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***  HYDROLASE 15-AUG-07 2QYM  ***

elNémo ID: 21062419021759262

Job options:

ID        	=	 21062419021759262
JOBID     	=	 HYDROLASE 15-AUG-07 2QYM
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    HYDROLASE                               15-AUG-07   2QYM              
TITLE     CRYSTAL STRUCTURE OF UNLIGANDED PDE4C2                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHODIESTERASE 4C;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: THE CATALYTIC DOMAIN OF PDE4C2 WITH RESIDUES 200-          
COMPND   5 558;                                                                 
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PDE4C2;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    PDE4C STRUCTURE, HYDROLASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.KE                                                                  
REVDAT   2   24-FEB-09 2QYM    1       VERSN                                    
REVDAT   1   08-APR-08 2QYM    0                                                
JRNL        AUTH   H.WANG,M.S.PENG,Y.CHEN,J.GENG,H.ROBINSON,                    
JRNL        AUTH 2 M.D.HOUSLAY,J.CAI,H.KE                                       
JRNL        TITL   STRUCTURES OF THE FOUR SUBFAMILIES OF                        
JRNL        TITL 2 PHOSPHODIESTERASE-4 PROVIDE INSIGHT INTO THE                 
JRNL        TITL 3 SELECTIVITY OF THEIR INHIBITORS.                             
JRNL        REF    BIOCHEM.J.                    V. 408   193 2007              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   17727341                                                     
JRNL        DOI    10.1042/BJ20070970                                           
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
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)   (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 36109                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3625                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2329                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 127                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.06                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2QYM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044208.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : 2006-04-30                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36952                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 36.200                             
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDE4D                                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG3350, 100 MM MGCL2, 0.1M          
REMARK 280  HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       91.97000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      183.94000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      137.95500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      229.92500            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       45.98500            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       91.97000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      183.94000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      229.92500            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      137.95500            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       45.98500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4240 ANGSTROM**2                          
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 350   BIOMT1   2  0.500000 -0.866025  0.000000       37.36900            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000       64.72501            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      229.92500            
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     THR A   200                                                      
REMARK 465     PHE A   333                                                      
REMARK 465     LEU A   334                                                      
REMARK 465     ILE A   335                                                      
REMARK 465     ASN A   336                                                      
REMARK 465     THR A   337                                                      
REMARK 465     ASN A   338                                                      
REMARK 465     SER A   339                                                      
REMARK 465     GLU A   340                                                      
REMARK 465     LEU A   341                                                      
REMARK 465     ALA A   342                                                      
REMARK 465     LEU A   343                                                      
REMARK 465     MET A   344                                                      
REMARK 465     TYR A   345                                                      
REMARK 465     GLY A   466                                                      
REMARK 465     ASP A   467                                                      
REMARK 465     ARG A   468                                                      
REMARK 465     GLU A   469                                                      
REMARK 465     ARG A   470                                                      
REMARK 465     GLU A   471                                                      
REMARK 465     SER A   472                                                      
REMARK 465     GLY A   473                                                      
REMARK 465     LEU A   474                                                      
REMARK 465     ASP A   475                                                      
REMARK 465     ILE A   476                                                      
REMARK 465     SER A   477                                                      
REMARK 465     PRO A   478                                                      
REMARK 465     MET A   479                                                      
REMARK 465     CYS A   480                                                      
REMARK 465     ASP A   481                                                      
REMARK 465     LYS A   482                                                      
REMARK 465     HIS A   483                                                      
REMARK 465     THR A   484                                                      
REMARK 465     ALA A   485                                                      
REMARK 465     SER A   486                                                      
REMARK 465     VAL A   487                                                      
REMARK 465     GLU A   488                                                      
REMARK 465     LYS A   489                                                      
REMARK 465     SER A   490                                                      
REMARK 465     SER A   530                                                      
REMARK 465     LYS A   531                                                      
REMARK 465     ILE A   532                                                      
REMARK 465     PRO A   533                                                      
REMARK 465     ARG A   534                                                      
REMARK 465     SER A   535                                                      
REMARK 465     PRO A   536                                                      
REMARK 465     SER A   537                                                      
REMARK 465     ASP A   538                                                      
REMARK 465     LEU A   539                                                      
REMARK 465     THR A   540                                                      
REMARK 465     ASN A   541                                                      
REMARK 465     PRO A   542                                                      
REMARK 465     GLU A   543                                                      
REMARK 465     ARG A   544                                                      
REMARK 465     ASP A   545                                                      
REMARK 465     GLY A   546                                                      
REMARK 465     PRO A   547                                                      
REMARK 465     ASP A   548                                                      
REMARK 465     ARG A   549                                                      
REMARK 465     PHE A   550                                                      
REMARK 465     GLN A   551                                                      
REMARK 465     PHE A   552                                                      
REMARK 465     GLU A   553                                                      
REMARK 465     LEU A   554                                                      
REMARK 465     THR A   555                                                      
REMARK 465     LEU A   556                                                      
REMARK 465     GLU A   557                                                      
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    GLN A 210       43.42    -97.04                                   
REMARK 500    LEU A 218        1.01    -69.26                                   
REMARK 500    ALA A 305       15.30     59.71                                   
REMARK 500    ALA A 348       78.18   -107.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   1  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 286   NE2                                                    
REMARK 620 2 HIS A 322   NE2  94.7                                              
REMARK 620 3 ASP A 323   OD2  86.1  81.6                                        
REMARK 620 4 ASP A 440   OD1  88.6  90.9 170.4                                  
REMARK 620 5 HOH A 559   O    85.7 175.5 102.9  84.6                            
REMARK 620 6 HOH A 558   O   170.0  94.9  98.2  88.4  84.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A   2  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 323   OD1                                                    
REMARK 620 2 HOH A 561   O   168.2                                              
REMARK 620 3 HOH A 560   O   101.2  87.3                                        
REMARK 620 4 HOH A 558   O    97.2  90.6  92.6                                  
REMARK 620 5 HOH A 562   O    88.7  83.4  87.1 174.0                            
REMARK 620 6 HOH A 563   O    81.8  89.1 174.0  92.2  87.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1                    
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2QYK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2QYL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2QYN   RELATED DB: PDB                                   
DBREF  2QYM A  200   557  UNP    Q7KYS4   Q7KYS4_HUMAN   200    557             
SEQADV 2QYM ARG A  238  UNP  Q7KYS4    GLN   238 CONFLICT                       
SEQRES   1 A  358  THR VAL PRO ARG PHE GLY VAL GLN THR ASP GLN GLU GLU          
SEQRES   2 A  358  GLN LEU ALA LYS GLU LEU GLU ASP THR ASN LYS TRP GLY          
SEQRES   3 A  358  LEU ASP VAL PHE LYS VAL ALA GLU LEU SER GLY ASN ARG          
SEQRES   4 A  358  PRO LEU THR ALA ILE ILE PHE SER ILE PHE GLN GLU ARG          
SEQRES   5 A  358  ASP LEU LEU LYS THR PHE GLN ILE PRO ALA ASP THR LEU          
SEQRES   6 A  358  ALA THR TYR LEU LEU MET LEU GLU GLY HIS TYR HIS ALA          
SEQRES   7 A  358  ASN VAL ALA TYR HIS ASN SER LEU HIS ALA ALA ASP VAL          
SEQRES   8 A  358  ALA GLN SER THR HIS VAL LEU LEU ALA THR PRO ALA LEU          
SEQRES   9 A  358  GLU ALA VAL PHE THR ASP LEU GLU ILE LEU ALA ALA LEU          
SEQRES  10 A  358  PHE ALA SER ALA ILE HIS ASP VAL ASP HIS PRO GLY VAL          
SEQRES  11 A  358  SER ASN GLN PHE LEU ILE ASN THR ASN SER GLU LEU ALA          
SEQRES  12 A  358  LEU MET TYR ASN ASP ALA SER VAL LEU GLU ASN HIS HIS          
SEQRES  13 A  358  LEU ALA VAL GLY PHE LYS LEU LEU GLN ALA GLU ASN CYS          
SEQRES  14 A  358  ASP ILE PHE GLN ASN LEU SER ALA LYS GLN ARG LEU SER          
SEQRES  15 A  358  LEU ARG ARG MET VAL ILE ASP MET VAL LEU ALA THR ASP          
SEQRES  16 A  358  MET SER LYS HIS MET ASN LEU LEU ALA ASP LEU LYS THR          
SEQRES  17 A  358  MET VAL GLU THR LYS LYS VAL THR SER LEU GLY VAL LEU          
SEQRES  18 A  358  LEU LEU ASP ASN TYR SER ASP ARG ILE GLN VAL LEU GLN          
SEQRES  19 A  358  ASN LEU VAL HIS CYS ALA ASP LEU SER ASN PRO THR LYS          
SEQRES  20 A  358  PRO LEU PRO LEU TYR ARG GLN TRP THR ASP ARG ILE MET          
SEQRES  21 A  358  ALA GLU PHE PHE GLN GLN GLY ASP ARG GLU ARG GLU SER          
SEQRES  22 A  358  GLY LEU ASP ILE SER PRO MET CYS ASP LYS HIS THR ALA          
SEQRES  23 A  358  SER VAL GLU LYS SER GLN VAL GLY PHE ILE ASP TYR ILE          
SEQRES  24 A  358  ALA HIS PRO LEU TRP GLU THR TRP ALA ASP LEU VAL HIS          
SEQRES  25 A  358  PRO ASP ALA GLN ASP LEU LEU ASP THR LEU GLU ASP ASN          
SEQRES  26 A  358  ARG GLU TRP TYR GLN SER LYS ILE PRO ARG SER PRO SER          
SEQRES  27 A  358  ASP LEU THR ASN PRO GLU ARG ASP GLY PRO ASP ARG PHE          
SEQRES  28 A  358  GLN PHE GLU LEU THR LEU GLU                                  
HET     ZN  A   1       1                                                       
HET     MG  A   2       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  HOH   *127(H2 O)                                                    
HELIX    1   1 GLN A  210  LEU A  218  1                                   9    
HELIX    2   2 GLU A  219  THR A  221  5                                   3    
HELIX    3   3 ASP A  227  SER A  235  1                                   9    
HELIX    4   4 ARG A  238  ARG A  251  1                                  14    
HELIX    5   5 ASP A  252  PHE A  257  1                                   6    
HELIX    6   6 PRO A  260  HIS A  274  1                                  15    
HELIX    7   7 ASN A  283  ALA A  299  1                                  17    
HELIX    8   8 THR A  300  GLU A  304  5                                   5    
HELIX    9   9 THR A  308  HIS A  322  1                                  15    
HELIX   10  10 GLY A  328  GLN A  332  5                                   5    
HELIX   11  11 SER A  349  LEU A  362  1                                  14    
HELIX   12  12 LEU A  363  ALA A  365  5                                   3    
HELIX   13  13 SER A  375  ALA A  392  1                                  18    
HELIX   14  14 THR A  393  SER A  396  5                                   4    
HELIX   15  15 LYS A  397  THR A  411  1                                  15    
HELIX   16  16 ASN A  424  LEU A  441  1                                  18    
HELIX   17  17 SER A  442  LYS A  446  5                                   5    
HELIX   18  18 PRO A  447  GLN A  464  1                                  18    
HELIX   19  19 GLY A  493  ILE A  498  1                                   6    
HELIX   20  20 ILE A  498  HIS A  511  1                                  14    
HELIX   21  21 ALA A  514  ARG A  525  1                                  12    
LINK         NE2 HIS A 286                ZN    ZN A   1     1555   1555  2.12  
LINK         NE2 HIS A 322                ZN    ZN A   1     1555   1555  2.10  
LINK         OD1 ASP A 323                MG    MG A   2     1555   1555  2.09  
LINK         OD2 ASP A 323                ZN    ZN A   1     1555   1555  2.06  
LINK         OD1 ASP A 440                ZN    ZN A   1     1555   1555  2.07  
LINK        ZN    ZN A   1                 O   HOH A 559     1555   1555  2.32  
LINK        ZN    ZN A   1                 O   HOH A 558     1555   1555  2.08  
LINK        MG    MG A   2                 O   HOH A 561     1555   1555  2.29  
LINK        MG    MG A   2                 O   HOH A 560     1555   1555  2.25  
LINK        MG    MG A   2                 O   HOH A 558     1555   1555  2.24  
LINK        MG    MG A   2                 O   HOH A 562     1555   1555  2.37  
LINK        MG    MG A   2                 O   HOH A 563     1555   1555  2.31  
CISPEP   1 HIS A  511    PRO A  512          0         0.59                     
SITE     1 AC1  6 HIS A 286  HIS A 322  ASP A 323  ASP A 440                    
SITE     2 AC1  6 HOH A 558  HOH A 559                                          
SITE     1 AC2  6 ASP A 323  HOH A 558  HOH A 560  HOH A 561                    
SITE     2 AC2  6 HOH A 562  HOH A 563                                          
CRYST1   74.738   74.738  275.910  90.00  90.00 120.00 P 61 2 2     12          
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      0.013380  0.007725  0.000000        0.00000                         
SCALE2      0.000000  0.015450  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003624        0.00000                         
ATOM      1  N   VAL A 201      36.940  61.059  95.473  1.00 55.70           N  
ATOM      2  CA  VAL A 201      36.320  59.767  95.892  1.00 55.30           C  
ATOM      3  C   VAL A 201      37.392  58.711  96.152  1.00 55.26           C  
ATOM      4  O   VAL A 201      38.180  58.382  95.265  1.00 54.81           O  
ATOM      5  CB  VAL A 201      35.360  59.228  94.805  1.00 55.39           C  
ATOM      6  CG1 VAL A 201      34.695  57.941  95.285  1.00 55.11           C  
ATOM      7  CG2 VAL A 201      34.314  60.278  94.470  1.00 55.17           C  
ATOM      8  N   PRO A 202      37.436  58.170  97.381  1.00 55.34           N  
ATOM      9  CA  PRO A 202      38.427  57.146  97.730  1.00 55.38           C  
ATOM     10  C   PRO A 202      38.352  55.900  96.843  1.00 55.26           C  
ATOM     11  O   PRO A 202      37.319  55.618  96.232  1.00 54.66           O  
ATOM     12  CB  PRO A 202      38.127  56.857  99.206  1.00 55.47           C  
ATOM     13  CG  PRO A 202      36.684  57.250  99.362  1.00 55.84           C  
ATOM     14  CD  PRO A 202      36.592  58.504  98.541  1.00 55.46           C  
ATOM     15  N   ARG A 203      39.460  55.167  96.779  1.00 55.21           N  
ATOM     16  CA  ARG A 203      39.567  53.963  95.959  1.00 55.39           C  
ATOM     17  C   ARG A 203      38.349  53.040  96.021  1.00 55.18           C  
ATOM     18  O   ARG A 203      37.930  52.492  94.999  1.00 54.99           O  
ATOM     19  CB  ARG A 203      40.828  53.184  96.347  1.00 55.88           C  
ATOM     20  CG  ARG A 203      41.108  51.981  95.461  1.00 56.57           C  
ATOM     21  CD  ARG A 203      42.443  51.345  95.800  1.00 56.99           C  
ATOM     22  NE  ARG A 203      42.709  50.173  94.971  1.00 57.81           N  
ATOM     23  CZ  ARG A 203      43.834  49.465  95.017  1.00 57.87           C  
ATOM     24  NH1 ARG A 203      44.805  49.811  95.852  1.00 57.75           N  
ATOM     25  NH2 ARG A 203      43.986  48.410  94.228  1.00 57.99           N  
ATOM     26  N   PHE A 204      37.787  52.863  97.212  1.00 54.87           N  
ATOM     27  CA  PHE A 204      36.618  52.005  97.374  1.00 54.76           C  
ATOM     28  C   PHE A 204      35.429  52.762  97.962  1.00 54.67           C  
ATOM     29  O   PHE A 204      34.598  52.185  98.664  1.00 54.16           O  
ATOM     30  CB  PHE A 204      36.963  50.795  98.251  1.00 54.52           C  
ATOM     31  CG  PHE A 204      37.983  49.876  97.634  1.00 54.63           C  
ATOM     32  CD1 PHE A 204      39.244  49.726  98.207  1.00 54.79           C  
ATOM     33  CD2 PHE A 204      37.691  49.176  96.465  1.00 54.57           C  
ATOM     34  CE1 PHE A 204      40.201  48.893  97.624  1.00 54.54           C  
ATOM     35  CE2 PHE A 204      38.640  48.341  95.873  1.00 54.54           C  
ATOM     36  CZ  PHE A 204      39.899  48.201  96.454  1.00 54.71           C  
ATOM     37  N   GLY A 205      35.360  54.058  97.667  1.00 54.75           N  
ATOM     38  CA  GLY A 205      34.267  54.885  98.148  1.00 55.37           C  
ATOM     39  C   GLY A 205      34.253  55.140  99.643  1.00 56.00           C  
ATOM     40  O   GLY A 205      33.446  55.932 100.134  1.00 55.52           O  
ATOM     41  N   VAL A 206      35.147  54.477 100.370  1.00 56.79           N  
ATOM     42  CA  VAL A 206      35.217  54.639 101.818  1.00 57.88           C  
ATOM     43  C   VAL A 206      36.550  55.218 102.276  1.00 59.08           C  
ATOM     44  O   VAL A 206      37.590  54.990 101.656  1.00 58.74           O  
ATOM     45  CB  VAL A 206      35.010  53.291 102.546  1.00 57.34           C  
ATOM     46  CG1 VAL A 206      33.652  52.713 102.195  1.00 57.18           C  
ATOM     47  CG2 VAL A 206      36.118  52.319 102.169  1.00 56.65           C  
ATOM     48  N   GLN A 207      36.507  55.971 103.369  1.00 60.64           N  
ATOM     49  CA  GLN A 207      37.704  56.574 103.937  1.00 62.44           C  
ATOM     50  C   GLN A 207      38.206  55.685 105.067  1.00 62.95           C  
ATOM     51  O   GLN A 207      37.454  55.347 105.982  1.00 63.22           O  
ATOM     52  CB  GLN A 207      37.388  57.973 104.470  1.00 63.25           C  
ATOM     53  CG  GLN A 207      36.981  58.961 103.388  1.00 64.92           C  
ATOM     54  CD  GLN A 207      36.595  60.316 103.946  1.00 65.86           C  
ATOM     55  OE1 GLN A 207      37.382  60.963 104.640  1.00 66.31           O  
ATOM     56  NE2 GLN A 207      35.377  60.754 103.644  1.00 66.29           N  
ATOM     57  N   THR A 208      39.475  55.302 104.997  1.00 63.58           N  
ATOM     58  CA  THR A 208      40.064  54.444 106.015  1.00 64.20           C  
ATOM     59  C   THR A 208      41.567  54.666 106.139  1.00 64.68           C  
ATOM     60  O   THR A 208      42.215  55.132 105.201  1.00 64.64           O  
ATOM     61  CB  THR A 208      39.807  52.957 105.698  1.00 64.07           C  
ATOM     62  OG1 THR A 208      40.477  52.137 106.663  1.00 64.05           O  
ATOM     63  CG2 THR A 208      40.314  52.614 104.304  1.00 63.98           C  
ATOM     64  N   ASP A 209      42.112  54.327 107.303  1.00 65.28           N  
ATOM     65  CA  ASP A 209      43.539  54.482 107.565  1.00 65.92           C  
ATOM     66  C   ASP A 209      44.315  53.300 106.999  1.00 65.97           C  
ATOM     67  O   ASP A 209      45.439  53.452 106.517  1.00 66.07           O  
ATOM     68  CB  ASP A 209      43.796  54.567 109.071  1.00 66.52           C  
ATOM     69  CG  ASP A 209      42.970  55.641 109.746  1.00 67.03           C  
ATOM     70  OD1 ASP A 209      43.077  56.820 109.345  1.00 67.36           O  
ATOM     71  OD2 ASP A 209      42.213  55.303 110.683  1.00 67.40           O  
ATOM     72  N   GLN A 210      43.704  52.122 107.062  1.00 65.77           N  
ATOM     73  CA  GLN A 210      44.333  50.901 106.577  1.00 65.37           C  
ATOM     74  C   GLN A 210      43.873  50.569 105.163  1.00 64.92           C  
ATOM     75  O   GLN A 210      43.578  49.414 104.851  1.00 64.69           O  
ATOM     76  CB  GLN A 210      43.999  49.743 107.519  1.00 65.55           C  
ATOM     77  CG  GLN A 210      44.008  50.134 108.989  1.00 66.09           C  
ATOM     78  CD  GLN A 210      43.834  48.946 109.915  1.00 66.59           C  
ATOM     79  OE1 GLN A 210      43.553  49.106 111.104  1.00 66.81           O  
ATOM     80  NE2 GLN A 210      44.014  47.746 109.378  1.00 66.61           N  
ATOM     81  N   GLU A 211      43.813  51.586 104.310  1.00 64.44           N  
ATOM     82  CA  GLU A 211      43.389  51.402 102.927  1.00 64.29           C  
ATOM     83  C   GLU A 211      44.284  50.386 102.231  1.00 63.40           C  
ATOM     84  O   GLU A 211      43.868  49.710 101.288  1.00 63.40           O  
ATOM     85  CB  GLU A 211      43.440  52.734 102.175  1.00 65.09           C  
ATOM     86  CG  GLU A 211      42.970  52.646 100.731  1.00 66.17           C  
ATOM     87  CD  GLU A 211      42.953  53.995 100.035  1.00 66.75           C  
ATOM     88  OE1 GLU A 211      42.208  54.893 100.488  1.00 66.68           O  
ATOM     89  OE2 GLU A 211      43.685  54.156  99.035  1.00 66.95           O  
ATOM     90  N   GLU A 212      45.518  50.283 102.710  1.00 62.43           N  
ATOM     91  CA  GLU A 212      46.490  49.357 102.148  1.00 61.08           C  
ATOM     92  C   GLU A 212      46.050  47.911 102.365  1.00 59.34           C  
ATOM     93  O   GLU A 212      45.993  47.125 101.420  1.00 58.98           O  
ATOM     94  CB  GLU A 212      47.858  49.595 102.792  1.00 62.44           C  
ATOM     95  CG  GLU A 212      48.995  48.808 102.166  1.00 64.18           C  
ATOM     96  CD  GLU A 212      50.351  49.213 102.719  1.00 65.31           C  
ATOM     97  OE1 GLU A 212      50.569  49.070 103.943  1.00 66.18           O  
ATOM     98  OE2 GLU A 212      51.198  49.678 101.927  1.00 65.64           O  
ATOM     99  N   GLN A 213      45.734  47.565 103.609  1.00 57.33           N  
ATOM    100  CA  GLN A 213      45.302  46.209 103.927  1.00 55.38           C  
ATOM    101  C   GLN A 213      43.925  45.905 103.344  1.00 53.34           C  
ATOM    102  O   GLN A 213      43.622  44.759 103.013  1.00 52.61           O  
ATOM    103  CB  GLN A 213      45.278  45.996 105.441  1.00 56.49           C  
ATOM    104  CG  GLN A 213      46.640  46.105 106.107  1.00 58.30           C  
ATOM    105  CD  GLN A 213      46.648  45.522 107.508  1.00 59.32           C  
ATOM    106  OE1 GLN A 213      45.864  45.927 108.370  1.00 59.62           O  
ATOM    107  NE2 GLN A 213      47.538  44.563 107.743  1.00 59.99           N  
ATOM    108  N   LEU A 214      43.093  46.935 103.225  1.00 51.03           N  
ATOM    109  CA  LEU A 214      41.754  46.767 102.674  1.00 48.87           C  
ATOM    110  C   LEU A 214      41.849  46.297 101.227  1.00 47.73           C  
ATOM    111  O   LEU A 214      41.157  45.363 100.823  1.00 47.35           O  
ATOM    112  CB  LEU A 214      40.978  48.086 102.748  1.00 47.63           C  
ATOM    113  CG  LEU A 214      39.555  48.089 102.177  1.00 46.81           C  
ATOM    114  CD1 LEU A 214      38.709  47.033 102.876  1.00 46.08           C  
ATOM    115  CD2 LEU A 214      38.940  49.469 102.356  1.00 46.54           C  
ATOM    116  N   ALA A 215      42.715  46.943 100.453  1.00 46.64           N  
ATOM    117  CA  ALA A 215      42.902  46.586  99.052  1.00 46.03           C  
ATOM    118  C   ALA A 215      43.381  45.144  98.920  1.00 45.58           C  
ATOM    119  O   ALA A 215      42.944  44.412  98.031  1.00 45.37           O  
ATOM    120  CB  ALA A 215      43.905  47.532  98.401  1.00 46.62           C  
ATOM    121  N   LYS A 216      44.284  44.739  99.808  1.00 45.29           N  
ATOM    122  CA  LYS A 216      44.810  43.380  99.782  1.00 44.85           C  
ATOM    123  C   LYS A 216      43.694  42.379 100.062  1.00 43.43           C  
ATOM    124  O   LYS A 216      43.566  41.367  99.374  1.00 42.84           O  
ATOM    125  CB  LYS A 216      45.915  43.209 100.825  1.00 46.22           C  
ATOM    126  CG  LYS A 216      46.451  41.788 100.904  1.00 48.19           C  
ATOM    127  CD  LYS A 216      47.304  41.581 102.143  1.00 50.20           C  
ATOM    128  CE  LYS A 216      47.726  40.124 102.282  1.00 51.14           C  
ATOM    129  NZ  LYS A 216      48.425  39.871 103.575  1.00 51.90           N  
ATOM    130  N   GLU A 217      42.884  42.665 101.076  1.00 42.03           N  
ATOM    131  CA  GLU A 217      41.790  41.771 101.421  1.00 41.21           C  
ATOM    132  C   GLU A 217      40.799  41.678 100.263  1.00 40.15           C  
ATOM    133  O   GLU A 217      40.302  40.600  99.948  1.00 39.83           O  
ATOM    134  CB  GLU A 217      41.069  42.263 102.675  1.00 41.53           C  
ATOM    135  CG  GLU A 217      40.257  41.177 103.348  1.00 42.03           C  
ATOM    136  CD  GLU A 217      41.139  40.087 103.927  1.00 43.35           C  
ATOM    137  OE1 GLU A 217      40.637  38.966 104.161  1.00 43.61           O  
ATOM    138  OE2 GLU A 217      42.339  40.358 104.155  1.00 43.64           O  
ATOM    139  N   LEU A 218      40.532  42.811  99.619  1.00 39.21           N  
ATOM    140  CA  LEU A 218      39.596  42.848  98.503  1.00 38.79           C  
ATOM    141  C   LEU A 218      40.099  42.138  97.249  1.00 38.55           C  
ATOM    142  O   LEU A 218      39.412  42.112  96.228  1.00 37.62           O  
ATOM    143  CB  LEU A 218      39.215  44.297  98.182  1.00 38.52           C  
ATOM    144  CG  LEU A 218      38.348  44.968  99.257  1.00 38.89           C  
ATOM    145  CD1 LEU A 218      38.053  46.405  98.867  1.00 37.99           C  
ATOM    146  CD2 LEU A 218      37.047  44.189  99.428  1.00 38.65           C  
ATOM    147  N   GLU A 219      41.296  41.562  97.322  1.00 38.97           N  
ATOM    148  CA  GLU A 219      41.841  40.825  96.186  1.00 38.98           C  
ATOM    149  C   GLU A 219      41.108  39.487  96.129  1.00 37.69           C  
ATOM    150  O   GLU A 219      41.192  38.753  95.143  1.00 37.26           O  
ATOM    151  CB  GLU A 219      43.349  40.587  96.351  1.00 40.97           C  
ATOM    152  CG  GLU A 219      44.184  41.857  96.429  1.00 43.81           C  
ATOM    153  CD  GLU A 219      45.681  41.589  96.311  1.00 46.26           C  
ATOM    154  OE1 GLU A 219      46.207  40.738  97.061  1.00 47.48           O  
ATOM    155  OE2 GLU A 219      46.334  42.236  95.466  1.00 48.15           O  
ATOM    156  N   ASP A 220      40.387  39.178  97.204  1.00 36.43           N  
ATOM    157  CA  ASP A 220      39.616  37.944  97.286  1.00 35.54           C  
ATOM    158  C   ASP A 220      38.154  38.183  96.912  1.00 34.66           C  
ATOM    159  O   ASP A 220      37.305  37.323  97.138  1.00 33.72           O  
ATOM    160  CB  ASP A 220      39.671  37.358  98.700  1.00 36.40           C  
ATOM    161  CG  ASP A 220      41.034  36.809  99.053  1.00 37.70           C  
ATOM    162  OD1 ASP A 220      41.709  36.284  98.145  1.00 38.07           O  
ATOM    163  OD2 ASP A 220      41.419  36.888 100.239  1.00 38.78           O  
ATOM    164  N   THR A 221      37.865  39.350  96.342  1.00 33.70           N  
ATOM    165  CA  THR A 221      36.499  39.686  95.945  1.00 33.30           C  
ATOM    166  C   THR A 221      35.857  38.623  95.059  1.00 32.33           C  
ATOM    167  O   THR A 221      34.651  38.393  95.133  1.00 32.06           O  
ATOM    168  CB  THR A 221      36.449  41.043  95.201  1.00 33.24           C  
ATOM    169  OG1 THR A 221      36.741  42.102  96.123  1.00 32.70           O  
ATOM    170  CG2 THR A 221      35.066  41.275  94.588  1.00 33.65           C  
ATOM    171  N   ASN A 222      36.661  37.972  94.224  1.00 32.36           N  
ATOM    172  CA  ASN A 222      36.145  36.944  93.327  1.00 31.99           C  
ATOM    173  C   ASN A 222      36.122  35.554  93.958  1.00 31.69           C  
ATOM    174  O   ASN A 222      35.763  34.574  93.302  1.00 30.39           O  
ATOM    175  CB  ASN A 222      36.977  36.891  92.040  1.00 33.84           C  
ATOM    176  CG  ASN A 222      36.976  38.207  91.287  1.00 35.87           C  
ATOM    177  OD1 ASN A 222      35.980  38.930  91.283  1.00 36.72           O  
ATOM    178  ND2 ASN A 222      38.090  38.518  90.631  1.00 35.95           N  
ATOM    179  N   LYS A 223      36.490  35.472  95.232  1.00 31.99           N  
ATOM    180  CA  LYS A 223      36.530  34.188  95.926  1.00 32.93           C  
ATOM    181  C   LYS A 223      35.384  33.963  96.908  1.00 31.82           C  
ATOM    182  O   LYS A 223      34.979  34.872  97.630  1.00 30.94           O  
ATOM    183  CB  LYS A 223      37.863  34.043  96.665  1.00 35.13           C  
ATOM    184  CG  LYS A 223      39.079  34.058  95.747  1.00 37.97           C  
ATOM    185  CD  LYS A 223      40.368  33.856  96.535  1.00 41.14           C  
ATOM    186  CE  LYS A 223      41.590  33.918  95.623  1.00 42.74           C  
ATOM    187  NZ  LYS A 223      42.862  33.700  96.372  1.00 44.75           N  
ATOM    188  N   TRP A 224      34.883  32.734  96.930  1.00 31.26           N  
ATOM    189  CA  TRP A 224      33.789  32.350  97.815  1.00 31.62           C  
ATOM    190  C   TRP A 224      34.221  32.468  99.277  1.00 32.89           C  
ATOM    191  O   TRP A 224      33.403  32.726 100.152  1.00 33.79           O  
ATOM    192  CB  TRP A 224      33.361  30.909  97.512  1.00 28.98           C  
ATOM    193  CG  TRP A 224      32.004  30.537  98.043  1.00 27.30           C  
ATOM    194  CD1 TRP A 224      31.723  29.632  99.031  1.00 26.18           C  
ATOM    195  CD2 TRP A 224      30.742  31.027  97.578  1.00 25.63           C  
ATOM    196  NE1 TRP A 224      30.360  29.525  99.204  1.00 24.98           N  
ATOM    197  CE2 TRP A 224      29.735  30.370  98.324  1.00 25.03           C  
ATOM    198  CE3 TRP A 224      30.362  31.957  96.600  1.00 24.27           C  
ATOM    199  CZ2 TRP A 224      28.370  30.614  98.120  1.00 23.69           C  
ATOM    200  CZ3 TRP A 224      29.002  32.198  96.396  1.00 23.68           C  
ATOM    201  CH2 TRP A 224      28.025  31.527  97.154  1.00 22.92           C  
ATOM    202  N   GLY A 225      35.511  32.293  99.540  1.00 33.99           N  
ATOM    203  CA  GLY A 225      35.984  32.378 100.913  1.00 35.07           C  
ATOM    204  C   GLY A 225      36.326  33.758 101.461  1.00 35.65           C  
ATOM    205  O   GLY A 225      36.889  33.860 102.550  1.00 35.70           O  
ATOM    206  N   LEU A 226      35.991  34.821 100.732  1.00 35.46           N  
ATOM    207  CA  LEU A 226      36.301  36.177 101.191  1.00 34.32           C  
ATOM    208  C   LEU A 226      35.967  36.384 102.664  1.00 34.02           C  
ATOM    209  O   LEU A 226      34.908  35.966 103.135  1.00 34.20           O  
ATOM    210  CB  LEU A 226      35.544  37.220 100.358  1.00 33.83           C  
ATOM    211  CG  LEU A 226      35.669  38.674 100.836  1.00 34.49           C  
ATOM    212  CD1 LEU A 226      37.117  39.135 100.737  1.00 34.78           C  
ATOM    213  CD2 LEU A 226      34.773  39.576  99.996  1.00 35.36           C  
ATOM    214  N   ASP A 227      36.876  37.024 103.392  1.00 32.58           N  
ATOM    215  CA  ASP A 227      36.652  37.298 104.808  1.00 32.74           C  
ATOM    216  C   ASP A 227      35.984  38.666 104.886  1.00 31.82           C  
ATOM    217  O   ASP A 227      36.651  39.675 105.109  1.00 32.19           O  
ATOM    218  CB  ASP A 227      37.978  37.335 105.568  1.00 33.00           C  
ATOM    219  CG  ASP A 227      37.788  37.332 107.076  1.00 35.31           C  
ATOM    220  OD1 ASP A 227      36.716  37.780 107.550  1.00 34.71           O  
ATOM    221  OD2 ASP A 227      38.718  36.890 107.788  1.00 34.96           O  
ATOM    222  N   VAL A 228      34.668  38.701 104.698  1.00 30.89           N  
ATOM    223  CA  VAL A 228      33.939  39.965 104.726  1.00 30.11           C  
ATOM    224  C   VAL A 228      33.991  40.646 106.093  1.00 29.97           C  
ATOM    225  O   VAL A 228      33.867  41.867 106.189  1.00 29.17           O  
ATOM    226  CB  VAL A 228      32.464  39.769 104.280  1.00 30.08           C  
ATOM    227  CG1 VAL A 228      31.711  38.933 105.296  1.00 29.98           C  
ATOM    228  CG2 VAL A 228      31.798  41.121 104.083  1.00 31.51           C  
ATOM    229  N   PHE A 229      34.175  39.862 107.152  1.00 29.71           N  
ATOM    230  CA  PHE A 229      34.268  40.430 108.494  1.00 30.62           C  
ATOM    231  C   PHE A 229      35.541  41.278 108.582  1.00 31.85           C  
ATOM    232  O   PHE A 229      35.557  42.328 109.227  1.00 31.02           O  
ATOM    233  CB  PHE A 229      34.294  39.317 109.538  1.00 29.84           C  
ATOM    234  CG  PHE A 229      33.042  38.493 109.562  1.00 28.90           C  
ATOM    235  CD1 PHE A 229      31.891  38.968 110.186  1.00 29.02           C  
ATOM    236  CD2 PHE A 229      32.995  37.265 108.913  1.00 28.11           C  
ATOM    237  CE1 PHE A 229      30.709  38.228 110.159  1.00 28.26           C  
ATOM    238  CE2 PHE A 229      31.818  36.518 108.879  1.00 28.60           C  
ATOM    239  CZ  PHE A 229      30.672  37.002 109.503  1.00 27.78           C  
ATOM    240  N   LYS A 230      36.601  40.818 107.923  1.00 33.09           N  
ATOM    241  CA  LYS A 230      37.866  41.550 107.902  1.00 34.85           C  
ATOM    242  C   LYS A 230      37.682  42.832 107.096  1.00 34.47           C  
ATOM    243  O   LYS A 230      38.192  43.891 107.465  1.00 34.89           O  
ATOM    244  CB  LYS A 230      38.974  40.709 107.261  1.00 36.44           C  
ATOM    245  CG  LYS A 230      39.975  40.138 108.249  1.00 41.08           C  
ATOM    246  CD  LYS A 230      41.171  39.508 107.539  1.00 42.73           C  
ATOM    247  CE  LYS A 230      42.181  38.967 108.542  1.00 44.50           C  
ATOM    248  NZ  LYS A 230      43.365  38.349 107.872  1.00 46.00           N  
ATOM    249  N   VAL A 231      36.958  42.723 105.985  1.00 34.32           N  
ATOM    250  CA  VAL A 231      36.693  43.874 105.131  1.00 34.24           C  
ATOM    251  C   VAL A 231      35.944  44.935 105.933  1.00 34.52           C  
ATOM    252  O   VAL A 231      36.228  46.129 105.821  1.00 34.80           O  
ATOM    253  CB  VAL A 231      35.837  43.482 103.900  1.00 33.76           C  
ATOM    254  CG1 VAL A 231      35.448  44.725 103.120  1.00 33.70           C  
ATOM    255  CG2 VAL A 231      36.611  42.528 103.004  1.00 33.26           C  
ATOM    256  N   ALA A 232      34.987  44.491 106.741  1.00 34.65           N  
ATOM    257  CA  ALA A 232      34.197  45.399 107.562  1.00 35.86           C  
ATOM    258  C   ALA A 232      35.106  46.241 108.455  1.00 36.94           C  
ATOM    259  O   ALA A 232      34.951  47.458 108.538  1.00 36.93           O  
ATOM    260  CB  ALA A 232      33.204  44.608 108.417  1.00 34.39           C  
ATOM    261  N   GLU A 233      36.055  45.589 109.119  1.00 38.58           N  
ATOM    262  CA  GLU A 233      36.982  46.296 109.999  1.00 41.11           C  
ATOM    263  C   GLU A 233      37.887  47.265 109.238  1.00 40.84           C  
ATOM    264  O   GLU A 233      38.003  48.435 109.600  1.00 41.57           O  
ATOM    265  CB  GLU A 233      37.859  45.301 110.766  1.00 43.30           C  
ATOM    266  CG  GLU A 233      37.107  44.399 111.730  1.00 47.20           C  
ATOM    267  CD  GLU A 233      38.041  43.672 112.683  1.00 49.92           C  
ATOM    268  OE1 GLU A 233      38.703  44.355 113.497  1.00 51.75           O  
ATOM    269  OE2 GLU A 233      38.118  42.425 112.617  1.00 51.18           O  
ATOM    270  N   LEU A 234      38.517  46.769 108.179  1.00 40.55           N  
ATOM    271  CA  LEU A 234      39.435  47.567 107.376  1.00 40.25           C  
ATOM    272  C   LEU A 234      38.789  48.701 106.582  1.00 40.33           C  
ATOM    273  O   LEU A 234      39.491  49.563 106.052  1.00 40.37           O  
ATOM    274  CB  LEU A 234      40.202  46.654 106.416  1.00 40.61           C  
ATOM    275  CG  LEU A 234      40.978  45.499 107.059  1.00 40.66           C  
ATOM    276  CD1 LEU A 234      41.616  44.647 105.974  1.00 41.63           C  
ATOM    277  CD2 LEU A 234      42.039  46.047 108.001  1.00 41.41           C  
ATOM    278  N   SER A 235      37.462  48.706 106.498  1.00 39.54           N  
ATOM    279  CA  SER A 235      36.761  49.743 105.745  1.00 38.63           C  
ATOM    280  C   SER A 235      36.123  50.787 106.653  1.00 38.59           C  
ATOM    281  O   SER A 235      35.294  51.581 106.210  1.00 38.74           O  
ATOM    282  CB  SER A 235      35.678  49.114 104.864  1.00 38.01           C  
ATOM    283  OG  SER A 235      34.654  48.536 105.654  1.00 36.43           O  
ATOM    284  N   GLY A 236      36.512  50.790 107.923  1.00 38.73           N  
ATOM    285  CA  GLY A 236      35.941  51.746 108.852  1.00 39.19           C  
ATOM    286  C   GLY A 236      34.488  51.404 109.112  1.00 39.30           C  
ATOM    287  O   GLY A 236      33.656  52.283 109.343  1.00 39.27           O  
ATOM    288  N   ASN A 237      34.193  50.108 109.062  1.00 39.54           N  
ATOM    289  CA  ASN A 237      32.854  49.584 109.285  1.00 39.56           C  
ATOM    290  C   ASN A 237      31.878  49.977 108.174  1.00 38.55           C  
ATOM    291  O   ASN A 237      30.718  50.303 108.429  1.00 38.28           O  
ATOM    292  CB  ASN A 237      32.332  50.043 110.650  1.00 42.93           C  
ATOM    293  CG  ASN A 237      31.120  49.258 111.103  1.00 45.39           C  
ATOM    294  OD1 ASN A 237      30.002  49.501 110.649  1.00 49.13           O  
ATOM    295  ND2 ASN A 237      31.337  48.297 111.995  1.00 47.15           N  
ATOM    296  N   ARG A 238      32.363  49.946 106.938  1.00 36.79           N  
ATOM    297  CA  ARG A 238      31.539  50.264 105.779  1.00 36.37           C  
ATOM    298  C   ARG A 238      31.765  49.187 104.717  1.00 33.83           C  
ATOM    299  O   ARG A 238      32.181  49.472 103.597  1.00 33.68           O  
ATOM    300  CB  ARG A 238      31.883  51.661 105.241  1.00 38.94           C  
ATOM    301  CG  ARG A 238      31.510  52.772 106.225  1.00 42.57           C  
ATOM    302  CD  ARG A 238      31.515  54.163 105.606  1.00 45.98           C  
ATOM    303  NE  ARG A 238      32.860  54.685 105.377  1.00 48.91           N  
ATOM    304  CZ  ARG A 238      33.115  55.928 104.974  1.00 50.97           C  
ATOM    305  NH1 ARG A 238      32.116  56.775 104.756  1.00 51.79           N  
ATOM    306  NH2 ARG A 238      34.365  56.330 104.791  1.00 51.62           N  
ATOM    307  N   PRO A 239      31.474  47.923 105.069  1.00 31.82           N  
ATOM    308  CA  PRO A 239      31.640  46.774 104.175  1.00 30.85           C  
ATOM    309  C   PRO A 239      30.843  46.833 102.877  1.00 29.32           C  
ATOM    310  O   PRO A 239      31.359  46.479 101.818  1.00 29.23           O  
ATOM    311  CB  PRO A 239      31.231  45.593 105.052  1.00 30.70           C  
ATOM    312  CG  PRO A 239      30.190  46.194 105.950  1.00 31.07           C  
ATOM    313  CD  PRO A 239      30.825  47.511 106.328  1.00 31.58           C  
ATOM    314  N   LEU A 240      29.592  47.276 102.956  1.00 28.37           N  
ATOM    315  CA  LEU A 240      28.753  47.343 101.763  1.00 27.88           C  
ATOM    316  C   LEU A 240      29.314  48.296 100.712  1.00 28.03           C  
ATOM    317  O   LEU A 240      29.428  47.941  99.541  1.00 27.39           O  
ATOM    318  CB  LEU A 240      27.327  47.757 102.133  1.00 26.65           C  
ATOM    319  CG  LEU A 240      26.307  47.744 100.987  1.00 26.20           C  
ATOM    320  CD1 LEU A 240      26.315  46.397 100.276  1.00 25.69           C  
ATOM    321  CD2 LEU A 240      24.924  48.047 101.548  1.00 26.38           C  
ATOM    322  N   THR A 241      29.658  49.509 101.128  1.00 28.70           N  
ATOM    323  CA  THR A 241      30.208  50.483 100.197  1.00 28.52           C  
ATOM    324  C   THR A 241      31.497  49.954  99.566  1.00 28.46           C  
ATOM    325  O   THR A 241      31.683  50.036  98.355  1.00 28.05           O  
ATOM    326  CB  THR A 241      30.489  51.834 100.904  1.00 29.88           C  
ATOM    327  OG1 THR A 241      29.257  52.382 101.401  1.00 30.45           O  
ATOM    328  CG2 THR A 241      31.118  52.819  99.934  1.00 29.56           C  
ATOM    329  N   ALA A 242      32.382  49.398 100.385  1.00 28.34           N  
ATOM    330  CA  ALA A 242      33.648  48.873  99.880  1.00 28.79           C  
ATOM    331  C   ALA A 242      33.454  47.709  98.913  1.00 28.58           C  
ATOM    332  O   ALA A 242      34.059  47.672  97.840  1.00 28.38           O  
ATOM    333  CB  ALA A 242      34.535  48.437 101.046  1.00 29.05           C  
ATOM    334  N   ILE A 243      32.605  46.760  99.296  1.00 28.77           N  
ATOM    335  CA  ILE A 243      32.348  45.586  98.472  1.00 28.74           C  
ATOM    336  C   ILE A 243      31.700  45.904  97.132  1.00 27.99           C  
ATOM    337  O   ILE A 243      32.096  45.355  96.104  1.00 27.24           O  
ATOM    338  CB  ILE A 243      31.468  44.557  99.229  1.00 29.46           C  
ATOM    339  CG1 ILE A 243      32.280  43.908 100.352  1.00 30.85           C  
ATOM    340  CG2 ILE A 243      30.944  43.498  98.270  1.00 30.25           C  
ATOM    341  CD1 ILE A 243      33.474  43.115  99.868  1.00 32.79           C  
ATOM    342  N   ILE A 244      30.700  46.779  97.133  1.00 28.00           N  
ATOM    343  CA  ILE A 244      30.042  47.123  95.880  1.00 27.51           C  
ATOM    344  C   ILE A 244      31.035  47.817  94.952  1.00 28.42           C  
ATOM    345  O   ILE A 244      31.071  47.533  93.757  1.00 28.49           O  
ATOM    346  CB  ILE A 244      28.808  48.033  96.106  1.00 27.26           C  
ATOM    347  CG1 ILE A 244      27.734  47.270  96.894  1.00 27.65           C  
ATOM    348  CG2 ILE A 244      28.234  48.485  94.759  1.00 25.91           C  
ATOM    349  CD1 ILE A 244      27.207  46.020  96.180  1.00 26.89           C  
ATOM    350  N   PHE A 245      31.850  48.717  95.494  1.00 29.11           N  
ATOM    351  CA  PHE A 245      32.838  49.395  94.656  1.00 30.27           C  
ATOM    352  C   PHE A 245      33.829  48.388  94.074  1.00 30.15           C  
ATOM    353  O   PHE A 245      34.173  48.459  92.893  1.00 31.06           O  
ATOM    354  CB  PHE A 245      33.597  50.468  95.448  1.00 30.64           C  
ATOM    355  CG  PHE A 245      33.097  51.871  95.205  1.00 32.04           C  
ATOM    356  CD1 PHE A 245      32.019  52.379  95.921  1.00 32.41           C  
ATOM    357  CD2 PHE A 245      33.699  52.677  94.239  1.00 32.47           C  
ATOM    358  CE1 PHE A 245      31.543  53.673  95.682  1.00 33.28           C  
ATOM    359  CE2 PHE A 245      33.233  53.971  93.989  1.00 32.82           C  
ATOM    360  CZ  PHE A 245      32.153  54.471  94.712  1.00 32.95           C  
ATOM    361  N   SER A 246      34.277  47.443  94.896  1.00 30.12           N  
ATOM    362  CA  SER A 246      35.231  46.436  94.436  1.00 29.50           C  
ATOM    363  C   SER A 246      34.608  45.578  93.338  1.00 29.63           C  
ATOM    364  O   SER A 246      35.242  45.301  92.318  1.00 29.17           O  
ATOM    365  CB  SER A 246      35.679  45.552  95.607  1.00 29.97           C  
ATOM    366  OG  SER A 246      36.685  44.631  95.206  1.00 28.86           O  
ATOM    367  N   ILE A 247      33.362  45.162  93.546  1.00 28.88           N  
ATOM    368  CA  ILE A 247      32.665  44.347  92.559  1.00 28.38           C  
ATOM    369  C   ILE A 247      32.441  45.119  91.257  1.00 29.05           C  
ATOM    370  O   ILE A 247      32.782  44.639  90.176  1.00 28.67           O  
ATOM    371  CB  ILE A 247      31.292  43.876  93.083  1.00 27.92           C  
ATOM    372  CG1 ILE A 247      31.477  42.970  94.304  1.00 28.86           C  
ATOM    373  CG2 ILE A 247      30.543  43.136  91.978  1.00 28.00           C  
ATOM    374  CD1 ILE A 247      30.160  42.488  94.918  1.00 28.01           C  
ATOM    375  N   PHE A 248      31.863  46.313  91.362  1.00 29.43           N  
ATOM    376  CA  PHE A 248      31.593  47.121  90.177  1.00 30.77           C  
ATOM    377  C   PHE A 248      32.852  47.409  89.359  1.00 31.87           C  
ATOM    378  O   PHE A 248      32.820  47.360  88.130  1.00 31.70           O  
ATOM    379  CB  PHE A 248      30.904  48.429  90.580  1.00 30.69           C  
ATOM    380  CG  PHE A 248      29.412  48.298  90.769  1.00 29.78           C  
ATOM    381  CD1 PHE A 248      28.858  47.128  91.282  1.00 28.98           C  
ATOM    382  CD2 PHE A 248      28.563  49.355  90.453  1.00 30.11           C  
ATOM    383  CE1 PHE A 248      27.482  47.010  91.479  1.00 29.28           C  
ATOM    384  CE2 PHE A 248      27.184  49.250  90.648  1.00 29.55           C  
ATOM    385  CZ  PHE A 248      26.644  48.074  91.162  1.00 29.05           C  
ATOM    386  N   GLN A 249      33.957  47.705  90.035  1.00 33.60           N  
ATOM    387  CA  GLN A 249      35.213  47.980  89.337  1.00 35.17           C  
ATOM    388  C   GLN A 249      35.677  46.712  88.627  1.00 35.44           C  
ATOM    389  O   GLN A 249      36.082  46.746  87.463  1.00 35.77           O  
ATOM    390  CB  GLN A 249      36.285  48.436  90.331  1.00 36.50           C  
ATOM    391  CG  GLN A 249      36.035  49.814  90.928  1.00 39.22           C  
ATOM    392  CD  GLN A 249      36.928  50.101  92.123  1.00 40.80           C  
ATOM    393  OE1 GLN A 249      36.975  51.225  92.624  1.00 42.07           O  
ATOM    394  NE2 GLN A 249      37.636  49.078  92.592  1.00 42.27           N  
ATOM    395  N   GLU A 250      35.606  45.594  89.343  1.00 35.12           N  
ATOM    396  CA  GLU A 250      36.001  44.297  88.812  1.00 34.84           C  
ATOM    397  C   GLU A 250      35.226  43.968  87.538  1.00 34.52           C  
ATOM    398  O   GLU A 250      35.794  43.449  86.575  1.00 34.31           O  
ATOM    399  CB  GLU A 250      35.761  43.218  89.875  1.00 36.46           C  
ATOM    400  CG  GLU A 250      35.963  41.777  89.420  1.00 39.32           C  
ATOM    401  CD  GLU A 250      37.375  41.494  88.943  1.00 41.52           C  
ATOM    402  OE1 GLU A 250      38.332  42.017  89.556  1.00 41.78           O  
ATOM    403  OE2 GLU A 250      37.524  40.732  87.962  1.00 43.67           O  
ATOM    404  N   ARG A 251      33.930  44.271  87.531  1.00 32.49           N  
ATOM    405  CA  ARG A 251      33.096  44.002  86.364  1.00 32.17           C  
ATOM    406  C   ARG A 251      33.043  45.188  85.398  1.00 31.82           C  
ATOM    407  O   ARG A 251      32.361  45.132  84.378  1.00 31.64           O  
ATOM    408  CB  ARG A 251      31.676  43.616  86.801  1.00 31.41           C  
ATOM    409  CG  ARG A 251      31.586  42.230  87.434  1.00 29.91           C  
ATOM    410  CD  ARG A 251      30.193  41.924  87.972  1.00 28.87           C  
ATOM    411  NE  ARG A 251      30.104  40.551  88.466  1.00 27.73           N  
ATOM    412  CZ  ARG A 251      29.980  39.480  87.686  1.00 28.21           C  
ATOM    413  NH1 ARG A 251      29.919  39.617  86.365  1.00 27.00           N  
ATOM    414  NH2 ARG A 251      29.942  38.266  88.225  1.00 27.77           N  
ATOM    415  N   ASP A 252      33.765  46.255  85.728  1.00 32.45           N  
ATOM    416  CA  ASP A 252      33.819  47.453  84.892  1.00 32.74           C  
ATOM    417  C   ASP A 252      32.418  48.016  84.639  1.00 32.58           C  
ATOM    418  O   ASP A 252      32.128  48.530  83.557  1.00 33.00           O  
ATOM    419  CB  ASP A 252      34.512  47.121  83.563  1.00 33.92           C  
ATOM    420  CG  ASP A 252      35.074  48.350  82.869  1.00 35.50           C  
ATOM    421  OD1 ASP A 252      35.597  49.242  83.568  1.00 36.01           O  
ATOM    422  OD2 ASP A 252      35.012  48.416  81.623  1.00 37.44           O  
ATOM    423  N   LEU A 253      31.560  47.923  85.652  1.00 31.94           N  
ATOM    424  CA  LEU A 253      30.187  48.403  85.553  1.00 31.49           C  
ATOM    425  C   LEU A 253      30.042  49.924  85.571  1.00 31.86           C  
ATOM    426  O   LEU A 253      29.092  50.460  85.001  1.00 31.31           O  
ATOM    427  CB  LEU A 253      29.337  47.792  86.673  1.00 30.95           C  
ATOM    428  CG  LEU A 253      29.012  46.305  86.506  1.00 29.84           C  
ATOM    429  CD1 LEU A 253      28.333  45.770  87.755  1.00 30.52           C  
ATOM    430  CD2 LEU A 253      28.127  46.118  85.294  1.00 30.50           C  
ATOM    431  N   LEU A 254      30.966  50.626  86.222  1.00 32.40           N  
ATOM    432  CA  LEU A 254      30.871  52.082  86.254  1.00 33.82           C  
ATOM    433  C   LEU A 254      31.002  52.650  84.845  1.00 34.63           C  
ATOM    434  O   LEU A 254      30.252  53.542  84.455  1.00 35.29           O  
ATOM    435  CB  LEU A 254      31.944  52.690  87.162  1.00 34.06           C  
ATOM    436  CG  LEU A 254      31.726  52.523  88.667  1.00 35.33           C  
ATOM    437  CD1 LEU A 254      32.595  51.399  89.199  1.00 35.49           C  
ATOM    438  CD2 LEU A 254      32.068  53.829  89.369  1.00 37.06           C  
ATOM    439  N   LYS A 255      31.949  52.120  84.077  1.00 35.17           N  
ATOM    440  CA  LYS A 255      32.162  52.586  82.712  1.00 35.68           C  
ATOM    441  C   LYS A 255      31.044  52.125  81.775  1.00 35.19           C  
ATOM    442  O   LYS A 255      30.570  52.890  80.935  1.00 34.45           O  
ATOM    443  CB  LYS A 255      33.512  52.080  82.200  1.00 37.85           C  
ATOM    444  CG  LYS A 255      33.830  52.469  80.767  1.00 40.53           C  
ATOM    445  CD  LYS A 255      35.147  51.846  80.327  1.00 43.21           C  
ATOM    446  CE  LYS A 255      35.404  52.074  78.847  1.00 44.74           C  
ATOM    447  NZ  LYS A 255      36.627  51.347  78.404  1.00 46.39           N  
ATOM    448  N   THR A 256      30.622  50.874  81.927  1.00 34.18           N  
ATOM    449  CA  THR A 256      29.569  50.307  81.091  1.00 33.06           C  
ATOM    450  C   THR A 256      28.257  51.090  81.158  1.00 32.46           C  
ATOM    451  O   THR A 256      27.620  51.331  80.133  1.00 31.64           O  
ATOM    452  CB  THR A 256      29.290  48.837  81.482  1.00 33.68           C  
ATOM    453  OG1 THR A 256      30.481  48.062  81.296  1.00 34.10           O  
ATOM    454  CG2 THR A 256      28.171  48.254  80.632  1.00 33.13           C  
ATOM    455  N   PHE A 257      27.857  51.488  82.361  1.00 31.42           N  
ATOM    456  CA  PHE A 257      26.609  52.227  82.538  1.00 31.60           C  
ATOM    457  C   PHE A 257      26.825  53.686  82.923  1.00 32.14           C  
ATOM    458  O   PHE A 257      25.908  54.358  83.399  1.00 31.52           O  
ATOM    459  CB  PHE A 257      25.742  51.523  83.586  1.00 29.64           C  
ATOM    460  CG  PHE A 257      25.202  50.201  83.124  1.00 29.09           C  
ATOM    461  CD1 PHE A 257      24.220  50.144  82.139  1.00 28.96           C  
ATOM    462  CD2 PHE A 257      25.698  49.009  83.646  1.00 29.08           C  
ATOM    463  CE1 PHE A 257      23.737  48.916  81.676  1.00 30.12           C  
ATOM    464  CE2 PHE A 257      25.223  47.775  83.192  1.00 29.04           C  
ATOM    465  CZ  PHE A 257      24.240  47.728  82.204  1.00 29.96           C  
ATOM    466  N   GLN A 258      28.045  54.169  82.709  1.00 33.23           N  
ATOM    467  CA  GLN A 258      28.390  55.547  83.021  1.00 33.98           C  
ATOM    468  C   GLN A 258      27.872  55.969  84.387  1.00 33.93           C  
ATOM    469  O   GLN A 258      27.146  56.958  84.518  1.00 33.37           O  
ATOM    470  CB  GLN A 258      27.849  56.482  81.936  1.00 35.62           C  
ATOM    471  CG  GLN A 258      28.539  56.305  80.590  1.00 38.08           C  
ATOM    472  CD  GLN A 258      30.029  56.602  80.667  1.00 40.90           C  
ATOM    473  OE1 GLN A 258      30.435  57.739  80.927  1.00 42.18           O  
ATOM    474  NE2 GLN A 258      30.852  55.577  80.452  1.00 41.28           N  
ATOM    475  N   ILE A 259      28.241  55.204  85.406  1.00 33.35           N  
ATOM    476  CA  ILE A 259      27.836  55.512  86.766  1.00 33.29           C  
ATOM    477  C   ILE A 259      28.921  56.399  87.364  1.00 33.97           C  
ATOM    478  O   ILE A 259      30.061  55.969  87.518  1.00 33.74           O  
ATOM    479  CB  ILE A 259      27.719  54.233  87.625  1.00 32.75           C  
ATOM    480  CG1 ILE A 259      26.712  53.268  86.997  1.00 31.64           C  
ATOM    481  CG2 ILE A 259      27.302  54.598  89.045  1.00 31.49           C  
ATOM    482  CD1 ILE A 259      26.649  51.909  87.695  1.00 31.86           C  
ATOM    483  N   PRO A 260      28.588  57.656  87.694  1.00 34.74           N  
ATOM    484  CA  PRO A 260      29.605  58.540  88.275  1.00 35.56           C  
ATOM    485  C   PRO A 260      30.104  57.959  89.600  1.00 36.04           C  
ATOM    486  O   PRO A 260      29.306  57.562  90.447  1.00 36.72           O  
ATOM    487  CB  PRO A 260      28.849  59.854  88.464  1.00 36.05           C  
ATOM    488  CG  PRO A 260      27.827  59.817  87.361  1.00 35.31           C  
ATOM    489  CD  PRO A 260      27.338  58.392  87.438  1.00 34.86           C  
ATOM    490  N   ALA A 261      31.421  57.909  89.774  1.00 35.58           N  
ATOM    491  CA  ALA A 261      32.005  57.366  90.994  1.00 35.32           C  
ATOM    492  C   ALA A 261      31.518  58.069  92.263  1.00 34.90           C  
ATOM    493  O   ALA A 261      31.219  57.411  93.262  1.00 33.84           O  
ATOM    494  CB  ALA A 261      33.527  57.423  90.914  1.00 35.23           C  
ATOM    495  N   ASP A 262      31.440  59.397  92.236  1.00 34.46           N  
ATOM    496  CA  ASP A 262      30.982  60.130  93.413  1.00 34.71           C  
ATOM    497  C   ASP A 262      29.513  59.841  93.705  1.00 33.43           C  
ATOM    498  O   ASP A 262      29.099  59.800  94.865  1.00 33.20           O  
ATOM    499  CB  ASP A 262      31.191  61.642  93.245  1.00 36.60           C  
ATOM    500  CG  ASP A 262      30.492  62.210  92.019  1.00 38.38           C  
ATOM    501  OD1 ASP A 262      30.097  63.395  92.062  1.00 39.87           O  
ATOM    502  OD2 ASP A 262      30.349  61.490  91.009  1.00 39.48           O  
ATOM    503  N   THR A 263      28.730  59.642  92.649  1.00 32.80           N  
ATOM    504  CA  THR A 263      27.311  59.341  92.797  1.00 32.06           C  
ATOM    505  C   THR A 263      27.169  57.991  93.502  1.00 31.08           C  
ATOM    506  O   THR A 263      26.396  57.846  94.444  1.00 29.94           O  
ATOM    507  CB  THR A 263      26.604  59.255  91.422  1.00 32.21           C  
ATOM    508  OG1 THR A 263      26.840  60.459  90.680  1.00 33.24           O  
ATOM    509  CG2 THR A 263      25.101  59.072  91.605  1.00 31.64           C  
ATOM    510  N   LEU A 264      27.930  57.006  93.041  1.00 30.92           N  
ATOM    511  CA  LEU A 264      27.875  55.674  93.638  1.00 30.81           C  
ATOM    512  C   LEU A 264      28.257  55.734  95.116  1.00 30.80           C  
ATOM    513  O   LEU A 264      27.593  55.132  95.962  1.00 29.99           O  
ATOM    514  CB  LEU A 264      28.810  54.719  92.891  1.00 30.34           C  
ATOM    515  CG  LEU A 264      28.790  53.254  93.342  1.00 30.54           C  
ATOM    516  CD1 LEU A 264      27.396  52.667  93.160  1.00 29.37           C  
ATOM    517  CD2 LEU A 264      29.811  52.467  92.536  1.00 29.74           C  
ATOM    518  N   ALA A 265      29.322  56.468  95.429  1.00 30.29           N  
ATOM    519  CA  ALA A 265      29.766  56.594  96.814  1.00 30.18           C  
ATOM    520  C   ALA A 265      28.672  57.215  97.680  1.00 30.38           C  
ATOM    521  O   ALA A 265      28.367  56.720  98.767  1.00 30.62           O  
ATOM    522  CB  ALA A 265      31.042  57.445  96.888  1.00 29.89           C  
ATOM    523  N   THR A 266      28.075  58.298  97.193  1.00 30.18           N  
ATOM    524  CA  THR A 266      27.027  58.980  97.942  1.00 30.24           C  
ATOM    525  C   THR A 266      25.820  58.064  98.163  1.00 29.23           C  
ATOM    526  O   THR A 266      25.298  57.982  99.270  1.00 29.18           O  
ATOM    527  CB  THR A 266      26.570  60.263  97.215  1.00 30.73           C  
ATOM    528  OG1 THR A 266      27.720  61.014  96.809  1.00 31.47           O  
ATOM    529  CG2 THR A 266      25.724  61.128  98.140  1.00 30.93           C  
ATOM    530  N   TYR A 267      25.381  57.375  97.114  1.00 28.87           N  
ATOM    531  CA  TYR A 267      24.240  56.475  97.247  1.00 28.98           C  
ATOM    532  C   TYR A 267      24.536  55.352  98.242  1.00 28.19           C  
ATOM    533  O   TYR A 267      23.747  55.093  99.151  1.00 28.64           O  
ATOM    534  CB  TYR A 267      23.864  55.848  95.901  1.00 28.24           C  
ATOM    535  CG  TYR A 267      22.751  54.824  96.040  1.00 27.05           C  
ATOM    536  CD1 TYR A 267      21.424  55.222  96.206  1.00 26.59           C  
ATOM    537  CD2 TYR A 267      23.040  53.459  96.096  1.00 26.55           C  
ATOM    538  CE1 TYR A 267      20.411  54.284  96.430  1.00 26.07           C  
ATOM    539  CE2 TYR A 267      22.040  52.516  96.322  1.00 25.04           C  
ATOM    540  CZ  TYR A 267      20.730  52.932  96.488  1.00 26.37           C  
ATOM    541  OH  TYR A 267      19.744  51.999  96.721  1.00 25.21           O  
ATOM    542  N   LEU A 268      25.672  54.688  98.061  1.00 28.44           N  
ATOM    543  CA  LEU A 268      26.067  53.582  98.936  1.00 29.35           C  
ATOM    544  C   LEU A 268      26.224  53.995 100.393  1.00 29.83           C  
ATOM    545  O   LEU A 268      25.771  53.288 101.293  1.00 29.54           O  
ATOM    546  CB  LEU A 268      27.367  52.950  98.438  1.00 28.77           C  
ATOM    547  CG  LEU A 268      27.254  52.128  97.152  1.00 29.01           C  
ATOM    548  CD1 LEU A 268      28.635  51.741  96.659  1.00 28.18           C  
ATOM    549  CD2 LEU A 268      26.407  50.882  97.413  1.00 29.21           C  
ATOM    550  N   LEU A 269      26.872  55.130 100.635  1.00 30.22           N  
ATOM    551  CA  LEU A 269      27.044  55.589 102.006  1.00 31.85           C  
ATOM    552  C   LEU A 269      25.670  55.798 102.630  1.00 31.66           C  
ATOM    553  O   LEU A 269      25.452  55.496 103.802  1.00 31.58           O  
ATOM    554  CB  LEU A 269      27.852  56.893 102.043  1.00 33.59           C  
ATOM    555  CG  LEU A 269      29.340  56.717 101.714  1.00 35.82           C  
ATOM    556  CD1 LEU A 269      30.041  58.068 101.718  1.00 36.91           C  
ATOM    557  CD2 LEU A 269      29.980  55.776 102.741  1.00 36.69           C  
ATOM    558  N   MET A 270      24.740  56.306 101.832  1.00 31.69           N  
ATOM    559  CA  MET A 270      23.386  56.544 102.307  1.00 31.85           C  
ATOM    560  C   MET A 270      22.640  55.217 102.492  1.00 29.89           C  
ATOM    561  O   MET A 270      21.921  55.034 103.469  1.00 29.95           O  
ATOM    562  CB  MET A 270      22.647  57.448 101.311  1.00 34.63           C  
ATOM    563  CG  MET A 270      21.218  57.782 101.695  1.00 39.74           C  
ATOM    564  SD  MET A 270      20.547  59.150 100.714  1.00 45.33           S  
ATOM    565  CE  MET A 270      20.540  60.460 101.949  1.00 44.63           C  
ATOM    566  N   LEU A 271      22.820  54.288 101.558  1.00 28.34           N  
ATOM    567  CA  LEU A 271      22.154  52.989 101.652  1.00 27.13           C  
ATOM    568  C   LEU A 271      22.651  52.221 102.875  1.00 26.67           C  
ATOM    569  O   LEU A 271      21.858  51.721 103.680  1.00 26.14           O  
ATOM    570  CB  LEU A 271      22.412  52.166 100.387  1.00 25.81           C  
ATOM    571  CG  LEU A 271      21.909  50.715 100.382  1.00 26.06           C  
ATOM    572  CD1 LEU A 271      20.379  50.676 100.396  1.00 25.20           C  
ATOM    573  CD2 LEU A 271      22.431  50.013  99.140  1.00 25.13           C  
ATOM    574  N   GLU A 272      23.968  52.132 103.008  1.00 26.47           N  
ATOM    575  CA  GLU A 272      24.576  51.432 104.129  1.00 27.06           C  
ATOM    576  C   GLU A 272      24.090  52.059 105.431  1.00 27.12           C  
ATOM    577  O   GLU A 272      23.917  51.371 106.436  1.00 26.77           O  
ATOM    578  CB  GLU A 272      26.107  51.505 104.017  1.00 27.64           C  
ATOM    579  CG  GLU A 272      26.873  50.816 105.144  1.00 28.24           C  
ATOM    580  CD  GLU A 272      28.144  50.139 104.659  1.00 28.65           C  
ATOM    581  OE1 GLU A 272      28.885  50.748 103.856  1.00 29.02           O  
ATOM    582  OE2 GLU A 272      28.408  48.993 105.086  1.00 28.14           O  
ATOM    583  N   GLY A 273      23.848  53.368 105.395  1.00 26.82           N  
ATOM    584  CA  GLY A 273      23.373  54.074 106.573  1.00 26.57           C  
ATOM    585  C   GLY A 273      21.941  53.728 106.939  1.00 26.68           C  
ATOM    586  O   GLY A 273      21.506  53.984 108.065  1.00 26.26           O  
ATOM    587  N   HIS A 274      21.197  53.150 105.998  1.00 26.27           N  
ATOM    588  CA  HIS A 274      19.817  52.774 106.278  1.00 27.26           C  
ATOM    589  C   HIS A 274      19.665  51.342 106.777  1.00 27.04           C  
ATOM    590  O   HIS A 274      18.552  50.868 106.997  1.00 25.72           O  
ATOM    591  CB  HIS A 274      18.923  53.039 105.068  1.00 29.10           C  
ATOM    592  CG  HIS A 274      18.495  54.470 104.958  1.00 32.35           C  
ATOM    593  ND1 HIS A 274      19.389  55.499 104.744  1.00 33.99           N  
ATOM    594  CD2 HIS A 274      17.278  55.051 105.094  1.00 32.86           C  
ATOM    595  CE1 HIS A 274      18.741  56.651 104.755  1.00 34.30           C  
ATOM    596  NE2 HIS A 274      17.460  56.407 104.967  1.00 34.36           N  
ATOM    597  N   TYR A 275      20.791  50.651 106.940  1.00 27.47           N  
ATOM    598  CA  TYR A 275      20.774  49.313 107.522  1.00 28.03           C  
ATOM    599  C   TYR A 275      21.016  49.619 109.001  1.00 29.25           C  
ATOM    600  O   TYR A 275      21.786  50.521 109.324  1.00 30.38           O  
ATOM    601  CB  TYR A 275      21.912  48.440 106.980  1.00 26.32           C  
ATOM    602  CG  TYR A 275      21.571  47.713 105.699  1.00 24.90           C  
ATOM    603  CD1 TYR A 275      21.771  48.309 104.454  1.00 24.15           C  
ATOM    604  CD2 TYR A 275      21.022  46.429 105.736  1.00 23.80           C  
ATOM    605  CE1 TYR A 275      21.431  47.642 103.272  1.00 23.01           C  
ATOM    606  CE2 TYR A 275      20.678  45.758 104.570  1.00 22.89           C  
ATOM    607  CZ  TYR A 275      20.883  46.367 103.345  1.00 22.77           C  
ATOM    608  OH  TYR A 275      20.527  45.701 102.199  1.00 21.07           O  
ATOM    609  N   HIS A 276      20.365  48.890 109.900  1.00 30.39           N  
ATOM    610  CA  HIS A 276      20.533  49.148 111.328  1.00 30.84           C  
ATOM    611  C   HIS A 276      21.727  48.396 111.921  1.00 31.13           C  
ATOM    612  O   HIS A 276      21.716  47.170 112.023  1.00 29.13           O  
ATOM    613  CB  HIS A 276      19.247  48.771 112.070  1.00 32.87           C  
ATOM    614  CG  HIS A 276      18.016  49.425 111.514  1.00 35.54           C  
ATOM    615  ND1 HIS A 276      16.751  49.161 111.993  1.00 37.04           N  
ATOM    616  CD2 HIS A 276      17.858  50.324 110.513  1.00 36.88           C  
ATOM    617  CE1 HIS A 276      15.867  49.867 111.310  1.00 37.28           C  
ATOM    618  NE2 HIS A 276      16.513  50.581 110.406  1.00 36.95           N  
ATOM    619  N   ALA A 277      22.752  49.144 112.322  1.00 31.81           N  
ATOM    620  CA  ALA A 277      23.954  48.554 112.898  1.00 32.74           C  
ATOM    621  C   ALA A 277      23.661  47.783 114.186  1.00 33.27           C  
ATOM    622  O   ALA A 277      24.383  46.847 114.530  1.00 34.04           O  
ATOM    623  CB  ALA A 277      24.991  49.641 113.164  1.00 34.03           C  
ATOM    624  N   ASN A 278      22.598  48.170 114.884  1.00 32.31           N  
ATOM    625  CA  ASN A 278      22.217  47.516 116.134  1.00 32.75           C  
ATOM    626  C   ASN A 278      21.484  46.198 115.899  1.00 30.97           C  
ATOM    627  O   ASN A 278      21.240  45.443 116.838  1.00 31.82           O  
ATOM    628  CB  ASN A 278      21.342  48.451 116.973  1.00 34.91           C  
ATOM    629  CG  ASN A 278      20.115  48.920 116.223  1.00 37.08           C  
ATOM    630  OD1 ASN A 278      20.223  49.587 115.193  1.00 38.85           O  
ATOM    631  ND2 ASN A 278      18.938  48.572 116.733  1.00 39.00           N  
ATOM    632  N   VAL A 279      21.112  45.937 114.649  1.00 28.46           N  
ATOM    633  CA  VAL A 279      20.443  44.689 114.297  1.00 27.04           C  
ATOM    634  C   VAL A 279      21.609  43.747 114.006  1.00 25.95           C  
ATOM    635  O   VAL A 279      22.356  43.951 113.055  1.00 25.81           O  
ATOM    636  CB  VAL A 279      19.539  44.878 113.058  1.00 26.85           C  
ATOM    637  CG1 VAL A 279      19.045  43.531 112.544  1.00 25.95           C  
ATOM    638  CG2 VAL A 279      18.345  45.757 113.441  1.00 26.62           C  
ATOM    639  N   ALA A 280      21.757  42.735 114.854  1.00 24.99           N  
ATOM    640  CA  ALA A 280      22.863  41.778 114.785  1.00 23.72           C  
ATOM    641  C   ALA A 280      23.204  41.091 113.460  1.00 22.68           C  
ATOM    642  O   ALA A 280      24.376  41.013 113.089  1.00 21.18           O  
ATOM    643  CB  ALA A 280      22.684  40.720 115.885  1.00 23.72           C  
ATOM    644  N   TYR A 281      22.206  40.575 112.752  1.00 21.27           N  
ATOM    645  CA  TYR A 281      22.486  39.884 111.493  1.00 20.44           C  
ATOM    646  C   TYR A 281      22.046  40.680 110.270  1.00 20.93           C  
ATOM    647  O   TYR A 281      22.829  40.894 109.343  1.00 21.25           O  
ATOM    648  CB  TYR A 281      21.801  38.514 111.480  1.00 19.81           C  
ATOM    649  CG  TYR A 281      21.990  37.728 110.200  1.00 20.53           C  
ATOM    650  CD1 TYR A 281      23.208  37.109 109.906  1.00 19.95           C  
ATOM    651  CD2 TYR A 281      20.939  37.576 109.295  1.00 21.13           C  
ATOM    652  CE1 TYR A 281      23.371  36.348 108.744  1.00 19.58           C  
ATOM    653  CE2 TYR A 281      21.088  36.822 108.135  1.00 21.33           C  
ATOM    654  CZ  TYR A 281      22.307  36.204 107.868  1.00 20.98           C  
ATOM    655  OH  TYR A 281      22.430  35.413 106.750  1.00 20.19           O  
ATOM    656  N   HIS A 282      20.794  41.126 110.265  1.00 21.13           N  
ATOM    657  CA  HIS A 282      20.299  41.884 109.122  1.00 21.67           C  
ATOM    658  C   HIS A 282      20.772  43.331 109.082  1.00 22.47           C  
ATOM    659  O   HIS A 282      19.985  44.269 109.249  1.00 22.94           O  
ATOM    660  CB  HIS A 282      18.774  41.812 109.067  1.00 20.46           C  
ATOM    661  CG  HIS A 282      18.257  40.459 108.693  1.00 20.58           C  
ATOM    662  ND1 HIS A 282      17.581  39.647 109.577  1.00 20.45           N  
ATOM    663  CD2 HIS A 282      18.317  39.776 107.525  1.00 20.86           C  
ATOM    664  CE1 HIS A 282      17.243  38.523 108.970  1.00 21.05           C  
ATOM    665  NE2 HIS A 282      17.677  38.576 107.724  1.00 20.78           N  
ATOM    666  N   ASN A 283      22.072  43.500 108.860  1.00 22.12           N  
ATOM    667  CA  ASN A 283      22.690  44.815 108.769  1.00 22.20           C  
ATOM    668  C   ASN A 283      23.473  44.896 107.455  1.00 23.08           C  
ATOM    669  O   ASN A 283      23.401  43.975 106.632  1.00 23.00           O  
ATOM    670  CB  ASN A 283      23.606  45.058 109.972  1.00 23.39           C  
ATOM    671  CG  ASN A 283      24.589  43.938 110.186  1.00 23.69           C  
ATOM    672  OD1 ASN A 283      25.384  43.623 109.304  1.00 24.81           O  
ATOM    673  ND2 ASN A 283      24.541  43.323 111.364  1.00 23.41           N  
ATOM    674  N   SER A 284      24.223  45.976 107.253  1.00 22.06           N  
ATOM    675  CA  SER A 284      24.958  46.151 106.002  1.00 22.58           C  
ATOM    676  C   SER A 284      26.029  45.102 105.734  1.00 22.72           C  
ATOM    677  O   SER A 284      26.443  44.934 104.596  1.00 23.77           O  
ATOM    678  CB  SER A 284      25.596  47.547 105.924  1.00 22.66           C  
ATOM    679  OG  SER A 284      26.732  47.648 106.761  1.00 22.83           O  
ATOM    680  N   LEU A 285      26.486  44.402 106.766  1.00 23.05           N  
ATOM    681  CA  LEU A 285      27.502  43.373 106.554  1.00 23.67           C  
ATOM    682  C   LEU A 285      26.859  42.180 105.839  1.00 22.70           C  
ATOM    683  O   LEU A 285      27.477  41.565 104.971  1.00 22.16           O  
ATOM    684  CB  LEU A 285      28.115  42.938 107.890  1.00 24.85           C  
ATOM    685  CG  LEU A 285      29.272  41.937 107.819  1.00 26.94           C  
ATOM    686  CD1 LEU A 285      30.362  42.455 106.893  1.00 27.66           C  
ATOM    687  CD2 LEU A 285      29.829  41.724 109.213  1.00 27.73           C  
ATOM    688  N   HIS A 286      25.618  41.857 106.205  1.00 21.90           N  
ATOM    689  CA  HIS A 286      24.894  40.760 105.559  1.00 21.13           C  
ATOM    690  C   HIS A 286      24.629  41.156 104.109  1.00 20.84           C  
ATOM    691  O   HIS A 286      24.716  40.329 103.204  1.00 20.97           O  
ATOM    692  CB  HIS A 286      23.558  40.490 106.276  1.00 21.12           C  
ATOM    693  CG  HIS A 286      22.593  39.646 105.491  1.00 21.06           C  
ATOM    694  ND1 HIS A 286      22.846  38.334 105.150  1.00 19.76           N  
ATOM    695  CD2 HIS A 286      21.355  39.925 105.010  1.00 20.91           C  
ATOM    696  CE1 HIS A 286      21.803  37.840 104.499  1.00 20.09           C  
ATOM    697  NE2 HIS A 286      20.883  38.785 104.402  1.00 20.46           N  
ATOM    698  N   ALA A 287      24.295  42.428 103.892  1.00 21.08           N  
ATOM    699  CA  ALA A 287      24.034  42.922 102.541  1.00 20.71           C  
ATOM    700  C   ALA A 287      25.294  42.796 101.688  1.00 20.86           C  
ATOM    701  O   ALA A 287      25.241  42.353 100.537  1.00 20.69           O  
ATOM    702  CB  ALA A 287      23.582  44.388 102.593  1.00 20.61           C  
ATOM    703  N   ALA A 288      26.429  43.196 102.255  1.00 21.01           N  
ATOM    704  CA  ALA A 288      27.700  43.120 101.543  1.00 21.26           C  
ATOM    705  C   ALA A 288      28.019  41.667 101.191  1.00 21.02           C  
ATOM    706  O   ALA A 288      28.449  41.362 100.082  1.00 21.44           O  
ATOM    707  CB  ALA A 288      28.809  43.707 102.402  1.00 21.20           C  
ATOM    708  N   ASP A 289      27.798  40.775 102.147  1.00 21.62           N  
ATOM    709  CA  ASP A 289      28.053  39.351 101.952  1.00 21.06           C  
ATOM    710  C   ASP A 289      27.172  38.770 100.838  1.00 21.01           C  
ATOM    711  O   ASP A 289      27.638  38.004  99.991  1.00 21.15           O  
ATOM    712  CB  ASP A 289      27.807  38.611 103.275  1.00 21.60           C  
ATOM    713  CG  ASP A 289      27.980  37.102 103.152  1.00 22.46           C  
ATOM    714  OD1 ASP A 289      29.034  36.659 102.653  1.00 22.97           O  
ATOM    715  OD2 ASP A 289      27.061  36.359 103.568  1.00 22.46           O  
ATOM    716  N   VAL A 290      25.895  39.132 100.826  1.00 20.32           N  
ATOM    717  CA  VAL A 290      24.996  38.618  99.798  1.00 19.83           C  
ATOM    718  C   VAL A 290      25.376  39.145  98.413  1.00 20.35           C  
ATOM    719  O   VAL A 290      25.351  38.397  97.435  1.00 20.26           O  
ATOM    720  CB  VAL A 290      23.521  38.970 100.123  1.00 19.88           C  
ATOM    721  CG1 VAL A 290      22.604  38.530  98.995  1.00 18.93           C  
ATOM    722  CG2 VAL A 290      23.110  38.265 101.415  1.00 19.78           C  
ATOM    723  N   ALA A 291      25.741  40.421  98.331  1.00 19.92           N  
ATOM    724  CA  ALA A 291      26.137  41.005  97.055  1.00 20.58           C  
ATOM    725  C   ALA A 291      27.401  40.315  96.528  1.00 21.56           C  
ATOM    726  O   ALA A 291      27.499  39.999  95.344  1.00 21.47           O  
ATOM    727  CB  ALA A 291      26.394  42.497  97.217  1.00 20.88           C  
ATOM    728  N   GLN A 292      28.365  40.088  97.416  1.00 21.48           N  
ATOM    729  CA  GLN A 292      29.614  39.439  97.026  1.00 22.27           C  
ATOM    730  C   GLN A 292      29.371  37.981  96.637  1.00 22.22           C  
ATOM    731  O   GLN A 292      29.993  37.476  95.703  1.00 22.40           O  
ATOM    732  CB  GLN A 292      30.633  39.536  98.165  1.00 22.55           C  
ATOM    733  CG  GLN A 292      32.062  39.154  97.791  1.00 24.79           C  
ATOM    734  CD  GLN A 292      32.359  37.688  98.016  1.00 24.93           C  
ATOM    735  OE1 GLN A 292      31.753  37.050  98.873  1.00 26.62           O  
ATOM    736  NE2 GLN A 292      33.310  37.149  97.258  1.00 25.12           N  
ATOM    737  N   SER A 293      28.463  37.307  97.335  1.00 21.30           N  
ATOM    738  CA  SER A 293      28.162  35.919  96.999  1.00 22.11           C  
ATOM    739  C   SER A 293      27.465  35.878  95.642  1.00 21.54           C  
ATOM    740  O   SER A 293      27.716  34.993  94.826  1.00 21.62           O  
ATOM    741  CB  SER A 293      27.275  35.287  98.072  1.00 22.70           C  
ATOM    742  OG  SER A 293      27.957  35.240  99.314  1.00 24.65           O  
ATOM    743  N   THR A 294      26.589  36.848  95.402  1.00 20.92           N  
ATOM    744  CA  THR A 294      25.885  36.934  94.130  1.00 20.85           C  
ATOM    745  C   THR A 294      26.921  37.143  93.019  1.00 21.10           C  
ATOM    746  O   THR A 294      26.827  36.549  91.948  1.00 22.18           O  
ATOM    747  CB  THR A 294      24.873  38.118  94.138  1.00 20.36           C  
ATOM    748  OG1 THR A 294      23.731  37.762  94.932  1.00 20.23           O  
ATOM    749  CG2 THR A 294      24.428  38.460  92.723  1.00 19.42           C  
ATOM    750  N   HIS A 295      27.915  37.980  93.294  1.00 22.24           N  
ATOM    751  CA  HIS A 295      28.972  38.271  92.329  1.00 23.44           C  
ATOM    752  C   HIS A 295      29.705  36.988  91.917  1.00 24.26           C  
ATOM    753  O   HIS A 295      29.965  36.757  90.731  1.00 23.25           O  
ATOM    754  CB  HIS A 295      29.958  39.278  92.940  1.00 24.66           C  
ATOM    755  CG  HIS A 295      31.246  39.409  92.187  1.00 26.54           C  
ATOM    756  ND1 HIS A 295      31.308  39.832  90.876  1.00 27.44           N  
ATOM    757  CD2 HIS A 295      32.525  39.159  92.561  1.00 27.73           C  
ATOM    758  CE1 HIS A 295      32.568  39.834  90.475  1.00 27.41           C  
ATOM    759  NE2 HIS A 295      33.326  39.429  91.478  1.00 26.78           N  
ATOM    760  N   VAL A 296      30.038  36.152  92.894  1.00 23.97           N  
ATOM    761  CA  VAL A 296      30.737  34.910  92.585  1.00 23.61           C  
ATOM    762  C   VAL A 296      29.827  33.893  91.892  1.00 23.15           C  
ATOM    763  O   VAL A 296      30.249  33.230  90.945  1.00 23.69           O  
ATOM    764  CB  VAL A 296      31.363  34.306  93.858  1.00 24.57           C  
ATOM    765  CG1 VAL A 296      31.979  32.934  93.552  1.00 24.69           C  
ATOM    766  CG2 VAL A 296      32.440  35.254  94.384  1.00 23.58           C  
ATOM    767  N   LEU A 297      28.578  33.775  92.337  1.00 22.02           N  
ATOM    768  CA  LEU A 297      27.647  32.837  91.709  1.00 21.97           C  
ATOM    769  C   LEU A 297      27.437  33.184  90.235  1.00 22.56           C  
ATOM    770  O   LEU A 297      27.330  32.298  89.382  1.00 22.74           O  
ATOM    771  CB  LEU A 297      26.296  32.845  92.438  1.00 22.24           C  
ATOM    772  CG  LEU A 297      26.282  32.188  93.826  1.00 23.49           C  
ATOM    773  CD1 LEU A 297      24.927  32.401  94.496  1.00 22.33           C  
ATOM    774  CD2 LEU A 297      26.585  30.693  93.680  1.00 22.67           C  
ATOM    775  N   LEU A 298      27.383  34.479  89.941  1.00 22.62           N  
ATOM    776  CA  LEU A 298      27.196  34.954  88.576  1.00 24.18           C  
ATOM    777  C   LEU A 298      28.389  34.594  87.699  1.00 24.80           C  
ATOM    778  O   LEU A 298      28.237  34.390  86.499  1.00 26.27           O  
ATOM    779  CB  LEU A 298      27.013  36.474  88.566  1.00 24.09           C  
ATOM    780  CG  LEU A 298      25.626  37.011  88.936  1.00 23.02           C  
ATOM    781  CD1 LEU A 298      25.707  38.505  89.201  1.00 22.60           C  
ATOM    782  CD2 LEU A 298      24.655  36.714  87.805  1.00 23.82           C  
ATOM    783  N   ALA A 299      29.569  34.527  88.306  1.00 25.36           N  
ATOM    784  CA  ALA A 299      30.793  34.208  87.578  1.00 27.17           C  
ATOM    785  C   ALA A 299      31.011  32.707  87.382  1.00 28.18           C  
ATOM    786  O   ALA A 299      32.025  32.293  86.824  1.00 28.83           O  
ATOM    787  CB  ALA A 299      31.989  34.817  88.292  1.00 26.51           C  
ATOM    788  N   THR A 300      30.056  31.898  87.828  1.00 28.97           N  
ATOM    789  CA  THR A 300      30.151  30.445  87.690  1.00 30.24           C  
ATOM    790  C   THR A 300      30.355  30.059  86.218  1.00 29.67           C  
ATOM    791  O   THR A 300      29.636  30.531  85.338  1.00 28.87           O  
ATOM    792  CB  THR A 300      28.873  29.772  88.223  1.00 31.83           C  
ATOM    793  OG1 THR A 300      28.608  30.238  89.555  1.00 35.69           O  
ATOM    794  CG2 THR A 300      29.046  28.282  88.275  1.00 33.72           C  
ATOM    795  N   PRO A 301      31.335  29.184  85.933  1.00 29.65           N  
ATOM    796  CA  PRO A 301      31.604  28.765  84.552  1.00 29.43           C  
ATOM    797  C   PRO A 301      30.375  28.381  83.747  1.00 28.92           C  
ATOM    798  O   PRO A 301      30.254  28.749  82.578  1.00 29.30           O  
ATOM    799  CB  PRO A 301      32.571  27.595  84.734  1.00 30.34           C  
ATOM    800  CG  PRO A 301      33.360  28.024  85.920  1.00 30.90           C  
ATOM    801  CD  PRO A 301      32.275  28.531  86.862  1.00 30.05           C  
ATOM    802  N   ALA A 302      29.459  27.647  84.374  1.00 28.39           N  
ATOM    803  CA  ALA A 302      28.241  27.205  83.706  1.00 28.87           C  
ATOM    804  C   ALA A 302      27.338  28.347  83.241  1.00 29.59           C  
ATOM    805  O   ALA A 302      26.484  28.152  82.378  1.00 29.60           O  
ATOM    806  CB  ALA A 302      27.455  26.276  84.625  1.00 29.85           C  
ATOM    807  N   LEU A 303      27.521  29.536  83.807  1.00 29.51           N  
ATOM    808  CA  LEU A 303      26.687  30.674  83.433  1.00 30.81           C  
ATOM    809  C   LEU A 303      27.404  31.701  82.559  1.00 31.65           C  
ATOM    810  O   LEU A 303      26.900  32.803  82.344  1.00 30.96           O  
ATOM    811  CB  LEU A 303      26.150  31.357  84.695  1.00 29.40           C  
ATOM    812  CG  LEU A 303      25.327  30.460  85.626  1.00 29.79           C  
ATOM    813  CD1 LEU A 303      24.904  31.235  86.876  1.00 28.89           C  
ATOM    814  CD2 LEU A 303      24.106  29.948  84.874  1.00 29.56           C  
ATOM    815  N   GLU A 304      28.570  31.331  82.043  1.00 33.05           N  
ATOM    816  CA  GLU A 304      29.357  32.229  81.204  1.00 35.14           C  
ATOM    817  C   GLU A 304      28.573  32.777  80.010  1.00 35.03           C  
ATOM    818  O   GLU A 304      27.949  32.025  79.263  1.00 35.18           O  
ATOM    819  CB  GLU A 304      30.618  31.510  80.715  1.00 37.37           C  
ATOM    820  CG  GLU A 304      31.477  32.320  79.760  1.00 41.70           C  
ATOM    821  CD  GLU A 304      32.773  31.608  79.405  1.00 44.30           C  
ATOM    822  OE1 GLU A 304      33.614  31.414  80.311  1.00 44.89           O  
ATOM    823  OE2 GLU A 304      32.947  31.238  78.223  1.00 46.01           O  
ATOM    824  N   ALA A 305      28.607  34.097  79.855  1.00 35.06           N  
ATOM    825  CA  ALA A 305      27.935  34.791  78.757  1.00 35.44           C  
ATOM    826  C   ALA A 305      26.424  34.592  78.693  1.00 34.99           C  
ATOM    827  O   ALA A 305      25.799  34.898  77.677  1.00 35.84           O  
ATOM    828  CB  ALA A 305      28.568  34.383  77.422  1.00 35.91           C  
ATOM    829  N   VAL A 306      25.827  34.096  79.769  1.00 33.29           N  
ATOM    830  CA  VAL A 306      24.387  33.875  79.775  1.00 32.24           C  
ATOM    831  C   VAL A 306      23.577  35.136  80.073  1.00 31.27           C  
ATOM    832  O   VAL A 306      22.541  35.372  79.453  1.00 31.26           O  
ATOM    833  CB  VAL A 306      23.992  32.790  80.804  1.00 33.24           C  
ATOM    834  CG1 VAL A 306      22.474  32.705  80.925  1.00 33.71           C  
ATOM    835  CG2 VAL A 306      24.558  31.443  80.378  1.00 33.06           C  
ATOM    836  N   PHE A 307      24.047  35.943  81.017  1.00 29.74           N  
ATOM    837  CA  PHE A 307      23.328  37.154  81.405  1.00 29.16           C  
ATOM    838  C   PHE A 307      23.911  38.440  80.837  1.00 29.06           C  
ATOM    839  O   PHE A 307      25.120  38.556  80.637  1.00 29.72           O  
ATOM    840  CB  PHE A 307      23.284  37.254  82.929  1.00 27.92           C  
ATOM    841  CG  PHE A 307      22.608  36.092  83.589  1.00 27.41           C  
ATOM    842  CD1 PHE A 307      21.248  35.872  83.408  1.00 26.47           C  
ATOM    843  CD2 PHE A 307      23.331  35.213  84.387  1.00 26.99           C  
ATOM    844  CE1 PHE A 307      20.616  34.794  84.011  1.00 27.07           C  
ATOM    845  CE2 PHE A 307      22.707  34.129  84.997  1.00 27.28           C  
ATOM    846  CZ  PHE A 307      21.346  33.919  84.808  1.00 27.18           C  
ATOM    847  N   THR A 308      23.039  39.412  80.591  1.00 29.55           N  
ATOM    848  CA  THR A 308      23.463  40.699  80.057  1.00 28.68           C  
ATOM    849  C   THR A 308      24.023  41.526  81.198  1.00 29.11           C  
ATOM    850  O   THR A 308      23.824  41.198  82.376  1.00 28.56           O  
ATOM    851  CB  THR A 308      22.281  41.474  79.447  1.00 29.05           C  
ATOM    852  OG1 THR A 308      21.354  41.822  80.485  1.00 28.06           O  
ATOM    853  CG2 THR A 308      21.569  40.624  78.397  1.00 28.26           C  
ATOM    854  N   ASP A 309      24.714  42.607  80.855  1.00 28.77           N  
ATOM    855  CA  ASP A 309      25.289  43.478  81.869  1.00 29.28           C  
ATOM    856  C   ASP A 309      24.180  44.099  82.720  1.00 27.36           C  
ATOM    857  O   ASP A 309      24.377  44.363  83.902  1.00 25.96           O  
ATOM    858  CB  ASP A 309      26.122  44.590  81.218  1.00 31.21           C  
ATOM    859  CG  ASP A 309      27.279  44.049  80.390  1.00 34.82           C  
ATOM    860  OD1 ASP A 309      28.009  43.169  80.899  1.00 35.29           O  
ATOM    861  OD2 ASP A 309      27.463  44.513  79.238  1.00 36.01           O  
ATOM    862  N   LEU A 310      23.017  44.326  82.115  1.00 26.76           N  
ATOM    863  CA  LEU A 310      21.897  44.924  82.843  1.00 26.07           C  
ATOM    864  C   LEU A 310      21.353  43.947  83.884  1.00 25.85           C  
ATOM    865  O   LEU A 310      21.043  44.335  85.009  1.00 25.40           O  
ATOM    866  CB  LEU A 310      20.771  45.325  81.880  1.00 24.95           C  
ATOM    867  CG  LEU A 310      19.663  46.185  82.514  1.00 24.16           C  
ATOM    868  CD1 LEU A 310      20.246  47.537  82.931  1.00 23.24           C  
ATOM    869  CD2 LEU A 310      18.523  46.386  81.530  1.00 23.99           C  
ATOM    870  N   GLU A 311      21.237  42.679  83.503  1.00 26.20           N  
ATOM    871  CA  GLU A 311      20.733  41.661  84.420  1.00 25.46           C  
ATOM    872  C   GLU A 311      21.719  41.483  85.570  1.00 24.95           C  
ATOM    873  O   GLU A 311      21.322  41.257  86.713  1.00 24.03           O  
ATOM    874  CB  GLU A 311      20.514  40.340  83.670  1.00 25.70           C  
ATOM    875  CG  GLU A 311      19.487  40.467  82.551  1.00 26.75           C  
ATOM    876  CD  GLU A 311      19.397  39.242  81.659  1.00 27.57           C  
ATOM    877  OE1 GLU A 311      20.440  38.597  81.408  1.00 26.87           O  
ATOM    878  OE2 GLU A 311      18.284  38.939  81.188  1.00 26.99           O  
ATOM    879  N   ILE A 312      23.007  41.605  85.263  1.00 24.27           N  
ATOM    880  CA  ILE A 312      24.053  41.479  86.272  1.00 24.12           C  
ATOM    881  C   ILE A 312      23.981  42.673  87.218  1.00 23.73           C  
ATOM    882  O   ILE A 312      24.059  42.519  88.436  1.00 22.84           O  
ATOM    883  CB  ILE A 312      25.458  41.427  85.615  1.00 24.44           C  
ATOM    884  CG1 ILE A 312      25.671  40.054  84.967  1.00 26.03           C  
ATOM    885  CG2 ILE A 312      26.544  41.732  86.648  1.00 24.23           C  
ATOM    886  CD1 ILE A 312      26.910  39.974  84.079  1.00 27.14           C  
ATOM    887  N   LEU A 313      23.825  43.865  86.652  1.00 23.21           N  
ATOM    888  CA  LEU A 313      23.731  45.071  87.466  1.00 23.37           C  
ATOM    889  C   LEU A 313      22.516  44.968  88.386  1.00 22.41           C  
ATOM    890  O   LEU A 313      22.590  45.317  89.561  1.00 22.71           O  
ATOM    891  CB  LEU A 313      23.599  46.311  86.572  1.00 24.13           C  
ATOM    892  CG  LEU A 313      23.366  47.664  87.258  1.00 25.24           C  
ATOM    893  CD1 LEU A 313      24.557  48.015  88.147  1.00 25.55           C  
ATOM    894  CD2 LEU A 313      23.167  48.748  86.187  1.00 24.94           C  
ATOM    895  N   ALA A 314      21.404  44.480  87.846  1.00 21.40           N  
ATOM    896  CA  ALA A 314      20.177  44.343  88.633  1.00 20.91           C  
ATOM    897  C   ALA A 314      20.345  43.364  89.796  1.00 21.12           C  
ATOM    898  O   ALA A 314      19.900  43.631  90.914  1.00 19.77           O  
ATOM    899  CB  ALA A 314      19.038  43.893  87.740  1.00 19.95           C  
ATOM    900  N   ALA A 315      20.981  42.226  89.530  1.00 20.60           N  
ATOM    901  CA  ALA A 315      21.192  41.218  90.571  1.00 20.52           C  
ATOM    902  C   ALA A 315      22.069  41.737  91.709  1.00 20.31           C  
ATOM    903  O   ALA A 315      21.817  41.453  92.879  1.00 19.77           O  
ATOM    904  CB  ALA A 315      21.809  39.950  89.958  1.00 20.59           C  
ATOM    905  N   LEU A 316      23.099  42.502  91.370  1.00 20.20           N  
ATOM    906  CA  LEU A 316      23.996  43.047  92.383  1.00 20.09           C  
ATOM    907  C   LEU A 316      23.313  44.167  93.171  1.00 21.04           C  
ATOM    908  O   LEU A 316      23.483  44.274  94.387  1.00 19.99           O  
ATOM    909  CB  LEU A 316      25.274  43.561  91.724  1.00 20.09           C  
ATOM    910  CG  LEU A 316      26.129  42.456  91.090  1.00 20.78           C  
ATOM    911  CD1 LEU A 316      27.156  43.063  90.146  1.00 20.54           C  
ATOM    912  CD2 LEU A 316      26.803  41.637  92.188  1.00 20.92           C  
ATOM    913  N   PHE A 317      22.535  44.996  92.481  1.00 20.53           N  
ATOM    914  CA  PHE A 317      21.831  46.084  93.159  1.00 20.65           C  
ATOM    915  C   PHE A 317      20.785  45.479  94.089  1.00 19.99           C  
ATOM    916  O   PHE A 317      20.648  45.892  95.238  1.00 20.51           O  
ATOM    917  CB  PHE A 317      21.140  47.003  92.146  1.00 20.37           C  
ATOM    918  CG  PHE A 317      20.402  48.155  92.781  1.00 20.84           C  
ATOM    919  CD1 PHE A 317      21.098  49.221  93.348  1.00 21.53           C  
ATOM    920  CD2 PHE A 317      19.012  48.165  92.824  1.00 21.01           C  
ATOM    921  CE1 PHE A 317      20.418  50.282  93.949  1.00 20.41           C  
ATOM    922  CE2 PHE A 317      18.322  49.222  93.426  1.00 21.81           C  
ATOM    923  CZ  PHE A 317      19.029  50.281  93.988  1.00 20.69           C  
ATOM    924  N   ALA A 318      20.044  44.496  93.585  1.00 20.66           N  
ATOM    925  CA  ALA A 318      19.030  43.837  94.395  1.00 20.69           C  
ATOM    926  C   ALA A 318      19.681  43.271  95.658  1.00 21.25           C  
ATOM    927  O   ALA A 318      19.155  43.432  96.756  1.00 20.61           O  
ATOM    928  CB  ALA A 318      18.358  42.712  93.600  1.00 21.54           C  
ATOM    929  N   SER A 319      20.822  42.607  95.496  1.00 21.17           N  
ATOM    930  CA  SER A 319      21.525  42.026  96.641  1.00 21.40           C  
ATOM    931  C   SER A 319      21.930  43.103  97.644  1.00 21.09           C  
ATOM    932  O   SER A 319      21.831  42.908  98.852  1.00 21.89           O  
ATOM    933  CB  SER A 319      22.775  41.271  96.176  1.00 21.21           C  
ATOM    934  OG  SER A 319      22.436  40.174  95.346  1.00 21.37           O  
ATOM    935  N   ALA A 320      22.377  44.247  97.142  1.00 21.06           N  
ATOM    936  CA  ALA A 320      22.805  45.329  98.021  1.00 21.32           C  
ATOM    937  C   ALA A 320      21.681  45.930  98.873  1.00 21.40           C  
ATOM    938  O   ALA A 320      21.885  46.238 100.050  1.00 21.44           O  
ATOM    939  CB  ALA A 320      23.480  46.424  97.199  1.00 21.73           C  
ATOM    940  N   ILE A 321      20.495  46.078  98.293  1.00 20.62           N  
ATOM    941  CA  ILE A 321      19.371  46.672  99.017  1.00 21.34           C  
ATOM    942  C   ILE A 321      18.365  45.662  99.563  1.00 21.81           C  
ATOM    943  O   ILE A 321      17.414  46.053 100.238  1.00 21.88           O  
ATOM    944  CB  ILE A 321      18.557  47.628  98.098  1.00 22.42           C  
ATOM    945  CG1 ILE A 321      17.775  46.802  97.063  1.00 22.57           C  
ATOM    946  CG2 ILE A 321      19.490  48.599  97.374  1.00 20.61           C  
ATOM    947  CD1 ILE A 321      16.667  47.563  96.342  1.00 21.77           C  
ATOM    948  N   HIS A 322      18.572  44.373  99.295  1.00 20.90           N  
ATOM    949  CA  HIS A 322      17.588  43.368  99.687  1.00 20.27           C  
ATOM    950  C   HIS A 322      17.085  43.309 101.128  1.00 20.55           C  
ATOM    951  O   HIS A 322      15.992  42.787 101.357  1.00 20.84           O  
ATOM    952  CB  HIS A 322      18.030  41.967  99.230  1.00 20.25           C  
ATOM    953  CG  HIS A 322      18.737  41.177 100.285  1.00 20.18           C  
ATOM    954  ND1 HIS A 322      20.065  41.373 100.595  1.00 19.03           N  
ATOM    955  CD2 HIS A 322      18.291  40.211 101.124  1.00 19.79           C  
ATOM    956  CE1 HIS A 322      20.407  40.562 101.581  1.00 19.96           C  
ATOM    957  NE2 HIS A 322      19.348  39.846 101.922  1.00 20.19           N  
ATOM    958  N   ASP A 323      17.851  43.823 102.093  1.00 20.26           N  
ATOM    959  CA  ASP A 323      17.414  43.825 103.497  1.00 20.82           C  
ATOM    960  C   ASP A 323      17.494  45.218 104.138  1.00 20.99           C  
ATOM    961  O   ASP A 323      17.444  45.335 105.357  1.00 21.75           O  
ATOM    962  CB  ASP A 323      18.263  42.856 104.357  1.00 20.27           C  
ATOM    963  CG  ASP A 323      17.766  41.418 104.310  1.00 20.79           C  
ATOM    964  OD1 ASP A 323      16.544  41.224 104.150  1.00 21.49           O  
ATOM    965  OD2 ASP A 323      18.591  40.479 104.457  1.00 20.88           O  
ATOM    966  N   VAL A 324      17.607  46.271 103.332  1.00 21.66           N  
ATOM    967  CA  VAL A 324      17.728  47.614 103.894  1.00 21.32           C  
ATOM    968  C   VAL A 324      16.568  48.015 104.817  1.00 22.29           C  
ATOM    969  O   VAL A 324      15.399  47.740 104.536  1.00 21.84           O  
ATOM    970  CB  VAL A 324      17.918  48.676 102.771  1.00 21.62           C  
ATOM    971  CG1 VAL A 324      16.638  48.822 101.951  1.00 20.49           C  
ATOM    972  CG2 VAL A 324      18.363  50.006 103.381  1.00 21.35           C  
ATOM    973  N   ASP A 325      16.927  48.640 105.936  1.00 22.75           N  
ATOM    974  CA  ASP A 325      15.984  49.087 106.960  1.00 24.32           C  
ATOM    975  C   ASP A 325      15.257  47.933 107.648  1.00 23.83           C  
ATOM    976  O   ASP A 325      14.131  48.091 108.116  1.00 24.42           O  
ATOM    977  CB  ASP A 325      14.972  50.079 106.366  1.00 25.49           C  
ATOM    978  CG  ASP A 325      14.229  50.871 107.438  1.00 28.20           C  
ATOM    979  OD1 ASP A 325      14.875  51.295 108.423  1.00 27.41           O  
ATOM    980  OD2 ASP A 325      13.007  51.078 107.287  1.00 28.54           O  
ATOM    981  N   HIS A 326      15.903  46.768 107.704  1.00 23.28           N  
ATOM    982  CA  HIS A 326      15.320  45.600 108.369  1.00 22.82           C  
ATOM    983  C   HIS A 326      15.342  45.939 109.862  1.00 23.56           C  
ATOM    984  O   HIS A 326      16.357  46.407 110.375  1.00 24.39           O  
ATOM    985  CB  HIS A 326      16.180  44.354 108.094  1.00 21.99           C  
ATOM    986  CG  HIS A 326      15.494  43.057 108.395  1.00 21.80           C  
ATOM    987  ND1 HIS A 326      15.049  42.720 109.656  1.00 21.97           N  
ATOM    988  CD2 HIS A 326      15.190  42.005 107.596  1.00 21.24           C  
ATOM    989  CE1 HIS A 326      14.502  41.518 109.622  1.00 22.24           C  
ATOM    990  NE2 HIS A 326      14.574  41.062 108.385  1.00 21.69           N  
ATOM    991  N   PRO A 327      14.221  45.730 110.572  1.00 24.83           N  
ATOM    992  CA  PRO A 327      14.169  46.038 112.005  1.00 26.10           C  
ATOM    993  C   PRO A 327      14.587  44.887 112.915  1.00 26.88           C  
ATOM    994  O   PRO A 327      14.669  45.054 114.133  1.00 26.08           O  
ATOM    995  CB  PRO A 327      12.707  46.411 112.213  1.00 26.12           C  
ATOM    996  CG  PRO A 327      12.018  45.422 111.337  1.00 26.90           C  
ATOM    997  CD  PRO A 327      12.876  45.412 110.062  1.00 25.66           C  
ATOM    998  N   GLY A 328      14.845  43.722 112.325  1.00 27.63           N  
ATOM    999  CA  GLY A 328      15.222  42.564 113.117  1.00 28.78           C  
ATOM   1000  C   GLY A 328      14.067  41.579 113.130  1.00 30.81           C  
ATOM   1001  O   GLY A 328      12.915  41.977 113.278  1.00 29.43           O  
ATOM   1002  N   VAL A 329      14.368  40.292 112.987  1.00 32.58           N  
ATOM   1003  CA  VAL A 329      13.332  39.263 112.949  1.00 36.07           C  
ATOM   1004  C   VAL A 329      12.284  39.305 114.066  1.00 38.70           C  
ATOM   1005  O   VAL A 329      11.118  38.997 113.826  1.00 39.34           O  
ATOM   1006  CB  VAL A 329      13.970  37.852 112.893  1.00 36.65           C  
ATOM   1007  CG1 VAL A 329      12.895  36.772 112.973  1.00 36.68           C  
ATOM   1008  CG2 VAL A 329      14.744  37.705 111.594  1.00 36.53           C  
ATOM   1009  N   SER A 330      12.676  39.689 115.276  1.00 41.51           N  
ATOM   1010  CA  SER A 330      11.713  39.738 116.375  1.00 44.79           C  
ATOM   1011  C   SER A 330      10.847  40.997 116.317  1.00 47.18           C  
ATOM   1012  O   SER A 330       9.829  41.096 117.009  1.00 47.53           O  
ATOM   1013  CB  SER A 330      12.435  39.671 117.727  1.00 45.06           C  
ATOM   1014  OG  SER A 330      13.151  40.865 117.995  1.00 45.73           O  
ATOM   1015  N   ASN A 331      11.249  41.952 115.482  1.00 48.99           N  
ATOM   1016  CA  ASN A 331      10.522  43.208 115.342  1.00 51.32           C  
ATOM   1017  C   ASN A 331       9.884  43.360 113.962  1.00 52.86           C  
ATOM   1018  O   ASN A 331       9.419  44.444 113.606  1.00 52.85           O  
ATOM   1019  CB  ASN A 331      11.471  44.383 115.590  1.00 51.46           C  
ATOM   1020  CG  ASN A 331      12.255  44.237 116.880  1.00 52.28           C  
ATOM   1021  OD1 ASN A 331      11.683  44.213 117.971  1.00 52.68           O  
ATOM   1022  ND2 ASN A 331      13.575  44.132 116.760  1.00 52.31           N  
ATOM   1023  N   GLN A 332       9.858  42.277 113.191  1.00 54.48           N  
ATOM   1024  CA  GLN A 332       9.286  42.318 111.847  1.00 56.34           C  
ATOM   1025  C   GLN A 332       7.775  42.088 111.844  1.00 57.09           C  
ATOM   1026  O   GLN A 332       7.054  42.958 111.309  1.00 58.13           O  
ATOM   1027  CB  GLN A 332       9.977  41.284 110.946  1.00 56.50           C  
ATOM   1028  CG  GLN A 332       9.728  39.834 111.338  1.00 57.43           C  
ATOM   1029  CD  GLN A 332      10.506  38.848 110.481  1.00 57.84           C  
ATOM   1030  OE1 GLN A 332      10.313  37.633 110.581  1.00 57.81           O  
ATOM   1031  NE2 GLN A 332      11.397  39.365 109.640  1.00 57.33           N  
ATOM   1032  N   ASN A 346      -0.569  43.529 104.952  1.00 66.80           N  
ATOM   1033  CA  ASN A 346      -0.942  42.353 104.111  1.00 66.52           C  
ATOM   1034  C   ASN A 346      -0.024  41.169 104.402  1.00 65.70           C  
ATOM   1035  O   ASN A 346       0.742  41.184 105.368  1.00 65.91           O  
ATOM   1036  CB  ASN A 346      -0.840  42.712 102.626  1.00 67.53           C  
ATOM   1037  CG  ASN A 346      -1.619  43.962 102.271  1.00 68.52           C  
ATOM   1038  OD1 ASN A 346      -2.845  44.008 102.402  1.00 68.99           O  
ATOM   1039  ND2 ASN A 346      -0.908  44.989 101.817  1.00 68.93           N  
ATOM   1040  N   ASP A 347      -0.110  40.145 103.558  1.00 64.42           N  
ATOM   1041  CA  ASP A 347       0.713  38.949 103.700  1.00 62.62           C  
ATOM   1042  C   ASP A 347       1.467  38.698 102.396  1.00 60.55           C  
ATOM   1043  O   ASP A 347       1.896  37.576 102.116  1.00 61.01           O  
ATOM   1044  CB  ASP A 347      -0.161  37.735 104.035  1.00 63.88           C  
ATOM   1045  CG  ASP A 347      -0.952  37.920 105.319  1.00 64.71           C  
ATOM   1046  OD1 ASP A 347      -0.328  38.174 106.372  1.00 65.07           O  
ATOM   1047  OD2 ASP A 347      -2.198  37.810 105.275  1.00 65.17           O  
ATOM   1048  N   ALA A 348       1.622  39.755 101.602  1.00 57.49           N  
ATOM   1049  CA  ALA A 348       2.316  39.665 100.322  1.00 53.77           C  
ATOM   1050  C   ALA A 348       3.685  40.341 100.363  1.00 50.65           C  
ATOM   1051  O   ALA A 348       3.848  41.461  99.877  1.00 50.17           O  
ATOM   1052  CB  ALA A 348       1.459  40.289  99.224  1.00 54.53           C  
ATOM   1053  N   SER A 349       4.661  39.651 100.949  1.00 46.89           N  
ATOM   1054  CA  SER A 349       6.030  40.158 101.055  1.00 42.71           C  
ATOM   1055  C   SER A 349       6.073  41.628 101.455  1.00 40.19           C  
ATOM   1056  O   SER A 349       6.780  42.430 100.843  1.00 39.14           O  
ATOM   1057  CB  SER A 349       6.760  39.972  99.724  1.00 42.35           C  
ATOM   1058  OG  SER A 349       6.808  38.605  99.348  1.00 42.53           O  
ATOM   1059  N   VAL A 350       5.321  41.979 102.489  1.00 37.37           N  
ATOM   1060  CA  VAL A 350       5.282  43.358 102.946  1.00 34.45           C  
ATOM   1061  C   VAL A 350       6.670  43.863 103.316  1.00 31.95           C  
ATOM   1062  O   VAL A 350       7.037  44.985 102.976  1.00 30.54           O  
ATOM   1063  CB  VAL A 350       4.344  43.515 104.163  1.00 35.43           C  
ATOM   1064  CG1 VAL A 350       4.309  44.970 104.611  1.00 35.51           C  
ATOM   1065  CG2 VAL A 350       2.945  43.053 103.795  1.00 35.90           C  
ATOM   1066  N   LEU A 351       7.450  43.036 104.003  1.00 29.60           N  
ATOM   1067  CA  LEU A 351       8.786  43.456 104.403  1.00 27.75           C  
ATOM   1068  C   LEU A 351       9.716  43.629 103.207  1.00 25.55           C  
ATOM   1069  O   LEU A 351      10.390  44.651 103.089  1.00 25.24           O  
ATOM   1070  CB  LEU A 351       9.390  42.460 105.402  1.00 28.85           C  
ATOM   1071  CG  LEU A 351      10.756  42.852 105.981  1.00 29.44           C  
ATOM   1072  CD1 LEU A 351      10.716  44.281 106.514  1.00 31.22           C  
ATOM   1073  CD2 LEU A 351      11.133  41.879 107.092  1.00 31.55           C  
ATOM   1074  N   GLU A 352       9.759  42.637 102.320  1.00 24.34           N  
ATOM   1075  CA  GLU A 352      10.628  42.737 101.150  1.00 23.04           C  
ATOM   1076  C   GLU A 352      10.224  43.923 100.262  1.00 23.36           C  
ATOM   1077  O   GLU A 352      11.072  44.558  99.637  1.00 22.47           O  
ATOM   1078  CB  GLU A 352      10.606  41.432 100.350  1.00 22.68           C  
ATOM   1079  CG  GLU A 352      11.343  40.251 101.023  1.00 23.12           C  
ATOM   1080  CD  GLU A 352      10.685  39.753 102.297  1.00 23.99           C  
ATOM   1081  OE1 GLU A 352       9.440  39.774 102.387  1.00 24.19           O  
ATOM   1082  OE2 GLU A 352      11.416  39.311 103.211  1.00 25.09           O  
ATOM   1083  N   ASN A 353       8.930  44.226 100.206  1.00 23.72           N  
ATOM   1084  CA  ASN A 353       8.487  45.365  99.410  1.00 24.91           C  
ATOM   1085  C   ASN A 353       8.954  46.651 100.074  1.00 24.35           C  
ATOM   1086  O   ASN A 353       9.183  47.655  99.403  1.00 24.92           O  
ATOM   1087  CB  ASN A 353       6.965  45.364  99.239  1.00 25.80           C  
ATOM   1088  CG  ASN A 353       6.530  44.616  97.992  1.00 27.11           C  
ATOM   1089  OD1 ASN A 353       7.047  44.863  96.903  1.00 27.20           O  
ATOM   1090  ND2 ASN A 353       5.578  43.705  98.142  1.00 27.57           N  
ATOM   1091  N   HIS A 354       9.108  46.618 101.394  1.00 23.25           N  
ATOM   1092  CA  HIS A 354       9.594  47.786 102.116  1.00 22.73           C  
ATOM   1093  C   HIS A 354      11.081  47.965 101.800  1.00 22.80           C  
ATOM   1094  O   HIS A 354      11.558  49.089 101.631  1.00 21.47           O  
ATOM   1095  CB  HIS A 354       9.405  47.610 103.626  1.00 23.84           C  
ATOM   1096  CG  HIS A 354       9.945  48.748 104.436  1.00 26.05           C  
ATOM   1097  ND1 HIS A 354       9.380  50.007 104.423  1.00 26.01           N  
ATOM   1098  CD2 HIS A 354      11.020  48.827 105.255  1.00 25.01           C  
ATOM   1099  CE1 HIS A 354      10.086  50.811 105.199  1.00 26.94           C  
ATOM   1100  NE2 HIS A 354      11.087  50.119 105.715  1.00 25.67           N  
ATOM   1101  N   HIS A 355      11.820  46.858 101.723  1.00 22.03           N  
ATOM   1102  CA  HIS A 355      13.245  46.941 101.398  1.00 21.81           C  
ATOM   1103  C   HIS A 355      13.394  47.613 100.036  1.00 21.07           C  
ATOM   1104  O   HIS A 355      14.249  48.472  99.838  1.00 21.01           O  
ATOM   1105  CB  HIS A 355      13.883  45.543 101.343  1.00 20.86           C  
ATOM   1106  CG  HIS A 355      13.847  44.809 102.646  1.00 20.86           C  
ATOM   1107  ND1 HIS A 355      14.168  45.407 103.847  1.00 21.28           N  
ATOM   1108  CD2 HIS A 355      13.558  43.517 102.935  1.00 20.77           C  
ATOM   1109  CE1 HIS A 355      14.078  44.515 104.819  1.00 20.19           C  
ATOM   1110  NE2 HIS A 355      13.710  43.361 104.292  1.00 20.23           N  
ATOM   1111  N   LEU A 356      12.557  47.203  99.092  1.00 21.83           N  
ATOM   1112  CA  LEU A 356      12.583  47.774  97.751  1.00 22.21           C  
ATOM   1113  C   LEU A 356      12.248  49.266  97.776  1.00 22.25           C  
ATOM   1114  O   LEU A 356      12.936  50.078  97.158  1.00 22.57           O  
ATOM   1115  CB  LEU A 356      11.583  47.044  96.859  1.00 20.85           C  
ATOM   1116  CG  LEU A 356      12.046  45.658  96.403  1.00 21.79           C  
ATOM   1117  CD1 LEU A 356      10.854  44.823  95.958  1.00 21.12           C  
ATOM   1118  CD2 LEU A 356      13.076  45.826  95.289  1.00 20.66           C  
ATOM   1119  N   ALA A 357      11.185  49.620  98.489  1.00 23.29           N  
ATOM   1120  CA  ALA A 357      10.771  51.014  98.574  1.00 23.36           C  
ATOM   1121  C   ALA A 357      11.922  51.878  99.074  1.00 22.71           C  
ATOM   1122  O   ALA A 357      12.221  52.922  98.491  1.00 22.92           O  
ATOM   1123  CB  ALA A 357       9.555  51.144  99.496  1.00 23.27           C  
ATOM   1124  N   VAL A 358      12.584  51.439 100.141  1.00 23.20           N  
ATOM   1125  CA  VAL A 358      13.704  52.198 100.695  1.00 23.02           C  
ATOM   1126  C   VAL A 358      14.883  52.250  99.727  1.00 23.52           C  
ATOM   1127  O   VAL A 358      15.460  53.315  99.497  1.00 23.63           O  
ATOM   1128  CB  VAL A 358      14.179  51.600 102.045  1.00 22.62           C  
ATOM   1129  CG1 VAL A 358      15.411  52.344 102.550  1.00 22.54           C  
ATOM   1130  CG2 VAL A 358      13.056  51.699 103.074  1.00 23.79           C  
ATOM   1131  N   GLY A 359      15.241  51.102  99.158  1.00 23.86           N  
ATOM   1132  CA  GLY A 359      16.349  51.072  98.220  1.00 23.40           C  
ATOM   1133  C   GLY A 359      16.121  52.008  97.040  1.00 24.49           C  
ATOM   1134  O   GLY A 359      17.050  52.676  96.575  1.00 24.16           O  
ATOM   1135  N   PHE A 360      14.881  52.061  96.560  1.00 23.68           N  
ATOM   1136  CA  PHE A 360      14.532  52.915  95.425  1.00 24.46           C  
ATOM   1137  C   PHE A 360      14.440  54.391  95.779  1.00 25.46           C  
ATOM   1138  O   PHE A 360      14.880  55.242  95.009  1.00 24.92           O  
ATOM   1139  CB  PHE A 360      13.188  52.496  94.811  1.00 24.94           C  
ATOM   1140  CG  PHE A 360      13.224  51.187  94.079  1.00 25.13           C  
ATOM   1141  CD1 PHE A 360      14.392  50.739  93.469  1.00 25.48           C  
ATOM   1142  CD2 PHE A 360      12.065  50.423  93.951  1.00 25.24           C  
ATOM   1143  CE1 PHE A 360      14.406  49.545  92.737  1.00 25.07           C  
ATOM   1144  CE2 PHE A 360      12.068  49.232  93.222  1.00 24.60           C  
ATOM   1145  CZ  PHE A 360      13.239  48.792  92.615  1.00 24.48           C  
ATOM   1146  N   LYS A 361      13.862  54.699  96.936  1.00 26.18           N  
ATOM   1147  CA  LYS A 361      13.704  56.098  97.335  1.00 27.80           C  
ATOM   1148  C   LYS A 361      15.033  56.817  97.513  1.00 28.64           C  
ATOM   1149  O   LYS A 361      15.141  58.011  97.216  1.00 28.11           O  
ATOM   1150  CB  LYS A 361      12.887  56.209  98.631  1.00 28.13           C  
ATOM   1151  CG  LYS A 361      13.699  56.126  99.910  1.00 31.33           C  
ATOM   1152  CD  LYS A 361      12.834  56.401 101.133  1.00 32.83           C  
ATOM   1153  CE  LYS A 361      13.657  56.377 102.415  1.00 33.64           C  
ATOM   1154  NZ  LYS A 361      12.799  56.543 103.621  1.00 34.43           N  
ATOM   1155  N   LEU A 362      16.046  56.095  97.987  1.00 28.26           N  
ATOM   1156  CA  LEU A 362      17.351  56.700  98.213  1.00 28.70           C  
ATOM   1157  C   LEU A 362      18.006  57.162  96.921  1.00 28.54           C  
ATOM   1158  O   LEU A 362      18.872  58.034  96.941  1.00 28.45           O  
ATOM   1159  CB  LEU A 362      18.270  55.724  98.962  1.00 29.21           C  
ATOM   1160  CG  LEU A 362      17.780  55.336 100.364  1.00 30.12           C  
ATOM   1161  CD1 LEU A 362      18.812  54.430 101.040  1.00 30.98           C  
ATOM   1162  CD2 LEU A 362      17.557  56.592 101.202  1.00 30.23           C  
ATOM   1163  N   LEU A 363      17.593  56.576  95.801  1.00 28.36           N  
ATOM   1164  CA  LEU A 363      18.130  56.950  94.495  1.00 29.21           C  
ATOM   1165  C   LEU A 363      17.705  58.369  94.131  1.00 30.56           C  
ATOM   1166  O   LEU A 363      18.312  59.002  93.269  1.00 30.70           O  
ATOM   1167  CB  LEU A 363      17.616  56.001  93.415  1.00 27.78           C  
ATOM   1168  CG  LEU A 363      18.137  54.563  93.425  1.00 28.17           C  
ATOM   1169  CD1 LEU A 363      17.270  53.703  92.504  1.00 27.34           C  
ATOM   1170  CD2 LEU A 363      19.593  54.545  92.987  1.00 26.57           C  
ATOM   1171  N   GLN A 364      16.656  58.854  94.787  1.00 31.30           N  
ATOM   1172  CA  GLN A 364      16.127  60.190  94.525  1.00 33.79           C  
ATOM   1173  C   GLN A 364      16.833  61.306  95.290  1.00 34.92           C  
ATOM   1174  O   GLN A 364      16.578  62.485  95.041  1.00 35.53           O  
ATOM   1175  CB  GLN A 364      14.629  60.232  94.841  1.00 33.53           C  
ATOM   1176  CG  GLN A 364      13.788  59.299  93.984  1.00 35.21           C  
ATOM   1177  CD  GLN A 364      14.021  59.521  92.503  1.00 37.06           C  
ATOM   1178  OE1 GLN A 364      13.957  60.647  92.021  1.00 37.47           O  
ATOM   1179  NE2 GLN A 364      14.298  58.443  91.773  1.00 39.32           N  
ATOM   1180  N   ALA A 365      17.711  60.942  96.220  1.00 35.51           N  
ATOM   1181  CA  ALA A 365      18.434  61.943  96.996  1.00 36.44           C  
ATOM   1182  C   ALA A 365      19.426  62.671  96.095  1.00 36.99           C  
ATOM   1183  O   ALA A 365      19.756  62.195  95.009  1.00 36.49           O  
ATOM   1184  CB  ALA A 365      19.163  61.287  98.160  1.00 36.19           C  
ATOM   1185  N   GLU A 366      19.904  63.825  96.546  1.00 38.00           N  
ATOM   1186  CA  GLU A 366      20.843  64.607  95.749  1.00 38.78           C  
ATOM   1187  C   GLU A 366      22.109  63.834  95.398  1.00 37.02           C  
ATOM   1188  O   GLU A 366      22.801  63.314  96.272  1.00 37.14           O  
ATOM   1189  CB  GLU A 366      21.206  65.903  96.481  1.00 41.46           C  
ATOM   1190  CG  GLU A 366      22.120  66.817  95.684  1.00 45.73           C  
ATOM   1191  CD  GLU A 366      22.202  68.207  96.280  1.00 48.49           C  
ATOM   1192  OE1 GLU A 366      21.161  68.900  96.307  1.00 50.69           O  
ATOM   1193  OE2 GLU A 366      23.299  68.605  96.724  1.00 50.27           O  
ATOM   1194  N   ASN A 367      22.390  63.766  94.100  1.00 36.19           N  
ATOM   1195  CA  ASN A 367      23.557  63.073  93.566  1.00 34.91           C  
ATOM   1196  C   ASN A 367      23.630  61.613  94.009  1.00 33.93           C  
ATOM   1197  O   ASN A 367      24.704  61.103  94.338  1.00 33.52           O  
ATOM   1198  CB  ASN A 367      24.841  63.818  93.959  1.00 35.60           C  
ATOM   1199  CG  ASN A 367      26.075  63.259  93.271  1.00 35.27           C  
ATOM   1200  OD1 ASN A 367      26.032  62.883  92.099  1.00 35.25           O  
ATOM   1201  ND2 ASN A 367      27.187  63.215  93.996  1.00 35.90           N  
ATOM   1202  N   CYS A 368      22.481  60.941  94.001  1.00 32.78           N  
ATOM   1203  CA  CYS A 368      22.409  59.536  94.391  1.00 31.80           C  
ATOM   1204  C   CYS A 368      21.868  58.617  93.299  1.00 31.39           C  
ATOM   1205  O   CYS A 368      21.870  57.397  93.466  1.00 30.20           O  
ATOM   1206  CB  CYS A 368      21.544  59.370  95.641  1.00 31.75           C  
ATOM   1207  SG  CYS A 368      22.336  59.865  97.178  1.00 33.42           S  
ATOM   1208  N   ASP A 369      21.410  59.181  92.183  1.00 30.22           N  
ATOM   1209  CA  ASP A 369      20.863  58.337  91.123  1.00 29.98           C  
ATOM   1210  C   ASP A 369      21.941  57.684  90.264  1.00 29.43           C  
ATOM   1211  O   ASP A 369      22.353  58.218  89.232  1.00 28.44           O  
ATOM   1212  CB  ASP A 369      19.892  59.125  90.239  1.00 30.43           C  
ATOM   1213  CG  ASP A 369      19.180  58.237  89.231  1.00 31.94           C  
ATOM   1214  OD1 ASP A 369      19.208  56.996  89.402  1.00 30.35           O  
ATOM   1215  OD2 ASP A 369      18.587  58.772  88.274  1.00 32.74           O  
ATOM   1216  N   ILE A 370      22.383  56.507  90.697  1.00 28.85           N  
ATOM   1217  CA  ILE A 370      23.420  55.775  89.986  1.00 28.64           C  
ATOM   1218  C   ILE A 370      22.945  55.269  88.628  1.00 28.91           C  
ATOM   1219  O   ILE A 370      23.756  54.861  87.801  1.00 29.68           O  
ATOM   1220  CB  ILE A 370      23.928  54.576  90.829  1.00 28.20           C  
ATOM   1221  CG1 ILE A 370      22.776  53.609  91.118  1.00 28.46           C  
ATOM   1222  CG2 ILE A 370      24.515  55.080  92.141  1.00 28.23           C  
ATOM   1223  CD1 ILE A 370      23.217  52.323  91.816  1.00 28.38           C  
ATOM   1224  N   PHE A 371      21.635  55.296  88.396  1.00 27.94           N  
ATOM   1225  CA  PHE A 371      21.087  54.832  87.124  1.00 28.48           C  
ATOM   1226  C   PHE A 371      20.740  55.980  86.173  1.00 28.69           C  
ATOM   1227  O   PHE A 371      20.075  55.768  85.161  1.00 28.23           O  
ATOM   1228  CB  PHE A 371      19.825  53.988  87.357  1.00 28.02           C  
ATOM   1229  CG  PHE A 371      20.040  52.806  88.262  1.00 27.51           C  
ATOM   1230  CD1 PHE A 371      21.121  51.948  88.066  1.00 26.71           C  
ATOM   1231  CD2 PHE A 371      19.154  52.543  89.300  1.00 27.13           C  
ATOM   1232  CE1 PHE A 371      21.314  50.845  88.894  1.00 26.69           C  
ATOM   1233  CE2 PHE A 371      19.340  51.441  90.135  1.00 27.26           C  
ATOM   1234  CZ  PHE A 371      20.423  50.592  89.930  1.00 26.09           C  
ATOM   1235  N   GLN A 372      21.194  57.186  86.502  1.00 30.05           N  
ATOM   1236  CA  GLN A 372      20.913  58.370  85.693  1.00 31.43           C  
ATOM   1237  C   GLN A 372      21.250  58.222  84.219  1.00 31.80           C  
ATOM   1238  O   GLN A 372      20.602  58.830  83.371  1.00 32.53           O  
ATOM   1239  CB  GLN A 372      21.657  59.585  86.254  1.00 32.99           C  
ATOM   1240  CG  GLN A 372      23.149  59.366  86.429  1.00 34.71           C  
ATOM   1241  CD  GLN A 372      23.855  60.579  86.999  1.00 36.59           C  
ATOM   1242  OE1 GLN A 372      24.295  61.463  86.260  1.00 38.14           O  
ATOM   1243  NE2 GLN A 372      23.955  60.636  88.324  1.00 35.90           N  
ATOM   1244  N   ASN A 373      22.257  57.418  83.901  1.00 31.55           N  
ATOM   1245  CA  ASN A 373      22.625  57.252  82.506  1.00 31.69           C  
ATOM   1246  C   ASN A 373      22.041  56.024  81.823  1.00 30.96           C  
ATOM   1247  O   ASN A 373      22.487  55.625  80.746  1.00 30.52           O  
ATOM   1248  CB  ASN A 373      24.146  57.305  82.354  1.00 32.34           C  
ATOM   1249  CG  ASN A 373      24.690  58.703  82.579  1.00 33.86           C  
ATOM   1250  OD1 ASN A 373      24.120  59.682  82.087  1.00 34.31           O  
ATOM   1251  ND2 ASN A 373      25.789  58.809  83.314  1.00 34.00           N  
ATOM   1252  N   LEU A 374      21.033  55.427  82.450  1.00 29.94           N  
ATOM   1253  CA  LEU A 374      20.352  54.284  81.857  1.00 29.18           C  
ATOM   1254  C   LEU A 374      19.154  54.847  81.099  1.00 28.95           C  
ATOM   1255  O   LEU A 374      18.581  55.860  81.503  1.00 29.64           O  
ATOM   1256  CB  LEU A 374      19.859  53.307  82.936  1.00 28.00           C  
ATOM   1257  CG  LEU A 374      20.764  52.127  83.317  1.00 27.90           C  
ATOM   1258  CD1 LEU A 374      22.072  52.628  83.903  1.00 27.85           C  
ATOM   1259  CD2 LEU A 374      20.032  51.233  84.319  1.00 26.75           C  
ATOM   1260  N   SER A 375      18.777  54.201  80.002  1.00 29.06           N  
ATOM   1261  CA  SER A 375      17.630  54.647  79.214  1.00 28.72           C  
ATOM   1262  C   SER A 375      16.360  54.322  79.994  1.00 28.44           C  
ATOM   1263  O   SER A 375      16.406  53.557  80.960  1.00 27.14           O  
ATOM   1264  CB  SER A 375      17.598  53.915  77.876  1.00 28.61           C  
ATOM   1265  OG  SER A 375      17.356  52.537  78.085  1.00 29.67           O  
ATOM   1266  N   ALA A 376      15.231  54.893  79.580  1.00 26.98           N  
ATOM   1267  CA  ALA A 376      13.965  54.633  80.263  1.00 27.37           C  
ATOM   1268  C   ALA A 376      13.658  53.145  80.158  1.00 27.44           C  
ATOM   1269  O   ALA A 376      13.185  52.521  81.108  1.00 27.02           O  
ATOM   1270  CB  ALA A 376      12.832  55.449  79.627  1.00 25.65           C  
ATOM   1271  N   LYS A 377      13.947  52.586  78.990  1.00 27.79           N  
ATOM   1272  CA  LYS A 377      13.719  51.173  78.721  1.00 28.59           C  
ATOM   1273  C   LYS A 377      14.543  50.307  79.681  1.00 28.06           C  
ATOM   1274  O   LYS A 377      14.043  49.319  80.229  1.00 27.71           O  
ATOM   1275  CB  LYS A 377      14.100  50.878  77.267  1.00 31.07           C  
ATOM   1276  CG  LYS A 377      13.623  49.550  76.722  1.00 35.28           C  
ATOM   1277  CD  LYS A 377      13.881  49.489  75.217  1.00 37.18           C  
ATOM   1278  CE  LYS A 377      13.366  48.200  74.601  1.00 39.07           C  
ATOM   1279  NZ  LYS A 377      13.543  48.203  73.117  1.00 40.12           N  
ATOM   1280  N   GLN A 378      15.804  50.682  79.880  1.00 27.17           N  
ATOM   1281  CA  GLN A 378      16.684  49.945  80.780  1.00 27.13           C  
ATOM   1282  C   GLN A 378      16.240  50.072  82.233  1.00 26.61           C  
ATOM   1283  O   GLN A 378      16.304  49.100  82.987  1.00 25.98           O  
ATOM   1284  CB  GLN A 378      18.129  50.437  80.649  1.00 27.44           C  
ATOM   1285  CG  GLN A 378      18.780  50.113  79.314  1.00 26.74           C  
ATOM   1286  CD  GLN A 378      20.171  50.697  79.204  1.00 27.26           C  
ATOM   1287  OE1 GLN A 378      20.368  51.896  79.414  1.00 26.98           O  
ATOM   1288  NE2 GLN A 378      21.147  49.854  78.873  1.00 27.87           N  
ATOM   1289  N   ARG A 379      15.802  51.266  82.630  1.00 25.95           N  
ATOM   1290  CA  ARG A 379      15.348  51.468  84.005  1.00 25.54           C  
ATOM   1291  C   ARG A 379      14.090  50.655  84.291  1.00 26.00           C  
ATOM   1292  O   ARG A 379      13.919  50.136  85.395  1.00 26.16           O  
ATOM   1293  CB  ARG A 379      15.100  52.953  84.285  1.00 26.53           C  
ATOM   1294  CG  ARG A 379      16.365  53.795  84.218  1.00 27.18           C  
ATOM   1295  CD  ARG A 379      16.147  55.218  84.710  1.00 28.90           C  
ATOM   1296  NE  ARG A 379      15.936  55.262  86.153  1.00 29.63           N  
ATOM   1297  CZ  ARG A 379      16.588  56.075  86.975  1.00 29.90           C  
ATOM   1298  NH1 ARG A 379      17.492  56.917  86.494  1.00 29.19           N  
ATOM   1299  NH2 ARG A 379      16.357  56.027  88.284  1.00 29.69           N  
ATOM   1300  N   LEU A 380      13.205  50.543  83.303  1.00 24.73           N  
ATOM   1301  CA  LEU A 380      11.982  49.761  83.482  1.00 24.79           C  
ATOM   1302  C   LEU A 380      12.336  48.281  83.652  1.00 25.22           C  
ATOM   1303  O   LEU A 380      11.801  47.590  84.524  1.00 24.43           O  
ATOM   1304  CB  LEU A 380      11.056  49.927  82.271  1.00 24.30           C  
ATOM   1305  CG  LEU A 380      10.232  51.221  82.216  1.00 24.55           C  
ATOM   1306  CD1 LEU A 380       9.563  51.353  80.856  1.00 24.82           C  
ATOM   1307  CD2 LEU A 380       9.183  51.213  83.318  1.00 22.72           C  
ATOM   1308  N   SER A 381      13.240  47.801  82.807  1.00 24.89           N  
ATOM   1309  CA  SER A 381      13.663  46.411  82.863  1.00 25.69           C  
ATOM   1310  C   SER A 381      14.368  46.118  84.183  1.00 25.24           C  
ATOM   1311  O   SER A 381      14.000  45.182  84.897  1.00 25.70           O  
ATOM   1312  CB  SER A 381      14.598  46.096  81.694  1.00 25.92           C  
ATOM   1313  OG  SER A 381      15.000  44.740  81.732  1.00 28.57           O  
ATOM   1314  N   LEU A 382      15.373  46.922  84.511  1.00 24.67           N  
ATOM   1315  CA  LEU A 382      16.114  46.720  85.750  1.00 25.26           C  
ATOM   1316  C   LEU A 382      15.220  46.798  86.984  1.00 24.86           C  
ATOM   1317  O   LEU A 382      15.333  45.968  87.888  1.00 24.03           O  
ATOM   1318  CB  LEU A 382      17.256  47.738  85.867  1.00 25.49           C  
ATOM   1319  CG  LEU A 382      18.138  47.650  87.122  1.00 25.38           C  
ATOM   1320  CD1 LEU A 382      19.597  47.892  86.762  1.00 26.84           C  
ATOM   1321  CD2 LEU A 382      17.669  48.672  88.150  1.00 26.96           C  
ATOM   1322  N   ARG A 383      14.325  47.783  87.024  1.00 23.40           N  
ATOM   1323  CA  ARG A 383      13.444  47.930  88.182  1.00 23.35           C  
ATOM   1324  C   ARG A 383      12.628  46.660  88.386  1.00 23.28           C  
ATOM   1325  O   ARG A 383      12.499  46.158  89.506  1.00 22.91           O  
ATOM   1326  CB  ARG A 383      12.495  49.123  87.999  1.00 23.51           C  
ATOM   1327  CG  ARG A 383      11.609  49.396  89.218  1.00 24.29           C  
ATOM   1328  CD  ARG A 383      10.467  50.349  88.864  1.00 23.21           C  
ATOM   1329  NE  ARG A 383       9.670  50.731  90.025  1.00 22.65           N  
ATOM   1330  CZ  ARG A 383      10.012  51.679  90.891  1.00 22.87           C  
ATOM   1331  NH1 ARG A 383      11.146  52.352  90.736  1.00 22.93           N  
ATOM   1332  NH2 ARG A 383       9.203  51.973  91.902  1.00 24.33           N  
ATOM   1333  N   ARG A 384      12.069  46.151  87.294  1.00 22.45           N  
ATOM   1334  CA  ARG A 384      11.271  44.932  87.329  1.00 22.85           C  
ATOM   1335  C   ARG A 384      12.095  43.738  87.835  1.00 22.18           C  
ATOM   1336  O   ARG A 384      11.638  42.975  88.686  1.00 21.65           O  
ATOM   1337  CB  ARG A 384      10.715  44.663  85.922  1.00 25.04           C  
ATOM   1338  CG  ARG A 384      10.022  43.335  85.718  1.00 27.91           C  
ATOM   1339  CD  ARG A 384       9.122  43.374  84.471  1.00 30.52           C  
ATOM   1340  NE  ARG A 384       9.791  43.875  83.266  1.00 31.61           N  
ATOM   1341  CZ  ARG A 384      10.824  43.284  82.668  1.00 32.72           C  
ATOM   1342  NH1 ARG A 384      11.328  42.158  83.157  1.00 33.59           N  
ATOM   1343  NH2 ARG A 384      11.351  43.812  81.569  1.00 31.80           N  
ATOM   1344  N   MET A 385      13.312  43.584  87.322  1.00 21.92           N  
ATOM   1345  CA  MET A 385      14.173  42.475  87.735  1.00 22.49           C  
ATOM   1346  C   MET A 385      14.588  42.590  89.204  1.00 22.67           C  
ATOM   1347  O   MET A 385      14.638  41.595  89.931  1.00 22.07           O  
ATOM   1348  CB  MET A 385      15.410  42.414  86.839  1.00 22.65           C  
ATOM   1349  CG  MET A 385      15.077  42.093  85.383  1.00 23.74           C  
ATOM   1350  SD  MET A 385      16.526  41.701  84.386  1.00 25.84           S  
ATOM   1351  CE  MET A 385      17.224  43.308  84.119  1.00 23.10           C  
ATOM   1352  N   VAL A 386      14.884  43.808  89.639  1.00 22.12           N  
ATOM   1353  CA  VAL A 386      15.271  44.031  91.022  1.00 22.62           C  
ATOM   1354  C   VAL A 386      14.118  43.652  91.945  1.00 22.80           C  
ATOM   1355  O   VAL A 386      14.320  42.985  92.960  1.00 23.88           O  
ATOM   1356  CB  VAL A 386      15.671  45.501  91.254  1.00 22.20           C  
ATOM   1357  CG1 VAL A 386      15.806  45.788  92.746  1.00 21.70           C  
ATOM   1358  CG2 VAL A 386      16.990  45.773  90.553  1.00 22.17           C  
ATOM   1359  N   ILE A 387      12.907  44.070  91.593  1.00 22.19           N  
ATOM   1360  CA  ILE A 387      11.745  43.738  92.406  1.00 22.50           C  
ATOM   1361  C   ILE A 387      11.610  42.217  92.477  1.00 22.95           C  
ATOM   1362  O   ILE A 387      11.440  41.651  93.556  1.00 22.46           O  
ATOM   1363  CB  ILE A 387      10.459  44.348  91.810  1.00 23.23           C  
ATOM   1364  CG1 ILE A 387      10.478  45.868  92.006  1.00 23.15           C  
ATOM   1365  CG2 ILE A 387       9.224  43.719  92.454  1.00 23.35           C  
ATOM   1366  CD1 ILE A 387       9.375  46.608  91.249  1.00 23.93           C  
ATOM   1367  N   ASP A 388      11.695  41.557  91.327  1.00 22.22           N  
ATOM   1368  CA  ASP A 388      11.586  40.099  91.291  1.00 23.68           C  
ATOM   1369  C   ASP A 388      12.641  39.406  92.158  1.00 22.90           C  
ATOM   1370  O   ASP A 388      12.341  38.439  92.857  1.00 22.49           O  
ATOM   1371  CB  ASP A 388      11.706  39.581  89.855  1.00 24.85           C  
ATOM   1372  CG  ASP A 388      10.469  39.865  89.021  1.00 27.50           C  
ATOM   1373  OD1 ASP A 388       9.359  39.925  89.587  1.00 27.94           O  
ATOM   1374  OD2 ASP A 388      10.607  40.008  87.790  1.00 30.28           O  
ATOM   1375  N   MET A 389      13.878  39.891  92.115  1.00 22.47           N  
ATOM   1376  CA  MET A 389      14.929  39.263  92.908  1.00 22.45           C  
ATOM   1377  C   MET A 389      14.832  39.547  94.406  1.00 22.70           C  
ATOM   1378  O   MET A 389      15.090  38.661  95.221  1.00 22.73           O  
ATOM   1379  CB  MET A 389      16.304  39.647  92.359  1.00 23.09           C  
ATOM   1380  CG  MET A 389      16.632  38.894  91.063  1.00 23.11           C  
ATOM   1381  SD  MET A 389      18.241  39.293  90.358  1.00 24.54           S  
ATOM   1382  CE  MET A 389      17.799  40.652  89.272  1.00 24.04           C  
ATOM   1383  N   VAL A 390      14.454  40.764  94.787  1.00 22.34           N  
ATOM   1384  CA  VAL A 390      14.328  41.049  96.214  1.00 21.52           C  
ATOM   1385  C   VAL A 390      13.125  40.303  96.789  1.00 22.31           C  
ATOM   1386  O   VAL A 390      13.187  39.798  97.911  1.00 21.70           O  
ATOM   1387  CB  VAL A 390      14.193  42.566  96.502  1.00 21.62           C  
ATOM   1388  CG1 VAL A 390      13.904  42.787  97.989  1.00 20.12           C  
ATOM   1389  CG2 VAL A 390      15.486  43.285  96.123  1.00 21.10           C  
ATOM   1390  N   LEU A 391      12.034  40.215  96.028  1.00 21.93           N  
ATOM   1391  CA  LEU A 391      10.862  39.492  96.514  1.00 22.41           C  
ATOM   1392  C   LEU A 391      11.204  38.008  96.647  1.00 23.29           C  
ATOM   1393  O   LEU A 391      10.605  37.287  97.455  1.00 22.14           O  
ATOM   1394  CB  LEU A 391       9.664  39.658  95.566  1.00 23.31           C  
ATOM   1395  CG  LEU A 391       9.024  41.051  95.496  1.00 23.09           C  
ATOM   1396  CD1 LEU A 391       7.776  41.007  94.609  1.00 22.95           C  
ATOM   1397  CD2 LEU A 391       8.662  41.513  96.901  1.00 23.12           C  
ATOM   1398  N   ALA A 392      12.169  37.558  95.851  1.00 23.01           N  
ATOM   1399  CA  ALA A 392      12.589  36.162  95.895  1.00 23.62           C  
ATOM   1400  C   ALA A 392      13.389  35.833  97.162  1.00 23.32           C  
ATOM   1401  O   ALA A 392      13.739  34.671  97.378  1.00 24.33           O  
ATOM   1402  CB  ALA A 392      13.410  35.817  94.653  1.00 23.02           C  
ATOM   1403  N   THR A 393      13.694  36.836  97.989  1.00 22.25           N  
ATOM   1404  CA  THR A 393      14.434  36.566  99.226  1.00 22.48           C  
ATOM   1405  C   THR A 393      13.460  36.344 100.384  1.00 22.95           C  
ATOM   1406  O   THR A 393      13.866  36.079 101.513  1.00 22.27           O  
ATOM   1407  CB  THR A 393      15.446  37.700  99.609  1.00 22.48           C  
ATOM   1408  OG1 THR A 393      14.758  38.942  99.810  1.00 20.15           O  
ATOM   1409  CG2 THR A 393      16.504  37.874  98.513  1.00 21.50           C  
ATOM   1410  N   ASP A 394      12.169  36.456 100.087  1.00 22.84           N  
ATOM   1411  CA  ASP A 394      11.115  36.243 101.079  1.00 23.40           C  
ATOM   1412  C   ASP A 394      11.026  34.727 101.273  1.00 23.18           C  
ATOM   1413  O   ASP A 394      10.672  34.005 100.344  1.00 22.53           O  
ATOM   1414  CB  ASP A 394       9.785  36.790 100.542  1.00 23.78           C  
ATOM   1415  CG  ASP A 394       8.611  36.511 101.465  1.00 26.04           C  
ATOM   1416  OD1 ASP A 394       8.788  35.837 102.503  1.00 25.11           O  
ATOM   1417  OD2 ASP A 394       7.495  36.968 101.139  1.00 26.96           O  
ATOM   1418  N   MET A 395      11.347  34.255 102.475  1.00 23.82           N  
ATOM   1419  CA  MET A 395      11.332  32.825 102.763  1.00 25.61           C  
ATOM   1420  C   MET A 395       9.985  32.144 102.541  1.00 26.69           C  
ATOM   1421  O   MET A 395       9.927  30.922 102.395  1.00 26.16           O  
ATOM   1422  CB  MET A 395      11.820  32.558 104.193  1.00 26.12           C  
ATOM   1423  CG  MET A 395      13.330  32.660 104.373  1.00 27.42           C  
ATOM   1424  SD  MET A 395      14.237  31.506 103.300  1.00 27.80           S  
ATOM   1425  CE  MET A 395      13.700  29.932 103.958  1.00 28.00           C  
ATOM   1426  N   SER A 396       8.901  32.916 102.508  1.00 27.25           N  
ATOM   1427  CA  SER A 396       7.594  32.310 102.276  1.00 29.03           C  
ATOM   1428  C   SER A 396       7.489  31.867 100.811  1.00 28.95           C  
ATOM   1429  O   SER A 396       6.574  31.134 100.440  1.00 30.03           O  
ATOM   1430  CB  SER A 396       6.462  33.296 102.606  1.00 29.67           C  
ATOM   1431  OG  SER A 396       6.324  34.271 101.592  1.00 32.36           O  
ATOM   1432  N   LYS A 397       8.430  32.307  99.979  1.00 28.70           N  
ATOM   1433  CA  LYS A 397       8.424  31.935  98.563  1.00 29.44           C  
ATOM   1434  C   LYS A 397       9.443  30.823  98.289  1.00 29.20           C  
ATOM   1435  O   LYS A 397       9.555  30.335  97.164  1.00 28.66           O  
ATOM   1436  CB  LYS A 397       8.771  33.142  97.681  1.00 30.94           C  
ATOM   1437  CG  LYS A 397       7.911  34.383  97.907  1.00 34.13           C  
ATOM   1438  CD  LYS A 397       6.436  34.113  97.639  1.00 36.04           C  
ATOM   1439  CE  LYS A 397       5.595  35.367  97.883  1.00 37.90           C  
ATOM   1440  NZ  LYS A 397       5.965  36.468  96.943  1.00 39.03           N  
ATOM   1441  N   HIS A 398      10.183  30.435  99.321  1.00 28.39           N  
ATOM   1442  CA  HIS A 398      11.207  29.405  99.199  1.00 28.88           C  
ATOM   1443  C   HIS A 398      10.756  28.108  98.523  1.00 29.15           C  
ATOM   1444  O   HIS A 398      11.361  27.673  97.543  1.00 27.48           O  
ATOM   1445  CB  HIS A 398      11.785  29.077 100.578  1.00 28.40           C  
ATOM   1446  CG  HIS A 398      12.771  27.951 100.565  1.00 28.05           C  
ATOM   1447  ND1 HIS A 398      14.019  28.060  99.990  1.00 28.75           N  
ATOM   1448  CD2 HIS A 398      12.678  26.680 101.024  1.00 28.31           C  
ATOM   1449  CE1 HIS A 398      14.651  26.905 100.094  1.00 29.30           C  
ATOM   1450  NE2 HIS A 398      13.860  26.049 100.717  1.00 27.96           N  
ATOM   1451  N   MET A 399       9.706  27.484  99.046  1.00 29.92           N  
ATOM   1452  CA  MET A 399       9.237  26.228  98.470  1.00 32.51           C  
ATOM   1453  C   MET A 399       8.871  26.320  96.990  1.00 32.40           C  
ATOM   1454  O   MET A 399       9.261  25.459  96.201  1.00 32.04           O  
ATOM   1455  CB  MET A 399       8.059  25.676  99.278  1.00 34.93           C  
ATOM   1456  CG  MET A 399       8.456  25.169 100.661  1.00 39.32           C  
ATOM   1457  SD  MET A 399       9.869  24.016 100.624  1.00 44.90           S  
ATOM   1458  CE  MET A 399      10.507  24.186 102.304  1.00 43.08           C  
ATOM   1459  N   ASN A 400       8.139  27.359  96.602  1.00 32.61           N  
ATOM   1460  CA  ASN A 400       7.761  27.507  95.200  1.00 32.87           C  
ATOM   1461  C   ASN A 400       8.973  27.812  94.316  1.00 32.12           C  
ATOM   1462  O   ASN A 400       9.051  27.348  93.178  1.00 31.22           O  
ATOM   1463  CB  ASN A 400       6.699  28.605  95.038  1.00 35.62           C  
ATOM   1464  CG  ASN A 400       5.348  28.200  95.610  1.00 37.76           C  
ATOM   1465  OD1 ASN A 400       4.818  27.134  95.290  1.00 40.32           O  
ATOM   1466  ND2 ASN A 400       4.781  29.053  96.455  1.00 39.38           N  
ATOM   1467  N   LEU A 401       9.917  28.594  94.833  1.00 30.99           N  
ATOM   1468  CA  LEU A 401      11.116  28.911  94.060  1.00 30.52           C  
ATOM   1469  C   LEU A 401      11.930  27.648  93.831  1.00 29.52           C  
ATOM   1470  O   LEU A 401      12.478  27.442  92.747  1.00 28.18           O  
ATOM   1471  CB  LEU A 401      11.989  29.940  94.783  1.00 31.77           C  
ATOM   1472  CG  LEU A 401      11.570  31.404  94.649  1.00 33.84           C  
ATOM   1473  CD1 LEU A 401      12.507  32.285  95.471  1.00 34.38           C  
ATOM   1474  CD2 LEU A 401      11.606  31.809  93.173  1.00 34.24           C  
ATOM   1475  N   LEU A 402      12.015  26.809  94.858  1.00 28.28           N  
ATOM   1476  CA  LEU A 402      12.774  25.572  94.746  1.00 29.21           C  
ATOM   1477  C   LEU A 402      12.134  24.679  93.688  1.00 30.14           C  
ATOM   1478  O   LEU A 402      12.832  24.027  92.915  1.00 30.45           O  
ATOM   1479  CB  LEU A 402      12.828  24.849  96.095  1.00 27.97           C  
ATOM   1480  CG  LEU A 402      13.634  23.543  96.138  1.00 28.83           C  
ATOM   1481  CD1 LEU A 402      15.061  23.785  95.644  1.00 27.81           C  
ATOM   1482  CD2 LEU A 402      13.648  23.009  97.565  1.00 29.20           C  
ATOM   1483  N   ALA A 403      10.805  24.655  93.652  1.00 31.43           N  
ATOM   1484  CA  ALA A 403      10.092  23.853  92.662  1.00 32.38           C  
ATOM   1485  C   ALA A 403      10.449  24.344  91.260  1.00 32.71           C  
ATOM   1486  O   ALA A 403      10.706  23.543  90.359  1.00 33.17           O  
ATOM   1487  CB  ALA A 403       8.587  23.950  92.889  1.00 33.04           C  
ATOM   1488  N   ASP A 404      10.465  25.663  91.077  1.00 33.01           N  
ATOM   1489  CA  ASP A 404      10.809  26.246  89.782  1.00 32.74           C  
ATOM   1490  C   ASP A 404      12.231  25.864  89.380  1.00 31.99           C  
ATOM   1491  O   ASP A 404      12.495  25.510  88.225  1.00 31.52           O  
ATOM   1492  CB  ASP A 404      10.725  27.779  89.819  1.00 35.41           C  
ATOM   1493  CG  ASP A 404       9.310  28.291  90.014  1.00 37.33           C  
ATOM   1494  OD1 ASP A 404       8.354  27.530  89.765  1.00 38.41           O  
ATOM   1495  OD2 ASP A 404       9.164  29.472  90.404  1.00 39.06           O  
ATOM   1496  N   LEU A 405      13.149  25.954  90.336  1.00 29.59           N  
ATOM   1497  CA  LEU A 405      14.541  25.635  90.073  1.00 28.93           C  
ATOM   1498  C   LEU A 405      14.692  24.171  89.661  1.00 28.82           C  
ATOM   1499  O   LEU A 405      15.437  23.860  88.733  1.00 28.70           O  
ATOM   1500  CB  LEU A 405      15.393  25.932  91.309  1.00 27.93           C  
ATOM   1501  CG  LEU A 405      16.909  25.812  91.122  1.00 28.05           C  
ATOM   1502  CD1 LEU A 405      17.367  26.734  90.002  1.00 28.62           C  
ATOM   1503  CD2 LEU A 405      17.612  26.160  92.422  1.00 27.90           C  
ATOM   1504  N   LYS A 406      13.986  23.276  90.346  1.00 28.96           N  
ATOM   1505  CA  LYS A 406      14.060  21.856  90.011  1.00 30.15           C  
ATOM   1506  C   LYS A 406      13.577  21.640  88.581  1.00 31.33           C  
ATOM   1507  O   LYS A 406      14.072  20.766  87.872  1.00 30.15           O  
ATOM   1508  CB  LYS A 406      13.221  21.027  90.987  1.00 30.08           C  
ATOM   1509  CG  LYS A 406      13.869  20.875  92.354  1.00 30.05           C  
ATOM   1510  CD  LYS A 406      12.992  20.081  93.304  1.00 30.63           C  
ATOM   1511  CE  LYS A 406      13.712  19.808  94.617  1.00 31.08           C  
ATOM   1512  NZ  LYS A 406      14.934  18.979  94.404  1.00 31.22           N  
ATOM   1513  N   THR A 407      12.613  22.447  88.155  1.00 32.02           N  
ATOM   1514  CA  THR A 407      12.104  22.338  86.795  1.00 33.93           C  
ATOM   1515  C   THR A 407      13.145  22.861  85.811  1.00 34.37           C  
ATOM   1516  O   THR A 407      13.283  22.332  84.709  1.00 36.22           O  
ATOM   1517  CB  THR A 407      10.786  23.118  86.625  1.00 34.26           C  
ATOM   1518  OG1 THR A 407       9.760  22.474  87.390  1.00 34.24           O  
ATOM   1519  CG2 THR A 407      10.369  23.160  85.153  1.00 35.41           C  
ATOM   1520  N   MET A 408      13.881  23.897  86.204  1.00 34.94           N  
ATOM   1521  CA  MET A 408      14.919  24.450  85.339  1.00 35.34           C  
ATOM   1522  C   MET A 408      16.022  23.403  85.183  1.00 34.93           C  
ATOM   1523  O   MET A 408      16.628  23.268  84.116  1.00 34.37           O  
ATOM   1524  CB  MET A 408      15.517  25.728  85.942  1.00 37.14           C  
ATOM   1525  CG  MET A 408      14.583  26.936  85.963  1.00 39.68           C  
ATOM   1526  SD  MET A 408      14.084  27.462  84.309  1.00 42.92           S  
ATOM   1527  CE  MET A 408      15.567  28.240  83.748  1.00 42.28           C  
ATOM   1528  N   VAL A 409      16.279  22.664  86.255  1.00 33.81           N  
ATOM   1529  CA  VAL A 409      17.305  21.631  86.224  1.00 33.81           C  
ATOM   1530  C   VAL A 409      16.913  20.476  85.308  1.00 34.37           C  
ATOM   1531  O   VAL A 409      17.688  20.087  84.435  1.00 34.17           O  
ATOM   1532  CB  VAL A 409      17.583  21.074  87.638  1.00 33.36           C  
ATOM   1533  CG1 VAL A 409      18.503  19.854  87.552  1.00 32.55           C  
ATOM   1534  CG2 VAL A 409      18.224  22.158  88.498  1.00 32.83           C  
ATOM   1535  N   GLU A 410      15.714  19.934  85.500  1.00 35.88           N  
ATOM   1536  CA  GLU A 410      15.263  18.808  84.685  1.00 38.59           C  
ATOM   1537  C   GLU A 410      15.201  19.124  83.190  1.00 39.57           C  
ATOM   1538  O   GLU A 410      15.487  18.263  82.361  1.00 39.31           O  
ATOM   1539  CB  GLU A 410      13.890  18.311  85.153  1.00 39.85           C  
ATOM   1540  CG  GLU A 410      12.746  19.266  84.884  1.00 42.71           C  
ATOM   1541  CD  GLU A 410      11.390  18.596  85.008  1.00 42.94           C  
ATOM   1542  OE1 GLU A 410      11.125  17.643  84.245  1.00 43.59           O  
ATOM   1543  OE2 GLU A 410      10.591  19.021  85.868  1.00 45.21           O  
ATOM   1544  N   THR A 411      14.835  20.356  82.849  1.00 40.42           N  
ATOM   1545  CA  THR A 411      14.731  20.760  81.449  1.00 41.59           C  
ATOM   1546  C   THR A 411      15.968  21.522  80.975  1.00 42.75           C  
ATOM   1547  O   THR A 411      15.949  22.167  79.924  1.00 42.78           O  
ATOM   1548  CB  THR A 411      13.489  21.648  81.222  1.00 41.48           C  
ATOM   1549  OG1 THR A 411      13.622  22.861  81.973  1.00 39.83           O  
ATOM   1550  CG2 THR A 411      12.229  20.921  81.672  1.00 41.00           C  
ATOM   1551  N   LYS A 412      17.042  21.437  81.752  1.00 43.84           N  
ATOM   1552  CA  LYS A 412      18.289  22.120  81.431  1.00 45.33           C  
ATOM   1553  C   LYS A 412      18.807  21.790  80.034  1.00 46.69           C  
ATOM   1554  O   LYS A 412      18.607  20.687  79.532  1.00 46.25           O  
ATOM   1555  CB  LYS A 412      19.368  21.748  82.446  1.00 46.01           C  
ATOM   1556  CG  LYS A 412      20.675  22.488  82.236  1.00 46.54           C  
ATOM   1557  CD  LYS A 412      21.881  21.664  82.665  1.00 46.97           C  
ATOM   1558  CE  LYS A 412      21.820  21.265  84.125  1.00 47.03           C  
ATOM   1559  NZ  LYS A 412      23.123  20.692  84.561  1.00 46.33           N  
ATOM   1560  N   LYS A 413      19.485  22.757  79.423  1.00 48.36           N  
ATOM   1561  CA  LYS A 413      20.064  22.593  78.093  1.00 50.88           C  
ATOM   1562  C   LYS A 413      21.411  23.310  78.065  1.00 51.98           C  
ATOM   1563  O   LYS A 413      21.492  24.498  78.377  1.00 52.10           O  
ATOM   1564  CB  LYS A 413      19.128  23.181  77.034  1.00 51.79           C  
ATOM   1565  CG  LYS A 413      17.766  22.504  76.995  1.00 53.87           C  
ATOM   1566  CD  LYS A 413      16.815  23.166  76.012  1.00 55.12           C  
ATOM   1567  CE  LYS A 413      15.462  22.465  76.027  1.00 56.15           C  
ATOM   1568  NZ  LYS A 413      14.484  23.090  75.097  1.00 56.80           N  
ATOM   1569  N   VAL A 414      22.467  22.587  77.707  1.00 53.36           N  
ATOM   1570  CA  VAL A 414      23.803  23.172  77.659  1.00 55.23           C  
ATOM   1571  C   VAL A 414      24.408  23.132  76.261  1.00 56.43           C  
ATOM   1572  O   VAL A 414      24.108  22.242  75.468  1.00 56.22           O  
ATOM   1573  CB  VAL A 414      24.767  22.443  78.624  1.00 55.39           C  
ATOM   1574  CG1 VAL A 414      24.230  22.508  80.045  1.00 55.16           C  
ATOM   1575  CG2 VAL A 414      24.950  20.996  78.185  1.00 55.84           C  
ATOM   1576  N   THR A 415      25.265  24.105  75.968  1.00 58.09           N  
ATOM   1577  CA  THR A 415      25.925  24.183  74.670  1.00 59.95           C  
ATOM   1578  C   THR A 415      27.080  23.188  74.648  1.00 61.09           C  
ATOM   1579  O   THR A 415      27.351  22.522  75.649  1.00 61.48           O  
ATOM   1580  CB  THR A 415      26.496  25.590  74.416  1.00 60.07           C  
ATOM   1581  OG1 THR A 415      27.605  25.821  75.295  1.00 60.18           O  
ATOM   1582  CG2 THR A 415      25.431  26.651  74.667  1.00 60.12           C  
ATOM   1583  N   SER A 416      27.759  23.087  73.510  1.00 62.20           N  
ATOM   1584  CA  SER A 416      28.889  22.174  73.390  1.00 63.27           C  
ATOM   1585  C   SER A 416      29.995  22.607  74.346  1.00 63.68           C  
ATOM   1586  O   SER A 416      30.774  21.782  74.830  1.00 63.77           O  
ATOM   1587  CB  SER A 416      29.418  22.167  71.953  1.00 63.55           C  
ATOM   1588  OG  SER A 416      28.438  21.678  71.054  1.00 64.12           O  
ATOM   1589  N   LEU A 417      30.048  23.908  74.619  1.00 63.91           N  
ATOM   1590  CA  LEU A 417      31.052  24.470  75.515  1.00 64.04           C  
ATOM   1591  C   LEU A 417      30.704  24.229  76.982  1.00 63.72           C  
ATOM   1592  O   LEU A 417      31.438  24.649  77.878  1.00 64.03           O  
ATOM   1593  CB  LEU A 417      31.205  25.973  75.256  1.00 64.41           C  
ATOM   1594  CG  LEU A 417      31.675  26.374  73.854  1.00 64.79           C  
ATOM   1595  CD1 LEU A 417      31.760  27.889  73.754  1.00 64.78           C  
ATOM   1596  CD2 LEU A 417      33.031  25.745  73.565  1.00 64.95           C  
ATOM   1597  N   GLY A 418      29.583  23.555  77.222  1.00 63.31           N  
ATOM   1598  CA  GLY A 418      29.172  23.265  78.585  1.00 62.67           C  
ATOM   1599  C   GLY A 418      28.602  24.458  79.330  1.00 62.20           C  
ATOM   1600  O   GLY A 418      28.768  24.578  80.545  1.00 62.11           O  
ATOM   1601  N   VAL A 419      27.930  25.342  78.602  1.00 61.69           N  
ATOM   1602  CA  VAL A 419      27.326  26.528  79.194  1.00 61.06           C  
ATOM   1603  C   VAL A 419      25.805  26.428  79.106  1.00 60.57           C  
ATOM   1604  O   VAL A 419      25.266  25.979  78.093  1.00 60.40           O  
ATOM   1605  CB  VAL A 419      27.786  27.810  78.464  1.00 61.26           C  
ATOM   1606  CG1 VAL A 419      27.106  29.029  79.069  1.00 61.50           C  
ATOM   1607  CG2 VAL A 419      29.297  27.945  78.558  1.00 61.36           C  
ATOM   1608  N   LEU A 420      25.118  26.844  80.167  1.00 59.56           N  
ATOM   1609  CA  LEU A 420      23.660  26.794  80.190  1.00 59.07           C  
ATOM   1610  C   LEU A 420      23.037  27.624  79.077  1.00 58.77           C  
ATOM   1611  O   LEU A 420      23.569  28.663  78.685  1.00 58.62           O  
ATOM   1612  CB  LEU A 420      23.121  27.281  81.538  1.00 59.06           C  
ATOM   1613  CG  LEU A 420      23.347  26.388  82.760  1.00 59.34           C  
ATOM   1614  CD1 LEU A 420      22.647  26.994  83.968  1.00 59.46           C  
ATOM   1615  CD2 LEU A 420      22.804  24.997  82.488  1.00 59.42           C  
ATOM   1616  N   LEU A 421      21.900  27.154  78.577  1.00 58.57           N  
ATOM   1617  CA  LEU A 421      21.177  27.837  77.513  1.00 58.68           C  
ATOM   1618  C   LEU A 421      19.867  28.396  78.057  1.00 58.19           C  
ATOM   1619  O   LEU A 421      18.918  27.653  78.304  1.00 57.80           O  
ATOM   1620  CB  LEU A 421      20.887  26.863  76.365  1.00 59.27           C  
ATOM   1621  CG  LEU A 421      20.074  27.385  75.175  1.00 59.97           C  
ATOM   1622  CD1 LEU A 421      20.871  28.447  74.430  1.00 60.18           C  
ATOM   1623  CD2 LEU A 421      19.734  26.228  74.243  1.00 59.89           C  
ATOM   1624  N   LEU A 422      19.827  29.708  78.251  1.00 58.13           N  
ATOM   1625  CA  LEU A 422      18.636  30.376  78.760  1.00 58.11           C  
ATOM   1626  C   LEU A 422      18.250  31.499  77.803  1.00 58.29           C  
ATOM   1627  O   LEU A 422      18.246  32.674  78.171  1.00 58.36           O  
ATOM   1628  CB  LEU A 422      18.905  30.948  80.156  1.00 57.76           C  
ATOM   1629  CG  LEU A 422      19.264  29.939  81.251  1.00 57.71           C  
ATOM   1630  CD1 LEU A 422      19.667  30.673  82.521  1.00 57.77           C  
ATOM   1631  CD2 LEU A 422      18.079  29.026  81.513  1.00 57.34           C  
ATOM   1632  N   ASP A 423      17.931  31.125  76.569  1.00 58.35           N  
ATOM   1633  CA  ASP A 423      17.551  32.091  75.545  1.00 58.34           C  
ATOM   1634  C   ASP A 423      16.253  32.826  75.866  1.00 57.54           C  
ATOM   1635  O   ASP A 423      16.024  33.930  75.370  1.00 57.53           O  
ATOM   1636  CB  ASP A 423      17.423  31.394  74.187  1.00 59.54           C  
ATOM   1637  CG  ASP A 423      18.764  30.945  73.631  1.00 60.79           C  
ATOM   1638  OD1 ASP A 423      18.774  30.255  72.589  1.00 61.68           O  
ATOM   1639  OD2 ASP A 423      19.808  31.286  74.231  1.00 61.33           O  
ATOM   1640  N   ASN A 424      15.407  32.217  76.691  1.00 56.21           N  
ATOM   1641  CA  ASN A 424      14.136  32.833  77.062  1.00 55.48           C  
ATOM   1642  C   ASN A 424      14.229  33.562  78.399  1.00 54.36           C  
ATOM   1643  O   ASN A 424      14.681  32.996  79.395  1.00 54.11           O  
ATOM   1644  CB  ASN A 424      13.035  31.772  77.131  1.00 56.54           C  
ATOM   1645  CG  ASN A 424      12.781  31.111  75.790  1.00 57.59           C  
ATOM   1646  OD1 ASN A 424      12.455  31.780  74.809  1.00 58.30           O  
ATOM   1647  ND2 ASN A 424      12.928  29.792  75.741  1.00 58.19           N  
ATOM   1648  N   TYR A 425      13.796  34.820  78.414  1.00 52.68           N  
ATOM   1649  CA  TYR A 425      13.828  35.627  79.630  1.00 50.67           C  
ATOM   1650  C   TYR A 425      13.086  34.956  80.782  1.00 49.63           C  
ATOM   1651  O   TYR A 425      13.553  34.967  81.925  1.00 49.17           O  
ATOM   1652  CB  TYR A 425      13.214  37.006  79.374  1.00 50.33           C  
ATOM   1653  CG  TYR A 425      13.073  37.833  80.632  1.00 49.74           C  
ATOM   1654  CD1 TYR A 425      14.197  38.334  81.291  1.00 49.67           C  
ATOM   1655  CD2 TYR A 425      11.819  38.072  81.196  1.00 48.82           C  
ATOM   1656  CE1 TYR A 425      14.075  39.052  82.482  1.00 49.03           C  
ATOM   1657  CE2 TYR A 425      11.688  38.788  82.385  1.00 48.59           C  
ATOM   1658  CZ  TYR A 425      12.819  39.273  83.023  1.00 48.38           C  
ATOM   1659  OH  TYR A 425      12.695  39.970  84.204  1.00 47.80           O  
ATOM   1660  N   SER A 426      11.924  34.384  80.481  1.00 48.07           N  
ATOM   1661  CA  SER A 426      11.114  33.709  81.491  1.00 46.78           C  
ATOM   1662  C   SER A 426      11.973  32.747  82.311  1.00 45.15           C  
ATOM   1663  O   SER A 426      11.791  32.610  83.521  1.00 44.94           O  
ATOM   1664  CB  SER A 426       9.970  32.940  80.821  1.00 48.06           C  
ATOM   1665  OG  SER A 426       9.141  33.810  80.064  1.00 50.02           O  
ATOM   1666  N   ASP A 427      12.909  32.081  81.644  1.00 43.24           N  
ATOM   1667  CA  ASP A 427      13.798  31.148  82.321  1.00 41.37           C  
ATOM   1668  C   ASP A 427      14.931  31.907  83.004  1.00 39.30           C  
ATOM   1669  O   ASP A 427      15.372  31.536  84.089  1.00 37.62           O  
ATOM   1670  CB  ASP A 427      14.384  30.141  81.325  1.00 42.54           C  
ATOM   1671  CG  ASP A 427      13.330  29.225  80.731  1.00 42.82           C  
ATOM   1672  OD1 ASP A 427      12.432  28.783  81.478  1.00 42.80           O  
ATOM   1673  OD2 ASP A 427      13.410  28.935  79.517  1.00 44.87           O  
ATOM   1674  N   ARG A 428      15.396  32.975  82.363  1.00 38.22           N  
ATOM   1675  CA  ARG A 428      16.477  33.782  82.917  1.00 37.34           C  
ATOM   1676  C   ARG A 428      16.132  34.353  84.291  1.00 35.16           C  
ATOM   1677  O   ARG A 428      16.931  34.265  85.220  1.00 33.87           O  
ATOM   1678  CB  ARG A 428      16.826  34.935  81.974  1.00 40.20           C  
ATOM   1679  CG  ARG A 428      17.593  34.538  80.724  1.00 44.17           C  
ATOM   1680  CD  ARG A 428      17.862  35.768  79.859  1.00 47.53           C  
ATOM   1681  NE  ARG A 428      18.533  35.430  78.608  1.00 51.76           N  
ATOM   1682  CZ  ARG A 428      18.780  36.306  77.639  1.00 54.02           C  
ATOM   1683  NH1 ARG A 428      18.409  37.573  77.781  1.00 55.53           N  
ATOM   1684  NH2 ARG A 428      19.394  35.919  76.528  1.00 55.13           N  
ATOM   1685  N   ILE A 429      14.946  34.938  84.418  1.00 33.39           N  
ATOM   1686  CA  ILE A 429      14.544  35.533  85.685  1.00 32.28           C  
ATOM   1687  C   ILE A 429      14.381  34.485  86.786  1.00 31.00           C  
ATOM   1688  O   ILE A 429      14.679  34.758  87.948  1.00 30.49           O  
ATOM   1689  CB  ILE A 429      13.240  36.361  85.539  1.00 32.90           C  
ATOM   1690  CG1 ILE A 429      12.984  37.148  86.825  1.00 32.74           C  
ATOM   1691  CG2 ILE A 429      12.062  35.450  85.228  1.00 33.39           C  
ATOM   1692  CD1 ILE A 429      14.106  38.113  87.190  1.00 32.33           C  
ATOM   1693  N   GLN A 430      13.920  33.288  86.427  1.00 29.65           N  
ATOM   1694  CA  GLN A 430      13.773  32.226  87.418  1.00 29.52           C  
ATOM   1695  C   GLN A 430      15.149  31.872  87.984  1.00 28.02           C  
ATOM   1696  O   GLN A 430      15.304  31.693  89.192  1.00 28.15           O  
ATOM   1697  CB  GLN A 430      13.145  30.972  86.798  1.00 31.54           C  
ATOM   1698  CG  GLN A 430      11.673  31.104  86.434  1.00 35.08           C  
ATOM   1699  CD  GLN A 430      11.096  29.805  85.888  1.00 36.76           C  
ATOM   1700  OE1 GLN A 430      11.048  28.795  86.589  1.00 37.96           O  
ATOM   1701  NE2 GLN A 430      10.664  29.827  84.628  1.00 37.11           N  
ATOM   1702  N   VAL A 431      16.150  31.771  87.114  1.00 26.60           N  
ATOM   1703  CA  VAL A 431      17.500  31.447  87.571  1.00 24.79           C  
ATOM   1704  C   VAL A 431      18.070  32.590  88.413  1.00 24.46           C  
ATOM   1705  O   VAL A 431      18.685  32.353  89.453  1.00 23.98           O  
ATOM   1706  CB  VAL A 431      18.449  31.158  86.382  1.00 24.86           C  
ATOM   1707  CG1 VAL A 431      19.870  30.936  86.882  1.00 23.40           C  
ATOM   1708  CG2 VAL A 431      17.964  29.921  85.628  1.00 25.20           C  
ATOM   1709  N   LEU A 432      17.858  33.827  87.972  1.00 23.53           N  
ATOM   1710  CA  LEU A 432      18.355  34.986  88.710  1.00 23.03           C  
ATOM   1711  C   LEU A 432      17.740  35.082  90.103  1.00 22.52           C  
ATOM   1712  O   LEU A 432      18.428  35.418  91.066  1.00 21.66           O  
ATOM   1713  CB  LEU A 432      18.082  36.273  87.925  1.00 24.39           C  
ATOM   1714  CG  LEU A 432      18.978  36.436  86.695  1.00 25.04           C  
ATOM   1715  CD1 LEU A 432      18.511  37.613  85.857  1.00 26.94           C  
ATOM   1716  CD2 LEU A 432      20.416  36.633  87.151  1.00 27.30           C  
ATOM   1717  N   GLN A 433      16.446  34.796  90.206  1.00 22.44           N  
ATOM   1718  CA  GLN A 433      15.760  34.832  91.496  1.00 22.68           C  
ATOM   1719  C   GLN A 433      16.362  33.799  92.429  1.00 22.80           C  
ATOM   1720  O   GLN A 433      16.636  34.079  93.601  1.00 22.67           O  
ATOM   1721  CB  GLN A 433      14.275  34.526  91.328  1.00 22.86           C  
ATOM   1722  CG  GLN A 433      13.488  35.616  90.637  1.00 24.46           C  
ATOM   1723  CD  GLN A 433      12.020  35.258  90.532  1.00 25.59           C  
ATOM   1724  OE1 GLN A 433      11.172  35.831  91.217  1.00 28.79           O  
ATOM   1725  NE2 GLN A 433      11.718  34.296  89.684  1.00 25.67           N  
ATOM   1726  N   ASN A 434      16.556  32.591  91.911  1.00 21.67           N  
ATOM   1727  CA  ASN A 434      17.138  31.534  92.721  1.00 22.17           C  
ATOM   1728  C   ASN A 434      18.587  31.833  93.085  1.00 21.14           C  
ATOM   1729  O   ASN A 434      19.032  31.506  94.185  1.00 21.72           O  
ATOM   1730  CB  ASN A 434      17.014  30.194  91.995  1.00 22.59           C  
ATOM   1731  CG  ASN A 434      15.672  29.535  92.247  1.00 23.74           C  
ATOM   1732  OD1 ASN A 434      15.429  28.997  93.326  1.00 25.13           O  
ATOM   1733  ND2 ASN A 434      14.787  29.593  91.263  1.00 24.07           N  
ATOM   1734  N   LEU A 435      19.312  32.479  92.176  1.00 20.74           N  
ATOM   1735  CA  LEU A 435      20.706  32.828  92.423  1.00 20.56           C  
ATOM   1736  C   LEU A 435      20.836  33.771  93.623  1.00 20.62           C  
ATOM   1737  O   LEU A 435      21.659  33.550  94.519  1.00 20.39           O  
ATOM   1738  CB  LEU A 435      21.314  33.475  91.172  1.00 20.46           C  
ATOM   1739  CG  LEU A 435      22.826  33.718  91.195  1.00 21.43           C  
ATOM   1740  CD1 LEU A 435      23.365  33.710  89.764  1.00 22.11           C  
ATOM   1741  CD2 LEU A 435      23.136  35.042  91.887  1.00 21.38           C  
ATOM   1742  N   VAL A 436      20.028  34.826  93.643  1.00 19.26           N  
ATOM   1743  CA  VAL A 436      20.077  35.772  94.750  1.00 19.27           C  
ATOM   1744  C   VAL A 436      19.540  35.125  96.038  1.00 18.47           C  
ATOM   1745  O   VAL A 436      20.031  35.410  97.129  1.00 18.88           O  
ATOM   1746  CB  VAL A 436      19.282  37.057  94.402  1.00 19.32           C  
ATOM   1747  CG1 VAL A 436      19.238  37.998  95.593  1.00 19.66           C  
ATOM   1748  CG2 VAL A 436      19.945  37.752  93.220  1.00 20.08           C  
ATOM   1749  N   HIS A 437      18.547  34.247  95.903  1.00 17.86           N  
ATOM   1750  CA  HIS A 437      17.975  33.539  97.053  1.00 19.14           C  
ATOM   1751  C   HIS A 437      19.078  32.647  97.639  1.00 19.09           C  
ATOM   1752  O   HIS A 437      19.242  32.560  98.858  1.00 18.05           O  
ATOM   1753  CB  HIS A 437      16.761  32.702  96.598  1.00 19.73           C  
ATOM   1754  CG  HIS A 437      16.164  31.831  97.667  1.00 21.15           C  
ATOM   1755  ND1 HIS A 437      15.817  32.302  98.917  1.00 22.14           N  
ATOM   1756  CD2 HIS A 437      15.798  30.527  97.645  1.00 20.93           C  
ATOM   1757  CE1 HIS A 437      15.264  31.327  99.617  1.00 21.47           C  
ATOM   1758  NE2 HIS A 437      15.240  30.239  98.867  1.00 22.08           N  
ATOM   1759  N   CYS A 438      19.835  31.987  96.764  1.00 19.34           N  
ATOM   1760  CA  CYS A 438      20.938  31.142  97.211  1.00 19.91           C  
ATOM   1761  C   CYS A 438      21.989  32.015  97.899  1.00 19.88           C  
ATOM   1762  O   CYS A 438      22.519  31.649  98.943  1.00 20.01           O  
ATOM   1763  CB  CYS A 438      21.564  30.390  96.027  1.00 19.32           C  
ATOM   1764  SG  CYS A 438      20.621  28.926  95.474  1.00 22.11           S  
ATOM   1765  N   ALA A 439      22.281  33.181  97.320  1.00 19.91           N  
ATOM   1766  CA  ALA A 439      23.262  34.083  97.910  1.00 20.05           C  
ATOM   1767  C   ALA A 439      22.846  34.477  99.332  1.00 20.62           C  
ATOM   1768  O   ALA A 439      23.683  34.550 100.240  1.00 19.90           O  
ATOM   1769  CB  ALA A 439      23.426  35.330  97.032  1.00 19.76           C  
ATOM   1770  N   ASP A 440      21.548  34.705  99.519  1.00 20.64           N  
ATOM   1771  CA  ASP A 440      20.986  35.089 100.816  1.00 21.14           C  
ATOM   1772  C   ASP A 440      21.075  33.921 101.808  1.00 21.78           C  
ATOM   1773  O   ASP A 440      21.161  34.134 103.016  1.00 22.49           O  
ATOM   1774  CB  ASP A 440      19.527  35.532 100.610  1.00 21.46           C  
ATOM   1775  CG  ASP A 440      18.894  36.149 101.854  1.00 22.29           C  
ATOM   1776  OD1 ASP A 440      19.541  36.952 102.569  1.00 21.21           O  
ATOM   1777  OD2 ASP A 440      17.706  35.839 102.102  1.00 23.75           O  
ATOM   1778  N   LEU A 441      21.063  32.693 101.290  1.00 20.94           N  
ATOM   1779  CA  LEU A 441      21.152  31.490 102.120  1.00 20.81           C  
ATOM   1780  C   LEU A 441      22.498  30.777 101.929  1.00 20.77           C  
ATOM   1781  O   LEU A 441      22.586  29.555 102.057  1.00 19.95           O  
ATOM   1782  CB  LEU A 441      20.013  30.521 101.768  1.00 21.16           C  
ATOM   1783  CG  LEU A 441      18.593  30.986 102.107  1.00 21.45           C  
ATOM   1784  CD1 LEU A 441      17.582  29.921 101.690  1.00 22.13           C  
ATOM   1785  CD2 LEU A 441      18.502  31.248 103.606  1.00 22.59           C  
ATOM   1786  N   SER A 442      23.550  31.537 101.651  1.00 20.46           N  
ATOM   1787  CA  SER A 442      24.860  30.934 101.409  1.00 20.74           C  
ATOM   1788  C   SER A 442      25.736  30.716 102.641  1.00 21.33           C  
ATOM   1789  O   SER A 442      26.768  30.046 102.548  1.00 21.02           O  
ATOM   1790  CB  SER A 442      25.633  31.769 100.385  1.00 19.96           C  
ATOM   1791  OG  SER A 442      25.877  33.068 100.889  1.00 21.28           O  
ATOM   1792  N   ASN A 443      25.327  31.255 103.791  1.00 20.84           N  
ATOM   1793  CA  ASN A 443      26.115  31.122 105.020  1.00 20.49           C  
ATOM   1794  C   ASN A 443      26.673  29.714 105.289  1.00 20.90           C  
ATOM   1795  O   ASN A 443      27.858  29.566 105.580  1.00 20.56           O  
ATOM   1796  CB  ASN A 443      25.299  31.550 106.247  1.00 20.39           C  
ATOM   1797  CG  ASN A 443      25.087  33.059 106.344  1.00 20.59           C  
ATOM   1798  OD1 ASN A 443      24.334  33.512 107.199  1.00 22.24           O  
ATOM   1799  ND2 ASN A 443      25.745  33.834 105.482  1.00 20.04           N  
ATOM   1800  N   PRO A 444      25.825  28.670 105.214  1.00 21.03           N  
ATOM   1801  CA  PRO A 444      26.318  27.312 105.474  1.00 21.69           C  
ATOM   1802  C   PRO A 444      27.290  26.717 104.447  1.00 22.20           C  
ATOM   1803  O   PRO A 444      27.878  25.663 104.698  1.00 22.98           O  
ATOM   1804  CB  PRO A 444      25.034  26.497 105.611  1.00 21.44           C  
ATOM   1805  CG  PRO A 444      24.092  27.201 104.676  1.00 21.17           C  
ATOM   1806  CD  PRO A 444      24.371  28.663 104.966  1.00 20.64           C  
ATOM   1807  N   THR A 445      27.464  27.380 103.305  1.00 21.90           N  
ATOM   1808  CA  THR A 445      28.397  26.890 102.292  1.00 22.29           C  
ATOM   1809  C   THR A 445      29.741  27.606 102.415  1.00 22.43           C  
ATOM   1810  O   THR A 445      30.638  27.402 101.600  1.00 23.25           O  
ATOM   1811  CB  THR A 445      27.868  27.099 100.846  1.00 21.57           C  
ATOM   1812  OG1 THR A 445      27.840  28.498 100.538  1.00 21.04           O  
ATOM   1813  CG2 THR A 445      26.477  26.509 100.694  1.00 21.23           C  
ATOM   1814  N   LYS A 446      29.873  28.455 103.429  1.00 22.80           N  
ATOM   1815  CA  LYS A 446      31.112  29.191 103.649  1.00 23.73           C  
ATOM   1816  C   LYS A 446      31.969  28.440 104.668  1.00 24.33           C  
ATOM   1817  O   LYS A 446      31.452  27.666 105.467  1.00 25.15           O  
ATOM   1818  CB  LYS A 446      30.814  30.606 104.177  1.00 22.83           C  
ATOM   1819  CG  LYS A 446      29.988  31.489 103.235  1.00 23.32           C  
ATOM   1820  CD  LYS A 446      30.726  31.761 101.927  1.00 24.12           C  
ATOM   1821  CE  LYS A 446      29.853  32.518 100.923  1.00 23.88           C  
ATOM   1822  NZ  LYS A 446      29.531  33.899 101.364  1.00 23.38           N  
ATOM   1823  N   PRO A 447      33.294  28.649 104.640  1.00 26.40           N  
ATOM   1824  CA  PRO A 447      34.190  27.975 105.589  1.00 27.08           C  
ATOM   1825  C   PRO A 447      33.672  28.144 107.018  1.00 27.58           C  
ATOM   1826  O   PRO A 447      33.210  29.224 107.394  1.00 26.44           O  
ATOM   1827  CB  PRO A 447      35.518  28.686 105.361  1.00 27.75           C  
ATOM   1828  CG  PRO A 447      35.486  28.947 103.885  1.00 28.69           C  
ATOM   1829  CD  PRO A 447      34.061  29.450 103.670  1.00 26.90           C  
ATOM   1830  N   LEU A 448      33.755  27.076 107.803  1.00 27.14           N  
ATOM   1831  CA  LEU A 448      33.266  27.074 109.176  1.00 27.66           C  
ATOM   1832  C   LEU A 448      33.537  28.332 110.011  1.00 27.20           C  
ATOM   1833  O   LEU A 448      32.636  28.831 110.684  1.00 27.24           O  
ATOM   1834  CB  LEU A 448      33.791  25.839 109.914  1.00 28.21           C  
ATOM   1835  CG  LEU A 448      33.199  25.604 111.304  1.00 30.01           C  
ATOM   1836  CD1 LEU A 448      31.666  25.586 111.224  1.00 29.42           C  
ATOM   1837  CD2 LEU A 448      33.730  24.288 111.865  1.00 29.99           C  
ATOM   1838  N   PRO A 449      34.770  28.859 109.985  1.00 27.23           N  
ATOM   1839  CA  PRO A 449      35.048  30.063 110.777  1.00 27.36           C  
ATOM   1840  C   PRO A 449      34.082  31.199 110.444  1.00 27.00           C  
ATOM   1841  O   PRO A 449      33.609  31.908 111.337  1.00 26.06           O  
ATOM   1842  CB  PRO A 449      36.488  30.396 110.403  1.00 28.26           C  
ATOM   1843  CG  PRO A 449      37.081  29.043 110.145  1.00 28.33           C  
ATOM   1844  CD  PRO A 449      35.995  28.382 109.316  1.00 28.05           C  
ATOM   1845  N   LEU A 450      33.792  31.364 109.156  1.00 25.66           N  
ATOM   1846  CA  LEU A 450      32.868  32.402 108.717  1.00 25.31           C  
ATOM   1847  C   LEU A 450      31.441  32.027 109.115  1.00 24.28           C  
ATOM   1848  O   LEU A 450      30.695  32.860 109.624  1.00 24.14           O  
ATOM   1849  CB  LEU A 450      32.940  32.584 107.195  1.00 25.89           C  
ATOM   1850  CG  LEU A 450      34.293  33.016 106.614  1.00 26.89           C  
ATOM   1851  CD1 LEU A 450      34.176  33.182 105.101  1.00 26.45           C  
ATOM   1852  CD2 LEU A 450      34.737  34.321 107.262  1.00 27.14           C  
ATOM   1853  N   TYR A 451      31.069  30.773 108.881  1.00 23.38           N  
ATOM   1854  CA  TYR A 451      29.728  30.303 109.219  1.00 23.44           C  
ATOM   1855  C   TYR A 451      29.417  30.479 110.699  1.00 23.29           C  
ATOM   1856  O   TYR A 451      28.316  30.887 111.062  1.00 22.29           O  
ATOM   1857  CB  TYR A 451      29.559  28.830 108.829  1.00 23.19           C  
ATOM   1858  CG  TYR A 451      28.152  28.304 109.019  1.00 23.34           C  
ATOM   1859  CD1 TYR A 451      27.046  29.045 108.595  1.00 22.70           C  
ATOM   1860  CD2 TYR A 451      27.925  27.050 109.587  1.00 24.07           C  
ATOM   1861  CE1 TYR A 451      25.751  28.552 108.730  1.00 23.01           C  
ATOM   1862  CE2 TYR A 451      26.631  26.544 109.728  1.00 24.07           C  
ATOM   1863  CZ  TYR A 451      25.549  27.301 109.294  1.00 24.21           C  
ATOM   1864  OH  TYR A 451      24.271  26.805 109.411  1.00 23.28           O  
ATOM   1865  N   ARG A 452      30.387  30.182 111.560  1.00 23.86           N  
ATOM   1866  CA  ARG A 452      30.166  30.330 112.995  1.00 24.78           C  
ATOM   1867  C   ARG A 452      29.911  31.779 113.383  1.00 24.32           C  
ATOM   1868  O   ARG A 452      29.127  32.046 114.295  1.00 23.65           O  
ATOM   1869  CB  ARG A 452      31.351  29.754 113.780  1.00 27.65           C  
ATOM   1870  CG  ARG A 452      31.384  28.225 113.718  1.00 31.56           C  
ATOM   1871  CD  ARG A 452      32.602  27.629 114.382  1.00 34.82           C  
ATOM   1872  NE  ARG A 452      32.643  27.868 115.823  1.00 37.97           N  
ATOM   1873  CZ  ARG A 452      33.619  27.434 116.610  1.00 39.57           C  
ATOM   1874  NH1 ARG A 452      34.626  26.737 116.090  1.00 40.06           N  
ATOM   1875  NH2 ARG A 452      33.600  27.704 117.907  1.00 40.48           N  
ATOM   1876  N   GLN A 453      30.556  32.715 112.688  1.00 22.92           N  
ATOM   1877  CA  GLN A 453      30.357  34.129 112.977  1.00 23.43           C  
ATOM   1878  C   GLN A 453      28.964  34.573 112.526  1.00 23.28           C  
ATOM   1879  O   GLN A 453      28.306  35.362 113.209  1.00 23.52           O  
ATOM   1880  CB  GLN A 453      31.445  34.969 112.302  1.00 24.12           C  
ATOM   1881  CG  GLN A 453      32.839  34.694 112.870  1.00 25.26           C  
ATOM   1882  CD  GLN A 453      33.924  35.495 112.186  1.00 26.21           C  
ATOM   1883  OE1 GLN A 453      34.037  36.708 112.382  1.00 27.44           O  
ATOM   1884  NE2 GLN A 453      34.725  34.823 111.366  1.00 24.97           N  
ATOM   1885  N   TRP A 454      28.512  34.064 111.384  1.00 23.14           N  
ATOM   1886  CA  TRP A 454      27.174  34.398 110.891  1.00 22.53           C  
ATOM   1887  C   TRP A 454      26.155  33.831 111.871  1.00 22.55           C  
ATOM   1888  O   TRP A 454      25.179  34.490 112.227  1.00 22.51           O  
ATOM   1889  CB  TRP A 454      26.929  33.781 109.511  1.00 20.70           C  
ATOM   1890  CG  TRP A 454      27.685  34.456 108.413  1.00 20.98           C  
ATOM   1891  CD1 TRP A 454      28.513  33.862 107.505  1.00 21.05           C  
ATOM   1892  CD2 TRP A 454      27.682  35.853 108.100  1.00 21.38           C  
ATOM   1893  NE1 TRP A 454      29.027  34.802 106.646  1.00 20.91           N  
ATOM   1894  CE2 TRP A 454      28.533  36.033 106.987  1.00 22.43           C  
ATOM   1895  CE3 TRP A 454      27.042  36.972 108.652  1.00 21.64           C  
ATOM   1896  CZ2 TRP A 454      28.763  37.289 106.410  1.00 22.11           C  
ATOM   1897  CZ3 TRP A 454      27.271  38.225 108.076  1.00 21.62           C  
ATOM   1898  CH2 TRP A 454      28.123  38.369 106.968  1.00 23.03           C  
ATOM   1899  N   THR A 455      26.389  32.592 112.285  1.00 22.44           N  
ATOM   1900  CA  THR A 455      25.515  31.908 113.226  1.00 23.24           C  
ATOM   1901  C   THR A 455      25.422  32.684 114.543  1.00 22.81           C  
ATOM   1902  O   THR A 455      24.337  32.821 115.118  1.00 21.76           O  
ATOM   1903  CB  THR A 455      26.038  30.467 113.487  1.00 24.84           C  
ATOM   1904  OG1 THR A 455      25.841  29.676 112.305  1.00 27.23           O  
ATOM   1905  CG2 THR A 455      25.310  29.826 114.642  1.00 27.17           C  
ATOM   1906  N   ASP A 456      26.555  33.196 115.019  1.00 21.84           N  
ATOM   1907  CA  ASP A 456      26.564  33.953 116.267  1.00 22.36           C  
ATOM   1908  C   ASP A 456      25.730  35.229 116.135  1.00 22.64           C  
ATOM   1909  O   ASP A 456      25.080  35.662 117.094  1.00 23.07           O  
ATOM   1910  CB  ASP A 456      27.997  34.324 116.668  1.00 23.62           C  
ATOM   1911  CG  ASP A 456      28.057  35.027 118.011  1.00 22.90           C  
ATOM   1912  OD1 ASP A 456      27.848  34.355 119.045  1.00 23.51           O  
ATOM   1913  OD2 ASP A 456      28.298  36.253 118.037  1.00 24.97           O  
ATOM   1914  N   ARG A 457      25.752  35.835 114.951  1.00 21.11           N  
ATOM   1915  CA  ARG A 457      24.977  37.051 114.725  1.00 22.21           C  
ATOM   1916  C   ARG A 457      23.495  36.736 114.658  1.00 20.93           C  
ATOM   1917  O   ARG A 457      22.679  37.454 115.228  1.00 21.06           O  
ATOM   1918  CB  ARG A 457      25.430  37.752 113.443  1.00 21.46           C  
ATOM   1919  CG  ARG A 457      26.806  38.356 113.597  1.00 24.12           C  
ATOM   1920  CD  ARG A 457      27.262  39.132 112.387  1.00 25.07           C  
ATOM   1921  NE  ARG A 457      28.393  39.966 112.771  1.00 26.26           N  
ATOM   1922  CZ  ARG A 457      28.563  41.222 112.383  1.00 27.69           C  
ATOM   1923  NH1 ARG A 457      27.672  41.796 111.580  1.00 29.34           N  
ATOM   1924  NH2 ARG A 457      29.602  41.914 112.829  1.00 26.78           N  
ATOM   1925  N   ILE A 458      23.152  35.656 113.965  1.00 21.40           N  
ATOM   1926  CA  ILE A 458      21.761  35.238 113.846  1.00 21.58           C  
ATOM   1927  C   ILE A 458      21.188  34.951 115.232  1.00 22.44           C  
ATOM   1928  O   ILE A 458      20.068  35.356 115.550  1.00 20.80           O  
ATOM   1929  CB  ILE A 458      21.641  33.981 112.945  1.00 21.56           C  
ATOM   1930  CG1 ILE A 458      21.912  34.377 111.489  1.00 21.65           C  
ATOM   1931  CG2 ILE A 458      20.265  33.337 113.105  1.00 21.14           C  
ATOM   1932  CD1 ILE A 458      22.023  33.204 110.509  1.00 22.74           C  
ATOM   1933  N   MET A 459      21.953  34.265 116.076  1.00 22.83           N  
ATOM   1934  CA  MET A 459      21.440  33.975 117.405  1.00 23.12           C  
ATOM   1935  C   MET A 459      21.204  35.240 118.226  1.00 22.10           C  
ATOM   1936  O   MET A 459      20.234  35.314 118.971  1.00 21.83           O  
ATOM   1937  CB  MET A 459      22.354  32.986 118.131  1.00 27.09           C  
ATOM   1938  CG  MET A 459      22.140  31.566 117.596  1.00 30.45           C  
ATOM   1939  SD  MET A 459      22.830  30.270 118.580  1.00 37.88           S  
ATOM   1940  CE  MET A 459      24.569  30.521 118.218  1.00 35.92           C  
ATOM   1941  N   ALA A 460      22.063  36.243 118.077  1.00 22.23           N  
ATOM   1942  CA  ALA A 460      21.872  37.490 118.815  1.00 22.74           C  
ATOM   1943  C   ALA A 460      20.568  38.161 118.380  1.00 23.50           C  
ATOM   1944  O   ALA A 460      19.790  38.628 119.214  1.00 23.37           O  
ATOM   1945  CB  ALA A 460      23.048  38.435 118.580  1.00 23.03           C  
ATOM   1946  N   GLU A 461      20.320  38.199 117.074  1.00 23.27           N  
ATOM   1947  CA  GLU A 461      19.096  38.828 116.570  1.00 23.18           C  
ATOM   1948  C   GLU A 461      17.870  38.025 117.005  1.00 23.90           C  
ATOM   1949  O   GLU A 461      16.816  38.591 117.315  1.00 23.11           O  
ATOM   1950  CB  GLU A 461      19.142  38.937 115.040  1.00 22.95           C  
ATOM   1951  CG  GLU A 461      18.028  39.791 114.465  1.00 21.74           C  
ATOM   1952  CD  GLU A 461      18.151  40.011 112.975  1.00 22.29           C  
ATOM   1953  OE1 GLU A 461      19.254  40.360 112.507  1.00 21.74           O  
ATOM   1954  OE2 GLU A 461      17.133  39.848 112.274  1.00 24.09           O  
ATOM   1955  N   PHE A 462      18.028  36.706 117.033  1.00 23.22           N  
ATOM   1956  CA  PHE A 462      16.973  35.780 117.435  1.00 24.40           C  
ATOM   1957  C   PHE A 462      16.537  36.055 118.880  1.00 26.57           C  
ATOM   1958  O   PHE A 462      15.355  35.955 119.213  1.00 25.91           O  
ATOM   1959  CB  PHE A 462      17.504  34.349 117.325  1.00 24.06           C  
ATOM   1960  CG  PHE A 462      16.491  33.277 117.638  1.00 23.71           C  
ATOM   1961  CD1 PHE A 462      15.574  32.863 116.675  1.00 23.02           C  
ATOM   1962  CD2 PHE A 462      16.506  32.628 118.873  1.00 24.20           C  
ATOM   1963  CE1 PHE A 462      14.691  31.810 116.929  1.00 23.52           C  
ATOM   1964  CE2 PHE A 462      15.631  31.576 119.141  1.00 23.25           C  
ATOM   1965  CZ  PHE A 462      14.721  31.164 118.163  1.00 24.35           C  
ATOM   1966  N   PHE A 463      17.498  36.393 119.734  1.00 28.34           N  
ATOM   1967  CA  PHE A 463      17.210  36.672 121.139  1.00 32.28           C  
ATOM   1968  C   PHE A 463      17.007  38.149 121.472  1.00 35.57           C  
ATOM   1969  O   PHE A 463      16.690  38.485 122.610  1.00 36.60           O  
ATOM   1970  CB  PHE A 463      18.325  36.104 122.022  1.00 31.07           C  
ATOM   1971  CG  PHE A 463      18.315  34.607 122.113  1.00 30.92           C  
ATOM   1972  CD1 PHE A 463      17.295  33.946 122.788  1.00 30.75           C  
ATOM   1973  CD2 PHE A 463      19.314  33.854 121.506  1.00 29.70           C  
ATOM   1974  CE1 PHE A 463      17.268  32.555 122.856  1.00 31.16           C  
ATOM   1975  CE2 PHE A 463      19.296  32.466 121.569  1.00 29.65           C  
ATOM   1976  CZ  PHE A 463      18.272  31.814 122.243  1.00 30.55           C  
ATOM   1977  N   GLN A 464      17.189  39.033 120.496  1.00 39.37           N  
ATOM   1978  CA  GLN A 464      17.007  40.462 120.744  1.00 44.82           C  
ATOM   1979  C   GLN A 464      15.563  40.736 121.137  1.00 47.54           C  
ATOM   1980  O   GLN A 464      14.655  40.611 120.315  1.00 48.67           O  
ATOM   1981  CB  GLN A 464      17.366  41.278 119.502  1.00 46.07           C  
ATOM   1982  CG  GLN A 464      18.833  41.199 119.120  1.00 49.47           C  
ATOM   1983  CD  GLN A 464      19.719  42.131 119.926  1.00 51.24           C  
ATOM   1984  OE1 GLN A 464      19.612  42.210 121.153  1.00 52.85           O  
ATOM   1985  NE2 GLN A 464      20.613  42.837 119.236  1.00 51.54           N  
ATOM   1986  N   GLN A 465      15.366  41.105 122.401  1.00 50.94           N  
ATOM   1987  CA  GLN A 465      14.043  41.398 122.949  1.00 53.78           C  
ATOM   1988  C   GLN A 465      12.942  40.590 122.264  1.00 54.63           C  
ATOM   1989  O   GLN A 465      12.155  41.189 121.496  1.00 55.59           O  
ATOM   1990  CB  GLN A 465      13.739  42.896 122.836  1.00 55.25           C  
ATOM   1991  CG  GLN A 465      12.422  43.301 123.490  1.00 57.38           C  
ATOM   1992  CD  GLN A 465      12.134  44.786 123.367  1.00 58.60           C  
ATOM   1993  OE1 GLN A 465      12.088  45.334 122.263  1.00 59.04           O  
ATOM   1994  NE2 GLN A 465      11.932  45.445 124.504  1.00 59.00           N  
ATOM   1995  N   GLN A 491      11.838  16.568 109.438  1.00 50.64           N  
ATOM   1996  CA  GLN A 491      11.619  17.098 110.812  1.00 49.83           C  
ATOM   1997  C   GLN A 491      12.206  18.500 110.994  1.00 48.18           C  
ATOM   1998  O   GLN A 491      11.698  19.463 110.417  1.00 49.04           O  
ATOM   1999  CB  GLN A 491      12.209  16.132 111.846  1.00 51.56           C  
ATOM   2000  CG  GLN A 491      11.832  16.446 113.287  1.00 53.38           C  
ATOM   2001  CD  GLN A 491      12.127  15.290 114.229  1.00 54.80           C  
ATOM   2002  OE1 GLN A 491      11.548  14.209 114.101  1.00 55.03           O  
ATOM   2003  NE2 GLN A 491      13.032  15.512 115.181  1.00 54.80           N  
ATOM   2004  N   VAL A 492      13.284  18.616 111.768  1.00 45.77           N  
ATOM   2005  CA  VAL A 492      13.885  19.923 112.039  1.00 42.68           C  
ATOM   2006  C   VAL A 492      15.386  20.061 111.772  1.00 40.25           C  
ATOM   2007  O   VAL A 492      16.151  19.115 111.954  1.00 40.82           O  
ATOM   2008  CB  VAL A 492      13.612  20.330 113.506  1.00 43.09           C  
ATOM   2009  CG1 VAL A 492      14.417  21.560 113.877  1.00 44.13           C  
ATOM   2010  CG2 VAL A 492      12.127  20.588 113.695  1.00 43.19           C  
ATOM   2011  N   GLY A 493      15.793  21.263 111.362  1.00 36.47           N  
ATOM   2012  CA  GLY A 493      17.192  21.538 111.082  1.00 32.66           C  
ATOM   2013  C   GLY A 493      17.386  22.457 109.884  1.00 30.08           C  
ATOM   2014  O   GLY A 493      16.831  22.216 108.817  1.00 29.68           O  
ATOM   2015  N   PHE A 494      18.185  23.506 110.053  1.00 27.55           N  
ATOM   2016  CA  PHE A 494      18.437  24.457 108.975  1.00 25.75           C  
ATOM   2017  C   PHE A 494      19.190  23.839 107.790  1.00 25.06           C  
ATOM   2018  O   PHE A 494      18.748  23.931 106.649  1.00 24.02           O  
ATOM   2019  CB  PHE A 494      19.220  25.659 109.516  1.00 24.40           C  
ATOM   2020  CG  PHE A 494      19.627  26.648 108.460  1.00 24.29           C  
ATOM   2021  CD1 PHE A 494      18.673  27.308 107.694  1.00 24.54           C  
ATOM   2022  CD2 PHE A 494      20.974  26.920 108.230  1.00 24.51           C  
ATOM   2023  CE1 PHE A 494      19.052  28.227 106.713  1.00 24.95           C  
ATOM   2024  CE2 PHE A 494      21.363  27.835 107.254  1.00 24.13           C  
ATOM   2025  CZ  PHE A 494      20.399  28.490 106.494  1.00 24.04           C  
ATOM   2026  N   ILE A 495      20.327  23.211 108.054  1.00 25.19           N  
ATOM   2027  CA  ILE A 495      21.091  22.613 106.964  1.00 25.71           C  
ATOM   2028  C   ILE A 495      20.317  21.501 106.271  1.00 25.90           C  
ATOM   2029  O   ILE A 495      20.202  21.492 105.046  1.00 25.33           O  
ATOM   2030  CB  ILE A 495      22.445  22.052 107.452  1.00 26.38           C  
ATOM   2031  CG1 ILE A 495      23.388  23.211 107.790  1.00 26.31           C  
ATOM   2032  CG2 ILE A 495      23.057  21.141 106.373  1.00 26.44           C  
ATOM   2033  CD1 ILE A 495      24.762  22.786 108.308  1.00 26.55           C  
ATOM   2034  N   ASP A 496      19.768  20.578 107.051  1.00 26.00           N  
ATOM   2035  CA  ASP A 496      19.036  19.455 106.475  1.00 28.68           C  
ATOM   2036  C   ASP A 496      17.781  19.793 105.686  1.00 28.76           C  
ATOM   2037  O   ASP A 496      17.561  19.241 104.610  1.00 29.19           O  
ATOM   2038  CB  ASP A 496      18.645  18.443 107.558  1.00 29.96           C  
ATOM   2039  CG  ASP A 496      19.825  17.672 108.092  1.00 32.07           C  
ATOM   2040  OD1 ASP A 496      20.918  17.760 107.496  1.00 32.48           O  
ATOM   2041  OD2 ASP A 496      19.653  16.968 109.112  1.00 34.59           O  
ATOM   2042  N   TYR A 497      16.958  20.697 106.204  1.00 28.56           N  
ATOM   2043  CA  TYR A 497      15.705  21.002 105.530  1.00 29.08           C  
ATOM   2044  C   TYR A 497      15.581  22.270 104.717  1.00 27.78           C  
ATOM   2045  O   TYR A 497      14.630  22.415 103.950  1.00 27.25           O  
ATOM   2046  CB  TYR A 497      14.563  20.930 106.539  1.00 32.35           C  
ATOM   2047  CG  TYR A 497      14.444  19.556 107.143  1.00 34.63           C  
ATOM   2048  CD1 TYR A 497      15.076  19.243 108.345  1.00 35.88           C  
ATOM   2049  CD2 TYR A 497      13.745  18.549 106.482  1.00 35.93           C  
ATOM   2050  CE1 TYR A 497      15.012  17.953 108.875  1.00 37.50           C  
ATOM   2051  CE2 TYR A 497      13.679  17.262 106.997  1.00 37.33           C  
ATOM   2052  CZ  TYR A 497      14.312  16.970 108.191  1.00 37.73           C  
ATOM   2053  OH  TYR A 497      14.240  15.690 108.695  1.00 40.16           O  
ATOM   2054  N   ILE A 498      16.524  23.190 104.867  1.00 26.01           N  
ATOM   2055  CA  ILE A 498      16.455  24.422 104.100  1.00 25.90           C  
ATOM   2056  C   ILE A 498      17.644  24.568 103.153  1.00 25.11           C  
ATOM   2057  O   ILE A 498      17.475  24.632 101.931  1.00 25.11           O  
ATOM   2058  CB  ILE A 498      16.384  25.654 105.034  1.00 27.26           C  
ATOM   2059  CG1 ILE A 498      15.127  25.568 105.908  1.00 29.56           C  
ATOM   2060  CG2 ILE A 498      16.348  26.932 104.211  1.00 27.91           C  
ATOM   2061  CD1 ILE A 498      15.059  26.639 106.995  1.00 32.07           C  
ATOM   2062  N   ALA A 499      18.845  24.592 103.717  1.00 23.03           N  
ATOM   2063  CA  ALA A 499      20.054  24.762 102.927  1.00 22.95           C  
ATOM   2064  C   ALA A 499      20.389  23.612 101.974  1.00 23.25           C  
ATOM   2065  O   ALA A 499      20.688  23.846 100.806  1.00 22.89           O  
ATOM   2066  CB  ALA A 499      21.242  25.031 103.854  1.00 22.00           C  
ATOM   2067  N   HIS A 500      20.341  22.370 102.447  1.00 23.84           N  
ATOM   2068  CA  HIS A 500      20.695  21.276 101.554  1.00 24.15           C  
ATOM   2069  C   HIS A 500      19.796  21.103 100.331  1.00 24.07           C  
ATOM   2070  O   HIS A 500      20.289  21.080  99.208  1.00 24.54           O  
ATOM   2071  CB  HIS A 500      20.798  19.940 102.297  1.00 23.98           C  
ATOM   2072  CG  HIS A 500      21.165  18.803 101.395  1.00 23.52           C  
ATOM   2073  ND1 HIS A 500      20.228  17.941 100.865  1.00 24.40           N  
ATOM   2074  CD2 HIS A 500      22.350  18.457 100.838  1.00 23.51           C  
ATOM   2075  CE1 HIS A 500      20.821  17.116 100.018  1.00 24.02           C  
ATOM   2076  NE2 HIS A 500      22.108  17.410  99.983  1.00 23.79           N  
ATOM   2077  N   PRO A 501      18.472  20.984 100.524  1.00 24.01           N  
ATOM   2078  CA  PRO A 501      17.597  20.815  99.361  1.00 23.59           C  
ATOM   2079  C   PRO A 501      17.808  21.892  98.296  1.00 23.65           C  
ATOM   2080  O   PRO A 501      17.741  21.615  97.100  1.00 23.19           O  
ATOM   2081  CB  PRO A 501      16.199  20.876  99.965  1.00 24.08           C  
ATOM   2082  CG  PRO A 501      16.406  20.337 101.348  1.00 24.71           C  
ATOM   2083  CD  PRO A 501      17.686  21.009 101.771  1.00 23.29           C  
ATOM   2084  N   LEU A 502      18.062  23.121  98.739  1.00 22.55           N  
ATOM   2085  CA  LEU A 502      18.278  24.232  97.816  1.00 22.15           C  
ATOM   2086  C   LEU A 502      19.643  24.175  97.129  1.00 21.90           C  
ATOM   2087  O   LEU A 502      19.735  24.249  95.904  1.00 21.06           O  
ATOM   2088  CB  LEU A 502      18.146  25.568  98.559  1.00 21.44           C  
ATOM   2089  CG  LEU A 502      18.518  26.818  97.757  1.00 21.81           C  
ATOM   2090  CD1 LEU A 502      17.523  27.006  96.608  1.00 21.67           C  
ATOM   2091  CD2 LEU A 502      18.516  28.033  98.675  1.00 20.99           C  
ATOM   2092  N   TRP A 503      20.704  24.047  97.916  1.00 22.11           N  
ATOM   2093  CA  TRP A 503      22.039  24.003  97.338  1.00 22.15           C  
ATOM   2094  C   TRP A 503      22.300  22.775  96.474  1.00 22.21           C  
ATOM   2095  O   TRP A 503      23.072  22.843  95.521  1.00 22.42           O  
ATOM   2096  CB  TRP A 503      23.102  24.131  98.434  1.00 22.04           C  
ATOM   2097  CG  TRP A 503      23.281  25.559  98.858  1.00 22.39           C  
ATOM   2098  CD1 TRP A 503      22.849  26.142 100.021  1.00 22.87           C  
ATOM   2099  CD2 TRP A 503      23.857  26.609  98.073  1.00 21.67           C  
ATOM   2100  NE1 TRP A 503      23.119  27.492 100.002  1.00 21.45           N  
ATOM   2101  CE2 TRP A 503      23.738  27.803  98.817  1.00 22.40           C  
ATOM   2102  CE3 TRP A 503      24.463  26.654  96.809  1.00 22.49           C  
ATOM   2103  CZ2 TRP A 503      24.204  29.031  98.338  1.00 21.77           C  
ATOM   2104  CZ3 TRP A 503      24.927  27.877  96.332  1.00 21.77           C  
ATOM   2105  CH2 TRP A 503      24.793  29.048  97.097  1.00 23.19           C  
ATOM   2106  N   GLU A 504      21.663  21.655  96.796  1.00 22.27           N  
ATOM   2107  CA  GLU A 504      21.850  20.450  95.994  1.00 23.20           C  
ATOM   2108  C   GLU A 504      21.252  20.698  94.614  1.00 23.62           C  
ATOM   2109  O   GLU A 504      21.818  20.296  93.598  1.00 23.12           O  
ATOM   2110  CB  GLU A 504      21.150  19.246  96.634  1.00 25.15           C  
ATOM   2111  CG  GLU A 504      21.315  17.953  95.828  1.00 26.65           C  
ATOM   2112  CD  GLU A 504      20.503  16.799  96.388  1.00 28.80           C  
ATOM   2113  OE1 GLU A 504      19.256  16.903  96.417  1.00 29.34           O  
ATOM   2114  OE2 GLU A 504      21.112  15.787  96.799  1.00 29.15           O  
ATOM   2115  N   THR A 505      20.101  21.365  94.586  1.00 23.89           N  
ATOM   2116  CA  THR A 505      19.424  21.665  93.330  1.00 23.21           C  
ATOM   2117  C   THR A 505      20.243  22.639  92.505  1.00 23.52           C  
ATOM   2118  O   THR A 505      20.380  22.468  91.292  1.00 24.10           O  
ATOM   2119  CB  THR A 505      18.017  22.252  93.580  1.00 23.39           C  
ATOM   2120  OG1 THR A 505      17.244  21.310  94.334  1.00 24.42           O  
ATOM   2121  CG2 THR A 505      17.306  22.542  92.252  1.00 23.89           C  
ATOM   2122  N   TRP A 506      20.790  23.661  93.159  1.00 23.56           N  
ATOM   2123  CA  TRP A 506      21.613  24.635  92.458  1.00 23.10           C  
ATOM   2124  C   TRP A 506      22.844  23.924  91.909  1.00 23.60           C  
ATOM   2125  O   TRP A 506      23.277  24.180  90.783  1.00 22.24           O  
ATOM   2126  CB  TRP A 506      22.044  25.768  93.401  1.00 23.22           C  
ATOM   2127  CG  TRP A 506      22.943  26.765  92.729  1.00 22.80           C  
ATOM   2128  CD1 TRP A 506      24.311  26.768  92.727  1.00 23.36           C  
ATOM   2129  CD2 TRP A 506      22.540  27.829  91.859  1.00 22.81           C  
ATOM   2130  NE1 TRP A 506      24.783  27.763  91.903  1.00 22.02           N  
ATOM   2131  CE2 TRP A 506      23.718  28.430  91.358  1.00 23.36           C  
ATOM   2132  CE3 TRP A 506      21.299  28.332  91.451  1.00 24.13           C  
ATOM   2133  CZ2 TRP A 506      23.689  29.510  90.467  1.00 23.33           C  
ATOM   2134  CZ3 TRP A 506      21.270  29.409  90.561  1.00 23.79           C  
ATOM   2135  CH2 TRP A 506      22.460  29.983  90.082  1.00 24.24           C  
ATOM   2136  N   ALA A 507      23.402  23.024  92.714  1.00 23.69           N  
ATOM   2137  CA  ALA A 507      24.586  22.277  92.312  1.00 24.35           C  
ATOM   2138  C   ALA A 507      24.303  21.464  91.051  1.00 24.33           C  
ATOM   2139  O   ALA A 507      25.175  21.322  90.192  1.00 24.97           O  
ATOM   2140  CB  ALA A 507      25.038  21.356  93.446  1.00 24.47           C  
ATOM   2141  N   ASP A 508      23.095  20.918  90.946  1.00 24.71           N  
ATOM   2142  CA  ASP A 508      22.728  20.149  89.761  1.00 24.79           C  
ATOM   2143  C   ASP A 508      22.685  21.069  88.541  1.00 25.09           C  
ATOM   2144  O   ASP A 508      23.103  20.689  87.447  1.00 23.40           O  
ATOM   2145  CB  ASP A 508      21.353  19.500  89.923  1.00 24.76           C  
ATOM   2146  CG  ASP A 508      21.386  18.259  90.789  1.00 25.57           C  
ATOM   2147  OD1 ASP A 508      22.475  17.678  90.974  1.00 26.15           O  
ATOM   2148  OD2 ASP A 508      20.308  17.858  91.272  1.00 27.50           O  
ATOM   2149  N   LEU A 509      22.179  22.283  88.735  1.00 23.75           N  
ATOM   2150  CA  LEU A 509      22.075  23.234  87.632  1.00 23.91           C  
ATOM   2151  C   LEU A 509      23.424  23.585  87.016  1.00 24.23           C  
ATOM   2152  O   LEU A 509      23.545  23.692  85.799  1.00 24.49           O  
ATOM   2153  CB  LEU A 509      21.393  24.532  88.097  1.00 24.26           C  
ATOM   2154  CG  LEU A 509      21.163  25.575  86.992  1.00 25.23           C  
ATOM   2155  CD1 LEU A 509      20.051  25.100  86.074  1.00 25.40           C  
ATOM   2156  CD2 LEU A 509      20.799  26.924  87.606  1.00 25.19           C  
ATOM   2157  N   VAL A 510      24.440  23.749  87.854  1.00 23.79           N  
ATOM   2158  CA  VAL A 510      25.753  24.146  87.365  1.00 24.08           C  
ATOM   2159  C   VAL A 510      26.863  23.107  87.496  1.00 24.04           C  
ATOM   2160  O   VAL A 510      28.038  23.450  87.368  1.00 24.29           O  
ATOM   2161  CB  VAL A 510      26.217  25.438  88.084  1.00 24.02           C  
ATOM   2162  CG1 VAL A 510      25.158  26.525  87.921  1.00 24.54           C  
ATOM   2163  CG2 VAL A 510      26.461  25.161  89.575  1.00 24.02           C  
ATOM   2164  N   HIS A 511      26.505  21.846  87.735  1.00 24.23           N  
ATOM   2165  CA  HIS A 511      27.521  20.809  87.908  1.00 24.91           C  
ATOM   2166  C   HIS A 511      28.596  20.878  86.829  1.00 25.55           C  
ATOM   2167  O   HIS A 511      28.285  20.976  85.639  1.00 26.20           O  
ATOM   2168  CB  HIS A 511      26.886  19.413  87.913  1.00 25.05           C  
ATOM   2169  CG  HIS A 511      27.868  18.321  88.194  1.00 25.91           C  
ATOM   2170  ND1 HIS A 511      28.628  17.728  87.207  1.00 26.26           N  
ATOM   2171  CD2 HIS A 511      28.282  17.778  89.364  1.00 25.08           C  
ATOM   2172  CE1 HIS A 511      29.467  16.869  87.758  1.00 25.42           C  
ATOM   2173  NE2 HIS A 511      29.278  16.881  89.064  1.00 27.00           N  
ATOM   2174  N   PRO A 512      29.874  20.745  87.221  1.00 26.24           N  
ATOM   2175  CA  PRO A 512      30.395  20.525  88.579  1.00 26.18           C  
ATOM   2176  C   PRO A 512      30.810  21.780  89.353  1.00 26.20           C  
ATOM   2177  O   PRO A 512      31.462  21.677  90.392  1.00 25.79           O  
ATOM   2178  CB  PRO A 512      31.596  19.641  88.312  1.00 27.24           C  
ATOM   2179  CG  PRO A 512      32.193  20.356  87.108  1.00 27.50           C  
ATOM   2180  CD  PRO A 512      30.970  20.661  86.235  1.00 26.48           C  
ATOM   2181  N   ASP A 513      30.423  22.952  88.865  1.00 26.57           N  
ATOM   2182  CA  ASP A 513      30.827  24.216  89.483  1.00 28.25           C  
ATOM   2183  C   ASP A 513      30.643  24.419  90.982  1.00 28.16           C  
ATOM   2184  O   ASP A 513      31.502  25.023  91.632  1.00 28.84           O  
ATOM   2185  CB  ASP A 513      30.148  25.388  88.775  1.00 29.66           C  
ATOM   2186  CG  ASP A 513      30.413  25.410  87.287  1.00 32.32           C  
ATOM   2187  OD1 ASP A 513      31.327  24.698  86.821  1.00 32.62           O  
ATOM   2188  OD2 ASP A 513      29.707  26.154  86.582  1.00 34.94           O  
ATOM   2189  N   ALA A 514      29.540  23.930  91.534  1.00 26.39           N  
ATOM   2190  CA  ALA A 514      29.261  24.142  92.951  1.00 25.91           C  
ATOM   2191  C   ALA A 514      29.494  22.979  93.909  1.00 24.88           C  
ATOM   2192  O   ALA A 514      29.085  23.045  95.068  1.00 23.59           O  
ATOM   2193  CB  ALA A 514      27.822  24.648  93.107  1.00 25.27           C  
ATOM   2194  N   GLN A 515      30.150  21.916  93.456  1.00 24.79           N  
ATOM   2195  CA  GLN A 515      30.375  20.782  94.347  1.00 24.96           C  
ATOM   2196  C   GLN A 515      31.154  21.192  95.602  1.00 25.10           C  
ATOM   2197  O   GLN A 515      30.897  20.676  96.688  1.00 26.27           O  
ATOM   2198  CB  GLN A 515      31.114  19.656  93.614  1.00 24.77           C  
ATOM   2199  CG  GLN A 515      31.195  18.351  94.405  1.00 23.70           C  
ATOM   2200  CD  GLN A 515      29.827  17.834  94.847  1.00 22.64           C  
ATOM   2201  OE1 GLN A 515      28.857  17.861  94.084  1.00 23.17           O  
ATOM   2202  NE2 GLN A 515      29.752  17.347  96.079  1.00 22.43           N  
ATOM   2203  N   ASP A 516      32.103  22.115  95.458  1.00 25.74           N  
ATOM   2204  CA  ASP A 516      32.888  22.574  96.603  1.00 26.58           C  
ATOM   2205  C   ASP A 516      31.969  23.124  97.698  1.00 25.85           C  
ATOM   2206  O   ASP A 516      32.226  22.933  98.887  1.00 25.12           O  
ATOM   2207  CB  ASP A 516      33.879  23.670  96.189  1.00 28.53           C  
ATOM   2208  CG  ASP A 516      35.135  23.118  95.542  1.00 31.21           C  
ATOM   2209  OD1 ASP A 516      35.994  23.928  95.135  1.00 32.90           O  
ATOM   2210  OD2 ASP A 516      35.272  21.881  95.442  1.00 33.39           O  
ATOM   2211  N   LEU A 517      30.905  23.812  97.291  1.00 24.95           N  
ATOM   2212  CA  LEU A 517      29.954  24.373  98.249  1.00 24.50           C  
ATOM   2213  C   LEU A 517      29.231  23.274  99.018  1.00 23.73           C  
ATOM   2214  O   LEU A 517      29.005  23.394 100.229  1.00 22.25           O  
ATOM   2215  CB  LEU A 517      28.938  25.269  97.530  1.00 24.79           C  
ATOM   2216  CG  LEU A 517      29.369  26.720  97.269  1.00 25.82           C  
ATOM   2217  CD1 LEU A 517      30.721  26.767  96.572  1.00 25.79           C  
ATOM   2218  CD2 LEU A 517      28.300  27.405  96.426  1.00 25.34           C  
ATOM   2219  N   LEU A 518      28.859  22.206  98.317  1.00 23.14           N  
ATOM   2220  CA  LEU A 518      28.189  21.086  98.967  1.00 24.38           C  
ATOM   2221  C   LEU A 518      29.161  20.397  99.922  1.00 24.37           C  
ATOM   2222  O   LEU A 518      28.777  19.997 101.025  1.00 24.39           O  
ATOM   2223  CB  LEU A 518      27.682  20.075  97.932  1.00 24.94           C  
ATOM   2224  CG  LEU A 518      26.512  20.497  97.043  1.00 25.97           C  
ATOM   2225  CD1 LEU A 518      26.110  19.327  96.145  1.00 26.28           C  
ATOM   2226  CD2 LEU A 518      25.330  20.932  97.910  1.00 26.35           C  
ATOM   2227  N   ASP A 519      30.418  20.262  99.501  1.00 24.94           N  
ATOM   2228  CA  ASP A 519      31.429  19.624 100.347  1.00 25.49           C  
ATOM   2229  C   ASP A 519      31.602  20.432 101.628  1.00 25.64           C  
ATOM   2230  O   ASP A 519      31.750  19.868 102.712  1.00 24.93           O  
ATOM   2231  CB  ASP A 519      32.780  19.523  99.626  1.00 25.60           C  
ATOM   2232  CG  ASP A 519      32.750  18.565  98.442  1.00 26.12           C  
ATOM   2233  OD1 ASP A 519      31.809  17.748  98.341  1.00 25.85           O  
ATOM   2234  OD2 ASP A 519      33.685  18.627  97.615  1.00 27.29           O  
ATOM   2235  N   THR A 520      31.584  21.758 101.504  1.00 25.36           N  
ATOM   2236  CA  THR A 520      31.725  22.616 102.674  1.00 25.05           C  
ATOM   2237  C   THR A 520      30.475  22.487 103.540  1.00 25.38           C  
ATOM   2238  O   THR A 520      30.566  22.406 104.768  1.00 24.80           O  
ATOM   2239  CB  THR A 520      31.928  24.092 102.273  1.00 25.27           C  
ATOM   2240  OG1 THR A 520      33.182  24.227 101.597  1.00 25.96           O  
ATOM   2241  CG2 THR A 520      31.928  24.996 103.511  1.00 25.70           C  
ATOM   2242  N   LEU A 521      29.309  22.472 102.899  1.00 24.87           N  
ATOM   2243  CA  LEU A 521      28.046  22.325 103.617  1.00 24.51           C  
ATOM   2244  C   LEU A 521      28.096  21.016 104.409  1.00 24.70           C  
ATOM   2245  O   LEU A 521      27.741  20.975 105.593  1.00 23.84           O  
ATOM   2246  CB  LEU A 521      26.872  22.299 102.624  1.00 25.29           C  
ATOM   2247  CG  LEU A 521      25.444  22.178 103.169  1.00 26.62           C  
ATOM   2248  CD1 LEU A 521      25.139  23.348 104.088  1.00 26.97           C  
ATOM   2249  CD2 LEU A 521      24.453  22.160 102.014  1.00 27.49           C  
ATOM   2250  N   GLU A 522      28.550  19.949 103.754  1.00 25.24           N  
ATOM   2251  CA  GLU A 522      28.655  18.646 104.405  1.00 25.99           C  
ATOM   2252  C   GLU A 522      29.589  18.725 105.608  1.00 25.81           C  
ATOM   2253  O   GLU A 522      29.298  18.152 106.658  1.00 26.63           O  
ATOM   2254  CB  GLU A 522      29.152  17.579 103.415  1.00 26.23           C  
ATOM   2255  CG  GLU A 522      29.386  16.201 104.047  1.00 27.77           C  
ATOM   2256  CD  GLU A 522      29.679  15.113 103.019  1.00 28.60           C  
ATOM   2257  OE1 GLU A 522      30.300  15.426 101.981  1.00 29.31           O  
ATOM   2258  OE2 GLU A 522      29.303  13.940 103.254  1.00 29.31           O  
ATOM   2259  N   ASP A 523      30.709  19.432 105.463  1.00 26.51           N  
ATOM   2260  CA  ASP A 523      31.646  19.584 106.574  1.00 26.74           C  
ATOM   2261  C   ASP A 523      30.982  20.317 107.740  1.00 27.08           C  
ATOM   2262  O   ASP A 523      31.101  19.905 108.897  1.00 26.25           O  
ATOM   2263  CB  ASP A 523      32.896  20.359 106.144  1.00 28.27           C  
ATOM   2264  CG  ASP A 523      33.828  19.532 105.280  1.00 30.90           C  
ATOM   2265  OD1 ASP A 523      33.753  18.285 105.350  1.00 32.49           O  
ATOM   2266  OD2 ASP A 523      34.643  20.128 104.543  1.00 31.24           O  
ATOM   2267  N   ASN A 524      30.276  21.402 107.433  1.00 26.28           N  
ATOM   2268  CA  ASN A 524      29.606  22.175 108.476  1.00 27.44           C  
ATOM   2269  C   ASN A 524      28.458  21.418 109.146  1.00 27.74           C  
ATOM   2270  O   ASN A 524      28.053  21.769 110.254  1.00 28.34           O  
ATOM   2271  CB  ASN A 524      29.083  23.501 107.909  1.00 26.94           C  
ATOM   2272  CG  ASN A 524      30.193  24.401 107.414  1.00 27.87           C  
ATOM   2273  OD1 ASN A 524      31.356  24.248 107.806  1.00 28.74           O  
ATOM   2274  ND2 ASN A 524      29.844  25.356 106.560  1.00 26.50           N  
ATOM   2275  N   ARG A 525      27.946  20.389 108.473  1.00 28.83           N  
ATOM   2276  CA  ARG A 525      26.845  19.560 108.976  1.00 30.94           C  
ATOM   2277  C   ARG A 525      27.329  18.452 109.924  1.00 32.38           C  
ATOM   2278  O   ARG A 525      26.525  17.764 110.553  1.00 32.05           O  
ATOM   2279  CB  ARG A 525      26.084  18.939 107.791  1.00 30.95           C  
ATOM   2280  CG  ARG A 525      24.987  17.932 108.156  1.00 32.88           C  
ATOM   2281  CD  ARG A 525      23.879  18.574 108.997  1.00 34.21           C  
ATOM   2282  NE  ARG A 525      22.793  17.643 109.298  1.00 34.40           N  
ATOM   2283  CZ  ARG A 525      22.889  16.614 110.139  1.00 35.41           C  
ATOM   2284  NH1 ARG A 525      24.026  16.373 110.779  1.00 34.97           N  
ATOM   2285  NH2 ARG A 525      21.843  15.823 110.342  1.00 35.39           N  
ATOM   2286  N   GLU A 526      28.643  18.279 110.020  1.00 34.32           N  
ATOM   2287  CA  GLU A 526      29.224  17.268 110.906  1.00 36.58           C  
ATOM   2288  C   GLU A 526      29.424  17.869 112.295  1.00 36.36           C  
ATOM   2289  O   GLU A 526      30.474  18.435 112.584  1.00 35.77           O  
ATOM   2290  CB  GLU A 526      30.569  16.787 110.346  1.00 38.72           C  
ATOM   2291  CG  GLU A 526      30.438  15.802 109.202  1.00 43.29           C  
ATOM   2292  CD  GLU A 526      30.062  14.404 109.673  1.00 45.70           C  
ATOM   2293  OE1 GLU A 526      29.136  14.270 110.503  1.00 47.71           O  
ATOM   2294  OE2 GLU A 526      30.692  13.434 109.202  1.00 48.02           O  
ATOM   2295  N   TRP A 527      28.406  17.736 113.143  1.00 37.22           N  
ATOM   2296  CA  TRP A 527      28.419  18.275 114.505  1.00 38.50           C  
ATOM   2297  C   TRP A 527      29.638  17.853 115.332  1.00 40.91           C  
ATOM   2298  O   TRP A 527      30.173  18.641 116.112  1.00 40.37           O  
ATOM   2299  CB  TRP A 527      27.163  17.831 115.263  1.00 35.85           C  
ATOM   2300  CG  TRP A 527      25.861  17.971 114.524  1.00 34.54           C  
ATOM   2301  CD1 TRP A 527      24.820  17.086 114.544  1.00 34.64           C  
ATOM   2302  CD2 TRP A 527      25.429  19.076 113.713  1.00 34.29           C  
ATOM   2303  NE1 TRP A 527      23.770  17.568 113.803  1.00 34.36           N  
ATOM   2304  CE2 TRP A 527      24.114  18.786 113.281  1.00 34.02           C  
ATOM   2305  CE3 TRP A 527      26.023  20.281 113.312  1.00 34.12           C  
ATOM   2306  CZ2 TRP A 527      23.380  19.659 112.467  1.00 34.49           C  
ATOM   2307  CZ3 TRP A 527      25.290  21.150 112.500  1.00 33.79           C  
ATOM   2308  CH2 TRP A 527      23.983  20.831 112.088  1.00 33.14           C  
ATOM   2309  N   TYR A 528      30.061  16.605 115.169  1.00 44.07           N  
ATOM   2310  CA  TYR A 528      31.191  16.073 115.923  1.00 47.93           C  
ATOM   2311  C   TYR A 528      32.529  16.128 115.195  1.00 50.70           C  
ATOM   2312  O   TYR A 528      33.490  15.475 115.604  1.00 51.42           O  
ATOM   2313  CB  TYR A 528      30.886  14.634 116.343  1.00 48.04           C  
ATOM   2314  CG  TYR A 528      29.843  14.545 117.432  1.00 48.47           C  
ATOM   2315  CD1 TYR A 528      30.196  14.701 118.772  1.00 48.54           C  
ATOM   2316  CD2 TYR A 528      28.496  14.352 117.121  1.00 48.57           C  
ATOM   2317  CE1 TYR A 528      29.233  14.668 119.779  1.00 48.81           C  
ATOM   2318  CE2 TYR A 528      27.523  14.319 118.121  1.00 48.80           C  
ATOM   2319  CZ  TYR A 528      27.900  14.479 119.447  1.00 48.95           C  
ATOM   2320  OH  TYR A 528      26.949  14.461 120.439  1.00 49.11           O  
ATOM   2321  N   GLN A 529      32.594  16.913 114.125  1.00 53.33           N  
ATOM   2322  CA  GLN A 529      33.829  17.047 113.361  1.00 56.19           C  
ATOM   2323  C   GLN A 529      34.482  18.394 113.656  1.00 57.03           C  
ATOM   2324  O   GLN A 529      33.812  19.245 114.277  1.00 58.06           O  
ATOM   2325  CB  GLN A 529      33.533  16.928 111.862  1.00 57.71           C  
ATOM   2326  CG  GLN A 529      34.761  16.971 110.966  1.00 60.00           C  
ATOM   2327  CD  GLN A 529      35.673  15.771 111.155  1.00 61.65           C  
ATOM   2328  OE1 GLN A 529      36.731  15.679 110.528  1.00 62.63           O  
ATOM   2329  NE2 GLN A 529      35.267  14.842 112.017  1.00 62.15           N  
TER    2330      GLN A 529                                                      
HETATM 2331 ZN    ZN A   1      18.934  38.639 103.595  1.00 25.23          ZN  
HETATM 2332 MG    MG A   2      15.378  39.510 103.892  1.00 24.34          MG  
HETATM 2333  O   HOH A 558      16.978  38.211 103.024  1.00 20.89           O  
HETATM 2334  O   HOH A 559      18.513  37.164 105.334  1.00 21.85           O  
HETATM 2335  O   HOH A 560      15.556  38.552 105.922  1.00 17.67           O  
HETATM 2336  O   HOH A 561      13.794  37.927 103.405  1.00 21.51           O  
HETATM 2337  O   HOH A 562      13.523  40.706 104.753  1.00 17.48           O  
HETATM 2338  O   HOH A 563      14.956  40.507 101.853  1.00 18.87           O  
HETATM 2339  O   HOH A 564      30.506  34.904 104.176  1.00 22.35           O  
HETATM 2340  O   HOH A 565      16.054  34.314 100.826  1.00 23.63           O  
HETATM 2341  O   HOH A 566      27.803  21.777  91.047  1.00 21.73           O  
HETATM 2342  O   HOH A 567      25.412  37.049 105.644  1.00 19.14           O  
HETATM 2343  O   HOH A 568      27.315  33.796 103.211  1.00 25.41           O  
HETATM 2344  O   HOH A 569      19.553  15.443  91.641  1.00 28.76           O  
HETATM 2345  O   HOH A 570      25.560  40.817 109.642  1.00 22.80           O  
HETATM 2346  O   HOH A 571      18.767  46.768 109.187  1.00 25.94           O  
HETATM 2347  O   HOH A 572      23.665  15.979  97.928  1.00 26.04           O  
HETATM 2348  O   HOH A 573      20.090  34.977 105.285  1.00 23.13           O  
HETATM 2349  O   HOH A 574       9.576  48.719  85.968  1.00 27.90           O  
HETATM 2350  O   HOH A 575      14.341  53.971  76.521  1.00 27.03           O  
HETATM 2351  O   HOH A 576      13.890  23.344 101.460  1.00 27.89           O  
HETATM 2352  O   HOH A 577      27.820  19.144  91.914  1.00 24.87           O  
HETATM 2353  O   HOH A 578      31.130  37.785 101.665  1.00 26.91           O  
HETATM 2354  O   HOH A 579      24.560  48.140 109.213  1.00 25.54           O  
HETATM 2355  O   HOH A 580      28.528  30.457 116.517  1.00 26.31           O  
HETATM 2356  O   HOH A 581      22.793  32.473 104.611  1.00 26.33           O  
HETATM 2357  O   HOH A 582      29.536  33.141  84.515  1.00 25.69           O  
HETATM 2358  O   HOH A 583      29.894  37.142 119.976  1.00 27.52           O  
HETATM 2359  O   HOH A 584      27.935  31.715 118.886  1.00 28.48           O  
HETATM 2360  O   HOH A 585      12.049  35.838 104.813  1.00 25.91           O  
HETATM 2361  O   HOH A 586      29.609  16.904  99.772  1.00 28.80           O  
HETATM 2362  O   HOH A 587       5.667  47.112 101.894  1.00 33.10           O  
HETATM 2363  O   HOH A 588      32.598  26.329 100.059  1.00 30.64           O  
HETATM 2364  O   HOH A 589      13.329  38.580 107.490  1.00 30.30           O  
HETATM 2365  O   HOH A 590      30.215  41.611  84.194  1.00 34.78           O  
HETATM 2366  O   HOH A 591      28.788  19.009  83.320  1.00 35.42           O  
HETATM 2367  O   HOH A 592      28.037  28.059  91.420  1.00 33.66           O  
HETATM 2368  O   HOH A 593      30.161  38.268 113.948  1.00 33.01           O  
HETATM 2369  O   HOH A 594      23.896  55.426  85.150  1.00 28.68           O  
HETATM 2370  O   HOH A 595      17.937  51.099  75.718  1.00 38.07           O  
HETATM 2371  O   HOH A 596      34.234  50.690  85.615  1.00 39.80           O  
HETATM 2372  O   HOH A 597      32.845  38.505 113.720  1.00 31.72           O  
HETATM 2373  O   HOH A 598      34.440  34.514  90.892  1.00 29.88           O  
HETATM 2374  O   HOH A 599      15.737  57.175  77.668  1.00 38.55           O  
HETATM 2375  O   HOH A 600      15.291  40.786 116.475  1.00 31.44           O  
HETATM 2376  O   HOH A 601      34.022  16.151  96.282  1.00 44.74           O  
HETATM 2377  O   HOH A 602      24.426  50.938 109.024  1.00 31.75           O  
HETATM 2378  O   HOH A 603      21.600  62.004  90.886  1.00 35.21           O  
HETATM 2379  O   HOH A 604       6.572  29.007  98.508  1.00 30.42           O  
HETATM 2380  O   HOH A 605      13.340  22.822 110.312  1.00 39.44           O  
HETATM 2381  O   HOH A 606       8.008  38.903 104.380  1.00 41.19           O  
HETATM 2382  O   HOH A 607      29.532  36.954  85.284  1.00 38.84           O  
HETATM 2383  O   HOH A 608      30.477  45.819  82.661  1.00 35.10           O  
HETATM 2384  O   HOH A 609      20.571  46.849  78.178  1.00 39.27           O  
HETATM 2385  O   HOH A 610      27.134  54.869 105.817  1.00 37.28           O  
HETATM 2386  O   HOH A 611      27.813  46.739 108.975  1.00 39.49           O  
HETATM 2387  O   HOH A 612      26.687  35.529  82.501  1.00 32.63           O  
HETATM 2388  O   HOH A 613      19.320  18.029 111.772  1.00 41.94           O  
HETATM 2389  O   HOH A 614      12.044  47.832  79.002  1.00 31.74           O  
HETATM 2390  O   HOH A 615      33.081  23.571  93.233  1.00 40.77           O  
HETATM 2391  O   HOH A 616      19.187  42.958  79.509  1.00 33.60           O  
HETATM 2392  O   HOH A 617      21.824  34.345  77.197  1.00 38.96           O  
HETATM 2393  O   HOH A 618      18.695  61.615  92.715  1.00 36.27           O  
HETATM 2394  O   HOH A 619      23.882  51.105  78.437  1.00 36.23           O  
HETATM 2395  O   HOH A 620       9.313  22.915  96.939  1.00 37.62           O  
HETATM 2396  O   HOH A 621      12.663  32.480  98.939  1.00 26.58           O  
HETATM 2397  O   HOH A 622      26.967  36.255  84.876  1.00 33.62           O  
HETATM 2398  O   HOH A 623       7.307  50.894 102.426  1.00 34.22           O  
HETATM 2399  O   HOH A 624      30.726  28.834 117.635  1.00 43.37           O  
HETATM 2400  O   HOH A 625       8.564  28.555 101.567  1.00 31.91           O  
HETATM 2401  O   HOH A 626      32.710  17.094 102.344  1.00 35.14           O  
HETATM 2402  O   HOH A 627      27.258  40.321  80.279  1.00 39.24           O  
HETATM 2403  O   HOH A 628      30.737  24.315  84.177  1.00 44.10           O  
HETATM 2404  O   HOH A 629      14.947  35.854 105.658  1.00 50.24           O  
HETATM 2405  O   HOH A 630      12.979  49.335 110.468  1.00 45.55           O  
HETATM 2406  O   HOH A 631      11.128  48.925  71.554  1.00 44.82           O  
HETATM 2407  O   HOH A 632      35.763  20.207  98.265  1.00 42.63           O  
HETATM 2408  O   HOH A 633      29.286  14.298 113.217  1.00 51.35           O  
HETATM 2409  O   HOH A 634      27.808  15.606 107.092  1.00 36.78           O  
HETATM 2410  O   HOH A 635      33.861  42.754 111.472  1.00 38.50           O  
HETATM 2411  O   HOH A 636      24.256  63.051  90.028  1.00 40.31           O  
HETATM 2412  O   HOH A 637      33.724  23.901 106.882  1.00 40.18           O  
HETATM 2413  O   HOH A 638      21.458  31.706  77.030  1.00 39.81           O  
HETATM 2414  O   HOH A 639      35.027  22.590  99.747  1.00 38.11           O  
HETATM 2415  O   HOH A 640      15.801  29.187  77.913  1.00 47.03           O  
HETATM 2416  O   HOH A 641      17.943  57.933  83.833  1.00 41.39           O  
HETATM 2417  O   HOH A 642      20.734  64.742  92.200  1.00 40.86           O  
HETATM 2418  O   HOH A 643      25.316  42.932  77.978  1.00 39.58           O  
HETATM 2419  O   HOH A 644      22.434  52.050 112.344  1.00 44.90           O  
HETATM 2420  O   HOH A 645      10.905  38.242 105.606  1.00 39.16           O  
HETATM 2421  O   HOH A 646      44.028  38.235 101.011  1.00 54.94           O  
HETATM 2422  O   HOH A 647      17.550  14.987 108.904  1.00 48.99           O  
HETATM 2423  O   HOH A 648      36.599  37.946 112.271  1.00 40.52           O  
HETATM 2424  O   HOH A 649      39.555  37.318 102.485  1.00 39.69           O  
HETATM 2425  O   HOH A 650      16.145  59.301  88.928  1.00 45.43           O  
HETATM 2426  O   HOH A 651      37.842  32.093 104.180  1.00 44.66           O  
HETATM 2427  O   HOH A 652      18.540  61.300  87.695  1.00 34.36           O  
HETATM 2428  O   HOH A 653      17.010  17.071  97.910  1.00 40.22           O  
HETATM 2429  O   HOH A 654      41.776  36.959 105.691  1.00 50.59           O  
HETATM 2430  O   HOH A 655      32.211  35.013 101.402  1.00 43.89           O  
HETATM 2431  O   HOH A 656      19.698  42.124 116.722  1.00 29.78           O  
HETATM 2432  O   HOH A 657      22.955  45.037  79.020  1.00 33.37           O  
HETATM 2433  O   HOH A 658      14.388  35.666 108.619  1.00 43.86           O  
HETATM 2434  O   HOH A 659      12.608  21.086 100.350  1.00 31.04           O  
HETATM 2435  O   HOH A 660      10.449  54.592 103.829  1.00 46.75           O  
HETATM 2436  O   HOH A 661      17.168  42.858 116.254  1.00 33.01           O  
HETATM 2437  O   HOH A 662      34.401  27.106  98.327  1.00 36.72           O  
HETATM 2438  O   HOH A 663      37.623  31.493 106.882  1.00 42.47           O  
HETATM 2439  O   HOH A 664      17.672  16.996 101.148  1.00 43.10           O  
HETATM 2440  O   HOH A 665      10.647  21.157  95.552  1.00 37.21           O  
HETATM 2441  O   HOH A 666      21.210  16.528 113.288  1.00 41.76           O  
HETATM 2442  O   HOH A 667      35.829  30.792  95.002  1.00 41.30           O  
HETATM 2443  O   HOH A 668      16.595  48.864 114.911  1.00 47.88           O  
HETATM 2444  O   HOH A 669      16.930  25.160  82.166  1.00 45.58           O  
HETATM 2445  O   HOH A 670      32.297  31.801  90.367  1.00 41.56           O  
HETATM 2446  O   HOH A 671      32.362  28.458  80.995  1.00 42.69           O  
HETATM 2447  O   HOH A 672      26.737  45.936 113.209  1.00 45.57           O  
HETATM 2448  O   HOH A 673      26.029  21.944  84.116  1.00 41.97           O  
HETATM 2449  O   HOH A 674      23.083  63.736  99.010  1.00 48.61           O  
HETATM 2450  O   HOH A 675      35.793  52.666  86.881  1.00 46.10           O  
HETATM 2451  O   HOH A 676       9.697  20.991  90.474  1.00 41.09           O  
HETATM 2452  O   HOH A 677      16.221  17.244 103.463  1.00 42.40           O  
HETATM 2453  O   HOH A 678      29.986  35.847  81.494  1.00 49.84           O  
HETATM 2454  O   HOH A 679      26.613  53.287 108.095  1.00 47.05           O  
HETATM 2455  O   HOH A 680      14.374  42.209  81.897  1.00 42.97           O  
HETATM 2456  O   HOH A 681      32.062  21.831  78.920  1.00 49.91           O  
HETATM 2457  O   HOH A 682      22.754  31.232 107.802  1.00 38.97           O  
HETATM 2458  O   HOH A 683      25.703  59.743 101.258  1.00 41.33           O  
HETATM 2459  O   HOH A 684      13.037  20.301 103.015  1.00 47.47           O  
CONECT  697 2331                                                                
CONECT  957 2331                                                                
CONECT  964 2332                                                                
CONECT  965 2331                                                                
CONECT 1776 2331                                                                
CONECT 2331  697  957  965 1776                                                 
CONECT 2331 2333 2334                                                           
CONECT 2332  964 2333 2335 2336                                                 
CONECT 2332 2337 2338                                                           
CONECT 2333 2331 2332                                                           
CONECT 2334 2331                                                                
CONECT 2335 2332                                                                
CONECT 2336 2332                                                                
CONECT 2337 2332                                                                
CONECT 2338 2332                                                                
MASTER      381    0    2   21    0    0    4    6 2458    1   15   28          
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.