CNRS Nantes University UFIP UFIP
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***  macro  ***

elNémo ID: 22120517321042468

Job options:

ID        	=	 22120517321042468
JOBID     	=	 macro
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 macro

HEADER    TRANSFERASE                             17-JUN-02   1M17              
TITLE     EPIDERMAL GROWTH FACTOR RECEPTOR TYROSINE KINASE DOMAIN               
TITLE    2 WITH 4-ANILINOQUINAZOLINE INHIBITOR ERLOTINIB                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: TYROSINE KINASE DOMAIN (RESIDUES 671-998);                 
COMPND   5 SYNONYM: RECEPTOR PROTEIN-TYROSINE KINASE ERBB-1;                    
COMPND   6 EC: 2.7.1.112;                                                       
COMPND   7 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: EGFR;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: AUTOGRAPHICA                               
SOURCE  10 CALIFORNICA/T.NICOPLUSIA;                                            
SOURCE  11 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PVL1392                                   
KEYWDS    TRANSFERASE, TYROSINE KINASE DOMAIN                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.STAMOS,M.X.SLIWKOWSKI,C.EIGENBROT                                   
REVDAT   3   24-FEB-09 1M17    1       VERSN                                    
REVDAT   2   25-FEB-03 1M17    1       JRNL                                     
REVDAT   1   04-SEP-02 1M17    0                                                
JRNL        AUTH   J.STAMOS,M.X.SLIWKOWSKI,C.EIGENBROT                          
JRNL        TITL   STRUCTURE OF THE EPIDERMAL GROWTH FACTOR RECEPTOR            
JRNL        TITL 2 KINASE DOMAIN ALONE AND IN COMPLEX WITH A                    
JRNL        TITL 3 4-ANILINOQUINAZOLINE INHIBITOR.                              
JRNL        REF    J.BIOL.CHEM.                  V. 277 46265 2002              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   12196540                                                     
JRNL        DOI    10.1074/JBC.M207135200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 98.1                                          
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.200                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 16628                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.251                           
REMARK   3   FREE R VALUE                     : 0.295                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 689                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.011                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.69                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1560                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5850                       
REMARK   3   BIN FREE R VALUE                    : 0.5770                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 53                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.059                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2511                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 20                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 88.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 9.70000                                              
REMARK   3    B22 (A**2) : 9.70000                                              
REMARK   3    B33 (A**2) : 9.70000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.36                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.33                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.41                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.41                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.81                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 4.850 ; 2.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 7.220 ; 3.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 10.250; 4.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 13.670; 6.000                
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  : MSI_XPLOR_PARHCSDX.PRO                         
REMARK   3  PARAMETER FILE  2  : TAR.PAR                                        
REMARK   3  PARAMETER FILE  3  : PARWAT.PRO                                     
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : MSI_XPLOR_TOPHCSDX.PRO                         
REMARK   3  TOPOLOGY FILE  2   : TAR.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : TOPWAT.PRO                                     
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 1M17 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016470.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-NOV-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : CURVED CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16628                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.000                             
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : 0.09300                            
REMARK 200   FOR THE DATA SET  : 27.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.50                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.99000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.99000                            
REMARK 200   FOR SHELL         : 2.800                              
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: PDB ENTRY 1FGK; POLY ALANINE                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TARTRATE, PH 7.0, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 292K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      14555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      15555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      16555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      18555   Z+1/2,-X+1/2,-Y+1/2                                     
REMARK 290      19555   -Z+1/2,-X+1/2,Y+1/2                                     
REMARK 290      20555   -Z+1/2,X+1/2,-Y+1/2                                     
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      22555   -Y+1/2,Z+1/2,-X+1/2                                     
REMARK 290      23555   Y+1/2,-Z+1/2,-X+1/2                                     
REMARK 290      24555   -Y+1/2,-Z+1/2,X+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       73.90000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       73.90000            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       73.90000            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       73.90000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       73.90000            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       73.90000            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       73.90000            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       73.90000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       73.90000            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       73.90000            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       73.90000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       73.90000            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       73.90000            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       73.90000            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       73.90000            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       73.90000            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       73.90000            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       73.90000            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       73.90000            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       73.90000            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       73.90000            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       73.90000            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       73.90000            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       73.90000            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       73.90000            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       73.90000            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       73.90000            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       73.90000            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       73.90000            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       73.90000            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       73.90000            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       73.90000            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       73.90000            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       73.90000            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       73.90000            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       73.90000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   666                                                      
REMARK 465     SER A   667                                                      
REMARK 465     HIS A   668                                                      
REMARK 465     MET A   669                                                      
REMARK 465     ALA A   670                                                      
REMARK 465     SER A   671                                                      
REMARK 465     LEU A   965                                                      
REMARK 465     PRO A   966                                                      
REMARK 465     SER A   967                                                      
REMARK 465     PRO A   968                                                      
REMARK 465     THR A   969                                                      
REMARK 465     ASP A   970                                                      
REMARK 465     SER A   971                                                      
REMARK 465     ASN A   972                                                      
REMARK 465     PHE A   973                                                      
REMARK 465     TYR A   974                                                      
REMARK 465     ARG A   975                                                      
REMARK 465     ALA A   976                                                      
REMARK 465     GLN A   996                                                      
REMARK 465     GLN A   997                                                      
REMARK 465     GLY A   998                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     GLU A  725                                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A  730   CG    CD    CE    NZ                                
REMARK 480     GLU A  961   CB    CG    CD    OE1   OE2                         
REMARK 480     ARG A  962   CB    CG    CD    NE    CZ    NH1   NH2             
REMARK 480     MET A  963   CB    CG    SD    CE                                
REMARK 480     MET A  978   CB    CG    SD    CE                                
REMARK 480     ILE A  994   CB    CG1   CG2   CD1                               
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    ILE A 691      -25.30   -142.93                                   
REMARK 500    LYS A 692      142.35   -174.91                                   
REMARK 500    SER A 696       64.50   -113.56                                   
REMARK 500    PHE A 699      -18.20   -164.03                                   
REMARK 500    GLU A 712     -179.24    -59.98                                   
REMARK 500    THR A 759     -148.11   -104.25                                   
REMARK 500    ASP A 783        2.15    -69.42                                   
REMARK 500    HIS A 811      -70.63    -22.63                                   
REMARK 500    ASP A 813       49.55   -155.75                                   
REMARK 500    ASP A 831       80.70     54.04                                   
REMARK 500    GLU A 848      -89.90   -131.32                                   
REMARK 500    LYS A 851       19.04   -142.06                                   
REMARK 500    ASP A 892      -38.02    -39.93                                   
REMARK 500    ILE A 894      130.75    -26.87                                   
REMARK 500    ALA A 896      -33.42    -36.08                                   
REMARK 500    GLU A 961      -95.66    171.34                                   
REMARK 500    ARG A 962      -41.08   -139.59                                   
REMARK 500    MET A 963       53.16     72.86                                   
REMARK 500    MET A 978      101.51    -50.90                                   
REMARK 500    ASP A 982       65.59   -103.83                                   
REMARK 500    ILE A 994       99.42    -19.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    HIS A 811        -14.02                                           
REMARK 500    ARG A 812        -10.68                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AQ4 A 999                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1M14   RELATED DB: PDB                                   
REMARK 900 APO-FORM EPIDERMAL GROWTH FACTOR RECEPTOR KINASE DOMAIN              
DBREF  1M17 A  671   998  UNP    P00533   EGFR_HUMAN     695   1022             
SEQADV 1M17 GLY A  666  UNP  P00533              CLONING ARTIFACT               
SEQADV 1M17 SER A  667  UNP  P00533              CLONING ARTIFACT               
SEQADV 1M17 HIS A  668  UNP  P00533              CLONING ARTIFACT               
SEQADV 1M17 MET A  669  UNP  P00533              CLONING ARTIFACT               
SEQADV 1M17 ALA A  670  UNP  P00533              CLONING ARTIFACT               
SEQRES   1 A  333  GLY SER HIS MET ALA SER GLY GLU ALA PRO ASN GLN ALA          
SEQRES   2 A  333  LEU LEU ARG ILE LEU LYS GLU THR GLU PHE LYS LYS ILE          
SEQRES   3 A  333  LYS VAL LEU GLY SER GLY ALA PHE GLY THR VAL TYR LYS          
SEQRES   4 A  333  GLY LEU TRP ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO          
SEQRES   5 A  333  VAL ALA ILE LYS GLU LEU ARG GLU ALA THR SER PRO LYS          
SEQRES   6 A  333  ALA ASN LYS GLU ILE LEU ASP GLU ALA TYR VAL MET ALA          
SEQRES   7 A  333  SER VAL ASP ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE          
SEQRES   8 A  333  CYS LEU THR SER THR VAL GLN LEU ILE THR GLN LEU MET          
SEQRES   9 A  333  PRO PHE GLY CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS          
SEQRES  10 A  333  ASP ASN ILE GLY SER GLN TYR LEU LEU ASN TRP CYS VAL          
SEQRES  11 A  333  GLN ILE ALA LYS GLY MET ASN TYR LEU GLU ASP ARG ARG          
SEQRES  12 A  333  LEU VAL HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL          
SEQRES  13 A  333  LYS THR PRO GLN HIS VAL LYS ILE THR ASP PHE GLY LEU          
SEQRES  14 A  333  ALA LYS LEU LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA          
SEQRES  15 A  333  GLU GLY GLY LYS VAL PRO ILE LYS TRP MET ALA LEU GLU          
SEQRES  16 A  333  SER ILE LEU HIS ARG ILE TYR THR HIS GLN SER ASP VAL          
SEQRES  17 A  333  TRP SER TYR GLY VAL THR VAL TRP GLU LEU MET THR PHE          
SEQRES  18 A  333  GLY SER LYS PRO TYR ASP GLY ILE PRO ALA SER GLU ILE          
SEQRES  19 A  333  SER SER ILE LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO          
SEQRES  20 A  333  PRO ILE CYS THR ILE ASP VAL TYR MET ILE MET VAL LYS          
SEQRES  21 A  333  CYS TRP MET ILE ASP ALA ASP SER ARG PRO LYS PHE ARG          
SEQRES  22 A  333  GLU LEU ILE ILE GLU PHE SER LYS MET ALA ARG ASP PRO          
SEQRES  23 A  333  GLN ARG TYR LEU VAL ILE GLN GLY ASP GLU ARG MET HIS          
SEQRES  24 A  333  LEU PRO SER PRO THR ASP SER ASN PHE TYR ARG ALA LEU          
SEQRES  25 A  333  MET ASP GLU GLU ASP MET ASP ASP VAL VAL ASP ALA ASP          
SEQRES  26 A  333  GLU TYR LEU ILE PRO GLN GLN GLY                              
HET    AQ4  A 999      29                                                       
HETNAM     AQ4 [6,7-BIS(2-METHOXY-ETHOXY)QUINAZOLINE-4-YL]-(3-                  
HETNAM   2 AQ4  ETHYNYLPHENYL)AMINE                                             
HETSYN     AQ4 ERLOTINIB                                                        
FORMUL   2  AQ4    C22 H23 N3 O4                                                
FORMUL   3  HOH   *20(H2 O)                                                     
HELIX    1   1 LYS A  684  THR A  686  5                                   3    
HELIX    2   2 SER A  728  ALA A  743  1                                  16    
HELIX    3   3 CYS A  773  GLU A  780  1                                   8    
HELIX    4   4 HIS A  781  ILE A  785  5                                   5    
HELIX    5   5 GLY A  786  ARG A  807  1                                  22    
HELIX    6   6 ALA A  815  ARG A  817  5                                   3    
HELIX    7   7 PRO A  853  MET A  857  5                                   5    
HELIX    8   8 ALA A  858  ARG A  865  1                                   8    
HELIX    9   9 THR A  868  THR A  885  1                                  18    
HELIX   10  10 PRO A  895  LYS A  905  1                                  11    
HELIX   11  11 THR A  916  CYS A  926  1                                  11    
HELIX   12  12 ASP A  930  ARG A  934  5                                   5    
HELIX   13  13 LYS A  936  ARG A  949  1                                  14    
HELIX   14  14 ASP A  950  TYR A  954  5                                   5    
HELIX   15  15 ASP A  988  TYR A  992  5                                   5    
SHEET    1   A 5 PHE A 688  GLY A 695  0                                        
SHEET    2   A 5 THR A 701  TRP A 707 -1  O  LEU A 706   N  LYS A 689           
SHEET    3   A 5 ILE A 716  GLU A 722 -1  O  ILE A 720   N  TYR A 703           
SHEET    4   A 5 VAL A 762  GLN A 767 -1  O  LEU A 764   N  LYS A 721           
SHEET    5   A 5 LEU A 753  LEU A 758 -1  N  GLY A 755   O  ILE A 765           
SHEET    1   B 2 LEU A 809  VAL A 810  0                                        
SHEET    2   B 2 LYS A 836  LEU A 837 -1  O  LYS A 836   N  VAL A 810           
SHEET    1   C 2 VAL A 819  THR A 823  0                                        
SHEET    2   C 2 HIS A 826  ILE A 829 -1  O  LYS A 828   N  LEU A 820           
SHEET    1   D 2 TYR A 845  HIS A 846  0                                        
SHEET    2   D 2 ILE A 866  TYR A 867 -1  O  TYR A 867   N  TYR A 845           
SITE     1 AC1 14 HOH A  10  LEU A 694  ALA A 719  LEU A 764                    
SITE     2 AC1 14 THR A 766  GLN A 767  LEU A 768  MET A 769                    
SITE     3 AC1 14 PRO A 770  PHE A 771  GLY A 772  LEU A 820                    
SITE     4 AC1 14 THR A 830  ASP A 831                                          
CRYST1  147.800  147.800  147.800  90.00  90.00  90.00 I 2 3        24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006766  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006766  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006766        0.00000                         
ATOM      1  N   GLY A 672      55.000   8.448  68.519  1.00101.99           N  
ATOM      2  CA  GLY A 672      54.168   8.340  69.707  1.00104.94           C  
ATOM      3  C   GLY A 672      52.692   8.194  69.380  1.00105.46           C  
ATOM      4  O   GLY A 672      51.877   9.045  69.750  1.00108.67           O  
ATOM      5  N   GLU A 673      52.359   7.101  68.691  1.00102.41           N  
ATOM      6  CA  GLU A 673      50.994   6.785  68.274  1.00 89.17           C  
ATOM      7  C   GLU A 673      50.624   5.325  68.585  1.00 81.77           C  
ATOM      8  O   GLU A 673      51.438   4.411  68.405  1.00 81.88           O  
ATOM      9  CB  GLU A 673      50.850   7.050  66.777  1.00 96.53           C  
ATOM     10  CG  GLU A 673      50.252   8.399  66.438  1.00 99.19           C  
ATOM     11  CD  GLU A 673      48.788   8.486  66.827  1.00115.45           C  
ATOM     12  OE1 GLU A 673      48.062   7.477  66.681  1.00116.71           O  
ATOM     13  OE2 GLU A 673      48.356   9.561  67.286  1.00113.58           O  
ATOM     14  N   ALA A 674      49.387   5.109  69.023  1.00 67.27           N  
ATOM     15  CA  ALA A 674      48.912   3.768  69.370  1.00 63.11           C  
ATOM     16  C   ALA A 674      48.702   2.826  68.174  1.00 58.54           C  
ATOM     17  O   ALA A 674      48.064   3.183  67.186  1.00 62.02           O  
ATOM     18  CB  ALA A 674      47.616   3.866  70.189  1.00 47.04           C  
ATOM     19  N   PRO A 675      49.260   1.612  68.240  1.00 55.66           N  
ATOM     20  CA  PRO A 675      49.087   0.665  67.134  1.00 52.95           C  
ATOM     21  C   PRO A 675      47.629   0.261  66.997  1.00 48.19           C  
ATOM     22  O   PRO A 675      46.975  -0.018  67.990  1.00 52.74           O  
ATOM     23  CB  PRO A 675      49.957  -0.520  67.559  1.00 47.27           C  
ATOM     24  CG  PRO A 675      49.985  -0.423  69.030  1.00 45.81           C  
ATOM     25  CD  PRO A 675      50.160   1.054  69.259  1.00 50.66           C  
ATOM     26  N   ASN A 676      47.124   0.267  65.767  1.00 44.01           N  
ATOM     27  CA  ASN A 676      45.735  -0.094  65.484  1.00 40.28           C  
ATOM     28  C   ASN A 676      45.670  -1.611  65.311  1.00 48.80           C  
ATOM     29  O   ASN A 676      45.949  -2.152  64.242  1.00 55.33           O  
ATOM     30  CB  ASN A 676      45.253   0.656  64.234  1.00 20.42           C  
ATOM     31  CG  ASN A 676      43.833   0.305  63.840  1.00 38.31           C  
ATOM     32  OD1 ASN A 676      43.184  -0.547  64.462  1.00 38.69           O  
ATOM     33  ND2 ASN A 676      43.352   0.935  62.761  1.00 34.99           N  
ATOM     34  N   GLN A 677      45.279  -2.295  66.375  1.00 48.40           N  
ATOM     35  CA  GLN A 677      45.231  -3.744  66.357  1.00 40.03           C  
ATOM     36  C   GLN A 677      43.926  -4.343  65.921  1.00 45.90           C  
ATOM     37  O   GLN A 677      43.625  -5.501  66.240  1.00 49.60           O  
ATOM     38  CB  GLN A 677      45.616  -4.279  67.715  1.00 29.98           C  
ATOM     39  CG  GLN A 677      47.009  -3.846  68.116  1.00 42.03           C  
ATOM     40  CD  GLN A 677      47.436  -4.467  69.415  1.00 62.22           C  
ATOM     41  OE1 GLN A 677      47.647  -5.682  69.495  1.00 70.94           O  
ATOM     42  NE2 GLN A 677      47.561  -3.643  70.450  1.00 59.09           N  
ATOM     43  N   ALA A 678      43.161  -3.570  65.163  1.00 34.42           N  
ATOM     44  CA  ALA A 678      41.893  -4.066  64.686  1.00 35.12           C  
ATOM     45  C   ALA A 678      42.111  -5.288  63.790  1.00 44.91           C  
ATOM     46  O   ALA A 678      43.117  -5.391  63.081  1.00 41.52           O  
ATOM     47  CB  ALA A 678      41.180  -2.978  63.914  1.00 32.34           C  
ATOM     48  N   LEU A 679      41.136  -6.189  63.819  1.00 48.66           N  
ATOM     49  CA  LEU A 679      41.137  -7.401  63.023  1.00 45.01           C  
ATOM     50  C   LEU A 679      40.349  -7.257  61.728  1.00 48.23           C  
ATOM     51  O   LEU A 679      39.169  -6.941  61.768  1.00 56.09           O  
ATOM     52  CB  LEU A 679      40.525  -8.546  63.825  1.00 44.12           C  
ATOM     53  CG  LEU A 679      41.521  -9.444  64.556  1.00 51.90           C  
ATOM     54  CD1 LEU A 679      42.537  -8.601  65.285  1.00 58.50           C  
ATOM     55  CD2 LEU A 679      40.775 -10.364  65.507  1.00 42.04           C  
ATOM     56  N   LEU A 680      40.996  -7.482  60.581  1.00 49.83           N  
ATOM     57  CA  LEU A 680      40.291  -7.423  59.298  1.00 43.39           C  
ATOM     58  C   LEU A 680      39.949  -8.882  58.974  1.00 48.99           C  
ATOM     59  O   LEU A 680      40.826  -9.740  58.934  1.00 53.76           O  
ATOM     60  CB  LEU A 680      41.175  -6.827  58.207  1.00 37.01           C  
ATOM     61  CG  LEU A 680      40.573  -6.816  56.796  1.00 35.30           C  
ATOM     62  CD1 LEU A 680      39.397  -5.821  56.701  1.00 37.97           C  
ATOM     63  CD2 LEU A 680      41.665  -6.429  55.796  1.00 35.95           C  
ATOM     64  N   ARG A 681      38.667  -9.166  58.795  1.00 44.02           N  
ATOM     65  CA  ARG A 681      38.223 -10.519  58.522  1.00 42.32           C  
ATOM     66  C   ARG A 681      37.949 -10.740  57.035  1.00 45.12           C  
ATOM     67  O   ARG A 681      37.255  -9.945  56.386  1.00 38.01           O  
ATOM     68  CB  ARG A 681      36.972 -10.804  59.347  1.00 41.38           C  
ATOM     69  CG  ARG A 681      36.533 -12.246  59.396  1.00 46.82           C  
ATOM     70  CD  ARG A 681      36.971 -12.935  60.685  1.00 82.56           C  
ATOM     71  NE  ARG A 681      36.424 -14.290  60.780  1.00 86.14           N  
ATOM     72  CZ  ARG A 681      35.187 -14.578  61.182  1.00 84.63           C  
ATOM     73  NH1 ARG A 681      34.352 -13.610  61.546  1.00 72.91           N  
ATOM     74  NH2 ARG A 681      34.766 -15.836  61.176  1.00 83.37           N  
ATOM     75  N   ILE A 682      38.552 -11.795  56.496  1.00 39.80           N  
ATOM     76  CA  ILE A 682      38.382 -12.164  55.101  1.00 47.32           C  
ATOM     77  C   ILE A 682      37.343 -13.270  55.114  1.00 51.12           C  
ATOM     78  O   ILE A 682      37.536 -14.301  55.751  1.00 59.26           O  
ATOM     79  CB  ILE A 682      39.697 -12.693  54.479  1.00 49.82           C  
ATOM     80  CG1 ILE A 682      40.840 -11.707  54.727  1.00 56.94           C  
ATOM     81  CG2 ILE A 682      39.533 -12.862  52.973  1.00 51.45           C  
ATOM     82  CD1 ILE A 682      40.727 -10.401  53.970  1.00 56.08           C  
ATOM     83  N   LEU A 683      36.228 -13.026  54.437  1.00 53.87           N  
ATOM     84  CA  LEU A 683      35.113 -13.966  54.380  1.00 52.97           C  
ATOM     85  C   LEU A 683      35.007 -14.617  53.017  1.00 56.46           C  
ATOM     86  O   LEU A 683      35.076 -13.933  51.990  1.00 55.89           O  
ATOM     87  CB  LEU A 683      33.800 -13.220  54.654  1.00 51.20           C  
ATOM     88  CG  LEU A 683      33.288 -12.808  56.041  1.00 54.79           C  
ATOM     89  CD1 LEU A 683      34.366 -12.460  56.994  1.00 51.48           C  
ATOM     90  CD2 LEU A 683      32.346 -11.632  55.877  1.00 66.29           C  
ATOM     91  N   LYS A 684      34.781 -15.928  53.010  1.00 58.26           N  
ATOM     92  CA  LYS A 684      34.639 -16.678  51.758  1.00 59.33           C  
ATOM     93  C   LYS A 684      33.318 -16.321  51.089  1.00 54.25           C  
ATOM     94  O   LYS A 684      32.303 -16.216  51.763  1.00 58.73           O  
ATOM     95  CB  LYS A 684      34.684 -18.185  52.032  1.00 67.19           C  
ATOM     96  CG  LYS A 684      36.076 -18.725  52.314  1.00 66.13           C  
ATOM     97  CD  LYS A 684      36.039 -20.146  52.877  1.00 88.84           C  
ATOM     98  CE  LYS A 684      36.020 -20.161  54.414  1.00 96.10           C  
ATOM     99  NZ  LYS A 684      37.299 -19.673  55.046  1.00 87.18           N  
ATOM    100  N   GLU A 685      33.343 -16.113  49.776  1.00 57.85           N  
ATOM    101  CA  GLU A 685      32.135 -15.771  49.021  1.00 62.13           C  
ATOM    102  C   GLU A 685      31.104 -16.891  49.081  1.00 62.48           C  
ATOM    103  O   GLU A 685      29.931 -16.662  48.802  1.00 63.27           O  
ATOM    104  CB  GLU A 685      32.453 -15.464  47.551  1.00 68.26           C  
ATOM    105  CG  GLU A 685      31.226 -15.010  46.765  1.00 84.32           C  
ATOM    106  CD  GLU A 685      31.443 -14.943  45.262  1.00 91.80           C  
ATOM    107  OE1 GLU A 685      32.017 -15.896  44.688  1.00 84.66           O  
ATOM    108  OE2 GLU A 685      31.002 -13.944  44.647  1.00 98.29           O  
ATOM    109  N   THR A 686      31.550 -18.099  49.421  1.00 61.51           N  
ATOM    110  CA  THR A 686      30.656 -19.251  49.526  1.00 58.28           C  
ATOM    111  C   THR A 686      29.838 -19.192  50.808  1.00 62.68           C  
ATOM    112  O   THR A 686      28.806 -19.855  50.926  1.00 66.33           O  
ATOM    113  CB  THR A 686      31.447 -20.581  49.535  1.00 63.51           C  
ATOM    114  OG1 THR A 686      32.425 -20.559  50.583  1.00 67.12           O  
ATOM    115  CG2 THR A 686      32.147 -20.796  48.205  1.00 67.37           C  
ATOM    116  N   GLU A 687      30.316 -18.412  51.775  1.00 60.23           N  
ATOM    117  CA  GLU A 687      29.646 -18.278  53.054  1.00 58.34           C  
ATOM    118  C   GLU A 687      28.446 -17.321  53.054  1.00 64.79           C  
ATOM    119  O   GLU A 687      27.706 -17.238  54.036  1.00 64.31           O  
ATOM    120  CB  GLU A 687      30.646 -17.874  54.130  1.00 58.34           C  
ATOM    121  CG  GLU A 687      31.562 -18.990  54.600  1.00 80.80           C  
ATOM    122  CD  GLU A 687      32.437 -18.572  55.784  1.00 97.59           C  
ATOM    123  OE1 GLU A 687      32.747 -17.356  55.913  1.00 75.67           O  
ATOM    124  OE2 GLU A 687      32.808 -19.466  56.587  1.00 97.68           O  
ATOM    125  N   PHE A 688      28.251 -16.580  51.975  1.00 64.31           N  
ATOM    126  CA  PHE A 688      27.116 -15.684  51.945  1.00 67.98           C  
ATOM    127  C   PHE A 688      26.294 -15.748  50.684  1.00 69.25           C  
ATOM    128  O   PHE A 688      26.815 -15.813  49.583  1.00 68.74           O  
ATOM    129  CB  PHE A 688      27.494 -14.240  52.322  1.00 70.10           C  
ATOM    130  CG  PHE A 688      28.572 -13.633  51.481  1.00 58.86           C  
ATOM    131  CD1 PHE A 688      28.279 -13.095  50.231  1.00 56.79           C  
ATOM    132  CD2 PHE A 688      29.870 -13.533  51.970  1.00 55.85           C  
ATOM    133  CE1 PHE A 688      29.266 -12.454  49.471  1.00 65.53           C  
ATOM    134  CE2 PHE A 688      30.866 -12.899  51.228  1.00 72.14           C  
ATOM    135  CZ  PHE A 688      30.562 -12.355  49.969  1.00 65.97           C  
ATOM    136  N   LYS A 689      24.983 -15.763  50.878  1.00 80.77           N  
ATOM    137  CA  LYS A 689      24.030 -15.845  49.785  1.00 91.79           C  
ATOM    138  C   LYS A 689      23.388 -14.498  49.462  1.00 96.14           C  
ATOM    139  O   LYS A 689      22.547 -14.029  50.231  1.00100.71           O  
ATOM    140  CB  LYS A 689      22.945 -16.878  50.142  1.00 83.32           C  
ATOM    141  CG  LYS A 689      23.489 -18.305  50.331  1.00100.98           C  
ATOM    142  CD  LYS A 689      22.477 -19.245  50.999  1.00115.48           C  
ATOM    143  CE  LYS A 689      23.006 -20.685  51.088  1.00116.29           C  
ATOM    144  NZ  LYS A 689      24.379 -20.774  51.687  1.00116.57           N  
ATOM    145  N   LYS A 690      23.804 -13.861  48.359  1.00 95.36           N  
ATOM    146  CA  LYS A 690      23.202 -12.584  47.943  1.00 95.83           C  
ATOM    147  C   LYS A 690      21.732 -12.882  47.677  1.00100.52           C  
ATOM    148  O   LYS A 690      21.374 -14.028  47.393  1.00105.12           O  
ATOM    149  CB  LYS A 690      23.821 -12.043  46.655  1.00 82.71           C  
ATOM    150  CG  LYS A 690      25.275 -11.623  46.754  1.00100.02           C  
ATOM    151  CD  LYS A 690      25.737 -10.992  45.442  1.00 99.11           C  
ATOM    152  CE  LYS A 690      27.224 -10.673  45.442  1.00106.97           C  
ATOM    153  NZ  LYS A 690      27.659 -10.051  44.153  1.00102.61           N  
ATOM    154  N   ILE A 691      20.882 -11.864  47.738  1.00100.52           N  
ATOM    155  CA  ILE A 691      19.458 -12.095  47.535  1.00103.05           C  
ATOM    156  C   ILE A 691      18.717 -10.999  46.775  1.00101.59           C  
ATOM    157  O   ILE A 691      17.699 -11.269  46.137  1.00102.59           O  
ATOM    158  CB  ILE A 691      18.750 -12.447  48.894  1.00106.08           C  
ATOM    159  CG1 ILE A 691      19.039 -13.922  49.260  1.00107.21           C  
ATOM    160  CG2 ILE A 691      17.249 -12.126  48.836  1.00 99.67           C  
ATOM    161  CD1 ILE A 691      18.389 -14.450  50.534  1.00 96.73           C  
ATOM    162  N   LYS A 692      19.232  -9.775  46.820  1.00 98.47           N  
ATOM    163  CA  LYS A 692      18.600  -8.669  46.111  1.00 99.96           C  
ATOM    164  C   LYS A 692      19.409  -7.388  46.189  1.00 99.94           C  
ATOM    165  O   LYS A 692      20.030  -7.092  47.206  1.00105.63           O  
ATOM    166  CB  LYS A 692      17.181  -8.414  46.637  1.00103.26           C  
ATOM    167  CG  LYS A 692      16.382  -7.413  45.792  1.00111.51           C  
ATOM    168  CD  LYS A 692      14.918  -7.296  46.228  1.00111.95           C  
ATOM    169  CE  LYS A 692      14.780  -6.664  47.611  1.00116.20           C  
ATOM    170  NZ  LYS A 692      13.355  -6.525  48.042  1.00109.63           N  
ATOM    171  N   VAL A 693      19.418  -6.644  45.092  1.00 97.62           N  
ATOM    172  CA  VAL A 693      20.135  -5.382  45.039  1.00 97.34           C  
ATOM    173  C   VAL A 693      19.298  -4.314  45.738  1.00 92.97           C  
ATOM    174  O   VAL A 693      18.082  -4.249  45.558  1.00 92.20           O  
ATOM    175  CB  VAL A 693      20.429  -4.968  43.570  1.00105.18           C  
ATOM    176  CG1 VAL A 693      19.148  -5.003  42.744  1.00119.10           C  
ATOM    177  CG2 VAL A 693      21.072  -3.579  43.511  1.00 97.02           C  
ATOM    178  N   LEU A 694      19.948  -3.530  46.592  1.00 91.31           N  
ATOM    179  CA  LEU A 694      19.280  -2.458  47.324  1.00 87.66           C  
ATOM    180  C   LEU A 694      19.436  -1.120  46.591  1.00 87.83           C  
ATOM    181  O   LEU A 694      18.608  -0.221  46.749  1.00 85.52           O  
ATOM    182  CB  LEU A 694      19.836  -2.349  48.753  1.00 72.62           C  
ATOM    183  CG  LEU A 694      19.623  -3.538  49.701  1.00 74.33           C  
ATOM    184  CD1 LEU A 694      20.383  -3.331  51.001  1.00 66.02           C  
ATOM    185  CD2 LEU A 694      18.159  -3.739  49.984  1.00 65.19           C  
ATOM    186  N   GLY A 695      20.488  -0.999  45.783  1.00 87.25           N  
ATOM    187  CA  GLY A 695      20.722   0.231  45.050  1.00 88.89           C  
ATOM    188  C   GLY A 695      21.960   0.190  44.182  1.00 92.19           C  
ATOM    189  O   GLY A 695      23.025  -0.204  44.642  1.00 93.06           O  
ATOM    190  N   SER A 696      21.821   0.632  42.935  1.00 96.47           N  
ATOM    191  CA  SER A 696      22.923   0.647  41.974  1.00101.62           C  
ATOM    192  C   SER A 696      23.323   2.078  41.602  1.00104.11           C  
ATOM    193  O   SER A 696      23.201   2.478  40.441  1.00108.43           O  
ATOM    194  CB  SER A 696      22.521  -0.115  40.699  1.00108.42           C  
ATOM    195  OG  SER A 696      22.151  -1.460  40.966  1.00108.36           O  
ATOM    196  N   GLY A 697      23.823   2.838  42.573  1.00103.19           N  
ATOM    197  CA  GLY A 697      24.214   4.215  42.311  1.00104.91           C  
ATOM    198  C   GLY A 697      25.517   4.427  41.555  1.00108.96           C  
ATOM    199  O   GLY A 697      26.128   3.482  41.054  1.00104.19           O  
ATOM    200  N   ALA A 698      25.933   5.689  41.469  1.00114.52           N  
ATOM    201  CA  ALA A 698      27.167   6.072  40.782  1.00117.16           C  
ATOM    202  C   ALA A 698      28.370   5.871  41.706  1.00118.16           C  
ATOM    203  O   ALA A 698      29.097   6.815  42.035  1.00119.72           O  
ATOM    204  CB  ALA A 698      27.083   7.533  40.316  1.00115.19           C  
ATOM    205  N   PHE A 699      28.558   4.623  42.122  1.00116.72           N  
ATOM    206  CA  PHE A 699      29.645   4.231  43.015  1.00113.53           C  
ATOM    207  C   PHE A 699      29.797   2.714  42.961  1.00109.26           C  
ATOM    208  O   PHE A 699      30.824   2.165  43.355  1.00111.65           O  
ATOM    209  CB  PHE A 699      29.338   4.667  44.456  1.00118.75           C  
ATOM    210  CG  PHE A 699      28.004   4.176  44.973  1.00118.74           C  
ATOM    211  CD1 PHE A 699      27.866   2.883  45.478  1.00111.76           C  
ATOM    212  CD2 PHE A 699      26.885   5.006  44.943  1.00107.12           C  
ATOM    213  CE1 PHE A 699      26.639   2.420  45.936  1.00 97.80           C  
ATOM    214  CE2 PHE A 699      25.652   4.554  45.399  1.00106.02           C  
ATOM    215  CZ  PHE A 699      25.529   3.258  45.898  1.00109.04           C  
ATOM    216  N   GLY A 700      28.753   2.052  42.474  1.00104.85           N  
ATOM    217  CA  GLY A 700      28.740   0.605  42.369  1.00 97.40           C  
ATOM    218  C   GLY A 700      27.358   0.121  42.761  1.00 93.71           C  
ATOM    219  O   GLY A 700      26.354   0.697  42.344  1.00 95.38           O  
ATOM    220  N   THR A 701      27.296  -0.906  43.599  1.00 87.61           N  
ATOM    221  CA  THR A 701      26.015  -1.440  44.039  1.00 86.49           C  
ATOM    222  C   THR A 701      26.071  -1.916  45.491  1.00 82.66           C  
ATOM    223  O   THR A 701      27.139  -2.237  46.011  1.00 85.92           O  
ATOM    224  CB  THR A 701      25.567  -2.640  43.161  1.00 91.10           C  
ATOM    225  OG1 THR A 701      26.550  -3.678  43.240  1.00102.39           O  
ATOM    226  CG2 THR A 701      25.401  -2.229  41.702  1.00 98.64           C  
ATOM    227  N   VAL A 702      24.908  -1.947  46.137  1.00 75.13           N  
ATOM    228  CA  VAL A 702      24.783  -2.409  47.510  1.00 64.88           C  
ATOM    229  C   VAL A 702      23.764  -3.539  47.482  1.00 61.79           C  
ATOM    230  O   VAL A 702      22.630  -3.357  47.065  1.00 63.97           O  
ATOM    231  CB  VAL A 702      24.297  -1.281  48.468  1.00 65.09           C  
ATOM    232  CG1 VAL A 702      24.107  -1.820  49.880  1.00 43.16           C  
ATOM    233  CG2 VAL A 702      25.304  -0.149  48.505  1.00 62.08           C  
ATOM    234  N   TYR A 703      24.185  -4.718  47.903  1.00 60.53           N  
ATOM    235  CA  TYR A 703      23.306  -5.870  47.920  1.00 63.58           C  
ATOM    236  C   TYR A 703      22.822  -6.169  49.326  1.00 68.03           C  
ATOM    237  O   TYR A 703      23.352  -5.659  50.309  1.00 66.69           O  
ATOM    238  CB  TYR A 703      24.037  -7.108  47.396  1.00 68.72           C  
ATOM    239  CG  TYR A 703      24.558  -6.999  45.981  1.00 79.26           C  
ATOM    240  CD1 TYR A 703      25.779  -6.382  45.713  1.00 79.20           C  
ATOM    241  CD2 TYR A 703      23.875  -7.599  44.920  1.00 88.24           C  
ATOM    242  CE1 TYR A 703      26.314  -6.377  44.426  1.00 98.08           C  
ATOM    243  CE2 TYR A 703      24.401  -7.601  43.628  1.00101.26           C  
ATOM    244  CZ  TYR A 703      25.624  -6.994  43.388  1.00102.01           C  
ATOM    245  OH  TYR A 703      26.174  -7.036  42.126  1.00103.20           O  
ATOM    246  N   LYS A 704      21.853  -7.070  49.395  1.00 70.52           N  
ATOM    247  CA  LYS A 704      21.250  -7.522  50.636  1.00 68.05           C  
ATOM    248  C   LYS A 704      21.421  -9.039  50.616  1.00 68.08           C  
ATOM    249  O   LYS A 704      21.176  -9.659  49.590  1.00 71.86           O  
ATOM    250  CB  LYS A 704      19.771  -7.140  50.612  1.00 61.42           C  
ATOM    251  CG  LYS A 704      18.866  -7.997  51.428  1.00 53.95           C  
ATOM    252  CD  LYS A 704      17.435  -7.552  51.228  1.00 73.29           C  
ATOM    253  CE  LYS A 704      16.456  -8.597  51.733  1.00 82.78           C  
ATOM    254  NZ  LYS A 704      16.843  -9.136  53.079  1.00 85.34           N  
ATOM    255  N   GLY A 705      21.871  -9.629  51.722  1.00 65.43           N  
ATOM    256  CA  GLY A 705      22.056 -11.074  51.766  1.00 60.14           C  
ATOM    257  C   GLY A 705      22.115 -11.706  53.149  1.00 58.50           C  
ATOM    258  O   GLY A 705      21.702 -11.117  54.135  1.00 60.85           O  
ATOM    259  N   LEU A 706      22.560 -12.952  53.207  1.00 58.10           N  
ATOM    260  CA  LEU A 706      22.689 -13.658  54.471  1.00 57.06           C  
ATOM    261  C   LEU A 706      24.086 -14.237  54.555  1.00 59.35           C  
ATOM    262  O   LEU A 706      24.561 -14.837  53.603  1.00 56.80           O  
ATOM    263  CB  LEU A 706      21.680 -14.794  54.588  1.00 60.00           C  
ATOM    264  CG  LEU A 706      20.246 -14.533  55.056  1.00 64.85           C  
ATOM    265  CD1 LEU A 706      19.525 -15.885  55.250  1.00 56.92           C  
ATOM    266  CD2 LEU A 706      20.246 -13.752  56.365  1.00 57.72           C  
ATOM    267  N   TRP A 707      24.749 -14.021  55.688  1.00 63.08           N  
ATOM    268  CA  TRP A 707      26.094 -14.530  55.914  1.00 60.99           C  
ATOM    269  C   TRP A 707      25.945 -15.759  56.789  1.00 60.81           C  
ATOM    270  O   TRP A 707      25.425 -15.681  57.900  1.00 62.18           O  
ATOM    271  CB  TRP A 707      26.990 -13.473  56.583  1.00 50.81           C  
ATOM    272  CG  TRP A 707      28.365 -13.973  56.903  1.00 50.75           C  
ATOM    273  CD1 TRP A 707      29.090 -14.906  56.203  1.00 55.14           C  
ATOM    274  CD2 TRP A 707      29.161 -13.616  58.033  1.00 49.31           C  
ATOM    275  NE1 TRP A 707      30.282 -15.157  56.841  1.00 53.37           N  
ATOM    276  CE2 TRP A 707      30.351 -14.382  57.968  1.00 46.91           C  
ATOM    277  CE3 TRP A 707      28.985 -12.728  59.100  1.00 51.20           C  
ATOM    278  CZ2 TRP A 707      31.355 -14.291  58.938  1.00 52.60           C  
ATOM    279  CZ3 TRP A 707      29.987 -12.637  60.065  1.00 55.46           C  
ATOM    280  CH2 TRP A 707      31.156 -13.417  59.978  1.00 45.68           C  
ATOM    281  N   ILE A 708      26.406 -16.893  56.275  1.00 64.37           N  
ATOM    282  CA  ILE A 708      26.296 -18.158  56.984  1.00 63.69           C  
ATOM    283  C   ILE A 708      27.651 -18.807  57.207  1.00 65.54           C  
ATOM    284  O   ILE A 708      28.080 -19.639  56.414  1.00 68.53           O  
ATOM    285  CB  ILE A 708      25.389 -19.127  56.190  1.00 65.24           C  
ATOM    286  CG1 ILE A 708      24.110 -18.389  55.759  1.00 67.60           C  
ATOM    287  CG2 ILE A 708      25.074 -20.368  57.028  1.00 60.81           C  
ATOM    288  CD1 ILE A 708      23.233 -19.119  54.753  1.00 73.96           C  
ATOM    289  N   PRO A 709      28.347 -18.433  58.294  1.00 72.97           N  
ATOM    290  CA  PRO A 709      29.667 -18.997  58.615  1.00 78.60           C  
ATOM    291  C   PRO A 709      29.562 -20.523  58.701  1.00 86.74           C  
ATOM    292  O   PRO A 709      28.729 -21.041  59.450  1.00 88.69           O  
ATOM    293  CB  PRO A 709      29.968 -18.396  59.983  1.00 70.40           C  
ATOM    294  CG  PRO A 709      29.209 -17.122  59.977  1.00 73.76           C  
ATOM    295  CD  PRO A 709      27.911 -17.494  59.339  1.00 78.48           C  
ATOM    296  N   GLU A 710      30.407 -21.229  57.944  1.00 94.33           N  
ATOM    297  CA  GLU A 710      30.396 -22.699  57.894  1.00100.22           C  
ATOM    298  C   GLU A 710      30.231 -23.433  59.229  1.00 98.25           C  
ATOM    299  O   GLU A 710      29.285 -24.211  59.404  1.00 95.41           O  
ATOM    300  CB  GLU A 710      31.632 -23.234  57.151  1.00114.07           C  
ATOM    301  CG  GLU A 710      31.685 -24.773  57.054  1.00118.28           C  
ATOM    302  CD  GLU A 710      32.772 -25.295  56.119  1.00120.00           C  
ATOM    303  OE1 GLU A 710      32.411 -25.917  55.093  1.00118.41           O  
ATOM    304  OE2 GLU A 710      33.978 -25.102  56.416  1.00116.49           O  
ATOM    305  N   GLY A 711      31.136 -23.172  60.164  1.00 95.50           N  
ATOM    306  CA  GLY A 711      31.072 -23.831  61.454  1.00 97.93           C  
ATOM    307  C   GLY A 711      29.738 -23.748  62.179  1.00102.52           C  
ATOM    308  O   GLY A 711      29.006 -24.742  62.257  1.00 98.79           O  
ATOM    309  N   GLU A 712      29.403 -22.545  62.649  1.00103.19           N  
ATOM    310  CA  GLU A 712      28.181 -22.286  63.417  1.00100.94           C  
ATOM    311  C   GLU A 712      26.840 -22.579  62.762  1.00 99.87           C  
ATOM    312  O   GLU A 712      26.761 -23.060  61.625  1.00101.77           O  
ATOM    313  CB  GLU A 712      28.167 -20.844  63.935  1.00104.15           C  
ATOM    314  CG  GLU A 712      29.306 -20.503  64.869  1.00106.45           C  
ATOM    315  CD  GLU A 712      30.641 -20.546  64.169  1.00 98.71           C  
ATOM    316  OE1 GLU A 712      30.834 -19.763  63.218  1.00 91.79           O  
ATOM    317  OE2 GLU A 712      31.487 -21.383  64.549  1.00118.28           O  
ATOM    318  N   LYS A 713      25.785 -22.300  63.524  1.00 93.08           N  
ATOM    319  CA  LYS A 713      24.415 -22.493  63.081  1.00 87.47           C  
ATOM    320  C   LYS A 713      23.717 -21.153  63.290  1.00 83.58           C  
ATOM    321  O   LYS A 713      22.860 -21.006  64.174  1.00 84.39           O  
ATOM    322  CB  LYS A 713      23.735 -23.601  63.899  1.00 92.63           C  
ATOM    323  CG  LYS A 713      22.389 -24.062  63.342  1.00 92.34           C  
ATOM    324  CD  LYS A 713      22.530 -24.637  61.931  1.00101.82           C  
ATOM    325  CE  LYS A 713      21.173 -24.861  61.270  1.00100.66           C  
ATOM    326  NZ  LYS A 713      20.439 -23.579  61.055  1.00 99.01           N  
ATOM    327  N   VAL A 714      24.136 -20.166  62.498  1.00 72.31           N  
ATOM    328  CA  VAL A 714      23.588 -18.814  62.567  1.00 64.14           C  
ATOM    329  C   VAL A 714      23.487 -18.202  61.172  1.00 59.62           C  
ATOM    330  O   VAL A 714      24.342 -18.437  60.317  1.00 62.40           O  
ATOM    331  CB  VAL A 714      24.491 -17.854  63.415  1.00 60.41           C  
ATOM    332  CG1 VAL A 714      24.682 -18.366  64.832  1.00 42.26           C  
ATOM    333  CG2 VAL A 714      25.840 -17.672  62.753  1.00 70.57           C  
ATOM    334  N   LYS A 715      22.429 -17.436  60.939  1.00 53.20           N  
ATOM    335  CA  LYS A 715      22.257 -16.754  59.662  1.00 56.88           C  
ATOM    336  C   LYS A 715      22.248 -15.265  59.979  1.00 52.12           C  
ATOM    337  O   LYS A 715      21.362 -14.786  60.671  1.00 55.66           O  
ATOM    338  CB  LYS A 715      20.963 -17.176  58.979  1.00 59.13           C  
ATOM    339  CG  LYS A 715      20.977 -18.618  58.545  1.00 70.74           C  
ATOM    340  CD  LYS A 715      19.929 -18.876  57.482  1.00 70.42           C  
ATOM    341  CE  LYS A 715      19.882 -20.345  57.096  1.00 64.16           C  
ATOM    342  NZ  LYS A 715      18.868 -20.569  56.035  1.00 73.90           N  
ATOM    343  N   ILE A 716      23.264 -14.553  59.499  1.00 49.01           N  
ATOM    344  CA  ILE A 716      23.427 -13.130  59.763  1.00 43.48           C  
ATOM    345  C   ILE A 716      23.045 -12.231  58.597  1.00 43.65           C  
ATOM    346  O   ILE A 716      23.736 -12.184  57.578  1.00 44.86           O  
ATOM    347  CB  ILE A 716      24.892 -12.832  60.184  1.00 46.06           C  
ATOM    348  CG1 ILE A 716      25.302 -13.800  61.299  1.00 52.43           C  
ATOM    349  CG2 ILE A 716      25.013 -11.389  60.712  1.00 42.87           C  
ATOM    350  CD1 ILE A 716      26.775 -13.824  61.601  1.00 55.45           C  
ATOM    351  N   PRO A 717      21.963 -11.461  58.752  1.00 39.57           N  
ATOM    352  CA  PRO A 717      21.509 -10.555  57.687  1.00 37.70           C  
ATOM    353  C   PRO A 717      22.577  -9.489  57.449  1.00 40.97           C  
ATOM    354  O   PRO A 717      22.945  -8.754  58.365  1.00 49.37           O  
ATOM    355  CB  PRO A 717      20.231  -9.960  58.271  1.00 24.14           C  
ATOM    356  CG  PRO A 717      19.759 -11.009  59.229  1.00 42.85           C  
ATOM    357  CD  PRO A 717      21.038 -11.449  59.891  1.00 42.06           C  
ATOM    358  N   VAL A 718      23.067  -9.398  56.217  1.00 42.07           N  
ATOM    359  CA  VAL A 718      24.124  -8.446  55.875  1.00 40.31           C  
ATOM    360  C   VAL A 718      23.873  -7.627  54.603  1.00 45.06           C  
ATOM    361  O   VAL A 718      22.966  -7.918  53.821  1.00 47.27           O  
ATOM    362  CB  VAL A 718      25.467  -9.186  55.679  1.00 44.95           C  
ATOM    363  CG1 VAL A 718      25.841  -9.940  56.936  1.00 55.08           C  
ATOM    364  CG2 VAL A 718      25.366 -10.168  54.500  1.00 34.55           C  
ATOM    365  N   ALA A 719      24.670  -6.577  54.437  1.00 43.24           N  
ATOM    366  CA  ALA A 719      24.618  -5.715  53.268  1.00 47.68           C  
ATOM    367  C   ALA A 719      26.002  -5.863  52.645  1.00 53.15           C  
ATOM    368  O   ALA A 719      27.024  -5.858  53.349  1.00 52.60           O  
ATOM    369  CB  ALA A 719      24.371  -4.263  53.658  1.00 36.19           C  
ATOM    370  N   ILE A 720      26.019  -6.026  51.326  1.00 55.00           N  
ATOM    371  CA  ILE A 720      27.254  -6.215  50.570  1.00 51.36           C  
ATOM    372  C   ILE A 720      27.472  -5.053  49.592  1.00 50.84           C  
ATOM    373  O   ILE A 720      26.635  -4.793  48.730  1.00 44.07           O  
ATOM    374  CB  ILE A 720      27.164  -7.543  49.809  1.00 51.98           C  
ATOM    375  CG1 ILE A 720      26.635  -8.615  50.754  1.00 45.10           C  
ATOM    376  CG2 ILE A 720      28.518  -7.958  49.265  1.00 47.66           C  
ATOM    377  CD1 ILE A 720      26.319  -9.897  50.086  1.00 45.86           C  
ATOM    378  N   LYS A 721      28.581  -4.340  49.744  1.00 46.92           N  
ATOM    379  CA  LYS A 721      28.881  -3.213  48.864  1.00 58.74           C  
ATOM    380  C   LYS A 721      30.122  -3.469  47.984  1.00 68.19           C  
ATOM    381  O   LYS A 721      31.195  -3.787  48.497  1.00 66.76           O  
ATOM    382  CB  LYS A 721      29.079  -1.966  49.720  1.00 50.56           C  
ATOM    383  CG  LYS A 721      29.406  -0.697  48.966  1.00 60.00           C  
ATOM    384  CD  LYS A 721      29.725   0.401  49.960  1.00 57.60           C  
ATOM    385  CE  LYS A 721      29.871   1.742  49.291  1.00 56.90           C  
ATOM    386  NZ  LYS A 721      30.122   2.791  50.314  1.00 79.32           N  
ATOM    387  N   GLU A 722      29.963  -3.329  46.666  1.00 78.88           N  
ATOM    388  CA  GLU A 722      31.054  -3.527  45.691  1.00 89.59           C  
ATOM    389  C   GLU A 722      30.942  -2.541  44.531  1.00 99.17           C  
ATOM    390  O   GLU A 722      29.935  -1.842  44.390  1.00100.93           O  
ATOM    391  CB  GLU A 722      31.025  -4.942  45.102  1.00 85.25           C  
ATOM    392  CG  GLU A 722      29.753  -5.252  44.317  1.00 93.73           C  
ATOM    393  CD  GLU A 722      29.906  -6.411  43.343  1.00107.08           C  
ATOM    394  OE1 GLU A 722      30.087  -7.566  43.787  1.00108.14           O  
ATOM    395  OE2 GLU A 722      29.827  -6.166  42.121  1.00114.47           O  
ATOM    396  N   LEU A 723      31.961  -2.528  43.673  1.00109.61           N  
ATOM    397  CA  LEU A 723      31.980  -1.644  42.502  1.00115.18           C  
ATOM    398  C   LEU A 723      31.444  -2.353  41.252  1.00116.14           C  
ATOM    399  O   LEU A 723      31.014  -3.508  41.318  1.00115.73           O  
ATOM    400  CB  LEU A 723      33.402  -1.147  42.236  1.00117.55           C  
ATOM    401  CG  LEU A 723      34.080  -0.347  43.351  1.00118.63           C  
ATOM    402  CD1 LEU A 723      35.577  -0.251  43.073  1.00114.88           C  
ATOM    403  CD2 LEU A 723      33.445   1.035  43.491  1.00 94.81           C  
ATOM    404  N   ARG A 724      31.470  -1.653  40.118  1.00117.88           N  
ATOM    405  CA  ARG A 724      30.997  -2.209  38.848  1.00118.87           C  
ATOM    406  C   ARG A 724      31.902  -3.370  38.402  1.00117.77           C  
ATOM    407  O   ARG A 724      33.056  -3.469  38.832  1.00116.51           O  
ATOM    408  CB  ARG A 724      30.944  -1.110  37.771  1.00117.03           C  
ATOM    409  CG  ARG A 724      30.270  -1.520  36.453  1.00120.00           C  
ATOM    410  CD  ARG A 724      28.782  -1.820  36.650  1.00120.00           C  
ATOM    411  NE  ARG A 724      28.180  -2.504  35.500  1.00120.00           N  
ATOM    412  CZ  ARG A 724      27.313  -1.948  34.656  1.00118.30           C  
ATOM    413  NH1 ARG A 724      26.940  -0.684  34.813  1.00119.88           N  
ATOM    414  NH2 ARG A 724      26.785  -2.672  33.675  1.00113.01           N  
ATOM    415  N   GLU A 725      31.367  -4.238  37.545  0.00118.05           N  
ATOM    416  CA  GLU A 725      32.083  -5.411  37.038  0.00118.88           C  
ATOM    417  C   GLU A 725      33.549  -5.195  36.652  0.00119.37           C  
ATOM    418  O   GLU A 725      34.411  -5.990  37.028  0.00119.89           O  
ATOM    419  CB  GLU A 725      31.310  -6.045  35.876  0.00118.16           C  
ATOM    420  CG  GLU A 725      30.993  -5.100  34.726  0.00113.14           C  
ATOM    421  CD  GLU A 725      30.112  -5.744  33.671  0.00116.04           C  
ATOM    422  OE1 GLU A 725      28.932  -5.350  33.562  0.00115.61           O  
ATOM    423  OE2 GLU A 725      30.598  -6.644  32.954  0.00110.87           O  
ATOM    424  N   ALA A 726      33.829  -4.131  35.903  1.00119.87           N  
ATOM    425  CA  ALA A 726      35.198  -3.828  35.494  1.00118.48           C  
ATOM    426  C   ALA A 726      35.989  -3.278  36.683  1.00118.95           C  
ATOM    427  O   ALA A 726      35.437  -2.589  37.549  1.00116.44           O  
ATOM    428  CB  ALA A 726      35.204  -2.832  34.341  1.00119.45           C  
ATOM    429  N   THR A 727      37.280  -3.601  36.724  1.00119.85           N  
ATOM    430  CA  THR A 727      38.153  -3.156  37.807  1.00119.78           C  
ATOM    431  C   THR A 727      38.641  -1.718  37.613  1.00120.00           C  
ATOM    432  O   THR A 727      39.152  -1.357  36.544  1.00119.35           O  
ATOM    433  CB  THR A 727      39.382  -4.091  37.970  1.00118.76           C  
ATOM    434  OG1 THR A 727      38.940  -5.446  38.127  1.00111.10           O  
ATOM    435  CG2 THR A 727      40.203  -3.688  39.202  1.00117.14           C  
ATOM    436  N   SER A 728      38.446  -0.898  38.645  1.00120.00           N  
ATOM    437  CA  SER A 728      38.878   0.497  38.624  1.00120.00           C  
ATOM    438  C   SER A 728      40.155   0.604  39.469  1.00120.00           C  
ATOM    439  O   SER A 728      40.294  -0.076  40.494  1.00119.72           O  
ATOM    440  CB  SER A 728      37.775   1.415  39.174  1.00120.00           C  
ATOM    441  OG  SER A 728      38.083   2.785  38.961  1.00112.66           O  
ATOM    442  N   PRO A 729      41.123   1.424  39.016  1.00120.00           N  
ATOM    443  CA  PRO A 729      42.419   1.659  39.676  1.00120.00           C  
ATOM    444  C   PRO A 729      42.347   2.277  41.074  1.00119.43           C  
ATOM    445  O   PRO A 729      42.668   1.626  42.071  1.00118.61           O  
ATOM    446  CB  PRO A 729      43.135   2.598  38.695  1.00120.00           C  
ATOM    447  CG  PRO A 729      42.535   2.225  37.361  1.00119.92           C  
ATOM    448  CD  PRO A 729      41.074   2.112  37.712  1.00120.00           C  
ATOM    449  N   LYS A 730      41.954   3.548  41.121  1.00120.00           N  
ATOM    450  CA  LYS A 730      41.840   4.313  42.362  1.00119.21           C  
ATOM    451  C   LYS A 730      40.632   3.936  43.225  1.00119.52           C  
ATOM    452  O   LYS A 730      40.668   4.098  44.446  1.00119.71           O  
ATOM    453  CB  LYS A 730      41.790   5.812  42.043  1.00115.30           C  
ATOM    454  CG  LYS A 730      40.654   6.196  41.102  0.00111.42           C  
ATOM    455  CD  LYS A 730      40.641   7.684  40.801  0.00112.24           C  
ATOM    456  CE  LYS A 730      39.494   8.038  39.867  0.00115.68           C  
ATOM    457  NZ  LYS A 730      39.456   9.492  39.551  0.00114.85           N  
ATOM    458  N   ALA A 731      39.562   3.457  42.593  1.00118.99           N  
ATOM    459  CA  ALA A 731      38.347   3.069  43.313  1.00115.58           C  
ATOM    460  C   ALA A 731      38.589   1.846  44.192  1.00112.61           C  
ATOM    461  O   ALA A 731      37.948   1.673  45.226  1.00111.65           O  
ATOM    462  CB  ALA A 731      37.215   2.804  42.333  1.00113.88           C  
ATOM    463  N   ASN A 732      39.530   1.011  43.771  1.00112.01           N  
ATOM    464  CA  ASN A 732      39.888  -0.194  44.504  1.00110.60           C  
ATOM    465  C   ASN A 732      40.576   0.162  45.817  1.00106.48           C  
ATOM    466  O   ASN A 732      40.358  -0.486  46.836  1.00105.64           O  
ATOM    467  CB  ASN A 732      40.809  -1.061  43.650  1.00118.92           C  
ATOM    468  CG  ASN A 732      41.126  -2.384  44.303  1.00120.00           C  
ATOM    469  OD1 ASN A 732      40.402  -3.374  44.118  1.00118.83           O  
ATOM    470  ND2 ASN A 732      42.214  -2.416  45.079  1.00116.78           N  
ATOM    471  N   LYS A 733      41.438   1.173  45.770  1.00103.25           N  
ATOM    472  CA  LYS A 733      42.141   1.636  46.958  1.00102.13           C  
ATOM    473  C   LYS A 733      41.124   2.239  47.918  1.00100.63           C  
ATOM    474  O   LYS A 733      41.157   1.973  49.118  1.00104.56           O  
ATOM    475  CB  LYS A 733      43.181   2.704  46.594  1.00 96.91           C  
ATOM    476  CG  LYS A 733      43.850   3.336  47.808  1.00110.43           C  
ATOM    477  CD  LYS A 733      44.779   4.473  47.439  1.00109.50           C  
ATOM    478  CE  LYS A 733      45.463   5.014  48.686  1.00119.19           C  
ATOM    479  NZ  LYS A 733      46.474   6.065  48.386  1.00120.00           N  
ATOM    480  N   GLU A 734      40.201   3.021  47.363  1.00 95.90           N  
ATOM    481  CA  GLU A 734      39.167   3.687  48.142  1.00 91.10           C  
ATOM    482  C   GLU A 734      38.256   2.750  48.944  1.00 84.46           C  
ATOM    483  O   GLU A 734      37.856   3.082  50.065  1.00 81.68           O  
ATOM    484  CB  GLU A 734      38.366   4.647  47.253  1.00 95.48           C  
ATOM    485  CG  GLU A 734      39.219   5.805  46.717  1.00102.59           C  
ATOM    486  CD  GLU A 734      38.412   6.909  46.039  1.00106.44           C  
ATOM    487  OE1 GLU A 734      37.289   6.637  45.552  1.00114.11           O  
ATOM    488  OE2 GLU A 734      38.913   8.058  45.989  1.00101.90           O  
ATOM    489  N   ILE A 735      37.938   1.580  48.396  1.00 76.67           N  
ATOM    490  CA  ILE A 735      37.106   0.646  49.143  1.00 70.69           C  
ATOM    491  C   ILE A 735      37.948   0.131  50.292  1.00 62.75           C  
ATOM    492  O   ILE A 735      37.466  -0.007  51.413  1.00 60.57           O  
ATOM    493  CB  ILE A 735      36.646  -0.578  48.329  1.00 71.12           C  
ATOM    494  CG1 ILE A 735      35.780  -0.159  47.148  1.00 92.52           C  
ATOM    495  CG2 ILE A 735      35.793  -1.478  49.207  1.00 71.12           C  
ATOM    496  CD1 ILE A 735      35.185  -1.353  46.396  1.00 95.31           C  
ATOM    497  N   LEU A 736      39.214  -0.150  50.013  1.00 55.25           N  
ATOM    498  CA  LEU A 736      40.074  -0.653  51.061  1.00 50.87           C  
ATOM    499  C   LEU A 736      40.323   0.404  52.134  1.00 50.02           C  
ATOM    500  O   LEU A 736      40.451   0.062  53.305  1.00 55.00           O  
ATOM    501  CB  LEU A 736      41.371  -1.240  50.490  1.00 57.16           C  
ATOM    502  CG  LEU A 736      41.367  -2.704  49.997  1.00 63.08           C  
ATOM    503  CD1 LEU A 736      40.552  -3.581  50.936  1.00 43.77           C  
ATOM    504  CD2 LEU A 736      40.814  -2.819  48.598  1.00 67.56           C  
ATOM    505  N   ASP A 737      40.350   1.682  51.751  1.00 46.92           N  
ATOM    506  CA  ASP A 737      40.530   2.763  52.719  1.00 45.62           C  
ATOM    507  C   ASP A 737      39.318   2.787  53.626  1.00 51.02           C  
ATOM    508  O   ASP A 737      39.451   2.899  54.843  1.00 48.39           O  
ATOM    509  CB  ASP A 737      40.635   4.121  52.046  1.00 44.18           C  
ATOM    510  CG  ASP A 737      42.036   4.440  51.575  1.00 65.81           C  
ATOM    511  OD1 ASP A 737      43.010   3.911  52.161  1.00 63.44           O  
ATOM    512  OD2 ASP A 737      42.160   5.241  50.622  1.00 84.30           O  
ATOM    513  N   GLU A 738      38.142   2.655  53.013  1.00 49.34           N  
ATOM    514  CA  GLU A 738      36.880   2.649  53.726  1.00 47.77           C  
ATOM    515  C   GLU A 738      36.775   1.436  54.641  1.00 52.97           C  
ATOM    516  O   GLU A 738      36.191   1.524  55.732  1.00 60.99           O  
ATOM    517  CB  GLU A 738      35.726   2.679  52.736  1.00 50.26           C  
ATOM    518  CG  GLU A 738      34.346   2.698  53.361  1.00 59.40           C  
ATOM    519  CD  GLU A 738      33.235   2.863  52.335  1.00 58.37           C  
ATOM    520  OE1 GLU A 738      33.541   3.249  51.188  1.00 72.29           O  
ATOM    521  OE2 GLU A 738      32.053   2.620  52.672  1.00 76.77           O  
ATOM    522  N   ALA A 739      37.367   0.319  54.216  1.00 48.57           N  
ATOM    523  CA  ALA A 739      37.364  -0.918  55.013  1.00 42.69           C  
ATOM    524  C   ALA A 739      38.196  -0.701  56.255  1.00 40.88           C  
ATOM    525  O   ALA A 739      37.799  -1.071  57.347  1.00 46.18           O  
ATOM    526  CB  ALA A 739      37.934  -2.062  54.221  1.00 38.75           C  
ATOM    527  N   TYR A 740      39.340  -0.050  56.069  1.00 43.89           N  
ATOM    528  CA  TYR A 740      40.257   0.252  57.151  1.00 40.40           C  
ATOM    529  C   TYR A 740      39.600   1.058  58.274  1.00 43.21           C  
ATOM    530  O   TYR A 740      39.842   0.786  59.443  1.00 45.45           O  
ATOM    531  CB  TYR A 740      41.481   1.018  56.617  1.00 30.08           C  
ATOM    532  CG  TYR A 740      42.484   1.396  57.701  1.00 39.41           C  
ATOM    533  CD1 TYR A 740      42.269   2.492  58.545  1.00 37.60           C  
ATOM    534  CD2 TYR A 740      43.611   0.620  57.927  1.00 35.27           C  
ATOM    535  CE1 TYR A 740      43.157   2.791  59.589  1.00 31.20           C  
ATOM    536  CE2 TYR A 740      44.499   0.915  58.974  1.00 45.40           C  
ATOM    537  CZ  TYR A 740      44.262   1.996  59.792  1.00 40.96           C  
ATOM    538  OH  TYR A 740      45.143   2.279  60.799  1.00 51.29           O  
ATOM    539  N   VAL A 741      38.805   2.068  57.927  1.00 46.94           N  
ATOM    540  CA  VAL A 741      38.160   2.885  58.952  1.00 48.54           C  
ATOM    541  C   VAL A 741      37.012   2.132  59.585  1.00 45.15           C  
ATOM    542  O   VAL A 741      36.920   2.086  60.809  1.00 46.30           O  
ATOM    543  CB  VAL A 741      37.656   4.248  58.420  1.00 51.92           C  
ATOM    544  CG1 VAL A 741      38.800   5.053  57.849  1.00 39.01           C  
ATOM    545  CG2 VAL A 741      36.639   4.037  57.363  1.00 76.92           C  
ATOM    546  N   MET A 742      36.183   1.472  58.771  1.00 37.09           N  
ATOM    547  CA  MET A 742      35.058   0.730  59.338  1.00 42.02           C  
ATOM    548  C   MET A 742      35.466  -0.411  60.251  1.00 46.34           C  
ATOM    549  O   MET A 742      34.734  -0.768  61.170  1.00 61.43           O  
ATOM    550  CB  MET A 742      34.133   0.192  58.266  1.00 46.91           C  
ATOM    551  CG  MET A 742      33.397   1.229  57.479  1.00 49.54           C  
ATOM    552  SD  MET A 742      32.244   0.362  56.443  1.00 63.27           S  
ATOM    553  CE  MET A 742      31.080  -0.114  57.631  1.00 46.43           C  
ATOM    554  N   ALA A 743      36.621  -1.001  59.980  1.00 47.70           N  
ATOM    555  CA  ALA A 743      37.125  -2.096  60.787  1.00 43.52           C  
ATOM    556  C   ALA A 743      37.750  -1.558  62.066  1.00 36.10           C  
ATOM    557  O   ALA A 743      38.013  -2.300  62.995  1.00 43.42           O  
ATOM    558  CB  ALA A 743      38.155  -2.897  59.985  1.00 39.05           C  
ATOM    559  N   SER A 744      37.973  -0.256  62.115  1.00 39.86           N  
ATOM    560  CA  SER A 744      38.603   0.362  63.278  1.00 47.26           C  
ATOM    561  C   SER A 744      37.661   1.072  64.251  1.00 50.31           C  
ATOM    562  O   SER A 744      38.122   1.797  65.140  1.00 58.89           O  
ATOM    563  CB  SER A 744      39.663   1.352  62.804  1.00 46.68           C  
ATOM    564  OG  SER A 744      40.569   0.726  61.911  1.00 61.12           O  
ATOM    565  N   VAL A 745      36.356   0.900  64.068  1.00 46.30           N  
ATOM    566  CA  VAL A 745      35.376   1.538  64.945  1.00 44.52           C  
ATOM    567  C   VAL A 745      34.450   0.491  65.530  1.00 47.41           C  
ATOM    568  O   VAL A 745      33.999  -0.410  64.840  1.00 49.93           O  
ATOM    569  CB  VAL A 745      34.499   2.560  64.193  1.00 42.20           C  
ATOM    570  CG1 VAL A 745      35.345   3.713  63.637  1.00 27.99           C  
ATOM    571  CG2 VAL A 745      33.726   1.853  63.081  1.00 37.55           C  
ATOM    572  N   ASP A 746      34.159   0.623  66.811  1.00 45.95           N  
ATOM    573  CA  ASP A 746      33.276  -0.307  67.482  1.00 42.74           C  
ATOM    574  C   ASP A 746      32.422   0.512  68.475  1.00 43.17           C  
ATOM    575  O   ASP A 746      32.898   0.954  69.530  1.00 42.31           O  
ATOM    576  CB  ASP A 746      34.111  -1.401  68.178  1.00 29.82           C  
ATOM    577  CG  ASP A 746      33.245  -2.457  68.879  1.00 55.09           C  
ATOM    578  OD1 ASP A 746      32.043  -2.581  68.564  1.00 52.73           O  
ATOM    579  OD2 ASP A 746      33.768  -3.173  69.758  1.00 74.69           O  
ATOM    580  N   ASN A 747      31.189   0.794  68.063  1.00 35.56           N  
ATOM    581  CA  ASN A 747      30.245   1.557  68.871  1.00 36.25           C  
ATOM    582  C   ASN A 747      28.820   1.270  68.415  1.00 34.56           C  
ATOM    583  O   ASN A 747      28.582   1.014  67.244  1.00 39.61           O  
ATOM    584  CB  ASN A 747      30.552   3.054  68.774  1.00 40.50           C  
ATOM    585  CG  ASN A 747      29.631   3.897  69.632  1.00 47.30           C  
ATOM    586  OD1 ASN A 747      28.535   4.272  69.206  1.00 39.04           O  
ATOM    587  ND2 ASN A 747      30.063   4.185  70.858  1.00 36.78           N  
ATOM    588  N   PRO A 748      27.852   1.296  69.345  1.00 36.26           N  
ATOM    589  CA  PRO A 748      26.438   1.036  69.033  1.00 26.39           C  
ATOM    590  C   PRO A 748      25.799   2.004  68.052  1.00 29.08           C  
ATOM    591  O   PRO A 748      24.785   1.704  67.440  1.00 34.03           O  
ATOM    592  CB  PRO A 748      25.784   1.108  70.396  1.00 26.22           C  
ATOM    593  CG  PRO A 748      26.891   0.586  71.335  1.00 20.21           C  
ATOM    594  CD  PRO A 748      28.071   1.336  70.805  1.00 31.84           C  
ATOM    595  N   HIS A 749      26.424   3.148  67.858  1.00 36.86           N  
ATOM    596  CA  HIS A 749      25.886   4.143  66.949  1.00 40.75           C  
ATOM    597  C   HIS A 749      26.748   4.411  65.732  1.00 43.31           C  
ATOM    598  O   HIS A 749      26.611   5.439  65.049  1.00 42.41           O  
ATOM    599  CB  HIS A 749      25.546   5.391  67.740  1.00 39.93           C  
ATOM    600  CG  HIS A 749      24.555   5.110  68.819  1.00 49.23           C  
ATOM    601  ND1 HIS A 749      23.249   4.765  68.545  1.00 41.45           N  
ATOM    602  CD2 HIS A 749      24.713   4.955  70.153  1.00 33.26           C  
ATOM    603  CE1 HIS A 749      22.650   4.397  69.664  1.00 46.00           C  
ATOM    604  NE2 HIS A 749      23.517   4.502  70.655  1.00 34.86           N  
ATOM    605  N   VAL A 750      27.644   3.463  65.467  1.00 45.15           N  
ATOM    606  CA  VAL A 750      28.491   3.515  64.286  1.00 40.34           C  
ATOM    607  C   VAL A 750      28.358   2.176  63.567  1.00 35.42           C  
ATOM    608  O   VAL A 750      28.265   1.117  64.201  1.00 30.82           O  
ATOM    609  CB  VAL A 750      29.939   3.823  64.645  1.00 34.23           C  
ATOM    610  CG1 VAL A 750      30.804   3.742  63.421  1.00 44.91           C  
ATOM    611  CG2 VAL A 750      30.017   5.244  65.201  1.00 34.34           C  
ATOM    612  N  ACYS A 751      28.271   2.223  62.244  0.50 35.58           N  
ATOM    613  N  BCYS A 751      28.282   2.243  62.246  0.50 37.41           N  
ATOM    614  CA ACYS A 751      28.168   0.990  61.469  0.50 42.09           C  
ATOM    615  CA BCYS A 751      28.150   1.062  61.389  0.50 45.23           C  
ATOM    616  C  ACYS A 751      29.518   0.324  61.402  0.50 42.98           C  
ATOM    617  C  BCYS A 751      29.496   0.320  61.313  0.50 44.85           C  
ATOM    618  O  ACYS A 751      30.528   0.968  61.135  0.50 51.40           O  
ATOM    619  O  BCYS A 751      30.500   0.925  60.946  0.50 52.45           O  
ATOM    620  CB ACYS A 751      27.653   1.255  60.060  0.50 32.54           C  
ATOM    621  CB BCYS A 751      27.681   1.539  60.003  0.50 41.91           C  
ATOM    622  SG ACYS A 751      25.899   1.515  60.033  0.50 33.14           S  
ATOM    623  SG BCYS A 751      27.776   0.394  58.620  0.50 52.82           S  
ATOM    624  N   ARG A 752      29.530  -0.967  61.673  1.00 48.20           N  
ATOM    625  CA  ARG A 752      30.785  -1.742  61.657  1.00 55.15           C  
ATOM    626  C   ARG A 752      30.913  -2.768  60.519  1.00 54.92           C  
ATOM    627  O   ARG A 752      29.924  -3.346  60.023  1.00 52.10           O  
ATOM    628  CB  ARG A 752      30.976  -2.431  63.014  1.00 73.03           C  
ATOM    629  CG  ARG A 752      32.335  -3.053  63.269  1.00 62.83           C  
ATOM    630  CD  ARG A 752      32.250  -3.889  64.539  1.00 74.46           C  
ATOM    631  NE  ARG A 752      33.423  -4.731  64.764  1.00 85.80           N  
ATOM    632  CZ  ARG A 752      34.644  -4.269  65.025  1.00100.40           C  
ATOM    633  NH1 ARG A 752      34.862  -2.962  65.089  1.00 94.64           N  
ATOM    634  NH2 ARG A 752      35.646  -5.116  65.241  1.00108.37           N  
ATOM    635  N   LEU A 753      32.156  -2.959  60.105  1.00 53.73           N  
ATOM    636  CA  LEU A 753      32.503  -3.877  59.045  1.00 45.35           C  
ATOM    637  C   LEU A 753      32.568  -5.290  59.601  1.00 45.62           C  
ATOM    638  O   LEU A 753      33.214  -5.520  60.617  1.00 48.14           O  
ATOM    639  CB  LEU A 753      33.875  -3.502  58.526  1.00 47.11           C  
ATOM    640  CG  LEU A 753      34.385  -4.207  57.280  1.00 60.05           C  
ATOM    641  CD1 LEU A 753      33.907  -3.452  56.049  1.00 48.93           C  
ATOM    642  CD2 LEU A 753      35.903  -4.223  57.324  1.00 59.98           C  
ATOM    643  N   LEU A 754      31.873  -6.228  58.969  1.00 45.61           N  
ATOM    644  CA  LEU A 754      31.927  -7.616  59.405  1.00 47.72           C  
ATOM    645  C   LEU A 754      33.143  -8.249  58.749  1.00 51.77           C  
ATOM    646  O   LEU A 754      33.798  -9.112  59.334  1.00 51.52           O  
ATOM    647  CB  LEU A 754      30.670  -8.368  59.006  1.00 41.87           C  
ATOM    648  CG  LEU A 754      29.466  -7.844  59.777  1.00 50.79           C  
ATOM    649  CD1 LEU A 754      28.185  -8.363  59.159  1.00 46.72           C  
ATOM    650  CD2 LEU A 754      29.585  -8.257  61.233  1.00 41.91           C  
ATOM    651  N   GLY A 755      33.474  -7.757  57.559  1.00 47.03           N  
ATOM    652  CA  GLY A 755      34.617  -8.276  56.839  1.00 53.28           C  
ATOM    653  C   GLY A 755      34.628  -7.921  55.365  1.00 48.72           C  
ATOM    654  O   GLY A 755      33.825  -7.121  54.895  1.00 48.41           O  
ATOM    655  N   ILE A 756      35.589  -8.478  54.643  1.00 47.20           N  
ATOM    656  CA  ILE A 756      35.681  -8.242  53.214  1.00 48.14           C  
ATOM    657  C   ILE A 756      35.803  -9.583  52.507  1.00 53.25           C  
ATOM    658  O   ILE A 756      36.169 -10.607  53.119  1.00 49.03           O  
ATOM    659  CB  ILE A 756      36.863  -7.303  52.836  1.00 51.35           C  
ATOM    660  CG1 ILE A 756      38.199  -7.864  53.317  1.00 47.55           C  
ATOM    661  CG2 ILE A 756      36.684  -5.931  53.466  1.00 45.34           C  
ATOM    662  CD1 ILE A 756      39.389  -7.073  52.782  1.00 60.62           C  
ATOM    663  N   CYS A 757      35.383  -9.589  51.247  1.00 56.20           N  
ATOM    664  CA  CYS A 757      35.446 -10.779  50.407  1.00 60.93           C  
ATOM    665  C   CYS A 757      36.230 -10.371  49.152  1.00 60.14           C  
ATOM    666  O   CYS A 757      35.819  -9.471  48.415  1.00 52.96           O  
ATOM    667  CB  CYS A 757      34.028 -11.270  50.060  1.00 64.83           C  
ATOM    668  SG  CYS A 757      33.975 -12.858  49.158  1.00 73.09           S  
ATOM    669  N   LEU A 758      37.393 -10.986  48.958  1.00 60.02           N  
ATOM    670  CA  LEU A 758      38.247 -10.664  47.820  1.00 63.37           C  
ATOM    671  C   LEU A 758      37.824 -11.392  46.550  1.00 66.93           C  
ATOM    672  O   LEU A 758      38.251 -12.510  46.295  1.00 71.90           O  
ATOM    673  CB  LEU A 758      39.710 -10.959  48.162  1.00 41.64           C  
ATOM    674  CG  LEU A 758      40.290 -10.165  49.340  1.00 61.61           C  
ATOM    675  CD1 LEU A 758      41.696 -10.655  49.616  1.00 67.38           C  
ATOM    676  CD2 LEU A 758      40.294  -8.646  49.083  1.00 34.49           C  
ATOM    677  N   THR A 759      36.977 -10.744  45.761  1.00 72.06           N  
ATOM    678  CA  THR A 759      36.477 -11.320  44.519  1.00 83.08           C  
ATOM    679  C   THR A 759      37.213 -10.638  43.367  1.00 86.16           C  
ATOM    680  O   THR A 759      38.379 -10.283  43.507  1.00 94.75           O  
ATOM    681  CB  THR A 759      34.949 -11.080  44.387  1.00 90.69           C  
ATOM    682  OG1 THR A 759      34.313 -11.358  45.640  1.00 85.09           O  
ATOM    683  CG2 THR A 759      34.342 -12.005  43.325  1.00 98.46           C  
ATOM    684  N   SER A 760      36.553 -10.483  42.224  1.00 86.22           N  
ATOM    685  CA  SER A 760      37.153  -9.809  41.083  1.00 91.65           C  
ATOM    686  C   SER A 760      37.433  -8.400  41.602  1.00 95.98           C  
ATOM    687  O   SER A 760      38.503  -7.829  41.375  1.00 98.69           O  
ATOM    688  CB  SER A 760      36.148  -9.764  39.937  1.00 98.60           C  
ATOM    689  OG  SER A 760      35.479 -11.009  39.818  1.00102.77           O  
ATOM    690  N   THR A 761      36.442  -7.863  42.312  1.00100.97           N  
ATOM    691  CA  THR A 761      36.518  -6.554  42.960  1.00 96.36           C  
ATOM    692  C   THR A 761      36.211  -6.823  44.430  1.00 92.44           C  
ATOM    693  O   THR A 761      35.461  -7.754  44.768  1.00 91.58           O  
ATOM    694  CB  THR A 761      35.479  -5.533  42.415  1.00 95.81           C  
ATOM    695  OG1 THR A 761      34.155  -6.078  42.515  1.00 99.68           O  
ATOM    696  CG2 THR A 761      35.785  -5.165  40.963  1.00102.36           C  
ATOM    697  N   VAL A 762      36.817  -6.032  45.302  1.00 84.88           N  
ATOM    698  CA  VAL A 762      36.612  -6.190  46.729  1.00 82.79           C  
ATOM    699  C   VAL A 762      35.181  -5.820  47.150  1.00 76.73           C  
ATOM    700  O   VAL A 762      34.583  -4.896  46.603  1.00 81.53           O  
ATOM    701  CB  VAL A 762      37.641  -5.358  47.511  1.00 84.24           C  
ATOM    702  CG1 VAL A 762      37.561  -3.908  47.085  1.00 83.27           C  
ATOM    703  CG2 VAL A 762      37.428  -5.511  49.011  1.00 86.10           C  
ATOM    704  N   GLN A 763      34.627  -6.599  48.076  1.00 68.77           N  
ATOM    705  CA  GLN A 763      33.279  -6.385  48.599  1.00 61.32           C  
ATOM    706  C   GLN A 763      33.321  -6.106  50.101  1.00 52.68           C  
ATOM    707  O   GLN A 763      33.977  -6.826  50.851  1.00 49.42           O  
ATOM    708  CB  GLN A 763      32.401  -7.624  48.384  1.00 60.21           C  
ATOM    709  CG  GLN A 763      32.276  -8.114  46.959  1.00 66.70           C  
ATOM    710  CD  GLN A 763      31.331  -9.308  46.830  1.00 64.39           C  
ATOM    711  OE1 GLN A 763      31.427 -10.288  47.577  1.00 69.45           O  
ATOM    712  NE2 GLN A 763      30.409  -9.223  45.881  1.00 66.28           N  
ATOM    713  N   LEU A 764      32.649  -5.043  50.531  1.00 51.46           N  
ATOM    714  CA  LEU A 764      32.572  -4.721  51.952  1.00 48.10           C  
ATOM    715  C   LEU A 764      31.303  -5.397  52.473  1.00 48.08           C  
ATOM    716  O   LEU A 764      30.284  -5.395  51.782  1.00 49.33           O  
ATOM    717  CB  LEU A 764      32.460  -3.224  52.158  1.00 46.76           C  
ATOM    718  CG  LEU A 764      33.668  -2.358  51.827  1.00 69.78           C  
ATOM    719  CD1 LEU A 764      33.274  -0.894  51.841  1.00 78.29           C  
ATOM    720  CD2 LEU A 764      34.745  -2.600  52.834  1.00 72.54           C  
ATOM    721  N   ILE A 765      31.388  -6.041  53.642  1.00 44.49           N  
ATOM    722  CA  ILE A 765      30.234  -6.712  54.242  1.00 48.31           C  
ATOM    723  C   ILE A 765      29.925  -6.093  55.607  1.00 52.32           C  
ATOM    724  O   ILE A 765      30.805  -5.981  56.462  1.00 52.23           O  
ATOM    725  CB  ILE A 765      30.460  -8.247  54.415  1.00 52.95           C  
ATOM    726  CG1 ILE A 765      30.676  -8.917  53.059  1.00 51.87           C  
ATOM    727  CG2 ILE A 765      29.234  -8.904  55.027  1.00 47.03           C  
ATOM    728  CD1 ILE A 765      32.075  -8.866  52.606  1.00 56.56           C  
ATOM    729  N   THR A 766      28.690  -5.637  55.789  1.00 44.63           N  
ATOM    730  CA  THR A 766      28.297  -5.044  57.053  1.00 44.23           C  
ATOM    731  C   THR A 766      26.947  -5.541  57.452  1.00 42.35           C  
ATOM    732  O   THR A 766      26.311  -6.242  56.692  1.00 41.20           O  
ATOM    733  CB  THR A 766      28.203  -3.507  57.003  1.00 38.85           C  
ATOM    734  OG1 THR A 766      27.403  -3.109  55.889  1.00 44.72           O  
ATOM    735  CG2 THR A 766      29.559  -2.884  56.910  1.00 58.58           C  
ATOM    736  N   GLN A 767      26.525  -5.165  58.659  1.00 41.76           N  
ATOM    737  CA  GLN A 767      25.224  -5.535  59.181  1.00 40.27           C  
ATOM    738  C   GLN A 767      24.127  -4.831  58.384  1.00 44.44           C  
ATOM    739  O   GLN A 767      24.253  -3.657  58.017  1.00 38.81           O  
ATOM    740  CB  GLN A 767      25.105  -5.121  60.639  1.00 31.22           C  
ATOM    741  CG  GLN A 767      23.684  -5.080  61.168  1.00 39.37           C  
ATOM    742  CD  GLN A 767      23.601  -4.560  62.595  1.00 48.51           C  
ATOM    743  OE1 GLN A 767      24.134  -3.495  62.922  1.00 55.48           O  
ATOM    744  NE2 GLN A 767      22.920  -5.303  63.446  1.00 42.62           N  
ATOM    745  N   LEU A 768      23.062  -5.574  58.100  1.00 43.01           N  
ATOM    746  CA  LEU A 768      21.930  -5.035  57.378  1.00 42.60           C  
ATOM    747  C   LEU A 768      21.127  -4.065  58.259  1.00 41.70           C  
ATOM    748  O   LEU A 768      20.777  -4.374  59.401  1.00 41.93           O  
ATOM    749  CB  LEU A 768      21.019  -6.172  56.932  1.00 38.39           C  
ATOM    750  CG  LEU A 768      19.813  -5.742  56.110  1.00 42.83           C  
ATOM    751  CD1 LEU A 768      20.318  -5.188  54.806  1.00 35.06           C  
ATOM    752  CD2 LEU A 768      18.862  -6.903  55.888  1.00 37.08           C  
ATOM    753  N   MET A 769      20.898  -2.866  57.744  1.00 45.02           N  
ATOM    754  CA  MET A 769      20.091  -1.872  58.436  1.00 41.73           C  
ATOM    755  C   MET A 769      18.783  -1.873  57.605  1.00 41.95           C  
ATOM    756  O   MET A 769      18.565  -1.027  56.748  1.00 32.59           O  
ATOM    757  CB  MET A 769      20.818  -0.533  58.411  1.00 40.44           C  
ATOM    758  CG  MET A 769      22.197  -0.579  59.047  1.00 36.98           C  
ATOM    759  SD  MET A 769      22.196  -1.163  60.774  1.00 44.95           S  
ATOM    760  CE  MET A 769      21.937   0.370  61.588  1.00 41.08           C  
ATOM    761  N   PRO A 770      17.864  -2.795  57.929  1.00 39.46           N  
ATOM    762  CA  PRO A 770      16.570  -3.027  57.284  1.00 46.88           C  
ATOM    763  C   PRO A 770      15.737  -1.836  56.847  1.00 50.74           C  
ATOM    764  O   PRO A 770      15.103  -1.888  55.798  1.00 54.51           O  
ATOM    765  CB  PRO A 770      15.805  -3.864  58.324  1.00 46.88           C  
ATOM    766  CG  PRO A 770      16.870  -4.471  59.171  1.00 37.04           C  
ATOM    767  CD  PRO A 770      17.843  -3.349  59.295  1.00 39.01           C  
ATOM    768  N   PHE A 771      15.718  -0.780  57.650  1.00 49.47           N  
ATOM    769  CA  PHE A 771      14.896   0.377  57.343  1.00 45.08           C  
ATOM    770  C   PHE A 771      15.564   1.455  56.499  1.00 49.13           C  
ATOM    771  O   PHE A 771      15.018   2.560  56.337  1.00 45.92           O  
ATOM    772  CB  PHE A 771      14.330   0.938  58.643  1.00 39.19           C  
ATOM    773  CG  PHE A 771      13.423  -0.022  59.350  1.00 54.15           C  
ATOM    774  CD1 PHE A 771      13.932  -0.915  60.284  1.00 42.10           C  
ATOM    775  CD2 PHE A 771      12.059  -0.069  59.047  1.00 49.19           C  
ATOM    776  CE1 PHE A 771      13.101  -1.852  60.913  1.00 40.02           C  
ATOM    777  CE2 PHE A 771      11.223  -0.993  59.663  1.00 48.79           C  
ATOM    778  CZ  PHE A 771      11.747  -1.888  60.601  1.00 45.29           C  
ATOM    779  N   GLY A 772      16.741   1.120  55.964  1.00 42.45           N  
ATOM    780  CA  GLY A 772      17.489   2.033  55.119  1.00 42.54           C  
ATOM    781  C   GLY A 772      17.961   3.315  55.768  1.00 43.91           C  
ATOM    782  O   GLY A 772      17.986   3.412  56.992  1.00 54.66           O  
ATOM    783  N   CYS A 773      18.316   4.305  54.947  1.00 45.01           N  
ATOM    784  CA  CYS A 773      18.810   5.587  55.443  1.00 48.25           C  
ATOM    785  C   CYS A 773      17.716   6.453  56.069  1.00 48.24           C  
ATOM    786  O   CYS A 773      16.572   6.447  55.616  1.00 53.93           O  
ATOM    787  CB  CYS A 773      19.566   6.358  54.350  1.00 49.39           C  
ATOM    788  SG  CYS A 773      18.542   7.150  53.121  1.00 64.70           S  
ATOM    789  N   LEU A 774      18.110   7.204  57.099  1.00 45.51           N  
ATOM    790  CA  LEU A 774      17.238   8.075  57.877  1.00 45.93           C  
ATOM    791  C   LEU A 774      16.503   9.156  57.090  1.00 42.62           C  
ATOM    792  O   LEU A 774      15.345   9.434  57.379  1.00 44.08           O  
ATOM    793  CB  LEU A 774      18.028   8.701  59.035  1.00 37.86           C  
ATOM    794  CG  LEU A 774      17.224   9.366  60.153  1.00 42.91           C  
ATOM    795  CD1 LEU A 774      16.227   8.375  60.729  1.00 38.44           C  
ATOM    796  CD2 LEU A 774      18.153   9.886  61.235  1.00 47.66           C  
ATOM    797  N   LEU A 775      17.179   9.768  56.121  1.00 44.71           N  
ATOM    798  CA  LEU A 775      16.583  10.797  55.273  1.00 45.97           C  
ATOM    799  C   LEU A 775      15.309  10.283  54.631  1.00 52.57           C  
ATOM    800  O   LEU A 775      14.226  10.821  54.880  1.00 59.37           O  
ATOM    801  CB  LEU A 775      17.543  11.226  54.166  1.00 41.57           C  
ATOM    802  CG  LEU A 775      17.033  12.336  53.239  1.00 59.61           C  
ATOM    803  CD1 LEU A 775      16.790  13.618  54.043  1.00 51.15           C  
ATOM    804  CD2 LEU A 775      18.051  12.595  52.119  1.00 44.66           C  
ATOM    805  N   ASP A 776      15.419   9.232  53.825  1.00 47.02           N  
ATOM    806  CA  ASP A 776      14.224   8.698  53.191  1.00 54.22           C  
ATOM    807  C   ASP A 776      13.247   8.165  54.195  1.00 51.83           C  
ATOM    808  O   ASP A 776      12.045   8.153  53.936  1.00 54.00           O  
ATOM    809  CB  ASP A 776      14.544   7.621  52.157  1.00 63.93           C  
ATOM    810  CG  ASP A 776      15.193   8.192  50.919  1.00 78.52           C  
ATOM    811  OD1 ASP A 776      16.228   7.634  50.489  1.00 91.07           O  
ATOM    812  OD2 ASP A 776      14.676   9.209  50.391  1.00 90.46           O  
ATOM    813  N   TYR A 777      13.746   7.736  55.349  1.00 47.56           N  
ATOM    814  CA  TYR A 777      12.849   7.220  56.374  1.00 51.27           C  
ATOM    815  C   TYR A 777      11.915   8.325  56.909  1.00 53.80           C  
ATOM    816  O   TYR A 777      10.698   8.130  56.987  1.00 51.44           O  
ATOM    817  CB  TYR A 777      13.631   6.552  57.508  1.00 52.40           C  
ATOM    818  CG  TYR A 777      12.740   5.855  58.502  1.00 47.33           C  
ATOM    819  CD1 TYR A 777      12.351   4.540  58.306  1.00 42.51           C  
ATOM    820  CD2 TYR A 777      12.245   6.533  59.620  1.00 50.30           C  
ATOM    821  CE1 TYR A 777      11.483   3.907  59.195  1.00 47.64           C  
ATOM    822  CE2 TYR A 777      11.380   5.917  60.513  1.00 40.37           C  
ATOM    823  CZ  TYR A 777      10.998   4.601  60.295  1.00 58.35           C  
ATOM    824  OH  TYR A 777      10.119   3.984  61.160  1.00 61.78           O  
ATOM    825  N   VAL A 778      12.463   9.497  57.227  1.00 50.37           N  
ATOM    826  CA  VAL A 778      11.612  10.569  57.729  1.00 57.80           C  
ATOM    827  C   VAL A 778      10.652  11.051  56.646  1.00 61.51           C  
ATOM    828  O   VAL A 778       9.542  11.486  56.945  1.00 63.01           O  
ATOM    829  CB  VAL A 778      12.399  11.767  58.330  1.00 44.85           C  
ATOM    830  CG1 VAL A 778      13.212  11.319  59.516  1.00 36.50           C  
ATOM    831  CG2 VAL A 778      13.268  12.433  57.293  1.00 31.46           C  
ATOM    832  N   ARG A 779      11.068  10.934  55.387  1.00 60.95           N  
ATOM    833  CA  ARG A 779      10.221  11.346  54.275  1.00 56.05           C  
ATOM    834  C   ARG A 779       8.988  10.449  54.107  1.00 56.04           C  
ATOM    835  O   ARG A 779       7.855  10.934  54.054  1.00 61.52           O  
ATOM    836  CB  ARG A 779      11.017  11.398  52.979  1.00 45.27           C  
ATOM    837  CG  ARG A 779      11.913  12.607  52.844  1.00 33.64           C  
ATOM    838  CD  ARG A 779      12.778  12.486  51.598  1.00 34.97           C  
ATOM    839  NE  ARG A 779      13.648  13.643  51.403  1.00 36.19           N  
ATOM    840  CZ  ARG A 779      14.596  13.716  50.468  1.00 55.14           C  
ATOM    841  NH1 ARG A 779      14.788  12.685  49.647  1.00 56.28           N  
ATOM    842  NH2 ARG A 779      15.356  14.814  50.349  1.00 34.22           N  
ATOM    843  N   GLU A 780       9.183   9.145  54.059  1.00 51.97           N  
ATOM    844  CA  GLU A 780       8.027   8.300  53.897  1.00 60.68           C  
ATOM    845  C   GLU A 780       7.336   7.921  55.198  1.00 62.37           C  
ATOM    846  O   GLU A 780       6.592   6.941  55.245  1.00 74.01           O  
ATOM    847  CB  GLU A 780       8.329   7.075  53.015  1.00 71.86           C  
ATOM    848  CG  GLU A 780       8.824   5.833  53.726  1.00 76.77           C  
ATOM    849  CD  GLU A 780       8.651   4.577  52.874  1.00104.17           C  
ATOM    850  OE1 GLU A 780       9.176   4.549  51.735  1.00112.27           O  
ATOM    851  OE2 GLU A 780       7.979   3.625  53.339  1.00100.28           O  
ATOM    852  N   HIS A 781       7.572   8.684  56.259  1.00 61.36           N  
ATOM    853  CA  HIS A 781       6.900   8.397  57.528  1.00 58.52           C  
ATOM    854  C   HIS A 781       6.506   9.666  58.306  1.00 57.06           C  
ATOM    855  O   HIS A 781       6.030   9.559  59.433  1.00 53.86           O  
ATOM    856  CB  HIS A 781       7.734   7.452  58.423  1.00 55.60           C  
ATOM    857  CG  HIS A 781       7.904   6.062  57.880  1.00 64.59           C  
ATOM    858  ND1 HIS A 781       9.013   5.669  57.160  1.00 58.35           N  
ATOM    859  CD2 HIS A 781       7.109   4.965  57.966  1.00 64.03           C  
ATOM    860  CE1 HIS A 781       8.894   4.395  56.824  1.00 61.92           C  
ATOM    861  NE2 HIS A 781       7.747   3.946  57.301  1.00 56.37           N  
ATOM    862  N   LYS A 782       6.663  10.848  57.690  1.00 55.91           N  
ATOM    863  CA  LYS A 782       6.326  12.144  58.320  1.00 63.44           C  
ATOM    864  C   LYS A 782       5.097  12.098  59.232  1.00 71.56           C  
ATOM    865  O   LYS A 782       5.121  12.598  60.358  1.00 82.57           O  
ATOM    866  CB  LYS A 782       6.010  13.241  57.285  1.00 64.38           C  
ATOM    867  CG  LYS A 782       6.653  13.152  55.915  1.00 84.37           C  
ATOM    868  CD  LYS A 782       5.941  14.098  54.933  1.00 86.64           C  
ATOM    869  CE  LYS A 782       6.654  14.195  53.573  1.00 92.68           C  
ATOM    870  NZ  LYS A 782       7.919  15.015  53.619  1.00 93.68           N  
ATOM    871  N   ASP A 783       4.011  11.529  58.717  1.00 70.30           N  
ATOM    872  CA  ASP A 783       2.746  11.453  59.441  1.00 73.87           C  
ATOM    873  C   ASP A 783       2.715  10.520  60.648  1.00 67.87           C  
ATOM    874  O   ASP A 783       1.674  10.372  61.287  1.00 74.14           O  
ATOM    875  CB  ASP A 783       1.604  11.092  58.472  1.00 82.36           C  
ATOM    876  CG  ASP A 783       1.507  12.049  57.278  1.00 81.42           C  
ATOM    877  OD1 ASP A 783       1.768  13.263  57.440  1.00 86.89           O  
ATOM    878  OD2 ASP A 783       1.167  11.582  56.168  1.00 86.70           O  
ATOM    879  N   ASN A 784       3.843   9.896  60.961  1.00 62.82           N  
ATOM    880  CA  ASN A 784       3.915   8.974  62.091  1.00 69.72           C  
ATOM    881  C   ASN A 784       5.193   9.144  62.910  1.00 71.25           C  
ATOM    882  O   ASN A 784       5.564   8.250  63.681  1.00 76.82           O  
ATOM    883  CB  ASN A 784       3.832   7.512  61.616  1.00 90.63           C  
ATOM    884  CG  ASN A 784       2.446   7.119  61.138  1.00107.35           C  
ATOM    885  OD1 ASN A 784       1.608   6.669  61.926  1.00105.06           O  
ATOM    886  ND2 ASN A 784       2.205   7.261  59.837  1.00103.68           N  
ATOM    887  N   ILE A 785       5.882  10.267  62.734  1.00 61.17           N  
ATOM    888  CA  ILE A 785       7.112  10.496  63.475  1.00 55.69           C  
ATOM    889  C   ILE A 785       6.895  11.507  64.590  1.00 53.27           C  
ATOM    890  O   ILE A 785       6.709  12.700  64.349  1.00 51.26           O  
ATOM    891  CB  ILE A 785       8.250  10.919  62.533  1.00 59.66           C  
ATOM    892  CG1 ILE A 785       8.606   9.748  61.607  1.00 53.69           C  
ATOM    893  CG2 ILE A 785       9.466  11.321  63.330  1.00 42.75           C  
ATOM    894  CD1 ILE A 785       9.490  10.135  60.435  1.00 38.87           C  
ATOM    895  N   GLY A 786       6.879  11.000  65.816  1.00 52.36           N  
ATOM    896  CA  GLY A 786       6.673  11.848  66.973  1.00 48.87           C  
ATOM    897  C   GLY A 786       7.954  12.390  67.568  1.00 52.55           C  
ATOM    898  O   GLY A 786       9.018  11.785  67.435  1.00 57.72           O  
ATOM    899  N   SER A 787       7.820  13.493  68.300  1.00 49.41           N  
ATOM    900  CA  SER A 787       8.932  14.186  68.935  1.00 46.89           C  
ATOM    901  C   SER A 787       9.927  13.323  69.710  1.00 44.61           C  
ATOM    902  O   SER A 787      11.097  13.669  69.793  1.00 45.04           O  
ATOM    903  CB  SER A 787       8.397  15.290  69.840  1.00 42.00           C  
ATOM    904  OG  SER A 787       7.544  14.743  70.825  1.00 47.09           O  
ATOM    905  N   GLN A 788       9.465  12.223  70.295  1.00 38.92           N  
ATOM    906  CA  GLN A 788      10.360  11.363  71.045  1.00 47.50           C  
ATOM    907  C   GLN A 788      11.384  10.692  70.127  1.00 49.03           C  
ATOM    908  O   GLN A 788      12.556  10.538  70.488  1.00 50.47           O  
ATOM    909  CB  GLN A 788       9.579  10.305  71.798  1.00 35.97           C  
ATOM    910  CG  GLN A 788      10.434   9.463  72.716  1.00 41.45           C  
ATOM    911  CD  GLN A 788      11.013  10.269  73.861  1.00 66.83           C  
ATOM    912  OE1 GLN A 788      10.393  10.386  74.922  1.00 81.93           O  
ATOM    913  NE2 GLN A 788      12.207  10.833  73.656  1.00 64.85           N  
ATOM    914  N   TYR A 789      10.931  10.294  68.946  1.00 45.79           N  
ATOM    915  CA  TYR A 789      11.806   9.658  67.986  1.00 41.58           C  
ATOM    916  C   TYR A 789      12.807  10.654  67.428  1.00 41.47           C  
ATOM    917  O   TYR A 789      14.010  10.362  67.353  1.00 41.43           O  
ATOM    918  CB  TYR A 789      11.001   8.993  66.880  1.00 44.50           C  
ATOM    919  CG  TYR A 789      10.392   7.671  67.290  1.00 41.58           C  
ATOM    920  CD1 TYR A 789       9.295   7.610  68.142  1.00 60.46           C  
ATOM    921  CD2 TYR A 789      10.902   6.482  66.804  1.00 62.73           C  
ATOM    922  CE1 TYR A 789       8.723   6.389  68.493  1.00 59.32           C  
ATOM    923  CE2 TYR A 789      10.344   5.261  67.148  1.00 64.34           C  
ATOM    924  CZ  TYR A 789       9.259   5.218  67.989  1.00 68.15           C  
ATOM    925  OH  TYR A 789       8.732   3.989  68.321  1.00 79.92           O  
ATOM    926  N   LEU A 790      12.339  11.851  67.093  1.00 40.35           N  
ATOM    927  CA  LEU A 790      13.255  12.869  66.579  1.00 37.27           C  
ATOM    928  C   LEU A 790      14.393  13.182  67.555  1.00 36.86           C  
ATOM    929  O   LEU A 790      15.572  13.142  67.178  1.00 41.71           O  
ATOM    930  CB  LEU A 790      12.508  14.141  66.222  1.00 34.87           C  
ATOM    931  CG  LEU A 790      11.669  14.039  64.944  1.00 50.24           C  
ATOM    932  CD1 LEU A 790      10.695  15.208  64.816  1.00 49.40           C  
ATOM    933  CD2 LEU A 790      12.611  14.011  63.755  1.00 45.56           C  
ATOM    934  N   LEU A 791      14.047  13.426  68.818  1.00 35.56           N  
ATOM    935  CA  LEU A 791      15.044  13.755  69.839  1.00 37.69           C  
ATOM    936  C   LEU A 791      15.975  12.598  70.185  1.00 34.67           C  
ATOM    937  O   LEU A 791      17.150  12.831  70.435  1.00 40.14           O  
ATOM    938  CB  LEU A 791      14.382  14.340  71.091  1.00 39.36           C  
ATOM    939  CG  LEU A 791      13.677  15.661  70.770  1.00 36.13           C  
ATOM    940  CD1 LEU A 791      12.700  16.007  71.870  1.00 41.31           C  
ATOM    941  CD2 LEU A 791      14.679  16.797  70.527  1.00 37.25           C  
ATOM    942  N   ASN A 792      15.458  11.370  70.235  1.00 30.38           N  
ATOM    943  CA  ASN A 792      16.315  10.202  70.489  1.00 38.22           C  
ATOM    944  C   ASN A 792      17.323  10.028  69.332  1.00 38.88           C  
ATOM    945  O   ASN A 792      18.470   9.664  69.571  1.00 41.61           O  
ATOM    946  CB  ASN A 792      15.507   8.905  70.660  1.00 34.49           C  
ATOM    947  CG  ASN A 792      14.829   8.794  72.036  1.00 63.91           C  
ATOM    948  OD1 ASN A 792      15.047   9.615  72.931  1.00 55.49           O  
ATOM    949  ND2 ASN A 792      14.019   7.752  72.208  1.00 50.57           N  
ATOM    950  N   TRP A 793      16.917  10.300  68.087  1.00 33.17           N  
ATOM    951  CA  TRP A 793      17.867  10.174  66.978  1.00 33.22           C  
ATOM    952  C   TRP A 793      18.986  11.198  67.131  1.00 29.40           C  
ATOM    953  O   TRP A 793      20.143  10.866  66.921  1.00 40.35           O  
ATOM    954  CB  TRP A 793      17.196  10.306  65.604  1.00 28.42           C  
ATOM    955  CG  TRP A 793      16.246   9.195  65.314  1.00 28.39           C  
ATOM    956  CD1 TRP A 793      16.295   7.929  65.818  1.00 24.44           C  
ATOM    957  CD2 TRP A 793      15.072   9.253  64.485  1.00 21.75           C  
ATOM    958  NE1 TRP A 793      15.217   7.187  65.357  1.00 27.89           N  
ATOM    959  CE2 TRP A 793      14.459   7.976  64.533  1.00 22.72           C  
ATOM    960  CE3 TRP A 793      14.482  10.252  63.709  1.00 26.78           C  
ATOM    961  CZ2 TRP A 793      13.289   7.677  63.829  1.00 31.94           C  
ATOM    962  CZ3 TRP A 793      13.309   9.954  63.005  1.00 26.47           C  
ATOM    963  CH2 TRP A 793      12.732   8.678  63.070  1.00 24.30           C  
ATOM    964  N   CYS A 794      18.656  12.420  67.557  1.00 34.46           N  
ATOM    965  CA  CYS A 794      19.671  13.454  67.761  1.00 29.94           C  
ATOM    966  C   CYS A 794      20.667  13.036  68.849  1.00 36.44           C  
ATOM    967  O   CYS A 794      21.868  13.279  68.724  1.00 43.89           O  
ATOM    968  CB  CYS A 794      19.030  14.778  68.127  1.00 35.59           C  
ATOM    969  SG  CYS A 794      18.079  15.523  66.796  1.00 34.86           S  
ATOM    970  N   VAL A 795      20.174  12.370  69.888  1.00 33.82           N  
ATOM    971  CA  VAL A 795      21.039  11.899  70.968  1.00 36.82           C  
ATOM    972  C   VAL A 795      21.974  10.804  70.433  1.00 39.85           C  
ATOM    973  O   VAL A 795      23.185  10.868  70.626  1.00 36.93           O  
ATOM    974  CB  VAL A 795      20.207  11.329  72.173  1.00 32.68           C  
ATOM    975  CG1 VAL A 795      21.099  10.583  73.129  1.00 22.10           C  
ATOM    976  CG2 VAL A 795      19.544  12.458  72.936  1.00 31.09           C  
ATOM    977  N   GLN A 796      21.391   9.806  69.769  1.00 41.72           N  
ATOM    978  CA  GLN A 796      22.124   8.679  69.197  1.00 33.94           C  
ATOM    979  C   GLN A 796      23.180   9.109  68.195  1.00 41.14           C  
ATOM    980  O   GLN A 796      24.333   8.636  68.242  1.00 31.84           O  
ATOM    981  CB  GLN A 796      21.145   7.704  68.562  1.00 34.71           C  
ATOM    982  CG  GLN A 796      20.380   6.910  69.622  1.00 35.30           C  
ATOM    983  CD  GLN A 796      19.397   5.936  69.035  1.00 39.76           C  
ATOM    984  OE1 GLN A 796      19.566   5.463  67.910  1.00 56.49           O  
ATOM    985  NE2 GLN A 796      18.360   5.622  69.790  1.00 47.78           N  
ATOM    986  N   ILE A 797      22.804  10.025  67.302  1.00 33.81           N  
ATOM    987  CA  ILE A 797      23.754  10.501  66.317  1.00 34.05           C  
ATOM    988  C   ILE A 797      24.864  11.244  67.060  1.00 39.39           C  
ATOM    989  O   ILE A 797      26.021  11.106  66.709  1.00 41.02           O  
ATOM    990  CB  ILE A 797      23.096  11.422  65.272  1.00 37.63           C  
ATOM    991  CG1 ILE A 797      22.082  10.634  64.450  1.00 22.87           C  
ATOM    992  CG2 ILE A 797      24.174  12.076  64.368  1.00 19.73           C  
ATOM    993  CD1 ILE A 797      21.257  11.506  63.506  1.00 33.35           C  
ATOM    994  N   ALA A 798      24.520  12.004  68.102  1.00 41.25           N  
ATOM    995  CA  ALA A 798      25.530  12.733  68.873  1.00 38.55           C  
ATOM    996  C   ALA A 798      26.474  11.784  69.623  1.00 41.17           C  
ATOM    997  O   ALA A 798      27.667  12.066  69.761  1.00 41.95           O  
ATOM    998  CB  ALA A 798      24.882  13.696  69.831  1.00 24.12           C  
ATOM    999  N   LYS A 799      25.945  10.662  70.099  1.00 36.30           N  
ATOM   1000  CA  LYS A 799      26.766   9.678  70.787  1.00 30.80           C  
ATOM   1001  C   LYS A 799      27.768   9.052  69.823  1.00 37.84           C  
ATOM   1002  O   LYS A 799      28.948   8.934  70.149  1.00 43.91           O  
ATOM   1003  CB  LYS A 799      25.908   8.577  71.371  1.00 23.13           C  
ATOM   1004  CG  LYS A 799      25.154   8.978  72.581  1.00 35.42           C  
ATOM   1005  CD  LYS A 799      24.384   7.804  73.169  1.00 25.21           C  
ATOM   1006  CE  LYS A 799      23.772   8.278  74.495  1.00 38.54           C  
ATOM   1007  NZ  LYS A 799      23.067   7.230  75.242  1.00 39.23           N  
ATOM   1008  N   GLY A 800      27.280   8.631  68.650  1.00 39.67           N  
ATOM   1009  CA  GLY A 800      28.136   8.037  67.637  1.00 24.71           C  
ATOM   1010  C   GLY A 800      29.265   8.986  67.264  1.00 43.88           C  
ATOM   1011  O   GLY A 800      30.439   8.592  67.210  1.00 48.37           O  
ATOM   1012  N   MET A 801      28.920  10.253  67.061  1.00 37.65           N  
ATOM   1013  CA  MET A 801      29.900  11.252  66.684  1.00 40.81           C  
ATOM   1014  C   MET A 801      30.933  11.512  67.781  1.00 40.95           C  
ATOM   1015  O   MET A 801      32.118  11.707  67.483  1.00 35.77           O  
ATOM   1016  CB  MET A 801      29.216  12.558  66.277  1.00 28.88           C  
ATOM   1017  CG  MET A 801      28.439  12.450  65.002  1.00 43.04           C  
ATOM   1018  SD  MET A 801      29.361  11.787  63.564  1.00 39.80           S  
ATOM   1019  CE  MET A 801      30.593  13.030  63.460  1.00 26.65           C  
ATOM   1020  N   ASN A 802      30.488  11.546  69.039  1.00 41.67           N  
ATOM   1021  CA  ASN A 802      31.397  11.781  70.168  1.00 38.89           C  
ATOM   1022  C   ASN A 802      32.385  10.623  70.197  1.00 38.51           C  
ATOM   1023  O   ASN A 802      33.570  10.831  70.432  1.00 36.70           O  
ATOM   1024  CB  ASN A 802      30.634  11.867  71.498  1.00 31.21           C  
ATOM   1025  CG  ASN A 802      31.562  11.946  72.722  1.00 38.28           C  
ATOM   1026  OD1 ASN A 802      32.309  12.913  72.899  1.00 48.15           O  
ATOM   1027  ND2 ASN A 802      31.501  10.932  73.575  1.00 30.97           N  
ATOM   1028  N   TYR A 803      31.896   9.421  69.888  1.00 39.61           N  
ATOM   1029  CA  TYR A 803      32.737   8.235  69.849  1.00 40.41           C  
ATOM   1030  C   TYR A 803      33.800   8.433  68.778  1.00 43.10           C  
ATOM   1031  O   TYR A 803      34.993   8.283  69.055  1.00 40.86           O  
ATOM   1032  CB  TYR A 803      31.924   6.976  69.556  1.00 38.80           C  
ATOM   1033  CG  TYR A 803      32.803   5.768  69.290  1.00 51.05           C  
ATOM   1034  CD1 TYR A 803      33.389   5.058  70.341  1.00 40.82           C  
ATOM   1035  CD2 TYR A 803      33.097   5.372  67.984  1.00 41.58           C  
ATOM   1036  CE1 TYR A 803      34.247   3.989  70.098  1.00 33.20           C  
ATOM   1037  CE2 TYR A 803      33.955   4.304  67.727  1.00 43.12           C  
ATOM   1038  CZ  TYR A 803      34.524   3.618  68.781  1.00 51.70           C  
ATOM   1039  OH  TYR A 803      35.357   2.563  68.503  1.00 52.98           O  
ATOM   1040  N   LEU A 804      33.367   8.790  67.569  1.00 36.41           N  
ATOM   1041  CA  LEU A 804      34.305   9.033  66.481  1.00 37.21           C  
ATOM   1042  C   LEU A 804      35.352  10.039  66.903  1.00 42.76           C  
ATOM   1043  O   LEU A 804      36.517   9.849  66.610  1.00 48.28           O  
ATOM   1044  CB  LEU A 804      33.600   9.520  65.210  1.00 26.16           C  
ATOM   1045  CG  LEU A 804      32.777   8.438  64.508  1.00 32.34           C  
ATOM   1046  CD1 LEU A 804      32.304   8.975  63.201  1.00 33.22           C  
ATOM   1047  CD2 LEU A 804      33.613   7.173  64.286  1.00 22.83           C  
ATOM   1048  N   GLU A 805      34.949  11.078  67.637  1.00 48.63           N  
ATOM   1049  CA  GLU A 805      35.894  12.103  68.091  1.00 45.78           C  
ATOM   1050  C   GLU A 805      36.916  11.506  69.060  1.00 46.23           C  
ATOM   1051  O   GLU A 805      38.102  11.821  69.002  1.00 49.92           O  
ATOM   1052  CB  GLU A 805      35.173  13.282  68.739  1.00 38.63           C  
ATOM   1053  CG  GLU A 805      36.136  14.387  69.171  1.00 48.99           C  
ATOM   1054  CD  GLU A 805      35.468  15.702  69.557  1.00 53.77           C  
ATOM   1055  OE1 GLU A 805      34.248  15.865  69.349  1.00 61.76           O  
ATOM   1056  OE2 GLU A 805      36.182  16.592  70.064  1.00 69.17           O  
ATOM   1057  N   ASP A 806      36.450  10.633  69.940  1.00 43.87           N  
ATOM   1058  CA  ASP A 806      37.326   9.969  70.882  1.00 42.71           C  
ATOM   1059  C   ASP A 806      38.347   9.122  70.109  1.00 47.19           C  
ATOM   1060  O   ASP A 806      39.509   9.032  70.486  1.00 48.32           O  
ATOM   1061  CB  ASP A 806      36.504   9.064  71.805  1.00 45.74           C  
ATOM   1062  CG  ASP A 806      35.943   9.801  73.009  1.00 55.06           C  
ATOM   1063  OD1 ASP A 806      36.425  10.915  73.305  1.00 65.72           O  
ATOM   1064  OD2 ASP A 806      35.035   9.255  73.675  1.00 59.34           O  
ATOM   1065  N   ARG A 807      37.915   8.556  68.990  1.00 45.21           N  
ATOM   1066  CA  ARG A 807      38.774   7.703  68.186  1.00 47.26           C  
ATOM   1067  C   ARG A 807      39.634   8.571  67.281  1.00 50.53           C  
ATOM   1068  O   ARG A 807      40.458   8.074  66.523  1.00 56.70           O  
ATOM   1069  CB  ARG A 807      37.890   6.740  67.376  1.00 36.57           C  
ATOM   1070  CG  ARG A 807      38.601   5.639  66.634  1.00 74.03           C  
ATOM   1071  CD  ARG A 807      39.130   4.547  67.552  1.00 85.23           C  
ATOM   1072  NE  ARG A 807      39.844   3.522  66.792  1.00 80.58           N  
ATOM   1073  CZ  ARG A 807      40.957   3.740  66.088  1.00 88.96           C  
ATOM   1074  NH1 ARG A 807      41.502   4.948  66.033  1.00 71.64           N  
ATOM   1075  NH2 ARG A 807      41.550   2.737  65.459  1.00 89.67           N  
ATOM   1076  N   ARG A 808      39.467   9.882  67.414  1.00 48.61           N  
ATOM   1077  CA  ARG A 808      40.186  10.860  66.604  1.00 47.56           C  
ATOM   1078  C   ARG A 808      39.818  10.788  65.131  1.00 45.27           C  
ATOM   1079  O   ARG A 808      40.637  11.061  64.266  1.00 50.55           O  
ATOM   1080  CB  ARG A 808      41.702  10.729  66.782  1.00 52.89           C  
ATOM   1081  CG  ARG A 808      42.196  11.179  68.144  1.00 69.77           C  
ATOM   1082  CD  ARG A 808      43.713  11.261  68.220  1.00 69.15           C  
ATOM   1083  NE  ARG A 808      44.099  11.842  69.500  1.00 94.06           N  
ATOM   1084  CZ  ARG A 808      44.409  13.122  69.683  1.00100.61           C  
ATOM   1085  NH1 ARG A 808      44.399  13.965  68.655  1.00 92.39           N  
ATOM   1086  NH2 ARG A 808      44.662  13.571  70.908  1.00105.11           N  
ATOM   1087  N   LEU A 809      38.565  10.467  64.849  1.00 43.95           N  
ATOM   1088  CA  LEU A 809      38.110  10.376  63.473  1.00 45.44           C  
ATOM   1089  C   LEU A 809      37.174  11.523  63.054  1.00 37.65           C  
ATOM   1090  O   LEU A 809      36.206  11.803  63.733  1.00 50.68           O  
ATOM   1091  CB  LEU A 809      37.406   9.049  63.268  1.00 43.62           C  
ATOM   1092  CG  LEU A 809      37.172   8.774  61.796  1.00 61.18           C  
ATOM   1093  CD1 LEU A 809      38.510   8.410  61.181  1.00 79.13           C  
ATOM   1094  CD2 LEU A 809      36.186   7.647  61.617  1.00 79.36           C  
ATOM   1095  N   VAL A 810      37.473  12.166  61.933  1.00 33.61           N  
ATOM   1096  CA  VAL A 810      36.674  13.254  61.405  1.00 33.29           C  
ATOM   1097  C   VAL A 810      35.856  12.732  60.204  1.00 43.06           C  
ATOM   1098  O   VAL A 810      36.368  12.615  59.105  1.00 60.59           O  
ATOM   1099  CB  VAL A 810      37.598  14.456  61.002  1.00 44.36           C  
ATOM   1100  CG1 VAL A 810      36.851  15.494  60.205  1.00 33.29           C  
ATOM   1101  CG2 VAL A 810      38.180  15.114  62.237  1.00 32.62           C  
ATOM   1102  N   HIS A 811      34.667  12.326  60.533  1.00 44.15           N  
ATOM   1103  CA  HIS A 811      33.711  11.967  59.538  1.00 42.88           C  
ATOM   1104  C   HIS A 811      33.869  12.518  58.168  1.00 50.87           C  
ATOM   1105  O   HIS A 811      34.642  11.883  57.384  1.00 79.26           O  
ATOM   1106  CB  HIS A 811      32.399  11.429  59.969  1.00 29.72           C  
ATOM   1107  CG  HIS A 811      31.482  10.742  59.051  1.00 26.61           C  
ATOM   1108  ND1 HIS A 811      30.777  11.308  58.034  1.00 26.25           N  
ATOM   1109  CD2 HIS A 811      31.041   9.439  59.073  1.00 26.55           C  
ATOM   1110  CE1 HIS A 811      30.038  10.434  57.399  1.00 25.30           C  
ATOM   1111  NE2 HIS A 811      30.158   9.279  58.040  1.00 29.81           N  
ATOM   1112  N   ARG A 812      33.654  13.795  57.914  1.00 43.22           N  
ATOM   1113  CA  ARG A 812      33.687  14.489  56.673  1.00 40.79           C  
ATOM   1114  C   ARG A 812      32.524  14.338  55.738  1.00 38.63           C  
ATOM   1115  O   ARG A 812      32.283  15.152  54.804  1.00 39.36           O  
ATOM   1116  CB  ARG A 812      34.999  14.790  56.040  1.00 48.30           C  
ATOM   1117  CG  ARG A 812      36.186  15.234  56.822  1.00 46.56           C  
ATOM   1118  CD  ARG A 812      37.458  15.150  56.006  1.00 59.48           C  
ATOM   1119  NE  ARG A 812      37.521  15.981  54.832  1.00 53.74           N  
ATOM   1120  CZ  ARG A 812      37.711  15.608  53.579  1.00 68.23           C  
ATOM   1121  NH1 ARG A 812      37.825  14.340  53.240  1.00 50.67           N  
ATOM   1122  NH2 ARG A 812      37.776  16.537  52.627  1.00 64.39           N  
ATOM   1123  N   ASP A 813      31.466  13.574  56.067  1.00 33.31           N  
ATOM   1124  CA  ASP A 813      30.284  13.508  55.232  1.00 36.43           C  
ATOM   1125  C   ASP A 813      29.051  13.099  56.051  1.00 44.24           C  
ATOM   1126  O   ASP A 813      28.286  12.201  55.672  1.00 38.40           O  
ATOM   1127  CB  ASP A 813      30.529  12.559  54.046  1.00 33.59           C  
ATOM   1128  CG  ASP A 813      29.416  12.603  53.004  1.00 46.44           C  
ATOM   1129  OD1 ASP A 813      28.721  13.633  52.893  1.00 58.19           O  
ATOM   1130  OD2 ASP A 813      29.230  11.599  52.290  1.00 53.78           O  
ATOM   1131  N   LEU A 814      28.860  13.785  57.173  1.00 44.31           N  
ATOM   1132  CA  LEU A 814      27.734  13.515  58.055  1.00 38.77           C  
ATOM   1133  C   LEU A 814      26.515  14.207  57.486  1.00 36.03           C  
ATOM   1134  O   LEU A 814      26.532  15.412  57.294  1.00 27.43           O  
ATOM   1135  CB  LEU A 814      28.015  14.060  59.462  1.00 47.33           C  
ATOM   1136  CG  LEU A 814      26.903  13.902  60.512  1.00 47.51           C  
ATOM   1137  CD1 LEU A 814      26.356  12.463  60.541  1.00 36.48           C  
ATOM   1138  CD2 LEU A 814      27.450  14.300  61.868  1.00 36.58           C  
ATOM   1139  N   ALA A 815      25.433  13.454  57.320  1.00 31.91           N  
ATOM   1140  CA  ALA A 815      24.198  13.990  56.774  1.00 30.48           C  
ATOM   1141  C   ALA A 815      23.151  12.900  56.943  1.00 38.98           C  
ATOM   1142  O   ALA A 815      23.513  11.738  57.146  1.00 39.49           O  
ATOM   1143  CB  ALA A 815      24.393  14.318  55.326  1.00 26.08           C  
ATOM   1144  N   ALA A 816      21.864  13.254  56.880  1.00 36.62           N  
ATOM   1145  CA  ALA A 816      20.812  12.244  57.062  1.00 36.89           C  
ATOM   1146  C   ALA A 816      20.942  11.013  56.161  1.00 34.00           C  
ATOM   1147  O   ALA A 816      20.623   9.898  56.579  1.00 45.11           O  
ATOM   1148  CB  ALA A 816      19.402  12.875  56.927  1.00 29.81           C  
ATOM   1149  N   ARG A 817      21.429  11.206  54.935  1.00 45.25           N  
ATOM   1150  CA  ARG A 817      21.578  10.086  53.999  1.00 48.10           C  
ATOM   1151  C   ARG A 817      22.586   9.048  54.494  1.00 44.86           C  
ATOM   1152  O   ARG A 817      22.506   7.886  54.116  1.00 47.75           O  
ATOM   1153  CB  ARG A 817      21.986  10.579  52.598  1.00 34.72           C  
ATOM   1154  CG  ARG A 817      23.366  11.192  52.520  1.00 44.13           C  
ATOM   1155  CD  ARG A 817      23.628  11.823  51.138  1.00 41.71           C  
ATOM   1156  NE  ARG A 817      24.198  13.163  51.290  1.00 44.49           N  
ATOM   1157  CZ  ARG A 817      25.471  13.403  51.581  1.00 57.10           C  
ATOM   1158  NH1 ARG A 817      26.327  12.396  51.723  1.00 70.85           N  
ATOM   1159  NH2 ARG A 817      25.861  14.638  51.848  1.00 48.19           N  
ATOM   1160  N   ASN A 818      23.484   9.475  55.379  1.00 38.66           N  
ATOM   1161  CA  ASN A 818      24.535   8.632  55.917  1.00 40.52           C  
ATOM   1162  C   ASN A 818      24.264   8.145  57.349  1.00 43.40           C  
ATOM   1163  O   ASN A 818      25.191   7.939  58.145  1.00 41.83           O  
ATOM   1164  CB  ASN A 818      25.885   9.370  55.840  1.00 29.76           C  
ATOM   1165  CG  ASN A 818      26.331   9.642  54.406  1.00 40.76           C  
ATOM   1166  OD1 ASN A 818      25.942   8.931  53.475  1.00 41.82           O  
ATOM   1167  ND2 ASN A 818      27.163  10.679  54.223  1.00 29.10           N  
ATOM   1168  N   VAL A 819      22.992   8.022  57.696  1.00 33.68           N  
ATOM   1169  CA  VAL A 819      22.628   7.511  59.007  1.00 36.69           C  
ATOM   1170  C   VAL A 819      21.658   6.416  58.630  1.00 42.20           C  
ATOM   1171  O   VAL A 819      20.719   6.665  57.867  1.00 39.63           O  
ATOM   1172  CB  VAL A 819      21.939   8.582  59.912  1.00 39.03           C  
ATOM   1173  CG1 VAL A 819      21.390   7.942  61.180  1.00 32.60           C  
ATOM   1174  CG2 VAL A 819      22.929   9.666  60.302  1.00 31.20           C  
ATOM   1175  N   LEU A 820      21.942   5.194  59.079  1.00 38.89           N  
ATOM   1176  CA  LEU A 820      21.098   4.056  58.748  1.00 40.83           C  
ATOM   1177  C   LEU A 820      20.188   3.713  59.905  1.00 42.46           C  
ATOM   1178  O   LEU A 820      20.485   4.047  61.049  1.00 41.65           O  
ATOM   1179  CB  LEU A 820      21.959   2.858  58.309  1.00 47.49           C  
ATOM   1180  CG  LEU A 820      22.793   3.129  57.035  1.00 42.68           C  
ATOM   1181  CD1 LEU A 820      23.654   1.948  56.676  1.00 44.67           C  
ATOM   1182  CD2 LEU A 820      21.887   3.463  55.869  1.00 30.23           C  
ATOM   1183  N   VAL A 821      19.067   3.070  59.598  1.00 36.86           N  
ATOM   1184  CA  VAL A 821      18.083   2.707  60.604  1.00 32.03           C  
ATOM   1185  C   VAL A 821      18.030   1.187  60.862  1.00 36.99           C  
ATOM   1186  O   VAL A 821      17.669   0.411  59.974  1.00 41.63           O  
ATOM   1187  CB  VAL A 821      16.683   3.201  60.156  1.00 42.85           C  
ATOM   1188  CG1 VAL A 821      15.654   2.955  61.246  1.00 29.15           C  
ATOM   1189  CG2 VAL A 821      16.729   4.678  59.763  1.00 25.63           C  
ATOM   1190  N   LYS A 822      18.441   0.753  62.051  1.00 34.10           N  
ATOM   1191  CA  LYS A 822      18.403  -0.678  62.395  1.00 43.02           C  
ATOM   1192  C   LYS A 822      16.955  -1.007  62.747  1.00 41.79           C  
ATOM   1193  O   LYS A 822      16.413  -2.027  62.320  1.00 40.06           O  
ATOM   1194  CB  LYS A 822      19.320  -1.002  63.590  1.00 43.66           C  
ATOM   1195  CG  LYS A 822      18.994  -2.347  64.244  1.00 36.78           C  
ATOM   1196  CD  LYS A 822      20.245  -3.112  64.610  1.00 43.51           C  
ATOM   1197  CE  LYS A 822      20.591  -2.972  66.057  1.00 47.74           C  
ATOM   1198  NZ  LYS A 822      20.226  -4.214  66.760  1.00 52.69           N  
ATOM   1199  N   THR A 823      16.376  -0.104  63.539  1.00 45.11           N  
ATOM   1200  CA  THR A 823      14.993  -0.112  64.008  1.00 49.31           C  
ATOM   1201  C   THR A 823      14.647   1.369  64.185  1.00 50.51           C  
ATOM   1202  O   THR A 823      15.542   2.210  64.313  1.00 48.71           O  
ATOM   1203  CB  THR A 823      14.831  -0.764  65.402  1.00 47.80           C  
ATOM   1204  OG1 THR A 823      15.463   0.050  66.393  1.00 60.85           O  
ATOM   1205  CG2 THR A 823      15.433  -2.153  65.432  1.00 43.68           C  
ATOM   1206  N   PRO A 824      13.350   1.711  64.200  1.00 51.63           N  
ATOM   1207  CA  PRO A 824      12.948   3.112  64.373  1.00 48.88           C  
ATOM   1208  C   PRO A 824      13.548   3.725  65.654  1.00 47.85           C  
ATOM   1209  O   PRO A 824      13.749   4.939  65.732  1.00 51.00           O  
ATOM   1210  CB  PRO A 824      11.430   3.010  64.443  1.00 52.73           C  
ATOM   1211  CG  PRO A 824      11.149   1.840  63.524  1.00 57.21           C  
ATOM   1212  CD  PRO A 824      12.176   0.847  63.993  1.00 48.93           C  
ATOM   1213  N   GLN A 825      13.867   2.877  66.631  1.00 38.49           N  
ATOM   1214  CA  GLN A 825      14.466   3.330  67.877  1.00 45.07           C  
ATOM   1215  C   GLN A 825      16.005   3.176  67.972  1.00 48.24           C  
ATOM   1216  O   GLN A 825      16.610   3.470  69.008  1.00 48.28           O  
ATOM   1217  CB  GLN A 825      13.778   2.678  69.096  1.00 42.30           C  
ATOM   1218  CG  GLN A 825      13.343   1.226  68.957  1.00 66.86           C  
ATOM   1219  CD  GLN A 825      11.994   1.054  68.244  1.00 70.98           C  
ATOM   1220  OE1 GLN A 825      11.879   0.264  67.315  1.00 69.95           O  
ATOM   1221  NE2 GLN A 825      10.972   1.778  68.699  1.00 76.17           N  
ATOM   1222  N   HIS A 826      16.651   2.801  66.876  1.00 38.77           N  
ATOM   1223  CA  HIS A 826      18.096   2.613  66.912  1.00 42.02           C  
ATOM   1224  C   HIS A 826      18.764   2.910  65.560  1.00 39.66           C  
ATOM   1225  O   HIS A 826      18.636   2.128  64.615  1.00 42.04           O  
ATOM   1226  CB  HIS A 826      18.406   1.172  67.368  1.00 23.62           C  
ATOM   1227  CG  HIS A 826      19.854   0.918  67.659  1.00 37.86           C  
ATOM   1228  ND1 HIS A 826      20.308  -0.253  68.226  1.00 39.94           N  
ATOM   1229  CD2 HIS A 826      20.956   1.690  67.474  1.00 39.90           C  
ATOM   1230  CE1 HIS A 826      21.619  -0.195  68.380  1.00 36.12           C  
ATOM   1231  NE2 HIS A 826      22.035   0.976  67.932  1.00 38.38           N  
ATOM   1232  N   VAL A 827      19.464   4.037  65.472  1.00 32.91           N  
ATOM   1233  CA  VAL A 827      20.161   4.417  64.239  1.00 35.49           C  
ATOM   1234  C   VAL A 827      21.686   4.429  64.440  1.00 40.79           C  
ATOM   1235  O   VAL A 827      22.166   4.458  65.582  1.00 38.18           O  
ATOM   1236  CB  VAL A 827      19.711   5.805  63.711  1.00 34.84           C  
ATOM   1237  CG1 VAL A 827      18.201   5.828  63.522  1.00 44.64           C  
ATOM   1238  CG2 VAL A 827      20.159   6.925  64.657  1.00 24.65           C  
ATOM   1239  N   LYS A 828      22.431   4.401  63.327  1.00 43.74           N  
ATOM   1240  CA  LYS A 828      23.905   4.400  63.329  1.00 36.35           C  
ATOM   1241  C   LYS A 828      24.485   5.185  62.164  1.00 35.34           C  
ATOM   1242  O   LYS A 828      23.919   5.220  61.070  1.00 43.44           O  
ATOM   1243  CB  LYS A 828      24.458   2.980  63.219  1.00 42.12           C  
ATOM   1244  CG  LYS A 828      23.916   1.974  64.210  1.00 47.39           C  
ATOM   1245  CD  LYS A 828      24.681   0.680  64.073  1.00 48.36           C  
ATOM   1246  CE  LYS A 828      23.978  -0.468  64.761  1.00 34.76           C  
ATOM   1247  NZ  LYS A 828      24.835  -1.702  64.709  1.00 40.58           N  
ATOM   1248  N   ILE A 829      25.655   5.762  62.387  1.00 30.08           N  
ATOM   1249  CA  ILE A 829      26.341   6.538  61.360  1.00 38.70           C  
ATOM   1250  C   ILE A 829      27.096   5.598  60.396  1.00 41.13           C  
ATOM   1251  O   ILE A 829      27.615   4.564  60.805  1.00 46.09           O  
ATOM   1252  CB  ILE A 829      27.335   7.502  62.007  1.00 38.85           C  
ATOM   1253  CG1 ILE A 829      26.610   8.449  62.960  1.00 38.83           C  
ATOM   1254  CG2 ILE A 829      28.042   8.301  60.959  1.00 34.04           C  
ATOM   1255  CD1 ILE A 829      27.569   9.284  63.764  1.00 34.00           C  
ATOM   1256  N   THR A 830      27.187   5.976  59.128  1.00 35.80           N  
ATOM   1257  CA  THR A 830      27.862   5.143  58.157  1.00 40.58           C  
ATOM   1258  C   THR A 830      28.557   5.994  57.099  1.00 46.89           C  
ATOM   1259  O   THR A 830      28.742   7.210  57.293  1.00 46.28           O  
ATOM   1260  CB  THR A 830      26.857   4.149  57.520  1.00 45.84           C  
ATOM   1261  OG1 THR A 830      27.557   3.072  56.887  1.00 55.49           O  
ATOM   1262  CG2 THR A 830      25.974   4.851  56.529  1.00 54.15           C  
ATOM   1263  N  AASP A 831      28.952   5.339  56.003  0.50 46.16           N  
ATOM   1264  N  BASP A 831      28.946   5.352  55.998  0.50 48.15           N  
ATOM   1265  CA AASP A 831      29.643   5.954  54.868  0.50 41.99           C  
ATOM   1266  CA BASP A 831      29.642   5.987  54.876  0.50 45.50           C  
ATOM   1267  C  AASP A 831      30.901   6.726  55.228  0.50 39.76           C  
ATOM   1268  C  BASP A 831      30.902   6.732  55.268  0.50 41.60           C  
ATOM   1269  O  AASP A 831      30.893   7.946  55.282  0.50 40.46           O  
ATOM   1270  O  BASP A 831      30.895   7.948  55.395  0.50 45.22           O  
ATOM   1271  CB AASP A 831      28.683   6.812  54.040  0.50 36.83           C  
ATOM   1272  CB BASP A 831      28.733   6.925  54.078  0.50 49.73           C  
ATOM   1273  CG AASP A 831      27.943   6.002  52.979  0.50 38.86           C  
ATOM   1274  CG BASP A 831      29.347   7.321  52.742  0.50 58.97           C  
ATOM   1275  OD1AASP A 831      28.489   5.849  51.866  0.50 64.02           O  
ATOM   1276  OD1BASP A 831      29.092   6.606  51.755  0.50 72.85           O  
ATOM   1277  OD2AASP A 831      26.827   5.510  53.247  0.50 35.84           O  
ATOM   1278  OD2BASP A 831      30.096   8.321  52.675  0.50 62.80           O  
ATOM   1279  N   PHE A 832      31.996   5.996  55.411  1.00 44.92           N  
ATOM   1280  CA  PHE A 832      33.281   6.583  55.779  1.00 43.17           C  
ATOM   1281  C   PHE A 832      34.200   6.881  54.604  1.00 46.94           C  
ATOM   1282  O   PHE A 832      35.402   7.100  54.784  1.00 45.58           O  
ATOM   1283  CB  PHE A 832      33.974   5.683  56.794  1.00 39.91           C  
ATOM   1284  CG  PHE A 832      33.245   5.605  58.109  1.00 50.66           C  
ATOM   1285  CD1 PHE A 832      32.296   4.619  58.336  1.00 49.56           C  
ATOM   1286  CD2 PHE A 832      33.443   6.573  59.084  1.00 48.51           C  
ATOM   1287  CE1 PHE A 832      31.548   4.610  59.510  1.00 49.07           C  
ATOM   1288  CE2 PHE A 832      32.701   6.568  60.258  1.00 28.64           C  
ATOM   1289  CZ  PHE A 832      31.754   5.591  60.472  1.00 38.59           C  
ATOM   1290  N   GLY A 833      33.602   6.987  53.417  1.00 48.67           N  
ATOM   1291  CA  GLY A 833      34.361   7.265  52.207  1.00 44.97           C  
ATOM   1292  C   GLY A 833      35.294   8.457  52.253  1.00 45.44           C  
ATOM   1293  O   GLY A 833      36.305   8.478  51.570  1.00 58.13           O  
ATOM   1294  N   LEU A 834      34.991   9.440  53.087  1.00 45.82           N  
ATOM   1295  CA  LEU A 834      35.820  10.628  53.168  1.00 36.57           C  
ATOM   1296  C   LEU A 834      36.482  10.795  54.529  1.00 41.93           C  
ATOM   1297  O   LEU A 834      37.194  11.791  54.762  1.00 39.29           O  
ATOM   1298  CB  LEU A 834      34.963  11.856  52.845  1.00 47.53           C  
ATOM   1299  CG  LEU A 834      34.528  12.161  51.399  1.00 55.51           C  
ATOM   1300  CD1 LEU A 834      34.028  10.951  50.650  1.00 80.50           C  
ATOM   1301  CD2 LEU A 834      33.437  13.218  51.422  1.00 66.67           C  
ATOM   1302  N   ALA A 835      36.274   9.822  55.420  1.00 38.33           N  
ATOM   1303  CA  ALA A 835      36.821   9.896  56.783  1.00 44.47           C  
ATOM   1304  C   ALA A 835      38.338   9.874  56.859  1.00 50.84           C  
ATOM   1305  O   ALA A 835      38.983   9.091  56.169  1.00 64.89           O  
ATOM   1306  CB  ALA A 835      36.243   8.774  57.643  1.00 42.10           C  
ATOM   1307  N   LYS A 836      38.904  10.723  57.712  1.00 50.08           N  
ATOM   1308  CA  LYS A 836      40.355  10.801  57.893  1.00 49.52           C  
ATOM   1309  C   LYS A 836      40.717  10.723  59.374  1.00 54.11           C  
ATOM   1310  O   LYS A 836      40.073  11.369  60.193  1.00 62.01           O  
ATOM   1311  CB  LYS A 836      40.897  12.125  57.334  1.00 45.56           C  
ATOM   1312  CG  LYS A 836      40.660  12.360  55.828  1.00 58.47           C  
ATOM   1313  CD  LYS A 836      41.473  11.395  54.978  1.00 61.89           C  
ATOM   1314  CE  LYS A 836      41.264  11.604  53.479  1.00 71.39           C  
ATOM   1315  NZ  LYS A 836      39.915  11.144  53.014  1.00 79.33           N  
ATOM   1316  N   LEU A 837      41.716   9.909  59.726  1.00 59.41           N  
ATOM   1317  CA  LEU A 837      42.172   9.804  61.119  1.00 63.16           C  
ATOM   1318  C   LEU A 837      43.249  10.865  61.352  1.00 64.99           C  
ATOM   1319  O   LEU A 837      44.182  10.982  60.560  1.00 75.83           O  
ATOM   1320  CB  LEU A 837      42.749   8.418  61.423  1.00 65.59           C  
ATOM   1321  CG  LEU A 837      41.804   7.239  61.190  1.00 81.66           C  
ATOM   1322  CD1 LEU A 837      41.731   6.954  59.696  1.00 92.32           C  
ATOM   1323  CD2 LEU A 837      42.271   5.998  61.937  1.00 80.11           C  
ATOM   1324  N   LEU A 838      43.111  11.656  62.411  1.00 61.87           N  
ATOM   1325  CA  LEU A 838      44.081  12.701  62.701  1.00 62.05           C  
ATOM   1326  C   LEU A 838      45.183  12.173  63.595  1.00 72.70           C  
ATOM   1327  O   LEU A 838      44.956  11.266  64.396  1.00 76.57           O  
ATOM   1328  CB  LEU A 838      43.421  13.882  63.401  1.00 57.41           C  
ATOM   1329  CG  LEU A 838      42.195  14.552  62.785  1.00 64.73           C  
ATOM   1330  CD1 LEU A 838      41.809  15.776  63.636  1.00 43.22           C  
ATOM   1331  CD2 LEU A 838      42.460  14.953  61.351  1.00 53.73           C  
ATOM   1332  N   GLY A 839      46.368  12.768  63.476  1.00 75.85           N  
ATOM   1333  CA  GLY A 839      47.498  12.363  64.293  1.00 76.63           C  
ATOM   1334  C   GLY A 839      47.292  12.628  65.775  1.00 80.92           C  
ATOM   1335  O   GLY A 839      46.178  12.903  66.229  1.00 82.23           O  
ATOM   1336  N   ALA A 840      48.365  12.506  66.545  1.00 86.34           N  
ATOM   1337  CA  ALA A 840      48.281  12.736  67.978  1.00 95.21           C  
ATOM   1338  C   ALA A 840      48.291  14.228  68.251  1.00 98.27           C  
ATOM   1339  O   ALA A 840      47.475  14.733  69.018  1.00102.27           O  
ATOM   1340  CB  ALA A 840      49.444  12.061  68.694  1.00108.61           C  
ATOM   1341  N   GLU A 841      49.226  14.928  67.622  1.00 98.92           N  
ATOM   1342  CA  GLU A 841      49.341  16.366  67.806  1.00105.76           C  
ATOM   1343  C   GLU A 841      48.789  17.096  66.586  1.00106.30           C  
ATOM   1344  O   GLU A 841      49.109  18.263  66.345  1.00107.09           O  
ATOM   1345  CB  GLU A 841      50.808  16.756  68.051  1.00113.03           C  
ATOM   1346  CG  GLU A 841      51.495  16.014  69.208  1.00113.21           C  
ATOM   1347  CD  GLU A 841      50.746  16.141  70.533  1.00119.82           C  
ATOM   1348  OE1 GLU A 841      50.266  15.101  71.042  1.00118.11           O  
ATOM   1349  OE2 GLU A 841      50.642  17.272  71.066  1.00101.46           O  
ATOM   1350  N   GLU A 842      47.973  16.388  65.809  1.00105.18           N  
ATOM   1351  CA  GLU A 842      47.358  16.946  64.609  1.00104.00           C  
ATOM   1352  C   GLU A 842      45.977  17.497  64.994  1.00102.97           C  
ATOM   1353  O   GLU A 842      45.166  16.795  65.603  1.00105.99           O  
ATOM   1354  CB  GLU A 842      47.240  15.859  63.541  1.00100.30           C  
ATOM   1355  CG  GLU A 842      47.102  16.360  62.118  1.00101.00           C  
ATOM   1356  CD  GLU A 842      46.873  15.227  61.128  1.00103.69           C  
ATOM   1357  OE1 GLU A 842      47.821  14.467  60.841  1.00104.94           O  
ATOM   1358  OE2 GLU A 842      45.736  15.091  60.639  1.00110.90           O  
ATOM   1359  N   LYS A 843      45.722  18.756  64.646  1.00100.06           N  
ATOM   1360  CA  LYS A 843      44.462  19.415  64.990  1.00 93.63           C  
ATOM   1361  C   LYS A 843      43.456  19.483  63.855  1.00 85.63           C  
ATOM   1362  O   LYS A 843      42.260  19.590  64.095  1.00 80.69           O  
ATOM   1363  CB  LYS A 843      44.741  20.840  65.476  1.00103.45           C  
ATOM   1364  CG  LYS A 843      45.401  21.720  64.409  1.00103.41           C  
ATOM   1365  CD  LYS A 843      45.764  23.105  64.929  1.00109.38           C  
ATOM   1366  CE  LYS A 843      46.384  23.972  63.824  1.00109.40           C  
ATOM   1367  NZ  LYS A 843      47.620  23.386  63.209  1.00 97.57           N  
ATOM   1368  N   GLU A 844      43.939  19.454  62.619  1.00 82.73           N  
ATOM   1369  CA  GLU A 844      43.045  19.547  61.475  1.00 78.81           C  
ATOM   1370  C   GLU A 844      43.560  18.863  60.229  1.00 74.67           C  
ATOM   1371  O   GLU A 844      44.760  18.658  60.066  1.00 83.49           O  
ATOM   1372  CB  GLU A 844      42.742  21.018  61.159  1.00 81.67           C  
ATOM   1373  CG  GLU A 844      43.967  21.890  60.919  1.00 78.85           C  
ATOM   1374  CD  GLU A 844      43.650  23.386  60.944  1.00 92.66           C  
ATOM   1375  OE1 GLU A 844      42.942  23.834  61.878  1.00107.61           O  
ATOM   1376  OE2 GLU A 844      44.121  24.115  60.039  1.00 85.28           O  
ATOM   1377  N   TYR A 845      42.630  18.516  59.351  1.00 62.83           N  
ATOM   1378  CA  TYR A 845      42.957  17.871  58.102  1.00 62.12           C  
ATOM   1379  C   TYR A 845      42.804  18.855  56.955  1.00 68.06           C  
ATOM   1380  O   TYR A 845      41.799  19.552  56.852  1.00 65.92           O  
ATOM   1381  CB  TYR A 845      42.060  16.656  57.872  1.00 60.32           C  
ATOM   1382  CG  TYR A 845      42.157  16.108  56.467  1.00 59.62           C  
ATOM   1383  CD1 TYR A 845      43.211  15.270  56.088  1.00 65.72           C  
ATOM   1384  CD2 TYR A 845      41.208  16.456  55.503  1.00 62.42           C  
ATOM   1385  CE1 TYR A 845      43.315  14.793  54.773  1.00 68.26           C  
ATOM   1386  CE2 TYR A 845      41.298  15.989  54.198  1.00 60.79           C  
ATOM   1387  CZ  TYR A 845      42.352  15.160  53.838  1.00 77.11           C  
ATOM   1388  OH  TYR A 845      42.430  14.705  52.546  1.00 71.74           O  
ATOM   1389  N   HIS A 846      43.799  18.865  56.071  1.00 79.11           N  
ATOM   1390  CA  HIS A 846      43.816  19.744  54.911  1.00 82.38           C  
ATOM   1391  C   HIS A 846      43.508  18.900  53.689  1.00 84.19           C  
ATOM   1392  O   HIS A 846      44.308  18.058  53.296  1.00 91.80           O  
ATOM   1393  CB  HIS A 846      45.193  20.398  54.788  1.00 94.00           C  
ATOM   1394  CG  HIS A 846      45.676  21.018  56.066  1.00 99.87           C  
ATOM   1395  ND1 HIS A 846      45.670  22.380  56.282  1.00110.18           N  
ATOM   1396  CD2 HIS A 846      46.136  20.457  57.211  1.00104.37           C  
ATOM   1397  CE1 HIS A 846      46.101  22.632  57.506  1.00113.99           C  
ATOM   1398  NE2 HIS A 846      46.390  21.482  58.091  1.00109.21           N  
ATOM   1399  N   ALA A 847      42.335  19.120  53.105  1.00 86.91           N  
ATOM   1400  CA  ALA A 847      41.881  18.363  51.942  1.00 87.82           C  
ATOM   1401  C   ALA A 847      42.546  18.739  50.628  1.00 92.21           C  
ATOM   1402  O   ALA A 847      43.412  19.612  50.583  1.00 90.71           O  
ATOM   1403  CB  ALA A 847      40.378  18.465  51.813  1.00 79.99           C  
ATOM   1404  N   GLU A 848      42.105  18.083  49.557  1.00 95.57           N  
ATOM   1405  CA  GLU A 848      42.645  18.304  48.224  1.00100.88           C  
ATOM   1406  C   GLU A 848      41.553  18.516  47.170  1.00105.24           C  
ATOM   1407  O   GLU A 848      41.116  19.643  46.944  1.00107.38           O  
ATOM   1408  CB  GLU A 848      43.583  17.142  47.833  1.00107.92           C  
ATOM   1409  CG  GLU A 848      42.957  15.722  47.817  1.00115.49           C  
ATOM   1410  CD  GLU A 848      42.469  15.231  49.189  1.00120.00           C  
ATOM   1411  OE1 GLU A 848      41.279  14.853  49.320  1.00120.00           O  
ATOM   1412  OE2 GLU A 848      43.284  15.215  50.136  1.00120.00           O  
ATOM   1413  N   GLY A 849      41.097  17.429  46.555  1.00110.25           N  
ATOM   1414  CA  GLY A 849      40.077  17.507  45.523  1.00115.58           C  
ATOM   1415  C   GLY A 849      38.689  17.950  45.948  1.00119.73           C  
ATOM   1416  O   GLY A 849      38.325  17.901  47.130  1.00120.00           O  
ATOM   1417  N   GLY A 850      37.909  18.378  44.958  1.00120.00           N  
ATOM   1418  CA  GLY A 850      36.552  18.838  45.201  1.00120.00           C  
ATOM   1419  C   GLY A 850      35.496  17.778  44.941  1.00118.42           C  
ATOM   1420  O   GLY A 850      34.973  17.650  43.830  1.00117.29           O  
ATOM   1421  N   LYS A 851      35.169  17.024  45.981  1.00114.16           N  
ATOM   1422  CA  LYS A 851      34.171  15.977  45.870  1.00112.90           C  
ATOM   1423  C   LYS A 851      33.323  15.911  47.136  1.00107.97           C  
ATOM   1424  O   LYS A 851      32.656  14.907  47.398  1.00109.24           O  
ATOM   1425  CB  LYS A 851      34.854  14.629  45.610  1.00120.00           C  
ATOM   1426  CG  LYS A 851      35.925  14.245  46.636  1.00120.00           C  
ATOM   1427  CD  LYS A 851      36.394  12.806  46.430  1.00113.74           C  
ATOM   1428  CE  LYS A 851      37.438  12.397  47.466  1.00115.06           C  
ATOM   1429  NZ  LYS A 851      37.725  10.929  47.416  1.00112.80           N  
ATOM   1430  N   VAL A 852      33.343  16.993  47.908  1.00101.57           N  
ATOM   1431  CA  VAL A 852      32.586  17.062  49.154  1.00 98.14           C  
ATOM   1432  C   VAL A 852      31.280  17.848  48.979  1.00 93.01           C  
ATOM   1433  O   VAL A 852      31.240  18.832  48.242  1.00 91.35           O  
ATOM   1434  CB  VAL A 852      33.439  17.710  50.280  1.00 94.32           C  
ATOM   1435  CG1 VAL A 852      32.775  17.525  51.639  1.00 98.15           C  
ATOM   1436  CG2 VAL A 852      34.826  17.104  50.300  1.00 93.53           C  
ATOM   1437  N   PRO A 853      30.176  17.365  49.584  1.00 90.04           N  
ATOM   1438  CA  PRO A 853      28.871  18.032  49.499  1.00 85.54           C  
ATOM   1439  C   PRO A 853      28.928  19.353  50.271  1.00 80.38           C  
ATOM   1440  O   PRO A 853      29.103  19.388  51.494  1.00 78.49           O  
ATOM   1441  CB  PRO A 853      27.926  17.012  50.129  1.00 86.88           C  
ATOM   1442  CG  PRO A 853      28.798  16.288  51.081  1.00 83.40           C  
ATOM   1443  CD  PRO A 853      30.046  16.079  50.285  1.00 91.17           C  
ATOM   1444  N   ILE A 854      28.788  20.432  49.514  1.00 72.97           N  
ATOM   1445  CA  ILE A 854      28.884  21.795  50.008  1.00 67.30           C  
ATOM   1446  C   ILE A 854      27.862  22.255  51.036  1.00 62.17           C  
ATOM   1447  O   ILE A 854      28.216  22.946  51.999  1.00 47.84           O  
ATOM   1448  CB  ILE A 854      28.918  22.777  48.808  1.00 69.55           C  
ATOM   1449  CG1 ILE A 854      30.055  22.362  47.858  1.00 85.91           C  
ATOM   1450  CG2 ILE A 854      29.173  24.211  49.294  1.00 56.17           C  
ATOM   1451  CD1 ILE A 854      29.760  22.535  46.374  1.00 94.34           C  
ATOM   1452  N   LYS A 855      26.611  21.845  50.854  1.00 55.72           N  
ATOM   1453  CA  LYS A 855      25.547  22.256  51.748  1.00 56.79           C  
ATOM   1454  C   LYS A 855      25.541  21.690  53.171  1.00 62.88           C  
ATOM   1455  O   LYS A 855      24.616  21.959  53.944  1.00 65.29           O  
ATOM   1456  CB  LYS A 855      24.203  22.075  51.064  1.00 45.78           C  
ATOM   1457  CG  LYS A 855      24.028  23.035  49.880  1.00 49.88           C  
ATOM   1458  CD  LYS A 855      22.685  22.822  49.216  1.00 55.16           C  
ATOM   1459  CE  LYS A 855      22.546  23.641  47.953  1.00 56.75           C  
ATOM   1460  NZ  LYS A 855      21.251  23.329  47.259  1.00 64.81           N  
ATOM   1461  N   TRP A 856      26.568  20.912  53.514  1.00 56.13           N  
ATOM   1462  CA  TRP A 856      26.697  20.351  54.848  1.00 37.60           C  
ATOM   1463  C   TRP A 856      28.013  20.733  55.478  1.00 41.96           C  
ATOM   1464  O   TRP A 856      28.292  20.331  56.608  1.00 40.21           O  
ATOM   1465  CB  TRP A 856      26.628  18.840  54.819  1.00 36.34           C  
ATOM   1466  CG  TRP A 856      25.284  18.299  54.737  1.00 34.65           C  
ATOM   1467  CD1 TRP A 856      24.567  17.791  55.764  1.00 32.37           C  
ATOM   1468  CD2 TRP A 856      24.467  18.167  53.557  1.00 29.13           C  
ATOM   1469  NE1 TRP A 856      23.338  17.345  55.309  1.00 44.21           N  
ATOM   1470  CE2 TRP A 856      23.250  17.568  53.959  1.00 33.03           C  
ATOM   1471  CE3 TRP A 856      24.652  18.477  52.203  1.00 46.84           C  
ATOM   1472  CZ2 TRP A 856      22.211  17.278  53.056  1.00 39.80           C  
ATOM   1473  CZ3 TRP A 856      23.613  18.178  51.290  1.00 37.32           C  
ATOM   1474  CH2 TRP A 856      22.411  17.589  51.730  1.00 45.88           C  
ATOM   1475  N   MET A 857      28.828  21.511  54.775  1.00 42.56           N  
ATOM   1476  CA  MET A 857      30.119  21.864  55.327  1.00 50.23           C  
ATOM   1477  C   MET A 857      30.305  23.203  55.994  1.00 52.17           C  
ATOM   1478  O   MET A 857      29.684  24.194  55.629  1.00 56.89           O  
ATOM   1479  CB  MET A 857      31.246  21.586  54.318  1.00 59.84           C  
ATOM   1480  CG  MET A 857      30.973  21.963  52.865  1.00 76.16           C  
ATOM   1481  SD  MET A 857      31.919  20.907  51.685  1.00 66.94           S  
ATOM   1482  CE  MET A 857      33.580  21.533  51.907  1.00 36.00           C  
ATOM   1483  N   ALA A 858      31.156  23.204  57.013  1.00 51.20           N  
ATOM   1484  CA  ALA A 858      31.478  24.410  57.752  1.00 54.29           C  
ATOM   1485  C   ALA A 858      31.986  25.425  56.748  1.00 58.76           C  
ATOM   1486  O   ALA A 858      32.401  25.049  55.664  1.00 51.68           O  
ATOM   1487  CB  ALA A 858      32.556  24.122  58.780  1.00 40.54           C  
ATOM   1488  N   LEU A 859      31.929  26.707  57.106  1.00 69.17           N  
ATOM   1489  CA  LEU A 859      32.389  27.780  56.228  1.00 65.10           C  
ATOM   1490  C   LEU A 859      33.886  27.641  55.982  1.00 64.58           C  
ATOM   1491  O   LEU A 859      34.337  27.707  54.844  1.00 61.58           O  
ATOM   1492  CB  LEU A 859      32.107  29.142  56.855  1.00 62.30           C  
ATOM   1493  CG  LEU A 859      32.456  30.359  55.991  1.00 68.90           C  
ATOM   1494  CD1 LEU A 859      31.554  30.404  54.751  1.00 53.78           C  
ATOM   1495  CD2 LEU A 859      32.309  31.635  56.823  1.00 59.88           C  
ATOM   1496  N   GLU A 860      34.646  27.419  57.055  1.00 63.16           N  
ATOM   1497  CA  GLU A 860      36.095  27.270  56.960  1.00 61.85           C  
ATOM   1498  C   GLU A 860      36.492  26.083  56.073  1.00 66.86           C  
ATOM   1499  O   GLU A 860      37.603  26.037  55.550  1.00 69.54           O  
ATOM   1500  CB  GLU A 860      36.739  27.151  58.350  1.00 52.67           C  
ATOM   1501  CG  GLU A 860      36.441  25.865  59.123  1.00 69.29           C  
ATOM   1502  CD  GLU A 860      35.135  25.897  59.928  1.00 68.29           C  
ATOM   1503  OE1 GLU A 860      34.298  26.807  59.730  1.00 57.68           O  
ATOM   1504  OE2 GLU A 860      34.943  24.981  60.758  1.00 57.06           O  
ATOM   1505  N   SER A 861      35.587  25.129  55.899  1.00 59.99           N  
ATOM   1506  CA  SER A 861      35.883  24.000  55.053  1.00 60.83           C  
ATOM   1507  C   SER A 861      35.855  24.457  53.605  1.00 65.66           C  
ATOM   1508  O   SER A 861      36.765  24.153  52.836  1.00 70.82           O  
ATOM   1509  CB  SER A 861      34.865  22.871  55.269  1.00 63.62           C  
ATOM   1510  OG  SER A 861      34.996  22.298  56.568  1.00 51.51           O  
ATOM   1511  N   ILE A 862      34.824  25.220  53.250  1.00 70.95           N  
ATOM   1512  CA  ILE A 862      34.630  25.715  51.883  1.00 72.41           C  
ATOM   1513  C   ILE A 862      35.659  26.759  51.485  1.00 73.84           C  
ATOM   1514  O   ILE A 862      36.031  26.876  50.319  1.00 75.38           O  
ATOM   1515  CB  ILE A 862      33.230  26.355  51.713  1.00 75.86           C  
ATOM   1516  CG1 ILE A 862      32.133  25.347  52.056  1.00 82.33           C  
ATOM   1517  CG2 ILE A 862      33.040  26.865  50.291  1.00 61.00           C  
ATOM   1518  CD1 ILE A 862      30.735  25.939  51.995  1.00 78.19           C  
ATOM   1519  N   LEU A 863      36.102  27.525  52.467  1.00 74.09           N  
ATOM   1520  CA  LEU A 863      37.060  28.578  52.224  1.00 80.31           C  
ATOM   1521  C   LEU A 863      38.516  28.147  52.330  1.00 81.76           C  
ATOM   1522  O   LEU A 863      39.358  28.638  51.574  1.00 87.29           O  
ATOM   1523  CB  LEU A 863      36.780  29.768  53.156  1.00 87.79           C  
ATOM   1524  CG  LEU A 863      35.675  30.769  52.770  1.00 90.84           C  
ATOM   1525  CD1 LEU A 863      36.089  31.539  51.532  1.00106.44           C  
ATOM   1526  CD2 LEU A 863      34.350  30.083  52.526  1.00 97.61           C  
ATOM   1527  N   HIS A 864      38.822  27.239  53.252  1.00 75.77           N  
ATOM   1528  CA  HIS A 864      40.204  26.802  53.439  1.00 77.04           C  
ATOM   1529  C   HIS A 864      40.456  25.294  53.349  1.00 74.54           C  
ATOM   1530  O   HIS A 864      41.584  24.841  53.556  1.00 71.29           O  
ATOM   1531  CB  HIS A 864      40.731  27.306  54.790  1.00 89.06           C  
ATOM   1532  CG  HIS A 864      40.632  28.790  54.976  1.00101.33           C  
ATOM   1533  ND1 HIS A 864      40.171  29.641  53.996  1.00 96.56           N  
ATOM   1534  CD2 HIS A 864      40.944  29.575  56.038  1.00104.71           C  
ATOM   1535  CE1 HIS A 864      40.203  30.884  54.441  1.00 97.95           C  
ATOM   1536  NE2 HIS A 864      40.669  30.871  55.678  1.00 94.10           N  
ATOM   1537  N   ARG A 865      39.425  24.520  53.029  1.00 76.08           N  
ATOM   1538  CA  ARG A 865      39.548  23.063  52.953  1.00 79.92           C  
ATOM   1539  C   ARG A 865      40.019  22.465  54.290  1.00 80.59           C  
ATOM   1540  O   ARG A 865      40.646  21.400  54.311  1.00 79.96           O  
ATOM   1541  CB  ARG A 865      40.503  22.632  51.830  1.00 85.88           C  
ATOM   1542  CG  ARG A 865      40.006  22.875  50.408  1.00 95.58           C  
ATOM   1543  CD  ARG A 865      41.088  22.482  49.404  1.00100.32           C  
ATOM   1544  NE  ARG A 865      40.771  22.860  48.026  1.00105.35           N  
ATOM   1545  CZ  ARG A 865      41.672  22.983  47.052  1.00 88.91           C  
ATOM   1546  NH1 ARG A 865      42.958  22.762  47.288  1.00 84.44           N  
ATOM   1547  NH2 ARG A 865      41.284  23.331  45.834  1.00 91.45           N  
ATOM   1548  N   ILE A 866      39.763  23.176  55.391  1.00 72.57           N  
ATOM   1549  CA  ILE A 866      40.127  22.702  56.728  1.00 68.39           C  
ATOM   1550  C   ILE A 866      38.942  21.905  57.324  1.00 67.59           C  
ATOM   1551  O   ILE A 866      37.771  22.271  57.145  1.00 68.97           O  
ATOM   1552  CB  ILE A 866      40.456  23.875  57.684  1.00 73.75           C  
ATOM   1553  CG1 ILE A 866      41.594  24.729  57.132  1.00 79.37           C  
ATOM   1554  CG2 ILE A 866      40.829  23.346  59.058  1.00 69.39           C  
ATOM   1555  CD1 ILE A 866      42.917  24.046  57.154  1.00 85.39           C  
ATOM   1556  N   TYR A 867      39.249  20.795  57.993  1.00 57.78           N  
ATOM   1557  CA  TYR A 867      38.228  19.957  58.613  1.00 46.91           C  
ATOM   1558  C   TYR A 867      38.616  19.575  60.025  1.00 47.40           C  
ATOM   1559  O   TYR A 867      39.766  19.275  60.311  1.00 50.13           O  
ATOM   1560  CB  TYR A 867      37.986  18.711  57.792  1.00 36.27           C  
ATOM   1561  CG  TYR A 867      37.416  19.008  56.441  1.00 48.68           C  
ATOM   1562  CD1 TYR A 867      38.216  19.562  55.438  1.00 48.05           C  
ATOM   1563  CD2 TYR A 867      36.095  18.697  56.139  1.00 30.60           C  
ATOM   1564  CE1 TYR A 867      37.723  19.796  54.172  1.00 42.98           C  
ATOM   1565  CE2 TYR A 867      35.585  18.922  54.853  1.00 46.74           C  
ATOM   1566  CZ  TYR A 867      36.416  19.475  53.877  1.00 45.09           C  
ATOM   1567  OH  TYR A 867      35.955  19.699  52.606  1.00 48.35           O  
ATOM   1568  N   THR A 868      37.648  19.590  60.923  1.00 44.34           N  
ATOM   1569  CA  THR A 868      37.935  19.277  62.309  1.00 45.71           C  
ATOM   1570  C   THR A 868      36.722  18.587  62.884  1.00 47.69           C  
ATOM   1571  O   THR A 868      35.730  18.376  62.181  1.00 54.68           O  
ATOM   1572  CB  THR A 868      38.154  20.581  63.084  1.00 57.55           C  
ATOM   1573  OG1 THR A 868      37.068  21.473  62.787  1.00 67.06           O  
ATOM   1574  CG2 THR A 868      39.475  21.266  62.675  1.00 49.57           C  
ATOM   1575  N   HIS A 869      36.818  18.174  64.141  1.00 46.30           N  
ATOM   1576  CA  HIS A 869      35.671  17.568  64.807  1.00 46.04           C  
ATOM   1577  C   HIS A 869      34.575  18.653  64.836  1.00 44.36           C  
ATOM   1578  O   HIS A 869      33.411  18.364  64.540  1.00 39.31           O  
ATOM   1579  CB  HIS A 869      36.030  17.131  66.237  1.00 38.94           C  
ATOM   1580  CG  HIS A 869      37.044  16.031  66.291  1.00 55.49           C  
ATOM   1581  ND1 HIS A 869      36.982  14.919  65.481  1.00 60.18           N  
ATOM   1582  CD2 HIS A 869      38.150  15.872  67.058  1.00 55.80           C  
ATOM   1583  CE1 HIS A 869      38.003  14.123  65.744  1.00 42.39           C  
ATOM   1584  NE2 HIS A 869      38.725  14.680  66.699  1.00 53.12           N  
ATOM   1585  N   GLN A 870      34.989  19.903  65.097  1.00 38.13           N  
ATOM   1586  CA  GLN A 870      34.080  21.047  65.145  1.00 47.26           C  
ATOM   1587  C   GLN A 870      33.450  21.328  63.784  1.00 46.64           C  
ATOM   1588  O   GLN A 870      32.377  21.920  63.680  1.00 48.50           O  
ATOM   1589  CB  GLN A 870      34.787  22.295  65.687  1.00 43.21           C  
ATOM   1590  CG  GLN A 870      35.165  22.207  67.173  1.00 44.89           C  
ATOM   1591  CD  GLN A 870      34.014  21.704  68.049  1.00 55.93           C  
ATOM   1592  OE1 GLN A 870      34.075  20.605  68.609  1.00 52.78           O  
ATOM   1593  NE2 GLN A 870      32.949  22.498  68.147  1.00 51.09           N  
ATOM   1594  N   SER A 871      34.114  20.866  62.738  1.00 45.92           N  
ATOM   1595  CA  SER A 871      33.612  21.035  61.382  1.00 41.71           C  
ATOM   1596  C   SER A 871      32.472  20.044  61.236  1.00 39.62           C  
ATOM   1597  O   SER A 871      31.515  20.274  60.496  1.00 40.23           O  
ATOM   1598  CB  SER A 871      34.718  20.707  60.368  1.00 49.46           C  
ATOM   1599  OG  SER A 871      34.226  20.813  59.047  1.00 65.84           O  
ATOM   1600  N   ASP A 872      32.602  18.919  61.935  1.00 36.76           N  
ATOM   1601  CA  ASP A 872      31.585  17.884  61.894  1.00 42.07           C  
ATOM   1602  C   ASP A 872      30.323  18.351  62.617  1.00 44.13           C  
ATOM   1603  O   ASP A 872      29.205  17.969  62.239  1.00 42.71           O  
ATOM   1604  CB  ASP A 872      32.124  16.566  62.485  1.00 43.22           C  
ATOM   1605  CG  ASP A 872      32.855  15.701  61.441  1.00 52.71           C  
ATOM   1606  OD1 ASP A 872      32.890  16.079  60.244  1.00 44.74           O  
ATOM   1607  OD2 ASP A 872      33.376  14.621  61.811  1.00 43.46           O  
ATOM   1608  N   VAL A 873      30.505  19.186  63.644  1.00 38.62           N  
ATOM   1609  CA  VAL A 873      29.377  19.715  64.385  1.00 43.88           C  
ATOM   1610  C   VAL A 873      28.464  20.528  63.461  1.00 44.53           C  
ATOM   1611  O   VAL A 873      27.242  20.346  63.492  1.00 47.58           O  
ATOM   1612  CB  VAL A 873      29.824  20.530  65.583  1.00 52.01           C  
ATOM   1613  CG1 VAL A 873      28.595  21.135  66.279  1.00 43.88           C  
ATOM   1614  CG2 VAL A 873      30.607  19.632  66.546  1.00 24.92           C  
ATOM   1615  N   TRP A 874      29.052  21.366  62.602  1.00 34.94           N  
ATOM   1616  CA  TRP A 874      28.261  22.137  61.636  1.00 39.19           C  
ATOM   1617  C   TRP A 874      27.383  21.169  60.862  1.00 42.81           C  
ATOM   1618  O   TRP A 874      26.182  21.369  60.725  1.00 51.78           O  
ATOM   1619  CB  TRP A 874      29.156  22.865  60.634  1.00 37.85           C  
ATOM   1620  CG  TRP A 874      28.400  23.745  59.647  1.00 37.55           C  
ATOM   1621  CD1 TRP A 874      27.470  23.349  58.716  1.00 31.62           C  
ATOM   1622  CD2 TRP A 874      28.516  25.168  59.511  1.00 26.63           C  
ATOM   1623  NE1 TRP A 874      27.005  24.440  58.016  1.00 36.13           N  
ATOM   1624  CE2 TRP A 874      27.629  25.567  58.495  1.00 37.51           C  
ATOM   1625  CE3 TRP A 874      29.283  26.143  60.161  1.00 42.94           C  
ATOM   1626  CZ2 TRP A 874      27.483  26.903  58.120  1.00 32.52           C  
ATOM   1627  CZ3 TRP A 874      29.141  27.463  59.786  1.00 32.60           C  
ATOM   1628  CH2 TRP A 874      28.249  27.832  58.780  1.00 36.94           C  
ATOM   1629  N   SER A 875      27.996  20.110  60.352  1.00 47.84           N  
ATOM   1630  CA  SER A 875      27.266  19.113  59.593  1.00 40.55           C  
ATOM   1631  C   SER A 875      26.225  18.457  60.465  1.00 40.22           C  
ATOM   1632  O   SER A 875      25.149  18.096  59.968  1.00 37.79           O  
ATOM   1633  CB  SER A 875      28.217  18.070  59.010  1.00 45.99           C  
ATOM   1634  OG  SER A 875      29.320  18.711  58.377  1.00 54.72           O  
ATOM   1635  N   TYR A 876      26.540  18.267  61.753  1.00 32.94           N  
ATOM   1636  CA  TYR A 876      25.555  17.676  62.659  1.00 35.18           C  
ATOM   1637  C   TYR A 876      24.318  18.606  62.727  1.00 39.79           C  
ATOM   1638  O   TYR A 876      23.183  18.131  62.698  1.00 34.33           O  
ATOM   1639  CB  TYR A 876      26.139  17.444  64.053  1.00 36.03           C  
ATOM   1640  CG  TYR A 876      25.119  16.961  65.086  1.00 41.88           C  
ATOM   1641  CD1 TYR A 876      24.888  15.602  65.288  1.00 35.74           C  
ATOM   1642  CD2 TYR A 876      24.418  17.874  65.892  1.00 42.01           C  
ATOM   1643  CE1 TYR A 876      23.995  15.153  66.267  1.00 38.92           C  
ATOM   1644  CE2 TYR A 876      23.515  17.435  66.872  1.00 31.92           C  
ATOM   1645  CZ  TYR A 876      23.312  16.074  67.049  1.00 39.35           C  
ATOM   1646  OH  TYR A 876      22.417  15.629  67.988  1.00 34.93           O  
ATOM   1647  N   GLY A 877      24.552  19.921  62.773  1.00 35.22           N  
ATOM   1648  CA  GLY A 877      23.458  20.882  62.807  1.00 41.84           C  
ATOM   1649  C   GLY A 877      22.541  20.743  61.604  1.00 44.84           C  
ATOM   1650  O   GLY A 877      21.300  20.674  61.741  1.00 48.16           O  
ATOM   1651  N   VAL A 878      23.148  20.697  60.420  1.00 38.89           N  
ATOM   1652  CA  VAL A 878      22.393  20.545  59.183  1.00 34.99           C  
ATOM   1653  C   VAL A 878      21.618  19.228  59.181  1.00 32.91           C  
ATOM   1654  O   VAL A 878      20.448  19.178  58.779  1.00 36.20           O  
ATOM   1655  CB  VAL A 878      23.312  20.589  57.965  1.00 43.75           C  
ATOM   1656  CG1 VAL A 878      22.499  20.390  56.706  1.00 32.58           C  
ATOM   1657  CG2 VAL A 878      24.045  21.908  57.927  1.00 20.51           C  
ATOM   1658  N   THR A 879      22.271  18.164  59.644  1.00 30.85           N  
ATOM   1659  CA  THR A 879      21.638  16.849  59.729  1.00 35.42           C  
ATOM   1660  C   THR A 879      20.404  16.938  60.620  1.00 37.48           C  
ATOM   1661  O   THR A 879      19.390  16.317  60.336  1.00 44.60           O  
ATOM   1662  CB  THR A 879      22.595  15.789  60.311  1.00 40.57           C  
ATOM   1663  OG1 THR A 879      23.794  15.756  59.532  1.00 41.23           O  
ATOM   1664  CG2 THR A 879      21.949  14.413  60.279  1.00 22.48           C  
ATOM   1665  N   VAL A 880      20.517  17.690  61.716  1.00 37.92           N  
ATOM   1666  CA  VAL A 880      19.417  17.902  62.648  1.00 37.92           C  
ATOM   1667  C   VAL A 880      18.284  18.636  61.907  1.00 42.69           C  
ATOM   1668  O   VAL A 880      17.119  18.246  61.993  1.00 41.81           O  
ATOM   1669  CB  VAL A 880      19.903  18.709  63.870  1.00 39.09           C  
ATOM   1670  CG1 VAL A 880      18.728  19.275  64.641  1.00 32.28           C  
ATOM   1671  CG2 VAL A 880      20.731  17.798  64.794  1.00 27.65           C  
ATOM   1672  N   TRP A 881      18.643  19.651  61.124  1.00 38.52           N  
ATOM   1673  CA  TRP A 881      17.663  20.406  60.338  1.00 34.16           C  
ATOM   1674  C   TRP A 881      16.880  19.487  59.382  1.00 42.10           C  
ATOM   1675  O   TRP A 881      15.653  19.571  59.280  1.00 42.01           O  
ATOM   1676  CB  TRP A 881      18.396  21.474  59.547  1.00 41.93           C  
ATOM   1677  CG  TRP A 881      17.528  22.465  58.907  1.00 54.28           C  
ATOM   1678  CD1 TRP A 881      17.127  23.658  59.431  1.00 45.14           C  
ATOM   1679  CD2 TRP A 881      16.929  22.369  57.612  1.00 58.96           C  
ATOM   1680  NE1 TRP A 881      16.304  24.305  58.549  1.00 45.48           N  
ATOM   1681  CE2 TRP A 881      16.162  23.540  57.422  1.00 55.71           C  
ATOM   1682  CE3 TRP A 881      16.965  21.411  56.592  1.00 55.70           C  
ATOM   1683  CZ2 TRP A 881      15.433  23.782  56.249  1.00 56.85           C  
ATOM   1684  CZ3 TRP A 881      16.237  21.655  55.421  1.00 67.37           C  
ATOM   1685  CH2 TRP A 881      15.483  22.833  55.264  1.00 46.32           C  
ATOM   1686  N   GLU A 882      17.583  18.593  58.690  1.00 44.93           N  
ATOM   1687  CA  GLU A 882      16.914  17.675  57.776  1.00 38.96           C  
ATOM   1688  C   GLU A 882      15.853  16.864  58.507  1.00 47.67           C  
ATOM   1689  O   GLU A 882      14.744  16.671  58.000  1.00 52.57           O  
ATOM   1690  CB  GLU A 882      17.910  16.718  57.147  1.00 41.57           C  
ATOM   1691  CG  GLU A 882      18.897  17.351  56.190  1.00 42.00           C  
ATOM   1692  CD  GLU A 882      19.960  16.364  55.770  1.00 54.77           C  
ATOM   1693  OE1 GLU A 882      19.658  15.471  54.944  1.00 64.48           O  
ATOM   1694  OE2 GLU A 882      21.098  16.473  56.283  1.00 50.07           O  
ATOM   1695  N   LEU A 883      16.194  16.387  59.699  1.00 42.41           N  
ATOM   1696  CA  LEU A 883      15.262  15.603  60.486  1.00 43.89           C  
ATOM   1697  C   LEU A 883      14.038  16.413  60.944  1.00 46.61           C  
ATOM   1698  O   LEU A 883      12.905  15.985  60.725  1.00 41.35           O  
ATOM   1699  CB  LEU A 883      15.979  15.006  61.686  1.00 47.94           C  
ATOM   1700  CG  LEU A 883      17.207  14.147  61.384  1.00 40.44           C  
ATOM   1701  CD1 LEU A 883      17.792  13.664  62.702  1.00 22.45           C  
ATOM   1702  CD2 LEU A 883      16.808  12.974  60.504  1.00 27.80           C  
ATOM   1703  N   MET A 884      14.260  17.585  61.549  1.00 51.07           N  
ATOM   1704  CA  MET A 884      13.153  18.429  62.042  1.00 54.93           C  
ATOM   1705  C   MET A 884      12.197  18.891  60.946  1.00 53.65           C  
ATOM   1706  O   MET A 884      11.016  19.117  61.213  1.00 47.38           O  
ATOM   1707  CB  MET A 884      13.666  19.640  62.826  1.00 47.94           C  
ATOM   1708  CG  MET A 884      14.515  19.295  64.047  1.00 40.93           C  
ATOM   1709  SD  MET A 884      13.765  18.040  65.105  1.00 43.08           S  
ATOM   1710  CE  MET A 884      15.132  17.661  66.291  1.00 40.50           C  
ATOM   1711  N   THR A 885      12.717  19.032  59.724  1.00 56.12           N  
ATOM   1712  CA  THR A 885      11.915  19.437  58.560  1.00 50.40           C  
ATOM   1713  C   THR A 885      11.350  18.219  57.820  1.00 51.58           C  
ATOM   1714  O   THR A 885      10.750  18.367  56.767  1.00 52.15           O  
ATOM   1715  CB  THR A 885      12.740  20.210  57.542  1.00 42.22           C  
ATOM   1716  OG1 THR A 885      13.864  19.414  57.145  1.00 44.04           O  
ATOM   1717  CG2 THR A 885      13.231  21.507  58.124  1.00 37.23           C  
ATOM   1718  N   PHE A 886      11.574  17.024  58.371  1.00 52.60           N  
ATOM   1719  CA  PHE A 886      11.117  15.758  57.795  1.00 48.48           C  
ATOM   1720  C   PHE A 886      11.711  15.385  56.428  1.00 47.47           C  
ATOM   1721  O   PHE A 886      11.082  14.680  55.643  1.00 54.64           O  
ATOM   1722  CB  PHE A 886       9.588  15.683  57.763  1.00 49.37           C  
ATOM   1723  CG  PHE A 886       8.959  15.801  59.111  1.00 51.23           C  
ATOM   1724  CD1 PHE A 886       8.910  14.712  59.960  1.00 43.11           C  
ATOM   1725  CD2 PHE A 886       8.476  17.027  59.562  1.00 43.45           C  
ATOM   1726  CE1 PHE A 886       8.391  14.836  61.269  1.00 45.93           C  
ATOM   1727  CE2 PHE A 886       7.962  17.166  60.852  1.00 43.47           C  
ATOM   1728  CZ  PHE A 886       7.919  16.066  61.712  1.00 44.23           C  
ATOM   1729  N   GLY A 887      12.930  15.839  56.157  1.00 43.49           N  
ATOM   1730  CA  GLY A 887      13.576  15.486  54.908  1.00 49.02           C  
ATOM   1731  C   GLY A 887      13.732  16.535  53.831  1.00 55.35           C  
ATOM   1732  O   GLY A 887      13.879  16.190  52.665  1.00 60.81           O  
ATOM   1733  N   SER A 888      13.742  17.806  54.202  1.00 54.70           N  
ATOM   1734  CA  SER A 888      13.876  18.863  53.209  1.00 57.45           C  
ATOM   1735  C   SER A 888      15.311  19.029  52.734  1.00 63.69           C  
ATOM   1736  O   SER A 888      16.261  18.685  53.440  1.00 68.90           O  
ATOM   1737  CB  SER A 888      13.342  20.189  53.757  1.00 55.72           C  
ATOM   1738  OG  SER A 888      11.958  20.080  54.045  1.00 59.11           O  
ATOM   1739  N   LYS A 889      15.460  19.537  51.516  1.00 63.91           N  
ATOM   1740  CA  LYS A 889      16.776  19.754  50.937  1.00 59.47           C  
ATOM   1741  C   LYS A 889      17.256  21.113  51.418  1.00 57.20           C  
ATOM   1742  O   LYS A 889      16.566  22.114  51.257  1.00 63.58           O  
ATOM   1743  CB  LYS A 889      16.689  19.703  49.399  1.00 60.28           C  
ATOM   1744  CG  LYS A 889      16.109  18.379  48.843  1.00 76.31           C  
ATOM   1745  CD  LYS A 889      15.484  18.517  47.440  1.00 79.63           C  
ATOM   1746  CE  LYS A 889      16.498  19.012  46.399  1.00100.56           C  
ATOM   1747  NZ  LYS A 889      15.908  19.336  45.056  1.00 96.73           N  
ATOM   1748  N   PRO A 890      18.404  21.150  52.099  1.00 53.44           N  
ATOM   1749  CA  PRO A 890      18.929  22.424  52.595  1.00 56.97           C  
ATOM   1750  C   PRO A 890      19.215  23.404  51.470  1.00 63.42           C  
ATOM   1751  O   PRO A 890      19.933  23.087  50.525  1.00 69.89           O  
ATOM   1752  CB  PRO A 890      20.193  22.013  53.364  1.00 50.25           C  
ATOM   1753  CG  PRO A 890      20.553  20.663  52.767  1.00 54.14           C  
ATOM   1754  CD  PRO A 890      19.220  20.017  52.556  1.00 46.07           C  
ATOM   1755  N   TYR A 891      18.649  24.605  51.600  1.00 70.10           N  
ATOM   1756  CA  TYR A 891      18.781  25.682  50.616  1.00 64.39           C  
ATOM   1757  C   TYR A 891      18.258  25.157  49.280  1.00 65.48           C  
ATOM   1758  O   TYR A 891      18.945  25.258  48.268  1.00 63.83           O  
ATOM   1759  CB  TYR A 891      20.241  26.125  50.459  1.00 53.66           C  
ATOM   1760  CG  TYR A 891      21.053  26.175  51.735  1.00 54.86           C  
ATOM   1761  CD1 TYR A 891      21.034  27.295  52.560  1.00 35.95           C  
ATOM   1762  CD2 TYR A 891      21.889  25.116  52.086  1.00 53.10           C  
ATOM   1763  CE1 TYR A 891      21.842  27.363  53.708  1.00 46.08           C  
ATOM   1764  CE2 TYR A 891      22.697  25.171  53.227  1.00 45.68           C  
ATOM   1765  CZ  TYR A 891      22.677  26.289  54.030  1.00 46.76           C  
ATOM   1766  OH  TYR A 891      23.519  26.334  55.127  1.00 42.39           O  
ATOM   1767  N   ASP A 892      17.036  24.616  49.293  1.00 68.49           N  
ATOM   1768  CA  ASP A 892      16.402  24.020  48.110  1.00 76.56           C  
ATOM   1769  C   ASP A 892      16.600  24.734  46.784  1.00 81.31           C  
ATOM   1770  O   ASP A 892      16.719  24.081  45.744  1.00 81.13           O  
ATOM   1771  CB  ASP A 892      14.908  23.787  48.342  1.00 88.49           C  
ATOM   1772  CG  ASP A 892      14.225  23.143  47.142  1.00 91.77           C  
ATOM   1773  OD1 ASP A 892      14.429  21.929  46.905  1.00 78.82           O  
ATOM   1774  OD2 ASP A 892      13.495  23.864  46.425  1.00102.90           O  
ATOM   1775  N   GLY A 893      16.593  26.063  46.806  1.00 80.64           N  
ATOM   1776  CA  GLY A 893      16.799  26.799  45.575  1.00 84.75           C  
ATOM   1777  C   GLY A 893      18.280  26.886  45.254  1.00 86.86           C  
ATOM   1778  O   GLY A 893      18.814  26.120  44.448  1.00 86.53           O  
ATOM   1779  N   ILE A 894      18.938  27.807  45.944  1.00 89.25           N  
ATOM   1780  CA  ILE A 894      20.361  28.090  45.815  1.00 90.31           C  
ATOM   1781  C   ILE A 894      21.240  26.930  45.342  1.00 93.65           C  
ATOM   1782  O   ILE A 894      21.094  25.806  45.809  1.00 96.52           O  
ATOM   1783  CB  ILE A 894      20.895  28.616  47.161  1.00 85.72           C  
ATOM   1784  CG1 ILE A 894      20.037  29.796  47.628  1.00 92.35           C  
ATOM   1785  CG2 ILE A 894      22.336  29.050  47.030  1.00 88.26           C  
ATOM   1786  CD1 ILE A 894      20.482  30.422  48.937  1.00100.49           C  
ATOM   1787  N   PRO A 895      22.095  27.176  44.333  1.00100.33           N  
ATOM   1788  CA  PRO A 895      23.005  26.165  43.785  1.00100.58           C  
ATOM   1789  C   PRO A 895      24.327  26.218  44.547  1.00 96.08           C  
ATOM   1790  O   PRO A 895      24.775  27.288  44.968  1.00 92.76           O  
ATOM   1791  CB  PRO A 895      23.176  26.618  42.340  1.00102.05           C  
ATOM   1792  CG  PRO A 895      23.223  28.103  42.489  1.00105.36           C  
ATOM   1793  CD  PRO A 895      22.078  28.373  43.469  1.00112.44           C  
ATOM   1794  N   ALA A 896      24.954  25.059  44.687  1.00 94.51           N  
ATOM   1795  CA  ALA A 896      26.210  24.905  45.415  1.00 90.41           C  
ATOM   1796  C   ALA A 896      27.224  26.042  45.316  1.00 87.90           C  
ATOM   1797  O   ALA A 896      27.946  26.324  46.275  1.00 81.76           O  
ATOM   1798  CB  ALA A 896      26.862  23.594  45.023  1.00 95.34           C  
ATOM   1799  N   SER A 897      27.266  26.698  44.163  1.00 92.28           N  
ATOM   1800  CA  SER A 897      28.211  27.789  43.926  1.00 97.61           C  
ATOM   1801  C   SER A 897      27.975  29.018  44.792  1.00 98.57           C  
ATOM   1802  O   SER A 897      28.926  29.717  45.159  1.00101.07           O  
ATOM   1803  CB  SER A 897      28.176  28.211  42.455  1.00100.16           C  
ATOM   1804  OG  SER A 897      28.393  27.103  41.603  1.00108.85           O  
ATOM   1805  N   GLU A 898      26.710  29.276  45.115  1.00 97.19           N  
ATOM   1806  CA  GLU A 898      26.340  30.445  45.907  1.00 91.79           C  
ATOM   1807  C   GLU A 898      26.438  30.277  47.415  1.00 83.70           C  
ATOM   1808  O   GLU A 898      26.700  31.256  48.123  1.00 81.80           O  
ATOM   1809  CB  GLU A 898      24.931  30.911  45.538  1.00 93.24           C  
ATOM   1810  CG  GLU A 898      24.753  31.241  44.069  1.00 94.50           C  
ATOM   1811  CD  GLU A 898      23.444  31.948  43.783  1.00111.25           C  
ATOM   1812  OE1 GLU A 898      22.410  31.589  44.391  1.00111.91           O  
ATOM   1813  OE2 GLU A 898      23.450  32.872  42.943  1.00120.00           O  
ATOM   1814  N   ILE A 899      26.271  29.037  47.883  1.00 75.33           N  
ATOM   1815  CA  ILE A 899      26.304  28.691  49.313  1.00 65.80           C  
ATOM   1816  C   ILE A 899      27.361  29.406  50.139  1.00 64.64           C  
ATOM   1817  O   ILE A 899      27.068  29.912  51.219  1.00 70.05           O  
ATOM   1818  CB  ILE A 899      26.450  27.173  49.529  1.00 43.47           C  
ATOM   1819  CG1 ILE A 899      25.308  26.427  48.835  1.00 62.40           C  
ATOM   1820  CG2 ILE A 899      26.475  26.843  51.002  1.00 56.71           C  
ATOM   1821  CD1 ILE A 899      23.909  26.883  49.223  1.00 60.09           C  
ATOM   1822  N   SER A 900      28.581  29.470  49.629  1.00 66.88           N  
ATOM   1823  CA  SER A 900      29.654  30.137  50.352  1.00 67.29           C  
ATOM   1824  C   SER A 900      29.289  31.585  50.662  1.00 67.66           C  
ATOM   1825  O   SER A 900      29.486  32.048  51.779  1.00 66.68           O  
ATOM   1826  CB  SER A 900      30.954  30.093  49.538  1.00 66.04           C  
ATOM   1827  OG  SER A 900      32.009  30.772  50.207  1.00 66.03           O  
ATOM   1828  N   SER A 901      28.727  32.277  49.675  1.00 69.06           N  
ATOM   1829  CA  SER A 901      28.360  33.682  49.819  1.00 73.94           C  
ATOM   1830  C   SER A 901      27.170  33.959  50.732  1.00 70.98           C  
ATOM   1831  O   SER A 901      27.201  34.900  51.537  1.00 66.69           O  
ATOM   1832  CB  SER A 901      28.138  34.320  48.444  1.00 79.40           C  
ATOM   1833  OG  SER A 901      29.358  34.390  47.724  1.00 96.62           O  
ATOM   1834  N   ILE A 902      26.113  33.168  50.599  1.00 63.68           N  
ATOM   1835  CA  ILE A 902      24.968  33.378  51.452  1.00 65.54           C  
ATOM   1836  C   ILE A 902      25.427  33.166  52.896  1.00 69.07           C  
ATOM   1837  O   ILE A 902      25.009  33.891  53.796  1.00 77.10           O  
ATOM   1838  CB  ILE A 902      23.798  32.434  51.110  1.00 74.17           C  
ATOM   1839  CG1 ILE A 902      24.059  31.035  51.646  1.00 66.26           C  
ATOM   1840  CG2 ILE A 902      23.546  32.417  49.607  1.00 58.72           C  
ATOM   1841  CD1 ILE A 902      22.809  30.210  51.746  1.00 92.86           C  
ATOM   1842  N   LEU A 903      26.352  32.227  53.098  1.00 65.02           N  
ATOM   1843  CA  LEU A 903      26.870  31.953  54.430  1.00 59.17           C  
ATOM   1844  C   LEU A 903      27.761  33.073  54.928  1.00 59.34           C  
ATOM   1845  O   LEU A 903      27.798  33.353  56.115  1.00 64.13           O  
ATOM   1846  CB  LEU A 903      27.614  30.619  54.471  1.00 64.94           C  
ATOM   1847  CG  LEU A 903      26.769  29.341  54.317  1.00 62.45           C  
ATOM   1848  CD1 LEU A 903      27.669  28.119  54.316  1.00 47.66           C  
ATOM   1849  CD2 LEU A 903      25.754  29.235  55.428  1.00 56.42           C  
ATOM   1850  N   GLU A 904      28.465  33.732  54.016  1.00 73.27           N  
ATOM   1851  CA  GLU A 904      29.349  34.837  54.384  1.00 74.37           C  
ATOM   1852  C   GLU A 904      28.517  36.044  54.824  1.00 72.34           C  
ATOM   1853  O   GLU A 904      28.928  36.798  55.710  1.00 69.86           O  
ATOM   1854  CB  GLU A 904      30.283  35.196  53.217  1.00 80.24           C  
ATOM   1855  CG  GLU A 904      31.300  34.101  52.873  1.00 87.87           C  
ATOM   1856  CD  GLU A 904      32.208  34.455  51.692  1.00 97.84           C  
ATOM   1857  OE1 GLU A 904      33.278  35.068  51.919  1.00 83.56           O  
ATOM   1858  OE2 GLU A 904      31.861  34.098  50.540  1.00100.45           O  
ATOM   1859  N   LYS A 905      27.330  36.190  54.231  1.00 72.48           N  
ATOM   1860  CA  LYS A 905      26.406  37.283  54.562  1.00 75.62           C  
ATOM   1861  C   LYS A 905      25.697  37.042  55.901  1.00 73.77           C  
ATOM   1862  O   LYS A 905      24.869  37.846  56.315  1.00 70.63           O  
ATOM   1863  CB  LYS A 905      25.334  37.453  53.477  1.00 84.87           C  
ATOM   1864  CG  LYS A 905      25.798  38.010  52.134  1.00 89.24           C  
ATOM   1865  CD  LYS A 905      24.648  37.914  51.121  1.00100.50           C  
ATOM   1866  CE  LYS A 905      24.997  38.483  49.745  1.00102.05           C  
ATOM   1867  NZ  LYS A 905      24.964  39.973  49.704  1.00103.54           N  
ATOM   1868  N   GLY A 906      25.980  35.907  56.540  1.00 72.04           N  
ATOM   1869  CA  GLY A 906      25.379  35.602  57.827  1.00 62.99           C  
ATOM   1870  C   GLY A 906      24.072  34.838  57.756  1.00 63.01           C  
ATOM   1871  O   GLY A 906      23.455  34.556  58.781  1.00 62.79           O  
ATOM   1872  N   GLU A 907      23.626  34.519  56.549  1.00 55.28           N  
ATOM   1873  CA  GLU A 907      22.388  33.768  56.393  1.00 53.60           C  
ATOM   1874  C   GLU A 907      22.580  32.320  56.883  1.00 59.27           C  
ATOM   1875  O   GLU A 907      23.708  31.787  56.860  1.00 58.09           O  
ATOM   1876  CB  GLU A 907      21.969  33.797  54.929  1.00 46.36           C  
ATOM   1877  CG  GLU A 907      20.601  33.181  54.598  1.00 54.18           C  
ATOM   1878  CD  GLU A 907      20.147  33.563  53.199  1.00 71.70           C  
ATOM   1879  OE1 GLU A 907      20.750  34.496  52.618  1.00 68.71           O  
ATOM   1880  OE2 GLU A 907      19.199  32.937  52.675  1.00 88.46           O  
ATOM   1881  N   ARG A 908      21.491  31.704  57.352  1.00 48.00           N  
ATOM   1882  CA  ARG A 908      21.528  30.338  57.847  1.00 40.97           C  
ATOM   1883  C   ARG A 908      20.252  29.618  57.515  1.00 38.02           C  
ATOM   1884  O   ARG A 908      19.362  30.198  56.938  1.00 46.84           O  
ATOM   1885  CB  ARG A 908      21.752  30.313  59.356  1.00 44.56           C  
ATOM   1886  CG  ARG A 908      23.137  30.772  59.789  1.00 48.20           C  
ATOM   1887  CD  ARG A 908      24.252  29.854  59.273  1.00 38.82           C  
ATOM   1888  NE  ARG A 908      25.547  30.254  59.832  1.00 42.22           N  
ATOM   1889  CZ  ARG A 908      26.303  31.243  59.356  1.00 40.71           C  
ATOM   1890  NH1 ARG A 908      25.931  31.949  58.289  1.00 32.91           N  
ATOM   1891  NH2 ARG A 908      27.386  31.599  60.014  1.00 42.84           N  
ATOM   1892  N   LEU A 909      20.169  28.336  57.852  1.00 46.82           N  
ATOM   1893  CA  LEU A 909      18.967  27.573  57.552  1.00 50.32           C  
ATOM   1894  C   LEU A 909      17.854  28.115  58.422  1.00 55.51           C  
ATOM   1895  O   LEU A 909      18.109  28.615  59.515  1.00 60.61           O  
ATOM   1896  CB  LEU A 909      19.190  26.069  57.774  1.00 52.53           C  
ATOM   1897  CG  LEU A 909      20.062  25.393  56.698  1.00 54.68           C  
ATOM   1898  CD1 LEU A 909      20.346  23.927  57.021  1.00 44.35           C  
ATOM   1899  CD2 LEU A 909      19.360  25.494  55.356  1.00 46.03           C  
ATOM   1900  N   PRO A 910      16.614  28.091  57.918  1.00 57.86           N  
ATOM   1901  CA  PRO A 910      15.462  28.597  58.668  1.00 56.33           C  
ATOM   1902  C   PRO A 910      14.984  27.694  59.817  1.00 57.65           C  
ATOM   1903  O   PRO A 910      15.282  26.508  59.852  1.00 58.73           O  
ATOM   1904  CB  PRO A 910      14.409  28.753  57.573  1.00 53.42           C  
ATOM   1905  CG  PRO A 910      14.703  27.576  56.684  1.00 55.12           C  
ATOM   1906  CD  PRO A 910      16.211  27.640  56.570  1.00 47.03           C  
ATOM   1907  N   GLN A 911      14.242  28.284  60.753  1.00 55.96           N  
ATOM   1908  CA  GLN A 911      13.697  27.585  61.908  1.00 46.66           C  
ATOM   1909  C   GLN A 911      12.567  26.662  61.445  1.00 45.18           C  
ATOM   1910  O   GLN A 911      11.588  27.106  60.876  1.00 55.50           O  
ATOM   1911  CB  GLN A 911      13.212  28.616  62.956  1.00 40.07           C  
ATOM   1912  CG  GLN A 911      12.588  28.034  64.242  1.00 35.29           C  
ATOM   1913  CD  GLN A 911      12.434  29.055  65.415  1.00 53.57           C  
ATOM   1914  OE1 GLN A 911      12.804  30.240  65.324  1.00 44.84           O  
ATOM   1915  NE2 GLN A 911      11.891  28.569  66.525  1.00 46.47           N  
ATOM   1916  N   PRO A 912      12.747  25.344  61.584  1.00 51.11           N  
ATOM   1917  CA  PRO A 912      11.715  24.388  61.167  1.00 49.52           C  
ATOM   1918  C   PRO A 912      10.461  24.669  61.973  1.00 54.69           C  
ATOM   1919  O   PRO A 912      10.545  24.912  63.179  1.00 56.20           O  
ATOM   1920  CB  PRO A 912      12.316  23.035  61.581  1.00 40.64           C  
ATOM   1921  CG  PRO A 912      13.777  23.269  61.485  1.00 45.74           C  
ATOM   1922  CD  PRO A 912      13.936  24.642  62.098  1.00 50.93           C  
ATOM   1923  N   PRO A 913       9.290  24.685  61.319  1.00 55.41           N  
ATOM   1924  CA  PRO A 913       8.011  24.942  61.980  1.00 54.44           C  
ATOM   1925  C   PRO A 913       7.736  24.197  63.271  1.00 50.72           C  
ATOM   1926  O   PRO A 913       7.132  24.763  64.174  1.00 56.73           O  
ATOM   1927  CB  PRO A 913       6.973  24.611  60.898  1.00 52.36           C  
ATOM   1928  CG  PRO A 913       7.762  24.119  59.720  1.00 52.87           C  
ATOM   1929  CD  PRO A 913       9.108  24.761  59.868  1.00 57.55           C  
ATOM   1930  N   ILE A 914       8.208  22.961  63.392  1.00 51.85           N  
ATOM   1931  CA  ILE A 914       7.963  22.189  64.616  1.00 39.36           C  
ATOM   1932  C   ILE A 914       8.942  22.498  65.746  1.00 35.86           C  
ATOM   1933  O   ILE A 914       8.796  21.988  66.879  1.00 34.47           O  
ATOM   1934  CB  ILE A 914       8.021  20.667  64.350  1.00 46.49           C  
ATOM   1935  CG1 ILE A 914       9.463  20.221  64.142  1.00 41.22           C  
ATOM   1936  CG2 ILE A 914       7.183  20.294  63.127  1.00 36.42           C  
ATOM   1937  CD1 ILE A 914       9.629  18.713  64.185  1.00 34.65           C  
ATOM   1938  N   CYS A 915       9.890  23.388  65.456  1.00 34.44           N  
ATOM   1939  CA  CYS A 915      10.947  23.727  66.403  1.00 43.79           C  
ATOM   1940  C   CYS A 915      10.785  24.842  67.394  1.00 47.38           C  
ATOM   1941  O   CYS A 915      10.647  26.002  67.013  1.00 52.88           O  
ATOM   1942  CB  CYS A 915      12.254  23.995  65.659  1.00 59.03           C  
ATOM   1943  SG  CYS A 915      13.108  22.535  65.086  1.00 45.18           S  
ATOM   1944  N   THR A 916      10.901  24.502  68.673  1.00 43.25           N  
ATOM   1945  CA  THR A 916      10.841  25.522  69.697  1.00 41.83           C  
ATOM   1946  C   THR A 916      12.155  26.259  69.542  1.00 40.20           C  
ATOM   1947  O   THR A 916      13.109  25.725  68.980  1.00 50.55           O  
ATOM   1948  CB  THR A 916      10.784  24.946  71.120  1.00 42.07           C  
ATOM   1949  OG1 THR A 916      11.865  24.033  71.312  1.00 48.03           O  
ATOM   1950  CG2 THR A 916       9.463  24.247  71.379  1.00 42.97           C  
ATOM   1951  N   ILE A 917      12.209  27.485  70.040  1.00 44.16           N  
ATOM   1952  CA  ILE A 917      13.423  28.276  69.949  1.00 42.89           C  
ATOM   1953  C   ILE A 917      14.598  27.564  70.643  1.00 38.64           C  
ATOM   1954  O   ILE A 917      15.731  27.744  70.247  1.00 38.32           O  
ATOM   1955  CB  ILE A 917      13.217  29.703  70.547  1.00 44.79           C  
ATOM   1956  CG1 ILE A 917      14.450  30.564  70.242  1.00 44.21           C  
ATOM   1957  CG2 ILE A 917      12.880  29.627  72.049  1.00 33.40           C  
ATOM   1958  CD1 ILE A 917      14.499  31.900  70.920  1.00 50.48           C  
ATOM   1959  N   ASP A 918      14.303  26.758  71.664  1.00 34.19           N  
ATOM   1960  CA  ASP A 918      15.291  26.011  72.428  1.00 33.48           C  
ATOM   1961  C   ASP A 918      16.088  25.078  71.504  1.00 44.55           C  
ATOM   1962  O   ASP A 918      17.318  25.016  71.566  1.00 41.25           O  
ATOM   1963  CB  ASP A 918      14.581  25.147  73.474  1.00 34.30           C  
ATOM   1964  CG  ASP A 918      13.876  25.964  74.533  1.00 50.76           C  
ATOM   1965  OD1 ASP A 918      12.719  26.387  74.308  1.00 43.90           O  
ATOM   1966  OD2 ASP A 918      14.466  26.154  75.612  1.00 49.86           O  
ATOM   1967  N   VAL A 919      15.369  24.312  70.687  1.00 41.36           N  
ATOM   1968  CA  VAL A 919      15.988  23.379  69.761  1.00 37.02           C  
ATOM   1969  C   VAL A 919      16.719  24.117  68.642  1.00 44.27           C  
ATOM   1970  O   VAL A 919      17.839  23.766  68.298  1.00 51.26           O  
ATOM   1971  CB  VAL A 919      14.936  22.420  69.140  1.00 32.63           C  
ATOM   1972  CG1 VAL A 919      15.531  21.657  67.948  1.00 26.21           C  
ATOM   1973  CG2 VAL A 919      14.459  21.420  70.182  1.00 28.40           C  
ATOM   1974  N   TYR A 920      16.075  25.129  68.068  1.00 44.12           N  
ATOM   1975  CA  TYR A 920      16.666  25.884  66.979  1.00 40.48           C  
ATOM   1976  C   TYR A 920      17.936  26.617  67.388  1.00 43.47           C  
ATOM   1977  O   TYR A 920      18.829  26.842  66.572  1.00 51.05           O  
ATOM   1978  CB  TYR A 920      15.654  26.866  66.404  1.00 43.40           C  
ATOM   1979  CG  TYR A 920      16.181  27.634  65.221  1.00 40.15           C  
ATOM   1980  CD1 TYR A 920      16.713  26.979  64.116  1.00 47.09           C  
ATOM   1981  CD2 TYR A 920      16.123  29.015  65.194  1.00 50.61           C  
ATOM   1982  CE1 TYR A 920      17.174  27.697  63.006  1.00 58.98           C  
ATOM   1983  CE2 TYR A 920      16.574  29.739  64.097  1.00 48.19           C  
ATOM   1984  CZ  TYR A 920      17.099  29.078  63.014  1.00 53.26           C  
ATOM   1985  OH  TYR A 920      17.590  29.816  61.971  1.00 45.81           O  
ATOM   1986  N   MET A 921      18.022  26.970  68.659  1.00 44.36           N  
ATOM   1987  CA  MET A 921      19.189  27.656  69.185  1.00 45.93           C  
ATOM   1988  C   MET A 921      20.383  26.682  69.183  1.00 47.62           C  
ATOM   1989  O   MET A 921      21.546  27.110  69.162  1.00 40.44           O  
ATOM   1990  CB  MET A 921      18.901  28.107  70.610  1.00 45.87           C  
ATOM   1991  CG  MET A 921      19.877  29.101  71.158  1.00 57.18           C  
ATOM   1992  SD  MET A 921      19.133  30.691  71.032  1.00 80.91           S  
ATOM   1993  CE  MET A 921      20.355  31.474  70.081  1.00 82.49           C  
ATOM   1994  N   ILE A 922      20.089  25.383  69.283  1.00 40.48           N  
ATOM   1995  CA  ILE A 922      21.139  24.364  69.263  1.00 49.52           C  
ATOM   1996  C   ILE A 922      21.713  24.299  67.839  1.00 46.88           C  
ATOM   1997  O   ILE A 922      22.927  24.342  67.661  1.00 47.97           O  
ATOM   1998  CB  ILE A 922      20.622  22.946  69.653  1.00 56.34           C  
ATOM   1999  CG1 ILE A 922      19.955  22.953  71.031  1.00 37.27           C  
ATOM   2000  CG2 ILE A 922      21.776  21.973  69.682  1.00 48.26           C  
ATOM   2001  CD1 ILE A 922      20.891  23.229  72.157  1.00 48.32           C  
ATOM   2002  N   MET A 923      20.830  24.241  66.841  1.00 41.32           N  
ATOM   2003  CA  MET A 923      21.229  24.190  65.440  1.00 40.08           C  
ATOM   2004  C   MET A 923      22.004  25.437  65.054  1.00 40.96           C  
ATOM   2005  O   MET A 923      23.027  25.358  64.389  1.00 50.36           O  
ATOM   2006  CB  MET A 923      20.004  24.033  64.537  1.00 34.16           C  
ATOM   2007  CG  MET A 923      19.175  22.782  64.835  1.00 39.27           C  
ATOM   2008  SD  MET A 923      17.581  22.722  63.984  1.00 53.56           S  
ATOM   2009  CE  MET A 923      17.994  23.546  62.618  1.00 37.06           C  
ATOM   2010  N   VAL A 924      21.534  26.590  65.499  1.00 46.48           N  
ATOM   2011  CA  VAL A 924      22.204  27.854  65.211  1.00 44.40           C  
ATOM   2012  C   VAL A 924      23.617  27.921  65.812  1.00 42.15           C  
ATOM   2013  O   VAL A 924      24.541  28.457  65.189  1.00 37.83           O  
ATOM   2014  CB  VAL A 924      21.321  29.049  65.685  1.00 44.34           C  
ATOM   2015  CG1 VAL A 924      22.075  30.385  65.628  1.00 35.94           C  
ATOM   2016  CG2 VAL A 924      20.087  29.106  64.822  1.00 25.11           C  
ATOM   2017  N   LYS A 925      23.794  27.352  67.001  1.00 43.48           N  
ATOM   2018  CA  LYS A 925      25.108  27.365  67.657  1.00 40.80           C  
ATOM   2019  C   LYS A 925      26.141  26.515  66.918  1.00 44.65           C  
ATOM   2020  O   LYS A 925      27.328  26.804  66.966  1.00 48.08           O  
ATOM   2021  CB  LYS A 925      25.006  26.874  69.094  1.00 40.04           C  
ATOM   2022  CG  LYS A 925      24.345  27.819  70.060  1.00 46.03           C  
ATOM   2023  CD  LYS A 925      24.275  27.160  71.438  1.00 55.99           C  
ATOM   2024  CE  LYS A 925      23.660  28.087  72.485  1.00 51.98           C  
ATOM   2025  NZ  LYS A 925      23.552  27.389  73.781  1.00 76.81           N  
ATOM   2026  N   CYS A 926      25.692  25.454  66.254  1.00 40.92           N  
ATOM   2027  CA  CYS A 926      26.593  24.584  65.506  1.00 41.05           C  
ATOM   2028  C   CYS A 926      27.088  25.314  64.246  1.00 46.96           C  
ATOM   2029  O   CYS A 926      28.036  24.862  63.592  1.00 45.06           O  
ATOM   2030  CB  CYS A 926      25.872  23.289  65.083  1.00 33.48           C  
ATOM   2031  SG  CYS A 926      25.267  22.189  66.390  1.00 43.38           S  
ATOM   2032  N   TRP A 927      26.435  26.436  63.924  1.00 45.45           N  
ATOM   2033  CA  TRP A 927      26.735  27.235  62.744  1.00 34.61           C  
ATOM   2034  C   TRP A 927      27.444  28.573  62.966  1.00 37.33           C  
ATOM   2035  O   TRP A 927      27.432  29.442  62.087  1.00 38.69           O  
ATOM   2036  CB  TRP A 927      25.463  27.442  61.932  1.00 29.93           C  
ATOM   2037  CG  TRP A 927      24.792  26.160  61.532  1.00 44.93           C  
ATOM   2038  CD1 TRP A 927      25.390  24.946  61.346  1.00 42.64           C  
ATOM   2039  CD2 TRP A 927      23.389  25.950  61.319  1.00 35.04           C  
ATOM   2040  NE1 TRP A 927      24.450  23.991  61.042  1.00 45.36           N  
ATOM   2041  CE2 TRP A 927      23.212  24.576  61.020  1.00 40.08           C  
ATOM   2042  CE3 TRP A 927      22.262  26.783  61.364  1.00 35.22           C  
ATOM   2043  CZ2 TRP A 927      21.950  24.010  60.762  1.00 45.51           C  
ATOM   2044  CZ3 TRP A 927      20.986  26.217  61.108  1.00 32.98           C  
ATOM   2045  CH2 TRP A 927      20.850  24.845  60.811  1.00 41.20           C  
ATOM   2046  N   MET A 928      28.059  28.736  64.134  1.00 40.15           N  
ATOM   2047  CA  MET A 928      28.826  29.942  64.452  1.00 47.61           C  
ATOM   2048  C   MET A 928      30.069  29.919  63.561  1.00 53.00           C  
ATOM   2049  O   MET A 928      30.506  28.848  63.160  1.00 61.95           O  
ATOM   2050  CB  MET A 928      29.311  29.893  65.901  1.00 42.38           C  
ATOM   2051  CG  MET A 928      28.229  29.672  66.947  1.00 60.23           C  
ATOM   2052  SD  MET A 928      27.304  31.160  67.360  1.00 64.93           S  
ATOM   2053  CE  MET A 928      28.256  31.741  68.635  1.00 54.96           C  
ATOM   2054  N   ILE A 929      30.637  31.086  63.259  1.00 62.12           N  
ATOM   2055  CA  ILE A 929      31.842  31.180  62.430  1.00 54.18           C  
ATOM   2056  C   ILE A 929      33.024  30.579  63.193  1.00 57.90           C  
ATOM   2057  O   ILE A 929      33.742  29.730  62.663  1.00 66.53           O  
ATOM   2058  CB  ILE A 929      32.156  32.670  62.019  1.00 68.40           C  
ATOM   2059  CG1 ILE A 929      31.554  33.002  60.647  1.00 65.06           C  
ATOM   2060  CG2 ILE A 929      33.667  32.920  61.938  1.00 84.32           C  
ATOM   2061  CD1 ILE A 929      30.052  32.974  60.594  1.00 82.00           C  
ATOM   2062  N   ASP A 930      33.217  31.013  64.435  1.00 56.88           N  
ATOM   2063  CA  ASP A 930      34.305  30.507  65.274  1.00 60.72           C  
ATOM   2064  C   ASP A 930      33.981  29.057  65.674  1.00 65.68           C  
ATOM   2065  O   ASP A 930      33.073  28.810  66.471  1.00 69.29           O  
ATOM   2066  CB  ASP A 930      34.464  31.396  66.516  1.00 49.19           C  
ATOM   2067  CG  ASP A 930      35.653  31.008  67.367  1.00 76.52           C  
ATOM   2068  OD1 ASP A 930      36.796  31.051  66.858  1.00 91.04           O  
ATOM   2069  OD2 ASP A 930      35.449  30.672  68.554  1.00 85.32           O  
ATOM   2070  N   ALA A 931      34.725  28.106  65.111  1.00 64.45           N  
ATOM   2071  CA  ALA A 931      34.500  26.684  65.363  1.00 54.95           C  
ATOM   2072  C   ALA A 931      34.458  26.271  66.836  1.00 50.32           C  
ATOM   2073  O   ALA A 931      33.625  25.440  67.206  1.00 44.54           O  
ATOM   2074  CB  ALA A 931      35.506  25.829  64.578  1.00 55.27           C  
ATOM   2075  N   ASP A 932      35.327  26.852  67.668  1.00 45.65           N  
ATOM   2076  CA  ASP A 932      35.351  26.541  69.109  1.00 49.79           C  
ATOM   2077  C   ASP A 932      34.110  27.039  69.846  1.00 51.78           C  
ATOM   2078  O   ASP A 932      33.817  26.598  70.951  1.00 56.79           O  
ATOM   2079  CB  ASP A 932      36.587  27.131  69.795  1.00 63.01           C  
ATOM   2080  CG  ASP A 932      37.896  26.559  69.261  1.00 84.76           C  
ATOM   2081  OD1 ASP A 932      38.005  25.320  69.088  1.00 75.16           O  
ATOM   2082  OD2 ASP A 932      38.823  27.367  69.024  1.00 81.12           O  
ATOM   2083  N   SER A 933      33.415  28.002  69.259  1.00 49.93           N  
ATOM   2084  CA  SER A 933      32.211  28.522  69.872  1.00 53.57           C  
ATOM   2085  C   SER A 933      31.081  27.511  69.739  1.00 55.00           C  
ATOM   2086  O   SER A 933      30.162  27.491  70.562  1.00 53.86           O  
ATOM   2087  CB  SER A 933      31.808  29.847  69.227  1.00 53.41           C  
ATOM   2088  OG  SER A 933      32.645  30.891  69.698  1.00 74.85           O  
ATOM   2089  N   ARG A 934      31.151  26.669  68.709  1.00 41.41           N  
ATOM   2090  CA  ARG A 934      30.115  25.672  68.505  1.00 42.43           C  
ATOM   2091  C   ARG A 934      30.166  24.667  69.635  1.00 39.42           C  
ATOM   2092  O   ARG A 934      31.171  24.577  70.336  1.00 41.44           O  
ATOM   2093  CB  ARG A 934      30.315  24.946  67.189  1.00 36.51           C  
ATOM   2094  CG  ARG A 934      30.461  25.871  66.050  1.00 46.26           C  
ATOM   2095  CD  ARG A 934      30.808  25.141  64.794  1.00 40.38           C  
ATOM   2096  NE  ARG A 934      31.186  26.119  63.780  1.00 60.06           N  
ATOM   2097  CZ  ARG A 934      32.044  25.902  62.794  1.00 46.49           C  
ATOM   2098  NH1 ARG A 934      32.651  24.729  62.664  1.00 35.72           N  
ATOM   2099  NH2 ARG A 934      32.230  26.846  61.896  1.00 32.88           N  
ATOM   2100  N   PRO A 935      29.040  23.997  69.909  1.00 38.15           N  
ATOM   2101  CA  PRO A 935      29.044  23.006  70.985  1.00 39.62           C  
ATOM   2102  C   PRO A 935      29.889  21.789  70.607  1.00 46.52           C  
ATOM   2103  O   PRO A 935      30.304  21.608  69.449  1.00 42.39           O  
ATOM   2104  CB  PRO A 935      27.563  22.623  71.127  1.00 29.89           C  
ATOM   2105  CG  PRO A 935      26.919  23.046  69.850  1.00 42.50           C  
ATOM   2106  CD  PRO A 935      27.670  24.268  69.425  1.00 37.33           C  
ATOM   2107  N   LYS A 936      30.145  20.968  71.609  1.00 43.51           N  
ATOM   2108  CA  LYS A 936      30.903  19.756  71.440  1.00 44.28           C  
ATOM   2109  C   LYS A 936      29.893  18.631  71.435  1.00 44.64           C  
ATOM   2110  O   LYS A 936      28.814  18.754  72.034  1.00 41.04           O  
ATOM   2111  CB  LYS A 936      31.893  19.586  72.600  1.00 39.02           C  
ATOM   2112  CG  LYS A 936      32.971  20.676  72.637  1.00 47.20           C  
ATOM   2113  CD  LYS A 936      33.993  20.415  73.748  1.00 75.87           C  
ATOM   2114  CE  LYS A 936      35.002  21.560  73.915  1.00 77.64           C  
ATOM   2115  NZ  LYS A 936      34.375  22.796  74.471  1.00 85.90           N  
ATOM   2116  N   PHE A 937      30.223  17.545  70.737  1.00 46.58           N  
ATOM   2117  CA  PHE A 937      29.336  16.401  70.681  1.00 36.52           C  
ATOM   2118  C   PHE A 937      28.941  15.916  72.086  1.00 39.44           C  
ATOM   2119  O   PHE A 937      27.763  15.612  72.328  1.00 40.59           O  
ATOM   2120  CB  PHE A 937      29.941  15.279  69.838  1.00 35.72           C  
ATOM   2121  CG  PHE A 937      29.852  15.530  68.364  1.00 35.87           C  
ATOM   2122  CD1 PHE A 937      28.613  15.652  67.743  1.00 35.97           C  
ATOM   2123  CD2 PHE A 937      31.006  15.692  67.601  1.00 40.42           C  
ATOM   2124  CE1 PHE A 937      28.522  15.938  66.381  1.00 42.10           C  
ATOM   2125  CE2 PHE A 937      30.927  15.981  66.234  1.00 33.24           C  
ATOM   2126  CZ  PHE A 937      29.678  16.105  65.629  1.00 55.65           C  
ATOM   2127  N   ARG A 938      29.884  15.922  73.032  1.00 30.91           N  
ATOM   2128  CA  ARG A 938      29.534  15.483  74.380  1.00 35.47           C  
ATOM   2129  C   ARG A 938      28.443  16.392  74.989  1.00 38.99           C  
ATOM   2130  O   ARG A 938      27.590  15.925  75.754  1.00 40.29           O  
ATOM   2131  CB  ARG A 938      30.766  15.383  75.297  1.00 33.40           C  
ATOM   2132  CG  ARG A 938      31.543  16.685  75.490  1.00 56.97           C  
ATOM   2133  CD  ARG A 938      32.552  16.596  76.620  1.00 63.24           C  
ATOM   2134  NE  ARG A 938      31.968  16.105  77.880  1.00 88.47           N  
ATOM   2135  CZ  ARG A 938      31.306  16.844  78.776  1.00 84.19           C  
ATOM   2136  NH1 ARG A 938      30.836  16.271  79.876  1.00 86.37           N  
ATOM   2137  NH2 ARG A 938      31.098  18.144  78.586  1.00 81.25           N  
ATOM   2138  N   GLU A 939      28.430  17.670  74.607  1.00 37.26           N  
ATOM   2139  CA  GLU A 939      27.409  18.594  75.118  1.00 39.02           C  
ATOM   2140  C   GLU A 939      26.082  18.416  74.397  1.00 42.19           C  
ATOM   2141  O   GLU A 939      25.022  18.536  75.014  1.00 41.43           O  
ATOM   2142  CB  GLU A 939      27.848  20.045  74.999  1.00 27.30           C  
ATOM   2143  CG  GLU A 939      28.987  20.415  75.928  1.00 33.07           C  
ATOM   2144  CD  GLU A 939      29.757  21.607  75.406  1.00 46.40           C  
ATOM   2145  OE1 GLU A 939      29.504  21.991  74.235  1.00 38.96           O  
ATOM   2146  OE2 GLU A 939      30.598  22.160  76.157  1.00 54.12           O  
ATOM   2147  N   LEU A 940      26.141  18.144  73.094  1.00 44.41           N  
ATOM   2148  CA  LEU A 940      24.929  17.926  72.314  1.00 35.45           C  
ATOM   2149  C   LEU A 940      24.155  16.743  72.898  1.00 36.59           C  
ATOM   2150  O   LEU A 940      22.929  16.760  72.918  1.00 41.71           O  
ATOM   2151  CB  LEU A 940      25.269  17.627  70.852  1.00 31.78           C  
ATOM   2152  CG  LEU A 940      25.457  18.719  69.789  1.00 35.75           C  
ATOM   2153  CD1 LEU A 940      24.419  19.821  69.948  1.00 30.93           C  
ATOM   2154  CD2 LEU A 940      26.801  19.285  69.834  1.00 45.73           C  
ATOM   2155  N   ILE A 941      24.881  15.737  73.393  1.00 33.71           N  
ATOM   2156  CA  ILE A 941      24.288  14.532  73.980  1.00 32.37           C  
ATOM   2157  C   ILE A 941      23.479  14.880  75.216  1.00 37.88           C  
ATOM   2158  O   ILE A 941      22.333  14.455  75.342  1.00 48.34           O  
ATOM   2159  CB  ILE A 941      25.374  13.524  74.380  1.00 34.04           C  
ATOM   2160  CG1 ILE A 941      26.124  13.043  73.145  1.00 27.29           C  
ATOM   2161  CG2 ILE A 941      24.778  12.333  75.163  1.00 18.00           C  
ATOM   2162  CD1 ILE A 941      27.371  12.199  73.497  1.00 28.95           C  
ATOM   2163  N   ILE A 942      24.093  15.649  76.123  1.00 45.39           N  
ATOM   2164  CA  ILE A 942      23.469  16.118  77.375  1.00 38.61           C  
ATOM   2165  C   ILE A 942      22.218  16.939  77.033  1.00 33.47           C  
ATOM   2166  O   ILE A 942      21.123  16.627  77.482  1.00 34.41           O  
ATOM   2167  CB  ILE A 942      24.473  17.007  78.179  1.00 41.34           C  
ATOM   2168  CG1 ILE A 942      25.632  16.146  78.669  1.00 38.77           C  
ATOM   2169  CG2 ILE A 942      23.795  17.679  79.392  1.00 36.18           C  
ATOM   2170  CD1 ILE A 942      26.789  16.937  79.223  1.00 30.80           C  
ATOM   2171  N   GLU A 943      22.391  17.960  76.198  1.00 28.84           N  
ATOM   2172  CA  GLU A 943      21.291  18.824  75.784  1.00 30.47           C  
ATOM   2173  C   GLU A 943      20.089  18.096  75.233  1.00 35.87           C  
ATOM   2174  O   GLU A 943      18.982  18.214  75.772  1.00 40.99           O  
ATOM   2175  CB  GLU A 943      21.762  19.871  74.779  1.00 35.02           C  
ATOM   2176  CG  GLU A 943      22.617  20.986  75.404  1.00 39.86           C  
ATOM   2177  CD  GLU A 943      22.041  21.483  76.733  1.00 77.41           C  
ATOM   2178  OE1 GLU A 943      20.966  22.134  76.724  1.00 85.94           O  
ATOM   2179  OE2 GLU A 943      22.660  21.205  77.789  1.00 72.26           O  
ATOM   2180  N   PHE A 944      20.300  17.320  74.179  1.00 38.26           N  
ATOM   2181  CA  PHE A 944      19.202  16.581  73.597  1.00 31.16           C  
ATOM   2182  C   PHE A 944      18.686  15.504  74.553  1.00 41.19           C  
ATOM   2183  O   PHE A 944      17.497  15.148  74.523  1.00 41.21           O  
ATOM   2184  CB  PHE A 944      19.590  16.017  72.237  1.00 24.37           C  
ATOM   2185  CG  PHE A 944      19.595  17.046  71.138  1.00 27.04           C  
ATOM   2186  CD1 PHE A 944      18.411  17.457  70.537  1.00 28.88           C  
ATOM   2187  CD2 PHE A 944      20.767  17.593  70.701  1.00 22.64           C  
ATOM   2188  CE1 PHE A 944      18.416  18.399  69.516  1.00 26.21           C  
ATOM   2189  CE2 PHE A 944      20.781  18.539  69.678  1.00 30.12           C  
ATOM   2190  CZ  PHE A 944      19.597  18.942  69.082  1.00 25.91           C  
ATOM   2191  N   SER A 945      19.532  15.027  75.459  1.00 32.00           N  
ATOM   2192  CA  SER A 945      19.027  14.020  76.389  1.00 34.64           C  
ATOM   2193  C   SER A 945      17.989  14.623  77.342  1.00 35.94           C  
ATOM   2194  O   SER A 945      16.975  13.992  77.616  1.00 40.02           O  
ATOM   2195  CB  SER A 945      20.150  13.365  77.177  1.00 23.33           C  
ATOM   2196  OG  SER A 945      19.937  11.977  77.248  1.00 58.22           O  
ATOM   2197  N   LYS A 946      18.247  15.833  77.850  1.00 37.03           N  
ATOM   2198  CA  LYS A 946      17.310  16.518  78.758  1.00 32.11           C  
ATOM   2199  C   LYS A 946      15.985  16.725  78.029  1.00 35.11           C  
ATOM   2200  O   LYS A 946      14.945  16.394  78.556  1.00 45.42           O  
ATOM   2201  CB  LYS A 946      17.836  17.890  79.192  1.00 29.76           C  
ATOM   2202  CG  LYS A 946      19.123  17.913  80.016  1.00 36.53           C  
ATOM   2203  CD  LYS A 946      19.429  19.361  80.407  1.00 41.91           C  
ATOM   2204  CE  LYS A 946      20.719  19.533  81.173  1.00 70.01           C  
ATOM   2205  NZ  LYS A 946      21.235  20.938  81.036  1.00 67.11           N  
ATOM   2206  N   MET A 947      16.040  17.250  76.805  1.00 31.98           N  
ATOM   2207  CA  MET A 947      14.850  17.472  75.994  1.00 33.38           C  
ATOM   2208  C   MET A 947      14.133  16.168  75.714  1.00 37.66           C  
ATOM   2209  O   MET A 947      12.928  16.142  75.542  1.00 43.14           O  
ATOM   2210  CB  MET A 947      15.213  18.100  74.639  1.00 27.03           C  
ATOM   2211  CG  MET A 947      15.830  19.490  74.725  1.00 26.82           C  
ATOM   2212  SD  MET A 947      16.241  20.172  73.148  1.00 42.66           S  
ATOM   2213  CE  MET A 947      16.471  21.663  73.619  1.00 27.60           C  
ATOM   2214  N   ALA A 948      14.874  15.079  75.615  1.00 40.01           N  
ATOM   2215  CA  ALA A 948      14.223  13.812  75.319  1.00 42.39           C  
ATOM   2216  C   ALA A 948      13.339  13.324  76.461  1.00 42.96           C  
ATOM   2217  O   ALA A 948      12.431  12.534  76.234  1.00 42.41           O  
ATOM   2218  CB  ALA A 948      15.245  12.759  74.944  1.00 38.29           C  
ATOM   2219  N   ARG A 949      13.589  13.814  77.673  1.00 42.09           N  
ATOM   2220  CA  ARG A 949      12.806  13.409  78.839  1.00 47.73           C  
ATOM   2221  C   ARG A 949      11.431  14.074  78.847  1.00 50.58           C  
ATOM   2222  O   ARG A 949      10.515  13.617  79.536  1.00 51.13           O  
ATOM   2223  CB  ARG A 949      13.547  13.738  80.138  1.00 49.42           C  
ATOM   2224  CG  ARG A 949      14.915  13.105  80.262  1.00 63.41           C  
ATOM   2225  CD  ARG A 949      15.643  13.621  81.489  1.00 71.71           C  
ATOM   2226  NE  ARG A 949      15.167  12.973  82.704  1.00 89.72           N  
ATOM   2227  CZ  ARG A 949      15.696  11.865  83.216  1.00100.01           C  
ATOM   2228  NH1 ARG A 949      16.727  11.278  82.617  1.00 83.06           N  
ATOM   2229  NH2 ARG A 949      15.202  11.351  84.336  1.00 95.80           N  
ATOM   2230  N   ASP A 950      11.286  15.132  78.052  1.00 43.83           N  
ATOM   2231  CA  ASP A 950      10.025  15.859  77.960  1.00 42.05           C  
ATOM   2232  C   ASP A 950       9.888  16.435  76.560  1.00 39.84           C  
ATOM   2233  O   ASP A 950       9.825  17.652  76.389  1.00 39.55           O  
ATOM   2234  CB  ASP A 950      10.005  16.983  78.998  1.00 51.48           C  
ATOM   2235  CG  ASP A 950       8.639  17.615  79.156  1.00 58.95           C  
ATOM   2236  OD1 ASP A 950       7.624  16.976  78.793  1.00 55.22           O  
ATOM   2237  OD2 ASP A 950       8.589  18.759  79.655  1.00 62.28           O  
ATOM   2238  N   PRO A 951       9.739  15.551  75.551  1.00 40.81           N  
ATOM   2239  CA  PRO A 951       9.599  15.784  74.103  1.00 36.20           C  
ATOM   2240  C   PRO A 951       8.714  16.936  73.658  1.00 37.25           C  
ATOM   2241  O   PRO A 951       9.136  17.804  72.904  1.00 45.03           O  
ATOM   2242  CB  PRO A 951       9.006  14.466  73.591  1.00 38.69           C  
ATOM   2243  CG  PRO A 951       9.428  13.443  74.585  1.00 30.83           C  
ATOM   2244  CD  PRO A 951       9.386  14.157  75.897  1.00 30.56           C  
ATOM   2245  N   GLN A 952       7.462  16.904  74.098  1.00 48.37           N  
ATOM   2246  CA  GLN A 952       6.474  17.902  73.714  1.00 47.07           C  
ATOM   2247  C   GLN A 952       6.749  19.343  74.138  1.00 44.39           C  
ATOM   2248  O   GLN A 952       6.193  20.273  73.559  1.00 49.87           O  
ATOM   2249  CB  GLN A 952       5.099  17.426  74.141  1.00 58.06           C  
ATOM   2250  CG  GLN A 952       4.902  15.952  73.801  1.00 64.13           C  
ATOM   2251  CD  GLN A 952       3.465  15.569  73.547  1.00 69.01           C  
ATOM   2252  OE1 GLN A 952       3.191  14.495  73.009  1.00 72.48           O  
ATOM   2253  NE2 GLN A 952       2.533  16.442  73.929  1.00 77.08           N  
ATOM   2254  N   ARG A 953       7.642  19.536  75.103  1.00 38.38           N  
ATOM   2255  CA  ARG A 953       8.006  20.885  75.526  1.00 41.33           C  
ATOM   2256  C   ARG A 953       8.999  21.472  74.539  1.00 46.11           C  
ATOM   2257  O   ARG A 953       9.222  22.690  74.520  1.00 41.69           O  
ATOM   2258  CB  ARG A 953       8.656  20.859  76.913  1.00 42.06           C  
ATOM   2259  CG  ARG A 953       9.232  22.194  77.380  1.00 40.58           C  
ATOM   2260  CD  ARG A 953       9.817  22.082  78.784  1.00 45.08           C  
ATOM   2261  NE  ARG A 953      10.380  23.346  79.259  1.00 54.96           N  
ATOM   2262  CZ  ARG A 953      10.877  23.539  80.480  1.00 53.15           C  
ATOM   2263  NH1 ARG A 953      10.872  22.559  81.373  1.00 54.51           N  
ATOM   2264  NH2 ARG A 953      11.461  24.687  80.782  1.00 56.52           N  
ATOM   2265  N   TYR A 954       9.595  20.604  73.717  1.00 45.84           N  
ATOM   2266  CA  TYR A 954      10.605  21.050  72.768  1.00 45.23           C  
ATOM   2267  C   TYR A 954      10.288  20.963  71.285  1.00 42.43           C  
ATOM   2268  O   TYR A 954      10.906  21.671  70.509  1.00 40.53           O  
ATOM   2269  CB  TYR A 954      11.936  20.393  73.097  1.00 41.53           C  
ATOM   2270  CG  TYR A 954      12.363  20.693  74.503  1.00 32.06           C  
ATOM   2271  CD1 TYR A 954      12.926  21.926  74.837  1.00 36.24           C  
ATOM   2272  CD2 TYR A 954      12.170  19.763  75.507  1.00 33.08           C  
ATOM   2273  CE1 TYR A 954      13.286  22.217  76.148  1.00 48.55           C  
ATOM   2274  CE2 TYR A 954      12.515  20.041  76.822  1.00 30.78           C  
ATOM   2275  CZ  TYR A 954      13.076  21.269  77.141  1.00 48.37           C  
ATOM   2276  OH  TYR A 954      13.429  21.530  78.454  1.00 43.57           O  
ATOM   2277  N   LEU A 955       9.380  20.071  70.885  1.00 36.81           N  
ATOM   2278  CA  LEU A 955       8.962  19.977  69.478  1.00 44.26           C  
ATOM   2279  C   LEU A 955       7.430  19.979  69.438  1.00 47.79           C  
ATOM   2280  O   LEU A 955       6.788  19.266  70.208  1.00 53.16           O  
ATOM   2281  CB  LEU A 955       9.513  18.710  68.808  1.00 44.08           C  
ATOM   2282  CG  LEU A 955      11.042  18.649  68.728  1.00 45.99           C  
ATOM   2283  CD1 LEU A 955      11.513  17.281  68.294  1.00 37.54           C  
ATOM   2284  CD2 LEU A 955      11.549  19.735  67.798  1.00 31.30           C  
ATOM   2285  N   VAL A 956       6.836  20.779  68.560  1.00 45.47           N  
ATOM   2286  CA  VAL A 956       5.375  20.832  68.486  1.00 52.78           C  
ATOM   2287  C   VAL A 956       4.863  20.158  67.203  1.00 53.17           C  
ATOM   2288  O   VAL A 956       4.915  20.717  66.101  1.00 55.14           O  
ATOM   2289  CB  VAL A 956       4.854  22.303  68.681  1.00 53.97           C  
ATOM   2290  CG1 VAL A 956       5.584  22.941  69.856  1.00 45.35           C  
ATOM   2291  CG2 VAL A 956       5.101  23.162  67.451  1.00 75.38           C  
ATOM   2292  N   ILE A 957       4.401  18.924  67.343  1.00 56.03           N  
ATOM   2293  CA  ILE A 957       3.944  18.169  66.179  1.00 57.87           C  
ATOM   2294  C   ILE A 957       2.466  17.847  66.285  1.00 66.18           C  
ATOM   2295  O   ILE A 957       2.038  17.212  67.258  1.00 66.05           O  
ATOM   2296  CB  ILE A 957       4.765  16.874  66.035  1.00 53.85           C  
ATOM   2297  CG1 ILE A 957       6.244  17.213  65.849  1.00 54.12           C  
ATOM   2298  CG2 ILE A 957       4.263  16.042  64.873  1.00 54.82           C  
ATOM   2299  CD1 ILE A 957       7.150  16.007  66.038  1.00 51.62           C  
ATOM   2300  N   GLN A 958       1.709  18.223  65.249  1.00 71.66           N  
ATOM   2301  CA  GLN A 958       0.257  18.028  65.226  1.00 73.95           C  
ATOM   2302  C   GLN A 958      -0.255  16.757  65.881  1.00 73.71           C  
ATOM   2303  O   GLN A 958      -0.976  16.824  66.878  1.00 85.17           O  
ATOM   2304  CB  GLN A 958      -0.311  18.205  63.814  1.00 86.01           C  
ATOM   2305  CG  GLN A 958      -0.287  19.673  63.331  1.00 96.70           C  
ATOM   2306  CD  GLN A 958      -0.889  19.883  61.938  1.00109.06           C  
ATOM   2307  OE1 GLN A 958      -1.102  21.024  61.501  1.00 92.87           O  
ATOM   2308  NE2 GLN A 958      -1.157  18.782  61.234  1.00108.78           N  
ATOM   2309  N   GLY A 959       0.175  15.606  65.394  1.00 67.82           N  
ATOM   2310  CA  GLY A 959      -0.286  14.372  65.993  1.00 75.47           C  
ATOM   2311  C   GLY A 959       0.354  14.001  67.311  1.00 83.33           C  
ATOM   2312  O   GLY A 959      -0.306  13.944  68.348  1.00 85.18           O  
ATOM   2313  N   ASP A 960       1.659  13.769  67.258  1.00 91.00           N  
ATOM   2314  CA  ASP A 960       2.460  13.364  68.408  1.00 97.35           C  
ATOM   2315  C   ASP A 960       1.929  12.134  69.151  1.00104.78           C  
ATOM   2316  O   ASP A 960       1.663  12.148  70.363  1.00105.25           O  
ATOM   2317  CB  ASP A 960       2.754  14.536  69.337  1.00 88.07           C  
ATOM   2318  CG  ASP A 960       4.243  14.778  69.480  1.00 82.75           C  
ATOM   2319  OD1 ASP A 960       4.663  15.953  69.615  1.00 94.90           O  
ATOM   2320  OD2 ASP A 960       4.991  13.776  69.441  1.00 44.80           O  
ATOM   2321  N   GLU A 961       1.813  11.070  68.357  1.00110.50           N  
ATOM   2322  CA  GLU A 961       1.346   9.741  68.738  1.00113.27           C  
ATOM   2323  C   GLU A 961       1.223   9.033  67.376  1.00116.78           C  
ATOM   2324  O   GLU A 961       2.233   8.581  66.814  1.00115.73           O  
ATOM   2325  CB  GLU A 961      -0.007   9.818  69.456  0.00107.62           C  
ATOM   2326  CG  GLU A 961      -0.443   8.523  70.136  0.00103.48           C  
ATOM   2327  CD  GLU A 961      -1.365   7.680  69.274  0.00107.05           C  
ATOM   2328  OE1 GLU A 961      -2.389   8.215  68.800  0.00103.70           O  
ATOM   2329  OE2 GLU A 961      -1.070   6.483  69.077  0.00111.53           O  
ATOM   2330  N   ARG A 962       0.014   9.028  66.808  1.00116.88           N  
ATOM   2331  CA  ARG A 962      -0.230   8.407  65.500  1.00116.76           C  
ATOM   2332  C   ARG A 962      -1.170   9.182  64.565  1.00116.92           C  
ATOM   2333  O   ARG A 962      -0.910   9.277  63.358  1.00117.27           O  
ATOM   2334  CB  ARG A 962      -0.771   6.982  65.655  0.00110.04           C  
ATOM   2335  CG  ARG A 962       0.287   5.908  65.839  0.00112.94           C  
ATOM   2336  CD  ARG A 962      -0.228   4.561  65.346  0.00104.53           C  
ATOM   2337  NE  ARG A 962      -0.509   4.587  63.911  0.00110.32           N  
ATOM   2338  CZ  ARG A 962      -1.144   3.627  63.244  0.00109.74           C  
ATOM   2339  NH1 ARG A 962      -1.347   3.751  61.939  0.00111.50           N  
ATOM   2340  NH2 ARG A 962      -1.581   2.546  63.876  0.00106.68           N  
ATOM   2341  N   MET A 963      -2.247   9.735  65.129  1.00116.91           N  
ATOM   2342  CA  MET A 963      -3.268  10.474  64.371  1.00115.26           C  
ATOM   2343  C   MET A 963      -4.108   9.501  63.556  1.00115.17           C  
ATOM   2344  O   MET A 963      -4.240   9.645  62.335  1.00114.82           O  
ATOM   2345  CB  MET A 963      -2.650  11.521  63.434  0.00107.81           C  
ATOM   2346  CG  MET A 963      -2.284  12.822  64.096  0.00109.34           C  
ATOM   2347  SD  MET A 963      -1.739  14.074  62.916  0.00105.34           S  
ATOM   2348  CE  MET A 963      -3.220  15.074  62.781  0.00108.60           C  
ATOM   2349  N   HIS A 964      -4.647   8.496  64.241  1.00112.44           N  
ATOM   2350  CA  HIS A 964      -5.470   7.475  63.606  1.00115.68           C  
ATOM   2351  C   HIS A 964      -6.806   8.052  63.112  1.00116.16           C  
ATOM   2352  O   HIS A 964      -7.013   8.227  61.906  1.00114.87           O  
ATOM   2353  CB  HIS A 964      -5.725   6.329  64.593  1.00113.98           C  
ATOM   2354  CG  HIS A 964      -5.734   4.971  63.957  1.00112.53           C  
ATOM   2355  ND1 HIS A 964      -5.380   3.830  64.649  1.00113.68           N  
ATOM   2356  CD2 HIS A 964      -6.032   4.572  62.699  1.00105.38           C  
ATOM   2357  CE1 HIS A 964      -5.457   2.788  63.840  1.00114.57           C  
ATOM   2358  NE2 HIS A 964      -5.850   3.209  62.651  1.00113.82           N  
ATOM   2359  N   LEU A 977     -11.036   6.578  61.901  1.00 98.67           N  
ATOM   2360  CA  LEU A 977     -12.096   6.763  60.910  1.00 97.99           C  
ATOM   2361  C   LEU A 977     -11.702   7.833  59.892  1.00100.95           C  
ATOM   2362  O   LEU A 977     -12.067   9.012  60.039  1.00100.25           O  
ATOM   2363  CB  LEU A 977     -13.399   7.183  61.600  1.00105.55           C  
ATOM   2364  CG  LEU A 977     -13.984   6.218  62.637  1.00111.80           C  
ATOM   2365  CD1 LEU A 977     -15.169   6.866  63.378  1.00108.54           C  
ATOM   2366  CD2 LEU A 977     -14.414   4.929  61.930  1.00109.36           C  
ATOM   2367  N   MET A 978     -10.962   7.413  58.867  1.00102.70           N  
ATOM   2368  CA  MET A 978     -10.504   8.315  57.817  1.00103.31           C  
ATOM   2369  C   MET A 978     -11.650   9.145  57.237  1.00106.84           C  
ATOM   2370  O   MET A 978     -12.444   8.661  56.414  1.00109.14           O  
ATOM   2371  CB  MET A 978      -9.778   7.537  56.713  0.00100.10           C  
ATOM   2372  CG  MET A 978      -8.293   7.385  56.958  0.00 98.27           C  
ATOM   2373  SD  MET A 978      -7.570   5.997  56.069  0.00 98.15           S  
ATOM   2374  CE  MET A 978      -7.350   6.699  54.437  0.00 96.91           C  
ATOM   2375  N   ASP A 979     -11.720  10.400  57.681  1.00106.02           N  
ATOM   2376  CA  ASP A 979     -12.744  11.335  57.231  1.00104.82           C  
ATOM   2377  C   ASP A 979     -12.565  11.582  55.749  1.00106.55           C  
ATOM   2378  O   ASP A 979     -13.533  11.544  54.977  1.00111.17           O  
ATOM   2379  CB  ASP A 979     -12.606  12.675  57.961  1.00100.55           C  
ATOM   2380  CG  ASP A 979     -12.518  12.517  59.463  1.00107.51           C  
ATOM   2381  OD1 ASP A 979     -13.409  13.052  60.162  1.00107.84           O  
ATOM   2382  OD2 ASP A 979     -11.546  11.879  59.938  1.00103.86           O  
ATOM   2383  N   GLU A 980     -11.314  11.834  55.363  1.00104.79           N  
ATOM   2384  CA  GLU A 980     -10.977  12.138  53.975  1.00104.15           C  
ATOM   2385  C   GLU A 980     -11.654  13.478  53.594  1.00107.13           C  
ATOM   2386  O   GLU A 980     -11.901  13.769  52.411  1.00105.70           O  
ATOM   2387  CB  GLU A 980     -11.416  10.988  53.045  1.00 95.70           C  
ATOM   2388  CG  GLU A 980     -10.265  10.243  52.348  1.00 86.65           C  
ATOM   2389  CD  GLU A 980      -9.884  10.848  50.990  1.00 99.25           C  
ATOM   2390  OE1 GLU A 980     -10.798  11.111  50.165  1.00 88.90           O  
ATOM   2391  OE2 GLU A 980      -8.668  11.043  50.740  1.00100.15           O  
ATOM   2392  N   GLU A 981     -11.939  14.284  54.623  1.00108.13           N  
ATOM   2393  CA  GLU A 981     -12.582  15.594  54.474  1.00109.23           C  
ATOM   2394  C   GLU A 981     -12.015  16.586  55.498  1.00109.07           C  
ATOM   2395  O   GLU A 981     -11.388  16.190  56.488  1.00110.13           O  
ATOM   2396  CB  GLU A 981     -14.106  15.483  54.675  1.00111.55           C  
ATOM   2397  CG  GLU A 981     -14.828  14.476  53.763  1.00108.91           C  
ATOM   2398  CD  GLU A 981     -14.838  14.889  52.290  1.00111.28           C  
ATOM   2399  OE1 GLU A 981     -15.248  16.034  51.989  1.00113.42           O  
ATOM   2400  OE2 GLU A 981     -14.446  14.063  51.434  1.00107.58           O  
ATOM   2401  N   ASP A 982     -12.282  17.872  55.273  1.00106.21           N  
ATOM   2402  CA  ASP A 982     -11.790  18.937  56.150  1.00101.89           C  
ATOM   2403  C   ASP A 982     -12.920  19.459  57.050  1.00101.15           C  
ATOM   2404  O   ASP A 982     -13.310  20.632  56.965  1.00 97.90           O  
ATOM   2405  CB  ASP A 982     -11.207  20.084  55.301  1.00100.37           C  
ATOM   2406  CG  ASP A 982     -10.352  19.582  54.120  1.00104.53           C  
ATOM   2407  OD1 ASP A 982      -9.101  19.526  54.251  1.00 92.22           O  
ATOM   2408  OD2 ASP A 982     -10.940  19.251  53.058  1.00 94.95           O  
ATOM   2409  N   MET A 983     -13.411  18.600  57.944  1.00100.30           N  
ATOM   2410  CA  MET A 983     -14.513  18.983  58.831  1.00 95.98           C  
ATOM   2411  C   MET A 983     -14.442  18.547  60.291  1.00 89.83           C  
ATOM   2412  O   MET A 983     -14.298  17.364  60.589  1.00 85.08           O  
ATOM   2413  CB  MET A 983     -15.836  18.509  58.233  1.00 93.83           C  
ATOM   2414  CG  MET A 983     -16.482  19.534  57.333  1.00 98.24           C  
ATOM   2415  SD  MET A 983     -16.887  21.091  58.209  1.00115.20           S  
ATOM   2416  CE  MET A 983     -17.448  20.486  59.827  1.00 75.13           C  
ATOM   2417  N   ASP A 984     -14.630  19.503  61.197  1.00 89.69           N  
ATOM   2418  CA  ASP A 984     -14.585  19.196  62.624  1.00 92.07           C  
ATOM   2419  C   ASP A 984     -15.917  19.307  63.369  1.00 88.52           C  
ATOM   2420  O   ASP A 984     -15.954  19.294  64.605  1.00 93.52           O  
ATOM   2421  CB  ASP A 984     -13.462  19.980  63.334  1.00101.91           C  
ATOM   2422  CG  ASP A 984     -13.486  21.471  63.026  1.00100.65           C  
ATOM   2423  OD1 ASP A 984     -13.756  22.263  63.962  1.00 92.14           O  
ATOM   2424  OD2 ASP A 984     -13.217  21.845  61.858  1.00 96.89           O  
ATOM   2425  N   ASP A 985     -17.003  19.442  62.612  1.00 80.70           N  
ATOM   2426  CA  ASP A 985     -18.350  19.482  63.184  1.00 73.66           C  
ATOM   2427  C   ASP A 985     -19.064  18.162  62.828  1.00 66.19           C  
ATOM   2428  O   ASP A 985     -20.287  18.042  62.888  1.00 57.52           O  
ATOM   2429  CB  ASP A 985     -19.144  20.697  62.689  1.00 80.53           C  
ATOM   2430  CG  ASP A 985     -18.979  21.918  63.593  1.00 85.08           C  
ATOM   2431  OD1 ASP A 985     -19.469  21.897  64.742  1.00 84.24           O  
ATOM   2432  OD2 ASP A 985     -18.365  22.911  63.149  1.00113.46           O  
ATOM   2433  N   VAL A 986     -18.270  17.171  62.444  1.00 60.54           N  
ATOM   2434  CA  VAL A 986     -18.783  15.857  62.110  1.00 61.25           C  
ATOM   2435  C   VAL A 986     -19.165  15.143  63.404  1.00 63.60           C  
ATOM   2436  O   VAL A 986     -18.457  15.231  64.413  1.00 68.55           O  
ATOM   2437  CB  VAL A 986     -17.728  15.022  61.328  1.00 56.02           C  
ATOM   2438  CG1 VAL A 986     -16.358  15.187  61.944  1.00 72.01           C  
ATOM   2439  CG2 VAL A 986     -18.114  13.549  61.314  1.00 56.88           C  
ATOM   2440  N   VAL A 987     -20.316  14.485  63.389  1.00 57.43           N  
ATOM   2441  CA  VAL A 987     -20.781  13.749  64.551  1.00 57.07           C  
ATOM   2442  C   VAL A 987     -21.338  12.423  64.059  1.00 49.36           C  
ATOM   2443  O   VAL A 987     -21.979  12.352  63.029  1.00 50.06           O  
ATOM   2444  CB  VAL A 987     -21.826  14.558  65.384  1.00 62.51           C  
ATOM   2445  CG1 VAL A 987     -23.176  14.602  64.699  1.00 72.99           C  
ATOM   2446  CG2 VAL A 987     -21.950  13.973  66.764  1.00 68.30           C  
ATOM   2447  N   ASP A 988     -21.030  11.357  64.768  1.00 51.01           N  
ATOM   2448  CA  ASP A 988     -21.487  10.043  64.369  1.00 51.26           C  
ATOM   2449  C   ASP A 988     -22.997   9.890  64.579  1.00 51.75           C  
ATOM   2450  O   ASP A 988     -23.565  10.436  65.525  1.00 38.97           O  
ATOM   2451  CB  ASP A 988     -20.704   8.991  65.148  1.00 64.52           C  
ATOM   2452  CG  ASP A 988     -20.941   7.601  64.643  1.00 72.88           C  
ATOM   2453  OD1 ASP A 988     -22.008   7.045  64.958  1.00 73.00           O  
ATOM   2454  OD2 ASP A 988     -20.065   7.065  63.934  1.00 79.97           O  
ATOM   2455  N   ALA A 989     -23.641   9.147  63.682  1.00 53.68           N  
ATOM   2456  CA  ALA A 989     -25.078   8.923  63.748  1.00 54.78           C  
ATOM   2457  C   ALA A 989     -25.592   8.400  65.086  1.00 53.06           C  
ATOM   2458  O   ALA A 989     -26.638   8.838  65.550  1.00 40.10           O  
ATOM   2459  CB  ALA A 989     -25.523   8.009  62.625  1.00 71.08           C  
ATOM   2460  N   ASP A 990     -24.909   7.451  65.714  1.00 56.09           N  
ATOM   2461  CA  ASP A 990     -25.451   7.012  66.988  1.00 65.16           C  
ATOM   2462  C   ASP A 990     -25.320   7.992  68.161  1.00 65.80           C  
ATOM   2463  O   ASP A 990     -25.670   7.672  69.293  1.00 75.94           O  
ATOM   2464  CB  ASP A 990     -25.102   5.557  67.342  1.00 65.84           C  
ATOM   2465  CG  ASP A 990     -23.709   5.159  66.952  1.00 83.21           C  
ATOM   2466  OD1 ASP A 990     -22.766   5.908  67.269  1.00105.89           O  
ATOM   2467  OD2 ASP A 990     -23.555   4.061  66.372  1.00 50.58           O  
ATOM   2468  N   GLU A 991     -24.898   9.218  67.854  1.00 68.05           N  
ATOM   2469  CA  GLU A 991     -24.777  10.297  68.836  1.00 61.35           C  
ATOM   2470  C   GLU A 991     -25.731  11.436  68.462  1.00 63.63           C  
ATOM   2471  O   GLU A 991     -25.868  12.407  69.196  1.00 70.81           O  
ATOM   2472  CB  GLU A 991     -23.355  10.840  68.920  1.00 69.24           C  
ATOM   2473  CG  GLU A 991     -22.473  10.174  69.951  1.00 75.90           C  
ATOM   2474  CD  GLU A 991     -21.844   8.900  69.449  1.00 87.85           C  
ATOM   2475  OE1 GLU A 991     -22.203   7.816  69.952  1.00 86.52           O  
ATOM   2476  OE2 GLU A 991     -20.981   8.983  68.553  1.00101.63           O  
ATOM   2477  N   TYR A 992     -26.373  11.323  67.303  1.00 64.88           N  
ATOM   2478  CA  TYR A 992     -27.326  12.326  66.853  1.00 66.42           C  
ATOM   2479  C   TYR A 992     -28.730  11.752  67.046  1.00 71.04           C  
ATOM   2480  O   TYR A 992     -29.200  10.939  66.238  1.00 72.58           O  
ATOM   2481  CB  TYR A 992     -27.088  12.685  65.388  1.00 59.44           C  
ATOM   2482  CG  TYR A 992     -27.873  13.890  64.961  1.00 51.29           C  
ATOM   2483  CD1 TYR A 992     -29.020  13.766  64.189  1.00 48.15           C  
ATOM   2484  CD2 TYR A 992     -27.513  15.150  65.402  1.00 67.10           C  
ATOM   2485  CE1 TYR A 992     -29.792  14.874  63.881  1.00 59.76           C  
ATOM   2486  CE2 TYR A 992     -28.275  16.264  65.099  1.00 68.08           C  
ATOM   2487  CZ  TYR A 992     -29.411  16.123  64.345  1.00 57.75           C  
ATOM   2488  OH  TYR A 992     -30.170  17.240  64.079  1.00 84.13           O  
ATOM   2489  N   LEU A 993     -29.392  12.186  68.119  1.00 76.45           N  
ATOM   2490  CA  LEU A 993     -30.731  11.698  68.469  1.00 77.52           C  
ATOM   2491  C   LEU A 993     -31.900  12.635  68.142  1.00 81.92           C  
ATOM   2492  O   LEU A 993     -31.709  13.828  67.872  1.00 80.06           O  
ATOM   2493  CB  LEU A 993     -30.756  11.271  69.945  1.00 70.42           C  
ATOM   2494  CG  LEU A 993     -29.680  10.238  70.327  1.00 72.50           C  
ATOM   2495  CD1 LEU A 993     -29.626  10.037  71.805  1.00 68.90           C  
ATOM   2496  CD2 LEU A 993     -29.940   8.920  69.632  1.00 76.90           C  
ATOM   2497  N   ILE A 994     -33.105  12.061  68.191  1.00 88.40           N  
ATOM   2498  CA  ILE A 994     -34.387  12.712  67.878  1.00 89.65           C  
ATOM   2499  C   ILE A 994     -34.482  14.259  67.897  1.00 97.21           C  
ATOM   2500  O   ILE A 994     -34.504  14.892  68.960  1.00104.38           O  
ATOM   2501  CB  ILE A 994     -35.581  12.038  68.674  0.00 85.68           C  
ATOM   2502  CG1 ILE A 994     -35.951  12.802  69.950  0.00 82.73           C  
ATOM   2503  CG2 ILE A 994     -35.222  10.605  69.055  0.00 78.46           C  
ATOM   2504  CD1 ILE A 994     -37.197  13.669  69.803  0.00 89.21           C  
ATOM   2505  N   PRO A 995     -34.413  14.890  66.708  1.00 96.35           N  
ATOM   2506  CA  PRO A 995     -34.506  16.354  66.608  1.00 96.33           C  
ATOM   2507  C   PRO A 995     -35.968  16.813  66.584  1.00 96.89           C  
ATOM   2508  O   PRO A 995     -36.887  16.005  66.390  1.00 98.69           O  
ATOM   2509  CB  PRO A 995     -33.814  16.651  65.275  1.00 97.60           C  
ATOM   2510  CG  PRO A 995     -34.154  15.455  64.454  1.00 95.62           C  
ATOM   2511  CD  PRO A 995     -33.927  14.315  65.439  1.00 98.63           C  
TER    2512      PRO A 995                                                      
HETATM 2513  C1  AQ4 A 999      29.552  -1.989  53.496  1.00 82.82           C  
HETATM 2514  C2  AQ4 A 999      28.841  -1.022  53.432  1.00 79.21           C  
HETATM 2515  C3  AQ4 A 999      27.989   0.094  53.366  1.00 77.10           C  
HETATM 2516  C4  AQ4 A 999      26.606  -0.119  53.323  1.00 78.64           C  
HETATM 2517  C5  AQ4 A 999      25.725   0.972  53.258  1.00 75.72           C  
HETATM 2518  N1  AQ4 A 999      24.289   0.712  53.215  1.00 63.33           N  
HETATM 2519  C6  AQ4 A 999      23.410  -0.217  53.908  1.00 56.92           C  
HETATM 2520  C7  AQ4 A 999      22.037  -0.309  53.572  1.00 52.23           C  
HETATM 2521  C8  AQ4 A 999      21.501   0.476  52.546  1.00 48.18           C  
HETATM 2522  C9  AQ4 A 999      20.143   0.376  52.218  1.00 52.11           C  
HETATM 2523  O1  AQ4 A 999      19.589   1.220  51.120  1.00 82.48           O  
HETATM 2524  C10 AQ4 A 999      20.550   1.362  50.041  1.00 83.98           C  
HETATM 2525  C11 AQ4 A 999      20.235   2.645  49.262  1.00 91.80           C  
HETATM 2526  O2  AQ4 A 999      18.990   2.485  48.543  1.00 96.57           O  
HETATM 2527  C12 AQ4 A 999      17.712   2.618  49.399  1.00 88.53           C  
HETATM 2528  C13 AQ4 A 999      19.301  -0.535  52.923  1.00 52.73           C  
HETATM 2529  O3  AQ4 A 999      17.828  -0.679  52.597  1.00 83.95           O  
HETATM 2530  C14 AQ4 A 999      17.227   0.601  52.220  1.00 98.66           C  
HETATM 2531  C15 AQ4 A 999      15.703   0.494  52.066  1.00102.19           C  
HETATM 2532  O4  AQ4 A 999      15.108   0.167  53.335  1.00 79.31           O  
HETATM 2533  C16 AQ4 A 999      13.843  -0.695  53.221  1.00 92.17           C  
HETATM 2534  C17 AQ4 A 999      19.845  -1.318  53.942  1.00 59.83           C  
HETATM 2535  C18 AQ4 A 999      21.199  -1.222  54.264  1.00 53.51           C  
HETATM 2536  N2  AQ4 A 999      21.747  -2.039  55.319  1.00 50.53           N  
HETATM 2537  C19 AQ4 A 999      23.117  -1.934  55.642  1.00 65.28           C  
HETATM 2538  N3  AQ4 A 999      23.943  -1.023  54.940  1.00 44.57           N  
HETATM 2539  C20 AQ4 A 999      26.234   2.292  53.236  1.00 77.38           C  
HETATM 2540  C21 AQ4 A 999      27.625   2.509  53.279  1.00 70.00           C  
HETATM 2541  C22 AQ4 A 999      28.508   1.410  53.344  1.00 71.32           C  
HETATM 2542  O   HOH A   1      32.732  20.638  57.020  1.00 49.98           O  
HETATM 2543  O   HOH A   2      32.882   9.700  55.317  1.00 47.81           O  
HETATM 2544  O   HOH A   3      27.504  -1.066  65.946  1.00 58.30           O  
HETATM 2545  O   HOH A   4      25.698  20.050  48.908  1.00 59.48           O  
HETATM 2546  O   HOH A   5      23.562  36.184  60.778  1.00 53.83           O  
HETATM 2547  O   HOH A   6      33.892  18.248  58.731  1.00 38.37           O  
HETATM 2548  O   HOH A   7      10.334  25.073  74.952  1.00 39.68           O  
HETATM 2549  O   HOH A   8      27.903  24.827  53.992  1.00 43.63           O  
HETATM 2550  O   HOH A   9      18.941  -2.491  68.885  1.00 52.41           O  
HETATM 2551  O   HOH A  10      25.979  -0.494  56.755  1.00 80.23           O  
HETATM 2552  O   HOH A  11      28.366  -5.361  64.274  1.00 82.86           O  
HETATM 2553  O   HOH A  12      22.492  -8.282  61.348  1.00 38.44           O  
HETATM 2554  O   HOH A  13      13.333  18.933  80.447  1.00 54.89           O  
HETATM 2555  O   HOH A  14      25.457  24.140  55.088  1.00 50.80           O  
HETATM 2556  O   HOH A  15      18.280  33.231  57.782  1.00 78.01           O  
HETATM 2557  O   HOH A  16      30.582  -0.221  65.350  1.00 40.66           O  
HETATM 2558  O   HOH A  17      32.987  24.038  72.100  1.00 63.73           O  
HETATM 2559  O   HOH A  18       9.251  21.560  60.778  1.00 45.40           O  
HETATM 2560  O   HOH A  19     -21.187   4.756  70.193  1.00 66.85           O  
HETATM 2561  O   HOH A  20      18.877  25.444  74.214  1.00 60.04           O  
CONECT 2513 2514                                                                
CONECT 2514 2513 2515                                                           
CONECT 2515 2514 2516 2541                                                      
CONECT 2516 2515 2517                                                           
CONECT 2517 2516 2518 2539                                                      
CONECT 2518 2517 2519                                                           
CONECT 2519 2518 2520 2538                                                      
CONECT 2520 2519 2521 2535                                                      
CONECT 2521 2520 2522                                                           
CONECT 2522 2521 2523 2528                                                      
CONECT 2523 2522 2524                                                           
CONECT 2524 2523 2525                                                           
CONECT 2525 2524 2526                                                           
CONECT 2526 2525 2527                                                           
CONECT 2527 2526                                                                
CONECT 2528 2522 2529 2534                                                      
CONECT 2529 2528 2530                                                           
CONECT 2530 2529 2531                                                           
CONECT 2531 2530 2532                                                           
CONECT 2532 2531 2533                                                           
CONECT 2533 2532                                                                
CONECT 2534 2528 2535                                                           
CONECT 2535 2520 2534 2536                                                      
CONECT 2536 2535 2537                                                           
CONECT 2537 2536 2538                                                           
CONECT 2538 2519 2537                                                           
CONECT 2539 2517 2540                                                           
CONECT 2540 2539 2541                                                           
CONECT 2541 2515 2540                                                           
MASTER      397    0    1   15   11    0    4    6 2560    1   29   26          
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.