CNRS Nantes University UFIP UFIP
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***  TRANSFERASE 27-OCT-11 3VJO  ***

elNémo ID: 21081010344211316

Job options:

ID        	=	 21081010344211316
JOBID     	=	 TRANSFERASE 27-OCT-11 3VJO
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSFERASE                             27-OCT-11   3VJO              
TITLE     CRYSTAL STRUCTURE OF THE WILD-TYPE EGFR KINASE DOMAIN IN COMPLEX WITH 
TITLE    2 AMPPNP.                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN (UNP RESIDUES 695-1022);                     
COMPND   5 EC: 2.7.10.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EGFR, ERBB1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC_HT_C                             
KEYWDS    RECEPTOR, DISEASE MUTATION, CELL CYCLE, DRUG RESISTANCE, KINASE,      
KEYWDS   2 TYROSINE-PROTEIN KINASE, TRANSFERASE, ATP BINDING, PHOSPHORYLATION,  
KEYWDS   3 TRANSMEMBRANE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.YOSHIKAWA,M.KUKIMOTO-NIINO,M.SHIROUZU,K.SEMBA,T.YAMAMOTO,S.YOKOYAMA 
REVDAT   2   26-JUN-13 3VJO    1       JRNL                                     
REVDAT   1   07-MAR-12 3VJO    0                                                
JRNL        AUTH   S.YOSHIKAWA,M.KUKIMOTO-NIINO,L.PARKER,N.HANDA,T.TERADA,      
JRNL        AUTH 2 T.FUJIMOTO,Y.TERAZAWA,M.WAKIYAMA,M.SATO,S.SANO,T.KOBAYASHI,  
JRNL        AUTH 3 T.TANAKA,L.CHEN,Z.J.LIU,B.C.WANG,M.SHIROUZU,S.KAWA,K.SEMBA,  
JRNL        AUTH 4 T.YAMAMOTO,S.YOKOYAMA                                        
JRNL        TITL   STRUCTURAL BASIS FOR THE ALTERED DRUG SENSITIVITIES OF       
JRNL        TITL 2 NON-SMALL CELL LUNG CANCER-ASSOCIATED MUTANTS OF HUMAN       
JRNL        TITL 3 EPIDERMAL GROWTH FACTOR RECEPTOR.                            
JRNL        REF    ONCOGENE                      V.  32    27 2013              
JRNL        REFN                   ISSN 0950-9232                               
JRNL        PMID   22349823                                                     
JRNL        DOI    10.1038/ONC.2012.21                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.64 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.64                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2304433.510                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 14505                          
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) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.200                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1473                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.64                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.81                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2113                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2890                       
REMARK   3   BIN FREE R VALUE                    : 0.3400                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.60                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 250                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2382                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 9                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 66.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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) : 0.30                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.30                            
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) : 0.38                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.41                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.80                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.05                            
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) : 6.810 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 9.190 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 10.220; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 12.340; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 53.10                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ANP.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ANP.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3VJO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-NOV-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB095128.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-AUG-07                          
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               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9786                             
REMARK 200  MONOCHROMATOR                  : LN2 COOLED FIXED-EXIT SI(111)      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14516                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.640                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 71.610                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.669                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04200                            
REMARK 200   FOR THE DATA SET  : 30.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.64                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.91                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.20800                            
REMARK 200   FOR SHELL         : 6.470                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2GS2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL(PH 7.0), 0.2M NACL, 1M     
REMARK 280  SODIUM CITRATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K     
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       71.68000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       71.68000            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       71.68000            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       71.68000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       71.68000            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       71.68000            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       71.68000            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       71.68000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       71.68000            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       71.68000            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       71.68000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       71.68000            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       71.68000            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       71.68000            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       71.68000            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       71.68000            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       71.68000            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       71.68000            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       71.68000            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       71.68000            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       71.68000            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       71.68000            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       71.68000            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       71.68000            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       71.68000            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       71.68000            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       71.68000            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       71.68000            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       71.68000            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       71.68000            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       71.68000            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       71.68000            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       71.68000            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       71.68000            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       71.68000            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       71.68000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      143.36000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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   689                                                      
REMARK 465     ALA A   690                                                      
REMARK 465     MET A   691                                                      
REMARK 465     GLY A   692                                                      
REMARK 465     ILE A   693                                                      
REMARK 465     ARG A   694                                                      
REMARK 465     SER A   695                                                      
REMARK 465     GLY A   721                                                      
REMARK 465     ALA A   722                                                      
REMARK 465     LEU A   747                                                      
REMARK 465     ARG A   748                                                      
REMARK 465     GLU A   749                                                      
REMARK 465     ARG A   986                                                      
REMARK 465     MET A   987                                                      
REMARK 465     HIS A   988                                                      
REMARK 465     LEU A   989                                                      
REMARK 465     PRO A   990                                                      
REMARK 465     SER A   991                                                      
REMARK 465     PRO A   992                                                      
REMARK 465     THR A   993                                                      
REMARK 465     ASP A   994                                                      
REMARK 465     SER A   995                                                      
REMARK 465     ASN A   996                                                      
REMARK 465     PHE A   997                                                      
REMARK 465     TYR A   998                                                      
REMARK 465     ARG A   999                                                      
REMARK 465     ALA A  1000                                                      
REMARK 465     LEU A  1001                                                      
REMARK 465     MET A  1002                                                      
REMARK 465     ASP A  1003                                                      
REMARK 465     GLU A  1004                                                      
REMARK 465     GLU A  1005                                                      
REMARK 465     PRO A  1019                                                      
REMARK 465     GLN A  1020                                                      
REMARK 465     GLN A  1021                                                      
REMARK 465     GLY A  1022                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A   736     OH   TYR A  1016              1.84            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    THR A 725      130.12   -176.86                                   
REMARK 500    LEU A 782       55.24    -94.40                                   
REMARK 500    ARG A 831       20.06    -78.95                                   
REMARK 500    ASP A 837       38.45   -148.08                                   
REMARK 500    ASP A 855       77.02     56.51                                   
REMARK 500    MET A1007       34.53   -155.95                                   
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 ANP A 2001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2EB2   RELATED DB: PDB                                   
REMARK 900 MUTATED EGFR KINASE DOMAIN(G719S)                                    
REMARK 900 RELATED ID: 2EB3   RELATED DB: PDB                                   
REMARK 900 MUTATED EGFR KINASE DOMAIN (L858R) IN COMPLEX WITH AMPPNP            
REMARK 900 RELATED ID: 3VJN   RELATED DB: PDB                                   
REMARK 900 MUTATED EGFR KINASE DOMAIN (G719S/T790M) IN COMPLEX WITH             
REMARK 900 AMPPNP                                                               
REMARK 900 RELATED ID: 3UG1   RELATED DB: PDB                                   
REMARK 900 MUTATED EGFR KINASE DOMAIN (G719S/T790M) IN THE APO FORM             
REMARK 900 RELATED ID: 3UG2   RELATED DB: PDB                                   
REMARK 900 MUTATED EGFR KINASE DOMAIN (G719S/T790M) IN COMPLEX WITH             
REMARK 900 GEFITINIB                                                            
DBREF  3VJO A  695  1022  UNP    P00533   EGFR_HUMAN     695   1022             
SEQADV 3VJO GLY A  689  UNP  P00533              EXPRESSION TAG                 
SEQADV 3VJO ALA A  690  UNP  P00533              EXPRESSION TAG                 
SEQADV 3VJO MET A  691  UNP  P00533              EXPRESSION TAG                 
SEQADV 3VJO GLY A  692  UNP  P00533              EXPRESSION TAG                 
SEQADV 3VJO ILE A  693  UNP  P00533              EXPRESSION TAG                 
SEQADV 3VJO ARG A  694  UNP  P00533              EXPRESSION TAG                 
SEQRES   1 A  334  GLY ALA MET GLY ILE ARG SER GLY GLU ALA PRO ASN GLN          
SEQRES   2 A  334  ALA LEU LEU ARG ILE LEU LYS GLU THR GLU PHE LYS LYS          
SEQRES   3 A  334  ILE LYS VAL LEU GLY SER GLY ALA PHE GLY THR VAL TYR          
SEQRES   4 A  334  LYS GLY LEU TRP ILE PRO GLU GLY GLU LYS VAL LYS ILE          
SEQRES   5 A  334  PRO VAL ALA ILE LYS GLU LEU ARG GLU ALA THR SER PRO          
SEQRES   6 A  334  LYS ALA ASN LYS GLU ILE LEU ASP GLU ALA TYR VAL MET          
SEQRES   7 A  334  ALA SER VAL ASP ASN PRO HIS VAL CYS ARG LEU LEU GLY          
SEQRES   8 A  334  ILE CYS LEU THR SER THR VAL GLN LEU ILE THR GLN LEU          
SEQRES   9 A  334  MET PRO PHE GLY CYS LEU LEU ASP TYR VAL ARG GLU HIS          
SEQRES  10 A  334  LYS ASP ASN ILE GLY SER GLN TYR LEU LEU ASN TRP CYS          
SEQRES  11 A  334  VAL GLN ILE ALA LYS GLY MET ASN TYR LEU GLU ASP ARG          
SEQRES  12 A  334  ARG LEU VAL HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU          
SEQRES  13 A  334  VAL LYS THR PRO GLN HIS VAL LYS ILE THR ASP PHE GLY          
SEQRES  14 A  334  LEU ALA LYS LEU LEU GLY ALA GLU GLU LYS GLU TYR HIS          
SEQRES  15 A  334  ALA GLU GLY GLY LYS VAL PRO ILE LYS TRP MET ALA LEU          
SEQRES  16 A  334  GLU SER ILE LEU HIS ARG ILE TYR THR HIS GLN SER ASP          
SEQRES  17 A  334  VAL TRP SER TYR GLY VAL THR VAL TRP GLU LEU MET THR          
SEQRES  18 A  334  PHE GLY SER LYS PRO TYR ASP GLY ILE PRO ALA SER GLU          
SEQRES  19 A  334  ILE SER SER ILE LEU GLU LYS GLY GLU ARG LEU PRO GLN          
SEQRES  20 A  334  PRO PRO ILE CYS THR ILE ASP VAL TYR MET ILE MET VAL          
SEQRES  21 A  334  LYS CYS TRP MET ILE ASP ALA ASP SER ARG PRO LYS PHE          
SEQRES  22 A  334  ARG GLU LEU ILE ILE GLU PHE SER LYS MET ALA ARG ASP          
SEQRES  23 A  334  PRO GLN ARG TYR LEU VAL ILE GLN GLY ASP GLU ARG MET          
SEQRES  24 A  334  HIS LEU PRO SER PRO THR ASP SER ASN PHE TYR ARG ALA          
SEQRES  25 A  334  LEU MET ASP GLU GLU ASP MET ASP ASP VAL VAL ASP ALA          
SEQRES  26 A  334  ASP GLU TYR LEU ILE PRO GLN GLN GLY                          
HET    ANP  A2001      31                                                       
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
FORMUL   2  ANP    C10 H17 N6 O12 P3                                            
FORMUL   3  HOH   *9(H2 O)                                                      
HELIX    1   1 LYS A  708  THR A  710  5                                   3    
HELIX    2   2 SER A  752  SER A  768  1                                  17    
HELIX    3   3 CYS A  797  LYS A  806  1                                  10    
HELIX    4   4 ASP A  807  ILE A  809  5                                   3    
HELIX    5   5 GLY A  810  ARG A  831  1                                  22    
HELIX    6   6 ALA A  839  ARG A  841  5                                   3    
HELIX    7   7 PRO A  877  MET A  881  5                                   5    
HELIX    8   8 ALA A  882  ARG A  889  1                                   8    
HELIX    9   9 THR A  892  THR A  909  1                                  18    
HELIX   10  10 PRO A  919  LYS A  929  1                                  11    
HELIX   11  11 THR A  940  TRP A  951  1                                  12    
HELIX   12  12 ASP A  954  ARG A  958  5                                   5    
HELIX   13  13 LYS A  960  ASP A  974  1                                  15    
HELIX   14  14 ASP A  974  LEU A  979  1                                   6    
HELIX   15  15 ASP A 1012  TYR A 1016  5                                   5    
SHEET    1   A 5 PHE A 712  GLY A 719  0                                        
SHEET    2   A 5 VAL A 726  TRP A 731 -1  O  VAL A 726   N  LEU A 718           
SHEET    3   A 5 ILE A 740  LYS A 745 -1  O  ILE A 744   N  TYR A 727           
SHEET    4   A 5 VAL A 786  GLN A 791 -1  O  THR A 790   N  ALA A 743           
SHEET    5   A 5 LEU A 777  LEU A 782 -1  N  GLY A 779   O  ILE A 789           
SHEET    1   B 2 LEU A 833  VAL A 834  0                                        
SHEET    2   B 2 LYS A 860  LEU A 861 -1  O  LYS A 860   N  VAL A 834           
SHEET    1   C 2 VAL A 843  THR A 847  0                                        
SHEET    2   C 2 HIS A 850  ILE A 853 -1  O  LYS A 852   N  LEU A 844           
SHEET    1   D 2 TYR A 869  HIS A 870  0                                        
SHEET    2   D 2 ILE A 890  TYR A 891 -1  O  TYR A 891   N  TYR A 869           
SITE     1 AC1  6 PHE A 723  ALA A 743  LYS A 745  THR A 790                    
SITE     2 AC1  6 GLN A 791  MET A 793                                          
CRYST1  143.360  143.360  143.360  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      0.006975  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006975  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006975        0.00000                         
ATOM      1  N   GLY A 696      67.955   7.275 -52.345  1.00 92.82           N  
ATOM      2  CA  GLY A 696      66.785   7.747 -51.535  1.00103.30           C  
ATOM      3  C   GLY A 696      67.116   7.759 -50.055  1.00106.71           C  
ATOM      4  O   GLY A 696      67.345   8.814 -49.473  1.00116.34           O  
ATOM      5  N   GLU A 697      67.121   6.577 -49.446  1.00102.47           N  
ATOM      6  CA  GLU A 697      67.463   6.410 -48.035  1.00 92.66           C  
ATOM      7  C   GLU A 697      67.653   4.907 -47.802  1.00 82.30           C  
ATOM      8  O   GLU A 697      67.400   4.109 -48.710  1.00 75.59           O  
ATOM      9  CB  GLU A 697      66.373   6.994 -47.121  1.00 97.05           C  
ATOM     10  CG  GLU A 697      66.816   7.184 -45.652  1.00109.54           C  
ATOM     11  CD  GLU A 697      68.204   7.826 -45.501  1.00116.67           C  
ATOM     12  OE1 GLU A 697      68.732   8.391 -46.485  1.00112.28           O  
ATOM     13  OE2 GLU A 697      68.767   7.772 -44.384  1.00115.87           O  
ATOM     14  N   ALA A 698      68.110   4.522 -46.609  1.00 67.10           N  
ATOM     15  CA  ALA A 698      68.359   3.111 -46.301  1.00 51.69           C  
ATOM     16  C   ALA A 698      67.102   2.245 -46.236  1.00 55.22           C  
ATOM     17  O   ALA A 698      66.027   2.716 -45.859  1.00 50.19           O  
ATOM     18  CB  ALA A 698      69.126   2.990 -44.995  1.00 32.20           C  
ATOM     19  N   PRO A 699      67.233   0.961 -46.623  1.00 54.52           N  
ATOM     20  CA  PRO A 699      66.193  -0.080 -46.654  1.00 49.49           C  
ATOM     21  C   PRO A 699      65.832  -0.515 -45.244  1.00 55.88           C  
ATOM     22  O   PRO A 699      66.704  -0.996 -44.514  1.00 55.70           O  
ATOM     23  CB  PRO A 699      66.857  -1.229 -47.410  1.00 48.50           C  
ATOM     24  CG  PRO A 699      67.916  -0.561 -48.242  1.00 33.75           C  
ATOM     25  CD  PRO A 699      68.449   0.505 -47.321  1.00 54.92           C  
ATOM     26  N   ASN A 700      64.561  -0.363 -44.864  1.00 50.00           N  
ATOM     27  CA  ASN A 700      64.146  -0.759 -43.527  1.00 26.95           C  
ATOM     28  C   ASN A 700      64.001  -2.257 -43.468  1.00 39.41           C  
ATOM     29  O   ASN A 700      62.953  -2.800 -43.795  1.00 45.82           O  
ATOM     30  CB  ASN A 700      62.833  -0.110 -43.159  1.00 32.53           C  
ATOM     31  CG  ASN A 700      62.403  -0.449 -41.766  1.00 41.39           C  
ATOM     32  OD1 ASN A 700      63.021  -1.295 -41.098  1.00 38.82           O  
ATOM     33  ND2 ASN A 700      61.332   0.199 -41.307  1.00 41.56           N  
ATOM     34  N   GLN A 701      65.065  -2.930 -43.051  1.00 44.69           N  
ATOM     35  CA  GLN A 701      65.048  -4.379 -42.984  1.00 46.37           C  
ATOM     36  C   GLN A 701      64.620  -4.918 -41.642  1.00 46.58           C  
ATOM     37  O   GLN A 701      64.962  -6.051 -41.283  1.00 52.43           O  
ATOM     38  CB  GLN A 701      66.413  -4.948 -43.343  1.00 28.92           C  
ATOM     39  CG  GLN A 701      66.889  -4.525 -44.707  1.00 54.72           C  
ATOM     40  CD  GLN A 701      68.130  -5.272 -45.130  1.00 52.70           C  
ATOM     41  OE1 GLN A 701      68.093  -6.486 -45.354  1.00 58.16           O  
ATOM     42  NE2 GLN A 701      69.241  -4.554 -45.235  1.00 54.75           N  
ATOM     43  N   ALA A 702      63.873  -4.117 -40.896  1.00 29.65           N  
ATOM     44  CA  ALA A 702      63.400  -4.594 -39.603  1.00 49.31           C  
ATOM     45  C   ALA A 702      62.569  -5.875 -39.858  1.00 48.70           C  
ATOM     46  O   ALA A 702      62.150  -6.140 -40.988  1.00 52.56           O  
ATOM     47  CB  ALA A 702      62.554  -3.508 -38.919  1.00 35.24           C  
ATOM     48  N   LEU A 703      62.351  -6.668 -38.821  1.00 48.74           N  
ATOM     49  CA  LEU A 703      61.587  -7.911 -38.941  1.00 47.81           C  
ATOM     50  C   LEU A 703      60.264  -7.814 -38.191  1.00 46.27           C  
ATOM     51  O   LEU A 703      60.252  -7.439 -37.018  1.00 53.55           O  
ATOM     52  CB  LEU A 703      62.389  -9.069 -38.355  1.00 33.32           C  
ATOM     53  CG  LEU A 703      62.986 -10.142 -39.255  1.00 55.91           C  
ATOM     54  CD1 LEU A 703      63.557  -9.519 -40.502  1.00 42.27           C  
ATOM     55  CD2 LEU A 703      64.045 -10.908 -38.479  1.00 39.79           C  
ATOM     56  N   LEU A 704      59.158  -8.137 -38.862  1.00 47.89           N  
ATOM     57  CA  LEU A 704      57.832  -8.113 -38.228  1.00 42.18           C  
ATOM     58  C   LEU A 704      57.546  -9.554 -37.859  1.00 45.48           C  
ATOM     59  O   LEU A 704      57.462 -10.418 -38.724  1.00 51.43           O  
ATOM     60  CB  LEU A 704      56.761  -7.648 -39.199  1.00 38.33           C  
ATOM     61  CG  LEU A 704      55.615  -6.767 -38.694  1.00 54.97           C  
ATOM     62  CD1 LEU A 704      54.440  -6.917 -39.655  1.00 47.83           C  
ATOM     63  CD2 LEU A 704      55.196  -7.158 -37.297  1.00 40.95           C  
ATOM     64  N   ARG A 705      57.412  -9.826 -36.576  1.00 43.60           N  
ATOM     65  CA  ARG A 705      57.165 -11.183 -36.160  1.00 35.18           C  
ATOM     66  C   ARG A 705      55.670 -11.420 -35.967  1.00 41.42           C  
ATOM     67  O   ARG A 705      54.994 -10.642 -35.297  1.00 42.65           O  
ATOM     68  CB  ARG A 705      57.923 -11.447 -34.879  1.00 34.10           C  
ATOM     69  CG  ARG A 705      57.772 -12.839 -34.346  1.00 63.36           C  
ATOM     70  CD  ARG A 705      58.895 -13.165 -33.368  1.00 80.77           C  
ATOM     71  NE  ARG A 705      58.725 -14.494 -32.792  1.00 92.66           N  
ATOM     72  CZ  ARG A 705      59.682 -15.181 -32.172  1.00 96.23           C  
ATOM     73  NH1 ARG A 705      60.902 -14.678 -32.037  1.00 90.46           N  
ATOM     74  NH2 ARG A 705      59.417 -16.385 -31.685  1.00 97.40           N  
ATOM     75  N   ILE A 706      55.146 -12.478 -36.581  1.00 38.82           N  
ATOM     76  CA  ILE A 706      53.734 -12.790 -36.436  1.00 43.72           C  
ATOM     77  C   ILE A 706      53.602 -13.905 -35.416  1.00 41.80           C  
ATOM     78  O   ILE A 706      54.155 -14.992 -35.599  1.00 39.79           O  
ATOM     79  CB  ILE A 706      53.116 -13.240 -37.763  1.00 56.54           C  
ATOM     80  CG1 ILE A 706      53.427 -12.208 -38.851  1.00 52.39           C  
ATOM     81  CG2 ILE A 706      51.613 -13.430 -37.587  1.00 54.20           C  
ATOM     82  CD1 ILE A 706      52.223 -11.597 -39.494  1.00 48.65           C  
ATOM     83  N   LEU A 707      52.873 -13.618 -34.338  1.00 35.20           N  
ATOM     84  CA  LEU A 707      52.673 -14.557 -33.235  1.00 46.67           C  
ATOM     85  C   LEU A 707      51.397 -15.371 -33.255  1.00 51.23           C  
ATOM     86  O   LEU A 707      50.317 -14.855 -33.564  1.00 52.03           O  
ATOM     87  CB  LEU A 707      52.701 -13.800 -31.916  1.00 56.84           C  
ATOM     88  CG  LEU A 707      54.038 -13.332 -31.350  1.00 68.99           C  
ATOM     89  CD1 LEU A 707      55.120 -13.291 -32.409  1.00 69.04           C  
ATOM     90  CD2 LEU A 707      53.825 -11.981 -30.739  1.00 59.06           C  
ATOM     91  N   LYS A 708      51.530 -16.645 -32.904  1.00 51.73           N  
ATOM     92  CA  LYS A 708      50.380 -17.543 -32.817  1.00 56.26           C  
ATOM     93  C   LYS A 708      49.657 -17.278 -31.498  1.00 54.31           C  
ATOM     94  O   LYS A 708      50.294 -17.165 -30.456  1.00 57.64           O  
ATOM     95  CB  LYS A 708      50.835 -18.989 -32.829  1.00 49.74           C  
ATOM     96  CG  LYS A 708      50.589 -19.676 -34.126  1.00 67.82           C  
ATOM     97  CD  LYS A 708      50.842 -21.159 -33.987  1.00 85.55           C  
ATOM     98  CE  LYS A 708      52.286 -21.440 -33.606  1.00 93.78           C  
ATOM     99  NZ  LYS A 708      52.616 -22.881 -33.769  1.00 92.32           N  
ATOM    100  N   GLU A 709      48.331 -17.193 -31.541  1.00 60.03           N  
ATOM    101  CA  GLU A 709      47.542 -16.921 -30.338  1.00 60.47           C  
ATOM    102  C   GLU A 709      47.690 -17.976 -29.251  1.00 63.12           C  
ATOM    103  O   GLU A 709      47.544 -17.696 -28.060  1.00 55.69           O  
ATOM    104  CB  GLU A 709      46.073 -16.806 -30.687  1.00 50.35           C  
ATOM    105  CG  GLU A 709      45.371 -15.806 -29.811  1.00 71.97           C  
ATOM    106  CD  GLU A 709      43.878 -15.834 -29.990  1.00 87.98           C  
ATOM    107  OE1 GLU A 709      43.221 -14.865 -29.540  1.00 87.44           O  
ATOM    108  OE2 GLU A 709      43.369 -16.828 -30.570  1.00 88.27           O  
ATOM    109  N   THR A 710      47.961 -19.199 -29.677  1.00 63.57           N  
ATOM    110  CA  THR A 710      48.126 -20.300 -28.750  1.00 69.90           C  
ATOM    111  C   THR A 710      49.356 -20.023 -27.892  1.00 66.32           C  
ATOM    112  O   THR A 710      49.442 -20.457 -26.747  1.00 69.40           O  
ATOM    113  CB  THR A 710      48.308 -21.624 -29.537  1.00 73.80           C  
ATOM    114  OG1 THR A 710      49.693 -21.826 -29.866  1.00 68.03           O  
ATOM    115  CG2 THR A 710      47.519 -21.557 -30.830  1.00 68.67           C  
ATOM    116  N   GLU A 711      50.291 -19.275 -28.471  1.00 63.21           N  
ATOM    117  CA  GLU A 711      51.556 -18.910 -27.850  1.00 50.20           C  
ATOM    118  C   GLU A 711      51.550 -17.968 -26.659  1.00 56.08           C  
ATOM    119  O   GLU A 711      52.603 -17.729 -26.069  1.00 54.37           O  
ATOM    120  CB  GLU A 711      52.464 -18.294 -28.882  1.00 54.79           C  
ATOM    121  CG  GLU A 711      53.133 -19.262 -29.783  1.00 62.43           C  
ATOM    122  CD  GLU A 711      54.190 -18.569 -30.602  1.00 67.14           C  
ATOM    123  OE1 GLU A 711      55.178 -19.246 -30.958  1.00 81.41           O  
ATOM    124  OE2 GLU A 711      54.028 -17.354 -30.886  1.00 53.98           O  
ATOM    125  N   PHE A 712      50.406 -17.398 -26.311  1.00 44.37           N  
ATOM    126  CA  PHE A 712      50.404 -16.513 -25.173  1.00 48.48           C  
ATOM    127  C   PHE A 712      49.059 -16.445 -24.498  1.00 47.68           C  
ATOM    128  O   PHE A 712      48.032 -16.672 -25.124  1.00 64.85           O  
ATOM    129  CB  PHE A 712      50.865 -15.117 -25.601  1.00 55.39           C  
ATOM    130  CG  PHE A 712      49.991 -14.479 -26.623  1.00 44.33           C  
ATOM    131  CD1 PHE A 712      48.881 -13.730 -26.244  1.00 47.91           C  
ATOM    132  CD2 PHE A 712      50.267 -14.642 -27.966  1.00 34.34           C  
ATOM    133  CE1 PHE A 712      48.044 -13.143 -27.211  1.00 56.40           C  
ATOM    134  CE2 PHE A 712      49.455 -14.072 -28.937  1.00 60.49           C  
ATOM    135  CZ  PHE A 712      48.333 -13.317 -28.562  1.00 61.02           C  
ATOM    136  N   LYS A 713      49.070 -16.135 -23.210  1.00 49.77           N  
ATOM    137  CA  LYS A 713      47.832 -16.041 -22.479  1.00 51.98           C  
ATOM    138  C   LYS A 713      47.655 -14.722 -21.751  1.00 57.58           C  
ATOM    139  O   LYS A 713      48.576 -14.229 -21.100  1.00 60.48           O  
ATOM    140  CB  LYS A 713      47.709 -17.210 -21.507  1.00 67.17           C  
ATOM    141  CG  LYS A 713      48.900 -17.458 -20.616  1.00 74.62           C  
ATOM    142  CD  LYS A 713      48.677 -18.746 -19.818  1.00 89.74           C  
ATOM    143  CE  LYS A 713      48.311 -18.478 -18.357  1.00 93.50           C  
ATOM    144  NZ  LYS A 713      47.765 -19.703 -17.685  1.00 83.08           N  
ATOM    145  N   LYS A 714      46.462 -14.150 -21.894  1.00 47.35           N  
ATOM    146  CA  LYS A 714      46.126 -12.899 -21.253  1.00 53.82           C  
ATOM    147  C   LYS A 714      45.936 -13.289 -19.810  1.00 65.55           C  
ATOM    148  O   LYS A 714      45.458 -14.379 -19.515  1.00 71.68           O  
ATOM    149  CB  LYS A 714      44.840 -12.317 -21.847  1.00 46.66           C  
ATOM    150  CG  LYS A 714      44.935 -12.094 -23.367  1.00 62.09           C  
ATOM    151  CD  LYS A 714      43.657 -11.497 -23.985  1.00 69.57           C  
ATOM    152  CE  LYS A 714      43.790 -11.274 -25.509  1.00 72.36           C  
ATOM    153  NZ  LYS A 714      44.088 -12.516 -26.320  1.00 68.36           N  
ATOM    154  N   ILE A 715      46.326 -12.414 -18.901  1.00 61.19           N  
ATOM    155  CA  ILE A 715      46.211 -12.752 -17.507  1.00 60.84           C  
ATOM    156  C   ILE A 715      45.314 -11.830 -16.712  1.00 66.40           C  
ATOM    157  O   ILE A 715      44.668 -12.275 -15.772  1.00 61.79           O  
ATOM    158  CB  ILE A 715      47.596 -12.781 -16.876  1.00 63.60           C  
ATOM    159  CG1 ILE A 715      48.408 -13.909 -17.519  1.00 60.25           C  
ATOM    160  CG2 ILE A 715      47.490 -12.912 -15.374  1.00 49.00           C  
ATOM    161  CD1 ILE A 715      48.516 -15.149 -16.703  1.00 53.50           C  
ATOM    162  N   LYS A 716      45.250 -10.566 -17.109  1.00 69.68           N  
ATOM    163  CA  LYS A 716      44.461  -9.587 -16.383  1.00 71.87           C  
ATOM    164  C   LYS A 716      44.335  -8.352 -17.232  1.00 70.29           C  
ATOM    165  O   LYS A 716      45.150  -8.122 -18.124  1.00 85.30           O  
ATOM    166  CB  LYS A 716      45.164  -9.264 -15.063  1.00 81.39           C  
ATOM    167  CG  LYS A 716      44.610  -8.093 -14.265  1.00 93.00           C  
ATOM    168  CD  LYS A 716      45.411  -7.937 -12.976  1.00 95.61           C  
ATOM    169  CE  LYS A 716      45.080  -6.645 -12.245  1.00107.49           C  
ATOM    170  NZ  LYS A 716      45.994  -6.418 -11.080  1.00110.17           N  
ATOM    171  N   VAL A 717      43.342  -7.543 -16.970  1.00 69.18           N  
ATOM    172  CA  VAL A 717      43.164  -6.347 -17.749  1.00 72.41           C  
ATOM    173  C   VAL A 717      43.946  -5.167 -17.270  1.00 79.61           C  
ATOM    174  O   VAL A 717      44.023  -4.923 -16.074  1.00 88.48           O  
ATOM    175  CB  VAL A 717      41.780  -5.882 -17.649  1.00 66.43           C  
ATOM    176  CG1 VAL A 717      41.706  -4.452 -18.090  1.00 67.63           C  
ATOM    177  CG2 VAL A 717      40.947  -6.739 -18.467  1.00 73.08           C  
ATOM    178  N   LEU A 718      44.481  -4.382 -18.187  1.00 84.78           N  
ATOM    179  CA  LEU A 718      45.221  -3.224 -17.748  1.00 85.39           C  
ATOM    180  C   LEU A 718      44.517  -1.963 -18.017  1.00 87.17           C  
ATOM    181  O   LEU A 718      44.581  -1.025 -17.231  1.00 87.09           O  
ATOM    182  CB  LEU A 718      46.562  -3.114 -18.419  1.00 81.51           C  
ATOM    183  CG  LEU A 718      47.403  -4.267 -17.908  1.00 82.78           C  
ATOM    184  CD1 LEU A 718      48.809  -3.864 -17.755  1.00 76.95           C  
ATOM    185  CD2 LEU A 718      46.862  -4.587 -16.560  1.00 93.56           C  
ATOM    186  N   GLY A 719      43.856  -1.899 -19.147  1.00 94.74           N  
ATOM    187  CA  GLY A 719      43.214  -0.656 -19.426  1.00107.69           C  
ATOM    188  C   GLY A 719      42.131  -0.708 -20.445  1.00112.24           C  
ATOM    189  O   GLY A 719      41.990  -1.680 -21.180  1.00116.34           O  
ATOM    190  N   SER A 720      41.349   0.358 -20.473  1.00120.46           N  
ATOM    191  CA  SER A 720      40.255   0.469 -21.411  1.00125.19           C  
ATOM    192  C   SER A 720      39.862   1.912 -21.587  1.00126.71           C  
ATOM    193  O   SER A 720      40.302   2.555 -22.531  1.00124.58           O  
ATOM    194  CB  SER A 720      39.066  -0.350 -20.959  1.00123.01           C  
ATOM    195  OG  SER A 720      39.104  -1.609 -21.588  1.00127.98           O  
ATOM    196  N   PHE A 723      39.457   2.489 -25.253  1.00120.65           N  
ATOM    197  CA  PHE A 723      39.686   2.356 -26.688  1.00127.69           C  
ATOM    198  C   PHE A 723      39.328   0.940 -27.119  1.00130.31           C  
ATOM    199  O   PHE A 723      38.194   0.657 -27.520  1.00129.59           O  
ATOM    200  CB  PHE A 723      41.157   2.634 -27.011  1.00128.98           C  
ATOM    201  CG  PHE A 723      41.537   2.305 -28.425  1.00131.09           C  
ATOM    202  CD1 PHE A 723      40.992   3.017 -29.489  1.00129.40           C  
ATOM    203  CD2 PHE A 723      42.417   1.260 -28.697  1.00133.67           C  
ATOM    204  CE1 PHE A 723      41.314   2.692 -30.807  1.00128.80           C  
ATOM    205  CE2 PHE A 723      42.745   0.927 -30.009  1.00135.96           C  
ATOM    206  CZ  PHE A 723      42.191   1.646 -31.067  1.00133.14           C  
ATOM    207  N   GLY A 724      40.330   0.069 -27.052  1.00129.56           N  
ATOM    208  CA  GLY A 724      40.154  -1.329 -27.379  1.00117.93           C  
ATOM    209  C   GLY A 724      40.197  -1.968 -26.009  1.00111.77           C  
ATOM    210  O   GLY A 724      39.239  -1.857 -25.243  1.00114.54           O  
ATOM    211  N   THR A 725      41.318  -2.593 -25.671  1.00 95.59           N  
ATOM    212  CA  THR A 725      41.459  -3.230 -24.370  1.00 85.46           C  
ATOM    213  C   THR A 725      42.872  -3.791 -24.246  1.00 81.01           C  
ATOM    214  O   THR A 725      43.332  -4.486 -25.150  1.00 88.34           O  
ATOM    215  CB  THR A 725      40.413  -4.358 -24.213  1.00 83.26           C  
ATOM    216  OG1 THR A 725      40.717  -5.149 -23.060  1.00 89.04           O  
ATOM    217  CG2 THR A 725      40.388  -5.239 -25.461  1.00 90.34           C  
ATOM    218  N   VAL A 726      43.557  -3.486 -23.138  1.00 76.08           N  
ATOM    219  CA  VAL A 726      44.941  -3.943 -22.904  1.00 65.66           C  
ATOM    220  C   VAL A 726      45.109  -4.959 -21.780  1.00 63.71           C  
ATOM    221  O   VAL A 726      44.551  -4.785 -20.698  1.00 70.26           O  
ATOM    222  CB  VAL A 726      45.885  -2.754 -22.577  1.00 58.65           C  
ATOM    223  CG1 VAL A 726      47.297  -3.265 -22.325  1.00 50.33           C  
ATOM    224  CG2 VAL A 726      45.907  -1.778 -23.721  1.00 51.40           C  
ATOM    225  N   TYR A 727      45.904  -6.002 -22.024  1.00 61.29           N  
ATOM    226  CA  TYR A 727      46.135  -7.035 -21.010  1.00 62.89           C  
ATOM    227  C   TYR A 727      47.591  -7.288 -20.639  1.00 59.66           C  
ATOM    228  O   TYR A 727      48.520  -6.964 -21.370  1.00 63.63           O  
ATOM    229  CB  TYR A 727      45.567  -8.381 -21.460  1.00 70.13           C  
ATOM    230  CG  TYR A 727      44.147  -8.335 -21.933  1.00 91.72           C  
ATOM    231  CD1 TYR A 727      43.819  -7.706 -23.127  1.00103.58           C  
ATOM    232  CD2 TYR A 727      43.125  -8.925 -21.195  1.00 96.41           C  
ATOM    233  CE1 TYR A 727      42.509  -7.663 -23.580  1.00109.37           C  
ATOM    234  CE2 TYR A 727      41.809  -8.887 -21.637  1.00 99.24           C  
ATOM    235  CZ  TYR A 727      41.509  -8.254 -22.834  1.00107.82           C  
ATOM    236  OH  TYR A 727      40.217  -8.216 -23.299  1.00112.95           O  
ATOM    237  N   LYS A 728      47.780  -7.895 -19.485  1.00 49.49           N  
ATOM    238  CA  LYS A 728      49.109  -8.258 -19.066  1.00 54.74           C  
ATOM    239  C   LYS A 728      49.050  -9.745 -19.291  1.00 50.60           C  
ATOM    240  O   LYS A 728      48.027 -10.362 -19.037  1.00 61.10           O  
ATOM    241  CB  LYS A 728      49.331  -7.994 -17.580  1.00 48.64           C  
ATOM    242  CG  LYS A 728      49.697  -9.266 -16.818  1.00 70.30           C  
ATOM    243  CD  LYS A 728      50.175  -8.970 -15.424  1.00 73.22           C  
ATOM    244  CE  LYS A 728      49.202  -8.029 -14.751  1.00 89.80           C  
ATOM    245  NZ  LYS A 728      49.465  -7.920 -13.300  1.00102.08           N  
ATOM    246  N   GLY A 729      50.133 -10.332 -19.758  1.00 45.44           N  
ATOM    247  CA  GLY A 729      50.101 -11.752 -19.976  1.00 48.55           C  
ATOM    248  C   GLY A 729      51.488 -12.297 -20.147  1.00 47.98           C  
ATOM    249  O   GLY A 729      52.466 -11.645 -19.798  1.00 47.26           O  
ATOM    250  N   LEU A 730      51.567 -13.497 -20.695  1.00 34.87           N  
ATOM    251  CA  LEU A 730      52.838 -14.134 -20.910  1.00 40.72           C  
ATOM    252  C   LEU A 730      52.863 -14.669 -22.304  1.00 52.41           C  
ATOM    253  O   LEU A 730      51.843 -15.160 -22.820  1.00 38.69           O  
ATOM    254  CB  LEU A 730      53.035 -15.279 -19.934  1.00 49.76           C  
ATOM    255  CG  LEU A 730      53.545 -14.954 -18.533  1.00 60.29           C  
ATOM    256  CD1 LEU A 730      53.132 -16.044 -17.581  1.00 46.04           C  
ATOM    257  CD2 LEU A 730      55.050 -14.816 -18.569  1.00 52.87           C  
ATOM    258  N   TRP A 731      54.015 -14.572 -22.937  1.00 56.57           N  
ATOM    259  CA  TRP A 731      54.215 -15.048 -24.269  1.00 46.76           C  
ATOM    260  C   TRP A 731      55.201 -16.164 -24.119  1.00 44.61           C  
ATOM    261  O   TRP A 731      56.253 -16.005 -23.530  1.00 44.12           O  
ATOM    262  CB  TRP A 731      54.812 -13.984 -25.154  1.00 41.97           C  
ATOM    263  CG  TRP A 731      55.199 -14.535 -26.439  1.00 40.91           C  
ATOM    264  CD1 TRP A 731      54.535 -15.464 -27.151  1.00 54.45           C  
ATOM    265  CD2 TRP A 731      56.310 -14.154 -27.224  1.00 42.08           C  
ATOM    266  NE1 TRP A 731      55.159 -15.706 -28.335  1.00 50.51           N  
ATOM    267  CE2 TRP A 731      56.260 -14.912 -28.406  1.00 46.17           C  
ATOM    268  CE3 TRP A 731      57.352 -13.244 -27.049  1.00 40.36           C  
ATOM    269  CZ2 TRP A 731      57.202 -14.789 -29.409  1.00 44.23           C  
ATOM    270  CZ3 TRP A 731      58.283 -13.126 -28.030  1.00 46.88           C  
ATOM    271  CH2 TRP A 731      58.206 -13.899 -29.203  1.00 49.85           C  
ATOM    272  N   ILE A 732      54.876 -17.304 -24.682  1.00 50.49           N  
ATOM    273  CA  ILE A 732      55.760 -18.408 -24.543  1.00 51.22           C  
ATOM    274  C   ILE A 732      56.100 -18.912 -25.908  1.00 57.07           C  
ATOM    275  O   ILE A 732      55.360 -19.707 -26.476  1.00 67.06           O  
ATOM    276  CB  ILE A 732      55.040 -19.452 -23.787  1.00 51.91           C  
ATOM    277  CG1 ILE A 732      54.557 -18.860 -22.484  1.00 59.18           C  
ATOM    278  CG2 ILE A 732      55.922 -20.582 -23.481  1.00 46.68           C  
ATOM    279  CD1 ILE A 732      53.792 -19.816 -21.681  1.00 44.74           C  
ATOM    280  N   PRO A 733      57.195 -18.438 -26.495  1.00 54.96           N  
ATOM    281  CA  PRO A 733      57.445 -18.983 -27.822  1.00 58.93           C  
ATOM    282  C   PRO A 733      57.479 -20.466 -27.680  1.00 67.79           C  
ATOM    283  O   PRO A 733      57.938 -21.007 -26.677  1.00 70.66           O  
ATOM    284  CB  PRO A 733      58.833 -18.499 -28.164  1.00 59.68           C  
ATOM    285  CG  PRO A 733      58.931 -17.282 -27.426  1.00 54.88           C  
ATOM    286  CD  PRO A 733      58.237 -17.481 -26.114  1.00 53.48           C  
ATOM    287  N   GLU A 734      57.017 -21.139 -28.704  1.00 78.90           N  
ATOM    288  CA  GLU A 734      56.974 -22.559 -28.649  1.00 79.27           C  
ATOM    289  C   GLU A 734      58.340 -23.178 -28.808  1.00 78.46           C  
ATOM    290  O   GLU A 734      59.086 -22.834 -29.731  1.00 65.43           O  
ATOM    291  CB  GLU A 734      56.094 -23.022 -29.764  1.00 89.21           C  
ATOM    292  CG  GLU A 734      55.515 -24.366 -29.580  1.00102.60           C  
ATOM    293  CD  GLU A 734      54.756 -24.725 -30.817  1.00101.90           C  
ATOM    294  OE1 GLU A 734      54.804 -23.905 -31.763  1.00 97.91           O  
ATOM    295  OE2 GLU A 734      54.131 -25.799 -30.846  1.00 97.14           O  
ATOM    296  N   GLY A 735      58.681 -24.087 -27.910  1.00 76.66           N  
ATOM    297  CA  GLY A 735      59.942 -24.770 -28.037  1.00 75.03           C  
ATOM    298  C   GLY A 735      61.175 -24.075 -27.535  1.00 68.08           C  
ATOM    299  O   GLY A 735      62.268 -24.589 -27.720  1.00 64.73           O  
ATOM    300  N   GLU A 736      61.020 -22.909 -26.928  1.00 66.51           N  
ATOM    301  CA  GLU A 736      62.148 -22.192 -26.369  1.00 66.63           C  
ATOM    302  C   GLU A 736      61.689 -22.258 -24.975  1.00 65.20           C  
ATOM    303  O   GLU A 736      60.496 -22.158 -24.752  1.00 88.02           O  
ATOM    304  CB  GLU A 736      62.117 -20.751 -26.773  1.00 68.40           C  
ATOM    305  CG  GLU A 736      61.966 -20.540 -28.220  1.00 78.18           C  
ATOM    306  CD  GLU A 736      62.700 -19.311 -28.612  1.00 90.34           C  
ATOM    307  OE1 GLU A 736      62.070 -18.423 -29.210  1.00 90.26           O  
ATOM    308  OE2 GLU A 736      63.904 -19.226 -28.295  1.00 86.81           O  
ATOM    309  N   LYS A 737      62.548 -22.419 -24.005  1.00 60.51           N  
ATOM    310  CA  LYS A 737      61.975 -22.494 -22.687  1.00 56.95           C  
ATOM    311  C   LYS A 737      61.881 -21.139 -22.069  1.00 53.54           C  
ATOM    312  O   LYS A 737      62.565 -20.882 -21.082  1.00 50.88           O  
ATOM    313  CB  LYS A 737      62.839 -23.315 -21.779  1.00 74.14           C  
ATOM    314  CG  LYS A 737      62.551 -24.763 -21.800  1.00 78.61           C  
ATOM    315  CD  LYS A 737      63.476 -25.454 -20.815  1.00 84.70           C  
ATOM    316  CE  LYS A 737      63.411 -24.814 -19.425  1.00 79.30           C  
ATOM    317  NZ  LYS A 737      64.208 -25.590 -18.437  1.00 71.82           N  
ATOM    318  N   VAL A 738      61.055 -20.250 -22.590  1.00 40.49           N  
ATOM    319  CA  VAL A 738      61.033 -18.933 -22.009  1.00 32.21           C  
ATOM    320  C   VAL A 738      59.631 -18.485 -21.881  1.00 37.47           C  
ATOM    321  O   VAL A 738      58.767 -18.950 -22.615  1.00 51.12           O  
ATOM    322  CB  VAL A 738      61.744 -17.929 -22.893  1.00 44.02           C  
ATOM    323  CG1 VAL A 738      63.202 -18.137 -22.866  1.00 37.20           C  
ATOM    324  CG2 VAL A 738      61.290 -18.121 -24.303  1.00 45.47           C  
ATOM    325  N   LYS A 739      59.418 -17.559 -20.962  1.00 46.11           N  
ATOM    326  CA  LYS A 739      58.117 -16.974 -20.752  1.00 53.47           C  
ATOM    327  C   LYS A 739      58.431 -15.500 -20.697  1.00 56.09           C  
ATOM    328  O   LYS A 739      59.320 -15.087 -19.954  1.00 67.08           O  
ATOM    329  CB  LYS A 739      57.528 -17.412 -19.431  1.00 49.55           C  
ATOM    330  CG  LYS A 739      57.428 -18.876 -19.295  1.00 54.65           C  
ATOM    331  CD  LYS A 739      56.511 -19.202 -18.166  1.00 48.21           C  
ATOM    332  CE  LYS A 739      56.541 -20.680 -17.908  1.00 56.72           C  
ATOM    333  NZ  LYS A 739      55.671 -21.007 -16.764  1.00 58.06           N  
ATOM    334  N   ILE A 740      57.707 -14.701 -21.467  1.00 49.49           N  
ATOM    335  CA  ILE A 740      57.972 -13.285 -21.495  1.00 37.55           C  
ATOM    336  C   ILE A 740      56.787 -12.446 -21.107  1.00 36.98           C  
ATOM    337  O   ILE A 740      55.711 -12.523 -21.711  1.00 39.99           O  
ATOM    338  CB  ILE A 740      58.448 -12.880 -22.884  1.00 41.23           C  
ATOM    339  CG1 ILE A 740      59.668 -13.710 -23.244  1.00 35.54           C  
ATOM    340  CG2 ILE A 740      58.820 -11.414 -22.906  1.00 32.88           C  
ATOM    341  CD1 ILE A 740      59.920 -13.758 -24.690  1.00 48.51           C  
ATOM    342  N   PRO A 741      56.960 -11.648 -20.062  1.00 36.56           N  
ATOM    343  CA  PRO A 741      55.887 -10.777 -19.598  1.00 33.66           C  
ATOM    344  C   PRO A 741      55.611  -9.838 -20.751  1.00 42.96           C  
ATOM    345  O   PRO A 741      56.528  -9.188 -21.253  1.00 37.64           O  
ATOM    346  CB  PRO A 741      56.519 -10.050 -18.421  1.00 35.67           C  
ATOM    347  CG  PRO A 741      57.447 -11.109 -17.858  1.00 38.01           C  
ATOM    348  CD  PRO A 741      58.082 -11.671 -19.111  1.00 45.73           C  
ATOM    349  N   VAL A 742      54.359  -9.770 -21.181  1.00 37.90           N  
ATOM    350  CA  VAL A 742      54.043  -8.908 -22.288  1.00 40.01           C  
ATOM    351  C   VAL A 742      52.760  -8.162 -22.049  1.00 40.75           C  
ATOM    352  O   VAL A 742      52.008  -8.456 -21.133  1.00 49.97           O  
ATOM    353  CB  VAL A 742      53.934  -9.708 -23.597  1.00 38.36           C  
ATOM    354  CG1 VAL A 742      55.174 -10.569 -23.767  1.00 40.25           C  
ATOM    355  CG2 VAL A 742      52.695 -10.565 -23.586  1.00 39.10           C  
ATOM    356  N   ALA A 743      52.555  -7.150 -22.864  1.00 38.14           N  
ATOM    357  CA  ALA A 743      51.356  -6.364 -22.804  1.00 50.02           C  
ATOM    358  C   ALA A 743      50.692  -6.756 -24.109  1.00 53.65           C  
ATOM    359  O   ALA A 743      51.351  -6.852 -25.147  1.00 48.98           O  
ATOM    360  CB  ALA A 743      51.677  -4.874 -22.796  1.00 37.39           C  
ATOM    361  N   ILE A 744      49.395  -7.017 -24.035  1.00 59.08           N  
ATOM    362  CA  ILE A 744      48.622  -7.401 -25.196  1.00 52.96           C  
ATOM    363  C   ILE A 744      47.515  -6.404 -25.386  1.00 57.49           C  
ATOM    364  O   ILE A 744      46.693  -6.190 -24.499  1.00 63.58           O  
ATOM    365  CB  ILE A 744      47.996  -8.771 -25.015  1.00 43.24           C  
ATOM    366  CG1 ILE A 744      49.088  -9.836 -25.028  1.00 41.15           C  
ATOM    367  CG2 ILE A 744      47.013  -9.031 -26.134  1.00 61.12           C  
ATOM    368  CD1 ILE A 744      48.781 -11.056 -24.173  1.00 37.29           C  
ATOM    369  N   LYS A 745      47.517  -5.772 -26.542  1.00 59.21           N  
ATOM    370  CA  LYS A 745      46.486  -4.821 -26.854  1.00 68.72           C  
ATOM    371  C   LYS A 745      45.630  -5.482 -27.929  1.00 79.47           C  
ATOM    372  O   LYS A 745      46.142  -5.956 -28.956  1.00 73.58           O  
ATOM    373  CB  LYS A 745      47.090  -3.529 -27.372  1.00 63.03           C  
ATOM    374  CG  LYS A 745      46.031  -2.498 -27.633  1.00 71.90           C  
ATOM    375  CD  LYS A 745      46.591  -1.288 -28.330  1.00 71.57           C  
ATOM    376  CE  LYS A 745      46.889  -0.174 -27.359  1.00 72.85           C  
ATOM    377  NZ  LYS A 745      47.262   1.032 -28.130  1.00 82.15           N  
ATOM    378  N   GLU A 746      44.327  -5.529 -27.676  1.00 85.68           N  
ATOM    379  CA  GLU A 746      43.394  -6.150 -28.603  1.00 83.28           C  
ATOM    380  C   GLU A 746      42.406  -5.123 -29.159  1.00 75.35           C  
ATOM    381  O   GLU A 746      42.387  -4.854 -30.365  1.00 74.03           O  
ATOM    382  CB  GLU A 746      42.649  -7.272 -27.883  1.00 81.39           C  
ATOM    383  CG  GLU A 746      42.202  -8.400 -28.782  1.00 81.49           C  
ATOM    384  CD  GLU A 746      41.223  -9.316 -28.086  1.00 91.57           C  
ATOM    385  OE1 GLU A 746      40.553  -8.841 -27.136  1.00 92.16           O  
ATOM    386  OE2 GLU A 746      41.113 -10.495 -28.497  1.00 94.60           O  
ATOM    387  N   ALA A 750      34.448  -3.544 -31.918  1.00114.54           N  
ATOM    388  CA  ALA A 750      34.200  -3.633 -33.350  1.00112.05           C  
ATOM    389  C   ALA A 750      35.505  -3.691 -34.126  1.00113.24           C  
ATOM    390  O   ALA A 750      36.592  -3.478 -33.582  1.00109.83           O  
ATOM    391  CB  ALA A 750      33.371  -2.429 -33.823  1.00 98.60           C  
ATOM    392  N   THR A 751      35.379  -3.996 -35.409  1.00114.57           N  
ATOM    393  CA  THR A 751      36.522  -4.056 -36.304  1.00111.84           C  
ATOM    394  C   THR A 751      36.299  -3.003 -37.384  1.00106.76           C  
ATOM    395  O   THR A 751      35.430  -3.144 -38.250  1.00 99.82           O  
ATOM    396  CB  THR A 751      36.668  -5.455 -36.940  1.00110.97           C  
ATOM    397  OG1 THR A 751      37.171  -6.367 -35.957  1.00109.66           O  
ATOM    398  CG2 THR A 751      37.625  -5.416 -38.123  1.00106.98           C  
ATOM    399  N   SER A 752      37.077  -1.933 -37.304  1.00101.68           N  
ATOM    400  CA  SER A 752      36.971  -0.842 -38.255  1.00100.71           C  
ATOM    401  C   SER A 752      38.150  -0.935 -39.207  1.00101.12           C  
ATOM    402  O   SER A 752      39.290  -1.038 -38.767  1.00107.37           O  
ATOM    403  CB  SER A 752      37.005   0.491 -37.510  1.00 92.78           C  
ATOM    404  OG  SER A 752      36.633   1.561 -38.357  1.00100.72           O  
ATOM    405  N   PRO A 753      37.895  -0.913 -40.526  1.00102.06           N  
ATOM    406  CA  PRO A 753      39.018  -1.000 -41.467  1.00 99.02           C  
ATOM    407  C   PRO A 753      40.026   0.130 -41.202  1.00 96.97           C  
ATOM    408  O   PRO A 753      41.233  -0.017 -41.432  1.00 89.13           O  
ATOM    409  CB  PRO A 753      38.326  -0.891 -42.831  1.00 96.07           C  
ATOM    410  CG  PRO A 753      37.124  -0.036 -42.537  1.00 95.13           C  
ATOM    411  CD  PRO A 753      36.633  -0.621 -41.231  1.00101.02           C  
ATOM    412  N   LYS A 754      39.509   1.248 -40.695  1.00 94.70           N  
ATOM    413  CA  LYS A 754      40.309   2.419 -40.370  1.00 90.86           C  
ATOM    414  C   LYS A 754      41.153   2.154 -39.134  1.00 95.34           C  
ATOM    415  O   LYS A 754      42.362   2.407 -39.129  1.00101.33           O  
ATOM    416  CB  LYS A 754      39.405   3.617 -40.097  1.00 89.63           C  
ATOM    417  CG  LYS A 754      40.180   4.871 -39.834  1.00 92.69           C  
ATOM    418  CD  LYS A 754      41.105   5.151 -41.008  1.00106.87           C  
ATOM    419  CE  LYS A 754      41.865   6.432 -40.782  1.00110.77           C  
ATOM    420  NZ  LYS A 754      40.918   7.494 -40.333  1.00118.01           N  
ATOM    421  N   ALA A 755      40.502   1.657 -38.084  1.00 89.53           N  
ATOM    422  CA  ALA A 755      41.181   1.342 -36.832  1.00 86.33           C  
ATOM    423  C   ALA A 755      42.347   0.369 -37.072  1.00 84.02           C  
ATOM    424  O   ALA A 755      43.444   0.583 -36.557  1.00 93.76           O  
ATOM    425  CB  ALA A 755      40.186   0.760 -35.831  1.00 70.00           C  
ATOM    426  N   ASN A 756      42.110  -0.687 -37.858  1.00 78.79           N  
ATOM    427  CA  ASN A 756      43.146  -1.679 -38.191  1.00 69.04           C  
ATOM    428  C   ASN A 756      44.313  -0.996 -38.902  1.00 61.09           C  
ATOM    429  O   ASN A 756      45.478  -1.288 -38.651  1.00 58.84           O  
ATOM    430  CB  ASN A 756      42.578  -2.749 -39.118  1.00 69.52           C  
ATOM    431  CG  ASN A 756      41.591  -3.668 -38.427  1.00 80.07           C  
ATOM    432  OD1 ASN A 756      41.957  -4.731 -37.922  1.00 80.06           O  
ATOM    433  ND2 ASN A 756      40.328  -3.260 -38.399  1.00 78.38           N  
ATOM    434  N   LYS A 757      43.977  -0.088 -39.803  1.00 63.09           N  
ATOM    435  CA  LYS A 757      44.969   0.657 -40.555  1.00 70.06           C  
ATOM    436  C   LYS A 757      45.903   1.342 -39.557  1.00 69.00           C  
ATOM    437  O   LYS A 757      47.118   1.223 -39.646  1.00 61.52           O  
ATOM    438  CB  LYS A 757      44.255   1.693 -41.435  1.00 75.75           C  
ATOM    439  CG  LYS A 757      45.040   2.193 -42.628  1.00 79.97           C  
ATOM    440  CD  LYS A 757      46.102   3.200 -42.238  1.00 86.87           C  
ATOM    441  CE  LYS A 757      46.640   3.910 -43.476  1.00 96.86           C  
ATOM    442  NZ  LYS A 757      48.087   3.644 -43.720  1.00 94.50           N  
ATOM    443  N   GLU A 758      45.332   2.040 -38.585  1.00 74.16           N  
ATOM    444  CA  GLU A 758      46.149   2.743 -37.602  1.00 77.05           C  
ATOM    445  C   GLU A 758      47.045   1.863 -36.745  1.00 72.35           C  
ATOM    446  O   GLU A 758      48.252   2.131 -36.600  1.00 61.83           O  
ATOM    447  CB  GLU A 758      45.261   3.600 -36.710  1.00 83.96           C  
ATOM    448  CG  GLU A 758      44.839   4.870 -37.397  1.00 93.79           C  
ATOM    449  CD  GLU A 758      43.720   5.551 -36.681  1.00106.19           C  
ATOM    450  OE1 GLU A 758      43.238   6.573 -37.205  1.00108.74           O  
ATOM    451  OE2 GLU A 758      43.325   5.059 -35.600  1.00113.84           O  
ATOM    452  N   ILE A 759      46.464   0.815 -36.178  1.00 62.45           N  
ATOM    453  CA  ILE A 759      47.239  -0.071 -35.347  1.00 58.40           C  
ATOM    454  C   ILE A 759      48.356  -0.731 -36.178  1.00 63.68           C  
ATOM    455  O   ILE A 759      49.490  -0.888 -35.699  1.00 49.58           O  
ATOM    456  CB  ILE A 759      46.338  -1.121 -34.673  1.00 58.85           C  
ATOM    457  CG1 ILE A 759      47.087  -1.726 -33.494  1.00 65.84           C  
ATOM    458  CG2 ILE A 759      45.912  -2.184 -35.663  1.00 71.30           C  
ATOM    459  CD1 ILE A 759      46.511  -3.031 -33.002  1.00 82.93           C  
ATOM    460  N   LEU A 760      48.057  -1.101 -37.423  1.00 53.89           N  
ATOM    461  CA  LEU A 760      49.091  -1.696 -38.252  1.00 49.31           C  
ATOM    462  C   LEU A 760      50.188  -0.654 -38.489  1.00 47.99           C  
ATOM    463  O   LEU A 760      51.373  -0.983 -38.480  1.00 54.12           O  
ATOM    464  CB  LEU A 760      48.531  -2.173 -39.593  1.00 48.49           C  
ATOM    465  CG  LEU A 760      48.164  -3.648 -39.769  1.00 58.80           C  
ATOM    466  CD1 LEU A 760      49.071  -4.520 -38.911  1.00 48.27           C  
ATOM    467  CD2 LEU A 760      46.728  -3.859 -39.369  1.00 61.79           C  
ATOM    468  N   ASP A 761      49.811   0.605 -38.694  1.00 45.36           N  
ATOM    469  CA  ASP A 761      50.830   1.628 -38.913  1.00 54.36           C  
ATOM    470  C   ASP A 761      51.699   1.777 -37.687  1.00 50.23           C  
ATOM    471  O   ASP A 761      52.906   1.956 -37.785  1.00 46.68           O  
ATOM    472  CB  ASP A 761      50.213   2.971 -39.275  1.00 55.37           C  
ATOM    473  CG  ASP A 761      49.711   3.002 -40.708  1.00 74.85           C  
ATOM    474  OD1 ASP A 761      50.183   2.176 -41.532  1.00 65.42           O  
ATOM    475  OD2 ASP A 761      48.850   3.855 -41.014  1.00 79.45           O  
ATOM    476  N   GLU A 762      51.090   1.671 -36.524  1.00 43.33           N  
ATOM    477  CA  GLU A 762      51.854   1.782 -35.310  1.00 47.61           C  
ATOM    478  C   GLU A 762      52.830   0.603 -35.221  1.00 54.10           C  
ATOM    479  O   GLU A 762      54.018   0.771 -34.919  1.00 53.63           O  
ATOM    480  CB  GLU A 762      50.915   1.778 -34.125  1.00 51.35           C  
ATOM    481  CG  GLU A 762      51.342   2.690 -33.021  1.00 71.07           C  
ATOM    482  CD  GLU A 762      50.530   2.464 -31.779  1.00 74.88           C  
ATOM    483  OE1 GLU A 762      49.308   2.720 -31.827  1.00 65.38           O  
ATOM    484  OE2 GLU A 762      51.118   2.017 -30.768  1.00 71.95           O  
ATOM    485  N   ALA A 763      52.322  -0.593 -35.492  1.00 58.03           N  
ATOM    486  CA  ALA A 763      53.141  -1.802 -35.447  1.00 45.76           C  
ATOM    487  C   ALA A 763      54.316  -1.604 -36.366  1.00 40.23           C  
ATOM    488  O   ALA A 763      55.441  -1.966 -36.050  1.00 53.77           O  
ATOM    489  CB  ALA A 763      52.331  -3.016 -35.904  1.00 55.06           C  
ATOM    490  N   TYR A 764      54.051  -1.036 -37.526  1.00 44.37           N  
ATOM    491  CA  TYR A 764      55.114  -0.786 -38.469  1.00 43.35           C  
ATOM    492  C   TYR A 764      56.198   0.094 -37.824  1.00 48.19           C  
ATOM    493  O   TYR A 764      57.390  -0.208 -37.904  1.00 49.52           O  
ATOM    494  CB  TYR A 764      54.545  -0.105 -39.719  1.00 41.61           C  
ATOM    495  CG  TYR A 764      55.619   0.419 -40.636  1.00 43.04           C  
ATOM    496  CD1 TYR A 764      55.998   1.758 -40.599  1.00 39.29           C  
ATOM    497  CD2 TYR A 764      56.316  -0.439 -41.479  1.00 46.40           C  
ATOM    498  CE1 TYR A 764      57.056   2.232 -41.382  1.00 55.15           C  
ATOM    499  CE2 TYR A 764      57.374   0.022 -42.265  1.00 64.94           C  
ATOM    500  CZ  TYR A 764      57.742   1.357 -42.214  1.00 60.75           C  
ATOM    501  OH  TYR A 764      58.795   1.805 -43.000  1.00 65.82           O  
ATOM    502  N   VAL A 765      55.792   1.174 -37.165  1.00 49.88           N  
ATOM    503  CA  VAL A 765      56.772   2.059 -36.554  1.00 51.20           C  
ATOM    504  C   VAL A 765      57.567   1.387 -35.450  1.00 45.79           C  
ATOM    505  O   VAL A 765      58.804   1.390 -35.462  1.00 43.15           O  
ATOM    506  CB  VAL A 765      56.103   3.324 -36.003  1.00 48.82           C  
ATOM    507  CG1 VAL A 765      57.122   4.134 -35.221  1.00 49.33           C  
ATOM    508  CG2 VAL A 765      55.554   4.161 -37.169  1.00 37.91           C  
ATOM    509  N   MET A 766      56.847   0.791 -34.504  1.00 52.70           N  
ATOM    510  CA  MET A 766      57.467   0.105 -33.375  1.00 45.52           C  
ATOM    511  C   MET A 766      58.395  -1.006 -33.784  1.00 46.22           C  
ATOM    512  O   MET A 766      59.373  -1.274 -33.096  1.00 59.38           O  
ATOM    513  CB  MET A 766      56.405  -0.455 -32.440  1.00 42.54           C  
ATOM    514  CG  MET A 766      55.683   0.618 -31.635  1.00 58.05           C  
ATOM    515  SD  MET A 766      54.432  -0.072 -30.534  1.00 79.44           S  
ATOM    516  CE  MET A 766      55.460  -0.638 -29.166  1.00 52.13           C  
ATOM    517  N   ALA A 767      58.097  -1.658 -34.901  1.00 47.76           N  
ATOM    518  CA  ALA A 767      58.933  -2.749 -35.365  1.00 45.10           C  
ATOM    519  C   ALA A 767      60.200  -2.207 -35.990  1.00 43.31           C  
ATOM    520  O   ALA A 767      61.191  -2.918 -36.135  1.00 33.02           O  
ATOM    521  CB  ALA A 767      58.185  -3.590 -36.371  1.00 40.92           C  
ATOM    522  N   SER A 768      60.181  -0.935 -36.350  1.00 38.91           N  
ATOM    523  CA  SER A 768      61.353  -0.362 -36.984  1.00 45.31           C  
ATOM    524  C   SER A 768      62.354   0.247 -36.018  1.00 49.45           C  
ATOM    525  O   SER A 768      63.418   0.689 -36.443  1.00 51.45           O  
ATOM    526  CB  SER A 768      60.910   0.695 -37.985  1.00 44.79           C  
ATOM    527  OG  SER A 768      59.808   0.226 -38.743  1.00 53.14           O  
ATOM    528  N   VAL A 769      62.029   0.273 -34.727  1.00 47.33           N  
ATOM    529  CA  VAL A 769      62.931   0.880 -33.752  1.00 41.99           C  
ATOM    530  C   VAL A 769      63.507  -0.138 -32.786  1.00 47.34           C  
ATOM    531  O   VAL A 769      62.876  -1.142 -32.476  1.00 49.93           O  
ATOM    532  CB  VAL A 769      62.210   2.006 -32.931  1.00 43.01           C  
ATOM    533  CG1 VAL A 769      61.824   3.179 -33.836  1.00 33.77           C  
ATOM    534  CG2 VAL A 769      60.961   1.461 -32.288  1.00 32.24           C  
ATOM    535  N   ASP A 770      64.728   0.116 -32.337  1.00 47.02           N  
ATOM    536  CA  ASP A 770      65.391  -0.759 -31.378  1.00 47.79           C  
ATOM    537  C   ASP A 770      66.323   0.049 -30.479  1.00 44.88           C  
ATOM    538  O   ASP A 770      67.461   0.334 -30.848  1.00 39.33           O  
ATOM    539  CB  ASP A 770      66.201  -1.851 -32.080  1.00 41.66           C  
ATOM    540  CG  ASP A 770      66.881  -2.784 -31.086  1.00 53.51           C  
ATOM    541  OD1 ASP A 770      66.451  -2.826 -29.904  1.00 51.12           O  
ATOM    542  OD2 ASP A 770      67.839  -3.478 -31.483  1.00 71.63           O  
ATOM    543  N   ASN A 771      65.856   0.401 -29.292  1.00 32.35           N  
ATOM    544  CA  ASN A 771      66.686   1.208 -28.408  1.00 45.00           C  
ATOM    545  C   ASN A 771      66.294   0.956 -26.964  1.00 36.53           C  
ATOM    546  O   ASN A 771      65.123   0.740 -26.655  1.00 31.06           O  
ATOM    547  CB  ASN A 771      66.528   2.684 -28.801  1.00 38.63           C  
ATOM    548  CG  ASN A 771      67.324   3.607 -27.930  1.00 44.64           C  
ATOM    549  OD1 ASN A 771      66.827   4.085 -26.899  1.00 33.92           O  
ATOM    550  ND2 ASN A 771      68.575   3.870 -28.327  1.00 30.49           N  
ATOM    551  N   PRO A 772      67.264   0.999 -26.053  1.00 33.36           N  
ATOM    552  CA  PRO A 772      66.899   0.737 -24.658  1.00 24.56           C  
ATOM    553  C   PRO A 772      65.877   1.656 -24.097  1.00 31.36           C  
ATOM    554  O   PRO A 772      65.300   1.342 -23.064  1.00 36.26           O  
ATOM    555  CB  PRO A 772      68.223   0.844 -23.905  1.00 32.02           C  
ATOM    556  CG  PRO A 772      69.258   0.434 -24.932  1.00 14.06           C  
ATOM    557  CD  PRO A 772      68.719   1.144 -26.212  1.00 34.04           C  
ATOM    558  N   HIS A 773      65.631   2.776 -24.777  1.00 30.24           N  
ATOM    559  CA  HIS A 773      64.659   3.737 -24.271  1.00 31.17           C  
ATOM    560  C   HIS A 773      63.429   3.998 -25.124  1.00 36.21           C  
ATOM    561  O   HIS A 773      62.769   5.041 -25.010  1.00 39.95           O  
ATOM    562  CB  HIS A 773      65.383   5.038 -23.909  1.00 27.05           C  
ATOM    563  CG  HIS A 773      66.433   4.835 -22.864  1.00 43.82           C  
ATOM    564  ND1 HIS A 773      66.134   4.389 -21.590  1.00 35.96           N  
ATOM    565  CD2 HIS A 773      67.784   4.891 -22.934  1.00 38.35           C  
ATOM    566  CE1 HIS A 773      67.257   4.176 -20.926  1.00 34.90           C  
ATOM    567  NE2 HIS A 773      68.273   4.468 -21.720  1.00 28.29           N  
ATOM    568  N   VAL A 774      63.119   3.037 -25.980  1.00 38.26           N  
ATOM    569  CA  VAL A 774      61.931   3.118 -26.811  1.00 35.40           C  
ATOM    570  C   VAL A 774      61.264   1.776 -26.632  1.00 37.52           C  
ATOM    571  O   VAL A 774      61.941   0.753 -26.487  1.00 39.55           O  
ATOM    572  CB  VAL A 774      62.267   3.334 -28.282  1.00 38.96           C  
ATOM    573  CG1 VAL A 774      60.993   3.316 -29.095  1.00 33.66           C  
ATOM    574  CG2 VAL A 774      62.967   4.671 -28.458  1.00 29.79           C  
ATOM    575  N   CYS A 775      59.939   1.777 -26.594  1.00 41.58           N  
ATOM    576  CA  CYS A 775      59.210   0.536 -26.405  1.00 51.09           C  
ATOM    577  C   CYS A 775      59.496  -0.442 -27.511  1.00 49.10           C  
ATOM    578  O   CYS A 775      59.569  -0.076 -28.684  1.00 64.31           O  
ATOM    579  CB  CYS A 775      57.706   0.790 -26.326  1.00 57.15           C  
ATOM    580  SG  CYS A 775      57.085   0.701 -24.651  1.00 81.93           S  
ATOM    581  N   ARG A 776      59.661  -1.696 -27.134  1.00 51.09           N  
ATOM    582  CA  ARG A 776      59.923  -2.736 -28.113  1.00 67.46           C  
ATOM    583  C   ARG A 776      58.663  -3.526 -28.422  1.00 65.04           C  
ATOM    584  O   ARG A 776      57.949  -3.967 -27.507  1.00 57.64           O  
ATOM    585  CB  ARG A 776      60.964  -3.689 -27.574  1.00 74.14           C  
ATOM    586  CG  ARG A 776      60.636  -4.120 -26.171  1.00 83.50           C  
ATOM    587  CD  ARG A 776      61.474  -5.302 -25.766  1.00105.41           C  
ATOM    588  NE  ARG A 776      62.896  -5.044 -25.952  1.00103.72           N  
ATOM    589  CZ  ARG A 776      63.663  -5.716 -26.801  1.00109.51           C  
ATOM    590  NH1 ARG A 776      63.132  -6.695 -27.542  1.00 94.79           N  
ATOM    591  NH2 ARG A 776      64.951  -5.401 -26.912  1.00 97.01           N  
ATOM    592  N   LEU A 777      58.408  -3.708 -29.716  1.00 58.44           N  
ATOM    593  CA  LEU A 777      57.254  -4.466 -30.197  1.00 50.49           C  
ATOM    594  C   LEU A 777      57.659  -5.920 -30.388  1.00 44.32           C  
ATOM    595  O   LEU A 777      58.526  -6.198 -31.192  1.00 58.48           O  
ATOM    596  CB  LEU A 777      56.801  -3.924 -31.540  1.00 41.25           C  
ATOM    597  CG  LEU A 777      55.841  -4.839 -32.300  1.00 57.57           C  
ATOM    598  CD1 LEU A 777      54.458  -4.800 -31.676  1.00 53.91           C  
ATOM    599  CD2 LEU A 777      55.774  -4.391 -33.735  1.00 51.18           C  
ATOM    600  N   LEU A 778      57.036  -6.852 -29.683  1.00 43.74           N  
ATOM    601  CA  LEU A 778      57.408  -8.246 -29.862  1.00 44.72           C  
ATOM    602  C   LEU A 778      56.762  -8.833 -31.108  1.00 43.69           C  
ATOM    603  O   LEU A 778      57.402  -9.545 -31.880  1.00 36.74           O  
ATOM    604  CB  LEU A 778      57.040  -9.028 -28.612  1.00 54.79           C  
ATOM    605  CG  LEU A 778      57.708  -8.280 -27.448  1.00 57.83           C  
ATOM    606  CD1 LEU A 778      57.234  -8.797 -26.136  1.00 58.51           C  
ATOM    607  CD2 LEU A 778      59.211  -8.425 -27.555  1.00 55.50           C  
ATOM    608  N   GLY A 779      55.500  -8.509 -31.333  1.00 40.63           N  
ATOM    609  CA  GLY A 779      54.862  -9.025 -32.524  1.00 39.02           C  
ATOM    610  C   GLY A 779      53.419  -8.609 -32.606  1.00 45.34           C  
ATOM    611  O   GLY A 779      52.948  -7.758 -31.848  1.00 44.11           O  
ATOM    612  N   ILE A 780      52.727  -9.188 -33.571  1.00 45.11           N  
ATOM    613  CA  ILE A 780      51.311  -8.942 -33.739  1.00 43.87           C  
ATOM    614  C   ILE A 780      50.749 -10.324 -33.968  1.00 48.64           C  
ATOM    615  O   ILE A 780      51.464 -11.245 -34.389  1.00 38.11           O  
ATOM    616  CB  ILE A 780      50.969  -8.064 -34.974  1.00 50.51           C  
ATOM    617  CG1 ILE A 780      51.630  -8.635 -36.226  1.00 43.91           C  
ATOM    618  CG2 ILE A 780      51.367  -6.618 -34.727  1.00 37.76           C  
ATOM    619  CD1 ILE A 780      51.405  -7.779 -37.427  1.00 57.07           C  
ATOM    620  N   CYS A 781      49.475 -10.471 -33.641  1.00 51.54           N  
ATOM    621  CA  CYS A 781      48.782 -11.718 -33.834  1.00 54.57           C  
ATOM    622  C   CYS A 781      47.620 -11.270 -34.702  1.00 51.59           C  
ATOM    623  O   CYS A 781      46.939 -10.283 -34.377  1.00 48.96           O  
ATOM    624  CB  CYS A 781      48.306 -12.273 -32.492  1.00 60.13           C  
ATOM    625  SG  CYS A 781      47.526 -13.884 -32.642  1.00 64.71           S  
ATOM    626  N   LEU A 782      47.416 -11.967 -35.817  1.00 52.95           N  
ATOM    627  CA  LEU A 782      46.352 -11.605 -36.758  1.00 57.17           C  
ATOM    628  C   LEU A 782      45.034 -12.334 -36.578  1.00 56.89           C  
ATOM    629  O   LEU A 782      44.525 -12.949 -37.508  1.00 67.29           O  
ATOM    630  CB  LEU A 782      46.820 -11.817 -38.196  1.00 50.93           C  
ATOM    631  CG  LEU A 782      47.936 -10.916 -38.696  1.00 57.45           C  
ATOM    632  CD1 LEU A 782      48.075 -11.083 -40.195  1.00 75.26           C  
ATOM    633  CD2 LEU A 782      47.596  -9.482 -38.358  1.00 47.39           C  
ATOM    634  N   THR A 783      44.478 -12.267 -35.384  1.00 57.75           N  
ATOM    635  CA  THR A 783      43.210 -12.910 -35.121  1.00 62.53           C  
ATOM    636  C   THR A 783      42.128 -11.958 -35.620  1.00 70.00           C  
ATOM    637  O   THR A 783      42.437 -10.836 -36.010  1.00 59.78           O  
ATOM    638  CB  THR A 783      43.066 -13.165 -33.622  1.00 66.79           C  
ATOM    639  OG1 THR A 783      43.499 -12.003 -32.898  1.00 58.08           O  
ATOM    640  CG2 THR A 783      43.921 -14.371 -33.215  1.00 58.37           C  
ATOM    641  N   SER A 784      40.873 -12.401 -35.623  1.00 76.54           N  
ATOM    642  CA  SER A 784      39.759 -11.566 -36.081  1.00 74.88           C  
ATOM    643  C   SER A 784      40.060 -10.123 -35.737  1.00 75.13           C  
ATOM    644  O   SER A 784      39.900  -9.220 -36.553  1.00 77.20           O  
ATOM    645  CB  SER A 784      38.488 -12.002 -35.389  1.00 70.51           C  
ATOM    646  OG  SER A 784      38.551 -13.399 -35.187  1.00 82.33           O  
ATOM    647  N   THR A 785      40.491  -9.910 -34.505  1.00 84.82           N  
ATOM    648  CA  THR A 785      40.874  -8.576 -34.082  1.00 89.23           C  
ATOM    649  C   THR A 785      42.390  -8.629 -33.936  1.00 84.80           C  
ATOM    650  O   THR A 785      42.940  -9.576 -33.365  1.00 80.25           O  
ATOM    651  CB  THR A 785      40.242  -8.187 -32.742  1.00 92.31           C  
ATOM    652  OG1 THR A 785      40.642  -6.850 -32.413  1.00105.05           O  
ATOM    653  CG2 THR A 785      40.678  -9.140 -31.638  1.00 81.87           C  
ATOM    654  N   VAL A 786      43.068  -7.622 -34.466  1.00 77.61           N  
ATOM    655  CA  VAL A 786      44.520  -7.601 -34.398  1.00 79.62           C  
ATOM    656  C   VAL A 786      45.015  -7.315 -32.979  1.00 76.14           C  
ATOM    657  O   VAL A 786      44.428  -6.512 -32.252  1.00 74.91           O  
ATOM    658  CB  VAL A 786      45.088  -6.555 -35.377  1.00 70.86           C  
ATOM    659  CG1 VAL A 786      46.590  -6.758 -35.570  1.00 58.25           C  
ATOM    660  CG2 VAL A 786      44.363  -6.672 -36.697  1.00 61.87           C  
ATOM    661  N   GLN A 787      46.088  -7.996 -32.589  1.00 66.96           N  
ATOM    662  CA  GLN A 787      46.655  -7.807 -31.270  1.00 58.05           C  
ATOM    663  C   GLN A 787      48.110  -7.395 -31.352  1.00 61.10           C  
ATOM    664  O   GLN A 787      48.897  -8.007 -32.081  1.00 49.50           O  
ATOM    665  CB  GLN A 787      46.562  -9.096 -30.466  1.00 53.99           C  
ATOM    666  CG  GLN A 787      45.149  -9.593 -30.249  1.00 49.52           C  
ATOM    667  CD  GLN A 787      45.120 -10.808 -29.371  1.00 56.57           C  
ATOM    668  OE1 GLN A 787      45.184 -10.702 -28.148  1.00 64.69           O  
ATOM    669  NE2 GLN A 787      45.054 -11.985 -29.987  1.00 61.37           N  
ATOM    670  N   LEU A 788      48.454  -6.344 -30.615  1.00 58.49           N  
ATOM    671  CA  LEU A 788      49.833  -5.878 -30.535  1.00 51.77           C  
ATOM    672  C   LEU A 788      50.501  -6.463 -29.293  1.00 48.44           C  
ATOM    673  O   LEU A 788      49.991  -6.305 -28.184  1.00 58.08           O  
ATOM    674  CB  LEU A 788      49.888  -4.361 -30.426  1.00 61.95           C  
ATOM    675  CG  LEU A 788      49.745  -3.573 -31.713  1.00 68.10           C  
ATOM    676  CD1 LEU A 788      50.447  -2.237 -31.556  1.00 65.93           C  
ATOM    677  CD2 LEU A 788      50.390  -4.347 -32.842  1.00 83.03           C  
ATOM    678  N   ILE A 789      51.630  -7.139 -29.462  1.00 53.46           N  
ATOM    679  CA  ILE A 789      52.338  -7.696 -28.307  1.00 47.12           C  
ATOM    680  C   ILE A 789      53.626  -6.889 -28.049  1.00 47.65           C  
ATOM    681  O   ILE A 789      54.550  -6.856 -28.878  1.00 41.63           O  
ATOM    682  CB  ILE A 789      52.728  -9.162 -28.531  1.00 52.02           C  
ATOM    683  CG1 ILE A 789      51.588  -9.903 -29.227  1.00 56.90           C  
ATOM    684  CG2 ILE A 789      53.037  -9.822 -27.184  1.00 39.99           C  
ATOM    685  CD1 ILE A 789      50.384 -10.125 -28.348  1.00 51.21           C  
ATOM    686  N   THR A 790      53.673  -6.236 -26.897  1.00 40.11           N  
ATOM    687  CA  THR A 790      54.829  -5.445 -26.533  1.00 41.18           C  
ATOM    688  C   THR A 790      55.326  -5.896 -25.187  1.00 37.61           C  
ATOM    689  O   THR A 790      54.666  -6.660 -24.502  1.00 43.22           O  
ATOM    690  CB  THR A 790      54.467  -3.996 -26.410  1.00 41.85           C  
ATOM    691  OG1 THR A 790      53.353  -3.874 -25.520  1.00 45.39           O  
ATOM    692  CG2 THR A 790      54.122  -3.422 -27.764  1.00 39.41           C  
ATOM    693  N   GLN A 791      56.498  -5.417 -24.809  1.00 38.02           N  
ATOM    694  CA  GLN A 791      57.067  -5.761 -23.517  1.00 31.97           C  
ATOM    695  C   GLN A 791      56.185  -5.184 -22.422  1.00 41.69           C  
ATOM    696  O   GLN A 791      55.678  -4.054 -22.527  1.00 31.90           O  
ATOM    697  CB  GLN A 791      58.472  -5.170 -23.396  1.00 38.73           C  
ATOM    698  CG  GLN A 791      59.070  -5.217 -22.006  1.00 53.08           C  
ATOM    699  CD  GLN A 791      60.443  -4.580 -21.960  1.00 57.36           C  
ATOM    700  OE1 GLN A 791      60.712  -3.610 -22.675  1.00 57.61           O  
ATOM    701  NE2 GLN A 791      61.315  -5.111 -21.112  1.00 50.07           N  
ATOM    702  N   LEU A 792      55.987  -5.969 -21.374  1.00 43.12           N  
ATOM    703  CA  LEU A 792      55.190  -5.513 -20.249  1.00 39.98           C  
ATOM    704  C   LEU A 792      55.970  -4.470 -19.448  1.00 40.89           C  
ATOM    705  O   LEU A 792      57.096  -4.726 -19.046  1.00 38.88           O  
ATOM    706  CB  LEU A 792      54.848  -6.690 -19.342  1.00 25.93           C  
ATOM    707  CG  LEU A 792      54.051  -6.279 -18.093  1.00 49.20           C  
ATOM    708  CD1 LEU A 792      52.731  -5.575 -18.477  1.00 30.16           C  
ATOM    709  CD2 LEU A 792      53.787  -7.517 -17.261  1.00 31.76           C  
ATOM    710  N   MET A 793      55.391  -3.290 -19.245  1.00 37.32           N  
ATOM    711  CA  MET A 793      56.054  -2.262 -18.459  1.00 37.07           C  
ATOM    712  C   MET A 793      55.255  -2.257 -17.150  1.00 37.65           C  
ATOM    713  O   MET A 793      54.247  -1.564 -17.014  1.00 44.53           O  
ATOM    714  CB  MET A 793      55.982  -0.917 -19.190  1.00 36.38           C  
ATOM    715  CG  MET A 793      56.746  -0.882 -20.513  1.00 41.84           C  
ATOM    716  SD  MET A 793      58.506  -1.342 -20.412  1.00 42.40           S  
ATOM    717  CE  MET A 793      59.238   0.280 -20.281  1.00 41.12           C  
ATOM    718  N   PRO A 794      55.721  -3.018 -16.157  1.00 39.37           N  
ATOM    719  CA  PRO A 794      55.061  -3.152 -14.851  1.00 38.58           C  
ATOM    720  C   PRO A 794      54.511  -1.928 -14.133  1.00 44.38           C  
ATOM    721  O   PRO A 794      53.384  -1.971 -13.646  1.00 53.90           O  
ATOM    722  CB  PRO A 794      56.100  -3.891 -13.999  1.00 32.74           C  
ATOM    723  CG  PRO A 794      56.984  -4.585 -15.008  1.00 35.80           C  
ATOM    724  CD  PRO A 794      57.098  -3.544 -16.096  1.00 38.80           C  
ATOM    725  N   PHE A 795      55.269  -0.839 -14.067  1.00 51.40           N  
ATOM    726  CA  PHE A 795      54.801   0.342 -13.332  1.00 39.66           C  
ATOM    727  C   PHE A 795      53.960   1.360 -14.089  1.00 40.27           C  
ATOM    728  O   PHE A 795      53.761   2.481 -13.627  1.00 48.98           O  
ATOM    729  CB  PHE A 795      55.993   1.003 -12.647  1.00 46.55           C  
ATOM    730  CG  PHE A 795      56.825   0.028 -11.815  1.00 54.66           C  
ATOM    731  CD1 PHE A 795      57.772  -0.803 -12.413  1.00 54.50           C  
ATOM    732  CD2 PHE A 795      56.644  -0.066 -10.440  1.00 35.52           C  
ATOM    733  CE1 PHE A 795      58.521  -1.709 -11.648  1.00 48.96           C  
ATOM    734  CE2 PHE A 795      57.386  -0.960  -9.675  1.00 32.44           C  
ATOM    735  CZ  PHE A 795      58.328  -1.785 -10.281  1.00 35.70           C  
ATOM    736  N   GLY A 796      53.452   0.952 -15.251  1.00 44.48           N  
ATOM    737  CA  GLY A 796      52.589   1.816 -16.043  1.00 34.93           C  
ATOM    738  C   GLY A 796      53.186   3.090 -16.591  1.00 38.20           C  
ATOM    739  O   GLY A 796      54.415   3.229 -16.632  1.00 44.53           O  
ATOM    740  N   CYS A 797      52.315   4.013 -17.021  1.00 41.66           N  
ATOM    741  CA  CYS A 797      52.768   5.282 -17.576  1.00 48.19           C  
ATOM    742  C   CYS A 797      53.409   6.133 -16.483  1.00 57.39           C  
ATOM    743  O   CYS A 797      52.986   6.099 -15.328  1.00 63.27           O  
ATOM    744  CB  CYS A 797      51.615   6.038 -18.255  1.00 38.97           C  
ATOM    745  SG  CYS A 797      50.290   6.598 -17.222  1.00 50.34           S  
ATOM    746  N   LEU A 798      54.437   6.887 -16.864  1.00 50.66           N  
ATOM    747  CA  LEU A 798      55.181   7.709 -15.936  1.00 45.21           C  
ATOM    748  C   LEU A 798      54.351   8.836 -15.338  1.00 48.72           C  
ATOM    749  O   LEU A 798      54.605   9.263 -14.208  1.00 50.27           O  
ATOM    750  CB  LEU A 798      56.436   8.264 -16.629  1.00 44.59           C  
ATOM    751  CG  LEU A 798      57.498   8.962 -15.769  1.00 41.72           C  
ATOM    752  CD1 LEU A 798      58.037   7.965 -14.786  1.00 37.67           C  
ATOM    753  CD2 LEU A 798      58.628   9.495 -16.633  1.00 42.68           C  
ATOM    754  N   LEU A 799      53.356   9.323 -16.073  1.00 50.30           N  
ATOM    755  CA  LEU A 799      52.544  10.399 -15.519  1.00 45.58           C  
ATOM    756  C   LEU A 799      51.827   9.919 -14.272  1.00 56.01           C  
ATOM    757  O   LEU A 799      51.806  10.620 -13.266  1.00 63.77           O  
ATOM    758  CB  LEU A 799      51.510  10.920 -16.514  1.00 36.27           C  
ATOM    759  CG  LEU A 799      50.576  11.968 -15.864  1.00 44.91           C  
ATOM    760  CD1 LEU A 799      51.420  13.109 -15.330  1.00 40.81           C  
ATOM    761  CD2 LEU A 799      49.552  12.515 -16.859  1.00 29.96           C  
ATOM    762  N   ASP A 800      51.237   8.725 -14.336  1.00 52.45           N  
ATOM    763  CA  ASP A 800      50.524   8.192 -13.181  1.00 53.60           C  
ATOM    764  C   ASP A 800      51.512   7.843 -12.103  1.00 50.60           C  
ATOM    765  O   ASP A 800      51.195   7.905 -10.923  1.00 70.55           O  
ATOM    766  CB  ASP A 800      49.748   6.914 -13.520  1.00 54.30           C  
ATOM    767  CG  ASP A 800      48.432   7.184 -14.221  1.00 65.31           C  
ATOM    768  OD1 ASP A 800      47.654   6.216 -14.381  1.00 79.53           O  
ATOM    769  OD2 ASP A 800      48.167   8.342 -14.614  1.00 59.33           O  
ATOM    770  N   TYR A 801      52.723   7.488 -12.504  1.00 48.60           N  
ATOM    771  CA  TYR A 801      53.720   7.074 -11.534  1.00 47.87           C  
ATOM    772  C   TYR A 801      54.344   8.168 -10.686  1.00 57.62           C  
ATOM    773  O   TYR A 801      54.689   7.912  -9.530  1.00 50.96           O  
ATOM    774  CB  TYR A 801      54.802   6.270 -12.218  1.00 39.05           C  
ATOM    775  CG  TYR A 801      55.844   5.734 -11.288  1.00 43.15           C  
ATOM    776  CD1 TYR A 801      56.897   6.541 -10.843  1.00 60.74           C  
ATOM    777  CD2 TYR A 801      55.815   4.412 -10.886  1.00 44.76           C  
ATOM    778  CE1 TYR A 801      57.898   6.040 -10.028  1.00 38.86           C  
ATOM    779  CE2 TYR A 801      56.797   3.900 -10.072  1.00 48.24           C  
ATOM    780  CZ  TYR A 801      57.838   4.715  -9.648  1.00 49.99           C  
ATOM    781  OH  TYR A 801      58.829   4.186  -8.857  1.00 52.38           O  
ATOM    782  N   VAL A 802      54.514   9.374 -11.218  1.00 49.08           N  
ATOM    783  CA  VAL A 802      55.082  10.397 -10.359  1.00 53.95           C  
ATOM    784  C   VAL A 802      53.969  10.895  -9.456  1.00 55.37           C  
ATOM    785  O   VAL A 802      54.207  11.345  -8.334  1.00 59.36           O  
ATOM    786  CB  VAL A 802      55.658  11.568 -11.132  1.00 35.34           C  
ATOM    787  CG1 VAL A 802      56.814  11.090 -11.965  1.00 41.94           C  
ATOM    788  CG2 VAL A 802      54.580  12.208 -11.960  1.00 36.69           C  
ATOM    789  N   ARG A 803      52.742  10.792  -9.934  1.00 47.64           N  
ATOM    790  CA  ARG A 803      51.631  11.233  -9.125  1.00 50.16           C  
ATOM    791  C   ARG A 803      51.463  10.350  -7.917  1.00 56.99           C  
ATOM    792  O   ARG A 803      51.257  10.821  -6.797  1.00 60.26           O  
ATOM    793  CB  ARG A 803      50.365  11.202  -9.939  1.00 39.79           C  
ATOM    794  CG  ARG A 803      50.272  12.398 -10.822  1.00 49.93           C  
ATOM    795  CD  ARG A 803      49.043  12.312 -11.628  1.00 43.14           C  
ATOM    796  NE  ARG A 803      48.921  13.446 -12.519  1.00 47.91           N  
ATOM    797  CZ  ARG A 803      48.103  13.441 -13.556  1.00 51.46           C  
ATOM    798  NH1 ARG A 803      47.372  12.356 -13.793  1.00 56.69           N  
ATOM    799  NH2 ARG A 803      48.000  14.503 -14.335  1.00 39.15           N  
ATOM    800  N   GLU A 804      51.584   9.056  -8.150  1.00 60.87           N  
ATOM    801  CA  GLU A 804      51.392   8.085  -7.100  1.00 58.14           C  
ATOM    802  C   GLU A 804      52.570   7.869  -6.182  1.00 57.79           C  
ATOM    803  O   GLU A 804      52.455   7.147  -5.196  1.00 60.02           O  
ATOM    804  CB  GLU A 804      50.984   6.773  -7.728  1.00 62.13           C  
ATOM    805  CG  GLU A 804      50.665   5.684  -6.763  1.00 83.75           C  
ATOM    806  CD  GLU A 804      49.782   4.664  -7.410  1.00104.93           C  
ATOM    807  OE1 GLU A 804      49.969   3.459  -7.140  1.00114.94           O  
ATOM    808  OE2 GLU A 804      48.897   5.085  -8.195  1.00114.57           O  
ATOM    809  N   HIS A 805      53.707   8.480  -6.490  1.00 57.60           N  
ATOM    810  CA  HIS A 805      54.871   8.290  -5.635  1.00 58.23           C  
ATOM    811  C   HIS A 805      55.650   9.580  -5.324  1.00 54.88           C  
ATOM    812  O   HIS A 805      56.827   9.503  -4.983  1.00 66.59           O  
ATOM    813  CB  HIS A 805      55.830   7.239  -6.238  1.00 45.70           C  
ATOM    814  CG  HIS A 805      55.232   5.870  -6.423  1.00 64.42           C  
ATOM    815  ND1 HIS A 805      54.182   5.615  -7.284  1.00 78.12           N  
ATOM    816  CD2 HIS A 805      55.592   4.668  -5.913  1.00 61.77           C  
ATOM    817  CE1 HIS A 805      53.927   4.318  -7.299  1.00 63.58           C  
ATOM    818  NE2 HIS A 805      54.768   3.721  -6.476  1.00 53.91           N  
ATOM    819  N   LYS A 806      54.996  10.745  -5.407  1.00 63.21           N  
ATOM    820  CA  LYS A 806      55.651  12.041  -5.127  1.00 71.54           C  
ATOM    821  C   LYS A 806      56.518  12.066  -3.877  1.00 77.22           C  
ATOM    822  O   LYS A 806      57.557  12.737  -3.829  1.00 82.37           O  
ATOM    823  CB  LYS A 806      54.640  13.160  -4.910  1.00 69.65           C  
ATOM    824  CG  LYS A 806      53.427  13.145  -5.772  1.00 89.82           C  
ATOM    825  CD  LYS A 806      52.563  14.353  -5.428  1.00105.24           C  
ATOM    826  CE  LYS A 806      52.092  14.322  -3.968  1.00114.37           C  
ATOM    827  NZ  LYS A 806      50.597  14.364  -3.860  1.00108.34           N  
ATOM    828  N   ASP A 807      56.065  11.363  -2.848  1.00 68.46           N  
ATOM    829  CA  ASP A 807      56.777  11.360  -1.586  1.00 68.77           C  
ATOM    830  C   ASP A 807      57.935  10.375  -1.529  1.00 61.11           C  
ATOM    831  O   ASP A 807      58.468  10.076  -0.464  1.00 64.43           O  
ATOM    832  CB  ASP A 807      55.785  11.106  -0.445  1.00 81.15           C  
ATOM    833  CG  ASP A 807      54.534  11.996  -0.537  1.00 86.69           C  
ATOM    834  OD1 ASP A 807      54.669  13.210  -0.831  1.00 82.81           O  
ATOM    835  OD2 ASP A 807      53.414  11.479  -0.304  1.00 78.64           O  
ATOM    836  N   ASN A 808      58.339   9.870  -2.677  1.00 54.04           N  
ATOM    837  CA  ASN A 808      59.449   8.942  -2.683  1.00 57.15           C  
ATOM    838  C   ASN A 808      60.276   9.168  -3.915  1.00 54.21           C  
ATOM    839  O   ASN A 808      61.210   8.413  -4.192  1.00 49.35           O  
ATOM    840  CB  ASN A 808      58.941   7.506  -2.630  1.00 71.95           C  
ATOM    841  CG  ASN A 808      58.228   7.211  -1.345  1.00 80.92           C  
ATOM    842  OD1 ASN A 808      58.758   7.477  -0.265  1.00 83.93           O  
ATOM    843  ND2 ASN A 808      57.016   6.666  -1.441  1.00 86.89           N  
ATOM    844  N   ILE A 809      59.940  10.222  -4.654  1.00 54.30           N  
ATOM    845  CA  ILE A 809      60.686  10.528  -5.862  1.00 58.29           C  
ATOM    846  C   ILE A 809      61.738  11.592  -5.627  1.00 55.75           C  
ATOM    847  O   ILE A 809      61.413  12.748  -5.344  1.00 55.31           O  
ATOM    848  CB  ILE A 809      59.763  10.964  -6.999  1.00 58.85           C  
ATOM    849  CG1 ILE A 809      58.907   9.772  -7.435  1.00 54.27           C  
ATOM    850  CG2 ILE A 809      60.586  11.445  -8.170  1.00 55.22           C  
ATOM    851  CD1 ILE A 809      57.855  10.109  -8.448  1.00 48.62           C  
ATOM    852  N   GLY A 810      63.001  11.170  -5.742  1.00 55.19           N  
ATOM    853  CA  GLY A 810      64.127  12.061  -5.557  1.00 49.01           C  
ATOM    854  C   GLY A 810      64.694  12.625  -6.848  1.00 53.20           C  
ATOM    855  O   GLY A 810      64.411  12.138  -7.957  1.00 48.63           O  
ATOM    856  N   SER A 811      65.509  13.663  -6.687  1.00 37.89           N  
ATOM    857  CA  SER A 811      66.140  14.338  -7.801  1.00 42.40           C  
ATOM    858  C   SER A 811      66.941  13.375  -8.665  1.00 46.56           C  
ATOM    859  O   SER A 811      66.981  13.528  -9.890  1.00 50.14           O  
ATOM    860  CB  SER A 811      67.030  15.482  -7.291  1.00 33.74           C  
ATOM    861  OG  SER A 811      68.004  15.021  -6.381  1.00 47.17           O  
ATOM    862  N   GLN A 812      67.567  12.377  -8.043  1.00 46.21           N  
ATOM    863  CA  GLN A 812      68.357  11.404  -8.802  1.00 46.40           C  
ATOM    864  C   GLN A 812      67.494  10.717  -9.860  1.00 51.39           C  
ATOM    865  O   GLN A 812      67.943  10.448 -10.975  1.00 45.21           O  
ATOM    866  CB  GLN A 812      68.934  10.337  -7.886  1.00 38.35           C  
ATOM    867  CG  GLN A 812      69.824   9.383  -8.613  1.00 47.53           C  
ATOM    868  CD  GLN A 812      71.045  10.073  -9.223  1.00 71.40           C  
ATOM    869  OE1 GLN A 812      72.161   9.936  -8.722  1.00 78.11           O  
ATOM    870  NE2 GLN A 812      70.834  10.823 -10.306  1.00 67.34           N  
ATOM    871  N   TYR A 813      66.252  10.436  -9.494  1.00 36.18           N  
ATOM    872  CA  TYR A 813      65.323   9.800 -10.394  1.00 42.14           C  
ATOM    873  C   TYR A 813      64.830  10.731 -11.487  1.00 48.15           C  
ATOM    874  O   TYR A 813      64.882  10.414 -12.686  1.00 47.40           O  
ATOM    875  CB  TYR A 813      64.136   9.286  -9.607  1.00 50.88           C  
ATOM    876  CG  TYR A 813      64.425   7.974  -8.977  1.00 57.66           C  
ATOM    877  CD1 TYR A 813      64.724   6.876  -9.767  1.00 56.48           C  
ATOM    878  CD2 TYR A 813      64.359   7.805  -7.594  1.00 74.31           C  
ATOM    879  CE1 TYR A 813      64.942   5.636  -9.215  1.00 65.32           C  
ATOM    880  CE2 TYR A 813      64.577   6.562  -7.027  1.00 69.19           C  
ATOM    881  CZ  TYR A 813      64.866   5.481  -7.852  1.00 65.71           C  
ATOM    882  OH  TYR A 813      65.075   4.232  -7.330  1.00 84.04           O  
ATOM    883  N   LEU A 814      64.322  11.877 -11.062  1.00 40.26           N  
ATOM    884  CA  LEU A 814      63.826  12.848 -12.007  1.00 34.86           C  
ATOM    885  C   LEU A 814      64.855  13.125 -13.105  1.00 37.23           C  
ATOM    886  O   LEU A 814      64.531  13.068 -14.285  1.00 41.58           O  
ATOM    887  CB  LEU A 814      63.461  14.119 -11.259  1.00 26.14           C  
ATOM    888  CG  LEU A 814      62.180  13.906 -10.439  1.00 39.52           C  
ATOM    889  CD1 LEU A 814      61.918  15.114  -9.543  1.00 32.77           C  
ATOM    890  CD2 LEU A 814      60.998  13.677 -11.396  1.00 32.69           C  
ATOM    891  N   LEU A 815      66.099  13.387 -12.718  1.00 31.73           N  
ATOM    892  CA  LEU A 815      67.137  13.689 -13.687  1.00 30.35           C  
ATOM    893  C   LEU A 815      67.491  12.490 -14.558  1.00 36.50           C  
ATOM    894  O   LEU A 815      67.785  12.652 -15.741  1.00 40.25           O  
ATOM    895  CB  LEU A 815      68.374  14.273 -12.973  1.00 27.85           C  
ATOM    896  CG  LEU A 815      68.016  15.584 -12.227  1.00 36.20           C  
ATOM    897  CD1 LEU A 815      69.215  16.078 -11.463  1.00 31.57           C  
ATOM    898  CD2 LEU A 815      67.532  16.675 -13.207  1.00 35.77           C  
ATOM    899  N   ASN A 816      67.444  11.285 -14.000  1.00 33.46           N  
ATOM    900  CA  ASN A 816      67.752  10.106 -14.806  1.00 37.70           C  
ATOM    901  C   ASN A 816      66.680   9.909 -15.869  1.00 39.83           C  
ATOM    902  O   ASN A 816      66.979   9.556 -17.010  1.00 45.22           O  
ATOM    903  CB  ASN A 816      67.860   8.864 -13.930  1.00 29.46           C  
ATOM    904  CG  ASN A 816      69.161   8.825 -13.164  1.00 60.58           C  
ATOM    905  OD1 ASN A 816      69.246   8.219 -12.091  1.00 65.07           O  
ATOM    906  ND2 ASN A 816      70.195   9.467 -13.717  1.00 48.01           N  
ATOM    907  N   TRP A 817      65.430  10.140 -15.495  1.00 37.21           N  
ATOM    908  CA  TRP A 817      64.363  10.006 -16.457  1.00 41.91           C  
ATOM    909  C   TRP A 817      64.506  11.029 -17.586  1.00 47.65           C  
ATOM    910  O   TRP A 817      64.287  10.685 -18.757  1.00 42.92           O  
ATOM    911  CB  TRP A 817      63.017  10.169 -15.778  1.00 34.72           C  
ATOM    912  CG  TRP A 817      62.725   9.101 -14.800  1.00 35.13           C  
ATOM    913  CD1 TRP A 817      63.215   7.828 -14.803  1.00 28.07           C  
ATOM    914  CD2 TRP A 817      61.839   9.193 -13.681  1.00 17.71           C  
ATOM    915  NE1 TRP A 817      62.682   7.121 -13.749  1.00 38.98           N  
ATOM    916  CE2 TRP A 817      61.836   7.939 -13.047  1.00 29.46           C  
ATOM    917  CE3 TRP A 817      61.044  10.221 -13.155  1.00 37.45           C  
ATOM    918  CZ2 TRP A 817      61.067   7.679 -11.907  1.00 40.05           C  
ATOM    919  CZ3 TRP A 817      60.271   9.964 -12.018  1.00 31.36           C  
ATOM    920  CH2 TRP A 817      60.292   8.699 -11.409  1.00 36.18           C  
ATOM    921  N   CYS A 818      64.873  12.272 -17.244  1.00 37.89           N  
ATOM    922  CA  CYS A 818      65.050  13.312 -18.262  1.00 35.58           C  
ATOM    923  C   CYS A 818      66.145  12.881 -19.217  1.00 38.05           C  
ATOM    924  O   CYS A 818      66.058  13.149 -20.411  1.00 40.83           O  
ATOM    925  CB  CYS A 818      65.435  14.656 -17.646  1.00 27.33           C  
ATOM    926  SG  CYS A 818      64.135  15.349 -16.638  1.00 40.64           S  
ATOM    927  N   VAL A 819      67.166  12.211 -18.679  1.00 26.66           N  
ATOM    928  CA  VAL A 819      68.291  11.717 -19.473  1.00 28.94           C  
ATOM    929  C   VAL A 819      67.875  10.595 -20.414  1.00 33.27           C  
ATOM    930  O   VAL A 819      68.183  10.629 -21.604  1.00 43.60           O  
ATOM    931  CB  VAL A 819      69.437  11.179 -18.565  1.00 35.83           C  
ATOM    932  CG1 VAL A 819      70.538  10.495 -19.415  1.00 21.05           C  
ATOM    933  CG2 VAL A 819      70.019  12.324 -17.757  1.00 35.20           C  
ATOM    934  N   GLN A 820      67.178   9.598 -19.879  1.00 36.76           N  
ATOM    935  CA  GLN A 820      66.738   8.468 -20.690  1.00 38.16           C  
ATOM    936  C   GLN A 820      65.767   8.885 -21.775  1.00 40.77           C  
ATOM    937  O   GLN A 820      65.883   8.438 -22.932  1.00 34.10           O  
ATOM    938  CB  GLN A 820      66.109   7.402 -19.812  1.00 32.11           C  
ATOM    939  CG  GLN A 820      67.075   6.873 -18.779  1.00 31.63           C  
ATOM    940  CD  GLN A 820      66.462   5.800 -17.922  1.00 31.05           C  
ATOM    941  OE1 GLN A 820      65.264   5.519 -18.015  1.00 55.32           O  
ATOM    942  NE2 GLN A 820      67.271   5.192 -17.080  1.00 31.33           N  
ATOM    943  N   ILE A 821      64.817   9.745 -21.413  1.00 31.00           N  
ATOM    944  CA  ILE A 821      63.867  10.213 -22.403  1.00 27.26           C  
ATOM    945  C   ILE A 821      64.616  10.948 -23.530  1.00 41.14           C  
ATOM    946  O   ILE A 821      64.306  10.744 -24.702  1.00 41.27           O  
ATOM    947  CB  ILE A 821      62.801  11.111 -21.775  1.00 33.18           C  
ATOM    948  CG1 ILE A 821      61.929  10.255 -20.845  1.00 31.72           C  
ATOM    949  CG2 ILE A 821      61.974  11.805 -22.884  1.00 21.17           C  
ATOM    950  CD1 ILE A 821      61.142  11.023 -19.834  1.00 35.61           C  
ATOM    951  N   ALA A 822      65.605  11.781 -23.197  1.00 33.85           N  
ATOM    952  CA  ALA A 822      66.361  12.462 -24.250  1.00 32.11           C  
ATOM    953  C   ALA A 822      67.117  11.422 -25.093  1.00 29.88           C  
ATOM    954  O   ALA A 822      67.228  11.580 -26.291  1.00 33.66           O  
ATOM    955  CB  ALA A 822      67.355  13.489 -23.659  1.00 20.82           C  
ATOM    956  N   LYS A 823      67.643  10.363 -24.481  1.00 30.20           N  
ATOM    957  CA  LYS A 823      68.351   9.351 -25.271  1.00 27.61           C  
ATOM    958  C   LYS A 823      67.381   8.692 -26.223  1.00 35.62           C  
ATOM    959  O   LYS A 823      67.711   8.453 -27.382  1.00 42.57           O  
ATOM    960  CB  LYS A 823      68.952   8.275 -24.389  1.00 23.08           C  
ATOM    961  CG  LYS A 823      70.185   8.732 -23.679  1.00 25.75           C  
ATOM    962  CD  LYS A 823      70.797   7.638 -22.823  1.00 21.21           C  
ATOM    963  CE  LYS A 823      72.062   8.187 -22.184  1.00 37.52           C  
ATOM    964  NZ  LYS A 823      72.885   7.111 -21.659  1.00 30.16           N  
ATOM    965  N   GLY A 824      66.185   8.387 -25.724  1.00 36.00           N  
ATOM    966  CA  GLY A 824      65.183   7.775 -26.572  1.00 26.55           C  
ATOM    967  C   GLY A 824      64.903   8.663 -27.771  1.00 40.54           C  
ATOM    968  O   GLY A 824      65.051   8.243 -28.925  1.00 40.40           O  
ATOM    969  N   MET A 825      64.500   9.902 -27.498  1.00 41.03           N  
ATOM    970  CA  MET A 825      64.196  10.860 -28.552  1.00 47.18           C  
ATOM    971  C   MET A 825      65.369  11.127 -29.484  1.00 42.30           C  
ATOM    972  O   MET A 825      65.174  11.306 -30.681  1.00 49.62           O  
ATOM    973  CB  MET A 825      63.709  12.173 -27.955  1.00 41.20           C  
ATOM    974  CG  MET A 825      62.446  12.019 -27.110  1.00 30.76           C  
ATOM    975  SD  MET A 825      61.074  11.322 -28.036  1.00 37.04           S  
ATOM    976  CE  MET A 825      60.858  12.504 -29.319  1.00 22.43           C  
ATOM    977  N   ASN A 826      66.588  11.141 -28.962  1.00 35.82           N  
ATOM    978  CA  ASN A 826      67.739  11.381 -29.831  1.00 39.91           C  
ATOM    979  C   ASN A 826      67.924  10.210 -30.773  1.00 44.50           C  
ATOM    980  O   ASN A 826      68.393  10.364 -31.901  1.00 47.62           O  
ATOM    981  CB  ASN A 826      69.010  11.544 -29.040  1.00 30.31           C  
ATOM    982  CG  ASN A 826      70.201  11.786 -29.933  1.00 43.91           C  
ATOM    983  OD1 ASN A 826      70.306  12.833 -30.580  1.00 33.79           O  
ATOM    984  ND2 ASN A 826      71.108  10.816 -29.983  1.00 22.80           N  
ATOM    985  N   TYR A 827      67.580   9.024 -30.289  1.00 40.80           N  
ATOM    986  CA  TYR A 827      67.669   7.836 -31.114  1.00 45.17           C  
ATOM    987  C   TYR A 827      66.621   7.973 -32.222  1.00 53.70           C  
ATOM    988  O   TYR A 827      66.910   7.728 -33.404  1.00 37.31           O  
ATOM    989  CB  TYR A 827      67.366   6.587 -30.292  1.00 35.99           C  
ATOM    990  CG  TYR A 827      67.087   5.384 -31.155  1.00 42.76           C  
ATOM    991  CD1 TYR A 827      68.133   4.622 -31.690  1.00 33.04           C  
ATOM    992  CD2 TYR A 827      65.774   5.029 -31.476  1.00 32.62           C  
ATOM    993  CE1 TYR A 827      67.876   3.534 -32.517  1.00 38.51           C  
ATOM    994  CE2 TYR A 827      65.509   3.944 -32.311  1.00 47.55           C  
ATOM    995  CZ  TYR A 827      66.561   3.200 -32.826  1.00 39.17           C  
ATOM    996  OH  TYR A 827      66.293   2.125 -33.643  1.00 43.91           O  
ATOM    997  N   LEU A 828      65.403   8.352 -31.832  1.00 46.58           N  
ATOM    998  CA  LEU A 828      64.328   8.517 -32.801  1.00 48.25           C  
ATOM    999  C   LEU A 828      64.750   9.530 -33.872  1.00 47.15           C  
ATOM   1000  O   LEU A 828      64.515   9.303 -35.041  1.00 46.66           O  
ATOM   1001  CB  LEU A 828      63.024   8.939 -32.089  1.00 38.99           C  
ATOM   1002  CG  LEU A 828      62.492   7.849 -31.136  1.00 39.60           C  
ATOM   1003  CD1 LEU A 828      61.188   8.233 -30.474  1.00 29.69           C  
ATOM   1004  CD2 LEU A 828      62.265   6.608 -31.937  1.00 38.57           C  
ATOM   1005  N   GLU A 829      65.405  10.622 -33.480  1.00 54.19           N  
ATOM   1006  CA  GLU A 829      65.851  11.630 -34.454  1.00 56.76           C  
ATOM   1007  C   GLU A 829      66.896  11.046 -35.402  1.00 53.61           C  
ATOM   1008  O   GLU A 829      66.950  11.395 -36.588  1.00 52.18           O  
ATOM   1009  CB  GLU A 829      66.430  12.864 -33.752  1.00 60.37           C  
ATOM   1010  CG  GLU A 829      67.061  13.864 -34.698  1.00 47.19           C  
ATOM   1011  CD  GLU A 829      67.422  15.169 -34.026  1.00 59.38           C  
ATOM   1012  OE1 GLU A 829      68.125  15.990 -34.652  1.00 56.21           O  
ATOM   1013  OE2 GLU A 829      67.001  15.381 -32.871  1.00 65.29           O  
ATOM   1014  N   ASP A 830      67.746  10.176 -34.874  1.00 38.28           N  
ATOM   1015  CA  ASP A 830      68.728   9.530 -35.715  1.00 44.36           C  
ATOM   1016  C   ASP A 830      67.987   8.713 -36.775  1.00 43.83           C  
ATOM   1017  O   ASP A 830      68.353   8.744 -37.944  1.00 47.50           O  
ATOM   1018  CB  ASP A 830      69.629   8.624 -34.885  1.00 31.04           C  
ATOM   1019  CG  ASP A 830      70.773   9.375 -34.268  1.00 52.29           C  
ATOM   1020  OD1 ASP A 830      71.596   8.749 -33.569  1.00 62.98           O  
ATOM   1021  OD2 ASP A 830      70.855  10.602 -34.490  1.00 59.81           O  
ATOM   1022  N   ARG A 831      66.929   8.014 -36.363  1.00 40.76           N  
ATOM   1023  CA  ARG A 831      66.143   7.184 -37.271  1.00 40.67           C  
ATOM   1024  C   ARG A 831      65.189   8.027 -38.092  1.00 40.37           C  
ATOM   1025  O   ARG A 831      64.207   7.515 -38.624  1.00 53.37           O  
ATOM   1026  CB  ARG A 831      65.355   6.120 -36.481  1.00 33.13           C  
ATOM   1027  CG  ARG A 831      66.245   5.003 -35.871  1.00 48.86           C  
ATOM   1028  CD  ARG A 831      66.870   4.168 -36.970  1.00 74.18           C  
ATOM   1029  NE  ARG A 831      65.956   4.087 -38.113  1.00 90.98           N  
ATOM   1030  CZ  ARG A 831      64.746   3.527 -38.086  1.00 81.58           C  
ATOM   1031  NH1 ARG A 831      64.292   2.974 -36.973  1.00 87.79           N  
ATOM   1032  NH2 ARG A 831      63.969   3.566 -39.163  1.00 77.98           N  
ATOM   1033  N   ARG A 832      65.484   9.323 -38.184  1.00 55.81           N  
ATOM   1034  CA  ARG A 832      64.662  10.275 -38.939  1.00 56.85           C  
ATOM   1035  C   ARG A 832      63.172  10.112 -38.623  1.00 55.70           C  
ATOM   1036  O   ARG A 832      62.319  10.199 -39.501  1.00 56.05           O  
ATOM   1037  CB  ARG A 832      64.877  10.099 -40.450  1.00 62.69           C  
ATOM   1038  CG  ARG A 832      66.279  10.428 -40.977  1.00 63.93           C  
ATOM   1039  CD  ARG A 832      66.325  10.224 -42.497  1.00 71.78           C  
ATOM   1040  NE  ARG A 832      65.329  11.066 -43.146  1.00 80.53           N  
ATOM   1041  CZ  ARG A 832      65.357  12.394 -43.117  1.00 86.51           C  
ATOM   1042  NH1 ARG A 832      66.337  13.025 -42.484  1.00 85.74           N  
ATOM   1043  NH2 ARG A 832      64.396  13.095 -43.693  1.00 90.66           N  
ATOM   1044  N   LEU A 833      62.857   9.891 -37.360  1.00 47.75           N  
ATOM   1045  CA  LEU A 833      61.478   9.717 -36.961  1.00 45.72           C  
ATOM   1046  C   LEU A 833      61.018  10.849 -36.023  1.00 45.39           C  
ATOM   1047  O   LEU A 833      61.747  11.237 -35.117  1.00 50.69           O  
ATOM   1048  CB  LEU A 833      61.371   8.358 -36.294  1.00 41.31           C  
ATOM   1049  CG  LEU A 833      60.047   7.639 -36.129  1.00 51.56           C  
ATOM   1050  CD1 LEU A 833      60.349   6.156 -36.031  1.00 65.40           C  
ATOM   1051  CD2 LEU A 833      59.327   8.118 -34.888  1.00 61.06           C  
ATOM   1052  N   VAL A 834      59.825  11.382 -36.267  1.00 35.10           N  
ATOM   1053  CA  VAL A 834      59.242  12.447 -35.466  1.00 23.23           C  
ATOM   1054  C   VAL A 834      58.062  11.856 -34.721  1.00 40.10           C  
ATOM   1055  O   VAL A 834      57.106  11.415 -35.344  1.00 53.14           O  
ATOM   1056  CB  VAL A 834      58.703  13.600 -36.344  1.00 36.58           C  
ATOM   1057  CG1 VAL A 834      57.988  14.591 -35.491  1.00 34.86           C  
ATOM   1058  CG2 VAL A 834      59.843  14.298 -37.077  1.00 30.46           C  
ATOM   1059  N   HIS A 835      58.112  11.896 -33.390  1.00 40.48           N  
ATOM   1060  CA  HIS A 835      57.081  11.307 -32.538  1.00 36.81           C  
ATOM   1061  C   HIS A 835      55.723  11.986 -32.541  1.00 39.90           C  
ATOM   1062  O   HIS A 835      54.698  11.310 -32.582  1.00 42.90           O  
ATOM   1063  CB  HIS A 835      57.600  11.219 -31.100  1.00 27.01           C  
ATOM   1064  CG  HIS A 835      56.725  10.421 -30.182  1.00 19.97           C  
ATOM   1065  ND1 HIS A 835      55.483  10.854 -29.766  1.00 28.52           N  
ATOM   1066  CD2 HIS A 835      56.926   9.221 -29.582  1.00 31.95           C  
ATOM   1067  CE1 HIS A 835      54.958   9.955 -28.946  1.00 32.94           C  
ATOM   1068  NE2 HIS A 835      55.812   8.953 -28.819  1.00 24.04           N  
ATOM   1069  N   ARG A 836      55.723  13.315 -32.484  1.00 44.45           N  
ATOM   1070  CA  ARG A 836      54.500  14.127 -32.470  1.00 44.22           C  
ATOM   1071  C   ARG A 836      53.547  13.960 -31.287  1.00 39.10           C  
ATOM   1072  O   ARG A 836      52.500  14.599 -31.256  1.00 45.05           O  
ATOM   1073  CB  ARG A 836      53.712  13.926 -33.762  1.00 45.75           C  
ATOM   1074  CG  ARG A 836      54.516  14.240 -34.999  1.00 48.18           C  
ATOM   1075  CD  ARG A 836      53.672  13.997 -36.231  1.00 51.56           C  
ATOM   1076  NE  ARG A 836      52.470  14.826 -36.226  1.00 60.81           N  
ATOM   1077  CZ  ARG A 836      51.231  14.356 -36.352  1.00 67.19           C  
ATOM   1078  NH1 ARG A 836      51.014  13.050 -36.494  1.00 45.53           N  
ATOM   1079  NH2 ARG A 836      50.202  15.197 -36.332  1.00 48.66           N  
ATOM   1080  N   ASP A 837      53.869  13.104 -30.326  1.00 38.97           N  
ATOM   1081  CA  ASP A 837      52.990  12.983 -29.174  1.00 34.39           C  
ATOM   1082  C   ASP A 837      53.719  12.644 -27.875  1.00 43.63           C  
ATOM   1083  O   ASP A 837      53.210  11.886 -27.035  1.00 33.08           O  
ATOM   1084  CB  ASP A 837      51.890  11.970 -29.435  1.00 29.55           C  
ATOM   1085  CG  ASP A 837      50.801  12.027 -28.380  1.00 47.86           C  
ATOM   1086  OD1 ASP A 837      50.635  13.096 -27.745  1.00 58.76           O  
ATOM   1087  OD2 ASP A 837      50.104  11.011 -28.188  1.00 48.39           O  
ATOM   1088  N   LEU A 838      54.902  13.239 -27.704  1.00 39.88           N  
ATOM   1089  CA  LEU A 838      55.712  13.019 -26.510  1.00 39.65           C  
ATOM   1090  C   LEU A 838      55.120  13.718 -25.298  1.00 41.11           C  
ATOM   1091  O   LEU A 838      54.899  14.927 -25.317  1.00 38.96           O  
ATOM   1092  CB  LEU A 838      57.131  13.528 -26.724  1.00 31.34           C  
ATOM   1093  CG  LEU A 838      58.055  13.459 -25.499  1.00 31.58           C  
ATOM   1094  CD1 LEU A 838      58.135  12.060 -24.944  1.00 22.93           C  
ATOM   1095  CD2 LEU A 838      59.420  13.900 -25.912  1.00 27.05           C  
ATOM   1096  N   ALA A 839      54.864  12.948 -24.247  1.00 33.13           N  
ATOM   1097  CA  ALA A 839      54.314  13.492 -23.020  1.00 34.40           C  
ATOM   1098  C   ALA A 839      54.469  12.447 -21.947  1.00 37.38           C  
ATOM   1099  O   ALA A 839      54.631  11.273 -22.239  1.00 36.39           O  
ATOM   1100  CB  ALA A 839      52.851  13.842 -23.186  1.00 25.23           C  
ATOM   1101  N   ALA A 840      54.400  12.876 -20.696  1.00 38.42           N  
ATOM   1102  CA  ALA A 840      54.566  11.960 -19.600  1.00 29.89           C  
ATOM   1103  C   ALA A 840      53.649  10.754 -19.682  1.00 45.18           C  
ATOM   1104  O   ALA A 840      54.046   9.647 -19.284  1.00 46.84           O  
ATOM   1105  CB  ALA A 840      54.367  12.681 -18.299  1.00 48.20           C  
ATOM   1106  N   ARG A 841      52.432  10.939 -20.195  1.00 40.55           N  
ATOM   1107  CA  ARG A 841      51.510   9.798 -20.270  1.00 45.48           C  
ATOM   1108  C   ARG A 841      52.039   8.791 -21.265  1.00 42.84           C  
ATOM   1109  O   ARG A 841      51.641   7.634 -21.248  1.00 45.81           O  
ATOM   1110  CB  ARG A 841      50.106  10.222 -20.704  1.00 43.00           C  
ATOM   1111  CG  ARG A 841      50.054  10.635 -22.146  1.00 39.97           C  
ATOM   1112  CD  ARG A 841      48.704  11.173 -22.570  1.00 41.37           C  
ATOM   1113  NE  ARG A 841      48.855  11.768 -23.895  1.00 62.34           N  
ATOM   1114  CZ  ARG A 841      49.073  13.063 -24.126  1.00 68.08           C  
ATOM   1115  NH1 ARG A 841      49.147  13.933 -23.124  1.00 58.64           N  
ATOM   1116  NH2 ARG A 841      49.266  13.484 -25.369  1.00 75.86           N  
ATOM   1117  N   ASN A 842      52.944   9.231 -22.132  1.00 36.07           N  
ATOM   1118  CA  ASN A 842      53.502   8.328 -23.123  1.00 35.01           C  
ATOM   1119  C   ASN A 842      54.901   7.799 -22.864  1.00 39.91           C  
ATOM   1120  O   ASN A 842      55.677   7.588 -23.803  1.00 33.76           O  
ATOM   1121  CB  ASN A 842      53.450   8.971 -24.503  1.00 46.23           C  
ATOM   1122  CG  ASN A 842      52.038   9.073 -25.027  1.00 49.82           C  
ATOM   1123  OD1 ASN A 842      51.200   8.231 -24.712  1.00 37.45           O  
ATOM   1124  ND2 ASN A 842      51.768  10.092 -25.837  1.00 50.78           N  
ATOM   1125  N   VAL A 843      55.228   7.581 -21.596  1.00 28.67           N  
ATOM   1126  CA  VAL A 843      56.532   7.031 -21.242  1.00 35.45           C  
ATOM   1127  C   VAL A 843      56.174   5.948 -20.240  1.00 39.73           C  
ATOM   1128  O   VAL A 843      55.408   6.185 -19.311  1.00 40.86           O  
ATOM   1129  CB  VAL A 843      57.466   8.124 -20.627  1.00 41.85           C  
ATOM   1130  CG1 VAL A 843      58.749   7.515 -20.119  1.00 30.28           C  
ATOM   1131  CG2 VAL A 843      57.796   9.168 -21.696  1.00 32.49           C  
ATOM   1132  N   LEU A 844      56.671   4.739 -20.447  1.00 35.48           N  
ATOM   1133  CA  LEU A 844      56.318   3.677 -19.527  1.00 37.08           C  
ATOM   1134  C   LEU A 844      57.469   3.350 -18.613  1.00 34.27           C  
ATOM   1135  O   LEU A 844      58.623   3.646 -18.921  1.00 36.10           O  
ATOM   1136  CB  LEU A 844      55.868   2.449 -20.313  1.00 41.07           C  
ATOM   1137  CG  LEU A 844      54.741   2.742 -21.320  1.00 46.18           C  
ATOM   1138  CD1 LEU A 844      54.551   1.524 -22.213  1.00 37.39           C  
ATOM   1139  CD2 LEU A 844      53.433   3.094 -20.603  1.00 41.64           C  
ATOM   1140  N   VAL A 845      57.149   2.748 -17.479  1.00 33.00           N  
ATOM   1141  CA  VAL A 845      58.167   2.407 -16.496  1.00 42.78           C  
ATOM   1142  C   VAL A 845      58.453   0.906 -16.442  1.00 47.97           C  
ATOM   1143  O   VAL A 845      57.581   0.106 -16.091  1.00 49.64           O  
ATOM   1144  CB  VAL A 845      57.732   2.894 -15.092  1.00 44.14           C  
ATOM   1145  CG1 VAL A 845      58.826   2.613 -14.077  1.00 29.31           C  
ATOM   1146  CG2 VAL A 845      57.401   4.376 -15.145  1.00 27.61           C  
ATOM   1147  N   LYS A 846      59.666   0.515 -16.814  1.00 42.02           N  
ATOM   1148  CA  LYS A 846      60.032  -0.893 -16.752  1.00 41.89           C  
ATOM   1149  C   LYS A 846      60.369  -1.122 -15.286  1.00 42.93           C  
ATOM   1150  O   LYS A 846      59.912  -2.080 -14.671  1.00 44.22           O  
ATOM   1151  CB  LYS A 846      61.245  -1.175 -17.603  1.00 38.99           C  
ATOM   1152  CG  LYS A 846      61.581  -2.629 -17.676  1.00 28.46           C  
ATOM   1153  CD  LYS A 846      62.914  -2.790 -18.381  1.00 35.51           C  
ATOM   1154  CE  LYS A 846      63.324  -4.239 -18.326  1.00 40.07           C  
ATOM   1155  NZ  LYS A 846      64.770  -4.402 -18.562  1.00 50.06           N  
ATOM   1156  N   THR A 847      61.194  -0.226 -14.755  1.00 44.91           N  
ATOM   1157  CA  THR A 847      61.581  -0.199 -13.349  1.00 48.35           C  
ATOM   1158  C   THR A 847      61.689   1.290 -13.071  1.00 51.23           C  
ATOM   1159  O   THR A 847      61.706   2.117 -13.989  1.00 57.38           O  
ATOM   1160  CB  THR A 847      62.975  -0.792 -13.039  1.00 45.86           C  
ATOM   1161  OG1 THR A 847      63.983   0.094 -13.533  1.00 54.42           O  
ATOM   1162  CG2 THR A 847      63.151  -2.159 -13.657  1.00 35.53           C  
ATOM   1163  N   PRO A 848      61.775   1.656 -11.799  1.00 49.01           N  
ATOM   1164  CA  PRO A 848      61.884   3.076 -11.470  1.00 44.57           C  
ATOM   1165  C   PRO A 848      63.185   3.675 -12.016  1.00 46.71           C  
ATOM   1166  O   PRO A 848      63.316   4.890 -12.159  1.00 51.15           O  
ATOM   1167  CB  PRO A 848      61.822   3.067  -9.947  1.00 45.59           C  
ATOM   1168  CG  PRO A 848      60.962   1.875  -9.660  1.00 49.86           C  
ATOM   1169  CD  PRO A 848      61.549   0.852 -10.591  1.00 46.89           C  
ATOM   1170  N   GLN A 849      64.144   2.812 -12.327  1.00 39.69           N  
ATOM   1171  CA  GLN A 849      65.423   3.251 -12.866  1.00 42.10           C  
ATOM   1172  C   GLN A 849      65.471   3.120 -14.390  1.00 47.54           C  
ATOM   1173  O   GLN A 849      66.501   3.425 -14.997  1.00 43.75           O  
ATOM   1174  CB  GLN A 849      66.582   2.404 -12.312  1.00 37.98           C  
ATOM   1175  CG  GLN A 849      66.754   2.367 -10.802  1.00 73.54           C  
ATOM   1176  CD  GLN A 849      65.816   1.377 -10.134  1.00 89.80           C  
ATOM   1177  OE1 GLN A 849      65.495   0.325 -10.697  1.00 96.10           O  
ATOM   1178  NE2 GLN A 849      65.384   1.698  -8.920  1.00100.56           N  
ATOM   1179  N   HIS A 850      64.387   2.671 -15.021  1.00 35.87           N  
ATOM   1180  CA  HIS A 850      64.465   2.473 -16.467  1.00 42.74           C  
ATOM   1181  C   HIS A 850      63.171   2.738 -17.193  1.00 34.07           C  
ATOM   1182  O   HIS A 850      62.288   1.897 -17.189  1.00 30.56           O  
ATOM   1183  CB  HIS A 850      64.926   1.041 -16.756  1.00 22.22           C  
ATOM   1184  CG  HIS A 850      65.141   0.763 -18.206  1.00 36.68           C  
ATOM   1185  ND1 HIS A 850      65.869  -0.321 -18.654  1.00 41.22           N  
ATOM   1186  CD2 HIS A 850      64.803   1.470 -19.309  1.00 30.53           C  
ATOM   1187  CE1 HIS A 850      65.983  -0.260 -19.970  1.00 28.02           C  
ATOM   1188  NE2 HIS A 850      65.347   0.819 -20.391  1.00 46.35           N  
ATOM   1189  N   VAL A 851      63.073   3.892 -17.838  1.00 23.57           N  
ATOM   1190  CA  VAL A 851      61.852   4.248 -18.553  1.00 30.15           C  
ATOM   1191  C   VAL A 851      62.035   4.163 -20.072  1.00 27.25           C  
ATOM   1192  O   VAL A 851      63.157   4.193 -20.559  1.00 35.71           O  
ATOM   1193  CB  VAL A 851      61.391   5.675 -18.150  1.00 28.15           C  
ATOM   1194  CG1 VAL A 851      61.224   5.742 -16.653  1.00 20.88           C  
ATOM   1195  CG2 VAL A 851      62.412   6.718 -18.605  1.00 22.89           C  
ATOM   1196  N   LYS A 852      60.937   4.034 -20.809  1.00 30.61           N  
ATOM   1197  CA  LYS A 852      60.987   3.959 -22.278  1.00 30.29           C  
ATOM   1198  C   LYS A 852      59.848   4.725 -22.902  1.00 27.24           C  
ATOM   1199  O   LYS A 852      58.759   4.807 -22.336  1.00 38.19           O  
ATOM   1200  CB  LYS A 852      60.883   2.526 -22.771  1.00 31.56           C  
ATOM   1201  CG  LYS A 852      61.888   1.599 -22.174  1.00 40.76           C  
ATOM   1202  CD  LYS A 852      61.755   0.239 -22.815  1.00 28.59           C  
ATOM   1203  CE  LYS A 852      62.838  -0.670 -22.277  1.00 38.44           C  
ATOM   1204  NZ  LYS A 852      62.916  -1.942 -23.039  1.00 32.13           N  
ATOM   1205  N   ILE A 853      60.095   5.263 -24.086  1.00 30.59           N  
ATOM   1206  CA  ILE A 853      59.091   6.033 -24.805  1.00 31.85           C  
ATOM   1207  C   ILE A 853      58.106   5.137 -25.541  1.00 38.45           C  
ATOM   1208  O   ILE A 853      58.487   4.108 -26.088  1.00 44.37           O  
ATOM   1209  CB  ILE A 853      59.769   6.951 -25.788  1.00 39.90           C  
ATOM   1210  CG1 ILE A 853      60.553   8.013 -24.999  1.00 26.96           C  
ATOM   1211  CG2 ILE A 853      58.744   7.509 -26.769  1.00 32.06           C  
ATOM   1212  CD1 ILE A 853      61.692   8.632 -25.796  1.00 33.21           C  
ATOM   1213  N   THR A 854      56.840   5.528 -25.563  1.00 34.04           N  
ATOM   1214  CA  THR A 854      55.846   4.700 -26.225  1.00 43.08           C  
ATOM   1215  C   THR A 854      54.820   5.506 -27.008  1.00 46.81           C  
ATOM   1216  O   THR A 854      55.015   6.700 -27.279  1.00 44.25           O  
ATOM   1217  CB  THR A 854      55.105   3.787 -25.189  1.00 44.40           C  
ATOM   1218  OG1 THR A 854      54.248   2.867 -25.877  1.00 48.60           O  
ATOM   1219  CG2 THR A 854      54.253   4.624 -24.232  1.00 49.14           C  
ATOM   1220  N   ASP A 855      53.739   4.818 -27.367  1.00 43.22           N  
ATOM   1221  CA  ASP A 855      52.617   5.366 -28.120  1.00 40.52           C  
ATOM   1222  C   ASP A 855      53.039   5.981 -29.461  1.00 51.37           C  
ATOM   1223  O   ASP A 855      53.124   7.209 -29.614  1.00 42.65           O  
ATOM   1224  CB  ASP A 855      51.899   6.392 -27.270  1.00 47.87           C  
ATOM   1225  CG  ASP A 855      50.490   6.663 -27.760  1.00 71.04           C  
ATOM   1226  OD1 ASP A 855      50.331   7.049 -28.951  1.00 55.42           O  
ATOM   1227  OD2 ASP A 855      49.548   6.487 -26.944  1.00 73.26           O  
ATOM   1228  N   PHE A 856      53.302   5.123 -30.442  1.00 47.67           N  
ATOM   1229  CA  PHE A 856      53.731   5.607 -31.744  1.00 53.20           C  
ATOM   1230  C   PHE A 856      52.577   5.869 -32.705  1.00 53.22           C  
ATOM   1231  O   PHE A 856      52.756   5.996 -33.919  1.00 59.70           O  
ATOM   1232  CB  PHE A 856      54.755   4.633 -32.313  1.00 51.71           C  
ATOM   1233  CG  PHE A 856      56.085   4.737 -31.641  1.00 55.01           C  
ATOM   1234  CD1 PHE A 856      57.012   5.686 -32.064  1.00 46.38           C  
ATOM   1235  CD2 PHE A 856      56.367   3.981 -30.506  1.00 52.06           C  
ATOM   1236  CE1 PHE A 856      58.196   5.891 -31.367  1.00 41.05           C  
ATOM   1237  CE2 PHE A 856      57.549   4.179 -29.799  1.00 37.05           C  
ATOM   1238  CZ  PHE A 856      58.466   5.145 -30.237  1.00 42.97           C  
ATOM   1239  N   GLY A 857      51.396   6.005 -32.118  1.00 48.20           N  
ATOM   1240  CA  GLY A 857      50.187   6.262 -32.873  1.00 52.02           C  
ATOM   1241  C   GLY A 857      50.116   7.537 -33.699  1.00 44.24           C  
ATOM   1242  O   GLY A 857      49.174   7.708 -34.460  1.00 69.23           O  
ATOM   1243  N   LEU A 858      51.087   8.430 -33.577  1.00 51.32           N  
ATOM   1244  CA  LEU A 858      51.072   9.663 -34.358  1.00 32.09           C  
ATOM   1245  C   LEU A 858      52.387   9.863 -35.051  1.00 41.22           C  
ATOM   1246  O   LEU A 858      52.529  10.758 -35.880  1.00 44.98           O  
ATOM   1247  CB  LEU A 858      50.842  10.844 -33.448  1.00 43.82           C  
ATOM   1248  CG  LEU A 858      49.370  11.135 -33.220  1.00 60.43           C  
ATOM   1249  CD1 LEU A 858      49.200  12.013 -31.991  1.00 66.55           C  
ATOM   1250  CD2 LEU A 858      48.815  11.819 -34.470  1.00 60.31           C  
ATOM   1251  N   ALA A 859      53.358   9.024 -34.712  1.00 38.89           N  
ATOM   1252  CA  ALA A 859      54.685   9.194 -35.267  1.00 42.17           C  
ATOM   1253  C   ALA A 859      54.703   9.153 -36.785  1.00 41.81           C  
ATOM   1254  O   ALA A 859      53.854   8.523 -37.401  1.00 51.82           O  
ATOM   1255  CB  ALA A 859      55.616   8.151 -34.687  1.00 29.62           C  
ATOM   1256  N   LYS A 860      55.673   9.854 -37.368  1.00 53.04           N  
ATOM   1257  CA  LYS A 860      55.880   9.912 -38.814  1.00 45.03           C  
ATOM   1258  C   LYS A 860      57.338   9.702 -39.093  1.00 48.03           C  
ATOM   1259  O   LYS A 860      58.177  10.257 -38.400  1.00 58.95           O  
ATOM   1260  CB  LYS A 860      55.549  11.285 -39.386  1.00 38.50           C  
ATOM   1261  CG  LYS A 860      54.145  11.710 -39.193  1.00 60.61           C  
ATOM   1262  CD  LYS A 860      53.244  10.630 -39.724  1.00 67.73           C  
ATOM   1263  CE  LYS A 860      51.803  11.030 -39.651  1.00 61.92           C  
ATOM   1264  NZ  LYS A 860      50.956   9.869 -39.988  1.00 79.36           N  
ATOM   1265  N   LEU A 861      57.646   8.891 -40.098  1.00 66.49           N  
ATOM   1266  CA  LEU A 861      59.029   8.701 -40.498  1.00 71.28           C  
ATOM   1267  C   LEU A 861      59.132   9.707 -41.624  1.00 73.99           C  
ATOM   1268  O   LEU A 861      58.375   9.646 -42.588  1.00 82.24           O  
ATOM   1269  CB  LEU A 861      59.278   7.280 -41.007  1.00 66.23           C  
ATOM   1270  CG  LEU A 861      59.499   6.273 -39.865  1.00 83.34           C  
ATOM   1271  CD1 LEU A 861      59.124   4.867 -40.297  1.00 82.01           C  
ATOM   1272  CD2 LEU A 861      60.952   6.326 -39.415  1.00 84.60           C  
ATOM   1273  N   LEU A 862      60.024  10.675 -41.470  1.00 74.50           N  
ATOM   1274  CA  LEU A 862      60.207  11.685 -42.489  1.00 71.02           C  
ATOM   1275  C   LEU A 862      60.719  10.976 -43.735  1.00 84.15           C  
ATOM   1276  O   LEU A 862      61.509  10.023 -43.639  1.00 74.26           O  
ATOM   1277  CB  LEU A 862      61.218  12.726 -42.017  1.00 72.44           C  
ATOM   1278  CG  LEU A 862      60.808  13.484 -40.754  1.00 60.51           C  
ATOM   1279  CD1 LEU A 862      61.967  14.338 -40.268  1.00 73.25           C  
ATOM   1280  CD2 LEU A 862      59.579  14.336 -41.048  1.00 55.01           C  
ATOM   1281  N   GLY A 863      60.244  11.430 -44.893  1.00 86.33           N  
ATOM   1282  CA  GLY A 863      60.654  10.846 -46.155  1.00 89.36           C  
ATOM   1283  C   GLY A 863      62.128  11.077 -46.428  1.00 91.96           C  
ATOM   1284  O   GLY A 863      62.855  11.582 -45.570  1.00 98.21           O  
ATOM   1285  N   ALA A 864      62.567  10.708 -47.627  1.00 91.95           N  
ATOM   1286  CA  ALA A 864      63.957  10.867 -48.014  1.00 97.09           C  
ATOM   1287  C   ALA A 864      64.514  12.244 -47.637  1.00104.18           C  
ATOM   1288  O   ALA A 864      65.355  12.338 -46.725  1.00 97.64           O  
ATOM   1289  CB  ALA A 864      64.102  10.623 -49.503  1.00 87.45           C  
ATOM   1290  N   GLU A 865      64.046  13.302 -48.312  1.00100.45           N  
ATOM   1291  CA  GLU A 865      64.534  14.660 -48.029  1.00 99.78           C  
ATOM   1292  C   GLU A 865      63.535  15.616 -47.396  1.00 95.73           C  
ATOM   1293  O   GLU A 865      63.780  16.822 -47.287  1.00 93.16           O  
ATOM   1294  CB  GLU A 865      65.134  15.284 -49.290  1.00 96.52           C  
ATOM   1295  CG  GLU A 865      66.356  14.524 -49.795  1.00 98.67           C  
ATOM   1296  CD  GLU A 865      67.355  14.205 -48.681  1.00105.66           C  
ATOM   1297  OE1 GLU A 865      66.938  13.748 -47.594  1.00117.09           O  
ATOM   1298  OE2 GLU A 865      68.568  14.396 -48.892  1.00 90.95           O  
ATOM   1299  N   GLU A 866      62.409  15.054 -46.981  1.00 91.55           N  
ATOM   1300  CA  GLU A 866      61.354  15.793 -46.306  1.00 91.63           C  
ATOM   1301  C   GLU A 866      61.922  16.136 -44.926  1.00 97.46           C  
ATOM   1302  O   GLU A 866      62.431  15.258 -44.229  1.00105.79           O  
ATOM   1303  CB  GLU A 866      60.125  14.884 -46.176  1.00 86.15           C  
ATOM   1304  CG  GLU A 866      59.041  15.348 -45.220  1.00 87.04           C  
ATOM   1305  CD  GLU A 866      57.935  14.314 -45.058  1.00 91.07           C  
ATOM   1306  OE1 GLU A 866      58.254  13.102 -45.096  1.00 86.58           O  
ATOM   1307  OE2 GLU A 866      56.756  14.708 -44.879  1.00 84.70           O  
ATOM   1308  N   LYS A 867      61.864  17.401 -44.525  1.00 95.67           N  
ATOM   1309  CA  LYS A 867      62.396  17.752 -43.212  1.00 93.88           C  
ATOM   1310  C   LYS A 867      61.392  18.310 -42.229  1.00 86.33           C  
ATOM   1311  O   LYS A 867      61.728  18.622 -41.099  1.00 83.97           O  
ATOM   1312  CB  LYS A 867      63.568  18.704 -43.342  1.00 99.33           C  
ATOM   1313  CG  LYS A 867      64.817  18.007 -43.805  1.00105.30           C  
ATOM   1314  CD  LYS A 867      66.016  18.849 -43.481  1.00111.28           C  
ATOM   1315  CE  LYS A 867      66.999  18.830 -44.621  1.00109.77           C  
ATOM   1316  NZ  LYS A 867      68.181  19.653 -44.275  1.00112.72           N  
ATOM   1317  N   GLU A 868      60.158  18.451 -42.674  1.00 86.10           N  
ATOM   1318  CA  GLU A 868      59.092  18.904 -41.811  1.00 75.51           C  
ATOM   1319  C   GLU A 868      57.985  17.964 -42.203  1.00 73.56           C  
ATOM   1320  O   GLU A 868      58.010  17.382 -43.289  1.00 67.57           O  
ATOM   1321  CB  GLU A 868      58.633  20.316 -42.140  1.00 80.17           C  
ATOM   1322  CG  GLU A 868      59.711  21.319 -42.387  1.00 81.05           C  
ATOM   1323  CD  GLU A 868      59.173  22.722 -42.250  1.00 91.11           C  
ATOM   1324  OE1 GLU A 868      57.978  22.931 -42.562  1.00 93.56           O  
ATOM   1325  OE2 GLU A 868      59.938  23.613 -41.830  1.00 88.48           O  
ATOM   1326  N   TYR A 869      57.021  17.800 -41.320  1.00 69.52           N  
ATOM   1327  CA  TYR A 869      55.891  16.955 -41.630  1.00 69.77           C  
ATOM   1328  C   TYR A 869      54.697  17.892 -41.582  1.00 75.94           C  
ATOM   1329  O   TYR A 869      54.530  18.640 -40.610  1.00 74.78           O  
ATOM   1330  CB  TYR A 869      55.735  15.849 -40.600  1.00 65.39           C  
ATOM   1331  CG  TYR A 869      54.462  15.092 -40.796  1.00 67.68           C  
ATOM   1332  CD1 TYR A 869      54.307  14.223 -41.873  1.00 76.57           C  
ATOM   1333  CD2 TYR A 869      53.380  15.296 -39.950  1.00 76.79           C  
ATOM   1334  CE1 TYR A 869      53.099  13.574 -42.108  1.00 68.27           C  
ATOM   1335  CE2 TYR A 869      52.164  14.656 -40.169  1.00 85.58           C  
ATOM   1336  CZ  TYR A 869      52.028  13.795 -41.250  1.00 89.31           C  
ATOM   1337  OH  TYR A 869      50.827  13.147 -41.461  1.00 74.84           O  
ATOM   1338  N   HIS A 870      53.882  17.884 -42.636  1.00 75.43           N  
ATOM   1339  CA  HIS A 870      52.720  18.762 -42.669  1.00 69.64           C  
ATOM   1340  C   HIS A 870      51.480  17.923 -42.598  1.00 62.04           C  
ATOM   1341  O   HIS A 870      51.041  17.337 -43.584  1.00 84.66           O  
ATOM   1342  CB  HIS A 870      52.742  19.642 -43.920  1.00 69.84           C  
ATOM   1343  CG  HIS A 870      54.086  20.250 -44.186  1.00 91.13           C  
ATOM   1344  ND1 HIS A 870      55.126  19.535 -44.745  1.00101.57           N  
ATOM   1345  CD2 HIS A 870      54.583  21.478 -43.908  1.00 95.90           C  
ATOM   1346  CE1 HIS A 870      56.205  20.296 -44.798  1.00 99.24           C  
ATOM   1347  NE2 HIS A 870      55.904  21.480 -44.295  1.00 93.25           N  
ATOM   1348  N   ALA A 871      50.948  17.833 -41.399  1.00 66.87           N  
ATOM   1349  CA  ALA A 871      49.764  17.074 -41.106  1.00 75.81           C  
ATOM   1350  C   ALA A 871      48.632  17.835 -41.750  1.00 83.26           C  
ATOM   1351  O   ALA A 871      48.816  18.986 -42.164  1.00 74.05           O  
ATOM   1352  CB  ALA A 871      49.556  16.995 -39.625  1.00 64.70           C  
ATOM   1353  N   GLU A 872      47.455  17.234 -41.851  1.00 90.65           N  
ATOM   1354  CA  GLU A 872      46.404  17.979 -42.514  1.00103.48           C  
ATOM   1355  C   GLU A 872      45.098  18.107 -41.780  1.00103.00           C  
ATOM   1356  O   GLU A 872      44.101  18.512 -42.377  1.00114.14           O  
ATOM   1357  CB  GLU A 872      46.155  17.460 -43.927  1.00105.31           C  
ATOM   1358  CG  GLU A 872      45.148  16.335 -44.000  1.00112.75           C  
ATOM   1359  CD  GLU A 872      45.802  15.025 -44.316  1.00116.11           C  
ATOM   1360  OE1 GLU A 872      46.164  14.833 -45.496  1.00119.68           O  
ATOM   1361  OE2 GLU A 872      45.961  14.201 -43.392  1.00116.61           O  
ATOM   1362  N   GLY A 873      45.069  17.774 -40.505  1.00 89.74           N  
ATOM   1363  CA  GLY A 873      43.824  17.900 -39.797  1.00 98.45           C  
ATOM   1364  C   GLY A 873      43.787  16.798 -38.795  1.00105.31           C  
ATOM   1365  O   GLY A 873      43.953  15.635 -39.147  1.00110.79           O  
ATOM   1366  N   GLY A 874      43.600  17.127 -37.536  1.00108.06           N  
ATOM   1367  CA  GLY A 874      43.583  16.060 -36.581  1.00104.25           C  
ATOM   1368  C   GLY A 874      43.205  16.498 -35.205  1.00104.73           C  
ATOM   1369  O   GLY A 874      43.025  17.682 -34.925  1.00104.37           O  
ATOM   1370  N   LYS A 875      43.057  15.499 -34.352  1.00103.42           N  
ATOM   1371  CA  LYS A 875      42.729  15.700 -32.965  1.00103.52           C  
ATOM   1372  C   LYS A 875      44.126  15.501 -32.385  1.00 98.86           C  
ATOM   1373  O   LYS A 875      44.674  14.389 -32.377  1.00 90.55           O  
ATOM   1374  CB  LYS A 875      41.706  14.640 -32.533  1.00103.11           C  
ATOM   1375  CG  LYS A 875      40.733  14.284 -33.691  1.00110.53           C  
ATOM   1376  CD  LYS A 875      39.566  13.324 -33.355  1.00107.28           C  
ATOM   1377  CE  LYS A 875      38.539  13.295 -34.525  1.00110.52           C  
ATOM   1378  NZ  LYS A 875      37.376  12.344 -34.429  1.00107.44           N  
ATOM   1379  N   VAL A 876      44.713  16.615 -31.972  1.00 97.13           N  
ATOM   1380  CA  VAL A 876      46.063  16.692 -31.435  1.00 89.21           C  
ATOM   1381  C   VAL A 876      46.058  17.291 -30.044  1.00 84.85           C  
ATOM   1382  O   VAL A 876      45.247  18.166 -29.749  1.00 92.09           O  
ATOM   1383  CB  VAL A 876      46.916  17.608 -32.293  1.00 87.47           C  
ATOM   1384  CG1 VAL A 876      47.314  16.915 -33.591  1.00 74.73           C  
ATOM   1385  CG2 VAL A 876      46.111  18.886 -32.577  1.00 73.71           C  
ATOM   1386  N   PRO A 877      46.978  16.839 -29.177  1.00 79.13           N  
ATOM   1387  CA  PRO A 877      47.095  17.335 -27.797  1.00 75.11           C  
ATOM   1388  C   PRO A 877      47.853  18.672 -27.825  1.00 69.72           C  
ATOM   1389  O   PRO A 877      49.078  18.710 -27.800  1.00 61.90           O  
ATOM   1390  CB  PRO A 877      47.860  16.212 -27.103  1.00 68.50           C  
ATOM   1391  CG  PRO A 877      48.782  15.727 -28.190  1.00 72.65           C  
ATOM   1392  CD  PRO A 877      47.917  15.732 -29.436  1.00 71.34           C  
ATOM   1393  N   ILE A 878      47.100  19.766 -27.878  1.00 75.35           N  
ATOM   1394  CA  ILE A 878      47.657  21.116 -27.985  1.00 73.10           C  
ATOM   1395  C   ILE A 878      48.600  21.619 -26.877  1.00 66.69           C  
ATOM   1396  O   ILE A 878      49.556  22.368 -27.143  1.00 58.97           O  
ATOM   1397  CB  ILE A 878      46.503  22.138 -28.187  1.00 72.28           C  
ATOM   1398  CG1 ILE A 878      46.968  23.283 -29.082  1.00 75.43           C  
ATOM   1399  CG2 ILE A 878      46.036  22.675 -26.861  1.00 67.28           C  
ATOM   1400  CD1 ILE A 878      46.051  23.511 -30.258  1.00 69.85           C  
ATOM   1401  N   LYS A 879      48.351  21.213 -25.640  1.00 55.97           N  
ATOM   1402  CA  LYS A 879      49.200  21.675 -24.561  1.00 57.38           C  
ATOM   1403  C   LYS A 879      50.650  21.173 -24.579  1.00 57.89           C  
ATOM   1404  O   LYS A 879      51.493  21.660 -23.830  1.00 55.73           O  
ATOM   1405  CB  LYS A 879      48.518  21.379 -23.244  1.00 46.70           C  
ATOM   1406  CG  LYS A 879      47.274  22.224 -23.101  1.00 56.27           C  
ATOM   1407  CD  LYS A 879      46.616  22.052 -21.766  1.00 55.90           C  
ATOM   1408  CE  LYS A 879      45.434  22.989 -21.655  1.00 61.95           C  
ATOM   1409  NZ  LYS A 879      44.585  22.603 -20.481  1.00 63.88           N  
ATOM   1410  N   TRP A 880      50.950  20.215 -25.444  1.00 47.36           N  
ATOM   1411  CA  TRP A 880      52.311  19.730 -25.540  1.00 45.13           C  
ATOM   1412  C   TRP A 880      52.899  20.096 -26.879  1.00 48.89           C  
ATOM   1413  O   TRP A 880      54.014  19.687 -27.180  1.00 50.86           O  
ATOM   1414  CB  TRP A 880      52.370  18.221 -25.427  1.00 30.58           C  
ATOM   1415  CG  TRP A 880      52.219  17.711 -24.070  1.00 38.99           C  
ATOM   1416  CD1 TRP A 880      53.182  17.135 -23.308  1.00 44.95           C  
ATOM   1417  CD2 TRP A 880      51.017  17.662 -23.309  1.00 41.15           C  
ATOM   1418  NE1 TRP A 880      52.657  16.716 -22.114  1.00 40.16           N  
ATOM   1419  CE2 TRP A 880      51.326  17.027 -22.084  1.00 43.13           C  
ATOM   1420  CE3 TRP A 880      49.701  18.086 -23.544  1.00 48.11           C  
ATOM   1421  CZ2 TRP A 880      50.366  16.800 -21.087  1.00 41.21           C  
ATOM   1422  CZ3 TRP A 880      48.738  17.856 -22.551  1.00 40.96           C  
ATOM   1423  CH2 TRP A 880      49.083  17.218 -21.336  1.00 50.66           C  
ATOM   1424  N   MET A 881      52.173  20.856 -27.693  1.00 52.21           N  
ATOM   1425  CA  MET A 881      52.704  21.167 -29.011  1.00 45.11           C  
ATOM   1426  C   MET A 881      53.402  22.487 -29.189  1.00 46.34           C  
ATOM   1427  O   MET A 881      53.084  23.517 -28.572  1.00 43.56           O  
ATOM   1428  CB  MET A 881      51.631  21.021 -30.115  1.00 52.83           C  
ATOM   1429  CG  MET A 881      50.283  20.457 -29.657  1.00 65.01           C  
ATOM   1430  SD  MET A 881      49.114  19.913 -30.961  1.00 52.71           S  
ATOM   1431  CE  MET A 881      49.842  20.681 -32.474  1.00 31.44           C  
ATOM   1432  N   ALA A 882      54.380  22.414 -30.077  1.00 43.77           N  
ATOM   1433  CA  ALA A 882      55.187  23.539 -30.441  1.00 45.55           C  
ATOM   1434  C   ALA A 882      54.246  24.539 -31.082  1.00 53.11           C  
ATOM   1435  O   ALA A 882      53.158  24.180 -31.526  1.00 61.78           O  
ATOM   1436  CB  ALA A 882      56.257  23.086 -31.421  1.00 37.65           C  
ATOM   1437  N   LEU A 883      54.662  25.798 -31.130  1.00 67.14           N  
ATOM   1438  CA  LEU A 883      53.830  26.840 -31.705  1.00 62.09           C  
ATOM   1439  C   LEU A 883      53.702  26.691 -33.207  1.00 56.16           C  
ATOM   1440  O   LEU A 883      52.641  26.963 -33.749  1.00 61.82           O  
ATOM   1441  CB  LEU A 883      54.384  28.225 -31.390  1.00 63.51           C  
ATOM   1442  CG  LEU A 883      53.461  29.341 -31.883  1.00 66.91           C  
ATOM   1443  CD1 LEU A 883      52.419  29.646 -30.817  1.00 54.45           C  
ATOM   1444  CD2 LEU A 883      54.282  30.578 -32.209  1.00 60.54           C  
ATOM   1445  N   GLU A 884      54.770  26.277 -33.887  1.00 43.05           N  
ATOM   1446  CA  GLU A 884      54.675  26.106 -35.334  1.00 46.22           C  
ATOM   1447  C   GLU A 884      53.645  25.014 -35.618  1.00 60.80           C  
ATOM   1448  O   GLU A 884      52.885  25.095 -36.580  1.00 63.66           O  
ATOM   1449  CB  GLU A 884      56.016  25.693 -35.947  1.00 52.70           C  
ATOM   1450  CG  GLU A 884      57.236  26.087 -35.123  1.00 68.38           C  
ATOM   1451  CD  GLU A 884      57.574  25.038 -34.099  1.00 58.02           C  
ATOM   1452  OE1 GLU A 884      58.364  24.116 -34.430  1.00 48.26           O  
ATOM   1453  OE2 GLU A 884      57.019  25.133 -32.983  1.00 49.14           O  
ATOM   1454  N   SER A 885      53.621  23.997 -34.763  1.00 63.81           N  
ATOM   1455  CA  SER A 885      52.697  22.888 -34.928  1.00 62.15           C  
ATOM   1456  C   SER A 885      51.254  23.334 -34.828  1.00 64.99           C  
ATOM   1457  O   SER A 885      50.412  22.902 -35.609  1.00 72.24           O  
ATOM   1458  CB  SER A 885      52.976  21.809 -33.884  1.00 61.67           C  
ATOM   1459  OG  SER A 885      54.290  21.303 -34.044  1.00 50.21           O  
ATOM   1460  N   ILE A 886      50.971  24.206 -33.869  1.00 68.07           N  
ATOM   1461  CA  ILE A 886      49.611  24.709 -33.657  1.00 69.94           C  
ATOM   1462  C   ILE A 886      49.114  25.609 -34.794  1.00 75.26           C  
ATOM   1463  O   ILE A 886      47.987  25.464 -35.279  1.00 62.70           O  
ATOM   1464  CB  ILE A 886      49.535  25.507 -32.354  1.00 64.90           C  
ATOM   1465  CG1 ILE A 886      49.968  24.623 -31.190  1.00 72.45           C  
ATOM   1466  CG2 ILE A 886      48.127  25.992 -32.119  1.00 52.79           C  
ATOM   1467  CD1 ILE A 886      50.352  25.396 -29.964  1.00 65.12           C  
ATOM   1468  N   LEU A 887      49.968  26.535 -35.211  1.00 75.04           N  
ATOM   1469  CA  LEU A 887      49.632  27.471 -36.270  1.00 71.49           C  
ATOM   1470  C   LEU A 887      49.748  26.892 -37.670  1.00 67.35           C  
ATOM   1471  O   LEU A 887      48.961  27.245 -38.539  1.00 68.56           O  
ATOM   1472  CB  LEU A 887      50.530  28.712 -36.187  1.00 64.07           C  
ATOM   1473  CG  LEU A 887      50.615  29.433 -34.839  1.00 61.27           C  
ATOM   1474  CD1 LEU A 887      51.522  30.632 -34.984  1.00 53.88           C  
ATOM   1475  CD2 LEU A 887      49.243  29.859 -34.371  1.00 33.07           C  
ATOM   1476  N   HIS A 888      50.719  26.011 -37.898  1.00 62.02           N  
ATOM   1477  CA  HIS A 888      50.918  25.458 -39.237  1.00 55.18           C  
ATOM   1478  C   HIS A 888      51.020  23.944 -39.380  1.00 59.46           C  
ATOM   1479  O   HIS A 888      51.545  23.454 -40.378  1.00 63.16           O  
ATOM   1480  CB  HIS A 888      52.169  26.060 -39.860  1.00 47.54           C  
ATOM   1481  CG  HIS A 888      52.365  27.505 -39.541  1.00 68.65           C  
ATOM   1482  ND1 HIS A 888      51.332  28.323 -39.139  1.00 71.81           N  
ATOM   1483  CD2 HIS A 888      53.470  28.286 -39.591  1.00 74.29           C  
ATOM   1484  CE1 HIS A 888      51.793  29.547 -38.952  1.00 78.95           C  
ATOM   1485  NE2 HIS A 888      53.087  29.551 -39.221  1.00 79.44           N  
ATOM   1486  N   ARG A 889      50.535  23.204 -38.399  1.00 57.32           N  
ATOM   1487  CA  ARG A 889      50.600  21.761 -38.481  1.00 62.56           C  
ATOM   1488  C   ARG A 889      51.954  21.270 -38.997  1.00 68.66           C  
ATOM   1489  O   ARG A 889      52.029  20.283 -39.725  1.00 72.02           O  
ATOM   1490  CB  ARG A 889      49.508  21.253 -39.398  1.00 59.43           C  
ATOM   1491  CG  ARG A 889      48.240  22.058 -39.342  1.00 65.54           C  
ATOM   1492  CD  ARG A 889      47.059  21.183 -39.742  1.00 82.49           C  
ATOM   1493  NE  ARG A 889      45.788  21.903 -39.752  1.00 94.55           N  
ATOM   1494  CZ  ARG A 889      45.316  22.632 -38.742  1.00 96.26           C  
ATOM   1495  NH1 ARG A 889      46.001  22.767 -37.609  1.00 90.30           N  
ATOM   1496  NH2 ARG A 889      44.135  23.220 -38.862  1.00 90.24           N  
ATOM   1497  N   ILE A 890      53.023  21.969 -38.647  1.00 59.68           N  
ATOM   1498  CA  ILE A 890      54.350  21.538 -39.060  1.00 54.45           C  
ATOM   1499  C   ILE A 890      54.982  20.819 -37.864  1.00 53.35           C  
ATOM   1500  O   ILE A 890      54.938  21.312 -36.734  1.00 63.15           O  
ATOM   1501  CB  ILE A 890      55.211  22.742 -39.438  1.00 56.42           C  
ATOM   1502  CG1 ILE A 890      54.499  23.551 -40.504  1.00 69.33           C  
ATOM   1503  CG2 ILE A 890      56.560  22.297 -39.967  1.00 62.67           C  
ATOM   1504  CD1 ILE A 890      55.222  24.813 -40.833  1.00 81.64           C  
ATOM   1505  N   TYR A 891      55.544  19.642 -38.104  1.00 54.43           N  
ATOM   1506  CA  TYR A 891      56.187  18.885 -37.039  1.00 53.75           C  
ATOM   1507  C   TYR A 891      57.629  18.631 -37.384  1.00 50.13           C  
ATOM   1508  O   TYR A 891      57.964  18.411 -38.545  1.00 51.68           O  
ATOM   1509  CB  TYR A 891      55.455  17.588 -36.811  1.00 38.77           C  
ATOM   1510  CG  TYR A 891      54.070  17.846 -36.320  1.00 42.58           C  
ATOM   1511  CD1 TYR A 891      53.759  17.767 -34.958  1.00 38.72           C  
ATOM   1512  CD2 TYR A 891      53.063  18.197 -37.214  1.00 40.07           C  
ATOM   1513  CE1 TYR A 891      52.457  18.026 -34.499  1.00 36.90           C  
ATOM   1514  CE2 TYR A 891      51.771  18.468 -36.771  1.00 40.33           C  
ATOM   1515  CZ  TYR A 891      51.464  18.381 -35.421  1.00 35.23           C  
ATOM   1516  OH  TYR A 891      50.170  18.641 -35.007  1.00 51.57           O  
ATOM   1517  N   THR A 892      58.476  18.660 -36.362  1.00 47.31           N  
ATOM   1518  CA  THR A 892      59.909  18.497 -36.555  1.00 39.94           C  
ATOM   1519  C   THR A 892      60.477  17.851 -35.320  1.00 42.91           C  
ATOM   1520  O   THR A 892      59.789  17.739 -34.319  1.00 50.96           O  
ATOM   1521  CB  THR A 892      60.531  19.897 -36.748  1.00 44.23           C  
ATOM   1522  OG1 THR A 892      60.354  20.284 -38.109  1.00 48.72           O  
ATOM   1523  CG2 THR A 892      62.010  19.942 -36.385  1.00 48.11           C  
ATOM   1524  N   HIS A 893      61.718  17.389 -35.401  1.00 47.23           N  
ATOM   1525  CA  HIS A 893      62.367  16.822 -34.233  1.00 46.84           C  
ATOM   1526  C   HIS A 893      62.399  17.980 -33.215  1.00 52.80           C  
ATOM   1527  O   HIS A 893      62.217  17.774 -32.005  1.00 52.01           O  
ATOM   1528  CB  HIS A 893      63.806  16.380 -34.547  1.00 43.80           C  
ATOM   1529  CG  HIS A 893      63.900  15.237 -35.503  1.00 49.34           C  
ATOM   1530  ND1 HIS A 893      63.171  14.079 -35.350  1.00 48.28           N  
ATOM   1531  CD2 HIS A 893      64.632  15.076 -36.631  1.00 57.26           C  
ATOM   1532  CE1 HIS A 893      63.446  13.254 -36.346  1.00 43.93           C  
ATOM   1533  NE2 HIS A 893      64.330  13.834 -37.137  1.00 50.91           N  
ATOM   1534  N   GLN A 894      62.614  19.202 -33.705  1.00 39.82           N  
ATOM   1535  CA  GLN A 894      62.655  20.351 -32.805  1.00 44.90           C  
ATOM   1536  C   GLN A 894      61.294  20.610 -32.212  1.00 40.39           C  
ATOM   1537  O   GLN A 894      61.180  21.115 -31.110  1.00 49.10           O  
ATOM   1538  CB  GLN A 894      63.187  21.576 -33.529  1.00 31.01           C  
ATOM   1539  CG  GLN A 894      64.647  21.389 -33.907  1.00 30.84           C  
ATOM   1540  CD  GLN A 894      65.486  20.926 -32.715  1.00 46.90           C  
ATOM   1541  OE1 GLN A 894      66.033  19.816 -32.703  1.00 39.47           O  
ATOM   1542  NE2 GLN A 894      65.584  21.780 -31.703  1.00 46.47           N  
ATOM   1543  N   SER A 895      60.261  20.247 -32.956  1.00 41.42           N  
ATOM   1544  CA  SER A 895      58.886  20.379 -32.491  1.00 32.56           C  
ATOM   1545  C   SER A 895      58.776  19.403 -31.303  1.00 36.18           C  
ATOM   1546  O   SER A 895      58.099  19.664 -30.297  1.00 30.39           O  
ATOM   1547  CB  SER A 895      57.937  19.948 -33.628  1.00 38.31           C  
ATOM   1548  OG  SER A 895      56.585  20.185 -33.302  1.00 64.00           O  
ATOM   1549  N   ASP A 896      59.461  18.265 -31.434  1.00 37.20           N  
ATOM   1550  CA  ASP A 896      59.450  17.233 -30.408  1.00 35.91           C  
ATOM   1551  C   ASP A 896      60.121  17.805 -29.174  1.00 45.31           C  
ATOM   1552  O   ASP A 896      59.645  17.612 -28.052  1.00 41.67           O  
ATOM   1553  CB  ASP A 896      60.196  15.971 -30.897  1.00 41.50           C  
ATOM   1554  CG  ASP A 896      59.279  14.983 -31.645  1.00 53.39           C  
ATOM   1555  OD1 ASP A 896      59.803  14.034 -32.274  1.00 41.75           O  
ATOM   1556  OD2 ASP A 896      58.034  15.147 -31.594  1.00 30.75           O  
ATOM   1557  N   VAL A 897      61.223  18.521 -29.389  1.00 32.27           N  
ATOM   1558  CA  VAL A 897      61.930  19.133 -28.283  1.00 39.12           C  
ATOM   1559  C   VAL A 897      60.961  19.962 -27.438  1.00 44.73           C  
ATOM   1560  O   VAL A 897      61.002  19.922 -26.191  1.00 37.46           O  
ATOM   1561  CB  VAL A 897      63.082  20.022 -28.783  1.00 43.39           C  
ATOM   1562  CG1 VAL A 897      63.690  20.792 -27.612  1.00 29.23           C  
ATOM   1563  CG2 VAL A 897      64.153  19.150 -29.459  1.00 28.76           C  
ATOM   1564  N   TRP A 898      60.071  20.696 -28.105  1.00 34.39           N  
ATOM   1565  CA  TRP A 898      59.115  21.487 -27.351  1.00 39.60           C  
ATOM   1566  C   TRP A 898      58.336  20.567 -26.428  1.00 37.14           C  
ATOM   1567  O   TRP A 898      58.203  20.836 -25.238  1.00 44.50           O  
ATOM   1568  CB  TRP A 898      58.147  22.233 -28.267  1.00 30.78           C  
ATOM   1569  CG  TRP A 898      57.181  23.137 -27.511  1.00 37.85           C  
ATOM   1570  CD1 TRP A 898      56.199  22.753 -26.635  1.00 43.77           C  
ATOM   1571  CD2 TRP A 898      57.054  24.561 -27.648  1.00 24.03           C  
ATOM   1572  NE1 TRP A 898      55.462  23.848 -26.233  1.00 41.49           N  
ATOM   1573  CE2 TRP A 898      55.968  24.966 -26.846  1.00 31.61           C  
ATOM   1574  CE3 TRP A 898      57.752  25.528 -28.380  1.00 35.67           C  
ATOM   1575  CZ2 TRP A 898      55.561  26.298 -26.761  1.00 25.44           C  
ATOM   1576  CZ3 TRP A 898      57.350  26.840 -28.297  1.00 31.35           C  
ATOM   1577  CH2 TRP A 898      56.262  27.217 -27.494  1.00 37.27           C  
ATOM   1578  N   SER A 899      57.824  19.470 -26.964  1.00 40.65           N  
ATOM   1579  CA  SER A 899      57.049  18.554 -26.127  1.00 36.72           C  
ATOM   1580  C   SER A 899      57.912  17.920 -25.044  1.00 38.17           C  
ATOM   1581  O   SER A 899      57.422  17.594 -23.953  1.00 30.08           O  
ATOM   1582  CB  SER A 899      56.395  17.475 -26.984  1.00 44.44           C  
ATOM   1583  OG  SER A 899      55.781  18.062 -28.121  1.00 49.83           O  
ATOM   1584  N   TYR A 900      59.195  17.734 -25.339  1.00 34.45           N  
ATOM   1585  CA  TYR A 900      60.103  17.178 -24.344  1.00 34.20           C  
ATOM   1586  C   TYR A 900      60.097  18.156 -23.170  1.00 45.10           C  
ATOM   1587  O   TYR A 900      59.962  17.759 -22.000  1.00 38.59           O  
ATOM   1588  CB  TYR A 900      61.502  17.057 -24.930  1.00 43.66           C  
ATOM   1589  CG  TYR A 900      62.548  16.657 -23.926  1.00 48.28           C  
ATOM   1590  CD1 TYR A 900      63.309  17.631 -23.264  1.00 34.28           C  
ATOM   1591  CD2 TYR A 900      62.773  15.307 -23.623  1.00 29.42           C  
ATOM   1592  CE1 TYR A 900      64.267  17.267 -22.318  1.00 47.57           C  
ATOM   1593  CE2 TYR A 900      63.724  14.936 -22.686  1.00 41.30           C  
ATOM   1594  CZ  TYR A 900      64.464  15.921 -22.034  1.00 42.27           C  
ATOM   1595  OH  TYR A 900      65.368  15.562 -21.071  1.00 42.03           O  
ATOM   1596  N   GLY A 901      60.210  19.445 -23.501  1.00 39.37           N  
ATOM   1597  CA  GLY A 901      60.192  20.488 -22.484  1.00 42.94           C  
ATOM   1598  C   GLY A 901      58.981  20.456 -21.552  1.00 39.85           C  
ATOM   1599  O   GLY A 901      59.110  20.584 -20.327  1.00 44.67           O  
ATOM   1600  N   VAL A 902      57.798  20.300 -22.135  1.00 45.36           N  
ATOM   1601  CA  VAL A 902      56.548  20.223 -21.387  1.00 27.55           C  
ATOM   1602  C   VAL A 902      56.531  18.919 -20.578  1.00 38.22           C  
ATOM   1603  O   VAL A 902      56.037  18.873 -19.447  1.00 39.62           O  
ATOM   1604  CB  VAL A 902      55.353  20.257 -22.368  1.00 30.50           C  
ATOM   1605  CG1 VAL A 902      54.093  20.011 -21.652  1.00 20.09           C  
ATOM   1606  CG2 VAL A 902      55.301  21.591 -23.074  1.00 27.26           C  
ATOM   1607  N   THR A 903      57.093  17.859 -21.155  1.00 44.48           N  
ATOM   1608  CA  THR A 903      57.144  16.558 -20.489  1.00 34.18           C  
ATOM   1609  C   THR A 903      57.963  16.682 -19.224  1.00 43.65           C  
ATOM   1610  O   THR A 903      57.545  16.240 -18.162  1.00 36.30           O  
ATOM   1611  CB  THR A 903      57.779  15.494 -21.411  1.00 36.84           C  
ATOM   1612  OG1 THR A 903      56.923  15.296 -22.542  1.00 37.39           O  
ATOM   1613  CG2 THR A 903      57.969  14.154 -20.675  1.00 22.73           C  
ATOM   1614  N   VAL A 904      59.142  17.288 -19.349  1.00 40.04           N  
ATOM   1615  CA  VAL A 904      60.010  17.489 -18.202  1.00 34.07           C  
ATOM   1616  C   VAL A 904      59.294  18.279 -17.116  1.00 41.08           C  
ATOM   1617  O   VAL A 904      59.445  17.985 -15.923  1.00 44.19           O  
ATOM   1618  CB  VAL A 904      61.283  18.225 -18.593  1.00 31.68           C  
ATOM   1619  CG1 VAL A 904      61.979  18.750 -17.356  1.00 36.74           C  
ATOM   1620  CG2 VAL A 904      62.203  17.275 -19.332  1.00 27.29           C  
ATOM   1621  N   TRP A 905      58.517  19.276 -17.532  1.00 40.52           N  
ATOM   1622  CA  TRP A 905      57.749  20.104 -16.601  1.00 39.94           C  
ATOM   1623  C   TRP A 905      56.723  19.229 -15.855  1.00 48.00           C  
ATOM   1624  O   TRP A 905      56.502  19.399 -14.653  1.00 43.78           O  
ATOM   1625  CB  TRP A 905      57.052  21.219 -17.377  1.00 50.35           C  
ATOM   1626  CG  TRP A 905      56.334  22.193 -16.531  1.00 53.25           C  
ATOM   1627  CD1 TRP A 905      56.807  23.386 -16.069  1.00 51.85           C  
ATOM   1628  CD2 TRP A 905      54.998  22.072 -16.049  1.00 45.25           C  
ATOM   1629  NE1 TRP A 905      55.845  24.018 -15.331  1.00 44.24           N  
ATOM   1630  CE2 TRP A 905      54.719  23.235 -15.302  1.00 54.18           C  
ATOM   1631  CE3 TRP A 905      54.007  21.096 -16.181  1.00 52.49           C  
ATOM   1632  CZ2 TRP A 905      53.478  23.454 -14.685  1.00 54.05           C  
ATOM   1633  CZ3 TRP A 905      52.773  21.308 -15.571  1.00 71.48           C  
ATOM   1634  CH2 TRP A 905      52.519  22.483 -14.831  1.00 61.30           C  
ATOM   1635  N   GLU A 906      56.095  18.290 -16.559  1.00 43.35           N  
ATOM   1636  CA  GLU A 906      55.155  17.403 -15.887  1.00 47.24           C  
ATOM   1637  C   GLU A 906      55.894  16.613 -14.792  1.00 46.53           C  
ATOM   1638  O   GLU A 906      55.397  16.459 -13.673  1.00 53.56           O  
ATOM   1639  CB  GLU A 906      54.529  16.414 -16.866  1.00 44.30           C  
ATOM   1640  CG  GLU A 906      53.679  17.026 -17.945  1.00 49.65           C  
ATOM   1641  CD  GLU A 906      53.071  15.962 -18.846  1.00 61.20           C  
ATOM   1642  OE1 GLU A 906      52.088  15.293 -18.432  1.00 55.04           O  
ATOM   1643  OE2 GLU A 906      53.594  15.785 -19.966  1.00 54.25           O  
ATOM   1644  N   LEU A 907      57.082  16.111 -15.113  1.00 42.58           N  
ATOM   1645  CA  LEU A 907      57.853  15.361 -14.134  1.00 39.71           C  
ATOM   1646  C   LEU A 907      58.246  16.220 -12.950  1.00 43.10           C  
ATOM   1647  O   LEU A 907      58.088  15.796 -11.817  1.00 40.34           O  
ATOM   1648  CB  LEU A 907      59.128  14.826 -14.742  1.00 39.65           C  
ATOM   1649  CG  LEU A 907      59.024  13.964 -15.973  1.00 48.60           C  
ATOM   1650  CD1 LEU A 907      60.400  13.379 -16.206  1.00 30.13           C  
ATOM   1651  CD2 LEU A 907      57.990  12.876 -15.780  1.00 33.34           C  
ATOM   1652  N   MET A 908      58.771  17.417 -13.226  1.00 47.33           N  
ATOM   1653  CA  MET A 908      59.220  18.350 -12.189  1.00 40.04           C  
ATOM   1654  C   MET A 908      58.118  18.828 -11.258  1.00 53.51           C  
ATOM   1655  O   MET A 908      58.402  19.216 -10.115  1.00 58.34           O  
ATOM   1656  CB  MET A 908      59.909  19.573 -12.810  1.00 44.57           C  
ATOM   1657  CG  MET A 908      61.266  19.280 -13.429  1.00 26.00           C  
ATOM   1658  SD  MET A 908      62.112  18.140 -12.354  1.00 49.56           S  
ATOM   1659  CE  MET A 908      63.284  17.460 -13.406  1.00 35.26           C  
ATOM   1660  N   THR A 909      56.871  18.815 -11.728  1.00 43.06           N  
ATOM   1661  CA  THR A 909      55.769  19.250 -10.873  1.00 37.21           C  
ATOM   1662  C   THR A 909      55.017  18.045 -10.368  1.00 34.58           C  
ATOM   1663  O   THR A 909      53.903  18.172  -9.882  1.00 43.79           O  
ATOM   1664  CB  THR A 909      54.752  20.138 -11.603  1.00 43.33           C  
ATOM   1665  OG1 THR A 909      53.972  19.326 -12.493  1.00 51.17           O  
ATOM   1666  CG2 THR A 909      55.453  21.220 -12.397  1.00 45.33           C  
ATOM   1667  N   PHE A 910      55.614  16.868 -10.506  1.00 41.78           N  
ATOM   1668  CA  PHE A 910      54.986  15.628 -10.030  1.00 53.27           C  
ATOM   1669  C   PHE A 910      53.620  15.293 -10.626  1.00 55.60           C  
ATOM   1670  O   PHE A 910      52.787  14.680  -9.965  1.00 64.25           O  
ATOM   1671  CB  PHE A 910      54.887  15.641  -8.501  1.00 34.42           C  
ATOM   1672  CG  PHE A 910      56.227  15.704  -7.829  1.00 53.59           C  
ATOM   1673  CD1 PHE A 910      57.036  14.574  -7.751  1.00 45.57           C  
ATOM   1674  CD2 PHE A 910      56.721  16.912  -7.345  1.00 34.37           C  
ATOM   1675  CE1 PHE A 910      58.324  14.648  -7.205  1.00 47.45           C  
ATOM   1676  CE2 PHE A 910      58.001  16.990  -6.799  1.00 45.51           C  
ATOM   1677  CZ  PHE A 910      58.804  15.858  -6.729  1.00 43.97           C  
ATOM   1678  N   GLY A 911      53.387  15.702 -11.866  1.00 50.04           N  
ATOM   1679  CA  GLY A 911      52.140  15.354 -12.502  1.00 51.44           C  
ATOM   1680  C   GLY A 911      51.092  16.414 -12.681  1.00 53.94           C  
ATOM   1681  O   GLY A 911      49.937  16.082 -12.916  1.00 64.31           O  
ATOM   1682  N   SER A 912      51.470  17.676 -12.578  1.00 50.84           N  
ATOM   1683  CA  SER A 912      50.502  18.747 -12.744  1.00 53.53           C  
ATOM   1684  C   SER A 912      50.117  18.860 -14.216  1.00 62.31           C  
ATOM   1685  O   SER A 912      50.892  18.498 -15.105  1.00 60.26           O  
ATOM   1686  CB  SER A 912      51.090  20.079 -12.269  1.00 59.39           C  
ATOM   1687  OG  SER A 912      51.646  19.952 -10.974  1.00 58.61           O  
ATOM   1688  N   LYS A 913      48.922  19.383 -14.467  1.00 65.08           N  
ATOM   1689  CA  LYS A 913      48.423  19.539 -15.823  1.00 49.85           C  
ATOM   1690  C   LYS A 913      48.881  20.861 -16.391  1.00 49.73           C  
ATOM   1691  O   LYS A 913      48.697  21.911 -15.784  1.00 65.51           O  
ATOM   1692  CB  LYS A 913      46.892  19.464 -15.810  1.00 50.13           C  
ATOM   1693  CG  LYS A 913      46.376  18.346 -14.904  1.00 66.72           C  
ATOM   1694  CD  LYS A 913      44.864  18.296 -14.858  1.00 79.77           C  
ATOM   1695  CE  LYS A 913      44.303  17.480 -16.010  1.00 92.43           C  
ATOM   1696  NZ  LYS A 913      42.820  17.606 -16.130  1.00 94.24           N  
ATOM   1697  N   PRO A 914      49.491  20.838 -17.573  1.00 49.13           N  
ATOM   1698  CA  PRO A 914      49.961  22.083 -18.188  1.00 44.10           C  
ATOM   1699  C   PRO A 914      48.839  23.081 -18.436  1.00 50.46           C  
ATOM   1700  O   PRO A 914      47.800  22.717 -18.978  1.00 61.32           O  
ATOM   1701  CB  PRO A 914      50.553  21.614 -19.514  1.00 41.80           C  
ATOM   1702  CG  PRO A 914      50.907  20.183 -19.271  1.00 41.29           C  
ATOM   1703  CD  PRO A 914      49.789  19.674 -18.424  1.00 40.86           C  
ATOM   1704  N   TYR A 915      49.053  24.339 -18.071  1.00 57.43           N  
ATOM   1705  CA  TYR A 915      48.048  25.369 -18.317  1.00 51.11           C  
ATOM   1706  C   TYR A 915      46.749  24.918 -17.734  1.00 60.27           C  
ATOM   1707  O   TYR A 915      45.694  25.142 -18.335  1.00 52.14           O  
ATOM   1708  CB  TYR A 915      47.839  25.525 -19.808  1.00 51.14           C  
ATOM   1709  CG  TYR A 915      49.119  25.638 -20.556  1.00 52.37           C  
ATOM   1710  CD1 TYR A 915      49.762  26.863 -20.661  1.00 37.70           C  
ATOM   1711  CD2 TYR A 915      49.705  24.512 -21.156  1.00 49.63           C  
ATOM   1712  CE1 TYR A 915      50.973  26.985 -21.350  1.00 48.87           C  
ATOM   1713  CE2 TYR A 915      50.911  24.619 -21.850  1.00 44.34           C  
ATOM   1714  CZ  TYR A 915      51.535  25.863 -21.937  1.00 48.14           C  
ATOM   1715  OH  TYR A 915      52.726  26.001 -22.597  1.00 48.34           O  
ATOM   1716  N   ASP A 916      46.816  24.261 -16.585  1.00 68.73           N  
ATOM   1717  CA  ASP A 916      45.603  23.756 -15.973  1.00 73.40           C  
ATOM   1718  C   ASP A 916      44.493  24.767 -16.087  1.00 79.40           C  
ATOM   1719  O   ASP A 916      44.689  25.950 -15.804  1.00 73.81           O  
ATOM   1720  CB  ASP A 916      45.798  23.428 -14.496  1.00 80.67           C  
ATOM   1721  CG  ASP A 916      44.593  22.714 -13.910  1.00 82.46           C  
ATOM   1722  OD1 ASP A 916      43.494  22.893 -14.467  1.00 88.87           O  
ATOM   1723  OD2 ASP A 916      44.731  21.981 -12.905  1.00 80.31           O  
ATOM   1724  N   GLY A 917      43.337  24.281 -16.528  1.00 88.32           N  
ATOM   1725  CA  GLY A 917      42.151  25.107 -16.661  1.00 91.58           C  
ATOM   1726  C   GLY A 917      42.119  26.157 -17.754  1.00 94.77           C  
ATOM   1727  O   GLY A 917      41.242  27.020 -17.751  1.00105.07           O  
ATOM   1728  N   ILE A 918      43.060  26.112 -18.686  1.00 89.54           N  
ATOM   1729  CA  ILE A 918      43.070  27.097 -19.757  1.00 82.52           C  
ATOM   1730  C   ILE A 918      42.655  26.417 -21.047  1.00 89.70           C  
ATOM   1731  O   ILE A 918      43.335  25.522 -21.531  1.00 90.54           O  
ATOM   1732  CB  ILE A 918      44.472  27.733 -19.936  1.00 80.50           C  
ATOM   1733  CG1 ILE A 918      44.805  28.633 -18.744  1.00 76.61           C  
ATOM   1734  CG2 ILE A 918      44.502  28.606 -21.196  1.00 70.96           C  
ATOM   1735  CD1 ILE A 918      44.181  28.235 -17.413  1.00 80.79           C  
ATOM   1736  N   PRO A 919      41.497  26.806 -21.595  1.00 96.99           N  
ATOM   1737  CA  PRO A 919      40.987  26.234 -22.842  1.00 89.99           C  
ATOM   1738  C   PRO A 919      42.062  26.174 -23.928  1.00 79.93           C  
ATOM   1739  O   PRO A 919      42.758  27.174 -24.196  1.00 72.47           O  
ATOM   1740  CB  PRO A 919      39.854  27.176 -23.219  1.00101.35           C  
ATOM   1741  CG  PRO A 919      39.373  27.754 -21.886  1.00 97.74           C  
ATOM   1742  CD  PRO A 919      40.435  27.505 -20.848  1.00101.67           C  
ATOM   1743  N   ALA A 920      42.182  25.002 -24.550  1.00 59.26           N  
ATOM   1744  CA  ALA A 920      43.169  24.789 -25.602  1.00 64.68           C  
ATOM   1745  C   ALA A 920      43.002  25.870 -26.651  1.00 74.71           C  
ATOM   1746  O   ALA A 920      43.955  26.259 -27.358  1.00 66.43           O  
ATOM   1747  CB  ALA A 920      42.966  23.435 -26.225  1.00 57.84           C  
ATOM   1748  N   SER A 921      41.761  26.337 -26.737  1.00 82.77           N  
ATOM   1749  CA  SER A 921      41.353  27.375 -27.666  1.00 82.60           C  
ATOM   1750  C   SER A 921      42.338  28.540 -27.648  1.00 84.52           C  
ATOM   1751  O   SER A 921      42.860  28.945 -28.691  1.00 76.33           O  
ATOM   1752  CB  SER A 921      39.955  27.869 -27.279  1.00 87.05           C  
ATOM   1753  OG  SER A 921      39.217  26.848 -26.611  1.00 72.89           O  
ATOM   1754  N   GLU A 922      42.620  29.053 -26.452  1.00 88.09           N  
ATOM   1755  CA  GLU A 922      43.512  30.205 -26.316  1.00 93.11           C  
ATOM   1756  C   GLU A 922      45.002  29.911 -26.173  1.00 81.92           C  
ATOM   1757  O   GLU A 922      45.825  30.820 -26.350  1.00 68.23           O  
ATOM   1758  CB  GLU A 922      43.064  31.061 -25.131  1.00 97.55           C  
ATOM   1759  CG  GLU A 922      41.569  31.079 -24.938  1.00105.44           C  
ATOM   1760  CD  GLU A 922      41.187  30.699 -23.529  1.00114.82           C  
ATOM   1761  OE1 GLU A 922      41.113  31.594 -22.659  1.00116.21           O  
ATOM   1762  OE2 GLU A 922      40.982  29.495 -23.287  1.00109.56           O  
ATOM   1763  N   ILE A 923      45.345  28.661 -25.857  1.00 69.06           N  
ATOM   1764  CA  ILE A 923      46.746  28.293 -25.678  1.00 60.53           C  
ATOM   1765  C   ILE A 923      47.616  28.963 -26.715  1.00 57.52           C  
ATOM   1766  O   ILE A 923      48.662  29.530 -26.393  1.00 73.01           O  
ATOM   1767  CB  ILE A 923      46.998  26.766 -25.787  1.00 56.92           C  
ATOM   1768  CG1 ILE A 923      46.395  26.017 -24.595  1.00 52.69           C  
ATOM   1769  CG2 ILE A 923      48.485  26.507 -25.855  1.00 36.93           C  
ATOM   1770  CD1 ILE A 923      46.982  26.407 -23.266  1.00 62.00           C  
ATOM   1771  N   SER A 924      47.191  28.909 -27.964  1.00 47.77           N  
ATOM   1772  CA  SER A 924      47.994  29.516 -29.011  1.00 64.39           C  
ATOM   1773  C   SER A 924      48.339  30.990 -28.783  1.00 72.14           C  
ATOM   1774  O   SER A 924      49.478  31.399 -29.028  1.00 67.78           O  
ATOM   1775  CB  SER A 924      47.305  29.371 -30.364  1.00 69.14           C  
ATOM   1776  OG  SER A 924      48.025  30.090 -31.354  1.00 79.25           O  
ATOM   1777  N   SER A 925      47.358  31.774 -28.325  1.00 79.52           N  
ATOM   1778  CA  SER A 925      47.516  33.220 -28.084  1.00 87.38           C  
ATOM   1779  C   SER A 925      48.607  33.499 -27.065  1.00 82.28           C  
ATOM   1780  O   SER A 925      49.551  34.285 -27.293  1.00 69.35           O  
ATOM   1781  CB  SER A 925      46.203  33.811 -27.559  1.00 91.08           C  
ATOM   1782  OG  SER A 925      45.108  33.450 -28.380  1.00 98.53           O  
ATOM   1783  N   ILE A 926      48.421  32.850 -25.925  1.00 64.07           N  
ATOM   1784  CA  ILE A 926      49.315  32.929 -24.798  1.00 65.07           C  
ATOM   1785  C   ILE A 926      50.775  32.809 -25.237  1.00 67.61           C  
ATOM   1786  O   ILE A 926      51.601  33.679 -24.947  1.00 73.06           O  
ATOM   1787  CB  ILE A 926      48.982  31.802 -23.815  1.00 61.52           C  
ATOM   1788  CG1 ILE A 926      47.699  32.127 -23.060  1.00 60.75           C  
ATOM   1789  CG2 ILE A 926      50.109  31.584 -22.873  1.00 57.94           C  
ATOM   1790  CD1 ILE A 926      47.291  31.035 -22.058  1.00 62.28           C  
ATOM   1791  N   LEU A 927      51.087  31.733 -25.945  1.00 59.63           N  
ATOM   1792  CA  LEU A 927      52.450  31.511 -26.378  1.00 63.02           C  
ATOM   1793  C   LEU A 927      53.031  32.653 -27.188  1.00 58.40           C  
ATOM   1794  O   LEU A 927      54.225  32.944 -27.077  1.00 72.92           O  
ATOM   1795  CB  LEU A 927      52.551  30.209 -27.178  1.00 64.68           C  
ATOM   1796  CG  LEU A 927      52.152  28.920 -26.456  1.00 67.32           C  
ATOM   1797  CD1 LEU A 927      52.307  27.756 -27.414  1.00 67.31           C  
ATOM   1798  CD2 LEU A 927      53.015  28.710 -25.222  1.00 58.96           C  
ATOM   1799  N   GLU A 928      52.206  33.300 -28.006  1.00 71.36           N  
ATOM   1800  CA  GLU A 928      52.692  34.402 -28.836  1.00 74.51           C  
ATOM   1801  C   GLU A 928      52.981  35.618 -27.974  1.00 78.42           C  
ATOM   1802  O   GLU A 928      53.889  36.403 -28.281  1.00 71.46           O  
ATOM   1803  CB  GLU A 928      51.672  34.747 -29.915  1.00 77.87           C  
ATOM   1804  CG  GLU A 928      51.510  33.668 -30.957  1.00 76.91           C  
ATOM   1805  CD  GLU A 928      50.062  33.448 -31.312  1.00 87.74           C  
ATOM   1806  OE1 GLU A 928      49.274  33.167 -30.389  1.00 80.72           O  
ATOM   1807  OE2 GLU A 928      49.709  33.556 -32.504  1.00 79.72           O  
ATOM   1808  N   LYS A 929      52.203  35.758 -26.897  1.00 74.82           N  
ATOM   1809  CA  LYS A 929      52.377  36.848 -25.942  1.00 76.94           C  
ATOM   1810  C   LYS A 929      53.750  36.789 -25.272  1.00 81.05           C  
ATOM   1811  O   LYS A 929      54.166  37.746 -24.617  1.00 82.83           O  
ATOM   1812  CB  LYS A 929      51.311  36.784 -24.856  1.00 76.16           C  
ATOM   1813  CG  LYS A 929      49.954  37.273 -25.293  1.00 92.41           C  
ATOM   1814  CD  LYS A 929      48.943  37.192 -24.158  1.00 98.90           C  
ATOM   1815  CE  LYS A 929      47.534  37.095 -24.719  1.00103.81           C  
ATOM   1816  NZ  LYS A 929      47.319  38.107 -25.795  1.00 95.75           N  
ATOM   1817  N   GLY A 930      54.440  35.659 -25.429  1.00 77.36           N  
ATOM   1818  CA  GLY A 930      55.756  35.489 -24.835  1.00 67.31           C  
ATOM   1819  C   GLY A 930      55.668  34.742 -23.518  1.00 50.95           C  
ATOM   1820  O   GLY A 930      56.645  34.635 -22.785  1.00 58.81           O  
ATOM   1821  N   GLU A 931      54.483  34.231 -23.221  1.00 37.87           N  
ATOM   1822  CA  GLU A 931      54.238  33.480 -21.995  1.00 47.22           C  
ATOM   1823  C   GLU A 931      54.577  31.983 -22.059  1.00 57.85           C  
ATOM   1824  O   GLU A 931      54.578  31.358 -23.127  1.00 60.76           O  
ATOM   1825  CB  GLU A 931      52.774  33.623 -21.584  1.00 34.66           C  
ATOM   1826  CG  GLU A 931      52.352  32.631 -20.515  1.00 55.64           C  
ATOM   1827  CD  GLU A 931      50.993  32.953 -19.924  1.00 80.52           C  
ATOM   1828  OE1 GLU A 931      50.537  32.194 -19.031  1.00 84.14           O  
ATOM   1829  OE2 GLU A 931      50.389  33.966 -20.354  1.00 80.97           O  
ATOM   1830  N   ARG A 932      54.844  31.406 -20.894  1.00 55.66           N  
ATOM   1831  CA  ARG A 932      55.183  29.995 -20.809  1.00 46.15           C  
ATOM   1832  C   ARG A 932      54.775  29.368 -19.491  1.00 43.43           C  
ATOM   1833  O   ARG A 932      54.206  30.027 -18.621  1.00 51.91           O  
ATOM   1834  CB  ARG A 932      56.674  29.815 -21.013  1.00 40.21           C  
ATOM   1835  CG  ARG A 932      57.137  30.221 -22.387  1.00 40.31           C  
ATOM   1836  CD  ARG A 932      56.657  29.263 -23.487  1.00 41.50           C  
ATOM   1837  NE  ARG A 932      57.335  29.582 -24.751  1.00 38.40           N  
ATOM   1838  CZ  ARG A 932      56.961  30.569 -25.562  1.00 52.70           C  
ATOM   1839  NH1 ARG A 932      55.895  31.306 -25.262  1.00 43.17           N  
ATOM   1840  NH2 ARG A 932      57.702  30.897 -26.617  1.00 26.90           N  
ATOM   1841  N   LEU A 933      55.039  28.077 -19.348  1.00 48.14           N  
ATOM   1842  CA  LEU A 933      54.692  27.417 -18.104  1.00 49.56           C  
ATOM   1843  C   LEU A 933      55.634  27.959 -17.031  1.00 55.64           C  
ATOM   1844  O   LEU A 933      56.785  28.297 -17.297  1.00 41.51           O  
ATOM   1845  CB  LEU A 933      54.850  25.907 -18.237  1.00 53.02           C  
ATOM   1846  CG  LEU A 933      53.786  25.199 -19.075  1.00 57.45           C  
ATOM   1847  CD1 LEU A 933      54.314  23.870 -19.578  1.00 39.00           C  
ATOM   1848  CD2 LEU A 933      52.536  25.001 -18.242  1.00 47.43           C  
ATOM   1849  N   PRO A 934      55.150  28.044 -15.797  1.00 52.50           N  
ATOM   1850  CA  PRO A 934      55.922  28.547 -14.661  1.00 51.08           C  
ATOM   1851  C   PRO A 934      56.993  27.591 -14.140  1.00 48.13           C  
ATOM   1852  O   PRO A 934      56.905  26.381 -14.302  1.00 50.34           O  
ATOM   1853  CB  PRO A 934      54.849  28.792 -13.621  1.00 49.91           C  
ATOM   1854  CG  PRO A 934      53.952  27.586 -13.847  1.00 59.83           C  
ATOM   1855  CD  PRO A 934      53.820  27.580 -15.370  1.00 56.04           C  
ATOM   1856  N   GLN A 935      57.989  28.166 -13.482  1.00 49.29           N  
ATOM   1857  CA  GLN A 935      59.095  27.422 -12.903  1.00 43.15           C  
ATOM   1858  C   GLN A 935      58.627  26.567 -11.749  1.00 41.78           C  
ATOM   1859  O   GLN A 935      58.067  27.075 -10.788  1.00 57.21           O  
ATOM   1860  CB  GLN A 935      60.131  28.399 -12.405  1.00 30.67           C  
ATOM   1861  CG  GLN A 935      61.386  27.777 -11.917  1.00 49.56           C  
ATOM   1862  CD  GLN A 935      62.379  28.824 -11.470  1.00 52.80           C  
ATOM   1863  OE1 GLN A 935      62.405  29.939 -11.995  1.00 60.82           O  
ATOM   1864  NE2 GLN A 935      63.212  28.471 -10.510  1.00 62.46           N  
ATOM   1865  N   PRO A 936      58.848  25.250 -11.823  1.00 41.69           N  
ATOM   1866  CA  PRO A 936      58.404  24.393 -10.722  1.00 52.54           C  
ATOM   1867  C   PRO A 936      59.221  24.620  -9.462  1.00 55.79           C  
ATOM   1868  O   PRO A 936      60.430  24.865  -9.519  1.00 65.08           O  
ATOM   1869  CB  PRO A 936      58.603  22.972 -11.270  1.00 43.12           C  
ATOM   1870  CG  PRO A 936      58.540  23.163 -12.749  1.00 46.09           C  
ATOM   1871  CD  PRO A 936      59.343  24.434 -12.934  1.00 38.82           C  
ATOM   1872  N   PRO A 937      58.565  24.531  -8.306  1.00 49.49           N  
ATOM   1873  CA  PRO A 937      59.127  24.701  -6.968  1.00 45.68           C  
ATOM   1874  C   PRO A 937      60.485  24.050  -6.762  1.00 41.06           C  
ATOM   1875  O   PRO A 937      61.390  24.674  -6.225  1.00 53.04           O  
ATOM   1876  CB  PRO A 937      58.069  24.071  -6.082  1.00 44.70           C  
ATOM   1877  CG  PRO A 937      56.839  24.481  -6.750  1.00 43.71           C  
ATOM   1878  CD  PRO A 937      57.127  24.246  -8.219  1.00 56.45           C  
ATOM   1879  N   ILE A 938      60.637  22.801  -7.188  1.00 41.97           N  
ATOM   1880  CA  ILE A 938      61.898  22.101  -6.985  1.00 31.41           C  
ATOM   1881  C   ILE A 938      63.002  22.478  -7.941  1.00 33.44           C  
ATOM   1882  O   ILE A 938      64.157  22.131  -7.715  1.00 45.90           O  
ATOM   1883  CB  ILE A 938      61.703  20.558  -7.039  1.00 42.63           C  
ATOM   1884  CG1 ILE A 938      61.328  20.088  -8.446  1.00 29.61           C  
ATOM   1885  CG2 ILE A 938      60.555  20.146  -6.133  1.00 36.40           C  
ATOM   1886  CD1 ILE A 938      61.157  18.556  -8.538  1.00 32.76           C  
ATOM   1887  N   CYS A 939      62.666  23.232  -8.979  1.00 35.26           N  
ATOM   1888  CA  CYS A 939      63.644  23.573 -10.005  1.00 35.77           C  
ATOM   1889  C   CYS A 939      64.595  24.711  -9.821  1.00 39.68           C  
ATOM   1890  O   CYS A 939      64.188  25.869  -9.717  1.00 42.69           O  
ATOM   1891  CB  CYS A 939      62.941  23.800 -11.346  1.00 50.49           C  
ATOM   1892  SG  CYS A 939      62.209  22.314 -12.061  1.00 42.42           S  
ATOM   1893  N   THR A 940      65.878  24.390  -9.810  1.00 36.69           N  
ATOM   1894  CA  THR A 940      66.866  25.444  -9.729  1.00 39.74           C  
ATOM   1895  C   THR A 940      66.751  26.127 -11.100  1.00 43.07           C  
ATOM   1896  O   THR A 940      66.277  25.540 -12.074  1.00 47.69           O  
ATOM   1897  CB  THR A 940      68.275  24.880  -9.572  1.00 49.99           C  
ATOM   1898  OG1 THR A 940      68.560  23.981 -10.656  1.00 42.67           O  
ATOM   1899  CG2 THR A 940      68.392  24.139  -8.258  1.00 48.38           C  
ATOM   1900  N   ILE A 941      67.174  27.369 -11.184  1.00 46.93           N  
ATOM   1901  CA  ILE A 941      67.067  28.057 -12.439  1.00 39.96           C  
ATOM   1902  C   ILE A 941      67.764  27.270 -13.544  1.00 38.17           C  
ATOM   1903  O   ILE A 941      67.314  27.284 -14.673  1.00 53.41           O  
ATOM   1904  CB  ILE A 941      67.633  29.491 -12.329  1.00 44.26           C  
ATOM   1905  CG1 ILE A 941      67.297  30.254 -13.608  1.00 30.15           C  
ATOM   1906  CG2 ILE A 941      69.153  29.459 -12.070  1.00 40.94           C  
ATOM   1907  CD1 ILE A 941      67.364  31.720 -13.462  1.00 39.18           C  
ATOM   1908  N   ASP A 942      68.837  26.558 -13.222  1.00 40.21           N  
ATOM   1909  CA  ASP A 942      69.554  25.769 -14.230  1.00 41.61           C  
ATOM   1910  C   ASP A 942      68.646  24.830 -15.029  1.00 45.40           C  
ATOM   1911  O   ASP A 942      68.737  24.748 -16.256  1.00 47.18           O  
ATOM   1912  CB  ASP A 942      70.619  24.904 -13.578  1.00 34.17           C  
ATOM   1913  CG  ASP A 942      71.628  25.701 -12.842  1.00 42.85           C  
ATOM   1914  OD1 ASP A 942      71.244  26.425 -11.902  1.00 59.62           O  
ATOM   1915  OD2 ASP A 942      72.809  25.605 -13.205  1.00 58.82           O  
ATOM   1916  N   VAL A 943      67.808  24.092 -14.310  1.00 38.82           N  
ATOM   1917  CA  VAL A 943      66.895  23.138 -14.919  1.00 43.67           C  
ATOM   1918  C   VAL A 943      65.813  23.882 -15.685  1.00 45.23           C  
ATOM   1919  O   VAL A 943      65.561  23.598 -16.857  1.00 42.04           O  
ATOM   1920  CB  VAL A 943      66.240  22.235 -13.831  1.00 43.09           C  
ATOM   1921  CG1 VAL A 943      65.085  21.433 -14.419  1.00 31.54           C  
ATOM   1922  CG2 VAL A 943      67.276  21.301 -13.264  1.00 26.67           C  
ATOM   1923  N   TYR A 944      65.195  24.850 -15.019  1.00 33.49           N  
ATOM   1924  CA  TYR A 944      64.137  25.609 -15.624  1.00 33.24           C  
ATOM   1925  C   TYR A 944      64.589  26.290 -16.913  1.00 35.61           C  
ATOM   1926  O   TYR A 944      63.848  26.385 -17.885  1.00 42.23           O  
ATOM   1927  CB  TYR A 944      63.625  26.633 -14.627  1.00 41.50           C  
ATOM   1928  CG  TYR A 944      62.398  27.358 -15.109  1.00 45.19           C  
ATOM   1929  CD1 TYR A 944      62.430  28.726 -15.339  1.00 41.61           C  
ATOM   1930  CD2 TYR A 944      61.209  26.671 -15.363  1.00 50.67           C  
ATOM   1931  CE1 TYR A 944      61.312  29.398 -15.811  1.00 50.78           C  
ATOM   1932  CE2 TYR A 944      60.078  27.340 -15.836  1.00 43.66           C  
ATOM   1933  CZ  TYR A 944      60.148  28.703 -16.052  1.00 42.09           C  
ATOM   1934  OH  TYR A 944      59.060  29.384 -16.489  1.00 42.79           O  
ATOM   1935  N   MET A 945      65.816  26.759 -16.914  1.00 39.35           N  
ATOM   1936  CA  MET A 945      66.376  27.440 -18.073  1.00 47.95           C  
ATOM   1937  C   MET A 945      66.291  26.493 -19.271  1.00 44.94           C  
ATOM   1938  O   MET A 945      65.962  26.888 -20.386  1.00 46.80           O  
ATOM   1939  CB  MET A 945      67.840  27.797 -17.774  1.00 52.36           C  
ATOM   1940  CG  MET A 945      68.459  28.862 -18.641  1.00 54.61           C  
ATOM   1941  SD  MET A 945      67.796  30.462 -18.265  1.00 64.75           S  
ATOM   1942  CE  MET A 945      67.139  30.832 -19.864  1.00 58.64           C  
ATOM   1943  N   ILE A 946      66.594  25.228 -19.028  1.00 40.21           N  
ATOM   1944  CA  ILE A 946      66.545  24.246 -20.092  1.00 43.60           C  
ATOM   1945  C   ILE A 946      65.121  24.087 -20.638  1.00 44.14           C  
ATOM   1946  O   ILE A 946      64.918  24.054 -21.845  1.00 36.46           O  
ATOM   1947  CB  ILE A 946      67.104  22.914 -19.602  1.00 41.76           C  
ATOM   1948  CG1 ILE A 946      68.600  23.072 -19.359  1.00 31.31           C  
ATOM   1949  CG2 ILE A 946      66.865  21.838 -20.616  1.00 40.21           C  
ATOM   1950  CD1 ILE A 946      69.257  21.827 -18.843  1.00 44.55           C  
ATOM   1951  N   MET A 947      64.137  23.995 -19.759  1.00 33.85           N  
ATOM   1952  CA  MET A 947      62.770  23.892 -20.218  1.00 41.55           C  
ATOM   1953  C   MET A 947      62.472  25.079 -21.124  1.00 47.63           C  
ATOM   1954  O   MET A 947      62.148  24.904 -22.298  1.00 54.23           O  
ATOM   1955  CB  MET A 947      61.814  23.895 -19.026  1.00 33.64           C  
ATOM   1956  CG  MET A 947      61.969  22.660 -18.158  1.00 38.91           C  
ATOM   1957  SD  MET A 947      60.923  22.688 -16.710  1.00 54.87           S  
ATOM   1958  CE  MET A 947      61.931  21.825 -15.643  1.00 59.63           C  
ATOM   1959  N   VAL A 948      62.600  26.285 -20.568  1.00 48.08           N  
ATOM   1960  CA  VAL A 948      62.343  27.528 -21.282  1.00 39.14           C  
ATOM   1961  C   VAL A 948      62.974  27.552 -22.680  1.00 44.50           C  
ATOM   1962  O   VAL A 948      62.369  28.055 -23.627  1.00 45.53           O  
ATOM   1963  CB  VAL A 948      62.817  28.729 -20.425  1.00 46.98           C  
ATOM   1964  CG1 VAL A 948      62.889  30.007 -21.250  1.00 36.81           C  
ATOM   1965  CG2 VAL A 948      61.859  28.906 -19.254  1.00 39.15           C  
ATOM   1966  N   LYS A 949      64.180  27.018 -22.824  1.00 37.07           N  
ATOM   1967  CA  LYS A 949      64.795  26.966 -24.147  1.00 38.36           C  
ATOM   1968  C   LYS A 949      64.072  26.014 -25.082  1.00 43.82           C  
ATOM   1969  O   LYS A 949      64.027  26.243 -26.284  1.00 44.30           O  
ATOM   1970  CB  LYS A 949      66.216  26.498 -24.062  1.00 38.17           C  
ATOM   1971  CG  LYS A 949      67.119  27.510 -23.558  1.00 40.23           C  
ATOM   1972  CD  LYS A 949      68.487  26.957 -23.561  1.00 46.94           C  
ATOM   1973  CE  LYS A 949      69.393  27.919 -22.879  1.00 50.25           C  
ATOM   1974  NZ  LYS A 949      70.618  27.201 -22.527  1.00 59.86           N  
ATOM   1975  N   CYS A 950      63.563  24.913 -24.537  1.00 31.30           N  
ATOM   1976  CA  CYS A 950      62.826  23.965 -25.350  1.00 45.14           C  
ATOM   1977  C   CYS A 950      61.587  24.678 -25.855  1.00 49.10           C  
ATOM   1978  O   CYS A 950      60.912  24.169 -26.737  1.00 74.33           O  
ATOM   1979  CB  CYS A 950      62.381  22.742 -24.535  1.00 36.37           C  
ATOM   1980  SG  CYS A 950      63.718  21.676 -24.030  1.00 41.11           S  
ATOM   1981  N   TRP A 951      61.288  25.860 -25.316  1.00 43.20           N  
ATOM   1982  CA  TRP A 951      60.084  26.586 -25.719  1.00 35.70           C  
ATOM   1983  C   TRP A 951      60.265  27.890 -26.469  1.00 39.41           C  
ATOM   1984  O   TRP A 951      59.360  28.723 -26.510  1.00 37.55           O  
ATOM   1985  CB  TRP A 951      59.206  26.857 -24.520  1.00 39.17           C  
ATOM   1986  CG  TRP A 951      58.875  25.638 -23.747  1.00 53.42           C  
ATOM   1987  CD1 TRP A 951      58.610  24.392 -24.246  1.00 51.33           C  
ATOM   1988  CD2 TRP A 951      58.664  25.560 -22.331  1.00 41.15           C  
ATOM   1989  NE1 TRP A 951      58.236  23.544 -23.223  1.00 55.45           N  
ATOM   1990  CE2 TRP A 951      58.261  24.235 -22.039  1.00 38.23           C  
ATOM   1991  CE3 TRP A 951      58.768  26.484 -21.283  1.00 45.08           C  
ATOM   1992  CZ2 TRP A 951      57.961  23.812 -20.742  1.00 35.38           C  
ATOM   1993  CZ3 TRP A 951      58.466  26.065 -19.985  1.00 45.77           C  
ATOM   1994  CH2 TRP A 951      58.065  24.735 -19.729  1.00 37.81           C  
ATOM   1995  N   MET A 952      61.444  28.069 -27.041  1.00 33.72           N  
ATOM   1996  CA  MET A 952      61.725  29.250 -27.828  1.00 46.83           C  
ATOM   1997  C   MET A 952      60.835  29.201 -29.050  1.00 48.59           C  
ATOM   1998  O   MET A 952      60.565  28.132 -29.586  1.00 66.61           O  
ATOM   1999  CB  MET A 952      63.169  29.228 -28.318  1.00 39.49           C  
ATOM   2000  CG  MET A 952      64.196  29.157 -27.221  1.00 67.78           C  
ATOM   2001  SD  MET A 952      64.538  30.785 -26.702  1.00 58.13           S  
ATOM   2002  CE  MET A 952      65.878  31.146 -27.731  1.00 57.59           C  
ATOM   2003  N   ILE A 953      60.395  30.356 -29.516  1.00 49.58           N  
ATOM   2004  CA  ILE A 953      59.580  30.369 -30.702  1.00 39.46           C  
ATOM   2005  C   ILE A 953      60.411  29.984 -31.919  1.00 43.90           C  
ATOM   2006  O   ILE A 953      59.908  29.370 -32.855  1.00 46.32           O  
ATOM   2007  CB  ILE A 953      58.955  31.725 -30.916  1.00 46.56           C  
ATOM   2008  CG1 ILE A 953      57.723  31.828 -30.028  1.00 48.89           C  
ATOM   2009  CG2 ILE A 953      58.620  31.921 -32.377  1.00 46.36           C  
ATOM   2010  CD1 ILE A 953      56.866  33.013 -30.337  1.00 56.37           C  
ATOM   2011  N   ASP A 954      61.680  30.344 -31.939  1.00 34.43           N  
ATOM   2012  CA  ASP A 954      62.461  29.925 -33.089  1.00 42.51           C  
ATOM   2013  C   ASP A 954      62.938  28.499 -32.826  1.00 48.96           C  
ATOM   2014  O   ASP A 954      63.833  28.279 -32.012  1.00 60.99           O  
ATOM   2015  CB  ASP A 954      63.670  30.836 -33.323  1.00 32.27           C  
ATOM   2016  CG  ASP A 954      64.674  30.210 -34.269  1.00 51.24           C  
ATOM   2017  OD1 ASP A 954      65.770  30.763 -34.470  1.00 60.29           O  
ATOM   2018  OD2 ASP A 954      64.372  29.133 -34.823  1.00 81.19           O  
ATOM   2019  N   ALA A 955      62.342  27.535 -33.520  1.00 55.38           N  
ATOM   2020  CA  ALA A 955      62.691  26.118 -33.371  1.00 54.40           C  
ATOM   2021  C   ALA A 955      64.183  25.745 -33.427  1.00 50.12           C  
ATOM   2022  O   ALA A 955      64.617  24.876 -32.671  1.00 50.28           O  
ATOM   2023  CB  ALA A 955      61.931  25.303 -34.395  1.00 48.14           C  
ATOM   2024  N   ASP A 956      64.955  26.362 -34.323  1.00 43.74           N  
ATOM   2025  CA  ASP A 956      66.400  26.074 -34.442  1.00 55.19           C  
ATOM   2026  C   ASP A 956      67.170  26.612 -33.239  1.00 55.51           C  
ATOM   2027  O   ASP A 956      68.360  26.339 -33.062  1.00 54.32           O  
ATOM   2028  CB  ASP A 956      66.994  26.719 -35.704  1.00 62.82           C  
ATOM   2029  CG  ASP A 956      66.523  26.062 -36.984  1.00 71.46           C  
ATOM   2030  OD1 ASP A 956      66.350  26.787 -37.985  1.00 86.09           O  
ATOM   2031  OD2 ASP A 956      66.336  24.827 -37.000  1.00 74.20           O  
ATOM   2032  N   SER A 957      66.482  27.408 -32.434  1.00 53.96           N  
ATOM   2033  CA  SER A 957      67.078  27.990 -31.254  1.00 53.26           C  
ATOM   2034  C   SER A 957      66.903  27.078 -30.057  1.00 49.39           C  
ATOM   2035  O   SER A 957      67.536  27.273 -29.030  1.00 55.76           O  
ATOM   2036  CB  SER A 957      66.476  29.369 -30.980  1.00 48.42           C  
ATOM   2037  OG  SER A 957      67.159  30.354 -31.739  1.00 58.33           O  
ATOM   2038  N   ARG A 958      66.031  26.087 -30.178  1.00 47.93           N  
ATOM   2039  CA  ARG A 958      65.854  25.135 -29.097  1.00 44.72           C  
ATOM   2040  C   ARG A 958      67.038  24.179 -29.127  1.00 45.22           C  
ATOM   2041  O   ARG A 958      67.744  24.064 -30.132  1.00 46.38           O  
ATOM   2042  CB  ARG A 958      64.584  24.349 -29.283  1.00 44.11           C  
ATOM   2043  CG  ARG A 958      63.413  25.232 -29.356  1.00 53.04           C  
ATOM   2044  CD  ARG A 958      62.275  24.539 -30.005  1.00 47.97           C  
ATOM   2045  NE  ARG A 958      61.223  25.497 -30.296  1.00 60.53           N  
ATOM   2046  CZ  ARG A 958      60.118  25.213 -30.965  1.00 53.35           C  
ATOM   2047  NH1 ARG A 958      59.907  23.991 -31.424  1.00 63.88           N  
ATOM   2048  NH2 ARG A 958      59.220  26.152 -31.165  1.00 57.53           N  
ATOM   2049  N   PRO A 959      67.282  23.496 -28.009  1.00 46.56           N  
ATOM   2050  CA  PRO A 959      68.405  22.565 -27.972  1.00 36.80           C  
ATOM   2051  C   PRO A 959      68.080  21.260 -28.658  1.00 41.64           C  
ATOM   2052  O   PRO A 959      66.921  20.912 -28.889  1.00 37.77           O  
ATOM   2053  CB  PRO A 959      68.649  22.384 -26.477  1.00 43.58           C  
ATOM   2054  CG  PRO A 959      67.297  22.552 -25.897  1.00 38.88           C  
ATOM   2055  CD  PRO A 959      66.731  23.717 -26.660  1.00 37.83           C  
ATOM   2056  N   LYS A 960      69.133  20.546 -28.992  1.00 39.32           N  
ATOM   2057  CA  LYS A 960      69.008  19.254 -29.619  1.00 43.62           C  
ATOM   2058  C   LYS A 960      68.975  18.185 -28.519  1.00 47.50           C  
ATOM   2059  O   LYS A 960      69.599  18.337 -27.457  1.00 50.76           O  
ATOM   2060  CB  LYS A 960      70.231  19.003 -30.484  1.00 47.99           C  
ATOM   2061  CG  LYS A 960      70.477  20.014 -31.556  1.00 48.74           C  
ATOM   2062  CD  LYS A 960      69.792  19.621 -32.844  1.00 69.66           C  
ATOM   2063  CE  LYS A 960      68.654  20.562 -33.118  1.00 83.56           C  
ATOM   2064  NZ  LYS A 960      69.104  21.983 -33.020  1.00 85.56           N  
ATOM   2065  N   PHE A 961      68.270  17.096 -28.786  1.00 30.76           N  
ATOM   2066  CA  PHE A 961      68.192  15.998 -27.841  1.00 33.57           C  
ATOM   2067  C   PHE A 961      69.582  15.571 -27.402  1.00 30.92           C  
ATOM   2068  O   PHE A 961      69.811  15.306 -26.218  1.00 48.59           O  
ATOM   2069  CB  PHE A 961      67.457  14.797 -28.458  1.00 26.07           C  
ATOM   2070  CG  PHE A 961      65.983  14.988 -28.542  1.00 27.41           C  
ATOM   2071  CD1 PHE A 961      65.219  15.110 -27.386  1.00 31.26           C  
ATOM   2072  CD2 PHE A 961      65.357  15.111 -29.768  1.00 22.25           C  
ATOM   2073  CE1 PHE A 961      63.846  15.364 -27.458  1.00 33.51           C  
ATOM   2074  CE2 PHE A 961      63.999  15.359 -29.848  1.00 26.88           C  
ATOM   2075  CZ  PHE A 961      63.239  15.489 -28.699  1.00 35.30           C  
ATOM   2076  N   ARG A 962      70.520  15.497 -28.334  1.00 27.32           N  
ATOM   2077  CA  ARG A 962      71.868  15.079 -27.946  1.00 41.02           C  
ATOM   2078  C   ARG A 962      72.497  16.072 -26.961  1.00 37.11           C  
ATOM   2079  O   ARG A 962      73.431  15.726 -26.248  1.00 46.65           O  
ATOM   2080  CB  ARG A 962      72.770  14.957 -29.162  1.00 29.13           C  
ATOM   2081  CG  ARG A 962      73.031  16.287 -29.819  1.00 33.51           C  
ATOM   2082  CD  ARG A 962      74.115  16.157 -30.825  1.00 47.34           C  
ATOM   2083  NE  ARG A 962      75.359  15.705 -30.198  1.00 73.35           N  
ATOM   2084  CZ  ARG A 962      76.243  16.498 -29.586  1.00 73.09           C  
ATOM   2085  NH1 ARG A 962      76.034  17.807 -29.505  1.00 62.12           N  
ATOM   2086  NH2 ARG A 962      77.350  15.981 -29.065  1.00 61.89           N  
ATOM   2087  N   GLU A 963      72.006  17.308 -26.938  1.00 34.33           N  
ATOM   2088  CA  GLU A 963      72.540  18.299 -26.011  1.00 41.97           C  
ATOM   2089  C   GLU A 963      71.785  18.127 -24.705  1.00 42.52           C  
ATOM   2090  O   GLU A 963      72.349  18.235 -23.618  1.00 41.60           O  
ATOM   2091  CB  GLU A 963      72.356  19.728 -26.550  1.00 36.35           C  
ATOM   2092  CG  GLU A 963      73.244  20.061 -27.732  1.00 41.41           C  
ATOM   2093  CD  GLU A 963      72.803  21.304 -28.481  1.00 43.80           C  
ATOM   2094  OE1 GLU A 963      71.621  21.710 -28.347  1.00 50.17           O  
ATOM   2095  OE2 GLU A 963      73.646  21.860 -29.224  1.00 64.82           O  
ATOM   2096  N   LEU A 964      70.492  17.853 -24.819  1.00 40.28           N  
ATOM   2097  CA  LEU A 964      69.677  17.646 -23.641  1.00 31.02           C  
ATOM   2098  C   LEU A 964      70.239  16.485 -22.810  1.00 28.28           C  
ATOM   2099  O   LEU A 964      70.119  16.486 -21.599  1.00 34.50           O  
ATOM   2100  CB  LEU A 964      68.248  17.347 -24.061  1.00 33.58           C  
ATOM   2101  CG  LEU A 964      67.156  18.426 -24.021  1.00 38.73           C  
ATOM   2102  CD1 LEU A 964      67.697  19.768 -23.614  1.00 42.07           C  
ATOM   2103  CD2 LEU A 964      66.507  18.489 -25.386  1.00 34.03           C  
ATOM   2104  N   ILE A 965      70.847  15.500 -23.470  1.00 38.30           N  
ATOM   2105  CA  ILE A 965      71.434  14.338 -22.791  1.00 30.15           C  
ATOM   2106  C   ILE A 965      72.623  14.770 -21.946  1.00 32.50           C  
ATOM   2107  O   ILE A 965      72.706  14.428 -20.773  1.00 42.26           O  
ATOM   2108  CB  ILE A 965      71.897  13.247 -23.816  1.00 35.55           C  
ATOM   2109  CG1 ILE A 965      70.676  12.647 -24.517  1.00 33.69           C  
ATOM   2110  CG2 ILE A 965      72.683  12.111 -23.116  1.00 17.84           C  
ATOM   2111  CD1 ILE A 965      71.054  11.658 -25.635  1.00 32.76           C  
ATOM   2112  N   ILE A 966      73.534  15.528 -22.548  1.00 32.99           N  
ATOM   2113  CA  ILE A 966      74.720  16.021 -21.854  1.00 34.52           C  
ATOM   2114  C   ILE A 966      74.348  16.876 -20.638  1.00 41.09           C  
ATOM   2115  O   ILE A 966      74.792  16.606 -19.520  1.00 42.64           O  
ATOM   2116  CB  ILE A 966      75.602  16.848 -22.815  1.00 38.89           C  
ATOM   2117  CG1 ILE A 966      76.151  15.932 -23.909  1.00 38.91           C  
ATOM   2118  CG2 ILE A 966      76.750  17.494 -22.064  1.00 26.76           C  
ATOM   2119  CD1 ILE A 966      76.695  16.662 -25.105  1.00 28.19           C  
ATOM   2120  N   GLU A 967      73.530  17.900 -20.860  1.00 35.10           N  
ATOM   2121  CA  GLU A 967      73.090  18.781 -19.787  1.00 34.05           C  
ATOM   2122  C   GLU A 967      72.424  18.044 -18.630  1.00 40.72           C  
ATOM   2123  O   GLU A 967      72.852  18.161 -17.484  1.00 45.30           O  
ATOM   2124  CB  GLU A 967      72.167  19.863 -20.349  1.00 33.14           C  
ATOM   2125  CG  GLU A 967      72.923  20.828 -21.265  1.00 37.57           C  
ATOM   2126  CD  GLU A 967      74.116  21.479 -20.546  1.00 72.07           C  
ATOM   2127  OE1 GLU A 967      75.270  21.390 -21.041  1.00 71.82           O  
ATOM   2128  OE2 GLU A 967      73.894  22.082 -19.472  1.00 82.22           O  
ATOM   2129  N   PHE A 968      71.389  17.268 -18.903  1.00 33.64           N  
ATOM   2130  CA  PHE A 968      70.761  16.556 -17.805  1.00 36.12           C  
ATOM   2131  C   PHE A 968      71.682  15.468 -17.249  1.00 38.05           C  
ATOM   2132  O   PHE A 968      71.564  15.054 -16.105  1.00 43.46           O  
ATOM   2133  CB  PHE A 968      69.438  15.971 -18.261  1.00 24.55           C  
ATOM   2134  CG  PHE A 968      68.311  16.979 -18.307  1.00 36.61           C  
ATOM   2135  CD1 PHE A 968      67.752  17.464 -17.138  1.00 30.33           C  
ATOM   2136  CD2 PHE A 968      67.764  17.389 -19.517  1.00 25.32           C  
ATOM   2137  CE1 PHE A 968      66.666  18.324 -17.171  1.00 35.90           C  
ATOM   2138  CE2 PHE A 968      66.674  18.249 -19.551  1.00 30.75           C  
ATOM   2139  CZ  PHE A 968      66.126  18.713 -18.382  1.00 19.65           C  
ATOM   2140  N   SER A 969      72.622  15.006 -18.046  1.00 35.73           N  
ATOM   2141  CA  SER A 969      73.523  13.980 -17.542  1.00 45.67           C  
ATOM   2142  C   SER A 969      74.432  14.592 -16.486  1.00 46.25           C  
ATOM   2143  O   SER A 969      74.655  14.007 -15.426  1.00 56.04           O  
ATOM   2144  CB  SER A 969      74.377  13.420 -18.670  1.00 23.71           C  
ATOM   2145  OG  SER A 969      74.452  12.023 -18.573  1.00 76.15           O  
ATOM   2146  N   LYS A 970      74.971  15.769 -16.796  1.00 46.84           N  
ATOM   2147  CA  LYS A 970      75.854  16.479 -15.877  1.00 44.02           C  
ATOM   2148  C   LYS A 970      75.124  16.703 -14.562  1.00 51.14           C  
ATOM   2149  O   LYS A 970      75.642  16.388 -13.495  1.00 52.16           O  
ATOM   2150  CB  LYS A 970      76.242  17.839 -16.437  1.00 26.48           C  
ATOM   2151  CG  LYS A 970      77.273  17.845 -17.544  1.00 48.50           C  
ATOM   2152  CD  LYS A 970      77.376  19.278 -18.053  1.00 31.63           C  
ATOM   2153  CE  LYS A 970      78.426  19.449 -19.111  1.00 46.74           C  
ATOM   2154  NZ  LYS A 970      78.157  20.739 -19.791  1.00 52.34           N  
ATOM   2155  N   MET A 971      73.921  17.264 -14.648  1.00 49.91           N  
ATOM   2156  CA  MET A 971      73.133  17.533 -13.468  1.00 46.45           C  
ATOM   2157  C   MET A 971      72.850  16.252 -12.677  1.00 49.13           C  
ATOM   2158  O   MET A 971      72.717  16.294 -11.455  1.00 39.50           O  
ATOM   2159  CB  MET A 971      71.828  18.230 -13.862  1.00 36.08           C  
ATOM   2160  CG  MET A 971      72.047  19.632 -14.386  1.00 32.78           C  
ATOM   2161  SD  MET A 971      70.536  20.581 -14.724  1.00 43.24           S  
ATOM   2162  CE  MET A 971      69.537  19.398 -15.417  1.00 39.74           C  
ATOM   2163  N   ALA A 972      72.779  15.119 -13.370  1.00 44.05           N  
ATOM   2164  CA  ALA A 972      72.515  13.846 -12.710  1.00 48.22           C  
ATOM   2165  C   ALA A 972      73.683  13.368 -11.869  1.00 44.11           C  
ATOM   2166  O   ALA A 972      73.500  12.481 -11.059  1.00 51.58           O  
ATOM   2167  CB  ALA A 972      72.153  12.778 -13.729  1.00 29.23           C  
ATOM   2168  N   ARG A 973      74.876  13.932 -12.065  1.00 46.63           N  
ATOM   2169  CA  ARG A 973      76.050  13.534 -11.272  1.00 44.64           C  
ATOM   2170  C   ARG A 973      75.955  14.160  -9.898  1.00 46.72           C  
ATOM   2171  O   ARG A 973      76.526  13.645  -8.948  1.00 67.05           O  
ATOM   2172  CB  ARG A 973      77.378  14.021 -11.863  1.00 37.79           C  
ATOM   2173  CG  ARG A 973      77.748  13.529 -13.237  1.00 60.23           C  
ATOM   2174  CD  ARG A 973      78.992  14.276 -13.737  1.00 71.55           C  
ATOM   2175  NE  ARG A 973      80.214  13.530 -13.469  1.00 94.18           N  
ATOM   2176  CZ  ARG A 973      80.495  12.357 -14.031  1.00108.26           C  
ATOM   2177  NH1 ARG A 973      79.636  11.817 -14.887  1.00108.53           N  
ATOM   2178  NH2 ARG A 973      81.624  11.717 -13.739  1.00106.69           N  
ATOM   2179  N   ASP A 974      75.265  15.292  -9.799  1.00 43.00           N  
ATOM   2180  CA  ASP A 974      75.104  15.984  -8.513  1.00 44.67           C  
ATOM   2181  C   ASP A 974      73.660  16.525  -8.436  1.00 39.01           C  
ATOM   2182  O   ASP A 974      73.413  17.732  -8.435  1.00 38.17           O  
ATOM   2183  CB  ASP A 974      76.119  17.116  -8.421  1.00 35.70           C  
ATOM   2184  CG  ASP A 974      76.272  17.638  -7.021  1.00 51.74           C  
ATOM   2185  OD1 ASP A 974      77.014  18.627  -6.850  1.00 65.78           O  
ATOM   2186  OD2 ASP A 974      75.647  17.063  -6.096  1.00 60.20           O  
ATOM   2187  N   PRO A 975      72.691  15.612  -8.334  1.00 39.14           N  
ATOM   2188  CA  PRO A 975      71.254  15.890  -8.274  1.00 35.48           C  
ATOM   2189  C   PRO A 975      70.810  16.961  -7.338  1.00 32.89           C  
ATOM   2190  O   PRO A 975      70.013  17.831  -7.698  1.00 41.48           O  
ATOM   2191  CB  PRO A 975      70.643  14.544  -7.891  1.00 44.60           C  
ATOM   2192  CG  PRO A 975      71.648  13.543  -8.360  1.00 49.52           C  
ATOM   2193  CD  PRO A 975      72.958  14.207  -7.981  1.00 27.04           C  
ATOM   2194  N   GLN A 976      71.311  16.889  -6.120  1.00 39.32           N  
ATOM   2195  CA  GLN A 976      70.904  17.833  -5.108  1.00 44.96           C  
ATOM   2196  C   GLN A 976      71.250  19.280  -5.440  1.00 41.78           C  
ATOM   2197  O   GLN A 976      70.635  20.207  -4.915  1.00 39.00           O  
ATOM   2198  CB  GLN A 976      71.478  17.368  -3.784  1.00 50.28           C  
ATOM   2199  CG  GLN A 976      71.177  15.882  -3.593  1.00 67.82           C  
ATOM   2200  CD  GLN A 976      70.611  15.545  -2.226  1.00 69.27           C  
ATOM   2201  OE1 GLN A 976      69.826  16.310  -1.663  1.00 78.06           O  
ATOM   2202  NE2 GLN A 976      70.989  14.381  -1.696  1.00 67.82           N  
ATOM   2203  N   ARG A 977      72.200  19.473  -6.348  1.00 36.43           N  
ATOM   2204  CA  ARG A 977      72.574  20.821  -6.746  1.00 44.47           C  
ATOM   2205  C   ARG A 977      71.576  21.450  -7.721  1.00 41.42           C  
ATOM   2206  O   ARG A 977      71.454  22.670  -7.798  1.00 48.14           O  
ATOM   2207  CB  ARG A 977      73.960  20.825  -7.404  1.00 42.34           C  
ATOM   2208  CG  ARG A 977      74.621  22.162  -7.227  1.00 46.09           C  
ATOM   2209  CD  ARG A 977      75.389  22.641  -8.415  1.00 45.90           C  
ATOM   2210  NE  ARG A 977      76.683  21.998  -8.538  1.00 53.55           N  
ATOM   2211  CZ  ARG A 977      77.729  22.571  -9.127  1.00 59.16           C  
ATOM   2212  NH1 ARG A 977      77.623  23.791  -9.634  1.00 45.99           N  
ATOM   2213  NH2 ARG A 977      78.877  21.922  -9.218  1.00 66.91           N  
ATOM   2214  N   TYR A 978      70.841  20.614  -8.448  1.00 31.55           N  
ATOM   2215  CA  TYR A 978      69.918  21.123  -9.453  1.00 40.46           C  
ATOM   2216  C   TYR A 978      68.426  21.002  -9.172  1.00 37.95           C  
ATOM   2217  O   TYR A 978      67.619  21.686  -9.802  1.00 36.42           O  
ATOM   2218  CB  TYR A 978      70.279  20.496 -10.812  1.00 32.53           C  
ATOM   2219  CG  TYR A 978      71.715  20.792 -11.189  1.00 35.61           C  
ATOM   2220  CD1 TYR A 978      72.715  19.830 -11.032  1.00 44.36           C  
ATOM   2221  CD2 TYR A 978      72.094  22.084 -11.586  1.00 43.16           C  
ATOM   2222  CE1 TYR A 978      74.065  20.147 -11.251  1.00 44.14           C  
ATOM   2223  CE2 TYR A 978      73.420  22.413 -11.802  1.00 34.78           C  
ATOM   2224  CZ  TYR A 978      74.408  21.443 -11.630  1.00 51.82           C  
ATOM   2225  OH  TYR A 978      75.733  21.782 -11.822  1.00 38.98           O  
ATOM   2226  N   LEU A 979      68.058  20.131  -8.241  1.00 41.37           N  
ATOM   2227  CA  LEU A 979      66.655  19.967  -7.858  1.00 39.75           C  
ATOM   2228  C   LEU A 979      66.594  19.958  -6.324  1.00 38.35           C  
ATOM   2229  O   LEU A 979      67.322  19.229  -5.658  1.00 41.31           O  
ATOM   2230  CB  LEU A 979      66.058  18.670  -8.451  1.00 45.19           C  
ATOM   2231  CG  LEU A 979      65.878  18.545  -9.981  1.00 38.41           C  
ATOM   2232  CD1 LEU A 979      65.625  17.089 -10.327  1.00 36.12           C  
ATOM   2233  CD2 LEU A 979      64.730  19.447 -10.497  1.00 27.58           C  
ATOM   2234  N   VAL A 980      65.734  20.787  -5.757  1.00 38.59           N  
ATOM   2235  CA  VAL A 980      65.648  20.861  -4.315  1.00 40.28           C  
ATOM   2236  C   VAL A 980      64.348  20.267  -3.831  1.00 47.18           C  
ATOM   2237  O   VAL A 980      63.300  20.917  -3.869  1.00 46.74           O  
ATOM   2238  CB  VAL A 980      65.749  22.319  -3.845  1.00 54.49           C  
ATOM   2239  CG1 VAL A 980      65.723  22.362  -2.344  1.00 43.46           C  
ATOM   2240  CG2 VAL A 980      67.035  22.965  -4.378  1.00 34.59           C  
ATOM   2241  N   ILE A 981      64.422  19.023  -3.372  1.00 47.59           N  
ATOM   2242  CA  ILE A 981      63.240  18.311  -2.913  1.00 42.55           C  
ATOM   2243  C   ILE A 981      63.356  17.953  -1.442  1.00 56.56           C  
ATOM   2244  O   ILE A 981      64.412  17.508  -0.985  1.00 57.73           O  
ATOM   2245  CB  ILE A 981      63.064  17.009  -3.686  1.00 38.72           C  
ATOM   2246  CG1 ILE A 981      63.028  17.279  -5.190  1.00 44.49           C  
ATOM   2247  CG2 ILE A 981      61.803  16.309  -3.230  1.00 48.13           C  
ATOM   2248  CD1 ILE A 981      63.168  16.009  -6.010  1.00 33.18           C  
ATOM   2249  N   GLN A 982      62.258  18.123  -0.711  1.00 61.53           N  
ATOM   2250  CA  GLN A 982      62.226  17.818   0.715  1.00 75.56           C  
ATOM   2251  C   GLN A 982      62.577  16.368   1.069  1.00 71.06           C  
ATOM   2252  O   GLN A 982      61.915  15.436   0.632  1.00 67.80           O  
ATOM   2253  CB  GLN A 982      60.850  18.169   1.279  1.00 90.69           C  
ATOM   2254  CG  GLN A 982      60.566  19.666   1.293  1.00105.10           C  
ATOM   2255  CD  GLN A 982      60.071  20.148   2.647  1.00113.73           C  
ATOM   2256  OE1 GLN A 982      58.958  19.824   3.071  1.00110.46           O  
ATOM   2257  NE2 GLN A 982      60.906  20.916   3.340  1.00112.40           N  
ATOM   2258  N   GLY A 983      63.624  16.198   1.868  1.00 61.56           N  
ATOM   2259  CA  GLY A 983      64.053  14.872   2.280  1.00 70.89           C  
ATOM   2260  C   GLY A 983      64.432  13.942   1.149  1.00 75.00           C  
ATOM   2261  O   GLY A 983      63.943  12.819   1.097  1.00 78.46           O  
ATOM   2262  N   ASP A 984      65.330  14.385   0.275  1.00 84.23           N  
ATOM   2263  CA  ASP A 984      65.726  13.604  -0.887  1.00 87.84           C  
ATOM   2264  C   ASP A 984      65.987  12.120  -0.657  1.00 99.52           C  
ATOM   2265  O   ASP A 984      65.470  11.300  -1.437  1.00109.92           O  
ATOM   2266  CB  ASP A 984      66.926  14.249  -1.580  1.00 82.12           C  
ATOM   2267  CG  ASP A 984      66.729  14.368  -3.090  1.00 63.12           C  
ATOM   2268  OD1 ASP A 984      66.741  13.328  -3.778  1.00 56.05           O  
ATOM   2269  OD2 ASP A 984      66.543  15.493  -3.593  1.00 74.09           O  
ATOM   2270  N   GLU A 985      66.711  11.702   0.316  1.00106.66           N  
ATOM   2271  CA  GLU A 985      66.804  10.261   0.398  1.00113.23           C  
ATOM   2272  C   GLU A 985      65.859   9.775   1.482  1.00111.70           C  
ATOM   2273  O   GLU A 985      66.207   9.786   2.656  1.00101.87           O  
ATOM   2274  CB  GLU A 985      68.226   9.805   0.632  1.00114.39           C  
ATOM   2275  CG  GLU A 985      69.210  10.545  -0.250  1.00124.49           C  
ATOM   2276  CD  GLU A 985      69.550  11.936   0.282  1.00130.48           C  
ATOM   2277  OE1 GLU A 985      68.648  12.794   0.413  1.00131.66           O  
ATOM   2278  OE2 GLU A 985      70.740  12.173   0.574  1.00129.22           O  
ATOM   2279  N   ASP A1006      54.396 -20.999 -12.010  1.00103.65           N  
ATOM   2280  CA  ASP A1006      55.835 -20.961 -11.780  1.00106.02           C  
ATOM   2281  C   ASP A1006      56.450 -19.883 -12.650  1.00102.22           C  
ATOM   2282  O   ASP A1006      55.781 -19.311 -13.510  1.00105.29           O  
ATOM   2283  CB  ASP A1006      56.468 -22.321 -12.105  1.00111.18           C  
ATOM   2284  CG  ASP A1006      57.982 -22.355 -11.859  1.00117.48           C  
ATOM   2285  OD1 ASP A1006      58.451 -21.765 -10.857  1.00120.53           O  
ATOM   2286  OD2 ASP A1006      58.704 -22.991 -12.661  1.00112.84           O  
ATOM   2287  N   MET A1007      57.726 -19.606 -12.431  1.00 95.43           N  
ATOM   2288  CA  MET A1007      58.382 -18.585 -13.210  1.00 83.69           C  
ATOM   2289  C   MET A1007      59.882 -18.769 -13.275  1.00 71.35           C  
ATOM   2290  O   MET A1007      60.635 -17.804 -13.308  1.00 67.91           O  
ATOM   2291  CB  MET A1007      58.028 -17.213 -12.643  1.00104.08           C  
ATOM   2292  CG  MET A1007      58.387 -17.004 -11.192  1.00118.88           C  
ATOM   2293  SD  MET A1007      57.341 -15.701 -10.509  1.00143.10           S  
ATOM   2294  CE  MET A1007      55.894 -16.687 -10.050  1.00137.42           C  
ATOM   2295  N   ASP A1008      60.325 -20.015 -13.298  1.00 66.70           N  
ATOM   2296  CA  ASP A1008      61.752 -20.264 -13.389  1.00 68.34           C  
ATOM   2297  C   ASP A1008      62.236 -19.835 -14.762  1.00 72.49           C  
ATOM   2298  O   ASP A1008      63.390 -19.412 -14.929  1.00 67.83           O  
ATOM   2299  CB  ASP A1008      62.064 -21.748 -13.213  1.00 78.82           C  
ATOM   2300  CG  ASP A1008      62.622 -22.072 -11.844  1.00 85.43           C  
ATOM   2301  OD1 ASP A1008      63.228 -23.157 -11.707  1.00 85.19           O  
ATOM   2302  OD2 ASP A1008      62.452 -21.253 -10.910  1.00 82.10           O  
ATOM   2303  N   ASP A1009      61.350 -19.932 -15.750  1.00 57.09           N  
ATOM   2304  CA  ASP A1009      61.754 -19.585 -17.091  1.00 53.22           C  
ATOM   2305  C   ASP A1009      61.353 -18.195 -17.557  1.00 56.72           C  
ATOM   2306  O   ASP A1009      61.325 -17.917 -18.760  1.00 53.60           O  
ATOM   2307  CB  ASP A1009      61.260 -20.649 -18.073  1.00 51.40           C  
ATOM   2308  CG  ASP A1009      61.868 -22.021 -17.806  1.00 61.99           C  
ATOM   2309  OD1 ASP A1009      63.112 -22.131 -17.665  1.00 56.68           O  
ATOM   2310  OD2 ASP A1009      61.091 -22.999 -17.750  1.00 75.17           O  
ATOM   2311  N   VAL A1010      61.051 -17.310 -16.617  1.00 43.02           N  
ATOM   2312  CA  VAL A1010      60.707 -15.959 -17.005  1.00 48.63           C  
ATOM   2313  C   VAL A1010      61.938 -15.190 -17.459  1.00 46.54           C  
ATOM   2314  O   VAL A1010      62.974 -15.178 -16.786  1.00 65.35           O  
ATOM   2315  CB  VAL A1010      60.069 -15.203 -15.873  1.00 50.07           C  
ATOM   2316  CG1 VAL A1010      59.501 -13.889 -16.380  1.00 52.76           C  
ATOM   2317  CG2 VAL A1010      58.989 -16.026 -15.304  1.00 51.81           C  
ATOM   2318  N   VAL A1011      61.803 -14.553 -18.617  1.00 47.51           N  
ATOM   2319  CA  VAL A1011      62.865 -13.768 -19.232  1.00 44.04           C  
ATOM   2320  C   VAL A1011      62.252 -12.460 -19.694  1.00 41.24           C  
ATOM   2321  O   VAL A1011      61.176 -12.445 -20.304  1.00 45.96           O  
ATOM   2322  CB  VAL A1011      63.444 -14.462 -20.481  1.00 51.44           C  
ATOM   2323  CG1 VAL A1011      64.521 -13.581 -21.110  1.00 48.30           C  
ATOM   2324  CG2 VAL A1011      64.003 -15.815 -20.115  1.00 51.96           C  
ATOM   2325  N   ASP A1012      62.937 -11.362 -19.404  1.00 43.66           N  
ATOM   2326  CA  ASP A1012      62.443 -10.056 -19.808  1.00 46.97           C  
ATOM   2327  C   ASP A1012      62.655  -9.918 -21.309  1.00 36.04           C  
ATOM   2328  O   ASP A1012      63.652 -10.397 -21.829  1.00 43.53           O  
ATOM   2329  CB  ASP A1012      63.219  -8.961 -19.091  1.00 48.21           C  
ATOM   2330  CG  ASP A1012      62.526  -7.636 -19.180  1.00 67.27           C  
ATOM   2331  OD1 ASP A1012      61.626  -7.398 -18.334  1.00 71.96           O  
ATOM   2332  OD2 ASP A1012      62.861  -6.854 -20.106  1.00 50.14           O  
ATOM   2333  N   ALA A1013      61.732  -9.283 -22.018  1.00 37.13           N  
ATOM   2334  CA  ALA A1013      61.918  -9.120 -23.465  1.00 36.77           C  
ATOM   2335  C   ALA A1013      63.277  -8.488 -23.829  1.00 34.30           C  
ATOM   2336  O   ALA A1013      63.794  -8.740 -24.902  1.00 39.45           O  
ATOM   2337  CB  ALA A1013      60.801  -8.282 -24.043  1.00 34.04           C  
ATOM   2338  N   ASP A1014      63.851  -7.673 -22.945  1.00 35.57           N  
ATOM   2339  CA  ASP A1014      65.134  -7.050 -23.245  1.00 41.63           C  
ATOM   2340  C   ASP A1014      66.238  -8.071 -23.347  1.00 50.91           C  
ATOM   2341  O   ASP A1014      67.337  -7.758 -23.805  1.00 61.46           O  
ATOM   2342  CB  ASP A1014      65.500  -6.001 -22.203  1.00 27.43           C  
ATOM   2343  CG  ASP A1014      64.634  -4.757 -22.315  1.00 35.85           C  
ATOM   2344  OD1 ASP A1014      64.219  -4.425 -23.441  1.00 49.96           O  
ATOM   2345  OD2 ASP A1014      64.363  -4.103 -21.293  1.00 39.60           O  
ATOM   2346  N   GLU A1015      65.953  -9.293 -22.915  1.00 40.26           N  
ATOM   2347  CA  GLU A1015      66.940 -10.351 -23.015  1.00 33.65           C  
ATOM   2348  C   GLU A1015      66.531 -11.413 -24.008  1.00 41.87           C  
ATOM   2349  O   GLU A1015      67.239 -12.400 -24.194  1.00 46.25           O  
ATOM   2350  CB  GLU A1015      67.200 -11.002 -21.664  1.00 42.81           C  
ATOM   2351  CG  GLU A1015      68.197 -10.241 -20.810  1.00 49.79           C  
ATOM   2352  CD  GLU A1015      67.572  -9.073 -20.112  1.00 44.28           C  
ATOM   2353  OE1 GLU A1015      68.087  -7.945 -20.261  1.00 57.84           O  
ATOM   2354  OE2 GLU A1015      66.558  -9.289 -19.412  1.00 68.14           O  
ATOM   2355  N   TYR A1016      65.381 -11.223 -24.641  1.00 31.34           N  
ATOM   2356  CA  TYR A1016      64.927 -12.185 -25.626  1.00 53.80           C  
ATOM   2357  C   TYR A1016      65.159 -11.598 -27.012  1.00 52.84           C  
ATOM   2358  O   TYR A1016      64.440 -10.680 -27.425  1.00 51.99           O  
ATOM   2359  CB  TYR A1016      63.438 -12.502 -25.438  1.00 48.16           C  
ATOM   2360  CG  TYR A1016      62.982 -13.610 -26.346  1.00 46.02           C  
ATOM   2361  CD1 TYR A1016      62.203 -13.339 -27.465  1.00 54.41           C  
ATOM   2362  CD2 TYR A1016      63.390 -14.934 -26.122  1.00 54.65           C  
ATOM   2363  CE1 TYR A1016      61.840 -14.349 -28.341  1.00 59.25           C  
ATOM   2364  CE2 TYR A1016      63.036 -15.960 -26.993  1.00 41.47           C  
ATOM   2365  CZ  TYR A1016      62.261 -15.649 -28.099  1.00 60.13           C  
ATOM   2366  OH  TYR A1016      61.911 -16.600 -29.004  1.00 65.72           O  
ATOM   2367  N   LEU A1017      66.151 -12.130 -27.724  1.00 50.93           N  
ATOM   2368  CA  LEU A1017      66.479 -11.638 -29.064  1.00 57.38           C  
ATOM   2369  C   LEU A1017      66.229 -12.618 -30.221  1.00 63.57           C  
ATOM   2370  O   LEU A1017      66.878 -13.657 -30.305  1.00 62.07           O  
ATOM   2371  CB  LEU A1017      67.937 -11.169 -29.083  1.00 40.83           C  
ATOM   2372  CG  LEU A1017      68.357 -10.336 -27.869  1.00 56.47           C  
ATOM   2373  CD1 LEU A1017      69.479  -9.432 -28.234  1.00 29.50           C  
ATOM   2374  CD2 LEU A1017      67.200  -9.474 -27.405  1.00 68.29           C  
ATOM   2375  N   ILE A1018      65.296 -12.245 -31.107  1.00 83.14           N  
ATOM   2376  CA  ILE A1018      64.875 -13.008 -32.300  1.00 86.69           C  
ATOM   2377  C   ILE A1018      65.023 -14.527 -32.248  1.00 87.13           C  
ATOM   2378  O   ILE A1018      65.703 -15.091 -33.151  1.00 80.41           O  
ATOM   2379  CB  ILE A1018      65.591 -12.505 -33.609  1.00 96.87           C  
ATOM   2380  CG1 ILE A1018      67.117 -12.659 -33.486  1.00 87.52           C  
ATOM   2381  CG2 ILE A1018      65.149 -11.072 -33.928  1.00 92.94           C  
ATOM   2382  CD1 ILE A1018      67.897 -11.356 -33.554  1.00 75.55           C  
TER    2383      ILE A1018                                                      
HETATM 2384  PG  ANP A2001      43.960   6.177 -25.143  1.00200.45           P  
HETATM 2385  O1G ANP A2001      45.036   7.038 -25.685  1.00200.45           O  
HETATM 2386  O2G ANP A2001      43.904   4.741 -25.871  1.00200.45           O  
HETATM 2387  O3G ANP A2001      42.503   6.828 -25.360  1.00200.45           O  
HETATM 2388  PB  ANP A2001      45.527   5.201 -23.212  1.00195.08           P  
HETATM 2389  O1B ANP A2001      46.671   6.034 -23.646  1.00199.97           O  
HETATM 2390  O2B ANP A2001      45.533   4.952 -21.621  1.00192.93           O  
HETATM 2391  N3B ANP A2001      44.095   5.886 -23.552  1.00200.45           N  
HETATM 2392  PA  ANP A2001      46.851   2.898 -24.054  1.00164.41           P  
HETATM 2393  O1A ANP A2001      46.771   1.912 -25.155  1.00167.41           O  
HETATM 2394  O2A ANP A2001      48.028   3.973 -24.279  1.00167.77           O  
HETATM 2395  O3A ANP A2001      45.493   3.746 -23.899  1.00179.32           O  
HETATM 2396  O5' ANP A2001      47.105   2.237 -22.609  1.00149.87           O  
HETATM 2397  C5' ANP A2001      45.990   1.930 -21.769  1.00123.06           C  
HETATM 2398  C4' ANP A2001      46.452   1.533 -20.366  1.00117.50           C  
HETATM 2399  O4' ANP A2001      47.392   0.449 -20.493  1.00110.93           O  
HETATM 2400  C3' ANP A2001      47.242   2.695 -19.758  1.00115.25           C  
HETATM 2401  O3' ANP A2001      47.332   2.526 -18.341  1.00113.54           O  
HETATM 2402  C2' ANP A2001      48.608   2.452 -20.394  1.00117.81           C  
HETATM 2403  O2' ANP A2001      49.611   3.139 -19.640  1.00115.54           O  
HETATM 2404  C1' ANP A2001      48.691   0.949 -20.126  1.00111.62           C  
HETATM 2405  N9  ANP A2001      49.758   0.297 -20.923  1.00 95.12           N  
HETATM 2406  C8  ANP A2001      49.923   0.415 -22.239  1.00 90.07           C  
HETATM 2407  N7  ANP A2001      50.963  -0.324 -22.626  1.00 82.48           N  
HETATM 2408  C5  ANP A2001      51.464  -0.915 -21.549  1.00 74.25           C  
HETATM 2409  C6  ANP A2001      52.529  -1.785 -21.334  1.00 61.36           C  
HETATM 2410  N6  ANP A2001      53.292  -2.174 -22.350  1.00 63.47           N  
HETATM 2411  N1  ANP A2001      52.776  -2.210 -20.083  1.00 45.63           N  
HETATM 2412  C2  ANP A2001      52.026  -1.813 -19.074  1.00 61.93           C  
HETATM 2413  N3  ANP A2001      51.004  -0.985 -19.240  1.00 59.03           N  
HETATM 2414  C4  ANP A2001      50.698  -0.520 -20.459  1.00 79.51           C  
HETATM 2415  O   HOH A   1      59.237  -8.347 -20.761  1.00 35.93           O  
HETATM 2416  O   HOH A   2      63.880  -1.536 -25.613  1.00 36.48           O  
HETATM 2417  O   HOH A   3      53.313   9.153 -31.955  1.00 51.61           O  
HETATM 2418  O   HOH A   4      66.912  17.461 -31.254  1.00 47.69           O  
HETATM 2419  O   HOH A   5      69.512  15.375 -31.207  1.00 41.87           O  
HETATM 2420  O   HOH A   6      68.456 -13.342 -26.198  1.00 36.01           O  
HETATM 2421  O   HOH A   7      62.178  13.198 -33.077  1.00 45.39           O  
HETATM 2422  O   HOH A   8      62.867  -0.663 -28.953  1.00 43.86           O  
HETATM 2423  O   HOH A   9      56.019  15.059 -29.493  1.00 35.99           O  
CONECT 2384 2385 2386 2387 2391                                                 
CONECT 2385 2384                                                                
CONECT 2386 2384                                                                
CONECT 2387 2384                                                                
CONECT 2388 2389 2390 2391 2395                                                 
CONECT 2389 2388                                                                
CONECT 2390 2388                                                                
CONECT 2391 2384 2388                                                           
CONECT 2392 2393 2394 2395 2396                                                 
CONECT 2393 2392                                                                
CONECT 2394 2392                                                                
CONECT 2395 2388 2392                                                           
CONECT 2396 2392 2397                                                           
CONECT 2397 2396 2398                                                           
CONECT 2398 2397 2399 2400                                                      
CONECT 2399 2398 2404                                                           
CONECT 2400 2398 2401 2402                                                      
CONECT 2401 2400                                                                
CONECT 2402 2400 2403 2404                                                      
CONECT 2403 2402                                                                
CONECT 2404 2399 2402 2405                                                      
CONECT 2405 2404 2406 2414                                                      
CONECT 2406 2405 2407                                                           
CONECT 2407 2406 2408                                                           
CONECT 2408 2407 2409 2414                                                      
CONECT 2409 2408 2410 2411                                                      
CONECT 2410 2409                                                                
CONECT 2411 2409 2412                                                           
CONECT 2412 2411 2413                                                           
CONECT 2413 2412 2414                                                           
CONECT 2414 2405 2408 2413                                                      
MASTER      392    0    1   15   11    0    2    6 2422    1   31   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.