2774  CD2 LEU A 432     -21.116  27.543   6.086  1.00 30.79           C  
ATOM   2775  N   ASP A 433     -18.169  30.352   2.607  1.00 26.95           N  
ATOM   2776  CA  ASP A 433     -17.671  31.667   2.210  1.00 25.55           C  
ATOM   2777  C   ASP A 433     -18.692  32.397   1.355  1.00 27.22           C  
ATOM   2778  O   ASP A 433     -18.894  33.610   1.503  1.00 32.50           O  
ATOM   2779  CB  ASP A 433     -16.361  31.524   1.437  1.00 33.74           C  
ATOM   2780  CG  ASP A 433     -15.151  31.489   2.335  1.00 44.68           C  
ATOM   2781  OD1 ASP A 433     -15.126  32.243   3.333  1.00 44.63           O  
ATOM   2782  OD2 ASP A 433     -14.221  30.715   2.032  1.00 51.04           O  
ATOM   2783  N   GLY A 434     -19.335  31.675   0.440  1.00 23.59           N  
ATOM   2784  CA  GLY A 434     -20.336  32.303  -0.400  1.00 25.68           C  
ATOM   2785  C   GLY A 434     -21.514  32.805   0.406  1.00 28.19           C  
ATOM   2786  O   GLY A 434     -21.964  33.936   0.228  1.00 30.68           O  
ATOM   2787  N   LEU A 435     -22.030  31.961   1.306  1.00 21.18           N  
ATOM   2788  CA  LEU A 435     -23.152  32.367   2.144  1.00 29.17           C  
ATOM   2789  C   LEU A 435     -22.779  33.565   3.001  1.00 31.95           C  
ATOM   2790  O   LEU A 435     -23.571  34.500   3.162  1.00 31.53           O  
ATOM   2791  CB  LEU A 435     -23.597  31.204   3.030  1.00 30.15           C  
ATOM   2792  CG  LEU A 435     -24.212  29.996   2.330  1.00 25.37           C  
ATOM   2793  CD1 LEU A 435     -24.475  28.889   3.341  1.00 32.65           C  
ATOM   2794  CD2 LEU A 435     -25.488  30.385   1.622  1.00 33.12           C  
ATOM   2795  N   SER A 436     -21.572  33.554   3.561  1.00 29.71           N  
ATOM   2796  CA  SER A 436     -21.121  34.680   4.361  1.00 34.02           C  
ATOM   2797  C   SER A 436     -21.129  35.951   3.534  1.00 32.60           C  
ATOM   2798  O   SER A 436     -21.638  36.985   3.975  1.00 38.07           O  
ATOM   2799  CB  SER A 436     -19.723  34.396   4.924  1.00 29.81           C  
ATOM   2800  OG  SER A 436     -19.226  35.503   5.660  1.00 36.60           O  
ATOM   2801  N   ASN A 437     -20.575  35.896   2.322  1.00 34.30           N  
ATOM   2802  CA  ASN A 437     -20.539  37.095   1.494  1.00 31.09           C  
ATOM   2803  C   ASN A 437     -21.940  37.545   1.110  1.00 29.17           C  
ATOM   2804  O   ASN A 437     -22.213  38.747   1.039  1.00 36.01           O  
ATOM   2805  CB  ASN A 437     -19.703  36.848   0.246  1.00 38.64           C  
ATOM   2806  CG  ASN A 437     -18.231  36.761   0.549  1.00 36.83           C  
ATOM   2807  OD1 ASN A 437     -17.828  36.647   1.708  1.00 36.96           O  
ATOM   2808  ND2 ASN A 437     -17.413  36.808  -0.491  1.00 34.13           N  
ATOM   2809  N   ILE A 438     -22.841  36.595   0.859  1.00 31.37           N  
ATOM   2810  CA  ILE A 438     -24.216  36.932   0.495  1.00 39.30           C  
ATOM   2811  C   ILE A 438     -24.895  37.676   1.638  1.00 38.10           C  
ATOM   2812  O   ILE A 438     -25.525  38.720   1.438  1.00 41.88           O  
ATOM   2813  CB  ILE A 438     -24.990  35.657   0.111  1.00 39.43           C  
ATOM   2814  CG1 ILE A 438     -24.480  35.105  -1.223  1.00 35.98           C  
ATOM   2815  CG2 ILE A 438     -26.498  35.926   0.022  1.00 36.29           C  
ATOM   2816  CD1 ILE A 438     -24.886  33.661  -1.486  1.00 29.54           C  
ATOM   2817  N   LEU A 439     -24.781  37.138   2.853  1.00 39.98           N  
ATOM   2818  CA  LEU A 439     -25.389  37.781   4.014  1.00 45.54           C  
ATOM   2819  C   LEU A 439     -24.754  39.137   4.298  1.00 41.59           C  
ATOM   2820  O   LEU A 439     -25.462  40.108   4.580  1.00 45.13           O  
ATOM   2821  CB  LEU A 439     -25.277  36.865   5.232  1.00 29.47           C  
ATOM   2822  CG  LEU A 439     -26.135  35.608   5.137  1.00 31.74           C  
ATOM   2823  CD1 LEU A 439     -25.717  34.598   6.181  1.00 37.84           C  
ATOM   2824  CD2 LEU A 439     -27.615  35.947   5.291  1.00 38.96           C  
ATOM   2825  N   LYS A 440     -23.423  39.223   4.233  1.00 33.72           N  
ATOM   2826  CA  LYS A 440     -22.744  40.495   4.460  1.00 40.77           C  
ATOM   2827  C   LYS A 440     -23.179  41.544   3.449  1.00 47.25           C  
ATOM   2828  O   LYS A 440     -23.302  42.728   3.783  1.00 51.79           O  
ATOM   2829  CB  LYS A 440     -21.231  40.304   4.381  1.00 47.29           C  
ATOM   2830  CG  LYS A 440     -20.576  39.815   5.650  1.00 52.87           C  
ATOM   2831  CD  LYS A 440     -19.070  39.709   5.468  1.00 45.20           C  
ATOM   2832  CE  LYS A 440     -18.431  38.882   6.572  1.00 62.18           C  
ATOM   2833  NZ  LYS A 440     -16.945  38.853   6.458  1.00 71.99           N  
ATOM   2834  N   MET A 441     -23.391  41.131   2.201  1.00 49.46           N  
ATOM   2835  CA  MET A 441     -23.740  42.077   1.148  1.00 53.58           C  
ATOM   2836  C   MET A 441     -25.150  42.614   1.340  1.00 58.06           C  
ATOM   2837  O   MET A 441     -25.392  43.816   1.176  1.00 60.57           O  
ATOM   2838  CB  MET A 441     -23.608  41.395  -0.210  1.00 56.96           C  
ATOM   2839  CG  MET A 441     -23.336  42.337  -1.362  1.00 62.39           C  
ATOM   2840  SD  MET A 441     -23.265  41.461  -2.933  1.00 69.03           S  
ATOM   2841  CE  MET A 441     -21.963  40.261  -2.633  1.00 58.74           C  
ATOM   2842  N   ALA A 442     -26.093  41.737   1.673  1.00 52.68           N  
ATOM   2843  CA  ALA A 442     -27.469  42.144   1.921  1.00 68.57           C  
ATOM   2844  C   ALA A 442     -27.528  42.924   3.224  1.00 73.26           C  
ATOM   2845  O   ALA A 442     -27.314  42.365   4.305  1.00 76.64           O  
ATOM   2846  CB  ALA A 442     -28.381  40.924   1.977  1.00 70.21           C  
ATOM   2847  N   GLU A 443     -27.812  44.221   3.128  1.00 65.93           N  
ATOM   2848  CA  GLU A 443     -27.933  45.040   4.326  1.00 78.45           C  
ATOM   2849  C   GLU A 443     -29.287  44.823   4.996  1.00 83.38           C  
ATOM   2850  O   GLU A 443     -29.360  44.410   6.159  1.00 79.66           O  
ATOM   2851  CB  GLU A 443     -27.728  46.511   3.967  1.00 83.87           C  
ATOM   2852  CG  GLU A 443     -26.327  46.830   3.469  1.00 80.10           C  
ATOM   2853  CD  GLU A 443     -26.301  48.012   2.520  1.00108.66           C  
ATOM   2854  OE1 GLU A 443     -27.165  48.071   1.618  1.00108.19           O  
ATOM   2855  OE2 GLU A 443     -25.420  48.884   2.678  1.00106.96           O  
ATOM   2856  N   ASP A 444     -30.369  45.085   4.266  1.00 85.40           N  
ATOM   2857  CA  ASP A 444     -31.717  44.931   4.798  1.00 88.11           C  
ATOM   2858  C   ASP A 444     -32.272  43.535   4.558  1.00 86.33           C  
ATOM   2859  O   ASP A 444     -32.878  42.945   5.460  1.00 88.21           O  
ATOM   2860  CB  ASP A 444     -32.645  45.974   4.172  1.00 90.78           C  
ATOM   2861  CG  ASP A 444     -32.248  47.393   4.530  1.00 91.72           C  
ATOM   2862  OD1 ASP A 444     -31.704  47.597   5.636  1.00 79.06           O  
ATOM   2863  OD2 ASP A 444     -32.475  48.302   3.704  1.00101.32           O  
ATOM   2864  N   GLU A 445     -32.061  42.988   3.363  1.00 84.51           N  
ATOM   2865  CA  GLU A 445     -32.579  41.668   3.032  1.00 86.29           C  
ATOM   2866  C   GLU A 445     -31.899  40.553   3.819  1.00 77.49           C  
ATOM   2867  O   GLU A 445     -32.252  39.386   3.622  1.00 81.65           O  
ATOM   2868  CB  GLU A 445     -32.425  41.413   1.530  1.00 80.87           C  
ATOM   2869  CG  GLU A 445     -33.114  42.447   0.645  1.00 87.01           C  
ATOM   2870  CD  GLU A 445     -32.816  42.246  -0.837  1.00103.93           C  
ATOM   2871  OE1 GLU A 445     -31.704  41.775  -1.167  1.00 98.29           O  
ATOM   2872  OE2 GLU A 445     -33.695  42.555  -1.672  1.00 93.18           O  
ATOM   2873  N   ALA A 446     -30.952  40.876   4.705  1.00 67.49           N  
ATOM   2874  CA  ALA A 446     -30.252  39.840   5.456  1.00 65.85           C  
ATOM   2875  C   ALA A 446     -31.225  38.917   6.180  1.00 65.30           C  
ATOM   2876  O   ALA A 446     -31.041  37.695   6.188  1.00 52.08           O  
ATOM   2877  CB  ALA A 446     -29.285  40.482   6.451  1.00 57.52           C  
ATOM   2878  N   GLU A 447     -32.268  39.481   6.793  1.00 68.00           N  
ATOM   2879  CA  GLU A 447     -33.227  38.650   7.515  1.00 57.80           C  
ATOM   2880  C   GLU A 447     -33.985  37.728   6.567  1.00 59.83           C  
ATOM   2881  O   GLU A 447     -34.220  36.558   6.885  1.00 68.37           O  
ATOM   2882  CB  GLU A 447     -34.197  39.532   8.297  1.00 68.47           C  
ATOM   2883  CG  GLU A 447     -35.194  38.756   9.148  1.00 82.26           C  
ATOM   2884  CD  GLU A 447     -36.126  39.663   9.928  1.00 87.64           C  
ATOM   2885  OE1 GLU A 447     -36.009  40.899   9.787  1.00 87.09           O  
ATOM   2886  OE2 GLU A 447     -36.975  39.139  10.680  1.00118.51           O  
ATOM   2887  N   THR A 448     -34.372  38.234   5.396  1.00 54.74           N  
ATOM   2888  CA  THR A 448     -35.082  37.405   4.427  1.00 61.19           C  
ATOM   2889  C   THR A 448     -34.209  36.255   3.938  1.00 64.26           C  
ATOM   2890  O   THR A 448     -34.669  35.107   3.831  1.00 56.33           O  
ATOM   2891  CB  THR A 448     -35.532  38.268   3.253  1.00 73.11           C  
ATOM   2892  OG1 THR A 448     -36.380  39.316   3.736  1.00 77.04           O  
ATOM   2893  CG2 THR A 448     -36.277  37.433   2.213  1.00 67.57           C  
ATOM   2894  N   ILE A 449     -32.944  36.546   3.627  1.00 58.83           N  
ATOM   2895  CA  ILE A 449     -32.033  35.507   3.163  1.00 58.95           C  
ATOM   2896  C   ILE A 449     -31.783  34.490   4.270  1.00 55.98           C  
ATOM   2897  O   ILE A 449     -31.700  33.282   4.014  1.00 40.90           O  
ATOM   2898  CB  ILE A 449     -30.726  36.145   2.654  1.00 57.73           C  
ATOM   2899  CG1 ILE A 449     -31.015  36.998   1.412  1.00 55.67           C  
ATOM   2900  CG2 ILE A 449     -29.679  35.070   2.338  1.00 50.52           C  
ATOM   2901  CD1 ILE A 449     -29.825  37.803   0.908  1.00 56.08           C  
ATOM   2902  N   GLY A 450     -31.667  34.952   5.516  1.00 54.05           N  
ATOM   2903  CA  GLY A 450     -31.538  34.020   6.624  1.00 45.09           C  
ATOM   2904  C   GLY A 450     -32.754  33.128   6.759  1.00 46.87           C  
ATOM   2905  O   GLY A 450     -32.635  31.934   7.051  1.00 44.00           O  
ATOM   2906  N   ASN A 451     -33.944  33.695   6.540  1.00 55.99           N  
ATOM   2907  CA  ASN A 451     -35.162  32.894   6.564  1.00 53.73           C  
ATOM   2908  C   ASN A 451     -35.137  31.835   5.473  1.00 40.73           C  
ATOM   2909  O   ASN A 451     -35.568  30.700   5.689  1.00 40.14           O  
ATOM   2910  CB  ASN A 451     -36.386  33.797   6.410  1.00 55.73           C  
ATOM   2911  CG  ASN A 451     -36.554  34.751   7.578  1.00 65.33           C  
ATOM   2912  OD1 ASN A 451     -36.032  34.513   8.668  1.00 62.54           O  
ATOM   2913  ND2 ASN A 451     -37.291  35.836   7.358  1.00 70.08           N  
ATOM   2914  N   LEU A 452     -34.635  32.187   4.290  1.00 46.97           N  
ATOM   2915  CA  LEU A 452     -34.522  31.197   3.220  1.00 45.44           C  
ATOM   2916  C   LEU A 452     -33.523  30.101   3.579  1.00 39.79           C  
ATOM   2917  O   LEU A 452     -33.785  28.915   3.347  1.00 36.96           O  
ATOM   2918  CB  LEU A 452     -34.122  31.879   1.911  1.00 39.34           C  
ATOM   2919  CG  LEU A 452     -35.166  32.812   1.302  1.00 42.18           C  
ATOM   2920  CD1 LEU A 452     -34.573  33.595   0.144  1.00 40.87           C  
ATOM   2921  CD2 LEU A 452     -36.386  32.015   0.856  1.00 37.04           C  
ATOM   2922  N   ILE A 453     -32.375  30.480   4.148  1.00 38.23           N  
ATOM   2923  CA  ILE A 453     -31.372  29.494   4.555  1.00 41.80           C  
ATOM   2924  C   ILE A 453     -31.948  28.541   5.593  1.00 41.29           C  
ATOM   2925  O   ILE A 453     -31.685  27.332   5.565  1.00 36.65           O  
ATOM   2926  CB  ILE A 453     -30.113  30.200   5.089  1.00 37.05           C  
ATOM   2927  CG1 ILE A 453     -29.408  30.949   3.961  1.00 37.13           C  
ATOM   2928  CG2 ILE A 453     -29.160  29.194   5.727  1.00 29.88           C  
ATOM   2929  CD1 ILE A 453     -28.500  32.057   4.438  1.00 38.95           C  
ATOM   2930  N   GLU A 454     -32.711  29.075   6.547  1.00 39.20           N  
ATOM   2931  CA  GLU A 454     -33.335  28.233   7.564  1.00 42.77           C  
ATOM   2932  C   GLU A 454     -34.399  27.328   6.949  1.00 40.42           C  
ATOM   2933  O   GLU A 454     -34.422  26.118   7.204  1.00 43.27           O  
ATOM   2934  CB  GLU A 454     -33.932  29.114   8.662  1.00 50.39           C  
ATOM   2935  CG  GLU A 454     -34.426  28.357   9.886  1.00 53.03           C  
ATOM   2936  CD  GLU A 454     -34.871  29.286  11.006  1.00 63.50           C  
ATOM   2937  OE1 GLU A 454     -35.441  28.791  12.002  1.00 70.84           O  
ATOM   2938  OE2 GLU A 454     -34.647  30.512  10.890  1.00 72.45           O  
ATOM   2939  N   GLU A 455     -35.283  27.902   6.128  1.00 45.72           N  
ATOM   2940  CA  GLU A 455     -36.360  27.160   5.478  1.00 44.77           C  
ATOM   2941  C   GLU A 455     -35.889  25.834   4.892  1.00 49.88           C  
ATOM   2942  O   GLU A 455     -36.511  24.789   5.110  1.00 48.81           O  
ATOM   2943  CB  GLU A 455     -36.972  28.025   4.368  1.00 55.80           C  
ATOM   2944  CG  GLU A 455     -38.278  28.724   4.726  1.00 64.35           C  
ATOM   2945  CD  GLU A 455     -38.834  29.562   3.570  1.00 69.90           C  
ATOM   2946  OE1 GLU A 455     -38.879  30.808   3.689  1.00 59.74           O  
ATOM   2947  OE2 GLU A 455     -39.217  28.975   2.531  1.00 70.01           O  
ATOM   2948  N   CYS A 456     -34.795  25.864   4.129  1.00 43.62           N  
ATOM   2949  CA  CYS A 456     -34.345  24.697   3.380  1.00 43.60           C  
ATOM   2950  C   CYS A 456     -33.464  23.759   4.194  1.00 42.28           C  
ATOM   2951  O   CYS A 456     -32.984  22.759   3.645  1.00 33.22           O  
ATOM   2952  CB  CYS A 456     -33.591  25.139   2.117  1.00 45.71           C  
ATOM   2953  SG  CYS A 456     -32.052  26.047   2.411  1.00 34.61           S  
ATOM   2954  N   GLY A 457     -33.259  24.038   5.483  1.00 43.21           N  
ATOM   2955  CA  GLY A 457     -32.382  23.241   6.313  1.00 35.56           C  
ATOM   2956  C   GLY A 457     -30.945  23.712   6.357  1.00 35.11           C  
ATOM   2957  O   GLY A 457     -30.132  23.102   7.062  1.00 37.47           O  
ATOM   2958  N   GLY A 458     -30.608  24.788   5.648  1.00 39.08           N  
ATOM   2959  CA  GLY A 458     -29.226  25.238   5.622  1.00 39.89           C  
ATOM   2960  C   GLY A 458     -28.708  25.600   6.996  1.00 33.54           C  
ATOM   2961  O   GLY A 458     -27.569  25.277   7.347  1.00 35.28           O  
ATOM   2962  N   LEU A 459     -29.534  26.276   7.795  1.00 43.12           N  
ATOM   2963  CA  LEU A 459     -29.085  26.713   9.110  1.00 39.47           C  
ATOM   2964  C   LEU A 459     -28.736  25.525   9.998  1.00 34.64           C  
ATOM   2965  O   LEU A 459     -27.734  25.559  10.719  1.00 39.21           O  
ATOM   2966  CB  LEU A 459     -30.158  27.576   9.772  1.00 53.99           C  
ATOM   2967  CG  LEU A 459     -29.839  28.048  11.191  1.00 44.49           C  
ATOM   2968  CD1 LEU A 459     -28.533  28.819  11.216  1.00 35.05           C  
ATOM   2969  CD2 LEU A 459     -30.983  28.896  11.724  1.00 53.39           C  
ATOM   2970  N   GLU A 460     -29.565  24.480   9.982  1.00 31.84           N  
ATOM   2971  CA  GLU A 460     -29.236  23.269  10.727  1.00 42.71           C  
ATOM   2972  C   GLU A 460     -27.896  22.700  10.278  1.00 43.79           C  
ATOM   2973  O   GLU A 460     -27.104  22.218  11.099  1.00 39.58           O  
ATOM   2974  CB  GLU A 460     -30.343  22.233  10.549  1.00 45.97           C  
ATOM   2975  CG  GLU A 460     -30.122  20.946  11.322  1.00 58.70           C  
ATOM   2976  CD  GLU A 460     -31.254  19.956  11.129  1.00 90.81           C  
ATOM   2977  OE1 GLU A 460     -32.154  20.234  10.305  1.00 80.31           O  
ATOM   2978  OE2 GLU A 460     -31.245  18.902  11.802  1.00 76.98           O  
ATOM   2979  N   LYS A 461     -27.622  22.760   8.973  1.00 41.03           N  
ATOM   2980  CA  LYS A 461     -26.356  22.261   8.447  1.00 39.78           C  
ATOM   2981  C   LYS A 461     -25.176  23.088   8.950  1.00 33.73           C  
ATOM   2982  O   LYS A 461     -24.125  22.535   9.289  1.00 32.36           O  
ATOM   2983  CB  LYS A 461     -26.407  22.257   6.922  1.00 37.12           C  
ATOM   2984  CG  LYS A 461     -27.075  21.032   6.343  1.00 42.98           C  
ATOM   2985  CD  LYS A 461     -28.112  21.381   5.296  1.00 55.52           C  
ATOM   2986  CE  LYS A 461     -28.483  20.166   4.469  1.00 42.97           C  
ATOM   2987  NZ  LYS A 461     -29.891  20.235   3.992  1.00 54.79           N  
ATOM   2988  N   ILE A 462     -25.327  24.413   9.002  1.00 24.83           N  
ATOM   2989  CA  ILE A 462     -24.263  25.273   9.527  1.00 35.53           C  
ATOM   2990  C   ILE A 462     -24.023  24.974  11.005  1.00 36.96           C  
ATOM   2991  O   ILE A 462     -22.877  24.820  11.463  1.00 34.36           O  
ATOM   2992  CB  ILE A 462     -24.626  26.752   9.297  1.00 34.82           C  
ATOM   2993  CG1 ILE A 462     -24.797  27.025   7.801  1.00 34.18           C  
ATOM   2994  CG2 ILE A 462     -23.558  27.674   9.874  1.00 34.28           C  
ATOM   2995  CD1 ILE A 462     -25.471  28.338   7.486  1.00 24.91           C  
ATOM   2996  N   GLU A 463     -25.109  24.904  11.776  1.00 35.95           N  
ATOM   2997  CA  GLU A 463     -25.007  24.539  13.183  1.00 39.33           C  
ATOM   2998  C   GLU A 463     -24.220  23.248  13.341  1.00 33.23           C  
ATOM   2999  O   GLU A 463     -23.313  23.157  14.174  1.00 39.89           O  
ATOM   3000  CB  GLU A 463     -26.409  24.411  13.792  1.00 46.51           C  
ATOM   3001  CG  GLU A 463     -27.118  25.747  14.006  1.00 45.32           C  
ATOM   3002  CD  GLU A 463     -28.586  25.589  14.374  1.00 52.30           C  
ATOM   3003  OE1 GLU A 463     -29.075  24.437  14.429  1.00 45.43           O  
ATOM   3004  OE2 GLU A 463     -29.251  26.623  14.608  1.00 48.08           O  
ATOM   3005  N   GLN A 464     -24.534  22.239  12.526  1.00 31.11           N  
ATOM   3006  CA  GLN A 464     -23.801  20.980  12.614  1.00 41.03           C  
ATOM   3007  C   GLN A 464     -22.333  21.165  12.238  1.00 39.60           C  
ATOM   3008  O   GLN A 464     -21.448  20.541  12.834  1.00 36.08           O  
ATOM   3009  CB  GLN A 464     -24.459  19.928  11.721  1.00 37.53           C  
ATOM   3010  CG  GLN A 464     -25.720  19.321  12.313  1.00 52.37           C  
ATOM   3011  CD  GLN A 464     -25.472  18.719  13.683  1.00 69.92           C  
ATOM   3012  OE1 GLN A 464     -26.148  19.061  14.655  1.00 71.30           O  
ATOM   3013  NE2 GLN A 464     -24.488  17.826  13.770  1.00 58.50           N  
ATOM   3014  N   LEU A 465     -22.056  22.012  11.244  1.00 36.89           N  
ATOM   3015  CA  LEU A 465     -20.679  22.266  10.836  1.00 26.85           C  
ATOM   3016  C   LEU A 465     -19.862  22.878  11.960  1.00 33.73           C  
ATOM   3017  O   LEU A 465     -18.629  22.812  11.929  1.00 32.73           O  
ATOM   3018  CB  LEU A 465     -20.653  23.189   9.617  1.00 39.57           C  
ATOM   3019  CG  LEU A 465     -21.048  22.567   8.271  1.00 40.96           C  
ATOM   3020  CD1 LEU A 465     -21.057  23.622   7.178  1.00 32.50           C  
ATOM   3021  CD2 LEU A 465     -20.102  21.442   7.903  1.00 32.91           C  
ATOM   3022  N   GLN A 466     -20.523  23.503  12.933  1.00 36.75           N  
ATOM   3023  CA  GLN A 466     -19.795  23.974  14.114  1.00 40.74           C  
ATOM   3024  C   GLN A 466     -18.952  22.867  14.747  1.00 41.22           C  
ATOM   3025  O   GLN A 466     -17.952  23.155  15.415  1.00 30.29           O  
ATOM   3026  CB  GLN A 466     -20.753  24.537  15.163  1.00 32.20           C  
ATOM   3027  CG  GLN A 466     -21.365  25.858  14.777  1.00 40.84           C  
ATOM   3028  CD  GLN A 466     -22.158  26.467  15.900  1.00 40.12           C  
ATOM   3029  OE1 GLN A 466     -22.009  27.647  16.208  1.00 42.99           O  
ATOM   3030  NE2 GLN A 466     -23.014  25.669  16.516  1.00 36.39           N  
ATOM   3031  N   ASN A 467     -19.338  21.601  14.565  1.00 39.23           N  
ATOM   3032  CA  ASN A 467     -18.577  20.473  15.090  1.00 36.02           C  
ATOM   3033  C   ASN A 467     -17.721  19.795  14.029  1.00 36.07           C  
ATOM   3034  O   ASN A 467     -17.321  18.641  14.211  1.00 35.51           O  
ATOM   3035  CB  ASN A 467     -19.509  19.443  15.723  1.00 45.56           C  
ATOM   3036  CG  ASN A 467     -20.326  20.011  16.857  1.00 58.41           C  
ATOM   3037  OD1 ASN A 467     -21.522  19.739  16.965  1.00 56.59           O  
ATOM   3038  ND2 ASN A 467     -19.688  20.808  17.716  1.00 52.87           N  
ATOM   3039  N   HIS A 468     -17.417  20.492  12.940  1.00 41.74           N  
ATOM   3040  CA  HIS A 468     -16.616  19.921  11.867  1.00 33.38           C  
ATOM   3041  C   HIS A 468     -15.162  19.803  12.306  1.00 32.34           C  
ATOM   3042  O   HIS A 468     -14.676  20.589  13.118  1.00 42.09           O  
ATOM   3043  CB  HIS A 468     -16.721  20.799  10.618  1.00 35.84           C  
ATOM   3044  CG  HIS A 468     -16.342  20.110   9.347  1.00 34.90           C  
ATOM   3045  ND1 HIS A 468     -15.045  20.050   8.882  1.00 36.01           N  
ATOM   3046  CD2 HIS A 468     -17.101  19.478   8.422  1.00 48.53           C  
ATOM   3047  CE1 HIS A 468     -15.021  19.395   7.735  1.00 37.91           C  
ATOM   3048  NE2 HIS A 468     -16.256  19.039   7.432  1.00 40.39           N  
ATOM   3049  N   GLU A 469     -14.465  18.808  11.749  1.00 38.43           N  
ATOM   3050  CA  GLU A 469     -13.047  18.619  12.051  1.00 38.22           C  
ATOM   3051  C   GLU A 469     -12.219  19.835  11.651  1.00 37.70           C  
ATOM   3052  O   GLU A 469     -11.297  20.233  12.371  1.00 38.19           O  
ATOM   3053  CB  GLU A 469     -12.534  17.369  11.336  1.00 39.33           C  
ATOM   3054  CG  GLU A 469     -11.009  17.232  11.274  1.00 57.62           C  
ATOM   3055  CD  GLU A 469     -10.557  16.020  10.455  1.00 70.82           C  
ATOM   3056  OE1 GLU A 469      -9.328  15.798  10.338  1.00 84.39           O  
ATOM   3057  OE2 GLU A 469     -11.431  15.293   9.923  1.00 56.15           O  
ATOM   3058  N   ASN A 470     -12.532  20.435  10.506  1.00 42.90           N  
ATOM   3059  CA  ASN A 470     -11.688  21.472   9.933  1.00 36.17           C  
ATOM   3060  C   ASN A 470     -11.824  22.777  10.705  1.00 30.30           C  
ATOM   3061  O   ASN A 470     -12.929  23.282  10.908  1.00 32.16           O  
ATOM   3062  CB  ASN A 470     -12.054  21.691   8.466  1.00 37.46           C  
ATOM   3063  CG  ASN A 470     -11.112  22.640   7.764  1.00 36.91           C  
ATOM   3064  OD1 ASN A 470     -11.230  23.857   7.897  1.00 46.64           O  
ATOM   3065  ND2 ASN A 470     -10.177  22.091   6.998  1.00 47.95           N  
ATOM   3066  N   GLU A 471     -10.681  23.333  11.107  1.00 41.42           N  
ATOM   3067  CA  GLU A 471     -10.638  24.593  11.840  1.00 42.59           C  
ATOM   3068  C   GLU A 471     -11.402  25.692  11.103  1.00 42.90           C  
ATOM   3069  O   GLU A 471     -12.327  26.307  11.645  1.00 36.52           O  
ATOM   3070  CB  GLU A 471      -9.170  24.982  12.052  1.00 58.06           C  
ATOM   3071  CG  GLU A 471      -8.922  26.371  12.625  1.00 76.53           C  
ATOM   3072  CD  GLU A 471      -7.760  27.092  11.942  1.00 86.09           C  
ATOM   3073  OE1 GLU A 471      -8.006  28.145  11.304  1.00 72.99           O  
ATOM   3074  OE2 GLU A 471      -6.609  26.601  12.026  1.00 96.75           O  
ATOM   3075  N   ASP A 472     -11.011  25.957   9.855  1.00 46.94           N  
ATOM   3076  CA  ASP A 472     -11.606  27.056   9.100  1.00 47.38           C  
ATOM   3077  C   ASP A 472     -13.118  26.902   8.980  1.00 42.80           C  
ATOM   3078  O   ASP A 472     -13.864  27.881   9.120  1.00 42.95           O  
ATOM   3079  CB  ASP A 472     -10.962  27.136   7.715  1.00 42.83           C  
ATOM   3080  CG  ASP A 472      -9.468  27.460   7.774  1.00 59.11           C  
ATOM   3081  OD1 ASP A 472      -9.081  28.406   8.496  1.00 48.18           O  
ATOM   3082  OD2 ASP A 472      -8.677  26.759   7.102  1.00 60.92           O  
ATOM   3083  N   ILE A 473     -13.592  25.679   8.739  1.00 30.23           N  
ATOM   3084  CA  ILE A 473     -15.024  25.466   8.551  1.00 26.69           C  
ATOM   3085  C   ILE A 473     -15.790  25.784   9.835  1.00 34.39           C  
ATOM   3086  O   ILE A 473     -16.766  26.541   9.813  1.00 30.70           O  
ATOM   3087  CB  ILE A 473     -15.288  24.036   8.048  1.00 26.17           C  
ATOM   3088  CG1 ILE A 473     -15.007  23.967   6.541  1.00 30.21           C  
ATOM   3089  CG2 ILE A 473     -16.712  23.594   8.358  1.00 27.62           C  
ATOM   3090  CD1 ILE A 473     -14.991  22.566   5.978  1.00 28.82           C  
ATOM   3091  N   TYR A 474     -15.377  25.215  10.974  1.00 33.64           N  
ATOM   3092  CA  TYR A 474     -16.189  25.435  12.169  1.00 36.30           C  
ATOM   3093  C   TYR A 474     -16.041  26.864  12.685  1.00 36.82           C  
ATOM   3094  O   TYR A 474     -17.018  27.442  13.182  1.00 34.81           O  
ATOM   3095  CB  TYR A 474     -15.886  24.389  13.254  1.00 32.87           C  
ATOM   3096  CG  TYR A 474     -14.559  24.431  14.001  1.00 31.14           C  
ATOM   3097  CD1 TYR A 474     -14.222  25.493  14.833  1.00 36.97           C  
ATOM   3098  CD2 TYR A 474     -13.684  23.352  13.947  1.00 28.95           C  
ATOM   3099  CE1 TYR A 474     -13.021  25.504  15.539  1.00 27.05           C  
ATOM   3100  CE2 TYR A 474     -12.496  23.346  14.656  1.00 30.47           C  
ATOM   3101  CZ  TYR A 474     -12.166  24.425  15.443  1.00 30.04           C  
ATOM   3102  OH  TYR A 474     -10.981  24.410  16.133  1.00 31.52           O  
ATOM   3103  N   LYS A 475     -14.862  27.468  12.521  1.00 35.60           N  
ATOM   3104  CA  LYS A 475     -14.716  28.890  12.819  1.00 32.25           C  
ATOM   3105  C   LYS A 475     -15.707  29.720  12.012  1.00 43.84           C  
ATOM   3106  O   LYS A 475     -16.398  30.592  12.559  1.00 41.53           O  
ATOM   3107  CB  LYS A 475     -13.283  29.342  12.536  1.00 45.42           C  
ATOM   3108  CG  LYS A 475     -12.436  29.560  13.781  1.00 52.53           C  
ATOM   3109  CD  LYS A 475     -11.026  29.043  13.587  1.00 66.24           C  
ATOM   3110  CE  LYS A 475     -10.073  29.562  14.658  1.00 64.84           C  
ATOM   3111  NZ  LYS A 475      -8.711  28.976  14.529  1.00 62.42           N  
ATOM   3112  N   LEU A 476     -15.803  29.459  10.700  1.00 38.25           N  
ATOM   3113  CA  LEU A 476     -16.706  30.255   9.879  1.00 40.18           C  
ATOM   3114  C   LEU A 476     -18.165  29.959  10.202  1.00 34.23           C  
ATOM   3115  O   LEU A 476     -19.008  30.857  10.113  1.00 27.57           O  
ATOM   3116  CB  LEU A 476     -16.426  30.010   8.397  1.00 45.31           C  
ATOM   3117  CG  LEU A 476     -17.181  30.901   7.404  1.00 38.53           C  
ATOM   3118  CD1 LEU A 476     -17.088  32.379   7.764  1.00 31.21           C  
ATOM   3119  CD2 LEU A 476     -16.638  30.675   6.004  1.00 41.27           C  
ATOM   3120  N   ALA A 477     -18.484  28.715  10.564  1.00 31.59           N  
ATOM   3121  CA  ALA A 477     -19.848  28.383  10.963  1.00 34.89           C  
ATOM   3122  C   ALA A 477     -20.255  29.188  12.189  1.00 38.68           C  
ATOM   3123  O   ALA A 477     -21.358  29.756  12.244  1.00 33.71           O  
ATOM   3124  CB  ALA A 477     -19.968  26.883  11.243  1.00 26.73           C  
ATOM   3125  N   TYR A 478     -19.363  29.246  13.185  1.00 49.01           N  
ATOM   3126  CA  TYR A 478     -19.593  30.110  14.338  1.00 48.34           C  
ATOM   3127  C   TYR A 478     -19.805  31.550  13.891  1.00 43.95           C  
ATOM   3128  O   TYR A 478     -20.776  32.197  14.294  1.00 41.90           O  
ATOM   3129  CB  TYR A 478     -18.416  30.030  15.316  1.00 47.58           C  
ATOM   3130  CG  TYR A 478     -18.297  28.730  16.093  1.00 62.57           C  
ATOM   3131  CD1 TYR A 478     -19.294  28.328  16.978  1.00 61.36           C  
ATOM   3132  CD2 TYR A 478     -17.168  27.924  15.970  1.00 54.91           C  
ATOM   3133  CE1 TYR A 478     -19.181  27.143  17.702  1.00 53.04           C  
ATOM   3134  CE2 TYR A 478     -17.043  26.739  16.688  1.00 51.76           C  
ATOM   3135  CZ  TYR A 478     -18.051  26.354  17.552  1.00 64.25           C  
ATOM   3136  OH  TYR A 478     -17.923  25.179  18.266  1.00 60.28           O  
ATOM   3137  N   GLU A 479     -18.888  32.079  13.079  1.00 39.11           N  
ATOM   3138  CA  GLU A 479     -18.995  33.470  12.645  1.00 39.36           C  
ATOM   3139  C   GLU A 479     -20.361  33.749  12.035  1.00 45.14           C  
ATOM   3140  O   GLU A 479     -21.022  34.734  12.379  1.00 36.80           O  
ATOM   3141  CB  GLU A 479     -17.897  33.794  11.633  1.00 34.48           C  
ATOM   3142  CG  GLU A 479     -16.589  34.247  12.227  1.00 50.89           C  
ATOM   3143  CD  GLU A 479     -15.576  34.605  11.152  1.00 65.90           C  
ATOM   3144  OE1 GLU A 479     -15.981  35.229  10.145  1.00 65.82           O  
ATOM   3145  OE2 GLU A 479     -14.385  34.249  11.297  1.00 60.37           O  
ATOM   3146  N   ILE A 480     -20.793  32.882  11.115  1.00 45.78           N  
ATOM   3147  CA  ILE A 480     -22.046  33.104  10.394  1.00 49.55           C  
ATOM   3148  C   ILE A 480     -23.223  33.082  11.360  1.00 48.33           C  
ATOM   3149  O   ILE A 480     -24.073  33.982  11.350  1.00 45.69           O  
ATOM   3150  CB  ILE A 480     -22.212  32.056   9.279  1.00 42.76           C  
ATOM   3151  CG1 ILE A 480     -21.283  32.385   8.111  1.00 44.78           C  
ATOM   3152  CG2 ILE A 480     -23.668  31.984   8.798  1.00 39.76           C  
ATOM   3153  CD1 ILE A 480     -21.016  31.217   7.202  1.00 40.09           C  
ATOM   3154  N   ILE A 481     -23.307  32.042  12.191  1.00 45.16           N  
ATOM   3155  CA  ILE A 481     -24.418  31.952  13.136  1.00 50.67           C  
ATOM   3156  C   ILE A 481     -24.449  33.187  14.024  1.00 46.06           C  
ATOM   3157  O   ILE A 481     -25.486  33.841  14.177  1.00 49.05           O  
ATOM   3158  CB  ILE A 481     -24.314  30.659  13.963  1.00 57.88           C  
ATOM   3159  CG1 ILE A 481     -24.656  29.457  13.085  1.00 52.34           C  
ATOM   3160  CG2 ILE A 481     -25.250  30.709  15.173  1.00 58.94           C  
ATOM   3161  CD1 ILE A 481     -24.017  28.173  13.547  1.00 52.53           C  
ATOM   3162  N   ASP A 482     -23.305  33.535  14.610  1.00 51.13           N  
ATOM   3163  CA  ASP A 482     -23.260  34.657  15.538  1.00 51.59           C  
ATOM   3164  C   ASP A 482     -23.683  35.948  14.860  1.00 52.57           C  
ATOM   3165  O   ASP A 482     -24.436  36.741  15.437  1.00 66.26           O  
ATOM   3166  CB  ASP A 482     -21.852  34.795  16.115  1.00 52.18           C  
ATOM   3167  CG  ASP A 482     -21.811  35.695  17.321  1.00 59.03           C  
ATOM   3168  OD1 ASP A 482     -22.692  35.545  18.196  1.00 58.73           O  
ATOM   3169  OD2 ASP A 482     -20.894  36.542  17.400  1.00 62.00           O  
ATOM   3170  N   GLN A 483     -23.223  36.173  13.630  1.00 51.03           N  
ATOM   3171  CA  GLN A 483     -23.454  37.446  12.967  1.00 49.76           C  
ATOM   3172  C   GLN A 483     -24.834  37.554  12.332  1.00 48.22           C  
ATOM   3173  O   GLN A 483     -25.286  38.675  12.076  1.00 52.37           O  
ATOM   3174  CB  GLN A 483     -22.385  37.675  11.897  1.00 49.31           C  
ATOM   3175  CG  GLN A 483     -22.454  39.039  11.231  1.00 55.74           C  
ATOM   3176  CD  GLN A 483     -21.318  39.254  10.250  1.00 67.32           C  
ATOM   3177  OE1 GLN A 483     -20.407  38.434  10.152  1.00 68.30           O  
ATOM   3178  NE2 GLN A 483     -21.372  40.357   9.511  1.00 71.60           N  
ATOM   3179  N   PHE A 484     -25.518  36.433  12.075  1.00 47.18           N  
ATOM   3180  CA  PHE A 484     -26.770  36.487  11.316  1.00 46.75           C  
ATOM   3181  C   PHE A 484     -27.895  35.616  11.856  1.00 43.29           C  
ATOM   3182  O   PHE A 484     -29.046  35.840  11.463  1.00 43.99           O  
ATOM   3183  CB  PHE A 484     -26.520  36.106   9.849  1.00 43.37           C  
ATOM   3184  CG  PHE A 484     -25.565  37.027   9.141  1.00 38.99           C  
ATOM   3185  CD1 PHE A 484     -25.978  38.278   8.712  1.00 39.21           C  
ATOM   3186  CD2 PHE A 484     -24.256  36.646   8.913  1.00 38.89           C  
ATOM   3187  CE1 PHE A 484     -25.103  39.132   8.066  1.00 30.29           C  
ATOM   3188  CE2 PHE A 484     -23.378  37.495   8.264  1.00 42.68           C  
ATOM   3189  CZ  PHE A 484     -23.803  38.739   7.840  1.00 37.84           C  
ATOM   3190  N   PHE A 485     -27.641  34.646  12.728  1.00 49.06           N  
ATOM   3191  CA  PHE A 485     -28.690  33.783  13.266  1.00 60.02           C  
ATOM   3192  C   PHE A 485     -28.702  33.804  14.793  1.00 62.13           C  
ATOM   3193  O   PHE A 485     -28.922  32.780  15.448  1.00 47.72           O  
ATOM   3194  CB  PHE A 485     -28.532  32.356  12.749  1.00 56.77           C  
ATOM   3195  CG  PHE A 485     -28.579  32.245  11.256  1.00 52.29           C  
ATOM   3196  CD1 PHE A 485     -29.767  31.955  10.607  1.00 53.28           C  
ATOM   3197  CD2 PHE A 485     -27.435  32.432  10.498  1.00 49.47           C  
ATOM   3198  CE1 PHE A 485     -29.814  31.846   9.230  1.00 53.07           C  
ATOM   3199  CE2 PHE A 485     -27.475  32.329   9.123  1.00 47.44           C  
ATOM   3200  CZ  PHE A 485     -28.669  32.034   8.487  1.00 52.41           C  
ATOM   3201  N   SER A 486     -28.479  34.982  15.379  1.00 76.81           N  
ATOM   3202  CA  SER A 486     -28.432  35.149  16.829  1.00 85.36           C  
ATOM   3203  C   SER A 486     -29.144  36.449  17.212  1.00 92.03           C  
ATOM   3204  O   SER A 486     -28.598  37.321  17.885  1.00 88.20           O  
ATOM   3205  CB  SER A 486     -26.987  35.133  17.331  1.00 76.67           C  
ATOM   3206  OG  SER A 486     -26.535  33.809  17.553  1.00 78.27           O  
ATOM   3207  N   SER A 487     -30.395  36.580  16.779  1.00109.90           N  
ATOM   3208  CA  SER A 487     -31.184  37.778  17.048  1.00127.08           C  
ATOM   3209  C   SER A 487     -32.289  37.481  18.061  1.00122.06           C  
ATOM   3210  O   SER A 487     -33.264  36.797  17.752  1.00104.22           O  
ATOM   3211  CB  SER A 487     -31.784  38.327  15.749  1.00112.56           C  
ATOM   3212  OG  SER A 487     -32.797  37.473  15.245  1.00 98.96           O  
TER    3213      SER A 487                                                      
ATOM   3214  N   CYS B 419     -10.200  29.366  -0.312  1.00 51.13           N  
ATOM   3215  CA  CYS B 419     -10.386  30.786  -0.597  1.00 64.89           C  
ATOM   3216  C   CYS B 419     -10.928  30.988  -2.016  1.00 55.87           C  
ATOM   3217  O   CYS B 419     -10.533  30.287  -2.947  1.00 47.87           O  
ATOM   3218  CB  CYS B 419      -9.070  31.543  -0.422  1.00 68.71           C  
ATOM   3219  SG  CYS B 419      -9.291  33.297  -0.074  1.00 73.19           S  
ATOM   3220  N   LEU B 420     -11.825  31.958  -2.175  1.00 52.95           N  
ATOM   3221  CA  LEU B 420     -12.512  32.163  -3.442  1.00 38.39           C  
ATOM   3222  C   LEU B 420     -11.603  32.839  -4.463  1.00 35.87           C  
ATOM   3223  O   LEU B 420     -10.682  33.579  -4.114  1.00 33.92           O  
ATOM   3224  CB  LEU B 420     -13.771  33.007  -3.238  1.00 26.47           C  
ATOM   3225  CG  LEU B 420     -14.819  32.444  -2.284  1.00 29.44           C  
ATOM   3226  CD1 LEU B 420     -15.987  33.408  -2.182  1.00 29.76           C  
ATOM   3227  CD2 LEU B 420     -15.303  31.077  -2.741  1.00 32.11           C  
ATOM   3228  N   GLY B 421     -11.887  32.587  -5.739  1.00 28.86           N  
ATOM   3229  CA  GLY B 421     -11.116  33.170  -6.821  1.00 24.89           C  
ATOM   3230  C   GLY B 421     -10.926  32.244  -8.008  1.00 24.19           C  
ATOM   3231  O   GLY B 421     -11.406  31.105  -8.011  1.00 22.36           O  
ATOM   3232  N   ARG B 422     -10.245  32.733  -9.035  1.00 18.52           N  
ATOM   3233  CA  ARG B 422      -9.975  31.912 -10.200  1.00 21.85           C  
ATOM   3234  C   ARG B 422      -9.064  30.743  -9.844  1.00 24.66           C  
ATOM   3235  O   ARG B 422      -8.246  30.817  -8.922  1.00 26.35           O  
ATOM   3236  CB  ARG B 422      -9.336  32.749 -11.294  1.00 23.12           C  
ATOM   3237  CG  ARG B 422     -10.223  33.860 -11.783  1.00 22.87           C  
ATOM   3238  CD  ARG B 422      -9.693  34.475 -13.073  1.00 18.54           C  
ATOM   3239  NE  ARG B 422     -10.771  35.154 -13.790  1.00 27.01           N  
ATOM   3240  CZ  ARG B 422     -10.833  36.454 -14.047  1.00 26.07           C  
ATOM   3241  NH1 ARG B 422      -9.863  37.279 -13.673  1.00 35.81           N  
ATOM   3242  NH2 ARG B 422     -11.879  36.933 -14.696  1.00 27.06           N  
ATOM   3243  N   ARG B 423      -9.207  29.656 -10.598  1.00 21.90           N  
ATOM   3244  CA  ARG B 423      -8.465  28.427 -10.359  1.00 25.17           C  
ATOM   3245  C   ARG B 423      -7.935  27.880 -11.679  1.00 19.18           C  
ATOM   3246  O   ARG B 423      -8.579  28.004 -12.725  1.00 20.50           O  
ATOM   3247  CB  ARG B 423      -9.344  27.360  -9.686  1.00 20.04           C  
ATOM   3248  CG  ARG B 423      -9.942  27.782  -8.356  1.00 22.33           C  
ATOM   3249  CD  ARG B 423     -11.043  26.835  -7.929  1.00 20.23           C  
ATOM   3250  NE  ARG B 423     -12.122  26.802  -8.921  1.00 24.70           N  
ATOM   3251  CZ  ARG B 423     -12.788  25.709  -9.290  1.00 23.20           C  
ATOM   3252  NH1 ARG B 423     -12.515  24.528  -8.754  1.00 22.11           N  
ATOM   3253  NH2 ARG B 423     -13.741  25.796 -10.209  1.00 25.17           N  
ATOM   3254  N   VAL B 424      -6.764  27.241 -11.611  1.00 23.93           N  
ATOM   3255  CA  VAL B 424      -6.155  26.584 -12.765  1.00 18.14           C  
ATOM   3256  C   VAL B 424      -6.877  25.265 -13.021  1.00 19.64           C  
ATOM   3257  O   VAL B 424      -7.704  24.836 -12.211  1.00 21.40           O  
ATOM   3258  CB  VAL B 424      -4.644  26.365 -12.551  1.00 30.65           C  
ATOM   3259  CG1 VAL B 424      -3.944  27.681 -12.330  1.00 22.95           C  
ATOM   3260  CG2 VAL B 424      -4.380  25.439 -11.366  1.00 17.16           C  
ATOM   3261  N   VAL B 425      -6.574  24.623 -14.153  1.00 20.99           N  
ATOM   3262  CA  VAL B 425      -7.153  23.321 -14.476  1.00 20.10           C  
ATOM   3263  C   VAL B 425      -7.028  22.395 -13.282  1.00 15.47           C  
ATOM   3264  O   VAL B 425      -5.946  22.240 -12.708  1.00 22.69           O  
ATOM   3265  CB  VAL B 425      -6.453  22.702 -15.700  1.00 27.85           C  
ATOM   3266  CG1 VAL B 425      -6.952  21.292 -15.945  1.00 42.34           C  
ATOM   3267  CG2 VAL B 425      -6.680  23.525 -16.916  1.00 31.21           C  
ATOM   3268  N   GLN B 426      -8.088  21.748 -12.963  1.00 18.25           N  
ATOM   3269  CA  GLN B 426      -8.216  20.875 -11.812  1.00 26.11           C  
ATOM   3270  C   GLN B 426      -7.866  19.436 -12.182  1.00 32.68           C  
ATOM   3271  O   GLN B 426      -7.980  19.046 -13.348  1.00 33.80           O  
ATOM   3272  CB  GLN B 426      -9.642  20.931 -11.267  1.00 22.21           C  
ATOM   3273  CG  GLN B 426     -10.054  22.309 -10.773  1.00 22.67           C  
ATOM   3274  CD  GLN B 426      -9.235  22.760  -9.575  1.00 30.47           C  
ATOM   3275  OE1 GLN B 426      -9.304  22.160  -8.504  1.00 37.11           O  
ATOM   3276  NE2 GLN B 426      -8.435  23.803  -9.758  1.00 26.12           N  
ATOM   3277  N   PRO B 427      -7.437  18.629 -11.210  1.00 30.89           N  
ATOM   3278  CA  PRO B 427      -7.140  17.221 -11.503  1.00 23.98           C  
ATOM   3279  C   PRO B 427      -8.347  16.491 -12.073  1.00 26.04           C  
ATOM   3280  O   PRO B 427      -9.486  16.723 -11.669  1.00 30.35           O  
ATOM   3281  CB  PRO B 427      -6.735  16.657 -10.139  1.00 29.75           C  
ATOM   3282  CG  PRO B 427      -6.205  17.838  -9.391  1.00 35.91           C  
ATOM   3283  CD  PRO B 427      -7.028  19.008  -9.843  1.00 30.28           C  
ATOM   3284  N   GLY B 428      -8.079  15.595 -13.024  1.00 25.23           N  
ATOM   3285  CA  GLY B 428      -9.110  14.822 -13.666  1.00 29.56           C  
ATOM   3286  C   GLY B 428      -9.736  15.481 -14.875  1.00 28.56           C  
ATOM   3287  O   GLY B 428     -10.422  14.798 -15.646  1.00 33.63           O  
ATOM   3288  N   MET B 429      -9.525  16.780 -15.065  1.00 24.58           N  
ATOM   3289  CA  MET B 429     -10.060  17.472 -16.226  1.00 22.88           C  
ATOM   3290  C   MET B 429      -9.171  17.228 -17.433  1.00 23.67           C  
ATOM   3291  O   MET B 429      -7.943  17.177 -17.316  1.00 20.85           O  
ATOM   3292  CB  MET B 429     -10.158  18.977 -15.974  1.00 23.68           C  
ATOM   3293  CG  MET B 429     -11.240  19.385 -14.997  1.00 22.33           C  
ATOM   3294  SD  MET B 429     -11.252  21.164 -14.660  1.00 22.25           S  
ATOM   3295  CE  MET B 429     -12.584  21.250 -13.463  1.00 25.20           C  
ATOM   3296  N   PHE B 430      -9.801  17.094 -18.598  1.00 20.85           N  
ATOM   3297  CA  PHE B 430      -9.081  16.933 -19.852  1.00 24.57           C  
ATOM   3298  C   PHE B 430      -8.048  15.810 -19.744  1.00 28.02           C  
ATOM   3299  O   PHE B 430      -6.855  15.991 -20.016  1.00 20.56           O  
ATOM   3300  CB  PHE B 430      -8.419  18.246 -20.255  1.00 21.76           C  
ATOM   3301  CG  PHE B 430      -9.321  19.435 -20.144  1.00 21.69           C  
ATOM   3302  CD1 PHE B 430     -10.345  19.636 -21.058  1.00 16.94           C  
ATOM   3303  CD2 PHE B 430      -9.138  20.362 -19.135  1.00 18.67           C  
ATOM   3304  CE1 PHE B 430     -11.172  20.734 -20.961  1.00 15.06           C  
ATOM   3305  CE2 PHE B 430      -9.963  21.470 -19.031  1.00 20.42           C  
ATOM   3306  CZ  PHE B 430     -10.983  21.655 -19.945  1.00 17.67           C  
ATOM   3307  N   ALA B 431      -8.522  14.636 -19.329  1.00 21.70           N  
ATOM   3308  CA  ALA B 431      -7.650  13.484 -19.144  1.00 19.72           C  
ATOM   3309  C   ALA B 431      -7.184  12.878 -20.457  1.00 28.06           C  
ATOM   3310  O   ALA B 431      -6.246  12.075 -20.448  1.00 29.25           O  
ATOM   3311  CB  ALA B 431      -8.372  12.417 -18.317  1.00 27.96           C  
ATOM   3312  N   ASP B 432      -7.802  13.251 -21.574  1.00 25.98           N  
ATOM   3313  CA  ASP B 432      -7.509  12.681 -22.886  1.00 20.96           C  
ATOM   3314  C   ASP B 432      -6.460  13.494 -23.635  1.00 20.87           C  
ATOM   3315  O   ASP B 432      -6.655  13.885 -24.783  1.00 22.78           O  
ATOM   3316  CB  ASP B 432      -8.796  12.581 -23.700  1.00 37.97           C  
ATOM   3317  CG  ASP B 432      -9.504  13.947 -23.878  1.00 53.09           C  
ATOM   3318  OD1 ASP B 432      -9.556  14.745 -22.904  1.00 42.63           O  
ATOM   3319  OD2 ASP B 432     -10.020  14.220 -24.991  1.00 33.20           O  
ATOM   3320  N   TYR B 433      -5.328  13.740 -22.995  1.00 18.18           N  
ATOM   3321  CA  TYR B 433      -4.293  14.535 -23.623  1.00 16.46           C  
ATOM   3322  C   TYR B 433      -3.569  13.726 -24.698  1.00 13.80           C  
ATOM   3323  O   TYR B 433      -3.610  12.496 -24.697  1.00 20.35           O  
ATOM   3324  CB  TYR B 433      -3.312  15.045 -22.565  1.00 16.80           C  
ATOM   3325  CG  TYR B 433      -2.725  13.978 -21.669  1.00 23.26           C  
ATOM   3326  CD1 TYR B 433      -1.586  13.276 -22.046  1.00 25.86           C  
ATOM   3327  CD2 TYR B 433      -3.295  13.685 -20.437  1.00 33.27           C  
ATOM   3328  CE1 TYR B 433      -1.034  12.305 -21.223  1.00 33.48           C  
ATOM   3329  CE2 TYR B 433      -2.758  12.718 -19.608  1.00 30.53           C  
ATOM   3330  CZ  TYR B 433      -1.622  12.030 -20.002  1.00 44.41           C  
ATOM   3331  OH  TYR B 433      -1.073  11.063 -19.178  1.00 43.65           O  
ATOM   3332  N   PRO B 434      -2.926  14.387 -25.652  1.00 16.54           N  
ATOM   3333  CA  PRO B 434      -2.169  13.651 -26.671  1.00 22.00           C  
ATOM   3334  C   PRO B 434      -0.969  12.969 -26.046  1.00 17.57           C  
ATOM   3335  O   PRO B 434      -0.278  13.565 -25.209  1.00 20.43           O  
ATOM   3336  CB  PRO B 434      -1.730  14.741 -27.663  1.00 19.50           C  
ATOM   3337  CG  PRO B 434      -2.577  15.922 -27.351  1.00 20.08           C  
ATOM   3338  CD  PRO B 434      -2.894  15.837 -25.893  1.00 14.05           C  
ATOM   3339  N   PRO B 435      -0.685  11.730 -26.419  1.00 20.87           N  
ATOM   3340  CA  PRO B 435       0.422  11.017 -25.778  1.00 19.11           C  
ATOM   3341  C   PRO B 435       1.735  11.761 -25.938  1.00 15.57           C  
ATOM   3342  O   PRO B 435       1.957  12.481 -26.914  1.00 13.10           O  
ATOM   3343  CB  PRO B 435       0.443   9.664 -26.502  1.00 20.97           C  
ATOM   3344  CG  PRO B 435      -0.269   9.894 -27.775  1.00 25.30           C  
ATOM   3345  CD  PRO B 435      -1.317  10.930 -27.478  1.00 17.87           C  
ATOM   3346  N   THR B 436       2.601  11.605 -24.939  1.00 13.91           N  
ATOM   3347  CA  THR B 436       3.942  12.157 -25.039  1.00 16.30           C  
ATOM   3348  C   THR B 436       4.810  11.331 -25.977  1.00 17.03           C  
ATOM   3349  O   THR B 436       5.713  11.876 -26.618  1.00 14.85           O  
ATOM   3350  CB  THR B 436       4.583  12.231 -23.654  1.00 17.66           C  
ATOM   3351  OG1 THR B 436       4.528  10.946 -23.037  1.00 25.94           O  
ATOM   3352  CG2 THR B 436       3.853  13.211 -22.767  1.00 20.29           C  
ATOM   3353  N   LYS B 437       4.542  10.028 -26.090  1.00 18.51           N  
ATOM   3354  CA  LYS B 437       5.384   9.131 -26.864  1.00 14.49           C  
ATOM   3355  C   LYS B 437       4.516   8.175 -27.667  1.00 13.39           C  
ATOM   3356  O   LYS B 437       3.466   7.735 -27.199  1.00 18.32           O  
ATOM   3357  CB  LYS B 437       6.332   8.352 -25.949  1.00 12.52           C  
ATOM   3358  CG  LYS B 437       7.224   9.222 -25.088  1.00 15.24           C  
ATOM   3359  CD  LYS B 437       8.165   8.369 -24.295  1.00 15.18           C  
ATOM   3360  CE  LYS B 437       9.033   9.205 -23.387  1.00 10.83           C  
ATOM   3361  NZ  LYS B 437       9.858   8.362 -22.485  1.00 13.48           N  
ATOM   3362  N   LYS B 438       4.963   7.868 -28.883  1.00 16.91           N  
ATOM   3363  CA  LYS B 438       4.252   6.984 -29.799  1.00 14.80           C  
ATOM   3364  C   LYS B 438       5.248   6.038 -30.448  1.00 14.54           C  
ATOM   3365  O   LYS B 438       6.236   6.487 -31.039  1.00 12.30           O  
ATOM   3366  CB  LYS B 438       3.531   7.762 -30.917  1.00 13.21           C  
ATOM   3367  CG  LYS B 438       2.597   8.840 -30.472  1.00 18.60           C  
ATOM   3368  CD  LYS B 438       1.870   9.441 -31.677  1.00 24.27           C  
ATOM   3369  CE  LYS B 438       1.109  10.702 -31.304  1.00 27.35           C  
ATOM   3370  NZ  LYS B 438       0.361  11.271 -32.461  1.00 35.47           N  
ATOM   3371  N   ALA B 439       4.975   4.745 -30.375  1.00  9.89           N  
ATOM   3372  CA  ALA B 439       5.745   3.774 -31.133  1.00 11.80           C  
ATOM   3373  C   ALA B 439       5.121   3.581 -32.508  1.00 13.16           C  
ATOM   3374  O   ALA B 439       3.907   3.702 -32.678  1.00 17.47           O  
ATOM   3375  CB  ALA B 439       5.812   2.438 -30.387  1.00 14.70           C  
ATOM   3376  N   ARG B 440       5.964   3.303 -33.499  1.00 12.50           N  
ATOM   3377  CA  ARG B 440       5.489   2.980 -34.840  1.00 12.69           C  
ATOM   3378  C   ARG B 440       5.335   1.469 -34.934  1.00 13.71           C  
ATOM   3379  O   ARG B 440       6.322   0.732 -34.897  1.00 16.05           O  
ATOM   3380  CB  ARG B 440       6.434   3.496 -35.919  1.00 13.04           C  
ATOM   3381  CG  ARG B 440       5.923   3.198 -37.315  1.00 16.05           C  
ATOM   3382  CD  ARG B 440       6.844   3.680 -38.422  1.00 20.22           C  
ATOM   3383  NE  ARG B 440       6.320   3.240 -39.707  1.00 21.90           N  
ATOM   3384  CZ  ARG B 440       6.586   3.803 -40.879  1.00 16.95           C  
ATOM   3385  NH1 ARG B 440       7.381   4.865 -40.960  1.00 14.48           N  
ATOM   3386  NH2 ARG B 440       6.031   3.299 -41.973  1.00 19.91           N  
ATOM   3387  N   VAL B 441       4.096   1.011 -35.064  1.00 18.54           N  
ATOM   3388  CA  VAL B 441       3.771  -0.407 -35.066  1.00 22.86           C  
ATOM   3389  C   VAL B 441       3.380  -0.788 -36.483  1.00 15.74           C  
ATOM   3390  O   VAL B 441       2.596  -0.087 -37.131  1.00 20.28           O  
ATOM   3391  CB  VAL B 441       2.655  -0.735 -34.057  1.00 27.98           C  
ATOM   3392  CG1 VAL B 441       2.232  -2.189 -34.162  1.00 32.47           C  
ATOM   3393  CG2 VAL B 441       3.144  -0.454 -32.645  1.00 22.54           C  
ATOM   3394  N   LEU B 442       3.969  -1.868 -36.973  1.00 17.66           N  
ATOM   3395  CA  LEU B 442       3.640  -2.397 -38.284  1.00 21.21           C  
ATOM   3396  C   LEU B 442       2.246  -3.003 -38.245  1.00 25.05           C  
ATOM   3397  O   LEU B 442       1.932  -3.803 -37.358  1.00 35.82           O  
ATOM   3398  CB  LEU B 442       4.669  -3.453 -38.675  1.00 18.94           C  
ATOM   3399  CG  LEU B 442       4.576  -4.032 -40.082  1.00 27.10           C  
ATOM   3400  CD1 LEU B 442       5.373  -3.186 -41.035  1.00 23.85           C  
ATOM   3401  CD2 LEU B 442       5.059  -5.477 -40.091  1.00 20.08           C  
ATOM   3402  N   LEU B 443       1.408  -2.613 -39.196  1.00 29.16           N  
ATOM   3403  CA  LEU B 443       0.054  -3.141 -39.389  1.00 36.22           C  
ATOM   3404  C   LEU B 443      -0.988  -2.480 -38.498  1.00 34.50           C  
ATOM   3405  O   LEU B 443      -2.122  -2.965 -38.450  1.00 29.77           O  
ATOM   3406  CB  LEU B 443      -0.035  -4.654 -39.154  1.00 29.25           C  
ATOM   3407  CG  LEU B 443       0.952  -5.546 -39.906  1.00 25.76           C  
ATOM   3408  CD1 LEU B 443       0.627  -7.008 -39.623  1.00 26.27           C  
ATOM   3409  CD2 LEU B 443       0.935  -5.263 -41.408  1.00 21.27           C  
ATOM   3410  N   ARG B 444      -0.664  -1.401 -37.801  1.00 33.65           N  
ATOM   3411  CA  ARG B 444      -1.649  -0.753 -36.936  1.00 44.54           C  
ATOM   3412  C   ARG B 444      -2.253   0.472 -37.616  1.00 32.48           C  
ATOM   3413  O   ARG B 444      -1.533   1.260 -38.231  1.00 54.70           O  
ATOM   3414  CB  ARG B 444      -1.008  -0.361 -35.606  1.00 37.84           C  
ATOM   3415  CG  ARG B 444      -1.980   0.236 -34.599  1.00 43.07           C  
ATOM   3416  CD  ARG B 444      -1.310   1.267 -33.690  1.00 37.22           C  
ATOM   3417  NE  ARG B 444      -0.643   0.657 -32.541  1.00 52.02           N  
ATOM   3418  CZ  ARG B 444       0.157   1.310 -31.703  1.00 47.06           C  
ATOM   3419  NH1 ARG B 444       0.722   0.671 -30.686  1.00 42.88           N  
ATOM   3420  NH2 ARG B 444       0.400   2.601 -31.883  1.00 51.54           N  
TER    3421      ARG B 444                                                      
HETATM 3422  O   HOH A 601     -24.833  14.899  -6.245  1.00 37.04           O  
HETATM 3423  O   HOH A 602      10.428   8.947 -49.036  1.00 32.83           O  
HETATM 3424  O   HOH A 603     -27.554  18.193   1.334  1.00 37.69           O  
HETATM 3425  O   HOH A 604       7.855  30.602 -36.724  1.00 26.65           O  
HETATM 3426  O   HOH A 605      -2.103  17.465 -20.119  1.00 20.57           O  
HETATM 3427  O   HOH A 606      22.486  11.260 -40.312  1.00 25.43           O  
HETATM 3428  O   HOH A 607      -6.886  30.180  15.736  1.00104.95           O  
HETATM 3429  O   HOH A 608       2.042  -4.107 -22.084  1.00 49.87           O  
HETATM 3430  O   HOH A 609      -0.746  22.526 -19.002  1.00 21.95           O  
HETATM 3431  O   HOH A 610      -1.596  15.128 -35.082  1.00 17.44           O  
HETATM 3432  O   HOH A 611      18.023  19.808 -38.409  1.00 27.56           O  
HETATM 3433  O   HOH A 612     -23.417  16.765 -14.777  1.00 20.71           O  
HETATM 3434  O   HOH A 613      24.298  14.013 -28.284  1.00 12.34           O  
HETATM 3435  O   HOH A 614      16.011  -5.592 -46.727  1.00 33.65           O  
HETATM 3436  O   HOH A 615       8.391  30.282 -21.588  1.00 25.10           O  
HETATM 3437  O   HOH A 616      -9.800  17.998 -43.843  1.00 28.07           O  
HETATM 3438  O   HOH A 617      13.297   1.608 -18.028  1.00 26.11           O  
HETATM 3439  O   HOH A 618      10.767  -1.155 -45.009  1.00 17.59           O  
HETATM 3440  O   HOH A 619      -1.961  22.138 -15.475  1.00 30.08           O  
HETATM 3441  O   HOH A 620      -0.647  19.313 -47.167  1.00 31.85           O  
HETATM 3442  O   HOH A 621       6.254  -1.527 -30.725  1.00 23.82           O  
HETATM 3443  O   HOH A 622     -12.759  21.833 -38.656  1.00 22.50           O  
HETATM 3444  O   HOH A 623     -28.436  34.087 -16.515  1.00 24.56           O  
HETATM 3445  O   HOH A 624       1.731  22.065 -19.242  1.00 31.15           O  
HETATM 3446  O   HOH A 625      19.608  10.778 -46.337  1.00 22.56           O  
HETATM 3447  O   HOH A 626      21.861  12.560 -28.486  1.00 10.78           O  
HETATM 3448  O   HOH A 627      22.740  -0.725 -26.827  1.00 25.09           O  
HETATM 3449  O   HOH A 628     -16.596  38.193  -8.844  1.00 29.34           O  
HETATM 3450  O   HOH A 629     -20.242  17.184 -28.808  1.00 10.25           O  
HETATM 3451  O   HOH A 630     -32.120  26.423 -12.387  1.00 24.10           O  
HETATM 3452  O   HOH A 631      12.686  18.800 -14.804  1.00 34.13           O  
HETATM 3453  O   HOH A 632       2.573  24.694 -19.930  1.00 23.72           O  
HETATM 3454  O   HOH A 633      13.731  27.290 -30.714  1.00 20.20           O  
HETATM 3455  O   HOH A 634     -21.216  16.603 -33.092  1.00 19.86           O  
HETATM 3456  O   HOH A 635     -13.508  16.510 -16.667  1.00 32.69           O  
HETATM 3457  O   HOH A 636      25.437  18.235 -28.954  1.00  9.61           O  
HETATM 3458  O   HOH A 637     -32.851  21.955 -10.277  1.00 30.71           O  
HETATM 3459  O   HOH A 638       6.754  11.663 -38.995  1.00 24.62           O  
HETATM 3460  O   HOH A 639     -29.433  19.887  -4.350  1.00 28.59           O  
HETATM 3461  O   HOH A 640     -32.725  28.774 -11.415  1.00 32.23           O  
HETATM 3462  O   HOH A 641     -10.830  24.048 -38.989  1.00 26.56           O  
HETATM 3463  O   HOH A 642     -29.699  32.729 -24.070  1.00 39.31           O  
HETATM 3464  O   HOH A 643      19.915  -8.599 -24.610  1.00 36.78           O  
HETATM 3465  O   HOH A 644     -18.833  36.306 -24.180  1.00 21.36           O  
HETATM 3466  O   HOH A 645     -20.776  24.489 -27.690  1.00 19.13           O  
HETATM 3467  O   HOH A 646      -7.427  38.055 -34.998  1.00 29.37           O  
HETATM 3468  O   HOH A 647     -29.257  17.479 -16.021  1.00 46.77           O  
HETATM 3469  O   HOH A 648      -9.194  16.734 -27.081  1.00 14.51           O  
HETATM 3470  O   HOH A 649     -18.176  27.237 -34.231  1.00 28.19           O  
HETATM 3471  O   HOH A 650     -11.396  28.338 -16.951  1.00 18.47           O  
HETATM 3472  O   HOH A 651      27.967  14.783 -29.981  1.00 17.96           O  
HETATM 3473  O   HOH A 652      -4.925  26.303 -15.949  1.00 17.76           O  
HETATM 3474  O   HOH A 653      20.724  12.678 -45.257  1.00 39.96           O  
HETATM 3475  O   HOH A 654      -2.688  20.041 -45.558  1.00 26.88           O  
HETATM 3476  O   HOH A 655     -20.987  20.838 -31.583  1.00 12.74           O  
HETATM 3477  O   HOH A 656     -11.938  28.323 -35.874  1.00 24.59           O  
HETATM 3478  O   HOH A 657     -13.400  39.996  -9.225  1.00 31.19           O  
HETATM 3479  O   HOH A 658       6.539   1.587 -26.957  1.00 25.21           O  
HETATM 3480  O   HOH A 659     -19.765  18.492   5.527  1.00 27.33           O  
HETATM 3481  O   HOH A 660     -32.783  25.160  -7.119  1.00 29.62           O  
HETATM 3482  O   HOH A 661      27.962  -2.322 -29.925  1.00 37.18           O  
HETATM 3483  O   HOH A 662      -5.576  19.360 -18.120  1.00 17.98           O  
HETATM 3484  O   HOH A 663      -1.317  29.987 -17.391  1.00 27.00           O  
HETATM 3485  O   HOH A 664     -12.245  16.811   2.701  1.00 31.30           O  
HETATM 3486  O   HOH A 665     -22.999  45.530 -15.059  1.00 30.13           O  
HETATM 3487  O   HOH A 666       4.888   4.540 -26.469  1.00 27.91           O  
HETATM 3488  O   HOH A 667      13.029 -10.120 -35.774  1.00 34.71           O  
HETATM 3489  O   HOH A 668     -26.933  20.455  -4.415  1.00 20.40           O  
HETATM 3490  O   HOH A 669     -31.059  20.483   7.517  1.00 37.69           O  
HETATM 3491  O   HOH A 670      21.417  -2.086 -48.655  1.00 37.45           O  
HETATM 3492  O   HOH A 671      -1.327  13.254 -31.116  1.00 29.38           O  
HETATM 3493  O   HOH A 672      -6.113  36.928 -30.036  1.00 18.88           O  
HETATM 3494  O   HOH A 673      11.576  12.078 -17.427  1.00 37.62           O  
HETATM 3495  O   HOH A 674      15.232  -8.896 -42.014  1.00 25.70           O  
HETATM 3496  O   HOH A 675     -22.879  37.920 -22.117  1.00 22.43           O  
HETATM 3497  O   HOH A 676       9.385   6.770 -17.606  1.00 18.68           O  
HETATM 3498  O   HOH A 677      20.854  10.753 -48.833  1.00 35.42           O  
HETATM 3499  O   HOH A 678      -3.408  41.599 -18.447  1.00 30.57           O  
HETATM 3500  O   HOH A 679     -14.576  36.498  -0.286  1.00 33.58           O  
HETATM 3501  O   HOH A 680      18.175   2.748 -49.895  1.00 19.09           O  
HETATM 3502  O   HOH A 681     -10.692  26.549 -37.839  1.00 15.93           O  
HETATM 3503  O   HOH A 682     -15.604  16.771  10.081  1.00 31.04           O  
HETATM 3504  O   HOH A 683       2.432  36.641 -30.198  1.00 32.82           O  
HETATM 3505  O   HOH A 684      30.234  -3.232 -48.377  1.00 36.54           O  
HETATM 3506  O   HOH A 685       4.713  24.758 -20.810  1.00 23.71           O  
HETATM 3507  O   HOH A 686      17.115  -8.201 -47.329  1.00 19.29           O  
HETATM 3508  O   HOH A 687     -11.489  25.107   4.416  1.00 36.66           O  
HETATM 3509  O   HOH A 688     -24.390  26.674 -27.101  1.00 13.86           O  
HETATM 3510  O   HOH A 689      17.359  25.259 -24.962  1.00 28.06           O  
HETATM 3511  O   HOH A 690      19.699   5.386 -19.887  1.00 26.69           O  
HETATM 3512  O   HOH A 691      14.301  32.601 -25.444  1.00 27.07           O  
HETATM 3513  O   HOH A 692     -19.988  25.330 -35.250  1.00 28.49           O  
HETATM 3514  O   HOH A 693       9.327   9.428 -16.107  1.00 39.03           O  
HETATM 3515  O   HOH A 694     -23.935  19.704   8.582  1.00 37.11           O  
HETATM 3516  O   HOH A 695      27.522   9.543 -33.131  1.00 17.38           O  
HETATM 3517  O   HOH A 696     -23.158  26.024 -29.449  1.00 29.29           O  
HETATM 3518  O   HOH A 697      -4.643  14.448 -32.594  1.00 24.80           O  
HETATM 3519  O   HOH A 698      20.756   9.654 -51.597  1.00 35.19           O  
HETATM 3520  O   HOH A 699     -11.327  44.603 -14.077  1.00 42.95           O  
HETATM 3521  O   HOH A 700     -11.737  18.059  -6.331  1.00 32.93           O  
HETATM 3522  O   HOH A 701     -10.951  42.188 -27.408  1.00 34.38           O  
HETATM 3523  O   HOH A 702       8.711  -7.142 -23.635  1.00 34.28           O  
HETATM 3524  O   HOH A 703      14.022   5.941 -48.822  1.00 37.42           O  
HETATM 3525  O   HOH A 704      15.231  25.254 -31.814  1.00  9.41           O  
HETATM 3526  O   HOH A 705      12.598  15.102 -48.391  1.00 38.84           O  
HETATM 3527  O   HOH A 706     -32.717  30.932  -3.406  1.00 36.74           O  
HETATM 3528  O   HOH A 707      15.391  26.506 -34.516  1.00 18.30           O  
HETATM 3529  O   HOH A 708       6.058   5.468 -22.790  1.00 18.47           O  
HETATM 3530  O   HOH A 709      -3.855  28.899 -42.527  1.00 28.10           O  
HETATM 3531  O   HOH A 710     -14.777  18.731  -9.503  1.00 31.98           O  
HETATM 3532  O   HOH A 711       0.528  10.548 -38.526  1.00 21.02           O  
HETATM 3533  O   HOH A 712      13.338   0.220 -46.025  1.00 31.84           O  
HETATM 3534  O   HOH A 713     -22.066  12.479 -26.411  1.00 23.30           O  
HETATM 3535  O   HOH A 714       8.827   0.290 -22.200  1.00 28.91           O  
HETATM 3536  O   HOH A 715     -17.931  14.201 -31.574  1.00 15.19           O  
HETATM 3537  O   HOH A 716     -22.130  20.567 -27.753  1.00 14.45           O  
HETATM 3538  O   HOH A 717      19.214  -5.951 -47.806  1.00 25.91           O  
HETATM 3539  O   HOH A 718      27.339  14.229 -33.908  1.00 12.05           O  
HETATM 3540  O   HOH A 719      26.649   5.597 -30.226  1.00 31.57           O  
HETATM 3541  O   HOH A 720      -7.558  10.092 -42.053  1.00 36.18           O  
HETATM 3542  O   HOH A 721      27.662   8.243 -27.331  1.00 34.20           O  
HETATM 3543  O   HOH A 722     -16.009  44.972 -10.274  1.00 35.54           O  
HETATM 3544  O   HOH A 723     -12.653  43.578 -17.834  1.00 38.81           O  
HETATM 3545  O   HOH A 724     -25.798  32.023 -24.298  1.00 30.11           O  
HETATM 3546  O   HOH A 725      27.282  -9.759 -31.450  1.00 41.85           O  
HETATM 3547  O   HOH A 726     -10.392  14.767 -40.453  1.00 25.81           O  
HETATM 3548  O   HOH A 727       7.483   8.357 -40.643  1.00 19.90           O  
HETATM 3549  O   HOH A 728      -1.886  13.737 -47.938  1.00 30.48           O  
HETATM 3550  O   HOH A 729       5.659  35.506 -32.372  1.00 33.20           O  
HETATM 3551  O   HOH A 730      13.859  15.712 -19.354  1.00 17.34           O  
HETATM 3552  O   HOH A 731     -22.700  12.169  -8.201  1.00 29.62           O  
HETATM 3553  O   HOH A 732       8.294   7.616 -42.895  1.00 25.84           O  
HETATM 3554  O   HOH A 733      -2.736  31.676 -15.094  1.00 29.76           O  
HETATM 3555  O   HOH A 734     -12.992  19.799 -44.743  1.00 27.31           O  
HETATM 3556  O   HOH A 735      11.612  -4.061 -22.169  1.00 28.02           O  
HETATM 3557  O   HOH A 736      -7.493  13.475 -32.336  1.00 33.49           O  
HETATM 3558  O   HOH A 737     -14.536  11.838 -30.443  1.00 28.32           O  
HETATM 3559  O   HOH A 738      -8.683  24.640  -5.724  1.00 29.19           O  
HETATM 3560  O   HOH A 739     -22.173  15.143 -36.507  1.00 31.08           O  
HETATM 3561  O   HOH A 740      19.175  -0.084 -50.081  1.00 27.24           O  
HETATM 3562  O   HOH A 741      31.609   0.441 -43.648  1.00 49.53           O  
HETATM 3563  O   HOH A 742       4.771  19.668 -16.670  1.00 31.96           O  
HETATM 3564  O   HOH A 743      -4.998  42.038 -23.406  1.00 39.25           O  
HETATM 3565  O   HOH A 744     -11.271  19.044  15.394  1.00 34.16           O  
HETATM 3566  O   HOH A 745      -1.666   9.679 -39.203  1.00 29.04           O  
HETATM 3567  O   HOH A 746      24.090  24.070 -30.576  1.00 22.47           O  
HETATM 3568  O   HOH A 747       7.375  -6.193 -21.812  1.00 41.57           O  
HETATM 3569  O   HOH A 748      16.016 -12.652 -31.119  1.00 47.42           O  
HETATM 3570  O   HOH A 749     -24.588  19.215 -33.904  1.00 22.24           O  
HETATM 3571  O   HOH A 750      12.823  -6.293 -22.978  1.00 30.17           O  
HETATM 3572  O   HOH A 751     -21.968  22.587 -29.549  1.00 16.06           O  
HETATM 3573  O   HOH A 752     -26.651  18.226  -3.278  1.00 29.58           O  
HETATM 3574  O   HOH A 753      14.487  -2.074 -48.073  1.00 28.48           O  
HETATM 3575  O   HOH A 754       9.943  -2.353 -22.207  1.00 29.35           O  
HETATM 3576  O   HOH A 755       7.527  18.748 -16.980  1.00 40.08           O  
HETATM 3577  O   HOH A 756      27.900  -2.529 -49.429  1.00 31.36           O  
HETATM 3578  O   HOH A 757      15.888 -10.020 -45.613  1.00 28.03           O  
HETATM 3579  O   HOH A 758     -15.894  25.612 -35.376  1.00 18.12           O  
HETATM 3580  O   HOH A 759      23.100   4.202 -23.548  1.00 38.93           O  
HETATM 3581  O   HOH A 760     -22.993  24.171 -33.465  1.00 33.46           O  
HETATM 3582  O   HOH A 761      17.099  25.752 -22.226  1.00 35.71           O  
HETATM 3583  O   HOH A 762      28.473  13.135 -27.519  1.00 18.05           O  
HETATM 3584  O   HOH A 763       6.864   2.172 -21.498  1.00 32.22           O  
HETATM 3585  O   HOH A 764      23.034  -2.390 -50.834  1.00 28.58           O  
HETATM 3586  O   HOH A 765      -1.996  12.754 -35.129  1.00 28.57           O  
HETATM 3587  O   HOH A 766       5.076  -0.290 -28.317  1.00 29.76           O  
HETATM 3588  O   HOH A 767     -20.495  38.148 -23.040  1.00 26.96           O  
HETATM 3589  O   HOH A 768      30.730  11.453 -30.945  1.00 27.89           O  
HETATM 3590  O   HOH A 769       2.909  35.234 -32.908  1.00 25.20           O  
HETATM 3591  O   HOH A 770      22.242  13.332 -48.956  1.00 33.93           O  
HETATM 3592  O   HOH A 771     -25.892  18.608   9.104  1.00 40.48           O  
HETATM 3593  O   HOH A 772      -7.635  39.264 -30.452  1.00 33.78           O  
HETATM 3594  O   HOH A 773      27.256   5.120 -27.714  1.00 29.02           O  
HETATM 3595  O   HOH A 774     -22.585  18.598 -31.667  1.00 17.70           O  
HETATM 3596  O   HOH A 775      29.544  11.188 -28.527  1.00 29.85           O  
HETATM 3597  O   HOH A 776       0.034  13.506 -50.003  1.00 30.72           O  
HETATM 3598  O   HOH A 777      23.675   4.734 -21.276  1.00 37.41           O  
HETATM 3599  O   HOH B 501      -4.795  16.761 -18.946  1.00 18.06           O  
HETATM 3600  O   HOH B 502       2.484   0.917 -28.853  1.00 37.25           O  
HETATM 3601  O   HOH B 503      -9.179  30.399  -5.170  1.00 38.45           O  
HETATM 3602  O   HOH B 504     -10.703  23.619  -6.709  1.00 23.84           O  
HETATM 3603  O   HOH B 505     -12.775  29.069 -10.296  1.00 21.63           O  
HETATM 3604  O   HOH B 506      -6.166  18.345 -15.346  1.00 22.24           O  
HETATM 3605  O   HOH B 507       0.982   6.533 -27.846  1.00 21.21           O  
HETATM 3606  O   HOH B 508      -5.461  11.462 -26.630  1.00 38.21           O  
HETATM 3607  O   HOH B 509       2.590   3.896 -28.955  1.00 23.34           O  
HETATM 3608  O   HOH B 510      -9.119  35.452  -9.023  1.00 26.92           O  
HETATM 3609  O   HOH B 511      -6.839  24.942  -7.540  1.00 27.14           O  
HETATM 3610  O   HOH B 512      -7.234  20.948  -6.764  1.00 36.15           O  
HETATM 3611  O   HOH B 513       3.919   1.477 -39.879  1.00 33.14           O  
HETATM 3612  O   HOH B 514       1.330  10.093 -22.560  1.00 32.31           O  
HETATM 3613  O   HOH B 515       1.124   0.256 -40.331  1.00 37.05           O  
HETATM 3614  O   HOH B 516       7.058   5.163 -44.239  1.00 30.79           O  
HETATM 3615  O   HOH B 517      -4.324  10.521 -22.351  1.00 41.24           O  
HETATM 3616  O   HOH B 518       6.612  11.367 -20.675  1.00 28.25           O  
HETATM 3617  O   HOH B 519       2.929   8.306 -23.884  1.00 28.86           O  
HETATM 3618  O   HOH B 520       3.287   1.805 -42.675  1.00 30.22           O  
HETATM 3619  O   HOH B 521      -2.857  23.116 -13.103  1.00 33.23           O  
HETATM 3620  O   HOH B 522      -5.862  27.214  -8.473  1.00 25.04           O  
HETATM 3621  O   HOH B 523      -0.084  10.946 -36.129  1.00 29.35           O  
HETATM 3622  O   HOH B 524       4.799   4.368 -45.395  1.00 33.52           O  
HETATM 3623  O   HOH B 525      -4.000  14.859 -17.093  1.00 27.45           O  
HETATM 3624  O   HOH B 526      -3.641  15.428 -12.625  1.00 41.04           O  
HETATM 3625  O   HOH B 527       1.000   7.774 -35.204  1.00 37.33           O  
HETATM 3626  O   HOH B 528      -3.598  14.892  -9.905  1.00 36.75           O  
MASTER      305    0    0   31    0    0    0    6 3624    2    0   40          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.