CNRS Nantes University UFIP UFIP
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***  NM_YT  ***

elNémo ID: 190112230616131899

Job options:

ID        	=	 190112230616131899
JOBID     	=	 NM_YT
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER NM_YT

HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       13-OCT-12   4HJO              
TITLE     CRYSTAL STRUCTURE OF THE INACTIVE EGFR TYROSINE KINASE DOMAIN WITH    
TITLE    2 ERLOTINIB                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: TYROSINE KINASE DOMAIN (UNP RESIDUES 696-1022);            
COMPND   5 SYNONYM: PROTO-ONCOGENE C-ERBB-1, RECEPTOR TYROSINE-PROTEIN KINASE   
COMPND   6 ERBB-1;                                                              
COMPND   7 EC: 2.7.10.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: 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, ERBB, ERBB1, HER1;                                       
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    INACTIVE TYROSINE KINASE DOMAIN, TRANSFERASE-TRANSFERASE INHIBITOR    
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.H.PARK,M.A.LEMMON                                                   
REVDAT   2   05-DEC-12 4HJO    1       JRNL                                     
REVDAT   1   14-NOV-12 4HJO    0                                                
JRNL        AUTH   J.H.PARK,Y.LIU,M.A.LEMMON,R.RADHAKRISHNAN                    
JRNL        TITL   ERLOTINIB BINDS BOTH INACTIVE AND ACTIVE CONFORMATIONS OF    
JRNL        TITL 2 THE EGFR TYROSINE KINASE DOMAIN.                             
JRNL        REF    BIOCHEM.J.                    V. 448   417 2012              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   23101586                                                     
JRNL        DOI    10.1042/BJ20121513                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 9413                           
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 + TEST SET) : 0.231                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 472                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 599                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.09                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2880                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 23                           
REMARK   3   BIN FREE R VALUE                    : 0.3590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2201                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 34                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.54000                                              
REMARK   3    B22 (A**2) : 0.59000                                              
REMARK   3    B33 (A**2) : -4.13000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.638         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.351         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.913                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2281 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2237 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3089 ; 1.081 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5138 ; 3.584 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   276 ; 4.994 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    90 ;36.604 ;23.222       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   404 ;15.544 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;11.297 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   347 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2488 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   502 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4HJO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB075549.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 6.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03319                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9863                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.15900                            
REMARK 200   FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.49400                            
REMARK 200   FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3GT8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.25 M SODIUM THIOCYANATE, 27% W/V       
REMARK 280  PEG3350, 10 MM TAURINE, PH 6.9, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 294.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.45900            
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       42.45900            
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  1.000000  0.000000  0.000000       38.98350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       57.14200            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       38.98350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       57.14200            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       42.45900            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       38.98350            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       57.14200            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       42.45900            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       38.98350            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       57.14200            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   662                                                      
REMARK 465     LYS A   663                                                      
REMARK 465     LYS A   664                                                      
REMARK 465     GLY A   665                                                      
REMARK 465     HIS A   666                                                      
REMARK 465     HIS A   667                                                      
REMARK 465     HIS A   668                                                      
REMARK 465     HIS A   669                                                      
REMARK 465     HIS A   670                                                      
REMARK 465     GLY A   671                                                      
REMARK 465     GLY A   672                                                      
REMARK 465     GLU A   673                                                      
REMARK 465     ALA A   674                                                      
REMARK 465     PRO A   675                                                      
REMARK 465     ASN A   676                                                      
REMARK 465     GLN A   677                                                      
REMARK 465     ALA A   678                                                      
REMARK 465     GLU A   710                                                      
REMARK 465     GLY A   711                                                      
REMARK 465     GLU A   712                                                      
REMARK 465     LYS A   713                                                      
REMARK 465     GLU A   961                                                      
REMARK 465     ARG A   962                                                      
REMARK 465     MET A   963                                                      
REMARK 465     HIS A   964                                                      
REMARK 465     LEU A   965                                                      
REMARK 465     PRO A   966                                                      
REMARK 465     SER A   967                                                      
REMARK 465     PRO A   968                                                      
REMARK 465     THR A   969                                                      
REMARK 465     ASP A   970                                                      
REMARK 465     SER A   971                                                      
REMARK 465     ASN A   972                                                      
REMARK 465     PHE A   973                                                      
REMARK 465     TYR A   974                                                      
REMARK 465     ARG A   975                                                      
REMARK 465     ALA A   976                                                      
REMARK 465     LEU A   977                                                      
REMARK 465     MET A   978                                                      
REMARK 465     ASP A   979                                                      
REMARK 465     GLU A   980                                                      
REMARK 465     GLU A   981                                                      
REMARK 465     ASP A   982                                                      
REMARK 465     MET A   983                                                      
REMARK 465     ASP A   984                                                      
REMARK 465     ASP A   985                                                      
REMARK 465     VAL A   986                                                      
REMARK 465     VAL A   987                                                      
REMARK 465     ASP A   988                                                      
REMARK 465     ALA A   989                                                      
REMARK 465     ASP A   990                                                      
REMARK 465     GLU A   991                                                      
REMARK 465     TYR A   992                                                      
REMARK 465     LEU A   993                                                      
REMARK 465     ILE A   994                                                      
REMARK 465     PRO A   995                                                      
REMARK 465     GLN A   996                                                      
REMARK 465     GLN A   997                                                      
REMARK 465     GLY A   998                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 689    CG   CD   CE   NZ                                   
REMARK 470     LYS A 715    CG   CD   CE   NZ                                   
REMARK 470     LYS A 733    CG   CD   CE   NZ                                   
REMARK 470     GLU A 734    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 776    CG   OD1  OD2                                       
REMARK 470     LYS A 843    CG   CD   CE   NZ                                   
REMARK 470     GLU A 844    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 943    CG   CD   OE1  OE2                                  
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 759     -153.28   -155.13                                   
REMARK 500    ARG A 812       -1.50     77.22                                   
REMARK 500    ASP A 813       60.85   -157.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AQ4 A 1001                
DBREF  4HJO A  672   998  UNP    P00533   EGFR_HUMAN     696   1022             
SEQADV 4HJO MET A  662  UNP  P00533              EXPRESSION TAG                 
SEQADV 4HJO LYS A  663  UNP  P00533              EXPRESSION TAG                 
SEQADV 4HJO LYS A  664  UNP  P00533              EXPRESSION TAG                 
SEQADV 4HJO GLY A  665  UNP  P00533              EXPRESSION TAG                 
SEQADV 4HJO HIS A  666  UNP  P00533              EXPRESSION TAG                 
SEQADV 4HJO HIS A  667  UNP  P00533              EXPRESSION TAG                 
SEQADV 4HJO HIS A  668  UNP  P00533              EXPRESSION TAG                 
SEQADV 4HJO HIS A  669  UNP  P00533              EXPRESSION TAG                 
SEQADV 4HJO HIS A  670  UNP  P00533              EXPRESSION TAG                 
SEQADV 4HJO GLY A  671  UNP  P00533              EXPRESSION TAG                 
SEQADV 4HJO ARG A  924  UNP  P00533    VAL   948 ENGINEERED MUTATION            
SEQRES   1 A  337  MET LYS LYS GLY HIS HIS HIS HIS HIS GLY GLY GLU ALA          
SEQRES   2 A  337  PRO ASN GLN ALA LEU LEU ARG ILE LEU LYS GLU THR GLU          
SEQRES   3 A  337  PHE LYS LYS ILE LYS VAL LEU GLY SER GLY ALA PHE GLY          
SEQRES   4 A  337  THR VAL TYR LYS GLY LEU TRP ILE PRO GLU GLY GLU LYS          
SEQRES   5 A  337  VAL LYS ILE PRO VAL ALA ILE LYS GLU LEU ARG GLU ALA          
SEQRES   6 A  337  THR SER PRO LYS ALA ASN LYS GLU ILE LEU ASP GLU ALA          
SEQRES   7 A  337  TYR VAL MET ALA SER VAL ASP ASN PRO HIS VAL CYS ARG          
SEQRES   8 A  337  LEU LEU GLY ILE CYS LEU THR SER THR VAL GLN LEU ILE          
SEQRES   9 A  337  THR GLN LEU MET PRO PHE GLY CYS LEU LEU ASP TYR VAL          
SEQRES  10 A  337  ARG GLU HIS LYS ASP ASN ILE GLY SER GLN TYR LEU LEU          
SEQRES  11 A  337  ASN TRP CYS VAL GLN ILE ALA LYS GLY MET ASN TYR LEU          
SEQRES  12 A  337  GLU ASP ARG ARG LEU VAL HIS ARG ASP LEU ALA ALA ARG          
SEQRES  13 A  337  ASN VAL LEU VAL LYS THR PRO GLN HIS VAL LYS ILE THR          
SEQRES  14 A  337  ASP PHE GLY LEU ALA LYS LEU LEU GLY ALA GLU GLU LYS          
SEQRES  15 A  337  GLU TYR HIS ALA GLU GLY GLY LYS VAL PRO ILE LYS TRP          
SEQRES  16 A  337  MET ALA LEU GLU SER ILE LEU HIS ARG ILE TYR THR HIS          
SEQRES  17 A  337  GLN SER ASP VAL TRP SER TYR GLY VAL THR VAL TRP GLU          
SEQRES  18 A  337  LEU MET THR PHE GLY SER LYS PRO TYR ASP GLY ILE PRO          
SEQRES  19 A  337  ALA SER GLU ILE SER SER ILE LEU GLU LYS GLY GLU ARG          
SEQRES  20 A  337  LEU PRO GLN PRO PRO ILE CYS THR ILE ASP VAL TYR MET          
SEQRES  21 A  337  ILE MET ARG LYS CYS TRP MET ILE ASP ALA ASP SER ARG          
SEQRES  22 A  337  PRO LYS PHE ARG GLU LEU ILE ILE GLU PHE SER LYS MET          
SEQRES  23 A  337  ALA ARG ASP PRO GLN ARG TYR LEU VAL ILE GLN GLY ASP          
SEQRES  24 A  337  GLU ARG MET HIS LEU PRO SER PRO THR ASP SER ASN PHE          
SEQRES  25 A  337  TYR ARG ALA LEU MET ASP GLU GLU ASP MET ASP ASP VAL          
SEQRES  26 A  337  VAL ASP ALA ASP GLU TYR LEU ILE PRO GLN GLN GLY              
HET    AQ4  A1001      29                                                       
HETNAM     AQ4 [6,7-BIS(2-METHOXY-ETHOXY)QUINAZOLINE-4-YL]-(3-                  
HETNAM   2 AQ4  ETHYNYLPHENYL)AMINE                                             
HETSYN     AQ4 ERLOTINIB                                                        
FORMUL   2  AQ4    C22 H23 N3 O4                                                
FORMUL   3  HOH   *34(H2 O)                                                     
HELIX    1   1 LYS A  684  THR A  686  5                                   3    
HELIX    2   2 ALA A  731  VAL A  745  1                                  15    
HELIX    3   3 LEU A  774  HIS A  781  1                                   8    
HELIX    4   4 GLY A  786  ARG A  807  1                                  22    
HELIX    5   5 ALA A  815  ARG A  817  5                                   3    
HELIX    6   6 GLY A  833  LEU A  838  1                                   6    
HELIX    7   7 PRO A  853  MET A  857  5                                   5    
HELIX    8   8 ALA A  858  ARG A  865  1                                   8    
HELIX    9   9 THR A  868  THR A  885  1                                  18    
HELIX   10  10 PRO A  895  SER A  897  5                                   3    
HELIX   11  11 GLU A  898  LYS A  905  1                                   8    
HELIX   12  12 THR A  916  CYS A  926  1                                  11    
HELIX   13  13 ASP A  930  ARG A  934  5                                   5    
HELIX   14  14 LYS A  936  ARG A  949  1                                  14    
HELIX   15  15 ASP A  950  LEU A  955  1                                   6    
SHEET    1   A 6 ARG A 681  ILE A 682  0                                        
SHEET    2   A 6 GLY A 755  LEU A 758  1  O  ILE A 756   N  ARG A 681           
SHEET    3   A 6 VAL A 762  GLN A 767 -1  O  GLN A 763   N  CYS A 757           
SHEET    4   A 6 ILE A 716  LEU A 723 -1  N  LEU A 723   O  VAL A 762           
SHEET    5   A 6 GLY A 700  TRP A 707 -1  N  TYR A 703   O  ILE A 720           
SHEET    6   A 6 PHE A 688  SER A 696 -1  N  LYS A 692   O  LYS A 704           
SHEET    1   B 3 GLY A 772  CYS A 773  0                                        
SHEET    2   B 3 VAL A 819  THR A 823 -1  O  VAL A 821   N  GLY A 772           
SHEET    3   B 3 HIS A 826  ILE A 829 -1  O  LYS A 828   N  LEU A 820           
SITE     1 AC1 16 VAL A 702  ALA A 719  LYS A 721  LEU A 764                    
SITE     2 AC1 16 THR A 766  GLN A 767  LEU A 768  MET A 769                    
SITE     3 AC1 16 PRO A 770  PHE A 771  GLY A 772  CYS A 773                    
SITE     4 AC1 16 LEU A 820  THR A 830  ASP A 831  HOH A1104                    
CRYST1   77.967  114.284   84.918  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012826  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008750  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011776        0.00000                         
ATOM      1  N   LEU A 679      43.836  16.026  -4.650  1.00 63.99           N  
ATOM      2  CA  LEU A 679      43.571  17.144  -5.541  1.00 64.75           C  
ATOM      3  C   LEU A 679      42.215  17.003  -6.208  1.00 62.85           C  
ATOM      4  O   LEU A 679      41.542  15.993  -6.059  1.00 64.21           O  
ATOM      5  CB  LEU A 679      44.652  17.236  -6.610  1.00 69.09           C  
ATOM      6  CG  LEU A 679      46.085  17.051  -6.123  1.00 72.14           C  
ATOM      7  CD1 LEU A 679      46.447  15.574  -6.103  1.00 71.82           C  
ATOM      8  CD2 LEU A 679      47.039  17.823  -7.019  1.00 70.89           C  
ATOM      9  N   LEU A 680      41.820  18.025  -6.951  1.00 58.53           N  
ATOM     10  CA  LEU A 680      40.576  17.978  -7.684  1.00 54.35           C  
ATOM     11  C   LEU A 680      40.821  17.386  -9.049  1.00 55.05           C  
ATOM     12  O   LEU A 680      41.626  17.893  -9.815  1.00 55.04           O  
ATOM     13  CB  LEU A 680      39.974  19.371  -7.836  1.00 51.29           C  
ATOM     14  CG  LEU A 680      38.602  19.386  -8.508  1.00 49.84           C  
ATOM     15  CD1 LEU A 680      37.562  18.703  -7.643  1.00 47.80           C  
ATOM     16  CD2 LEU A 680      38.167  20.789  -8.859  1.00 47.48           C  
ATOM     17  N   ARG A 681      40.117  16.306  -9.343  1.00 55.96           N  
ATOM     18  CA  ARG A 681      40.155  15.672 -10.661  1.00 55.98           C  
ATOM     19  C   ARG A 681      39.095  16.280 -11.578  1.00 54.16           C  
ATOM     20  O   ARG A 681      37.950  16.469 -11.166  1.00 55.41           O  
ATOM     21  CB  ARG A 681      39.914  14.164 -10.542  1.00 59.97           C  
ATOM     22  CG  ARG A 681      40.859  13.415  -9.615  1.00 65.14           C  
ATOM     23  CD  ARG A 681      42.146  13.007 -10.318  1.00 70.55           C  
ATOM     24  NE  ARG A 681      42.915  12.051  -9.519  1.00 75.02           N  
ATOM     25  CZ  ARG A 681      43.816  12.381  -8.595  1.00 75.94           C  
ATOM     26  NH1 ARG A 681      44.453  11.429  -7.927  1.00 76.76           N  
ATOM     27  NH2 ARG A 681      44.084  13.656  -8.334  1.00 75.33           N  
ATOM     28  N   ILE A 682      39.483  16.600 -12.811  1.00 51.93           N  
ATOM     29  CA  ILE A 682      38.541  17.053 -13.835  1.00 51.10           C  
ATOM     30  C   ILE A 682      38.159  15.840 -14.678  1.00 51.76           C  
ATOM     31  O   ILE A 682      39.025  15.158 -15.232  1.00 52.98           O  
ATOM     32  CB  ILE A 682      39.121  18.199 -14.710  1.00 50.04           C  
ATOM     33  CG1 ILE A 682      38.923  19.566 -14.044  1.00 48.42           C  
ATOM     34  CG2 ILE A 682      38.439  18.255 -16.071  1.00 48.76           C  
ATOM     35  CD1 ILE A 682      39.552  19.722 -12.673  1.00 48.85           C  
ATOM     36  N   LEU A 683      36.863  15.568 -14.762  1.00 52.05           N  
ATOM     37  CA  LEU A 683      36.382  14.340 -15.378  1.00 53.15           C  
ATOM     38  C   LEU A 683      35.650  14.562 -16.691  1.00 55.24           C  
ATOM     39  O   LEU A 683      35.065  15.620 -16.917  1.00 55.86           O  
ATOM     40  CB  LEU A 683      35.463  13.592 -14.413  1.00 52.91           C  
ATOM     41  CG  LEU A 683      36.115  12.711 -13.350  1.00 53.70           C  
ATOM     42  CD1 LEU A 683      36.696  13.544 -12.220  1.00 55.76           C  
ATOM     43  CD2 LEU A 683      35.086  11.743 -12.795  1.00 54.99           C  
ATOM     44  N   LYS A 684      35.699  13.550 -17.553  1.00 57.03           N  
ATOM     45  CA  LYS A 684      34.836  13.478 -18.722  1.00 58.88           C  
ATOM     46  C   LYS A 684      33.671  12.555 -18.390  1.00 58.35           C  
ATOM     47  O   LYS A 684      33.806  11.679 -17.537  1.00 56.48           O  
ATOM     48  CB  LYS A 684      35.600  12.921 -19.925  1.00 60.91           C  
ATOM     49  CG  LYS A 684      36.565  13.893 -20.584  1.00 61.73           C  
ATOM     50  CD  LYS A 684      37.187  13.277 -21.832  1.00 65.75           C  
ATOM     51  CE  LYS A 684      36.204  13.212 -22.997  1.00 67.79           C  
ATOM     52  NZ  LYS A 684      36.658  12.282 -24.070  1.00 64.81           N  
ATOM     53  N   GLU A 685      32.540  12.753 -19.070  1.00 60.87           N  
ATOM     54  CA  GLU A 685      31.340  11.917 -18.912  1.00 63.80           C  
ATOM     55  C   GLU A 685      31.634  10.422 -19.089  1.00 61.46           C  
ATOM     56  O   GLU A 685      30.990   9.574 -18.474  1.00 61.30           O  
ATOM     57  CB  GLU A 685      30.253  12.354 -19.903  1.00 68.68           C  
ATOM     58  CG  GLU A 685      28.897  11.684 -19.705  1.00 75.11           C  
ATOM     59  CD  GLU A 685      27.996  11.763 -20.931  1.00 81.52           C  
ATOM     60  OE1 GLU A 685      28.511  11.733 -22.074  1.00 83.43           O  
ATOM     61  OE2 GLU A 685      26.760  11.843 -20.753  1.00 82.19           O  
ATOM     62  N   THR A 686      32.620  10.119 -19.925  1.00 59.29           N  
ATOM     63  CA  THR A 686      33.003   8.746 -20.235  1.00 58.38           C  
ATOM     64  C   THR A 686      33.778   8.060 -19.100  1.00 56.15           C  
ATOM     65  O   THR A 686      33.995   6.850 -19.140  1.00 54.78           O  
ATOM     66  CB  THR A 686      33.859   8.693 -21.522  1.00 60.15           C  
ATOM     67  OG1 THR A 686      35.094   9.395 -21.312  1.00 60.31           O  
ATOM     68  CG2 THR A 686      33.114   9.313 -22.707  1.00 57.86           C  
ATOM     69  N   GLU A 687      34.189   8.834 -18.096  1.00 55.74           N  
ATOM     70  CA  GLU A 687      35.050   8.331 -17.015  1.00 53.11           C  
ATOM     71  C   GLU A 687      34.284   7.826 -15.792  1.00 51.08           C  
ATOM     72  O   GLU A 687      34.884   7.295 -14.858  1.00 52.42           O  
ATOM     73  CB  GLU A 687      36.067   9.395 -16.592  1.00 53.04           C  
ATOM     74  CG  GLU A 687      37.045   9.794 -17.688  1.00 55.82           C  
ATOM     75  CD  GLU A 687      38.013  10.878 -17.242  1.00 58.51           C  
ATOM     76  OE1 GLU A 687      38.002  11.980 -17.840  1.00 58.91           O  
ATOM     77  OE2 GLU A 687      38.783  10.635 -16.285  1.00 59.39           O  
ATOM     78  N   PHE A 688      32.965   7.993 -15.795  1.00 49.01           N  
ATOM     79  CA  PHE A 688      32.129   7.492 -14.706  1.00 47.50           C  
ATOM     80  C   PHE A 688      30.743   7.065 -15.183  1.00 45.20           C  
ATOM     81  O   PHE A 688      30.262   7.519 -16.223  1.00 44.00           O  
ATOM     82  CB  PHE A 688      32.023   8.522 -13.568  1.00 49.15           C  
ATOM     83  CG  PHE A 688      31.318   9.798 -13.952  1.00 51.75           C  
ATOM     84  CD1 PHE A 688      29.922   9.897 -13.883  1.00 51.22           C  
ATOM     85  CD2 PHE A 688      32.046  10.911 -14.370  1.00 51.59           C  
ATOM     86  CE1 PHE A 688      29.274  11.072 -14.236  1.00 51.17           C  
ATOM     87  CE2 PHE A 688      31.401  12.088 -14.722  1.00 52.31           C  
ATOM     88  CZ  PHE A 688      30.014  12.169 -14.655  1.00 52.05           C  
ATOM     89  N   LYS A 689      30.109   6.189 -14.410  1.00 44.90           N  
ATOM     90  CA  LYS A 689      28.751   5.735 -14.709  1.00 45.36           C  
ATOM     91  C   LYS A 689      27.849   5.874 -13.489  1.00 43.53           C  
ATOM     92  O   LYS A 689      28.262   5.571 -12.375  1.00 42.31           O  
ATOM     93  CB  LYS A 689      28.756   4.284 -15.214  1.00 45.25           C  
ATOM     94  N   LYS A 690      26.630   6.359 -13.714  1.00 44.41           N  
ATOM     95  CA  LYS A 690      25.594   6.411 -12.680  1.00 44.68           C  
ATOM     96  C   LYS A 690      24.750   5.149 -12.783  1.00 44.32           C  
ATOM     97  O   LYS A 690      24.266   4.809 -13.864  1.00 44.13           O  
ATOM     98  CB  LYS A 690      24.695   7.631 -12.860  1.00 45.40           C  
ATOM     99  CG  LYS A 690      25.430   8.931 -13.130  1.00 47.81           C  
ATOM    100  CD  LYS A 690      24.441  10.038 -13.451  1.00 48.23           C  
ATOM    101  CE  LYS A 690      25.055  11.075 -14.370  1.00 48.09           C  
ATOM    102  NZ  LYS A 690      25.318  10.532 -15.731  1.00 47.93           N  
ATOM    103  N   ILE A 691      24.665   4.413 -11.686  1.00 43.94           N  
ATOM    104  CA  ILE A 691      23.955   3.153 -11.692  1.00 45.11           C  
ATOM    105  C   ILE A 691      22.611   3.181 -10.979  1.00 45.81           C  
ATOM    106  O   ILE A 691      21.634   2.669 -11.493  1.00 44.80           O  
ATOM    107  CB  ILE A 691      24.834   2.024 -11.144  1.00 44.78           C  
ATOM    108  CG1 ILE A 691      26.180   2.029 -11.852  1.00 44.28           C  
ATOM    109  CG2 ILE A 691      24.158   0.687 -11.345  1.00 44.24           C  
ATOM    110  CD1 ILE A 691      27.353   1.856 -10.920  1.00 46.19           C  
ATOM    111  N   LYS A 692      22.563   3.775  -9.796  1.00 47.51           N  
ATOM    112  CA  LYS A 692      21.314   3.840  -9.050  1.00 49.98           C  
ATOM    113  C   LYS A 692      21.036   5.188  -8.413  1.00 49.60           C  
ATOM    114  O   LYS A 692      21.943   5.843  -7.928  1.00 50.57           O  
ATOM    115  CB  LYS A 692      21.285   2.767  -7.968  1.00 52.24           C  
ATOM    116  CG  LYS A 692      19.938   2.652  -7.284  1.00 53.85           C  
ATOM    117  CD  LYS A 692      19.970   1.610  -6.190  1.00 57.13           C  
ATOM    118  CE  LYS A 692      21.045   1.928  -5.173  1.00 60.65           C  
ATOM    119  NZ  LYS A 692      20.614   1.552  -3.799  1.00 61.81           N  
ATOM    120  N   VAL A 693      19.766   5.576  -8.382  1.00 46.54           N  
ATOM    121  CA  VAL A 693      19.357   6.794  -7.683  1.00 45.75           C  
ATOM    122  C   VAL A 693      19.325   6.542  -6.177  1.00 47.28           C  
ATOM    123  O   VAL A 693      18.547   5.720  -5.693  1.00 49.81           O  
ATOM    124  CB  VAL A 693      17.980   7.315  -8.155  1.00 42.46           C  
ATOM    125  CG1 VAL A 693      17.525   8.484  -7.294  1.00 40.75           C  
ATOM    126  CG2 VAL A 693      18.027   7.717  -9.622  1.00 40.77           C  
ATOM    127  N   LEU A 694      20.183   7.247  -5.448  1.00 48.64           N  
ATOM    128  CA  LEU A 694      20.214   7.173  -3.991  1.00 48.22           C  
ATOM    129  C   LEU A 694      19.220   8.132  -3.348  1.00 48.87           C  
ATOM    130  O   LEU A 694      18.631   7.817  -2.311  1.00 50.59           O  
ATOM    131  CB  LEU A 694      21.621   7.470  -3.467  1.00 46.92           C  
ATOM    132  CG  LEU A 694      22.669   6.360  -3.530  1.00 45.55           C  
ATOM    133  CD1 LEU A 694      24.001   6.911  -3.047  1.00 43.76           C  
ATOM    134  CD2 LEU A 694      22.252   5.149  -2.705  1.00 44.48           C  
ATOM    135  N   GLY A 695      19.140   9.325  -3.921  1.00 49.62           N  
ATOM    136  CA  GLY A 695      18.317  10.394  -3.406  1.00 49.26           C  
ATOM    137  C   GLY A 695      17.956  11.393  -4.478  1.00 50.07           C  
ATOM    138  O   GLY A 695      18.605  11.479  -5.503  1.00 50.28           O  
ATOM    139  N   SER A 696      16.914  12.163  -4.222  1.00 53.23           N  
ATOM    140  CA  SER A 696      16.467  13.179  -5.146  1.00 55.49           C  
ATOM    141  C   SER A 696      16.177  14.464  -4.398  1.00 57.60           C  
ATOM    142  O   SER A 696      15.935  14.453  -3.200  1.00 61.14           O  
ATOM    143  CB  SER A 696      15.234  12.713  -5.897  1.00 56.05           C  
ATOM    144  OG  SER A 696      15.452  12.821  -7.286  1.00 57.50           O  
ATOM    145  N   GLY A 697      16.223  15.574  -5.117  1.00 58.10           N  
ATOM    146  CA  GLY A 697      16.072  16.888  -4.531  1.00 57.89           C  
ATOM    147  C   GLY A 697      15.445  17.831  -5.529  1.00 60.03           C  
ATOM    148  O   GLY A 697      15.255  17.484  -6.689  1.00 57.56           O  
ATOM    149  N   ALA A 698      15.079  19.016  -5.072  1.00 62.17           N  
ATOM    150  CA  ALA A 698      14.599  20.042  -5.979  1.00 61.98           C  
ATOM    151  C   ALA A 698      15.692  20.438  -6.959  1.00 61.47           C  
ATOM    152  O   ALA A 698      15.442  20.624  -8.139  1.00 61.37           O  
ATOM    153  CB  ALA A 698      14.141  21.252  -5.191  1.00 62.03           C  
ATOM    154  N   PHE A 699      16.909  20.554  -6.449  1.00 60.60           N  
ATOM    155  CA  PHE A 699      18.057  21.030  -7.214  1.00 60.46           C  
ATOM    156  C   PHE A 699      18.827  19.952  -7.978  1.00 57.06           C  
ATOM    157  O   PHE A 699      19.596  20.272  -8.881  1.00 56.94           O  
ATOM    158  CB  PHE A 699      19.009  21.800  -6.300  1.00 65.06           C  
ATOM    159  CG  PHE A 699      18.373  22.971  -5.603  1.00 68.27           C  
ATOM    160  CD1 PHE A 699      17.828  24.028  -6.333  1.00 69.58           C  
ATOM    161  CD2 PHE A 699      18.333  23.028  -4.211  1.00 70.32           C  
ATOM    162  CE1 PHE A 699      17.251  25.113  -5.689  1.00 71.36           C  
ATOM    163  CE2 PHE A 699      17.762  24.113  -3.560  1.00 72.73           C  
ATOM    164  CZ  PHE A 699      17.220  25.156  -4.300  1.00 73.43           C  
ATOM    165  N   GLY A 700      18.626  18.685  -7.626  1.00 55.25           N  
ATOM    166  CA  GLY A 700      19.318  17.597  -8.317  1.00 52.26           C  
ATOM    167  C   GLY A 700      19.055  16.198  -7.794  1.00 49.11           C  
ATOM    168  O   GLY A 700      18.042  15.949  -7.137  1.00 47.54           O  
ATOM    169  N   THR A 701      19.984  15.289  -8.095  1.00 46.70           N  
ATOM    170  CA  THR A 701      19.841  13.864  -7.783  1.00 45.50           C  
ATOM    171  C   THR A 701      21.194  13.241  -7.419  1.00 43.24           C  
ATOM    172  O   THR A 701      22.211  13.534  -8.053  1.00 41.03           O  
ATOM    173  CB  THR A 701      19.209  13.102  -8.977  1.00 47.15           C  
ATOM    174  OG1 THR A 701      17.963  13.716  -9.334  1.00 48.16           O  
ATOM    175  CG2 THR A 701      18.954  11.635  -8.642  1.00 46.69           C  
ATOM    176  N   VAL A 702      21.191  12.387  -6.396  1.00 41.30           N  
ATOM    177  CA  VAL A 702      22.398  11.690  -5.958  1.00 41.18           C  
ATOM    178  C   VAL A 702      22.405  10.232  -6.431  1.00 41.94           C  
ATOM    179  O   VAL A 702      21.434   9.496  -6.238  1.00 40.60           O  
ATOM    180  CB  VAL A 702      22.594  11.765  -4.426  1.00 40.61           C  
ATOM    181  CG1 VAL A 702      23.918  11.126  -4.018  1.00 39.58           C  
ATOM    182  CG2 VAL A 702      22.552  13.211  -3.953  1.00 40.29           C  
ATOM    183  N   TYR A 703      23.520   9.831  -7.041  1.00 42.38           N  
ATOM    184  CA  TYR A 703      23.655   8.521  -7.669  1.00 41.85           C  
ATOM    185  C   TYR A 703      24.700   7.645  -7.021  1.00 40.64           C  
ATOM    186  O   TYR A 703      25.731   8.124  -6.562  1.00 40.27           O  
ATOM    187  CB  TYR A 703      24.026   8.683  -9.138  1.00 43.39           C  
ATOM    188  CG  TYR A 703      22.891   9.169  -9.989  1.00 45.94           C  
ATOM    189  CD1 TYR A 703      21.986   8.271 -10.553  1.00 46.19           C  
ATOM    190  CD2 TYR A 703      22.710  10.528 -10.228  1.00 46.23           C  
ATOM    191  CE1 TYR A 703      20.939   8.715 -11.338  1.00 46.88           C  
ATOM    192  CE2 TYR A 703      21.662  10.980 -11.008  1.00 47.01           C  
ATOM    193  CZ  TYR A 703      20.784  10.068 -11.557  1.00 47.26           C  
ATOM    194  OH  TYR A 703      19.747  10.513 -12.333  1.00 52.35           O  
ATOM    195  N   LYS A 704      24.419   6.349  -6.993  1.00 41.26           N  
ATOM    196  CA  LYS A 704      25.434   5.360  -6.698  1.00 42.41           C  
ATOM    197  C   LYS A 704      26.036   5.005  -8.041  1.00 41.55           C  
ATOM    198  O   LYS A 704      25.311   4.657  -8.982  1.00 40.35           O  
ATOM    199  CB  LYS A 704      24.822   4.128  -6.040  1.00 44.36           C  
ATOM    200  CG  LYS A 704      25.819   3.219  -5.341  1.00 46.50           C  
ATOM    201  CD  LYS A 704      25.103   2.012  -4.754  1.00 49.45           C  
ATOM    202  CE  LYS A 704      25.820   1.475  -3.525  1.00 51.95           C  
ATOM    203  NZ  LYS A 704      24.946   0.532  -2.768  1.00 52.92           N  
ATOM    204  N   GLY A 705      27.354   5.129  -8.142  1.00 40.55           N  
ATOM    205  CA  GLY A 705      28.033   4.871  -9.400  1.00 40.86           C  
ATOM    206  C   GLY A 705      29.449   4.355  -9.264  1.00 41.81           C  
ATOM    207  O   GLY A 705      29.912   4.022  -8.164  1.00 40.90           O  
ATOM    208  N   LEU A 706      30.134   4.288 -10.399  1.00 43.17           N  
ATOM    209  CA  LEU A 706      31.529   3.897 -10.436  1.00 44.93           C  
ATOM    210  C   LEU A 706      32.381   4.963 -11.080  1.00 45.80           C  
ATOM    211  O   LEU A 706      31.916   5.730 -11.919  1.00 45.52           O  
ATOM    212  CB  LEU A 706      31.700   2.595 -11.205  1.00 46.87           C  
ATOM    213  CG  LEU A 706      31.257   1.321 -10.496  1.00 48.34           C  
ATOM    214  CD1 LEU A 706      31.026   0.253 -11.545  1.00 50.41           C  
ATOM    215  CD2 LEU A 706      32.275   0.870  -9.457  1.00 47.72           C  
ATOM    216  N   TRP A 707      33.645   4.987 -10.687  1.00 48.63           N  
ATOM    217  CA  TRP A 707      34.612   5.900 -11.253  1.00 50.13           C  
ATOM    218  C   TRP A 707      35.776   5.110 -11.758  1.00 50.57           C  
ATOM    219  O   TRP A 707      36.364   4.312 -11.026  1.00 47.31           O  
ATOM    220  CB  TRP A 707      35.034   6.904 -10.193  1.00 51.81           C  
ATOM    221  CG  TRP A 707      36.101   7.889 -10.600  1.00 53.47           C  
ATOM    222  CD1 TRP A 707      36.400   8.359 -11.880  1.00 54.11           C  
ATOM    223  CD2 TRP A 707      37.025   8.599  -9.707  1.00 54.64           C  
ATOM    224  NE1 TRP A 707      37.431   9.266 -11.839  1.00 55.59           N  
ATOM    225  CE2 TRP A 707      37.847   9.460 -10.567  1.00 56.10           C  
ATOM    226  CE3 TRP A 707      37.248   8.603  -8.334  1.00 54.99           C  
ATOM    227  CZ2 TRP A 707      38.844  10.276 -10.051  1.00 58.38           C  
ATOM    228  CZ3 TRP A 707      38.251   9.435  -7.824  1.00 56.87           C  
ATOM    229  CH2 TRP A 707      39.031  10.248  -8.663  1.00 58.96           C  
ATOM    230  N   ILE A 708      36.093   5.317 -13.034  1.00 54.97           N  
ATOM    231  CA  ILE A 708      37.219   4.660 -13.694  1.00 57.73           C  
ATOM    232  C   ILE A 708      38.264   5.729 -14.020  1.00 57.50           C  
ATOM    233  O   ILE A 708      38.192   6.344 -15.084  1.00 58.15           O  
ATOM    234  CB  ILE A 708      36.798   3.918 -15.001  1.00 59.48           C  
ATOM    235  CG1 ILE A 708      35.433   3.217 -14.866  1.00 60.00           C  
ATOM    236  CG2 ILE A 708      37.859   2.904 -15.414  1.00 60.36           C  
ATOM    237  CD1 ILE A 708      34.258   3.991 -15.441  1.00 58.76           C  
ATOM    238  N   PRO A 709      39.222   5.972 -13.096  1.00 58.51           N  
ATOM    239  CA  PRO A 709      40.273   6.978 -13.311  1.00 59.55           C  
ATOM    240  C   PRO A 709      41.281   6.556 -14.379  1.00 61.54           C  
ATOM    241  O   PRO A 709      41.035   6.751 -15.573  1.00 62.35           O  
ATOM    242  CB  PRO A 709      40.968   7.065 -11.946  1.00 58.74           C  
ATOM    243  CG  PRO A 709      40.010   6.459 -10.974  1.00 57.93           C  
ATOM    244  CD  PRO A 709      39.316   5.384 -11.750  1.00 57.58           C  
ATOM    245  N   VAL A 714      41.222   0.396 -13.494  1.00 73.08           N  
ATOM    246  CA  VAL A 714      40.519   0.016 -12.266  1.00 77.21           C  
ATOM    247  C   VAL A 714      39.261   0.869 -12.017  1.00 80.16           C  
ATOM    248  O   VAL A 714      39.207   2.043 -12.405  1.00 82.50           O  
ATOM    249  CB  VAL A 714      41.456   0.037 -11.032  1.00 77.11           C  
ATOM    250  CG1 VAL A 714      42.551  -1.013 -11.176  1.00 75.61           C  
ATOM    251  CG2 VAL A 714      42.056   1.421 -10.809  1.00 76.87           C  
ATOM    252  N   LYS A 715      38.255   0.270 -11.377  1.00 75.87           N  
ATOM    253  CA  LYS A 715      36.967   0.932 -11.147  1.00 69.99           C  
ATOM    254  C   LYS A 715      36.548   0.864  -9.680  1.00 66.07           C  
ATOM    255  O   LYS A 715      36.447  -0.220  -9.108  1.00 67.75           O  
ATOM    256  CB  LYS A 715      35.880   0.323 -12.041  1.00 68.41           C  
ATOM    257  N   ILE A 716      36.309   2.027  -9.078  1.00 62.29           N  
ATOM    258  CA  ILE A 716      35.918   2.100  -7.667  1.00 59.68           C  
ATOM    259  C   ILE A 716      34.587   2.845  -7.462  1.00 56.77           C  
ATOM    260  O   ILE A 716      34.255   3.747  -8.236  1.00 56.49           O  
ATOM    261  CB  ILE A 716      37.053   2.672  -6.776  1.00 61.74           C  
ATOM    262  CG1 ILE A 716      37.392   4.122  -7.140  1.00 60.16           C  
ATOM    263  CG2 ILE A 716      38.285   1.769  -6.817  1.00 64.33           C  
ATOM    264  CD1 ILE A 716      36.776   5.130  -6.190  1.00 59.85           C  
ATOM    265  N   PRO A 717      33.817   2.469  -6.422  1.00 54.04           N  
ATOM    266  CA  PRO A 717      32.461   2.999  -6.308  1.00 51.31           C  
ATOM    267  C   PRO A 717      32.383   4.360  -5.622  1.00 47.37           C  
ATOM    268  O   PRO A 717      33.031   4.585  -4.598  1.00 46.46           O  
ATOM    269  CB  PRO A 717      31.727   1.925  -5.488  1.00 52.17           C  
ATOM    270  CG  PRO A 717      32.792   1.150  -4.781  1.00 54.76           C  
ATOM    271  CD  PRO A 717      34.144   1.568  -5.301  1.00 55.63           C  
ATOM    272  N   VAL A 718      31.575   5.251  -6.192  1.00 43.76           N  
ATOM    273  CA  VAL A 718      31.435   6.614  -5.685  1.00 41.27           C  
ATOM    274  C   VAL A 718      29.982   7.072  -5.617  1.00 40.72           C  
ATOM    275  O   VAL A 718      29.075   6.415  -6.155  1.00 40.51           O  
ATOM    276  CB  VAL A 718      32.211   7.633  -6.546  1.00 40.79           C  
ATOM    277  CG1 VAL A 718      33.714   7.411  -6.437  1.00 41.05           C  
ATOM    278  CG2 VAL A 718      31.731   7.605  -7.997  1.00 39.76           C  
ATOM    279  N   ALA A 719      29.781   8.203  -4.943  1.00 38.77           N  
ATOM    280  CA  ALA A 719      28.523   8.927  -4.983  1.00 37.80           C  
ATOM    281  C   ALA A 719      28.628  10.031  -6.015  1.00 38.58           C  
ATOM    282  O   ALA A 719      29.670  10.690  -6.137  1.00 38.48           O  
ATOM    283  CB  ALA A 719      28.203   9.516  -3.628  1.00 37.85           C  
ATOM    284  N   ILE A 720      27.545  10.227  -6.760  1.00 38.64           N  
ATOM    285  CA  ILE A 720      27.509  11.234  -7.805  1.00 39.28           C  
ATOM    286  C   ILE A 720      26.291  12.140  -7.648  1.00 39.87           C  
ATOM    287  O   ILE A 720      25.154  11.698  -7.786  1.00 41.75           O  
ATOM    288  CB  ILE A 720      27.547  10.591  -9.208  1.00 40.00           C  
ATOM    289  CG1 ILE A 720      28.853   9.814  -9.402  1.00 40.24           C  
ATOM    290  CG2 ILE A 720      27.412  11.660 -10.288  1.00 41.39           C  
ATOM    291  CD1 ILE A 720      28.742   8.643 -10.354  1.00 40.41           C  
ATOM    292  N   LYS A 721      26.549  13.407  -7.345  1.00 40.36           N  
ATOM    293  CA  LYS A 721      25.515  14.422  -7.229  1.00 40.28           C  
ATOM    294  C   LYS A 721      25.456  15.176  -8.538  1.00 40.74           C  
ATOM    295  O   LYS A 721      26.411  15.859  -8.906  1.00 39.35           O  
ATOM    296  CB  LYS A 721      25.860  15.390  -6.095  1.00 41.57           C  
ATOM    297  CG  LYS A 721      24.924  16.579  -5.915  1.00 42.19           C  
ATOM    298  CD  LYS A 721      23.873  16.283  -4.858  1.00 43.27           C  
ATOM    299  CE  LYS A 721      23.491  17.525  -4.068  1.00 43.37           C  
ATOM    300  NZ  LYS A 721      23.103  17.163  -2.672  1.00 42.95           N  
ATOM    301  N   GLU A 722      24.339  15.038  -9.244  1.00 43.46           N  
ATOM    302  CA  GLU A 722      24.104  15.809 -10.454  1.00 46.03           C  
ATOM    303  C   GLU A 722      23.140  16.946 -10.151  1.00 46.43           C  
ATOM    304  O   GLU A 722      22.136  16.751  -9.463  1.00 49.18           O  
ATOM    305  CB  GLU A 722      23.563  14.922 -11.576  1.00 49.50           C  
ATOM    306  CG  GLU A 722      23.394  15.647 -12.909  1.00 54.72           C  
ATOM    307  CD  GLU A 722      23.260  14.706 -14.101  1.00 59.20           C  
ATOM    308  OE1 GLU A 722      22.789  13.552 -13.920  1.00 59.50           O  
ATOM    309  OE2 GLU A 722      23.620  15.131 -15.228  1.00 58.15           O  
ATOM    310  N   LEU A 723      23.460  18.136 -10.647  1.00 45.88           N  
ATOM    311  CA  LEU A 723      22.576  19.287 -10.497  1.00 45.23           C  
ATOM    312  C   LEU A 723      21.894  19.582 -11.814  1.00 44.89           C  
ATOM    313  O   LEU A 723      22.556  19.656 -12.851  1.00 44.02           O  
ATOM    314  CB  LEU A 723      23.347  20.521 -10.038  1.00 44.29           C  
ATOM    315  CG  LEU A 723      24.027  20.494  -8.677  1.00 44.24           C  
ATOM    316  CD1 LEU A 723      24.694  21.836  -8.437  1.00 44.07           C  
ATOM    317  CD2 LEU A 723      23.030  20.175  -7.573  1.00 45.97           C  
ATOM    318  N   ARG A 724      20.571  19.749 -11.767  1.00 46.16           N  
ATOM    319  CA  ARG A 724      19.783  20.038 -12.963  1.00 46.31           C  
ATOM    320  C   ARG A 724      20.328  21.286 -13.648  1.00 44.40           C  
ATOM    321  O   ARG A 724      20.788  22.210 -12.982  1.00 43.34           O  
ATOM    322  CB  ARG A 724      18.296  20.194 -12.624  1.00 47.49           C  
ATOM    323  CG  ARG A 724      17.616  18.897 -12.189  1.00 50.54           C  
ATOM    324  CD  ARG A 724      16.095  19.014 -12.103  1.00 51.39           C  
ATOM    325  NE  ARG A 724      15.662  20.201 -11.358  1.00 52.50           N  
ATOM    326  CZ  ARG A 724      15.219  21.322 -11.926  1.00 53.88           C  
ATOM    327  NH1 ARG A 724      15.136  21.412 -13.249  1.00 55.59           N  
ATOM    328  NH2 ARG A 724      14.855  22.355 -11.176  1.00 52.82           N  
ATOM    329  N   GLU A 725      20.309  21.296 -14.976  1.00 43.63           N  
ATOM    330  CA  GLU A 725      20.853  22.418 -15.728  1.00 44.27           C  
ATOM    331  C   GLU A 725      20.213  23.744 -15.281  1.00 44.57           C  
ATOM    332  O   GLU A 725      18.999  23.807 -15.036  1.00 44.33           O  
ATOM    333  CB  GLU A 725      20.694  22.197 -17.242  1.00 43.51           C  
ATOM    334  CG  GLU A 725      21.415  23.244 -18.083  1.00 44.61           C  
ATOM    335  CD  GLU A 725      21.445  22.941 -19.574  1.00 46.41           C  
ATOM    336  OE1 GLU A 725      21.052  21.824 -19.990  1.00 46.17           O  
ATOM    337  OE2 GLU A 725      21.875  23.837 -20.341  1.00 46.24           O  
ATOM    338  N   ALA A 726      21.052  24.777 -15.154  1.00 44.17           N  
ATOM    339  CA  ALA A 726      20.635  26.154 -14.837  1.00 44.63           C  
ATOM    340  C   ALA A 726      20.049  26.328 -13.438  1.00 45.45           C  
ATOM    341  O   ALA A 726      19.285  27.261 -13.186  1.00 45.45           O  
ATOM    342  CB  ALA A 726      19.677  26.691 -15.896  1.00 46.93           C  
ATOM    343  N   THR A 727      20.430  25.432 -12.532  1.00 46.57           N  
ATOM    344  CA  THR A 727      19.995  25.477 -11.141  1.00 45.96           C  
ATOM    345  C   THR A 727      20.937  26.355 -10.305  1.00 46.03           C  
ATOM    346  O   THR A 727      20.622  26.701  -9.166  1.00 48.25           O  
ATOM    347  CB  THR A 727      19.895  24.047 -10.554  1.00 47.71           C  
ATOM    348  OG1 THR A 727      19.028  24.036  -9.413  1.00 49.52           O  
ATOM    349  CG2 THR A 727      21.277  23.498 -10.168  1.00 47.43           C  
ATOM    350  N   SER A 728      22.089  26.705 -10.879  1.00 45.01           N  
ATOM    351  CA  SER A 728      23.078  27.556 -10.219  1.00 43.89           C  
ATOM    352  C   SER A 728      23.264  28.900 -10.926  1.00 44.03           C  
ATOM    353  O   SER A 728      23.424  28.943 -12.147  1.00 42.78           O  
ATOM    354  CB  SER A 728      24.429  26.843 -10.127  1.00 43.76           C  
ATOM    355  OG  SER A 728      25.459  27.765  -9.788  1.00 43.27           O  
ATOM    356  N   PRO A 729      23.278  29.999 -10.151  1.00 44.91           N  
ATOM    357  CA  PRO A 729      23.504  31.341 -10.694  1.00 45.61           C  
ATOM    358  C   PRO A 729      24.962  31.609 -11.087  1.00 47.24           C  
ATOM    359  O   PRO A 729      25.254  32.632 -11.715  1.00 49.26           O  
ATOM    360  CB  PRO A 729      23.103  32.274  -9.541  1.00 44.53           C  
ATOM    361  CG  PRO A 729      22.671  31.402  -8.412  1.00 45.72           C  
ATOM    362  CD  PRO A 729      23.142  30.014  -8.685  1.00 44.60           C  
ATOM    363  N   LYS A 730      25.864  30.701 -10.728  1.00 47.11           N  
ATOM    364  CA  LYS A 730      27.288  30.903 -10.965  1.00 46.62           C  
ATOM    365  C   LYS A 730      27.703  30.486 -12.370  1.00 45.36           C  
ATOM    366  O   LYS A 730      27.171  29.524 -12.923  1.00 44.35           O  
ATOM    367  CB  LYS A 730      28.116  30.128  -9.935  1.00 48.24           C  
ATOM    368  CG  LYS A 730      27.688  30.315  -8.488  1.00 49.43           C  
ATOM    369  CD  LYS A 730      28.144  31.655  -7.936  1.00 50.37           C  
ATOM    370  CE  LYS A 730      27.632  31.864  -6.522  1.00 49.93           C  
ATOM    371  NZ  LYS A 730      28.026  33.205  -6.011  1.00 51.12           N  
ATOM    372  N   ALA A 731      28.659  31.221 -12.935  1.00 45.93           N  
ATOM    373  CA  ALA A 731      29.303  30.848 -14.196  1.00 46.40           C  
ATOM    374  C   ALA A 731      30.333  29.742 -13.956  1.00 46.73           C  
ATOM    375  O   ALA A 731      30.750  29.506 -12.816  1.00 45.86           O  
ATOM    376  CB  ALA A 731      29.957  32.063 -14.840  1.00 45.18           C  
ATOM    377  N   ASN A 732      30.748  29.077 -15.031  1.00 46.53           N  
ATOM    378  CA  ASN A 732      31.650  27.930 -14.926  1.00 48.21           C  
ATOM    379  C   ASN A 732      33.012  28.196 -14.271  1.00 48.25           C  
ATOM    380  O   ASN A 732      33.574  27.300 -13.643  1.00 48.90           O  
ATOM    381  CB  ASN A 732      31.825  27.248 -16.286  1.00 48.94           C  
ATOM    382  CG  ASN A 732      30.704  26.269 -16.601  1.00 50.40           C  
ATOM    383  OD1 ASN A 732      29.934  25.862 -15.723  1.00 49.91           O  
ATOM    384  ND2 ASN A 732      30.615  25.877 -17.865  1.00 52.17           N  
ATOM    385  N   LYS A 733      33.535  29.413 -14.420  1.00 47.37           N  
ATOM    386  CA  LYS A 733      34.782  29.803 -13.758  1.00 46.71           C  
ATOM    387  C   LYS A 733      34.600  29.843 -12.239  1.00 46.70           C  
ATOM    388  O   LYS A 733      35.442  29.338 -11.492  1.00 48.03           O  
ATOM    389  CB  LYS A 733      35.279  31.160 -14.268  1.00 46.39           C  
ATOM    390  N   GLU A 734      33.488  30.428 -11.794  1.00 44.68           N  
ATOM    391  CA  GLU A 734      33.188  30.554 -10.372  1.00 42.17           C  
ATOM    392  C   GLU A 734      32.893  29.200  -9.724  1.00 41.76           C  
ATOM    393  O   GLU A 734      33.272  28.965  -8.576  1.00 42.43           O  
ATOM    394  CB  GLU A 734      32.026  31.530 -10.148  1.00 40.65           C  
ATOM    395  N   ILE A 735      32.235  28.322 -10.460  1.00 40.43           N  
ATOM    396  CA  ILE A 735      31.910  27.008  -9.951  1.00 39.65           C  
ATOM    397  C   ILE A 735      33.170  26.184  -9.798  1.00 40.67           C  
ATOM    398  O   ILE A 735      33.331  25.462  -8.829  1.00 40.78           O  
ATOM    399  CB  ILE A 735      30.923  26.295 -10.877  1.00 39.55           C  
ATOM    400  CG1 ILE A 735      29.578  27.002 -10.832  1.00 39.59           C  
ATOM    401  CG2 ILE A 735      30.743  24.845 -10.477  1.00 39.02           C  
ATOM    402  CD1 ILE A 735      28.569  26.428 -11.789  1.00 40.12           C  
ATOM    403  N   LEU A 736      34.067  26.310 -10.759  1.00 42.09           N  
ATOM    404  CA  LEU A 736      35.329  25.609 -10.712  1.00 42.74           C  
ATOM    405  C   LEU A 736      36.180  26.082  -9.554  1.00 42.87           C  
ATOM    406  O   LEU A 736      36.921  25.312  -8.968  1.00 41.95           O  
ATOM    407  CB  LEU A 736      36.085  25.805 -12.011  1.00 45.34           C  
ATOM    408  CG  LEU A 736      37.218  24.809 -12.193  1.00 47.03           C  
ATOM    409  CD1 LEU A 736      36.645  23.442 -12.521  1.00 46.78           C  
ATOM    410  CD2 LEU A 736      38.146  25.278 -13.292  1.00 47.86           C  
ATOM    411  N   ASP A 737      36.069  27.357  -9.218  1.00 43.11           N  
ATOM    412  CA  ASP A 737      36.795  27.899  -8.082  1.00 45.58           C  
ATOM    413  C   ASP A 737      36.290  27.324  -6.773  1.00 45.56           C  
ATOM    414  O   ASP A 737      37.066  26.893  -5.938  1.00 45.43           O  
ATOM    415  CB  ASP A 737      36.674  29.415  -8.048  1.00 47.41           C  
ATOM    416  CG  ASP A 737      37.355  30.075  -9.214  1.00 51.70           C  
ATOM    417  OD1 ASP A 737      37.681  29.371 -10.188  1.00 52.29           O  
ATOM    418  OD2 ASP A 737      37.556  31.302  -9.161  1.00 52.89           O  
ATOM    419  N   GLU A 738      34.975  27.334  -6.602  1.00 47.16           N  
ATOM    420  CA  GLU A 738      34.339  26.787  -5.403  1.00 45.43           C  
ATOM    421  C   GLU A 738      34.590  25.288  -5.294  1.00 41.88           C  
ATOM    422  O   GLU A 738      34.643  24.746  -4.193  1.00 40.81           O  
ATOM    423  CB  GLU A 738      32.837  27.088  -5.397  1.00 49.30           C  
ATOM    424  CG  GLU A 738      32.499  28.574  -5.503  1.00 55.41           C  
ATOM    425  CD  GLU A 738      31.000  28.856  -5.590  1.00 59.99           C  
ATOM    426  OE1 GLU A 738      30.219  28.181  -4.876  1.00 62.99           O  
ATOM    427  OE2 GLU A 738      30.604  29.765  -6.364  1.00 57.90           O  
ATOM    428  N   ALA A 739      34.761  24.636  -6.442  1.00 39.45           N  
ATOM    429  CA  ALA A 739      35.123  23.221  -6.502  1.00 39.06           C  
ATOM    430  C   ALA A 739      36.501  22.914  -5.905  1.00 38.87           C  
ATOM    431  O   ALA A 739      36.662  21.913  -5.206  1.00 38.66           O  
ATOM    432  CB  ALA A 739      35.030  22.706  -7.926  1.00 39.30           C  
ATOM    433  N   TYR A 740      37.486  23.770  -6.175  1.00 38.97           N  
ATOM    434  CA  TYR A 740      38.820  23.614  -5.581  1.00 37.85           C  
ATOM    435  C   TYR A 740      38.836  23.797  -4.062  1.00 37.50           C  
ATOM    436  O   TYR A 740      39.585  23.111  -3.361  1.00 37.79           O  
ATOM    437  CB  TYR A 740      39.834  24.532  -6.257  1.00 37.45           C  
ATOM    438  CG  TYR A 740      40.388  23.946  -7.533  1.00 39.19           C  
ATOM    439  CD1 TYR A 740      39.744  24.153  -8.751  1.00 39.43           C  
ATOM    440  CD2 TYR A 740      41.551  23.171  -7.524  1.00 40.16           C  
ATOM    441  CE1 TYR A 740      40.238  23.613  -9.925  1.00 39.83           C  
ATOM    442  CE2 TYR A 740      42.057  22.626  -8.695  1.00 40.20           C  
ATOM    443  CZ  TYR A 740      41.396  22.854  -9.894  1.00 41.57           C  
ATOM    444  OH  TYR A 740      41.879  22.319 -11.073  1.00 43.09           O  
ATOM    445  N   VAL A 741      38.011  24.711  -3.557  1.00 36.75           N  
ATOM    446  CA  VAL A 741      37.855  24.887  -2.111  1.00 36.49           C  
ATOM    447  C   VAL A 741      37.260  23.624  -1.481  1.00 37.42           C  
ATOM    448  O   VAL A 741      37.780  23.121  -0.487  1.00 37.86           O  
ATOM    449  CB  VAL A 741      36.990  26.118  -1.761  1.00 35.08           C  
ATOM    450  CG1 VAL A 741      36.784  26.218  -0.259  1.00 33.97           C  
ATOM    451  CG2 VAL A 741      37.630  27.392  -2.288  1.00 33.90           C  
ATOM    452  N   MET A 742      36.184  23.108  -2.074  1.00 38.24           N  
ATOM    453  CA  MET A 742      35.537  21.883  -1.594  1.00 39.03           C  
ATOM    454  C   MET A 742      36.497  20.691  -1.623  1.00 38.24           C  
ATOM    455  O   MET A 742      36.425  19.805  -0.772  1.00 37.47           O  
ATOM    456  CB  MET A 742      34.276  21.574  -2.412  1.00 40.49           C  
ATOM    457  CG  MET A 742      33.218  22.671  -2.372  1.00 43.83           C  
ATOM    458  SD  MET A 742      31.709  22.333  -3.313  1.00 47.54           S  
ATOM    459  CE  MET A 742      32.198  22.583  -5.013  1.00 44.59           C  
ATOM    460  N   ALA A 743      37.395  20.682  -2.605  1.00 38.47           N  
ATOM    461  CA  ALA A 743      38.370  19.604  -2.765  1.00 38.45           C  
ATOM    462  C   ALA A 743      39.514  19.710  -1.771  1.00 38.57           C  
ATOM    463  O   ALA A 743      40.113  18.704  -1.409  1.00 39.85           O  
ATOM    464  CB  ALA A 743      38.910  19.584  -4.182  1.00 38.84           C  
ATOM    465  N   SER A 744      39.813  20.929  -1.333  1.00 39.33           N  
ATOM    466  CA  SER A 744      40.903  21.173  -0.388  1.00 39.85           C  
ATOM    467  C   SER A 744      40.516  20.800   1.041  1.00 41.94           C  
ATOM    468  O   SER A 744      41.381  20.692   1.910  1.00 45.67           O  
ATOM    469  CB  SER A 744      41.328  22.639  -0.428  1.00 38.16           C  
ATOM    470  OG  SER A 744      40.481  23.430   0.390  1.00 37.22           O  
ATOM    471  N   VAL A 745      39.219  20.624   1.285  1.00 42.77           N  
ATOM    472  CA  VAL A 745      38.716  20.285   2.615  1.00 44.05           C  
ATOM    473  C   VAL A 745      39.355  18.978   3.088  1.00 46.01           C  
ATOM    474  O   VAL A 745      39.192  17.935   2.458  1.00 49.54           O  
ATOM    475  CB  VAL A 745      37.169  20.206   2.637  1.00 42.83           C  
ATOM    476  CG1 VAL A 745      36.678  19.435   3.850  1.00 43.50           C  
ATOM    477  CG2 VAL A 745      36.562  21.603   2.612  1.00 41.31           C  
ATOM    478  N   ASP A 746      40.098  19.053   4.186  1.00 47.42           N  
ATOM    479  CA  ASP A 746      40.875  17.916   4.674  1.00 47.90           C  
ATOM    480  C   ASP A 746      40.650  17.678   6.176  1.00 46.18           C  
ATOM    481  O   ASP A 746      41.360  18.224   7.024  1.00 46.95           O  
ATOM    482  CB  ASP A 746      42.358  18.128   4.342  1.00 51.29           C  
ATOM    483  CG  ASP A 746      43.225  16.936   4.710  1.00 53.91           C  
ATOM    484  OD1 ASP A 746      42.792  15.776   4.509  1.00 54.28           O  
ATOM    485  OD2 ASP A 746      44.356  17.172   5.190  1.00 54.80           O  
ATOM    486  N   ASN A 747      39.645  16.858   6.480  1.00 43.15           N  
ATOM    487  CA  ASN A 747      39.210  16.578   7.845  1.00 40.80           C  
ATOM    488  C   ASN A 747      38.439  15.254   7.895  1.00 40.55           C  
ATOM    489  O   ASN A 747      37.632  14.973   7.004  1.00 41.73           O  
ATOM    490  CB  ASN A 747      38.331  17.722   8.363  1.00 40.65           C  
ATOM    491  CG  ASN A 747      37.901  17.529   9.807  1.00 41.12           C  
ATOM    492  OD1 ASN A 747      36.919  16.848  10.093  1.00 41.62           O  
ATOM    493  ND2 ASN A 747      38.635  18.135  10.725  1.00 41.69           N  
ATOM    494  N   PRO A 748      38.594  14.513   8.974  1.00 39.48           N  
ATOM    495  CA  PRO A 748      37.956  13.212   9.110  1.00 39.18           C  
ATOM    496  C   PRO A 748      36.441  13.281   9.054  1.00 40.00           C  
ATOM    497  O   PRO A 748      35.814  12.367   8.556  1.00 40.42           O  
ATOM    498  CB  PRO A 748      38.392  12.773  10.499  1.00 38.75           C  
ATOM    499  CG  PRO A 748      39.657  13.508  10.763  1.00 39.83           C  
ATOM    500  CD  PRO A 748      39.839  14.581   9.740  1.00 38.80           C  
ATOM    501  N   HIS A 749      35.856  14.321   9.621  1.00 40.16           N  
ATOM    502  CA  HIS A 749      34.410  14.396   9.741  1.00 40.84           C  
ATOM    503  C   HIS A 749      33.709  15.283   8.717  1.00 40.39           C  
ATOM    504  O   HIS A 749      32.535  15.583   8.851  1.00 39.53           O  
ATOM    505  CB  HIS A 749      34.029  14.733  11.175  1.00 42.20           C  
ATOM    506  CG  HIS A 749      34.773  13.920  12.183  1.00 43.46           C  
ATOM    507  ND1 HIS A 749      35.777  14.442  12.965  1.00 44.30           N  
ATOM    508  CD2 HIS A 749      34.688  12.612  12.507  1.00 44.25           C  
ATOM    509  CE1 HIS A 749      36.268  13.493  13.740  1.00 45.86           C  
ATOM    510  NE2 HIS A 749      35.623  12.373  13.482  1.00 45.57           N  
ATOM    511  N   VAL A 750      34.448  15.717   7.705  1.00 40.05           N  
ATOM    512  CA  VAL A 750      33.872  16.422   6.568  1.00 40.06           C  
ATOM    513  C   VAL A 750      34.225  15.739   5.255  1.00 40.02           C  
ATOM    514  O   VAL A 750      35.371  15.423   5.014  1.00 38.63           O  
ATOM    515  CB  VAL A 750      34.341  17.883   6.498  1.00 40.19           C  
ATOM    516  CG1 VAL A 750      33.527  18.650   5.475  1.00 38.83           C  
ATOM    517  CG2 VAL A 750      34.231  18.544   7.855  1.00 39.74           C  
ATOM    518  N   CYS A 751      33.228  15.526   4.409  1.00 40.97           N  
ATOM    519  CA  CYS A 751      33.409  14.886   3.116  1.00 42.05           C  
ATOM    520  C   CYS A 751      34.189  15.763   2.153  1.00 43.04           C  
ATOM    521  O   CYS A 751      33.977  16.977   2.091  1.00 44.91           O  
ATOM    522  CB  CYS A 751      32.057  14.532   2.511  1.00 42.52           C  
ATOM    523  SG  CYS A 751      31.129  13.351   3.508  1.00 46.97           S  
ATOM    524  N   ARG A 752      35.086  15.130   1.403  1.00 42.41           N  
ATOM    525  CA  ARG A 752      35.933  15.821   0.445  1.00 42.03           C  
ATOM    526  C   ARG A 752      35.422  15.610  -0.978  1.00 41.07           C  
ATOM    527  O   ARG A 752      34.974  14.515  -1.332  1.00 40.93           O  
ATOM    528  CB  ARG A 752      37.372  15.313   0.574  1.00 43.67           C  
ATOM    529  CG  ARG A 752      38.388  16.147  -0.172  1.00 44.69           C  
ATOM    530  CD  ARG A 752      39.786  15.558  -0.111  1.00 46.19           C  
ATOM    531  NE  ARG A 752      40.517  15.969  -1.306  1.00 47.72           N  
ATOM    532  CZ  ARG A 752      40.705  15.201  -2.377  1.00 49.35           C  
ATOM    533  NH1 ARG A 752      40.256  13.949  -2.400  1.00 48.65           N  
ATOM    534  NH2 ARG A 752      41.361  15.684  -3.426  1.00 50.47           N  
ATOM    535  N   LEU A 753      35.531  16.633  -1.809  1.00 40.18           N  
ATOM    536  CA  LEU A 753      35.209  16.491  -3.214  1.00 38.30           C  
ATOM    537  C   LEU A 753      36.379  15.855  -3.951  1.00 38.63           C  
ATOM    538  O   LEU A 753      37.485  16.368  -3.924  1.00 36.88           O  
ATOM    539  CB  LEU A 753      34.873  17.841  -3.834  1.00 36.25           C  
ATOM    540  CG  LEU A 753      34.326  17.761  -5.251  1.00 35.41           C  
ATOM    541  CD1 LEU A 753      32.948  17.136  -5.260  1.00 34.77           C  
ATOM    542  CD2 LEU A 753      34.297  19.125  -5.895  1.00 35.91           C  
ATOM    543  N   LEU A 754      36.120  14.731  -4.607  1.00 38.94           N  
ATOM    544  CA  LEU A 754      37.148  14.005  -5.334  1.00 38.70           C  
ATOM    545  C   LEU A 754      37.284  14.509  -6.742  1.00 37.77           C  
ATOM    546  O   LEU A 754      38.382  14.645  -7.253  1.00 38.73           O  
ATOM    547  CB  LEU A 754      36.812  12.524  -5.404  1.00 38.99           C  
ATOM    548  CG  LEU A 754      36.564  11.837  -4.080  1.00 39.89           C  
ATOM    549  CD1 LEU A 754      36.576  10.336  -4.272  1.00 42.09           C  
ATOM    550  CD2 LEU A 754      37.624  12.276  -3.096  1.00 39.36           C  
ATOM    551  N   GLY A 755      36.156  14.744  -7.385  1.00 35.96           N  
ATOM    552  CA  GLY A 755      36.160  15.102  -8.780  1.00 36.11           C  
ATOM    553  C   GLY A 755      34.948  15.890  -9.182  1.00 36.52           C  
ATOM    554  O   GLY A 755      33.958  15.931  -8.478  1.00 35.81           O  
ATOM    555  N   ILE A 756      35.042  16.539 -10.325  1.00 36.58           N  
ATOM    556  CA  ILE A 756      33.911  17.246 -10.860  1.00 37.66           C  
ATOM    557  C   ILE A 756      33.825  17.033 -12.356  1.00 38.60           C  
ATOM    558  O   ILE A 756      34.832  16.986 -13.037  1.00 38.87           O  
ATOM    559  CB  ILE A 756      34.005  18.746 -10.549  1.00 37.68           C  
ATOM    560  CG1 ILE A 756      32.656  19.420 -10.774  1.00 38.28           C  
ATOM    561  CG2 ILE A 756      35.092  19.398 -11.382  1.00 36.50           C  
ATOM    562  CD1 ILE A 756      32.626  20.873 -10.372  1.00 37.72           C  
ATOM    563  N   CYS A 757      32.613  16.920 -12.866  1.00 39.85           N  
ATOM    564  CA  CYS A 757      32.413  16.927 -14.293  1.00 41.40           C  
ATOM    565  C   CYS A 757      31.628  18.175 -14.623  1.00 41.82           C  
ATOM    566  O   CYS A 757      30.503  18.341 -14.184  1.00 40.94           O  
ATOM    567  CB  CYS A 757      31.646  15.687 -14.734  1.00 42.22           C  
ATOM    568  SG  CYS A 757      31.725  15.345 -16.501  1.00 46.02           S  
ATOM    569  N   LEU A 758      32.217  19.047 -15.422  1.00 42.60           N  
ATOM    570  CA  LEU A 758      31.565  20.290 -15.754  1.00 43.93           C  
ATOM    571  C   LEU A 758      31.196  20.324 -17.210  1.00 46.12           C  
ATOM    572  O   LEU A 758      32.018  20.155 -18.093  1.00 46.84           O  
ATOM    573  CB  LEU A 758      32.434  21.488 -15.395  1.00 44.02           C  
ATOM    574  CG  LEU A 758      31.659  22.728 -14.962  1.00 45.02           C  
ATOM    575  CD1 LEU A 758      30.489  22.339 -14.083  1.00 45.16           C  
ATOM    576  CD2 LEU A 758      32.565  23.701 -14.234  1.00 45.18           C  
ATOM    577  N   THR A 759      29.923  20.566 -17.429  1.00 47.17           N  
ATOM    578  CA  THR A 759      29.307  20.532 -18.722  1.00 47.56           C  
ATOM    579  C   THR A 759      28.150  21.446 -18.479  1.00 47.03           C  
ATOM    580  O   THR A 759      28.215  22.298 -17.609  1.00 45.46           O  
ATOM    581  CB  THR A 759      28.811  19.131 -19.085  1.00 49.13           C  
ATOM    582  OG1 THR A 759      27.863  18.689 -18.109  1.00 52.42           O  
ATOM    583  CG2 THR A 759      29.961  18.169 -19.110  1.00 48.24           C  
ATOM    584  N   SER A 760      27.072  21.265 -19.222  1.00 47.95           N  
ATOM    585  CA  SER A 760      25.863  22.050 -19.020  1.00 47.98           C  
ATOM    586  C   SER A 760      25.305  21.791 -17.639  1.00 46.69           C  
ATOM    587  O   SER A 760      24.735  22.673 -17.016  1.00 46.60           O  
ATOM    588  CB  SER A 760      24.833  21.761 -20.096  1.00 49.43           C  
ATOM    589  OG  SER A 760      25.192  22.405 -21.301  1.00 53.88           O  
ATOM    590  N   THR A 761      25.536  20.590 -17.136  1.00 46.27           N  
ATOM    591  CA  THR A 761      25.148  20.255 -15.777  1.00 47.22           C  
ATOM    592  C   THR A 761      26.372  20.014 -14.910  1.00 45.87           C  
ATOM    593  O   THR A 761      27.350  19.442 -15.351  1.00 47.13           O  
ATOM    594  CB  THR A 761      24.228  19.023 -15.724  1.00 47.61           C  
ATOM    595  OG1 THR A 761      24.984  17.848 -16.019  1.00 50.67           O  
ATOM    596  CG2 THR A 761      23.114  19.152 -16.726  1.00 46.40           C  
ATOM    597  N   VAL A 762      26.323  20.492 -13.679  1.00 43.55           N  
ATOM    598  CA  VAL A 762      27.382  20.223 -12.733  1.00 41.94           C  
ATOM    599  C   VAL A 762      27.191  18.857 -12.105  1.00 40.79           C  
ATOM    600  O   VAL A 762      26.124  18.544 -11.609  1.00 39.57           O  
ATOM    601  CB  VAL A 762      27.402  21.262 -11.609  1.00 41.23           C  
ATOM    602  CG1 VAL A 762      28.535  20.973 -10.648  1.00 39.97           C  
ATOM    603  CG2 VAL A 762      27.524  22.656 -12.185  1.00 41.90           C  
ATOM    604  N   GLN A 763      28.252  18.063 -12.114  1.00 40.09           N  
ATOM    605  CA  GLN A 763      28.253  16.753 -11.501  1.00 39.78           C  
ATOM    606  C   GLN A 763      29.423  16.602 -10.558  1.00 39.73           C  
ATOM    607  O   GLN A 763      30.532  16.989 -10.868  1.00 39.68           O  
ATOM    608  CB  GLN A 763      28.303  15.684 -12.567  1.00 41.15           C  
ATOM    609  CG  GLN A 763      26.954  15.395 -13.173  1.00 43.05           C  
ATOM    610  CD  GLN A 763      27.066  14.563 -14.414  1.00 44.71           C  
ATOM    611  OE1 GLN A 763      26.771  13.375 -14.403  1.00 45.77           O  
ATOM    612  NE2 GLN A 763      27.509  15.181 -15.494  1.00 45.17           N  
ATOM    613  N   LEU A 764      29.159  16.036  -9.395  1.00 38.35           N  
ATOM    614  CA  LEU A 764      30.136  16.007  -8.322  1.00 36.98           C  
ATOM    615  C   LEU A 764      30.378  14.590  -7.813  1.00 38.09           C  
ATOM    616  O   LEU A 764      29.428  13.864  -7.521  1.00 37.79           O  
ATOM    617  CB  LEU A 764      29.643  16.891  -7.176  1.00 35.57           C  
ATOM    618  CG  LEU A 764      29.370  18.363  -7.506  1.00 35.38           C  
ATOM    619  CD1 LEU A 764      28.487  19.010  -6.448  1.00 34.52           C  
ATOM    620  CD2 LEU A 764      30.665  19.145  -7.683  1.00 35.20           C  
ATOM    621  N   ILE A 765      31.645  14.193  -7.703  1.00 38.87           N  
ATOM    622  CA  ILE A 765      31.963  12.879  -7.144  1.00 40.96           C  
ATOM    623  C   ILE A 765      32.638  12.939  -5.765  1.00 41.84           C  
ATOM    624  O   ILE A 765      33.614  13.662  -5.555  1.00 41.44           O  
ATOM    625  CB  ILE A 765      32.768  11.977  -8.116  1.00 42.41           C  
ATOM    626  CG1 ILE A 765      34.258  12.311  -8.064  1.00 44.63           C  
ATOM    627  CG2 ILE A 765      32.201  12.035  -9.534  1.00 42.07           C  
ATOM    628  CD1 ILE A 765      35.160  11.341  -8.802  1.00 48.32           C  
ATOM    629  N   THR A 766      32.080  12.189  -4.824  1.00 42.10           N  
ATOM    630  CA  THR A 766      32.687  12.003  -3.520  1.00 43.62           C  
ATOM    631  C   THR A 766      32.747  10.504  -3.267  1.00 44.26           C  
ATOM    632  O   THR A 766      32.172   9.715  -4.024  1.00 43.26           O  
ATOM    633  CB  THR A 766      31.873  12.667  -2.377  1.00 46.34           C  
ATOM    634  OG1 THR A 766      30.563  12.082  -2.302  1.00 47.62           O  
ATOM    635  CG2 THR A 766      31.756  14.184  -2.565  1.00 46.39           C  
ATOM    636  N   GLN A 767      33.439  10.124  -2.198  1.00 45.29           N  
ATOM    637  CA  GLN A 767      33.467   8.747  -1.733  1.00 45.21           C  
ATOM    638  C   GLN A 767      32.070   8.288  -1.316  1.00 44.86           C  
ATOM    639  O   GLN A 767      31.237   9.089  -0.893  1.00 44.68           O  
ATOM    640  CB  GLN A 767      34.429   8.621  -0.557  1.00 47.57           C  
ATOM    641  CG  GLN A 767      34.954   7.217  -0.306  1.00 49.07           C  
ATOM    642  CD  GLN A 767      35.759   7.130   0.975  1.00 52.28           C  
ATOM    643  OE1 GLN A 767      36.298   8.133   1.453  1.00 55.20           O  
ATOM    644  NE2 GLN A 767      35.847   5.928   1.542  1.00 53.64           N  
ATOM    645  N   LEU A 768      31.832   6.990  -1.454  1.00 44.55           N  
ATOM    646  CA  LEU A 768      30.568   6.372  -1.108  1.00 43.12           C  
ATOM    647  C   LEU A 768      30.594   5.949   0.358  1.00 45.11           C  
ATOM    648  O   LEU A 768      31.579   5.365   0.830  1.00 46.34           O  
ATOM    649  CB  LEU A 768      30.348   5.164  -2.013  1.00 42.88           C  
ATOM    650  CG  LEU A 768      29.012   4.427  -2.078  1.00 44.18           C  
ATOM    651  CD1 LEU A 768      27.871   5.341  -2.516  1.00 43.27           C  
ATOM    652  CD2 LEU A 768      29.153   3.247  -3.030  1.00 43.87           C  
ATOM    653  N   MET A 769      29.518   6.262   1.079  1.00 45.73           N  
ATOM    654  CA  MET A 769      29.384   5.892   2.484  1.00 46.11           C  
ATOM    655  C   MET A 769      28.482   4.670   2.604  1.00 47.90           C  
ATOM    656  O   MET A 769      27.280   4.758   2.345  1.00 49.19           O  
ATOM    657  CB  MET A 769      28.826   7.052   3.311  1.00 46.46           C  
ATOM    658  CG  MET A 769      29.671   8.315   3.273  1.00 48.20           C  
ATOM    659  SD  MET A 769      31.379   8.046   3.785  1.00 51.61           S  
ATOM    660  CE  MET A 769      32.146   9.549   3.200  1.00 51.61           C  
ATOM    661  N   PRO A 770      29.059   3.519   2.998  1.00 47.58           N  
ATOM    662  CA  PRO A 770      28.301   2.272   3.051  1.00 46.89           C  
ATOM    663  C   PRO A 770      26.949   2.415   3.755  1.00 45.43           C  
ATOM    664  O   PRO A 770      25.960   1.842   3.297  1.00 45.17           O  
ATOM    665  CB  PRO A 770      29.224   1.325   3.841  1.00 47.20           C  
ATOM    666  CG  PRO A 770      30.288   2.191   4.432  1.00 48.45           C  
ATOM    667  CD  PRO A 770      30.437   3.333   3.478  1.00 47.69           C  
ATOM    668  N   PHE A 771      26.902   3.193   4.833  1.00 42.34           N  
ATOM    669  CA  PHE A 771      25.714   3.227   5.686  1.00 40.99           C  
ATOM    670  C   PHE A 771      24.773   4.397   5.429  1.00 39.99           C  
ATOM    671  O   PHE A 771      23.670   4.444   5.968  1.00 39.45           O  
ATOM    672  CB  PHE A 771      26.110   3.107   7.161  1.00 41.23           C  
ATOM    673  CG  PHE A 771      26.792   1.807   7.481  1.00 41.95           C  
ATOM    674  CD1 PHE A 771      26.048   0.666   7.758  1.00 40.65           C  
ATOM    675  CD2 PHE A 771      28.186   1.712   7.459  1.00 41.94           C  
ATOM    676  CE1 PHE A 771      26.683  -0.538   8.028  1.00 42.46           C  
ATOM    677  CE2 PHE A 771      28.822   0.510   7.727  1.00 41.67           C  
ATOM    678  CZ  PHE A 771      28.071  -0.618   8.011  1.00 41.41           C  
ATOM    679  N   GLY A 772      25.209   5.330   4.593  1.00 39.94           N  
ATOM    680  CA  GLY A 772      24.339   6.389   4.115  1.00 39.43           C  
ATOM    681  C   GLY A 772      24.046   7.514   5.085  1.00 39.38           C  
ATOM    682  O   GLY A 772      24.814   7.788   6.005  1.00 38.81           O  
ATOM    683  N   CYS A 773      22.906   8.152   4.858  1.00 40.16           N  
ATOM    684  CA  CYS A 773      22.486   9.344   5.572  1.00 40.47           C  
ATOM    685  C   CYS A 773      22.131   9.097   7.038  1.00 39.44           C  
ATOM    686  O   CYS A 773      21.428   8.137   7.373  1.00 41.08           O  
ATOM    687  CB  CYS A 773      21.292   9.950   4.843  1.00 43.38           C  
ATOM    688  SG  CYS A 773      20.494  11.286   5.743  1.00 49.63           S  
ATOM    689  N   LEU A 774      22.598   9.986   7.904  1.00 37.67           N  
ATOM    690  CA  LEU A 774      22.395   9.837   9.344  1.00 37.50           C  
ATOM    691  C   LEU A 774      20.949  10.071   9.809  1.00 37.78           C  
ATOM    692  O   LEU A 774      20.544   9.533  10.845  1.00 37.85           O  
ATOM    693  CB  LEU A 774      23.364  10.740  10.116  1.00 37.11           C  
ATOM    694  CG  LEU A 774      23.356  10.731  11.647  1.00 35.80           C  
ATOM    695  CD1 LEU A 774      23.829   9.398  12.203  1.00 35.75           C  
ATOM    696  CD2 LEU A 774      24.225  11.861  12.167  1.00 35.80           C  
ATOM    697  N   LEU A 775      20.186  10.871   9.059  1.00 36.38           N  
ATOM    698  CA  LEU A 775      18.765  11.077   9.355  1.00 36.14           C  
ATOM    699  C   LEU A 775      17.968   9.784   9.209  1.00 35.96           C  
ATOM    700  O   LEU A 775      17.177   9.434  10.084  1.00 34.67           O  
ATOM    701  CB  LEU A 775      18.161  12.162   8.456  1.00 36.74           C  
ATOM    702  CG  LEU A 775      16.670  12.489   8.634  1.00 36.14           C  
ATOM    703  CD1 LEU A 775      16.383  13.087  10.008  1.00 34.97           C  
ATOM    704  CD2 LEU A 775      16.202  13.420   7.524  1.00 35.49           C  
ATOM    705  N   ASP A 776      18.188   9.079   8.100  1.00 36.54           N  
ATOM    706  CA  ASP A 776      17.511   7.813   7.843  1.00 36.80           C  
ATOM    707  C   ASP A 776      17.935   6.725   8.829  1.00 37.40           C  
ATOM    708  O   ASP A 776      17.099   5.932   9.266  1.00 38.77           O  
ATOM    709  CB  ASP A 776      17.740   7.357   6.404  1.00 36.60           C  
ATOM    710  N   TYR A 777      19.223   6.708   9.182  1.00 37.15           N  
ATOM    711  CA  TYR A 777      19.792   5.723  10.114  1.00 36.80           C  
ATOM    712  C   TYR A 777      19.120   5.760  11.492  1.00 37.59           C  
ATOM    713  O   TYR A 777      18.767   4.716  12.041  1.00 37.57           O  
ATOM    714  CB  TYR A 777      21.314   5.923  10.246  1.00 37.36           C  
ATOM    715  CG  TYR A 777      22.019   4.914  11.135  1.00 36.64           C  
ATOM    716  CD1 TYR A 777      22.051   5.077  12.519  1.00 37.10           C  
ATOM    717  CD2 TYR A 777      22.659   3.801  10.592  1.00 37.00           C  
ATOM    718  CE1 TYR A 777      22.688   4.160  13.338  1.00 37.58           C  
ATOM    719  CE2 TYR A 777      23.303   2.874  11.403  1.00 36.91           C  
ATOM    720  CZ  TYR A 777      23.318   3.058  12.776  1.00 37.66           C  
ATOM    721  OH  TYR A 777      23.948   2.146  13.599  1.00 37.71           O  
ATOM    722  N   VAL A 778      18.943   6.961  12.041  1.00 38.47           N  
ATOM    723  CA  VAL A 778      18.302   7.124  13.356  1.00 39.18           C  
ATOM    724  C   VAL A 778      16.786   6.912  13.320  1.00 40.56           C  
ATOM    725  O   VAL A 778      16.133   6.894  14.363  1.00 42.00           O  
ATOM    726  CB  VAL A 778      18.611   8.493  14.017  1.00 38.24           C  
ATOM    727  CG1 VAL A 778      20.114   8.720  14.114  1.00 37.88           C  
ATOM    728  CG2 VAL A 778      17.929   9.629  13.271  1.00 36.96           C  
ATOM    729  N   ARG A 779      16.229   6.767  12.122  1.00 41.14           N  
ATOM    730  CA  ARG A 779      14.831   6.391  11.984  1.00 41.26           C  
ATOM    731  C   ARG A 779      14.719   4.878  11.913  1.00 43.89           C  
ATOM    732  O   ARG A 779      13.804   4.297  12.490  1.00 44.51           O  
ATOM    733  CB  ARG A 779      14.213   7.035  10.749  1.00 39.30           C  
ATOM    734  CG  ARG A 779      13.920   8.508  10.925  1.00 36.85           C  
ATOM    735  CD  ARG A 779      13.656   9.174   9.594  1.00 34.98           C  
ATOM    736  NE  ARG A 779      13.338  10.582   9.795  1.00 34.57           N  
ATOM    737  CZ  ARG A 779      13.050  11.439   8.823  1.00 34.62           C  
ATOM    738  NH1 ARG A 779      13.031  11.034   7.561  1.00 35.15           N  
ATOM    739  NH2 ARG A 779      12.772  12.704   9.113  1.00 34.03           N  
ATOM    740  N   GLU A 780      15.660   4.246  11.213  1.00 46.78           N  
ATOM    741  CA  GLU A 780      15.700   2.791  11.114  1.00 49.65           C  
ATOM    742  C   GLU A 780      16.050   2.160  12.456  1.00 49.77           C  
ATOM    743  O   GLU A 780      15.483   1.134  12.823  1.00 49.93           O  
ATOM    744  CB  GLU A 780      16.703   2.335  10.049  1.00 53.68           C  
ATOM    745  CG  GLU A 780      16.430   2.846   8.635  1.00 59.33           C  
ATOM    746  CD  GLU A 780      15.495   1.958   7.822  1.00 62.63           C  
ATOM    747  OE1 GLU A 780      15.782   1.741   6.621  1.00 63.63           O  
ATOM    748  OE2 GLU A 780      14.474   1.481   8.366  1.00 62.26           O  
ATOM    749  N   HIS A 781      16.914   2.813  13.220  1.00 51.29           N  
ATOM    750  CA  HIS A 781      17.494   2.231  14.419  1.00 53.50           C  
ATOM    751  C   HIS A 781      17.101   2.794  15.756  1.00 54.89           C  
ATOM    752  O   HIS A 781      17.911   2.778  16.694  1.00 56.48           O  
ATOM    753  CB  HIS A 781      19.010   2.168  14.300  1.00 53.67           C  
ATOM    754  CG  HIS A 781      19.480   1.427  13.087  1.00 54.83           C  
ATOM    755  ND1 HIS A 781      19.610   2.014  11.895  1.00 56.75           N  
ATOM    756  CD2 HIS A 781      19.827   0.103  12.910  1.00 55.67           C  
ATOM    757  CE1 HIS A 781      20.028   1.116  10.997  1.00 55.99           C  
ATOM    758  NE2 HIS A 781      20.160  -0.054  11.618  1.00 56.56           N  
ATOM    759  N   LYS A 782      15.877   3.279  15.901  1.00 56.96           N  
ATOM    760  CA  LYS A 782      15.487   3.947  17.134  1.00 58.98           C  
ATOM    761  C   LYS A 782      15.669   3.035  18.331  1.00 62.03           C  
ATOM    762  O   LYS A 782      16.192   3.439  19.363  1.00 63.77           O  
ATOM    763  CB  LYS A 782      13.994   4.248  17.088  1.00 56.08           C  
ATOM    764  CG  LYS A 782      13.564   5.390  16.202  1.00 55.74           C  
ATOM    765  CD  LYS A 782      12.109   5.738  16.458  1.00 57.94           C  
ATOM    766  CE  LYS A 782      11.813   5.880  17.944  1.00 58.91           C  
ATOM    767  NZ  LYS A 782      11.364   7.245  18.332  1.00 56.88           N  
ATOM    768  N   ASP A 783      15.241   1.793  18.180  1.00 63.81           N  
ATOM    769  CA  ASP A 783      15.229   0.827  19.266  1.00 65.80           C  
ATOM    770  C   ASP A 783      16.617   0.455  19.752  1.00 65.27           C  
ATOM    771  O   ASP A 783      16.803   0.031  20.885  1.00 66.25           O  
ATOM    772  CB  ASP A 783      14.458  -0.417  18.847  1.00 68.65           C  
ATOM    773  CG  ASP A 783      13.054  -0.100  18.403  1.00 70.74           C  
ATOM    774  OD1 ASP A 783      12.524   0.951  18.809  1.00 71.13           O  
ATOM    775  OD2 ASP A 783      12.480  -0.901  17.644  1.00 71.99           O  
ATOM    776  N   ASN A 784      17.574   0.577  18.852  1.00 62.96           N  
ATOM    777  CA  ASN A 784      18.918   0.022  18.989  1.00 61.23           C  
ATOM    778  C   ASN A 784      20.013   1.050  19.338  1.00 58.58           C  
ATOM    779  O   ASN A 784      21.103   0.661  19.767  1.00 59.78           O  
ATOM    780  CB  ASN A 784      19.265  -0.782  17.719  1.00 63.32           C  
ATOM    781  CG  ASN A 784      20.743  -1.135  17.614  1.00 64.35           C  
ATOM    782  OD1 ASN A 784      21.234  -2.038  18.297  1.00 64.61           O  
ATOM    783  ND2 ASN A 784      21.455  -0.430  16.741  1.00 63.55           N  
ATOM    784  N   ILE A 785      19.726   2.345  19.180  1.00 54.04           N  
ATOM    785  CA  ILE A 785      20.745   3.396  19.391  1.00 51.35           C  
ATOM    786  C   ILE A 785      20.904   3.843  20.853  1.00 50.99           C  
ATOM    787  O   ILE A 785      19.942   4.261  21.502  1.00 51.12           O  
ATOM    788  CB  ILE A 785      20.524   4.634  18.488  1.00 49.64           C  
ATOM    789  CG1 ILE A 785      20.582   4.245  17.014  1.00 48.01           C  
ATOM    790  CG2 ILE A 785      21.583   5.698  18.759  1.00 50.56           C  
ATOM    791  CD1 ILE A 785      20.073   5.321  16.084  1.00 46.70           C  
ATOM    792  N   GLY A 786      22.139   3.765  21.349  1.00 50.01           N  
ATOM    793  CA  GLY A 786      22.460   4.150  22.715  1.00 49.78           C  
ATOM    794  C   GLY A 786      22.964   5.574  22.849  1.00 49.40           C  
ATOM    795  O   GLY A 786      23.306   6.221  21.855  1.00 49.57           O  
ATOM    796  N   SER A 787      23.008   6.047  24.095  1.00 49.57           N  
ATOM    797  CA  SER A 787      23.462   7.393  24.450  1.00 49.31           C  
ATOM    798  C   SER A 787      24.862   7.724  23.929  1.00 48.31           C  
ATOM    799  O   SER A 787      25.084   8.808  23.391  1.00 46.19           O  
ATOM    800  CB  SER A 787      23.447   7.570  25.971  1.00 50.59           C  
ATOM    801  OG  SER A 787      22.171   7.292  26.512  1.00 55.99           O  
ATOM    802  N   GLN A 788      25.792   6.787  24.110  1.00 49.33           N  
ATOM    803  CA  GLN A 788      27.188   6.945  23.709  1.00 49.11           C  
ATOM    804  C   GLN A 788      27.281   7.405  22.257  1.00 48.53           C  
ATOM    805  O   GLN A 788      27.936   8.407  21.947  1.00 47.88           O  
ATOM    806  CB  GLN A 788      27.928   5.615  23.895  1.00 52.57           C  
ATOM    807  CG  GLN A 788      29.430   5.658  23.650  1.00 53.86           C  
ATOM    808  CD  GLN A 788      30.192   6.264  24.809  1.00 56.57           C  
ATOM    809  OE1 GLN A 788      30.748   7.355  24.690  1.00 58.55           O  
ATOM    810  NE2 GLN A 788      30.215   5.563  25.945  1.00 56.58           N  
ATOM    811  N   TYR A 789      26.594   6.680  21.380  1.00 47.11           N  
ATOM    812  CA  TYR A 789      26.593   6.988  19.958  1.00 46.17           C  
ATOM    813  C   TYR A 789      26.076   8.395  19.682  1.00 43.54           C  
ATOM    814  O   TYR A 789      26.783   9.196  19.077  1.00 45.62           O  
ATOM    815  CB  TYR A 789      25.821   5.921  19.175  1.00 49.14           C  
ATOM    816  CG  TYR A 789      26.592   4.620  19.015  1.00 52.81           C  
ATOM    817  CD1 TYR A 789      27.101   3.940  20.130  1.00 54.69           C  
ATOM    818  CD2 TYR A 789      26.815   4.069  17.756  1.00 53.53           C  
ATOM    819  CE1 TYR A 789      27.813   2.758  19.989  1.00 56.21           C  
ATOM    820  CE2 TYR A 789      27.521   2.883  17.610  1.00 55.51           C  
ATOM    821  CZ  TYR A 789      28.017   2.232  18.726  1.00 56.07           C  
ATOM    822  OH  TYR A 789      28.718   1.053  18.583  1.00 56.65           O  
ATOM    823  N   LEU A 790      24.876   8.705  20.161  1.00 40.42           N  
ATOM    824  CA  LEU A 790      24.261  10.012  19.923  1.00 39.61           C  
ATOM    825  C   LEU A 790      25.170  11.189  20.275  1.00 39.74           C  
ATOM    826  O   LEU A 790      25.270  12.159  19.521  1.00 39.63           O  
ATOM    827  CB  LEU A 790      22.932  10.116  20.668  1.00 39.26           C  
ATOM    828  CG  LEU A 790      21.811   9.346  19.973  1.00 39.40           C  
ATOM    829  CD1 LEU A 790      20.826   8.784  20.980  1.00 39.18           C  
ATOM    830  CD2 LEU A 790      21.115  10.227  18.949  1.00 39.19           C  
ATOM    831  N   LEU A 791      25.844  11.088  21.413  1.00 39.80           N  
ATOM    832  CA  LEU A 791      26.776  12.117  21.850  1.00 40.05           C  
ATOM    833  C   LEU A 791      28.065  12.135  21.017  1.00 41.04           C  
ATOM    834  O   LEU A 791      28.597  13.209  20.729  1.00 40.36           O  
ATOM    835  CB  LEU A 791      27.080  11.960  23.345  1.00 39.12           C  
ATOM    836  CG  LEU A 791      25.889  12.160  24.293  1.00 38.56           C  
ATOM    837  CD1 LEU A 791      26.187  11.648  25.694  1.00 37.90           C  
ATOM    838  CD2 LEU A 791      25.448  13.617  24.328  1.00 37.90           C  
ATOM    839  N   ASN A 792      28.556  10.959  20.624  1.00 40.98           N  
ATOM    840  CA  ASN A 792      29.738  10.882  19.767  1.00 42.50           C  
ATOM    841  C   ASN A 792      29.536  11.574  18.420  1.00 42.75           C  
ATOM    842  O   ASN A 792      30.465  12.199  17.895  1.00 44.11           O  
ATOM    843  CB  ASN A 792      30.185   9.435  19.559  1.00 44.83           C  
ATOM    844  CG  ASN A 792      30.810   8.831  20.804  1.00 48.11           C  
ATOM    845  OD1 ASN A 792      31.281   9.545  21.694  1.00 48.24           O  
ATOM    846  ND2 ASN A 792      30.812   7.499  20.874  1.00 49.17           N  
ATOM    847  N   TRP A 793      28.324  11.466  17.875  1.00 40.58           N  
ATOM    848  CA  TRP A 793      27.973  12.140  16.626  1.00 39.66           C  
ATOM    849  C   TRP A 793      27.958  13.632  16.791  1.00 39.80           C  
ATOM    850  O   TRP A 793      28.377  14.358  15.894  1.00 41.16           O  
ATOM    851  CB  TRP A 793      26.617  11.676  16.103  1.00 39.19           C  
ATOM    852  CG  TRP A 793      26.498  10.191  15.841  1.00 38.70           C  
ATOM    853  CD1 TRP A 793      27.513   9.292  15.526  1.00 38.41           C  
ATOM    854  CD2 TRP A 793      25.268   9.389  15.825  1.00 38.51           C  
ATOM    855  NE1 TRP A 793      27.011   8.031  15.346  1.00 37.94           N  
ATOM    856  CE2 TRP A 793      25.677   8.017  15.506  1.00 37.97           C  
ATOM    857  CE3 TRP A 793      23.919   9.659  16.044  1.00 38.11           C  
ATOM    858  CZ2 TRP A 793      24.761   6.978  15.414  1.00 38.83           C  
ATOM    859  CZ3 TRP A 793      23.006   8.602  15.953  1.00 38.31           C  
ATOM    860  CH2 TRP A 793      23.417   7.294  15.643  1.00 38.04           C  
ATOM    861  N   CYS A 794      27.476  14.101  17.940  1.00 39.75           N  
ATOM    862  CA  CYS A 794      27.429  15.530  18.243  1.00 39.61           C  
ATOM    863  C   CYS A 794      28.817  16.141  18.308  1.00 37.90           C  
ATOM    864  O   CYS A 794      29.034  17.237  17.792  1.00 37.91           O  
ATOM    865  CB  CYS A 794      26.682  15.783  19.551  1.00 41.70           C  
ATOM    866  SG  CYS A 794      24.907  15.501  19.412  1.00 49.07           S  
ATOM    867  N   VAL A 795      29.749  15.426  18.934  1.00 35.93           N  
ATOM    868  CA  VAL A 795      31.141  15.851  19.003  1.00 35.62           C  
ATOM    869  C   VAL A 795      31.749  15.941  17.602  1.00 35.15           C  
ATOM    870  O   VAL A 795      32.474  16.888  17.288  1.00 34.56           O  
ATOM    871  CB  VAL A 795      31.986  14.897  19.886  1.00 36.56           C  
ATOM    872  CG1 VAL A 795      33.462  15.279  19.849  1.00 34.79           C  
ATOM    873  CG2 VAL A 795      31.476  14.892  21.324  1.00 35.75           C  
ATOM    874  N   GLN A 796      31.437  14.961  16.758  1.00 34.58           N  
ATOM    875  CA  GLN A 796      32.050  14.867  15.433  1.00 33.95           C  
ATOM    876  C   GLN A 796      31.570  15.958  14.466  1.00 33.62           C  
ATOM    877  O   GLN A 796      32.381  16.577  13.771  1.00 32.39           O  
ATOM    878  CB  GLN A 796      31.867  13.466  14.858  1.00 33.61           C  
ATOM    879  CG  GLN A 796      32.799  12.458  15.510  1.00 34.48           C  
ATOM    880  CD  GLN A 796      32.461  11.016  15.188  1.00 34.61           C  
ATOM    881  OE1 GLN A 796      32.073  10.682  14.070  1.00 35.84           O  
ATOM    882  NE2 GLN A 796      32.621  10.149  16.173  1.00 35.19           N  
ATOM    883  N   ILE A 797      30.258  16.188  14.436  1.00 33.08           N  
ATOM    884  CA  ILE A 797      29.682  17.290  13.672  1.00 32.32           C  
ATOM    885  C   ILE A 797      30.355  18.596  14.104  1.00 31.98           C  
ATOM    886  O   ILE A 797      30.848  19.349  13.273  1.00 32.10           O  
ATOM    887  CB  ILE A 797      28.147  17.376  13.858  1.00 32.21           C  
ATOM    888  CG1 ILE A 797      27.487  16.033  13.523  1.00 32.73           C  
ATOM    889  CG2 ILE A 797      27.560  18.479  12.991  1.00 31.37           C  
ATOM    890  CD1 ILE A 797      26.036  15.923  13.954  1.00 33.32           C  
ATOM    891  N   ALA A 798      30.393  18.843  15.409  1.00 31.97           N  
ATOM    892  CA  ALA A 798      31.114  19.988  15.948  1.00 32.61           C  
ATOM    893  C   ALA A 798      32.566  20.020  15.465  1.00 33.76           C  
ATOM    894  O   ALA A 798      33.021  21.057  14.981  1.00 34.32           O  
ATOM    895  CB  ALA A 798      31.050  19.997  17.469  1.00 32.08           C  
ATOM    896  N   LYS A 799      33.275  18.887  15.575  1.00 33.88           N  
ATOM    897  CA  LYS A 799      34.692  18.809  15.180  1.00 34.12           C  
ATOM    898  C   LYS A 799      34.911  19.170  13.720  1.00 35.03           C  
ATOM    899  O   LYS A 799      35.880  19.843  13.377  1.00 37.22           O  
ATOM    900  CB  LYS A 799      35.285  17.432  15.470  1.00 34.39           C  
ATOM    901  CG  LYS A 799      35.807  17.272  16.885  1.00 34.56           C  
ATOM    902  CD  LYS A 799      36.584  15.980  17.041  1.00 34.96           C  
ATOM    903  CE  LYS A 799      36.873  15.702  18.509  1.00 36.06           C  
ATOM    904  NZ  LYS A 799      37.627  14.429  18.688  1.00 37.86           N  
ATOM    905  N   GLY A 800      34.000  18.724  12.865  1.00 35.81           N  
ATOM    906  CA  GLY A 800      34.026  19.087  11.453  1.00 36.80           C  
ATOM    907  C   GLY A 800      33.636  20.531  11.203  1.00 36.57           C  
ATOM    908  O   GLY A 800      34.239  21.205  10.378  1.00 37.27           O  
ATOM    909  N   MET A 801      32.624  21.009  11.918  1.00 37.67           N  
ATOM    910  CA  MET A 801      32.176  22.399  11.784  1.00 39.08           C  
ATOM    911  C   MET A 801      33.246  23.381  12.253  1.00 37.43           C  
ATOM    912  O   MET A 801      33.439  24.437  11.651  1.00 36.21           O  
ATOM    913  CB  MET A 801      30.866  22.632  12.549  1.00 40.22           C  
ATOM    914  CG  MET A 801      29.627  22.026  11.905  1.00 41.62           C  
ATOM    915  SD  MET A 801      29.419  22.471  10.165  1.00 47.42           S  
ATOM    916  CE  MET A 801      29.177  24.243  10.277  1.00 47.35           C  
ATOM    917  N   ASN A 802      33.938  23.016  13.327  1.00 36.69           N  
ATOM    918  CA  ASN A 802      35.057  23.793  13.823  1.00 37.70           C  
ATOM    919  C   ASN A 802      36.209  23.864  12.822  1.00 37.26           C  
ATOM    920  O   ASN A 802      36.895  24.886  12.724  1.00 35.34           O  
ATOM    921  CB  ASN A 802      35.560  23.215  15.142  1.00 39.71           C  
ATOM    922  CG  ASN A 802      36.604  24.098  15.800  1.00 41.27           C  
ATOM    923  OD1 ASN A 802      37.768  23.723  15.903  1.00 42.42           O  
ATOM    924  ND2 ASN A 802      36.193  25.288  16.230  1.00 42.51           N  
ATOM    925  N   TYR A 803      36.419  22.777  12.084  1.00 36.60           N  
ATOM    926  CA  TYR A 803      37.467  22.753  11.082  1.00 37.23           C  
ATOM    927  C   TYR A 803      37.161  23.772  10.002  1.00 38.01           C  
ATOM    928  O   TYR A 803      38.034  24.558   9.610  1.00 39.33           O  
ATOM    929  CB  TYR A 803      37.614  21.365  10.480  1.00 37.42           C  
ATOM    930  CG  TYR A 803      38.523  21.336   9.284  1.00 37.74           C  
ATOM    931  CD1 TYR A 803      39.905  21.481   9.430  1.00 38.66           C  
ATOM    932  CD2 TYR A 803      38.006  21.178   7.997  1.00 39.42           C  
ATOM    933  CE1 TYR A 803      40.749  21.459   8.330  1.00 38.60           C  
ATOM    934  CE2 TYR A 803      38.843  21.153   6.887  1.00 40.00           C  
ATOM    935  CZ  TYR A 803      40.211  21.294   7.063  1.00 39.31           C  
ATOM    936  OH  TYR A 803      41.039  21.264   5.971  1.00 41.40           O  
ATOM    937  N   LEU A 804      35.911  23.761   9.544  1.00 38.24           N  
ATOM    938  CA  LEU A 804      35.422  24.714   8.553  1.00 38.14           C  
ATOM    939  C   LEU A 804      35.573  26.164   9.014  1.00 39.14           C  
ATOM    940  O   LEU A 804      35.955  27.027   8.216  1.00 38.01           O  
ATOM    941  CB  LEU A 804      33.965  24.410   8.182  1.00 37.10           C  
ATOM    942  CG  LEU A 804      33.719  23.161   7.325  1.00 36.72           C  
ATOM    943  CD1 LEU A 804      32.243  23.000   6.992  1.00 36.52           C  
ATOM    944  CD2 LEU A 804      34.558  23.167   6.051  1.00 36.49           C  
ATOM    945  N   GLU A 805      35.287  26.413  10.295  1.00 40.47           N  
ATOM    946  CA  GLU A 805      35.424  27.744  10.893  1.00 43.28           C  
ATOM    947  C   GLU A 805      36.875  28.237  10.905  1.00 44.09           C  
ATOM    948  O   GLU A 805      37.128  29.412  10.641  1.00 43.55           O  
ATOM    949  CB  GLU A 805      34.845  27.779  12.312  1.00 45.28           C  
ATOM    950  CG  GLU A 805      34.663  29.191  12.859  1.00 49.59           C  
ATOM    951  CD  GLU A 805      34.404  29.258  14.359  1.00 54.25           C  
ATOM    952  OE1 GLU A 805      34.395  28.199  15.034  1.00 59.75           O  
ATOM    953  OE2 GLU A 805      34.212  30.386  14.872  1.00 53.05           O  
ATOM    954  N   ASP A 806      37.812  27.335  11.212  1.00 45.43           N  
ATOM    955  CA  ASP A 806      39.248  27.647  11.222  1.00 46.59           C  
ATOM    956  C   ASP A 806      39.758  28.016   9.835  1.00 46.07           C  
ATOM    957  O   ASP A 806      40.673  28.834   9.694  1.00 45.19           O  
ATOM    958  CB  ASP A 806      40.063  26.465  11.760  1.00 48.23           C  
ATOM    959  CG  ASP A 806      40.057  26.388  13.274  1.00 51.83           C  
ATOM    960  OD1 ASP A 806      39.729  27.402  13.937  1.00 53.49           O  
ATOM    961  OD2 ASP A 806      40.388  25.306  13.809  1.00 54.80           O  
ATOM    962  N   ARG A 807      39.158  27.406   8.818  1.00 44.83           N  
ATOM    963  CA  ARG A 807      39.515  27.682   7.434  1.00 43.70           C  
ATOM    964  C   ARG A 807      38.668  28.797   6.814  1.00 43.69           C  
ATOM    965  O   ARG A 807      38.649  28.970   5.592  1.00 41.66           O  
ATOM    966  CB  ARG A 807      39.444  26.399   6.612  1.00 42.07           C  
ATOM    967  CG  ARG A 807      40.593  25.452   6.916  1.00 41.45           C  
ATOM    968  CD  ARG A 807      40.881  24.534   5.746  1.00 40.46           C  
ATOM    969  NE  ARG A 807      40.929  25.258   4.482  1.00 39.29           N  
ATOM    970  CZ  ARG A 807      40.788  24.691   3.288  1.00 40.71           C  
ATOM    971  NH1 ARG A 807      40.592  23.376   3.179  1.00 40.12           N  
ATOM    972  NH2 ARG A 807      40.835  25.444   2.196  1.00 40.21           N  
ATOM    973  N   ARG A 808      37.980  29.547   7.678  1.00 45.39           N  
ATOM    974  CA  ARG A 808      37.113  30.668   7.289  1.00 47.13           C  
ATOM    975  C   ARG A 808      36.010  30.287   6.290  1.00 46.16           C  
ATOM    976  O   ARG A 808      35.619  31.091   5.449  1.00 47.69           O  
ATOM    977  CB  ARG A 808      37.946  31.852   6.775  1.00 50.63           C  
ATOM    978  CG  ARG A 808      38.907  32.418   7.811  1.00 57.29           C  
ATOM    979  CD  ARG A 808      39.526  33.723   7.352  1.00 63.23           C  
ATOM    980  NE  ARG A 808      40.411  34.297   8.369  1.00 70.23           N  
ATOM    981  CZ  ARG A 808      41.743  34.248   8.332  1.00 74.96           C  
ATOM    982  NH1 ARG A 808      42.373  33.649   7.326  1.00 76.44           N  
ATOM    983  NH2 ARG A 808      42.454  34.802   9.308  1.00 75.96           N  
ATOM    984  N   LEU A 809      35.463  29.086   6.421  1.00 43.48           N  
ATOM    985  CA  LEU A 809      34.412  28.619   5.525  1.00 41.06           C  
ATOM    986  C   LEU A 809      33.103  28.370   6.250  1.00 39.86           C  
ATOM    987  O   LEU A 809      33.093  27.872   7.355  1.00 39.34           O  
ATOM    988  CB  LEU A 809      34.843  27.342   4.817  1.00 40.60           C  
ATOM    989  CG  LEU A 809      36.158  27.377   4.052  1.00 40.52           C  
ATOM    990  CD1 LEU A 809      36.612  25.985   3.698  1.00 39.21           C  
ATOM    991  CD2 LEU A 809      36.034  28.226   2.823  1.00 39.55           C  
ATOM    992  N   VAL A 810      31.996  28.730   5.620  1.00 39.22           N  
ATOM    993  CA  VAL A 810      30.679  28.547   6.210  1.00 39.23           C  
ATOM    994  C   VAL A 810      29.894  27.527   5.410  1.00 38.43           C  
ATOM    995  O   VAL A 810      29.782  27.653   4.210  1.00 38.14           O  
ATOM    996  CB  VAL A 810      29.897  29.863   6.216  1.00 39.51           C  
ATOM    997  CG1 VAL A 810      28.510  29.646   6.743  1.00 39.72           C  
ATOM    998  CG2 VAL A 810      30.618  30.901   7.028  1.00 38.30           C  
ATOM    999  N   HIS A 811      29.421  26.481   6.071  1.00 39.02           N  
ATOM   1000  CA  HIS A 811      28.698  25.438   5.369  1.00 39.70           C  
ATOM   1001  C   HIS A 811      27.397  25.930   4.766  1.00 39.95           C  
ATOM   1002  O   HIS A 811      27.115  25.687   3.604  1.00 38.46           O  
ATOM   1003  CB  HIS A 811      28.405  24.289   6.329  1.00 39.62           C  
ATOM   1004  CG  HIS A 811      27.690  23.141   5.695  1.00 39.08           C  
ATOM   1005  ND1 HIS A 811      26.486  23.284   5.053  1.00 38.80           N  
ATOM   1006  CD2 HIS A 811      28.006  21.830   5.611  1.00 39.71           C  
ATOM   1007  CE1 HIS A 811      26.091  22.113   4.592  1.00 39.28           C  
ATOM   1008  NE2 HIS A 811      26.995  21.214   4.921  1.00 39.72           N  
ATOM   1009  N   ARG A 812      26.620  26.644   5.562  1.00 40.74           N  
ATOM   1010  CA  ARG A 812      25.384  27.256   5.110  1.00 42.09           C  
ATOM   1011  C   ARG A 812      24.202  26.306   4.967  1.00 43.22           C  
ATOM   1012  O   ARG A 812      23.115  26.744   4.633  1.00 46.18           O  
ATOM   1013  CB  ARG A 812      25.596  27.961   3.788  1.00 42.87           C  
ATOM   1014  CG  ARG A 812      26.145  29.332   3.914  1.00 46.64           C  
ATOM   1015  CD  ARG A 812      26.376  29.911   2.555  1.00 48.09           C  
ATOM   1016  NE  ARG A 812      27.467  30.865   2.595  1.00 51.73           N  
ATOM   1017  CZ  ARG A 812      28.740  30.533   2.474  1.00 52.76           C  
ATOM   1018  NH1 ARG A 812      29.079  29.271   2.295  1.00 54.55           N  
ATOM   1019  NH2 ARG A 812      29.673  31.462   2.531  1.00 55.19           N  
ATOM   1020  N   ASP A 813      24.393  25.021   5.229  1.00 42.15           N  
ATOM   1021  CA  ASP A 813      23.279  24.087   5.152  1.00 42.51           C  
ATOM   1022  C   ASP A 813      23.507  22.837   5.980  1.00 42.92           C  
ATOM   1023  O   ASP A 813      23.511  21.728   5.472  1.00 41.82           O  
ATOM   1024  CB  ASP A 813      22.979  23.715   3.704  1.00 44.59           C  
ATOM   1025  CG  ASP A 813      21.618  23.077   3.538  1.00 46.82           C  
ATOM   1026  OD1 ASP A 813      20.789  23.204   4.454  1.00 47.06           O  
ATOM   1027  OD2 ASP A 813      21.377  22.448   2.493  1.00 47.26           O  
ATOM   1028  N   LEU A 814      23.666  23.024   7.269  1.00 42.75           N  
ATOM   1029  CA  LEU A 814      23.881  21.916   8.167  1.00 41.08           C  
ATOM   1030  C   LEU A 814      22.542  21.365   8.615  1.00 42.70           C  
ATOM   1031  O   LEU A 814      21.701  22.088   9.112  1.00 43.80           O  
ATOM   1032  CB  LEU A 814      24.702  22.356   9.371  1.00 38.92           C  
ATOM   1033  CG  LEU A 814      25.126  21.189  10.240  1.00 38.16           C  
ATOM   1034  CD1 LEU A 814      25.886  20.191   9.391  1.00 37.73           C  
ATOM   1035  CD2 LEU A 814      25.960  21.661  11.411  1.00 37.88           C  
ATOM   1036  N   ALA A 815      22.355  20.071   8.415  1.00 42.50           N  
ATOM   1037  CA  ALA A 815      21.150  19.385   8.813  1.00 41.11           C  
ATOM   1038  C   ALA A 815      21.513  17.923   8.861  1.00 41.87           C  
ATOM   1039  O   ALA A 815      22.579  17.552   8.401  1.00 42.19           O  
ATOM   1040  CB  ALA A 815      20.056  19.624   7.800  1.00 40.51           C  
ATOM   1041  N   ALA A 816      20.635  17.099   9.418  1.00 41.16           N  
ATOM   1042  CA  ALA A 816      20.887  15.670   9.539  1.00 40.50           C  
ATOM   1043  C   ALA A 816      20.940  14.983   8.189  1.00 40.42           C  
ATOM   1044  O   ALA A 816      21.775  14.128   7.956  1.00 40.51           O  
ATOM   1045  CB  ALA A 816      19.840  15.021  10.418  1.00 42.12           C  
ATOM   1046  N   ARG A 817      20.042  15.357   7.294  1.00 41.50           N  
ATOM   1047  CA  ARG A 817      20.094  14.834   5.926  1.00 41.40           C  
ATOM   1048  C   ARG A 817      21.479  15.050   5.292  1.00 40.84           C  
ATOM   1049  O   ARG A 817      21.869  14.316   4.388  1.00 42.77           O  
ATOM   1050  CB  ARG A 817      18.987  15.445   5.052  1.00 40.74           C  
ATOM   1051  CG  ARG A 817      19.107  16.945   4.836  1.00 42.48           C  
ATOM   1052  CD  ARG A 817      18.082  17.478   3.841  1.00 44.51           C  
ATOM   1053  NE  ARG A 817      18.216  18.929   3.694  1.00 45.94           N  
ATOM   1054  CZ  ARG A 817      17.701  19.827   4.536  1.00 45.71           C  
ATOM   1055  NH1 ARG A 817      16.994  19.437   5.592  1.00 44.84           N  
ATOM   1056  NH2 ARG A 817      17.897  21.122   4.322  1.00 45.03           N  
ATOM   1057  N   ASN A 818      22.208  16.047   5.795  1.00 39.38           N  
ATOM   1058  CA  ASN A 818      23.495  16.465   5.249  1.00 38.50           C  
ATOM   1059  C   ASN A 818      24.676  15.865   5.996  1.00 37.82           C  
ATOM   1060  O   ASN A 818      25.823  16.281   5.801  1.00 36.55           O  
ATOM   1061  CB  ASN A 818      23.594  17.992   5.264  1.00 39.84           C  
ATOM   1062  CG  ASN A 818      22.870  18.632   4.095  1.00 41.62           C  
ATOM   1063  OD1 ASN A 818      22.905  18.118   2.982  1.00 43.30           O  
ATOM   1064  ND2 ASN A 818      22.215  19.763   4.341  1.00 41.08           N  
ATOM   1065  N   VAL A 819      24.381  14.902   6.867  1.00 36.28           N  
ATOM   1066  CA  VAL A 819      25.406  14.170   7.595  1.00 35.95           C  
ATOM   1067  C   VAL A 819      25.349  12.696   7.216  1.00 35.90           C  
ATOM   1068  O   VAL A 819      24.292  12.066   7.287  1.00 34.28           O  
ATOM   1069  CB  VAL A 819      25.248  14.306   9.117  1.00 36.63           C  
ATOM   1070  CG1 VAL A 819      26.364  13.548   9.830  1.00 36.53           C  
ATOM   1071  CG2 VAL A 819      25.235  15.774   9.525  1.00 35.71           C  
ATOM   1072  N   LEU A 820      26.496  12.156   6.810  1.00 35.93           N  
ATOM   1073  CA  LEU A 820      26.566  10.783   6.333  1.00 34.78           C  
ATOM   1074  C   LEU A 820      27.289   9.914   7.321  1.00 34.12           C  
ATOM   1075  O   LEU A 820      28.152  10.386   8.051  1.00 33.56           O  
ATOM   1076  CB  LEU A 820      27.272  10.710   4.982  1.00 35.15           C  
ATOM   1077  CG  LEU A 820      26.655  11.505   3.832  1.00 36.58           C  
ATOM   1078  CD1 LEU A 820      27.629  11.522   2.669  1.00 37.52           C  
ATOM   1079  CD2 LEU A 820      25.298  10.947   3.410  1.00 36.87           C  
ATOM   1080  N   VAL A 821      26.938   8.633   7.310  1.00 35.39           N  
ATOM   1081  CA  VAL A 821      27.509   7.640   8.203  1.00 37.07           C  
ATOM   1082  C   VAL A 821      28.569   6.830   7.466  1.00 38.05           C  
ATOM   1083  O   VAL A 821      28.247   6.087   6.542  1.00 39.79           O  
ATOM   1084  CB  VAL A 821      26.408   6.688   8.730  1.00 37.29           C  
ATOM   1085  CG1 VAL A 821      26.948   5.768   9.815  1.00 37.63           C  
ATOM   1086  CG2 VAL A 821      25.221   7.477   9.261  1.00 36.82           C  
ATOM   1087  N   LYS A 822      29.833   6.988   7.850  1.00 40.72           N  
ATOM   1088  CA  LYS A 822      30.877   6.070   7.376  1.00 43.00           C  
ATOM   1089  C   LYS A 822      30.773   4.762   8.158  1.00 42.66           C  
ATOM   1090  O   LYS A 822      30.731   3.682   7.568  1.00 43.48           O  
ATOM   1091  CB  LYS A 822      32.284   6.672   7.505  1.00 45.67           C  
ATOM   1092  CG  LYS A 822      33.385   5.734   7.029  1.00 47.96           C  
ATOM   1093  CD  LYS A 822      34.660   6.473   6.657  1.00 51.97           C  
ATOM   1094  CE  LYS A 822      35.458   5.685   5.624  1.00 54.69           C  
ATOM   1095  NZ  LYS A 822      36.890   6.097   5.573  1.00 57.04           N  
ATOM   1096  N   THR A 823      30.749   4.884   9.486  1.00 41.84           N  
ATOM   1097  CA  THR A 823      30.449   3.784  10.409  1.00 42.54           C  
ATOM   1098  C   THR A 823      29.570   4.355  11.532  1.00 42.97           C  
ATOM   1099  O   THR A 823      29.517   5.576  11.706  1.00 43.08           O  
ATOM   1100  CB  THR A 823      31.728   3.138  11.016  1.00 41.59           C  
ATOM   1101  OG1 THR A 823      32.348   4.036  11.940  1.00 41.07           O  
ATOM   1102  CG2 THR A 823      32.738   2.732   9.936  1.00 40.61           C  
ATOM   1103  N   PRO A 824      28.855   3.490  12.282  1.00 43.35           N  
ATOM   1104  CA  PRO A 824      28.132   3.971  13.462  1.00 44.65           C  
ATOM   1105  C   PRO A 824      28.976   4.850  14.394  1.00 45.19           C  
ATOM   1106  O   PRO A 824      28.446   5.767  15.019  1.00 45.49           O  
ATOM   1107  CB  PRO A 824      27.736   2.678  14.166  1.00 43.20           C  
ATOM   1108  CG  PRO A 824      27.522   1.718  13.052  1.00 43.42           C  
ATOM   1109  CD  PRO A 824      28.424   2.130  11.914  1.00 43.93           C  
ATOM   1110  N   GLN A 825      30.276   4.577  14.463  1.00 46.42           N  
ATOM   1111  CA  GLN A 825      31.190   5.335  15.309  1.00 46.92           C  
ATOM   1112  C   GLN A 825      31.813   6.546  14.599  1.00 46.68           C  
ATOM   1113  O   GLN A 825      32.531   7.326  15.228  1.00 47.32           O  
ATOM   1114  CB  GLN A 825      32.292   4.416  15.837  1.00 50.44           C  
ATOM   1115  CG  GLN A 825      31.793   3.225  16.646  1.00 53.38           C  
ATOM   1116  CD  GLN A 825      32.916   2.470  17.340  1.00 55.44           C  
ATOM   1117  OE1 GLN A 825      34.009   2.301  16.791  1.00 55.95           O  
ATOM   1118  NE2 GLN A 825      32.648   2.005  18.555  1.00 56.98           N  
ATOM   1119  N   HIS A 826      31.524   6.711  13.305  1.00 44.46           N  
ATOM   1120  CA  HIS A 826      32.157   7.747  12.479  1.00 41.14           C  
ATOM   1121  C   HIS A 826      31.221   8.371  11.468  1.00 39.04           C  
ATOM   1122  O   HIS A 826      30.904   7.759  10.450  1.00 38.56           O  
ATOM   1123  CB  HIS A 826      33.376   7.164  11.766  1.00 41.32           C  
ATOM   1124  CG  HIS A 826      34.243   8.193  11.077  1.00 42.29           C  
ATOM   1125  ND1 HIS A 826      35.461   7.897  10.597  1.00 43.10           N  
ATOM   1126  CD2 HIS A 826      34.035   9.544  10.811  1.00 43.52           C  
ATOM   1127  CE1 HIS A 826      36.004   8.992  10.040  1.00 43.22           C  
ATOM   1128  NE2 HIS A 826      35.133  10.002  10.175  1.00 44.78           N  
ATOM   1129  N   VAL A 827      30.793   9.606  11.725  1.00 37.10           N  
ATOM   1130  CA  VAL A 827      29.938  10.336  10.782  1.00 36.34           C  
ATOM   1131  C   VAL A 827      30.672  11.509  10.136  1.00 37.87           C  
ATOM   1132  O   VAL A 827      31.641  12.026  10.705  1.00 39.86           O  
ATOM   1133  CB  VAL A 827      28.612  10.819  11.419  1.00 35.80           C  
ATOM   1134  CG1 VAL A 827      27.687   9.638  11.711  1.00 34.26           C  
ATOM   1135  CG2 VAL A 827      28.869  11.653  12.667  1.00 35.51           C  
ATOM   1136  N   LYS A 828      30.208  11.911   8.948  1.00 37.34           N  
ATOM   1137  CA  LYS A 828      30.803  13.005   8.179  1.00 37.45           C  
ATOM   1138  C   LYS A 828      29.770  14.031   7.711  1.00 38.30           C  
ATOM   1139  O   LYS A 828      28.651  13.675   7.313  1.00 37.06           O  
ATOM   1140  CB  LYS A 828      31.521  12.461   6.952  1.00 38.68           C  
ATOM   1141  CG  LYS A 828      32.897  11.875   7.206  1.00 40.49           C  
ATOM   1142  CD  LYS A 828      33.621  11.701   5.879  1.00 41.92           C  
ATOM   1143  CE  LYS A 828      34.731  10.669   5.964  1.00 44.57           C  
ATOM   1144  NZ  LYS A 828      35.199  10.255   4.610  1.00 46.46           N  
ATOM   1145  N   ILE A 829      30.160  15.304   7.751  1.00 38.33           N  
ATOM   1146  CA  ILE A 829      29.354  16.385   7.198  1.00 38.48           C  
ATOM   1147  C   ILE A 829      29.506  16.395   5.677  1.00 39.68           C  
ATOM   1148  O   ILE A 829      30.619  16.309   5.153  1.00 40.43           O  
ATOM   1149  CB  ILE A 829      29.774  17.753   7.774  1.00 38.46           C  
ATOM   1150  CG1 ILE A 829      29.453  17.832   9.264  1.00 38.07           C  
ATOM   1151  CG2 ILE A 829      29.076  18.898   7.047  1.00 39.61           C  
ATOM   1152  CD1 ILE A 829      30.212  18.930   9.984  1.00 37.76           C  
ATOM   1153  N   THR A 830      28.386  16.499   4.972  1.00 40.53           N  
ATOM   1154  CA  THR A 830      28.401  16.506   3.515  1.00 41.75           C  
ATOM   1155  C   THR A 830      27.698  17.757   2.975  1.00 42.92           C  
ATOM   1156  O   THR A 830      27.136  18.535   3.747  1.00 44.32           O  
ATOM   1157  CB  THR A 830      27.801  15.195   2.947  1.00 42.07           C  
ATOM   1158  OG1 THR A 830      28.358  14.928   1.656  1.00 43.58           O  
ATOM   1159  CG2 THR A 830      26.268  15.246   2.859  1.00 41.85           C  
ATOM   1160  N   ASP A 831      27.748  17.949   1.659  1.00 44.87           N  
ATOM   1161  CA  ASP A 831      27.125  19.099   0.986  1.00 46.48           C  
ATOM   1162  C   ASP A 831      27.802  20.438   1.270  1.00 44.81           C  
ATOM   1163  O   ASP A 831      27.180  21.499   1.116  1.00 44.22           O  
ATOM   1164  CB  ASP A 831      25.619  19.192   1.300  1.00 50.07           C  
ATOM   1165  CG  ASP A 831      24.769  18.412   0.322  1.00 52.71           C  
ATOM   1166  OD1 ASP A 831      24.731  18.790  -0.870  1.00 54.05           O  
ATOM   1167  OD2 ASP A 831      24.135  17.421   0.744  1.00 55.21           O  
ATOM   1168  N   PHE A 832      29.060  20.406   1.671  1.00 43.21           N  
ATOM   1169  CA  PHE A 832      29.772  21.647   1.845  1.00 42.52           C  
ATOM   1170  C   PHE A 832      29.933  22.311   0.495  1.00 42.47           C  
ATOM   1171  O   PHE A 832      30.327  21.673  -0.461  1.00 42.96           O  
ATOM   1172  CB  PHE A 832      31.144  21.442   2.477  1.00 42.67           C  
ATOM   1173  CG  PHE A 832      31.990  22.673   2.439  1.00 43.38           C  
ATOM   1174  CD1 PHE A 832      31.625  23.789   3.160  1.00 42.90           C  
ATOM   1175  CD2 PHE A 832      33.106  22.737   1.634  1.00 44.33           C  
ATOM   1176  CE1 PHE A 832      32.378  24.937   3.107  1.00 43.53           C  
ATOM   1177  CE2 PHE A 832      33.862  23.883   1.573  1.00 44.40           C  
ATOM   1178  CZ  PHE A 832      33.496  24.984   2.311  1.00 44.51           C  
ATOM   1179  N   GLY A 833      29.626  23.597   0.426  1.00 42.30           N  
ATOM   1180  CA  GLY A 833      29.820  24.357  -0.786  1.00 41.25           C  
ATOM   1181  C   GLY A 833      28.655  24.338  -1.739  1.00 41.10           C  
ATOM   1182  O   GLY A 833      28.629  25.104  -2.683  1.00 42.34           O  
ATOM   1183  N   LEU A 834      27.688  23.479  -1.480  1.00 41.34           N  
ATOM   1184  CA  LEU A 834      26.546  23.366  -2.357  1.00 42.23           C  
ATOM   1185  C   LEU A 834      25.618  24.556  -2.202  1.00 42.20           C  
ATOM   1186  O   LEU A 834      25.138  25.092  -3.180  1.00 42.51           O  
ATOM   1187  CB  LEU A 834      25.792  22.075  -2.090  1.00 42.71           C  
ATOM   1188  CG  LEU A 834      25.481  21.291  -3.355  1.00 43.19           C  
ATOM   1189  CD1 LEU A 834      26.618  20.324  -3.611  1.00 43.80           C  
ATOM   1190  CD2 LEU A 834      24.180  20.534  -3.192  1.00 43.01           C  
ATOM   1191  N   ALA A 835      25.367  24.978  -0.973  1.00 41.59           N  
ATOM   1192  CA  ALA A 835      24.484  26.109  -0.769  1.00 42.57           C  
ATOM   1193  C   ALA A 835      24.995  27.340  -1.494  1.00 45.19           C  
ATOM   1194  O   ALA A 835      24.218  28.150  -1.964  1.00 49.14           O  
ATOM   1195  CB  ALA A 835      24.336  26.392   0.708  1.00 40.17           C  
ATOM   1196  N   LYS A 836      26.308  27.476  -1.568  1.00 45.06           N  
ATOM   1197  CA  LYS A 836      26.945  28.568  -2.293  1.00 46.06           C  
ATOM   1198  C   LYS A 836      26.795  28.412  -3.811  1.00 47.49           C  
ATOM   1199  O   LYS A 836      26.511  29.388  -4.517  1.00 47.34           O  
ATOM   1200  CB  LYS A 836      28.422  28.662  -1.901  1.00 47.42           C  
ATOM   1201  CG  LYS A 836      29.157  29.846  -2.502  1.00 48.11           C  
ATOM   1202  CD  LYS A 836      30.342  30.244  -1.640  1.00 50.73           C  
ATOM   1203  CE  LYS A 836      31.258  31.198  -2.386  1.00 51.97           C  
ATOM   1204  NZ  LYS A 836      32.175  31.900  -1.448  1.00 53.95           N  
ATOM   1205  N   LEU A 837      26.986  27.189  -4.308  1.00 47.41           N  
ATOM   1206  CA  LEU A 837      26.774  26.894  -5.726  1.00 47.43           C  
ATOM   1207  C   LEU A 837      25.327  27.160  -6.129  1.00 46.87           C  
ATOM   1208  O   LEU A 837      25.070  27.659  -7.214  1.00 48.19           O  
ATOM   1209  CB  LEU A 837      27.136  25.445  -6.055  1.00 49.00           C  
ATOM   1210  CG  LEU A 837      28.565  24.947  -5.827  1.00 52.22           C  
ATOM   1211  CD1 LEU A 837      28.601  23.428  -5.932  1.00 51.11           C  
ATOM   1212  CD2 LEU A 837      29.559  25.583  -6.793  1.00 53.71           C  
ATOM   1213  N   LEU A 838      24.387  26.836  -5.248  1.00 46.63           N  
ATOM   1214  CA  LEU A 838      22.972  27.091  -5.499  1.00 47.45           C  
ATOM   1215  C   LEU A 838      22.580  28.543  -5.200  1.00 50.41           C  
ATOM   1216  O   LEU A 838      21.395  28.892  -5.208  1.00 49.93           O  
ATOM   1217  CB  LEU A 838      22.104  26.101  -4.721  1.00 46.16           C  
ATOM   1218  CG  LEU A 838      22.263  24.647  -5.178  1.00 45.65           C  
ATOM   1219  CD1 LEU A 838      21.663  23.681  -4.170  1.00 45.61           C  
ATOM   1220  CD2 LEU A 838      21.662  24.441  -6.560  1.00 45.73           C  
ATOM   1221  N   GLY A 839      23.590  29.375  -4.942  1.00 52.44           N  
ATOM   1222  CA  GLY A 839      23.431  30.824  -4.835  1.00 54.07           C  
ATOM   1223  C   GLY A 839      22.650  31.309  -3.634  1.00 56.42           C  
ATOM   1224  O   GLY A 839      21.846  32.236  -3.750  1.00 57.87           O  
ATOM   1225  N   ALA A 840      22.836  30.632  -2.507  1.00 58.85           N  
ATOM   1226  CA  ALA A 840      22.204  30.992  -1.244  1.00 61.65           C  
ATOM   1227  C   ALA A 840      22.665  32.336  -0.706  1.00 65.61           C  
ATOM   1228  O   ALA A 840      21.874  33.121  -0.197  1.00 68.40           O  
ATOM   1229  CB  ALA A 840      22.449  29.909  -0.213  1.00 57.64           C  
ATOM   1230  N   GLU A 841      23.960  32.588  -0.811  1.00 70.84           N  
ATOM   1231  CA  GLU A 841      24.541  33.808  -0.287  1.00 75.05           C  
ATOM   1232  C   GLU A 841      24.007  35.042  -0.991  1.00 77.20           C  
ATOM   1233  O   GLU A 841      23.777  36.067  -0.362  1.00 78.22           O  
ATOM   1234  CB  GLU A 841      26.068  33.767  -0.350  1.00 76.43           C  
ATOM   1235  CG  GLU A 841      26.654  34.218  -1.671  1.00 78.41           C  
ATOM   1236  CD  GLU A 841      26.703  33.104  -2.677  1.00 81.40           C  
ATOM   1237  OE1 GLU A 841      25.976  32.113  -2.484  1.00 81.28           O  
ATOM   1238  OE2 GLU A 841      27.467  33.215  -3.654  1.00 81.12           O  
ATOM   1239  N   GLU A 842      23.804  34.943  -2.298  1.00 78.56           N  
ATOM   1240  CA  GLU A 842      23.493  36.121  -3.077  1.00 78.18           C  
ATOM   1241  C   GLU A 842      22.026  36.446  -2.910  1.00 76.62           C  
ATOM   1242  O   GLU A 842      21.153  35.806  -3.479  1.00 73.31           O  
ATOM   1243  CB  GLU A 842      23.810  35.862  -4.542  1.00 80.15           C  
ATOM   1244  CG  GLU A 842      25.269  36.084  -4.897  1.00 83.33           C  
ATOM   1245  CD  GLU A 842      25.745  37.481  -4.550  1.00 85.15           C  
ATOM   1246  OE1 GLU A 842      24.890  38.373  -4.375  1.00 83.33           O  
ATOM   1247  OE2 GLU A 842      26.971  37.686  -4.451  1.00 85.68           O  
ATOM   1248  N   LYS A 843      21.774  37.490  -2.133  1.00 76.01           N  
ATOM   1249  CA  LYS A 843      20.449  37.844  -1.647  1.00 77.07           C  
ATOM   1250  C   LYS A 843      19.467  38.170  -2.755  1.00 76.73           C  
ATOM   1251  O   LYS A 843      18.285  37.872  -2.650  1.00 77.18           O  
ATOM   1252  CB  LYS A 843      20.535  39.004  -0.658  1.00 77.65           C  
ATOM   1253  N   GLU A 844      19.960  38.798  -3.811  1.00 76.45           N  
ATOM   1254  CA  GLU A 844      19.123  39.197  -4.932  1.00 73.24           C  
ATOM   1255  C   GLU A 844      18.448  37.998  -5.594  1.00 72.02           C  
ATOM   1256  O   GLU A 844      17.324  38.106  -6.062  1.00 72.11           O  
ATOM   1257  CB  GLU A 844      19.941  39.972  -5.960  1.00 70.98           C  
ATOM   1258  N   TYR A 845      19.145  36.872  -5.663  1.00 69.57           N  
ATOM   1259  CA  TYR A 845      18.620  35.664  -6.296  1.00 64.98           C  
ATOM   1260  C   TYR A 845      17.392  35.036  -5.626  1.00 64.35           C  
ATOM   1261  O   TYR A 845      17.362  34.828  -4.423  1.00 64.17           O  
ATOM   1262  CB  TYR A 845      19.738  34.632  -6.339  1.00 63.52           C  
ATOM   1263  CG  TYR A 845      19.462  33.423  -7.182  1.00 62.64           C  
ATOM   1264  CD1 TYR A 845      19.056  33.541  -8.494  1.00 61.86           C  
ATOM   1265  CD2 TYR A 845      19.631  32.157  -6.669  1.00 60.93           C  
ATOM   1266  CE1 TYR A 845      18.812  32.433  -9.268  1.00 60.30           C  
ATOM   1267  CE2 TYR A 845      19.393  31.042  -7.435  1.00 59.89           C  
ATOM   1268  CZ  TYR A 845      18.984  31.185  -8.733  1.00 59.62           C  
ATOM   1269  OH  TYR A 845      18.744  30.072  -9.497  1.00 58.57           O  
ATOM   1270  N   HIS A 846      16.402  34.699  -6.444  1.00 66.77           N  
ATOM   1271  CA  HIS A 846      15.222  33.940  -6.047  1.00 67.14           C  
ATOM   1272  C   HIS A 846      15.034  32.785  -6.985  1.00 66.92           C  
ATOM   1273  O   HIS A 846      14.633  32.965  -8.132  1.00 66.03           O  
ATOM   1274  CB  HIS A 846      13.985  34.838  -6.039  1.00 67.25           C  
ATOM   1275  CG  HIS A 846      14.085  36.019  -5.095  1.00 69.87           C  
ATOM   1276  ND1 HIS A 846      14.887  37.162  -5.134  1.00 71.28           N  
ATOM   1277  CD2 HIS A 846      13.330  36.125  -3.986  1.00 70.72           C  
ATOM   1278  CE1 HIS A 846      14.584  37.906  -4.049  1.00 71.52           C  
ATOM   1279  NE2 HIS A 846      13.629  37.273  -3.346  1.00 71.52           N  
ATOM   1280  N   ALA A 847      15.366  31.600  -6.502  1.00 68.98           N  
ATOM   1281  CA  ALA A 847      15.254  30.388  -7.283  1.00 72.30           C  
ATOM   1282  C   ALA A 847      13.799  30.045  -7.503  1.00 75.97           C  
ATOM   1283  O   ALA A 847      12.949  30.359  -6.678  1.00 76.25           O  
ATOM   1284  CB  ALA A 847      15.963  29.247  -6.582  1.00 71.10           C  
ATOM   1285  N   GLU A 848      13.510  29.398  -8.620  1.00 80.40           N  
ATOM   1286  CA  GLU A 848      12.158  28.959  -8.883  1.00 84.94           C  
ATOM   1287  C   GLU A 848      12.079  27.490  -8.540  1.00 87.56           C  
ATOM   1288  O   GLU A 848      12.827  26.678  -9.072  1.00 87.22           O  
ATOM   1289  CB  GLU A 848      11.797  29.167 -10.349  1.00 85.78           C  
ATOM   1290  CG  GLU A 848      10.370  28.773 -10.689  1.00 86.56           C  
ATOM   1291  CD  GLU A 848       9.342  29.696 -10.065  1.00 86.90           C  
ATOM   1292  OE1 GLU A 848       8.915  30.655 -10.738  1.00 86.88           O  
ATOM   1293  OE2 GLU A 848       8.958  29.463  -8.901  1.00 86.17           O  
ATOM   1294  N   GLY A 849      11.169  27.157  -7.635  1.00 90.86           N  
ATOM   1295  CA  GLY A 849      11.007  25.789  -7.195  1.00 93.63           C  
ATOM   1296  C   GLY A 849      12.134  25.387  -6.271  1.00 94.55           C  
ATOM   1297  O   GLY A 849      12.328  24.208  -5.983  1.00 92.19           O  
ATOM   1298  N   GLY A 850      12.883  26.372  -5.797  1.00 94.76           N  
ATOM   1299  CA  GLY A 850      13.976  26.080  -4.898  1.00 92.37           C  
ATOM   1300  C   GLY A 850      13.580  26.343  -3.465  1.00 91.78           C  
ATOM   1301  O   GLY A 850      13.330  27.481  -3.068  1.00 90.18           O  
ATOM   1302  N   LYS A 851      13.529  25.273  -2.684  1.00 88.13           N  
ATOM   1303  CA  LYS A 851      13.209  25.382  -1.276  1.00 83.43           C  
ATOM   1304  C   LYS A 851      14.388  25.950  -0.510  1.00 78.98           C  
ATOM   1305  O   LYS A 851      15.533  25.807  -0.921  1.00 78.90           O  
ATOM   1306  CB  LYS A 851      12.776  24.033  -0.706  1.00 83.98           C  
ATOM   1307  CG  LYS A 851      11.497  24.108   0.113  1.00 86.80           C  
ATOM   1308  CD  LYS A 851      11.095  22.753   0.675  1.00 86.55           C  
ATOM   1309  CE  LYS A 851       9.605  22.499   0.488  1.00 84.46           C  
ATOM   1310  NZ  LYS A 851       9.073  21.438   1.388  1.00 82.02           N  
ATOM   1311  N   VAL A 852      14.096  26.604   0.603  1.00 71.22           N  
ATOM   1312  CA  VAL A 852      15.126  27.104   1.486  1.00 64.94           C  
ATOM   1313  C   VAL A 852      14.981  26.370   2.798  1.00 61.51           C  
ATOM   1314  O   VAL A 852      13.859  26.152   3.258  1.00 62.47           O  
ATOM   1315  CB  VAL A 852      15.009  28.617   1.707  1.00 65.15           C  
ATOM   1316  CG1 VAL A 852      14.943  29.333   0.374  1.00 65.54           C  
ATOM   1317  CG2 VAL A 852      13.792  28.952   2.549  1.00 67.64           C  
ATOM   1318  N   PRO A 853      16.083  26.024   3.440  1.00 58.15           N  
ATOM   1319  CA  PRO A 853      15.988  25.252   4.676  1.00 53.55           C  
ATOM   1320  C   PRO A 853      15.680  26.208   5.804  1.00 51.08           C  
ATOM   1321  O   PRO A 853      16.458  26.389   6.722  1.00 50.02           O  
ATOM   1322  CB  PRO A 853      17.398  24.688   4.844  1.00 52.69           C  
ATOM   1323  CG  PRO A 853      18.055  24.842   3.519  1.00 52.72           C  
ATOM   1324  CD  PRO A 853      17.453  26.060   2.915  1.00 54.82           C  
ATOM   1325  N   ILE A 854      14.505  26.806   5.719  1.00 47.89           N  
ATOM   1326  CA  ILE A 854      14.102  27.876   6.608  1.00 47.00           C  
ATOM   1327  C   ILE A 854      14.024  27.415   8.052  1.00 44.12           C  
ATOM   1328  O   ILE A 854      14.409  28.131   8.960  1.00 42.10           O  
ATOM   1329  CB  ILE A 854      12.768  28.480   6.148  1.00 49.60           C  
ATOM   1330  CG1 ILE A 854      12.919  29.175   4.810  1.00 50.99           C  
ATOM   1331  CG2 ILE A 854      12.239  29.446   7.184  1.00 50.56           C  
ATOM   1332  CD1 ILE A 854      11.594  29.547   4.202  1.00 54.63           C  
ATOM   1333  N   LYS A 855      13.525  26.207   8.253  1.00 42.66           N  
ATOM   1334  CA  LYS A 855      13.454  25.609   9.592  1.00 41.19           C  
ATOM   1335  C   LYS A 855      14.815  25.167  10.166  1.00 40.27           C  
ATOM   1336  O   LYS A 855      14.884  24.675  11.295  1.00 40.74           O  
ATOM   1337  CB  LYS A 855      12.469  24.437   9.599  1.00 40.92           C  
ATOM   1338  CG  LYS A 855      11.050  24.854   9.271  1.00 40.95           C  
ATOM   1339  CD  LYS A 855      10.134  23.659   9.096  1.00 41.10           C  
ATOM   1340  CE  LYS A 855       8.708  24.134   8.872  1.00 40.95           C  
ATOM   1341  NZ  LYS A 855       7.697  23.078   9.160  1.00 40.69           N  
ATOM   1342  N   TRP A 856      15.885  25.346   9.396  1.00 38.48           N  
ATOM   1343  CA  TRP A 856      17.242  25.108   9.888  1.00 38.90           C  
ATOM   1344  C   TRP A 856      18.041  26.378   9.984  1.00 39.23           C  
ATOM   1345  O   TRP A 856      19.228  26.352  10.319  1.00 39.89           O  
ATOM   1346  CB  TRP A 856      17.968  24.100   9.000  1.00 38.45           C  
ATOM   1347  CG  TRP A 856      17.532  22.685   9.249  1.00 38.51           C  
ATOM   1348  CD1 TRP A 856      18.168  21.732  10.036  1.00 38.70           C  
ATOM   1349  CD2 TRP A 856      16.323  22.019   8.744  1.00 38.83           C  
ATOM   1350  NE1 TRP A 856      17.467  20.556  10.043  1.00 38.95           N  
ATOM   1351  CE2 TRP A 856      16.348  20.658   9.293  1.00 39.38           C  
ATOM   1352  CE3 TRP A 856      15.266  22.394   7.917  1.00 38.72           C  
ATOM   1353  CZ2 TRP A 856      15.349  19.729   9.011  1.00 38.65           C  
ATOM   1354  CZ3 TRP A 856      14.268  21.447   7.638  1.00 38.18           C  
ATOM   1355  CH2 TRP A 856      14.309  20.151   8.175  1.00 37.21           C  
ATOM   1356  N   MET A 857      17.399  27.506   9.703  1.00 38.64           N  
ATOM   1357  CA  MET A 857      18.109  28.769   9.568  1.00 39.41           C  
ATOM   1358  C   MET A 857      17.980  29.690  10.773  1.00 39.50           C  
ATOM   1359  O   MET A 857      16.906  29.839  11.362  1.00 38.80           O  
ATOM   1360  CB  MET A 857      17.633  29.518   8.328  1.00 41.29           C  
ATOM   1361  CG  MET A 857      17.996  28.876   7.005  1.00 42.04           C  
ATOM   1362  SD  MET A 857      17.330  29.895   5.677  1.00 46.30           S  
ATOM   1363  CE  MET A 857      17.833  28.948   4.249  1.00 46.61           C  
ATOM   1364  N   ALA A 858      19.095  30.324  11.116  1.00 40.82           N  
ATOM   1365  CA  ALA A 858      19.110  31.382  12.111  1.00 40.02           C  
ATOM   1366  C   ALA A 858      18.191  32.527  11.662  1.00 41.13           C  
ATOM   1367  O   ALA A 858      17.975  32.724  10.460  1.00 41.94           O  
ATOM   1368  CB  ALA A 858      20.531  31.868  12.309  1.00 38.97           C  
ATOM   1369  N   LEU A 859      17.641  33.268  12.620  1.00 41.03           N  
ATOM   1370  CA  LEU A 859      16.711  34.347  12.312  1.00 41.75           C  
ATOM   1371  C   LEU A 859      17.292  35.373  11.330  1.00 42.50           C  
ATOM   1372  O   LEU A 859      16.599  35.803  10.396  1.00 43.36           O  
ATOM   1373  CB  LEU A 859      16.228  35.032  13.593  1.00 42.77           C  
ATOM   1374  CG  LEU A 859      14.960  35.892  13.502  1.00 43.30           C  
ATOM   1375  CD1 LEU A 859      13.736  35.052  13.148  1.00 42.98           C  
ATOM   1376  CD2 LEU A 859      14.740  36.637  14.809  1.00 42.58           C  
ATOM   1377  N   GLU A 860      18.557  35.744  11.536  1.00 40.96           N  
ATOM   1378  CA  GLU A 860      19.262  36.677  10.646  1.00 41.86           C  
ATOM   1379  C   GLU A 860      19.503  36.106   9.240  1.00 43.00           C  
ATOM   1380  O   GLU A 860      19.715  36.856   8.286  1.00 44.46           O  
ATOM   1381  CB  GLU A 860      20.579  37.170  11.276  1.00 42.54           C  
ATOM   1382  CG  GLU A 860      21.674  36.115  11.457  1.00 44.75           C  
ATOM   1383  CD  GLU A 860      21.484  35.210  12.681  1.00 47.33           C  
ATOM   1384  OE1 GLU A 860      20.656  35.520  13.573  1.00 47.01           O  
ATOM   1385  OE2 GLU A 860      22.180  34.171  12.755  1.00 47.69           O  
ATOM   1386  N   SER A 861      19.481  34.782   9.112  1.00 43.31           N  
ATOM   1387  CA  SER A 861      19.587  34.152   7.802  1.00 43.16           C  
ATOM   1388  C   SER A 861      18.241  34.200   7.110  1.00 43.64           C  
ATOM   1389  O   SER A 861      18.177  34.432   5.909  1.00 45.08           O  
ATOM   1390  CB  SER A 861      20.069  32.714   7.921  1.00 43.40           C  
ATOM   1391  OG  SER A 861      21.380  32.668   8.442  1.00 42.58           O  
ATOM   1392  N   ILE A 862      17.173  33.982   7.881  1.00 43.61           N  
ATOM   1393  CA  ILE A 862      15.803  34.098   7.390  1.00 43.74           C  
ATOM   1394  C   ILE A 862      15.518  35.527   6.933  1.00 45.13           C  
ATOM   1395  O   ILE A 862      15.155  35.752   5.777  1.00 45.09           O  
ATOM   1396  CB  ILE A 862      14.771  33.660   8.462  1.00 44.61           C  
ATOM   1397  CG1 ILE A 862      14.847  32.152   8.692  1.00 44.52           C  
ATOM   1398  CG2 ILE A 862      13.348  34.055   8.066  1.00 43.42           C  
ATOM   1399  CD1 ILE A 862      14.058  31.666   9.891  1.00 44.18           C  
ATOM   1400  N   LEU A 863      15.711  36.485   7.835  1.00 47.41           N  
ATOM   1401  CA  LEU A 863      15.337  37.879   7.583  1.00 49.50           C  
ATOM   1402  C   LEU A 863      16.268  38.613   6.612  1.00 51.60           C  
ATOM   1403  O   LEU A 863      15.801  39.249   5.667  1.00 54.15           O  
ATOM   1404  CB  LEU A 863      15.219  38.653   8.905  1.00 48.41           C  
ATOM   1405  CG  LEU A 863      14.237  38.140   9.972  1.00 48.29           C  
ATOM   1406  CD1 LEU A 863      14.282  39.021  11.213  1.00 47.28           C  
ATOM   1407  CD2 LEU A 863      12.813  38.028   9.436  1.00 46.98           C  
ATOM   1408  N   HIS A 864      17.575  38.512   6.838  1.00 53.28           N  
ATOM   1409  CA  HIS A 864      18.551  39.319   6.103  1.00 53.94           C  
ATOM   1410  C   HIS A 864      19.478  38.519   5.231  1.00 53.67           C  
ATOM   1411  O   HIS A 864      20.416  39.071   4.661  1.00 54.55           O  
ATOM   1412  CB  HIS A 864      19.364  40.173   7.073  1.00 54.43           C  
ATOM   1413  CG  HIS A 864      18.518  40.980   8.033  1.00 56.71           C  
ATOM   1414  ND1 HIS A 864      17.778  42.035   7.637  1.00 56.58           N  
ATOM   1415  CD2 HIS A 864      18.320  40.852   9.407  1.00 57.44           C  
ATOM   1416  CE1 HIS A 864      17.136  42.557   8.701  1.00 57.92           C  
ATOM   1417  NE2 HIS A 864      17.468  41.833   9.784  1.00 58.74           N  
ATOM   1418  N   ARG A 865      19.219  37.219   5.109  1.00 54.60           N  
ATOM   1419  CA  ARG A 865      20.120  36.286   4.413  1.00 56.06           C  
ATOM   1420  C   ARG A 865      21.621  36.510   4.704  1.00 53.82           C  
ATOM   1421  O   ARG A 865      22.461  36.514   3.802  1.00 50.94           O  
ATOM   1422  CB  ARG A 865      19.802  36.211   2.912  1.00 58.95           C  
ATOM   1423  CG  ARG A 865      18.662  35.246   2.595  1.00 63.87           C  
ATOM   1424  CD  ARG A 865      18.111  35.432   1.185  1.00 68.49           C  
ATOM   1425  NE  ARG A 865      18.919  34.767   0.158  1.00 71.32           N  
ATOM   1426  CZ  ARG A 865      18.703  34.863  -1.154  1.00 71.91           C  
ATOM   1427  NH1 ARG A 865      17.703  35.606  -1.621  1.00 72.51           N  
ATOM   1428  NH2 ARG A 865      19.492  34.219  -2.007  1.00 69.78           N  
ATOM   1429  N   ILE A 866      21.927  36.690   5.988  1.00 52.24           N  
ATOM   1430  CA  ILE A 866      23.293  36.814   6.479  1.00 51.94           C  
ATOM   1431  C   ILE A 866      23.757  35.475   7.063  1.00 49.32           C  
ATOM   1432  O   ILE A 866      23.191  34.988   8.039  1.00 48.42           O  
ATOM   1433  CB  ILE A 866      23.404  37.943   7.542  1.00 53.12           C  
ATOM   1434  CG1 ILE A 866      23.300  39.336   6.886  1.00 53.44           C  
ATOM   1435  CG2 ILE A 866      24.670  37.795   8.389  1.00 53.21           C  
ATOM   1436  CD1 ILE A 866      24.382  39.676   5.871  1.00 52.83           C  
ATOM   1437  N   TYR A 867      24.778  34.885   6.449  1.00 48.38           N  
ATOM   1438  CA  TYR A 867      25.348  33.621   6.917  1.00 48.11           C  
ATOM   1439  C   TYR A 867      26.727  33.830   7.539  1.00 47.64           C  
ATOM   1440  O   TYR A 867      27.609  34.456   6.951  1.00 47.68           O  
ATOM   1441  CB  TYR A 867      25.429  32.595   5.782  1.00 48.71           C  
ATOM   1442  CG  TYR A 867      24.090  32.199   5.195  1.00 49.68           C  
ATOM   1443  CD1 TYR A 867      23.325  31.184   5.772  1.00 49.81           C  
ATOM   1444  CD2 TYR A 867      23.589  32.837   4.061  1.00 50.66           C  
ATOM   1445  CE1 TYR A 867      22.096  30.820   5.242  1.00 50.78           C  
ATOM   1446  CE2 TYR A 867      22.358  32.482   3.522  1.00 52.08           C  
ATOM   1447  CZ  TYR A 867      21.614  31.474   4.113  1.00 52.10           C  
ATOM   1448  OH  TYR A 867      20.391  31.117   3.577  1.00 50.87           O  
ATOM   1449  N   THR A 868      26.895  33.306   8.743  1.00 46.61           N  
ATOM   1450  CA  THR A 868      28.140  33.416   9.481  1.00 46.40           C  
ATOM   1451  C   THR A 868      28.470  32.060  10.079  1.00 45.25           C  
ATOM   1452  O   THR A 868      27.753  31.086   9.846  1.00 45.56           O  
ATOM   1453  CB  THR A 868      28.013  34.439  10.622  1.00 46.93           C  
ATOM   1454  OG1 THR A 868      26.780  34.214  11.319  1.00 48.57           O  
ATOM   1455  CG2 THR A 868      28.044  35.863  10.077  1.00 45.22           C  
ATOM   1456  N   HIS A 869      29.553  31.993  10.846  1.00 44.73           N  
ATOM   1457  CA  HIS A 869      29.877  30.786  11.595  1.00 45.37           C  
ATOM   1458  C   HIS A 869      28.886  30.604  12.706  1.00 45.27           C  
ATOM   1459  O   HIS A 869      28.568  29.477  13.089  1.00 44.86           O  
ATOM   1460  CB  HIS A 869      31.295  30.859  12.153  1.00 47.71           C  
ATOM   1461  CG  HIS A 869      32.357  31.067  11.095  1.00 50.31           C  
ATOM   1462  ND1 HIS A 869      32.697  30.106  10.206  1.00 50.80           N  
ATOM   1463  CD2 HIS A 869      33.160  32.170  10.809  1.00 50.37           C  
ATOM   1464  CE1 HIS A 869      33.663  30.575   9.391  1.00 50.30           C  
ATOM   1465  NE2 HIS A 869      33.947  31.836   9.762  1.00 50.95           N  
ATOM   1466  N   GLN A 870      28.371  31.722  13.219  1.00 45.24           N  
ATOM   1467  CA  GLN A 870      27.415  31.704  14.325  1.00 43.38           C  
ATOM   1468  C   GLN A 870      25.996  31.353  13.892  1.00 41.60           C  
ATOM   1469  O   GLN A 870      25.223  30.811  14.679  1.00 42.05           O  
ATOM   1470  CB  GLN A 870      27.449  33.021  15.109  1.00 42.97           C  
ATOM   1471  CG  GLN A 870      28.681  33.173  15.993  1.00 43.14           C  
ATOM   1472  CD  GLN A 870      28.832  32.041  16.999  1.00 43.84           C  
ATOM   1473  OE1 GLN A 870      29.574  31.084  16.769  1.00 43.33           O  
ATOM   1474  NE2 GLN A 870      28.120  32.141  18.116  1.00 43.86           N  
ATOM   1475  N   SER A 871      25.653  31.639  12.642  1.00 40.27           N  
ATOM   1476  CA  SER A 871      24.386  31.149  12.113  1.00 39.09           C  
ATOM   1477  C   SER A 871      24.475  29.630  11.901  1.00 37.60           C  
ATOM   1478  O   SER A 871      23.496  28.918  12.119  1.00 37.10           O  
ATOM   1479  CB  SER A 871      23.951  31.911  10.848  1.00 38.34           C  
ATOM   1480  OG  SER A 871      24.750  31.596   9.723  1.00 38.82           O  
ATOM   1481  N   ASP A 872      25.658  29.142  11.517  1.00 37.29           N  
ATOM   1482  CA  ASP A 872      25.930  27.696  11.430  1.00 37.41           C  
ATOM   1483  C   ASP A 872      25.720  26.969  12.765  1.00 35.26           C  
ATOM   1484  O   ASP A 872      25.293  25.810  12.790  1.00 35.11           O  
ATOM   1485  CB  ASP A 872      27.348  27.419  10.904  1.00 39.69           C  
ATOM   1486  CG  ASP A 872      27.411  27.274   9.371  1.00 43.89           C  
ATOM   1487  OD1 ASP A 872      26.356  27.308   8.694  1.00 44.33           O  
ATOM   1488  OD2 ASP A 872      28.536  27.122   8.834  1.00 45.85           O  
ATOM   1489  N   VAL A 873      26.022  27.652  13.867  1.00 32.70           N  
ATOM   1490  CA  VAL A 873      25.819  27.096  15.201  1.00 31.64           C  
ATOM   1491  C   VAL A 873      24.333  26.828  15.462  1.00 31.53           C  
ATOM   1492  O   VAL A 873      23.975  25.811  16.056  1.00 30.97           O  
ATOM   1493  CB  VAL A 873      26.406  28.016  16.287  1.00 31.23           C  
ATOM   1494  CG1 VAL A 873      26.014  27.539  17.675  1.00 31.53           C  
ATOM   1495  CG2 VAL A 873      27.916  28.075  16.164  1.00 31.59           C  
ATOM   1496  N   TRP A 874      23.480  27.744  15.005  1.00 30.62           N  
ATOM   1497  CA  TRP A 874      22.038  27.588  15.105  1.00 29.31           C  
ATOM   1498  C   TRP A 874      21.603  26.324  14.421  1.00 29.53           C  
ATOM   1499  O   TRP A 874      20.838  25.535  14.985  1.00 28.70           O  
ATOM   1500  CB  TRP A 874      21.337  28.786  14.479  1.00 28.71           C  
ATOM   1501  CG  TRP A 874      19.837  28.696  14.534  1.00 27.86           C  
ATOM   1502  CD1 TRP A 874      19.021  27.709  13.982  1.00 27.43           C  
ATOM   1503  CD2 TRP A 874      18.916  29.631  15.183  1.00 28.00           C  
ATOM   1504  NE1 TRP A 874      17.703  27.956  14.244  1.00 27.61           N  
ATOM   1505  CE2 TRP A 874      17.563  29.098  14.953  1.00 27.73           C  
ATOM   1506  CE3 TRP A 874      19.066  30.818  15.899  1.00 27.67           C  
ATOM   1507  CZ2 TRP A 874      16.429  29.739  15.430  1.00 27.24           C  
ATOM   1508  CZ3 TRP A 874      17.913  31.455  16.375  1.00 27.85           C  
ATOM   1509  CH2 TRP A 874      16.626  30.925  16.146  1.00 27.67           C  
ATOM   1510  N   SER A 875      22.082  26.135  13.192  1.00 30.24           N  
ATOM   1511  CA  SER A 875      21.799  24.936  12.411  1.00 31.41           C  
ATOM   1512  C   SER A 875      22.296  23.689  13.126  1.00 32.29           C  
ATOM   1513  O   SER A 875      21.619  22.656  13.140  1.00 33.11           O  
ATOM   1514  CB  SER A 875      22.449  25.034  11.031  1.00 32.37           C  
ATOM   1515  OG  SER A 875      21.658  25.811  10.147  1.00 33.41           O  
ATOM   1516  N   TYR A 876      23.480  23.797  13.729  1.00 32.28           N  
ATOM   1517  CA  TYR A 876      24.039  22.716  14.524  1.00 31.28           C  
ATOM   1518  C   TYR A 876      23.075  22.276  15.627  1.00 31.67           C  
ATOM   1519  O   TYR A 876      22.904  21.074  15.861  1.00 32.37           O  
ATOM   1520  CB  TYR A 876      25.392  23.115  15.119  1.00 30.02           C  
ATOM   1521  CG  TYR A 876      25.952  22.055  16.026  1.00 29.56           C  
ATOM   1522  CD1 TYR A 876      26.673  20.977  15.506  1.00 29.65           C  
ATOM   1523  CD2 TYR A 876      25.738  22.106  17.402  1.00 29.25           C  
ATOM   1524  CE1 TYR A 876      27.175  19.988  16.338  1.00 29.93           C  
ATOM   1525  CE2 TYR A 876      26.238  21.122  18.240  1.00 29.88           C  
ATOM   1526  CZ  TYR A 876      26.953  20.069  17.703  1.00 29.63           C  
ATOM   1527  OH  TYR A 876      27.439  19.098  18.535  1.00 30.43           O  
ATOM   1528  N   GLY A 877      22.466  23.253  16.301  1.00 31.23           N  
ATOM   1529  CA  GLY A 877      21.485  22.994  17.350  1.00 32.06           C  
ATOM   1530  C   GLY A 877      20.257  22.240  16.851  1.00 33.23           C  
ATOM   1531  O   GLY A 877      19.791  21.309  17.504  1.00 33.69           O  
ATOM   1532  N   VAL A 878      19.734  22.636  15.692  1.00 33.20           N  
ATOM   1533  CA  VAL A 878      18.575  21.962  15.110  1.00 34.57           C  
ATOM   1534  C   VAL A 878      18.930  20.519  14.721  1.00 35.15           C  
ATOM   1535  O   VAL A 878      18.123  19.605  14.898  1.00 35.71           O  
ATOM   1536  CB  VAL A 878      17.981  22.740  13.906  1.00 34.58           C  
ATOM   1537  CG1 VAL A 878      16.661  22.123  13.465  1.00 34.33           C  
ATOM   1538  CG2 VAL A 878      17.754  24.202  14.266  1.00 34.66           C  
ATOM   1539  N   THR A 879      20.148  20.329  14.217  1.00 35.50           N  
ATOM   1540  CA  THR A 879      20.677  19.011  13.854  1.00 34.73           C  
ATOM   1541  C   THR A 879      20.729  18.062  15.063  1.00 34.66           C  
ATOM   1542  O   THR A 879      20.280  16.914  14.986  1.00 33.99           O  
ATOM   1543  CB  THR A 879      22.067  19.158  13.204  1.00 34.60           C  
ATOM   1544  OG1 THR A 879      21.939  19.914  11.993  1.00 34.41           O  
ATOM   1545  CG2 THR A 879      22.687  17.798  12.892  1.00 34.76           C  
ATOM   1546  N   VAL A 880      21.262  18.555  16.179  1.00 34.84           N  
ATOM   1547  CA  VAL A 880      21.291  17.792  17.422  1.00 35.55           C  
ATOM   1548  C   VAL A 880      19.863  17.400  17.806  1.00 36.42           C  
ATOM   1549  O   VAL A 880      19.603  16.241  18.132  1.00 38.99           O  
ATOM   1550  CB  VAL A 880      22.010  18.564  18.559  1.00 34.96           C  
ATOM   1551  CG1 VAL A 880      21.860  17.849  19.891  1.00 34.15           C  
ATOM   1552  CG2 VAL A 880      23.486  18.739  18.228  1.00 35.16           C  
ATOM   1553  N   TRP A 881      18.941  18.356  17.727  1.00 35.79           N  
ATOM   1554  CA  TRP A 881      17.526  18.096  17.994  1.00 36.39           C  
ATOM   1555  C   TRP A 881      16.959  16.988  17.133  1.00 36.70           C  
ATOM   1556  O   TRP A 881      16.210  16.148  17.630  1.00 36.37           O  
ATOM   1557  CB  TRP A 881      16.704  19.378  17.848  1.00 35.23           C  
ATOM   1558  CG  TRP A 881      15.261  19.218  18.252  1.00 33.96           C  
ATOM   1559  CD1 TRP A 881      14.692  19.479  19.494  1.00 34.10           C  
ATOM   1560  CD2 TRP A 881      14.149  18.741  17.416  1.00 33.81           C  
ATOM   1561  NE1 TRP A 881      13.342  19.209  19.487  1.00 34.07           N  
ATOM   1562  CE2 TRP A 881      12.952  18.762  18.274  1.00 33.73           C  
ATOM   1563  CE3 TRP A 881      14.028  18.317  16.098  1.00 32.86           C  
ATOM   1564  CZ2 TRP A 881      11.705  18.370  17.807  1.00 33.17           C  
ATOM   1565  CZ3 TRP A 881      12.764  17.923  15.641  1.00 33.95           C  
ATOM   1566  CH2 TRP A 881      11.631  17.948  16.477  1.00 33.21           C  
ATOM   1567  N   GLU A 882      17.309  16.977  15.845  1.00 37.68           N  
ATOM   1568  CA  GLU A 882      16.871  15.924  14.920  1.00 39.27           C  
ATOM   1569  C   GLU A 882      17.340  14.545  15.382  1.00 39.44           C  
ATOM   1570  O   GLU A 882      16.622  13.562  15.226  1.00 39.49           O  
ATOM   1571  CB  GLU A 882      17.397  16.159  13.495  1.00 40.99           C  
ATOM   1572  CG  GLU A 882      16.920  17.415  12.778  1.00 43.75           C  
ATOM   1573  CD  GLU A 882      17.365  17.449  11.313  1.00 48.23           C  
ATOM   1574  OE1 GLU A 882      16.782  16.706  10.488  1.00 49.41           O  
ATOM   1575  OE2 GLU A 882      18.302  18.217  10.976  1.00 48.63           O  
ATOM   1576  N   LEU A 883      18.554  14.477  15.927  1.00 39.40           N  
ATOM   1577  CA  LEU A 883      19.123  13.205  16.378  1.00 40.48           C  
ATOM   1578  C   LEU A 883      18.482  12.736  17.672  1.00 40.46           C  
ATOM   1579  O   LEU A 883      18.171  11.552  17.821  1.00 39.96           O  
ATOM   1580  CB  LEU A 883      20.638  13.310  16.585  1.00 41.44           C  
ATOM   1581  CG  LEU A 883      21.541  13.928  15.514  1.00 41.61           C  
ATOM   1582  CD1 LEU A 883      22.982  13.940  16.009  1.00 41.84           C  
ATOM   1583  CD2 LEU A 883      21.418  13.220  14.170  1.00 40.63           C  
ATOM   1584  N   MET A 884      18.295  13.674  18.599  1.00 41.57           N  
ATOM   1585  CA  MET A 884      17.704  13.398  19.910  1.00 42.94           C  
ATOM   1586  C   MET A 884      16.247  12.959  19.827  1.00 41.27           C  
ATOM   1587  O   MET A 884      15.738  12.318  20.740  1.00 42.67           O  
ATOM   1588  CB  MET A 884      17.811  14.623  20.824  1.00 46.24           C  
ATOM   1589  CG  MET A 884      19.221  15.153  21.025  1.00 50.34           C  
ATOM   1590  SD  MET A 884      20.416  13.852  21.373  1.00 58.73           S  
ATOM   1591  CE  MET A 884      21.821  14.822  21.927  1.00 57.21           C  
ATOM   1592  N   THR A 885      15.581  13.309  18.735  1.00 39.68           N  
ATOM   1593  CA  THR A 885      14.187  12.952  18.544  1.00 38.96           C  
ATOM   1594  C   THR A 885      14.076  11.738  17.631  1.00 40.49           C  
ATOM   1595  O   THR A 885      12.971  11.251  17.350  1.00 42.50           O  
ATOM   1596  CB  THR A 885      13.384  14.130  17.968  1.00 38.50           C  
ATOM   1597  OG1 THR A 885      14.054  14.662  16.815  1.00 37.92           O  
ATOM   1598  CG2 THR A 885      13.232  15.223  19.007  1.00 37.90           C  
ATOM   1599  N   PHE A 886      15.237  11.255  17.187  1.00 40.11           N  
ATOM   1600  CA  PHE A 886      15.367  10.115  16.271  1.00 39.31           C  
ATOM   1601  C   PHE A 886      14.772  10.399  14.897  1.00 40.40           C  
ATOM   1602  O   PHE A 886      14.177   9.518  14.258  1.00 43.31           O  
ATOM   1603  CB  PHE A 886      14.820   8.817  16.888  1.00 39.03           C  
ATOM   1604  CG  PHE A 886      15.596   8.346  18.087  1.00 38.09           C  
ATOM   1605  CD1 PHE A 886      16.794   7.646  17.929  1.00 37.79           C  
ATOM   1606  CD2 PHE A 886      15.139   8.608  19.372  1.00 36.84           C  
ATOM   1607  CE1 PHE A 886      17.522   7.220  19.032  1.00 36.70           C  
ATOM   1608  CE2 PHE A 886      15.861   8.179  20.476  1.00 36.62           C  
ATOM   1609  CZ  PHE A 886      17.053   7.486  20.306  1.00 35.90           C  
ATOM   1610  N   GLY A 887      14.949  11.637  14.447  1.00 39.83           N  
ATOM   1611  CA  GLY A 887      14.604  12.016  13.087  1.00 40.81           C  
ATOM   1612  C   GLY A 887      13.189  12.519  12.891  1.00 41.83           C  
ATOM   1613  O   GLY A 887      12.629  12.394  11.797  1.00 41.16           O  
ATOM   1614  N   SER A 888      12.600  13.094  13.936  1.00 42.93           N  
ATOM   1615  CA  SER A 888      11.311  13.758  13.764  1.00 44.57           C  
ATOM   1616  C   SER A 888      11.550  15.130  13.141  1.00 44.67           C  
ATOM   1617  O   SER A 888      12.660  15.667  13.212  1.00 44.86           O  
ATOM   1618  CB  SER A 888      10.527  13.844  15.076  1.00 45.23           C  
ATOM   1619  OG  SER A 888      11.168  14.685  16.010  1.00 47.44           O  
ATOM   1620  N   LYS A 889      10.513  15.678  12.514  1.00 44.82           N  
ATOM   1621  CA  LYS A 889      10.637  16.903  11.723  1.00 42.83           C  
ATOM   1622  C   LYS A 889      10.516  18.160  12.579  1.00 41.83           C  
ATOM   1623  O   LYS A 889       9.637  18.241  13.437  1.00 43.04           O  
ATOM   1624  CB  LYS A 889       9.611  16.898  10.593  1.00 42.93           C  
ATOM   1625  CG  LYS A 889       9.713  15.651   9.730  1.00 45.13           C  
ATOM   1626  CD  LYS A 889       8.647  15.582   8.654  1.00 46.96           C  
ATOM   1627  CE  LYS A 889       8.844  14.333   7.812  1.00 47.61           C  
ATOM   1628  NZ  LYS A 889       8.328  14.534   6.430  1.00 51.33           N  
ATOM   1629  N   PRO A 890      11.418  19.139  12.363  1.00 40.51           N  
ATOM   1630  CA  PRO A 890      11.372  20.374  13.142  1.00 39.66           C  
ATOM   1631  C   PRO A 890      10.149  21.214  12.786  1.00 39.76           C  
ATOM   1632  O   PRO A 890       9.807  21.341  11.607  1.00 38.10           O  
ATOM   1633  CB  PRO A 890      12.660  21.102  12.730  1.00 38.09           C  
ATOM   1634  CG  PRO A 890      13.514  20.066  12.092  1.00 38.81           C  
ATOM   1635  CD  PRO A 890      12.550  19.141  11.424  1.00 39.11           C  
ATOM   1636  N   TYR A 891       9.504  21.771  13.811  1.00 41.71           N  
ATOM   1637  CA  TYR A 891       8.299  22.594  13.658  1.00 42.99           C  
ATOM   1638  C   TYR A 891       7.291  21.914  12.728  1.00 45.41           C  
ATOM   1639  O   TYR A 891       6.811  22.507  11.754  1.00 45.05           O  
ATOM   1640  CB  TYR A 891       8.646  24.001  13.152  1.00 42.10           C  
ATOM   1641  CG  TYR A 891       9.868  24.644  13.792  1.00 41.16           C  
ATOM   1642  CD1 TYR A 891       9.776  25.310  15.018  1.00 40.99           C  
ATOM   1643  CD2 TYR A 891      11.108  24.616  13.150  1.00 39.89           C  
ATOM   1644  CE1 TYR A 891      10.889  25.914  15.590  1.00 41.52           C  
ATOM   1645  CE2 TYR A 891      12.226  25.215  13.713  1.00 39.59           C  
ATOM   1646  CZ  TYR A 891      12.117  25.863  14.931  1.00 40.77           C  
ATOM   1647  OH  TYR A 891      13.232  26.454  15.495  1.00 38.97           O  
ATOM   1648  N   ASP A 892       7.004  20.648  13.026  1.00 48.16           N  
ATOM   1649  CA  ASP A 892       6.092  19.844  12.223  1.00 50.07           C  
ATOM   1650  C   ASP A 892       4.672  20.413  12.294  1.00 50.64           C  
ATOM   1651  O   ASP A 892       4.184  20.770  13.373  1.00 49.45           O  
ATOM   1652  CB  ASP A 892       6.120  18.391  12.702  1.00 51.75           C  
ATOM   1653  CG  ASP A 892       5.481  17.429  11.713  1.00 54.31           C  
ATOM   1654  OD1 ASP A 892       5.435  17.728  10.495  1.00 55.19           O  
ATOM   1655  OD2 ASP A 892       5.032  16.354  12.164  1.00 55.46           O  
ATOM   1656  N   GLY A 893       4.029  20.518  11.135  1.00 50.26           N  
ATOM   1657  CA  GLY A 893       2.697  21.102  11.048  1.00 52.69           C  
ATOM   1658  C   GLY A 893       2.709  22.601  10.807  1.00 53.20           C  
ATOM   1659  O   GLY A 893       1.739  23.159  10.289  1.00 55.78           O  
ATOM   1660  N   ILE A 894       3.807  23.255  11.180  1.00 51.20           N  
ATOM   1661  CA  ILE A 894       3.951  24.701  11.009  1.00 48.66           C  
ATOM   1662  C   ILE A 894       4.523  25.037   9.624  1.00 47.93           C  
ATOM   1663  O   ILE A 894       5.657  24.675   9.322  1.00 47.47           O  
ATOM   1664  CB  ILE A 894       4.834  25.315  12.118  1.00 47.51           C  
ATOM   1665  CG1 ILE A 894       4.230  25.038  13.502  1.00 47.24           C  
ATOM   1666  CG2 ILE A 894       5.028  26.809  11.888  1.00 47.55           C  
ATOM   1667  CD1 ILE A 894       5.217  25.118  14.651  1.00 46.97           C  
ATOM   1668  N   PRO A 895       3.736  25.732   8.775  1.00 47.76           N  
ATOM   1669  CA  PRO A 895       4.259  26.135   7.463  1.00 46.84           C  
ATOM   1670  C   PRO A 895       5.482  27.054   7.570  1.00 45.80           C  
ATOM   1671  O   PRO A 895       5.601  27.822   8.524  1.00 45.53           O  
ATOM   1672  CB  PRO A 895       3.078  26.873   6.817  1.00 45.87           C  
ATOM   1673  CG  PRO A 895       2.192  27.261   7.946  1.00 45.80           C  
ATOM   1674  CD  PRO A 895       2.349  26.191   8.981  1.00 46.03           C  
ATOM   1675  N   ALA A 896       6.371  26.967   6.585  1.00 45.60           N  
ATOM   1676  CA  ALA A 896       7.641  27.705   6.572  1.00 45.18           C  
ATOM   1677  C   ALA A 896       7.515  29.224   6.749  1.00 46.19           C  
ATOM   1678  O   ALA A 896       8.363  29.850   7.392  1.00 47.69           O  
ATOM   1679  CB  ALA A 896       8.411  27.387   5.300  1.00 42.70           C  
ATOM   1680  N   SER A 897       6.457  29.805   6.187  1.00 46.80           N  
ATOM   1681  CA  SER A 897       6.237  31.259   6.213  1.00 47.05           C  
ATOM   1682  C   SER A 897       6.024  31.843   7.613  1.00 46.59           C  
ATOM   1683  O   SER A 897       6.022  33.063   7.784  1.00 46.87           O  
ATOM   1684  CB  SER A 897       5.041  31.617   5.329  1.00 48.33           C  
ATOM   1685  OG  SER A 897       3.875  30.939   5.771  1.00 49.50           O  
ATOM   1686  N   GLU A 898       5.853  30.974   8.607  1.00 46.08           N  
ATOM   1687  CA  GLU A 898       5.507  31.404   9.959  1.00 45.57           C  
ATOM   1688  C   GLU A 898       6.668  31.294  10.928  1.00 44.46           C  
ATOM   1689  O   GLU A 898       6.568  31.760  12.067  1.00 44.44           O  
ATOM   1690  CB  GLU A 898       4.330  30.591  10.490  1.00 46.95           C  
ATOM   1691  CG  GLU A 898       3.127  30.580   9.561  1.00 49.94           C  
ATOM   1692  CD  GLU A 898       1.899  29.929  10.176  1.00 51.73           C  
ATOM   1693  OE1 GLU A 898       0.895  29.777   9.445  1.00 52.03           O  
ATOM   1694  OE2 GLU A 898       1.934  29.570  11.378  1.00 50.17           O  
ATOM   1695  N   ILE A 899       7.763  30.686  10.475  1.00 42.51           N  
ATOM   1696  CA  ILE A 899       8.903  30.386  11.347  1.00 41.92           C  
ATOM   1697  C   ILE A 899       9.514  31.645  11.973  1.00 41.95           C  
ATOM   1698  O   ILE A 899       9.679  31.705  13.196  1.00 43.12           O  
ATOM   1699  CB  ILE A 899       9.977  29.496  10.646  1.00 41.50           C  
ATOM   1700  CG1 ILE A 899       9.373  28.161  10.182  1.00 39.70           C  
ATOM   1701  CG2 ILE A 899      11.190  29.256  11.543  1.00 38.42           C  
ATOM   1702  CD1 ILE A 899       8.824  27.287  11.296  1.00 40.47           C  
ATOM   1703  N   SER A 900       9.816  32.656  11.160  1.00 40.78           N  
ATOM   1704  CA  SER A 900      10.421  33.874  11.700  1.00 41.75           C  
ATOM   1705  C   SER A 900       9.617  34.455  12.861  1.00 42.23           C  
ATOM   1706  O   SER A 900      10.167  34.696  13.933  1.00 43.69           O  
ATOM   1707  CB  SER A 900      10.674  34.929  10.616  1.00 41.65           C  
ATOM   1708  OG  SER A 900       9.542  35.127   9.796  1.00 43.45           O  
ATOM   1709  N   SER A 901       8.313  34.631  12.657  1.00 43.63           N  
ATOM   1710  CA  SER A 901       7.428  35.233  13.660  1.00 43.76           C  
ATOM   1711  C   SER A 901       7.256  34.415  14.941  1.00 44.30           C  
ATOM   1712  O   SER A 901       7.177  34.990  16.025  1.00 45.32           O  
ATOM   1713  CB  SER A 901       6.067  35.560  13.052  1.00 44.15           C  
ATOM   1714  OG  SER A 901       5.664  34.544  12.157  1.00 45.99           O  
ATOM   1715  N   ILE A 902       7.198  33.091  14.827  1.00 44.24           N  
ATOM   1716  CA  ILE A 902       7.173  32.241  16.027  1.00 43.04           C  
ATOM   1717  C   ILE A 902       8.536  32.223  16.725  1.00 42.34           C  
ATOM   1718  O   ILE A 902       8.604  32.072  17.945  1.00 42.34           O  
ATOM   1719  CB  ILE A 902       6.638  30.799  15.774  1.00 44.20           C  
ATOM   1720  CG1 ILE A 902       7.649  29.917  15.025  1.00 44.94           C  
ATOM   1721  CG2 ILE A 902       5.296  30.826  15.055  1.00 44.33           C  
ATOM   1722  CD1 ILE A 902       8.524  29.065  15.922  1.00 44.26           C  
ATOM   1723  N   LEU A 903       9.612  32.380  15.951  1.00 41.21           N  
ATOM   1724  CA  LEU A 903      10.952  32.539  16.524  1.00 40.27           C  
ATOM   1725  C   LEU A 903      11.074  33.844  17.297  1.00 41.07           C  
ATOM   1726  O   LEU A 903      11.680  33.877  18.374  1.00 39.97           O  
ATOM   1727  CB  LEU A 903      12.042  32.450  15.450  1.00 39.15           C  
ATOM   1728  CG  LEU A 903      12.373  31.083  14.831  1.00 38.55           C  
ATOM   1729  CD1 LEU A 903      13.446  31.238  13.765  1.00 37.55           C  
ATOM   1730  CD2 LEU A 903      12.790  30.047  15.867  1.00 37.02           C  
ATOM   1731  N   GLU A 904      10.482  34.910  16.748  1.00 42.52           N  
ATOM   1732  CA  GLU A 904      10.488  36.230  17.386  1.00 42.78           C  
ATOM   1733  C   GLU A 904       9.597  36.270  18.624  1.00 42.63           C  
ATOM   1734  O   GLU A 904       9.811  37.084  19.514  1.00 42.47           O  
ATOM   1735  CB  GLU A 904      10.088  37.331  16.405  1.00 45.65           C  
ATOM   1736  CG  GLU A 904      10.941  37.394  15.148  1.00 50.76           C  
ATOM   1737  CD  GLU A 904      11.460  38.789  14.850  1.00 55.25           C  
ATOM   1738  OE1 GLU A 904      11.095  39.352  13.790  1.00 55.67           O  
ATOM   1739  OE2 GLU A 904      12.243  39.320  15.677  1.00 56.84           O  
ATOM   1740  N   LYS A 905       8.600  35.388  18.673  1.00 44.39           N  
ATOM   1741  CA  LYS A 905       7.793  35.180  19.875  1.00 46.59           C  
ATOM   1742  C   LYS A 905       8.582  34.379  20.906  1.00 47.35           C  
ATOM   1743  O   LYS A 905       8.148  34.226  22.052  1.00 48.47           O  
ATOM   1744  CB  LYS A 905       6.503  34.426  19.545  1.00 48.51           C  
ATOM   1745  CG  LYS A 905       5.437  35.243  18.830  1.00 51.48           C  
ATOM   1746  CD  LYS A 905       4.251  34.369  18.431  1.00 52.97           C  
ATOM   1747  CE  LYS A 905       3.435  33.948  19.647  1.00 54.16           C  
ATOM   1748  NZ  LYS A 905       2.479  32.852  19.353  1.00 54.00           N  
ATOM   1749  N   GLY A 906       9.728  33.848  20.485  1.00 47.63           N  
ATOM   1750  CA  GLY A 906      10.616  33.117  21.378  1.00 47.58           C  
ATOM   1751  C   GLY A 906      10.300  31.640  21.491  1.00 47.47           C  
ATOM   1752  O   GLY A 906      10.790  30.968  22.395  1.00 47.32           O  
ATOM   1753  N   GLU A 907       9.490  31.141  20.571  1.00 48.93           N  
ATOM   1754  CA  GLU A 907       9.210  29.720  20.481  1.00 49.18           C  
ATOM   1755  C   GLU A 907      10.395  28.967  19.917  1.00 45.52           C  
ATOM   1756  O   GLU A 907      11.073  29.448  19.027  1.00 44.58           O  
ATOM   1757  CB  GLU A 907       7.970  29.472  19.636  1.00 53.78           C  
ATOM   1758  CG  GLU A 907       6.686  29.948  20.287  1.00 59.95           C  
ATOM   1759  CD  GLU A 907       5.456  29.516  19.518  1.00 66.82           C  
ATOM   1760  OE1 GLU A 907       4.575  30.366  19.297  1.00 70.66           O  
ATOM   1761  OE2 GLU A 907       5.372  28.329  19.132  1.00 68.63           O  
ATOM   1762  N   ARG A 908      10.618  27.771  20.438  1.00 42.03           N  
ATOM   1763  CA  ARG A 908      11.765  26.954  20.084  1.00 40.93           C  
ATOM   1764  C   ARG A 908      11.335  25.508  20.007  1.00 41.93           C  
ATOM   1765  O   ARG A 908      10.238  25.164  20.413  1.00 42.54           O  
ATOM   1766  CB  ARG A 908      12.877  27.098  21.116  1.00 38.39           C  
ATOM   1767  CG  ARG A 908      13.519  28.465  21.164  1.00 37.38           C  
ATOM   1768  CD  ARG A 908      14.126  28.822  19.832  1.00 37.53           C  
ATOM   1769  NE  ARG A 908      14.744  30.136  19.865  1.00 38.12           N  
ATOM   1770  CZ  ARG A 908      14.099  31.274  19.659  1.00 37.59           C  
ATOM   1771  NH1 ARG A 908      12.809  31.271  19.405  1.00 37.02           N  
ATOM   1772  NH2 ARG A 908      14.750  32.417  19.710  1.00 36.81           N  
ATOM   1773  N   LEU A 909      12.190  24.663  19.453  1.00 41.07           N  
ATOM   1774  CA  LEU A 909      11.933  23.238  19.445  1.00 38.98           C  
ATOM   1775  C   LEU A 909      11.892  22.736  20.877  1.00 38.67           C  
ATOM   1776  O   LEU A 909      12.703  23.145  21.694  1.00 37.97           O  
ATOM   1777  CB  LEU A 909      13.031  22.528  18.676  1.00 37.28           C  
ATOM   1778  CG  LEU A 909      13.093  22.916  17.211  1.00 35.74           C  
ATOM   1779  CD1 LEU A 909      14.446  22.574  16.628  1.00 35.18           C  
ATOM   1780  CD2 LEU A 909      11.995  22.191  16.473  1.00 35.66           C  
ATOM   1781  N   PRO A 910      10.948  21.853  21.183  1.00 38.20           N  
ATOM   1782  CA  PRO A 910      10.747  21.420  22.568  1.00 38.78           C  
ATOM   1783  C   PRO A 910      11.821  20.432  23.031  1.00 39.75           C  
ATOM   1784  O   PRO A 910      12.476  19.795  22.197  1.00 39.69           O  
ATOM   1785  CB  PRO A 910       9.375  20.741  22.521  1.00 37.54           C  
ATOM   1786  CG  PRO A 910       9.265  20.218  21.133  1.00 36.88           C  
ATOM   1787  CD  PRO A 910      10.040  21.160  20.249  1.00 37.29           C  
ATOM   1788  N   GLN A 911      11.996  20.316  24.346  1.00 40.36           N  
ATOM   1789  CA  GLN A 911      12.925  19.346  24.919  1.00 41.12           C  
ATOM   1790  C   GLN A 911      12.556  17.939  24.451  1.00 41.95           C  
ATOM   1791  O   GLN A 911      11.424  17.493  24.653  1.00 42.21           O  
ATOM   1792  CB  GLN A 911      12.934  19.430  26.448  1.00 40.87           C  
ATOM   1793  CG  GLN A 911      14.066  18.658  27.113  1.00 42.13           C  
ATOM   1794  CD  GLN A 911      14.065  18.762  28.635  1.00 43.38           C  
ATOM   1795  OE1 GLN A 911      13.595  19.745  29.211  1.00 44.10           O  
ATOM   1796  NE2 GLN A 911      14.608  17.743  29.294  1.00 45.07           N  
ATOM   1797  N   PRO A 912      13.505  17.245  23.794  1.00 43.10           N  
ATOM   1798  CA  PRO A 912      13.231  15.888  23.346  1.00 43.45           C  
ATOM   1799  C   PRO A 912      13.124  14.959  24.547  1.00 45.03           C  
ATOM   1800  O   PRO A 912      13.901  15.104  25.495  1.00 45.69           O  
ATOM   1801  CB  PRO A 912      14.457  15.545  22.491  1.00 42.61           C  
ATOM   1802  CG  PRO A 912      15.076  16.858  22.149  1.00 42.03           C  
ATOM   1803  CD  PRO A 912      14.847  17.684  23.376  1.00 42.97           C  
ATOM   1804  N   PRO A 913      12.155  14.023  24.523  1.00 47.00           N  
ATOM   1805  CA  PRO A 913      11.890  13.139  25.668  1.00 46.72           C  
ATOM   1806  C   PRO A 913      13.140  12.493  26.287  1.00 46.20           C  
ATOM   1807  O   PRO A 913      13.238  12.428  27.511  1.00 47.79           O  
ATOM   1808  CB  PRO A 913      10.949  12.082  25.080  1.00 46.06           C  
ATOM   1809  CG  PRO A 913      10.215  12.820  24.010  1.00 45.98           C  
ATOM   1810  CD  PRO A 913      11.224  13.760  23.406  1.00 46.01           C  
ATOM   1811  N   ILE A 914      14.092  12.048  25.467  1.00 45.56           N  
ATOM   1812  CA  ILE A 914      15.306  11.400  25.994  1.00 48.14           C  
ATOM   1813  C   ILE A 914      16.335  12.356  26.624  1.00 49.72           C  
ATOM   1814  O   ILE A 914      17.257  11.905  27.304  1.00 51.45           O  
ATOM   1815  CB  ILE A 914      16.025  10.507  24.945  1.00 48.02           C  
ATOM   1816  CG1 ILE A 914      16.581  11.353  23.791  1.00 48.99           C  
ATOM   1817  CG2 ILE A 914      15.108   9.392  24.452  1.00 46.73           C  
ATOM   1818  CD1 ILE A 914      17.835  10.793  23.153  1.00 48.24           C  
ATOM   1819  N   CYS A 915      16.171  13.661  26.401  1.00 51.59           N  
ATOM   1820  CA  CYS A 915      17.151  14.667  26.833  1.00 53.43           C  
ATOM   1821  C   CYS A 915      17.042  15.105  28.286  1.00 52.42           C  
ATOM   1822  O   CYS A 915      15.968  15.471  28.758  1.00 51.85           O  
ATOM   1823  CB  CYS A 915      17.055  15.921  25.965  1.00 57.09           C  
ATOM   1824  SG  CYS A 915      17.991  15.846  24.429  1.00 66.70           S  
ATOM   1825  N   THR A 916      18.172  15.088  28.984  1.00 52.91           N  
ATOM   1826  CA  THR A 916      18.276  15.795  30.254  1.00 53.00           C  
ATOM   1827  C   THR A 916      18.366  17.288  29.951  1.00 52.64           C  
ATOM   1828  O   THR A 916      18.749  17.684  28.845  1.00 51.67           O  
ATOM   1829  CB  THR A 916      19.500  15.361  31.080  1.00 51.13           C  
ATOM   1830  OG1 THR A 916      20.696  15.577  30.318  1.00 51.04           O  
ATOM   1831  CG2 THR A 916      19.386  13.896  31.477  1.00 50.19           C  
ATOM   1832  N   ILE A 917      18.018  18.106  30.939  1.00 51.30           N  
ATOM   1833  CA  ILE A 917      17.943  19.548  30.753  1.00 51.00           C  
ATOM   1834  C   ILE A 917      19.304  20.190  30.431  1.00 53.13           C  
ATOM   1835  O   ILE A 917      19.359  21.216  29.747  1.00 52.93           O  
ATOM   1836  CB  ILE A 917      17.207  20.237  31.936  1.00 48.90           C  
ATOM   1837  CG1 ILE A 917      16.910  21.707  31.627  1.00 46.98           C  
ATOM   1838  CG2 ILE A 917      17.959  20.047  33.248  1.00 49.64           C  
ATOM   1839  CD1 ILE A 917      15.820  21.902  30.597  1.00 45.73           C  
ATOM   1840  N   ASP A 918      20.390  19.568  30.891  1.00 55.51           N  
ATOM   1841  CA  ASP A 918      21.744  20.056  30.595  1.00 57.17           C  
ATOM   1842  C   ASP A 918      22.106  19.939  29.116  1.00 54.25           C  
ATOM   1843  O   ASP A 918      22.786  20.807  28.565  1.00 53.96           O  
ATOM   1844  CB  ASP A 918      22.789  19.348  31.461  1.00 62.49           C  
ATOM   1845  CG  ASP A 918      22.914  19.964  32.850  1.00 69.00           C  
ATOM   1846  OD1 ASP A 918      22.808  21.207  32.978  1.00 69.68           O  
ATOM   1847  OD2 ASP A 918      23.124  19.201  33.820  1.00 73.83           O  
ATOM   1848  N   VAL A 919      21.649  18.865  28.480  1.00 50.73           N  
ATOM   1849  CA  VAL A 919      21.816  18.702  27.044  1.00 47.30           C  
ATOM   1850  C   VAL A 919      20.923  19.703  26.315  1.00 46.77           C  
ATOM   1851  O   VAL A 919      21.351  20.330  25.345  1.00 47.85           O  
ATOM   1852  CB  VAL A 919      21.494  17.266  26.584  1.00 46.36           C  
ATOM   1853  CG1 VAL A 919      21.732  17.112  25.090  1.00 45.61           C  
ATOM   1854  CG2 VAL A 919      22.345  16.266  27.345  1.00 46.77           C  
ATOM   1855  N   TYR A 920      19.695  19.871  26.799  1.00 45.86           N  
ATOM   1856  CA  TYR A 920      18.753  20.776  26.152  1.00 44.23           C  
ATOM   1857  C   TYR A 920      19.183  22.239  26.206  1.00 42.91           C  
ATOM   1858  O   TYR A 920      18.931  22.993  25.264  1.00 42.41           O  
ATOM   1859  CB  TYR A 920      17.331  20.622  26.703  1.00 44.68           C  
ATOM   1860  CG  TYR A 920      16.358  21.524  25.979  1.00 45.12           C  
ATOM   1861  CD1 TYR A 920      16.049  21.300  24.641  1.00 46.32           C  
ATOM   1862  CD2 TYR A 920      15.790  22.626  26.609  1.00 44.69           C  
ATOM   1863  CE1 TYR A 920      15.181  22.133  23.956  1.00 47.16           C  
ATOM   1864  CE2 TYR A 920      14.920  23.465  25.933  1.00 45.12           C  
ATOM   1865  CZ  TYR A 920      14.620  23.213  24.607  1.00 46.21           C  
ATOM   1866  OH  TYR A 920      13.757  24.031  23.921  1.00 47.44           O  
ATOM   1867  N   MET A 921      19.821  22.646  27.299  1.00 42.50           N  
ATOM   1868  CA  MET A 921      20.259  24.033  27.420  1.00 43.11           C  
ATOM   1869  C   MET A 921      21.339  24.362  26.409  1.00 43.83           C  
ATOM   1870  O   MET A 921      21.378  25.473  25.890  1.00 45.04           O  
ATOM   1871  CB  MET A 921      20.692  24.388  28.841  1.00 43.83           C  
ATOM   1872  CG  MET A 921      19.529  24.496  29.823  1.00 46.28           C  
ATOM   1873  SD  MET A 921      17.993  25.153  29.118  1.00 49.56           S  
ATOM   1874  CE  MET A 921      18.360  26.906  29.075  1.00 48.05           C  
ATOM   1875  N   ILE A 922      22.187  23.385  26.100  1.00 43.37           N  
ATOM   1876  CA  ILE A 922      23.171  23.561  25.043  1.00 43.30           C  
ATOM   1877  C   ILE A 922      22.470  23.859  23.712  1.00 43.45           C  
ATOM   1878  O   ILE A 922      22.762  24.871  23.073  1.00 43.78           O  
ATOM   1879  CB  ILE A 922      24.177  22.389  24.968  1.00 43.02           C  
ATOM   1880  CG1 ILE A 922      25.164  22.504  26.131  1.00 43.40           C  
ATOM   1881  CG2 ILE A 922      24.939  22.411  23.648  1.00 42.57           C  
ATOM   1882  CD1 ILE A 922      26.043  21.291  26.331  1.00 47.02           C  
ATOM   1883  N   MET A 923      21.533  22.993  23.323  1.00 43.73           N  
ATOM   1884  CA  MET A 923      20.680  23.226  22.150  1.00 44.28           C  
ATOM   1885  C   MET A 923      20.019  24.609  22.187  1.00 43.37           C  
ATOM   1886  O   MET A 923      20.028  25.344  21.194  1.00 41.83           O  
ATOM   1887  CB  MET A 923      19.590  22.157  22.061  1.00 46.13           C  
ATOM   1888  CG  MET A 923      20.042  20.826  21.482  1.00 49.79           C  
ATOM   1889  SD  MET A 923      18.872  19.482  21.797  1.00 53.31           S  
ATOM   1890  CE  MET A 923      17.319  20.280  21.406  1.00 52.21           C  
ATOM   1891  N   ARG A 924      19.457  24.956  23.343  1.00 41.81           N  
ATOM   1892  CA  ARG A 924      18.759  26.221  23.518  1.00 40.91           C  
ATOM   1893  C   ARG A 924      19.683  27.434  23.341  1.00 40.44           C  
ATOM   1894  O   ARG A 924      19.291  28.435  22.734  1.00 40.33           O  
ATOM   1895  CB  ARG A 924      18.051  26.245  24.876  1.00 40.43           C  
ATOM   1896  CG  ARG A 924      17.291  27.525  25.176  1.00 40.99           C  
ATOM   1897  CD  ARG A 924      16.186  27.778  24.164  1.00 41.09           C  
ATOM   1898  NE  ARG A 924      15.604  29.106  24.340  1.00 41.69           N  
ATOM   1899  CZ  ARG A 924      15.921  30.177  23.613  1.00 43.34           C  
ATOM   1900  NH1 ARG A 924      16.820  30.098  22.636  1.00 43.39           N  
ATOM   1901  NH2 ARG A 924      15.326  31.336  23.859  1.00 44.75           N  
ATOM   1902  N   LYS A 925      20.908  27.330  23.855  1.00 39.39           N  
ATOM   1903  CA  LYS A 925      21.900  28.404  23.744  1.00 38.77           C  
ATOM   1904  C   LYS A 925      22.283  28.716  22.295  1.00 39.15           C  
ATOM   1905  O   LYS A 925      22.645  29.849  21.973  1.00 39.70           O  
ATOM   1906  CB  LYS A 925      23.143  28.065  24.563  1.00 39.06           C  
ATOM   1907  CG  LYS A 925      23.015  28.407  26.038  1.00 39.42           C  
ATOM   1908  CD  LYS A 925      23.955  27.561  26.880  1.00 41.46           C  
ATOM   1909  CE  LYS A 925      24.117  28.133  28.283  1.00 43.14           C  
ATOM   1910  NZ  LYS A 925      22.835  28.134  29.044  1.00 45.29           N  
ATOM   1911  N   CYS A 926      22.140  27.721  21.434  1.00 39.36           N  
ATOM   1912  CA  CYS A 926      22.388  27.844  20.007  1.00 37.91           C  
ATOM   1913  C   CYS A 926      21.326  28.660  19.285  1.00 36.94           C  
ATOM   1914  O   CYS A 926      21.519  29.057  18.154  1.00 36.84           O  
ATOM   1915  CB  CYS A 926      22.504  26.464  19.375  1.00 39.75           C  
ATOM   1916  SG  CYS A 926      23.858  25.444  20.000  1.00 44.77           S  
ATOM   1917  N   TRP A 927      20.197  28.882  19.943  1.00 36.70           N  
ATOM   1918  CA  TRP A 927      19.027  29.506  19.351  1.00 35.57           C  
ATOM   1919  C   TRP A 927      18.763  30.890  19.862  1.00 37.08           C  
ATOM   1920  O   TRP A 927      17.605  31.303  20.022  1.00 35.84           O  
ATOM   1921  CB  TRP A 927      17.804  28.629  19.529  1.00 33.61           C  
ATOM   1922  CG  TRP A 927      17.957  27.283  18.888  1.00 32.46           C  
ATOM   1923  CD1 TRP A 927      18.688  26.964  17.759  1.00 32.62           C  
ATOM   1924  CD2 TRP A 927      17.379  26.015  19.332  1.00 32.52           C  
ATOM   1925  NE1 TRP A 927      18.605  25.636  17.483  1.00 32.50           N  
ATOM   1926  CE2 TRP A 927      17.836  25.008  18.385  1.00 32.81           C  
ATOM   1927  CE3 TRP A 927      16.561  25.631  20.376  1.00 31.98           C  
ATOM   1928  CZ2 TRP A 927      17.473  23.687  18.496  1.00 32.67           C  
ATOM   1929  CZ3 TRP A 927      16.208  24.293  20.479  1.00 31.67           C  
ATOM   1930  CH2 TRP A 927      16.653  23.347  19.560  1.00 32.65           C  
ATOM   1931  N   MET A 928      19.832  31.597  20.184  1.00 38.45           N  
ATOM   1932  CA  MET A 928      19.753  32.938  20.732  1.00 39.52           C  
ATOM   1933  C   MET A 928      19.667  33.958  19.621  1.00 40.28           C  
ATOM   1934  O   MET A 928      20.288  33.783  18.572  1.00 40.35           O  
ATOM   1935  CB  MET A 928      20.948  33.215  21.639  1.00 41.28           C  
ATOM   1936  CG  MET A 928      20.826  32.526  22.984  1.00 44.80           C  
ATOM   1937  SD  MET A 928      22.350  32.520  23.938  1.00 51.39           S  
ATOM   1938  CE  MET A 928      22.185  34.039  24.873  1.00 51.66           C  
ATOM   1939  N   ILE A 929      18.889  35.017  19.850  1.00 40.54           N  
ATOM   1940  CA  ILE A 929      18.733  36.091  18.865  1.00 42.35           C  
ATOM   1941  C   ILE A 929      20.083  36.719  18.534  1.00 43.05           C  
ATOM   1942  O   ILE A 929      20.437  36.833  17.367  1.00 44.70           O  
ATOM   1943  CB  ILE A 929      17.706  37.176  19.299  1.00 42.29           C  
ATOM   1944  CG1 ILE A 929      16.337  36.551  19.642  1.00 42.45           C  
ATOM   1945  CG2 ILE A 929      17.563  38.251  18.225  1.00 40.83           C  
ATOM   1946  CD1 ILE A 929      15.644  35.801  18.514  1.00 41.90           C  
ATOM   1947  N   ASP A 930      20.837  37.107  19.555  1.00 45.18           N  
ATOM   1948  CA  ASP A 930      22.184  37.630  19.343  1.00 47.77           C  
ATOM   1949  C   ASP A 930      23.143  36.497  18.974  1.00 45.92           C  
ATOM   1950  O   ASP A 930      23.349  35.562  19.754  1.00 44.56           O  
ATOM   1951  CB  ASP A 930      22.671  38.382  20.588  1.00 52.21           C  
ATOM   1952  CG  ASP A 930      23.933  39.205  20.334  1.00 54.50           C  
ATOM   1953  OD1 ASP A 930      24.353  39.359  19.162  1.00 55.03           O  
ATOM   1954  OD2 ASP A 930      24.506  39.705  21.327  1.00 56.55           O  
ATOM   1955  N   ALA A 931      23.720  36.597  17.778  1.00 45.67           N  
ATOM   1956  CA  ALA A 931      24.609  35.566  17.230  1.00 47.43           C  
ATOM   1957  C   ALA A 931      25.903  35.375  18.029  1.00 49.30           C  
ATOM   1958  O   ALA A 931      26.359  34.242  18.208  1.00 49.84           O  
ATOM   1959  CB  ALA A 931      24.920  35.848  15.764  1.00 45.40           C  
ATOM   1960  N   ASP A 932      26.479  36.477  18.513  1.00 50.40           N  
ATOM   1961  CA  ASP A 932      27.740  36.437  19.268  1.00 50.70           C  
ATOM   1962  C   ASP A 932      27.616  35.853  20.681  1.00 48.24           C  
ATOM   1963  O   ASP A 932      28.621  35.626  21.358  1.00 49.02           O  
ATOM   1964  CB  ASP A 932      28.381  37.830  19.320  1.00 54.17           C  
ATOM   1965  CG  ASP A 932      29.077  38.209  18.014  1.00 57.10           C  
ATOM   1966  OD1 ASP A 932      29.148  37.359  17.092  1.00 58.34           O  
ATOM   1967  OD2 ASP A 932      29.555  39.363  17.914  1.00 57.10           O  
ATOM   1968  N   SER A 933      26.385  35.612  21.118  1.00 45.61           N  
ATOM   1969  CA  SER A 933      26.133  35.023  22.429  1.00 43.45           C  
ATOM   1970  C   SER A 933      25.972  33.508  22.338  1.00 42.12           C  
ATOM   1971  O   SER A 933      26.118  32.809  23.341  1.00 41.22           O  
ATOM   1972  CB  SER A 933      24.898  35.655  23.063  1.00 43.17           C  
ATOM   1973  OG  SER A 933      25.022  37.064  23.081  1.00 43.37           O  
ATOM   1974  N   ARG A 934      25.660  33.023  21.135  1.00 40.02           N  
ATOM   1975  CA  ARG A 934      25.587  31.592  20.866  1.00 38.06           C  
ATOM   1976  C   ARG A 934      26.944  30.958  21.120  1.00 38.37           C  
ATOM   1977  O   ARG A 934      27.972  31.582  20.859  1.00 39.09           O  
ATOM   1978  CB  ARG A 934      25.191  31.333  19.413  1.00 36.82           C  
ATOM   1979  CG  ARG A 934      23.717  31.502  19.112  1.00 34.72           C  
ATOM   1980  CD  ARG A 934      23.502  31.617  17.615  1.00 32.56           C  
ATOM   1981  NE  ARG A 934      22.408  32.535  17.322  1.00 31.47           N  
ATOM   1982  CZ  ARG A 934      22.138  33.030  16.120  1.00 31.21           C  
ATOM   1983  NH1 ARG A 934      22.879  32.705  15.064  1.00 31.62           N  
ATOM   1984  NH2 ARG A 934      21.122  33.862  15.976  1.00 30.37           N  
ATOM   1985  N   PRO A 935      26.957  29.704  21.606  1.00 38.97           N  
ATOM   1986  CA  PRO A 935      28.231  29.029  21.838  1.00 39.27           C  
ATOM   1987  C   PRO A 935      29.059  28.971  20.560  1.00 39.31           C  
ATOM   1988  O   PRO A 935      28.529  29.176  19.468  1.00 38.84           O  
ATOM   1989  CB  PRO A 935      27.812  27.607  22.238  1.00 40.12           C  
ATOM   1990  CG  PRO A 935      26.373  27.698  22.623  1.00 39.38           C  
ATOM   1991  CD  PRO A 935      25.809  28.793  21.779  1.00 38.90           C  
ATOM   1992  N   LYS A 936      30.351  28.708  20.694  1.00 41.33           N  
ATOM   1993  CA  LYS A 936      31.190  28.468  19.520  1.00 43.20           C  
ATOM   1994  C   LYS A 936      31.452  26.971  19.352  1.00 41.78           C  
ATOM   1995  O   LYS A 936      31.559  26.242  20.341  1.00 42.36           O  
ATOM   1996  CB  LYS A 936      32.504  29.256  19.608  1.00 44.76           C  
ATOM   1997  CG  LYS A 936      32.403  30.702  19.142  1.00 46.20           C  
ATOM   1998  CD  LYS A 936      31.918  31.626  20.249  1.00 49.31           C  
ATOM   1999  CE  LYS A 936      31.812  33.064  19.760  1.00 51.89           C  
ATOM   2000  NZ  LYS A 936      31.517  33.998  20.879  1.00 53.79           N  
ATOM   2001  N   PHE A 937      31.541  26.514  18.105  1.00 39.91           N  
ATOM   2002  CA  PHE A 937      31.863  25.109  17.822  1.00 41.90           C  
ATOM   2003  C   PHE A 937      33.036  24.571  18.661  1.00 44.08           C  
ATOM   2004  O   PHE A 937      32.993  23.435  19.151  1.00 43.53           O  
ATOM   2005  CB  PHE A 937      32.117  24.890  16.325  1.00 38.84           C  
ATOM   2006  CG  PHE A 937      30.874  24.945  15.491  1.00 37.70           C  
ATOM   2007  CD1 PHE A 937      29.872  23.984  15.647  1.00 37.65           C  
ATOM   2008  CD2 PHE A 937      30.691  25.959  14.554  1.00 37.13           C  
ATOM   2009  CE1 PHE A 937      28.716  24.037  14.883  1.00 36.77           C  
ATOM   2010  CE2 PHE A 937      29.539  26.010  13.784  1.00 35.86           C  
ATOM   2011  CZ  PHE A 937      28.552  25.049  13.949  1.00 35.87           C  
ATOM   2012  N   ARG A 938      34.063  25.406  18.832  1.00 46.38           N  
ATOM   2013  CA  ARG A 938      35.214  25.098  19.670  1.00 46.89           C  
ATOM   2014  C   ARG A 938      34.808  24.697  21.091  1.00 46.04           C  
ATOM   2015  O   ARG A 938      35.315  23.709  21.617  1.00 43.81           O  
ATOM   2016  CB  ARG A 938      36.159  26.299  19.706  1.00 51.38           C  
ATOM   2017  CG  ARG A 938      37.582  25.958  20.097  1.00 55.22           C  
ATOM   2018  CD  ARG A 938      38.341  25.301  18.956  1.00 64.59           C  
ATOM   2019  NE  ARG A 938      39.478  24.516  19.437  1.00 76.14           N  
ATOM   2020  CZ  ARG A 938      39.427  23.221  19.754  1.00 75.26           C  
ATOM   2021  NH1 ARG A 938      38.291  22.543  19.651  1.00 77.40           N  
ATOM   2022  NH2 ARG A 938      40.517  22.597  20.181  1.00 89.24           N  
ATOM   2023  N   GLU A 939      33.887  25.457  21.693  1.00 46.42           N  
ATOM   2024  CA  GLU A 939      33.390  25.175  23.045  1.00 45.99           C  
ATOM   2025  C   GLU A 939      32.465  23.965  23.045  1.00 44.93           C  
ATOM   2026  O   GLU A 939      32.491  23.156  23.979  1.00 47.10           O  
ATOM   2027  CB  GLU A 939      32.628  26.362  23.630  1.00 49.30           C  
ATOM   2028  CG  GLU A 939      33.148  27.744  23.270  1.00 56.13           C  
ATOM   2029  CD  GLU A 939      32.167  28.843  23.664  1.00 61.30           C  
ATOM   2030  OE1 GLU A 939      31.943  29.035  24.880  1.00 66.05           O  
ATOM   2031  OE2 GLU A 939      31.613  29.516  22.763  1.00 60.22           O  
ATOM   2032  N   LEU A 940      31.649  23.849  21.998  1.00 42.68           N  
ATOM   2033  CA  LEU A 940      30.687  22.750  21.865  1.00 40.70           C  
ATOM   2034  C   LEU A 940      31.348  21.369  21.834  1.00 40.85           C  
ATOM   2035  O   LEU A 940      30.746  20.389  22.281  1.00 39.76           O  
ATOM   2036  CB  LEU A 940      29.795  22.949  20.631  1.00 39.33           C  
ATOM   2037  CG  LEU A 940      28.774  24.098  20.652  1.00 37.81           C  
ATOM   2038  CD1 LEU A 940      28.159  24.303  19.281  1.00 36.21           C  
ATOM   2039  CD2 LEU A 940      27.680  23.849  21.674  1.00 37.91           C  
ATOM   2040  N   ILE A 941      32.578  21.299  21.312  1.00 40.16           N  
ATOM   2041  CA  ILE A 941      33.367  20.060  21.323  1.00 39.09           C  
ATOM   2042  C   ILE A 941      33.689  19.667  22.759  1.00 39.91           C  
ATOM   2043  O   ILE A 941      33.505  18.513  23.146  1.00 41.29           O  
ATOM   2044  CB  ILE A 941      34.682  20.179  20.513  1.00 39.29           C  
ATOM   2045  CG1 ILE A 941      34.391  20.442  19.031  1.00 38.24           C  
ATOM   2046  CG2 ILE A 941      35.530  18.914  20.662  1.00 38.26           C  
ATOM   2047  CD1 ILE A 941      35.589  20.915  18.228  1.00 37.86           C  
ATOM   2048  N   ILE A 942      34.157  20.633  23.545  1.00 39.90           N  
ATOM   2049  CA  ILE A 942      34.474  20.401  24.955  1.00 39.88           C  
ATOM   2050  C   ILE A 942      33.243  20.010  25.767  1.00 38.62           C  
ATOM   2051  O   ILE A 942      33.306  19.081  26.573  1.00 36.98           O  
ATOM   2052  CB  ILE A 942      35.154  21.632  25.591  1.00 40.81           C  
ATOM   2053  CG1 ILE A 942      36.623  21.691  25.176  1.00 42.32           C  
ATOM   2054  CG2 ILE A 942      35.051  21.592  27.109  1.00 40.56           C  
ATOM   2055  CD1 ILE A 942      37.366  22.887  25.731  1.00 44.29           C  
ATOM   2056  N   GLU A 943      32.133  20.721  25.549  1.00 37.90           N  
ATOM   2057  CA  GLU A 943      30.903  20.472  26.296  1.00 37.94           C  
ATOM   2058  C   GLU A 943      30.309  19.097  25.962  1.00 39.17           C  
ATOM   2059  O   GLU A 943      29.934  18.341  26.864  1.00 39.71           O  
ATOM   2060  CB  GLU A 943      29.880  21.591  26.075  1.00 36.34           C  
ATOM   2061  N   PHE A 944      30.252  18.763  24.675  1.00 39.27           N  
ATOM   2062  CA  PHE A 944      29.721  17.471  24.260  1.00 40.28           C  
ATOM   2063  C   PHE A 944      30.658  16.303  24.577  1.00 41.11           C  
ATOM   2064  O   PHE A 944      30.180  15.205  24.888  1.00 42.55           O  
ATOM   2065  CB  PHE A 944      29.307  17.477  22.783  1.00 41.93           C  
ATOM   2066  CG  PHE A 944      27.925  18.033  22.540  1.00 43.80           C  
ATOM   2067  CD1 PHE A 944      26.791  17.311  22.912  1.00 44.60           C  
ATOM   2068  CD2 PHE A 944      27.754  19.274  21.933  1.00 44.12           C  
ATOM   2069  CE1 PHE A 944      25.519  17.822  22.687  1.00 45.15           C  
ATOM   2070  CE2 PHE A 944      26.489  19.788  21.705  1.00 43.55           C  
ATOM   2071  CZ  PHE A 944      25.369  19.062  22.085  1.00 44.97           C  
ATOM   2072  N   SER A 945      31.974  16.536  24.509  1.00 39.95           N  
ATOM   2073  CA  SER A 945      32.970  15.529  24.913  1.00 39.27           C  
ATOM   2074  C   SER A 945      32.815  15.135  26.380  1.00 40.47           C  
ATOM   2075  O   SER A 945      32.868  13.946  26.719  1.00 38.89           O  
ATOM   2076  CB  SER A 945      34.390  16.030  24.675  1.00 38.73           C  
ATOM   2077  OG  SER A 945      34.697  16.050  23.292  1.00 39.31           O  
ATOM   2078  N   LYS A 946      32.616  16.139  27.239  1.00 41.21           N  
ATOM   2079  CA  LYS A 946      32.406  15.915  28.658  1.00 42.62           C  
ATOM   2080  C   LYS A 946      31.214  14.993  28.889  1.00 44.73           C  
ATOM   2081  O   LYS A 946      31.305  14.032  29.660  1.00 46.01           O  
ATOM   2082  CB  LYS A 946      32.221  17.239  29.400  1.00 44.17           C  
ATOM   2083  CG  LYS A 946      31.913  17.065  30.883  1.00 46.49           C  
ATOM   2084  CD  LYS A 946      32.016  18.365  31.667  1.00 48.97           C  
ATOM   2085  CE  LYS A 946      31.645  18.138  33.131  1.00 51.19           C  
ATOM   2086  NZ  LYS A 946      32.075  19.243  34.037  1.00 50.44           N  
ATOM   2087  N   MET A 947      30.111  15.283  28.203  1.00 45.28           N  
ATOM   2088  CA  MET A 947      28.888  14.492  28.312  1.00 45.52           C  
ATOM   2089  C   MET A 947      29.045  13.062  27.805  1.00 45.46           C  
ATOM   2090  O   MET A 947      28.504  12.132  28.403  1.00 46.09           O  
ATOM   2091  CB  MET A 947      27.740  15.182  27.578  1.00 46.79           C  
ATOM   2092  CG  MET A 947      27.207  16.399  28.305  1.00 48.18           C  
ATOM   2093  SD  MET A 947      26.207  17.471  27.261  1.00 50.70           S  
ATOM   2094  CE  MET A 947      25.516  18.541  28.523  1.00 50.28           C  
ATOM   2095  N   ALA A 948      29.789  12.897  26.710  1.00 45.33           N  
ATOM   2096  CA  ALA A 948      30.018  11.587  26.088  1.00 45.82           C  
ATOM   2097  C   ALA A 948      30.875  10.622  26.926  1.00 47.31           C  
ATOM   2098  O   ALA A 948      30.944   9.432  26.618  1.00 46.97           O  
ATOM   2099  CB  ALA A 948      30.623  11.766  24.704  1.00 45.98           C  
ATOM   2100  N   ARG A 949      31.524  11.136  27.970  1.00 48.47           N  
ATOM   2101  CA  ARG A 949      32.303  10.310  28.892  1.00 50.14           C  
ATOM   2102  C   ARG A 949      31.426   9.734  30.004  1.00 53.63           C  
ATOM   2103  O   ARG A 949      31.818   8.775  30.675  1.00 56.48           O  
ATOM   2104  CB  ARG A 949      33.485  11.095  29.475  1.00 49.31           C  
ATOM   2105  CG  ARG A 949      34.497  11.544  28.427  1.00 49.54           C  
ATOM   2106  CD  ARG A 949      35.753  12.132  29.048  1.00 49.48           C  
ATOM   2107  NE  ARG A 949      35.515  13.428  29.689  1.00 50.07           N  
ATOM   2108  CZ  ARG A 949      35.737  14.613  29.121  1.00 48.62           C  
ATOM   2109  NH1 ARG A 949      36.203  14.691  27.879  1.00 48.86           N  
ATOM   2110  NH2 ARG A 949      35.489  15.729  29.798  1.00 45.66           N  
ATOM   2111  N   ASP A 950      30.246  10.325  30.199  1.00 54.98           N  
ATOM   2112  CA  ASP A 950      29.226   9.765  31.094  1.00 55.36           C  
ATOM   2113  C   ASP A 950      27.832   9.841  30.444  1.00 54.29           C  
ATOM   2114  O   ASP A 950      26.955  10.568  30.919  1.00 54.08           O  
ATOM   2115  CB  ASP A 950      29.246  10.456  32.467  1.00 57.10           C  
ATOM   2116  CG  ASP A 950      28.540   9.636  33.553  1.00 59.33           C  
ATOM   2117  OD1 ASP A 950      28.196   8.460  33.294  1.00 59.32           O  
ATOM   2118  OD2 ASP A 950      28.328  10.166  34.669  1.00 59.48           O  
ATOM   2119  N   PRO A 951      27.623   9.064  29.364  1.00 52.54           N  
ATOM   2120  CA  PRO A 951      26.455   9.208  28.485  1.00 52.38           C  
ATOM   2121  C   PRO A 951      25.092   9.018  29.165  1.00 52.17           C  
ATOM   2122  O   PRO A 951      24.158   9.761  28.874  1.00 51.06           O  
ATOM   2123  CB  PRO A 951      26.675   8.122  27.420  1.00 51.35           C  
ATOM   2124  CG  PRO A 951      28.094   7.692  27.566  1.00 51.59           C  
ATOM   2125  CD  PRO A 951      28.420   7.879  29.010  1.00 51.08           C  
ATOM   2126  N   GLN A 952      24.991   8.037  30.059  1.00 54.42           N  
ATOM   2127  CA  GLN A 952      23.725   7.678  30.710  1.00 55.89           C  
ATOM   2128  C   GLN A 952      23.176   8.840  31.534  1.00 54.27           C  
ATOM   2129  O   GLN A 952      21.966   9.054  31.598  1.00 53.25           O  
ATOM   2130  CB  GLN A 952      23.911   6.458  31.622  1.00 58.90           C  
ATOM   2131  CG  GLN A 952      25.025   5.503  31.213  1.00 63.56           C  
ATOM   2132  CD  GLN A 952      24.677   4.666  29.995  1.00 67.20           C  
ATOM   2133  OE1 GLN A 952      23.669   3.955  29.980  1.00 69.32           O  
ATOM   2134  NE2 GLN A 952      25.522   4.735  28.969  1.00 69.22           N  
ATOM   2135  N   ARG A 953      24.090   9.580  32.153  1.00 54.32           N  
ATOM   2136  CA  ARG A 953      23.778  10.717  33.009  1.00 53.92           C  
ATOM   2137  C   ARG A 953      23.077  11.843  32.239  1.00 53.61           C  
ATOM   2138  O   ARG A 953      22.244  12.559  32.800  1.00 53.84           O  
ATOM   2139  CB  ARG A 953      25.079  11.215  33.645  1.00 56.02           C  
ATOM   2140  CG  ARG A 953      24.956  12.323  34.674  1.00 60.31           C  
ATOM   2141  CD  ARG A 953      26.344  12.784  35.095  1.00 64.25           C  
ATOM   2142  NE  ARG A 953      26.379  14.203  35.446  1.00 68.93           N  
ATOM   2143  CZ  ARG A 953      26.657  14.680  36.657  1.00 70.48           C  
ATOM   2144  NH1 ARG A 953      26.657  15.992  36.865  1.00 69.63           N  
ATOM   2145  NH2 ARG A 953      26.941  13.853  37.657  1.00 72.42           N  
ATOM   2146  N   TYR A 954      23.396  11.973  30.952  1.00 51.94           N  
ATOM   2147  CA  TYR A 954      22.924  13.095  30.138  1.00 49.93           C  
ATOM   2148  C   TYR A 954      21.801  12.727  29.159  1.00 48.87           C  
ATOM   2149  O   TYR A 954      21.096  13.600  28.651  1.00 47.59           O  
ATOM   2150  CB  TYR A 954      24.102  13.747  29.406  1.00 50.18           C  
ATOM   2151  CG  TYR A 954      25.141  14.330  30.336  1.00 51.63           C  
ATOM   2152  CD1 TYR A 954      24.936  15.562  30.960  1.00 52.81           C  
ATOM   2153  CD2 TYR A 954      26.330  13.649  30.601  1.00 51.99           C  
ATOM   2154  CE1 TYR A 954      25.887  16.101  31.819  1.00 52.83           C  
ATOM   2155  CE2 TYR A 954      27.288  14.178  31.457  1.00 52.24           C  
ATOM   2156  CZ  TYR A 954      27.064  15.405  32.063  1.00 53.20           C  
ATOM   2157  OH  TYR A 954      28.016  15.938  32.913  1.00 53.27           O  
ATOM   2158  N   LEU A 955      21.632  11.437  28.901  1.00 48.42           N  
ATOM   2159  CA  LEU A 955      20.554  10.966  28.040  1.00 48.28           C  
ATOM   2160  C   LEU A 955      19.883   9.736  28.642  1.00 49.42           C  
ATOM   2161  O   LEU A 955      20.557   8.789  29.049  1.00 47.47           O  
ATOM   2162  CB  LEU A 955      21.072  10.665  26.629  1.00 47.51           C  
ATOM   2163  CG  LEU A 955      21.626  11.805  25.760  1.00 47.20           C  
ATOM   2164  CD1 LEU A 955      22.241  11.240  24.489  1.00 45.16           C  
ATOM   2165  CD2 LEU A 955      20.568  12.849  25.419  1.00 46.99           C  
ATOM   2166  N   VAL A 956      18.553   9.764  28.704  1.00 52.58           N  
ATOM   2167  CA  VAL A 956      17.785   8.665  29.297  1.00 55.08           C  
ATOM   2168  C   VAL A 956      17.018   7.852  28.248  1.00 56.33           C  
ATOM   2169  O   VAL A 956      15.914   8.218  27.832  1.00 55.85           O  
ATOM   2170  CB  VAL A 956      16.865   9.145  30.446  1.00 55.96           C  
ATOM   2171  CG1 VAL A 956      17.689   9.429  31.694  1.00 57.19           C  
ATOM   2172  CG2 VAL A 956      16.070  10.381  30.041  1.00 58.09           C  
ATOM   2173  N   ILE A 957      17.633   6.748  27.826  1.00 58.50           N  
ATOM   2174  CA  ILE A 957      17.068   5.854  26.812  1.00 61.26           C  
ATOM   2175  C   ILE A 957      16.756   4.483  27.423  1.00 66.24           C  
ATOM   2176  O   ILE A 957      17.598   3.892  28.103  1.00 66.97           O  
ATOM   2177  CB  ILE A 957      18.015   5.722  25.595  1.00 60.03           C  
ATOM   2178  CG1 ILE A 957      18.175   7.080  24.900  1.00 59.23           C  
ATOM   2179  CG2 ILE A 957      17.509   4.673  24.610  1.00 60.62           C  
ATOM   2180  CD1 ILE A 957      19.459   7.243  24.114  1.00 58.66           C  
ATOM   2181  N   GLN A 958      15.541   3.991  27.186  1.00 70.74           N  
ATOM   2182  CA  GLN A 958      15.093   2.719  27.759  1.00 75.23           C  
ATOM   2183  C   GLN A 958      15.709   1.507  27.052  1.00 76.81           C  
ATOM   2184  O   GLN A 958      15.606   1.365  25.832  1.00 78.37           O  
ATOM   2185  CB  GLN A 958      13.561   2.642  27.774  1.00 76.49           C  
ATOM   2186  CG  GLN A 958      12.923   3.531  28.837  1.00 80.50           C  
ATOM   2187  CD  GLN A 958      11.434   3.759  28.629  1.00 81.30           C  
ATOM   2188  OE1 GLN A 958      10.993   4.136  27.541  1.00 81.15           O  
ATOM   2189  NE2 GLN A 958      10.653   3.548  29.684  1.00 79.70           N  
ATOM   2190  N   GLY A 959      16.359   0.645  27.832  1.00 78.79           N  
ATOM   2191  CA  GLY A 959      17.003  -0.561  27.309  1.00 82.56           C  
ATOM   2192  C   GLY A 959      18.451  -0.352  26.903  1.00 85.72           C  
ATOM   2193  O   GLY A 959      18.949  -1.021  25.993  1.00 85.83           O  
ATOM   2194  N   ASP A 960      19.123   0.579  27.581  1.00 86.73           N  
ATOM   2195  CA  ASP A 960      20.518   0.916  27.303  1.00 86.72           C  
ATOM   2196  C   ASP A 960      21.219   1.363  28.583  1.00 85.81           C  
ATOM   2197  O   ASP A 960      21.742   0.540  29.334  1.00 86.00           O  
ATOM   2198  CB  ASP A 960      20.602   2.023  26.243  1.00 89.97           C  
ATOM   2199  CG  ASP A 960      22.040   2.361  25.848  1.00 91.82           C  
ATOM   2200  OD1 ASP A 960      22.725   1.495  25.258  1.00 90.67           O  
ATOM   2201  OD2 ASP A 960      22.477   3.504  26.112  1.00 90.58           O  
TER    2202      ASP A 960                                                      
HETATM 2203  C1  AQ4 A1001      28.817  13.925  -4.697  1.00 48.08           C  
HETATM 2204  C2  AQ4 A1001      28.030  13.958  -3.776  1.00 47.53           C  
HETATM 2205  C3  AQ4 A1001      27.044  14.033  -2.619  1.00 45.89           C  
HETATM 2206  C4  AQ4 A1001      26.549  12.865  -2.088  1.00 45.21           C  
HETATM 2207  C5  AQ4 A1001      25.643  12.898  -1.014  1.00 44.12           C  
HETATM 2208  N1  AQ4 A1001      25.105  11.629  -0.449  1.00 43.99           N  
HETATM 2209  C6  AQ4 A1001      25.967  10.424  -0.284  1.00 43.34           C  
HETATM 2210  C7  AQ4 A1001      25.404   9.137   0.050  1.00 43.78           C  
HETATM 2211  C8  AQ4 A1001      24.033   8.934   0.232  1.00 44.05           C  
HETATM 2212  C9  AQ4 A1001      23.564   7.659   0.552  1.00 45.82           C  
HETATM 2213  O1  AQ4 A1001      22.216   7.435   0.736  1.00 48.33           O  
HETATM 2214  C10 AQ4 A1001      21.271   8.435   0.576  1.00 50.85           C  
HETATM 2215  C11 AQ4 A1001      20.229   8.360   1.696  1.00 53.18           C  
HETATM 2216  O2  AQ4 A1001      19.997   7.009   2.075  1.00 55.72           O  
HETATM 2217  C12 AQ4 A1001      20.045   6.645   3.424  1.00 54.57           C  
HETATM 2218  C13 AQ4 A1001      24.438   6.592   0.687  1.00 45.78           C  
HETATM 2219  O3  AQ4 A1001      23.900   5.328   1.021  1.00 48.16           O  
HETATM 2220  C14 AQ4 A1001      24.516   4.122   0.731  1.00 50.62           C  
HETATM 2221  C15 AQ4 A1001      23.602   2.988   1.208  1.00 53.90           C  
HETATM 2222  O4  AQ4 A1001      23.232   3.205   2.541  1.00 57.36           O  
HETATM 2223  C16 AQ4 A1001      21.862   3.277   2.890  1.00 56.68           C  
HETATM 2224  C17 AQ4 A1001      25.825   6.767   0.515  1.00 44.07           C  
HETATM 2225  C18 AQ4 A1001      26.314   8.035   0.196  1.00 43.69           C  
HETATM 2226  N2  AQ4 A1001      27.664   8.247   0.012  1.00 43.42           N  
HETATM 2227  C19 AQ4 A1001      28.136   9.461  -0.290  1.00 42.58           C  
HETATM 2228  N3  AQ4 A1001      27.338  10.510  -0.440  1.00 43.25           N  
HETATM 2229  C20 AQ4 A1001      25.232  14.145  -0.483  1.00 43.73           C  
HETATM 2230  C21 AQ4 A1001      25.732  15.314  -1.018  1.00 44.92           C  
HETATM 2231  C22 AQ4 A1001      26.632  15.287  -2.080  1.00 45.24           C  
HETATM 2232  O   HOH A1101      14.501  26.271  17.651  1.00 37.01           O  
HETATM 2233  O   HOH A1102      23.823  24.304 -15.123  1.00 33.58           O  
HETATM 2234  O   HOH A1103      38.254  16.049   4.197  1.00 33.16           O  
HETATM 2235  O   HOH A1104      29.037  12.845  -0.205  1.00 42.31           O  
HETATM 2236  O   HOH A1105      31.418  29.123  16.002  1.00 35.86           O  
HETATM 2237  O   HOH A1106      14.972  27.007  13.561  1.00 31.13           O  
HETATM 2238  O   HOH A1107      28.560  17.291 -16.044  1.00 35.75           O  
HETATM 2239  O   HOH A1108      25.113  29.550   7.948  1.00 40.02           O  
HETATM 2240  O   HOH A1109      17.568  17.145   7.876  1.00 48.01           O  
HETATM 2241  O   HOH A1110      31.051  18.273   2.498  1.00 44.80           O  
HETATM 2242  O   HOH A1111      13.285  28.351  25.515  1.00 41.89           O  
HETATM 2243  O   HOH A1112      27.418  24.204 -15.499  1.00 46.93           O  
HETATM 2244  O   HOH A1113      35.544  17.614  27.723  1.00 33.19           O  
HETATM 2245  O   HOH A1114      23.789  23.041  29.687  1.00 50.09           O  
HETATM 2246  O   HOH A1115      31.351  27.251  10.339  1.00 47.20           O  
HETATM 2247  O   HOH A1116      38.142  21.141  14.475  1.00 42.95           O  
HETATM 2248  O   HOH A1117      13.965   5.989  25.891  1.00 52.39           O  
HETATM 2249  O   HOH A1118      32.335  29.546   2.425  1.00 31.93           O  
HETATM 2250  O   HOH A1119      28.351   9.468 -17.286  1.00 51.70           O  
HETATM 2251  O   HOH A1120      15.440  17.657  -9.097  1.00 58.70           O  
HETATM 2252  O   HOH A1121      38.842  -2.221  -8.861  1.00 49.16           O  
HETATM 2253  O   HOH A1122      13.096   7.708  27.580  1.00 50.33           O  
HETATM 2254  O   HOH A1123      34.707  17.938 -16.979  1.00 44.62           O  
HETATM 2255  O   HOH A1124      10.594  21.876  26.147  1.00 44.79           O  
HETATM 2256  O   HOH A1125       9.161  18.739  25.381  1.00 39.04           O  
HETATM 2257  O   HOH A1126      20.457   5.281 -12.615  1.00 46.65           O  
HETATM 2258  O   HOH A1127      33.060  19.326  -0.125  1.00 48.97           O  
HETATM 2259  O   HOH A1128       8.264  19.947  16.094  1.00 39.44           O  
HETATM 2260  O   HOH A1129      33.235  10.810  19.406  1.00 40.77           O  
HETATM 2261  O   HOH A1130       8.093  14.157  12.690  1.00 50.63           O  
HETATM 2262  O   HOH A1131      38.470  28.674 -12.504  1.00 47.08           O  
HETATM 2263  O   HOH A1132      24.033  22.252 -13.237  1.00 39.07           O  
HETATM 2264  O   HOH A1133      14.480  28.331  11.493  1.00 37.70           O  
HETATM 2265  O   HOH A1134      31.445  10.877   0.766  1.00 54.44           O  
CONECT 2203 2204                                                                
CONECT 2204 2203 2205                                                           
CONECT 2205 2204 2206 2231                                                      
CONECT 2206 2205 2207                                                           
CONECT 2207 2206 2208 2229                                                      
CONECT 2208 2207 2209                                                           
CONECT 2209 2208 2210 2228                                                      
CONECT 2210 2209 2211 2225                                                      
CONECT 2211 2210 2212                                                           
CONECT 2212 2211 2213 2218                                                      
CONECT 2213 2212 2214                                                           
CONECT 2214 2213 2215                                                           
CONECT 2215 2214 2216                                                           
CONECT 2216 2215 2217                                                           
CONECT 2217 2216                                                                
CONECT 2218 2212 2219 2224                                                      
CONECT 2219 2218 2220                                                           
CONECT 2220 2219 2221                                                           
CONECT 2221 2220 2222                                                           
CONECT 2222 2221 2223                                                           
CONECT 2223 2222                                                                
CONECT 2224 2218 2225                                                           
CONECT 2225 2210 2224 2226                                                      
CONECT 2226 2225 2227                                                           
CONECT 2227 2226 2228                                                           
CONECT 2228 2209 2227                                                           
CONECT 2229 2207 2230                                                           
CONECT 2230 2229 2231                                                           
CONECT 2231 2205 2230                                                           
MASTER      352    0    1   15    9    0    4    6 2264    1   29   26          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.