CNRS Nantes University UFIP UFIP
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***  1BA3-open-state  ***

elNémo ID: 22040417491570403

Job options:

ID        	=	 22040417491570403
JOBID     	=	 1BA3-open-state
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 1BA3-open-state

HEADER    OXIDOREDUCTASE                          21-APR-98   1BA3              
TITLE     FIREFLY LUCIFERASE IN COMPLEX WITH BROMOFORM                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LUCIFERASE;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.13.12.7;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PHOTINUS PYRALIS;                               
SOURCE   3 ORGANISM_COMMON: COMMON EASTERN FIREFLY;                             
SOURCE   4 ORGANISM_TAXID: 7054;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    OXIDOREDUCTASE, MONOOXYGENASE, PHOTOPROTEIN, LUMINESCENCE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.P.FRANKS,A.JENKINS,E.CONTI,W.R.LIEB,P.BRICK                         
REVDAT   2   24-FEB-09 1BA3    1       VERSN                                    
REVDAT   1   11-NOV-98 1BA3    0                                                
JRNL        AUTH   N.P.FRANKS,A.JENKINS,E.CONTI,W.R.LIEB,P.BRICK                
JRNL        TITL   STRUCTURAL BASIS FOR THE INHIBITION OF FIREFLY               
JRNL        TITL 2 LUCIFERASE BY A GENERAL ANESTHETIC.                          
JRNL        REF    BIOPHYS.J.                    V.  75  2205 1998              
JRNL        REFN                   ISSN 0006-3495                               
JRNL        PMID   9788915                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.CONTI,T.STACHELHAUS,M.A.MARAHIEL,P.BRICK                   
REMARK   1  TITL   STRUCTURAL BASIS FOR THE ACTIVATION OF                       
REMARK   1  TITL 2 PHENYLALANINE IN THE NON-RIBOSOMAL BIOSYNTHESIS OF           
REMARK   1  TITL 3 GRAMICIDIN S                                                 
REMARK   1  REF    EMBO J.                       V.  16  4174 1997              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   E.CONTI,N.P.FRANKS,P.BRICK                                   
REMARK   1  TITL   CRYSTAL STRUCTURE OF FIREFLY LUCIFERASE THROWS               
REMARK   1  TITL 2 LIGHT ON A SUPERFAMILY OF ADENYLATE-FORMING ENZYMES          
REMARK   1  REF    STRUCTURE                     V.   4   287 1996              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   E.CONTI,L.F.LLOYD,J.AKINS,N.P.FRANKS,P.BRICK                 
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY DIFFRACTION                  
REMARK   1  TITL 2 STUDIES OF FIREFLY LUCIFERASE FROM PHOTINUS PYRALIS          
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  52   876 1996              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.40                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 35006                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1737                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.30                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.11                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 223                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2900                       
REMARK   3   BIN FREE R VALUE                    : 0.3000                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 223                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4130                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 353                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 18.40                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.51                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.10                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.260 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.420 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.540 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.830 ; 2.500                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT CORRECTION APPLIED           
REMARK   4                                                                      
REMARK   4 1BA3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JAN-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.5                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : Y                                  
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35038                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 18.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 3.130                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : 0.07100                            
REMARK 200   FOR THE DATA SET  : 6.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.23500                            
REMARK 200   FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.851                                          
REMARK 200 STARTING MODEL: 1LCI                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 MICROLITRE OF LUCIFERASE (20 MG/       
REMARK 280  ML) IN 0.2M AMMONIUM SULFATE, 0.001M EDTA, 0.001M DTT, 10%          
REMARK 280  GLYCEROL, 25% ETHYLENE GLYCOL, 0.025M TRIS-HCL PH7.8 + 2            
REMARK 280  MICROLITRE 0.5M LITHIUM SULFATE, 26% PEG 8000, 0.1M TRIS-HCL        
REMARK 280  PH7.8 AT 10 DEGREES CELSIUS IN MICROBATCH UNDER OIL.,               
REMARK 280  MICROBATCH UNDER OIL, TEMPERATURE 283K                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.90000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       59.78000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       59.78000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       23.95000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       59.78000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       59.78000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       71.85000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       59.78000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       59.78000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       23.95000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       59.78000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       59.78000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       71.85000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       47.90000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     SER A   199                                                      
REMARK 465     GLY A   200                                                      
REMARK 465     GLY A   545                                                      
REMARK 465     GLY A   546                                                      
REMARK 465     LYS A   547                                                      
REMARK 465     SER A   548                                                      
REMARK 465     LYS A   549                                                      
REMARK 465     LEU A   550                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A   3    CG   OD1  OD2                                       
REMARK 470     LYS A   5    CG   CD   CE   NZ                                   
REMARK 470     ARG A 112    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 134    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 190    CG   CD   CE   NZ                                   
REMARK 470     LYS A 380    CG   CD   CE   NZ                                   
REMARK 470     GLU A 406    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 414    CG   CD   CE   NZ                                   
REMARK 470     GLU A 428    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 443    CG   CD   CE   NZ                                   
REMARK 470     TYR A 447    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A 475    CG   OD1  OD2                                       
REMARK 470     ASP A 476    CG   OD1  OD2                                       
REMARK 470     THR A 492    OG1  CG2                                            
REMARK 470     THR A 508    OG1  CG2                                            
REMARK 470     LYS A 529    CG   CD   CE   NZ                                   
REMARK 470     ARG A 533    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 534    CG   CD   CE   NZ                                   
REMARK 470     GLU A 537    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 541    CG   CD   CE   NZ                                   
REMARK 470     LYS A 544    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A   4      -59.67     62.16                                   
REMARK 500    ASP A 153       53.14    -95.28                                   
REMARK 500    THR A 346      -64.51     72.14                                   
REMARK 500    PHE A 368      -12.38     81.05                                   
REMARK 500    ASP A 377      -66.66   -106.06                                   
REMARK 500    ASN A 385       19.31     48.00                                   
REMARK 500    PRO A 395        1.58    -67.47                                   
REMARK 500    ASN A 404       64.65   -150.06                                   
REMARK 500    LEU A 441      130.41     65.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 936        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH A 960        DISTANCE =  5.62 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MBR A 990                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MBR A 991                 
DBREF  1BA3 A    1   550  UNP    P08659   LUCI_PHOPY       1    550             
SEQRES   1 A  550  MET GLU ASP ALA LYS ASN ILE LYS LYS GLY PRO ALA PRO          
SEQRES   2 A  550  PHE TYR PRO LEU GLU ASP GLY THR ALA GLY GLU GLN LEU          
SEQRES   3 A  550  HIS LYS ALA MET LYS ARG TYR ALA LEU VAL PRO GLY THR          
SEQRES   4 A  550  ILE ALA PHE THR ASP ALA HIS ILE GLU VAL ASN ILE THR          
SEQRES   5 A  550  TYR ALA GLU TYR PHE GLU MET SER VAL ARG LEU ALA GLU          
SEQRES   6 A  550  ALA MET LYS ARG TYR GLY LEU ASN THR ASN HIS ARG ILE          
SEQRES   7 A  550  VAL VAL CYS SER GLU ASN SER LEU GLN PHE PHE MET PRO          
SEQRES   8 A  550  VAL LEU GLY ALA LEU PHE ILE GLY VAL ALA VAL ALA PRO          
SEQRES   9 A  550  ALA ASN ASP ILE TYR ASN GLU ARG GLU LEU LEU ASN SER          
SEQRES  10 A  550  MET ASN ILE SER GLN PRO THR VAL VAL PHE VAL SER LYS          
SEQRES  11 A  550  LYS GLY LEU GLN LYS ILE LEU ASN VAL GLN LYS LYS LEU          
SEQRES  12 A  550  PRO ILE ILE GLN LYS ILE ILE ILE MET ASP SER LYS THR          
SEQRES  13 A  550  ASP TYR GLN GLY PHE GLN SER MET TYR THR PHE VAL THR          
SEQRES  14 A  550  SER HIS LEU PRO PRO GLY PHE ASN GLU TYR ASP PHE VAL          
SEQRES  15 A  550  PRO GLU SER PHE ASP ARG ASP LYS THR ILE ALA LEU ILE          
SEQRES  16 A  550  MET ASN SER SER GLY SER THR GLY LEU PRO LYS GLY VAL          
SEQRES  17 A  550  ALA LEU PRO HIS ARG THR ALA CYS VAL ARG PHE SER HIS          
SEQRES  18 A  550  ALA ARG ASP PRO ILE PHE GLY ASN GLN ILE ILE PRO ASP          
SEQRES  19 A  550  THR ALA ILE LEU SER VAL VAL PRO PHE HIS HIS GLY PHE          
SEQRES  20 A  550  GLY MET PHE THR THR LEU GLY TYR LEU ILE CYS GLY PHE          
SEQRES  21 A  550  ARG VAL VAL LEU MET TYR ARG PHE GLU GLU GLU LEU PHE          
SEQRES  22 A  550  LEU ARG SER LEU GLN ASP TYR LYS ILE GLN SER ALA LEU          
SEQRES  23 A  550  LEU VAL PRO THR LEU PHE SER PHE PHE ALA LYS SER THR          
SEQRES  24 A  550  LEU ILE ASP LYS TYR ASP LEU SER ASN LEU HIS GLU ILE          
SEQRES  25 A  550  ALA SER GLY GLY ALA PRO LEU SER LYS GLU VAL GLY GLU          
SEQRES  26 A  550  ALA VAL ALA LYS ARG PHE HIS LEU PRO GLY ILE ARG GLN          
SEQRES  27 A  550  GLY TYR GLY LEU THR GLU THR THR SER ALA ILE LEU ILE          
SEQRES  28 A  550  THR PRO GLU GLY ASP ASP LYS PRO GLY ALA VAL GLY LYS          
SEQRES  29 A  550  VAL VAL PRO PHE PHE GLU ALA LYS VAL VAL ASP LEU ASP          
SEQRES  30 A  550  THR GLY LYS THR LEU GLY VAL ASN GLN ARG GLY GLU LEU          
SEQRES  31 A  550  CYS VAL ARG GLY PRO MET ILE MET SER GLY TYR VAL ASN          
SEQRES  32 A  550  ASN PRO GLU ALA THR ASN ALA LEU ILE ASP LYS ASP GLY          
SEQRES  33 A  550  TRP LEU HIS SER GLY ASP ILE ALA TYR TRP ASP GLU ASP          
SEQRES  34 A  550  GLU HIS PHE PHE ILE VAL ASP ARG LEU LYS SER LEU ILE          
SEQRES  35 A  550  LYS TYR LYS GLY TYR GLN VAL ALA PRO ALA GLU LEU GLU          
SEQRES  36 A  550  SER ILE LEU LEU GLN HIS PRO ASN ILE PHE ASP ALA GLY          
SEQRES  37 A  550  VAL ALA GLY LEU PRO ASP ASP ASP ALA GLY GLU LEU PRO          
SEQRES  38 A  550  ALA ALA VAL VAL VAL LEU GLU HIS GLY LYS THR MET THR          
SEQRES  39 A  550  GLU LYS GLU ILE VAL ASP TYR VAL ALA SER GLN VAL THR          
SEQRES  40 A  550  THR ALA LYS LYS LEU ARG GLY GLY VAL VAL PHE VAL ASP          
SEQRES  41 A  550  GLU VAL PRO LYS GLY LEU THR GLY LYS LEU ASP ALA ARG          
SEQRES  42 A  550  LYS ILE ARG GLU ILE LEU ILE LYS ALA LYS LYS GLY GLY          
SEQRES  43 A  550  LYS SER LYS LEU                                              
HET    MBR  A 990       4                                                       
HET    MBR  A 991       4                                                       
HETNAM     MBR TRIBROMOMETHANE                                                  
FORMUL   2  MBR    2(C H BR3)                                                   
FORMUL   4  HOH   *353(H2 O)                                                    
HELIX    1   1 ALA A   22  ALA A   34  1                                  13    
HELIX    2   2 TYR A   53  TYR A   70  1                                  18    
HELIX    3   3 PHE A   88  ILE A   98  1                                  11    
HELIX    4   4 GLU A  111  SER A  121  1                                  11    
HELIX    5   5 LYS A  130  LYS A  142  5                                  13    
HELIX    6   6 MET A  164  HIS A  171  1                                   8    
HELIX    7   7 HIS A  212  ALA A  222  1                                  11    
HELIX    8   8 GLY A  246  CYS A  258  1                                  13    
HELIX    9   9 GLU A  270  ASP A  279  1                                  10    
HELIX   10  10 PRO A  289  LYS A  297  1                                   9    
HELIX   11  11 ILE A  301  LYS A  303  5                                   3    
HELIX   12  12 LYS A  321  ARG A  330  1                                  10    
HELIX   13  13 THR A  343  THR A  345  5                                   3    
HELIX   14  14 PRO A  405  LEU A  411  1                                   7    
HELIX   15  15 ARG A  437  LYS A  439  5                                   3    
HELIX   16  16 PRO A  451  LEU A  459  1                                   9    
HELIX   17  17 GLU A  495  GLN A  505  1                                  11    
HELIX   18  18 ALA A  532  ALA A  542  1                                  11    
SHEET    1   A 6 GLU A 311  ALA A 313  0                                        
SHEET    2   A 6 SER A 284  LEU A 286  1  N  ALA A 285   O  GLU A 311           
SHEET    3   A 6 ALA A 236  SER A 239  1  N  LEU A 238   O  SER A 284           
SHEET    4   A 6 ARG A 261  LEU A 264  1  N  ARG A 261   O  ILE A 237           
SHEET    5   A 6 ILE A  40  ASP A  44  1  N  THR A  43   O  VAL A 262           
SHEET    6   A 6 ASN A  50  THR A  52 -1  N  ILE A  51   O  ALA A  41           
SHEET    1   B 4 ALA A 101  PRO A 104  0                                        
SHEET    2   B 4 ARG A  77  CYS A  81  1  N  ILE A  78   O  ALA A 101           
SHEET    3   B 4 VAL A 125  VAL A 128  1  N  VAL A 125   O  VAL A  79           
SHEET    4   B 4 LYS A 148  ILE A 151  1  N  LYS A 148   O  VAL A 126           
SHEET    1   C 2 PHE A 369  VAL A 374  0                                        
SHEET    2   C 2 GLU A 389  GLY A 394 -1  N  ARG A 393   O  GLU A 370           
SHEET    1   D 2 ALA A 424  TRP A 426  0                                        
SHEET    2   D 2 PHE A 432  ILE A 434 -1  N  PHE A 433   O  TYR A 425           
SHEET    1   E 2 ILE A 442  TYR A 444  0                                        
SHEET    2   E 2 TYR A 447  VAL A 449 -1  N  VAL A 449   O  ILE A 442           
SHEET    1   F 3 GLY A 515  PHE A 518  0                                        
SHEET    2   F 3 GLY A 478  LEU A 487  1  N  ALA A 483   O  GLY A 515           
SHEET    3   F 3 ILE A 464  ASP A 474 -1  N  ASP A 474   O  GLY A 478           
SHEET    1   G 2 ILE A 192  ASN A 197  0                                        
SHEET    2   G 2 GLY A 207  PRO A 211 -1  N  LEU A 210   O  ALA A 193           
SHEET    1   H 2 GLY A 339  GLY A 341  0                                        
SHEET    2   H 2 ALA A 348  ILE A 351 -1  N  LEU A 350   O  TYR A 340           
SITE     1 AC1  4 ARG A 337  THR A 352  GLU A 354  HOH A 711                    
SITE     1 AC2  1 GLY A 315                                                     
CRYST1  119.560  119.560   95.800  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008364  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008364  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010438        0.00000                         
ATOM      1  N   ASP A   3      31.596 108.808  55.073  1.00 72.97           N  
ATOM      2  CA  ASP A   3      31.686 107.786  56.111  1.00 74.06           C  
ATOM      3  C   ASP A   3      32.282 106.501  55.551  1.00 75.02           C  
ATOM      4  O   ASP A   3      33.156 105.900  56.172  1.00 74.63           O  
ATOM      5  CB  ASP A   3      30.305 107.505  56.700  1.00 74.12           C  
ATOM      6  N   ALA A   4      31.786 106.087  54.383  1.00 77.53           N  
ATOM      7  CA  ALA A   4      32.231 104.876  53.669  1.00 78.01           C  
ATOM      8  C   ALA A   4      32.015 103.550  54.406  1.00 76.80           C  
ATOM      9  O   ALA A   4      31.322 102.670  53.900  1.00 78.48           O  
ATOM     10  CB  ALA A   4      33.691 105.011  53.218  1.00 80.24           C  
ATOM     11  N   LYS A   5      32.614 103.410  55.587  1.00 74.25           N  
ATOM     12  CA  LYS A   5      32.482 102.200  56.402  1.00 70.70           C  
ATOM     13  C   LYS A   5      31.040 101.962  56.875  1.00 68.09           C  
ATOM     14  O   LYS A   5      30.724 100.899  57.409  1.00 67.63           O  
ATOM     15  CB  LYS A   5      33.424 102.271  57.609  1.00 67.07           C  
ATOM     16  N   ASN A   6      30.181 102.964  56.686  1.00 63.06           N  
ATOM     17  CA  ASN A   6      28.773 102.872  57.072  1.00 58.19           C  
ATOM     18  C   ASN A   6      27.909 102.251  55.976  1.00 55.44           C  
ATOM     19  O   ASN A   6      26.686 102.148  56.125  1.00 54.72           O  
ATOM     20  CB  ASN A   6      28.211 104.246  57.444  1.00 58.29           C  
ATOM     21  CG  ASN A   6      28.593 104.677  58.852  1.00 56.55           C  
ATOM     22  OD1 ASN A   6      28.992 103.865  59.679  1.00 54.97           O  
ATOM     23  ND2 ASN A   6      28.463 105.972  59.130  1.00 54.79           N  
ATOM     24  N   ILE A   7      28.529 101.921  54.846  1.00 51.86           N  
ATOM     25  CA  ILE A   7      27.822 101.296  53.732  1.00 50.19           C  
ATOM     26  C   ILE A   7      28.268  99.841  53.676  1.00 45.90           C  
ATOM     27  O   ILE A   7      29.458  99.549  53.530  1.00 46.54           O  
ATOM     28  CB  ILE A   7      28.107 102.010  52.383  1.00 49.45           C  
ATOM     29  CG1 ILE A   7      27.453 103.392  52.374  1.00 48.24           C  
ATOM     30  CG2 ILE A   7      27.567 101.189  51.220  1.00 50.94           C  
ATOM     31  CD1 ILE A   7      27.597 104.143  51.067  1.00 49.83           C  
ATOM     32  N   LYS A   8      27.320  98.935  53.872  1.00 43.91           N  
ATOM     33  CA  LYS A   8      27.620  97.513  53.850  1.00 39.91           C  
ATOM     34  C   LYS A   8      27.616  97.018  52.415  1.00 36.51           C  
ATOM     35  O   LYS A   8      26.670  97.270  51.668  1.00 36.50           O  
ATOM     36  CB  LYS A   8      26.592  96.743  54.682  1.00 39.90           C  
ATOM     37  CG  LYS A   8      26.387  97.260  56.099  1.00 35.15           C  
ATOM     38  CD  LYS A   8      27.567  96.971  57.018  1.00 40.60           C  
ATOM     39  CE  LYS A   8      28.668  98.007  56.886  1.00 39.75           C  
ATOM     40  NZ  LYS A   8      29.727  97.769  57.894  1.00 43.94           N  
ATOM     41  N   LYS A   9      28.680  96.322  52.036  1.00 35.90           N  
ATOM     42  CA  LYS A   9      28.817  95.798  50.686  1.00 37.60           C  
ATOM     43  C   LYS A   9      28.838  94.278  50.701  1.00 36.13           C  
ATOM     44  O   LYS A   9      29.374  93.659  51.631  1.00 32.40           O  
ATOM     45  CB  LYS A   9      30.128  96.286  50.033  1.00 43.45           C  
ATOM     46  CG  LYS A   9      30.228  97.785  49.742  1.00 49.93           C  
ATOM     47  CD  LYS A   9      31.027  98.525  50.818  1.00 51.35           C  
ATOM     48  CE  LYS A   9      31.393  99.936  50.362  1.00 51.80           C  
ATOM     49  NZ  LYS A   9      32.026 100.749  51.441  1.00 49.22           N  
ATOM     50  N   GLY A  10      28.241  93.678  49.678  1.00 37.11           N  
ATOM     51  CA  GLY A  10      28.260  92.231  49.568  1.00 37.76           C  
ATOM     52  C   GLY A  10      29.655  91.837  49.118  1.00 36.09           C  
ATOM     53  O   GLY A  10      30.324  92.622  48.443  1.00 38.18           O  
ATOM     54  N   PRO A  11      30.129  90.635  49.469  1.00 33.17           N  
ATOM     55  CA  PRO A  11      31.475  90.232  49.059  1.00 29.66           C  
ATOM     56  C   PRO A  11      31.576  89.941  47.559  1.00 32.16           C  
ATOM     57  O   PRO A  11      30.634  90.172  46.792  1.00 30.81           O  
ATOM     58  CB  PRO A  11      31.708  88.981  49.897  1.00 29.89           C  
ATOM     59  CG  PRO A  11      30.346  88.368  49.915  1.00 31.18           C  
ATOM     60  CD  PRO A  11      29.454  89.554  50.204  1.00 28.77           C  
ATOM     61  N   ALA A  12      32.753  89.496  47.137  1.00 29.55           N  
ATOM     62  CA  ALA A  12      32.957  89.150  45.740  1.00 31.22           C  
ATOM     63  C   ALA A  12      32.193  87.838  45.525  1.00 32.06           C  
ATOM     64  O   ALA A  12      32.188  86.965  46.406  1.00 34.71           O  
ATOM     65  CB  ALA A  12      34.447  88.954  45.461  1.00 27.67           C  
ATOM     66  N   PRO A  13      31.466  87.717  44.399  1.00 28.12           N  
ATOM     67  CA  PRO A  13      30.715  86.489  44.128  1.00 25.29           C  
ATOM     68  C   PRO A  13      31.673  85.335  43.885  1.00 27.40           C  
ATOM     69  O   PRO A  13      32.821  85.551  43.518  1.00 28.72           O  
ATOM     70  CB  PRO A  13      29.941  86.846  42.860  1.00 24.30           C  
ATOM     71  CG  PRO A  13      30.868  87.777  42.161  1.00 25.18           C  
ATOM     72  CD  PRO A  13      31.318  88.674  43.290  1.00 28.18           C  
ATOM     73  N   PHE A  14      31.216  84.114  44.128  1.00 26.40           N  
ATOM     74  CA  PHE A  14      32.052  82.938  43.901  1.00 30.58           C  
ATOM     75  C   PHE A  14      32.101  82.687  42.397  1.00 32.92           C  
ATOM     76  O   PHE A  14      33.111  82.241  41.853  1.00 34.08           O  
ATOM     77  CB  PHE A  14      31.466  81.723  44.628  1.00 26.72           C  
ATOM     78  CG  PHE A  14      32.127  80.413  44.273  1.00 28.90           C  
ATOM     79  CD1 PHE A  14      33.356  80.064  44.823  1.00 26.77           C  
ATOM     80  CD2 PHE A  14      31.500  79.513  43.410  1.00 26.28           C  
ATOM     81  CE1 PHE A  14      33.949  78.838  44.525  1.00 25.82           C  
ATOM     82  CE2 PHE A  14      32.084  78.287  43.105  1.00 25.23           C  
ATOM     83  CZ  PHE A  14      33.311  77.946  43.664  1.00 23.84           C  
ATOM     84  N   TYR A  15      30.986  82.970  41.736  1.00 35.88           N  
ATOM     85  CA  TYR A  15      30.868  82.788  40.300  1.00 38.47           C  
ATOM     86  C   TYR A  15      30.656  84.167  39.683  1.00 38.50           C  
ATOM     87  O   TYR A  15      29.645  84.825  39.945  1.00 35.06           O  
ATOM     88  CB  TYR A  15      29.675  81.879  39.986  1.00 42.81           C  
ATOM     89  CG  TYR A  15      29.953  80.919  38.862  1.00 48.81           C  
ATOM     90  CD1 TYR A  15      29.835  81.317  37.527  1.00 48.93           C  
ATOM     91  CD2 TYR A  15      30.399  79.627  39.129  1.00 49.03           C  
ATOM     92  CE1 TYR A  15      30.165  80.450  36.488  1.00 52.47           C  
ATOM     93  CE2 TYR A  15      30.732  78.751  38.099  1.00 50.87           C  
ATOM     94  CZ  TYR A  15      30.617  79.167  36.780  1.00 52.12           C  
ATOM     95  OH  TYR A  15      30.974  78.304  35.763  1.00 55.51           O  
ATOM     96  N   PRO A  16      31.633  84.643  38.891  1.00 38.34           N  
ATOM     97  CA  PRO A  16      31.520  85.958  38.256  1.00 34.79           C  
ATOM     98  C   PRO A  16      30.288  86.070  37.386  1.00 31.74           C  
ATOM     99  O   PRO A  16      29.729  85.066  36.945  1.00 31.29           O  
ATOM    100  CB  PRO A  16      32.793  86.036  37.405  1.00 33.75           C  
ATOM    101  CG  PRO A  16      33.765  85.232  38.193  1.00 38.76           C  
ATOM    102  CD  PRO A  16      32.936  84.031  38.596  1.00 41.27           C  
ATOM    103  N   LEU A  17      29.822  87.299  37.222  1.00 31.28           N  
ATOM    104  CA  LEU A  17      28.681  87.572  36.368  1.00 32.54           C  
ATOM    105  C   LEU A  17      29.141  87.218  34.954  1.00 33.43           C  
ATOM    106  O   LEU A  17      30.158  87.726  34.490  1.00 33.40           O  
ATOM    107  CB  LEU A  17      28.328  89.053  36.446  1.00 26.68           C  
ATOM    108  CG  LEU A  17      27.155  89.534  35.608  1.00 28.83           C  
ATOM    109  CD1 LEU A  17      25.898  88.863  36.119  1.00 33.52           C  
ATOM    110  CD2 LEU A  17      27.030  91.050  35.693  1.00 28.16           C  
ATOM    111  N   GLU A  18      28.424  86.319  34.290  1.00 33.24           N  
ATOM    112  CA  GLU A  18      28.793  85.898  32.944  1.00 32.66           C  
ATOM    113  C   GLU A  18      28.162  86.744  31.852  1.00 32.83           C  
ATOM    114  O   GLU A  18      27.110  87.345  32.055  1.00 34.23           O  
ATOM    115  CB  GLU A  18      28.428  84.433  32.735  1.00 31.06           C  
ATOM    116  CG  GLU A  18      29.129  83.518  33.687  1.00 38.74           C  
ATOM    117  CD  GLU A  18      29.331  82.135  33.120  1.00 44.37           C  
ATOM    118  OE1 GLU A  18      28.329  81.414  32.935  1.00 49.06           O  
ATOM    119  OE2 GLU A  18      30.498  81.773  32.859  1.00 49.31           O  
ATOM    120  N   ASP A  19      28.812  86.780  30.691  1.00 31.23           N  
ATOM    121  CA  ASP A  19      28.307  87.549  29.555  1.00 31.13           C  
ATOM    122  C   ASP A  19      27.057  86.895  28.999  1.00 25.98           C  
ATOM    123  O   ASP A  19      26.791  85.728  29.263  1.00 28.97           O  
ATOM    124  CB  ASP A  19      29.352  87.623  28.434  1.00 34.61           C  
ATOM    125  CG  ASP A  19      30.624  88.325  28.855  1.00 40.95           C  
ATOM    126  OD1 ASP A  19      30.544  89.466  29.370  1.00 35.97           O  
ATOM    127  OD2 ASP A  19      31.707  87.733  28.658  1.00 44.58           O  
ATOM    128  N   GLY A  20      26.313  87.651  28.206  1.00 23.74           N  
ATOM    129  CA  GLY A  20      25.111  87.134  27.593  1.00 24.66           C  
ATOM    130  C   GLY A  20      23.821  87.547  28.264  1.00 27.35           C  
ATOM    131  O   GLY A  20      23.810  87.994  29.409  1.00 30.32           O  
ATOM    132  N   THR A  21      22.731  87.440  27.516  1.00 26.94           N  
ATOM    133  CA  THR A  21      21.407  87.769  28.016  1.00 25.95           C  
ATOM    134  C   THR A  21      20.984  86.611  28.926  1.00 26.21           C  
ATOM    135  O   THR A  21      21.633  85.560  28.946  1.00 27.54           O  
ATOM    136  CB  THR A  21      20.390  87.870  26.853  1.00 25.98           C  
ATOM    137  OG1 THR A  21      20.024  86.554  26.417  1.00 26.91           O  
ATOM    138  CG2 THR A  21      20.991  88.628  25.670  1.00 23.63           C  
ATOM    139  N   ALA A  22      19.904  86.810  29.678  1.00 27.35           N  
ATOM    140  CA  ALA A  22      19.381  85.774  30.567  1.00 24.03           C  
ATOM    141  C   ALA A  22      18.950  84.552  29.746  1.00 19.75           C  
ATOM    142  O   ALA A  22      19.153  83.415  30.166  1.00 24.23           O  
ATOM    143  CB  ALA A  22      18.203  86.317  31.396  1.00 20.63           C  
ATOM    144  N   GLY A  23      18.391  84.796  28.564  1.00 18.73           N  
ATOM    145  CA  GLY A  23      17.958  83.713  27.697  1.00 19.14           C  
ATOM    146  C   GLY A  23      19.146  82.926  27.159  1.00 22.86           C  
ATOM    147  O   GLY A  23      19.077  81.704  27.011  1.00 26.20           O  
ATOM    148  N   GLU A  24      20.251  83.614  26.892  1.00 21.60           N  
ATOM    149  CA  GLU A  24      21.445  82.949  26.393  1.00 20.88           C  
ATOM    150  C   GLU A  24      22.085  82.080  27.469  1.00 21.71           C  
ATOM    151  O   GLU A  24      22.551  80.965  27.193  1.00 23.28           O  
ATOM    152  CB  GLU A  24      22.465  83.966  25.892  1.00 18.73           C  
ATOM    153  CG  GLU A  24      22.067  84.685  24.624  1.00 24.00           C  
ATOM    154  CD  GLU A  24      23.140  85.657  24.151  1.00 27.03           C  
ATOM    155  OE1 GLU A  24      23.647  86.450  24.968  1.00 26.25           O  
ATOM    156  OE2 GLU A  24      23.478  85.640  22.951  1.00 31.07           O  
ATOM    157  N   GLN A  25      22.147  82.602  28.688  1.00 18.88           N  
ATOM    158  CA  GLN A  25      22.737  81.845  29.786  1.00 20.32           C  
ATOM    159  C   GLN A  25      21.867  80.634  30.122  1.00 19.24           C  
ATOM    160  O   GLN A  25      22.375  79.546  30.416  1.00 20.55           O  
ATOM    161  CB  GLN A  25      22.937  82.737  31.013  1.00 20.12           C  
ATOM    162  CG  GLN A  25      23.740  83.999  30.709  1.00 25.57           C  
ATOM    163  CD  GLN A  25      24.295  84.669  31.945  1.00 25.15           C  
ATOM    164  OE1 GLN A  25      24.437  84.045  33.000  1.00 28.40           O  
ATOM    165  NE2 GLN A  25      24.618  85.947  31.823  1.00 25.78           N  
ATOM    166  N   LEU A  26      20.553  80.822  30.059  1.00 18.56           N  
ATOM    167  CA  LEU A  26      19.619  79.733  30.330  1.00 21.73           C  
ATOM    168  C   LEU A  26      19.737  78.673  29.241  1.00 18.70           C  
ATOM    169  O   LEU A  26      19.847  77.476  29.527  1.00 19.36           O  
ATOM    170  CB  LEU A  26      18.185  80.266  30.412  1.00 18.06           C  
ATOM    171  CG  LEU A  26      17.842  80.939  31.744  1.00 19.47           C  
ATOM    172  CD1 LEU A  26      16.566  81.741  31.610  1.00 13.87           C  
ATOM    173  CD2 LEU A  26      17.721  79.876  32.841  1.00 12.90           C  
ATOM    174  N   HIS A  27      19.748  79.127  27.993  1.00 20.85           N  
ATOM    175  CA  HIS A  27      19.873  78.240  26.846  1.00 20.42           C  
ATOM    176  C   HIS A  27      21.148  77.418  26.940  1.00 21.69           C  
ATOM    177  O   HIS A  27      21.126  76.194  26.760  1.00 23.13           O  
ATOM    178  CB  HIS A  27      19.885  79.044  25.546  1.00 19.79           C  
ATOM    179  CG  HIS A  27      20.004  78.195  24.321  1.00 21.73           C  
ATOM    180  ND1 HIS A  27      21.216  77.786  23.817  1.00 21.31           N  
ATOM    181  CD2 HIS A  27      19.061  77.624  23.533  1.00 19.39           C  
ATOM    182  CE1 HIS A  27      21.024  77.000  22.777  1.00 24.66           C  
ATOM    183  NE2 HIS A  27      19.722  76.883  22.584  1.00 27.25           N  
ATOM    184  N   LYS A  28      22.252  78.089  27.241  1.00 20.70           N  
ATOM    185  CA  LYS A  28      23.538  77.419  27.355  1.00 23.51           C  
ATOM    186  C   LYS A  28      23.516  76.341  28.432  1.00 23.14           C  
ATOM    187  O   LYS A  28      23.875  75.194  28.169  1.00 24.00           O  
ATOM    188  CB  LYS A  28      24.650  78.432  27.642  1.00 25.72           C  
ATOM    189  CG  LYS A  28      26.038  77.819  27.758  1.00 30.50           C  
ATOM    190  CD  LYS A  28      27.108  78.897  27.839  1.00 40.05           C  
ATOM    191  CE  LYS A  28      28.500  78.293  27.996  1.00 43.78           C  
ATOM    192  NZ  LYS A  28      28.696  77.696  29.347  1.00 49.02           N  
ATOM    193  N   ALA A  29      23.076  76.705  29.632  1.00 21.27           N  
ATOM    194  CA  ALA A  29      23.024  75.754  30.734  1.00 20.33           C  
ATOM    195  C   ALA A  29      22.135  74.553  30.426  1.00 22.51           C  
ATOM    196  O   ALA A  29      22.590  73.410  30.447  1.00 24.64           O  
ATOM    197  CB  ALA A  29      22.542  76.441  32.001  1.00 20.59           C  
ATOM    198  N   MET A  30      20.881  74.812  30.079  1.00 21.17           N  
ATOM    199  CA  MET A  30      19.939  73.740  29.793  1.00 22.17           C  
ATOM    200  C   MET A  30      20.335  72.805  28.658  1.00 24.29           C  
ATOM    201  O   MET A  30      20.013  71.612  28.700  1.00 21.70           O  
ATOM    202  CB  MET A  30      18.543  74.309  29.575  1.00 20.35           C  
ATOM    203  CG  MET A  30      18.009  74.980  30.817  1.00 22.17           C  
ATOM    204  SD  MET A  30      16.393  75.634  30.581  1.00 26.82           S  
ATOM    205  CE  MET A  30      15.435  74.083  30.637  1.00 17.30           C  
ATOM    206  N   LYS A  31      21.050  73.329  27.663  1.00 23.40           N  
ATOM    207  CA  LYS A  31      21.490  72.512  26.539  1.00 20.85           C  
ATOM    208  C   LYS A  31      22.448  71.413  26.997  1.00 21.52           C  
ATOM    209  O   LYS A  31      22.284  70.253  26.625  1.00 19.53           O  
ATOM    210  CB  LYS A  31      22.142  73.372  25.458  1.00 22.87           C  
ATOM    211  CG  LYS A  31      22.497  72.610  24.182  1.00 21.37           C  
ATOM    212  CD  LYS A  31      22.840  73.573  23.070  1.00 23.17           C  
ATOM    213  CE  LYS A  31      23.305  72.855  21.822  1.00 25.44           C  
ATOM    214  NZ  LYS A  31      23.508  73.823  20.696  1.00 23.40           N  
ATOM    215  N   ARG A  32      23.415  71.759  27.841  1.00 22.80           N  
ATOM    216  CA  ARG A  32      24.355  70.757  28.323  1.00 26.44           C  
ATOM    217  C   ARG A  32      23.640  69.692  29.147  1.00 23.37           C  
ATOM    218  O   ARG A  32      23.979  68.512  29.067  1.00 25.79           O  
ATOM    219  CB  ARG A  32      25.518  71.389  29.106  1.00 31.61           C  
ATOM    220  CG  ARG A  32      25.152  71.996  30.443  1.00 48.51           C  
ATOM    221  CD  ARG A  32      26.352  72.631  31.134  1.00 56.21           C  
ATOM    222  NE  ARG A  32      25.923  73.557  32.188  1.00 62.03           N  
ATOM    223  CZ  ARG A  32      26.526  74.710  32.475  1.00 68.71           C  
ATOM    224  NH1 ARG A  32      27.598  75.101  31.789  1.00 71.69           N  
ATOM    225  NH2 ARG A  32      26.036  75.493  33.440  1.00 69.45           N  
ATOM    226  N   TYR A  33      22.625  70.092  29.906  1.00 21.80           N  
ATOM    227  CA  TYR A  33      21.873  69.139  30.719  1.00 22.74           C  
ATOM    228  C   TYR A  33      21.023  68.256  29.819  1.00 20.82           C  
ATOM    229  O   TYR A  33      20.903  67.059  30.051  1.00 24.40           O  
ATOM    230  CB  TYR A  33      20.992  69.868  31.741  1.00 23.39           C  
ATOM    231  CG  TYR A  33      21.784  70.670  32.750  1.00 25.50           C  
ATOM    232  CD1 TYR A  33      22.862  70.097  33.427  1.00 28.36           C  
ATOM    233  CD2 TYR A  33      21.499  72.015  32.984  1.00 21.60           C  
ATOM    234  CE1 TYR A  33      23.647  70.840  34.304  1.00 27.67           C  
ATOM    235  CE2 TYR A  33      22.286  72.774  33.869  1.00 25.66           C  
ATOM    236  CZ  TYR A  33      23.359  72.174  34.522  1.00 26.25           C  
ATOM    237  OH  TYR A  33      24.154  72.899  35.381  1.00 28.62           O  
ATOM    238  N   ALA A  34      20.456  68.854  28.777  1.00 21.01           N  
ATOM    239  CA  ALA A  34      19.626  68.134  27.818  1.00 19.56           C  
ATOM    240  C   ALA A  34      20.393  67.002  27.152  1.00 17.93           C  
ATOM    241  O   ALA A  34      19.805  65.985  26.781  1.00 17.49           O  
ATOM    242  CB  ALA A  34      19.099  69.099  26.758  1.00 17.58           C  
ATOM    243  N   LEU A  35      21.706  67.182  27.018  1.00 21.29           N  
ATOM    244  CA  LEU A  35      22.576  66.191  26.391  1.00 21.36           C  
ATOM    245  C   LEU A  35      22.797  64.942  27.240  1.00 22.46           C  
ATOM    246  O   LEU A  35      23.324  63.936  26.756  1.00 25.83           O  
ATOM    247  CB  LEU A  35      23.908  66.828  25.991  1.00 16.83           C  
ATOM    248  CG  LEU A  35      23.774  67.926  24.928  1.00 17.46           C  
ATOM    249  CD1 LEU A  35      25.142  68.415  24.494  1.00 19.59           C  
ATOM    250  CD2 LEU A  35      23.011  67.396  23.725  1.00 18.01           C  
ATOM    251  N   VAL A  36      22.379  65.002  28.502  1.00 23.69           N  
ATOM    252  CA  VAL A  36      22.504  63.864  29.409  1.00 21.48           C  
ATOM    253  C   VAL A  36      21.090  63.339  29.652  1.00 22.21           C  
ATOM    254  O   VAL A  36      20.331  63.922  30.427  1.00 26.11           O  
ATOM    255  CB  VAL A  36      23.141  64.273  30.764  1.00 24.31           C  
ATOM    256  CG1 VAL A  36      23.418  63.038  31.620  1.00 21.48           C  
ATOM    257  CG2 VAL A  36      24.432  65.050  30.534  1.00 22.67           C  
ATOM    258  N   PRO A  37      20.703  62.255  28.949  1.00 24.13           N  
ATOM    259  CA  PRO A  37      19.374  61.634  29.071  1.00 20.22           C  
ATOM    260  C   PRO A  37      19.023  61.274  30.513  1.00 22.76           C  
ATOM    261  O   PRO A  37      19.862  60.778  31.265  1.00 20.32           O  
ATOM    262  CB  PRO A  37      19.509  60.376  28.212  1.00 22.70           C  
ATOM    263  CG  PRO A  37      20.498  60.792  27.159  1.00 24.28           C  
ATOM    264  CD  PRO A  37      21.531  61.538  27.964  1.00 22.10           C  
ATOM    265  N   GLY A  38      17.787  61.563  30.903  1.00 20.86           N  
ATOM    266  CA  GLY A  38      17.353  61.240  32.246  1.00 20.59           C  
ATOM    267  C   GLY A  38      17.503  62.334  33.284  1.00 19.99           C  
ATOM    268  O   GLY A  38      16.970  62.197  34.384  1.00 24.60           O  
ATOM    269  N   THR A  39      18.227  63.405  32.965  1.00 17.59           N  
ATOM    270  CA  THR A  39      18.411  64.514  33.905  1.00 18.47           C  
ATOM    271  C   THR A  39      17.050  65.184  34.095  1.00 17.50           C  
ATOM    272  O   THR A  39      16.501  65.748  33.143  1.00 18.41           O  
ATOM    273  CB  THR A  39      19.435  65.534  33.366  1.00 20.25           C  
ATOM    274  OG1 THR A  39      20.653  64.854  33.037  1.00 19.84           O  
ATOM    275  CG2 THR A  39      19.744  66.585  34.411  1.00 19.80           C  
ATOM    276  N   ILE A  40      16.518  65.130  35.318  1.00 16.66           N  
ATOM    277  CA  ILE A  40      15.197  65.686  35.631  1.00 16.66           C  
ATOM    278  C   ILE A  40      15.171  67.198  35.929  1.00 17.69           C  
ATOM    279  O   ILE A  40      15.886  67.693  36.811  1.00 18.08           O  
ATOM    280  CB  ILE A  40      14.530  64.921  36.811  1.00 16.36           C  
ATOM    281  CG1 ILE A  40      14.631  63.415  36.591  1.00  9.76           C  
ATOM    282  CG2 ILE A  40      13.052  65.317  36.950  1.00 10.53           C  
ATOM    283  CD1 ILE A  40      14.052  62.607  37.720  1.00 15.17           C  
ATOM    284  N   ALA A  41      14.322  67.915  35.196  1.00 14.21           N  
ATOM    285  CA  ALA A  41      14.179  69.362  35.356  1.00 17.07           C  
ATOM    286  C   ALA A  41      13.087  69.685  36.358  1.00 17.35           C  
ATOM    287  O   ALA A  41      13.291  70.458  37.285  1.00 17.80           O  
ATOM    288  CB  ALA A  41      13.849  70.010  34.016  1.00 14.90           C  
ATOM    289  N   PHE A  42      11.913  69.105  36.143  1.00 18.88           N  
ATOM    290  CA  PHE A  42      10.761  69.321  37.013  1.00 17.58           C  
ATOM    291  C   PHE A  42      10.073  67.999  37.290  1.00 16.00           C  
ATOM    292  O   PHE A  42      10.081  67.095  36.448  1.00 16.56           O  
ATOM    293  CB  PHE A  42       9.732  70.247  36.344  1.00 15.98           C  
ATOM    294  CG  PHE A  42      10.172  71.671  36.223  1.00 17.77           C  
ATOM    295  CD1 PHE A  42       9.942  72.572  37.261  1.00 20.80           C  
ATOM    296  CD2 PHE A  42      10.775  72.131  35.056  1.00 17.46           C  
ATOM    297  CE1 PHE A  42      10.305  73.923  37.135  1.00 19.67           C  
ATOM    298  CE2 PHE A  42      11.140  73.474  34.919  1.00 16.11           C  
ATOM    299  CZ  PHE A  42      10.902  74.372  35.963  1.00 17.53           C  
ATOM    300  N   THR A  43       9.458  67.919  38.462  1.00 17.45           N  
ATOM    301  CA  THR A  43       8.696  66.757  38.878  1.00 14.74           C  
ATOM    302  C   THR A  43       7.431  67.297  39.526  1.00 16.46           C  
ATOM    303  O   THR A  43       7.503  68.152  40.414  1.00 18.34           O  
ATOM    304  CB  THR A  43       9.450  65.915  39.912  1.00 12.68           C  
ATOM    305  OG1 THR A  43      10.700  65.500  39.358  1.00 14.45           O  
ATOM    306  CG2 THR A  43       8.627  64.693  40.317  1.00 15.24           C  
ATOM    307  N   ASP A  44       6.278  66.864  39.038  1.00 13.46           N  
ATOM    308  CA  ASP A  44       5.012  67.292  39.606  1.00 16.90           C  
ATOM    309  C   ASP A  44       4.701  66.291  40.722  1.00 16.74           C  
ATOM    310  O   ASP A  44       4.389  65.139  40.436  1.00 16.41           O  
ATOM    311  CB  ASP A  44       3.921  67.264  38.531  1.00 16.34           C  
ATOM    312  CG  ASP A  44       2.574  67.756  39.041  1.00 20.37           C  
ATOM    313  OD1 ASP A  44       2.096  67.272  40.090  1.00 22.59           O  
ATOM    314  OD2 ASP A  44       1.976  68.623  38.380  1.00 19.84           O  
ATOM    315  N   ALA A  45       4.756  66.734  41.979  1.00 17.70           N  
ATOM    316  CA  ALA A  45       4.501  65.853  43.125  1.00 16.65           C  
ATOM    317  C   ALA A  45       3.084  65.260  43.169  1.00 17.07           C  
ATOM    318  O   ALA A  45       2.884  64.160  43.685  1.00 17.38           O  
ATOM    319  CB  ALA A  45       4.811  66.580  44.423  1.00 12.52           C  
ATOM    320  N   HIS A  46       2.113  65.967  42.590  1.00 15.56           N  
ATOM    321  CA  HIS A  46       0.722  65.505  42.572  1.00 14.83           C  
ATOM    322  C   HIS A  46       0.450  64.369  41.597  1.00 14.96           C  
ATOM    323  O   HIS A  46      -0.242  63.418  41.935  1.00 17.35           O  
ATOM    324  CB  HIS A  46      -0.226  66.669  42.272  1.00 20.54           C  
ATOM    325  CG  HIS A  46      -0.108  67.805  43.234  1.00 22.09           C  
ATOM    326  ND1 HIS A  46      -0.814  67.869  44.408  1.00 19.65           N  
ATOM    327  CD2 HIS A  46       0.656  68.923  43.201  1.00 21.30           C  
ATOM    328  CE1 HIS A  46      -0.491  68.967  45.063  1.00 20.95           C  
ATOM    329  NE2 HIS A  46       0.403  69.627  44.352  1.00 22.19           N  
ATOM    330  N   ILE A  47       0.964  64.481  40.377  1.00 18.53           N  
ATOM    331  CA  ILE A  47       0.756  63.436  39.370  1.00 17.29           C  
ATOM    332  C   ILE A  47       1.972  62.523  39.222  1.00 15.31           C  
ATOM    333  O   ILE A  47       1.938  61.534  38.496  1.00 14.71           O  
ATOM    334  CB  ILE A  47       0.358  64.029  37.991  1.00 17.62           C  
ATOM    335  CG1 ILE A  47       1.466  64.934  37.444  1.00 14.50           C  
ATOM    336  CG2 ILE A  47      -0.950  64.801  38.119  1.00 16.62           C  
ATOM    337  CD1 ILE A  47       1.186  65.471  36.055  1.00 17.66           C  
ATOM    338  N   GLU A  48       3.053  62.883  39.908  1.00 16.89           N  
ATOM    339  CA  GLU A  48       4.295  62.112  39.914  1.00 16.88           C  
ATOM    340  C   GLU A  48       5.060  62.037  38.597  1.00 21.03           C  
ATOM    341  O   GLU A  48       5.992  61.235  38.466  1.00 21.00           O  
ATOM    342  CB  GLU A  48       4.022  60.705  40.445  1.00 17.19           C  
ATOM    343  CG  GLU A  48       3.618  60.694  41.900  1.00 22.80           C  
ATOM    344  CD  GLU A  48       3.103  59.348  42.356  1.00 30.24           C  
ATOM    345  OE1 GLU A  48       3.880  58.369  42.370  1.00 32.22           O  
ATOM    346  OE2 GLU A  48       1.908  59.264  42.698  1.00 40.46           O  
ATOM    347  N   VAL A  49       4.694  62.886  37.638  1.00 20.07           N  
ATOM    348  CA  VAL A  49       5.356  62.884  36.338  1.00 16.68           C  
ATOM    349  C   VAL A  49       6.628  63.722  36.340  1.00 18.92           C  
ATOM    350  O   VAL A  49       6.664  64.802  36.927  1.00 20.12           O  
ATOM    351  CB  VAL A  49       4.400  63.360  35.218  1.00 15.90           C  
ATOM    352  CG1 VAL A  49       5.131  63.432  33.873  1.00 11.92           C  
ATOM    353  CG2 VAL A  49       3.225  62.405  35.126  1.00 15.12           C  
ATOM    354  N   ASN A  50       7.675  63.189  35.713  1.00 18.18           N  
ATOM    355  CA  ASN A  50       8.965  63.858  35.607  1.00 18.65           C  
ATOM    356  C   ASN A  50       9.169  64.323  34.181  1.00 20.28           C  
ATOM    357  O   ASN A  50       8.771  63.636  33.229  1.00 15.46           O  
ATOM    358  CB  ASN A  50      10.106  62.894  35.940  1.00 18.93           C  
ATOM    359  CG  ASN A  50      10.105  62.449  37.374  1.00 18.15           C  
ATOM    360  OD1 ASN A  50      10.562  63.171  38.252  1.00 20.57           O  
ATOM    361  ND2 ASN A  50       9.648  61.229  37.615  1.00 16.04           N  
ATOM    362  N   ILE A  51       9.760  65.498  34.024  1.00 19.35           N  
ATOM    363  CA  ILE A  51      10.066  66.013  32.698  1.00 20.39           C  
ATOM    364  C   ILE A  51      11.549  66.344  32.719  1.00 20.35           C  
ATOM    365  O   ILE A  51      12.039  67.022  33.629  1.00 17.00           O  
ATOM    366  CB  ILE A  51       9.171  67.208  32.282  1.00 22.05           C  
ATOM    367  CG1 ILE A  51       9.518  67.655  30.863  1.00 14.71           C  
ATOM    368  CG2 ILE A  51       9.275  68.359  33.283  1.00 22.12           C  
ATOM    369  CD1 ILE A  51       8.513  68.608  30.277  1.00 19.88           C  
ATOM    370  N   THR A  52      12.279  65.765  31.777  1.00 18.16           N  
ATOM    371  CA  THR A  52      13.714  65.944  31.712  1.00 20.11           C  
ATOM    372  C   THR A  52      14.169  67.251  31.086  1.00 16.73           C  
ATOM    373  O   THR A  52      13.386  67.962  30.459  1.00 16.84           O  
ATOM    374  CB  THR A  52      14.390  64.760  30.965  1.00 21.42           C  
ATOM    375  OG1 THR A  52      13.918  64.713  29.608  1.00 23.19           O  
ATOM    376  CG2 THR A  52      14.096  63.436  31.674  1.00 18.45           C  
ATOM    377  N   TYR A  53      15.451  67.554  31.276  1.00 17.02           N  
ATOM    378  CA  TYR A  53      16.042  68.753  30.704  1.00 17.67           C  
ATOM    379  C   TYR A  53      15.972  68.696  29.184  1.00 18.19           C  
ATOM    380  O   TYR A  53      15.709  69.703  28.549  1.00 21.68           O  
ATOM    381  CB  TYR A  53      17.480  68.928  31.196  1.00 16.08           C  
ATOM    382  CG  TYR A  53      17.566  69.727  32.483  1.00 16.79           C  
ATOM    383  CD1 TYR A  53      17.595  71.128  32.459  1.00 13.80           C  
ATOM    384  CD2 TYR A  53      17.577  69.089  33.726  1.00 14.15           C  
ATOM    385  CE1 TYR A  53      17.628  71.875  33.641  1.00 19.49           C  
ATOM    386  CE2 TYR A  53      17.609  69.824  34.918  1.00 17.77           C  
ATOM    387  CZ  TYR A  53      17.631  71.215  34.870  1.00 21.19           C  
ATOM    388  OH  TYR A  53      17.642  71.942  36.042  1.00 21.48           O  
ATOM    389  N   ALA A  54      16.160  67.514  28.601  1.00 18.39           N  
ATOM    390  CA  ALA A  54      16.079  67.356  27.149  1.00 15.06           C  
ATOM    391  C   ALA A  54      14.697  67.755  26.647  1.00 17.66           C  
ATOM    392  O   ALA A  54      14.572  68.542  25.704  1.00 18.56           O  
ATOM    393  CB  ALA A  54      16.376  65.938  26.757  1.00 15.98           C  
ATOM    394  N   GLU A  55      13.658  67.207  27.277  1.00 18.88           N  
ATOM    395  CA  GLU A  55      12.291  67.528  26.889  1.00 15.69           C  
ATOM    396  C   GLU A  55      12.026  69.013  27.075  1.00 17.31           C  
ATOM    397  O   GLU A  55      11.438  69.653  26.205  1.00 20.74           O  
ATOM    398  CB  GLU A  55      11.290  66.766  27.741  1.00 16.52           C  
ATOM    399  CG  GLU A  55      11.290  65.288  27.545  1.00 14.14           C  
ATOM    400  CD  GLU A  55      10.570  64.599  28.669  1.00 14.97           C  
ATOM    401  OE1 GLU A  55       9.325  64.538  28.637  1.00 14.11           O  
ATOM    402  OE2 GLU A  55      11.259  64.136  29.595  1.00 12.92           O  
ATOM    403  N   TYR A  56      12.461  69.555  28.211  1.00 16.86           N  
ATOM    404  CA  TYR A  56      12.245  70.963  28.516  1.00 18.29           C  
ATOM    405  C   TYR A  56      12.977  71.907  27.560  1.00 17.84           C  
ATOM    406  O   TYR A  56      12.397  72.876  27.058  1.00 18.21           O  
ATOM    407  CB  TYR A  56      12.636  71.270  29.966  1.00 13.61           C  
ATOM    408  CG  TYR A  56      11.572  72.072  30.666  1.00 16.51           C  
ATOM    409  CD1 TYR A  56      11.516  73.460  30.540  1.00 13.56           C  
ATOM    410  CD2 TYR A  56      10.547  71.433  31.361  1.00 17.04           C  
ATOM    411  CE1 TYR A  56      10.454  74.190  31.075  1.00 13.65           C  
ATOM    412  CE2 TYR A  56       9.482  72.153  31.902  1.00 15.53           C  
ATOM    413  CZ  TYR A  56       9.438  73.524  31.753  1.00 15.28           C  
ATOM    414  OH  TYR A  56       8.374  74.219  32.272  1.00 16.80           O  
ATOM    415  N   PHE A  57      14.251  71.617  27.320  1.00 19.58           N  
ATOM    416  CA  PHE A  57      15.096  72.410  26.435  1.00 19.22           C  
ATOM    417  C   PHE A  57      14.510  72.418  25.023  1.00 21.98           C  
ATOM    418  O   PHE A  57      14.343  73.474  24.403  1.00 23.57           O  
ATOM    419  CB  PHE A  57      16.513  71.819  26.414  1.00 17.55           C  
ATOM    420  CG  PHE A  57      17.411  72.426  25.371  1.00 24.00           C  
ATOM    421  CD1 PHE A  57      17.966  73.689  25.561  1.00 21.54           C  
ATOM    422  CD2 PHE A  57      17.676  71.744  24.181  1.00 20.20           C  
ATOM    423  CE1 PHE A  57      18.772  74.267  24.579  1.00 24.14           C  
ATOM    424  CE2 PHE A  57      18.480  72.313  23.192  1.00 17.81           C  
ATOM    425  CZ  PHE A  57      19.028  73.577  23.391  1.00 19.91           C  
ATOM    426  N   GLU A  58      14.171  71.234  24.527  1.00 22.03           N  
ATOM    427  CA  GLU A  58      13.615  71.116  23.194  1.00 19.58           C  
ATOM    428  C   GLU A  58      12.297  71.861  23.024  1.00 19.70           C  
ATOM    429  O   GLU A  58      12.116  72.583  22.042  1.00 18.54           O  
ATOM    430  CB  GLU A  58      13.491  69.642  22.803  1.00 21.49           C  
ATOM    431  CG  GLU A  58      14.857  68.988  22.544  1.00 16.74           C  
ATOM    432  CD  GLU A  58      14.805  67.466  22.469  1.00 20.62           C  
ATOM    433  OE1 GLU A  58      13.786  66.902  22.008  1.00 22.49           O  
ATOM    434  OE2 GLU A  58      15.798  66.830  22.878  1.00 21.03           O  
ATOM    435  N   MET A  59      11.404  71.754  24.000  1.00 18.35           N  
ATOM    436  CA  MET A  59      10.118  72.435  23.888  1.00 22.65           C  
ATOM    437  C   MET A  59      10.268  73.950  24.003  1.00 23.55           C  
ATOM    438  O   MET A  59       9.609  74.708  23.280  1.00 24.01           O  
ATOM    439  CB  MET A  59       9.118  71.913  24.927  1.00 22.71           C  
ATOM    440  CG  MET A  59       7.706  72.472  24.754  1.00 21.44           C  
ATOM    441  SD  MET A  59       7.035  72.148  23.103  1.00 27.95           S  
ATOM    442  CE  MET A  59       5.556  73.079  23.129  1.00 21.55           C  
ATOM    443  N   SER A  60      11.147  74.390  24.895  1.00 22.51           N  
ATOM    444  CA  SER A  60      11.374  75.815  25.093  1.00 21.85           C  
ATOM    445  C   SER A  60      11.988  76.444  23.845  1.00 19.08           C  
ATOM    446  O   SER A  60      11.581  77.522  23.416  1.00 21.94           O  
ATOM    447  CB  SER A  60      12.253  76.032  26.322  1.00 22.04           C  
ATOM    448  OG  SER A  60      11.619  75.502  27.479  1.00 20.99           O  
ATOM    449  N   VAL A  61      12.941  75.741  23.244  1.00 22.12           N  
ATOM    450  CA  VAL A  61      13.597  76.195  22.023  1.00 19.65           C  
ATOM    451  C   VAL A  61      12.583  76.244  20.876  1.00 21.87           C  
ATOM    452  O   VAL A  61      12.597  77.164  20.048  1.00 17.24           O  
ATOM    453  CB  VAL A  61      14.766  75.260  21.660  1.00 21.41           C  
ATOM    454  CG1 VAL A  61      15.149  75.429  20.211  1.00 25.33           C  
ATOM    455  CG2 VAL A  61      15.967  75.549  22.554  1.00 18.71           C  
ATOM    456  N   ARG A  62      11.701  75.251  20.833  1.00 23.21           N  
ATOM    457  CA  ARG A  62      10.681  75.198  19.803  1.00 22.44           C  
ATOM    458  C   ARG A  62       9.702  76.350  19.962  1.00 23.78           C  
ATOM    459  O   ARG A  62       9.262  76.923  18.971  1.00 24.66           O  
ATOM    460  CB  ARG A  62       9.956  73.856  19.833  1.00 21.63           C  
ATOM    461  CG  ARG A  62      10.796  72.728  19.256  1.00 25.32           C  
ATOM    462  CD  ARG A  62      10.206  71.365  19.543  1.00 21.53           C  
ATOM    463  NE  ARG A  62       8.876  71.201  18.972  1.00 30.07           N  
ATOM    464  CZ  ARG A  62       8.638  70.632  17.794  1.00 36.42           C  
ATOM    465  NH1 ARG A  62       9.651  70.179  17.061  1.00 37.58           N  
ATOM    466  NH2 ARG A  62       7.392  70.513  17.350  1.00 29.33           N  
ATOM    467  N   LEU A  63       9.374  76.692  21.205  1.00 23.79           N  
ATOM    468  CA  LEU A  63       8.460  77.796  21.484  1.00 22.14           C  
ATOM    469  C   LEU A  63       9.101  79.129  21.132  1.00 22.02           C  
ATOM    470  O   LEU A  63       8.420  80.043  20.661  1.00 23.66           O  
ATOM    471  CB  LEU A  63       8.038  77.805  22.956  1.00 20.97           C  
ATOM    472  CG  LEU A  63       6.795  76.995  23.327  1.00 22.10           C  
ATOM    473  CD1 LEU A  63       6.764  76.742  24.820  1.00 22.63           C  
ATOM    474  CD2 LEU A  63       5.543  77.719  22.865  1.00 17.86           C  
ATOM    475  N   ALA A  64      10.402  79.243  21.388  1.00 19.63           N  
ATOM    476  CA  ALA A  64      11.147  80.465  21.084  1.00 20.15           C  
ATOM    477  C   ALA A  64      11.099  80.707  19.580  1.00 21.24           C  
ATOM    478  O   ALA A  64      10.692  81.778  19.121  1.00 24.46           O  
ATOM    479  CB  ALA A  64      12.590  80.340  21.558  1.00 12.51           C  
ATOM    480  N   GLU A  65      11.450  79.684  18.814  1.00 23.01           N  
ATOM    481  CA  GLU A  65      11.432  79.794  17.365  1.00 22.92           C  
ATOM    482  C   GLU A  65      10.018  80.047  16.839  1.00 21.76           C  
ATOM    483  O   GLU A  65       9.808  80.927  16.007  1.00 25.46           O  
ATOM    484  CB  GLU A  65      12.017  78.535  16.727  1.00 22.49           C  
ATOM    485  CG  GLU A  65      12.108  78.585  15.196  1.00 24.16           C  
ATOM    486  CD  GLU A  65      13.150  79.566  14.699  1.00 24.32           C  
ATOM    487  OE1 GLU A  65      14.094  79.863  15.452  1.00 28.67           O  
ATOM    488  OE2 GLU A  65      13.034  80.038  13.553  1.00 28.79           O  
ATOM    489  N   ALA A  66       9.045  79.300  17.345  1.00 20.97           N  
ATOM    490  CA  ALA A  66       7.664  79.453  16.908  1.00 17.58           C  
ATOM    491  C   ALA A  66       7.148  80.877  17.141  1.00 22.49           C  
ATOM    492  O   ALA A  66       6.464  81.447  16.283  1.00 25.70           O  
ATOM    493  CB  ALA A  66       6.776  78.432  17.607  1.00 14.99           C  
ATOM    494  N   MET A  67       7.471  81.451  18.296  1.00 23.20           N  
ATOM    495  CA  MET A  67       7.044  82.813  18.606  1.00 24.16           C  
ATOM    496  C   MET A  67       7.766  83.789  17.688  1.00 23.42           C  
ATOM    497  O   MET A  67       7.166  84.746  17.203  1.00 23.80           O  
ATOM    498  CB  MET A  67       7.312  83.160  20.074  1.00 26.28           C  
ATOM    499  CG  MET A  67       6.359  82.492  21.073  1.00 27.86           C  
ATOM    500  SD  MET A  67       6.578  83.077  22.776  1.00 26.09           S  
ATOM    501  CE  MET A  67       7.901  82.054  23.311  1.00 17.35           C  
ATOM    502  N   LYS A  68       9.049  83.536  17.447  1.00 24.74           N  
ATOM    503  CA  LYS A  68       9.843  84.375  16.554  1.00 25.40           C  
ATOM    504  C   LYS A  68       9.191  84.396  15.173  1.00 27.05           C  
ATOM    505  O   LYS A  68       8.914  85.464  14.633  1.00 30.27           O  
ATOM    506  CB  LYS A  68      11.274  83.844  16.461  1.00 26.83           C  
ATOM    507  CG  LYS A  68      12.147  84.550  15.434  1.00 28.56           C  
ATOM    508  CD  LYS A  68      13.610  84.181  15.600  1.00 33.01           C  
ATOM    509  CE  LYS A  68      14.459  84.810  14.505  1.00 42.36           C  
ATOM    510  NZ  LYS A  68      15.925  84.630  14.727  1.00 46.07           N  
ATOM    511  N   ARG A  69       8.897  83.213  14.639  1.00 28.95           N  
ATOM    512  CA  ARG A  69       8.255  83.069  13.334  1.00 27.03           C  
ATOM    513  C   ARG A  69       6.875  83.724  13.298  1.00 26.37           C  
ATOM    514  O   ARG A  69       6.431  84.203  12.254  1.00 29.00           O  
ATOM    515  CB  ARG A  69       8.117  81.590  12.981  1.00 24.47           C  
ATOM    516  CG  ARG A  69       9.433  80.866  12.781  1.00 27.03           C  
ATOM    517  CD  ARG A  69      10.074  81.254  11.466  1.00 30.88           C  
ATOM    518  NE  ARG A  69      11.389  80.645  11.311  1.00 35.53           N  
ATOM    519  CZ  ARG A  69      12.075  80.590  10.169  1.00 35.88           C  
ATOM    520  NH1 ARG A  69      11.574  81.096   9.050  1.00 32.74           N  
ATOM    521  NH2 ARG A  69      13.291  80.063  10.157  1.00 33.41           N  
ATOM    522  N   TYR A  70       6.178  83.684  14.427  1.00 29.24           N  
ATOM    523  CA  TYR A  70       4.849  84.273  14.546  1.00 29.11           C  
ATOM    524  C   TYR A  70       4.908  85.796  14.448  1.00 28.20           C  
ATOM    525  O   TYR A  70       3.922  86.433  14.084  1.00 33.21           O  
ATOM    526  CB  TYR A  70       4.209  83.854  15.875  1.00 29.06           C  
ATOM    527  CG  TYR A  70       2.849  84.463  16.154  1.00 27.09           C  
ATOM    528  CD1 TYR A  70       1.693  83.904  15.616  1.00 30.03           C  
ATOM    529  CD2 TYR A  70       2.719  85.588  16.968  1.00 28.49           C  
ATOM    530  CE1 TYR A  70       0.433  84.446  15.883  1.00 34.58           C  
ATOM    531  CE2 TYR A  70       1.466  86.144  17.241  1.00 34.11           C  
ATOM    532  CZ  TYR A  70       0.322  85.567  16.697  1.00 35.67           C  
ATOM    533  OH  TYR A  70      -0.930  86.093  16.979  1.00 33.25           O  
ATOM    534  N   GLY A  71       6.037  86.381  14.832  1.00 30.33           N  
ATOM    535  CA  GLY A  71       6.173  87.824  14.760  1.00 29.59           C  
ATOM    536  C   GLY A  71       6.510  88.548  16.052  1.00 31.01           C  
ATOM    537  O   GLY A  71       6.469  89.781  16.094  1.00 35.59           O  
ATOM    538  N   LEU A  72       6.846  87.816  17.111  1.00 27.91           N  
ATOM    539  CA  LEU A  72       7.176  88.469  18.373  1.00 24.47           C  
ATOM    540  C   LEU A  72       8.657  88.755  18.465  1.00 25.00           C  
ATOM    541  O   LEU A  72       9.488  87.963  18.030  1.00 26.48           O  
ATOM    542  CB  LEU A  72       6.729  87.640  19.579  1.00 25.39           C  
ATOM    543  CG  LEU A  72       5.264  87.193  19.626  1.00 26.13           C  
ATOM    544  CD1 LEU A  72       4.985  86.531  20.958  1.00 28.38           C  
ATOM    545  CD2 LEU A  72       4.322  88.365  19.410  1.00 23.90           C  
ATOM    546  N   ASN A  73       8.976  89.897  19.052  1.00 23.64           N  
ATOM    547  CA  ASN A  73      10.354  90.333  19.225  1.00 27.64           C  
ATOM    548  C   ASN A  73      10.357  91.231  20.458  1.00 27.25           C  
ATOM    549  O   ASN A  73       9.332  91.335  21.130  1.00 28.72           O  
ATOM    550  CB  ASN A  73      10.846  91.086  17.979  1.00 30.19           C  
ATOM    551  CG  ASN A  73       9.940  92.248  17.595  1.00 33.84           C  
ATOM    552  OD1 ASN A  73       9.792  93.210  18.348  1.00 37.28           O  
ATOM    553  ND2 ASN A  73       9.302  92.147  16.442  1.00 33.51           N  
ATOM    554  N   THR A  74      11.462  91.925  20.715  1.00 26.67           N  
ATOM    555  CA  THR A  74      11.587  92.792  21.887  1.00 27.16           C  
ATOM    556  C   THR A  74      10.519  93.877  22.065  1.00 28.91           C  
ATOM    557  O   THR A  74      10.467  94.524  23.110  1.00 31.56           O  
ATOM    558  CB  THR A  74      12.969  93.459  21.940  1.00 29.41           C  
ATOM    559  OG1 THR A  74      13.168  94.236  20.752  1.00 34.68           O  
ATOM    560  CG2 THR A  74      14.071  92.409  22.061  1.00 23.41           C  
ATOM    561  N   ASN A  75       9.690  94.095  21.045  1.00 27.16           N  
ATOM    562  CA  ASN A  75       8.622  95.095  21.114  1.00 29.09           C  
ATOM    563  C   ASN A  75       7.326  94.469  21.617  1.00 32.41           C  
ATOM    564  O   ASN A  75       6.271  95.120  21.655  1.00 30.28           O  
ATOM    565  CB  ASN A  75       8.368  95.714  19.735  1.00 34.27           C  
ATOM    566  CG  ASN A  75       9.516  96.590  19.257  1.00 40.17           C  
ATOM    567  OD1 ASN A  75       9.919  97.536  19.934  1.00 41.74           O  
ATOM    568  ND2 ASN A  75      10.043  96.278  18.083  1.00 42.44           N  
ATOM    569  N   HIS A  76       7.396  93.193  21.987  1.00 34.32           N  
ATOM    570  CA  HIS A  76       6.223  92.472  22.459  1.00 32.30           C  
ATOM    571  C   HIS A  76       6.402  91.886  23.848  1.00 31.06           C  
ATOM    572  O   HIS A  76       7.522  91.772  24.360  1.00 25.36           O  
ATOM    573  CB  HIS A  76       5.865  91.359  21.473  1.00 35.11           C  
ATOM    574  CG  HIS A  76       5.667  91.840  20.071  1.00 35.94           C  
ATOM    575  ND1 HIS A  76       6.717  92.074  19.210  1.00 38.05           N  
ATOM    576  CD2 HIS A  76       4.541  92.130  19.375  1.00 38.32           C  
ATOM    577  CE1 HIS A  76       6.247  92.483  18.044  1.00 38.54           C  
ATOM    578  NE2 HIS A  76       4.929  92.526  18.123  1.00 38.49           N  
ATOM    579  N   ARG A  77       5.275  91.529  24.455  1.00 32.97           N  
ATOM    580  CA  ARG A  77       5.253  90.938  25.783  1.00 29.18           C  
ATOM    581  C   ARG A  77       4.224  89.834  25.752  1.00 27.57           C  
ATOM    582  O   ARG A  77       3.306  89.852  24.923  1.00 25.58           O  
ATOM    583  CB  ARG A  77       4.845  91.988  26.820  1.00 30.49           C  
ATOM    584  CG  ARG A  77       5.839  93.138  26.937  1.00 36.51           C  
ATOM    585  CD  ARG A  77       5.171  94.404  27.415  1.00 40.61           C  
ATOM    586  NE  ARG A  77       4.082  94.815  26.529  1.00 41.72           N  
ATOM    587  CZ  ARG A  77       4.240  95.497  25.400  1.00 44.37           C  
ATOM    588  NH1 ARG A  77       5.455  95.851  24.997  1.00 47.47           N  
ATOM    589  NH2 ARG A  77       3.180  95.831  24.678  1.00 43.95           N  
ATOM    590  N   ILE A  78       4.445  88.812  26.562  1.00 26.24           N  
ATOM    591  CA  ILE A  78       3.492  87.721  26.656  1.00 27.23           C  
ATOM    592  C   ILE A  78       3.131  87.572  28.121  1.00 26.01           C  
ATOM    593  O   ILE A  78       3.865  88.027  29.004  1.00 27.33           O  
ATOM    594  CB  ILE A  78       4.050  86.365  26.144  1.00 25.92           C  
ATOM    595  CG1 ILE A  78       5.302  85.961  26.924  1.00 22.88           C  
ATOM    596  CG2 ILE A  78       4.285  86.421  24.640  1.00 23.93           C  
ATOM    597  CD1 ILE A  78       5.628  84.487  26.824  1.00 15.43           C  
ATOM    598  N   VAL A  79       1.970  86.994  28.374  1.00 24.86           N  
ATOM    599  CA  VAL A  79       1.530  86.753  29.732  1.00 26.26           C  
ATOM    600  C   VAL A  79       1.441  85.245  29.926  1.00 27.59           C  
ATOM    601  O   VAL A  79       1.086  84.509  29.001  1.00 26.35           O  
ATOM    602  CB  VAL A  79       0.151  87.422  30.010  1.00 25.66           C  
ATOM    603  CG1 VAL A  79      -0.593  86.722  31.156  1.00 22.10           C  
ATOM    604  CG2 VAL A  79       0.362  88.885  30.360  1.00 23.91           C  
ATOM    605  N   VAL A  80       1.881  84.781  31.088  1.00 24.25           N  
ATOM    606  CA  VAL A  80       1.802  83.363  31.420  1.00 22.04           C  
ATOM    607  C   VAL A  80       0.935  83.321  32.673  1.00 19.97           C  
ATOM    608  O   VAL A  80       1.312  83.851  33.721  1.00 21.41           O  
ATOM    609  CB  VAL A  80       3.200  82.759  31.687  1.00 22.20           C  
ATOM    610  CG1 VAL A  80       3.093  81.319  32.166  1.00 15.43           C  
ATOM    611  CG2 VAL A  80       4.038  82.821  30.421  1.00 15.66           C  
ATOM    612  N   CYS A  81      -0.282  82.823  32.519  1.00 17.28           N  
ATOM    613  CA  CYS A  81      -1.211  82.734  33.632  1.00 21.68           C  
ATOM    614  C   CYS A  81      -1.525  81.278  33.906  1.00 21.87           C  
ATOM    615  O   CYS A  81      -2.291  80.647  33.173  1.00 21.96           O  
ATOM    616  CB  CYS A  81      -2.501  83.502  33.329  1.00 23.07           C  
ATOM    617  SG  CYS A  81      -3.653  83.450  34.711  1.00 26.52           S  
ATOM    618  N   SER A  82      -0.933  80.753  34.969  1.00 22.66           N  
ATOM    619  CA  SER A  82      -1.122  79.364  35.312  1.00 21.08           C  
ATOM    620  C   SER A  82      -0.669  79.078  36.730  1.00 23.45           C  
ATOM    621  O   SER A  82       0.154  79.800  37.298  1.00 21.77           O  
ATOM    622  CB  SER A  82      -0.297  78.497  34.347  1.00 16.23           C  
ATOM    623  OG  SER A  82      -0.443  77.123  34.636  1.00 20.84           O  
ATOM    624  N   GLU A  83      -1.251  78.032  37.301  1.00 21.66           N  
ATOM    625  CA  GLU A  83      -0.878  77.570  38.620  1.00 20.06           C  
ATOM    626  C   GLU A  83       0.464  76.885  38.351  1.00 22.87           C  
ATOM    627  O   GLU A  83       0.814  76.653  37.188  1.00 21.98           O  
ATOM    628  CB  GLU A  83      -1.905  76.556  39.138  1.00 19.69           C  
ATOM    629  CG  GLU A  83      -2.151  75.331  38.245  1.00 28.47           C  
ATOM    630  CD  GLU A  83      -3.142  75.558  37.079  1.00 32.35           C  
ATOM    631  OE1 GLU A  83      -3.631  76.702  36.854  1.00 27.26           O  
ATOM    632  OE2 GLU A  83      -3.439  74.556  36.379  1.00 20.13           O  
ATOM    633  N   ASN A  84       1.234  76.600  39.396  1.00 20.90           N  
ATOM    634  CA  ASN A  84       2.517  75.932  39.210  1.00 19.30           C  
ATOM    635  C   ASN A  84       2.246  74.635  38.458  1.00 22.03           C  
ATOM    636  O   ASN A  84       1.293  73.916  38.769  1.00 19.13           O  
ATOM    637  CB  ASN A  84       3.188  75.625  40.553  1.00 19.15           C  
ATOM    638  CG  ASN A  84       3.764  76.864  41.224  1.00 26.24           C  
ATOM    639  OD1 ASN A  84       3.581  77.993  40.746  1.00 25.75           O  
ATOM    640  ND2 ASN A  84       4.456  76.662  42.340  1.00 24.24           N  
ATOM    641  N   SER A  85       3.060  74.362  37.444  1.00 22.10           N  
ATOM    642  CA  SER A  85       2.894  73.164  36.634  1.00 19.03           C  
ATOM    643  C   SER A  85       4.189  72.844  35.916  1.00 21.10           C  
ATOM    644  O   SER A  85       5.146  73.633  35.941  1.00 22.55           O  
ATOM    645  CB  SER A  85       1.824  73.398  35.580  1.00 15.56           C  
ATOM    646  OG  SER A  85       2.283  74.347  34.633  1.00 17.63           O  
ATOM    647  N   LEU A  86       4.194  71.696  35.246  1.00 18.92           N  
ATOM    648  CA  LEU A  86       5.355  71.259  34.482  1.00 20.12           C  
ATOM    649  C   LEU A  86       5.518  72.119  33.227  1.00 18.37           C  
ATOM    650  O   LEU A  86       6.616  72.228  32.688  1.00 21.81           O  
ATOM    651  CB  LEU A  86       5.188  69.794  34.068  1.00 22.70           C  
ATOM    652  CG  LEU A  86       5.124  68.698  35.136  1.00 20.83           C  
ATOM    653  CD1 LEU A  86       4.816  67.366  34.478  1.00 17.46           C  
ATOM    654  CD2 LEU A  86       6.443  68.640  35.883  1.00 16.54           C  
ATOM    655  N   GLN A  87       4.422  72.711  32.758  1.00 18.98           N  
ATOM    656  CA  GLN A  87       4.445  73.537  31.555  1.00 19.79           C  
ATOM    657  C   GLN A  87       4.772  75.005  31.783  1.00 19.32           C  
ATOM    658  O   GLN A  87       5.172  75.696  30.848  1.00 23.81           O  
ATOM    659  CB  GLN A  87       3.098  73.462  30.816  1.00 17.33           C  
ATOM    660  CG  GLN A  87       2.736  72.101  30.279  1.00 17.87           C  
ATOM    661  CD  GLN A  87       2.315  71.142  31.370  1.00 17.42           C  
ATOM    662  OE1 GLN A  87       1.624  71.520  32.315  1.00 19.45           O  
ATOM    663  NE2 GLN A  87       2.746  69.896  31.254  1.00 17.34           N  
ATOM    664  N   PHE A  88       4.599  75.475  33.015  1.00 20.14           N  
ATOM    665  CA  PHE A  88       4.819  76.876  33.365  1.00 19.20           C  
ATOM    666  C   PHE A  88       6.024  77.579  32.730  1.00 18.29           C  
ATOM    667  O   PHE A  88       5.889  78.630  32.098  1.00 15.62           O  
ATOM    668  CB  PHE A  88       4.889  77.043  34.889  1.00 15.53           C  
ATOM    669  CG  PHE A  88       4.743  78.468  35.338  1.00 15.39           C  
ATOM    670  CD1 PHE A  88       5.826  79.346  35.289  1.00 15.53           C  
ATOM    671  CD2 PHE A  88       3.502  78.956  35.729  1.00 16.92           C  
ATOM    672  CE1 PHE A  88       5.676  80.687  35.611  1.00 16.08           C  
ATOM    673  CE2 PHE A  88       3.338  80.300  36.056  1.00 19.01           C  
ATOM    674  CZ  PHE A  88       4.429  81.168  35.994  1.00 20.46           C  
ATOM    675  N   PHE A  89       7.208  77.016  32.911  1.00 19.42           N  
ATOM    676  CA  PHE A  89       8.406  77.644  32.380  1.00 20.77           C  
ATOM    677  C   PHE A  89       8.704  77.484  30.897  1.00 20.52           C  
ATOM    678  O   PHE A  89       9.615  78.134  30.385  1.00 23.16           O  
ATOM    679  CB  PHE A  89       9.623  77.283  33.243  1.00 19.61           C  
ATOM    680  CG  PHE A  89       9.676  78.045  34.530  1.00 16.00           C  
ATOM    681  CD1 PHE A  89       9.006  77.587  35.655  1.00 14.53           C  
ATOM    682  CD2 PHE A  89      10.334  79.268  34.596  1.00 19.24           C  
ATOM    683  CE1 PHE A  89       8.987  78.338  36.823  1.00 16.79           C  
ATOM    684  CE2 PHE A  89      10.320  80.026  35.765  1.00 16.38           C  
ATOM    685  CZ  PHE A  89       9.642  79.559  36.879  1.00 17.35           C  
ATOM    686  N   MET A  90       7.927  76.669  30.193  1.00 20.68           N  
ATOM    687  CA  MET A  90       8.163  76.483  28.764  1.00 18.00           C  
ATOM    688  C   MET A  90       8.028  77.818  28.024  1.00 19.96           C  
ATOM    689  O   MET A  90       8.966  78.246  27.341  1.00 21.13           O  
ATOM    690  CB  MET A  90       7.236  75.406  28.184  1.00 14.06           C  
ATOM    691  CG  MET A  90       7.569  73.990  28.648  1.00 11.74           C  
ATOM    692  SD  MET A  90       6.347  72.759  28.160  1.00 20.13           S  
ATOM    693  CE  MET A  90       7.072  71.293  28.804  1.00 10.57           C  
ATOM    694  N   PRO A  91       6.876  78.505  28.155  1.00 17.33           N  
ATOM    695  CA  PRO A  91       6.770  79.787  27.446  1.00 16.25           C  
ATOM    696  C   PRO A  91       7.701  80.855  28.015  1.00 21.48           C  
ATOM    697  O   PRO A  91       8.166  81.727  27.282  1.00 24.45           O  
ATOM    698  CB  PRO A  91       5.298  80.161  27.607  1.00 14.54           C  
ATOM    699  CG  PRO A  91       4.862  79.420  28.844  1.00 17.56           C  
ATOM    700  CD  PRO A  91       5.572  78.102  28.716  1.00 14.94           C  
ATOM    701  N   VAL A  92       7.998  80.760  29.309  1.00 19.52           N  
ATOM    702  CA  VAL A  92       8.891  81.705  29.979  1.00 17.63           C  
ATOM    703  C   VAL A  92      10.283  81.646  29.337  1.00 19.81           C  
ATOM    704  O   VAL A  92      10.829  82.670  28.909  1.00 19.31           O  
ATOM    705  CB  VAL A  92       8.998  81.387  31.502  1.00 14.82           C  
ATOM    706  CG1 VAL A  92      10.024  82.282  32.185  1.00 15.38           C  
ATOM    707  CG2 VAL A  92       7.651  81.551  32.158  1.00 12.73           C  
ATOM    708  N   LEU A  93      10.837  80.439  29.250  1.00 19.23           N  
ATOM    709  CA  LEU A  93      12.155  80.232  28.664  1.00 22.39           C  
ATOM    710  C   LEU A  93      12.155  80.589  27.181  1.00 23.80           C  
ATOM    711  O   LEU A  93      13.061  81.269  26.706  1.00 24.45           O  
ATOM    712  CB  LEU A  93      12.613  78.790  28.866  1.00 19.70           C  
ATOM    713  CG  LEU A  93      12.893  78.416  30.322  1.00 19.80           C  
ATOM    714  CD1 LEU A  93      13.275  76.955  30.434  1.00 22.29           C  
ATOM    715  CD2 LEU A  93      14.004  79.297  30.867  1.00 16.06           C  
ATOM    716  N   GLY A  94      11.125  80.149  26.464  1.00 23.74           N  
ATOM    717  CA  GLY A  94      11.018  80.456  25.048  1.00 23.88           C  
ATOM    718  C   GLY A  94      11.099  81.951  24.773  1.00 27.82           C  
ATOM    719  O   GLY A  94      11.817  82.373  23.866  1.00 27.67           O  
ATOM    720  N   ALA A  95      10.376  82.749  25.560  1.00 26.40           N  
ATOM    721  CA  ALA A  95      10.371  84.205  25.405  1.00 21.90           C  
ATOM    722  C   ALA A  95      11.729  84.811  25.747  1.00 21.90           C  
ATOM    723  O   ALA A  95      12.221  85.695  25.041  1.00 23.78           O  
ATOM    724  CB  ALA A  95       9.287  84.828  26.267  1.00 16.27           C  
ATOM    725  N   LEU A  96      12.331  84.347  26.833  1.00 19.78           N  
ATOM    726  CA  LEU A  96      13.633  84.852  27.232  1.00 23.93           C  
ATOM    727  C   LEU A  96      14.680  84.539  26.167  1.00 25.86           C  
ATOM    728  O   LEU A  96      15.634  85.304  25.991  1.00 26.12           O  
ATOM    729  CB  LEU A  96      14.058  84.266  28.577  1.00 24.50           C  
ATOM    730  CG  LEU A  96      13.184  84.654  29.769  1.00 25.74           C  
ATOM    731  CD1 LEU A  96      13.754  84.030  31.025  1.00 23.18           C  
ATOM    732  CD2 LEU A  96      13.108  86.171  29.893  1.00 20.47           C  
ATOM    733  N   PHE A  97      14.508  83.411  25.475  1.00 25.37           N  
ATOM    734  CA  PHE A  97      15.430  83.010  24.414  1.00 23.86           C  
ATOM    735  C   PHE A  97      15.404  84.019  23.260  1.00 24.03           C  
ATOM    736  O   PHE A  97      16.428  84.275  22.637  1.00 26.60           O  
ATOM    737  CB  PHE A  97      15.093  81.609  23.883  1.00 17.45           C  
ATOM    738  CG  PHE A  97      15.429  80.484  24.834  1.00 16.28           C  
ATOM    739  CD1 PHE A  97      16.122  80.720  26.013  1.00 14.52           C  
ATOM    740  CD2 PHE A  97      15.036  79.178  24.540  1.00 16.59           C  
ATOM    741  CE1 PHE A  97      16.417  79.676  26.887  1.00 18.57           C  
ATOM    742  CE2 PHE A  97      15.327  78.127  25.408  1.00 15.98           C  
ATOM    743  CZ  PHE A  97      16.017  78.377  26.583  1.00 18.95           C  
ATOM    744  N   ILE A  98      14.240  84.604  22.986  1.00 23.38           N  
ATOM    745  CA  ILE A  98      14.128  85.580  21.910  1.00 23.19           C  
ATOM    746  C   ILE A  98      13.955  87.044  22.345  1.00 26.65           C  
ATOM    747  O   ILE A  98      13.712  87.914  21.505  1.00 31.24           O  
ATOM    748  CB  ILE A  98      13.027  85.202  20.881  1.00 23.88           C  
ATOM    749  CG1 ILE A  98      11.665  85.042  21.555  1.00 19.33           C  
ATOM    750  CG2 ILE A  98      13.417  83.939  20.141  1.00 24.23           C  
ATOM    751  CD1 ILE A  98      10.535  84.884  20.571  1.00 15.19           C  
ATOM    752  N   GLY A  99      14.078  87.320  23.641  1.00 24.88           N  
ATOM    753  CA  GLY A  99      13.962  88.685  24.122  1.00 21.51           C  
ATOM    754  C   GLY A  99      12.574  89.273  24.255  1.00 25.87           C  
ATOM    755  O   GLY A  99      12.410  90.493  24.245  1.00 26.97           O  
ATOM    756  N   VAL A 100      11.566  88.414  24.325  1.00 27.11           N  
ATOM    757  CA  VAL A 100      10.188  88.860  24.499  1.00 24.15           C  
ATOM    758  C   VAL A 100       9.979  88.932  26.013  1.00 25.97           C  
ATOM    759  O   VAL A 100      10.393  88.020  26.735  1.00 27.76           O  
ATOM    760  CB  VAL A 100       9.203  87.857  23.863  1.00 25.15           C  
ATOM    761  CG1 VAL A 100       7.780  88.134  24.297  1.00 22.93           C  
ATOM    762  CG2 VAL A 100       9.316  87.917  22.344  1.00 24.04           C  
ATOM    763  N   ALA A 101       9.411  90.036  26.494  1.00 25.81           N  
ATOM    764  CA  ALA A 101       9.173  90.226  27.929  1.00 23.85           C  
ATOM    765  C   ALA A 101       8.050  89.333  28.465  1.00 24.26           C  
ATOM    766  O   ALA A 101       6.969  89.258  27.873  1.00 25.20           O  
ATOM    767  CB  ALA A 101       8.875  91.684  28.220  1.00 23.75           C  
ATOM    768  N   VAL A 102       8.308  88.665  29.588  1.00 24.01           N  
ATOM    769  CA  VAL A 102       7.332  87.766  30.201  1.00 21.38           C  
ATOM    770  C   VAL A 102       6.644  88.426  31.395  1.00 22.09           C  
ATOM    771  O   VAL A 102       7.303  88.901  32.322  1.00 24.60           O  
ATOM    772  CB  VAL A 102       8.008  86.455  30.685  1.00 22.17           C  
ATOM    773  CG1 VAL A 102       6.969  85.508  31.267  1.00 16.86           C  
ATOM    774  CG2 VAL A 102       8.748  85.789  29.537  1.00 14.99           C  
ATOM    775  N   ALA A 103       5.318  88.442  31.374  1.00 20.59           N  
ATOM    776  CA  ALA A 103       4.547  89.041  32.451  1.00 20.33           C  
ATOM    777  C   ALA A 103       3.657  87.980  33.106  1.00 18.86           C  
ATOM    778  O   ALA A 103       2.569  87.691  32.612  1.00 19.76           O  
ATOM    779  CB  ALA A 103       3.705  90.179  31.907  1.00 20.73           C  
ATOM    780  N   PRO A 104       4.134  87.354  34.204  1.00 18.87           N  
ATOM    781  CA  PRO A 104       3.414  86.314  34.958  1.00 20.43           C  
ATOM    782  C   PRO A 104       2.192  86.892  35.679  1.00 22.99           C  
ATOM    783  O   PRO A 104       2.329  87.791  36.517  1.00 27.11           O  
ATOM    784  CB  PRO A 104       4.458  85.839  35.975  1.00 16.17           C  
ATOM    785  CG  PRO A 104       5.774  86.283  35.406  1.00 15.90           C  
ATOM    786  CD  PRO A 104       5.454  87.606  34.807  1.00 15.31           C  
ATOM    787  N   ALA A 105       1.005  86.381  35.364  1.00 26.21           N  
ATOM    788  CA  ALA A 105      -0.220  86.877  35.993  1.00 29.78           C  
ATOM    789  C   ALA A 105      -0.688  85.927  37.090  1.00 31.73           C  
ATOM    790  O   ALA A 105      -0.861  84.724  36.856  1.00 32.37           O  
ATOM    791  CB  ALA A 105      -1.314  87.077  34.956  1.00 28.56           C  
ATOM    792  N   ASN A 106      -0.893  86.470  38.288  1.00 30.19           N  
ATOM    793  CA  ASN A 106      -1.330  85.673  39.430  1.00 30.45           C  
ATOM    794  C   ASN A 106      -2.610  84.922  39.072  1.00 30.85           C  
ATOM    795  O   ASN A 106      -3.647  85.533  38.818  1.00 35.15           O  
ATOM    796  CB  ASN A 106      -1.548  86.564  40.648  1.00 25.95           C  
ATOM    797  CG  ASN A 106      -1.871  85.774  41.905  1.00 28.73           C  
ATOM    798  OD1 ASN A 106      -2.413  84.670  41.841  1.00 25.25           O  
ATOM    799  ND2 ASN A 106      -1.511  86.325  43.057  1.00 26.22           N  
ATOM    800  N   ASP A 107      -2.529  83.594  39.084  1.00 30.08           N  
ATOM    801  CA  ASP A 107      -3.653  82.730  38.728  1.00 28.80           C  
ATOM    802  C   ASP A 107      -4.894  82.719  39.655  1.00 32.99           C  
ATOM    803  O   ASP A 107      -5.919  82.110  39.325  1.00 26.08           O  
ATOM    804  CB  ASP A 107      -3.145  81.313  38.495  1.00 26.50           C  
ATOM    805  CG  ASP A 107      -2.597  80.679  39.759  1.00 25.80           C  
ATOM    806  OD1 ASP A 107      -1.647  81.225  40.359  1.00 24.67           O  
ATOM    807  OD2 ASP A 107      -3.130  79.631  40.157  1.00 25.48           O  
ATOM    808  N   ILE A 108      -4.778  83.308  40.843  1.00 37.02           N  
ATOM    809  CA  ILE A 108      -5.934  83.388  41.746  1.00 42.69           C  
ATOM    810  C   ILE A 108      -6.445  84.826  41.788  1.00 42.41           C  
ATOM    811  O   ILE A 108      -7.152  85.221  42.722  1.00 38.99           O  
ATOM    812  CB  ILE A 108      -5.655  82.896  43.191  1.00 43.11           C  
ATOM    813  CG1 ILE A 108      -4.393  83.562  43.763  1.00 43.58           C  
ATOM    814  CG2 ILE A 108      -5.649  81.367  43.242  1.00 40.17           C  
ATOM    815  CD1 ILE A 108      -4.256  83.436  45.261  1.00 47.02           C  
ATOM    816  N   TYR A 109      -6.005  85.627  40.816  1.00 42.27           N  
ATOM    817  CA  TYR A 109      -6.450  87.001  40.685  1.00 39.56           C  
ATOM    818  C   TYR A 109      -7.887  86.865  40.193  1.00 38.45           C  
ATOM    819  O   TYR A 109      -8.201  85.949  39.431  1.00 29.27           O  
ATOM    820  CB  TYR A 109      -5.660  87.727  39.594  1.00 32.69           C  
ATOM    821  CG  TYR A 109      -4.486  88.589  40.032  1.00 32.82           C  
ATOM    822  CD1 TYR A 109      -4.280  88.926  41.377  1.00 28.37           C  
ATOM    823  CD2 TYR A 109      -3.601  89.096  39.089  1.00 34.32           C  
ATOM    824  CE1 TYR A 109      -3.220  89.750  41.747  1.00 29.90           C  
ATOM    825  CE2 TYR A 109      -2.543  89.915  39.449  1.00 33.90           C  
ATOM    826  CZ  TYR A 109      -2.356  90.241  40.777  1.00 33.10           C  
ATOM    827  OH  TYR A 109      -1.304  91.066  41.123  1.00 38.11           O  
ATOM    828  N   ASN A 110      -8.785  87.697  40.702  1.00 42.96           N  
ATOM    829  CA  ASN A 110     -10.152  87.662  40.216  1.00 46.51           C  
ATOM    830  C   ASN A 110     -10.049  88.457  38.923  1.00 48.10           C  
ATOM    831  O   ASN A 110      -9.030  89.109  38.692  1.00 49.56           O  
ATOM    832  CB  ASN A 110     -11.131  88.297  41.217  1.00 46.86           C  
ATOM    833  CG  ASN A 110     -10.683  89.668  41.698  1.00 47.23           C  
ATOM    834  OD1 ASN A 110      -9.795  90.285  41.123  1.00 51.58           O  
ATOM    835  ND2 ASN A 110     -11.307  90.153  42.765  1.00 43.46           N  
ATOM    836  N   GLU A 111     -11.067  88.408  38.072  1.00 50.38           N  
ATOM    837  CA  GLU A 111     -11.008  89.136  36.805  1.00 48.87           C  
ATOM    838  C   GLU A 111     -10.575  90.600  36.889  1.00 46.94           C  
ATOM    839  O   GLU A 111      -9.959  91.119  35.955  1.00 45.23           O  
ATOM    840  CB  GLU A 111     -12.326  89.012  36.051  1.00 52.72           C  
ATOM    841  CG  GLU A 111     -12.426  87.727  35.259  1.00 58.38           C  
ATOM    842  CD  GLU A 111     -13.819  87.452  34.743  1.00 63.23           C  
ATOM    843  OE1 GLU A 111     -14.443  88.369  34.171  1.00 68.71           O  
ATOM    844  OE2 GLU A 111     -14.294  86.308  34.911  1.00 68.39           O  
ATOM    845  N   ARG A 112     -10.862  91.254  38.012  1.00 43.64           N  
ATOM    846  CA  ARG A 112     -10.486  92.656  38.197  1.00 44.42           C  
ATOM    847  C   ARG A 112      -8.969  92.833  38.357  1.00 44.01           C  
ATOM    848  O   ARG A 112      -8.359  93.681  37.699  1.00 46.07           O  
ATOM    849  CB  ARG A 112     -11.222  93.244  39.403  1.00 40.56           C  
ATOM    850  N   GLU A 113      -8.358  92.028  39.221  1.00 43.67           N  
ATOM    851  CA  GLU A 113      -6.912  92.102  39.443  1.00 43.03           C  
ATOM    852  C   GLU A 113      -6.186  91.621  38.186  1.00 36.86           C  
ATOM    853  O   GLU A 113      -5.090  92.087  37.855  1.00 33.72           O  
ATOM    854  CB  GLU A 113      -6.507  91.226  40.629  1.00 45.52           C  
ATOM    855  CG  GLU A 113      -7.143  91.598  41.964  1.00 54.27           C  
ATOM    856  CD  GLU A 113      -6.881  90.554  43.046  1.00 56.65           C  
ATOM    857  OE1 GLU A 113      -7.300  89.387  42.873  1.00 54.89           O  
ATOM    858  OE2 GLU A 113      -6.257  90.901  44.073  1.00 58.25           O  
ATOM    859  N   LEU A 114      -6.800  90.660  37.510  1.00 29.37           N  
ATOM    860  CA  LEU A 114      -6.253  90.097  36.291  1.00 32.04           C  
ATOM    861  C   LEU A 114      -6.183  91.193  35.226  1.00 34.24           C  
ATOM    862  O   LEU A 114      -5.136  91.412  34.611  1.00 36.36           O  
ATOM    863  CB  LEU A 114      -7.148  88.951  35.830  1.00 31.34           C  
ATOM    864  CG  LEU A 114      -6.572  87.920  34.869  1.00 28.40           C  
ATOM    865  CD1 LEU A 114      -5.230  87.416  35.385  1.00 30.39           C  
ATOM    866  CD2 LEU A 114      -7.550  86.779  34.745  1.00 25.76           C  
ATOM    867  N   LEU A 115      -7.292  91.906  35.053  1.00 33.53           N  
ATOM    868  CA  LEU A 115      -7.383  92.997  34.096  1.00 31.13           C  
ATOM    869  C   LEU A 115      -6.322  94.062  34.372  1.00 30.88           C  
ATOM    870  O   LEU A 115      -5.593  94.469  33.467  1.00 30.28           O  
ATOM    871  CB  LEU A 115      -8.773  93.629  34.158  1.00 34.05           C  
ATOM    872  CG  LEU A 115      -9.087  94.728  33.142  1.00 37.97           C  
ATOM    873  CD1 LEU A 115      -9.126  94.142  31.724  1.00 38.90           C  
ATOM    874  CD2 LEU A 115     -10.415  95.375  33.496  1.00 37.11           C  
ATOM    875  N   ASN A 116      -6.219  94.495  35.625  1.00 31.32           N  
ATOM    876  CA  ASN A 116      -5.237  95.504  35.988  1.00 31.21           C  
ATOM    877  C   ASN A 116      -3.826  95.101  35.577  1.00 30.42           C  
ATOM    878  O   ASN A 116      -3.115  95.876  34.936  1.00 28.98           O  
ATOM    879  CB  ASN A 116      -5.267  95.790  37.492  1.00 34.81           C  
ATOM    880  CG  ASN A 116      -4.162  96.758  37.924  1.00 43.68           C  
ATOM    881  OD1 ASN A 116      -3.466  96.523  38.907  1.00 49.08           O  
ATOM    882  ND2 ASN A 116      -3.992  97.843  37.175  1.00 41.94           N  
ATOM    883  N   SER A 117      -3.446  93.870  35.898  1.00 28.59           N  
ATOM    884  CA  SER A 117      -2.112  93.377  35.587  1.00 32.44           C  
ATOM    885  C   SER A 117      -1.795  93.386  34.093  1.00 32.16           C  
ATOM    886  O   SER A 117      -0.753  93.891  33.659  1.00 30.45           O  
ATOM    887  CB  SER A 117      -1.938  91.958  36.136  1.00 31.48           C  
ATOM    888  OG  SER A 117      -0.630  91.485  35.879  1.00 28.27           O  
ATOM    889  N   MET A 118      -2.702  92.819  33.312  1.00 30.66           N  
ATOM    890  CA  MET A 118      -2.519  92.723  31.877  1.00 31.80           C  
ATOM    891  C   MET A 118      -2.711  94.061  31.189  1.00 34.48           C  
ATOM    892  O   MET A 118      -2.201  94.289  30.094  1.00 31.38           O  
ATOM    893  CB  MET A 118      -3.450  91.659  31.316  1.00 31.50           C  
ATOM    894  CG  MET A 118      -3.178  90.294  31.914  1.00 30.42           C  
ATOM    895  SD  MET A 118      -4.304  89.076  31.289  1.00 37.82           S  
ATOM    896  CE  MET A 118      -3.594  88.788  29.775  1.00 28.77           C  
ATOM    897  N   ASN A 119      -3.425  94.961  31.850  1.00 36.39           N  
ATOM    898  CA  ASN A 119      -3.638  96.286  31.299  1.00 37.32           C  
ATOM    899  C   ASN A 119      -2.282  96.979  31.329  1.00 34.29           C  
ATOM    900  O   ASN A 119      -1.964  97.773  30.446  1.00 37.28           O  
ATOM    901  CB  ASN A 119      -4.656  97.059  32.135  1.00 42.27           C  
ATOM    902  CG  ASN A 119      -5.097  98.336  31.465  1.00 47.32           C  
ATOM    903  OD1 ASN A 119      -5.990  98.332  30.619  1.00 52.19           O  
ATOM    904  ND2 ASN A 119      -4.459  99.440  31.822  1.00 50.83           N  
ATOM    905  N   ILE A 120      -1.476  96.644  32.332  1.00 31.27           N  
ATOM    906  CA  ILE A 120      -0.143  97.212  32.472  1.00 31.70           C  
ATOM    907  C   ILE A 120       0.839  96.515  31.525  1.00 32.56           C  
ATOM    908  O   ILE A 120       1.585  97.175  30.797  1.00 31.81           O  
ATOM    909  CB  ILE A 120       0.379  97.083  33.929  1.00 29.69           C  
ATOM    910  CG1 ILE A 120      -0.483  97.917  34.872  1.00 28.96           C  
ATOM    911  CG2 ILE A 120       1.832  97.524  34.025  1.00 30.03           C  
ATOM    912  CD1 ILE A 120      -0.089  97.764  36.333  1.00 31.25           C  
ATOM    913  N   SER A 121       0.809  95.185  31.507  1.00 33.47           N  
ATOM    914  CA  SER A 121       1.719  94.420  30.657  1.00 29.60           C  
ATOM    915  C   SER A 121       1.426  94.464  29.155  1.00 30.02           C  
ATOM    916  O   SER A 121       2.328  94.243  28.360  1.00 31.41           O  
ATOM    917  CB  SER A 121       1.835  92.970  31.143  1.00 26.36           C  
ATOM    918  OG  SER A 121       0.579  92.310  31.180  1.00 31.93           O  
ATOM    919  N   GLN A 122       0.179  94.716  28.765  1.00 26.83           N  
ATOM    920  CA  GLN A 122      -0.193  94.791  27.343  1.00 30.41           C  
ATOM    921  C   GLN A 122       0.455  93.693  26.492  1.00 32.07           C  
ATOM    922  O   GLN A 122       1.244  93.980  25.588  1.00 35.00           O  
ATOM    923  CB  GLN A 122       0.192  96.160  26.765  1.00 32.46           C  
ATOM    924  CG  GLN A 122      -0.590  97.334  27.337  1.00 35.22           C  
ATOM    925  CD  GLN A 122      -2.037  97.333  26.893  1.00 35.52           C  
ATOM    926  OE1 GLN A 122      -2.337  97.083  25.726  1.00 41.62           O  
ATOM    927  NE2 GLN A 122      -2.941  97.635  27.813  1.00 32.92           N  
ATOM    928  N   PRO A 123       0.128  92.419  26.779  1.00 32.21           N  
ATOM    929  CA  PRO A 123       0.686  91.283  26.041  1.00 28.39           C  
ATOM    930  C   PRO A 123       0.011  91.041  24.701  1.00 31.72           C  
ATOM    931  O   PRO A 123      -1.201  91.209  24.554  1.00 32.52           O  
ATOM    932  CB  PRO A 123       0.411  90.123  26.987  1.00 30.26           C  
ATOM    933  CG  PRO A 123      -0.950  90.481  27.502  1.00 29.87           C  
ATOM    934  CD  PRO A 123      -0.775  91.949  27.844  1.00 31.16           C  
ATOM    935  N   THR A 124       0.797  90.602  23.731  1.00 31.99           N  
ATOM    936  CA  THR A 124       0.260  90.305  22.417  1.00 31.18           C  
ATOM    937  C   THR A 124      -0.300  88.886  22.442  1.00 30.24           C  
ATOM    938  O   THR A 124      -1.347  88.601  21.843  1.00 31.01           O  
ATOM    939  CB  THR A 124       1.366  90.384  21.353  1.00 30.80           C  
ATOM    940  OG1 THR A 124       1.932  91.702  21.345  1.00 27.14           O  
ATOM    941  CG2 THR A 124       0.824  90.031  19.993  1.00 24.12           C  
ATOM    942  N   VAL A 125       0.412  88.001  23.138  1.00 29.58           N  
ATOM    943  CA  VAL A 125       0.022  86.596  23.247  1.00 28.72           C  
ATOM    944  C   VAL A 125      -0.086  86.186  24.717  1.00 27.90           C  
ATOM    945  O   VAL A 125       0.737  86.578  25.552  1.00 23.88           O  
ATOM    946  CB  VAL A 125       1.047  85.646  22.523  1.00 28.63           C  
ATOM    947  CG1 VAL A 125       0.601  84.186  22.648  1.00 20.10           C  
ATOM    948  CG2 VAL A 125       1.196  86.020  21.056  1.00 26.85           C  
ATOM    949  N   VAL A 126      -1.103  85.390  25.020  1.00 27.52           N  
ATOM    950  CA  VAL A 126      -1.319  84.913  26.373  1.00 27.17           C  
ATOM    951  C   VAL A 126      -1.298  83.386  26.443  1.00 24.76           C  
ATOM    952  O   VAL A 126      -1.998  82.708  25.692  1.00 23.64           O  
ATOM    953  CB  VAL A 126      -2.669  85.418  26.932  1.00 24.82           C  
ATOM    954  CG1 VAL A 126      -2.884  84.907  28.358  1.00 19.94           C  
ATOM    955  CG2 VAL A 126      -2.707  86.937  26.884  1.00 23.67           C  
ATOM    956  N   PHE A 127      -0.431  82.860  27.299  1.00 24.67           N  
ATOM    957  CA  PHE A 127      -0.332  81.423  27.533  1.00 25.93           C  
ATOM    958  C   PHE A 127      -1.119  81.219  28.820  1.00 23.87           C  
ATOM    959  O   PHE A 127      -0.863  81.909  29.810  1.00 25.01           O  
ATOM    960  CB  PHE A 127       1.120  81.007  27.744  1.00 21.16           C  
ATOM    961  CG  PHE A 127       1.927  80.998  26.480  1.00 25.37           C  
ATOM    962  CD1 PHE A 127       2.606  82.139  26.061  1.00 23.39           C  
ATOM    963  CD2 PHE A 127       2.019  79.841  25.710  1.00 22.73           C  
ATOM    964  CE1 PHE A 127       3.368  82.129  24.896  1.00 26.46           C  
ATOM    965  CE2 PHE A 127       2.777  79.817  24.546  1.00 27.01           C  
ATOM    966  CZ  PHE A 127       3.456  80.966  24.136  1.00 26.07           C  
ATOM    967  N   VAL A 128      -2.089  80.316  28.811  1.00 22.20           N  
ATOM    968  CA  VAL A 128      -2.897  80.096  29.997  1.00 24.34           C  
ATOM    969  C   VAL A 128      -3.210  78.614  30.225  1.00 24.95           C  
ATOM    970  O   VAL A 128      -3.166  77.806  29.292  1.00 24.51           O  
ATOM    971  CB  VAL A 128      -4.226  80.914  29.881  1.00 22.62           C  
ATOM    972  CG1 VAL A 128      -5.141  80.300  28.829  1.00 20.44           C  
ATOM    973  CG2 VAL A 128      -4.916  81.015  31.236  1.00 21.70           C  
ATOM    974  N   SER A 129      -3.453  78.243  31.477  1.00 22.56           N  
ATOM    975  CA  SER A 129      -3.810  76.864  31.781  1.00 21.75           C  
ATOM    976  C   SER A 129      -5.308  76.769  31.495  1.00 22.45           C  
ATOM    977  O   SER A 129      -6.005  77.787  31.479  1.00 24.58           O  
ATOM    978  CB  SER A 129      -3.539  76.555  33.247  1.00 19.03           C  
ATOM    979  OG  SER A 129      -4.443  77.255  34.079  1.00 25.05           O  
ATOM    980  N   LYS A 130      -5.809  75.558  31.282  1.00 20.79           N  
ATOM    981  CA  LYS A 130      -7.222  75.356  30.990  1.00 18.98           C  
ATOM    982  C   LYS A 130      -8.149  76.066  31.975  1.00 19.70           C  
ATOM    983  O   LYS A 130      -9.119  76.687  31.564  1.00 24.98           O  
ATOM    984  CB  LYS A 130      -7.576  73.869  31.009  1.00 17.00           C  
ATOM    985  CG  LYS A 130      -6.902  73.024  29.963  1.00 15.65           C  
ATOM    986  CD  LYS A 130      -7.130  71.566  30.293  1.00 15.11           C  
ATOM    987  CE  LYS A 130      -6.663  70.665  29.195  1.00 22.62           C  
ATOM    988  NZ  LYS A 130      -6.736  69.254  29.651  1.00 29.42           N  
ATOM    989  N   LYS A 131      -7.852  75.967  33.270  1.00 21.54           N  
ATOM    990  CA  LYS A 131      -8.707  76.570  34.297  1.00 22.65           C  
ATOM    991  C   LYS A 131      -8.702  78.088  34.347  1.00 25.57           C  
ATOM    992  O   LYS A 131      -9.557  78.685  35.016  1.00 27.10           O  
ATOM    993  CB  LYS A 131      -8.420  75.977  35.685  1.00 20.98           C  
ATOM    994  CG  LYS A 131      -7.057  76.295  36.255  1.00 22.43           C  
ATOM    995  CD  LYS A 131      -6.766  75.403  37.452  1.00 23.87           C  
ATOM    996  CE  LYS A 131      -7.686  75.700  38.618  1.00 28.28           C  
ATOM    997  NZ  LYS A 131      -7.450  74.748  39.739  1.00 27.61           N  
ATOM    998  N   GLY A 132      -7.763  78.711  33.632  1.00 24.77           N  
ATOM    999  CA  GLY A 132      -7.697  80.163  33.590  1.00 21.62           C  
ATOM   1000  C   GLY A 132      -8.266  80.749  32.303  1.00 24.08           C  
ATOM   1001  O   GLY A 132      -8.346  81.969  32.159  1.00 24.20           O  
ATOM   1002  N   LEU A 133      -8.713  79.889  31.390  1.00 23.43           N  
ATOM   1003  CA  LEU A 133      -9.233  80.311  30.092  1.00 26.40           C  
ATOM   1004  C   LEU A 133     -10.395  81.303  30.124  1.00 30.12           C  
ATOM   1005  O   LEU A 133     -10.317  82.354  29.503  1.00 34.29           O  
ATOM   1006  CB  LEU A 133      -9.602  79.086  29.233  1.00 23.64           C  
ATOM   1007  CG  LEU A 133     -10.033  79.328  27.776  1.00 20.73           C  
ATOM   1008  CD1 LEU A 133      -8.980  80.123  27.027  1.00 22.76           C  
ATOM   1009  CD2 LEU A 133     -10.276  78.003  27.084  1.00 21.97           C  
ATOM   1010  N   GLN A 134     -11.466  80.976  30.845  1.00 28.50           N  
ATOM   1011  CA  GLN A 134     -12.650  81.836  30.929  1.00 26.32           C  
ATOM   1012  C   GLN A 134     -12.279  83.259  31.334  1.00 29.64           C  
ATOM   1013  O   GLN A 134     -12.642  84.228  30.660  1.00 31.42           O  
ATOM   1014  CB  GLN A 134     -13.658  81.259  31.928  1.00 26.73           C  
ATOM   1015  N   LYS A 135     -11.531  83.378  32.425  1.00 30.25           N  
ATOM   1016  CA  LYS A 135     -11.098  84.680  32.924  1.00 30.35           C  
ATOM   1017  C   LYS A 135     -10.314  85.453  31.857  1.00 30.26           C  
ATOM   1018  O   LYS A 135     -10.597  86.624  31.598  1.00 31.38           O  
ATOM   1019  CB  LYS A 135     -10.239  84.507  34.181  1.00 27.26           C  
ATOM   1020  CG  LYS A 135     -10.999  84.086  35.428  1.00 27.23           C  
ATOM   1021  CD  LYS A 135     -10.039  83.895  36.601  1.00 28.97           C  
ATOM   1022  CE  LYS A 135      -9.196  82.634  36.432  1.00 28.55           C  
ATOM   1023  NZ  LYS A 135      -8.135  82.504  37.474  1.00 25.36           N  
ATOM   1024  N   ILE A 136      -9.343  84.790  31.232  1.00 30.36           N  
ATOM   1025  CA  ILE A 136      -8.519  85.416  30.199  1.00 31.81           C  
ATOM   1026  C   ILE A 136      -9.349  85.861  28.998  1.00 34.01           C  
ATOM   1027  O   ILE A 136      -9.064  86.900  28.411  1.00 36.59           O  
ATOM   1028  CB  ILE A 136      -7.377  84.484  29.733  1.00 30.67           C  
ATOM   1029  CG1 ILE A 136      -6.381  84.256  30.876  1.00 31.31           C  
ATOM   1030  CG2 ILE A 136      -6.681  85.053  28.492  1.00 29.40           C  
ATOM   1031  CD1 ILE A 136      -5.676  85.506  31.375  1.00 24.59           C  
ATOM   1032  N   LEU A 137     -10.364  85.080  28.632  1.00 34.50           N  
ATOM   1033  CA  LEU A 137     -11.230  85.437  27.508  1.00 36.05           C  
ATOM   1034  C   LEU A 137     -11.995  86.702  27.846  1.00 38.38           C  
ATOM   1035  O   LEU A 137     -12.112  87.608  27.018  1.00 41.19           O  
ATOM   1036  CB  LEU A 137     -12.225  84.325  27.195  1.00 30.63           C  
ATOM   1037  CG  LEU A 137     -11.642  83.128  26.455  1.00 35.01           C  
ATOM   1038  CD1 LEU A 137     -12.691  82.037  26.317  1.00 25.03           C  
ATOM   1039  CD2 LEU A 137     -11.124  83.584  25.099  1.00 32.89           C  
ATOM   1040  N   ASN A 138     -12.503  86.765  29.070  1.00 36.21           N  
ATOM   1041  CA  ASN A 138     -13.247  87.932  29.513  1.00 37.75           C  
ATOM   1042  C   ASN A 138     -12.340  89.153  29.509  1.00 36.81           C  
ATOM   1043  O   ASN A 138     -12.762  90.247  29.145  1.00 40.86           O  
ATOM   1044  CB  ASN A 138     -13.855  87.689  30.891  1.00 33.73           C  
ATOM   1045  CG  ASN A 138     -14.892  86.572  30.878  1.00 35.65           C  
ATOM   1046  OD1 ASN A 138     -15.372  86.159  29.820  1.00 37.75           O  
ATOM   1047  ND2 ASN A 138     -15.232  86.070  32.055  1.00 31.91           N  
ATOM   1048  N   VAL A 139     -11.078  88.949  29.869  1.00 36.77           N  
ATOM   1049  CA  VAL A 139     -10.093  90.023  29.869  1.00 34.81           C  
ATOM   1050  C   VAL A 139      -9.755  90.442  28.432  1.00 36.40           C  
ATOM   1051  O   VAL A 139      -9.615  91.632  28.146  1.00 37.77           O  
ATOM   1052  CB  VAL A 139      -8.804  89.600  30.612  1.00 34.04           C  
ATOM   1053  CG1 VAL A 139      -7.681  90.596  30.357  1.00 39.14           C  
ATOM   1054  CG2 VAL A 139      -9.074  89.506  32.104  1.00 35.98           C  
ATOM   1055  N   GLN A 140      -9.654  89.468  27.530  1.00 37.09           N  
ATOM   1056  CA  GLN A 140      -9.345  89.743  26.127  1.00 38.11           C  
ATOM   1057  C   GLN A 140     -10.355  90.718  25.518  1.00 38.04           C  
ATOM   1058  O   GLN A 140      -9.983  91.628  24.772  1.00 38.75           O  
ATOM   1059  CB  GLN A 140      -9.316  88.452  25.315  1.00 34.84           C  
ATOM   1060  CG  GLN A 140      -9.062  88.679  23.828  1.00 39.44           C  
ATOM   1061  CD  GLN A 140      -8.917  87.394  23.052  1.00 44.28           C  
ATOM   1062  OE1 GLN A 140      -9.763  86.504  23.133  1.00 47.06           O  
ATOM   1063  NE2 GLN A 140      -7.845  87.292  22.280  1.00 40.41           N  
ATOM   1064  N   LYS A 141     -11.629  90.525  25.843  1.00 39.94           N  
ATOM   1065  CA  LYS A 141     -12.691  91.403  25.357  1.00 41.29           C  
ATOM   1066  C   LYS A 141     -12.356  92.876  25.634  1.00 39.90           C  
ATOM   1067  O   LYS A 141     -12.687  93.755  24.842  1.00 40.74           O  
ATOM   1068  CB  LYS A 141     -14.019  91.058  26.043  1.00 41.02           C  
ATOM   1069  CG  LYS A 141     -14.656  89.735  25.632  1.00 43.98           C  
ATOM   1070  CD  LYS A 141     -15.771  89.371  26.618  1.00 45.34           C  
ATOM   1071  CE  LYS A 141     -16.551  88.139  26.186  1.00 45.31           C  
ATOM   1072  NZ  LYS A 141     -17.356  87.598  27.323  1.00 45.21           N  
ATOM   1073  N   LYS A 142     -11.673  93.131  26.747  1.00 40.72           N  
ATOM   1074  CA  LYS A 142     -11.316  94.485  27.153  1.00 38.28           C  
ATOM   1075  C   LYS A 142      -9.928  94.958  26.729  1.00 40.17           C  
ATOM   1076  O   LYS A 142      -9.607  96.142  26.854  1.00 43.83           O  
ATOM   1077  CB  LYS A 142     -11.469  94.623  28.666  1.00 37.82           C  
ATOM   1078  CG  LYS A 142     -12.895  94.426  29.153  1.00 41.54           C  
ATOM   1079  CD  LYS A 142     -13.007  94.513  30.666  1.00 46.68           C  
ATOM   1080  CE  LYS A 142     -14.460  94.454  31.126  1.00 47.32           C  
ATOM   1081  NZ  LYS A 142     -15.184  93.309  30.500  1.00 52.35           N  
ATOM   1082  N   LEU A 143      -9.094  94.039  26.263  1.00 40.39           N  
ATOM   1083  CA  LEU A 143      -7.749  94.394  25.831  1.00 40.57           C  
ATOM   1084  C   LEU A 143      -7.529  93.944  24.394  1.00 41.65           C  
ATOM   1085  O   LEU A 143      -7.162  92.798  24.135  1.00 42.02           O  
ATOM   1086  CB  LEU A 143      -6.699  93.768  26.755  1.00 39.53           C  
ATOM   1087  CG  LEU A 143      -6.660  94.296  28.189  1.00 36.56           C  
ATOM   1088  CD1 LEU A 143      -5.640  93.525  29.004  1.00 32.57           C  
ATOM   1089  CD2 LEU A 143      -6.330  95.774  28.175  1.00 36.57           C  
ATOM   1090  N   PRO A 144      -7.741  94.855  23.436  1.00 42.13           N  
ATOM   1091  CA  PRO A 144      -7.571  94.551  22.012  1.00 41.93           C  
ATOM   1092  C   PRO A 144      -6.164  94.097  21.598  1.00 39.83           C  
ATOM   1093  O   PRO A 144      -5.993  93.472  20.554  1.00 41.46           O  
ATOM   1094  CB  PRO A 144      -7.984  95.859  21.332  1.00 43.66           C  
ATOM   1095  CG  PRO A 144      -7.691  96.908  22.376  1.00 44.69           C  
ATOM   1096  CD  PRO A 144      -8.187  96.246  23.627  1.00 44.52           C  
ATOM   1097  N   ILE A 145      -5.158  94.395  22.412  1.00 36.36           N  
ATOM   1098  CA  ILE A 145      -3.802  93.991  22.075  1.00 34.14           C  
ATOM   1099  C   ILE A 145      -3.595  92.474  22.132  1.00 34.21           C  
ATOM   1100  O   ILE A 145      -2.695  91.943  21.478  1.00 36.62           O  
ATOM   1101  CB  ILE A 145      -2.760  94.711  22.958  1.00 32.25           C  
ATOM   1102  CG1 ILE A 145      -1.355  94.487  22.391  1.00 33.78           C  
ATOM   1103  CG2 ILE A 145      -2.867  94.243  24.410  1.00 31.39           C  
ATOM   1104  CD1 ILE A 145      -0.288  95.376  22.988  1.00 35.21           C  
ATOM   1105  N   ILE A 146      -4.442  91.781  22.888  1.00 34.15           N  
ATOM   1106  CA  ILE A 146      -4.344  90.328  23.021  1.00 33.42           C  
ATOM   1107  C   ILE A 146      -4.896  89.679  21.763  1.00 34.00           C  
ATOM   1108  O   ILE A 146      -6.110  89.556  21.596  1.00 35.83           O  
ATOM   1109  CB  ILE A 146      -5.119  89.818  24.264  1.00 33.43           C  
ATOM   1110  CG1 ILE A 146      -4.491  90.389  25.539  1.00 29.96           C  
ATOM   1111  CG2 ILE A 146      -5.094  88.302  24.324  1.00 29.45           C  
ATOM   1112  CD1 ILE A 146      -5.276  90.088  26.788  1.00 31.93           C  
ATOM   1113  N   GLN A 147      -3.995  89.225  20.901  1.00 33.13           N  
ATOM   1114  CA  GLN A 147      -4.376  88.613  19.637  1.00 32.77           C  
ATOM   1115  C   GLN A 147      -4.455  87.101  19.637  1.00 30.56           C  
ATOM   1116  O   GLN A 147      -5.184  86.518  18.839  1.00 33.07           O  
ATOM   1117  CB  GLN A 147      -3.376  89.009  18.555  1.00 37.14           C  
ATOM   1118  CG  GLN A 147      -3.172  90.488  18.378  1.00 46.13           C  
ATOM   1119  CD  GLN A 147      -2.125  90.784  17.321  1.00 50.52           C  
ATOM   1120  OE1 GLN A 147      -1.196  90.003  17.111  1.00 51.63           O  
ATOM   1121  NE2 GLN A 147      -2.276  91.910  16.641  1.00 57.76           N  
ATOM   1122  N   LYS A 148      -3.711  86.461  20.525  1.00 29.87           N  
ATOM   1123  CA  LYS A 148      -3.653  85.010  20.532  1.00 28.13           C  
ATOM   1124  C   LYS A 148      -3.594  84.431  21.946  1.00 29.20           C  
ATOM   1125  O   LYS A 148      -2.856  84.930  22.804  1.00 24.03           O  
ATOM   1126  CB  LYS A 148      -2.407  84.608  19.715  1.00 31.14           C  
ATOM   1127  CG  LYS A 148      -2.053  83.142  19.610  1.00 26.15           C  
ATOM   1128  CD  LYS A 148      -2.911  82.412  18.614  1.00 31.39           C  
ATOM   1129  CE  LYS A 148      -2.312  81.050  18.321  1.00 31.60           C  
ATOM   1130  NZ  LYS A 148      -3.233  80.201  17.524  1.00 29.38           N  
ATOM   1131  N   ILE A 149      -4.444  83.432  22.190  1.00 27.77           N  
ATOM   1132  CA  ILE A 149      -4.505  82.720  23.468  1.00 30.72           C  
ATOM   1133  C   ILE A 149      -3.989  81.309  23.195  1.00 27.82           C  
ATOM   1134  O   ILE A 149      -4.386  80.694  22.202  1.00 25.12           O  
ATOM   1135  CB  ILE A 149      -5.963  82.582  23.993  1.00 33.75           C  
ATOM   1136  CG1 ILE A 149      -6.670  83.947  24.035  1.00 33.05           C  
ATOM   1137  CG2 ILE A 149      -5.963  81.913  25.367  1.00 30.55           C  
ATOM   1138  CD1 ILE A 149      -5.962  84.990  24.849  1.00 31.81           C  
ATOM   1139  N   ILE A 150      -3.111  80.800  24.056  1.00 26.41           N  
ATOM   1140  CA  ILE A 150      -2.544  79.459  23.885  1.00 24.45           C  
ATOM   1141  C   ILE A 150      -2.666  78.654  25.180  1.00 25.24           C  
ATOM   1142  O   ILE A 150      -2.293  79.128  26.264  1.00 20.21           O  
ATOM   1143  CB  ILE A 150      -1.055  79.525  23.443  1.00 25.84           C  
ATOM   1144  CG1 ILE A 150      -0.935  80.224  22.083  1.00 21.18           C  
ATOM   1145  CG2 ILE A 150      -0.447  78.119  23.368  1.00 20.64           C  
ATOM   1146  CD1 ILE A 150       0.471  80.612  21.722  1.00 12.35           C  
ATOM   1147  N   ILE A 151      -3.213  77.446  25.054  1.00 24.25           N  
ATOM   1148  CA  ILE A 151      -3.418  76.545  26.192  1.00 24.72           C  
ATOM   1149  C   ILE A 151      -2.137  75.799  26.557  1.00 25.17           C  
ATOM   1150  O   ILE A 151      -1.598  75.043  25.750  1.00 26.71           O  
ATOM   1151  CB  ILE A 151      -4.547  75.535  25.905  1.00 25.58           C  
ATOM   1152  CG1 ILE A 151      -5.812  76.283  25.478  1.00 20.88           C  
ATOM   1153  CG2 ILE A 151      -4.835  74.681  27.144  1.00 25.74           C  
ATOM   1154  CD1 ILE A 151      -6.267  77.300  26.491  1.00 21.59           C  
ATOM   1155  N   MET A 152      -1.692  75.977  27.797  1.00 22.58           N  
ATOM   1156  CA  MET A 152      -0.462  75.372  28.291  1.00 20.50           C  
ATOM   1157  C   MET A 152      -0.498  73.889  28.638  1.00 18.73           C  
ATOM   1158  O   MET A 152       0.385  73.129  28.251  1.00 19.00           O  
ATOM   1159  CB  MET A 152       0.028  76.154  29.509  1.00 20.23           C  
ATOM   1160  CG  MET A 152       0.466  77.556  29.184  1.00 16.60           C  
ATOM   1161  SD  MET A 152       0.626  78.562  30.671  1.00 22.29           S  
ATOM   1162  CE  MET A 152       2.065  77.857  31.420  1.00 19.86           C  
ATOM   1163  N   ASP A 153      -1.507  73.490  29.401  1.00 18.46           N  
ATOM   1164  CA  ASP A 153      -1.621  72.102  29.858  1.00 18.25           C  
ATOM   1165  C   ASP A 153      -2.503  71.206  29.002  1.00 20.67           C  
ATOM   1166  O   ASP A 153      -3.394  70.521  29.515  1.00 19.95           O  
ATOM   1167  CB  ASP A 153      -2.067  72.059  31.332  1.00 20.95           C  
ATOM   1168  CG  ASP A 153      -3.341  72.857  31.601  1.00 21.85           C  
ATOM   1169  OD1 ASP A 153      -3.708  73.738  30.792  1.00 26.27           O  
ATOM   1170  OD2 ASP A 153      -3.986  72.603  32.634  1.00 22.55           O  
ATOM   1171  N   SER A 154      -2.211  71.182  27.704  1.00 23.47           N  
ATOM   1172  CA  SER A 154      -2.946  70.372  26.740  1.00 20.80           C  
ATOM   1173  C   SER A 154      -1.992  69.985  25.612  1.00 23.20           C  
ATOM   1174  O   SER A 154      -1.017  70.685  25.354  1.00 23.35           O  
ATOM   1175  CB  SER A 154      -4.117  71.174  26.163  1.00 20.75           C  
ATOM   1176  OG  SER A 154      -4.965  70.353  25.378  1.00 22.46           O  
ATOM   1177  N   LYS A 155      -2.236  68.834  24.996  1.00 25.37           N  
ATOM   1178  CA  LYS A 155      -1.420  68.381  23.882  1.00 23.99           C  
ATOM   1179  C   LYS A 155      -2.111  68.788  22.582  1.00 25.95           C  
ATOM   1180  O   LYS A 155      -1.505  69.430  21.725  1.00 30.07           O  
ATOM   1181  CB  LYS A 155      -1.215  66.868  23.944  1.00 23.30           C  
ATOM   1182  CG  LYS A 155      -0.271  66.423  25.046  1.00 29.09           C  
ATOM   1183  CD  LYS A 155       1.100  67.064  24.868  1.00 30.73           C  
ATOM   1184  CE  LYS A 155       2.030  66.761  26.028  1.00 33.54           C  
ATOM   1185  NZ  LYS A 155       2.279  65.302  26.168  1.00 37.54           N  
ATOM   1186  N   THR A 156      -3.383  68.431  22.454  1.00 23.38           N  
ATOM   1187  CA  THR A 156      -4.172  68.771  21.282  1.00 25.56           C  
ATOM   1188  C   THR A 156      -4.812  70.133  21.529  1.00 24.91           C  
ATOM   1189  O   THR A 156      -4.626  70.731  22.590  1.00 25.94           O  
ATOM   1190  CB  THR A 156      -5.302  67.750  21.067  1.00 27.26           C  
ATOM   1191  OG1 THR A 156      -6.144  67.716  22.228  1.00 29.38           O  
ATOM   1192  CG2 THR A 156      -4.726  66.367  20.834  1.00 28.83           C  
ATOM   1193  N   ASP A 157      -5.555  70.635  20.547  1.00 26.03           N  
ATOM   1194  CA  ASP A 157      -6.246  71.912  20.715  1.00 28.47           C  
ATOM   1195  C   ASP A 157      -7.239  71.742  21.857  1.00 29.14           C  
ATOM   1196  O   ASP A 157      -7.661  70.623  22.159  1.00 30.42           O  
ATOM   1197  CB  ASP A 157      -7.007  72.305  19.444  1.00 28.76           C  
ATOM   1198  CG  ASP A 157      -6.094  72.660  18.286  1.00 33.61           C  
ATOM   1199  OD1 ASP A 157      -4.944  73.094  18.530  1.00 33.77           O  
ATOM   1200  OD2 ASP A 157      -6.532  72.516  17.127  1.00 38.06           O  
ATOM   1201  N   TYR A 158      -7.626  72.849  22.469  1.00 29.02           N  
ATOM   1202  CA  TYR A 158      -8.570  72.827  23.570  1.00 29.19           C  
ATOM   1203  C   TYR A 158      -9.592  73.952  23.418  1.00 29.08           C  
ATOM   1204  O   TYR A 158      -9.257  75.136  23.484  1.00 26.21           O  
ATOM   1205  CB  TYR A 158      -7.821  72.949  24.901  1.00 26.97           C  
ATOM   1206  CG  TYR A 158      -8.709  73.048  26.126  1.00 27.38           C  
ATOM   1207  CD1 TYR A 158      -9.254  71.907  26.718  1.00 26.35           C  
ATOM   1208  CD2 TYR A 158      -8.974  74.286  26.717  1.00 27.67           C  
ATOM   1209  CE1 TYR A 158     -10.036  71.998  27.873  1.00 26.60           C  
ATOM   1210  CE2 TYR A 158      -9.753  74.387  27.868  1.00 26.13           C  
ATOM   1211  CZ  TYR A 158     -10.278  73.241  28.445  1.00 27.63           C  
ATOM   1212  OH  TYR A 158     -11.004  73.345  29.612  1.00 26.83           O  
ATOM   1213  N   GLN A 159     -10.833  73.557  23.165  1.00 32.20           N  
ATOM   1214  CA  GLN A 159     -11.942  74.487  22.999  1.00 35.25           C  
ATOM   1215  C   GLN A 159     -11.694  75.538  21.920  1.00 33.27           C  
ATOM   1216  O   GLN A 159     -11.951  76.727  22.121  1.00 33.19           O  
ATOM   1217  CB  GLN A 159     -12.284  75.136  24.340  1.00 34.19           C  
ATOM   1218  CG  GLN A 159     -12.708  74.125  25.383  1.00 33.86           C  
ATOM   1219  CD  GLN A 159     -13.315  74.766  26.613  1.00 36.79           C  
ATOM   1220  OE1 GLN A 159     -13.524  75.978  26.661  1.00 42.24           O  
ATOM   1221  NE2 GLN A 159     -13.625  73.950  27.608  1.00 38.98           N  
ATOM   1222  N   GLY A 160     -11.183  75.084  20.778  1.00 29.86           N  
ATOM   1223  CA  GLY A 160     -10.906  75.968  19.662  1.00 30.76           C  
ATOM   1224  C   GLY A 160      -9.583  76.706  19.757  1.00 30.84           C  
ATOM   1225  O   GLY A 160      -9.200  77.406  18.826  1.00 35.41           O  
ATOM   1226  N   PHE A 161      -8.893  76.577  20.884  1.00 31.66           N  
ATOM   1227  CA  PHE A 161      -7.607  77.248  21.059  1.00 28.73           C  
ATOM   1228  C   PHE A 161      -6.462  76.271  20.879  1.00 27.71           C  
ATOM   1229  O   PHE A 161      -6.595  75.082  21.175  1.00 28.28           O  
ATOM   1230  CB  PHE A 161      -7.526  77.916  22.438  1.00 26.79           C  
ATOM   1231  CG  PHE A 161      -8.527  79.013  22.627  1.00 27.39           C  
ATOM   1232  CD1 PHE A 161      -8.236  80.314  22.224  1.00 29.09           C  
ATOM   1233  CD2 PHE A 161      -9.782  78.739  23.162  1.00 25.00           C  
ATOM   1234  CE1 PHE A 161      -9.187  81.325  22.348  1.00 29.43           C  
ATOM   1235  CE2 PHE A 161     -10.735  79.736  23.288  1.00 23.34           C  
ATOM   1236  CZ  PHE A 161     -10.438  81.031  22.881  1.00 29.45           C  
ATOM   1237  N   GLN A 162      -5.343  76.768  20.373  1.00 25.65           N  
ATOM   1238  CA  GLN A 162      -4.181  75.928  20.159  1.00 24.74           C  
ATOM   1239  C   GLN A 162      -3.457  75.696  21.464  1.00 24.94           C  
ATOM   1240  O   GLN A 162      -3.561  76.502  22.394  1.00 22.22           O  
ATOM   1241  CB  GLN A 162      -3.208  76.577  19.171  1.00 24.83           C  
ATOM   1242  CG  GLN A 162      -3.698  76.649  17.739  1.00 21.93           C  
ATOM   1243  CD  GLN A 162      -2.547  76.798  16.755  1.00 27.21           C  
ATOM   1244  OE1 GLN A 162      -1.859  77.820  16.732  1.00 23.32           O  
ATOM   1245  NE2 GLN A 162      -2.326  75.771  15.942  1.00 20.58           N  
ATOM   1246  N   SER A 163      -2.780  74.558  21.546  1.00 23.81           N  
ATOM   1247  CA  SER A 163      -1.988  74.223  22.713  1.00 23.52           C  
ATOM   1248  C   SER A 163      -0.605  74.739  22.337  1.00 24.62           C  
ATOM   1249  O   SER A 163      -0.408  75.240  21.223  1.00 24.55           O  
ATOM   1250  CB  SER A 163      -1.934  72.709  22.901  1.00 20.18           C  
ATOM   1251  OG  SER A 163      -1.231  72.096  21.837  1.00 20.42           O  
ATOM   1252  N   MET A 164       0.348  74.644  23.254  1.00 23.74           N  
ATOM   1253  CA  MET A 164       1.697  75.084  22.947  1.00 20.31           C  
ATOM   1254  C   MET A 164       2.285  74.160  21.872  1.00 20.22           C  
ATOM   1255  O   MET A 164       3.090  74.583  21.050  1.00 19.27           O  
ATOM   1256  CB  MET A 164       2.566  75.074  24.203  1.00 22.79           C  
ATOM   1257  CG  MET A 164       2.044  75.973  25.320  1.00 20.60           C  
ATOM   1258  SD  MET A 164       3.223  76.172  26.670  1.00 23.45           S  
ATOM   1259  CE  MET A 164       3.465  74.444  27.183  1.00 22.50           C  
ATOM   1260  N   TYR A 165       1.809  72.919  21.841  1.00 21.03           N  
ATOM   1261  CA  TYR A 165       2.275  71.929  20.884  1.00 20.66           C  
ATOM   1262  C   TYR A 165       1.771  72.165  19.469  1.00 21.15           C  
ATOM   1263  O   TYR A 165       2.560  72.167  18.520  1.00 26.17           O  
ATOM   1264  CB  TYR A 165       1.918  70.526  21.359  1.00 19.65           C  
ATOM   1265  CG  TYR A 165       2.730  70.121  22.551  1.00 18.71           C  
ATOM   1266  CD1 TYR A 165       2.359  70.513  23.838  1.00 20.99           C  
ATOM   1267  CD2 TYR A 165       3.908  69.393  22.394  1.00 19.12           C  
ATOM   1268  CE1 TYR A 165       3.149  70.196  24.941  1.00 21.16           C  
ATOM   1269  CE2 TYR A 165       4.704  69.069  23.488  1.00 18.89           C  
ATOM   1270  CZ  TYR A 165       4.321  69.477  24.754  1.00 21.67           C  
ATOM   1271  OH  TYR A 165       5.138  69.196  25.817  1.00 20.59           O  
ATOM   1272  N   THR A 166       0.469  72.360  19.311  1.00 20.09           N  
ATOM   1273  CA  THR A 166      -0.065  72.616  17.980  1.00 21.74           C  
ATOM   1274  C   THR A 166       0.406  73.985  17.473  1.00 25.38           C  
ATOM   1275  O   THR A 166       0.669  74.148  16.279  1.00 27.96           O  
ATOM   1276  CB  THR A 166      -1.595  72.509  17.948  1.00 17.53           C  
ATOM   1277  OG1 THR A 166      -2.164  73.395  18.913  1.00 21.36           O  
ATOM   1278  CG2 THR A 166      -2.020  71.102  18.276  1.00 19.15           C  
ATOM   1279  N   PHE A 167       0.531  74.958  18.378  1.00 26.48           N  
ATOM   1280  CA  PHE A 167       0.997  76.294  18.012  1.00 22.88           C  
ATOM   1281  C   PHE A 167       2.409  76.192  17.451  1.00 22.86           C  
ATOM   1282  O   PHE A 167       2.729  76.806  16.439  1.00 24.36           O  
ATOM   1283  CB  PHE A 167       0.985  77.238  19.222  1.00 18.65           C  
ATOM   1284  CG  PHE A 167       1.714  78.548  18.983  1.00 22.22           C  
ATOM   1285  CD1 PHE A 167       1.147  79.547  18.185  1.00 22.98           C  
ATOM   1286  CD2 PHE A 167       2.971  78.776  19.540  1.00 19.72           C  
ATOM   1287  CE1 PHE A 167       1.818  80.753  17.943  1.00 16.59           C  
ATOM   1288  CE2 PHE A 167       3.656  79.984  19.305  1.00 20.13           C  
ATOM   1289  CZ  PHE A 167       3.073  80.972  18.502  1.00 16.99           C  
ATOM   1290  N   VAL A 168       3.253  75.421  18.121  1.00 25.33           N  
ATOM   1291  CA  VAL A 168       4.630  75.237  17.686  1.00 27.07           C  
ATOM   1292  C   VAL A 168       4.645  74.648  16.264  1.00 29.36           C  
ATOM   1293  O   VAL A 168       5.256  75.219  15.349  1.00 30.11           O  
ATOM   1294  CB  VAL A 168       5.413  74.367  18.719  1.00 23.03           C  
ATOM   1295  CG1 VAL A 168       6.420  73.467  18.047  1.00 23.16           C  
ATOM   1296  CG2 VAL A 168       6.111  75.263  19.732  1.00 18.02           C  
ATOM   1297  N   THR A 169       3.877  73.584  16.064  1.00 27.07           N  
ATOM   1298  CA  THR A 169       3.775  72.921  14.767  1.00 27.20           C  
ATOM   1299  C   THR A 169       3.333  73.866  13.634  1.00 29.12           C  
ATOM   1300  O   THR A 169       3.769  73.720  12.487  1.00 29.67           O  
ATOM   1301  CB  THR A 169       2.794  71.742  14.863  1.00 25.89           C  
ATOM   1302  OG1 THR A 169       3.281  70.815  15.836  1.00 27.28           O  
ATOM   1303  CG2 THR A 169       2.648  71.046  13.536  1.00 30.98           C  
ATOM   1304  N   SER A 170       2.467  74.823  13.960  1.00 26.40           N  
ATOM   1305  CA  SER A 170       1.973  75.778  12.981  1.00 22.37           C  
ATOM   1306  C   SER A 170       3.001  76.810  12.556  1.00 25.52           C  
ATOM   1307  O   SER A 170       2.778  77.514  11.572  1.00 30.69           O  
ATOM   1308  CB  SER A 170       0.777  76.553  13.536  1.00 17.89           C  
ATOM   1309  OG  SER A 170      -0.295  75.703  13.849  1.00 29.62           O  
ATOM   1310  N   HIS A 171       4.098  76.955  13.296  1.00 24.16           N  
ATOM   1311  CA  HIS A 171       5.065  77.989  12.944  1.00 22.88           C  
ATOM   1312  C   HIS A 171       6.512  77.594  12.745  1.00 24.99           C  
ATOM   1313  O   HIS A 171       7.298  78.392  12.248  1.00 27.43           O  
ATOM   1314  CB  HIS A 171       5.004  79.124  13.959  1.00 27.09           C  
ATOM   1315  CG  HIS A 171       3.633  79.680  14.145  1.00 28.10           C  
ATOM   1316  ND1 HIS A 171       3.099  80.644  13.317  1.00 31.87           N  
ATOM   1317  CD2 HIS A 171       2.660  79.359  15.027  1.00 30.03           C  
ATOM   1318  CE1 HIS A 171       1.851  80.889  13.680  1.00 32.14           C  
ATOM   1319  NE2 HIS A 171       1.563  80.119  14.714  1.00 30.42           N  
ATOM   1320  N   LEU A 172       6.896  76.410  13.197  1.00 24.62           N  
ATOM   1321  CA  LEU A 172       8.279  75.982  13.025  1.00 26.79           C  
ATOM   1322  C   LEU A 172       8.564  75.737  11.547  1.00 28.25           C  
ATOM   1323  O   LEU A 172       7.720  75.201  10.817  1.00 31.75           O  
ATOM   1324  CB  LEU A 172       8.559  74.709  13.823  1.00 26.79           C  
ATOM   1325  CG  LEU A 172       8.625  74.796  15.351  1.00 24.36           C  
ATOM   1326  CD1 LEU A 172       8.948  73.424  15.883  1.00 20.97           C  
ATOM   1327  CD2 LEU A 172       9.683  75.793  15.795  1.00 21.19           C  
ATOM   1328  N   PRO A 173       9.744  76.167  11.072  1.00 28.04           N  
ATOM   1329  CA  PRO A 173      10.094  75.965   9.663  1.00 29.39           C  
ATOM   1330  C   PRO A 173      10.427  74.493   9.464  1.00 30.59           C  
ATOM   1331  O   PRO A 173      10.763  73.792  10.426  1.00 28.08           O  
ATOM   1332  CB  PRO A 173      11.344  76.826   9.509  1.00 27.72           C  
ATOM   1333  CG  PRO A 173      12.015  76.633  10.830  1.00 26.81           C  
ATOM   1334  CD  PRO A 173      10.850  76.809  11.798  1.00 28.60           C  
ATOM   1335  N   PRO A 174      10.283  73.985   8.230  1.00 31.61           N  
ATOM   1336  CA  PRO A 174      10.602  72.572   8.008  1.00 31.05           C  
ATOM   1337  C   PRO A 174      12.074  72.291   8.322  1.00 27.15           C  
ATOM   1338  O   PRO A 174      12.930  73.167   8.166  1.00 31.31           O  
ATOM   1339  CB  PRO A 174      10.261  72.367   6.527  1.00 29.16           C  
ATOM   1340  CG  PRO A 174      10.355  73.744   5.940  1.00 32.63           C  
ATOM   1341  CD  PRO A 174       9.760  74.612   7.005  1.00 29.97           C  
ATOM   1342  N   GLY A 175      12.342  71.109   8.857  1.00 28.06           N  
ATOM   1343  CA  GLY A 175      13.702  70.731   9.192  1.00 26.68           C  
ATOM   1344  C   GLY A 175      14.289  71.435  10.407  1.00 29.28           C  
ATOM   1345  O   GLY A 175      15.512  71.435  10.589  1.00 28.71           O  
ATOM   1346  N   PHE A 176      13.430  72.020  11.245  1.00 27.61           N  
ATOM   1347  CA  PHE A 176      13.892  72.720  12.440  1.00 23.45           C  
ATOM   1348  C   PHE A 176      14.697  71.796  13.334  1.00 23.70           C  
ATOM   1349  O   PHE A 176      14.296  70.667  13.625  1.00 21.27           O  
ATOM   1350  CB  PHE A 176      12.722  73.308  13.243  1.00 23.95           C  
ATOM   1351  CG  PHE A 176      13.159  74.073  14.468  1.00 21.69           C  
ATOM   1352  CD1 PHE A 176      13.854  75.275  14.342  1.00 20.04           C  
ATOM   1353  CD2 PHE A 176      12.934  73.560  15.744  1.00 16.88           C  
ATOM   1354  CE1 PHE A 176      14.323  75.950  15.475  1.00 22.48           C  
ATOM   1355  CE2 PHE A 176      13.400  74.229  16.882  1.00 14.66           C  
ATOM   1356  CZ  PHE A 176      14.094  75.420  16.748  1.00 17.73           C  
ATOM   1357  N   ASN A 177      15.828  72.304  13.794  1.00 22.93           N  
ATOM   1358  CA  ASN A 177      16.708  71.542  14.662  1.00 24.77           C  
ATOM   1359  C   ASN A 177      16.853  72.300  15.983  1.00 25.85           C  
ATOM   1360  O   ASN A 177      17.458  73.378  16.038  1.00 23.04           O  
ATOM   1361  CB  ASN A 177      18.071  71.358  13.995  1.00 24.33           C  
ATOM   1362  CG  ASN A 177      18.911  70.283  14.655  1.00 24.22           C  
ATOM   1363  OD1 ASN A 177      19.336  69.335  14.008  1.00 30.47           O  
ATOM   1364  ND2 ASN A 177      19.187  70.447  15.940  1.00 22.58           N  
ATOM   1365  N   GLU A 178      16.304  71.712  17.042  1.00 23.39           N  
ATOM   1366  CA  GLU A 178      16.326  72.291  18.386  1.00 24.09           C  
ATOM   1367  C   GLU A 178      17.740  72.577  18.886  1.00 23.23           C  
ATOM   1368  O   GLU A 178      17.964  73.526  19.633  1.00 21.56           O  
ATOM   1369  CB  GLU A 178      15.624  71.358  19.390  1.00 21.44           C  
ATOM   1370  CG  GLU A 178      14.165  71.042  19.079  1.00 23.06           C  
ATOM   1371  CD  GLU A 178      13.969  69.938  18.044  1.00 28.89           C  
ATOM   1372  OE1 GLU A 178      14.959  69.296  17.630  1.00 30.00           O  
ATOM   1373  OE2 GLU A 178      12.805  69.707  17.651  1.00 32.65           O  
ATOM   1374  N   TYR A 179      18.686  71.732  18.488  1.00 22.43           N  
ATOM   1375  CA  TYR A 179      20.069  71.890  18.910  1.00 19.51           C  
ATOM   1376  C   TYR A 179      20.907  72.848  18.061  1.00 22.80           C  
ATOM   1377  O   TYR A 179      21.978  73.273  18.476  1.00 23.21           O  
ATOM   1378  CB  TYR A 179      20.727  70.521  19.054  1.00 19.86           C  
ATOM   1379  CG  TYR A 179      20.108  69.731  20.184  1.00 19.30           C  
ATOM   1380  CD1 TYR A 179      18.864  69.128  20.032  1.00 21.88           C  
ATOM   1381  CD2 TYR A 179      20.722  69.663  21.436  1.00 21.57           C  
ATOM   1382  CE1 TYR A 179      18.236  68.483  21.097  1.00 21.14           C  
ATOM   1383  CE2 TYR A 179      20.104  69.017  22.513  1.00 23.36           C  
ATOM   1384  CZ  TYR A 179      18.858  68.429  22.337  1.00 25.62           C  
ATOM   1385  OH  TYR A 179      18.226  67.786  23.387  1.00 23.54           O  
ATOM   1386  N   ASP A 180      20.402  73.216  16.889  1.00 23.21           N  
ATOM   1387  CA  ASP A 180      21.110  74.156  16.021  1.00 24.73           C  
ATOM   1388  C   ASP A 180      20.624  75.574  16.332  1.00 26.52           C  
ATOM   1389  O   ASP A 180      21.265  76.563  15.965  1.00 28.36           O  
ATOM   1390  CB  ASP A 180      20.858  73.838  14.545  1.00 23.11           C  
ATOM   1391  CG  ASP A 180      21.568  72.569  14.074  1.00 26.40           C  
ATOM   1392  OD1 ASP A 180      22.495  72.082  14.758  1.00 25.33           O  
ATOM   1393  OD2 ASP A 180      21.204  72.074  12.985  1.00 26.03           O  
ATOM   1394  N   PHE A 181      19.471  75.660  16.993  1.00 27.37           N  
ATOM   1395  CA  PHE A 181      18.888  76.941  17.376  1.00 24.17           C  
ATOM   1396  C   PHE A 181      19.864  77.773  18.201  1.00 26.89           C  
ATOM   1397  O   PHE A 181      20.507  77.263  19.133  1.00 25.28           O  
ATOM   1398  CB  PHE A 181      17.602  76.716  18.181  1.00 22.78           C  
ATOM   1399  CG  PHE A 181      17.026  77.971  18.782  1.00 18.08           C  
ATOM   1400  CD1 PHE A 181      16.162  78.779  18.048  1.00 19.18           C  
ATOM   1401  CD2 PHE A 181      17.334  78.340  20.086  1.00 16.99           C  
ATOM   1402  CE1 PHE A 181      15.611  79.934  18.606  1.00 14.54           C  
ATOM   1403  CE2 PHE A 181      16.788  79.494  20.652  1.00 16.21           C  
ATOM   1404  CZ  PHE A 181      15.925  80.290  19.909  1.00 14.43           C  
ATOM   1405  N   VAL A 182      19.952  79.054  17.856  1.00 21.32           N  
ATOM   1406  CA  VAL A 182      20.814  79.997  18.553  1.00 22.43           C  
ATOM   1407  C   VAL A 182      19.906  81.090  19.109  1.00 24.91           C  
ATOM   1408  O   VAL A 182      19.141  81.708  18.366  1.00 28.67           O  
ATOM   1409  CB  VAL A 182      21.860  80.613  17.595  1.00 24.89           C  
ATOM   1410  CG1 VAL A 182      22.717  81.646  18.323  1.00 19.22           C  
ATOM   1411  CG2 VAL A 182      22.747  79.513  17.022  1.00 22.16           C  
ATOM   1412  N   PRO A 183      19.907  81.278  20.438  1.00 24.64           N  
ATOM   1413  CA  PRO A 183      19.057  82.312  21.042  1.00 27.55           C  
ATOM   1414  C   PRO A 183      19.447  83.732  20.614  1.00 25.84           C  
ATOM   1415  O   PRO A 183      20.591  83.987  20.243  1.00 22.82           O  
ATOM   1416  CB  PRO A 183      19.256  82.082  22.545  1.00 21.92           C  
ATOM   1417  CG  PRO A 183      20.665  81.560  22.626  1.00 23.29           C  
ATOM   1418  CD  PRO A 183      20.703  80.580  21.466  1.00 24.45           C  
ATOM   1419  N   GLU A 184      18.486  84.647  20.652  1.00 26.15           N  
ATOM   1420  CA  GLU A 184      18.742  86.032  20.270  1.00 29.06           C  
ATOM   1421  C   GLU A 184      19.762  86.686  21.198  1.00 29.90           C  
ATOM   1422  O   GLU A 184      19.884  86.320  22.370  1.00 32.81           O  
ATOM   1423  CB  GLU A 184      17.445  86.844  20.281  1.00 26.90           C  
ATOM   1424  CG  GLU A 184      16.430  86.421  19.231  1.00 30.85           C  
ATOM   1425  CD  GLU A 184      16.944  86.598  17.813  1.00 33.79           C  
ATOM   1426  OE1 GLU A 184      17.051  87.755  17.359  1.00 38.73           O  
ATOM   1427  OE2 GLU A 184      17.250  85.584  17.156  1.00 29.22           O  
ATOM   1428  N   SER A 185      20.524  87.620  20.648  1.00 28.88           N  
ATOM   1429  CA  SER A 185      21.518  88.355  21.406  1.00 25.02           C  
ATOM   1430  C   SER A 185      20.953  89.758  21.426  1.00 26.25           C  
ATOM   1431  O   SER A 185      20.299  90.169  20.464  1.00 27.85           O  
ATOM   1432  CB  SER A 185      22.859  88.333  20.683  1.00 30.74           C  
ATOM   1433  OG  SER A 185      23.850  89.015  21.426  1.00 36.56           O  
ATOM   1434  N   PHE A 186      21.119  90.463  22.540  1.00 27.64           N  
ATOM   1435  CA  PHE A 186      20.612  91.828  22.681  1.00 29.77           C  
ATOM   1436  C   PHE A 186      21.129  92.476  23.955  1.00 31.05           C  
ATOM   1437  O   PHE A 186      21.798  91.828  24.772  1.00 30.17           O  
ATOM   1438  CB  PHE A 186      19.069  91.873  22.635  1.00 30.89           C  
ATOM   1439  CG  PHE A 186      18.394  90.823  23.481  1.00 31.75           C  
ATOM   1440  CD1 PHE A 186      18.413  90.906  24.870  1.00 29.57           C  
ATOM   1441  CD2 PHE A 186      17.773  89.725  22.884  1.00 30.94           C  
ATOM   1442  CE1 PHE A 186      17.832  89.913  25.649  1.00 34.68           C  
ATOM   1443  CE2 PHE A 186      17.191  88.727  23.659  1.00 31.71           C  
ATOM   1444  CZ  PHE A 186      17.221  88.820  25.042  1.00 31.66           C  
ATOM   1445  N   ASP A 187      20.802  93.753  24.130  1.00 31.39           N  
ATOM   1446  CA  ASP A 187      21.237  94.516  25.292  1.00 32.94           C  
ATOM   1447  C   ASP A 187      20.491  94.025  26.534  1.00 29.01           C  
ATOM   1448  O   ASP A 187      19.284  94.222  26.668  1.00 28.27           O  
ATOM   1449  CB  ASP A 187      20.990  96.016  25.065  1.00 39.79           C  
ATOM   1450  CG  ASP A 187      21.625  96.896  26.135  1.00 42.14           C  
ATOM   1451  OD1 ASP A 187      22.870  96.901  26.255  1.00 49.83           O  
ATOM   1452  OD2 ASP A 187      20.884  97.599  26.845  1.00 45.16           O  
ATOM   1453  N   ARG A 188      21.221  93.366  27.427  1.00 29.65           N  
ATOM   1454  CA  ARG A 188      20.654  92.824  28.655  1.00 33.11           C  
ATOM   1455  C   ARG A 188      20.201  93.913  29.642  1.00 35.46           C  
ATOM   1456  O   ARG A 188      19.526  93.609  30.627  1.00 37.86           O  
ATOM   1457  CB  ARG A 188      21.674  91.903  29.335  1.00 26.79           C  
ATOM   1458  CG  ARG A 188      22.964  92.609  29.639  1.00 28.97           C  
ATOM   1459  CD  ARG A 188      23.629  92.092  30.883  1.00 28.50           C  
ATOM   1460  NE  ARG A 188      24.357  90.857  30.650  1.00 25.70           N  
ATOM   1461  CZ  ARG A 188      25.436  90.489  31.335  1.00 32.35           C  
ATOM   1462  NH1 ARG A 188      25.931  91.264  32.294  1.00 27.51           N  
ATOM   1463  NH2 ARG A 188      26.005  89.322  31.085  1.00 35.03           N  
ATOM   1464  N   ASP A 189      20.585  95.166  29.393  1.00 37.75           N  
ATOM   1465  CA  ASP A 189      20.211  96.284  30.272  1.00 32.95           C  
ATOM   1466  C   ASP A 189      18.896  96.943  29.894  1.00 28.30           C  
ATOM   1467  O   ASP A 189      18.127  97.347  30.762  1.00 33.77           O  
ATOM   1468  CB  ASP A 189      21.307  97.354  30.290  1.00 34.87           C  
ATOM   1469  CG  ASP A 189      22.609  96.853  30.874  1.00 38.13           C  
ATOM   1470  OD1 ASP A 189      22.581  95.943  31.733  1.00 41.55           O  
ATOM   1471  OD2 ASP A 189      23.669  97.380  30.475  1.00 42.37           O  
ATOM   1472  N   LYS A 190      18.653  97.075  28.598  1.00 26.96           N  
ATOM   1473  CA  LYS A 190      17.431  97.704  28.124  1.00 29.02           C  
ATOM   1474  C   LYS A 190      16.321  96.700  27.826  1.00 30.06           C  
ATOM   1475  O   LYS A 190      15.137  97.051  27.864  1.00 30.62           O  
ATOM   1476  CB  LYS A 190      17.716  98.551  26.880  1.00 32.43           C  
ATOM   1477  N   THR A 191      16.693  95.464  27.503  1.00 29.09           N  
ATOM   1478  CA  THR A 191      15.696  94.445  27.193  1.00 31.09           C  
ATOM   1479  C   THR A 191      15.106  93.844  28.472  1.00 29.95           C  
ATOM   1480  O   THR A 191      15.831  93.285  29.312  1.00 31.67           O  
ATOM   1481  CB  THR A 191      16.275  93.344  26.298  1.00 28.48           C  
ATOM   1482  OG1 THR A 191      17.039  93.946  25.248  1.00 31.43           O  
ATOM   1483  CG2 THR A 191      15.151  92.533  25.674  1.00 27.36           C  
ATOM   1484  N   ILE A 192      13.788  93.970  28.610  1.00 28.57           N  
ATOM   1485  CA  ILE A 192      13.074  93.476  29.776  1.00 30.05           C  
ATOM   1486  C   ILE A 192      12.823  91.980  29.697  1.00 28.03           C  
ATOM   1487  O   ILE A 192      12.352  91.462  28.684  1.00 29.99           O  
ATOM   1488  CB  ILE A 192      11.730  94.217  29.980  1.00 30.84           C  
ATOM   1489  CG1 ILE A 192      11.979  95.722  30.132  1.00 31.88           C  
ATOM   1490  CG2 ILE A 192      11.024  93.703  31.227  1.00 30.04           C  
ATOM   1491  CD1 ILE A 192      12.948  96.081  31.254  1.00 30.46           C  
ATOM   1492  N   ALA A 193      13.185  91.298  30.776  1.00 27.64           N  
ATOM   1493  CA  ALA A 193      13.020  89.856  30.898  1.00 23.95           C  
ATOM   1494  C   ALA A 193      11.667  89.545  31.517  1.00 22.89           C  
ATOM   1495  O   ALA A 193      10.849  88.827  30.929  1.00 19.94           O  
ATOM   1496  CB  ALA A 193      14.134  89.290  31.767  1.00 16.72           C  
ATOM   1497  N   LEU A 194      11.433  90.121  32.693  1.00 23.63           N  
ATOM   1498  CA  LEU A 194      10.201  89.906  33.437  1.00 25.31           C  
ATOM   1499  C   LEU A 194       9.503  91.182  33.835  1.00 21.79           C  
ATOM   1500  O   LEU A 194      10.147  92.182  34.138  1.00 24.68           O  
ATOM   1501  CB  LEU A 194      10.483  89.135  34.741  1.00 20.32           C  
ATOM   1502  CG  LEU A 194      10.696  87.622  34.790  1.00 18.84           C  
ATOM   1503  CD1 LEU A 194       9.531  86.935  34.105  1.00 21.14           C  
ATOM   1504  CD2 LEU A 194      12.014  87.239  34.145  1.00 21.14           C  
ATOM   1505  N   ILE A 195       8.178  91.141  33.808  1.00 22.79           N  
ATOM   1506  CA  ILE A 195       7.354  92.244  34.278  1.00 24.23           C  
ATOM   1507  C   ILE A 195       6.510  91.574  35.368  1.00 23.96           C  
ATOM   1508  O   ILE A 195       5.558  90.844  35.066  1.00 20.42           O  
ATOM   1509  CB  ILE A 195       6.465  92.854  33.181  1.00 26.60           C  
ATOM   1510  CG1 ILE A 195       7.338  93.539  32.119  1.00 23.60           C  
ATOM   1511  CG2 ILE A 195       5.508  93.885  33.800  1.00 16.08           C  
ATOM   1512  CD1 ILE A 195       6.591  93.951  30.863  1.00 27.56           C  
ATOM   1513  N   MET A 196       6.939  91.746  36.621  1.00 21.07           N  
ATOM   1514  CA  MET A 196       6.288  91.149  37.782  1.00 25.88           C  
ATOM   1515  C   MET A 196       5.306  92.111  38.442  1.00 28.52           C  
ATOM   1516  O   MET A 196       5.491  93.317  38.358  1.00 30.94           O  
ATOM   1517  CB  MET A 196       7.351  90.767  38.815  1.00 25.01           C  
ATOM   1518  CG  MET A 196       8.552  90.002  38.281  1.00 26.61           C  
ATOM   1519  SD  MET A 196       8.134  88.397  37.600  1.00 23.92           S  
ATOM   1520  CE  MET A 196       7.693  87.502  39.071  1.00 22.63           C  
ATOM   1521  N   ASN A 197       4.287  91.586  39.126  1.00 32.37           N  
ATOM   1522  CA  ASN A 197       3.311  92.436  39.832  1.00 32.62           C  
ATOM   1523  C   ASN A 197       3.697  92.659  41.287  1.00 33.78           C  
ATOM   1524  O   ASN A 197       4.055  91.716  41.994  1.00 30.02           O  
ATOM   1525  CB  ASN A 197       1.897  91.859  39.759  1.00 27.07           C  
ATOM   1526  CG  ASN A 197       1.281  91.999  38.379  1.00 33.75           C  
ATOM   1527  OD1 ASN A 197       0.977  91.007  37.725  1.00 36.89           O  
ATOM   1528  ND2 ASN A 197       1.109  93.234  37.924  1.00 33.99           N  
ATOM   1529  N   SER A 198       3.649  93.914  41.724  1.00 40.05           N  
ATOM   1530  CA  SER A 198       3.989  94.262  43.103  1.00 46.12           C  
ATOM   1531  C   SER A 198       2.847  93.871  44.045  1.00 49.53           C  
ATOM   1532  O   SER A 198       1.670  94.043  43.717  1.00 51.84           O  
ATOM   1533  CB  SER A 198       4.261  95.759  43.227  1.00 43.88           C  
ATOM   1534  OG  SER A 198       3.105  96.508  42.892  1.00 41.76           O  
ATOM   1535  N   SER A 201       1.566  96.979  48.194  1.00 86.84           N  
ATOM   1536  CA  SER A 201       1.397  98.135  49.067  1.00 85.76           C  
ATOM   1537  C   SER A 201       0.004  98.780  48.938  1.00 85.35           C  
ATOM   1538  O   SER A 201      -1.014  98.084  48.960  1.00 85.67           O  
ATOM   1539  CB  SER A 201       2.511  99.157  48.801  1.00 85.08           C  
ATOM   1540  OG  SER A 201       2.623  99.458  47.415  1.00 85.93           O  
ATOM   1541  N   THR A 202      -0.041 100.104  48.813  1.00 83.69           N  
ATOM   1542  CA  THR A 202      -1.296 100.842  48.696  1.00 81.88           C  
ATOM   1543  C   THR A 202      -1.658 101.078  47.222  1.00 79.46           C  
ATOM   1544  O   THR A 202      -0.773 101.203  46.368  1.00 82.07           O  
ATOM   1545  CB  THR A 202      -1.174 102.210  49.417  1.00 83.23           C  
ATOM   1546  OG1 THR A 202      -0.511 102.034  50.676  1.00 85.73           O  
ATOM   1547  CG2 THR A 202      -2.542 102.808  49.682  1.00 81.95           C  
ATOM   1548  N   GLY A 203      -2.954 101.172  46.934  1.00 73.21           N  
ATOM   1549  CA  GLY A 203      -3.394 101.399  45.567  1.00 67.58           C  
ATOM   1550  C   GLY A 203      -3.476 100.102  44.785  1.00 65.40           C  
ATOM   1551  O   GLY A 203      -3.639  99.032  45.373  1.00 65.53           O  
ATOM   1552  N   LEU A 204      -3.412 100.194  43.460  1.00 62.26           N  
ATOM   1553  CA  LEU A 204      -3.471  99.003  42.618  1.00 59.64           C  
ATOM   1554  C   LEU A 204      -2.068  98.470  42.361  1.00 56.88           C  
ATOM   1555  O   LEU A 204      -1.093  99.227  42.434  1.00 56.84           O  
ATOM   1556  CB  LEU A 204      -4.161  99.305  41.282  1.00 60.00           C  
ATOM   1557  CG  LEU A 204      -5.693  99.291  41.259  1.00 62.37           C  
ATOM   1558  CD1 LEU A 204      -6.190  99.568  39.851  1.00 61.34           C  
ATOM   1559  CD2 LEU A 204      -6.208  97.944  41.738  1.00 63.69           C  
ATOM   1560  N   PRO A 205      -1.934  97.150  42.136  1.00 54.05           N  
ATOM   1561  CA  PRO A 205      -0.615  96.567  41.876  1.00 50.84           C  
ATOM   1562  C   PRO A 205       0.026  97.130  40.604  1.00 45.63           C  
ATOM   1563  O   PRO A 205      -0.658  97.418  39.618  1.00 42.36           O  
ATOM   1564  CB  PRO A 205      -0.902  95.060  41.782  1.00 51.79           C  
ATOM   1565  CG  PRO A 205      -2.365  94.979  41.470  1.00 53.24           C  
ATOM   1566  CD  PRO A 205      -2.951  96.090  42.288  1.00 52.76           C  
ATOM   1567  N   LYS A 206       1.339  97.319  40.660  1.00 41.14           N  
ATOM   1568  CA  LYS A 206       2.100  97.861  39.544  1.00 38.16           C  
ATOM   1569  C   LYS A 206       2.903  96.786  38.809  1.00 36.50           C  
ATOM   1570  O   LYS A 206       2.973  95.636  39.252  1.00 33.54           O  
ATOM   1571  CB  LYS A 206       3.044  98.957  40.044  1.00 35.04           C  
ATOM   1572  CG  LYS A 206       2.374  99.988  40.930  1.00 36.43           C  
ATOM   1573  CD  LYS A 206       3.299 101.166  41.184  1.00 40.20           C  
ATOM   1574  CE  LYS A 206       2.877 101.981  42.397  1.00 41.16           C  
ATOM   1575  NZ  LYS A 206       3.042 101.222  43.677  1.00 43.08           N  
ATOM   1576  N   GLY A 207       3.470  97.166  37.666  1.00 36.26           N  
ATOM   1577  CA  GLY A 207       4.281  96.262  36.870  1.00 30.73           C  
ATOM   1578  C   GLY A 207       5.742  96.619  37.063  1.00 28.19           C  
ATOM   1579  O   GLY A 207       6.158  97.749  36.817  1.00 32.54           O  
ATOM   1580  N   VAL A 208       6.519  95.667  37.545  1.00 23.83           N  
ATOM   1581  CA  VAL A 208       7.933  95.876  37.793  1.00 26.81           C  
ATOM   1582  C   VAL A 208       8.748  95.329  36.623  1.00 30.53           C  
ATOM   1583  O   VAL A 208       8.777  94.114  36.383  1.00 29.84           O  
ATOM   1584  CB  VAL A 208       8.355  95.185  39.109  1.00 21.73           C  
ATOM   1585  CG1 VAL A 208       9.845  95.291  39.309  1.00 22.86           C  
ATOM   1586  CG2 VAL A 208       7.602  95.798  40.285  1.00 22.10           C  
ATOM   1587  N   ALA A 209       9.361  96.236  35.868  1.00 29.42           N  
ATOM   1588  CA  ALA A 209      10.176  95.859  34.721  1.00 27.00           C  
ATOM   1589  C   ALA A 209      11.558  95.455  35.202  1.00 29.68           C  
ATOM   1590  O   ALA A 209      12.256  96.240  35.851  1.00 32.50           O  
ATOM   1591  CB  ALA A 209      10.271  97.011  33.747  1.00 24.57           C  
ATOM   1592  N   LEU A 210      11.934  94.213  34.918  1.00 29.04           N  
ATOM   1593  CA  LEU A 210      13.233  93.686  35.322  1.00 29.98           C  
ATOM   1594  C   LEU A 210      14.038  93.304  34.082  1.00 33.69           C  
ATOM   1595  O   LEU A 210      13.655  92.387  33.344  1.00 33.40           O  
ATOM   1596  CB  LEU A 210      13.055  92.451  36.215  1.00 24.45           C  
ATOM   1597  CG  LEU A 210      12.247  92.606  37.507  1.00 23.04           C  
ATOM   1598  CD1 LEU A 210      12.141  91.272  38.217  1.00 13.83           C  
ATOM   1599  CD2 LEU A 210      12.908  93.640  38.408  1.00 22.74           C  
ATOM   1600  N   PRO A 211      15.126  94.045  33.797  1.00 34.52           N  
ATOM   1601  CA  PRO A 211      15.994  93.789  32.641  1.00 29.55           C  
ATOM   1602  C   PRO A 211      16.671  92.428  32.773  1.00 27.90           C  
ATOM   1603  O   PRO A 211      16.849  91.922  33.888  1.00 22.57           O  
ATOM   1604  CB  PRO A 211      17.030  94.909  32.744  1.00 29.68           C  
ATOM   1605  CG  PRO A 211      16.273  96.013  33.407  1.00 29.17           C  
ATOM   1606  CD  PRO A 211      15.548  95.274  34.494  1.00 32.02           C  
ATOM   1607  N   HIS A 212      17.080  91.862  31.638  1.00 25.44           N  
ATOM   1608  CA  HIS A 212      17.754  90.563  31.622  1.00 23.69           C  
ATOM   1609  C   HIS A 212      18.944  90.528  32.566  1.00 24.09           C  
ATOM   1610  O   HIS A 212      19.290  89.473  33.107  1.00 28.45           O  
ATOM   1611  CB  HIS A 212      18.211  90.196  30.204  1.00 24.03           C  
ATOM   1612  CG  HIS A 212      17.124  89.637  29.339  1.00 16.97           C  
ATOM   1613  ND1 HIS A 212      17.085  88.312  28.959  1.00 19.72           N  
ATOM   1614  CD2 HIS A 212      16.039  90.220  28.779  1.00 19.11           C  
ATOM   1615  CE1 HIS A 212      16.021  88.103  28.200  1.00 14.61           C  
ATOM   1616  NE2 HIS A 212      15.375  89.246  28.074  1.00 18.78           N  
ATOM   1617  N   ARG A 213      19.571  91.681  32.755  1.00 23.88           N  
ATOM   1618  CA  ARG A 213      20.728  91.808  33.623  1.00 23.76           C  
ATOM   1619  C   ARG A 213      20.453  91.348  35.055  1.00 22.57           C  
ATOM   1620  O   ARG A 213      21.302  90.705  35.681  1.00 26.84           O  
ATOM   1621  CB  ARG A 213      21.207  93.263  33.633  1.00 27.56           C  
ATOM   1622  CG  ARG A 213      22.434  93.524  34.510  1.00 32.71           C  
ATOM   1623  CD  ARG A 213      22.587  95.012  34.816  1.00 36.44           C  
ATOM   1624  NE  ARG A 213      21.484  95.530  35.629  1.00 34.85           N  
ATOM   1625  CZ  ARG A 213      20.559  96.388  35.204  1.00 32.88           C  
ATOM   1626  NH1 ARG A 213      20.591  96.846  33.957  1.00 36.29           N  
ATOM   1627  NH2 ARG A 213      19.596  96.785  36.026  1.00 31.78           N  
ATOM   1628  N   THR A 214      19.269  91.661  35.576  1.00 24.11           N  
ATOM   1629  CA  THR A 214      18.934  91.289  36.956  1.00 25.72           C  
ATOM   1630  C   THR A 214      18.903  89.765  37.130  1.00 24.47           C  
ATOM   1631  O   THR A 214      19.373  89.223  38.138  1.00 22.93           O  
ATOM   1632  CB  THR A 214      17.614  91.947  37.421  1.00 23.45           C  
ATOM   1633  OG1 THR A 214      16.498  91.298  36.809  1.00 24.25           O  
ATOM   1634  CG2 THR A 214      17.601  93.430  37.047  1.00 20.78           C  
ATOM   1635  N   ALA A 215      18.384  89.076  36.120  1.00 22.13           N  
ATOM   1636  CA  ALA A 215      18.345  87.623  36.143  1.00 21.08           C  
ATOM   1637  C   ALA A 215      19.782  87.108  36.068  1.00 23.20           C  
ATOM   1638  O   ALA A 215      20.174  86.210  36.827  1.00 21.95           O  
ATOM   1639  CB  ALA A 215      17.538  87.107  34.968  1.00 21.10           C  
ATOM   1640  N   CYS A 216      20.584  87.713  35.193  1.00 21.00           N  
ATOM   1641  CA  CYS A 216      21.979  87.309  35.041  1.00 23.36           C  
ATOM   1642  C   CYS A 216      22.722  87.418  36.371  1.00 22.46           C  
ATOM   1643  O   CYS A 216      23.490  86.528  36.731  1.00 22.96           O  
ATOM   1644  CB  CYS A 216      22.677  88.129  33.954  1.00 18.84           C  
ATOM   1645  SG  CYS A 216      21.951  87.942  32.304  1.00 23.12           S  
ATOM   1646  N   VAL A 217      22.472  88.492  37.116  1.00 25.78           N  
ATOM   1647  CA  VAL A 217      23.101  88.682  38.425  1.00 25.31           C  
ATOM   1648  C   VAL A 217      22.555  87.621  39.387  1.00 27.15           C  
ATOM   1649  O   VAL A 217      23.296  87.050  40.198  1.00 27.51           O  
ATOM   1650  CB  VAL A 217      22.819  90.096  38.980  1.00 26.15           C  
ATOM   1651  CG1 VAL A 217      23.367  90.240  40.388  1.00 21.79           C  
ATOM   1652  CG2 VAL A 217      23.431  91.148  38.059  1.00 24.68           C  
ATOM   1653  N   ARG A 218      21.262  87.338  39.267  1.00 25.51           N  
ATOM   1654  CA  ARG A 218      20.619  86.334  40.105  1.00 27.98           C  
ATOM   1655  C   ARG A 218      21.243  84.948  39.899  1.00 26.85           C  
ATOM   1656  O   ARG A 218      21.416  84.187  40.860  1.00 26.85           O  
ATOM   1657  CB  ARG A 218      19.114  86.302  39.814  1.00 25.78           C  
ATOM   1658  CG  ARG A 218      18.368  85.118  40.410  1.00 26.65           C  
ATOM   1659  CD  ARG A 218      18.441  85.089  41.929  1.00 21.50           C  
ATOM   1660  NE  ARG A 218      18.127  83.759  42.438  1.00 21.49           N  
ATOM   1661  CZ  ARG A 218      18.302  83.374  43.694  1.00 19.64           C  
ATOM   1662  NH1 ARG A 218      18.782  84.221  44.592  1.00 21.16           N  
ATOM   1663  NH2 ARG A 218      18.061  82.119  44.038  1.00 22.39           N  
ATOM   1664  N   PHE A 219      21.632  84.644  38.664  1.00 24.82           N  
ATOM   1665  CA  PHE A 219      22.236  83.350  38.354  1.00 22.83           C  
ATOM   1666  C   PHE A 219      23.562  83.147  39.074  1.00 25.48           C  
ATOM   1667  O   PHE A 219      23.981  82.008  39.316  1.00 22.26           O  
ATOM   1668  CB  PHE A 219      22.409  83.173  36.848  1.00 17.74           C  
ATOM   1669  CG  PHE A 219      21.113  83.170  36.086  1.00 21.50           C  
ATOM   1670  CD1 PHE A 219      19.904  82.932  36.739  1.00 20.42           C  
ATOM   1671  CD2 PHE A 219      21.094  83.435  34.717  1.00 18.75           C  
ATOM   1672  CE1 PHE A 219      18.696  82.959  36.046  1.00 20.52           C  
ATOM   1673  CE2 PHE A 219      19.889  83.466  34.016  1.00 19.52           C  
ATOM   1674  CZ  PHE A 219      18.687  83.228  34.681  1.00 21.28           C  
ATOM   1675  N   SER A 220      24.229  84.252  39.403  1.00 24.33           N  
ATOM   1676  CA  SER A 220      25.489  84.190  40.129  1.00 24.61           C  
ATOM   1677  C   SER A 220      25.173  83.778  41.571  1.00 30.03           C  
ATOM   1678  O   SER A 220      25.819  82.874  42.126  1.00 27.99           O  
ATOM   1679  CB  SER A 220      26.189  85.552  40.110  1.00 26.02           C  
ATOM   1680  OG  SER A 220      27.338  85.532  40.939  1.00 30.45           O  
ATOM   1681  N   HIS A 221      24.149  84.426  42.144  1.00 28.66           N  
ATOM   1682  CA  HIS A 221      23.699  84.164  43.512  1.00 26.18           C  
ATOM   1683  C   HIS A 221      23.252  82.714  43.678  1.00 25.78           C  
ATOM   1684  O   HIS A 221      23.588  82.064  44.679  1.00 23.25           O  
ATOM   1685  CB  HIS A 221      22.515  85.079  43.890  1.00 24.51           C  
ATOM   1686  CG  HIS A 221      22.855  86.534  44.000  1.00 29.70           C  
ATOM   1687  ND1 HIS A 221      21.908  87.527  43.881  1.00 24.35           N  
ATOM   1688  CD2 HIS A 221      24.035  87.166  44.212  1.00 27.61           C  
ATOM   1689  CE1 HIS A 221      22.487  88.706  44.015  1.00 29.30           C  
ATOM   1690  NE2 HIS A 221      23.779  88.513  44.212  1.00 25.90           N  
ATOM   1691  N   ALA A 222      22.505  82.219  42.689  1.00 24.70           N  
ATOM   1692  CA  ALA A 222      21.949  80.861  42.696  1.00 24.45           C  
ATOM   1693  C   ALA A 222      22.955  79.747  42.953  1.00 26.35           C  
ATOM   1694  O   ALA A 222      22.667  78.806  43.697  1.00 25.55           O  
ATOM   1695  CB  ALA A 222      21.202  80.593  41.389  1.00 26.37           C  
ATOM   1696  N   ARG A 223      24.145  79.870  42.369  1.00 27.30           N  
ATOM   1697  CA  ARG A 223      25.183  78.844  42.518  1.00 29.21           C  
ATOM   1698  C   ARG A 223      26.287  79.203  43.510  1.00 28.18           C  
ATOM   1699  O   ARG A 223      27.309  78.520  43.598  1.00 30.00           O  
ATOM   1700  CB  ARG A 223      25.779  78.510  41.149  1.00 34.60           C  
ATOM   1701  CG  ARG A 223      26.308  79.715  40.410  1.00 40.89           C  
ATOM   1702  CD  ARG A 223      26.421  79.430  38.928  1.00 49.26           C  
ATOM   1703  NE  ARG A 223      27.350  78.335  38.642  1.00 54.76           N  
ATOM   1704  CZ  ARG A 223      27.566  77.842  37.426  1.00 55.26           C  
ATOM   1705  NH1 ARG A 223      26.926  78.341  36.377  1.00 55.54           N  
ATOM   1706  NH2 ARG A 223      28.424  76.848  37.262  1.00 54.53           N  
ATOM   1707  N   ASP A 224      26.078  80.280  44.256  1.00 30.57           N  
ATOM   1708  CA  ASP A 224      27.047  80.724  45.247  1.00 28.40           C  
ATOM   1709  C   ASP A 224      26.926  79.804  46.463  1.00 30.79           C  
ATOM   1710  O   ASP A 224      25.852  79.655  47.038  1.00 31.10           O  
ATOM   1711  CB  ASP A 224      26.754  82.176  45.643  1.00 32.85           C  
ATOM   1712  CG  ASP A 224      27.928  82.849  46.344  1.00 34.79           C  
ATOM   1713  OD1 ASP A 224      28.240  82.474  47.493  1.00 35.02           O  
ATOM   1714  OD2 ASP A 224      28.520  83.777  45.754  1.00 33.19           O  
ATOM   1715  N   PRO A 225      28.046  79.192  46.880  1.00 30.38           N  
ATOM   1716  CA  PRO A 225      28.113  78.278  48.025  1.00 29.08           C  
ATOM   1717  C   PRO A 225      27.669  78.935  49.326  1.00 29.82           C  
ATOM   1718  O   PRO A 225      27.251  78.253  50.263  1.00 29.13           O  
ATOM   1719  CB  PRO A 225      29.600  77.934  48.084  1.00 28.33           C  
ATOM   1720  CG  PRO A 225      30.038  78.071  46.666  1.00 24.54           C  
ATOM   1721  CD  PRO A 225      29.362  79.326  46.243  1.00 30.47           C  
ATOM   1722  N   ILE A 226      27.796  80.258  49.382  1.00 30.26           N  
ATOM   1723  CA  ILE A 226      27.433  81.018  50.566  1.00 30.18           C  
ATOM   1724  C   ILE A 226      26.048  81.646  50.482  1.00 30.12           C  
ATOM   1725  O   ILE A 226      25.288  81.592  51.446  1.00 34.60           O  
ATOM   1726  CB  ILE A 226      28.479  82.144  50.872  1.00 29.26           C  
ATOM   1727  CG1 ILE A 226      29.889  81.558  50.962  1.00 23.11           C  
ATOM   1728  CG2 ILE A 226      28.149  82.833  52.200  1.00 26.15           C  
ATOM   1729  CD1 ILE A 226      30.055  80.515  52.050  1.00 30.60           C  
ATOM   1730  N   PHE A 227      25.715  82.238  49.340  1.00 31.60           N  
ATOM   1731  CA  PHE A 227      24.419  82.903  49.179  1.00 33.03           C  
ATOM   1732  C   PHE A 227      23.356  82.165  48.372  1.00 29.62           C  
ATOM   1733  O   PHE A 227      22.249  82.680  48.199  1.00 32.36           O  
ATOM   1734  CB  PHE A 227      24.619  84.313  48.609  1.00 31.68           C  
ATOM   1735  CG  PHE A 227      25.386  85.229  49.523  1.00 39.37           C  
ATOM   1736  CD1 PHE A 227      26.772  85.123  49.634  1.00 38.44           C  
ATOM   1737  CD2 PHE A 227      24.720  86.180  50.297  1.00 38.00           C  
ATOM   1738  CE1 PHE A 227      27.484  85.952  50.509  1.00 40.14           C  
ATOM   1739  CE2 PHE A 227      25.422  87.009  51.169  1.00 38.01           C  
ATOM   1740  CZ  PHE A 227      26.805  86.895  51.276  1.00 39.07           C  
ATOM   1741  N   GLY A 228      23.689  80.978  47.879  1.00 24.99           N  
ATOM   1742  CA  GLY A 228      22.744  80.199  47.096  1.00 24.96           C  
ATOM   1743  C   GLY A 228      22.904  78.717  47.365  1.00 26.36           C  
ATOM   1744  O   GLY A 228      22.849  78.289  48.521  1.00 27.31           O  
ATOM   1745  N   ASN A 229      23.106  77.929  46.313  1.00 24.97           N  
ATOM   1746  CA  ASN A 229      23.289  76.489  46.459  1.00 27.43           C  
ATOM   1747  C   ASN A 229      24.511  76.013  45.716  1.00 30.37           C  
ATOM   1748  O   ASN A 229      24.761  76.425  44.583  1.00 38.30           O  
ATOM   1749  CB  ASN A 229      22.097  75.707  45.891  1.00 28.34           C  
ATOM   1750  CG  ASN A 229      20.823  75.921  46.652  1.00 29.60           C  
ATOM   1751  OD1 ASN A 229      19.847  76.428  46.109  1.00 29.18           O  
ATOM   1752  ND2 ASN A 229      20.810  75.514  47.910  1.00 30.18           N  
ATOM   1753  N   GLN A 230      25.272  75.132  46.341  1.00 28.25           N  
ATOM   1754  CA  GLN A 230      26.428  74.557  45.677  1.00 33.30           C  
ATOM   1755  C   GLN A 230      25.876  73.639  44.593  1.00 33.03           C  
ATOM   1756  O   GLN A 230      24.941  72.874  44.846  1.00 31.87           O  
ATOM   1757  CB  GLN A 230      27.238  73.692  46.643  1.00 36.44           C  
ATOM   1758  CG  GLN A 230      27.864  74.428  47.804  1.00 46.21           C  
ATOM   1759  CD  GLN A 230      28.635  73.486  48.705  1.00 49.38           C  
ATOM   1760  OE1 GLN A 230      28.856  72.322  48.371  1.00 55.09           O  
ATOM   1761  NE2 GLN A 230      29.022  73.975  49.866  1.00 57.30           N  
ATOM   1762  N   ILE A 231      26.427  73.711  43.390  1.00 31.71           N  
ATOM   1763  CA  ILE A 231      25.967  72.831  42.331  1.00 26.99           C  
ATOM   1764  C   ILE A 231      26.535  71.439  42.565  1.00 28.59           C  
ATOM   1765  O   ILE A 231      27.671  71.147  42.225  1.00 30.61           O  
ATOM   1766  CB  ILE A 231      26.351  73.344  40.935  1.00 27.30           C  
ATOM   1767  CG1 ILE A 231      25.747  74.735  40.711  1.00 22.68           C  
ATOM   1768  CG2 ILE A 231      25.876  72.361  39.868  1.00 26.46           C  
ATOM   1769  CD1 ILE A 231      25.972  75.283  39.326  1.00 22.32           C  
ATOM   1770  N   ILE A 232      25.744  70.613  43.233  1.00 30.77           N  
ATOM   1771  CA  ILE A 232      26.113  69.243  43.542  1.00 29.37           C  
ATOM   1772  C   ILE A 232      25.157  68.376  42.748  1.00 32.75           C  
ATOM   1773  O   ILE A 232      24.006  68.759  42.514  1.00 33.25           O  
ATOM   1774  CB  ILE A 232      25.930  68.964  45.051  1.00 30.05           C  
ATOM   1775  CG1 ILE A 232      26.926  69.801  45.861  1.00 34.47           C  
ATOM   1776  CG2 ILE A 232      26.068  67.484  45.351  1.00 25.72           C  
ATOM   1777  CD1 ILE A 232      26.638  69.822  47.357  1.00 38.31           C  
ATOM   1778  N   PRO A 233      25.639  67.243  42.237  1.00 34.48           N  
ATOM   1779  CA  PRO A 233      24.784  66.347  41.459  1.00 33.51           C  
ATOM   1780  C   PRO A 233      23.652  65.752  42.304  1.00 33.11           C  
ATOM   1781  O   PRO A 233      23.818  65.496  43.502  1.00 31.65           O  
ATOM   1782  CB  PRO A 233      25.758  65.267  40.990  1.00 36.64           C  
ATOM   1783  CG  PRO A 233      27.058  66.021  40.874  1.00 36.47           C  
ATOM   1784  CD  PRO A 233      27.054  66.833  42.143  1.00 36.01           C  
ATOM   1785  N   ASP A 234      22.508  65.559  41.659  1.00 29.39           N  
ATOM   1786  CA  ASP A 234      21.315  64.993  42.273  1.00 29.60           C  
ATOM   1787  C   ASP A 234      20.641  65.866  43.326  1.00 30.80           C  
ATOM   1788  O   ASP A 234      19.943  65.365  44.212  1.00 32.59           O  
ATOM   1789  CB  ASP A 234      21.597  63.591  42.814  1.00 28.40           C  
ATOM   1790  CG  ASP A 234      21.999  62.621  41.721  1.00 37.96           C  
ATOM   1791  OD1 ASP A 234      21.404  62.663  40.619  1.00 43.36           O  
ATOM   1792  OD2 ASP A 234      22.927  61.819  41.956  1.00 45.73           O  
ATOM   1793  N   THR A 235      20.795  67.179  43.181  1.00 28.77           N  
ATOM   1794  CA  THR A 235      20.177  68.128  44.098  1.00 25.46           C  
ATOM   1795  C   THR A 235      18.701  68.331  43.728  1.00 23.66           C  
ATOM   1796  O   THR A 235      18.381  68.672  42.586  1.00 25.01           O  
ATOM   1797  CB  THR A 235      20.928  69.481  44.084  1.00 21.78           C  
ATOM   1798  OG1 THR A 235      22.268  69.278  44.537  1.00 22.21           O  
ATOM   1799  CG2 THR A 235      20.250  70.487  44.988  1.00 18.26           C  
ATOM   1800  N   ALA A 236      17.810  68.091  44.688  1.00 19.73           N  
ATOM   1801  CA  ALA A 236      16.374  68.250  44.483  1.00 19.14           C  
ATOM   1802  C   ALA A 236      15.817  69.275  45.466  1.00 18.44           C  
ATOM   1803  O   ALA A 236      16.187  69.290  46.650  1.00 15.85           O  
ATOM   1804  CB  ALA A 236      15.648  66.906  44.635  1.00 15.25           C  
ATOM   1805  N   ILE A 237      14.934  70.126  44.952  1.00 17.70           N  
ATOM   1806  CA  ILE A 237      14.288  71.188  45.703  1.00 15.94           C  
ATOM   1807  C   ILE A 237      12.783  70.944  45.665  1.00 18.19           C  
ATOM   1808  O   ILE A 237      12.260  70.474  44.658  1.00 17.49           O  
ATOM   1809  CB  ILE A 237      14.517  72.571  45.014  1.00 20.22           C  
ATOM   1810  CG1 ILE A 237      15.997  72.783  44.670  1.00 19.35           C  
ATOM   1811  CG2 ILE A 237      13.956  73.705  45.879  1.00 15.80           C  
ATOM   1812  CD1 ILE A 237      16.925  72.815  45.863  1.00 25.66           C  
ATOM   1813  N   LEU A 238      12.090  71.237  46.761  1.00 17.62           N  
ATOM   1814  CA  LEU A 238      10.638  71.097  46.780  1.00 19.02           C  
ATOM   1815  C   LEU A 238      10.124  72.517  46.884  1.00 18.42           C  
ATOM   1816  O   LEU A 238      10.338  73.192  47.895  1.00 17.62           O  
ATOM   1817  CB  LEU A 238      10.149  70.261  47.969  1.00 20.95           C  
ATOM   1818  CG  LEU A 238       8.636  70.004  48.068  1.00 16.96           C  
ATOM   1819  CD1 LEU A 238       8.089  69.371  46.784  1.00 14.77           C  
ATOM   1820  CD2 LEU A 238       8.344  69.116  49.270  1.00 13.71           C  
ATOM   1821  N   SER A 239       9.488  72.978  45.816  1.00 19.05           N  
ATOM   1822  CA  SER A 239       8.972  74.336  45.742  1.00 18.60           C  
ATOM   1823  C   SER A 239       7.453  74.365  45.786  1.00 20.77           C  
ATOM   1824  O   SER A 239       6.773  73.762  44.949  1.00 21.57           O  
ATOM   1825  CB  SER A 239       9.484  75.013  44.461  1.00 18.21           C  
ATOM   1826  OG  SER A 239       9.033  76.352  44.372  1.00 22.53           O  
ATOM   1827  N   VAL A 240       6.923  75.034  46.801  1.00 25.21           N  
ATOM   1828  CA  VAL A 240       5.483  75.156  46.941  1.00 31.88           C  
ATOM   1829  C   VAL A 240       5.095  76.623  46.708  1.00 35.60           C  
ATOM   1830  O   VAL A 240       3.911  76.945  46.598  1.00 47.48           O  
ATOM   1831  CB  VAL A 240       4.998  74.655  48.334  1.00 31.48           C  
ATOM   1832  CG1 VAL A 240       5.369  75.645  49.411  1.00 41.09           C  
ATOM   1833  CG2 VAL A 240       3.501  74.399  48.333  1.00 26.29           C  
ATOM   1834  N   VAL A 241       6.099  77.489  46.580  1.00 30.69           N  
ATOM   1835  CA  VAL A 241       5.891  78.916  46.350  1.00 24.48           C  
ATOM   1836  C   VAL A 241       5.484  79.213  44.905  1.00 22.74           C  
ATOM   1837  O   VAL A 241       5.958  78.577  43.970  1.00 22.57           O  
ATOM   1838  CB  VAL A 241       7.144  79.731  46.734  1.00 25.83           C  
ATOM   1839  CG1 VAL A 241       7.387  79.616  48.231  1.00 18.95           C  
ATOM   1840  CG2 VAL A 241       8.363  79.244  45.955  1.00 24.60           C  
ATOM   1841  N   PRO A 242       4.568  80.182  44.711  1.00 19.98           N  
ATOM   1842  CA  PRO A 242       4.102  80.534  43.360  1.00 20.67           C  
ATOM   1843  C   PRO A 242       5.157  81.011  42.353  1.00 19.70           C  
ATOM   1844  O   PRO A 242       5.937  81.928  42.632  1.00 18.10           O  
ATOM   1845  CB  PRO A 242       3.000  81.570  43.636  1.00 21.22           C  
ATOM   1846  CG  PRO A 242       3.371  82.130  44.996  1.00 21.28           C  
ATOM   1847  CD  PRO A 242       3.818  80.910  45.742  1.00 18.59           C  
ATOM   1848  N   PHE A 243       5.141  80.385  41.174  1.00 19.25           N  
ATOM   1849  CA  PHE A 243       6.079  80.677  40.087  1.00 21.77           C  
ATOM   1850  C   PHE A 243       5.902  82.058  39.478  1.00 22.08           C  
ATOM   1851  O   PHE A 243       6.840  82.611  38.915  1.00 23.91           O  
ATOM   1852  CB  PHE A 243       5.959  79.640  38.967  1.00 18.81           C  
ATOM   1853  CG  PHE A 243       6.485  78.277  39.323  1.00 17.62           C  
ATOM   1854  CD1 PHE A 243       7.287  78.080  40.448  1.00 15.58           C  
ATOM   1855  CD2 PHE A 243       6.172  77.183  38.523  1.00 15.44           C  
ATOM   1856  CE1 PHE A 243       7.766  76.808  40.768  1.00 16.67           C  
ATOM   1857  CE2 PHE A 243       6.645  75.908  38.832  1.00 16.25           C  
ATOM   1858  CZ  PHE A 243       7.444  75.719  39.958  1.00 17.30           C  
ATOM   1859  N   HIS A 244       4.686  82.590  39.552  1.00 23.71           N  
ATOM   1860  CA  HIS A 244       4.391  83.915  38.999  1.00 26.55           C  
ATOM   1861  C   HIS A 244       4.858  85.059  39.902  1.00 29.43           C  
ATOM   1862  O   HIS A 244       4.644  86.230  39.588  1.00 29.80           O  
ATOM   1863  CB  HIS A 244       2.892  84.061  38.737  1.00 25.79           C  
ATOM   1864  CG  HIS A 244       2.048  83.883  39.959  1.00 27.58           C  
ATOM   1865  ND1 HIS A 244       2.024  84.800  40.986  1.00 27.53           N  
ATOM   1866  CD2 HIS A 244       1.243  82.865  40.348  1.00 27.26           C  
ATOM   1867  CE1 HIS A 244       1.244  84.359  41.956  1.00 26.65           C  
ATOM   1868  NE2 HIS A 244       0.761  83.185  41.593  1.00 27.45           N  
ATOM   1869  N   HIS A 245       5.448  84.715  41.044  1.00 26.04           N  
ATOM   1870  CA  HIS A 245       5.949  85.693  42.002  1.00 23.06           C  
ATOM   1871  C   HIS A 245       7.479  85.578  41.994  1.00 23.91           C  
ATOM   1872  O   HIS A 245       8.014  84.513  41.692  1.00 24.03           O  
ATOM   1873  CB  HIS A 245       5.380  85.367  43.390  1.00 27.84           C  
ATOM   1874  CG  HIS A 245       5.753  86.351  44.456  1.00 32.67           C  
ATOM   1875  ND1 HIS A 245       6.658  86.064  45.453  1.00 36.97           N  
ATOM   1876  CD2 HIS A 245       5.344  87.627  44.673  1.00 34.65           C  
ATOM   1877  CE1 HIS A 245       6.802  87.118  46.237  1.00 37.52           C  
ATOM   1878  NE2 HIS A 245       6.017  88.080  45.782  1.00 40.72           N  
ATOM   1879  N   GLY A 246       8.177  86.654  42.351  1.00 21.88           N  
ATOM   1880  CA  GLY A 246       9.636  86.662  42.358  1.00 21.56           C  
ATOM   1881  C   GLY A 246      10.358  85.546  43.101  1.00 25.51           C  
ATOM   1882  O   GLY A 246      11.420  85.086  42.662  1.00 24.36           O  
ATOM   1883  N   PHE A 247       9.821  85.126  44.245  1.00 24.56           N  
ATOM   1884  CA  PHE A 247      10.460  84.047  44.991  1.00 25.85           C  
ATOM   1885  C   PHE A 247      10.507  82.779  44.116  1.00 25.91           C  
ATOM   1886  O   PHE A 247      11.588  82.257  43.841  1.00 25.08           O  
ATOM   1887  CB  PHE A 247       9.725  83.786  46.318  1.00 29.44           C  
ATOM   1888  CG  PHE A 247      10.468  82.850  47.274  1.00 37.09           C  
ATOM   1889  CD1 PHE A 247      11.830  82.574  47.104  1.00 34.76           C  
ATOM   1890  CD2 PHE A 247       9.794  82.227  48.328  1.00 30.86           C  
ATOM   1891  CE1 PHE A 247      12.501  81.694  47.961  1.00 30.42           C  
ATOM   1892  CE2 PHE A 247      10.460  81.349  49.186  1.00 29.63           C  
ATOM   1893  CZ  PHE A 247      11.814  81.082  49.002  1.00 25.94           C  
ATOM   1894  N   GLY A 248       9.345  82.332  43.640  1.00 20.36           N  
ATOM   1895  CA  GLY A 248       9.283  81.149  42.800  1.00 18.39           C  
ATOM   1896  C   GLY A 248       9.939  81.333  41.441  1.00 21.37           C  
ATOM   1897  O   GLY A 248      10.622  80.434  40.942  1.00 23.47           O  
ATOM   1898  N   MET A 249       9.763  82.505  40.844  1.00 17.42           N  
ATOM   1899  CA  MET A 249      10.329  82.792  39.540  1.00 17.16           C  
ATOM   1900  C   MET A 249      11.844  82.740  39.522  1.00 17.60           C  
ATOM   1901  O   MET A 249      12.443  81.945  38.793  1.00 16.58           O  
ATOM   1902  CB  MET A 249       9.862  84.171  39.054  1.00 18.72           C  
ATOM   1903  CG  MET A 249      10.494  84.650  37.736  1.00 19.59           C  
ATOM   1904  SD  MET A 249      10.259  83.574  36.302  1.00 19.30           S  
ATOM   1905  CE  MET A 249       8.546  83.710  36.057  1.00 11.12           C  
ATOM   1906  N   PHE A 250      12.468  83.565  40.351  1.00 20.15           N  
ATOM   1907  CA  PHE A 250      13.919  83.637  40.365  1.00 20.78           C  
ATOM   1908  C   PHE A 250      14.687  82.516  41.047  1.00 21.73           C  
ATOM   1909  O   PHE A 250      15.882  82.349  40.800  1.00 21.26           O  
ATOM   1910  CB  PHE A 250      14.369  85.037  40.769  1.00 18.82           C  
ATOM   1911  CG  PHE A 250      13.914  86.088  39.798  1.00 20.73           C  
ATOM   1912  CD1 PHE A 250      14.538  86.217  38.560  1.00 20.55           C  
ATOM   1913  CD2 PHE A 250      12.796  86.873  40.068  1.00 17.58           C  
ATOM   1914  CE1 PHE A 250      14.049  87.105  37.599  1.00 16.75           C  
ATOM   1915  CE2 PHE A 250      12.300  87.763  39.114  1.00 15.74           C  
ATOM   1916  CZ  PHE A 250      12.927  87.878  37.874  1.00 16.58           C  
ATOM   1917  N   THR A 251      14.013  81.732  41.883  1.00 19.39           N  
ATOM   1918  CA  THR A 251      14.677  80.588  42.477  1.00 20.14           C  
ATOM   1919  C   THR A 251      14.714  79.505  41.378  1.00 20.66           C  
ATOM   1920  O   THR A 251      15.777  78.938  41.090  1.00 20.85           O  
ATOM   1921  CB  THR A 251      13.937  80.045  43.735  1.00 22.64           C  
ATOM   1922  OG1 THR A 251      12.536  79.920  43.464  1.00 21.82           O  
ATOM   1923  CG2 THR A 251      14.157  80.967  44.938  1.00 23.92           C  
ATOM   1924  N   THR A 252      13.584  79.301  40.701  1.00 17.91           N  
ATOM   1925  CA  THR A 252      13.490  78.291  39.649  1.00 21.80           C  
ATOM   1926  C   THR A 252      14.452  78.491  38.477  1.00 22.37           C  
ATOM   1927  O   THR A 252      15.154  77.552  38.080  1.00 23.36           O  
ATOM   1928  CB  THR A 252      12.058  78.157  39.104  1.00 17.58           C  
ATOM   1929  OG1 THR A 252      11.156  77.942  40.189  1.00 17.29           O  
ATOM   1930  CG2 THR A 252      11.962  76.963  38.179  1.00 19.25           C  
ATOM   1931  N   LEU A 253      14.481  79.700  37.919  1.00 24.66           N  
ATOM   1932  CA  LEU A 253      15.379  80.002  36.805  1.00 21.79           C  
ATOM   1933  C   LEU A 253      16.810  79.691  37.214  1.00 22.71           C  
ATOM   1934  O   LEU A 253      17.575  79.132  36.434  1.00 27.53           O  
ATOM   1935  CB  LEU A 253      15.257  81.464  36.372  1.00 20.92           C  
ATOM   1936  CG  LEU A 253      13.926  81.881  35.737  1.00 18.32           C  
ATOM   1937  CD1 LEU A 253      13.960  83.357  35.379  1.00 15.70           C  
ATOM   1938  CD2 LEU A 253      13.641  81.041  34.502  1.00 15.88           C  
ATOM   1939  N   GLY A 254      17.148  80.005  38.462  1.00 25.51           N  
ATOM   1940  CA  GLY A 254      18.483  79.728  38.963  1.00 21.42           C  
ATOM   1941  C   GLY A 254      18.727  78.237  39.061  1.00 21.25           C  
ATOM   1942  O   GLY A 254      19.818  77.757  38.745  1.00 20.30           O  
ATOM   1943  N   TYR A 255      17.700  77.500  39.483  1.00 21.10           N  
ATOM   1944  CA  TYR A 255      17.793  76.052  39.620  1.00 20.09           C  
ATOM   1945  C   TYR A 255      18.043  75.417  38.260  1.00 21.78           C  
ATOM   1946  O   TYR A 255      18.784  74.436  38.153  1.00 20.97           O  
ATOM   1947  CB  TYR A 255      16.517  75.477  40.231  1.00 20.67           C  
ATOM   1948  CG  TYR A 255      16.254  75.903  41.663  1.00 25.87           C  
ATOM   1949  CD1 TYR A 255      17.304  76.229  42.528  1.00 25.67           C  
ATOM   1950  CD2 TYR A 255      14.949  75.976  42.157  1.00 24.72           C  
ATOM   1951  CE1 TYR A 255      17.061  76.617  43.849  1.00 21.29           C  
ATOM   1952  CE2 TYR A 255      14.697  76.362  43.478  1.00 20.69           C  
ATOM   1953  CZ  TYR A 255      15.755  76.676  44.313  1.00 21.29           C  
ATOM   1954  OH  TYR A 255      15.503  77.028  45.615  1.00 21.01           O  
ATOM   1955  N   LEU A 256      17.422  75.985  37.227  1.00 21.77           N  
ATOM   1956  CA  LEU A 256      17.586  75.499  35.858  1.00 23.16           C  
ATOM   1957  C   LEU A 256      19.031  75.688  35.417  1.00 23.44           C  
ATOM   1958  O   LEU A 256      19.599  74.830  34.750  1.00 24.77           O  
ATOM   1959  CB  LEU A 256      16.614  76.204  34.915  1.00 20.32           C  
ATOM   1960  CG  LEU A 256      15.147  75.866  35.227  1.00 19.91           C  
ATOM   1961  CD1 LEU A 256      14.199  76.652  34.338  1.00 16.19           C  
ATOM   1962  CD2 LEU A 256      14.916  74.356  35.073  1.00 19.44           C  
ATOM   1963  N   ILE A 257      19.632  76.798  35.826  1.00 25.66           N  
ATOM   1964  CA  ILE A 257      21.031  77.075  35.524  1.00 23.60           C  
ATOM   1965  C   ILE A 257      21.908  76.041  36.225  1.00 21.86           C  
ATOM   1966  O   ILE A 257      22.908  75.588  35.669  1.00 24.95           O  
ATOM   1967  CB  ILE A 257      21.435  78.481  36.032  1.00 24.80           C  
ATOM   1968  CG1 ILE A 257      20.860  79.559  35.116  1.00 22.56           C  
ATOM   1969  CG2 ILE A 257      22.949  78.592  36.155  1.00 19.84           C  
ATOM   1970  CD1 ILE A 257      21.425  79.518  33.720  1.00 24.42           C  
ATOM   1971  N   CYS A 258      21.523  75.674  37.444  1.00 21.49           N  
ATOM   1972  CA  CYS A 258      22.275  74.705  38.236  1.00 20.46           C  
ATOM   1973  C   CYS A 258      22.013  73.237  37.888  1.00 20.33           C  
ATOM   1974  O   CYS A 258      22.673  72.344  38.441  1.00 16.88           O  
ATOM   1975  CB  CYS A 258      22.008  74.920  39.730  1.00 25.58           C  
ATOM   1976  SG  CYS A 258      22.530  76.514  40.404  1.00 28.83           S  
ATOM   1977  N   GLY A 259      21.042  72.982  37.013  1.00 16.77           N  
ATOM   1978  CA  GLY A 259      20.721  71.614  36.634  1.00 19.09           C  
ATOM   1979  C   GLY A 259      20.045  70.784  37.718  1.00 22.19           C  
ATOM   1980  O   GLY A 259      20.105  69.548  37.698  1.00 21.34           O  
ATOM   1981  N   PHE A 260      19.378  71.463  38.648  1.00 23.36           N  
ATOM   1982  CA  PHE A 260      18.691  70.793  39.754  1.00 23.08           C  
ATOM   1983  C   PHE A 260      17.347  70.217  39.331  1.00 20.44           C  
ATOM   1984  O   PHE A 260      16.817  70.563  38.272  1.00 22.92           O  
ATOM   1985  CB  PHE A 260      18.442  71.776  40.914  1.00 21.54           C  
ATOM   1986  CG  PHE A 260      19.692  72.318  41.546  1.00 19.36           C  
ATOM   1987  CD1 PHE A 260      20.912  71.665  41.405  1.00 17.44           C  
ATOM   1988  CD2 PHE A 260      19.638  73.476  42.308  1.00 16.80           C  
ATOM   1989  CE1 PHE A 260      22.054  72.163  42.016  1.00 19.93           C  
ATOM   1990  CE2 PHE A 260      20.773  73.979  42.921  1.00 15.58           C  
ATOM   1991  CZ  PHE A 260      21.982  73.325  42.777  1.00 16.55           C  
ATOM   1992  N   ARG A 261      16.808  69.339  40.177  1.00 22.13           N  
ATOM   1993  CA  ARG A 261      15.499  68.723  39.962  1.00 18.92           C  
ATOM   1994  C   ARG A 261      14.529  69.553  40.797  1.00 18.47           C  
ATOM   1995  O   ARG A 261      14.682  69.635  42.018  1.00 18.38           O  
ATOM   1996  CB  ARG A 261      15.506  67.281  40.474  1.00 17.77           C  
ATOM   1997  CG  ARG A 261      14.166  66.584  40.379  1.00 13.67           C  
ATOM   1998  CD  ARG A 261      14.202  65.231  41.062  1.00 16.07           C  
ATOM   1999  NE  ARG A 261      13.014  64.442  40.769  1.00 13.70           N  
ATOM   2000  CZ  ARG A 261      12.803  63.207  41.212  1.00 13.96           C  
ATOM   2001  NH1 ARG A 261      13.702  62.613  41.980  1.00 14.54           N  
ATOM   2002  NH2 ARG A 261      11.699  62.558  40.872  1.00 19.52           N  
ATOM   2003  N   VAL A 262      13.581  70.213  40.141  1.00 16.62           N  
ATOM   2004  CA  VAL A 262      12.597  71.044  40.829  1.00 19.98           C  
ATOM   2005  C   VAL A 262      11.264  70.306  41.006  1.00 18.48           C  
ATOM   2006  O   VAL A 262      10.484  70.156  40.058  1.00 15.46           O  
ATOM   2007  CB  VAL A 262      12.362  72.398  40.078  1.00 19.83           C  
ATOM   2008  CG1 VAL A 262      11.325  73.266  40.822  1.00 14.09           C  
ATOM   2009  CG2 VAL A 262      13.680  73.151  39.934  1.00 15.00           C  
ATOM   2010  N   VAL A 263      11.030  69.813  42.217  1.00 17.88           N  
ATOM   2011  CA  VAL A 263       9.791  69.113  42.534  1.00 17.04           C  
ATOM   2012  C   VAL A 263       8.780  70.184  42.948  1.00 20.14           C  
ATOM   2013  O   VAL A 263       9.016  70.965  43.884  1.00 18.52           O  
ATOM   2014  CB  VAL A 263       9.999  68.074  43.654  1.00 13.61           C  
ATOM   2015  CG1 VAL A 263       8.747  67.249  43.847  1.00 14.10           C  
ATOM   2016  CG2 VAL A 263      11.172  67.169  43.315  1.00  8.34           C  
ATOM   2017  N   LEU A 264       7.666  70.245  42.229  1.00 15.48           N  
ATOM   2018  CA  LEU A 264       6.662  71.256  42.500  1.00 20.47           C  
ATOM   2019  C   LEU A 264       5.349  70.763  43.086  1.00 20.50           C  
ATOM   2020  O   LEU A 264       4.965  69.600  42.941  1.00 17.34           O  
ATOM   2021  CB  LEU A 264       6.389  72.071  41.223  1.00 19.34           C  
ATOM   2022  CG  LEU A 264       5.761  71.350  40.016  1.00 24.31           C  
ATOM   2023  CD1 LEU A 264       4.230  71.397  40.069  1.00 20.40           C  
ATOM   2024  CD2 LEU A 264       6.250  71.991  38.728  1.00 17.27           C  
ATOM   2025  N   MET A 265       4.671  71.681  43.756  1.00 24.82           N  
ATOM   2026  CA  MET A 265       3.368  71.427  44.339  1.00 29.65           C  
ATOM   2027  C   MET A 265       2.554  72.677  44.057  1.00 29.88           C  
ATOM   2028  O   MET A 265       3.074  73.786  44.173  1.00 33.16           O  
ATOM   2029  CB  MET A 265       3.472  71.241  45.856  1.00 29.04           C  
ATOM   2030  CG  MET A 265       3.899  69.856  46.315  1.00 30.95           C  
ATOM   2031  SD  MET A 265       3.953  69.705  48.120  1.00 29.35           S  
ATOM   2032  CE  MET A 265       2.211  69.619  48.527  1.00 22.39           C  
ATOM   2033  N   TYR A 266       1.324  72.503  43.589  1.00 28.14           N  
ATOM   2034  CA  TYR A 266       0.466  73.652  43.356  1.00 30.36           C  
ATOM   2035  C   TYR A 266      -0.629  73.765  44.425  1.00 28.82           C  
ATOM   2036  O   TYR A 266      -1.303  74.784  44.532  1.00 30.66           O  
ATOM   2037  CB  TYR A 266      -0.113  73.651  41.937  1.00 33.19           C  
ATOM   2038  CG  TYR A 266      -0.704  72.350  41.456  1.00 36.50           C  
ATOM   2039  CD1 TYR A 266      -2.024  72.006  41.747  1.00 38.83           C  
ATOM   2040  CD2 TYR A 266       0.060  71.462  40.694  1.00 45.88           C  
ATOM   2041  CE1 TYR A 266      -2.577  70.795  41.291  1.00 45.78           C  
ATOM   2042  CE2 TYR A 266      -0.477  70.252  40.228  1.00 48.93           C  
ATOM   2043  CZ  TYR A 266      -1.795  69.922  40.531  1.00 50.43           C  
ATOM   2044  OH  TYR A 266      -2.322  68.723  40.080  1.00 48.75           O  
ATOM   2045  N   ARG A 267      -0.787  72.718  45.229  1.00 26.25           N  
ATOM   2046  CA  ARG A 267      -1.778  72.699  46.303  1.00 27.44           C  
ATOM   2047  C   ARG A 267      -1.078  72.124  47.520  1.00 26.80           C  
ATOM   2048  O   ARG A 267      -0.534  71.019  47.454  1.00 27.31           O  
ATOM   2049  CB  ARG A 267      -2.971  71.813  45.941  1.00 29.14           C  
ATOM   2050  CG  ARG A 267      -3.791  72.327  44.768  1.00 43.91           C  
ATOM   2051  CD  ARG A 267      -4.989  71.429  44.436  1.00 50.47           C  
ATOM   2052  NE  ARG A 267      -4.603  70.060  44.108  1.00 47.61           N  
ATOM   2053  CZ  ARG A 267      -4.675  69.048  44.964  1.00 47.61           C  
ATOM   2054  NH1 ARG A 267      -5.127  69.256  46.197  1.00 48.97           N  
ATOM   2055  NH2 ARG A 267      -4.270  67.839  44.599  1.00 44.11           N  
ATOM   2056  N   PHE A 268      -1.022  72.899  48.599  1.00 23.02           N  
ATOM   2057  CA  PHE A 268      -0.372  72.432  49.814  1.00 23.52           C  
ATOM   2058  C   PHE A 268      -1.200  71.373  50.532  1.00 23.39           C  
ATOM   2059  O   PHE A 268      -2.428  71.458  50.591  1.00 24.61           O  
ATOM   2060  CB  PHE A 268      -0.087  73.577  50.790  1.00 19.65           C  
ATOM   2061  CG  PHE A 268       0.500  73.111  52.097  1.00 18.12           C  
ATOM   2062  CD1 PHE A 268       1.839  72.722  52.172  1.00 14.58           C  
ATOM   2063  CD2 PHE A 268      -0.299  72.989  53.233  1.00 15.51           C  
ATOM   2064  CE1 PHE A 268       2.371  72.216  53.351  1.00 17.89           C  
ATOM   2065  CE2 PHE A 268       0.227  72.480  54.422  1.00 13.83           C  
ATOM   2066  CZ  PHE A 268       1.564  72.092  54.478  1.00 16.81           C  
ATOM   2067  N   GLU A 269      -0.500  70.379  51.067  1.00 19.97           N  
ATOM   2068  CA  GLU A 269      -1.086  69.287  51.827  1.00 18.25           C  
ATOM   2069  C   GLU A 269       0.056  68.814  52.701  1.00 19.69           C  
ATOM   2070  O   GLU A 269       1.167  68.567  52.202  1.00 14.78           O  
ATOM   2071  CB  GLU A 269      -1.534  68.165  50.908  1.00 21.14           C  
ATOM   2072  CG  GLU A 269      -2.684  68.538  49.990  1.00 18.40           C  
ATOM   2073  CD  GLU A 269      -3.232  67.358  49.232  1.00 22.13           C  
ATOM   2074  OE1 GLU A 269      -2.969  66.205  49.640  1.00 18.43           O  
ATOM   2075  OE2 GLU A 269      -3.931  67.588  48.226  1.00 25.94           O  
ATOM   2076  N   GLU A 270      -0.211  68.694  54.000  1.00 17.82           N  
ATOM   2077  CA  GLU A 270       0.807  68.305  54.967  1.00 16.86           C  
ATOM   2078  C   GLU A 270       1.528  67.000  54.657  1.00 16.51           C  
ATOM   2079  O   GLU A 270       2.753  66.981  54.513  1.00 15.98           O  
ATOM   2080  CB  GLU A 270       0.226  68.251  56.379  1.00 19.11           C  
ATOM   2081  CG  GLU A 270       1.297  68.131  57.465  1.00 18.43           C  
ATOM   2082  CD  GLU A 270       0.734  68.080  58.875  1.00 22.94           C  
ATOM   2083  OE1 GLU A 270      -0.504  68.087  59.042  1.00 21.91           O  
ATOM   2084  OE2 GLU A 270       1.544  68.033  59.825  1.00 18.98           O  
ATOM   2085  N   GLU A 271       0.770  65.915  54.559  1.00 14.75           N  
ATOM   2086  CA  GLU A 271       1.353  64.606  54.277  1.00 17.89           C  
ATOM   2087  C   GLU A 271       2.072  64.522  52.944  1.00 17.67           C  
ATOM   2088  O   GLU A 271       3.156  63.949  52.878  1.00 19.97           O  
ATOM   2089  CB  GLU A 271       0.294  63.518  54.348  1.00 18.42           C  
ATOM   2090  CG  GLU A 271      -0.174  63.247  55.737  1.00 19.13           C  
ATOM   2091  CD  GLU A 271      -1.423  62.423  55.735  1.00 24.25           C  
ATOM   2092  OE1 GLU A 271      -2.461  62.941  55.272  1.00 22.06           O  
ATOM   2093  OE2 GLU A 271      -1.368  61.260  56.182  1.00 27.98           O  
ATOM   2094  N   LEU A 272       1.467  65.060  51.884  1.00 17.64           N  
ATOM   2095  CA  LEU A 272       2.093  65.042  50.564  1.00 13.37           C  
ATOM   2096  C   LEU A 272       3.407  65.823  50.601  1.00 16.57           C  
ATOM   2097  O   LEU A 272       4.393  65.410  49.989  1.00 17.94           O  
ATOM   2098  CB  LEU A 272       1.160  65.625  49.497  1.00 14.91           C  
ATOM   2099  CG  LEU A 272       1.753  65.677  48.076  1.00 19.94           C  
ATOM   2100  CD1 LEU A 272       2.091  64.278  47.574  1.00 14.13           C  
ATOM   2101  CD2 LEU A 272       0.790  66.345  47.119  1.00 13.73           C  
ATOM   2102  N   PHE A 273       3.429  66.927  51.346  1.00 13.59           N  
ATOM   2103  CA  PHE A 273       4.637  67.736  51.465  1.00 13.29           C  
ATOM   2104  C   PHE A 273       5.772  66.967  52.142  1.00 13.68           C  
ATOM   2105  O   PHE A 273       6.866  66.826  51.588  1.00 16.82           O  
ATOM   2106  CB  PHE A 273       4.353  69.019  52.253  1.00 15.31           C  
ATOM   2107  CG  PHE A 273       5.553  69.914  52.403  1.00 17.45           C  
ATOM   2108  CD1 PHE A 273       5.864  70.854  51.417  1.00 20.60           C  
ATOM   2109  CD2 PHE A 273       6.389  69.804  53.514  1.00 14.62           C  
ATOM   2110  CE1 PHE A 273       6.991  71.665  51.536  1.00 17.29           C  
ATOM   2111  CE2 PHE A 273       7.515  70.612  53.639  1.00 16.51           C  
ATOM   2112  CZ  PHE A 273       7.817  71.542  52.648  1.00 14.24           C  
ATOM   2113  N   LEU A 274       5.511  66.463  53.340  1.00 14.70           N  
ATOM   2114  CA  LEU A 274       6.524  65.724  54.086  1.00 16.27           C  
ATOM   2115  C   LEU A 274       6.977  64.450  53.364  1.00 15.49           C  
ATOM   2116  O   LEU A 274       8.175  64.153  53.308  1.00 17.06           O  
ATOM   2117  CB  LEU A 274       6.022  65.423  55.504  1.00 15.04           C  
ATOM   2118  CG  LEU A 274       5.778  66.667  56.368  1.00 12.50           C  
ATOM   2119  CD1 LEU A 274       4.992  66.317  57.603  1.00 14.19           C  
ATOM   2120  CD2 LEU A 274       7.105  67.289  56.746  1.00 11.41           C  
ATOM   2121  N   ARG A 275       6.032  63.730  52.766  1.00 13.31           N  
ATOM   2122  CA  ARG A 275       6.363  62.505  52.043  1.00 15.63           C  
ATOM   2123  C   ARG A 275       7.219  62.834  50.823  1.00 14.40           C  
ATOM   2124  O   ARG A 275       8.090  62.054  50.437  1.00 15.52           O  
ATOM   2125  CB  ARG A 275       5.094  61.758  51.627  1.00 16.10           C  
ATOM   2126  CG  ARG A 275       5.354  60.361  51.113  1.00 14.89           C  
ATOM   2127  CD  ARG A 275       4.058  59.615  50.851  1.00 20.11           C  
ATOM   2128  NE  ARG A 275       3.202  60.301  49.884  1.00 22.10           N  
ATOM   2129  CZ  ARG A 275       2.097  60.972  50.198  1.00 21.45           C  
ATOM   2130  NH1 ARG A 275       1.701  61.062  51.458  1.00 19.50           N  
ATOM   2131  NH2 ARG A 275       1.375  61.545  49.246  1.00 21.83           N  
ATOM   2132  N   SER A 276       6.989  64.004  50.235  1.00 15.77           N  
ATOM   2133  CA  SER A 276       7.764  64.434  49.082  1.00 16.56           C  
ATOM   2134  C   SER A 276       9.192  64.763  49.499  1.00 17.15           C  
ATOM   2135  O   SER A 276      10.145  64.441  48.785  1.00 15.64           O  
ATOM   2136  CB  SER A 276       7.104  65.634  48.407  1.00 14.74           C  
ATOM   2137  OG  SER A 276       5.905  65.250  47.751  1.00 12.40           O  
ATOM   2138  N   LEU A 277       9.342  65.397  50.658  1.00 18.49           N  
ATOM   2139  CA  LEU A 277      10.666  65.734  51.170  1.00 17.41           C  
ATOM   2140  C   LEU A 277      11.452  64.448  51.340  1.00 17.91           C  
ATOM   2141  O   LEU A 277      12.631  64.368  50.976  1.00 18.09           O  
ATOM   2142  CB  LEU A 277      10.560  66.423  52.527  1.00 16.04           C  
ATOM   2143  CG  LEU A 277      10.037  67.850  52.554  1.00 18.12           C  
ATOM   2144  CD1 LEU A 277       9.958  68.311  53.996  1.00 14.35           C  
ATOM   2145  CD2 LEU A 277      10.954  68.759  51.738  1.00 19.02           C  
ATOM   2146  N   GLN A 278      10.771  63.445  51.887  1.00 15.62           N  
ATOM   2147  CA  GLN A 278      11.357  62.143  52.121  1.00 16.93           C  
ATOM   2148  C   GLN A 278      11.687  61.381  50.847  1.00 18.99           C  
ATOM   2149  O   GLN A 278      12.849  61.107  50.569  1.00 20.48           O  
ATOM   2150  CB  GLN A 278      10.413  61.290  52.963  1.00 17.94           C  
ATOM   2151  CG  GLN A 278      10.832  59.840  53.049  1.00 16.72           C  
ATOM   2152  CD  GLN A 278       9.866  59.003  53.856  1.00 20.80           C  
ATOM   2153  OE1 GLN A 278       9.956  58.941  55.082  1.00 21.04           O  
ATOM   2154  NE2 GLN A 278       8.934  58.355  53.175  1.00 17.55           N  
ATOM   2155  N   ASP A 279      10.656  61.059  50.075  1.00 16.51           N  
ATOM   2156  CA  ASP A 279      10.797  60.277  48.856  1.00 16.42           C  
ATOM   2157  C   ASP A 279      11.713  60.869  47.781  1.00 19.43           C  
ATOM   2158  O   ASP A 279      12.503  60.151  47.168  1.00 16.19           O  
ATOM   2159  CB  ASP A 279       9.410  59.947  48.280  1.00 16.03           C  
ATOM   2160  CG  ASP A 279       8.619  58.983  49.161  1.00 15.30           C  
ATOM   2161  OD1 ASP A 279       9.141  58.514  50.193  1.00 19.52           O  
ATOM   2162  OD2 ASP A 279       7.458  58.679  48.816  1.00 21.24           O  
ATOM   2163  N   TYR A 280      11.614  62.175  47.558  1.00 18.41           N  
ATOM   2164  CA  TYR A 280      12.448  62.818  46.557  1.00 16.93           C  
ATOM   2165  C   TYR A 280      13.799  63.233  47.120  1.00 18.09           C  
ATOM   2166  O   TYR A 280      14.576  63.899  46.438  1.00 20.39           O  
ATOM   2167  CB  TYR A 280      11.727  64.016  45.944  1.00 16.49           C  
ATOM   2168  CG  TYR A 280      10.456  63.639  45.212  1.00 17.30           C  
ATOM   2169  CD1 TYR A 280      10.496  62.825  44.080  1.00 16.64           C  
ATOM   2170  CD2 TYR A 280       9.214  64.092  45.651  1.00 17.80           C  
ATOM   2171  CE1 TYR A 280       9.324  62.471  43.397  1.00 17.14           C  
ATOM   2172  CE2 TYR A 280       8.035  63.743  44.975  1.00 14.99           C  
ATOM   2173  CZ  TYR A 280       8.098  62.933  43.850  1.00 17.53           C  
ATOM   2174  OH  TYR A 280       6.941  62.593  43.179  1.00 13.23           O  
ATOM   2175  N   LYS A 281      14.073  62.847  48.364  1.00 19.27           N  
ATOM   2176  CA  LYS A 281      15.345  63.156  49.023  1.00 20.59           C  
ATOM   2177  C   LYS A 281      15.715  64.626  48.847  1.00 21.44           C  
ATOM   2178  O   LYS A 281      16.847  64.966  48.492  1.00 22.14           O  
ATOM   2179  CB  LYS A 281      16.441  62.252  48.463  1.00 20.78           C  
ATOM   2180  CG  LYS A 281      16.095  60.786  48.547  1.00 20.15           C  
ATOM   2181  CD  LYS A 281      17.112  59.958  47.802  1.00 26.95           C  
ATOM   2182  CE  LYS A 281      16.902  58.488  48.074  1.00 31.46           C  
ATOM   2183  NZ  LYS A 281      17.820  57.681  47.238  1.00 41.99           N  
ATOM   2184  N   ILE A 282      14.743  65.483  49.133  1.00 20.97           N  
ATOM   2185  CA  ILE A 282      14.877  66.923  49.004  1.00 19.71           C  
ATOM   2186  C   ILE A 282      15.957  67.534  49.904  1.00 21.00           C  
ATOM   2187  O   ILE A 282      16.036  67.212  51.095  1.00 18.17           O  
ATOM   2188  CB  ILE A 282      13.522  67.602  49.327  1.00 18.77           C  
ATOM   2189  CG1 ILE A 282      12.417  67.056  48.413  1.00 16.34           C  
ATOM   2190  CG2 ILE A 282      13.648  69.116  49.261  1.00 15.77           C  
ATOM   2191  CD1 ILE A 282      12.546  67.420  46.959  1.00 10.23           C  
ATOM   2192  N   GLN A 283      16.773  68.416  49.325  1.00 19.59           N  
ATOM   2193  CA  GLN A 283      17.827  69.117  50.064  1.00 20.77           C  
ATOM   2194  C   GLN A 283      17.344  70.488  50.534  1.00 19.60           C  
ATOM   2195  O   GLN A 283      17.797  70.981  51.571  1.00 19.71           O  
ATOM   2196  CB  GLN A 283      19.083  69.324  49.203  1.00 18.14           C  
ATOM   2197  CG  GLN A 283      20.037  68.138  49.127  1.00 25.85           C  
ATOM   2198  CD  GLN A 283      19.614  67.098  48.105  1.00 32.14           C  
ATOM   2199  OE1 GLN A 283      18.749  67.346  47.262  1.00 34.11           O  
ATOM   2200  NE2 GLN A 283      20.240  65.936  48.161  1.00 32.87           N  
ATOM   2201  N   SER A 284      16.453  71.110  49.758  1.00 20.19           N  
ATOM   2202  CA  SER A 284      15.919  72.440  50.063  1.00 20.68           C  
ATOM   2203  C   SER A 284      14.424  72.533  49.787  1.00 20.41           C  
ATOM   2204  O   SER A 284      13.948  72.058  48.760  1.00 23.23           O  
ATOM   2205  CB  SER A 284      16.626  73.514  49.221  1.00 15.02           C  
ATOM   2206  OG  SER A 284      18.034  73.405  49.320  1.00 25.82           O  
ATOM   2207  N   ALA A 285      13.699  73.174  50.695  1.00 20.30           N  
ATOM   2208  CA  ALA A 285      12.258  73.370  50.567  1.00 20.05           C  
ATOM   2209  C   ALA A 285      12.009  74.873  50.639  1.00 18.89           C  
ATOM   2210  O   ALA A 285      12.659  75.575  51.419  1.00 17.79           O  
ATOM   2211  CB  ALA A 285      11.520  72.661  51.710  1.00 17.42           C  
ATOM   2212  N   LEU A 286      11.115  75.371  49.791  1.00 20.90           N  
ATOM   2213  CA  LEU A 286      10.781  76.791  49.772  1.00 19.34           C  
ATOM   2214  C   LEU A 286       9.338  76.919  50.223  1.00 21.69           C  
ATOM   2215  O   LEU A 286       8.453  76.261  49.662  1.00 17.90           O  
ATOM   2216  CB  LEU A 286      10.928  77.357  48.361  1.00 18.60           C  
ATOM   2217  CG  LEU A 286      12.254  77.099  47.646  1.00 19.99           C  
ATOM   2218  CD1 LEU A 286      12.228  77.777  46.283  1.00 22.95           C  
ATOM   2219  CD2 LEU A 286      13.408  77.630  48.478  1.00 15.84           C  
ATOM   2220  N   LEU A 287       9.098  77.760  51.224  1.00 21.23           N  
ATOM   2221  CA  LEU A 287       7.750  77.949  51.750  1.00 22.04           C  
ATOM   2222  C   LEU A 287       7.378  79.414  51.797  1.00 25.69           C  
ATOM   2223  O   LEU A 287       8.245  80.279  51.937  1.00 27.61           O  
ATOM   2224  CB  LEU A 287       7.654  77.418  53.190  1.00 18.32           C  
ATOM   2225  CG  LEU A 287       7.941  75.962  53.533  1.00 24.44           C  
ATOM   2226  CD1 LEU A 287       8.031  75.819  55.042  1.00 21.60           C  
ATOM   2227  CD2 LEU A 287       6.850  75.072  52.953  1.00 24.29           C  
ATOM   2228  N   VAL A 288       6.083  79.685  51.667  1.00 28.03           N  
ATOM   2229  CA  VAL A 288       5.584  81.044  51.788  1.00 23.69           C  
ATOM   2230  C   VAL A 288       5.540  81.266  53.316  1.00 24.87           C  
ATOM   2231  O   VAL A 288       5.510  80.304  54.090  1.00 26.33           O  
ATOM   2232  CB  VAL A 288       4.171  81.218  51.115  1.00 23.94           C  
ATOM   2233  CG1 VAL A 288       4.246  80.898  49.631  1.00 20.02           C  
ATOM   2234  CG2 VAL A 288       3.124  80.344  51.762  1.00 24.39           C  
ATOM   2235  N   PRO A 289       5.582  82.524  53.772  1.00 29.38           N  
ATOM   2236  CA  PRO A 289       5.556  82.847  55.208  1.00 28.72           C  
ATOM   2237  C   PRO A 289       4.530  82.116  56.095  1.00 23.71           C  
ATOM   2238  O   PRO A 289       4.894  81.567  57.136  1.00 21.78           O  
ATOM   2239  CB  PRO A 289       5.312  84.353  55.201  1.00 34.36           C  
ATOM   2240  CG  PRO A 289       6.044  84.789  53.972  1.00 32.61           C  
ATOM   2241  CD  PRO A 289       5.610  83.756  52.963  1.00 31.85           C  
ATOM   2242  N   THR A 290       3.259  82.095  55.696  1.00 20.81           N  
ATOM   2243  CA  THR A 290       2.230  81.441  56.502  1.00 18.12           C  
ATOM   2244  C   THR A 290       2.380  79.929  56.600  1.00 18.72           C  
ATOM   2245  O   THR A 290       1.760  79.292  57.449  1.00 20.74           O  
ATOM   2246  CB  THR A 290       0.806  81.814  56.048  1.00 19.32           C  
ATOM   2247  OG1 THR A 290       0.697  81.713  54.624  1.00 23.19           O  
ATOM   2248  CG2 THR A 290       0.476  83.233  56.473  1.00 21.10           C  
ATOM   2249  N   LEU A 291       3.207  79.349  55.740  1.00 18.13           N  
ATOM   2250  CA  LEU A 291       3.432  77.912  55.811  1.00 19.93           C  
ATOM   2251  C   LEU A 291       4.526  77.605  56.837  1.00 18.10           C  
ATOM   2252  O   LEU A 291       4.644  76.479  57.306  1.00 18.24           O  
ATOM   2253  CB  LEU A 291       3.734  77.314  54.435  1.00 21.96           C  
ATOM   2254  CG  LEU A 291       2.504  77.192  53.518  1.00 19.36           C  
ATOM   2255  CD1 LEU A 291       2.870  76.556  52.186  1.00 15.86           C  
ATOM   2256  CD2 LEU A 291       1.428  76.372  54.203  1.00 13.65           C  
ATOM   2257  N   PHE A 292       5.325  78.612  57.189  1.00 18.56           N  
ATOM   2258  CA  PHE A 292       6.351  78.449  58.222  1.00 20.63           C  
ATOM   2259  C   PHE A 292       5.585  78.346  59.548  1.00 21.24           C  
ATOM   2260  O   PHE A 292       5.847  77.470  60.377  1.00 23.06           O  
ATOM   2261  CB  PHE A 292       7.296  79.652  58.258  1.00 22.69           C  
ATOM   2262  CG  PHE A 292       8.520  79.491  57.387  1.00 24.35           C  
ATOM   2263  CD1 PHE A 292       9.661  78.861  57.879  1.00 22.65           C  
ATOM   2264  CD2 PHE A 292       8.532  79.966  56.078  1.00 22.59           C  
ATOM   2265  CE1 PHE A 292      10.788  78.707  57.086  1.00 24.24           C  
ATOM   2266  CE2 PHE A 292       9.652  79.816  55.277  1.00 21.08           C  
ATOM   2267  CZ  PHE A 292      10.784  79.186  55.780  1.00 24.24           C  
ATOM   2268  N   SER A 293       4.604  79.228  59.715  1.00 19.51           N  
ATOM   2269  CA  SER A 293       3.767  79.223  60.900  1.00 23.23           C  
ATOM   2270  C   SER A 293       3.071  77.868  60.992  1.00 23.67           C  
ATOM   2271  O   SER A 293       2.990  77.282  62.073  1.00 29.30           O  
ATOM   2272  CB  SER A 293       2.720  80.332  60.828  1.00 26.26           C  
ATOM   2273  OG  SER A 293       3.310  81.593  60.553  1.00 37.50           O  
ATOM   2274  N   PHE A 294       2.582  77.365  59.857  1.00 20.69           N  
ATOM   2275  CA  PHE A 294       1.913  76.073  59.835  1.00 18.62           C  
ATOM   2276  C   PHE A 294       2.820  74.960  60.351  1.00 18.55           C  
ATOM   2277  O   PHE A 294       2.421  74.187  61.224  1.00 20.40           O  
ATOM   2278  CB  PHE A 294       1.413  75.727  58.425  1.00 16.85           C  
ATOM   2279  CG  PHE A 294       0.924  74.306  58.290  1.00 14.44           C  
ATOM   2280  CD1 PHE A 294       1.803  73.275  57.948  1.00 11.02           C  
ATOM   2281  CD2 PHE A 294      -0.402  73.988  58.550  1.00 14.83           C  
ATOM   2282  CE1 PHE A 294       1.364  71.948  57.874  1.00  8.47           C  
ATOM   2283  CE2 PHE A 294      -0.852  72.660  58.476  1.00 13.81           C  
ATOM   2284  CZ  PHE A 294       0.032  71.645  58.139  1.00 10.60           C  
ATOM   2285  N   PHE A 295       4.042  74.877  59.829  1.00 19.12           N  
ATOM   2286  CA  PHE A 295       4.945  73.815  60.258  1.00 20.81           C  
ATOM   2287  C   PHE A 295       5.414  73.876  61.697  1.00 20.50           C  
ATOM   2288  O   PHE A 295       5.805  72.864  62.263  1.00 17.27           O  
ATOM   2289  CB  PHE A 295       6.102  73.625  59.287  1.00 18.79           C  
ATOM   2290  CG  PHE A 295       5.740  72.772  58.115  1.00 20.45           C  
ATOM   2291  CD1 PHE A 295       5.398  71.439  58.305  1.00 17.21           C  
ATOM   2292  CD2 PHE A 295       5.645  73.318  56.843  1.00 19.19           C  
ATOM   2293  CE1 PHE A 295       4.956  70.662  57.256  1.00 16.89           C  
ATOM   2294  CE2 PHE A 295       5.205  72.550  55.779  1.00 23.13           C  
ATOM   2295  CZ  PHE A 295       4.857  71.215  55.986  1.00 23.06           C  
ATOM   2296  N   ALA A 296       5.329  75.055  62.297  1.00 21.14           N  
ATOM   2297  CA  ALA A 296       5.692  75.209  63.693  1.00 20.80           C  
ATOM   2298  C   ALA A 296       4.671  74.408  64.523  1.00 20.69           C  
ATOM   2299  O   ALA A 296       4.961  73.981  65.640  1.00 23.28           O  
ATOM   2300  CB  ALA A 296       5.656  76.687  64.070  1.00 21.09           C  
ATOM   2301  N   LYS A 297       3.489  74.182  63.951  1.00 23.43           N  
ATOM   2302  CA  LYS A 297       2.409  73.432  64.599  1.00 21.33           C  
ATOM   2303  C   LYS A 297       2.406  71.937  64.268  1.00 23.60           C  
ATOM   2304  O   LYS A 297       1.728  71.160  64.939  1.00 25.66           O  
ATOM   2305  CB  LYS A 297       1.048  74.001  64.181  1.00 19.74           C  
ATOM   2306  CG  LYS A 297       0.850  75.475  64.475  1.00 22.46           C  
ATOM   2307  CD  LYS A 297      -0.334  76.032  63.691  1.00 24.45           C  
ATOM   2308  CE  LYS A 297      -0.556  77.496  64.025  1.00 29.24           C  
ATOM   2309  NZ  LYS A 297      -1.637  78.119  63.214  1.00 33.94           N  
ATOM   2310  N   SER A 298       3.146  71.540  63.231  1.00 24.05           N  
ATOM   2311  CA  SER A 298       3.184  70.148  62.782  1.00 18.33           C  
ATOM   2312  C   SER A 298       3.798  69.146  63.754  1.00 17.72           C  
ATOM   2313  O   SER A 298       4.911  69.334  64.238  1.00 21.55           O  
ATOM   2314  CB  SER A 298       3.903  70.052  61.435  1.00 20.81           C  
ATOM   2315  OG  SER A 298       3.966  68.706  60.967  1.00 18.86           O  
ATOM   2316  N   THR A 299       3.084  68.054  64.001  1.00 16.99           N  
ATOM   2317  CA  THR A 299       3.588  67.019  64.891  1.00 18.79           C  
ATOM   2318  C   THR A 299       3.912  65.735  64.124  1.00 21.16           C  
ATOM   2319  O   THR A 299       4.257  64.723  64.734  1.00 16.98           O  
ATOM   2320  CB  THR A 299       2.571  66.689  66.031  1.00 20.99           C  
ATOM   2321  OG1 THR A 299       1.378  66.121  65.473  1.00 18.43           O  
ATOM   2322  CG2 THR A 299       2.207  67.948  66.829  1.00 14.28           C  
ATOM   2323  N   LEU A 300       3.849  65.788  62.791  1.00 23.63           N  
ATOM   2324  CA  LEU A 300       4.100  64.611  61.945  1.00 24.29           C  
ATOM   2325  C   LEU A 300       5.498  64.475  61.343  1.00 23.98           C  
ATOM   2326  O   LEU A 300       5.839  63.423  60.796  1.00 25.27           O  
ATOM   2327  CB  LEU A 300       3.070  64.547  60.807  1.00 22.77           C  
ATOM   2328  CG  LEU A 300       1.645  64.149  61.179  1.00 18.35           C  
ATOM   2329  CD1 LEU A 300       0.740  64.350  59.981  1.00 24.67           C  
ATOM   2330  CD2 LEU A 300       1.609  62.711  61.638  1.00 16.28           C  
ATOM   2331  N   ILE A 301       6.313  65.515  61.477  1.00 22.17           N  
ATOM   2332  CA  ILE A 301       7.659  65.521  60.911  1.00 21.17           C  
ATOM   2333  C   ILE A 301       8.553  64.320  61.253  1.00 21.81           C  
ATOM   2334  O   ILE A 301       9.198  63.748  60.372  1.00 22.18           O  
ATOM   2335  CB  ILE A 301       8.381  66.843  61.259  1.00 20.18           C  
ATOM   2336  CG1 ILE A 301       7.663  68.003  60.562  1.00 16.92           C  
ATOM   2337  CG2 ILE A 301       9.843  66.786  60.846  1.00 19.64           C  
ATOM   2338  CD1 ILE A 301       7.970  69.379  61.129  1.00 19.58           C  
ATOM   2339  N   ASP A 302       8.560  63.902  62.511  1.00 23.12           N  
ATOM   2340  CA  ASP A 302       9.411  62.791  62.935  1.00 25.74           C  
ATOM   2341  C   ASP A 302       9.067  61.451  62.300  1.00 27.24           C  
ATOM   2342  O   ASP A 302       9.832  60.497  62.429  1.00 32.78           O  
ATOM   2343  CB  ASP A 302       9.444  62.656  64.466  1.00 30.58           C  
ATOM   2344  CG  ASP A 302      10.172  63.814  65.150  1.00 36.43           C  
ATOM   2345  OD1 ASP A 302      10.641  64.745  64.465  1.00 33.19           O  
ATOM   2346  OD2 ASP A 302      10.270  63.792  66.399  1.00 44.71           O  
ATOM   2347  N   LYS A 303       7.926  61.374  61.621  1.00 27.60           N  
ATOM   2348  CA  LYS A 303       7.533  60.131  60.960  1.00 30.06           C  
ATOM   2349  C   LYS A 303       8.215  59.915  59.605  1.00 30.23           C  
ATOM   2350  O   LYS A 303       8.100  58.833  59.023  1.00 33.82           O  
ATOM   2351  CB  LYS A 303       6.012  60.065  60.797  1.00 28.98           C  
ATOM   2352  CG  LYS A 303       5.292  59.685  62.076  1.00 34.66           C  
ATOM   2353  CD  LYS A 303       3.792  59.675  61.868  1.00 46.89           C  
ATOM   2354  CE  LYS A 303       3.070  59.140  63.104  1.00 52.75           C  
ATOM   2355  NZ  LYS A 303       1.583  59.250  62.987  1.00 53.41           N  
ATOM   2356  N   TYR A 304       8.956  60.914  59.128  1.00 26.03           N  
ATOM   2357  CA  TYR A 304       9.615  60.815  57.831  1.00 21.03           C  
ATOM   2358  C   TYR A 304      11.121  60.890  57.885  1.00 21.67           C  
ATOM   2359  O   TYR A 304      11.694  61.588  58.719  1.00 25.28           O  
ATOM   2360  CB  TYR A 304       9.118  61.916  56.890  1.00 15.63           C  
ATOM   2361  CG  TYR A 304       7.638  61.874  56.656  1.00 15.23           C  
ATOM   2362  CD1 TYR A 304       6.765  62.474  57.552  1.00 15.83           C  
ATOM   2363  CD2 TYR A 304       7.109  61.231  55.546  1.00 16.40           C  
ATOM   2364  CE1 TYR A 304       5.394  62.439  57.349  1.00 17.32           C  
ATOM   2365  CE2 TYR A 304       5.735  61.188  55.334  1.00 20.57           C  
ATOM   2366  CZ  TYR A 304       4.885  61.797  56.240  1.00 18.76           C  
ATOM   2367  OH  TYR A 304       3.529  61.783  56.034  1.00 17.88           O  
ATOM   2368  N   ASP A 305      11.763  60.171  56.973  1.00 18.44           N  
ATOM   2369  CA  ASP A 305      13.208  60.202  56.878  1.00 18.97           C  
ATOM   2370  C   ASP A 305      13.559  61.434  56.056  1.00 20.25           C  
ATOM   2371  O   ASP A 305      13.435  61.433  54.832  1.00 21.47           O  
ATOM   2372  CB  ASP A 305      13.732  58.926  56.204  1.00 20.69           C  
ATOM   2373  CG  ASP A 305      15.246  58.922  56.013  1.00 23.04           C  
ATOM   2374  OD1 ASP A 305      15.916  59.924  56.314  1.00 28.37           O  
ATOM   2375  OD2 ASP A 305      15.776  57.894  55.549  1.00 32.61           O  
ATOM   2376  N   LEU A 306      13.950  62.499  56.744  1.00 21.16           N  
ATOM   2377  CA  LEU A 306      14.333  63.739  56.088  1.00 21.09           C  
ATOM   2378  C   LEU A 306      15.835  63.974  56.233  1.00 22.98           C  
ATOM   2379  O   LEU A 306      16.284  65.115  56.333  1.00 25.19           O  
ATOM   2380  CB  LEU A 306      13.557  64.917  56.698  1.00 18.15           C  
ATOM   2381  CG  LEU A 306      12.029  64.815  56.738  1.00 19.68           C  
ATOM   2382  CD1 LEU A 306      11.447  66.021  57.455  1.00 17.12           C  
ATOM   2383  CD2 LEU A 306      11.482  64.703  55.320  1.00 15.90           C  
ATOM   2384  N   SER A 307      16.616  62.898  56.193  1.00 23.65           N  
ATOM   2385  CA  SER A 307      18.066  63.004  56.355  1.00 25.99           C  
ATOM   2386  C   SER A 307      18.783  63.927  55.374  1.00 27.19           C  
ATOM   2387  O   SER A 307      19.811  64.508  55.718  1.00 28.56           O  
ATOM   2388  CB  SER A 307      18.714  61.616  56.342  1.00 23.03           C  
ATOM   2389  OG  SER A 307      18.212  60.828  55.284  1.00 31.54           O  
ATOM   2390  N   ASN A 308      18.245  64.062  54.164  1.00 27.98           N  
ATOM   2391  CA  ASN A 308      18.853  64.910  53.136  1.00 24.45           C  
ATOM   2392  C   ASN A 308      18.491  66.379  53.258  1.00 22.69           C  
ATOM   2393  O   ASN A 308      19.192  67.234  52.716  1.00 22.17           O  
ATOM   2394  CB  ASN A 308      18.461  64.433  51.732  1.00 27.23           C  
ATOM   2395  CG  ASN A 308      19.112  63.121  51.353  1.00 33.06           C  
ATOM   2396  OD1 ASN A 308      20.295  63.078  51.014  1.00 36.37           O  
ATOM   2397  ND2 ASN A 308      18.346  62.038  51.417  1.00 37.06           N  
ATOM   2398  N   LEU A 309      17.381  66.678  53.931  1.00 21.07           N  
ATOM   2399  CA  LEU A 309      16.935  68.063  54.067  1.00 20.99           C  
ATOM   2400  C   LEU A 309      17.971  68.897  54.781  1.00 21.03           C  
ATOM   2401  O   LEU A 309      18.393  68.571  55.885  1.00 23.69           O  
ATOM   2402  CB  LEU A 309      15.592  68.163  54.799  1.00 20.23           C  
ATOM   2403  CG  LEU A 309      15.028  69.583  54.930  1.00 18.52           C  
ATOM   2404  CD1 LEU A 309      14.708  70.146  53.558  1.00 18.33           C  
ATOM   2405  CD2 LEU A 309      13.787  69.577  55.793  1.00 14.15           C  
ATOM   2406  N   HIS A 310      18.347  70.001  54.155  1.00 21.44           N  
ATOM   2407  CA  HIS A 310      19.338  70.884  54.724  1.00 24.41           C  
ATOM   2408  C   HIS A 310      18.858  72.328  54.781  1.00 26.10           C  
ATOM   2409  O   HIS A 310      19.197  73.070  55.703  1.00 29.44           O  
ATOM   2410  CB  HIS A 310      20.623  70.806  53.888  1.00 28.99           C  
ATOM   2411  CG  HIS A 310      21.685  71.765  54.325  1.00 35.58           C  
ATOM   2412  ND1 HIS A 310      21.830  73.018  53.766  1.00 37.63           N  
ATOM   2413  CD2 HIS A 310      22.642  71.666  55.280  1.00 34.95           C  
ATOM   2414  CE1 HIS A 310      22.830  73.650  54.360  1.00 35.70           C  
ATOM   2415  NE2 HIS A 310      23.335  72.849  55.280  1.00 35.44           N  
ATOM   2416  N   GLU A 311      18.062  72.729  53.800  1.00 25.51           N  
ATOM   2417  CA  GLU A 311      17.616  74.103  53.741  1.00 23.20           C  
ATOM   2418  C   GLU A 311      16.114  74.280  53.606  1.00 24.43           C  
ATOM   2419  O   GLU A 311      15.456  73.558  52.860  1.00 25.37           O  
ATOM   2420  CB  GLU A 311      18.325  74.815  52.575  1.00 25.36           C  
ATOM   2421  CG  GLU A 311      17.824  76.234  52.261  1.00 28.26           C  
ATOM   2422  CD  GLU A 311      18.403  76.817  50.966  1.00 32.55           C  
ATOM   2423  OE1 GLU A 311      19.128  76.114  50.226  1.00 34.15           O  
ATOM   2424  OE2 GLU A 311      18.117  77.995  50.671  1.00 33.61           O  
ATOM   2425  N   ILE A 312      15.574  75.216  54.383  1.00 23.95           N  
ATOM   2426  CA  ILE A 312      14.161  75.588  54.326  1.00 21.61           C  
ATOM   2427  C   ILE A 312      14.272  77.098  54.159  1.00 20.98           C  
ATOM   2428  O   ILE A 312      14.889  77.763  54.998  1.00 20.47           O  
ATOM   2429  CB  ILE A 312      13.405  75.228  55.603  1.00 20.08           C  
ATOM   2430  CG1 ILE A 312      13.421  73.711  55.798  1.00 22.95           C  
ATOM   2431  CG2 ILE A 312      11.957  75.704  55.507  1.00 22.51           C  
ATOM   2432  CD1 ILE A 312      12.653  73.223  57.002  1.00 21.51           C  
ATOM   2433  N   ALA A 313      13.718  77.639  53.079  1.00 19.76           N  
ATOM   2434  CA  ALA A 313      13.850  79.060  52.820  1.00 17.19           C  
ATOM   2435  C   ALA A 313      12.585  79.874  52.676  1.00 21.61           C  
ATOM   2436  O   ALA A 313      11.541  79.360  52.256  1.00 20.40           O  
ATOM   2437  CB  ALA A 313      14.739  79.267  51.594  1.00 21.13           C  
ATOM   2438  N   SER A 314      12.722  81.170  52.968  1.00 23.21           N  
ATOM   2439  CA  SER A 314      11.619  82.123  52.888  1.00 28.07           C  
ATOM   2440  C   SER A 314      11.819  83.173  51.798  1.00 29.39           C  
ATOM   2441  O   SER A 314      10.965  84.042  51.595  1.00 31.39           O  
ATOM   2442  CB  SER A 314      11.410  82.818  54.237  1.00 28.94           C  
ATOM   2443  OG  SER A 314      12.532  83.601  54.592  1.00 31.72           O  
ATOM   2444  N   GLY A 315      12.948  83.104  51.101  1.00 34.99           N  
ATOM   2445  CA  GLY A 315      13.214  84.045  50.023  1.00 36.62           C  
ATOM   2446  C   GLY A 315      13.295  85.489  50.468  1.00 38.95           C  
ATOM   2447  O   GLY A 315      14.057  85.811  51.382  1.00 42.79           O  
ATOM   2448  N   GLY A 316      12.510  86.355  49.834  1.00 37.76           N  
ATOM   2449  CA  GLY A 316      12.528  87.763  50.193  1.00 38.17           C  
ATOM   2450  C   GLY A 316      11.668  88.125  51.387  1.00 37.99           C  
ATOM   2451  O   GLY A 316      11.565  89.298  51.755  1.00 41.60           O  
ATOM   2452  N   ALA A 317      11.029  87.128  51.985  1.00 37.32           N  
ATOM   2453  CA  ALA A 317      10.168  87.366  53.134  1.00 41.94           C  
ATOM   2454  C   ALA A 317      10.874  87.160  54.474  1.00 42.12           C  
ATOM   2455  O   ALA A 317      11.381  86.064  54.754  1.00 43.83           O  
ATOM   2456  CB  ALA A 317       8.931  86.481  53.052  1.00 36.45           C  
ATOM   2457  N   PRO A 318      10.980  88.222  55.288  1.00 43.01           N  
ATOM   2458  CA  PRO A 318      11.628  88.156  56.605  1.00 40.56           C  
ATOM   2459  C   PRO A 318      10.717  87.366  57.560  1.00 37.71           C  
ATOM   2460  O   PRO A 318       9.498  87.382  57.401  1.00 36.99           O  
ATOM   2461  CB  PRO A 318      11.720  89.625  57.030  1.00 39.64           C  
ATOM   2462  CG  PRO A 318      11.740  90.371  55.723  1.00 41.49           C  
ATOM   2463  CD  PRO A 318      10.704  89.632  54.916  1.00 43.41           C  
ATOM   2464  N   LEU A 319      11.293  86.665  58.525  1.00 38.13           N  
ATOM   2465  CA  LEU A 319      10.491  85.885  59.468  1.00 41.08           C  
ATOM   2466  C   LEU A 319      10.828  86.264  60.898  1.00 41.73           C  
ATOM   2467  O   LEU A 319      11.956  86.672  61.185  1.00 41.97           O  
ATOM   2468  CB  LEU A 319      10.735  84.386  59.273  1.00 42.16           C  
ATOM   2469  CG  LEU A 319      10.343  83.774  57.929  1.00 43.51           C  
ATOM   2470  CD1 LEU A 319      10.821  82.348  57.883  1.00 42.09           C  
ATOM   2471  CD2 LEU A 319       8.840  83.842  57.725  1.00 44.02           C  
ATOM   2472  N   SER A 320       9.860  86.114  61.799  1.00 41.11           N  
ATOM   2473  CA  SER A 320      10.092  86.444  63.201  1.00 41.49           C  
ATOM   2474  C   SER A 320      11.072  85.432  63.764  1.00 40.64           C  
ATOM   2475  O   SER A 320      11.093  84.274  63.339  1.00 41.10           O  
ATOM   2476  CB  SER A 320       8.785  86.419  64.003  1.00 42.84           C  
ATOM   2477  OG  SER A 320       8.269  85.107  64.134  1.00 45.77           O  
ATOM   2478  N   LYS A 321      11.890  85.869  64.712  1.00 40.71           N  
ATOM   2479  CA  LYS A 321      12.863  84.984  65.320  1.00 42.59           C  
ATOM   2480  C   LYS A 321      12.158  83.743  65.882  1.00 45.44           C  
ATOM   2481  O   LYS A 321      12.658  82.622  65.752  1.00 47.63           O  
ATOM   2482  CB  LYS A 321      13.629  85.726  66.418  1.00 41.99           C  
ATOM   2483  CG  LYS A 321      14.639  84.864  67.153  1.00 49.09           C  
ATOM   2484  CD  LYS A 321      15.347  85.627  68.261  1.00 51.55           C  
ATOM   2485  CE  LYS A 321      15.784  84.674  69.360  1.00 55.45           C  
ATOM   2486  NZ  LYS A 321      16.794  85.273  70.267  1.00 63.51           N  
ATOM   2487  N   GLU A 322      10.963  83.945  66.435  1.00 42.87           N  
ATOM   2488  CA  GLU A 322      10.177  82.859  67.020  1.00 42.30           C  
ATOM   2489  C   GLU A 322       9.774  81.789  66.005  1.00 38.50           C  
ATOM   2490  O   GLU A 322      10.048  80.605  66.201  1.00 37.95           O  
ATOM   2491  CB  GLU A 322       8.923  83.413  67.712  1.00 44.43           C  
ATOM   2492  CG  GLU A 322       9.186  84.164  69.022  1.00 51.10           C  
ATOM   2493  CD  GLU A 322       9.982  85.448  68.834  1.00 54.37           C  
ATOM   2494  OE1 GLU A 322       9.714  86.196  67.867  1.00 54.73           O  
ATOM   2495  OE2 GLU A 322      10.877  85.713  69.664  1.00 59.22           O  
ATOM   2496  N   VAL A 323       9.141  82.211  64.914  1.00 38.33           N  
ATOM   2497  CA  VAL A 323       8.698  81.282  63.875  1.00 36.17           C  
ATOM   2498  C   VAL A 323       9.880  80.549  63.236  1.00 35.34           C  
ATOM   2499  O   VAL A 323       9.843  79.328  63.073  1.00 36.32           O  
ATOM   2500  CB  VAL A 323       7.863  82.000  62.790  1.00 35.46           C  
ATOM   2501  CG1 VAL A 323       7.475  81.026  61.691  1.00 35.58           C  
ATOM   2502  CG2 VAL A 323       6.606  82.598  63.409  1.00 32.04           C  
ATOM   2503  N   GLY A 324      10.938  81.283  62.907  1.00 34.71           N  
ATOM   2504  CA  GLY A 324      12.110  80.660  62.318  1.00 30.10           C  
ATOM   2505  C   GLY A 324      12.678  79.565  63.209  1.00 31.71           C  
ATOM   2506  O   GLY A 324      12.901  78.435  62.761  1.00 29.12           O  
ATOM   2507  N   GLU A 325      12.896  79.896  64.481  1.00 31.69           N  
ATOM   2508  CA  GLU A 325      13.436  78.939  65.445  1.00 31.26           C  
ATOM   2509  C   GLU A 325      12.508  77.747  65.662  1.00 27.19           C  
ATOM   2510  O   GLU A 325      12.966  76.617  65.844  1.00 23.24           O  
ATOM   2511  CB  GLU A 325      13.695  79.613  66.794  1.00 38.71           C  
ATOM   2512  CG  GLU A 325      14.762  80.692  66.781  1.00 49.31           C  
ATOM   2513  CD  GLU A 325      14.996  81.303  68.157  1.00 54.23           C  
ATOM   2514  OE1 GLU A 325      14.013  81.509  68.912  1.00 57.63           O  
ATOM   2515  OE2 GLU A 325      16.172  81.578  68.479  1.00 55.12           O  
ATOM   2516  N   ALA A 326      11.207  78.011  65.693  1.00 22.36           N  
ATOM   2517  CA  ALA A 326      10.222  76.959  65.896  1.00 22.67           C  
ATOM   2518  C   ALA A 326      10.293  75.945  64.754  1.00 21.15           C  
ATOM   2519  O   ALA A 326      10.362  74.738  64.980  1.00 21.86           O  
ATOM   2520  CB  ALA A 326       8.830  77.564  65.991  1.00 16.55           C  
ATOM   2521  N   VAL A 327      10.328  76.450  63.529  1.00 21.01           N  
ATOM   2522  CA  VAL A 327      10.400  75.599  62.353  1.00 20.57           C  
ATOM   2523  C   VAL A 327      11.718  74.817  62.319  1.00 21.64           C  
ATOM   2524  O   VAL A 327      11.713  73.592  62.148  1.00 22.33           O  
ATOM   2525  CB  VAL A 327      10.194  76.433  61.079  1.00 18.84           C  
ATOM   2526  CG1 VAL A 327      10.315  75.569  59.840  1.00 23.12           C  
ATOM   2527  CG2 VAL A 327       8.827  77.073  61.122  1.00 17.21           C  
ATOM   2528  N   ALA A 328      12.838  75.506  62.537  1.00 22.25           N  
ATOM   2529  CA  ALA A 328      14.146  74.848  62.544  1.00 22.52           C  
ATOM   2530  C   ALA A 328      14.177  73.728  63.590  1.00 22.37           C  
ATOM   2531  O   ALA A 328      14.670  72.635  63.321  1.00 25.09           O  
ATOM   2532  CB  ALA A 328      15.261  75.863  62.804  1.00 20.15           C  
ATOM   2533  N   LYS A 329      13.606  73.988  64.763  1.00 25.59           N  
ATOM   2534  CA  LYS A 329      13.559  72.996  65.836  1.00 25.22           C  
ATOM   2535  C   LYS A 329      12.729  71.791  65.397  1.00 24.61           C  
ATOM   2536  O   LYS A 329      13.137  70.645  65.603  1.00 25.54           O  
ATOM   2537  CB  LYS A 329      12.975  73.614  67.114  1.00 27.57           C  
ATOM   2538  CG  LYS A 329      13.156  72.781  68.377  1.00 27.88           C  
ATOM   2539  CD  LYS A 329      12.619  73.526  69.591  1.00 29.35           C  
ATOM   2540  CE  LYS A 329      12.935  72.792  70.883  1.00 34.39           C  
ATOM   2541  NZ  LYS A 329      12.265  71.469  70.957  1.00 35.03           N  
ATOM   2542  N   ARG A 330      11.586  72.051  64.762  1.00 21.96           N  
ATOM   2543  CA  ARG A 330      10.714  70.977  64.284  1.00 20.93           C  
ATOM   2544  C   ARG A 330      11.420  70.097  63.252  1.00 21.72           C  
ATOM   2545  O   ARG A 330      11.249  68.874  63.231  1.00 21.55           O  
ATOM   2546  CB  ARG A 330       9.449  71.553  63.654  1.00 22.26           C  
ATOM   2547  CG  ARG A 330       8.420  72.108  64.622  1.00 23.13           C  
ATOM   2548  CD  ARG A 330       7.693  71.012  65.376  1.00 21.62           C  
ATOM   2549  NE  ARG A 330       6.439  71.511  65.939  1.00 24.70           N  
ATOM   2550  CZ  ARG A 330       5.727  70.888  66.873  1.00 24.78           C  
ATOM   2551  NH1 ARG A 330       6.143  69.729  67.369  1.00 25.47           N  
ATOM   2552  NH2 ARG A 330       4.583  71.405  67.289  1.00 21.46           N  
ATOM   2553  N   PHE A 331      12.214  70.721  62.394  1.00 21.42           N  
ATOM   2554  CA  PHE A 331      12.928  69.979  61.369  1.00 22.56           C  
ATOM   2555  C   PHE A 331      14.346  69.604  61.771  1.00 26.68           C  
ATOM   2556  O   PHE A 331      15.132  69.152  60.939  1.00 29.82           O  
ATOM   2557  CB  PHE A 331      12.937  70.758  60.060  1.00 18.50           C  
ATOM   2558  CG  PHE A 331      11.622  70.736  59.334  1.00 20.19           C  
ATOM   2559  CD1 PHE A 331      11.305  69.676  58.484  1.00 17.38           C  
ATOM   2560  CD2 PHE A 331      10.711  71.782  59.477  1.00 18.61           C  
ATOM   2561  CE1 PHE A 331      10.105  69.658  57.786  1.00 18.18           C  
ATOM   2562  CE2 PHE A 331       9.505  71.775  58.785  1.00 17.75           C  
ATOM   2563  CZ  PHE A 331       9.202  70.710  57.936  1.00 18.51           C  
ATOM   2564  N   HIS A 332      14.669  69.786  63.049  1.00 27.89           N  
ATOM   2565  CA  HIS A 332      15.989  69.450  63.587  1.00 27.32           C  
ATOM   2566  C   HIS A 332      17.130  70.041  62.768  1.00 22.56           C  
ATOM   2567  O   HIS A 332      18.088  69.354  62.439  1.00 27.09           O  
ATOM   2568  CB  HIS A 332      16.152  67.929  63.694  1.00 26.52           C  
ATOM   2569  CG  HIS A 332      14.971  67.240  64.303  1.00 32.89           C  
ATOM   2570  ND1 HIS A 332      14.595  67.428  65.615  1.00 40.40           N  
ATOM   2571  CD2 HIS A 332      14.047  66.410  63.762  1.00 33.75           C  
ATOM   2572  CE1 HIS A 332      13.487  66.748  65.857  1.00 40.96           C  
ATOM   2573  NE2 HIS A 332      13.135  66.123  64.749  1.00 39.05           N  
ATOM   2574  N   LEU A 333      17.020  71.320  62.444  1.00 24.26           N  
ATOM   2575  CA  LEU A 333      18.041  72.011  61.668  1.00 25.46           C  
ATOM   2576  C   LEU A 333      18.583  73.152  62.522  1.00 27.86           C  
ATOM   2577  O   LEU A 333      17.844  73.728  63.320  1.00 28.45           O  
ATOM   2578  CB  LEU A 333      17.434  72.559  60.370  1.00 23.57           C  
ATOM   2579  CG  LEU A 333      16.878  71.503  59.401  1.00 23.23           C  
ATOM   2580  CD1 LEU A 333      16.202  72.178  58.230  1.00 19.54           C  
ATOM   2581  CD2 LEU A 333      17.988  70.575  58.929  1.00 20.01           C  
ATOM   2582  N   PRO A 334      19.873  73.512  62.350  1.00 32.68           N  
ATOM   2583  CA  PRO A 334      20.481  74.598  63.133  1.00 32.82           C  
ATOM   2584  C   PRO A 334      19.827  75.961  62.913  1.00 33.18           C  
ATOM   2585  O   PRO A 334      19.945  76.853  63.751  1.00 39.95           O  
ATOM   2586  CB  PRO A 334      21.939  74.584  62.663  1.00 27.45           C  
ATOM   2587  CG  PRO A 334      21.835  74.102  61.258  1.00 31.71           C  
ATOM   2588  CD  PRO A 334      20.846  72.967  61.384  1.00 34.33           C  
ATOM   2589  N   GLY A 335      19.131  76.115  61.793  1.00 33.30           N  
ATOM   2590  CA  GLY A 335      18.474  77.370  61.489  1.00 28.68           C  
ATOM   2591  C   GLY A 335      17.750  77.236  60.172  1.00 31.32           C  
ATOM   2592  O   GLY A 335      17.653  76.131  59.631  1.00 31.83           O  
ATOM   2593  N   ILE A 336      17.216  78.341  59.672  1.00 30.01           N  
ATOM   2594  CA  ILE A 336      16.517  78.349  58.398  1.00 32.36           C  
ATOM   2595  C   ILE A 336      17.105  79.494  57.571  1.00 32.61           C  
ATOM   2596  O   ILE A 336      17.728  80.407  58.121  1.00 34.60           O  
ATOM   2597  CB  ILE A 336      14.994  78.591  58.566  1.00 31.91           C  
ATOM   2598  CG1 ILE A 336      14.740  79.967  59.171  1.00 31.25           C  
ATOM   2599  CG2 ILE A 336      14.361  77.488  59.400  1.00 29.97           C  
ATOM   2600  CD1 ILE A 336      13.524  80.620  58.619  1.00 36.13           C  
ATOM   2601  N   ARG A 337      16.939  79.434  56.256  1.00 30.23           N  
ATOM   2602  CA  ARG A 337      17.445  80.501  55.418  1.00 29.44           C  
ATOM   2603  C   ARG A 337      16.353  81.490  55.075  1.00 29.03           C  
ATOM   2604  O   ARG A 337      15.328  81.137  54.505  1.00 34.34           O  
ATOM   2605  CB  ARG A 337      18.067  79.989  54.124  1.00 25.82           C  
ATOM   2606  CG  ARG A 337      18.268  81.121  53.115  1.00 27.38           C  
ATOM   2607  CD  ARG A 337      19.063  80.702  51.924  1.00 24.27           C  
ATOM   2608  NE  ARG A 337      20.488  80.934  52.114  1.00 27.00           N  
ATOM   2609  CZ  ARG A 337      21.442  80.296  51.445  1.00 26.76           C  
ATOM   2610  NH1 ARG A 337      21.125  79.362  50.555  1.00 27.69           N  
ATOM   2611  NH2 ARG A 337      22.704  80.665  51.587  1.00 27.68           N  
ATOM   2612  N   GLN A 338      16.571  82.740  55.427  1.00 31.68           N  
ATOM   2613  CA  GLN A 338      15.605  83.756  55.106  1.00 33.03           C  
ATOM   2614  C   GLN A 338      16.373  84.860  54.444  1.00 31.31           C  
ATOM   2615  O   GLN A 338      17.576  84.730  54.203  1.00 31.68           O  
ATOM   2616  CB  GLN A 338      14.874  84.248  56.353  1.00 37.98           C  
ATOM   2617  CG  GLN A 338      15.752  84.688  57.505  1.00 42.15           C  
ATOM   2618  CD  GLN A 338      14.924  85.264  58.623  1.00 42.90           C  
ATOM   2619  OE1 GLN A 338      14.053  86.102  58.391  1.00 46.78           O  
ATOM   2620  NE2 GLN A 338      15.159  84.798  59.836  1.00 46.28           N  
ATOM   2621  N   GLY A 339      15.674  85.925  54.099  1.00 32.80           N  
ATOM   2622  CA  GLY A 339      16.316  87.042  53.457  1.00 33.06           C  
ATOM   2623  C   GLY A 339      15.314  88.147  53.264  1.00 32.39           C  
ATOM   2624  O   GLY A 339      14.121  87.992  53.555  1.00 33.26           O  
ATOM   2625  N   TYR A 340      15.801  89.277  52.780  1.00 29.85           N  
ATOM   2626  CA  TYR A 340      14.942  90.408  52.541  1.00 28.97           C  
ATOM   2627  C   TYR A 340      15.040  90.754  51.077  1.00 25.87           C  
ATOM   2628  O   TYR A 340      16.138  90.908  50.543  1.00 29.12           O  
ATOM   2629  CB  TYR A 340      15.376  91.590  53.399  1.00 29.77           C  
ATOM   2630  CG  TYR A 340      14.531  92.809  53.184  1.00 31.51           C  
ATOM   2631  CD1 TYR A 340      13.372  93.015  53.928  1.00 33.61           C  
ATOM   2632  CD2 TYR A 340      14.881  93.757  52.227  1.00 32.08           C  
ATOM   2633  CE1 TYR A 340      12.577  94.142  53.727  1.00 34.28           C  
ATOM   2634  CE2 TYR A 340      14.093  94.887  52.015  1.00 38.98           C  
ATOM   2635  CZ  TYR A 340      12.943  95.075  52.771  1.00 37.45           C  
ATOM   2636  OH  TYR A 340      12.182  96.208  52.586  1.00 38.97           O  
ATOM   2637  N   GLY A 341      13.890  90.851  50.427  1.00 28.63           N  
ATOM   2638  CA  GLY A 341      13.859  91.182  49.019  1.00 26.35           C  
ATOM   2639  C   GLY A 341      12.517  91.764  48.659  1.00 25.46           C  
ATOM   2640  O   GLY A 341      11.539  91.569  49.377  1.00 28.58           O  
ATOM   2641  N   LEU A 342      12.487  92.511  47.565  1.00 26.59           N  
ATOM   2642  CA  LEU A 342      11.269  93.134  47.078  1.00 27.02           C  
ATOM   2643  C   LEU A 342      11.129  92.715  45.629  1.00 28.86           C  
ATOM   2644  O   LEU A 342      12.091  92.253  45.018  1.00 28.14           O  
ATOM   2645  CB  LEU A 342      11.375  94.665  47.118  1.00 26.32           C  
ATOM   2646  CG  LEU A 342      11.629  95.384  48.443  1.00 33.75           C  
ATOM   2647  CD1 LEU A 342      11.723  96.881  48.168  1.00 29.39           C  
ATOM   2648  CD2 LEU A 342      10.521  95.072  49.450  1.00 31.18           C  
ATOM   2649  N   THR A 343       9.934  92.882  45.079  1.00 27.20           N  
ATOM   2650  CA  THR A 343       9.706  92.566  43.678  1.00 30.92           C  
ATOM   2651  C   THR A 343      10.643  93.499  42.904  1.00 30.50           C  
ATOM   2652  O   THR A 343      11.257  93.111  41.915  1.00 31.09           O  
ATOM   2653  CB  THR A 343       8.258  92.886  43.278  1.00 29.82           C  
ATOM   2654  OG1 THR A 343       7.358  92.227  44.178  1.00 35.23           O  
ATOM   2655  CG2 THR A 343       7.984  92.433  41.861  1.00 25.07           C  
ATOM   2656  N   GLU A 344      10.810  94.697  43.457  1.00 28.64           N  
ATOM   2657  CA  GLU A 344      11.641  95.747  42.896  1.00 27.82           C  
ATOM   2658  C   GLU A 344      13.150  95.479  42.956  1.00 28.60           C  
ATOM   2659  O   GLU A 344      13.944  96.281  42.449  1.00 28.13           O  
ATOM   2660  CB  GLU A 344      11.314  97.085  43.574  1.00 30.34           C  
ATOM   2661  CG  GLU A 344       9.904  97.651  43.279  1.00 31.89           C  
ATOM   2662  CD  GLU A 344       8.788  97.063  44.153  1.00 33.48           C  
ATOM   2663  OE1 GLU A 344       9.049  96.133  44.944  1.00 33.72           O  
ATOM   2664  OE2 GLU A 344       7.636  97.539  44.055  1.00 32.10           O  
ATOM   2665  N   THR A 345      13.552  94.399  43.624  1.00 28.84           N  
ATOM   2666  CA  THR A 345      14.970  94.049  43.707  1.00 27.93           C  
ATOM   2667  C   THR A 345      15.201  92.684  43.057  1.00 24.18           C  
ATOM   2668  O   THR A 345      16.255  92.068  43.245  1.00 24.65           O  
ATOM   2669  CB  THR A 345      15.503  94.027  45.181  1.00 27.65           C  
ATOM   2670  OG1 THR A 345      14.830  93.016  45.944  1.00 21.61           O  
ATOM   2671  CG2 THR A 345      15.307  95.382  45.852  1.00 27.19           C  
ATOM   2672  N   THR A 346      14.214  92.230  42.285  1.00 26.74           N  
ATOM   2673  CA  THR A 346      14.256  90.928  41.610  1.00 26.51           C  
ATOM   2674  C   THR A 346      14.084  89.802  42.642  1.00 24.41           C  
ATOM   2675  O   THR A 346      13.070  89.081  42.633  1.00 23.72           O  
ATOM   2676  CB  THR A 346      15.563  90.756  40.769  1.00 23.73           C  
ATOM   2677  OG1 THR A 346      15.620  91.772  39.763  1.00 20.33           O  
ATOM   2678  CG2 THR A 346      15.610  89.394  40.083  1.00 21.68           C  
ATOM   2679  N   SER A 347      15.042  89.674  43.553  1.00 23.13           N  
ATOM   2680  CA  SER A 347      14.985  88.673  44.603  1.00 26.42           C  
ATOM   2681  C   SER A 347      15.654  89.185  45.880  1.00 27.00           C  
ATOM   2682  O   SER A 347      15.846  90.398  46.048  1.00 27.15           O  
ATOM   2683  CB  SER A 347      15.590  87.346  44.121  1.00 29.32           C  
ATOM   2684  OG  SER A 347      16.827  87.539  43.461  1.00 36.36           O  
ATOM   2685  N   ALA A 348      15.983  88.291  46.804  1.00 27.85           N  
ATOM   2686  CA  ALA A 348      16.594  88.685  48.062  1.00 29.61           C  
ATOM   2687  C   ALA A 348      17.972  89.326  47.895  1.00 29.77           C  
ATOM   2688  O   ALA A 348      18.850  88.779  47.237  1.00 31.07           O  
ATOM   2689  CB  ALA A 348      16.672  87.493  49.011  1.00 22.46           C  
ATOM   2690  N   ILE A 349      18.135  90.497  48.501  1.00 27.44           N  
ATOM   2691  CA  ILE A 349      19.395  91.243  48.454  1.00 30.08           C  
ATOM   2692  C   ILE A 349      20.127  91.123  49.794  1.00 31.12           C  
ATOM   2693  O   ILE A 349      21.289  91.520  49.924  1.00 29.44           O  
ATOM   2694  CB  ILE A 349      19.138  92.708  48.108  1.00 33.66           C  
ATOM   2695  CG1 ILE A 349      18.028  93.262  49.014  1.00 34.67           C  
ATOM   2696  CG2 ILE A 349      18.798  92.835  46.627  1.00 28.40           C  
ATOM   2697  CD1 ILE A 349      17.447  94.543  48.579  1.00 40.38           C  
ATOM   2698  N   LEU A 350      19.407  90.627  50.797  1.00 31.47           N  
ATOM   2699  CA  LEU A 350      19.953  90.367  52.120  1.00 29.12           C  
ATOM   2700  C   LEU A 350      19.568  88.901  52.278  1.00 28.41           C  
ATOM   2701  O   LEU A 350      18.397  88.559  52.143  1.00 27.41           O  
ATOM   2702  CB  LEU A 350      19.272  91.227  53.188  1.00 27.55           C  
ATOM   2703  CG  LEU A 350      19.458  92.744  53.081  1.00 30.61           C  
ATOM   2704  CD1 LEU A 350      18.744  93.441  54.236  1.00 27.22           C  
ATOM   2705  CD2 LEU A 350      20.941  93.087  53.080  1.00 27.42           C  
ATOM   2706  N   ILE A 351      20.554  88.035  52.475  1.00 29.20           N  
ATOM   2707  CA  ILE A 351      20.315  86.604  52.587  1.00 30.70           C  
ATOM   2708  C   ILE A 351      21.133  85.999  53.717  1.00 32.77           C  
ATOM   2709  O   ILE A 351      22.228  86.481  54.008  1.00 36.69           O  
ATOM   2710  CB  ILE A 351      20.725  85.897  51.256  1.00 29.08           C  
ATOM   2711  CG1 ILE A 351      19.799  86.333  50.116  1.00 32.13           C  
ATOM   2712  CG2 ILE A 351      20.719  84.385  51.423  1.00 29.38           C  
ATOM   2713  CD1 ILE A 351      20.117  85.683  48.778  1.00 29.34           C  
ATOM   2714  N   THR A 352      20.587  84.969  54.366  1.00 33.54           N  
ATOM   2715  CA  THR A 352      21.283  84.257  55.445  1.00 33.23           C  
ATOM   2716  C   THR A 352      22.436  83.459  54.823  1.00 35.85           C  
ATOM   2717  O   THR A 352      22.203  82.521  54.059  1.00 37.03           O  
ATOM   2718  CB  THR A 352      20.349  83.250  56.144  1.00 27.88           C  
ATOM   2719  OG1 THR A 352      19.189  83.933  56.632  1.00 31.29           O  
ATOM   2720  CG2 THR A 352      21.069  82.546  57.290  1.00 20.41           C  
ATOM   2721  N   PRO A 353      23.693  83.837  55.127  1.00 37.33           N  
ATOM   2722  CA  PRO A 353      24.857  83.130  54.576  1.00 38.81           C  
ATOM   2723  C   PRO A 353      25.042  81.742  55.184  1.00 40.57           C  
ATOM   2724  O   PRO A 353      24.795  81.536  56.380  1.00 42.87           O  
ATOM   2725  CB  PRO A 353      26.029  84.048  54.961  1.00 36.47           C  
ATOM   2726  CG  PRO A 353      25.395  85.383  55.185  1.00 39.29           C  
ATOM   2727  CD  PRO A 353      24.122  85.014  55.891  1.00 39.50           C  
ATOM   2728  N   GLU A 354      25.464  80.789  54.357  1.00 40.03           N  
ATOM   2729  CA  GLU A 354      25.712  79.433  54.824  1.00 42.88           C  
ATOM   2730  C   GLU A 354      26.823  79.511  55.864  1.00 47.26           C  
ATOM   2731  O   GLU A 354      27.845  80.156  55.636  1.00 48.11           O  
ATOM   2732  CB  GLU A 354      26.145  78.535  53.662  1.00 43.50           C  
ATOM   2733  CG  GLU A 354      26.457  77.099  54.058  1.00 46.30           C  
ATOM   2734  CD  GLU A 354      25.233  76.340  54.540  1.00 46.54           C  
ATOM   2735  OE1 GLU A 354      24.235  76.281  53.791  1.00 48.27           O  
ATOM   2736  OE2 GLU A 354      25.272  75.803  55.666  1.00 43.78           O  
ATOM   2737  N   GLY A 355      26.596  78.898  57.021  1.00 49.84           N  
ATOM   2738  CA  GLY A 355      27.584  78.916  58.087  1.00 52.77           C  
ATOM   2739  C   GLY A 355      27.759  80.238  58.825  1.00 53.99           C  
ATOM   2740  O   GLY A 355      28.599  80.337  59.719  1.00 56.88           O  
ATOM   2741  N   ASP A 356      26.938  81.232  58.500  1.00 55.19           N  
ATOM   2742  CA  ASP A 356      27.031  82.547  59.135  1.00 53.49           C  
ATOM   2743  C   ASP A 356      25.645  82.971  59.653  1.00 53.06           C  
ATOM   2744  O   ASP A 356      25.170  84.088  59.402  1.00 49.59           O  
ATOM   2745  CB  ASP A 356      27.573  83.560  58.111  1.00 55.33           C  
ATOM   2746  CG  ASP A 356      28.262  84.763  58.747  1.00 55.44           C  
ATOM   2747  OD1 ASP A 356      28.179  84.953  59.983  1.00 57.61           O  
ATOM   2748  OD2 ASP A 356      28.894  85.531  57.990  1.00 54.33           O  
ATOM   2749  N   ASP A 357      24.995  82.059  60.370  1.00 55.12           N  
ATOM   2750  CA  ASP A 357      23.671  82.322  60.924  1.00 56.58           C  
ATOM   2751  C   ASP A 357      23.810  83.096  62.236  1.00 57.40           C  
ATOM   2752  O   ASP A 357      24.785  82.917  62.970  1.00 58.25           O  
ATOM   2753  CB  ASP A 357      22.928  80.995  61.151  1.00 57.04           C  
ATOM   2754  CG  ASP A 357      21.456  81.190  61.495  1.00 58.95           C  
ATOM   2755  OD1 ASP A 357      20.853  82.205  61.071  1.00 55.06           O  
ATOM   2756  OD2 ASP A 357      20.901  80.309  62.190  1.00 56.92           O  
ATOM   2757  N   LYS A 358      22.859  83.987  62.497  1.00 56.70           N  
ATOM   2758  CA  LYS A 358      22.847  84.796  63.714  1.00 54.41           C  
ATOM   2759  C   LYS A 358      21.384  84.987  64.092  1.00 53.04           C  
ATOM   2760  O   LYS A 358      20.578  85.434  63.273  1.00 54.99           O  
ATOM   2761  CB  LYS A 358      23.505  86.151  63.452  1.00 55.15           C  
ATOM   2762  CG  LYS A 358      23.800  86.972  64.696  1.00 56.13           C  
ATOM   2763  CD  LYS A 358      24.557  88.215  64.304  1.00 56.69           C  
ATOM   2764  CE  LYS A 358      25.423  88.737  65.421  1.00 56.88           C  
ATOM   2765  NZ  LYS A 358      26.513  89.589  64.859  1.00 56.08           N  
ATOM   2766  N   PRO A 359      21.015  84.632  65.329  1.00 50.04           N  
ATOM   2767  CA  PRO A 359      19.644  84.748  65.835  1.00 48.19           C  
ATOM   2768  C   PRO A 359      18.988  86.107  65.602  1.00 45.81           C  
ATOM   2769  O   PRO A 359      19.509  87.136  66.029  1.00 44.92           O  
ATOM   2770  CB  PRO A 359      19.812  84.462  67.325  1.00 48.08           C  
ATOM   2771  CG  PRO A 359      20.944  83.492  67.343  1.00 49.41           C  
ATOM   2772  CD  PRO A 359      21.913  84.117  66.378  1.00 48.89           C  
ATOM   2773  N   GLY A 360      17.858  86.102  64.903  1.00 45.48           N  
ATOM   2774  CA  GLY A 360      17.133  87.336  64.644  1.00 45.85           C  
ATOM   2775  C   GLY A 360      17.568  88.163  63.444  1.00 45.52           C  
ATOM   2776  O   GLY A 360      16.861  89.093  63.035  1.00 44.65           O  
ATOM   2777  N   ALA A 361      18.734  87.851  62.889  1.00 44.31           N  
ATOM   2778  CA  ALA A 361      19.238  88.582  61.733  1.00 41.88           C  
ATOM   2779  C   ALA A 361      18.568  88.089  60.458  1.00 40.92           C  
ATOM   2780  O   ALA A 361      18.284  86.893  60.315  1.00 37.94           O  
ATOM   2781  CB  ALA A 361      20.744  88.420  61.627  1.00 38.94           C  
ATOM   2782  N   VAL A 362      18.285  89.016  59.550  1.00 39.17           N  
ATOM   2783  CA  VAL A 362      17.667  88.657  58.279  1.00 39.46           C  
ATOM   2784  C   VAL A 362      18.733  88.135  57.304  1.00 39.41           C  
ATOM   2785  O   VAL A 362      18.422  87.404  56.368  1.00 40.48           O  
ATOM   2786  CB  VAL A 362      16.905  89.859  57.658  1.00 39.11           C  
ATOM   2787  CG1 VAL A 362      17.864  90.845  57.008  1.00 35.12           C  
ATOM   2788  CG2 VAL A 362      15.863  89.366  56.666  1.00 37.41           C  
ATOM   2789  N   GLY A 363      19.988  88.511  57.535  1.00 38.17           N  
ATOM   2790  CA  GLY A 363      21.068  88.068  56.675  1.00 37.30           C  
ATOM   2791  C   GLY A 363      22.112  89.143  56.433  1.00 39.09           C  
ATOM   2792  O   GLY A 363      22.282  90.050  57.254  1.00 38.70           O  
ATOM   2793  N   LYS A 364      22.820  89.031  55.309  1.00 39.09           N  
ATOM   2794  CA  LYS A 364      23.859  89.985  54.922  1.00 34.30           C  
ATOM   2795  C   LYS A 364      23.679  90.399  53.467  1.00 34.91           C  
ATOM   2796  O   LYS A 364      23.009  89.709  52.699  1.00 37.51           O  
ATOM   2797  CB  LYS A 364      25.246  89.371  55.100  1.00 30.64           C  
ATOM   2798  CG  LYS A 364      25.635  89.106  56.533  1.00 31.65           C  
ATOM   2799  CD  LYS A 364      27.101  88.752  56.619  1.00 32.63           C  
ATOM   2800  CE  LYS A 364      27.594  88.849  58.042  1.00 30.93           C  
ATOM   2801  NZ  LYS A 364      29.036  88.520  58.141  1.00 34.76           N  
ATOM   2802  N   VAL A 365      24.248  91.544  53.102  1.00 33.79           N  
ATOM   2803  CA  VAL A 365      24.164  92.049  51.735  1.00 33.15           C  
ATOM   2804  C   VAL A 365      24.784  91.055  50.754  1.00 33.45           C  
ATOM   2805  O   VAL A 365      25.912  90.587  50.957  1.00 34.32           O  
ATOM   2806  CB  VAL A 365      24.876  93.411  51.594  1.00 30.78           C  
ATOM   2807  CG1 VAL A 365      24.737  93.933  50.195  1.00 32.70           C  
ATOM   2808  CG2 VAL A 365      24.281  94.405  52.555  1.00 34.74           C  
ATOM   2809  N   VAL A 366      24.030  90.739  49.703  1.00 32.49           N  
ATOM   2810  CA  VAL A 366      24.461  89.799  48.672  1.00 30.79           C  
ATOM   2811  C   VAL A 366      25.483  90.425  47.727  1.00 34.01           C  
ATOM   2812  O   VAL A 366      25.529  91.654  47.570  1.00 34.15           O  
ATOM   2813  CB  VAL A 366      23.262  89.305  47.825  1.00 26.81           C  
ATOM   2814  CG1 VAL A 366      22.262  88.586  48.708  1.00 20.90           C  
ATOM   2815  CG2 VAL A 366      22.602  90.479  47.087  1.00 22.36           C  
ATOM   2816  N   PRO A 367      26.328  89.584  47.092  1.00 31.82           N  
ATOM   2817  CA  PRO A 367      27.353  90.046  46.151  1.00 27.50           C  
ATOM   2818  C   PRO A 367      26.709  90.945  45.108  1.00 27.19           C  
ATOM   2819  O   PRO A 367      25.546  90.738  44.751  1.00 30.72           O  
ATOM   2820  CB  PRO A 367      27.837  88.742  45.528  1.00 25.20           C  
ATOM   2821  CG  PRO A 367      27.771  87.800  46.669  1.00 23.91           C  
ATOM   2822  CD  PRO A 367      26.429  88.127  47.295  1.00 29.37           C  
ATOM   2823  N   PHE A 368      27.467  91.933  44.635  1.00 26.43           N  
ATOM   2824  CA  PHE A 368      27.017  92.911  43.637  1.00 27.62           C  
ATOM   2825  C   PHE A 368      26.191  94.037  44.253  1.00 28.97           C  
ATOM   2826  O   PHE A 368      25.937  95.052  43.594  1.00 27.78           O  
ATOM   2827  CB  PHE A 368      26.181  92.263  42.519  1.00 28.53           C  
ATOM   2828  CG  PHE A 368      26.930  91.271  41.684  1.00 28.04           C  
ATOM   2829  CD1 PHE A 368      27.969  91.676  40.863  1.00 30.08           C  
ATOM   2830  CD2 PHE A 368      26.582  89.927  41.710  1.00 28.49           C  
ATOM   2831  CE1 PHE A 368      28.654  90.754  40.082  1.00 32.15           C  
ATOM   2832  CE2 PHE A 368      27.257  89.000  40.936  1.00 29.65           C  
ATOM   2833  CZ  PHE A 368      28.295  89.412  40.121  1.00 33.20           C  
ATOM   2834  N   PHE A 369      25.777  93.866  45.505  1.00 30.47           N  
ATOM   2835  CA  PHE A 369      24.940  94.852  46.175  1.00 31.21           C  
ATOM   2836  C   PHE A 369      25.563  95.558  47.362  1.00 32.84           C  
ATOM   2837  O   PHE A 369      26.570  95.106  47.919  1.00 34.67           O  
ATOM   2838  CB  PHE A 369      23.639  94.193  46.643  1.00 28.39           C  
ATOM   2839  CG  PHE A 369      22.514  94.341  45.683  1.00 27.44           C  
ATOM   2840  CD1 PHE A 369      22.486  93.601  44.507  1.00 25.78           C  
ATOM   2841  CD2 PHE A 369      21.487  95.240  45.942  1.00 25.07           C  
ATOM   2842  CE1 PHE A 369      21.448  93.757  43.599  1.00 23.18           C  
ATOM   2843  CE2 PHE A 369      20.441  95.407  45.044  1.00 24.40           C  
ATOM   2844  CZ  PHE A 369      20.419  94.664  43.867  1.00 24.03           C  
ATOM   2845  N   GLU A 370      24.941  96.670  47.740  1.00 33.93           N  
ATOM   2846  CA  GLU A 370      25.341  97.442  48.907  1.00 37.41           C  
ATOM   2847  C   GLU A 370      24.068  98.011  49.529  1.00 38.66           C  
ATOM   2848  O   GLU A 370      23.089  98.287  48.820  1.00 38.00           O  
ATOM   2849  CB  GLU A 370      26.355  98.536  48.556  1.00 40.69           C  
ATOM   2850  CG  GLU A 370      25.894  99.584  47.556  1.00 46.58           C  
ATOM   2851  CD  GLU A 370      27.049 100.416  47.015  1.00 48.30           C  
ATOM   2852  OE1 GLU A 370      28.074 100.575  47.716  1.00 45.32           O  
ATOM   2853  OE2 GLU A 370      26.932 100.902  45.873  1.00 49.94           O  
ATOM   2854  N   ALA A 371      24.048  98.084  50.855  1.00 40.07           N  
ATOM   2855  CA  ALA A 371      22.889  98.588  51.575  1.00 42.20           C  
ATOM   2856  C   ALA A 371      23.323  99.485  52.725  1.00 42.75           C  
ATOM   2857  O   ALA A 371      24.461  99.394  53.204  1.00 43.89           O  
ATOM   2858  CB  ALA A 371      22.048  97.421  52.095  1.00 37.92           C  
ATOM   2859  N   LYS A 372      22.401 100.334  53.172  1.00 44.13           N  
ATOM   2860  CA  LYS A 372      22.645 101.274  54.265  1.00 41.62           C  
ATOM   2861  C   LYS A 372      21.319 101.640  54.922  1.00 41.20           C  
ATOM   2862  O   LYS A 372      20.247 101.381  54.372  1.00 40.05           O  
ATOM   2863  CB  LYS A 372      23.287 102.562  53.721  1.00 36.82           C  
ATOM   2864  CG  LYS A 372      22.390 103.301  52.732  1.00 27.74           C  
ATOM   2865  CD  LYS A 372      22.940 104.637  52.298  1.00 25.19           C  
ATOM   2866  CE  LYS A 372      21.981 105.287  51.310  1.00 27.37           C  
ATOM   2867  NZ  LYS A 372      22.356 106.668  50.909  1.00 28.44           N  
ATOM   2868  N   VAL A 373      21.409 102.240  56.103  1.00 44.10           N  
ATOM   2869  CA  VAL A 373      20.237 102.700  56.840  1.00 44.31           C  
ATOM   2870  C   VAL A 373      20.414 104.215  56.922  1.00 44.34           C  
ATOM   2871  O   VAL A 373      21.492 104.698  57.278  1.00 45.28           O  
ATOM   2872  CB  VAL A 373      20.128 102.073  58.262  1.00 40.59           C  
ATOM   2873  CG1 VAL A 373      19.945 100.563  58.165  1.00 40.74           C  
ATOM   2874  CG2 VAL A 373      21.348 102.393  59.102  1.00 41.80           C  
ATOM   2875  N   VAL A 374      19.392 104.957  56.518  1.00 44.65           N  
ATOM   2876  CA  VAL A 374      19.451 106.410  56.527  1.00 44.78           C  
ATOM   2877  C   VAL A 374      18.477 107.031  57.518  1.00 48.41           C  
ATOM   2878  O   VAL A 374      17.461 106.428  57.870  1.00 49.52           O  
ATOM   2879  CB  VAL A 374      19.147 106.980  55.124  1.00 43.12           C  
ATOM   2880  CG1 VAL A 374      20.090 106.375  54.103  1.00 44.46           C  
ATOM   2881  CG2 VAL A 374      17.692 106.720  54.740  1.00 38.67           C  
ATOM   2882  N   ASP A 375      18.797 108.243  57.963  1.00 50.78           N  
ATOM   2883  CA  ASP A 375      17.951 108.972  58.903  1.00 51.65           C  
ATOM   2884  C   ASP A 375      16.643 109.316  58.194  1.00 50.29           C  
ATOM   2885  O   ASP A 375      16.652 109.884  57.104  1.00 49.58           O  
ATOM   2886  CB  ASP A 375      18.659 110.251  59.368  1.00 55.52           C  
ATOM   2887  CG  ASP A 375      17.963 110.919  60.549  1.00 58.50           C  
ATOM   2888  OD1 ASP A 375      17.059 111.751  60.327  1.00 55.18           O  
ATOM   2889  OD2 ASP A 375      18.329 110.619  61.705  1.00 60.65           O  
ATOM   2890  N   LEU A 376      15.523 108.977  58.822  1.00 48.80           N  
ATOM   2891  CA  LEU A 376      14.207 109.239  58.256  1.00 50.70           C  
ATOM   2892  C   LEU A 376      13.944 110.727  58.017  1.00 54.37           C  
ATOM   2893  O   LEU A 376      13.016 111.094  57.299  1.00 54.97           O  
ATOM   2894  CB  LEU A 376      13.125 108.639  59.159  1.00 50.24           C  
ATOM   2895  CG  LEU A 376      13.086 107.106  59.222  1.00 47.67           C  
ATOM   2896  CD1 LEU A 376      12.229 106.635  60.376  1.00 47.64           C  
ATOM   2897  CD2 LEU A 376      12.548 106.549  57.918  1.00 51.11           C  
ATOM   2898  N   ASP A 377      14.768 111.579  58.619  1.00 57.53           N  
ATOM   2899  CA  ASP A 377      14.625 113.023  58.473  1.00 60.00           C  
ATOM   2900  C   ASP A 377      15.700 113.615  57.565  1.00 61.38           C  
ATOM   2901  O   ASP A 377      15.395 114.082  56.472  1.00 63.85           O  
ATOM   2902  CB  ASP A 377      14.664 113.704  59.846  1.00 61.90           C  
ATOM   2903  CG  ASP A 377      13.620 113.158  60.799  1.00 62.56           C  
ATOM   2904  OD1 ASP A 377      12.417 113.366  60.537  1.00 62.88           O  
ATOM   2905  OD2 ASP A 377      14.002 112.519  61.804  1.00 60.63           O  
ATOM   2906  N   THR A 378      16.955 113.572  58.008  1.00 63.14           N  
ATOM   2907  CA  THR A 378      18.071 114.123  57.239  1.00 64.21           C  
ATOM   2908  C   THR A 378      18.467 113.297  56.015  1.00 64.00           C  
ATOM   2909  O   THR A 378      19.184 113.781  55.134  1.00 64.79           O  
ATOM   2910  CB  THR A 378      19.334 114.319  58.127  1.00 65.81           C  
ATOM   2911  OG1 THR A 378      19.794 113.050  58.611  1.00 64.54           O  
ATOM   2912  CG2 THR A 378      19.024 115.230  59.310  1.00 66.92           C  
ATOM   2913  N   GLY A 379      18.031 112.042  55.980  1.00 63.44           N  
ATOM   2914  CA  GLY A 379      18.366 111.175  54.865  1.00 61.39           C  
ATOM   2915  C   GLY A 379      19.838 110.798  54.863  1.00 60.07           C  
ATOM   2916  O   GLY A 379      20.313 110.142  53.935  1.00 59.92           O  
ATOM   2917  N   LYS A 380      20.552 111.198  55.914  1.00 55.27           N  
ATOM   2918  CA  LYS A 380      21.974 110.918  56.048  1.00 49.93           C  
ATOM   2919  C   LYS A 380      22.243 109.475  56.501  1.00 47.24           C  
ATOM   2920  O   LYS A 380      21.494 108.916  57.307  1.00 45.08           O  
ATOM   2921  CB  LYS A 380      22.606 111.916  57.024  1.00 46.30           C  
ATOM   2922  N   THR A 381      23.307 108.882  55.966  1.00 46.34           N  
ATOM   2923  CA  THR A 381      23.709 107.514  56.283  1.00 45.19           C  
ATOM   2924  C   THR A 381      24.066 107.354  57.757  1.00 44.80           C  
ATOM   2925  O   THR A 381      25.023 107.960  58.235  1.00 47.15           O  
ATOM   2926  CB  THR A 381      24.936 107.097  55.434  1.00 43.33           C  
ATOM   2927  OG1 THR A 381      24.628 107.235  54.041  1.00 43.48           O  
ATOM   2928  CG2 THR A 381      25.341 105.666  55.723  1.00 41.00           C  
ATOM   2929  N   LEU A 382      23.316 106.510  58.459  1.00 44.58           N  
ATOM   2930  CA  LEU A 382      23.547 106.260  59.878  1.00 42.90           C  
ATOM   2931  C   LEU A 382      24.692 105.272  60.087  1.00 41.40           C  
ATOM   2932  O   LEU A 382      25.248 104.746  59.125  1.00 44.00           O  
ATOM   2933  CB  LEU A 382      22.263 105.754  60.537  1.00 45.40           C  
ATOM   2934  CG  LEU A 382      21.072 106.715  60.440  1.00 44.09           C  
ATOM   2935  CD1 LEU A 382      19.857 106.129  61.123  1.00 43.96           C  
ATOM   2936  CD2 LEU A 382      21.435 108.048  61.069  1.00 48.37           C  
ATOM   2937  N   GLY A 383      25.044 105.026  61.345  1.00 40.12           N  
ATOM   2938  CA  GLY A 383      26.138 104.119  61.649  1.00 35.77           C  
ATOM   2939  C   GLY A 383      25.733 102.766  62.199  1.00 36.40           C  
ATOM   2940  O   GLY A 383      24.591 102.330  62.038  1.00 39.17           O  
ATOM   2941  N   VAL A 384      26.673 102.115  62.879  1.00 38.75           N  
ATOM   2942  CA  VAL A 384      26.448 100.789  63.458  1.00 41.28           C  
ATOM   2943  C   VAL A 384      25.308 100.761  64.469  1.00 43.96           C  
ATOM   2944  O   VAL A 384      25.107 101.717  65.219  1.00 47.25           O  
ATOM   2945  CB  VAL A 384      27.702 100.259  64.179  1.00 39.00           C  
ATOM   2946  CG1 VAL A 384      27.689  98.739  64.186  1.00 37.10           C  
ATOM   2947  CG2 VAL A 384      28.966 100.801  63.532  1.00 45.80           C  
ATOM   2948  N   ASN A 385      24.573  99.654  64.479  1.00 45.93           N  
ATOM   2949  CA  ASN A 385      23.453  99.433  65.395  1.00 45.30           C  
ATOM   2950  C   ASN A 385      22.436 100.567  65.521  1.00 43.20           C  
ATOM   2951  O   ASN A 385      21.676 100.614  66.486  1.00 41.91           O  
ATOM   2952  CB  ASN A 385      23.973  99.041  66.786  1.00 48.39           C  
ATOM   2953  CG  ASN A 385      24.630  97.671  66.802  1.00 52.72           C  
ATOM   2954  OD1 ASN A 385      23.993  96.659  66.508  1.00 58.64           O  
ATOM   2955  ND2 ASN A 385      25.903  97.628  67.169  1.00 52.40           N  
ATOM   2956  N   GLN A 386      22.405 101.466  64.546  1.00 43.10           N  
ATOM   2957  CA  GLN A 386      21.467 102.583  64.575  1.00 45.95           C  
ATOM   2958  C   GLN A 386      20.341 102.317  63.601  1.00 45.95           C  
ATOM   2959  O   GLN A 386      20.582 102.033  62.429  1.00 49.39           O  
ATOM   2960  CB  GLN A 386      22.182 103.885  64.237  1.00 47.94           C  
ATOM   2961  CG  GLN A 386      23.173 104.299  65.309  1.00 50.27           C  
ATOM   2962  CD  GLN A 386      24.210 105.282  64.811  1.00 57.43           C  
ATOM   2963  OE1 GLN A 386      23.928 106.136  63.967  1.00 60.33           O  
ATOM   2964  NE2 GLN A 386      25.431 105.150  65.314  1.00 57.98           N  
ATOM   2965  N   ARG A 387      19.110 102.433  64.087  1.00 45.90           N  
ATOM   2966  CA  ARG A 387      17.929 102.159  63.273  1.00 46.33           C  
ATOM   2967  C   ARG A 387      17.555 103.303  62.332  1.00 46.23           C  
ATOM   2968  O   ARG A 387      17.481 104.468  62.741  1.00 45.68           O  
ATOM   2969  CB  ARG A 387      16.729 101.813  64.167  1.00 45.78           C  
ATOM   2970  CG  ARG A 387      17.107 101.165  65.483  1.00 49.15           C  
ATOM   2971  CD  ARG A 387      16.476  99.797  65.658  1.00 50.24           C  
ATOM   2972  NE  ARG A 387      16.883  99.153  66.910  1.00 53.45           N  
ATOM   2973  CZ  ARG A 387      18.140  98.880  67.253  1.00 53.98           C  
ATOM   2974  NH1 ARG A 387      19.144  99.199  66.449  1.00 59.29           N  
ATOM   2975  NH2 ARG A 387      18.396  98.272  68.402  1.00 56.32           N  
ATOM   2976  N   GLY A 388      17.313 102.947  61.073  1.00 47.65           N  
ATOM   2977  CA  GLY A 388      16.924 103.910  60.056  1.00 43.91           C  
ATOM   2978  C   GLY A 388      16.329 103.180  58.862  1.00 41.59           C  
ATOM   2979  O   GLY A 388      16.203 101.951  58.891  1.00 40.50           O  
ATOM   2980  N   GLU A 389      15.953 103.920  57.821  1.00 40.24           N  
ATOM   2981  CA  GLU A 389      15.372 103.306  56.625  1.00 40.78           C  
ATOM   2982  C   GLU A 389      16.413 102.574  55.779  1.00 39.20           C  
ATOM   2983  O   GLU A 389      17.472 103.121  55.456  1.00 38.62           O  
ATOM   2984  CB  GLU A 389      14.638 104.336  55.758  1.00 37.21           C  
ATOM   2985  CG  GLU A 389      13.963 103.711  54.537  1.00 37.19           C  
ATOM   2986  CD  GLU A 389      13.207 104.709  53.688  1.00 40.62           C  
ATOM   2987  OE1 GLU A 389      13.219 105.914  54.014  1.00 53.74           O  
ATOM   2988  OE2 GLU A 389      12.589 104.294  52.688  1.00 41.72           O  
ATOM   2989  N   LEU A 390      16.092 101.333  55.429  1.00 37.17           N  
ATOM   2990  CA  LEU A 390      16.964 100.501  54.625  1.00 33.03           C  
ATOM   2991  C   LEU A 390      16.935 100.944  53.167  1.00 32.75           C  
ATOM   2992  O   LEU A 390      15.874 101.111  52.554  1.00 31.47           O  
ATOM   2993  CB  LEU A 390      16.544  99.033  54.739  1.00 33.88           C  
ATOM   2994  CG  LEU A 390      17.350  97.992  53.962  1.00 29.57           C  
ATOM   2995  CD1 LEU A 390      18.790  97.966  54.436  1.00 31.49           C  
ATOM   2996  CD2 LEU A 390      16.712  96.638  54.165  1.00 28.08           C  
ATOM   2997  N   CYS A 391      18.116 101.177  52.628  1.00 33.68           N  
ATOM   2998  CA  CYS A 391      18.250 101.584  51.250  1.00 32.59           C  
ATOM   2999  C   CYS A 391      19.217 100.591  50.656  1.00 31.26           C  
ATOM   3000  O   CYS A 391      20.147 100.143  51.333  1.00 30.78           O  
ATOM   3001  CB  CYS A 391      18.813 102.999  51.165  1.00 37.02           C  
ATOM   3002  SG  CYS A 391      17.675 104.265  51.746  1.00 40.63           S  
ATOM   3003  N   VAL A 392      18.975 100.201  49.415  1.00 30.23           N  
ATOM   3004  CA  VAL A 392      19.846  99.241  48.758  1.00 30.32           C  
ATOM   3005  C   VAL A 392      20.186  99.706  47.356  1.00 28.70           C  
ATOM   3006  O   VAL A 392      19.418 100.439  46.727  1.00 29.09           O  
ATOM   3007  CB  VAL A 392      19.204  97.835  48.705  1.00 29.89           C  
ATOM   3008  CG1 VAL A 392      19.099  97.252  50.105  1.00 28.31           C  
ATOM   3009  CG2 VAL A 392      17.832  97.901  48.045  1.00 30.66           C  
ATOM   3010  N   ARG A 393      21.349  99.284  46.880  1.00 29.35           N  
ATOM   3011  CA  ARG A 393      21.806  99.654  45.557  1.00 31.21           C  
ATOM   3012  C   ARG A 393      22.531  98.470  44.922  1.00 29.32           C  
ATOM   3013  O   ARG A 393      23.379  97.825  45.558  1.00 29.52           O  
ATOM   3014  CB  ARG A 393      22.736 100.861  45.658  1.00 32.69           C  
ATOM   3015  CG  ARG A 393      22.997 101.547  44.340  1.00 37.52           C  
ATOM   3016  CD  ARG A 393      23.637 102.906  44.545  1.00 38.18           C  
ATOM   3017  NE  ARG A 393      24.927 102.831  45.229  1.00 39.72           N  
ATOM   3018  CZ  ARG A 393      25.847 103.793  45.189  1.00 41.02           C  
ATOM   3019  NH1 ARG A 393      25.628 104.905  44.498  1.00 36.44           N  
ATOM   3020  NH2 ARG A 393      26.987 103.650  45.852  1.00 40.72           N  
ATOM   3021  N   GLY A 394      22.161  98.170  43.682  1.00 26.33           N  
ATOM   3022  CA  GLY A 394      22.774  97.066  42.971  1.00 27.32           C  
ATOM   3023  C   GLY A 394      22.161  96.823  41.604  1.00 27.38           C  
ATOM   3024  O   GLY A 394      21.075  97.331  41.310  1.00 26.40           O  
ATOM   3025  N   PRO A 395      22.807  95.985  40.772  1.00 26.20           N  
ATOM   3026  CA  PRO A 395      22.367  95.643  39.417  1.00 25.57           C  
ATOM   3027  C   PRO A 395      21.077  94.825  39.322  1.00 30.05           C  
ATOM   3028  O   PRO A 395      20.653  94.458  38.227  1.00 31.96           O  
ATOM   3029  CB  PRO A 395      23.564  94.883  38.860  1.00 23.95           C  
ATOM   3030  CG  PRO A 395      24.118  94.206  40.063  1.00 26.16           C  
ATOM   3031  CD  PRO A 395      24.063  95.289  41.105  1.00 26.38           C  
ATOM   3032  N   MET A 396      20.457  94.527  40.463  1.00 30.19           N  
ATOM   3033  CA  MET A 396      19.212  93.773  40.455  1.00 29.59           C  
ATOM   3034  C   MET A 396      17.990  94.644  40.707  1.00 29.24           C  
ATOM   3035  O   MET A 396      16.869  94.153  40.674  1.00 32.04           O  
ATOM   3036  CB  MET A 396      19.262  92.615  41.449  1.00 29.78           C  
ATOM   3037  CG  MET A 396      19.550  91.266  40.807  1.00 26.60           C  
ATOM   3038  SD  MET A 396      19.696  89.908  41.985  1.00 31.56           S  
ATOM   3039  CE  MET A 396      18.814  90.542  43.403  1.00 29.31           C  
ATOM   3040  N   ILE A 397      18.202  95.931  40.971  1.00 30.17           N  
ATOM   3041  CA  ILE A 397      17.085  96.852  41.195  1.00 28.14           C  
ATOM   3042  C   ILE A 397      16.368  96.996  39.853  1.00 29.90           C  
ATOM   3043  O   ILE A 397      17.009  96.996  38.796  1.00 34.47           O  
ATOM   3044  CB  ILE A 397      17.568  98.265  41.671  1.00 29.57           C  
ATOM   3045  CG1 ILE A 397      18.437  98.158  42.932  1.00 28.13           C  
ATOM   3046  CG2 ILE A 397      16.370  99.179  41.929  1.00 23.43           C  
ATOM   3047  CD1 ILE A 397      17.725  97.615  44.149  1.00 30.12           C  
ATOM   3048  N   MET A 398      15.047  97.101  39.894  1.00 29.24           N  
ATOM   3049  CA  MET A 398      14.245  97.240  38.686  1.00 32.30           C  
ATOM   3050  C   MET A 398      14.623  98.469  37.861  1.00 33.01           C  
ATOM   3051  O   MET A 398      15.272  99.389  38.352  1.00 32.73           O  
ATOM   3052  CB  MET A 398      12.756  97.332  39.045  1.00 32.50           C  
ATOM   3053  CG  MET A 398      12.405  98.532  39.923  1.00 31.74           C  
ATOM   3054  SD  MET A 398      10.641  98.928  39.978  1.00 31.41           S  
ATOM   3055  CE  MET A 398      10.671 100.374  41.016  1.00 31.75           C  
ATOM   3056  N   SER A 399      14.222  98.470  36.598  1.00 33.53           N  
ATOM   3057  CA  SER A 399      14.488  99.611  35.742  1.00 36.65           C  
ATOM   3058  C   SER A 399      13.382 100.632  36.015  1.00 38.60           C  
ATOM   3059  O   SER A 399      13.507 101.808  35.669  1.00 41.79           O  
ATOM   3060  CB  SER A 399      14.491  99.194  34.269  1.00 33.79           C  
ATOM   3061  OG  SER A 399      13.236  98.663  33.866  1.00 37.75           O  
ATOM   3062  N   GLY A 400      12.291 100.169  36.620  1.00 38.52           N  
ATOM   3063  CA  GLY A 400      11.187 101.052  36.937  1.00 38.51           C  
ATOM   3064  C   GLY A 400       9.816 100.428  36.742  1.00 38.97           C  
ATOM   3065  O   GLY A 400       9.690  99.336  36.180  1.00 37.71           O  
ATOM   3066  N   TYR A 401       8.792 101.106  37.257  1.00 36.56           N  
ATOM   3067  CA  TYR A 401       7.414 100.648  37.131  1.00 34.45           C  
ATOM   3068  C   TYR A 401       6.931 100.984  35.731  1.00 36.80           C  
ATOM   3069  O   TYR A 401       7.090 102.117  35.260  1.00 37.51           O  
ATOM   3070  CB  TYR A 401       6.500 101.347  38.145  1.00 35.47           C  
ATOM   3071  CG  TYR A 401       6.760 101.017  39.601  1.00 36.10           C  
ATOM   3072  CD1 TYR A 401       6.564  99.723  40.100  1.00 33.91           C  
ATOM   3073  CD2 TYR A 401       7.168 102.010  40.491  1.00 35.41           C  
ATOM   3074  CE1 TYR A 401       6.767  99.436  41.454  1.00 36.23           C  
ATOM   3075  CE2 TYR A 401       7.374 101.739  41.840  1.00 35.69           C  
ATOM   3076  CZ  TYR A 401       7.172 100.455  42.320  1.00 37.93           C  
ATOM   3077  OH  TYR A 401       7.374 100.205  43.663  1.00 33.65           O  
ATOM   3078  N   VAL A 402       6.329 100.001  35.077  1.00 37.92           N  
ATOM   3079  CA  VAL A 402       5.809 100.167  33.731  1.00 37.04           C  
ATOM   3080  C   VAL A 402       4.825 101.326  33.660  1.00 41.43           C  
ATOM   3081  O   VAL A 402       3.838 101.361  34.398  1.00 41.05           O  
ATOM   3082  CB  VAL A 402       5.126  98.869  33.233  1.00 33.94           C  
ATOM   3083  CG1 VAL A 402       4.437  99.096  31.899  1.00 29.29           C  
ATOM   3084  CG2 VAL A 402       6.154  97.759  33.107  1.00 34.57           C  
ATOM   3085  N   ASN A 403       5.146 102.300  32.810  1.00 47.28           N  
ATOM   3086  CA  ASN A 403       4.315 103.482  32.581  1.00 50.70           C  
ATOM   3087  C   ASN A 403       3.966 104.276  33.842  1.00 49.85           C  
ATOM   3088  O   ASN A 403       2.884 104.853  33.942  1.00 53.00           O  
ATOM   3089  CB  ASN A 403       3.032 103.100  31.816  1.00 54.98           C  
ATOM   3090  CG  ASN A 403       3.307 102.737  30.360  1.00 61.71           C  
ATOM   3091  OD1 ASN A 403       3.209 101.572  29.957  1.00 60.62           O  
ATOM   3092  ND2 ASN A 403       3.678 103.733  29.568  1.00 66.44           N  
ATOM   3093  N   ASN A 404       4.893 104.323  34.791  1.00 46.76           N  
ATOM   3094  CA  ASN A 404       4.668 105.059  36.028  1.00 45.80           C  
ATOM   3095  C   ASN A 404       6.008 105.580  36.564  1.00 45.91           C  
ATOM   3096  O   ASN A 404       6.467 105.193  37.645  1.00 45.47           O  
ATOM   3097  CB  ASN A 404       3.967 104.153  37.051  1.00 44.90           C  
ATOM   3098  CG  ASN A 404       3.472 104.912  38.272  1.00 46.14           C  
ATOM   3099  OD1 ASN A 404       3.670 106.118  38.392  1.00 52.48           O  
ATOM   3100  ND2 ASN A 404       2.841 104.199  39.197  1.00 43.49           N  
ATOM   3101  N   PRO A 405       6.651 106.486  35.810  1.00 45.94           N  
ATOM   3102  CA  PRO A 405       7.940 107.044  36.228  1.00 45.56           C  
ATOM   3103  C   PRO A 405       7.860 107.821  37.540  1.00 45.97           C  
ATOM   3104  O   PRO A 405       8.851 107.923  38.268  1.00 45.92           O  
ATOM   3105  CB  PRO A 405       8.324 107.936  35.048  1.00 44.19           C  
ATOM   3106  CG  PRO A 405       6.999 108.371  34.511  1.00 44.66           C  
ATOM   3107  CD  PRO A 405       6.201 107.097  34.547  1.00 44.88           C  
ATOM   3108  N   GLU A 406       6.677 108.352  37.848  1.00 45.71           N  
ATOM   3109  CA  GLU A 406       6.482 109.109  39.080  1.00 47.95           C  
ATOM   3110  C   GLU A 406       6.716 108.196  40.293  1.00 47.83           C  
ATOM   3111  O   GLU A 406       7.486 108.533  41.204  1.00 49.44           O  
ATOM   3112  CB  GLU A 406       5.073 109.722  39.115  1.00 45.72           C  
ATOM   3113  N   ALA A 407       6.113 107.010  40.262  1.00 45.06           N  
ATOM   3114  CA  ALA A 407       6.259 106.046  41.348  1.00 39.67           C  
ATOM   3115  C   ALA A 407       7.689 105.532  41.419  1.00 39.85           C  
ATOM   3116  O   ALA A 407       8.213 105.277  42.508  1.00 38.63           O  
ATOM   3117  CB  ALA A 407       5.304 104.900  41.159  1.00 36.69           C  
ATOM   3118  N   THR A 408       8.311 105.369  40.254  1.00 39.82           N  
ATOM   3119  CA  THR A 408       9.685 104.893  40.186  1.00 40.38           C  
ATOM   3120  C   THR A 408      10.590 105.869  40.928  1.00 42.66           C  
ATOM   3121  O   THR A 408      11.290 105.486  41.870  1.00 40.82           O  
ATOM   3122  CB  THR A 408      10.173 104.773  38.723  1.00 37.58           C  
ATOM   3123  OG1 THR A 408       9.292 103.914  37.988  1.00 36.56           O  
ATOM   3124  CG2 THR A 408      11.580 104.200  38.676  1.00 36.83           C  
ATOM   3125  N   ASN A 409      10.509 107.141  40.542  1.00 46.67           N  
ATOM   3126  CA  ASN A 409      11.324 108.198  41.138  1.00 49.81           C  
ATOM   3127  C   ASN A 409      11.095 108.383  42.637  1.00 48.45           C  
ATOM   3128  O   ASN A 409      12.013 108.756  43.368  1.00 49.45           O  
ATOM   3129  CB  ASN A 409      11.102 109.525  40.405  1.00 54.11           C  
ATOM   3130  CG  ASN A 409      11.512 109.465  38.940  1.00 58.70           C  
ATOM   3131  OD1 ASN A 409      12.439 108.747  38.561  1.00 58.91           O  
ATOM   3132  ND2 ASN A 409      10.805 110.214  38.104  1.00 60.30           N  
ATOM   3133  N   ALA A 410       9.870 108.140  43.093  1.00 43.64           N  
ATOM   3134  CA  ALA A 410       9.554 108.269  44.511  1.00 44.22           C  
ATOM   3135  C   ALA A 410      10.213 107.148  45.317  1.00 44.08           C  
ATOM   3136  O   ALA A 410      10.345 107.234  46.539  1.00 44.93           O  
ATOM   3137  CB  ALA A 410       8.046 108.241  44.714  1.00 43.94           C  
ATOM   3138  N   LEU A 411      10.647 106.107  44.621  1.00 45.24           N  
ATOM   3139  CA  LEU A 411      11.270 104.966  45.265  1.00 44.45           C  
ATOM   3140  C   LEU A 411      12.786 104.885  45.067  1.00 43.50           C  
ATOM   3141  O   LEU A 411      13.520 104.496  45.980  1.00 42.13           O  
ATOM   3142  CB  LEU A 411      10.612 103.685  44.748  1.00 45.01           C  
ATOM   3143  CG  LEU A 411      10.967 102.392  45.470  1.00 45.73           C  
ATOM   3144  CD1 LEU A 411      10.419 102.448  46.883  1.00 48.46           C  
ATOM   3145  CD2 LEU A 411      10.386 101.215  44.717  1.00 47.92           C  
ATOM   3146  N   ILE A 412      13.249 105.225  43.868  1.00 44.44           N  
ATOM   3147  CA  ILE A 412      14.676 105.166  43.534  1.00 45.73           C  
ATOM   3148  C   ILE A 412      15.241 106.583  43.362  1.00 47.68           C  
ATOM   3149  O   ILE A 412      14.758 107.362  42.529  1.00 44.14           O  
ATOM   3150  CB  ILE A 412      14.904 104.347  42.231  1.00 43.66           C  
ATOM   3151  CG1 ILE A 412      14.228 102.976  42.353  1.00 38.17           C  
ATOM   3152  CG2 ILE A 412      16.401 104.171  41.957  1.00 31.04           C  
ATOM   3153  CD1 ILE A 412      14.099 102.227  41.047  1.00 42.72           C  
ATOM   3154  N   ASP A 413      16.269 106.909  44.145  1.00 48.64           N  
ATOM   3155  CA  ASP A 413      16.872 108.240  44.076  1.00 52.72           C  
ATOM   3156  C   ASP A 413      17.935 108.402  42.983  1.00 56.55           C  
ATOM   3157  O   ASP A 413      18.384 107.417  42.384  1.00 55.27           O  
ATOM   3158  CB  ASP A 413      17.425 108.686  45.447  1.00 51.97           C  
ATOM   3159  CG  ASP A 413      18.616 107.849  45.937  1.00 49.90           C  
ATOM   3160  OD1 ASP A 413      19.483 107.447  45.128  1.00 45.46           O  
ATOM   3161  OD2 ASP A 413      18.713 107.640  47.165  1.00 48.67           O  
ATOM   3162  N   LYS A 414      18.375 109.646  42.791  1.00 57.60           N  
ATOM   3163  CA  LYS A 414      19.382 110.000  41.789  1.00 56.09           C  
ATOM   3164  C   LYS A 414      20.650 109.141  41.837  1.00 54.25           C  
ATOM   3165  O   LYS A 414      21.249 108.851  40.806  1.00 54.21           O  
ATOM   3166  CB  LYS A 414      19.752 111.483  41.926  1.00 58.49           C  
ATOM   3167  N   ASP A 415      21.048 108.724  43.032  1.00 52.84           N  
ATOM   3168  CA  ASP A 415      22.249 107.914  43.189  1.00 52.05           C  
ATOM   3169  C   ASP A 415      22.017 106.408  43.033  1.00 50.07           C  
ATOM   3170  O   ASP A 415      22.894 105.608  43.358  1.00 49.14           O  
ATOM   3171  CB  ASP A 415      22.916 108.205  44.538  1.00 57.79           C  
ATOM   3172  CG  ASP A 415      23.292 109.674  44.704  1.00 62.43           C  
ATOM   3173  OD1 ASP A 415      23.663 110.320  43.698  1.00 60.91           O  
ATOM   3174  OD2 ASP A 415      23.209 110.178  45.849  1.00 63.67           O  
ATOM   3175  N   GLY A 416      20.837 106.022  42.557  1.00 48.10           N  
ATOM   3176  CA  GLY A 416      20.540 104.609  42.365  1.00 45.32           C  
ATOM   3177  C   GLY A 416      20.070 103.830  43.586  1.00 43.22           C  
ATOM   3178  O   GLY A 416      19.837 102.626  43.497  1.00 46.41           O  
ATOM   3179  N   TRP A 417      19.930 104.500  44.725  1.00 38.83           N  
ATOM   3180  CA  TRP A 417      19.471 103.835  45.943  1.00 37.20           C  
ATOM   3181  C   TRP A 417      17.956 103.704  45.942  1.00 38.29           C  
ATOM   3182  O   TRP A 417      17.241 104.661  45.621  1.00 36.33           O  
ATOM   3183  CB  TRP A 417      19.885 104.619  47.198  1.00 32.95           C  
ATOM   3184  CG  TRP A 417      21.348 104.637  47.464  1.00 31.98           C  
ATOM   3185  CD1 TRP A 417      22.245 105.582  47.053  1.00 28.38           C  
ATOM   3186  CD2 TRP A 417      22.093 103.655  48.190  1.00 28.06           C  
ATOM   3187  NE1 TRP A 417      23.506 105.244  47.477  1.00 30.75           N  
ATOM   3188  CE2 TRP A 417      23.444 104.068  48.177  1.00 29.58           C  
ATOM   3189  CE3 TRP A 417      21.753 102.471  48.854  1.00 25.94           C  
ATOM   3190  CZ2 TRP A 417      24.458 103.329  48.800  1.00 31.70           C  
ATOM   3191  CZ3 TRP A 417      22.753 101.740  49.472  1.00 28.08           C  
ATOM   3192  CH2 TRP A 417      24.094 102.174  49.442  1.00 33.92           C  
ATOM   3193  N   LEU A 418      17.473 102.510  46.265  1.00 37.39           N  
ATOM   3194  CA  LEU A 418      16.048 102.268  46.348  1.00 36.08           C  
ATOM   3195  C   LEU A 418      15.736 102.378  47.829  1.00 34.36           C  
ATOM   3196  O   LEU A 418      16.434 101.784  48.652  1.00 33.31           O  
ATOM   3197  CB  LEU A 418      15.694 100.872  45.811  1.00 31.01           C  
ATOM   3198  CG  LEU A 418      14.284 100.327  46.081  1.00 30.55           C  
ATOM   3199  CD1 LEU A 418      13.806  99.470  44.930  1.00 25.21           C  
ATOM   3200  CD2 LEU A 418      14.252  99.537  47.385  1.00 26.38           C  
ATOM   3201  N   HIS A 419      14.745 103.201  48.162  1.00 35.83           N  
ATOM   3202  CA  HIS A 419      14.321 103.404  49.546  1.00 39.37           C  
ATOM   3203  C   HIS A 419      13.235 102.375  49.821  1.00 38.74           C  
ATOM   3204  O   HIS A 419      12.125 102.493  49.308  1.00 38.19           O  
ATOM   3205  CB  HIS A 419      13.775 104.824  49.735  1.00 43.68           C  
ATOM   3206  CG  HIS A 419      14.790 105.897  49.486  1.00 52.27           C  
ATOM   3207  ND1 HIS A 419      15.841 106.144  50.344  1.00 52.06           N  
ATOM   3208  CD2 HIS A 419      14.936 106.767  48.456  1.00 53.87           C  
ATOM   3209  CE1 HIS A 419      16.593 107.113  49.855  1.00 48.71           C  
ATOM   3210  NE2 HIS A 419      16.062 107.510  48.711  1.00 53.15           N  
ATOM   3211  N   SER A 420      13.555 101.376  50.637  1.00 39.24           N  
ATOM   3212  CA  SER A 420      12.622 100.293  50.939  1.00 39.29           C  
ATOM   3213  C   SER A 420      11.382 100.705  51.713  1.00 42.18           C  
ATOM   3214  O   SER A 420      10.321 100.093  51.569  1.00 42.61           O  
ATOM   3215  CB  SER A 420      13.340  99.189  51.712  1.00 37.12           C  
ATOM   3216  OG  SER A 420      13.722  99.645  52.999  1.00 33.53           O  
ATOM   3217  N   GLY A 421      11.523 101.717  52.562  1.00 44.30           N  
ATOM   3218  CA  GLY A 421      10.402 102.158  53.371  1.00 44.79           C  
ATOM   3219  C   GLY A 421      10.300 101.306  54.623  1.00 46.65           C  
ATOM   3220  O   GLY A 421       9.332 101.421  55.367  1.00 50.98           O  
ATOM   3221  N   ASP A 422      11.286 100.433  54.836  1.00 45.80           N  
ATOM   3222  CA  ASP A 422      11.332  99.554  56.004  1.00 44.13           C  
ATOM   3223  C   ASP A 422      12.490  99.981  56.894  1.00 42.63           C  
ATOM   3224  O   ASP A 422      13.542 100.377  56.399  1.00 45.40           O  
ATOM   3225  CB  ASP A 422      11.561  98.098  55.586  1.00 49.50           C  
ATOM   3226  CG  ASP A 422      10.310  97.422  55.043  1.00 56.30           C  
ATOM   3227  OD1 ASP A 422       9.375  98.116  54.584  1.00 57.07           O  
ATOM   3228  OD2 ASP A 422      10.275  96.173  55.076  1.00 58.83           O  
ATOM   3229  N   ILE A 423      12.307  99.898  58.205  1.00 40.10           N  
ATOM   3230  CA  ILE A 423      13.356 100.278  59.140  1.00 40.57           C  
ATOM   3231  C   ILE A 423      14.170  99.048  59.523  1.00 38.51           C  
ATOM   3232  O   ILE A 423      13.610  97.962  59.733  1.00 35.95           O  
ATOM   3233  CB  ILE A 423      12.766 100.983  60.402  1.00 45.17           C  
ATOM   3234  CG1 ILE A 423      12.289 102.399  60.046  1.00 46.85           C  
ATOM   3235  CG2 ILE A 423      13.806 101.065  61.514  1.00 43.06           C  
ATOM   3236  CD1 ILE A 423      11.033 102.457  59.176  1.00 52.37           C  
ATOM   3237  N   ALA A 424      15.486  99.222  59.603  1.00 39.03           N  
ATOM   3238  CA  ALA A 424      16.391  98.135  59.948  1.00 39.18           C  
ATOM   3239  C   ALA A 424      17.696  98.686  60.509  1.00 39.50           C  
ATOM   3240  O   ALA A 424      17.823  99.895  60.732  1.00 40.73           O  
ATOM   3241  CB  ALA A 424      16.673  97.290  58.706  1.00 38.84           C  
ATOM   3242  N   TYR A 425      18.646  97.790  60.763  1.00 34.49           N  
ATOM   3243  CA  TYR A 425      19.951  98.175  61.272  1.00 35.19           C  
ATOM   3244  C   TYR A 425      20.915  97.009  61.103  1.00 36.00           C  
ATOM   3245  O   TYR A 425      20.489  95.861  60.966  1.00 36.77           O  
ATOM   3246  CB  TYR A 425      19.867  98.590  62.749  1.00 34.57           C  
ATOM   3247  CG  TYR A 425      19.602  97.461  63.728  1.00 32.15           C  
ATOM   3248  CD1 TYR A 425      20.657  96.739  64.290  1.00 28.59           C  
ATOM   3249  CD2 TYR A 425      18.295  97.120  64.095  1.00 31.14           C  
ATOM   3250  CE1 TYR A 425      20.422  95.704  65.188  1.00 32.44           C  
ATOM   3251  CE2 TYR A 425      18.045  96.082  64.999  1.00 30.73           C  
ATOM   3252  CZ  TYR A 425      19.114  95.375  65.540  1.00 33.89           C  
ATOM   3253  OH  TYR A 425      18.885  94.323  66.412  1.00 33.74           O  
ATOM   3254  N   TRP A 426      22.207  97.318  61.076  1.00 37.81           N  
ATOM   3255  CA  TRP A 426      23.262  96.314  60.945  1.00 36.52           C  
ATOM   3256  C   TRP A 426      24.208  96.421  62.138  1.00 36.75           C  
ATOM   3257  O   TRP A 426      24.386  97.503  62.710  1.00 33.37           O  
ATOM   3258  CB  TRP A 426      24.024  96.486  59.629  1.00 38.36           C  
ATOM   3259  CG  TRP A 426      24.313  97.909  59.275  1.00 35.29           C  
ATOM   3260  CD1 TRP A 426      23.485  98.774  58.620  1.00 35.05           C  
ATOM   3261  CD2 TRP A 426      25.504  98.640  59.580  1.00 36.67           C  
ATOM   3262  NE1 TRP A 426      24.084 100.004  58.502  1.00 33.83           N  
ATOM   3263  CE2 TRP A 426      25.325  99.954  59.081  1.00 36.49           C  
ATOM   3264  CE3 TRP A 426      26.707  98.323  60.227  1.00 38.43           C  
ATOM   3265  CZ2 TRP A 426      26.302 100.945  59.210  1.00 36.55           C  
ATOM   3266  CZ3 TRP A 426      27.680  99.309  60.356  1.00 35.86           C  
ATOM   3267  CH2 TRP A 426      27.469 100.604  59.849  1.00 32.24           C  
ATOM   3268  N   ASP A 427      24.794  95.296  62.524  1.00 36.38           N  
ATOM   3269  CA  ASP A 427      25.693  95.270  63.669  1.00 39.54           C  
ATOM   3270  C   ASP A 427      27.179  95.234  63.310  1.00 40.37           C  
ATOM   3271  O   ASP A 427      27.554  95.340  62.147  1.00 36.40           O  
ATOM   3272  CB  ASP A 427      25.330  94.105  64.608  1.00 43.62           C  
ATOM   3273  CG  ASP A 427      25.385  92.729  63.924  1.00 43.39           C  
ATOM   3274  OD1 ASP A 427      26.080  92.561  62.900  1.00 41.94           O  
ATOM   3275  OD2 ASP A 427      24.736  91.796  64.435  1.00 45.70           O  
ATOM   3276  N   GLU A 428      28.011  95.023  64.325  1.00 41.55           N  
ATOM   3277  CA  GLU A 428      29.458  94.964  64.165  1.00 44.12           C  
ATOM   3278  C   GLU A 428      29.944  93.864  63.212  1.00 46.55           C  
ATOM   3279  O   GLU A 428      31.108  93.853  62.816  1.00 44.80           O  
ATOM   3280  CB  GLU A 428      30.113  94.798  65.538  1.00 45.56           C  
ATOM   3281  N   ASP A 429      29.057  92.935  62.857  1.00 49.90           N  
ATOM   3282  CA  ASP A 429      29.399  91.836  61.945  1.00 49.37           C  
ATOM   3283  C   ASP A 429      28.717  91.954  60.581  1.00 47.21           C  
ATOM   3284  O   ASP A 429      28.764  91.020  59.786  1.00 48.24           O  
ATOM   3285  CB  ASP A 429      29.041  90.480  62.566  1.00 50.27           C  
ATOM   3286  CG  ASP A 429      29.905  90.136  63.760  1.00 50.04           C  
ATOM   3287  OD1 ASP A 429      31.147  90.264  63.662  1.00 49.84           O  
ATOM   3288  OD2 ASP A 429      29.338  89.727  64.795  1.00 49.02           O  
ATOM   3289  N   GLU A 430      28.046  93.078  60.340  1.00 46.86           N  
ATOM   3290  CA  GLU A 430      27.342  93.340  59.082  1.00 45.21           C  
ATOM   3291  C   GLU A 430      26.041  92.552  58.875  1.00 44.23           C  
ATOM   3292  O   GLU A 430      25.511  92.493  57.767  1.00 44.63           O  
ATOM   3293  CB  GLU A 430      28.286  93.180  57.882  1.00 49.31           C  
ATOM   3294  CG  GLU A 430      29.487  94.127  57.918  1.00 54.47           C  
ATOM   3295  CD  GLU A 430      30.397  94.018  56.703  1.00 58.13           C  
ATOM   3296  OE1 GLU A 430      30.792  92.886  56.343  1.00 58.23           O  
ATOM   3297  OE2 GLU A 430      30.725  95.073  56.114  1.00 53.86           O  
ATOM   3298  N   HIS A 431      25.534  91.941  59.946  1.00 41.76           N  
ATOM   3299  CA  HIS A 431      24.268  91.203  59.889  1.00 36.76           C  
ATOM   3300  C   HIS A 431      23.174  92.254  59.967  1.00 34.84           C  
ATOM   3301  O   HIS A 431      23.287  93.203  60.746  1.00 31.35           O  
ATOM   3302  CB  HIS A 431      24.121  90.259  61.085  1.00 34.02           C  
ATOM   3303  CG  HIS A 431      24.797  88.935  60.904  1.00 36.76           C  
ATOM   3304  ND1 HIS A 431      25.975  88.605  61.542  1.00 42.04           N  
ATOM   3305  CD2 HIS A 431      24.446  87.845  60.182  1.00 39.90           C  
ATOM   3306  CE1 HIS A 431      26.316  87.368  61.227  1.00 41.50           C  
ATOM   3307  NE2 HIS A 431      25.405  86.885  60.403  1.00 40.04           N  
ATOM   3308  N   PHE A 432      22.143  92.114  59.143  1.00 33.51           N  
ATOM   3309  CA  PHE A 432      21.037  93.059  59.157  1.00 34.03           C  
ATOM   3310  C   PHE A 432      19.854  92.534  59.957  1.00 36.71           C  
ATOM   3311  O   PHE A 432      19.670  91.318  60.094  1.00 34.18           O  
ATOM   3312  CB  PHE A 432      20.585  93.395  57.741  1.00 29.39           C  
ATOM   3313  CG  PHE A 432      21.406  94.461  57.077  1.00 29.74           C  
ATOM   3314  CD1 PHE A 432      22.645  94.162  56.530  1.00 27.68           C  
ATOM   3315  CD2 PHE A 432      20.919  95.761  56.964  1.00 32.52           C  
ATOM   3316  CE1 PHE A 432      23.385  95.137  55.880  1.00 30.11           C  
ATOM   3317  CE2 PHE A 432      21.652  96.746  56.313  1.00 29.13           C  
ATOM   3318  CZ  PHE A 432      22.886  96.434  55.769  1.00 28.43           C  
ATOM   3319  N   PHE A 433      19.066  93.461  60.495  1.00 35.68           N  
ATOM   3320  CA  PHE A 433      17.884  93.129  61.278  1.00 34.43           C  
ATOM   3321  C   PHE A 433      16.747  94.026  60.824  1.00 33.47           C  
ATOM   3322  O   PHE A 433      16.907  95.244  60.750  1.00 34.45           O  
ATOM   3323  CB  PHE A 433      18.144  93.364  62.764  1.00 29.47           C  
ATOM   3324  CG  PHE A 433      19.273  92.554  63.321  1.00 28.80           C  
ATOM   3325  CD1 PHE A 433      20.594  92.924  63.086  1.00 28.46           C  
ATOM   3326  CD2 PHE A 433      19.017  91.432  64.097  1.00 26.82           C  
ATOM   3327  CE1 PHE A 433      21.650  92.186  63.617  1.00 31.57           C  
ATOM   3328  CE2 PHE A 433      20.065  90.684  64.638  1.00 32.80           C  
ATOM   3329  CZ  PHE A 433      21.387  91.063  64.396  1.00 32.66           C  
ATOM   3330  N   ILE A 434      15.622  93.424  60.461  1.00 37.31           N  
ATOM   3331  CA  ILE A 434      14.460  94.193  60.022  1.00 44.45           C  
ATOM   3332  C   ILE A 434      13.574  94.410  61.240  1.00 46.09           C  
ATOM   3333  O   ILE A 434      13.134  93.446  61.863  1.00 52.23           O  
ATOM   3334  CB  ILE A 434      13.657  93.446  58.929  1.00 43.56           C  
ATOM   3335  CG1 ILE A 434      14.547  93.184  57.710  1.00 43.95           C  
ATOM   3336  CG2 ILE A 434      12.423  94.247  58.528  1.00 41.43           C  
ATOM   3337  CD1 ILE A 434      15.093  94.436  57.064  1.00 43.08           C  
ATOM   3338  N   VAL A 435      13.331  95.665  61.596  1.00 47.57           N  
ATOM   3339  CA  VAL A 435      12.508  95.959  62.758  1.00 46.27           C  
ATOM   3340  C   VAL A 435      11.080  95.481  62.517  1.00 49.22           C  
ATOM   3341  O   VAL A 435      10.379  95.980  61.632  1.00 44.70           O  
ATOM   3342  CB  VAL A 435      12.522  97.465  63.107  1.00 44.11           C  
ATOM   3343  CG1 VAL A 435      11.662  97.730  64.326  1.00 44.42           C  
ATOM   3344  CG2 VAL A 435      13.944  97.927  63.373  1.00 44.75           C  
ATOM   3345  N   ASP A 436      10.678  94.475  63.286  1.00 55.46           N  
ATOM   3346  CA  ASP A 436       9.342  93.895  63.191  1.00 59.71           C  
ATOM   3347  C   ASP A 436       8.328  94.902  63.721  1.00 60.17           C  
ATOM   3348  O   ASP A 436       8.291  95.184  64.923  1.00 58.45           O  
ATOM   3349  CB  ASP A 436       9.280  92.602  64.013  1.00 64.07           C  
ATOM   3350  CG  ASP A 436       8.061  91.744  63.688  1.00 68.40           C  
ATOM   3351  OD1 ASP A 436       7.173  92.198  62.927  1.00 70.56           O  
ATOM   3352  OD2 ASP A 436       8.001  90.601  64.194  1.00 71.17           O  
ATOM   3353  N   ARG A 437       7.491  95.429  62.831  1.00 60.28           N  
ATOM   3354  CA  ARG A 437       6.494  96.413  63.234  1.00 63.69           C  
ATOM   3355  C   ARG A 437       5.420  95.806  64.143  1.00 65.64           C  
ATOM   3356  O   ARG A 437       4.706  96.524  64.841  1.00 67.11           O  
ATOM   3357  CB  ARG A 437       5.890  97.096  62.000  1.00 65.26           C  
ATOM   3358  CG  ARG A 437       4.628  96.472  61.451  1.00 67.05           C  
ATOM   3359  CD  ARG A 437       3.412  97.269  61.896  1.00 64.14           C  
ATOM   3360  NE  ARG A 437       2.214  96.446  61.834  1.00 63.17           N  
ATOM   3361  CZ  ARG A 437       1.067  96.738  62.433  1.00 61.30           C  
ATOM   3362  NH1 ARG A 437       0.938  97.853  63.144  1.00 60.50           N  
ATOM   3363  NH2 ARG A 437       0.061  95.887  62.352  1.00 59.20           N  
ATOM   3364  N   LEU A 438       5.327  94.479  64.147  1.00 65.69           N  
ATOM   3365  CA  LEU A 438       4.353  93.781  64.982  1.00 64.82           C  
ATOM   3366  C   LEU A 438       4.822  93.729  66.433  1.00 64.66           C  
ATOM   3367  O   LEU A 438       4.032  93.469  67.347  1.00 68.15           O  
ATOM   3368  CB  LEU A 438       4.112  92.368  64.443  1.00 63.11           C  
ATOM   3369  CG  LEU A 438       3.387  92.307  63.094  1.00 63.81           C  
ATOM   3370  CD1 LEU A 438       3.322  90.869  62.581  1.00 61.35           C  
ATOM   3371  CD2 LEU A 438       1.986  92.901  63.237  1.00 61.40           C  
ATOM   3372  N   LYS A 439       6.115  93.972  66.629  1.00 62.54           N  
ATOM   3373  CA  LYS A 439       6.717  93.978  67.955  1.00 61.92           C  
ATOM   3374  C   LYS A 439       6.913  95.410  68.455  1.00 62.56           C  
ATOM   3375  O   LYS A 439       7.406  95.614  69.567  1.00 61.16           O  
ATOM   3376  CB  LYS A 439       8.075  93.266  67.927  1.00 59.49           C  
ATOM   3377  CG  LYS A 439       8.012  91.750  67.860  1.00 59.58           C  
ATOM   3378  CD  LYS A 439       9.416  91.162  67.828  1.00 61.49           C  
ATOM   3379  CE  LYS A 439       9.409  89.668  68.118  1.00 63.17           C  
ATOM   3380  NZ  LYS A 439      10.776  89.080  68.040  1.00 62.18           N  
ATOM   3381  N   SER A 440       6.481  96.382  67.650  1.00 63.08           N  
ATOM   3382  CA  SER A 440       6.610  97.812  67.939  1.00 63.58           C  
ATOM   3383  C   SER A 440       6.240  98.268  69.355  1.00 65.60           C  
ATOM   3384  O   SER A 440       7.012  98.980  70.002  1.00 67.60           O  
ATOM   3385  CB  SER A 440       5.799  98.617  66.922  1.00 64.89           C  
ATOM   3386  OG  SER A 440       4.445  98.192  66.904  1.00 65.05           O  
ATOM   3387  N   LEU A 441       5.044  97.889  69.803  1.00 61.66           N  
ATOM   3388  CA  LEU A 441       4.550  98.238  71.138  1.00 60.04           C  
ATOM   3389  C   LEU A 441       4.295  99.720  71.406  1.00 59.39           C  
ATOM   3390  O   LEU A 441       5.131 100.587  71.142  1.00 58.08           O  
ATOM   3391  CB  LEU A 441       5.471  97.684  72.230  1.00 58.79           C  
ATOM   3392  CG  LEU A 441       5.580  96.168  72.335  1.00 61.37           C  
ATOM   3393  CD1 LEU A 441       6.449  95.817  73.525  1.00 64.36           C  
ATOM   3394  CD2 LEU A 441       4.203  95.557  72.490  1.00 63.07           C  
ATOM   3395  N   ILE A 442       3.111  99.991  71.935  1.00 60.02           N  
ATOM   3396  CA  ILE A 442       2.695 101.338  72.286  1.00 60.15           C  
ATOM   3397  C   ILE A 442       2.746 101.359  73.812  1.00 62.54           C  
ATOM   3398  O   ILE A 442       2.266 100.422  74.461  1.00 61.29           O  
ATOM   3399  CB  ILE A 442       1.259 101.601  71.796  1.00 58.91           C  
ATOM   3400  CG1 ILE A 442       1.167 101.342  70.287  1.00 57.64           C  
ATOM   3401  CG2 ILE A 442       0.839 103.020  72.133  1.00 56.19           C  
ATOM   3402  CD1 ILE A 442      -0.242 101.328  69.741  1.00 55.32           C  
ATOM   3403  N   LYS A 443       3.357 102.393  74.384  1.00 62.46           N  
ATOM   3404  CA  LYS A 443       3.482 102.488  75.834  1.00 63.53           C  
ATOM   3405  C   LYS A 443       2.654 103.600  76.457  1.00 62.34           C  
ATOM   3406  O   LYS A 443       2.991 104.780  76.331  1.00 61.20           O  
ATOM   3407  CB  LYS A 443       4.953 102.653  76.236  1.00 63.94           C  
ATOM   3408  N   TYR A 444       1.567 103.212  77.118  1.00 63.89           N  
ATOM   3409  CA  TYR A 444       0.687 104.157  77.800  1.00 66.76           C  
ATOM   3410  C   TYR A 444       1.035 104.136  79.289  1.00 69.03           C  
ATOM   3411  O   TYR A 444       0.719 103.170  79.994  1.00 68.76           O  
ATOM   3412  CB  TYR A 444      -0.790 103.783  77.588  1.00 64.01           C  
ATOM   3413  CG  TYR A 444      -1.762 104.696  78.309  1.00 60.68           C  
ATOM   3414  CD1 TYR A 444      -1.888 106.037  77.947  1.00 57.90           C  
ATOM   3415  CD2 TYR A 444      -2.529 104.228  79.380  1.00 58.63           C  
ATOM   3416  CE1 TYR A 444      -2.747 106.894  78.633  1.00 59.60           C  
ATOM   3417  CE2 TYR A 444      -3.393 105.079  80.073  1.00 59.42           C  
ATOM   3418  CZ  TYR A 444      -3.496 106.411  79.695  1.00 59.05           C  
ATOM   3419  OH  TYR A 444      -4.340 107.261  80.379  1.00 58.73           O  
ATOM   3420  N   LYS A 445       1.714 105.185  79.753  1.00 69.42           N  
ATOM   3421  CA  LYS A 445       2.126 105.288  81.150  1.00 69.56           C  
ATOM   3422  C   LYS A 445       2.825 103.997  81.584  1.00 70.64           C  
ATOM   3423  O   LYS A 445       2.475 103.388  82.597  1.00 70.90           O  
ATOM   3424  CB  LYS A 445       0.913 105.572  82.042  1.00 69.30           C  
ATOM   3425  CG  LYS A 445       0.292 106.952  81.845  1.00 67.84           C  
ATOM   3426  CD  LYS A 445      -0.982 107.110  82.663  1.00 66.01           C  
ATOM   3427  CE  LYS A 445      -1.463 108.555  82.673  1.00 66.03           C  
ATOM   3428  NZ  LYS A 445      -2.763 108.716  83.390  1.00 64.62           N  
ATOM   3429  N   GLY A 446       3.794 103.563  80.786  1.00 71.19           N  
ATOM   3430  CA  GLY A 446       4.517 102.347  81.106  1.00 72.72           C  
ATOM   3431  C   GLY A 446       3.856 101.087  80.579  1.00 74.53           C  
ATOM   3432  O   GLY A 446       4.546 100.197  80.079  1.00 76.37           O  
ATOM   3433  N   TYR A 447       2.532 100.995  80.694  1.00 74.02           N  
ATOM   3434  CA  TYR A 447       1.803  99.820  80.211  1.00 72.75           C  
ATOM   3435  C   TYR A 447       1.973  99.672  78.697  1.00 70.85           C  
ATOM   3436  O   TYR A 447       1.795 100.635  77.945  1.00 68.73           O  
ATOM   3437  CB  TYR A 447       0.319  99.926  80.570  1.00 74.37           C  
ATOM   3438  N   GLN A 448       2.331  98.470  78.257  1.00 68.84           N  
ATOM   3439  CA  GLN A 448       2.550  98.211  76.838  1.00 67.97           C  
ATOM   3440  C   GLN A 448       1.428  97.438  76.170  1.00 65.54           C  
ATOM   3441  O   GLN A 448       0.869  96.503  76.747  1.00 65.20           O  
ATOM   3442  CB  GLN A 448       3.857  97.444  76.633  1.00 70.95           C  
ATOM   3443  CG  GLN A 448       5.110  98.199  77.021  1.00 73.37           C  
ATOM   3444  CD  GLN A 448       6.348  97.322  76.953  1.00 74.86           C  
ATOM   3445  OE1 GLN A 448       6.258  96.112  76.759  1.00 75.94           O  
ATOM   3446  NE2 GLN A 448       7.510  97.929  77.124  1.00 76.37           N  
ATOM   3447  N   VAL A 449       1.140  97.805  74.926  1.00 63.31           N  
ATOM   3448  CA  VAL A 449       0.106  97.134  74.150  1.00 58.78           C  
ATOM   3449  C   VAL A 449       0.531  97.021  72.683  1.00 55.74           C  
ATOM   3450  O   VAL A 449       1.020  97.981  72.086  1.00 51.65           O  
ATOM   3451  CB  VAL A 449      -1.266  97.857  74.274  1.00 56.41           C  
ATOM   3452  CG1 VAL A 449      -1.174  99.295  73.769  1.00 49.55           C  
ATOM   3453  CG2 VAL A 449      -2.342  97.080  73.530  1.00 53.93           C  
ATOM   3454  N   ALA A 450       0.398  95.818  72.132  1.00 53.40           N  
ATOM   3455  CA  ALA A 450       0.755  95.566  70.743  1.00 56.04           C  
ATOM   3456  C   ALA A 450      -0.344  96.076  69.815  1.00 56.96           C  
ATOM   3457  O   ALA A 450      -1.513  95.702  69.959  1.00 55.76           O  
ATOM   3458  CB  ALA A 450       0.980  94.074  70.520  1.00 56.67           C  
ATOM   3459  N   PRO A 451       0.021  96.906  68.822  1.00 56.15           N  
ATOM   3460  CA  PRO A 451      -0.954  97.452  67.874  1.00 54.69           C  
ATOM   3461  C   PRO A 451      -1.738  96.343  67.172  1.00 54.19           C  
ATOM   3462  O   PRO A 451      -2.925  96.495  66.870  1.00 53.26           O  
ATOM   3463  CB  PRO A 451      -0.070  98.237  66.901  1.00 54.04           C  
ATOM   3464  CG  PRO A 451       1.241  97.514  66.959  1.00 53.43           C  
ATOM   3465  CD  PRO A 451       1.391  97.287  68.435  1.00 55.57           C  
ATOM   3466  N   ALA A 452      -1.074  95.212  66.962  1.00 53.93           N  
ATOM   3467  CA  ALA A 452      -1.678  94.058  66.309  1.00 51.53           C  
ATOM   3468  C   ALA A 452      -2.887  93.534  67.088  1.00 49.98           C  
ATOM   3469  O   ALA A 452      -3.869  93.073  66.501  1.00 47.21           O  
ATOM   3470  CB  ALA A 452      -0.636  92.957  66.148  1.00 52.72           C  
ATOM   3471  N   GLU A 453      -2.811  93.623  68.413  1.00 49.90           N  
ATOM   3472  CA  GLU A 453      -3.884  93.158  69.287  1.00 50.13           C  
ATOM   3473  C   GLU A 453      -5.136  93.997  69.060  1.00 47.88           C  
ATOM   3474  O   GLU A 453      -6.209  93.470  68.750  1.00 46.44           O  
ATOM   3475  CB  GLU A 453      -3.456  93.267  70.751  1.00 51.63           C  
ATOM   3476  CG  GLU A 453      -4.412  92.591  71.728  1.00 57.03           C  
ATOM   3477  CD  GLU A 453      -4.118  92.930  73.180  1.00 59.18           C  
ATOM   3478  OE1 GLU A 453      -2.935  93.163  73.522  1.00 64.31           O  
ATOM   3479  OE2 GLU A 453      -5.079  92.968  73.980  1.00 58.08           O  
ATOM   3480  N   LEU A 454      -4.978  95.309  69.198  1.00 46.52           N  
ATOM   3481  CA  LEU A 454      -6.074  96.253  69.014  1.00 43.06           C  
ATOM   3482  C   LEU A 454      -6.637  96.175  67.600  1.00 41.85           C  
ATOM   3483  O   LEU A 454      -7.842  96.330  67.403  1.00 42.05           O  
ATOM   3484  CB  LEU A 454      -5.603  97.671  69.320  1.00 41.42           C  
ATOM   3485  CG  LEU A 454      -5.127  97.897  70.753  1.00 38.40           C  
ATOM   3486  CD1 LEU A 454      -4.560  99.286  70.895  1.00 36.41           C  
ATOM   3487  CD2 LEU A 454      -6.283  97.691  71.715  1.00 37.63           C  
ATOM   3488  N   GLU A 455      -5.770  95.937  66.620  1.00 36.49           N  
ATOM   3489  CA  GLU A 455      -6.206  95.817  65.237  1.00 37.80           C  
ATOM   3490  C   GLU A 455      -7.069  94.581  65.093  1.00 37.21           C  
ATOM   3491  O   GLU A 455      -8.088  94.603  64.402  1.00 36.17           O  
ATOM   3492  CB  GLU A 455      -5.011  95.733  64.300  1.00 39.32           C  
ATOM   3493  CG  GLU A 455      -4.253  97.040  64.186  1.00 42.42           C  
ATOM   3494  CD  GLU A 455      -2.865  96.864  63.622  1.00 43.54           C  
ATOM   3495  OE1 GLU A 455      -2.549  95.751  63.143  1.00 43.91           O  
ATOM   3496  OE2 GLU A 455      -2.089  97.841  63.665  1.00 39.57           O  
ATOM   3497  N   SER A 456      -6.670  93.516  65.779  1.00 39.38           N  
ATOM   3498  CA  SER A 456      -7.402  92.257  65.758  1.00 40.82           C  
ATOM   3499  C   SER A 456      -8.821  92.514  66.273  1.00 41.04           C  
ATOM   3500  O   SER A 456      -9.801  92.044  65.691  1.00 43.76           O  
ATOM   3501  CB  SER A 456      -6.682  91.236  66.639  1.00 43.16           C  
ATOM   3502  OG  SER A 456      -7.104  89.920  66.349  1.00 51.93           O  
ATOM   3503  N   ILE A 457      -8.919  93.309  67.337  1.00 38.65           N  
ATOM   3504  CA  ILE A 457     -10.204  93.671  67.936  1.00 37.47           C  
ATOM   3505  C   ILE A 457     -11.058  94.527  66.994  1.00 38.16           C  
ATOM   3506  O   ILE A 457     -12.245  94.257  66.807  1.00 40.25           O  
ATOM   3507  CB  ILE A 457      -9.998  94.414  69.274  1.00 38.90           C  
ATOM   3508  CG1 ILE A 457      -9.406  93.448  70.301  1.00 39.88           C  
ATOM   3509  CG2 ILE A 457     -11.310  95.032  69.773  1.00 32.84           C  
ATOM   3510  CD1 ILE A 457      -9.281  94.021  71.679  1.00 46.33           C  
ATOM   3511  N   LEU A 458     -10.457  95.553  66.400  1.00 35.53           N  
ATOM   3512  CA  LEU A 458     -11.178  96.425  65.481  1.00 31.96           C  
ATOM   3513  C   LEU A 458     -11.698  95.651  64.276  1.00 33.70           C  
ATOM   3514  O   LEU A 458     -12.881  95.749  63.936  1.00 29.39           O  
ATOM   3515  CB  LEU A 458     -10.284  97.577  65.025  1.00 29.32           C  
ATOM   3516  CG  LEU A 458      -9.972  98.617  66.108  1.00 29.26           C  
ATOM   3517  CD1 LEU A 458      -8.940  99.619  65.622  1.00 24.16           C  
ATOM   3518  CD2 LEU A 458     -11.256  99.320  66.503  1.00 24.66           C  
ATOM   3519  N   LEU A 459     -10.821  94.855  63.662  1.00 34.30           N  
ATOM   3520  CA  LEU A 459     -11.170  94.045  62.495  1.00 34.87           C  
ATOM   3521  C   LEU A 459     -12.323  93.103  62.817  1.00 37.71           C  
ATOM   3522  O   LEU A 459     -13.032  92.628  61.929  1.00 39.96           O  
ATOM   3523  CB  LEU A 459      -9.961  93.225  62.038  1.00 35.21           C  
ATOM   3524  CG  LEU A 459      -8.782  93.951  61.385  1.00 34.57           C  
ATOM   3525  CD1 LEU A 459      -7.588  93.020  61.341  1.00 35.50           C  
ATOM   3526  CD2 LEU A 459      -9.149  94.418  59.988  1.00 34.62           C  
ATOM   3527  N   GLN A 460     -12.493  92.834  64.102  1.00 38.47           N  
ATOM   3528  CA  GLN A 460     -13.540  91.954  64.585  1.00 41.16           C  
ATOM   3529  C   GLN A 460     -14.950  92.559  64.487  1.00 38.99           C  
ATOM   3530  O   GLN A 460     -15.947  91.831  64.515  1.00 36.96           O  
ATOM   3531  CB  GLN A 460     -13.220  91.577  66.033  1.00 46.91           C  
ATOM   3532  CG  GLN A 460     -14.111  90.518  66.624  1.00 54.55           C  
ATOM   3533  CD  GLN A 460     -13.608  90.014  67.964  1.00 53.61           C  
ATOM   3534  OE1 GLN A 460     -12.421  90.111  68.288  1.00 48.95           O  
ATOM   3535  NE2 GLN A 460     -14.505  89.423  68.726  1.00 49.91           N  
ATOM   3536  N   HIS A 461     -15.033  93.879  64.333  1.00 35.93           N  
ATOM   3537  CA  HIS A 461     -16.322  94.558  64.255  1.00 35.52           C  
ATOM   3538  C   HIS A 461     -16.964  94.480  62.869  1.00 35.86           C  
ATOM   3539  O   HIS A 461     -16.329  94.795  61.870  1.00 38.85           O  
ATOM   3540  CB  HIS A 461     -16.172  96.019  64.687  1.00 35.27           C  
ATOM   3541  CG  HIS A 461     -17.427  96.610  65.239  1.00 29.97           C  
ATOM   3542  ND1 HIS A 461     -18.395  97.182  64.441  1.00 31.21           N  
ATOM   3543  CD2 HIS A 461     -17.902  96.670  66.506  1.00 28.55           C  
ATOM   3544  CE1 HIS A 461     -19.417  97.558  65.193  1.00 30.11           C  
ATOM   3545  NE2 HIS A 461     -19.137  97.260  66.449  1.00 31.44           N  
ATOM   3546  N   PRO A 462     -18.269  94.155  62.806  1.00 38.15           N  
ATOM   3547  CA  PRO A 462     -18.996  94.045  61.534  1.00 40.78           C  
ATOM   3548  C   PRO A 462     -18.950  95.276  60.637  1.00 42.33           C  
ATOM   3549  O   PRO A 462     -19.090  95.169  59.417  1.00 46.51           O  
ATOM   3550  CB  PRO A 462     -20.433  93.746  61.984  1.00 38.33           C  
ATOM   3551  CG  PRO A 462     -20.500  94.324  63.365  1.00 37.26           C  
ATOM   3552  CD  PRO A 462     -19.178  93.895  63.935  1.00 35.81           C  
ATOM   3553  N   ASN A 463     -18.763  96.441  61.246  1.00 41.40           N  
ATOM   3554  CA  ASN A 463     -18.723  97.692  60.499  1.00 40.22           C  
ATOM   3555  C   ASN A 463     -17.330  98.059  60.019  1.00 40.33           C  
ATOM   3556  O   ASN A 463     -17.179  98.884  59.121  1.00 41.85           O  
ATOM   3557  CB  ASN A 463     -19.252  98.846  61.360  1.00 41.27           C  
ATOM   3558  CG  ASN A 463     -20.734  98.741  61.650  1.00 41.41           C  
ATOM   3559  OD1 ASN A 463     -21.435  97.878  61.120  1.00 44.81           O  
ATOM   3560  ND2 ASN A 463     -21.218  99.621  62.508  1.00 41.32           N  
ATOM   3561  N   ILE A 464     -16.311  97.467  60.626  1.00 38.48           N  
ATOM   3562  CA  ILE A 464     -14.945  97.796  60.264  1.00 34.53           C  
ATOM   3563  C   ILE A 464     -14.347  96.842  59.247  1.00 35.64           C  
ATOM   3564  O   ILE A 464     -14.361  95.627  59.424  1.00 37.78           O  
ATOM   3565  CB  ILE A 464     -14.061  97.892  61.522  1.00 35.80           C  
ATOM   3566  CG1 ILE A 464     -14.615  98.987  62.446  1.00 29.24           C  
ATOM   3567  CG2 ILE A 464     -12.610  98.177  61.137  1.00 34.09           C  
ATOM   3568  CD1 ILE A 464     -13.844  99.182  63.725  1.00 30.13           C  
ATOM   3569  N   PHE A 465     -13.862  97.416  58.156  1.00 38.27           N  
ATOM   3570  CA  PHE A 465     -13.250  96.653  57.075  1.00 38.26           C  
ATOM   3571  C   PHE A 465     -11.759  96.448  57.339  1.00 37.18           C  
ATOM   3572  O   PHE A 465     -11.258  95.324  57.280  1.00 33.90           O  
ATOM   3573  CB  PHE A 465     -13.472  97.382  55.741  1.00 38.93           C  
ATOM   3574  CG  PHE A 465     -12.666  96.832  54.608  1.00 43.98           C  
ATOM   3575  CD1 PHE A 465     -12.764  95.495  54.252  1.00 48.82           C  
ATOM   3576  CD2 PHE A 465     -11.793  97.651  53.906  1.00 43.11           C  
ATOM   3577  CE1 PHE A 465     -12.003  94.978  53.214  1.00 51.35           C  
ATOM   3578  CE2 PHE A 465     -11.028  97.146  52.868  1.00 46.46           C  
ATOM   3579  CZ  PHE A 465     -11.133  95.803  52.519  1.00 48.63           C  
ATOM   3580  N   ASP A 466     -11.062  97.535  57.657  1.00 35.43           N  
ATOM   3581  CA  ASP A 466      -9.627  97.489  57.926  1.00 37.50           C  
ATOM   3582  C   ASP A 466      -9.329  98.499  59.033  1.00 35.45           C  
ATOM   3583  O   ASP A 466     -10.100  99.440  59.240  1.00 31.15           O  
ATOM   3584  CB  ASP A 466      -8.844  97.847  56.646  1.00 41.18           C  
ATOM   3585  CG  ASP A 466      -7.421  97.289  56.630  1.00 43.29           C  
ATOM   3586  OD1 ASP A 466      -7.062  96.437  57.479  1.00 41.83           O  
ATOM   3587  OD2 ASP A 466      -6.658  97.699  55.729  1.00 47.90           O  
ATOM   3588  N   ALA A 467      -8.217  98.297  59.736  1.00 35.75           N  
ATOM   3589  CA  ALA A 467      -7.808  99.183  60.820  1.00 35.94           C  
ATOM   3590  C   ALA A 467      -6.299  99.151  60.998  1.00 37.36           C  
ATOM   3591  O   ALA A 467      -5.649  98.122  60.771  1.00 37.88           O  
ATOM   3592  CB  ALA A 467      -8.491  98.784  62.124  1.00 31.64           C  
ATOM   3593  N   GLY A 468      -5.747 100.292  61.391  1.00 35.70           N  
ATOM   3594  CA  GLY A 468      -4.318 100.400  61.615  1.00 35.84           C  
ATOM   3595  C   GLY A 468      -4.121 101.119  62.929  1.00 33.62           C  
ATOM   3596  O   GLY A 468      -4.528 102.275  63.069  1.00 29.37           O  
ATOM   3597  N   VAL A 469      -3.543 100.430  63.904  1.00 36.09           N  
ATOM   3598  CA  VAL A 469      -3.324 101.013  65.214  1.00 40.58           C  
ATOM   3599  C   VAL A 469      -1.886 101.461  65.402  1.00 42.86           C  
ATOM   3600  O   VAL A 469      -0.945 100.703  65.147  1.00 41.37           O  
ATOM   3601  CB  VAL A 469      -3.699 100.018  66.350  1.00 42.34           C  
ATOM   3602  CG1 VAL A 469      -3.457 100.666  67.718  1.00 42.50           C  
ATOM   3603  CG2 VAL A 469      -5.154  99.597  66.222  1.00 36.58           C  
ATOM   3604  N   ALA A 470      -1.728 102.706  65.837  1.00 48.62           N  
ATOM   3605  CA  ALA A 470      -0.411 103.289  66.096  1.00 55.31           C  
ATOM   3606  C   ALA A 470      -0.544 104.214  67.309  1.00 59.40           C  
ATOM   3607  O   ALA A 470      -1.646 104.683  67.625  1.00 58.87           O  
ATOM   3608  CB  ALA A 470       0.091 104.054  64.883  1.00 55.14           C  
ATOM   3609  N   GLY A 471       0.568 104.462  67.993  1.00 61.92           N  
ATOM   3610  CA  GLY A 471       0.536 105.320  69.165  1.00 65.86           C  
ATOM   3611  C   GLY A 471       0.669 106.814  68.925  1.00 66.61           C  
ATOM   3612  O   GLY A 471       1.730 107.284  68.507  1.00 67.60           O  
ATOM   3613  N   LEU A 472      -0.410 107.553  69.175  1.00 68.20           N  
ATOM   3614  CA  LEU A 472      -0.417 109.007  69.025  1.00 71.29           C  
ATOM   3615  C   LEU A 472       0.401 109.560  70.189  1.00 77.08           C  
ATOM   3616  O   LEU A 472      -0.049 109.517  71.339  1.00 80.27           O  
ATOM   3617  CB  LEU A 472      -1.856 109.542  69.094  1.00 66.54           C  
ATOM   3618  CG  LEU A 472      -2.100 111.054  69.192  1.00 66.36           C  
ATOM   3619  CD1 LEU A 472      -1.556 111.779  67.969  1.00 63.58           C  
ATOM   3620  CD2 LEU A 472      -3.588 111.322  69.344  1.00 65.00           C  
ATOM   3621  N   PRO A 473       1.620 110.058  69.918  1.00 80.23           N  
ATOM   3622  CA  PRO A 473       2.467 110.602  70.983  1.00 80.27           C  
ATOM   3623  C   PRO A 473       1.769 111.651  71.853  1.00 80.59           C  
ATOM   3624  O   PRO A 473       1.149 112.598  71.351  1.00 77.13           O  
ATOM   3625  CB  PRO A 473       3.669 111.168  70.221  1.00 80.27           C  
ATOM   3626  CG  PRO A 473       3.112 111.470  68.856  1.00 80.27           C  
ATOM   3627  CD  PRO A 473       2.250 110.268  68.599  1.00 80.47           C  
ATOM   3628  N   ASP A 474       1.845 111.440  73.162  1.00 82.09           N  
ATOM   3629  CA  ASP A 474       1.236 112.335  74.131  1.00 84.37           C  
ATOM   3630  C   ASP A 474       2.215 112.551  75.280  1.00 87.27           C  
ATOM   3631  O   ASP A 474       2.580 111.604  75.980  1.00 86.07           O  
ATOM   3632  CB  ASP A 474      -0.071 111.738  74.662  1.00 82.23           C  
ATOM   3633  CG  ASP A 474      -0.758 112.638  75.675  1.00 82.48           C  
ATOM   3634  OD1 ASP A 474      -1.016 113.817  75.344  1.00 82.90           O  
ATOM   3635  OD2 ASP A 474      -1.034 112.170  76.802  1.00 79.89           O  
ATOM   3636  N   ASP A 475       2.606 113.807  75.483  1.00 90.38           N  
ATOM   3637  CA  ASP A 475       3.550 114.185  76.536  1.00 91.87           C  
ATOM   3638  C   ASP A 475       3.120 113.754  77.942  1.00 93.07           C  
ATOM   3639  O   ASP A 475       3.935 113.261  78.721  1.00 95.20           O  
ATOM   3640  CB  ASP A 475       3.791 115.699  76.507  1.00 88.45           C  
ATOM   3641  N   ASP A 476       1.832 113.897  78.248  1.00 92.47           N  
ATOM   3642  CA  ASP A 476       1.309 113.537  79.565  1.00 90.25           C  
ATOM   3643  C   ASP A 476       1.206 112.031  79.863  1.00 89.32           C  
ATOM   3644  O   ASP A 476       1.051 111.649  81.024  1.00 91.97           O  
ATOM   3645  CB  ASP A 476      -0.051 114.208  79.794  1.00 87.41           C  
ATOM   3646  N   ALA A 477       1.317 111.180  78.839  1.00 86.62           N  
ATOM   3647  CA  ALA A 477       1.206 109.733  79.053  1.00 82.22           C  
ATOM   3648  C   ALA A 477       2.103 108.854  78.183  1.00 79.14           C  
ATOM   3649  O   ALA A 477       1.998 107.622  78.213  1.00 77.59           O  
ATOM   3650  CB  ALA A 477      -0.245 109.302  78.895  1.00 81.37           C  
ATOM   3651  N   GLY A 478       3.024 109.473  77.457  1.00 77.19           N  
ATOM   3652  CA  GLY A 478       3.907 108.717  76.587  1.00 75.85           C  
ATOM   3653  C   GLY A 478       3.243 108.554  75.234  1.00 73.59           C  
ATOM   3654  O   GLY A 478       3.570 109.268  74.280  1.00 73.31           O  
ATOM   3655  N   GLU A 479       2.279 107.644  75.161  1.00 71.08           N  
ATOM   3656  CA  GLU A 479       1.551 107.400  73.926  1.00 68.13           C  
ATOM   3657  C   GLU A 479       0.081 107.077  74.187  1.00 65.14           C  
ATOM   3658  O   GLU A 479      -0.258 106.436  75.185  1.00 63.76           O  
ATOM   3659  CB  GLU A 479       2.176 106.238  73.152  1.00 69.31           C  
ATOM   3660  CG  GLU A 479       3.524 106.516  72.528  1.00 68.87           C  
ATOM   3661  CD  GLU A 479       4.006 105.345  71.702  1.00 72.13           C  
ATOM   3662  OE1 GLU A 479       4.449 104.339  72.298  1.00 74.80           O  
ATOM   3663  OE2 GLU A 479       3.929 105.425  70.457  1.00 72.08           O  
ATOM   3664  N   LEU A 480      -0.780 107.537  73.284  1.00 61.51           N  
ATOM   3665  CA  LEU A 480      -2.209 107.284  73.361  1.00 53.88           C  
ATOM   3666  C   LEU A 480      -2.573 106.360  72.213  1.00 48.74           C  
ATOM   3667  O   LEU A 480      -2.373 106.708  71.054  1.00 49.94           O  
ATOM   3668  CB  LEU A 480      -2.987 108.589  73.231  1.00 52.38           C  
ATOM   3669  CG  LEU A 480      -3.007 109.478  74.473  1.00 57.14           C  
ATOM   3670  CD1 LEU A 480      -3.849 110.715  74.212  1.00 55.00           C  
ATOM   3671  CD2 LEU A 480      -3.563 108.684  75.655  1.00 59.02           C  
ATOM   3672  N   PRO A 481      -3.055 105.143  72.515  1.00 45.23           N  
ATOM   3673  CA  PRO A 481      -3.421 104.223  71.432  1.00 44.24           C  
ATOM   3674  C   PRO A 481      -4.490 104.852  70.535  1.00 43.71           C  
ATOM   3675  O   PRO A 481      -5.535 105.293  71.019  1.00 45.04           O  
ATOM   3676  CB  PRO A 481      -3.960 103.009  72.190  1.00 42.20           C  
ATOM   3677  CG  PRO A 481      -3.177 103.034  73.470  1.00 39.26           C  
ATOM   3678  CD  PRO A 481      -3.209 104.497  73.830  1.00 43.69           C  
ATOM   3679  N   ALA A 482      -4.205 104.936  69.240  1.00 40.18           N  
ATOM   3680  CA  ALA A 482      -5.138 105.513  68.283  1.00 37.45           C  
ATOM   3681  C   ALA A 482      -5.186 104.615  67.053  1.00 38.40           C  
ATOM   3682  O   ALA A 482      -4.340 103.722  66.895  1.00 36.64           O  
ATOM   3683  CB  ALA A 482      -4.708 106.913  67.908  1.00 38.72           C  
ATOM   3684  N   ALA A 483      -6.161 104.851  66.181  1.00 37.94           N  
ATOM   3685  CA  ALA A 483      -6.297 104.038  64.989  1.00 35.80           C  
ATOM   3686  C   ALA A 483      -6.955 104.711  63.792  1.00 35.54           C  
ATOM   3687  O   ALA A 483      -7.812 105.582  63.936  1.00 35.40           O  
ATOM   3688  CB  ALA A 483      -7.077 102.771  65.338  1.00 35.62           C  
ATOM   3689  N   VAL A 484      -6.483 104.356  62.603  1.00 33.00           N  
ATOM   3690  CA  VAL A 484      -7.073 104.856  61.367  1.00 31.82           C  
ATOM   3691  C   VAL A 484      -8.018 103.707  60.996  1.00 33.25           C  
ATOM   3692  O   VAL A 484      -7.614 102.536  61.039  1.00 34.15           O  
ATOM   3693  CB  VAL A 484      -6.019 105.117  60.260  1.00 28.62           C  
ATOM   3694  CG1 VAL A 484      -5.112 106.261  60.665  1.00 29.44           C  
ATOM   3695  CG2 VAL A 484      -5.197 103.871  59.952  1.00 27.09           C  
ATOM   3696  N   VAL A 485      -9.277 104.018  60.705  1.00 33.29           N  
ATOM   3697  CA  VAL A 485     -10.252 102.989  60.394  1.00 30.42           C  
ATOM   3698  C   VAL A 485     -10.947 103.127  59.045  1.00 32.94           C  
ATOM   3699  O   VAL A 485     -11.434 104.201  58.688  1.00 33.06           O  
ATOM   3700  CB  VAL A 485     -11.346 102.918  61.511  1.00 29.69           C  
ATOM   3701  CG1 VAL A 485     -12.464 101.985  61.093  1.00 26.86           C  
ATOM   3702  CG2 VAL A 485     -10.737 102.451  62.818  1.00 24.12           C  
ATOM   3703  N   VAL A 486     -10.998 102.017  58.314  1.00 35.52           N  
ATOM   3704  CA  VAL A 486     -11.666 101.949  57.010  1.00 34.39           C  
ATOM   3705  C   VAL A 486     -12.972 101.191  57.233  1.00 34.46           C  
ATOM   3706  O   VAL A 486     -12.950  99.987  57.478  1.00 34.81           O  
ATOM   3707  CB  VAL A 486     -10.831 101.155  55.973  1.00 34.82           C  
ATOM   3708  CG1 VAL A 486     -11.564 101.088  54.650  1.00 29.02           C  
ATOM   3709  CG2 VAL A 486      -9.451 101.786  55.798  1.00 29.81           C  
ATOM   3710  N   LEU A 487     -14.099 101.892  57.183  1.00 36.93           N  
ATOM   3711  CA  LEU A 487     -15.395 101.264  57.383  1.00 37.04           C  
ATOM   3712  C   LEU A 487     -15.801 100.385  56.201  1.00 40.59           C  
ATOM   3713  O   LEU A 487     -15.338 100.568  55.073  1.00 41.06           O  
ATOM   3714  CB  LEU A 487     -16.476 102.318  57.640  1.00 32.89           C  
ATOM   3715  CG  LEU A 487     -16.403 103.132  58.933  1.00 32.07           C  
ATOM   3716  CD1 LEU A 487     -17.570 104.101  58.994  1.00 29.05           C  
ATOM   3717  CD2 LEU A 487     -16.437 102.210  60.125  1.00 28.68           C  
ATOM   3718  N   GLU A 488     -16.632  99.393  56.495  1.00 43.09           N  
ATOM   3719  CA  GLU A 488     -17.148  98.470  55.494  1.00 44.77           C  
ATOM   3720  C   GLU A 488     -18.052  99.332  54.623  1.00 47.61           C  
ATOM   3721  O   GLU A 488     -18.746 100.210  55.141  1.00 49.37           O  
ATOM   3722  CB  GLU A 488     -17.980  97.394  56.184  1.00 42.98           C  
ATOM   3723  CG  GLU A 488     -17.983  96.059  55.491  1.00 49.86           C  
ATOM   3724  CD  GLU A 488     -16.685  95.309  55.695  1.00 54.24           C  
ATOM   3725  OE1 GLU A 488     -16.365  94.970  56.858  1.00 54.89           O  
ATOM   3726  OE2 GLU A 488     -15.986  95.057  54.691  1.00 58.06           O  
ATOM   3727  N   HIS A 489     -18.051  99.101  53.313  1.00 48.91           N  
ATOM   3728  CA  HIS A 489     -18.879  99.901  52.420  1.00 47.98           C  
ATOM   3729  C   HIS A 489     -20.357  99.897  52.805  1.00 46.53           C  
ATOM   3730  O   HIS A 489     -20.969  98.838  52.976  1.00 43.86           O  
ATOM   3731  CB  HIS A 489     -18.738  99.446  50.966  1.00 52.17           C  
ATOM   3732  CG  HIS A 489     -19.672 100.153  50.032  1.00 55.19           C  
ATOM   3733  ND1 HIS A 489     -20.889  99.628  49.655  1.00 57.14           N  
ATOM   3734  CD2 HIS A 489     -19.592 101.371  49.442  1.00 57.64           C  
ATOM   3735  CE1 HIS A 489     -21.521 100.488  48.877  1.00 55.58           C  
ATOM   3736  NE2 HIS A 489     -20.753 101.553  48.731  1.00 57.43           N  
ATOM   3737  N   GLY A 490     -20.920 101.094  52.929  1.00 46.35           N  
ATOM   3738  CA  GLY A 490     -22.326 101.225  53.263  1.00 49.81           C  
ATOM   3739  C   GLY A 490     -22.668 101.279  54.740  1.00 52.38           C  
ATOM   3740  O   GLY A 490     -23.806 101.587  55.094  1.00 53.09           O  
ATOM   3741  N   LYS A 491     -21.698 101.010  55.608  1.00 52.77           N  
ATOM   3742  CA  LYS A 491     -21.946 101.016  57.047  1.00 50.77           C  
ATOM   3743  C   LYS A 491     -21.454 102.313  57.695  1.00 50.61           C  
ATOM   3744  O   LYS A 491     -20.464 102.905  57.252  1.00 50.98           O  
ATOM   3745  CB  LYS A 491     -21.299  99.782  57.687  1.00 50.94           C  
ATOM   3746  CG  LYS A 491     -21.334  98.558  56.769  1.00 56.88           C  
ATOM   3747  CD  LYS A 491     -21.596  97.248  57.496  1.00 61.18           C  
ATOM   3748  CE  LYS A 491     -23.027  97.175  58.004  1.00 64.68           C  
ATOM   3749  NZ  LYS A 491     -23.357  95.818  58.532  1.00 67.84           N  
ATOM   3750  N   THR A 492     -22.181 102.783  58.707  1.00 49.59           N  
ATOM   3751  CA  THR A 492     -21.829 104.019  59.409  1.00 48.60           C  
ATOM   3752  C   THR A 492     -21.458 103.746  60.868  1.00 48.71           C  
ATOM   3753  O   THR A 492     -22.147 102.990  61.559  1.00 50.26           O  
ATOM   3754  CB  THR A 492     -22.992 105.031  59.386  1.00 49.02           C  
ATOM   3755  N   MET A 493     -20.373 104.364  61.334  1.00 44.17           N  
ATOM   3756  CA  MET A 493     -19.912 104.188  62.709  1.00 41.39           C  
ATOM   3757  C   MET A 493     -19.151 105.428  63.175  1.00 41.74           C  
ATOM   3758  O   MET A 493     -18.368 105.999  62.414  1.00 44.18           O  
ATOM   3759  CB  MET A 493     -19.023 102.945  62.812  1.00 38.77           C  
ATOM   3760  CG  MET A 493     -18.824 102.458  64.228  1.00 35.56           C  
ATOM   3761  SD  MET A 493     -18.236 100.768  64.281  1.00 39.82           S  
ATOM   3762  CE  MET A 493     -18.105 100.523  66.037  1.00 31.48           C  
ATOM   3763  N   THR A 494     -19.413 105.863  64.407  1.00 41.31           N  
ATOM   3764  CA  THR A 494     -18.760 107.047  64.967  1.00 41.78           C  
ATOM   3765  C   THR A 494     -17.490 106.699  65.738  1.00 42.02           C  
ATOM   3766  O   THR A 494     -17.310 105.561  66.190  1.00 44.39           O  
ATOM   3767  CB  THR A 494     -19.713 107.838  65.909  1.00 41.75           C  
ATOM   3768  OG1 THR A 494     -19.790 107.194  67.189  1.00 40.97           O  
ATOM   3769  CG2 THR A 494     -21.114 107.907  65.315  1.00 45.50           C  
ATOM   3770  N   GLU A 495     -16.614 107.687  65.888  1.00 40.15           N  
ATOM   3771  CA  GLU A 495     -15.370 107.500  66.618  1.00 39.41           C  
ATOM   3772  C   GLU A 495     -15.689 106.998  68.019  1.00 40.80           C  
ATOM   3773  O   GLU A 495     -15.039 106.078  68.517  1.00 36.08           O  
ATOM   3774  CB  GLU A 495     -14.607 108.820  66.706  1.00 42.03           C  
ATOM   3775  CG  GLU A 495     -13.366 108.769  67.592  1.00 47.83           C  
ATOM   3776  CD  GLU A 495     -12.772 110.143  67.847  1.00 50.81           C  
ATOM   3777  OE1 GLU A 495     -13.548 111.094  68.076  1.00 54.99           O  
ATOM   3778  OE2 GLU A 495     -11.530 110.274  67.822  1.00 52.80           O  
ATOM   3779  N   LYS A 496     -16.713 107.589  68.633  1.00 39.98           N  
ATOM   3780  CA  LYS A 496     -17.130 107.215  69.976  1.00 37.60           C  
ATOM   3781  C   LYS A 496     -17.524 105.747  70.043  1.00 35.86           C  
ATOM   3782  O   LYS A 496     -17.068 105.024  70.922  1.00 38.11           O  
ATOM   3783  CB  LYS A 496     -18.293 108.087  70.451  1.00 42.22           C  
ATOM   3784  CG  LYS A 496     -18.856 107.683  71.818  1.00 47.54           C  
ATOM   3785  CD  LYS A 496     -20.035 108.553  72.245  1.00 50.72           C  
ATOM   3786  CE  LYS A 496     -20.582 108.117  73.603  1.00 53.64           C  
ATOM   3787  NZ  LYS A 496     -19.530 108.107  74.665  1.00 53.33           N  
ATOM   3788  N   GLU A 497     -18.362 105.308  69.111  1.00 32.47           N  
ATOM   3789  CA  GLU A 497     -18.795 103.918  69.093  1.00 29.93           C  
ATOM   3790  C   GLU A 497     -17.590 102.993  69.034  1.00 28.91           C  
ATOM   3791  O   GLU A 497     -17.516 102.014  69.775  1.00 32.07           O  
ATOM   3792  CB  GLU A 497     -19.711 103.641  67.901  1.00 32.27           C  
ATOM   3793  CG  GLU A 497     -21.052 104.343  67.962  1.00 37.01           C  
ATOM   3794  CD  GLU A 497     -21.953 103.989  66.793  1.00 39.86           C  
ATOM   3795  OE1 GLU A 497     -21.543 104.176  65.627  1.00 41.32           O  
ATOM   3796  OE2 GLU A 497     -23.083 103.526  67.043  1.00 42.13           O  
ATOM   3797  N   ILE A 498     -16.638 103.318  68.166  1.00 29.83           N  
ATOM   3798  CA  ILE A 498     -15.431 102.510  68.016  1.00 31.93           C  
ATOM   3799  C   ILE A 498     -14.617 102.478  69.314  1.00 33.84           C  
ATOM   3800  O   ILE A 498     -14.237 101.404  69.787  1.00 31.62           O  
ATOM   3801  CB  ILE A 498     -14.566 103.017  66.842  1.00 33.44           C  
ATOM   3802  CG1 ILE A 498     -15.337 102.854  65.526  1.00 30.39           C  
ATOM   3803  CG2 ILE A 498     -13.242 102.261  66.793  1.00 33.63           C  
ATOM   3804  CD1 ILE A 498     -14.633 103.398  64.306  1.00 29.95           C  
ATOM   3805  N   VAL A 499     -14.386 103.651  69.902  1.00 35.99           N  
ATOM   3806  CA  VAL A 499     -13.633 103.770  71.151  1.00 35.56           C  
ATOM   3807  C   VAL A 499     -14.317 102.974  72.266  1.00 37.29           C  
ATOM   3808  O   VAL A 499     -13.668 102.215  72.992  1.00 36.43           O  
ATOM   3809  CB  VAL A 499     -13.485 105.253  71.587  1.00 33.22           C  
ATOM   3810  CG1 VAL A 499     -12.843 105.345  72.967  1.00 32.03           C  
ATOM   3811  CG2 VAL A 499     -12.638 106.019  70.566  1.00 34.42           C  
ATOM   3812  N   ASP A 500     -15.635 103.125  72.376  1.00 36.72           N  
ATOM   3813  CA  ASP A 500     -16.410 102.418  73.391  1.00 34.73           C  
ATOM   3814  C   ASP A 500     -16.351 100.915  73.168  1.00 33.13           C  
ATOM   3815  O   ASP A 500     -16.212 100.149  74.121  1.00 34.87           O  
ATOM   3816  CB  ASP A 500     -17.857 102.915  73.416  1.00 34.17           C  
ATOM   3817  CG  ASP A 500     -17.984 104.319  73.992  1.00 36.65           C  
ATOM   3818  OD1 ASP A 500     -17.016 104.804  74.614  1.00 41.12           O  
ATOM   3819  OD2 ASP A 500     -19.053 104.943  73.828  1.00 38.83           O  
ATOM   3820  N   TYR A 501     -16.419 100.496  71.911  1.00 32.48           N  
ATOM   3821  CA  TYR A 501     -16.337  99.077  71.581  1.00 34.84           C  
ATOM   3822  C   TYR A 501     -14.990  98.517  72.027  1.00 36.28           C  
ATOM   3823  O   TYR A 501     -14.919  97.437  72.619  1.00 38.52           O  
ATOM   3824  CB  TYR A 501     -16.505  98.861  70.079  1.00 31.62           C  
ATOM   3825  CG  TYR A 501     -16.015  97.514  69.599  1.00 33.42           C  
ATOM   3826  CD1 TYR A 501     -16.600  96.332  70.053  1.00 33.65           C  
ATOM   3827  CD2 TYR A 501     -14.977  97.425  68.675  1.00 30.11           C  
ATOM   3828  CE1 TYR A 501     -16.164  95.101  69.596  1.00 36.22           C  
ATOM   3829  CE2 TYR A 501     -14.535  96.199  68.210  1.00 31.22           C  
ATOM   3830  CZ  TYR A 501     -15.134  95.042  68.672  1.00 34.53           C  
ATOM   3831  OH  TYR A 501     -14.719  93.825  68.191  1.00 39.15           O  
ATOM   3832  N   VAL A 502     -13.920  99.240  71.719  1.00 32.59           N  
ATOM   3833  CA  VAL A 502     -12.595  98.801  72.106  1.00 34.49           C  
ATOM   3834  C   VAL A 502     -12.528  98.649  73.623  1.00 36.08           C  
ATOM   3835  O   VAL A 502     -12.062  97.622  74.123  1.00 38.84           O  
ATOM   3836  CB  VAL A 502     -11.508  99.788  71.629  1.00 33.30           C  
ATOM   3837  CG1 VAL A 502     -10.155  99.398  72.200  1.00 29.73           C  
ATOM   3838  CG2 VAL A 502     -11.444  99.795  70.114  1.00 28.72           C  
ATOM   3839  N   ALA A 503     -13.051  99.644  74.340  1.00 37.41           N  
ATOM   3840  CA  ALA A 503     -13.055  99.642  75.801  1.00 37.37           C  
ATOM   3841  C   ALA A 503     -13.743  98.410  76.392  1.00 41.83           C  
ATOM   3842  O   ALA A 503     -13.262  97.832  77.371  1.00 44.34           O  
ATOM   3843  CB  ALA A 503     -13.704 100.912  76.330  1.00 31.22           C  
ATOM   3844  N   SER A 504     -14.842  97.981  75.775  1.00 43.72           N  
ATOM   3845  CA  SER A 504     -15.582  96.816  76.251  1.00 43.98           C  
ATOM   3846  C   SER A 504     -14.848  95.507  75.964  1.00 47.39           C  
ATOM   3847  O   SER A 504     -15.371  94.420  76.238  1.00 48.01           O  
ATOM   3848  CB  SER A 504     -16.973  96.780  75.607  1.00 41.20           C  
ATOM   3849  OG  SER A 504     -16.895  96.530  74.214  1.00 41.66           O  
ATOM   3850  N   GLN A 505     -13.632  95.604  75.431  1.00 48.99           N  
ATOM   3851  CA  GLN A 505     -12.854  94.419  75.085  1.00 50.28           C  
ATOM   3852  C   GLN A 505     -11.466  94.349  75.703  1.00 51.75           C  
ATOM   3853  O   GLN A 505     -10.862  93.277  75.723  1.00 56.45           O  
ATOM   3854  CB  GLN A 505     -12.707  94.326  73.566  1.00 48.80           C  
ATOM   3855  CG  GLN A 505     -14.013  94.286  72.820  1.00 46.25           C  
ATOM   3856  CD  GLN A 505     -14.662  92.931  72.869  1.00 42.86           C  
ATOM   3857  OE1 GLN A 505     -14.715  92.235  71.866  1.00 44.63           O  
ATOM   3858  NE2 GLN A 505     -15.180  92.553  74.029  1.00 48.61           N  
ATOM   3859  N   VAL A 506     -10.952  95.470  76.196  1.00 53.38           N  
ATOM   3860  CA  VAL A 506      -9.606  95.483  76.765  1.00 54.97           C  
ATOM   3861  C   VAL A 506      -9.489  96.097  78.154  1.00 57.81           C  
ATOM   3862  O   VAL A 506     -10.393  96.792  78.623  1.00 58.64           O  
ATOM   3863  CB  VAL A 506      -8.616  96.224  75.839  1.00 52.70           C  
ATOM   3864  CG1 VAL A 506      -8.389  95.433  74.572  1.00 48.00           C  
ATOM   3865  CG2 VAL A 506      -9.144  97.608  75.521  1.00 46.19           C  
ATOM   3866  N   THR A 507      -8.347  95.845  78.792  1.00 58.78           N  
ATOM   3867  CA  THR A 507      -8.063  96.360  80.129  1.00 59.47           C  
ATOM   3868  C   THR A 507      -7.993  97.884  80.033  1.00 56.13           C  
ATOM   3869  O   THR A 507      -7.672  98.417  78.973  1.00 56.28           O  
ATOM   3870  CB  THR A 507      -6.708  95.810  80.664  1.00 63.41           C  
ATOM   3871  OG1 THR A 507      -5.618  96.491  80.024  1.00 67.48           O  
ATOM   3872  CG2 THR A 507      -6.585  94.310  80.379  1.00 59.85           C  
ATOM   3873  N   THR A 508      -8.248  98.582  81.137  1.00 56.34           N  
ATOM   3874  CA  THR A 508      -8.220 100.047  81.142  1.00 57.39           C  
ATOM   3875  C   THR A 508      -6.904 100.628  80.616  1.00 59.87           C  
ATOM   3876  O   THR A 508      -6.827 101.817  80.289  1.00 60.59           O  
ATOM   3877  CB  THR A 508      -8.487 100.615  82.552  1.00 52.25           C  
ATOM   3878  N   ALA A 509      -5.880  99.780  80.527  1.00 61.76           N  
ATOM   3879  CA  ALA A 509      -4.559 100.182  80.050  1.00 61.14           C  
ATOM   3880  C   ALA A 509      -4.436 100.183  78.522  1.00 61.95           C  
ATOM   3881  O   ALA A 509      -3.597 100.892  77.956  1.00 63.52           O  
ATOM   3882  CB  ALA A 509      -3.502  99.262  80.649  1.00 60.22           C  
ATOM   3883  N   LYS A 510      -5.284  99.407  77.857  1.00 59.09           N  
ATOM   3884  CA  LYS A 510      -5.248  99.285  76.404  1.00 53.57           C  
ATOM   3885  C   LYS A 510      -6.344 100.035  75.640  1.00 54.02           C  
ATOM   3886  O   LYS A 510      -6.580  99.751  74.468  1.00 54.65           O  
ATOM   3887  CB  LYS A 510      -5.299  97.800  76.038  1.00 54.10           C  
ATOM   3888  CG  LYS A 510      -4.203  96.969  76.682  1.00 53.57           C  
ATOM   3889  CD  LYS A 510      -4.457  95.490  76.482  1.00 52.80           C  
ATOM   3890  CE  LYS A 510      -3.164  94.714  76.526  1.00 51.72           C  
ATOM   3891  NZ  LYS A 510      -3.430  93.265  76.372  1.00 53.56           N  
ATOM   3892  N   LYS A 511      -6.991 101.002  76.282  1.00 52.79           N  
ATOM   3893  CA  LYS A 511      -8.068 101.767  75.642  1.00 53.67           C  
ATOM   3894  C   LYS A 511      -7.614 102.688  74.500  1.00 52.68           C  
ATOM   3895  O   LYS A 511      -6.509 103.244  74.543  1.00 55.11           O  
ATOM   3896  CB  LYS A 511      -8.826 102.584  76.697  1.00 52.38           C  
ATOM   3897  CG  LYS A 511      -9.683 101.743  77.620  1.00 56.35           C  
ATOM   3898  CD  LYS A 511     -10.326 102.587  78.702  1.00 61.63           C  
ATOM   3899  CE  LYS A 511     -11.323 101.777  79.510  1.00 66.31           C  
ATOM   3900  NZ  LYS A 511     -11.848 102.541  80.675  1.00 69.57           N  
ATOM   3901  N   LEU A 512      -8.471 102.848  73.488  1.00 49.10           N  
ATOM   3902  CA  LEU A 512      -8.187 103.700  72.330  1.00 43.80           C  
ATOM   3903  C   LEU A 512      -8.359 105.177  72.666  1.00 42.50           C  
ATOM   3904  O   LEU A 512      -9.132 105.884  72.015  1.00 44.20           O  
ATOM   3905  CB  LEU A 512      -9.121 103.359  71.164  1.00 41.05           C  
ATOM   3906  CG  LEU A 512      -8.617 102.658  69.902  1.00 36.78           C  
ATOM   3907  CD1 LEU A 512      -9.437 103.146  68.715  1.00 29.65           C  
ATOM   3908  CD2 LEU A 512      -7.164 102.956  69.663  1.00 32.62           C  
ATOM   3909  N   ARG A 513      -7.609 105.656  73.649  1.00 42.73           N  
ATOM   3910  CA  ARG A 513      -7.705 107.048  74.067  1.00 45.84           C  
ATOM   3911  C   ARG A 513      -7.300 108.018  72.960  1.00 43.67           C  
ATOM   3912  O   ARG A 513      -7.821 109.127  72.879  1.00 43.62           O  
ATOM   3913  CB  ARG A 513      -6.858 107.276  75.323  1.00 49.17           C  
ATOM   3914  CG  ARG A 513      -7.277 106.398  76.488  1.00 56.02           C  
ATOM   3915  CD  ARG A 513      -6.366 106.561  77.695  1.00 58.28           C  
ATOM   3916  NE  ARG A 513      -6.610 105.528  78.700  1.00 57.20           N  
ATOM   3917  CZ  ARG A 513      -7.510 105.621  79.674  1.00 60.15           C  
ATOM   3918  NH1 ARG A 513      -8.261 106.713  79.798  1.00 63.06           N  
ATOM   3919  NH2 ARG A 513      -7.674 104.608  80.514  1.00 59.93           N  
ATOM   3920  N   GLY A 514      -6.390 107.581  72.097  1.00 45.15           N  
ATOM   3921  CA  GLY A 514      -5.922 108.420  71.007  1.00 46.92           C  
ATOM   3922  C   GLY A 514      -7.014 108.766  70.014  1.00 48.74           C  
ATOM   3923  O   GLY A 514      -6.905 109.755  69.282  1.00 50.09           O  
ATOM   3924  N   GLY A 515      -8.044 107.924  69.954  1.00 48.01           N  
ATOM   3925  CA  GLY A 515      -9.152 108.174  69.049  1.00 45.74           C  
ATOM   3926  C   GLY A 515      -9.086 107.480  67.701  1.00 41.50           C  
ATOM   3927  O   GLY A 515      -8.179 106.680  67.438  1.00 39.43           O  
ATOM   3928  N   VAL A 516     -10.045 107.820  66.841  1.00 38.75           N  
ATOM   3929  CA  VAL A 516     -10.169 107.238  65.510  1.00 37.73           C  
ATOM   3930  C   VAL A 516     -10.167 108.260  64.380  1.00 38.82           C  
ATOM   3931  O   VAL A 516     -10.801 109.318  64.464  1.00 39.72           O  
ATOM   3932  CB  VAL A 516     -11.485 106.422  65.379  1.00 33.65           C  
ATOM   3933  CG1 VAL A 516     -11.652 105.917  63.945  1.00 28.36           C  
ATOM   3934  CG2 VAL A 516     -11.478 105.269  66.355  1.00 33.49           C  
ATOM   3935  N   VAL A 517      -9.445 107.925  63.320  1.00 39.08           N  
ATOM   3936  CA  VAL A 517      -9.371 108.762  62.134  1.00 38.37           C  
ATOM   3937  C   VAL A 517      -9.832 107.869  60.984  1.00 37.26           C  
ATOM   3938  O   VAL A 517      -9.212 106.841  60.695  1.00 33.69           O  
ATOM   3939  CB  VAL A 517      -7.939 109.274  61.872  1.00 37.82           C  
ATOM   3940  CG1 VAL A 517      -7.871 110.008  60.551  1.00 38.72           C  
ATOM   3941  CG2 VAL A 517      -7.506 110.206  62.992  1.00 38.83           C  
ATOM   3942  N   PHE A 518     -10.985 108.204  60.415  1.00 36.14           N  
ATOM   3943  CA  PHE A 518     -11.542 107.454  59.302  1.00 37.58           C  
ATOM   3944  C   PHE A 518     -10.792 107.730  58.005  1.00 37.12           C  
ATOM   3945  O   PHE A 518     -10.708 108.872  57.555  1.00 39.20           O  
ATOM   3946  CB  PHE A 518     -13.029 107.775  59.146  1.00 35.64           C  
ATOM   3947  CG  PHE A 518     -13.865 107.332  60.309  1.00 34.24           C  
ATOM   3948  CD1 PHE A 518     -14.090 105.979  60.541  1.00 37.27           C  
ATOM   3949  CD2 PHE A 518     -14.400 108.261  61.192  1.00 34.60           C  
ATOM   3950  CE1 PHE A 518     -14.835 105.552  61.641  1.00 37.64           C  
ATOM   3951  CE2 PHE A 518     -15.147 107.849  62.298  1.00 36.81           C  
ATOM   3952  CZ  PHE A 518     -15.364 106.491  62.524  1.00 39.22           C  
ATOM   3953  N   VAL A 519     -10.203 106.680  57.445  1.00 39.04           N  
ATOM   3954  CA  VAL A 519      -9.452 106.769  56.197  1.00 40.45           C  
ATOM   3955  C   VAL A 519     -10.098 105.806  55.200  1.00 46.64           C  
ATOM   3956  O   VAL A 519     -10.840 104.901  55.586  1.00 48.24           O  
ATOM   3957  CB  VAL A 519      -7.948 106.382  56.385  1.00 35.33           C  
ATOM   3958  CG1 VAL A 519      -7.281 107.288  57.404  1.00 32.08           C  
ATOM   3959  CG2 VAL A 519      -7.810 104.929  56.806  1.00 32.38           C  
ATOM   3960  N   ASP A 520      -9.841 106.018  53.917  1.00 49.24           N  
ATOM   3961  CA  ASP A 520     -10.397 105.150  52.890  1.00 52.38           C  
ATOM   3962  C   ASP A 520      -9.443 103.984  52.630  1.00 53.69           C  
ATOM   3963  O   ASP A 520      -9.833 102.968  52.044  1.00 53.89           O  
ATOM   3964  CB  ASP A 520     -10.656 105.947  51.606  1.00 54.48           C  
ATOM   3965  CG  ASP A 520     -11.515 107.187  51.851  1.00 59.00           C  
ATOM   3966  OD1 ASP A 520     -12.570 107.070  52.511  1.00 58.16           O  
ATOM   3967  OD2 ASP A 520     -11.127 108.283  51.396  1.00 62.37           O  
ATOM   3968  N   GLU A 521      -8.204 104.118  53.104  1.00 55.57           N  
ATOM   3969  CA  GLU A 521      -7.198 103.078  52.925  1.00 57.42           C  
ATOM   3970  C   GLU A 521      -6.076 103.197  53.959  1.00 55.79           C  
ATOM   3971  O   GLU A 521      -5.512 104.276  54.157  1.00 56.32           O  
ATOM   3972  CB  GLU A 521      -6.634 103.152  51.502  1.00 64.40           C  
ATOM   3973  CG  GLU A 521      -5.931 101.883  51.028  1.00 70.77           C  
ATOM   3974  CD  GLU A 521      -5.661 101.884  49.524  1.00 74.36           C  
ATOM   3975  OE1 GLU A 521      -5.727 102.967  48.894  1.00 72.18           O  
ATOM   3976  OE2 GLU A 521      -5.374 100.796  48.975  1.00 75.72           O  
ATOM   3977  N   VAL A 522      -5.792 102.097  54.651  1.00 52.24           N  
ATOM   3978  CA  VAL A 522      -4.732 102.063  55.657  1.00 50.90           C  
ATOM   3979  C   VAL A 522      -3.397 101.945  54.936  1.00 51.89           C  
ATOM   3980  O   VAL A 522      -3.197 101.025  54.142  1.00 52.15           O  
ATOM   3981  CB  VAL A 522      -4.889 100.857  56.631  1.00 51.12           C  
ATOM   3982  CG1 VAL A 522      -3.722 100.803  57.613  1.00 46.22           C  
ATOM   3983  CG2 VAL A 522      -6.211 100.959  57.390  1.00 47.18           C  
ATOM   3984  N   PRO A 523      -2.484 102.904  55.166  1.00 52.07           N  
ATOM   3985  CA  PRO A 523      -1.165 102.892  54.528  1.00 51.48           C  
ATOM   3986  C   PRO A 523      -0.366 101.606  54.755  1.00 53.17           C  
ATOM   3987  O   PRO A 523      -0.142 101.180  55.893  1.00 53.97           O  
ATOM   3988  CB  PRO A 523      -0.480 104.126  55.125  1.00 50.50           C  
ATOM   3989  CG  PRO A 523      -1.240 104.391  56.396  1.00 51.91           C  
ATOM   3990  CD  PRO A 523      -2.648 104.102  56.005  1.00 52.18           C  
ATOM   3991  N   LYS A 524       0.023 100.979  53.649  1.00 54.46           N  
ATOM   3992  CA  LYS A 524       0.790  99.742  53.668  1.00 54.72           C  
ATOM   3993  C   LYS A 524       2.175 100.020  53.102  1.00 57.23           C  
ATOM   3994  O   LYS A 524       2.389 101.021  52.413  1.00 54.08           O  
ATOM   3995  CB  LYS A 524       0.109  98.684  52.793  1.00 54.73           C  
ATOM   3996  CG  LYS A 524      -1.341  98.427  53.126  1.00 54.34           C  
ATOM   3997  CD  LYS A 524      -1.490  97.316  54.140  1.00 54.88           C  
ATOM   3998  CE  LYS A 524      -2.939  97.186  54.593  1.00 57.61           C  
ATOM   3999  NZ  LYS A 524      -3.907  97.186  53.464  1.00 56.46           N  
ATOM   4000  N   GLY A 525       3.108  99.122  53.397  1.00 60.83           N  
ATOM   4001  CA  GLY A 525       4.463  99.252  52.903  1.00 65.53           C  
ATOM   4002  C   GLY A 525       4.714  98.210  51.834  1.00 68.70           C  
ATOM   4003  O   GLY A 525       3.933  97.265  51.690  1.00 70.45           O  
ATOM   4004  N   LEU A 526       5.798  98.377  51.085  1.00 69.59           N  
ATOM   4005  CA  LEU A 526       6.165  97.443  50.023  1.00 70.20           C  
ATOM   4006  C   LEU A 526       6.291  96.000  50.526  1.00 73.78           C  
ATOM   4007  O   LEU A 526       6.078  95.053  49.764  1.00 73.97           O  
ATOM   4008  CB  LEU A 526       7.476  97.889  49.366  1.00 64.39           C  
ATOM   4009  CG  LEU A 526       7.454  99.194  48.569  1.00 58.47           C  
ATOM   4010  CD1 LEU A 526       8.858  99.533  48.124  1.00 57.53           C  
ATOM   4011  CD2 LEU A 526       6.533  99.062  47.365  1.00 57.01           C  
ATOM   4012  N   THR A 527       6.641  95.841  51.802  1.00 78.67           N  
ATOM   4013  CA  THR A 527       6.784  94.518  52.403  1.00 79.43           C  
ATOM   4014  C   THR A 527       5.448  93.796  52.361  1.00 79.31           C  
ATOM   4015  O   THR A 527       5.396  92.576  52.198  1.00 78.99           O  
ATOM   4016  CB  THR A 527       7.200  94.601  53.896  1.00 80.18           C  
ATOM   4017  OG1 THR A 527       7.401  95.973  54.271  1.00 81.69           O  
ATOM   4018  CG2 THR A 527       8.468  93.779  54.149  1.00 79.00           C  
ATOM   4019  N   GLY A 528       4.376  94.578  52.470  1.00 80.35           N  
ATOM   4020  CA  GLY A 528       3.026  94.043  52.488  1.00 78.37           C  
ATOM   4021  C   GLY A 528       2.535  94.099  53.923  1.00 75.13           C  
ATOM   4022  O   GLY A 528       1.622  93.374  54.319  1.00 76.21           O  
ATOM   4023  N   LYS A 529       3.170  94.966  54.706  1.00 69.62           N  
ATOM   4024  CA  LYS A 529       2.845  95.144  56.108  1.00 65.91           C  
ATOM   4025  C   LYS A 529       2.415  96.588  56.313  1.00 64.22           C  
ATOM   4026  O   LYS A 529       2.733  97.452  55.499  1.00 62.34           O  
ATOM   4027  CB  LYS A 529       4.062  94.821  56.979  1.00 62.80           C  
ATOM   4028  N   LEU A 530       1.674  96.836  57.389  1.00 63.29           N  
ATOM   4029  CA  LEU A 530       1.182  98.174  57.713  1.00 61.23           C  
ATOM   4030  C   LEU A 530       2.327  99.142  57.947  1.00 59.75           C  
ATOM   4031  O   LEU A 530       3.372  98.759  58.475  1.00 59.04           O  
ATOM   4032  CB  LEU A 530       0.296  98.131  58.961  1.00 60.46           C  
ATOM   4033  CG  LEU A 530      -0.984  97.301  58.893  1.00 59.27           C  
ATOM   4034  CD1 LEU A 530      -1.718  97.390  60.213  1.00 59.06           C  
ATOM   4035  CD2 LEU A 530      -1.866  97.813  57.775  1.00 63.72           C  
ATOM   4036  N   ASP A 531       2.117 100.397  57.566  1.00 59.37           N  
ATOM   4037  CA  ASP A 531       3.130 101.426  57.738  1.00 62.37           C  
ATOM   4038  C   ASP A 531       2.813 102.308  58.943  1.00 61.53           C  
ATOM   4039  O   ASP A 531       2.108 103.316  58.823  1.00 60.57           O  
ATOM   4040  CB  ASP A 531       3.255 102.278  56.466  1.00 67.67           C  
ATOM   4041  CG  ASP A 531       4.341 103.354  56.573  1.00 71.15           C  
ATOM   4042  OD1 ASP A 531       5.367 103.125  57.257  1.00 73.35           O  
ATOM   4043  OD2 ASP A 531       4.170 104.431  55.961  1.00 72.18           O  
ATOM   4044  N   ALA A 532       3.396 101.951  60.085  1.00 61.16           N  
ATOM   4045  CA  ALA A 532       3.204 102.676  61.340  1.00 58.98           C  
ATOM   4046  C   ALA A 532       3.510 104.177  61.248  1.00 56.93           C  
ATOM   4047  O   ALA A 532       2.789 104.994  61.819  1.00 55.48           O  
ATOM   4048  CB  ALA A 532       4.043 102.032  62.444  1.00 57.26           C  
ATOM   4049  N   ARG A 533       4.563 104.535  60.513  1.00 56.28           N  
ATOM   4050  CA  ARG A 533       4.964 105.937  60.362  1.00 55.06           C  
ATOM   4051  C   ARG A 533       3.896 106.788  59.675  1.00 54.95           C  
ATOM   4052  O   ARG A 533       3.601 107.899  60.123  1.00 57.44           O  
ATOM   4053  CB  ARG A 533       6.297 106.044  59.609  1.00 53.94           C  
ATOM   4054  N   LYS A 534       3.302 106.270  58.601  1.00 52.17           N  
ATOM   4055  CA  LYS A 534       2.270 107.017  57.888  1.00 49.68           C  
ATOM   4056  C   LYS A 534       0.995 107.115  58.723  1.00 48.14           C  
ATOM   4057  O   LYS A 534       0.336 108.153  58.731  1.00 48.13           O  
ATOM   4058  CB  LYS A 534       1.971 106.387  56.532  1.00 48.88           C  
ATOM   4059  N   ILE A 535       0.648 106.033  59.421  1.00 48.04           N  
ATOM   4060  CA  ILE A 535      -0.544 106.011  60.282  1.00 48.14           C  
ATOM   4061  C   ILE A 535      -0.384 107.095  61.346  1.00 48.98           C  
ATOM   4062  O   ILE A 535      -1.314 107.862  61.617  1.00 47.54           O  
ATOM   4063  CB  ILE A 535      -0.719 104.639  60.996  1.00 46.53           C  
ATOM   4064  CG1 ILE A 535      -0.887 103.516  59.970  1.00 46.57           C  
ATOM   4065  CG2 ILE A 535      -1.920 104.679  61.940  1.00 45.61           C  
ATOM   4066  CD1 ILE A 535      -0.866 102.120  60.572  1.00 43.61           C  
ATOM   4067  N   ARG A 536       0.812 107.153  61.931  1.00 51.33           N  
ATOM   4068  CA  ARG A 536       1.143 108.136  62.957  1.00 52.33           C  
ATOM   4069  C   ARG A 536       0.951 109.537  62.387  1.00 51.95           C  
ATOM   4070  O   ARG A 536       0.323 110.388  63.024  1.00 53.16           O  
ATOM   4071  CB  ARG A 536       2.594 107.952  63.402  1.00 54.99           C  
ATOM   4072  CG  ARG A 536       2.824 108.029  64.906  1.00 61.15           C  
ATOM   4073  CD  ARG A 536       3.523 106.767  65.407  1.00 64.07           C  
ATOM   4074  NE  ARG A 536       4.746 106.488  64.654  1.00 69.10           N  
ATOM   4075  CZ  ARG A 536       5.364 105.310  64.628  1.00 71.99           C  
ATOM   4076  NH1 ARG A 536       4.884 104.282  65.317  1.00 74.17           N  
ATOM   4077  NH2 ARG A 536       6.459 105.154  63.889  1.00 72.44           N  
ATOM   4078  N   GLU A 537       1.462 109.757  61.174  1.00 52.62           N  
ATOM   4079  CA  GLU A 537       1.358 111.046  60.488  1.00 52.88           C  
ATOM   4080  C   GLU A 537      -0.100 111.486  60.298  1.00 51.42           C  
ATOM   4081  O   GLU A 537      -0.460 112.631  60.602  1.00 53.91           O  
ATOM   4082  CB  GLU A 537       2.074 110.991  59.134  1.00 52.47           C  
ATOM   4083  N   ILE A 538      -0.937 110.563  59.830  1.00 49.13           N  
ATOM   4084  CA  ILE A 538      -2.358 110.842  59.609  1.00 47.00           C  
ATOM   4085  C   ILE A 538      -3.037 111.238  60.925  1.00 45.21           C  
ATOM   4086  O   ILE A 538      -3.777 112.226  60.976  1.00 41.20           O  
ATOM   4087  CB  ILE A 538      -3.090 109.612  59.008  1.00 45.06           C  
ATOM   4088  CG1 ILE A 538      -2.430 109.178  57.697  1.00 39.08           C  
ATOM   4089  CG2 ILE A 538      -4.556 109.936  58.762  1.00 47.96           C  
ATOM   4090  CD1 ILE A 538      -2.980 107.882  57.143  1.00 37.98           C  
ATOM   4091  N   LEU A 539      -2.764 110.473  61.982  1.00 45.01           N  
ATOM   4092  CA  LEU A 539      -3.324 110.722  63.311  1.00 47.61           C  
ATOM   4093  C   LEU A 539      -2.926 112.093  63.849  1.00 50.33           C  
ATOM   4094  O   LEU A 539      -3.743 112.800  64.442  1.00 52.20           O  
ATOM   4095  CB  LEU A 539      -2.858 109.643  64.294  1.00 47.29           C  
ATOM   4096  CG  LEU A 539      -3.400 108.226  64.101  1.00 50.88           C  
ATOM   4097  CD1 LEU A 539      -2.565 107.225  64.892  1.00 43.87           C  
ATOM   4098  CD2 LEU A 539      -4.866 108.180  64.516  1.00 49.51           C  
ATOM   4099  N   ILE A 540      -1.667 112.467  63.640  1.00 51.65           N  
ATOM   4100  CA  ILE A 540      -1.165 113.752  64.109  1.00 48.68           C  
ATOM   4101  C   ILE A 540      -1.795 114.903  63.340  1.00 45.56           C  
ATOM   4102  O   ILE A 540      -2.391 115.798  63.936  1.00 41.77           O  
ATOM   4103  CB  ILE A 540       0.377 113.813  64.022  1.00 49.68           C  
ATOM   4104  CG1 ILE A 540       0.980 112.784  64.986  1.00 50.65           C  
ATOM   4105  CG2 ILE A 540       0.876 115.206  64.374  1.00 49.40           C  
ATOM   4106  CD1 ILE A 540       2.491 112.681  64.947  1.00 51.37           C  
ATOM   4107  N   LYS A 541      -1.719 114.841  62.015  1.00 47.10           N  
ATOM   4108  CA  LYS A 541      -2.284 115.892  61.171  1.00 52.14           C  
ATOM   4109  C   LYS A 541      -3.766 116.123  61.455  1.00 51.90           C  
ATOM   4110  O   LYS A 541      -4.243 117.250  61.407  1.00 54.86           O  
ATOM   4111  CB  LYS A 541      -2.087 115.559  59.686  1.00 48.36           C  
ATOM   4112  N   ALA A 542      -4.485 115.051  61.765  1.00 59.18           N  
ATOM   4113  CA  ALA A 542      -5.914 115.139  62.044  1.00 62.50           C  
ATOM   4114  C   ALA A 542      -6.241 115.718  63.422  1.00 66.19           C  
ATOM   4115  O   ALA A 542      -7.194 116.489  63.570  1.00 67.76           O  
ATOM   4116  CB  ALA A 542      -6.556 113.767  61.887  1.00 60.67           C  
ATOM   4117  N   LYS A 543      -5.458 115.351  64.429  1.00 70.88           N  
ATOM   4118  CA  LYS A 543      -5.694 115.835  65.785  1.00 76.00           C  
ATOM   4119  C   LYS A 543      -5.111 117.233  66.016  1.00 78.83           C  
ATOM   4120  O   LYS A 543      -4.147 117.402  66.774  1.00 78.10           O  
ATOM   4121  CB  LYS A 543      -5.143 114.835  66.812  1.00 77.71           C  
ATOM   4122  CG  LYS A 543      -5.698 113.418  66.664  1.00 76.50           C  
ATOM   4123  CD  LYS A 543      -7.211 113.365  66.843  1.00 74.82           C  
ATOM   4124  CE  LYS A 543      -7.768 112.022  66.394  1.00 73.94           C  
ATOM   4125  NZ  LYS A 543      -9.240 111.916  66.598  1.00 71.05           N  
ATOM   4126  N   LYS A 544      -5.722 118.227  65.368  1.00 80.00           N  
ATOM   4127  CA  LYS A 544      -5.312 119.630  65.469  1.00 78.88           C  
ATOM   4128  C   LYS A 544      -3.796 119.810  65.387  1.00 78.53           C  
ATOM   4129  O   LYS A 544      -3.221 119.818  64.299  1.00 76.64           O  
ATOM   4130  CB  LYS A 544      -5.846 120.258  66.762  1.00 77.58           C  
TER    4131      LYS A 544                                                      
HETATM 4132  C1  MBR A 990      21.543  77.472  55.083  0.50 30.59           C  
HETATM 4133 BR2  MBR A 990      21.643  79.333  55.361  0.50 30.78          BR  
HETATM 4134 BR1  MBR A 990      21.429  77.130  53.246  0.50 32.68          BR  
HETATM 4135 BR3  MBR A 990      19.973  76.873  55.854  0.50 27.15          BR  
HETATM 4136  C1  MBR A 991      17.084  82.676  48.808  0.50 40.40           C  
HETATM 4137 BR2  MBR A 991      16.403  83.297  50.484  0.50 43.44          BR  
HETATM 4138 BR1  MBR A 991      16.324  83.730  47.435  0.50 34.88          BR  
HETATM 4139 BR3  MBR A 991      16.498  80.889  48.559  0.50 37.16          BR  
HETATM 4140  O   HOH A 601      30.329  92.121  44.858  1.00 31.36           O  
HETATM 4141  O   HOH A 602      26.496  81.765  30.305  1.00 40.64           O  
HETATM 4142  O   HOH A 603      18.381  85.459  24.690  1.00 17.66           O  
HETATM 4143  O   HOH A 604      31.001  84.951  30.539  1.00 57.75           O  
HETATM 4144  O   HOH A 605      25.628  85.635  35.224  1.00 28.57           O  
HETATM 4145  O   HOH A 606      22.982  84.123  20.860  1.00 24.12           O  
HETATM 4146  O   HOH A 607      20.048  75.189  20.526  1.00 17.82           O  
HETATM 4147  O   HOH A 608      17.728  65.425  29.835  1.00 17.44           O  
HETATM 4148  O   HOH A 609      16.160  63.065  29.015  1.00 18.31           O  
HETATM 4149  O   HOH A 610      16.936  62.375  26.521  1.00 21.18           O  
HETATM 4150  O   HOH A 611      17.686  60.728  36.659  1.00 18.35           O  
HETATM 4151  O   HOH A 612      20.509  62.967  37.465  1.00 29.65           O  
HETATM 4152  O   HOH A 613      18.189  64.444  37.551  1.00 18.39           O  
HETATM 4153  O   HOH A 614      18.231  67.367  38.017  1.00 16.97           O  
HETATM 4154  O   HOH A 615      21.928  68.301  40.599  1.00 32.89           O  
HETATM 4155  O   HOH A 616      23.182  71.877  47.041  1.00 40.86           O  
HETATM 4156  O   HOH A 617      20.337  61.903  46.597  1.00 43.66           O  
HETATM 4157  O   HOH A 618      18.668  64.381  46.461  1.00 36.95           O  
HETATM 4158  O   HOH A 619      15.688  63.410  43.972  1.00 16.60           O  
HETATM 4159  O   HOH A 620      17.258  63.760  40.514  1.00 27.32           O  
HETATM 4160  O   HOH A 621       0.108  75.040  33.021  1.00 15.80           O  
HETATM 4161  O   HOH A 622      -1.649  73.485  34.444  1.00 24.06           O  
HETATM 4162  O   HOH A 623      -0.658  71.767  37.197  1.00 43.83           O  
HETATM 4163  O   HOH A 624       2.102  69.914  35.887  1.00 18.82           O  
HETATM 4164  O   HOH A 625       0.774  69.048  33.724  1.00 45.03           O  
HETATM 4165  O   HOH A 626       0.600  72.742  25.294  1.00 24.50           O  
HETATM 4166  O   HOH A 627       1.784  66.662  31.964  1.00 33.87           O  
HETATM 4167  O   HOH A 628       3.976  68.988  28.562  1.00 25.45           O  
HETATM 4168  O   HOH A 629       7.328  67.659  25.689  1.00 27.35           O  
HETATM 4169  O   HOH A 630       7.259  66.052  27.796  1.00 21.65           O  
HETATM 4170  O   HOH A 631       3.370  66.259  29.096  1.00 34.60           O  
HETATM 4171  O   HOH A 632       7.614  63.828  30.784  1.00 19.61           O  
HETATM 4172  O   HOH A 633      10.324  62.194  31.226  1.00 19.61           O  
HETATM 4173  O   HOH A 634       7.622  59.087  38.260  1.00 13.69           O  
HETATM 4174  O   HOH A 635       9.878  60.326  40.405  1.00 14.52           O  
HETATM 4175  O   HOH A 636       7.274  60.892  41.263  1.00 29.39           O  
HETATM 4176  O   HOH A 637      12.212  60.253  42.638  1.00 28.94           O  
HETATM 4177  O   HOH A 638      13.626  59.535  44.591  1.00 29.93           O  
HETATM 4178  O   HOH A 639      21.266  62.549  34.560  1.00 33.15           O  
HETATM 4179  O   HOH A 640       0.351  90.658  33.546  1.00 28.92           O  
HETATM 4180  O   HOH A 641       2.853  90.962  35.093  1.00 21.78           O  
HETATM 4181  O   HOH A 642       3.607  88.792  38.557  1.00 25.65           O  
HETATM 4182  O   HOH A 643       2.396  87.514  41.030  1.00 24.87           O  
HETATM 4183  O   HOH A 644       5.336  89.403  41.696  1.00 32.45           O  
HETATM 4184  O   HOH A 645       7.672  89.288  42.975  1.00 45.27           O  
HETATM 4185  O   HOH A 646      10.537  90.065  41.683  1.00 24.01           O  
HETATM 4186  O   HOH A 647      -2.890  93.194  39.073  1.00 49.22           O  
HETATM 4187  O   HOH A 648      11.283  77.467  43.085  1.00 16.45           O  
HETATM 4188  O   HOH A 649       6.899  83.227  44.916  1.00 35.82           O  
HETATM 4189  O   HOH A 650       5.924  83.478  47.576  1.00 21.39           O  
HETATM 4190  O   HOH A 651       8.437  83.040  51.830  1.00 23.74           O  
HETATM 4191  O   HOH A 653      18.133  79.520  42.542  1.00 17.94           O  
HETATM 4192  O   HOH A 654       7.435  74.757  35.090  1.00 16.48           O  
HETATM 4193  O   HOH A 655       2.106  79.957  39.587  1.00 21.55           O  
HETATM 4194  O   HOH A 656      -2.078  65.595  54.277  1.00 16.28           O  
HETATM 4195  O   HOH A 657      -1.358  65.156  51.709  1.00 19.43           O  
HETATM 4196  O   HOH A 658      -2.705  64.399  47.783  1.00 29.30           O  
HETATM 4197  O   HOH A 659      -6.153  65.868  47.679  1.00 28.51           O  
HETATM 4198  O   HOH A 660      -2.256  65.758  45.199  1.00 31.58           O  
HETATM 4199  O   HOH A 661      -2.845  60.891  51.383  1.00 39.94           O  
HETATM 4200  O   HOH A 662      16.795  74.775  12.916  1.00 23.64           O  
HETATM 4201  O   HOH A 663      22.069  69.873  16.008  1.00 29.60           O  
HETATM 4202  O   HOH A 664      21.167  70.836  10.195  1.00 33.71           O  
HETATM 4203  O   HOH A 665      11.889  69.268  13.049  1.00 53.13           O  
HETATM 4204  O   HOH A 666      10.158  69.445   9.085  1.00 34.79           O  
HETATM 4205  O   HOH A 667      -6.565  80.425  37.072  1.00 19.89           O  
HETATM 4206  O   HOH A 668      -4.900  78.491  38.244  1.00 28.30           O  
HETATM 4207  O   HOH A 669      -4.524  79.916  35.162  1.00 34.20           O  
HETATM 4208  O   HOH A 670      -5.568  73.965  34.224  1.00 25.15           O  
HETATM 4209  O   HOH A 671      16.423  83.151  18.121  1.00 28.12           O  
HETATM 4210  O   HOH A 672      16.199  81.803  15.783  1.00 36.52           O  
HETATM 4211  O   HOH A 673      18.446  80.021  15.667  1.00 28.57           O  
HETATM 4212  O   HOH A 674       0.160  77.277  41.894  1.00 24.07           O  
HETATM 4213  O   HOH A 675       0.202  80.043  41.955  1.00 53.59           O  
HETATM 4214  O   HOH A 676       9.736  68.508  24.407  1.00 21.56           O  
HETATM 4215  O   HOH A 677       9.448  68.862  21.557  1.00 31.64           O  
HETATM 4216  O   HOH A 678       6.874  70.168  20.600  1.00 79.34           O  
HETATM 4217  O   HOH A 679      27.093  84.178  37.128  1.00 22.57           O  
HETATM 4218  O   HOH A 680      14.700  65.384  52.648  1.00 19.92           O  
HETATM 4219  O   HOH A 681      15.841  63.045  52.955  1.00 22.40           O  
HETATM 4220  O   HOH A 682      25.780  92.993  54.850  1.00 30.89           O  
HETATM 4221  O   HOH A 683      28.020  90.331  53.160  1.00 30.50           O  
HETATM 4222  O   HOH A 684      27.076  85.546  44.012  1.00 18.21           O  
HETATM 4223  O   HOH A 685      28.447  82.653  43.020  1.00 26.74           O  
HETATM 4224  O   HOH A 686      -4.834  79.445  19.845  1.00 26.82           O  
HETATM 4225  O   HOH A 687      -6.378  82.623  20.137  1.00 29.19           O  
HETATM 4226  O   HOH A 688      -7.754  85.179  20.443  1.00 33.41           O  
HETATM 4227  O   HOH A 689      -1.043  80.325  15.206  1.00 95.03           O  
HETATM 4228  O   HOH A 690      -3.936  73.520  15.632  1.00 21.25           O  
HETATM 4229  O   HOH A 691      -5.744  69.378  17.972  1.00 33.42           O  
HETATM 4230  O   HOH A 692     -10.690  72.481  20.001  1.00 29.86           O  
HETATM 4231  O   HOH A 693      12.854  89.037  27.442  1.00 17.21           O  
HETATM 4232  O   HOH A 694      12.346  95.050  26.595  1.00 29.39           O  
HETATM 4233  O   HOH A 695      -0.223  79.676  59.413  1.00 33.62           O  
HETATM 4234  O   HOH A 696       2.417  78.931  64.587  1.00 56.71           O  
HETATM 4235  O   HOH A 697     -11.198 102.403  73.991  1.00 36.09           O  
HETATM 4236  O   HOH A 698      19.419  87.075  44.705  1.00 23.25           O  
HETATM 4237  O   HOH A 700       9.568  86.695  48.691  1.00 25.85           O  
HETATM 4238  O   HOH A 701       7.755  88.898  55.853  1.00 46.20           O  
HETATM 4239  O   HOH A 702      14.476  67.298  58.973  1.00 36.27           O  
HETATM 4240  O   HOH A 703      17.312  66.894  58.068  1.00 26.13           O  
HETATM 4241  O   HOH A 704      12.133  63.669  60.547  1.00 21.22           O  
HETATM 4242  O   HOH A 705      14.848  62.527  59.388  1.00 29.76           O  
HETATM 4243  O   HOH A 706       2.937  92.685  23.579  1.00 31.52           O  
HETATM 4244  O   HOH A 707      -0.267  60.554  37.044  1.00 34.69           O  
HETATM 4245  O   HOH A 708      -4.083  66.897  24.800  1.00 48.60           O  
HETATM 4246  O   HOH A 709       0.664  82.720  37.001  1.00 34.69           O  
HETATM 4247  O   HOH A 710     -13.767 104.708  56.255  1.00 44.50           O  
HETATM 4248  O   HOH A 711      17.405  75.526  56.778  1.00 26.14           O  
HETATM 4249  O   HOH A 713      11.776  67.976  20.352  1.00 28.89           O  
HETATM 4250  O   HOH A 714       6.765  75.428  67.129  1.00 60.00           O  
HETATM 4251  O   HOH A 715       9.134  73.953  67.295  1.00 28.93           O  
HETATM 4252  O   HOH A 716      28.404  76.042  43.149  1.00 29.96           O  
HETATM 4253  O   HOH A 717       2.838  60.217  53.972  1.00 26.43           O  
HETATM 4254  O   HOH A 718     -11.725  75.893  30.545  1.00 31.97           O  
HETATM 4255  O   HOH A 719      -0.671  67.483  19.628  1.00 57.41           O  
HETATM 4256  O   HOH A 720       3.276  99.842  36.792  1.00 26.45           O  
HETATM 4257  O   HOH A 721       6.665  67.185  63.828  1.00 37.28           O  
HETATM 4258  O   HOH A 722      21.037 100.220  42.067  1.00 42.20           O  
HETATM 4259  O   HOH A 723      22.890  76.540  19.951  1.00 29.13           O  
HETATM 4260  O   HOH A 724      23.899  90.772  26.570  1.00 29.51           O  
HETATM 4261  O   HOH A 725      15.517  89.520  35.038  1.00 33.71           O  
HETATM 4262  O   HOH A 726      25.796  74.714  26.496  1.00 31.81           O  
HETATM 4263  O   HOH A 727      15.679 108.874  61.486  1.00 86.79           O  
HETATM 4264  O   HOH A 728      17.541  76.982  47.462  1.00 48.57           O  
HETATM 4265  O   HOH A 729       0.569  88.575  39.029  1.00 23.49           O  
HETATM 4266  O   HOH A 730       7.712  84.635  49.653  1.00 29.77           O  
HETATM 4267  O   HOH A 732      12.753  67.610  10.762  1.00 43.00           O  
HETATM 4268  O   HOH A 733       1.608  93.669  35.271  1.00 29.94           O  
HETATM 4269  O   HOH A 734       1.512  93.742  59.312  1.00 37.69           O  
HETATM 4270  O   HOH A 735       4.939  64.820  27.560  1.00 24.46           O  
HETATM 4271  O   HOH A 736      15.803  75.858  66.570  1.00 54.59           O  
HETATM 4272  O   HOH A 737       0.967  99.919  30.722  1.00 57.55           O  
HETATM 4273  O   HOH A 738      -0.463  67.856  29.198  1.00 41.07           O  
HETATM 4274  O   HOH A 739      19.608  74.007  11.723  1.00 46.11           O  
HETATM 4275  O   HOH A 740       9.406  67.419  64.720  1.00 26.50           O  
HETATM 4276  O   HOH A 741      14.041  65.473  60.849  1.00 32.69           O  
HETATM 4277  O   HOH A 742      -5.987  77.593  41.137  1.00 77.74           O  
HETATM 4278  O   HOH A 743       3.193  84.294  47.586  1.00 46.99           O  
HETATM 4279  O   HOH A 744      -2.409  78.306  42.326  1.00 35.54           O  
HETATM 4280  O   HOH A 745      -3.785  74.065  50.807  1.00 45.37           O  
HETATM 4281  O   HOH A 746      28.438  93.233  54.332  1.00 31.80           O  
HETATM 4282  O   HOH A 747      -6.902  68.558  25.928  1.00 35.97           O  
HETATM 4283  O   HOH A 748      19.075  63.636  25.639  1.00 27.63           O  
HETATM 4284  O   HOH A 749      31.441  89.472  38.125  1.00 41.56           O  
HETATM 4285  O   HOH A 750      19.696  82.652  46.923  1.00 40.73           O  
HETATM 4286  O   HOH A 751     -14.274  78.402  25.083  1.00 65.68           O  
HETATM 4287  O   HOH A 752       4.616  70.316  18.652  1.00 30.64           O  
HETATM 4288  O   HOH A 753      18.446 108.798  64.130  1.00 85.58           O  
HETATM 4289  O   HOH A 754      24.044  62.144  35.036  1.00 43.44           O  
HETATM 4290  O   HOH A 755      -1.149  82.591  43.387  1.00 37.97           O  
HETATM 4291  O   HOH A 756      17.245  72.916  66.040  1.00 39.92           O  
HETATM 4292  O   HOH A 757     -15.280  73.207  29.918  1.00 46.37           O  
HETATM 4293  O   HOH A 758      15.246  63.057  24.467  1.00 36.34           O  
HETATM 4294  O   HOH A 759       1.818  93.167  19.102  1.00 65.52           O  
HETATM 4295  O   HOH A 760       6.275  56.806  50.505  1.00 30.66           O  
HETATM 4296  O   HOH A 761       9.384  71.098  68.512  1.00 70.19           O  
HETATM 4297  O   HOH A 762      26.568  67.739  28.356  1.00 29.31           O  
HETATM 4298  O   HOH A 763     -11.458  78.517  31.975  1.00 28.64           O  
HETATM 4299  O   HOH A 764      -4.166  72.268  38.025  1.00 56.25           O  
HETATM 4300  O   HOH A 765      22.440  67.884  37.325  1.00 33.51           O  
HETATM 4301  O   HOH A 766      -4.991  96.875  24.296  1.00 35.86           O  
HETATM 4302  O   HOH A 767      21.687  77.039  59.176  1.00 45.68           O  
HETATM 4303  O   HOH A 768     -11.617  70.924  23.628  1.00 35.77           O  
HETATM 4304  O   HOH A 769      16.125  63.784  21.824  1.00 44.70           O  
HETATM 4305  O   HOH A 770      25.256 106.901  49.694  1.00 57.94           O  
HETATM 4306  O   HOH A 771      14.998  60.203  52.118  1.00 42.68           O  
HETATM 4307  O   HOH A 773      19.088  66.779  40.582  1.00 32.78           O  
HETATM 4308  O   HOH A 774      12.254  87.592  17.559  1.00 35.90           O  
HETATM 4309  O   HOH A 775      26.698  83.326  27.796  1.00 42.95           O  
HETATM 4310  O   HOH A 776      22.068  65.582  38.946  1.00 49.85           O  
HETATM 4311  O   HOH A 777      24.622  74.075  48.942  1.00 50.11           O  
HETATM 4312  O   HOH A 778      13.837  89.214  18.967  1.00 38.12           O  
HETATM 4313  O   HOH A 779      -6.429  84.806  37.800  1.00 47.72           O  
HETATM 4314  O   HOH A 781      24.843  79.459  31.526  1.00 33.49           O  
HETATM 4315  O   HOH A 782      27.433  64.951  28.624  1.00 45.64           O  
HETATM 4316  O   HOH A 783       0.401  88.436  42.628  1.00 57.87           O  
HETATM 4317  O   HOH A 784       2.523  86.073  45.118  1.00 41.44           O  
HETATM 4318  O   HOH A 785      15.484  78.550  11.462  1.00 50.37           O  
HETATM 4319  O   HOH A 787      25.200  81.275  33.646  1.00 54.03           O  
HETATM 4320  O   HOH A 788      -1.042  62.178  48.118  1.00 31.15           O  
HETATM 4321  O   HOH A 789       2.519  78.200  49.041  1.00 67.96           O  
HETATM 4322  O   HOH A 790      20.049  67.720  16.906  1.00 48.00           O  
HETATM 4323  O   HOH A 791      24.458  70.298  17.495  1.00 43.10           O  
HETATM 4324  O   HOH A 792      17.889  80.560  61.378  1.00 43.02           O  
HETATM 4325  O   HOH A 793      25.785  71.766  25.208  1.00 27.07           O  
HETATM 4326  O   HOH A 795      15.964  60.633  43.987  1.00 32.49           O  
HETATM 4327  O   HOH A 796      23.661  78.805  23.974  1.00 43.73           O  
HETATM 4328  O   HOH A 797      -8.315  96.899  36.946  1.00 47.04           O  
HETATM 4329  O   HOH A 798     -12.957  71.013  26.596  1.00 45.87           O  
HETATM 4330  O   HOH A 799       9.376  67.984  67.619  1.00 66.73           O  
HETATM 4331  O   HOH A 800      31.782  92.048  52.210  1.00 39.33           O  
HETATM 4332  O   HOH A 801      25.225  88.751  24.574  1.00 60.28           O  
HETATM 4333  O   HOH A 802      18.224  62.892  43.027  1.00 68.74           O  
HETATM 4334  O   HOH A 804      13.849  88.161  15.266  1.00 40.08           O  
HETATM 4335  O   HOH A 805      -7.000  80.464  18.510  1.00 37.56           O  
HETATM 4336  O   HOH A 806      -6.841  76.528  17.353  1.00 47.78           O  
HETATM 4337  O   HOH A 807       1.900  59.864  58.201  1.00 53.28           O  
HETATM 4338  O   HOH A 808      25.311  76.527  24.155  1.00 29.70           O  
HETATM 4339  O   HOH A 809      20.906  72.894  50.939  1.00 51.08           O  
HETATM 4340  O   HOH A 810       1.802  77.298  45.182  1.00 24.57           O  
HETATM 4341  O   HOH A 811       6.121 102.368  44.881  1.00 83.38           O  
HETATM 4342  O   HOH A 812       3.505  95.324  21.637  1.00 40.63           O  
HETATM 4343  O   HOH A 813      -4.721 103.285  76.782  1.00 47.43           O  
HETATM 4344  O   HOH A 814      32.507  86.097  33.068  1.00 77.37           O  
HETATM 4345  O   HOH A 815      22.719 100.178  62.183  1.00 45.17           O  
HETATM 4346  O   HOH A 816     -12.578  87.401  24.313  1.00 41.55           O  
HETATM 4347  O   HOH A 817      10.682  90.858  14.692  1.00 54.42           O  
HETATM 4348  O   HOH A 818      26.915 107.235  52.034  1.00 45.01           O  
HETATM 4349  O   HOH A 819       1.068  69.793  27.775  1.00 21.38           O  
HETATM 4350  O   HOH A 820     -21.477 107.462  69.391  1.00 72.86           O  
HETATM 4351  O   HOH A 821      24.400  78.454  58.311  1.00 57.13           O  
HETATM 4352  O   HOH A 822      14.166  65.520  18.574  1.00 63.11           O  
HETATM 4353  O   HOH A 823      22.701  85.953  58.653  1.00 38.21           O  
HETATM 4354  O   HOH A 824       7.927  94.226  46.566  1.00 39.41           O  
HETATM 4355  O   HOH A 825      -8.048 107.808  52.910  1.00 44.51           O  
HETATM 4356  O   HOH A 826      -6.373 112.175  73.528  1.00 91.04           O  
HETATM 4357  O   HOH A 827     -17.556  99.975  76.686  1.00 51.88           O  
HETATM 4358  O   HOH A 828       5.600  97.685  28.438  1.00 39.03           O  
HETATM 4359  O   HOH A 829       0.361  76.563  48.178  1.00 21.55           O  
HETATM 4360  O   HOH A 830      29.467  71.757  38.553  1.00 78.50           O  
HETATM 4361  O   HOH A 831      17.093  78.451  64.779  1.00 47.21           O  
HETATM 4362  O   HOH A 833     -21.231 103.811  72.071  1.00 47.31           O  
HETATM 4363  O   HOH A 835      24.374  81.527  22.620  1.00 36.85           O  
HETATM 4364  O   HOH A 837     -11.352  68.883  27.348  1.00 52.57           O  
HETATM 4365  O   HOH A 838       3.279  65.263  23.588  1.00 32.58           O  
HETATM 4366  O   HOH A 839      20.880  97.202  68.626  1.00 44.82           O  
HETATM 4367  O   HOH A 840      -0.201  84.366  45.978  1.00 41.43           O  
HETATM 4368  O   HOH A 842      -0.257  72.487  14.168  1.00 37.09           O  
HETATM 4369  O   HOH A 843       1.179  82.227  48.341  1.00 44.28           O  
HETATM 4370  O   HOH A 844       7.036  67.054  21.051  1.00 45.73           O  
HETATM 4371  O   HOH A 845      26.077  74.854  21.579  1.00 36.31           O  
HETATM 4372  O   HOH A 846      22.565 108.745  53.144  1.00 42.97           O  
HETATM 4373  O   HOH A 847      16.809  90.206  18.541  1.00 33.96           O  
HETATM 4374  O   HOH A 848       3.161  73.991  68.220  1.00 49.42           O  
HETATM 4375  O   HOH A 849       3.183  70.425  69.742  1.00 25.13           O  
HETATM 4376  O   HOH A 850     -11.218 104.555  76.081  1.00 51.56           O  
HETATM 4377  O   HOH A 851      24.999 111.127  54.405  1.00 46.74           O  
HETATM 4378  O   HOH A 852     -21.404 110.366  76.746  1.00 67.44           O  
HETATM 4379  O   HOH A 853      -4.526  61.206  54.812  1.00 35.05           O  
HETATM 4380  O   HOH A 854      30.817  83.341  47.895  1.00 35.96           O  
HETATM 4381  O   HOH A 855      17.401 101.565  38.171  1.00 50.03           O  
HETATM 4382  O   HOH A 856      27.039  71.907  21.942  1.00 86.18           O  
HETATM 4383  O   HOH A 857      13.058  92.831  18.362  1.00 35.71           O  
HETATM 4384  O   HOH A 858       8.930 104.334  35.049  1.00 39.19           O  
HETATM 4385  O   HOH A 859      30.430  88.859  53.762  1.00 57.33           O  
HETATM 4386  O   HOH A 860       8.515  69.205   6.514  1.00 73.79           O  
HETATM 4387  O   HOH A 861      24.965  94.790  30.520  1.00 74.04           O  
HETATM 4388  O   HOH A 862      25.589  94.358  33.613  1.00 45.07           O  
HETATM 4389  O   HOH A 863       0.553 115.485  68.960  1.00 99.00           O  
HETATM 4390  O   HOH A 864       1.950  61.757  44.944  1.00 31.64           O  
HETATM 4391  O   HOH A 865      -3.639  93.762  61.006  1.00 64.35           O  
HETATM 4392  O   HOH A 866       5.501  65.299  30.255  1.00 73.90           O  
HETATM 4393  O   HOH A 867      -0.103  59.748  54.155  1.00 34.14           O  
HETATM 4394  O   HOH A 869      26.628  94.733  36.316  1.00 48.47           O  
HETATM 4395  O   HOH A 870      30.821  96.468  53.732  1.00 39.54           O  
HETATM 4396  O   HOH A 871      16.636  78.414  14.093  1.00 42.99           O  
HETATM 4397  O   HOH A 873     -11.050  84.743  21.346  1.00 49.81           O  
HETATM 4398  O   HOH A 874      10.429  80.053  69.208  1.00 49.04           O  
HETATM 4399  O   HOH A 875      -6.842  99.714  53.739  1.00 61.70           O  
HETATM 4400  O   HOH A 876      30.199  86.107  53.150  1.00 56.64           O  
HETATM 4401  O   HOH A 877       9.236  88.255  15.149  1.00 46.75           O  
HETATM 4402  O   HOH A 878       4.129  91.016  45.359  1.00 77.94           O  
HETATM 4403  O   HOH A 879      10.888  97.734  59.477  1.00 42.09           O  
HETATM 4404  O   HOH A 880     -22.665  93.088  59.437  1.00 99.00           O  
HETATM 4405  O   HOH A 881      24.350  78.929  20.621  1.00 43.70           O  
HETATM 4406  O   HOH A 882      -9.868  68.876  23.949  1.00 42.61           O  
HETATM 4407  O   HOH A 883      12.089  86.203  12.304  1.00 63.55           O  
HETATM 4408  O   HOH A 884      15.800  93.410  65.980  1.00 84.30           O  
HETATM 4409  O   HOH A 885       7.319  85.141  60.689  1.00 60.21           O  
HETATM 4410  O   HOH A 886     -16.464  97.019  52.517  1.00 42.52           O  
HETATM 4411  O   HOH A 887       8.221  99.006  30.463  1.00 72.37           O  
HETATM 4412  O   HOH A 888      10.262  75.698  69.491  1.00 39.08           O  
HETATM 4413  O   HOH A 889       2.371  83.404  53.371  1.00 41.34           O  
HETATM 4414  O   HOH A 890       1.757 101.759  37.962  1.00 62.59           O  
HETATM 4415  O   HOH A 891      11.107  92.602  25.851  1.00 34.73           O  
HETATM 4416  O   HOH A 892      19.701  95.043  21.943  1.00 59.48           O  
HETATM 4417  O   HOH A 893     -24.493 104.367  69.808  1.00 48.34           O  
HETATM 4418  O   HOH A 894      14.349  82.398  12.209  1.00 39.68           O  
HETATM 4419  O   HOH A 895       1.061  69.512  16.446  1.00 33.35           O  
HETATM 4420  O   HOH A 896       6.564  59.719  45.864  1.00 33.27           O  
HETATM 4421  O   HOH A 897       1.726  83.944  50.665  1.00 80.09           O  
HETATM 4422  O   HOH A 898      14.963  89.939  65.041  1.00 60.44           O  
HETATM 4423  O   HOH A 899      23.927  74.810  11.309  1.00 43.38           O  
HETATM 4424  O   HOH A 900       4.429  61.368  46.974  1.00 37.84           O  
HETATM 4425  O   HOH A 901      18.973  79.886  46.345  1.00 29.85           O  
HETATM 4426  O   HOH A 903      29.674  94.405  37.510  1.00 51.48           O  
HETATM 4427  O   HOH A 904       7.179  98.942  25.575  1.00 98.99           O  
HETATM 4428  O   HOH A 905       9.611 100.679  32.578  1.00 40.17           O  
HETATM 4429  O   HOH A 906      15.693  80.612  62.753  1.00 71.13           O  
HETATM 4430  O   HOH A 907      29.520  89.833  32.669  1.00 49.67           O  
HETATM 4431  O   HOH A 909       7.238  64.404  64.775  1.00 26.12           O  
HETATM 4432  O   HOH A 910      -4.149  93.116  44.529  1.00 77.31           O  
HETATM 4433  O   HOH A 911       9.647  71.695  11.937  1.00 41.72           O  
HETATM 4434  O   HOH A 912      20.317  87.907  17.715  1.00 42.06           O  
HETATM 4435  O   HOH A 913       0.857  79.598  47.321  1.00 38.72           O  
HETATM 4436  O   HOH A 914      14.353  98.172  67.368  1.00 68.30           O  
HETATM 4437  O   HOH A 915       3.982  81.980  11.080  1.00 62.61           O  
HETATM 4438  O   HOH A 917      15.245  75.696  10.554  1.00 38.96           O  
HETATM 4439  O   HOH A 918      26.567  77.537  31.216  1.00 63.91           O  
HETATM 4440  O   HOH A 919       5.360  92.519  15.243  1.00 82.37           O  
HETATM 4441  O   HOH A 920     -15.387  81.891  29.706  1.00 36.94           O  
HETATM 4442  O   HOH A 921     -14.320  84.930  23.395  1.00 99.00           O  
HETATM 4443  O   HOH A 922      21.652  71.692  64.244  1.00 73.40           O  
HETATM 4444  O   HOH A 924      -1.250  93.193  19.233  1.00 61.15           O  
HETATM 4445  O   HOH A 925      27.276  69.923  26.778  1.00 57.19           O  
HETATM 4446  O   HOH A 926      28.830 103.459  48.042  1.00 56.42           O  
HETATM 4447  O   HOH A 927     -13.229 110.846  64.451  1.00 64.85           O  
HETATM 4448  O   HOH A 928      22.163  75.143  50.189  1.00 34.99           O  
HETATM 4449  O   HOH A 929       6.526  72.557  12.133  1.00 41.48           O  
HETATM 4450  O   HOH A 930      22.336  86.224  17.484  1.00 62.94           O  
HETATM 4451  O   HOH A 935     -10.786  90.706  72.859  1.00 60.43           O  
HETATM 4452  O   HOH A 936     -11.700  95.133  41.633  1.00 99.00           O  
HETATM 4453  O   HOH A 937      24.420  77.926  50.810  1.00 49.61           O  
HETATM 4454  O   HOH A 938     -14.715  88.857  63.936  1.00 99.00           O  
HETATM 4455  O   HOH A 939      28.966  68.634  24.297  1.00 56.93           O  
HETATM 4456  O   HOH A 940      23.859  93.799  26.847  1.00 58.01           O  
HETATM 4457  O   HOH A 941      -5.274  83.977  17.346  1.00 51.59           O  
HETATM 4458  O   HOH A 942      24.042 102.692  56.977  1.00 40.90           O  
HETATM 4459  O   HOH A 944     -13.743  89.415  22.516  1.00 89.92           O  
HETATM 4460  O   HOH A 945     -14.685  99.361  51.461  1.00 66.31           O  
HETATM 4461  O   HOH A 946      -2.223  80.479  45.241  1.00 45.58           O  
HETATM 4462  O   HOH A 947      -1.687  56.933  54.170  1.00 92.90           O  
HETATM 4463  O   HOH A 948       7.575 100.021  52.378  1.00 62.60           O  
HETATM 4464  O   HOH A 949      -0.525  67.792  38.455  1.00 55.15           O  
HETATM 4465  O   HOH A 950      -8.879 112.061  57.186  1.00 59.45           O  
HETATM 4466  O   HOH A 951      -8.602  91.513  21.767  1.00 67.41           O  
HETATM 4467  O   HOH A 952      29.818  96.113  60.410  1.00 42.40           O  
HETATM 4468  O   HOH A 953      18.063  72.315  10.341  1.00 34.67           O  
HETATM 4469  O   HOH A 954     -12.022 110.749  60.820  1.00 41.73           O  
HETATM 4470  O   HOH A 955      -5.421 107.269  53.480  1.00 65.01           O  
HETATM 4471  O   HOH A 956      -2.873  92.956  63.626  1.00 75.36           O  
HETATM 4472  O   HOH A 957      -3.727  81.884  15.242  1.00 72.74           O  
HETATM 4473  O   HOH A 958      18.592  99.575  33.557  1.00 49.36           O  
HETATM 4474  O   HOH A 959       7.438  99.660  62.597  1.00 47.22           O  
HETATM 4475  O   HOH A 960      10.735 100.901  64.319  1.00 75.92           O  
HETATM 4476  O   HOH A 961       6.422 101.261  64.759  1.00 43.53           O  
HETATM 4477  O   HOH A 962      22.003  67.444  52.457  1.00 38.78           O  
HETATM 4478  O   HOH A 963      22.057  68.817  56.456  1.00 48.57           O  
HETATM 4479  O   HOH A 964      20.070  78.252  44.064  1.00 27.49           O  
HETATM 4480  O   HOH A 965      29.597  76.965  40.428  1.00 40.98           O  
HETATM 4481  O   HOH A 966      30.467  75.372  46.759  1.00 83.51           O  
HETATM 4482  O   HOH A 967     -14.770  92.580  59.689  1.00 49.58           O  
HETATM 4483  O   HOH A 968      -0.538  60.033  41.154  1.00 40.92           O  
HETATM 4484  O   HOH A 969      26.370  81.084  36.454  1.00 33.64           O  
HETATM 4485  O   HOH A 970      24.020  69.949  38.608  1.00 40.92           O  
HETATM 4486  O   HOH A 971      19.846  97.571  38.829  1.00 42.22           O  
HETATM 4487  O   HOH A 972      12.124  77.561  69.234  1.00 35.36           O  
HETATM 4488  O   HOH A 973      35.749  82.266  43.466  1.00 41.68           O  
HETATM 4489  O   HOH A 974      -0.825  62.490  51.169  1.00 26.74           O  
HETATM 4490  O   HOH A 975      19.430  64.952  23.418  1.00 39.37           O  
HETATM 4491  O   HOH A 976      11.188  88.981  45.291  1.00 26.42           O  
HETATM 4492  O   HOH A 977      12.586  87.955  47.177  1.00 39.17           O  
CONECT 4132 4133 4134 4135                                                      
CONECT 4133 4132                                                                
CONECT 4134 4132                                                                
CONECT 4135 4132                                                                
CONECT 4136 4137 4138 4139                                                      
CONECT 4137 4136                                                                
CONECT 4138 4136                                                                
CONECT 4139 4136                                                                
MASTER      334    0    2   18   23    0    2    6 4491    1    8   43          
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: October 18th, 2018.