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***  OXIDOREDUCTASE 03-JUL-97 1AOG  ***

elNémo ID: 22011404374435814

Job options:

ID        	=	 22011404374435814
JOBID     	=	 OXIDOREDUCTASE 03-JUL-97 1AOG
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    OXIDOREDUCTASE                          03-JUL-97   1AOG              
TITLE     TRYPANOSOMA CRUZI TRYPANOTHIONE REDUCTASE (OXIDIZED FORM)             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPANOTHIONE REDUCTASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.6.4.8                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI;                              
SOURCE   3 ORGANISM_TAXID: 5693;                                                
SOURCE   4 STRAIN: BRAZILIAN SILVIO STRAIN CLONE X10/1                          
KEYWDS    TRYPANOTHIONE REDUCTASE, FAD DEPENDENT DISULPHIDE                     
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.S.BOND,Y.ZHANG,W.N.HUNTER                                           
REVDAT   3   24-FEB-09 1AOG    1       VERSN                                    
REVDAT   2   01-APR-03 1AOG    1       JRNL                                     
REVDAT   1   17-SEP-97 1AOG    0                                                
JRNL        AUTH   Y.ZHANG,C.S.BOND,S.BAILEY,M.L.CUNNINGHAM,                    
JRNL        AUTH 2 A.H.FAIRLAMB,W.N.HUNTER                                      
JRNL        TITL   THE CRYSTAL STRUCTURE OF TRYPANOTHIONE REDUCTASE             
JRNL        TITL 2 FROM THE HUMAN PATHOGEN TRYPANOSOMA CRUZI AT 2.3 A           
JRNL        TITL 3 RESOLUTION.                                                  
JRNL        REF    PROTEIN SCI.                  V.   5    52 1996              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   8771196                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.BORGES,M.L.CUNNINGHAM,J.TOVAR,A.H.FAIRLAMB                 
REMARK   1  TITL   SITE-DIRECTED MUTAGENESIS OF THE REDOX-ACTIVE                
REMARK   1  TITL 2 CYSTEINES OF TRYPANOSOMA CRUZI TRYPANOTHIONE                 
REMARK   1  TITL 3 REDUCTASE                                                    
REMARK   1  REF    EUR.J.BIOCHEM.                V. 228   745 1995              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.ZHANG,S.BAILEY,J.H.NAISMITH,C.S.BOND,J.HABASH,             
REMARK   1  AUTH 2 P.MCLAUGHLIN,M.Z.PAPIZ,A.BORGES,M.L.CUNNINGHAM,              
REMARK   1  AUTH 3 A.H.FAIRLAMB,W.N.HUNTER                                      
REMARK   1  TITL   TRYPANOSOMA CRUZI TRYPANOTHIONE REDUCTASE                    
REMARK   1  TITL 2 CRYSTALLISATION, UNIT CELL DIMENSIONS AND                    
REMARK   1  TITL 3 STRUCTURE SOLUTION                                           
REMARK   1  REF    J.MOL.BIOL.                   V. 233  1217 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 53868                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7451                                    
REMARK   3   NUCLEIC ACID ATOMS       : NULL                                    
REMARK   3   HETEROGEN ATOMS          : 122                                     
REMARK   3   SOLVENT ATOMS            : 419                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.40                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1AOG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : MAR-91                             
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 7                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55392                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.10900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: PDB ENTRY 1TYT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
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       78.34500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      117.51750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       39.17250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     SER B     3                                                      
REMARK 465     LYS B     4                                                      
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     PRO A 487    O                                                   
REMARK 470     PRO B 487    O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A  41   NE2   HIS A  41   CD2    -0.069                       
REMARK 500    HIS A 156   NE2   HIS A 156   CD2    -0.068                       
REMARK 500    HIS A 166   NE2   HIS A 166   CD2    -0.084                       
REMARK 500    ASP A 215   CA    ASP A 215   CB      0.196                       
REMARK 500    HIS A 233   NE2   HIS A 233   CD2    -0.068                       
REMARK 500    HIS A 359   NE2   HIS A 359   CD2    -0.068                       
REMARK 500    HIS A 461   NE2   HIS A 461   CD2    -0.069                       
REMARK 500    HIS B  41   NE2   HIS B  41   CD2    -0.071                       
REMARK 500    HIS B 156   NE2   HIS B 156   CD2    -0.069                       
REMARK 500    HIS B 166   NE2   HIS B 166   CD2    -0.075                       
REMARK 500    HIS B 175   NE2   HIS B 175   CD2    -0.073                       
REMARK 500    HIS B 233   NE2   HIS B 233   CD2    -0.067                       
REMARK 500    HIS B 359   NE2   HIS B 359   CD2    -0.074                       
REMARK 500    HIS B 419   NE2   HIS B 419   CD2    -0.074                       
REMARK 500    HIS B 428   NE2   HIS B 428   CD2    -0.068                       
REMARK 500    HIS B 461   NE2   HIS B 461   CD2    -0.073                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS A   4   N   -  CA  -  C   ANGL. DEV. =  17.6 DEGREES          
REMARK 500    LYS A   4   CA  -  C   -  N   ANGL. DEV. = -21.6 DEGREES          
REMARK 500    LYS A   4   O   -  C   -  N   ANGL. DEV. =  10.0 DEGREES          
REMARK 500    TRP A  22   CD1 -  CG  -  CD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    TRP A  22   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    TRP A  82   CD1 -  CG  -  CD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    TRP A  82   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG A  90   CA  -  CB  -  CG  ANGL. DEV. =  13.6 DEGREES          
REMARK 500    TRP A  93   CD1 -  CG  -  CD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    TRP A  93   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    TRP A 127   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    TRP A 127   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    TRP A 164   CD1 -  CG  -  CD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    TRP A 164   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP A 215   CB  -  CA  -  C   ANGL. DEV. =  15.9 DEGREES          
REMARK 500    ASP A 215   CB  -  CG  -  OD1 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ASP A 215   C   -  N   -  CA  ANGL. DEV. = -17.6 DEGREES          
REMARK 500    ASP A 215   CA  -  C   -  N   ANGL. DEV. = -13.8 DEGREES          
REMARK 500    LEU A 220   CA  -  CB  -  CG  ANGL. DEV. =  16.5 DEGREES          
REMARK 500    GLU A 225   CB  -  CA  -  C   ANGL. DEV. = -13.0 DEGREES          
REMARK 500    GLU A 225   CA  -  CB  -  CG  ANGL. DEV. =  39.7 DEGREES          
REMARK 500    LYS A 305   CA  -  CB  -  CG  ANGL. DEV. =  13.3 DEGREES          
REMARK 500    ARG A 331   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 355   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    HIS A 359   CB  -  CG  -  CD2 ANGL. DEV. = -10.0 DEGREES          
REMARK 500    LYS A 480   CG  -  CD  -  CE  ANGL. DEV. =  38.4 DEGREES          
REMARK 500    TRP B  22   CD1 -  CG  -  CD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    TRP B  22   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG B  31   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG B  31   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ARG B  75   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    TRP B  82   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    TRP B  82   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG B  90   CA  -  CB  -  CG  ANGL. DEV. =  13.2 DEGREES          
REMARK 500    TRP B  93   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    TRP B  93   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    TRP B 127   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    TRP B 127   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    TRP B 164   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    TRP B 164   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    TYR B 222   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG B 229   CG  -  CD  -  NE  ANGL. DEV. = -13.7 DEGREES          
REMARK 500    ARG B 229   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    GLN B 249   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    LEU B 261   CA  -  CB  -  CG  ANGL. DEV. =  14.9 DEGREES          
REMARK 500    ARG B 291   CB  -  CG  -  CD  ANGL. DEV. = -16.4 DEGREES          
REMARK 500    ARG B 291   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    TYR B 392   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A   4      114.99     70.05                                   
REMARK 500    ILE A   5      -70.26     -7.13                                   
REMARK 500    ALA A  13       58.33   -100.45                                   
REMARK 500    PHE A  46      -60.77     65.81                                   
REMARK 500    ALA A  48     -167.06   -165.83                                   
REMARK 500    VAL A  56       46.06   -144.36                                   
REMARK 500    LYS A 214      -71.88    -41.93                                   
REMARK 500    ASP A 215       67.18   -114.64                                   
REMARK 500    ALA A 285       57.54   -141.42                                   
REMARK 500    ASN A 306       60.89     34.45                                   
REMARK 500    ARG A 331      -91.35    -86.16                                   
REMARK 500    ALA B  13       57.84   -104.82                                   
REMARK 500    LYS B  29       29.11     41.62                                   
REMARK 500    PHE B  46      -63.20     66.62                                   
REMARK 500    PRO B 144       21.26    -65.55                                   
REMARK 500    ALA B 160       45.87   -147.27                                   
REMARK 500    PRO B 213      174.87    -58.07                                   
REMARK 500    LYS B 305     -103.88   -120.07                                   
REMARK 500    GLU B 313       -9.50    -59.31                                   
REMARK 500    THR B 317     -142.35    -89.59                                   
REMARK 500    ARG B 331      -87.03   -100.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ASN B 299         0.08    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ASP A 215        -12.97                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 618        DISTANCE =  5.46 ANGSTROMS                       
REMARK 525    HOH B 649        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH B 653        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH A 723        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH A 725        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH A 726        DISTANCE =  6.20 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 492                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAE A 500                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAE A 501                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 492                 
DBREF  1AOG A    3   487  UNP    P28593   TYTR_TRYCR       3    487             
DBREF  1AOG B    3   487  UNP    P28593   TYTR_TRYCR       3    487             
SEQRES   1 A  485  SER LYS ILE PHE ASP LEU VAL VAL ILE GLY ALA GLY SER          
SEQRES   2 A  485  GLY GLY LEU GLU ALA ALA TRP ASN ALA ALA THR LEU TYR          
SEQRES   3 A  485  LYS LYS ARG VAL ALA VAL ILE ASP VAL GLN MET VAL HIS          
SEQRES   4 A  485  GLY PRO PRO PHE PHE SER ALA LEU GLY GLY THR CYS VAL          
SEQRES   5 A  485  ASN VAL GLY CYS VAL PRO LYS LYS LEU MET VAL THR GLY          
SEQRES   6 A  485  ALA GLN TYR MET GLU HIS LEU ARG GLU SER ALA GLY PHE          
SEQRES   7 A  485  GLY TRP GLU PHE ASP ARG THR THR LEU ARG ALA GLU TRP          
SEQRES   8 A  485  LYS ASN LEU ILE ALA VAL LYS ASP GLU ALA VAL LEU ASN          
SEQRES   9 A  485  ILE ASN LYS SER TYR ASP GLU MET PHE ARG ASP THR GLU          
SEQRES  10 A  485  GLY LEU GLU PHE PHE LEU GLY TRP GLY SER LEU GLU SER          
SEQRES  11 A  485  LYS ASN VAL VAL ASN VAL ARG GLU SER ALA ASP PRO ALA          
SEQRES  12 A  485  SER ALA VAL LYS GLU ARG LEU GLU THR GLU HIS ILE LEU          
SEQRES  13 A  485  LEU ALA SER GLY SER TRP PRO HIS MET PRO ASN ILE PRO          
SEQRES  14 A  485  GLY ILE GLU HIS CYS ILE SER SER ASN GLU ALA PHE TYR          
SEQRES  15 A  485  LEU PRO GLU PRO PRO ARG ARG VAL LEU THR VAL GLY GLY          
SEQRES  16 A  485  GLY PHE ILE SER VAL GLU PHE ALA GLY ILE PHE ASN ALA          
SEQRES  17 A  485  TYR LYS PRO LYS ASP GLY GLN VAL THR LEU CYS TYR ARG          
SEQRES  18 A  485  GLY GLU MET ILE LEU ARG GLY PHE ASP HIS THR LEU ARG          
SEQRES  19 A  485  GLU GLU LEU THR LYS GLN LEU THR ALA ASN GLY ILE GLN          
SEQRES  20 A  485  ILE LEU THR LYS GLU ASN PRO ALA LYS VAL GLU LEU ASN          
SEQRES  21 A  485  ALA ASP GLY SER LYS SER VAL THR PHE GLU SER GLY LYS          
SEQRES  22 A  485  LYS MET ASP PHE ASP LEU VAL MET MET ALA ILE GLY ARG          
SEQRES  23 A  485  SER PRO ARG THR LYS ASP LEU GLN LEU GLN ASN ALA GLY          
SEQRES  24 A  485  VAL MET ILE LYS ASN GLY GLY VAL GLN VAL ASP GLU TYR          
SEQRES  25 A  485  SER ARG THR ASN VAL SER ASN ILE TYR ALA ILE GLY ASP          
SEQRES  26 A  485  VAL THR ASN ARG VAL MET LEU THR PRO VAL ALA ILE ASN          
SEQRES  27 A  485  GLU ALA ALA ALA LEU VAL ASP THR VAL PHE GLY THR THR          
SEQRES  28 A  485  PRO ARG LYS THR ASP HIS THR ARG VAL ALA SER ALA VAL          
SEQRES  29 A  485  PHE SER ILE PRO PRO ILE GLY THR CYS GLY LEU ILE GLU          
SEQRES  30 A  485  GLU VAL ALA SER LYS ARG TYR GLU VAL VAL ALA VAL TYR          
SEQRES  31 A  485  LEU SER SER PHE THR PRO LEU MET HIS LYS VAL SER GLY          
SEQRES  32 A  485  SER LYS TYR LYS THR PHE VAL ALA LYS ILE ILE THR ASN          
SEQRES  33 A  485  HIS SER ASP GLY THR VAL LEU GLY VAL HIS LEU LEU GLY          
SEQRES  34 A  485  ASP ASN ALA PRO GLU ILE ILE GLN GLY ILE GLY ILE CYS          
SEQRES  35 A  485  LEU LYS LEU ASN ALA LYS ILE SER ASP PHE TYR ASN THR          
SEQRES  36 A  485  ILE GLY VAL HIS PRO THR SER ALA GLU GLU LEU CYS SER          
SEQRES  37 A  485  MET ARG THR PRO SER TYR TYR TYR VAL LYS GLY GLU LYS          
SEQRES  38 A  485  MET GLU LYS PRO                                              
SEQRES   1 B  485  SER LYS ILE PHE ASP LEU VAL VAL ILE GLY ALA GLY SER          
SEQRES   2 B  485  GLY GLY LEU GLU ALA ALA TRP ASN ALA ALA THR LEU TYR          
SEQRES   3 B  485  LYS LYS ARG VAL ALA VAL ILE ASP VAL GLN MET VAL HIS          
SEQRES   4 B  485  GLY PRO PRO PHE PHE SER ALA LEU GLY GLY THR CYS VAL          
SEQRES   5 B  485  ASN VAL GLY CYS VAL PRO LYS LYS LEU MET VAL THR GLY          
SEQRES   6 B  485  ALA GLN TYR MET GLU HIS LEU ARG GLU SER ALA GLY PHE          
SEQRES   7 B  485  GLY TRP GLU PHE ASP ARG THR THR LEU ARG ALA GLU TRP          
SEQRES   8 B  485  LYS ASN LEU ILE ALA VAL LYS ASP GLU ALA VAL LEU ASN          
SEQRES   9 B  485  ILE ASN LYS SER TYR ASP GLU MET PHE ARG ASP THR GLU          
SEQRES  10 B  485  GLY LEU GLU PHE PHE LEU GLY TRP GLY SER LEU GLU SER          
SEQRES  11 B  485  LYS ASN VAL VAL ASN VAL ARG GLU SER ALA ASP PRO ALA          
SEQRES  12 B  485  SER ALA VAL LYS GLU ARG LEU GLU THR GLU HIS ILE LEU          
SEQRES  13 B  485  LEU ALA SER GLY SER TRP PRO HIS MET PRO ASN ILE PRO          
SEQRES  14 B  485  GLY ILE GLU HIS CYS ILE SER SER ASN GLU ALA PHE TYR          
SEQRES  15 B  485  LEU PRO GLU PRO PRO ARG ARG VAL LEU THR VAL GLY GLY          
SEQRES  16 B  485  GLY PHE ILE SER VAL GLU PHE ALA GLY ILE PHE ASN ALA          
SEQRES  17 B  485  TYR LYS PRO LYS ASP GLY GLN VAL THR LEU CYS TYR ARG          
SEQRES  18 B  485  GLY GLU MET ILE LEU ARG GLY PHE ASP HIS THR LEU ARG          
SEQRES  19 B  485  GLU GLU LEU THR LYS GLN LEU THR ALA ASN GLY ILE GLN          
SEQRES  20 B  485  ILE LEU THR LYS GLU ASN PRO ALA LYS VAL GLU LEU ASN          
SEQRES  21 B  485  ALA ASP GLY SER LYS SER VAL THR PHE GLU SER GLY LYS          
SEQRES  22 B  485  LYS MET ASP PHE ASP LEU VAL MET MET ALA ILE GLY ARG          
SEQRES  23 B  485  SER PRO ARG THR LYS ASP LEU GLN LEU GLN ASN ALA GLY          
SEQRES  24 B  485  VAL MET ILE LYS ASN GLY GLY VAL GLN VAL ASP GLU TYR          
SEQRES  25 B  485  SER ARG THR ASN VAL SER ASN ILE TYR ALA ILE GLY ASP          
SEQRES  26 B  485  VAL THR ASN ARG VAL MET LEU THR PRO VAL ALA ILE ASN          
SEQRES  27 B  485  GLU ALA ALA ALA LEU VAL ASP THR VAL PHE GLY THR THR          
SEQRES  28 B  485  PRO ARG LYS THR ASP HIS THR ARG VAL ALA SER ALA VAL          
SEQRES  29 B  485  PHE SER ILE PRO PRO ILE GLY THR CYS GLY LEU ILE GLU          
SEQRES  30 B  485  GLU VAL ALA SER LYS ARG TYR GLU VAL VAL ALA VAL TYR          
SEQRES  31 B  485  LEU SER SER PHE THR PRO LEU MET HIS LYS VAL SER GLY          
SEQRES  32 B  485  SER LYS TYR LYS THR PHE VAL ALA LYS ILE ILE THR ASN          
SEQRES  33 B  485  HIS SER ASP GLY THR VAL LEU GLY VAL HIS LEU LEU GLY          
SEQRES  34 B  485  ASP ASN ALA PRO GLU ILE ILE GLN GLY ILE GLY ILE CYS          
SEQRES  35 B  485  LEU LYS LEU ASN ALA LYS ILE SER ASP PHE TYR ASN THR          
SEQRES  36 B  485  ILE GLY VAL HIS PRO THR SER ALA GLU GLU LEU CYS SER          
SEQRES  37 B  485  MET ARG THR PRO SER TYR TYR TYR VAL LYS GLY GLU LYS          
SEQRES  38 B  485  MET GLU LYS PRO                                              
HET    FAD  A 492      53                                                       
HET    MAE  A 500       8                                                       
HET    MAE  A 501       8                                                       
HET    FAD  B 492      53                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     MAE MALEIC ACID                                                      
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   4  MAE    2(C4 H4 O4)                                                  
FORMUL   7  HOH   *419(H2 O)                                                    
HELIX    1   1 SER A   15  THR A   26  1                                  12    
HELIX    2   2 GLY A   51  VAL A   56  1                                   6    
HELIX    3   3 CYS A   58  PHE A   80  1                                  23    
HELIX    4   4 ARG A   86  THR A   88  5                                   3    
HELIX    5   5 TRP A   93  ASP A  117  1                                  25    
HELIX    6   6 ILE A  173  HIS A  175  5                                   3    
HELIX    7   7 SER A  179  TYR A  184  1                                   6    
HELIX    8   8 PHE A  199  TYR A  211  1                                  13    
HELIX    9   9 HIS A  233  ASN A  246  1                                  14    
HELIX   10  10 LYS A  293  LEU A  295  5                                   3    
HELIX   11  11 LEU A  297  ASN A  299  5                                   3    
HELIX   12  12 GLY A  326  THR A  329  5                                   4    
HELIX   13  13 THR A  335  PHE A  350  1                                  16    
HELIX   14  14 GLU A  379  ARG A  385  1                                   7    
HELIX   15  15 LEU A  399  SER A  404  1                                   6    
HELIX   16  16 ALA A  434  LYS A  446  1                                  13    
HELIX   17  17 ILE A  451  TYR A  455  1                                   5    
HELIX   18  18 ALA A  465  CYS A  469  5                                   5    
HELIX   19  19 SER B   15  LEU B   27  1                                  13    
HELIX   20  20 THR B   52  VAL B   56  1                                   5    
HELIX   21  21 CYS B   58  PHE B   80  1                                  23    
HELIX   22  22 ARG B   86  THR B   88  5                                   3    
HELIX   23  23 TRP B   93  ASP B  117  1                                  25    
HELIX   24  24 ILE B  173  HIS B  175  5                                   3    
HELIX   25  25 SER B  179  TYR B  184  1                                   6    
HELIX   26  26 PHE B  199  TYR B  211  1                                  13    
HELIX   27  27 HIS B  233  ALA B  245  1                                  13    
HELIX   28  28 LYS B  293  LEU B  295  5                                   3    
HELIX   29  29 LEU B  297  ALA B  300  5                                   4    
HELIX   30  30 GLY B  326  THR B  329  5                                   4    
HELIX   31  31 THR B  335  PHE B  350  1                                  16    
HELIX   32  32 GLU B  379  ARG B  385  1                                   7    
HELIX   33  33 LEU B  399  SER B  404  1                                   6    
HELIX   34  34 ALA B  434  LYS B  446  1                                  13    
HELIX   35  35 ILE B  451  TYR B  455  1                                   5    
HELIX   36  36 ALA B  465  CYS B  469  5                                   5    
SHEET    1   A 5 ILE A 322  ALA A 324  0                                        
SHEET    2   A 5 ILE A 157  LEU A 159  1  N  ILE A 157   O  TYR A 323           
SHEET    3   A 5 LEU A   8  ILE A  11  1  N  VAL A   9   O  LEU A 158           
SHEET    4   A 5 VAL A  32  ASP A  36  1  N  ALA A  33   O  LEU A   8           
SHEET    5   A 5 LEU A 121  LEU A 125  1  N  GLU A 122   O  VAL A  32           
SHEET    1   B 2 SER A 163  PRO A 165  0                                        
SHEET    2   B 2 ARG A 288  PRO A 290 -1  N  SER A 289   O  TRP A 164           
SHEET    1   C 4 LEU A 281  MET A 284  0                                        
SHEET    2   C 4 ARG A 191  VAL A 195  1  N  LEU A 193   O  LEU A 281           
SHEET    3   C 4 GLN A 217  TYR A 222  1  N  GLN A 217   O  VAL A 192           
SHEET    4   C 4 GLN A 249  THR A 252  1  N  GLN A 249   O  LEU A 220           
SHEET    1   D 3 LYS A 276  PHE A 279  0                                        
SHEET    2   D 3 LYS A 267  PHE A 271 -1  N  VAL A 269   O  MET A 277           
SHEET    3   D 3 PRO A 256  LEU A 261 -1  N  GLU A 260   O  SER A 268           
SHEET    1   E 7 SER A 364  VAL A 366  0                                        
SHEET    2   E 7 ILE A 372  GLY A 376 -1  N  THR A 374   O  SER A 364           
SHEET    3   E 7 THR A 423  LEU A 430 -1  N  LEU A 429   O  GLY A 373           
SHEET    4   E 7 THR A 410  ASN A 418 -1  N  ASN A 418   O  THR A 423           
SHEET    5   E 7 VAL A 388  THR A 397 -1  N  PHE A 396   O  PHE A 411           
SHEET    6   E 7 TYR A 476  VAL A 479 -1  N  TYR A 478   O  VAL A 389           
SHEET    7   E 7 GLU A 482  MET A 484 -1  N  MET A 484   O  TYR A 477           
SHEET    1   F 3 TRP A 127  SER A 132  0                                        
SHEET    2   F 3 VAL A 135  ARG A 139 -1  N  ARG A 139   O  TRP A 127           
SHEET    3   F 3 VAL A 148  GLU A 153 -1  N  LEU A 152   O  VAL A 136           
SHEET    1   G 5 ILE B 322  ALA B 324  0                                        
SHEET    2   G 5 ILE B 157  LEU B 159  1  N  ILE B 157   O  TYR B 323           
SHEET    3   G 5 LEU B   8  ILE B  11  1  N  VAL B   9   O  LEU B 158           
SHEET    4   G 5 VAL B  32  ASP B  36  1  N  ALA B  33   O  LEU B   8           
SHEET    5   G 5 LEU B 121  LEU B 125  1  N  GLU B 122   O  VAL B  32           
SHEET    1   H 3 GLU B 150  GLU B 153  0                                        
SHEET    2   H 3 VAL B 135  ARG B 139 -1  N  VAL B 138   O  GLU B 150           
SHEET    3   H 3 TRP B 127  SER B 132 -1  N  SER B 132   O  VAL B 135           
SHEET    1   I 2 SER B 163  PRO B 165  0                                        
SHEET    2   I 2 ARG B 288  PRO B 290 -1  N  SER B 289   O  TRP B 164           
SHEET    1   J 4 LEU B 281  MET B 284  0                                        
SHEET    2   J 4 ARG B 191  VAL B 195  1  N  LEU B 193   O  LEU B 281           
SHEET    3   J 4 GLN B 217  TYR B 222  1  N  GLN B 217   O  VAL B 192           
SHEET    4   J 4 ILE B 248  THR B 252  1  N  GLN B 249   O  VAL B 218           
SHEET    1   K 3 LYS B 276  PHE B 279  0                                        
SHEET    2   K 3 LYS B 267  PHE B 271 -1  N  VAL B 269   O  MET B 277           
SHEET    3   K 3 PRO B 256  LEU B 261 -1  N  GLU B 260   O  SER B 268           
SHEET    1   L 7 ALA B 363  VAL B 366  0                                        
SHEET    2   L 7 ILE B 372  GLY B 376 -1  N  THR B 374   O  SER B 364           
SHEET    3   L 7 VAL B 424  LEU B 430 -1  N  LEU B 429   O  GLY B 373           
SHEET    4   L 7 THR B 410  ASN B 418 -1  N  ILE B 416   O  LEU B 425           
SHEET    5   L 7 VAL B 388  THR B 397 -1  N  PHE B 396   O  PHE B 411           
SHEET    6   L 7 TYR B 476  VAL B 479 -1  N  TYR B 478   O  VAL B 389           
SHEET    7   L 7 GLU B 482  MET B 484 -1  N  MET B 484   O  TYR B 477           
SSBOND   1 CYS A   53    CYS A   58                          1555   1555  1.99  
SSBOND   2 CYS B   53    CYS B   58                          1555   1555  2.02  
CISPEP   1 PRO A   43    PRO A   44          0         2.89                     
CISPEP   2 ILE A  369    PRO A  370          0         0.16                     
CISPEP   3 HIS A  461    PRO A  462          0        -5.92                     
CISPEP   4 PRO B   43    PRO B   44          0        15.25                     
CISPEP   5 ILE B  369    PRO B  370          0        -1.86                     
CISPEP   6 HIS B  461    PRO B  462          0        -5.99                     
SITE     1 AC1 37 ILE A  11  GLY A  12  GLY A  14  SER A  15                    
SITE     2 AC1 37 GLY A  16  ASP A  36  VAL A  37  SER A  47                    
SITE     3 AC1 37 ALA A  48  GLY A  51  THR A  52  CYS A  53                    
SITE     4 AC1 37 VAL A  56  CYS A  58  LYS A  61  GLY A 126                    
SITE     5 AC1 37 TRP A 127  GLY A 128  ALA A 160  SER A 161                    
SITE     6 AC1 37 GLY A 162  ARG A 288  ARG A 291  GLY A 326                    
SITE     7 AC1 37 ASP A 327  MET A 333  LEU A 334  THR A 335                    
SITE     8 AC1 37 PRO A 336  HOH A 502  HOH A 506  HOH A 513                    
SITE     9 AC1 37 HOH A 514  HOH A 572  HOH A 659  HIS B 461                    
SITE    10 AC1 37 PRO B 462                                                     
SITE     1 AC2  4 TYR A 222  ARG A 223  ILE A 286  ASN B 169                    
SITE     1 AC3  7 ALA A 257  LYS A 258  THR A 270  PHE A 271                    
SITE     2 AC3  7 GLU A 272  HOH A 735  HIS B 166                               
SITE     1 AC4 36 HIS A 461  HOH A 551  ILE B  11  GLY B  12                    
SITE     2 AC4 36 GLY B  14  SER B  15  GLY B  16  ASP B  36                    
SITE     3 AC4 36 VAL B  37  SER B  47  ALA B  48  GLY B  51                    
SITE     4 AC4 36 THR B  52  CYS B  53  VAL B  56  GLY B  57                    
SITE     5 AC4 36 CYS B  58  LYS B  61  GLY B 126  TRP B 127                    
SITE     6 AC4 36 GLY B 128  ALA B 160  SER B 161  GLY B 162                    
SITE     7 AC4 36 PHE B 199  ARG B 288  ARG B 291  GLY B 326                    
SITE     8 AC4 36 ASP B 327  MET B 333  LEU B 334  THR B 335                    
SITE     9 AC4 36 PRO B 336  HOH B 500  HOH B 504  HOH B 505                    
CRYST1   92.810   92.810  156.690  90.00  90.00  90.00 P 43          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      0.010775  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010775  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006382        0.00000                         
ATOM      1  N   SER A   3      -1.635  31.156 -16.795  1.00 77.00           N  
ATOM      2  CA  SER A   3      -0.423  31.074 -16.009  1.00 78.90           C  
ATOM      3  C   SER A   3       0.240  29.738 -16.290  1.00 78.41           C  
ATOM      4  O   SER A   3       1.219  29.724 -16.960  1.00 79.75           O  
ATOM      5  CB  SER A   3      -0.803  31.254 -14.566  1.00 80.22           C  
ATOM      6  OG  SER A   3      -1.654  32.390 -14.500  1.00 80.97           O  
ATOM      7  N   LYS A   4      -0.297  28.571 -15.982  1.00 75.92           N  
ATOM      8  CA  LYS A   4       0.281  27.247 -16.208  1.00 71.07           C  
ATOM      9  C   LYS A   4       1.474  26.599 -15.514  1.00 66.53           C  
ATOM     10  O   LYS A   4       2.665  26.738 -15.750  1.00 65.33           O  
ATOM     11  CB  LYS A   4       0.496  27.040 -17.702  1.00 74.75           C  
ATOM     12  CG  LYS A   4      -0.696  26.235 -18.185  1.00 84.24           C  
ATOM     13  CD  LYS A   4      -2.046  26.915 -17.964  1.00 94.44           C  
ATOM     14  CE  LYS A   4      -3.206  25.938 -17.948  1.00 91.97           C  
ATOM     15  NZ  LYS A   4      -4.343  26.605 -17.344  1.00 97.88           N  
ATOM     16  N   ILE A   5       0.771  25.617 -14.935  1.00 60.65           N  
ATOM     17  CA  ILE A   5       1.135  24.558 -14.028  1.00 55.11           C  
ATOM     18  C   ILE A   5       2.552  24.187 -13.582  1.00 52.26           C  
ATOM     19  O   ILE A   5       2.768  24.410 -12.385  1.00 56.55           O  
ATOM     20  CB  ILE A   5       0.290  23.365 -14.623  1.00 52.86           C  
ATOM     21  CG1 ILE A   5      -1.127  23.356 -14.012  1.00 53.72           C  
ATOM     22  CG2 ILE A   5       0.840  22.031 -14.207  1.00 53.95           C  
ATOM     23  CD1 ILE A   5      -2.161  24.485 -14.251  1.00 56.28           C  
ATOM     24  N   PHE A   6       3.521  23.622 -14.306  1.00 43.85           N  
ATOM     25  CA  PHE A   6       4.765  23.289 -13.629  1.00 33.38           C  
ATOM     26  C   PHE A   6       5.773  24.408 -13.680  1.00 30.92           C  
ATOM     27  O   PHE A   6       5.776  25.257 -14.570  1.00 31.62           O  
ATOM     28  CB  PHE A   6       5.371  22.021 -14.221  1.00 30.73           C  
ATOM     29  CG  PHE A   6       4.647  20.770 -13.745  1.00 21.95           C  
ATOM     30  CD1 PHE A   6       4.872  20.301 -12.454  1.00 21.25           C  
ATOM     31  CD2 PHE A   6       3.767  20.082 -14.586  1.00 24.02           C  
ATOM     32  CE1 PHE A   6       4.218  19.156 -12.003  1.00 14.52           C  
ATOM     33  CE2 PHE A   6       3.112  18.936 -14.127  1.00 21.13           C  
ATOM     34  CZ  PHE A   6       3.339  18.468 -12.838  1.00 17.02           C  
ATOM     35  N   ASP A   7       6.628  24.487 -12.677  1.00 28.40           N  
ATOM     36  CA  ASP A   7       7.667  25.487 -12.705  1.00 26.41           C  
ATOM     37  C   ASP A   7       8.860  24.980 -13.491  1.00 26.47           C  
ATOM     38  O   ASP A   7       9.566  25.750 -14.157  1.00 28.12           O  
ATOM     39  CB  ASP A   7       8.102  25.833 -11.294  1.00 32.75           C  
ATOM     40  CG  ASP A   7       7.039  26.628 -10.554  1.00 33.95           C  
ATOM     41  OD1 ASP A   7       6.798  27.772 -10.913  1.00 42.58           O  
ATOM     42  OD2 ASP A   7       6.431  26.104  -9.626  1.00 33.33           O  
ATOM     43  N   LEU A   8       9.078  23.681 -13.447  1.00 21.97           N  
ATOM     44  CA  LEU A   8      10.216  23.077 -14.098  1.00 23.02           C  
ATOM     45  C   LEU A   8       9.768  21.692 -14.512  1.00 22.53           C  
ATOM     46  O   LEU A   8       8.999  21.061 -13.770  1.00 22.14           O  
ATOM     47  CB  LEU A   8      11.386  22.993 -13.109  1.00 18.07           C  
ATOM     48  CG  LEU A   8      12.686  22.329 -13.524  1.00 24.13           C  
ATOM     49  CD1 LEU A   8      13.228  23.059 -14.743  1.00 19.37           C  
ATOM     50  CD2 LEU A   8      13.690  22.350 -12.376  1.00 23.15           C  
ATOM     51  N   VAL A   9      10.119  21.285 -15.739  1.00 19.65           N  
ATOM     52  CA  VAL A   9       9.952  19.903 -16.161  1.00 17.64           C  
ATOM     53  C   VAL A   9      11.382  19.504 -16.477  1.00 16.61           C  
ATOM     54  O   VAL A   9      12.121  20.268 -17.100  1.00 19.89           O  
ATOM     55  CB  VAL A   9       9.075  19.749 -17.431  1.00 20.91           C  
ATOM     56  CG1 VAL A   9       9.055  18.293 -17.910  1.00 10.17           C  
ATOM     57  CG2 VAL A   9       7.643  20.122 -17.097  1.00 15.73           C  
ATOM     58  N   VAL A  10      11.786  18.345 -15.975  1.00 17.86           N  
ATOM     59  CA  VAL A  10      13.122  17.797 -16.122  1.00 15.14           C  
ATOM     60  C   VAL A  10      13.001  16.519 -16.939  1.00 15.30           C  
ATOM     61  O   VAL A  10      12.304  15.570 -16.568  1.00 16.26           O  
ATOM     62  CB  VAL A  10      13.726  17.476 -14.722  1.00 19.87           C  
ATOM     63  CG1 VAL A  10      15.124  16.884 -14.887  1.00 12.76           C  
ATOM     64  CG2 VAL A  10      13.784  18.730 -13.871  1.00  7.42           C  
ATOM     65  N   ILE A  11      13.647  16.451 -18.084  1.00 15.84           N  
ATOM     66  CA  ILE A  11      13.604  15.245 -18.892  1.00 15.21           C  
ATOM     67  C   ILE A  11      14.876  14.494 -18.548  1.00 13.07           C  
ATOM     68  O   ILE A  11      15.977  14.944 -18.892  1.00 15.88           O  
ATOM     69  CB  ILE A  11      13.540  15.651 -20.388  1.00 16.12           C  
ATOM     70  CG1 ILE A  11      12.290  16.495 -20.628  1.00 10.74           C  
ATOM     71  CG2 ILE A  11      13.570  14.399 -21.256  1.00  8.15           C  
ATOM     72  CD1 ILE A  11      12.204  17.027 -22.059  1.00 13.49           C  
ATOM     73  N   GLY A  12      14.714  13.356 -17.886  1.00 13.91           N  
ATOM     74  CA  GLY A  12      15.843  12.586 -17.424  1.00 11.90           C  
ATOM     75  C   GLY A  12      15.934  12.643 -15.906  1.00 13.96           C  
ATOM     76  O   GLY A  12      16.178  13.678 -15.279  1.00 14.40           O  
ATOM     77  N   ALA A  13      15.689  11.498 -15.276  1.00 13.07           N  
ATOM     78  CA  ALA A  13      15.769  11.379 -13.835  1.00 12.65           C  
ATOM     79  C   ALA A  13      17.092  10.740 -13.484  1.00 10.82           C  
ATOM     80  O   ALA A  13      17.125   9.656 -12.899  1.00 13.77           O  
ATOM     81  CB  ALA A  13      14.631  10.502 -13.323  1.00 11.73           C  
ATOM     82  N   GLY A  14      18.219  11.324 -13.873  1.00  9.29           N  
ATOM     83  CA  GLY A  14      19.505  10.708 -13.590  1.00  6.81           C  
ATOM     84  C   GLY A  14      20.300  11.505 -12.579  1.00 11.57           C  
ATOM     85  O   GLY A  14      19.701  12.328 -11.889  1.00 14.09           O  
ATOM     86  N   SER A  15      21.633  11.428 -12.560  1.00 12.16           N  
ATOM     87  CA  SER A  15      22.406  12.164 -11.574  1.00  9.84           C  
ATOM     88  C   SER A  15      22.087  13.642 -11.508  1.00 13.51           C  
ATOM     89  O   SER A  15      21.785  14.154 -10.432  1.00 17.38           O  
ATOM     90  CB  SER A  15      23.872  12.030 -11.846  1.00  3.29           C  
ATOM     91  OG  SER A  15      24.225  10.668 -11.913  1.00 11.14           O  
ATOM     92  N   GLY A  16      22.052  14.373 -12.626  1.00 17.70           N  
ATOM     93  CA  GLY A  16      21.775  15.805 -12.576  1.00 12.19           C  
ATOM     94  C   GLY A  16      20.287  16.129 -12.474  1.00 15.94           C  
ATOM     95  O   GLY A  16      19.875  17.043 -11.760  1.00 18.22           O  
ATOM     96  N   GLY A  17      19.450  15.408 -13.216  1.00 14.94           N  
ATOM     97  CA  GLY A  17      18.018  15.619 -13.196  1.00 14.38           C  
ATOM     98  C   GLY A  17      17.452  15.487 -11.797  1.00 19.39           C  
ATOM     99  O   GLY A  17      16.746  16.393 -11.355  1.00 21.12           O  
ATOM    100  N   LEU A  18      17.779  14.410 -11.061  1.00 18.61           N  
ATOM    101  CA  LEU A  18      17.242  14.228  -9.723  1.00 17.17           C  
ATOM    102  C   LEU A  18      17.782  15.239  -8.735  1.00 18.08           C  
ATOM    103  O   LEU A  18      17.038  15.696  -7.866  1.00 21.28           O  
ATOM    104  CB  LEU A  18      17.539  12.843  -9.221  1.00 14.18           C  
ATOM    105  CG  LEU A  18      16.655  11.777  -9.809  1.00 13.99           C  
ATOM    106  CD1 LEU A  18      17.143  10.416  -9.365  1.00 13.97           C  
ATOM    107  CD2 LEU A  18      15.229  12.034  -9.399  1.00 11.28           C  
ATOM    108  N   GLU A  19      19.031  15.660  -8.873  1.00 17.07           N  
ATOM    109  CA  GLU A  19      19.572  16.709  -8.041  1.00 18.81           C  
ATOM    110  C   GLU A  19      18.806  18.014  -8.265  1.00 22.94           C  
ATOM    111  O   GLU A  19      18.354  18.662  -7.307  1.00 25.28           O  
ATOM    112  CB  GLU A  19      21.033  16.904  -8.380  1.00 14.03           C  
ATOM    113  CG  GLU A  19      21.752  17.920  -7.500  1.00 19.77           C  
ATOM    114  CD  GLU A  19      21.919  17.550  -6.023  1.00 28.16           C  
ATOM    115  OE1 GLU A  19      21.782  16.376  -5.644  1.00 29.07           O  
ATOM    116  OE2 GLU A  19      22.204  18.465  -5.251  1.00 30.42           O  
ATOM    117  N   ALA A  20      18.600  18.404  -9.528  1.00 21.97           N  
ATOM    118  CA  ALA A  20      17.911  19.640  -9.861  1.00 17.24           C  
ATOM    119  C   ALA A  20      16.477  19.623  -9.404  1.00 16.44           C  
ATOM    120  O   ALA A  20      15.985  20.572  -8.792  1.00 16.24           O  
ATOM    121  CB  ALA A  20      17.909  19.859 -11.344  1.00 14.63           C  
ATOM    122  N   ALA A  21      15.810  18.511  -9.679  1.00 16.46           N  
ATOM    123  CA  ALA A  21      14.423  18.323  -9.299  1.00 20.58           C  
ATOM    124  C   ALA A  21      14.230  18.409  -7.780  1.00 23.76           C  
ATOM    125  O   ALA A  21      13.384  19.167  -7.294  1.00 27.85           O  
ATOM    126  CB  ALA A  21      13.965  16.965  -9.801  1.00  9.65           C  
ATOM    127  N   TRP A  22      15.038  17.668  -7.012  1.00 24.22           N  
ATOM    128  CA  TRP A  22      14.991  17.685  -5.570  1.00 23.28           C  
ATOM    129  C   TRP A  22      15.197  19.090  -5.021  1.00 23.89           C  
ATOM    130  O   TRP A  22      14.380  19.554  -4.222  1.00 27.87           O  
ATOM    131  CB  TRP A  22      16.066  16.768  -5.010  1.00 25.43           C  
ATOM    132  CG  TRP A  22      16.104  16.796  -3.487  1.00 37.20           C  
ATOM    133  CD1 TRP A  22      17.058  17.512  -2.786  1.00 38.80           C  
ATOM    134  CD2 TRP A  22      15.212  16.153  -2.676  1.00 34.29           C  
ATOM    135  NE1 TRP A  22      16.770  17.324  -1.521  1.00 36.43           N  
ATOM    136  CE2 TRP A  22      15.692  16.523  -1.411  1.00 39.59           C  
ATOM    137  CE3 TRP A  22      14.105  15.324  -2.818  1.00 31.86           C  
ATOM    138  CZ2 TRP A  22      15.052  16.064  -0.259  1.00 44.74           C  
ATOM    139  CZ3 TRP A  22      13.469  14.869  -1.663  1.00 42.87           C  
ATOM    140  CH2 TRP A  22      13.938  15.228  -0.394  1.00 42.44           C  
ATOM    141  N   ASN A  23      16.273  19.783  -5.420  1.00 21.78           N  
ATOM    142  CA  ASN A  23      16.578  21.111  -4.910  1.00 23.38           C  
ATOM    143  C   ASN A  23      15.509  22.140  -5.189  1.00 26.84           C  
ATOM    144  O   ASN A  23      15.146  22.917  -4.306  1.00 28.71           O  
ATOM    145  CB  ASN A  23      17.887  21.634  -5.481  1.00 21.49           C  
ATOM    146  CG  ASN A  23      19.107  20.975  -4.870  1.00 22.99           C  
ATOM    147  OD1 ASN A  23      20.190  21.548  -4.840  1.00 36.67           O  
ATOM    148  ND2 ASN A  23      19.035  19.780  -4.317  1.00 21.65           N  
ATOM    149  N   ALA A  24      14.940  22.161  -6.388  1.00 26.14           N  
ATOM    150  CA  ALA A  24      13.894  23.106  -6.697  1.00 23.60           C  
ATOM    151  C   ALA A  24      12.641  22.818  -5.885  1.00 23.41           C  
ATOM    152  O   ALA A  24      11.986  23.757  -5.435  1.00 23.50           O  
ATOM    153  CB  ALA A  24      13.557  23.029  -8.178  1.00 23.82           C  
ATOM    154  N   ALA A  25      12.272  21.566  -5.649  1.00 23.53           N  
ATOM    155  CA  ALA A  25      11.063  21.269  -4.913  1.00 25.30           C  
ATOM    156  C   ALA A  25      11.249  21.537  -3.430  1.00 28.80           C  
ATOM    157  O   ALA A  25      10.363  22.106  -2.804  1.00 31.96           O  
ATOM    158  CB  ALA A  25      10.685  19.821  -5.091  1.00 18.97           C  
ATOM    159  N   THR A  26      12.406  21.229  -2.850  1.00 31.36           N  
ATOM    160  CA  THR A  26      12.586  21.401  -1.418  1.00 30.24           C  
ATOM    161  C   THR A  26      13.160  22.760  -1.048  1.00 32.61           C  
ATOM    162  O   THR A  26      12.570  23.457  -0.226  1.00 34.97           O  
ATOM    163  CB  THR A  26      13.490  20.255  -0.855  1.00 31.87           C  
ATOM    164  OG1 THR A  26      14.775  20.343  -1.458  1.00 34.36           O  
ATOM    165  CG2 THR A  26      12.886  18.885  -1.132  1.00 22.54           C  
ATOM    166  N   LEU A  27      14.267  23.216  -1.638  1.00 30.91           N  
ATOM    167  CA  LEU A  27      14.829  24.506  -1.281  1.00 28.94           C  
ATOM    168  C   LEU A  27      13.993  25.683  -1.719  1.00 30.63           C  
ATOM    169  O   LEU A  27      13.950  26.721  -1.055  1.00 35.25           O  
ATOM    170  CB  LEU A  27      16.188  24.761  -1.898  1.00 26.53           C  
ATOM    171  CG  LEU A  27      17.293  23.738  -1.786  1.00 38.18           C  
ATOM    172  CD1 LEU A  27      18.559  24.392  -2.312  1.00 38.27           C  
ATOM    173  CD2 LEU A  27      17.479  23.263  -0.347  1.00 44.07           C  
ATOM    174  N   TYR A  28      13.402  25.543  -2.902  1.00 30.89           N  
ATOM    175  CA  TYR A  28      12.693  26.650  -3.503  1.00 28.91           C  
ATOM    176  C   TYR A  28      11.191  26.498  -3.570  1.00 31.53           C  
ATOM    177  O   TYR A  28      10.522  27.439  -3.995  1.00 34.99           O  
ATOM    178  CB  TYR A  28      13.272  26.888  -4.902  1.00 27.71           C  
ATOM    179  CG  TYR A  28      14.695  27.418  -4.804  1.00 27.62           C  
ATOM    180  CD1 TYR A  28      14.909  28.706  -4.310  1.00 30.14           C  
ATOM    181  CD2 TYR A  28      15.788  26.616  -5.147  1.00 28.32           C  
ATOM    182  CE1 TYR A  28      16.210  29.194  -4.146  1.00 30.70           C  
ATOM    183  CE2 TYR A  28      17.089  27.098  -4.986  1.00 28.84           C  
ATOM    184  CZ  TYR A  28      17.294  28.385  -4.484  1.00 33.86           C  
ATOM    185  OH  TYR A  28      18.581  28.854  -4.319  1.00 34.32           O  
ATOM    186  N   LYS A  29      10.638  25.364  -3.122  1.00 33.73           N  
ATOM    187  CA  LYS A  29       9.198  25.081  -3.104  1.00 38.44           C  
ATOM    188  C   LYS A  29       8.517  25.143  -4.477  1.00 38.09           C  
ATOM    189  O   LYS A  29       7.346  25.519  -4.631  1.00 40.58           O  
ATOM    190  CB  LYS A  29       8.482  26.054  -2.149  1.00 44.01           C  
ATOM    191  CG  LYS A  29       8.946  26.123  -0.702  1.00 55.87           C  
ATOM    192  CD  LYS A  29       8.184  27.333  -0.166  1.00 68.83           C  
ATOM    193  CE  LYS A  29       8.394  27.726   1.297  1.00 72.59           C  
ATOM    194  NZ  LYS A  29       7.605  28.914   1.598  1.00 70.16           N  
ATOM    195  N   LYS A  30       9.226  24.738  -5.526  1.00 35.77           N  
ATOM    196  CA  LYS A  30       8.683  24.807  -6.867  1.00 30.18           C  
ATOM    197  C   LYS A  30       8.006  23.501  -7.190  1.00 29.03           C  
ATOM    198  O   LYS A  30       8.400  22.482  -6.628  1.00 33.23           O  
ATOM    199  CB  LYS A  30       9.802  25.069  -7.855  1.00 30.35           C  
ATOM    200  CG  LYS A  30      10.433  26.424  -7.597  1.00 33.44           C  
ATOM    201  CD  LYS A  30       9.476  27.528  -7.985  1.00 32.73           C  
ATOM    202  CE  LYS A  30       9.908  28.831  -7.370  1.00 38.96           C  
ATOM    203  NZ  LYS A  30       9.515  29.902  -8.258  1.00 44.46           N  
ATOM    204  N   ARG A  31       6.982  23.470  -8.043  1.00 28.49           N  
ATOM    205  CA  ARG A  31       6.345  22.220  -8.427  1.00 25.51           C  
ATOM    206  C   ARG A  31       7.145  21.732  -9.627  1.00 21.47           C  
ATOM    207  O   ARG A  31       7.302  22.446 -10.613  1.00 23.51           O  
ATOM    208  CB  ARG A  31       4.901  22.523  -8.764  1.00 32.59           C  
ATOM    209  CG  ARG A  31       4.022  21.288  -8.755  1.00 49.49           C  
ATOM    210  CD  ARG A  31       2.575  21.669  -9.063  1.00 56.60           C  
ATOM    211  NE  ARG A  31       1.732  20.480  -9.133  1.00 70.80           N  
ATOM    212  CZ  ARG A  31       1.011  20.166 -10.220  1.00 68.70           C  
ATOM    213  NH1 ARG A  31       1.024  20.924 -11.314  1.00 73.55           N  
ATOM    214  NH2 ARG A  31       0.259  19.065 -10.223  1.00 77.15           N  
ATOM    215  N   VAL A  32       7.719  20.553  -9.544  1.00 21.78           N  
ATOM    216  CA  VAL A  32       8.642  20.026 -10.523  1.00 18.79           C  
ATOM    217  C   VAL A  32       8.117  18.702 -11.049  1.00 20.79           C  
ATOM    218  O   VAL A  32       7.629  17.888 -10.260  1.00 22.20           O  
ATOM    219  CB  VAL A  32      10.028  19.841  -9.840  1.00 18.85           C  
ATOM    220  CG1 VAL A  32      11.058  19.359 -10.855  1.00 20.45           C  
ATOM    221  CG2 VAL A  32      10.519  21.163  -9.260  1.00 17.64           C  
ATOM    222  N   ALA A  33       8.156  18.454 -12.360  1.00 19.66           N  
ATOM    223  CA  ALA A  33       7.811  17.157 -12.912  1.00 15.75           C  
ATOM    224  C   ALA A  33       9.109  16.564 -13.439  1.00 18.16           C  
ATOM    225  O   ALA A  33       9.957  17.303 -13.959  1.00 19.10           O  
ATOM    226  CB  ALA A  33       6.862  17.284 -14.073  1.00 15.27           C  
ATOM    227  N   VAL A  34       9.356  15.264 -13.315  1.00 17.76           N  
ATOM    228  CA  VAL A  34      10.574  14.644 -13.793  1.00 18.74           C  
ATOM    229  C   VAL A  34      10.072  13.476 -14.621  1.00 20.78           C  
ATOM    230  O   VAL A  34       9.104  12.804 -14.227  1.00 18.71           O  
ATOM    231  CB  VAL A  34      11.441  14.142 -12.610  1.00 23.60           C  
ATOM    232  CG1 VAL A  34      12.781  13.594 -13.084  1.00 17.83           C  
ATOM    233  CG2 VAL A  34      11.739  15.308 -11.688  1.00 21.19           C  
ATOM    234  N   ILE A  35      10.718  13.208 -15.764  1.00 20.99           N  
ATOM    235  CA  ILE A  35      10.290  12.164 -16.694  1.00 18.88           C  
ATOM    236  C   ILE A  35      11.414  11.171 -16.888  1.00 15.72           C  
ATOM    237  O   ILE A  35      12.573  11.579 -16.984  1.00 16.28           O  
ATOM    238  CB  ILE A  35       9.922  12.788 -18.075  1.00 21.74           C  
ATOM    239  CG1 ILE A  35       8.857  13.847 -17.889  1.00 18.77           C  
ATOM    240  CG2 ILE A  35       9.390  11.728 -19.033  1.00 22.39           C  
ATOM    241  CD1 ILE A  35       8.942  14.869 -19.020  1.00 24.42           C  
ATOM    242  N   ASP A  36      11.124   9.882 -16.954  1.00 16.45           N  
ATOM    243  CA  ASP A  36      12.116   8.906 -17.347  1.00 15.89           C  
ATOM    244  C   ASP A  36      11.355   7.721 -17.913  1.00 18.27           C  
ATOM    245  O   ASP A  36      10.160   7.533 -17.692  1.00 16.71           O  
ATOM    246  CB  ASP A  36      12.960   8.463 -16.159  1.00 20.37           C  
ATOM    247  CG  ASP A  36      14.373   8.067 -16.556  1.00 15.59           C  
ATOM    248  OD1 ASP A  36      14.559   7.109 -17.293  1.00 22.18           O  
ATOM    249  OD2 ASP A  36      15.315   8.709 -16.114  1.00 19.70           O  
ATOM    250  N   VAL A  37      12.088   6.885 -18.629  1.00 20.37           N  
ATOM    251  CA  VAL A  37      11.519   5.808 -19.416  1.00 21.52           C  
ATOM    252  C   VAL A  37      11.252   4.510 -18.683  1.00 23.97           C  
ATOM    253  O   VAL A  37      10.441   3.702 -19.153  1.00 27.45           O  
ATOM    254  CB  VAL A  37      12.456   5.562 -20.635  1.00 20.17           C  
ATOM    255  CG1 VAL A  37      12.618   6.882 -21.373  1.00 19.36           C  
ATOM    256  CG2 VAL A  37      13.843   5.071 -20.218  1.00 22.95           C  
ATOM    257  N   GLN A  38      11.926   4.243 -17.570  1.00 23.74           N  
ATOM    258  CA  GLN A  38      11.690   3.024 -16.815  1.00 23.32           C  
ATOM    259  C   GLN A  38      11.763   3.338 -15.340  1.00 27.22           C  
ATOM    260  O   GLN A  38      12.431   4.285 -14.914  1.00 27.59           O  
ATOM    261  CB  GLN A  38      12.723   1.947 -17.051  1.00 23.44           C  
ATOM    262  CG  GLN A  38      12.690   1.231 -18.365  1.00 29.95           C  
ATOM    263  CD  GLN A  38      13.701   0.102 -18.484  1.00 32.98           C  
ATOM    264  OE1 GLN A  38      13.614  -0.783 -19.324  1.00 39.93           O  
ATOM    265  NE2 GLN A  38      14.750   0.126 -17.666  1.00 34.61           N  
ATOM    266  N   MET A  39      11.053   2.511 -14.578  1.00 27.91           N  
ATOM    267  CA  MET A  39      11.046   2.600 -13.131  1.00 25.89           C  
ATOM    268  C   MET A  39      12.229   1.863 -12.506  1.00 25.05           C  
ATOM    269  O   MET A  39      12.818   2.328 -11.535  1.00 25.51           O  
ATOM    270  CB  MET A  39       9.763   1.999 -12.588  1.00 31.44           C  
ATOM    271  CG  MET A  39       8.483   2.754 -12.865  1.00 34.56           C  
ATOM    272  SD  MET A  39       8.380   4.316 -11.967  1.00 44.32           S  
ATOM    273  CE  MET A  39       8.031   3.696 -10.351  1.00 43.05           C  
ATOM    274  N   VAL A  40      12.581   0.673 -12.991  1.00 25.02           N  
ATOM    275  CA  VAL A  40      13.684  -0.109 -12.432  1.00 24.54           C  
ATOM    276  C   VAL A  40      14.633  -0.465 -13.568  1.00 26.29           C  
ATOM    277  O   VAL A  40      14.208  -0.542 -14.723  1.00 23.55           O  
ATOM    278  CB  VAL A  40      13.191  -1.437 -11.735  1.00 26.06           C  
ATOM    279  CG1 VAL A  40      12.154  -1.093 -10.656  1.00 19.37           C  
ATOM    280  CG2 VAL A  40      12.575  -2.397 -12.729  1.00 17.27           C  
ATOM    281  N   HIS A  41      15.908  -0.613 -13.224  1.00 24.35           N  
ATOM    282  CA  HIS A  41      16.956  -0.949 -14.166  1.00 23.43           C  
ATOM    283  C   HIS A  41      16.691  -2.142 -15.066  1.00 23.18           C  
ATOM    284  O   HIS A  41      16.008  -3.092 -14.670  1.00 21.84           O  
ATOM    285  CB  HIS A  41      18.262  -1.245 -13.423  1.00 22.17           C  
ATOM    286  CG  HIS A  41      18.282  -2.568 -12.661  1.00 24.40           C  
ATOM    287  ND1 HIS A  41      18.900  -3.680 -13.031  1.00 23.40           N  
ATOM    288  CD2 HIS A  41      17.646  -2.845 -11.476  1.00 24.63           C  
ATOM    289  CE1 HIS A  41      18.673  -4.608 -12.145  1.00 23.09           C  
ATOM    290  NE2 HIS A  41      17.918  -4.094 -11.217  1.00 21.80           N  
ATOM    291  N   GLY A  42      17.411  -2.173 -16.184  1.00 24.51           N  
ATOM    292  CA  GLY A  42      17.426  -3.358 -17.010  1.00 23.74           C  
ATOM    293  C   GLY A  42      16.842  -3.228 -18.398  1.00 25.13           C  
ATOM    294  O   GLY A  42      16.333  -2.185 -18.807  1.00 23.59           O  
ATOM    295  N   PRO A  43      16.949  -4.295 -19.200  1.00 27.07           N  
ATOM    296  CA  PRO A  43      16.366  -4.376 -20.535  1.00 26.49           C  
ATOM    297  C   PRO A  43      14.885  -4.003 -20.480  1.00 26.63           C  
ATOM    298  O   PRO A  43      14.229  -4.331 -19.489  1.00 29.29           O  
ATOM    299  CB  PRO A  43      16.624  -5.815 -20.951  1.00 30.37           C  
ATOM    300  CG  PRO A  43      17.831  -6.228 -20.143  1.00 25.28           C  
ATOM    301  CD  PRO A  43      17.498  -5.596 -18.807  1.00 28.22           C  
ATOM    302  N   PRO A  44      14.262  -3.330 -21.447  1.00 24.85           N  
ATOM    303  CA  PRO A  44      14.856  -2.904 -22.706  1.00 23.24           C  
ATOM    304  C   PRO A  44      15.632  -1.599 -22.714  1.00 23.95           C  
ATOM    305  O   PRO A  44      16.530  -1.424 -23.523  1.00 26.01           O  
ATOM    306  CB  PRO A  44      13.672  -2.885 -23.630  1.00 23.86           C  
ATOM    307  CG  PRO A  44      12.568  -2.361 -22.739  1.00 20.69           C  
ATOM    308  CD  PRO A  44      12.811  -3.164 -21.481  1.00 23.64           C  
ATOM    309  N   PHE A  45      15.308  -0.660 -21.826  1.00 22.01           N  
ATOM    310  CA  PHE A  45      15.927   0.643 -21.912  1.00 21.12           C  
ATOM    311  C   PHE A  45      17.137   0.871 -21.040  1.00 22.20           C  
ATOM    312  O   PHE A  45      17.751   1.929 -21.154  1.00 22.84           O  
ATOM    313  CB  PHE A  45      14.857   1.679 -21.629  1.00 21.35           C  
ATOM    314  CG  PHE A  45      13.679   1.522 -22.580  1.00 27.87           C  
ATOM    315  CD1 PHE A  45      13.888   1.328 -23.956  1.00 32.30           C  
ATOM    316  CD2 PHE A  45      12.385   1.544 -22.063  1.00 28.40           C  
ATOM    317  CE1 PHE A  45      12.797   1.144 -24.806  1.00 32.77           C  
ATOM    318  CE2 PHE A  45      11.301   1.361 -22.921  1.00 31.31           C  
ATOM    319  CZ  PHE A  45      11.505   1.163 -24.287  1.00 31.80           C  
ATOM    320  N   PHE A  46      17.492  -0.126 -20.214  1.00 21.45           N  
ATOM    321  CA  PHE A  46      18.660  -0.200 -19.341  1.00 21.87           C  
ATOM    322  C   PHE A  46      18.707   0.791 -18.206  1.00 25.15           C  
ATOM    323  O   PHE A  46      18.806   0.401 -17.032  1.00 28.38           O  
ATOM    324  CB  PHE A  46      19.935  -0.096 -20.188  1.00 18.56           C  
ATOM    325  CG  PHE A  46      20.042  -1.362 -21.025  1.00 19.07           C  
ATOM    326  CD1 PHE A  46      20.433  -2.561 -20.423  1.00 15.08           C  
ATOM    327  CD2 PHE A  46      19.686  -1.336 -22.376  1.00 18.79           C  
ATOM    328  CE1 PHE A  46      20.466  -3.736 -21.167  1.00 17.24           C  
ATOM    329  CE2 PHE A  46      19.721  -2.518 -23.114  1.00 16.41           C  
ATOM    330  CZ  PHE A  46      20.107  -3.718 -22.513  1.00 14.74           C  
ATOM    331  N   SER A  47      18.715   2.064 -18.552  1.00 26.43           N  
ATOM    332  CA  SER A  47      18.634   3.120 -17.576  1.00 28.28           C  
ATOM    333  C   SER A  47      17.154   3.283 -17.200  1.00 27.33           C  
ATOM    334  O   SER A  47      16.232   2.901 -17.930  1.00 25.24           O  
ATOM    335  CB  SER A  47      19.200   4.391 -18.181  1.00 30.17           C  
ATOM    336  OG  SER A  47      19.712   5.199 -17.133  1.00 34.42           O  
ATOM    337  N   ALA A  48      16.963   3.945 -16.067  1.00 22.86           N  
ATOM    338  CA  ALA A  48      15.682   4.071 -15.409  1.00 19.11           C  
ATOM    339  C   ALA A  48      15.845   5.169 -14.385  1.00 16.94           C  
ATOM    340  O   ALA A  48      16.837   5.900 -14.386  1.00 18.70           O  
ATOM    341  CB  ALA A  48      15.371   2.787 -14.682  1.00 22.88           C  
ATOM    342  N   LEU A  49      14.880   5.279 -13.483  1.00 20.12           N  
ATOM    343  CA  LEU A  49      14.892   6.182 -12.343  1.00 19.70           C  
ATOM    344  C   LEU A  49      16.230   6.022 -11.621  1.00 19.87           C  
ATOM    345  O   LEU A  49      16.647   4.920 -11.228  1.00 22.34           O  
ATOM    346  CB  LEU A  49      13.688   5.789 -11.488  1.00 17.29           C  
ATOM    347  CG  LEU A  49      13.239   6.537 -10.262  1.00 19.47           C  
ATOM    348  CD1 LEU A  49      13.286   8.026 -10.490  1.00 16.00           C  
ATOM    349  CD2 LEU A  49      11.814   6.107  -9.950  1.00 16.27           C  
ATOM    350  N   GLY A  50      16.976   7.122 -11.539  1.00 18.97           N  
ATOM    351  CA  GLY A  50      18.297   7.107 -10.937  1.00 14.35           C  
ATOM    352  C   GLY A  50      19.354   7.443 -11.972  1.00 16.20           C  
ATOM    353  O   GLY A  50      20.401   7.983 -11.635  1.00 16.61           O  
ATOM    354  N   GLY A  51      19.144   7.123 -13.249  1.00 17.26           N  
ATOM    355  CA  GLY A  51      20.101   7.432 -14.285  1.00 13.32           C  
ATOM    356  C   GLY A  51      21.102   6.337 -14.527  1.00 16.18           C  
ATOM    357  O   GLY A  51      21.096   5.256 -13.924  1.00 21.16           O  
ATOM    358  N   THR A  52      22.035   6.679 -15.400  1.00 17.11           N  
ATOM    359  CA  THR A  52      23.053   5.756 -15.864  1.00 16.87           C  
ATOM    360  C   THR A  52      24.016   5.329 -14.779  1.00 15.99           C  
ATOM    361  O   THR A  52      24.326   4.143 -14.692  1.00 16.07           O  
ATOM    362  CB  THR A  52      23.802   6.418 -17.023  1.00 17.74           C  
ATOM    363  OG1 THR A  52      22.754   6.837 -17.886  1.00 22.03           O  
ATOM    364  CG2 THR A  52      24.823   5.534 -17.707  1.00 11.88           C  
ATOM    365  N   CYS A  53      24.464   6.240 -13.915  1.00 12.93           N  
ATOM    366  CA  CYS A  53      25.402   5.891 -12.869  1.00 15.22           C  
ATOM    367  C   CYS A  53      24.804   4.834 -11.945  1.00 11.50           C  
ATOM    368  O   CYS A  53      25.425   3.794 -11.732  1.00 10.08           O  
ATOM    369  CB  CYS A  53      25.749   7.156 -12.108  1.00 19.12           C  
ATOM    370  SG  CYS A  53      26.922   6.981 -10.758  1.00 23.19           S  
ATOM    371  N   VAL A  54      23.590   5.064 -11.461  1.00 11.30           N  
ATOM    372  CA  VAL A  54      22.933   4.095 -10.602  1.00 14.05           C  
ATOM    373  C   VAL A  54      22.645   2.779 -11.332  1.00 15.55           C  
ATOM    374  O   VAL A  54      22.980   1.703 -10.848  1.00 12.65           O  
ATOM    375  CB  VAL A  54      21.640   4.752 -10.066  1.00 14.68           C  
ATOM    376  CG1 VAL A  54      20.704   3.737  -9.403  1.00 15.61           C  
ATOM    377  CG2 VAL A  54      22.060   5.802  -9.053  1.00  8.14           C  
ATOM    378  N   ASN A  55      22.108   2.840 -12.549  1.00 16.44           N  
ATOM    379  CA  ASN A  55      21.655   1.624 -13.200  1.00 13.12           C  
ATOM    380  C   ASN A  55      22.619   0.818 -14.025  1.00 14.40           C  
ATOM    381  O   ASN A  55      22.618  -0.419 -13.981  1.00 15.47           O  
ATOM    382  CB  ASN A  55      20.462   1.963 -14.059  1.00 18.35           C  
ATOM    383  CG  ASN A  55      19.300   2.421 -13.207  1.00 14.79           C  
ATOM    384  OD1 ASN A  55      18.660   1.586 -12.585  1.00 17.93           O  
ATOM    385  ND2 ASN A  55      18.960   3.701 -13.102  1.00 14.91           N  
ATOM    386  N   VAL A  56      23.425   1.490 -14.834  1.00 13.52           N  
ATOM    387  CA  VAL A  56      24.344   0.825 -15.737  1.00 13.88           C  
ATOM    388  C   VAL A  56      25.604   1.662 -15.815  1.00 15.61           C  
ATOM    389  O   VAL A  56      26.131   1.924 -16.894  1.00 17.72           O  
ATOM    390  CB  VAL A  56      23.737   0.656 -17.196  1.00 12.36           C  
ATOM    391  CG1 VAL A  56      22.787  -0.530 -17.210  1.00 11.66           C  
ATOM    392  CG2 VAL A  56      23.035   1.941 -17.664  1.00 10.84           C  
ATOM    393  N   GLY A  57      26.104   2.100 -14.665  1.00 15.73           N  
ATOM    394  CA  GLY A  57      27.260   2.967 -14.629  1.00 12.55           C  
ATOM    395  C   GLY A  57      28.080   2.751 -13.382  1.00 12.86           C  
ATOM    396  O   GLY A  57      28.388   1.609 -13.032  1.00 16.79           O  
ATOM    397  N   CYS A  58      28.400   3.837 -12.690  1.00 15.67           N  
ATOM    398  CA  CYS A  58      29.283   3.819 -11.530  1.00 15.18           C  
ATOM    399  C   CYS A  58      29.015   2.781 -10.464  1.00 11.64           C  
ATOM    400  O   CYS A  58      29.906   2.033 -10.079  1.00 14.35           O  
ATOM    401  CB  CYS A  58      29.273   5.154 -10.816  1.00 15.72           C  
ATOM    402  SG  CYS A  58      28.655   6.613 -11.669  1.00 14.58           S  
ATOM    403  N   VAL A  59      27.756   2.717 -10.033  1.00 16.87           N  
ATOM    404  CA  VAL A  59      27.400   1.878  -8.914  1.00 14.96           C  
ATOM    405  C   VAL A  59      27.511   0.422  -9.324  1.00 14.28           C  
ATOM    406  O   VAL A  59      28.357  -0.224  -8.687  1.00 17.76           O  
ATOM    407  CB  VAL A  59      25.980   2.301  -8.431  1.00 14.91           C  
ATOM    408  CG1 VAL A  59      25.485   1.356  -7.346  1.00 15.51           C  
ATOM    409  CG2 VAL A  59      26.039   3.733  -7.909  1.00  6.82           C  
ATOM    410  N   PRO A  60      26.856  -0.178 -10.336  1.00 14.58           N  
ATOM    411  CA  PRO A  60      27.128  -1.564 -10.694  1.00 12.39           C  
ATOM    412  C   PRO A  60      28.579  -1.877 -11.078  1.00 16.55           C  
ATOM    413  O   PRO A  60      29.116  -2.915 -10.640  1.00 17.53           O  
ATOM    414  CB  PRO A  60      26.104  -1.842 -11.791  1.00 11.80           C  
ATOM    415  CG  PRO A  60      25.687  -0.513 -12.327  1.00 12.64           C  
ATOM    416  CD  PRO A  60      25.738   0.363 -11.112  1.00  7.76           C  
ATOM    417  N   LYS A  61      29.292  -0.991 -11.810  1.00 17.01           N  
ATOM    418  CA  LYS A  61      30.637  -1.349 -12.210  1.00 15.05           C  
ATOM    419  C   LYS A  61      31.589  -1.338 -11.020  1.00 15.77           C  
ATOM    420  O   LYS A  61      32.481  -2.188 -10.969  1.00 17.23           O  
ATOM    421  CB  LYS A  61      31.073  -0.399 -13.335  1.00  8.15           C  
ATOM    422  CG  LYS A  61      31.585   0.960 -13.009  1.00 11.99           C  
ATOM    423  CD  LYS A  61      33.070   0.827 -12.864  1.00  4.43           C  
ATOM    424  CE  LYS A  61      33.641   2.042 -12.199  1.00  8.88           C  
ATOM    425  NZ  LYS A  61      33.432   3.220 -13.009  1.00 14.11           N  
ATOM    426  N   LYS A  62      31.457  -0.463 -10.024  1.00 15.01           N  
ATOM    427  CA  LYS A  62      32.335  -0.502  -8.860  1.00 16.34           C  
ATOM    428  C   LYS A  62      32.091  -1.810  -8.095  1.00 13.51           C  
ATOM    429  O   LYS A  62      33.056  -2.432  -7.669  1.00 17.60           O  
ATOM    430  CB  LYS A  62      32.050   0.743  -8.003  1.00 18.32           C  
ATOM    431  CG  LYS A  62      32.781   0.939  -6.674  1.00 16.95           C  
ATOM    432  CD  LYS A  62      34.285   1.009  -6.849  1.00 24.37           C  
ATOM    433  CE  LYS A  62      34.929   1.094  -5.475  1.00 31.23           C  
ATOM    434  NZ  LYS A  62      34.833   2.423  -4.898  1.00 28.52           N  
ATOM    435  N   LEU A  63      30.867  -2.330  -7.949  1.00 14.52           N  
ATOM    436  CA  LEU A  63      30.617  -3.625  -7.324  1.00 13.16           C  
ATOM    437  C   LEU A  63      31.277  -4.727  -8.117  1.00 13.10           C  
ATOM    438  O   LEU A  63      31.878  -5.635  -7.536  1.00 15.34           O  
ATOM    439  CB  LEU A  63      29.129  -3.980  -7.254  1.00 18.21           C  
ATOM    440  CG  LEU A  63      28.229  -3.131  -6.383  1.00 21.18           C  
ATOM    441  CD1 LEU A  63      26.802  -3.615  -6.477  1.00 16.30           C  
ATOM    442  CD2 LEU A  63      28.719  -3.211  -4.947  1.00 23.93           C  
ATOM    443  N   MET A  64      31.224  -4.670  -9.450  1.00 13.10           N  
ATOM    444  CA  MET A  64      31.844  -5.712 -10.266  1.00 12.79           C  
ATOM    445  C   MET A  64      33.369  -5.639 -10.258  1.00 11.06           C  
ATOM    446  O   MET A  64      34.061  -6.666 -10.244  1.00 17.04           O  
ATOM    447  CB  MET A  64      31.267  -5.597 -11.684  1.00 17.05           C  
ATOM    448  CG  MET A  64      29.786  -5.922 -11.726  1.00 17.09           C  
ATOM    449  SD  MET A  64      29.015  -5.629 -13.332  1.00 23.10           S  
ATOM    450  CE  MET A  64      29.549  -7.080 -14.176  1.00 11.59           C  
ATOM    451  N   VAL A  65      33.962  -4.447 -10.216  1.00 12.90           N  
ATOM    452  CA  VAL A  65      35.408  -4.265 -10.084  1.00 12.93           C  
ATOM    453  C   VAL A  65      35.844  -4.705  -8.678  1.00 13.78           C  
ATOM    454  O   VAL A  65      36.898  -5.330  -8.541  1.00 13.83           O  
ATOM    455  CB  VAL A  65      35.753  -2.776 -10.330  1.00 15.78           C  
ATOM    456  CG1 VAL A  65      37.222  -2.511 -10.067  1.00 17.99           C  
ATOM    457  CG2 VAL A  65      35.443  -2.424 -11.769  1.00 11.99           C  
ATOM    458  N   THR A  66      35.090  -4.453  -7.606  1.00 12.60           N  
ATOM    459  CA  THR A  66      35.459  -4.920  -6.285  1.00 11.06           C  
ATOM    460  C   THR A  66      35.430  -6.423  -6.294  1.00  9.89           C  
ATOM    461  O   THR A  66      36.329  -7.050  -5.739  1.00 14.26           O  
ATOM    462  CB  THR A  66      34.489  -4.372  -5.249  1.00 15.98           C  
ATOM    463  OG1 THR A  66      34.673  -2.961  -5.278  1.00 19.97           O  
ATOM    464  CG2 THR A  66      34.738  -4.896  -3.843  1.00  9.16           C  
ATOM    465  N   GLY A  67      34.460  -7.039  -6.953  1.00 11.81           N  
ATOM    466  CA  GLY A  67      34.435  -8.488  -7.059  1.00 15.37           C  
ATOM    467  C   GLY A  67      35.667  -9.001  -7.789  1.00 18.52           C  
ATOM    468  O   GLY A  67      36.337  -9.940  -7.342  1.00 22.04           O  
ATOM    469  N   ALA A  68      36.036  -8.368  -8.899  1.00 16.65           N  
ATOM    470  CA  ALA A  68      37.188  -8.810  -9.658  1.00 13.77           C  
ATOM    471  C   ALA A  68      38.478  -8.725  -8.869  1.00 15.60           C  
ATOM    472  O   ALA A  68      39.375  -9.576  -8.953  1.00 16.71           O  
ATOM    473  CB  ALA A  68      37.325  -7.951 -10.906  1.00 18.29           C  
ATOM    474  N   GLN A  69      38.554  -7.690  -8.048  1.00 15.37           N  
ATOM    475  CA  GLN A  69      39.719  -7.442  -7.219  1.00 17.47           C  
ATOM    476  C   GLN A  69      40.011  -8.600  -6.256  1.00 15.00           C  
ATOM    477  O   GLN A  69      41.167  -8.852  -5.882  1.00 13.41           O  
ATOM    478  CB  GLN A  69      39.464  -6.141  -6.487  1.00 22.70           C  
ATOM    479  CG  GLN A  69      40.598  -5.719  -5.585  1.00 32.67           C  
ATOM    480  CD  GLN A  69      41.962  -5.576  -6.232  1.00 41.81           C  
ATOM    481  OE1 GLN A  69      42.143  -5.125  -7.355  1.00 51.75           O  
ATOM    482  NE2 GLN A  69      43.008  -5.973  -5.502  1.00 40.85           N  
ATOM    483  N   TYR A  70      38.997  -9.359  -5.849  1.00 15.41           N  
ATOM    484  CA  TYR A  70      39.235 -10.506  -5.009  1.00 19.77           C  
ATOM    485  C   TYR A  70      40.099 -11.534  -5.694  1.00 22.67           C  
ATOM    486  O   TYR A  70      40.769 -12.270  -4.972  1.00 25.71           O  
ATOM    487  CB  TYR A  70      37.927 -11.155  -4.580  1.00 14.26           C  
ATOM    488  CG  TYR A  70      37.272 -10.315  -3.505  1.00 14.45           C  
ATOM    489  CD1 TYR A  70      37.908 -10.118  -2.271  1.00 18.18           C  
ATOM    490  CD2 TYR A  70      36.056  -9.712  -3.772  1.00 12.78           C  
ATOM    491  CE1 TYR A  70      37.317  -9.301  -1.304  1.00 12.77           C  
ATOM    492  CE2 TYR A  70      35.466  -8.898  -2.808  1.00 16.18           C  
ATOM    493  CZ  TYR A  70      36.099  -8.698  -1.588  1.00 10.56           C  
ATOM    494  OH  TYR A  70      35.535  -7.879  -0.636  1.00 18.46           O  
ATOM    495  N   MET A  71      40.219 -11.591  -7.023  1.00 22.30           N  
ATOM    496  CA  MET A  71      41.128 -12.540  -7.637  1.00 21.31           C  
ATOM    497  C   MET A  71      42.541 -12.147  -7.228  1.00 20.77           C  
ATOM    498  O   MET A  71      43.380 -13.020  -6.987  1.00 24.58           O  
ATOM    499  CB  MET A  71      40.995 -12.513  -9.166  1.00 23.96           C  
ATOM    500  CG  MET A  71      41.840 -13.595  -9.874  1.00 26.59           C  
ATOM    501  SD  MET A  71      41.793 -13.609 -11.688  1.00 33.70           S  
ATOM    502  CE  MET A  71      42.926 -12.350 -12.197  1.00 16.07           C  
ATOM    503  N   GLU A  72      42.805 -10.840  -7.087  1.00 17.83           N  
ATOM    504  CA  GLU A  72      44.105 -10.367  -6.649  1.00 18.54           C  
ATOM    505  C   GLU A  72      44.359 -10.782  -5.208  1.00 16.81           C  
ATOM    506  O   GLU A  72      45.397 -11.337  -4.869  1.00 18.70           O  
ATOM    507  CB  GLU A  72      44.201  -8.839  -6.715  1.00 17.49           C  
ATOM    508  CG  GLU A  72      43.865  -8.284  -8.086  1.00 19.75           C  
ATOM    509  CD  GLU A  72      44.676  -8.894  -9.207  1.00 15.68           C  
ATOM    510  OE1 GLU A  72      45.875  -8.645  -9.266  1.00 14.70           O  
ATOM    511  OE2 GLU A  72      44.118  -9.633 -10.015  1.00 16.28           O  
ATOM    512  N   HIS A  73      43.389 -10.485  -4.345  1.00 19.07           N  
ATOM    513  CA  HIS A  73      43.465 -10.788  -2.927  1.00 18.87           C  
ATOM    514  C   HIS A  73      43.699 -12.246  -2.639  1.00 18.80           C  
ATOM    515  O   HIS A  73      44.584 -12.580  -1.855  1.00 20.88           O  
ATOM    516  CB  HIS A  73      42.184 -10.366  -2.234  1.00 13.65           C  
ATOM    517  CG  HIS A  73      42.097  -8.855  -2.173  1.00 13.46           C  
ATOM    518  ND1 HIS A  73      43.139  -8.050  -1.987  1.00 14.72           N  
ATOM    519  CD2 HIS A  73      40.980  -8.059  -2.290  1.00 16.38           C  
ATOM    520  CE1 HIS A  73      42.736  -6.808  -1.983  1.00  9.68           C  
ATOM    521  NE2 HIS A  73      41.436  -6.836  -2.165  1.00 17.95           N  
ATOM    522  N   LEU A  74      42.907 -13.095  -3.291  1.00 20.83           N  
ATOM    523  CA  LEU A  74      43.012 -14.537  -3.123  1.00 20.24           C  
ATOM    524  C   LEU A  74      44.360 -15.055  -3.597  1.00 21.54           C  
ATOM    525  O   LEU A  74      44.951 -15.930  -2.961  1.00 23.76           O  
ATOM    526  CB  LEU A  74      41.871 -15.224  -3.880  1.00 22.20           C  
ATOM    527  CG  LEU A  74      40.484 -15.024  -3.229  1.00 24.88           C  
ATOM    528  CD1 LEU A  74      39.387 -15.400  -4.185  1.00 28.51           C  
ATOM    529  CD2 LEU A  74      40.329 -15.913  -2.009  1.00 32.72           C  
ATOM    530  N   ARG A  75      44.912 -14.510  -4.677  1.00 20.50           N  
ATOM    531  CA  ARG A  75      46.244 -14.920  -5.109  1.00 21.56           C  
ATOM    532  C   ARG A  75      47.323 -14.386  -4.157  1.00 21.25           C  
ATOM    533  O   ARG A  75      48.209 -15.103  -3.688  1.00 22.82           O  
ATOM    534  CB  ARG A  75      46.502 -14.400  -6.529  1.00 22.92           C  
ATOM    535  CG  ARG A  75      47.862 -14.790  -7.104  1.00 21.50           C  
ATOM    536  CD  ARG A  75      48.115 -14.175  -8.478  1.00 30.65           C  
ATOM    537  NE  ARG A  75      48.520 -12.774  -8.420  1.00 33.78           N  
ATOM    538  CZ  ARG A  75      47.748 -11.794  -8.918  1.00 42.85           C  
ATOM    539  NH1 ARG A  75      46.561 -12.037  -9.498  1.00 36.70           N  
ATOM    540  NH2 ARG A  75      48.175 -10.537  -8.841  1.00 38.15           N  
ATOM    541  N   GLU A  76      47.259 -13.095  -3.860  1.00 19.81           N  
ATOM    542  CA  GLU A  76      48.255 -12.471  -3.013  1.00 20.03           C  
ATOM    543  C   GLU A  76      48.238 -12.909  -1.553  1.00 21.63           C  
ATOM    544  O   GLU A  76      49.275 -12.766  -0.890  1.00 20.95           O  
ATOM    545  CB  GLU A  76      48.066 -10.983  -3.109  1.00 20.73           C  
ATOM    546  CG  GLU A  76      48.400 -10.514  -4.516  1.00 26.70           C  
ATOM    547  CD  GLU A  76      48.029  -9.076  -4.851  1.00 31.02           C  
ATOM    548  OE1 GLU A  76      47.253  -8.439  -4.146  1.00 34.13           O  
ATOM    549  OE2 GLU A  76      48.512  -8.572  -5.847  1.00 29.75           O  
ATOM    550  N   SER A  77      47.139 -13.459  -1.004  1.00 20.31           N  
ATOM    551  CA  SER A  77      47.083 -13.893   0.383  1.00 19.83           C  
ATOM    552  C   SER A  77      48.168 -14.909   0.695  1.00 23.43           C  
ATOM    553  O   SER A  77      48.732 -14.883   1.798  1.00 27.59           O  
ATOM    554  CB  SER A  77      45.734 -14.505   0.688  1.00 10.61           C  
ATOM    555  OG  SER A  77      45.529 -15.578  -0.186  1.00 18.30           O  
ATOM    556  N   ALA A  78      48.533 -15.760  -0.273  1.00 22.10           N  
ATOM    557  CA  ALA A  78      49.564 -16.762  -0.087  1.00 19.89           C  
ATOM    558  C   ALA A  78      50.914 -16.206   0.345  1.00 20.53           C  
ATOM    559  O   ALA A  78      51.599 -16.846   1.133  1.00 25.47           O  
ATOM    560  CB  ALA A  78      49.772 -17.535  -1.370  1.00 17.51           C  
ATOM    561  N   GLY A  79      51.319 -14.997  -0.020  1.00 22.07           N  
ATOM    562  CA  GLY A  79      52.625 -14.465   0.344  1.00 20.39           C  
ATOM    563  C   GLY A  79      52.678 -14.042   1.799  1.00 24.21           C  
ATOM    564  O   GLY A  79      53.724 -13.672   2.332  1.00 24.95           O  
ATOM    565  N   PHE A  80      51.518 -14.031   2.444  1.00 22.84           N  
ATOM    566  CA  PHE A  80      51.437 -13.695   3.841  1.00 22.23           C  
ATOM    567  C   PHE A  80      51.065 -14.946   4.631  1.00 24.75           C  
ATOM    568  O   PHE A  80      50.706 -14.851   5.802  1.00 27.68           O  
ATOM    569  CB  PHE A  80      50.401 -12.585   4.018  1.00 18.92           C  
ATOM    570  CG  PHE A  80      50.905 -11.287   3.402  1.00 21.83           C  
ATOM    571  CD1 PHE A  80      50.714 -11.038   2.038  1.00 20.02           C  
ATOM    572  CD2 PHE A  80      51.582 -10.353   4.189  1.00 22.09           C  
ATOM    573  CE1 PHE A  80      51.203  -9.865   1.471  1.00 17.07           C  
ATOM    574  CE2 PHE A  80      52.069  -9.177   3.615  1.00 19.82           C  
ATOM    575  CZ  PHE A  80      51.875  -8.935   2.257  1.00 20.25           C  
ATOM    576  N   GLY A  81      51.110 -16.143   4.054  1.00 24.75           N  
ATOM    577  CA  GLY A  81      50.879 -17.347   4.819  1.00 22.15           C  
ATOM    578  C   GLY A  81      49.466 -17.880   4.783  1.00 23.56           C  
ATOM    579  O   GLY A  81      49.177 -18.802   5.546  1.00 22.97           O  
ATOM    580  N   TRP A  82      48.531 -17.384   3.975  1.00 24.77           N  
ATOM    581  CA  TRP A  82      47.181 -17.943   3.969  1.00 24.34           C  
ATOM    582  C   TRP A  82      47.146 -19.080   2.979  1.00 26.45           C  
ATOM    583  O   TRP A  82      47.596 -18.905   1.848  1.00 27.82           O  
ATOM    584  CB  TRP A  82      46.164 -16.875   3.568  1.00 24.83           C  
ATOM    585  CG  TRP A  82      45.971 -15.877   4.688  1.00 16.98           C  
ATOM    586  CD1 TRP A  82      46.720 -14.737   4.787  1.00 21.58           C  
ATOM    587  CD2 TRP A  82      45.094 -16.038   5.718  1.00 18.86           C  
ATOM    588  NE1 TRP A  82      46.320 -14.177   5.903  1.00 16.69           N  
ATOM    589  CE2 TRP A  82      45.364 -14.906   6.492  1.00 16.25           C  
ATOM    590  CE3 TRP A  82      44.131 -16.971   6.120  1.00 22.23           C  
ATOM    591  CZ2 TRP A  82      44.665 -14.682   7.679  1.00 19.27           C  
ATOM    592  CZ3 TRP A  82      43.431 -16.744   7.309  1.00 19.17           C  
ATOM    593  CH2 TRP A  82      43.701 -15.612   8.082  1.00 12.73           C  
ATOM    594  N   GLU A  83      46.671 -20.254   3.347  1.00 28.48           N  
ATOM    595  CA  GLU A  83      46.633 -21.373   2.435  1.00 29.52           C  
ATOM    596  C   GLU A  83      45.248 -21.974   2.444  1.00 31.06           C  
ATOM    597  O   GLU A  83      44.541 -21.942   3.455  1.00 30.04           O  
ATOM    598  CB  GLU A  83      47.632 -22.441   2.847  1.00 35.90           C  
ATOM    599  CG  GLU A  83      49.110 -22.031   2.920  1.00 51.39           C  
ATOM    600  CD  GLU A  83      49.708 -21.346   1.680  1.00 70.06           C  
ATOM    601  OE1 GLU A  83      49.429 -21.751   0.541  1.00 69.83           O  
ATOM    602  OE2 GLU A  83      50.466 -20.385   1.863  1.00 76.12           O  
ATOM    603  N   PHE A  84      44.793 -22.411   1.285  1.00 30.68           N  
ATOM    604  CA  PHE A  84      43.547 -23.138   1.163  1.00 31.85           C  
ATOM    605  C   PHE A  84      43.674 -24.032  -0.059  1.00 32.91           C  
ATOM    606  O   PHE A  84      44.664 -23.967  -0.789  1.00 30.82           O  
ATOM    607  CB  PHE A  84      42.353 -22.168   1.018  1.00 28.99           C  
ATOM    608  CG  PHE A  84      42.369 -21.138  -0.110  1.00 32.14           C  
ATOM    609  CD1 PHE A  84      43.075 -19.931   0.024  1.00 27.57           C  
ATOM    610  CD2 PHE A  84      41.632 -21.386  -1.276  1.00 30.75           C  
ATOM    611  CE1 PHE A  84      43.032 -18.987  -1.006  1.00 27.50           C  
ATOM    612  CE2 PHE A  84      41.597 -20.435  -2.296  1.00 31.49           C  
ATOM    613  CZ  PHE A  84      42.296 -19.237  -2.161  1.00 29.20           C  
ATOM    614  N   ASP A  85      42.712 -24.905  -0.366  1.00 35.44           N  
ATOM    615  CA  ASP A  85      42.857 -25.745  -1.545  1.00 37.39           C  
ATOM    616  C   ASP A  85      42.555 -24.884  -2.754  1.00 36.09           C  
ATOM    617  O   ASP A  85      41.410 -24.726  -3.174  1.00 31.96           O  
ATOM    618  CB  ASP A  85      41.890 -26.935  -1.525  1.00 41.79           C  
ATOM    619  CG  ASP A  85      42.213 -28.042  -2.537  1.00 48.41           C  
ATOM    620  OD1 ASP A  85      43.204 -27.952  -3.273  1.00 45.35           O  
ATOM    621  OD2 ASP A  85      41.462 -29.020  -2.565  1.00 55.90           O  
ATOM    622  N   ARG A  86      43.598 -24.327  -3.357  1.00 37.18           N  
ATOM    623  CA  ARG A  86      43.384 -23.409  -4.457  1.00 41.13           C  
ATOM    624  C   ARG A  86      42.820 -24.056  -5.714  1.00 42.59           C  
ATOM    625  O   ARG A  86      42.427 -23.347  -6.637  1.00 45.11           O  
ATOM    626  CB  ARG A  86      44.705 -22.673  -4.745  1.00 40.87           C  
ATOM    627  CG  ARG A  86      44.904 -21.567  -3.698  1.00 47.36           C  
ATOM    628  CD  ARG A  86      45.988 -20.528  -4.017  1.00 53.72           C  
ATOM    629  NE  ARG A  86      45.897 -19.324  -3.182  1.00 51.88           N  
ATOM    630  CZ  ARG A  86      46.430 -19.255  -1.955  1.00 54.82           C  
ATOM    631  NH1 ARG A  86      47.073 -20.292  -1.420  1.00 58.44           N  
ATOM    632  NH2 ARG A  86      46.335 -18.134  -1.243  1.00 54.49           N  
ATOM    633  N   THR A  87      42.719 -25.388  -5.751  1.00 43.67           N  
ATOM    634  CA  THR A  87      42.110 -26.079  -6.876  1.00 44.47           C  
ATOM    635  C   THR A  87      40.591 -26.075  -6.728  1.00 41.63           C  
ATOM    636  O   THR A  87      39.887 -26.485  -7.649  1.00 45.50           O  
ATOM    637  CB  THR A  87      42.666 -27.542  -6.969  1.00 45.73           C  
ATOM    638  OG1 THR A  87      42.419 -28.205  -5.737  1.00 46.34           O  
ATOM    639  CG2 THR A  87      44.171 -27.562  -7.234  1.00 46.26           C  
ATOM    640  N   THR A  88      40.031 -25.630  -5.604  1.00 39.83           N  
ATOM    641  CA  THR A  88      38.583 -25.577  -5.484  1.00 38.92           C  
ATOM    642  C   THR A  88      38.013 -24.190  -5.783  1.00 39.21           C  
ATOM    643  O   THR A  88      36.789 -23.967  -5.728  1.00 39.84           O  
ATOM    644  CB  THR A  88      38.162 -26.024  -4.057  1.00 39.88           C  
ATOM    645  OG1 THR A  88      38.817 -25.205  -3.084  1.00 33.02           O  
ATOM    646  CG2 THR A  88      38.510 -27.480  -3.828  1.00 42.45           C  
ATOM    647  N   LEU A  89      38.920 -23.262  -6.097  1.00 36.82           N  
ATOM    648  CA  LEU A  89      38.568 -21.872  -6.278  1.00 36.72           C  
ATOM    649  C   LEU A  89      37.792 -21.597  -7.544  1.00 37.75           C  
ATOM    650  O   LEU A  89      38.299 -21.902  -8.624  1.00 40.27           O  
ATOM    651  CB  LEU A  89      39.837 -21.028  -6.283  1.00 28.75           C  
ATOM    652  CG  LEU A  89      39.685 -19.516  -6.333  1.00 26.95           C  
ATOM    653  CD1 LEU A  89      38.877 -19.021  -5.135  1.00 22.28           C  
ATOM    654  CD2 LEU A  89      41.065 -18.901  -6.376  1.00 24.75           C  
ATOM    655  N   ARG A  90      36.585 -21.039  -7.463  1.00 39.35           N  
ATOM    656  CA  ARG A  90      35.909 -20.613  -8.668  1.00 39.14           C  
ATOM    657  C   ARG A  90      35.143 -19.310  -8.462  1.00 35.83           C  
ATOM    658  O   ARG A  90      34.821 -18.926  -7.336  1.00 35.64           O  
ATOM    659  CB  ARG A  90      35.010 -21.752  -9.137  1.00 40.87           C  
ATOM    660  CG  ARG A  90      33.690 -22.178  -8.533  1.00 54.08           C  
ATOM    661  CD  ARG A  90      33.143 -23.091  -9.672  1.00 70.24           C  
ATOM    662  NE  ARG A  90      31.960 -22.579 -10.380  1.00 81.10           N  
ATOM    663  CZ  ARG A  90      31.908 -21.458 -11.120  1.00 82.35           C  
ATOM    664  NH1 ARG A  90      32.983 -20.709 -11.349  1.00 88.58           N  
ATOM    665  NH2 ARG A  90      30.756 -21.106 -11.685  1.00 79.91           N  
ATOM    666  N   ALA A  91      34.962 -18.541  -9.534  1.00 33.31           N  
ATOM    667  CA  ALA A  91      34.254 -17.273  -9.492  1.00 32.74           C  
ATOM    668  C   ALA A  91      32.852 -17.530  -9.992  1.00 32.13           C  
ATOM    669  O   ALA A  91      32.698 -18.083 -11.072  1.00 36.94           O  
ATOM    670  CB  ALA A  91      34.923 -16.280 -10.407  1.00 29.30           C  
ATOM    671  N   GLU A  92      31.790 -17.147  -9.329  1.00 30.64           N  
ATOM    672  CA  GLU A  92      30.484 -17.491  -9.797  1.00 30.45           C  
ATOM    673  C   GLU A  92      29.823 -16.222 -10.307  1.00 29.76           C  
ATOM    674  O   GLU A  92      29.157 -15.505  -9.547  1.00 32.05           O  
ATOM    675  CB  GLU A  92      29.809 -18.131  -8.605  1.00 39.48           C  
ATOM    676  CG  GLU A  92      28.406 -18.687  -8.798  1.00 56.65           C  
ATOM    677  CD  GLU A  92      28.309 -19.963  -9.624  1.00 65.42           C  
ATOM    678  OE1 GLU A  92      29.061 -20.909  -9.358  1.00 68.90           O  
ATOM    679  OE2 GLU A  92      27.460 -20.005 -10.520  1.00 67.99           O  
ATOM    680  N   TRP A  93      29.942 -15.958 -11.615  1.00 26.76           N  
ATOM    681  CA  TRP A  93      29.387 -14.782 -12.278  1.00 24.75           C  
ATOM    682  C   TRP A  93      27.921 -14.525 -11.952  1.00 24.51           C  
ATOM    683  O   TRP A  93      27.535 -13.406 -11.597  1.00 26.25           O  
ATOM    684  CB  TRP A  93      29.565 -14.941 -13.793  1.00 22.52           C  
ATOM    685  CG  TRP A  93      29.045 -13.785 -14.640  1.00 19.75           C  
ATOM    686  CD1 TRP A  93      27.809 -13.856 -15.233  1.00 15.83           C  
ATOM    687  CD2 TRP A  93      29.706 -12.615 -14.914  1.00 12.58           C  
ATOM    688  NE1 TRP A  93      27.685 -12.736 -15.890  1.00 17.46           N  
ATOM    689  CE2 TRP A  93      28.776 -11.970 -15.731  1.00 21.16           C  
ATOM    690  CE3 TRP A  93      30.917 -12.005 -14.606  1.00 20.25           C  
ATOM    691  CZ2 TRP A  93      29.046 -10.709 -16.260  1.00 24.75           C  
ATOM    692  CZ3 TRP A  93      31.194 -10.739 -15.133  1.00 21.19           C  
ATOM    693  CH2 TRP A  93      30.261 -10.096 -15.952  1.00 19.43           C  
ATOM    694  N   LYS A  94      27.089 -15.559 -11.993  1.00 28.12           N  
ATOM    695  CA  LYS A  94      25.669 -15.433 -11.687  1.00 29.57           C  
ATOM    696  C   LYS A  94      25.358 -14.867 -10.305  1.00 29.27           C  
ATOM    697  O   LYS A  94      24.412 -14.081 -10.130  1.00 30.32           O  
ATOM    698  CB  LYS A  94      25.068 -16.806 -11.883  1.00 35.91           C  
ATOM    699  CG  LYS A  94      24.688 -16.958 -13.352  1.00 53.55           C  
ATOM    700  CD  LYS A  94      24.805 -18.398 -13.840  1.00 62.57           C  
ATOM    701  CE  LYS A  94      24.016 -18.617 -15.140  1.00 65.19           C  
ATOM    702  NZ  LYS A  94      24.261 -19.936 -15.709  1.00 67.86           N  
ATOM    703  N   ASN A  95      26.208 -15.178  -9.323  1.00 27.59           N  
ATOM    704  CA  ASN A  95      26.010 -14.631  -8.001  1.00 24.42           C  
ATOM    705  C   ASN A  95      26.365 -13.153  -7.992  1.00 22.29           C  
ATOM    706  O   ASN A  95      25.658 -12.354  -7.381  1.00 23.66           O  
ATOM    707  CB  ASN A  95      26.870 -15.331  -6.976  1.00 31.87           C  
ATOM    708  CG  ASN A  95      26.473 -14.788  -5.609  1.00 50.21           C  
ATOM    709  OD1 ASN A  95      25.368 -15.037  -5.118  1.00 66.82           O  
ATOM    710  ND2 ASN A  95      27.326 -13.982  -4.982  1.00 60.55           N  
ATOM    711  N   LEU A  96      27.435 -12.764  -8.687  1.00 20.19           N  
ATOM    712  CA  LEU A  96      27.829 -11.372  -8.788  1.00 18.06           C  
ATOM    713  C   LEU A  96      26.728 -10.558  -9.432  1.00 18.49           C  
ATOM    714  O   LEU A  96      26.371  -9.504  -8.904  1.00 24.46           O  
ATOM    715  CB  LEU A  96      29.089 -11.212  -9.625  1.00 15.18           C  
ATOM    716  CG  LEU A  96      29.561  -9.760  -9.804  1.00 21.42           C  
ATOM    717  CD1 LEU A  96      30.087  -9.216  -8.479  1.00 17.15           C  
ATOM    718  CD2 LEU A  96      30.626  -9.703 -10.874  1.00 12.49           C  
ATOM    719  N   ILE A  97      26.117 -11.014 -10.530  1.00 19.07           N  
ATOM    720  CA  ILE A  97      25.037 -10.280 -11.178  1.00 17.39           C  
ATOM    721  C   ILE A  97      23.814 -10.237 -10.284  1.00 19.44           C  
ATOM    722  O   ILE A  97      23.120  -9.221 -10.200  1.00 21.13           O  
ATOM    723  CB  ILE A  97      24.691 -10.943 -12.554  1.00 16.94           C  
ATOM    724  CG1 ILE A  97      25.897 -10.849 -13.487  1.00 13.68           C  
ATOM    725  CG2 ILE A  97      23.493 -10.262 -13.203  1.00 16.28           C  
ATOM    726  CD1 ILE A  97      26.496  -9.435 -13.655  1.00 22.25           C  
ATOM    727  N   ALA A  98      23.500 -11.331  -9.593  1.00 21.75           N  
ATOM    728  CA  ALA A  98      22.358 -11.356  -8.693  1.00 19.01           C  
ATOM    729  C   ALA A  98      22.480 -10.345  -7.546  1.00 17.31           C  
ATOM    730  O   ALA A  98      21.535  -9.582  -7.318  1.00 16.57           O  
ATOM    731  CB  ALA A  98      22.218 -12.757  -8.125  1.00 21.13           C  
ATOM    732  N   VAL A  99      23.617 -10.230  -6.856  1.00 16.97           N  
ATOM    733  CA  VAL A  99      23.733  -9.261  -5.775  1.00 18.34           C  
ATOM    734  C   VAL A  99      23.855  -7.851  -6.337  1.00 22.06           C  
ATOM    735  O   VAL A  99      23.382  -6.914  -5.684  1.00 26.15           O  
ATOM    736  CB  VAL A  99      24.958  -9.551  -4.817  1.00 18.91           C  
ATOM    737  CG1 VAL A  99      24.802 -10.972  -4.283  1.00 17.30           C  
ATOM    738  CG2 VAL A  99      26.305  -9.384  -5.498  1.00 16.72           C  
ATOM    739  N   LYS A 100      24.424  -7.618  -7.538  1.00 22.80           N  
ATOM    740  CA  LYS A 100      24.435  -6.288  -8.167  1.00 16.51           C  
ATOM    741  C   LYS A 100      23.008  -5.854  -8.491  1.00 14.43           C  
ATOM    742  O   LYS A 100      22.599  -4.718  -8.227  1.00 14.97           O  
ATOM    743  CB  LYS A 100      25.303  -6.362  -9.427  1.00 18.25           C  
ATOM    744  CG  LYS A 100      25.400  -5.135 -10.324  1.00 16.40           C  
ATOM    745  CD  LYS A 100      24.302  -5.069 -11.373  1.00 15.99           C  
ATOM    746  CE  LYS A 100      24.477  -6.111 -12.474  1.00 23.06           C  
ATOM    747  NZ  LYS A 100      23.368  -6.043 -13.412  1.00 12.49           N  
ATOM    748  N   ASP A 101      22.194  -6.773  -9.019  1.00 16.24           N  
ATOM    749  CA  ASP A 101      20.816  -6.480  -9.356  1.00 16.51           C  
ATOM    750  C   ASP A 101      19.989  -6.058  -8.161  1.00 20.29           C  
ATOM    751  O   ASP A 101      19.191  -5.113  -8.266  1.00 23.86           O  
ATOM    752  CB  ASP A 101      20.175  -7.692 -10.009  1.00 17.00           C  
ATOM    753  CG  ASP A 101      20.495  -7.907 -11.488  1.00 24.36           C  
ATOM    754  OD1 ASP A 101      21.148  -7.082 -12.105  1.00 20.58           O  
ATOM    755  OD2 ASP A 101      20.069  -8.903 -12.055  1.00 29.86           O  
ATOM    756  N   GLU A 102      20.173  -6.725  -7.023  1.00 17.41           N  
ATOM    757  CA  GLU A 102      19.493  -6.370  -5.791  1.00 17.01           C  
ATOM    758  C   GLU A 102      19.955  -5.014  -5.288  1.00 14.53           C  
ATOM    759  O   GLU A 102      19.103  -4.176  -4.993  1.00 18.60           O  
ATOM    760  CB  GLU A 102      19.779  -7.422  -4.762  1.00 24.55           C  
ATOM    761  CG  GLU A 102      19.069  -7.197  -3.439  1.00 46.81           C  
ATOM    762  CD  GLU A 102      19.273  -8.360  -2.479  1.00 59.70           C  
ATOM    763  OE1 GLU A 102      20.376  -8.512  -1.941  1.00 62.24           O  
ATOM    764  OE2 GLU A 102      18.315  -9.114  -2.287  1.00 68.82           O  
ATOM    765  N   ALA A 103      21.260  -4.760  -5.264  1.00 12.09           N  
ATOM    766  CA  ALA A 103      21.773  -3.468  -4.848  1.00 13.44           C  
ATOM    767  C   ALA A 103      21.207  -2.327  -5.683  1.00 17.55           C  
ATOM    768  O   ALA A 103      20.763  -1.308  -5.146  1.00 22.97           O  
ATOM    769  CB  ALA A 103      23.281  -3.440  -4.985  1.00 11.84           C  
ATOM    770  N   VAL A 104      21.159  -2.459  -7.021  1.00 21.25           N  
ATOM    771  CA  VAL A 104      20.636  -1.412  -7.900  1.00 17.83           C  
ATOM    772  C   VAL A 104      19.132  -1.321  -7.718  1.00 16.65           C  
ATOM    773  O   VAL A 104      18.584  -0.227  -7.588  1.00 18.94           O  
ATOM    774  CB  VAL A 104      21.008  -1.734  -9.375  1.00 20.42           C  
ATOM    775  CG1 VAL A 104      20.412  -0.693 -10.301  1.00 19.88           C  
ATOM    776  CG2 VAL A 104      22.521  -1.671  -9.570  1.00 15.47           C  
ATOM    777  N   LEU A 105      18.422  -2.441  -7.616  1.00 17.59           N  
ATOM    778  CA  LEU A 105      16.986  -2.421  -7.408  1.00 18.02           C  
ATOM    779  C   LEU A 105      16.585  -1.650  -6.167  1.00 20.03           C  
ATOM    780  O   LEU A 105      15.592  -0.916  -6.184  1.00 20.20           O  
ATOM    781  CB  LEU A 105      16.481  -3.833  -7.302  1.00 19.26           C  
ATOM    782  CG  LEU A 105      15.004  -4.050  -7.010  1.00 25.60           C  
ATOM    783  CD1 LEU A 105      14.125  -3.390  -8.053  1.00 29.90           C  
ATOM    784  CD2 LEU A 105      14.748  -5.529  -7.002  1.00 22.34           C  
ATOM    785  N   ASN A 106      17.357  -1.766  -5.083  1.00 21.80           N  
ATOM    786  CA  ASN A 106      17.045  -1.062  -3.849  1.00 21.03           C  
ATOM    787  C   ASN A 106      17.176   0.436  -3.981  1.00 20.22           C  
ATOM    788  O   ASN A 106      16.401   1.156  -3.359  1.00 26.03           O  
ATOM    789  CB  ASN A 106      17.942  -1.564  -2.707  1.00 27.32           C  
ATOM    790  CG  ASN A 106      17.642  -3.017  -2.279  1.00 38.40           C  
ATOM    791  OD1 ASN A 106      18.496  -3.717  -1.723  1.00 39.12           O  
ATOM    792  ND2 ASN A 106      16.463  -3.617  -2.491  1.00 40.54           N  
ATOM    793  N   ILE A 107      18.088   0.958  -4.811  1.00 24.23           N  
ATOM    794  CA  ILE A 107      18.208   2.392  -5.069  1.00 19.97           C  
ATOM    795  C   ILE A 107      17.061   2.802  -5.995  1.00 20.41           C  
ATOM    796  O   ILE A 107      16.449   3.861  -5.804  1.00 25.01           O  
ATOM    797  CB  ILE A 107      19.576   2.713  -5.724  1.00 16.75           C  
ATOM    798  CG1 ILE A 107      20.744   2.281  -4.852  1.00 16.60           C  
ATOM    799  CG2 ILE A 107      19.686   4.215  -5.883  1.00 13.57           C  
ATOM    800  CD1 ILE A 107      22.147   2.314  -5.522  1.00 13.38           C  
ATOM    801  N   ASN A 108      16.700   1.990  -6.998  1.00 19.38           N  
ATOM    802  CA  ASN A 108      15.539   2.289  -7.826  1.00 22.75           C  
ATOM    803  C   ASN A 108      14.317   2.472  -6.932  1.00 25.89           C  
ATOM    804  O   ASN A 108      13.593   3.468  -7.047  1.00 25.71           O  
ATOM    805  CB  ASN A 108      15.176   1.174  -8.794  1.00 23.79           C  
ATOM    806  CG  ASN A 108      16.134   0.962  -9.948  1.00 18.38           C  
ATOM    807  OD1 ASN A 108      16.394  -0.176 -10.350  1.00 19.71           O  
ATOM    808  ND2 ASN A 108      16.684   1.980 -10.582  1.00 21.87           N  
ATOM    809  N   LYS A 109      14.118   1.550  -5.974  1.00 27.69           N  
ATOM    810  CA  LYS A 109      13.008   1.636  -5.033  1.00 27.42           C  
ATOM    811  C   LYS A 109      13.074   2.855  -4.137  1.00 25.19           C  
ATOM    812  O   LYS A 109      12.024   3.463  -3.883  1.00 26.95           O  
ATOM    813  CB  LYS A 109      12.936   0.395  -4.144  1.00 28.60           C  
ATOM    814  CG  LYS A 109      12.304  -0.784  -4.886  1.00 37.45           C  
ATOM    815  CD  LYS A 109      12.138  -2.007  -3.981  1.00 53.39           C  
ATOM    816  CE  LYS A 109      11.358  -3.118  -4.700  1.00 56.82           C  
ATOM    817  NZ  LYS A 109      11.136  -4.301  -3.875  1.00 63.79           N  
ATOM    818  N   SER A 110      14.226   3.309  -3.662  1.00 22.91           N  
ATOM    819  CA  SER A 110      14.182   4.478  -2.818  1.00 26.05           C  
ATOM    820  C   SER A 110      13.916   5.785  -3.563  1.00 28.87           C  
ATOM    821  O   SER A 110      13.274   6.688  -3.002  1.00 30.88           O  
ATOM    822  CB  SER A 110      15.470   4.570  -2.024  1.00 23.46           C  
ATOM    823  OG  SER A 110      16.648   4.778  -2.775  1.00 33.35           O  
ATOM    824  N   TYR A 111      14.322   5.938  -4.829  1.00 29.26           N  
ATOM    825  CA  TYR A 111      13.996   7.151  -5.558  1.00 27.10           C  
ATOM    826  C   TYR A 111      12.496   7.225  -5.762  1.00 25.97           C  
ATOM    827  O   TYR A 111      11.880   8.281  -5.644  1.00 27.26           O  
ATOM    828  CB  TYR A 111      14.711   7.173  -6.906  1.00 24.34           C  
ATOM    829  CG  TYR A 111      16.177   7.569  -6.785  1.00 19.87           C  
ATOM    830  CD1 TYR A 111      16.535   8.753  -6.130  1.00 22.62           C  
ATOM    831  CD2 TYR A 111      17.170   6.755  -7.331  1.00 18.87           C  
ATOM    832  CE1 TYR A 111      17.880   9.124  -6.020  1.00 22.00           C  
ATOM    833  CE2 TYR A 111      18.512   7.124  -7.223  1.00 15.38           C  
ATOM    834  CZ  TYR A 111      18.858   8.302  -6.570  1.00 17.33           C  
ATOM    835  OH  TYR A 111      20.188   8.648  -6.475  1.00 26.70           O  
ATOM    836  N   ASP A 112      11.869   6.076  -5.966  1.00 29.70           N  
ATOM    837  CA  ASP A 112      10.434   5.983  -6.125  1.00 34.31           C  
ATOM    838  C   ASP A 112       9.722   6.486  -4.860  1.00 35.53           C  
ATOM    839  O   ASP A 112       8.863   7.379  -4.890  1.00 35.26           O  
ATOM    840  CB  ASP A 112      10.133   4.524  -6.424  1.00 32.37           C  
ATOM    841  CG  ASP A 112       8.676   4.222  -6.736  1.00 42.54           C  
ATOM    842  OD1 ASP A 112       8.019   5.016  -7.411  1.00 52.12           O  
ATOM    843  OD2 ASP A 112       8.202   3.171  -6.308  1.00 51.24           O  
ATOM    844  N   GLU A 113      10.149   5.960  -3.715  1.00 36.82           N  
ATOM    845  CA  GLU A 113       9.650   6.373  -2.419  1.00 36.96           C  
ATOM    846  C   GLU A 113       9.840   7.875  -2.222  1.00 34.95           C  
ATOM    847  O   GLU A 113       8.909   8.552  -1.795  1.00 35.67           O  
ATOM    848  CB  GLU A 113      10.398   5.557  -1.408  1.00 39.02           C  
ATOM    849  CG  GLU A 113      10.283   6.029   0.010  1.00 62.39           C  
ATOM    850  CD  GLU A 113      11.591   5.835   0.748  1.00 74.71           C  
ATOM    851  OE1 GLU A 113      12.557   6.527   0.411  1.00 82.16           O  
ATOM    852  OE2 GLU A 113      11.644   4.991   1.644  1.00 84.62           O  
ATOM    853  N   MET A 114      11.000   8.417  -2.588  1.00 32.87           N  
ATOM    854  CA  MET A 114      11.302   9.838  -2.533  1.00 32.31           C  
ATOM    855  C   MET A 114      10.241  10.643  -3.269  1.00 35.15           C  
ATOM    856  O   MET A 114       9.811  11.697  -2.794  1.00 36.18           O  
ATOM    857  CB  MET A 114      12.669  10.096  -3.175  1.00 33.85           C  
ATOM    858  CG  MET A 114      13.034  11.565  -3.367  1.00 32.33           C  
ATOM    859  SD  MET A 114      14.459  11.892  -4.438  1.00 44.94           S  
ATOM    860  CE  MET A 114      13.638  11.918  -5.999  1.00 32.90           C  
ATOM    861  N   PHE A 115       9.804  10.169  -4.438  1.00 35.91           N  
ATOM    862  CA  PHE A 115       8.766  10.861  -5.174  1.00 38.25           C  
ATOM    863  C   PHE A 115       7.454  10.795  -4.405  1.00 43.00           C  
ATOM    864  O   PHE A 115       6.796  11.825  -4.249  1.00 44.14           O  
ATOM    865  CB  PHE A 115       8.599  10.246  -6.578  1.00 37.59           C  
ATOM    866  CG  PHE A 115       9.592  10.854  -7.559  1.00 30.16           C  
ATOM    867  CD1 PHE A 115       9.341  12.112  -8.114  1.00 29.46           C  
ATOM    868  CD2 PHE A 115      10.776  10.183  -7.865  1.00 30.53           C  
ATOM    869  CE1 PHE A 115      10.285  12.701  -8.958  1.00 25.41           C  
ATOM    870  CE2 PHE A 115      11.712  10.779  -8.708  1.00 31.27           C  
ATOM    871  CZ  PHE A 115      11.470  12.036  -9.257  1.00 27.53           C  
ATOM    872  N   ARG A 116       7.077   9.636  -3.841  1.00 45.05           N  
ATOM    873  CA  ARG A 116       5.846   9.524  -3.059  1.00 47.45           C  
ATOM    874  C   ARG A 116       5.816  10.452  -1.851  1.00 47.59           C  
ATOM    875  O   ARG A 116       4.771  10.923  -1.410  1.00 50.84           O  
ATOM    876  CB  ARG A 116       5.631   8.135  -2.483  1.00 51.34           C  
ATOM    877  CG  ARG A 116       5.463   6.899  -3.355  1.00 60.61           C  
ATOM    878  CD  ARG A 116       5.116   5.698  -2.444  1.00 69.27           C  
ATOM    879  NE  ARG A 116       6.175   5.219  -1.554  1.00 74.03           N  
ATOM    880  CZ  ARG A 116       6.276   5.537  -0.252  1.00 79.92           C  
ATOM    881  NH1 ARG A 116       5.416   6.350   0.374  1.00 78.63           N  
ATOM    882  NH2 ARG A 116       7.245   4.957   0.445  1.00 76.01           N  
ATOM    883  N   ASP A 117       6.981  10.635  -1.253  1.00 49.24           N  
ATOM    884  CA  ASP A 117       7.084  11.425  -0.051  1.00 50.65           C  
ATOM    885  C   ASP A 117       7.237  12.930  -0.264  1.00 51.86           C  
ATOM    886  O   ASP A 117       6.976  13.678   0.687  1.00 54.43           O  
ATOM    887  CB  ASP A 117       8.258  10.846   0.775  1.00 50.62           C  
ATOM    888  CG  ASP A 117       8.092   9.426   1.284  1.00 55.95           C  
ATOM    889  OD1 ASP A 117       7.053   8.780   1.018  1.00 51.47           O  
ATOM    890  OD2 ASP A 117       9.037   8.976   1.961  1.00 59.61           O  
ATOM    891  N   THR A 118       7.599  13.457  -1.438  1.00 50.78           N  
ATOM    892  CA  THR A 118       7.796  14.888  -1.555  1.00 47.07           C  
ATOM    893  C   THR A 118       6.647  15.585  -2.273  1.00 49.94           C  
ATOM    894  O   THR A 118       6.242  15.272  -3.398  1.00 52.90           O  
ATOM    895  CB  THR A 118       9.151  15.092  -2.248  1.00 41.35           C  
ATOM    896  OG1 THR A 118      10.119  14.314  -1.547  1.00 41.21           O  
ATOM    897  CG2 THR A 118       9.613  16.528  -2.186  1.00 37.76           C  
ATOM    898  N   GLU A 119       6.032  16.543  -1.584  1.00 53.43           N  
ATOM    899  CA  GLU A 119       4.966  17.344  -2.170  1.00 55.09           C  
ATOM    900  C   GLU A 119       5.545  18.250  -3.247  1.00 51.34           C  
ATOM    901  O   GLU A 119       6.575  18.901  -3.047  1.00 50.01           O  
ATOM    902  CB  GLU A 119       4.294  18.240  -1.128  1.00 64.31           C  
ATOM    903  CG  GLU A 119       3.694  17.481   0.051  1.00 74.76           C  
ATOM    904  CD  GLU A 119       2.530  16.578  -0.337  1.00 82.45           C  
ATOM    905  OE1 GLU A 119       1.411  17.087  -0.440  1.00 95.41           O  
ATOM    906  OE2 GLU A 119       2.742  15.377  -0.531  1.00 90.17           O  
ATOM    907  N   GLY A 120       4.885  18.302  -4.394  1.00 46.65           N  
ATOM    908  CA  GLY A 120       5.373  19.164  -5.447  1.00 41.80           C  
ATOM    909  C   GLY A 120       6.431  18.512  -6.314  1.00 37.47           C  
ATOM    910  O   GLY A 120       7.015  19.215  -7.123  1.00 38.95           O  
ATOM    911  N   LEU A 121       6.705  17.217  -6.235  1.00 33.56           N  
ATOM    912  CA  LEU A 121       7.687  16.587  -7.089  1.00 29.59           C  
ATOM    913  C   LEU A 121       6.936  15.466  -7.773  1.00 31.69           C  
ATOM    914  O   LEU A 121       6.478  14.551  -7.091  1.00 33.53           O  
ATOM    915  CB  LEU A 121       8.805  16.071  -6.216  1.00 27.51           C  
ATOM    916  CG  LEU A 121      10.092  15.560  -6.802  1.00 26.70           C  
ATOM    917  CD1 LEU A 121      10.728  16.630  -7.652  1.00 27.09           C  
ATOM    918  CD2 LEU A 121      11.037  15.183  -5.676  1.00 25.77           C  
ATOM    919  N   GLU A 122       6.700  15.496  -9.077  1.00 29.50           N  
ATOM    920  CA  GLU A 122       5.958  14.428  -9.702  1.00 28.98           C  
ATOM    921  C   GLU A 122       6.779  13.679 -10.721  1.00 28.28           C  
ATOM    922  O   GLU A 122       7.552  14.292 -11.453  1.00 28.43           O  
ATOM    923  CB  GLU A 122       4.727  15.024 -10.327  1.00 33.32           C  
ATOM    924  CG  GLU A 122       3.648  15.218  -9.262  1.00 48.51           C  
ATOM    925  CD  GLU A 122       2.343  15.771  -9.819  1.00 61.36           C  
ATOM    926  OE1 GLU A 122       1.622  15.031 -10.495  1.00 64.87           O  
ATOM    927  OE2 GLU A 122       2.051  16.945  -9.578  1.00 69.00           O  
ATOM    928  N   PHE A 123       6.694  12.353 -10.725  1.00 27.35           N  
ATOM    929  CA  PHE A 123       7.396  11.515 -11.672  1.00 27.29           C  
ATOM    930  C   PHE A 123       6.414  11.087 -12.769  1.00 27.17           C  
ATOM    931  O   PHE A 123       5.273  10.725 -12.474  1.00 26.05           O  
ATOM    932  CB  PHE A 123       7.972  10.272 -10.949  1.00 21.69           C  
ATOM    933  CG  PHE A 123       8.699   9.350 -11.917  1.00 21.38           C  
ATOM    934  CD1 PHE A 123       9.916   9.747 -12.467  1.00 16.53           C  
ATOM    935  CD2 PHE A 123       8.108   8.147 -12.309  1.00 18.47           C  
ATOM    936  CE1 PHE A 123      10.527   8.929 -13.415  1.00 21.56           C  
ATOM    937  CE2 PHE A 123       8.729   7.341 -13.257  1.00 15.62           C  
ATOM    938  CZ  PHE A 123       9.937   7.732 -13.813  1.00 16.74           C  
ATOM    939  N   PHE A 124       6.807  11.126 -14.045  1.00 26.26           N  
ATOM    940  CA  PHE A 124       5.984  10.669 -15.154  1.00 18.84           C  
ATOM    941  C   PHE A 124       6.813   9.653 -15.906  1.00 18.95           C  
ATOM    942  O   PHE A 124       7.980   9.877 -16.223  1.00 22.65           O  
ATOM    943  CB  PHE A 124       5.627  11.824 -16.070  1.00 18.86           C  
ATOM    944  CG  PHE A 124       4.678  12.798 -15.395  1.00 18.04           C  
ATOM    945  CD1 PHE A 124       3.310  12.535 -15.391  1.00 20.24           C  
ATOM    946  CD2 PHE A 124       5.174  13.922 -14.747  1.00 19.17           C  
ATOM    947  CE1 PHE A 124       2.436  13.401 -14.736  1.00 20.53           C  
ATOM    948  CE2 PHE A 124       4.297  14.785 -14.094  1.00 24.42           C  
ATOM    949  CZ  PHE A 124       2.928  14.528 -14.083  1.00 23.07           C  
ATOM    950  N   LEU A 125       6.229   8.490 -16.122  1.00 20.54           N  
ATOM    951  CA  LEU A 125       6.907   7.415 -16.803  1.00 22.21           C  
ATOM    952  C   LEU A 125       6.626   7.543 -18.282  1.00 22.28           C  
ATOM    953  O   LEU A 125       5.464   7.517 -18.674  1.00 23.95           O  
ATOM    954  CB  LEU A 125       6.374   6.107 -16.213  1.00 21.84           C  
ATOM    955  CG  LEU A 125       6.980   4.719 -16.455  1.00 23.99           C  
ATOM    956  CD1 LEU A 125       6.561   4.180 -17.805  1.00 30.02           C  
ATOM    957  CD2 LEU A 125       8.487   4.810 -16.306  1.00 24.60           C  
ATOM    958  N   GLY A 126       7.647   7.668 -19.106  1.00 24.36           N  
ATOM    959  CA  GLY A 126       7.474   7.748 -20.540  1.00 21.75           C  
ATOM    960  C   GLY A 126       8.680   8.430 -21.161  1.00 22.20           C  
ATOM    961  O   GLY A 126       9.698   8.698 -20.506  1.00 22.89           O  
ATOM    962  N   TRP A 127       8.561   8.714 -22.459  1.00 19.48           N  
ATOM    963  CA  TRP A 127       9.593   9.396 -23.211  1.00 16.99           C  
ATOM    964  C   TRP A 127       9.203  10.851 -23.335  1.00 16.84           C  
ATOM    965  O   TRP A 127       8.106  11.136 -23.819  1.00 22.26           O  
ATOM    966  CB  TRP A 127       9.718   8.771 -24.577  1.00 11.76           C  
ATOM    967  CG  TRP A 127      10.312   7.376 -24.492  1.00 13.58           C  
ATOM    968  CD1 TRP A 127       9.560   6.287 -24.143  1.00 12.53           C  
ATOM    969  CD2 TRP A 127      11.617   7.053 -24.731  1.00 18.27           C  
ATOM    970  NE1 TRP A 127      10.384   5.265 -24.160  1.00 18.14           N  
ATOM    971  CE2 TRP A 127      11.620   5.667 -24.495  1.00 17.93           C  
ATOM    972  CE3 TRP A 127      12.789   7.727 -25.087  1.00 16.04           C  
ATOM    973  CZ2 TRP A 127      12.794   4.925 -24.625  1.00 20.12           C  
ATOM    974  CZ3 TRP A 127      13.963   6.979 -25.213  1.00 23.32           C  
ATOM    975  CH2 TRP A 127      13.972   5.595 -24.978  1.00 20.52           C  
ATOM    976  N   GLY A 128      10.023  11.772 -22.852  1.00 15.00           N  
ATOM    977  CA  GLY A 128       9.719  13.184 -22.926  1.00 14.96           C  
ATOM    978  C   GLY A 128      10.319  13.795 -24.182  1.00 17.32           C  
ATOM    979  O   GLY A 128      11.385  13.363 -24.628  1.00 17.68           O  
ATOM    980  N   SER A 129       9.631  14.781 -24.732  1.00 17.90           N  
ATOM    981  CA  SER A 129      10.094  15.523 -25.879  1.00 22.85           C  
ATOM    982  C   SER A 129       9.364  16.857 -25.910  1.00 22.60           C  
ATOM    983  O   SER A 129       8.297  17.023 -25.315  1.00 20.76           O  
ATOM    984  CB  SER A 129       9.818  14.743 -27.163  1.00 26.66           C  
ATOM    985  OG  SER A 129       8.450  14.627 -27.500  1.00 27.58           O  
ATOM    986  N   LEU A 130       9.943  17.864 -26.544  1.00 23.61           N  
ATOM    987  CA  LEU A 130       9.350  19.184 -26.614  1.00 26.44           C  
ATOM    988  C   LEU A 130       8.294  19.312 -27.706  1.00 28.68           C  
ATOM    989  O   LEU A 130       8.507  18.899 -28.849  1.00 29.66           O  
ATOM    990  CB  LEU A 130      10.475  20.200 -26.836  1.00 26.16           C  
ATOM    991  CG  LEU A 130      11.287  20.711 -25.639  1.00 25.02           C  
ATOM    992  CD1 LEU A 130      11.675  19.616 -24.685  1.00 26.04           C  
ATOM    993  CD2 LEU A 130      12.562  21.302 -26.169  1.00 26.20           C  
ATOM    994  N   GLU A 131       7.114  19.842 -27.380  1.00 29.70           N  
ATOM    995  CA  GLU A 131       6.115  20.159 -28.384  1.00 28.86           C  
ATOM    996  C   GLU A 131       6.389  21.606 -28.786  1.00 27.99           C  
ATOM    997  O   GLU A 131       6.224  21.970 -29.947  1.00 30.53           O  
ATOM    998  CB  GLU A 131       4.708  20.050 -27.821  1.00 31.70           C  
ATOM    999  CG  GLU A 131       3.605  20.232 -28.859  1.00 41.47           C  
ATOM   1000  CD  GLU A 131       2.207  20.272 -28.256  1.00 52.79           C  
ATOM   1001  OE1 GLU A 131       1.619  19.206 -28.034  1.00 61.43           O  
ATOM   1002  OE2 GLU A 131       1.704  21.374 -28.006  1.00 51.90           O  
ATOM   1003  N   SER A 132       6.783  22.457 -27.857  1.00 24.83           N  
ATOM   1004  CA  SER A 132       7.164  23.830 -28.126  1.00 23.25           C  
ATOM   1005  C   SER A 132       8.101  24.192 -26.987  1.00 23.22           C  
ATOM   1006  O   SER A 132       8.401  23.336 -26.145  1.00 26.26           O  
ATOM   1007  CB  SER A 132       5.941  24.726 -28.105  1.00 23.15           C  
ATOM   1008  OG  SER A 132       5.306  24.759 -26.849  1.00 27.00           O  
ATOM   1009  N   LYS A 133       8.561  25.426 -26.841  1.00 21.61           N  
ATOM   1010  CA  LYS A 133       9.414  25.755 -25.717  1.00 20.26           C  
ATOM   1011  C   LYS A 133       8.721  25.827 -24.358  1.00 19.90           C  
ATOM   1012  O   LYS A 133       9.404  26.118 -23.392  1.00 22.56           O  
ATOM   1013  CB  LYS A 133      10.135  27.076 -25.999  1.00 15.07           C  
ATOM   1014  CG  LYS A 133       9.309  28.323 -26.173  1.00 15.80           C  
ATOM   1015  CD  LYS A 133      10.282  29.472 -26.414  1.00 25.49           C  
ATOM   1016  CE  LYS A 133      11.005  29.877 -25.135  1.00 26.73           C  
ATOM   1017  NZ  LYS A 133      11.799  31.069 -25.363  1.00 29.19           N  
ATOM   1018  N   ASN A 134       7.414  25.612 -24.215  1.00 18.39           N  
ATOM   1019  CA  ASN A 134       6.785  25.617 -22.902  1.00 17.56           C  
ATOM   1020  C   ASN A 134       5.772  24.486 -22.729  1.00 17.72           C  
ATOM   1021  O   ASN A 134       4.922  24.505 -21.834  1.00 19.16           O  
ATOM   1022  CB  ASN A 134       6.112  26.983 -22.635  1.00 14.98           C  
ATOM   1023  CG  ASN A 134       4.996  27.395 -23.582  1.00 22.23           C  
ATOM   1024  OD1 ASN A 134       4.616  26.672 -24.506  1.00 28.33           O  
ATOM   1025  ND2 ASN A 134       4.431  28.592 -23.438  1.00 16.85           N  
ATOM   1026  N   VAL A 135       5.864  23.438 -23.558  1.00 17.60           N  
ATOM   1027  CA  VAL A 135       5.024  22.252 -23.456  1.00 15.93           C  
ATOM   1028  C   VAL A 135       5.943  21.071 -23.728  1.00 19.83           C  
ATOM   1029  O   VAL A 135       6.696  21.047 -24.712  1.00 21.83           O  
ATOM   1030  CB  VAL A 135       3.877  22.223 -24.499  1.00 17.62           C  
ATOM   1031  CG1 VAL A 135       3.111  20.907 -24.403  1.00 11.17           C  
ATOM   1032  CG2 VAL A 135       2.894  23.351 -24.227  1.00 17.43           C  
ATOM   1033  N   VAL A 136       5.887  20.086 -22.841  1.00 18.96           N  
ATOM   1034  CA  VAL A 136       6.661  18.873 -22.930  1.00 18.56           C  
ATOM   1035  C   VAL A 136       5.631  17.765 -23.070  1.00 22.95           C  
ATOM   1036  O   VAL A 136       4.645  17.744 -22.332  1.00 23.63           O  
ATOM   1037  CB  VAL A 136       7.489  18.683 -21.640  1.00 20.53           C  
ATOM   1038  CG1 VAL A 136       8.160  17.322 -21.634  1.00 17.38           C  
ATOM   1039  CG2 VAL A 136       8.590  19.720 -21.564  1.00 23.13           C  
ATOM   1040  N   ASN A 137       5.791  16.862 -24.024  1.00 25.20           N  
ATOM   1041  CA  ASN A 137       4.908  15.715 -24.151  1.00 26.07           C  
ATOM   1042  C   ASN A 137       5.554  14.494 -23.542  1.00 24.58           C  
ATOM   1043  O   ASN A 137       6.777  14.322 -23.627  1.00 26.27           O  
ATOM   1044  CB  ASN A 137       4.611  15.378 -25.611  1.00 32.64           C  
ATOM   1045  CG  ASN A 137       3.807  16.430 -26.342  1.00 28.55           C  
ATOM   1046  OD1 ASN A 137       4.112  16.769 -27.480  1.00 40.09           O  
ATOM   1047  ND2 ASN A 137       2.767  17.010 -25.738  1.00 27.19           N  
ATOM   1048  N   VAL A 138       4.764  13.649 -22.898  1.00 21.18           N  
ATOM   1049  CA  VAL A 138       5.278  12.390 -22.395  1.00 22.96           C  
ATOM   1050  C   VAL A 138       4.545  11.397 -23.263  1.00 23.63           C  
ATOM   1051  O   VAL A 138       3.320  11.429 -23.293  1.00 24.59           O  
ATOM   1052  CB  VAL A 138       4.911  12.172 -20.925  1.00 22.92           C  
ATOM   1053  CG1 VAL A 138       5.399  10.816 -20.484  1.00 16.18           C  
ATOM   1054  CG2 VAL A 138       5.556  13.232 -20.065  1.00 20.50           C  
ATOM   1055  N   ARG A 139       5.254  10.592 -24.034  1.00 24.86           N  
ATOM   1056  CA  ARG A 139       4.671   9.619 -24.930  1.00 26.18           C  
ATOM   1057  C   ARG A 139       5.067   8.219 -24.535  1.00 28.63           C  
ATOM   1058  O   ARG A 139       6.021   8.008 -23.779  1.00 31.24           O  
ATOM   1059  CB  ARG A 139       5.127   9.794 -26.353  1.00 25.53           C  
ATOM   1060  CG  ARG A 139       4.566  11.016 -27.019  1.00 26.35           C  
ATOM   1061  CD  ARG A 139       5.179  10.969 -28.391  1.00 28.82           C  
ATOM   1062  NE  ARG A 139       5.227  12.311 -28.926  1.00 38.70           N  
ATOM   1063  CZ  ARG A 139       4.194  12.845 -29.572  1.00 42.02           C  
ATOM   1064  NH1 ARG A 139       3.071  12.158 -29.799  1.00 47.69           N  
ATOM   1065  NH2 ARG A 139       4.311  14.086 -30.028  1.00 44.24           N  
ATOM   1066  N   GLU A 140       4.336   7.274 -25.107  1.00 30.83           N  
ATOM   1067  CA  GLU A 140       4.578   5.883 -24.838  1.00 34.10           C  
ATOM   1068  C   GLU A 140       5.916   5.397 -25.336  1.00 31.53           C  
ATOM   1069  O   GLU A 140       6.417   4.435 -24.770  1.00 35.27           O  
ATOM   1070  CB  GLU A 140       3.544   5.015 -25.488  1.00 42.29           C  
ATOM   1071  CG  GLU A 140       2.148   5.092 -24.924  1.00 58.09           C  
ATOM   1072  CD  GLU A 140       1.127   4.231 -25.669  1.00 68.87           C  
ATOM   1073  OE1 GLU A 140       1.395   3.728 -26.770  1.00 74.29           O  
ATOM   1074  OE2 GLU A 140       0.031   4.075 -25.133  1.00 78.31           O  
ATOM   1075  N   SER A 141       6.513   5.946 -26.402  1.00 31.32           N  
ATOM   1076  CA  SER A 141       7.796   5.434 -26.865  1.00 30.39           C  
ATOM   1077  C   SER A 141       8.662   6.513 -27.489  1.00 30.44           C  
ATOM   1078  O   SER A 141       8.250   7.678 -27.548  1.00 26.93           O  
ATOM   1079  CB  SER A 141       7.538   4.277 -27.860  1.00 37.22           C  
ATOM   1080  OG  SER A 141       7.166   4.584 -29.201  1.00 38.72           O  
ATOM   1081  N   ALA A 142       9.870   6.176 -27.946  1.00 30.82           N  
ATOM   1082  CA  ALA A 142      10.745   7.157 -28.578  1.00 33.00           C  
ATOM   1083  C   ALA A 142      10.212   7.693 -29.904  1.00 35.54           C  
ATOM   1084  O   ALA A 142      10.641   8.736 -30.406  1.00 34.30           O  
ATOM   1085  CB  ALA A 142      12.114   6.529 -28.824  1.00 29.37           C  
ATOM   1086  N   ASP A 143       9.276   6.944 -30.494  1.00 38.94           N  
ATOM   1087  CA  ASP A 143       8.713   7.332 -31.769  1.00 39.41           C  
ATOM   1088  C   ASP A 143       7.865   8.583 -31.585  1.00 38.54           C  
ATOM   1089  O   ASP A 143       6.845   8.515 -30.901  1.00 31.63           O  
ATOM   1090  CB  ASP A 143       7.853   6.200 -32.308  1.00 45.79           C  
ATOM   1091  CG  ASP A 143       7.397   6.356 -33.760  1.00 52.34           C  
ATOM   1092  OD1 ASP A 143       6.893   7.406 -34.170  1.00 46.95           O  
ATOM   1093  OD2 ASP A 143       7.544   5.379 -34.488  1.00 61.37           O  
ATOM   1094  N   PRO A 144       8.154   9.686 -32.286  1.00 40.55           N  
ATOM   1095  CA  PRO A 144       7.452  10.953 -32.139  1.00 44.00           C  
ATOM   1096  C   PRO A 144       5.967  10.907 -32.457  1.00 44.57           C  
ATOM   1097  O   PRO A 144       5.273  11.898 -32.261  1.00 46.99           O  
ATOM   1098  CB  PRO A 144       8.188  11.911 -33.046  1.00 42.41           C  
ATOM   1099  CG  PRO A 144       9.526  11.257 -33.253  1.00 47.03           C  
ATOM   1100  CD  PRO A 144       9.190   9.782 -33.306  1.00 43.75           C  
ATOM   1101  N   ALA A 145       5.469   9.806 -32.996  1.00 45.94           N  
ATOM   1102  CA  ALA A 145       4.068   9.722 -33.329  1.00 47.25           C  
ATOM   1103  C   ALA A 145       3.338   8.772 -32.405  1.00 47.18           C  
ATOM   1104  O   ALA A 145       2.188   8.436 -32.689  1.00 48.47           O  
ATOM   1105  CB  ALA A 145       3.939   9.240 -34.764  1.00 52.83           C  
ATOM   1106  N   SER A 146       3.958   8.247 -31.346  1.00 46.70           N  
ATOM   1107  CA  SER A 146       3.229   7.338 -30.490  1.00 43.75           C  
ATOM   1108  C   SER A 146       2.337   8.163 -29.581  1.00 42.17           C  
ATOM   1109  O   SER A 146       2.421   9.393 -29.525  1.00 40.96           O  
ATOM   1110  CB  SER A 146       4.213   6.473 -29.697  1.00 45.90           C  
ATOM   1111  OG  SER A 146       5.086   7.150 -28.805  1.00 47.31           O  
ATOM   1112  N   ALA A 147       1.444   7.485 -28.869  1.00 40.14           N  
ATOM   1113  CA  ALA A 147       0.478   8.184 -28.056  1.00 38.82           C  
ATOM   1114  C   ALA A 147       1.042   9.033 -26.941  1.00 38.21           C  
ATOM   1115  O   ALA A 147       1.931   8.626 -26.179  1.00 38.97           O  
ATOM   1116  CB  ALA A 147      -0.489   7.194 -27.428  1.00 41.43           C  
ATOM   1117  N   VAL A 148       0.513  10.248 -26.928  1.00 36.73           N  
ATOM   1118  CA  VAL A 148       0.778  11.162 -25.846  1.00 38.04           C  
ATOM   1119  C   VAL A 148      -0.004  10.627 -24.671  1.00 39.34           C  
ATOM   1120  O   VAL A 148      -1.189  10.313 -24.726  1.00 46.33           O  
ATOM   1121  CB  VAL A 148       0.313  12.575 -26.194  1.00 37.38           C  
ATOM   1122  CG1 VAL A 148       0.429  13.540 -25.021  1.00 31.31           C  
ATOM   1123  CG2 VAL A 148       1.235  13.094 -27.277  1.00 35.77           C  
ATOM   1124  N   LYS A 149       0.782  10.478 -23.637  1.00 39.46           N  
ATOM   1125  CA  LYS A 149       0.383   9.944 -22.364  1.00 39.83           C  
ATOM   1126  C   LYS A 149       0.179  11.148 -21.446  1.00 39.82           C  
ATOM   1127  O   LYS A 149      -0.740  11.137 -20.629  1.00 43.33           O  
ATOM   1128  CB  LYS A 149       1.533   9.024 -22.023  1.00 40.78           C  
ATOM   1129  CG  LYS A 149       1.467   7.997 -20.944  1.00 44.50           C  
ATOM   1130  CD  LYS A 149       2.652   7.106 -21.280  1.00 43.02           C  
ATOM   1131  CE  LYS A 149       2.935   6.162 -20.126  1.00 50.52           C  
ATOM   1132  NZ  LYS A 149       3.909   5.142 -20.480  1.00 55.99           N  
ATOM   1133  N   GLU A 150       0.978  12.221 -21.527  1.00 36.11           N  
ATOM   1134  CA  GLU A 150       0.777  13.418 -20.716  1.00 30.58           C  
ATOM   1135  C   GLU A 150       1.242  14.610 -21.511  1.00 29.17           C  
ATOM   1136  O   GLU A 150       2.140  14.477 -22.346  1.00 30.63           O  
ATOM   1137  CB  GLU A 150       1.593  13.401 -19.428  1.00 37.16           C  
ATOM   1138  CG  GLU A 150       1.127  12.481 -18.304  1.00 47.66           C  
ATOM   1139  CD  GLU A 150      -0.173  12.897 -17.612  1.00 62.75           C  
ATOM   1140  OE1 GLU A 150      -0.395  14.090 -17.367  1.00 70.94           O  
ATOM   1141  OE2 GLU A 150      -0.967  12.006 -17.304  1.00 72.54           O  
ATOM   1142  N   ARG A 151       0.633  15.768 -21.313  1.00 28.07           N  
ATOM   1143  CA  ARG A 151       1.056  16.995 -21.970  1.00 27.58           C  
ATOM   1144  C   ARG A 151       1.303  17.904 -20.777  1.00 26.64           C  
ATOM   1145  O   ARG A 151       0.426  18.109 -19.939  1.00 26.79           O  
ATOM   1146  CB  ARG A 151      -0.063  17.524 -22.860  1.00 29.34           C  
ATOM   1147  CG  ARG A 151       0.363  18.687 -23.745  1.00 39.51           C  
ATOM   1148  CD  ARG A 151      -0.814  19.261 -24.533  1.00 40.24           C  
ATOM   1149  NE  ARG A 151      -0.405  20.410 -25.324  1.00 45.25           N  
ATOM   1150  CZ  ARG A 151      -0.582  21.680 -24.924  1.00 52.08           C  
ATOM   1151  NH1 ARG A 151      -1.165  22.009 -23.761  1.00 52.15           N  
ATOM   1152  NH2 ARG A 151      -0.160  22.654 -25.731  1.00 50.43           N  
ATOM   1153  N   LEU A 152       2.528  18.383 -20.654  1.00 24.68           N  
ATOM   1154  CA  LEU A 152       2.944  19.127 -19.488  1.00 21.68           C  
ATOM   1155  C   LEU A 152       3.270  20.537 -19.896  1.00 22.25           C  
ATOM   1156  O   LEU A 152       4.130  20.765 -20.749  1.00 22.41           O  
ATOM   1157  CB  LEU A 152       4.173  18.449 -18.875  1.00 17.57           C  
ATOM   1158  CG  LEU A 152       4.061  16.988 -18.445  1.00 18.06           C  
ATOM   1159  CD1 LEU A 152       5.427  16.457 -18.059  1.00 16.40           C  
ATOM   1160  CD2 LEU A 152       3.097  16.874 -17.276  1.00 21.99           C  
ATOM   1161  N   GLU A 153       2.507  21.482 -19.368  1.00 24.26           N  
ATOM   1162  CA  GLU A 153       2.767  22.901 -19.568  1.00 25.67           C  
ATOM   1163  C   GLU A 153       3.750  23.346 -18.504  1.00 24.23           C  
ATOM   1164  O   GLU A 153       3.636  22.910 -17.354  1.00 23.96           O  
ATOM   1165  CB  GLU A 153       1.479  23.680 -19.448  1.00 21.63           C  
ATOM   1166  CG  GLU A 153       0.689  23.348 -20.688  1.00 31.02           C  
ATOM   1167  CD  GLU A 153      -0.565  24.169 -20.861  1.00 31.71           C  
ATOM   1168  OE1 GLU A 153      -1.568  23.876 -20.217  1.00 41.49           O  
ATOM   1169  OE2 GLU A 153      -0.527  25.101 -21.656  1.00 45.55           O  
ATOM   1170  N   THR A 154       4.714  24.184 -18.852  1.00 24.90           N  
ATOM   1171  CA  THR A 154       5.749  24.567 -17.927  1.00 24.13           C  
ATOM   1172  C   THR A 154       6.352  25.903 -18.316  1.00 25.82           C  
ATOM   1173  O   THR A 154       6.296  26.363 -19.463  1.00 27.97           O  
ATOM   1174  CB  THR A 154       6.809  23.420 -17.906  1.00 22.81           C  
ATOM   1175  OG1 THR A 154       7.770  23.750 -16.914  1.00 24.64           O  
ATOM   1176  CG2 THR A 154       7.485  23.209 -19.242  1.00 18.39           C  
ATOM   1177  N   GLU A 155       6.900  26.547 -17.289  1.00 23.29           N  
ATOM   1178  CA  GLU A 155       7.609  27.788 -17.451  1.00 23.48           C  
ATOM   1179  C   GLU A 155       9.085  27.528 -17.661  1.00 22.16           C  
ATOM   1180  O   GLU A 155       9.779  28.447 -18.082  1.00 24.56           O  
ATOM   1181  CB  GLU A 155       7.499  28.685 -16.234  1.00 26.74           C  
ATOM   1182  CG  GLU A 155       6.076  28.780 -15.687  1.00 43.33           C  
ATOM   1183  CD  GLU A 155       5.737  29.960 -14.774  1.00 50.74           C  
ATOM   1184  OE1 GLU A 155       6.639  30.615 -14.231  1.00 44.20           O  
ATOM   1185  OE2 GLU A 155       4.535  30.219 -14.626  1.00 51.27           O  
ATOM   1186  N   HIS A 156       9.669  26.387 -17.283  1.00 18.93           N  
ATOM   1187  CA  HIS A 156      11.096  26.157 -17.481  1.00 15.57           C  
ATOM   1188  C   HIS A 156      11.262  24.697 -17.794  1.00 15.40           C  
ATOM   1189  O   HIS A 156      10.480  23.866 -17.311  1.00 15.91           O  
ATOM   1190  CB  HIS A 156      11.932  26.438 -16.238  1.00 16.63           C  
ATOM   1191  CG  HIS A 156      11.802  27.834 -15.656  1.00 17.17           C  
ATOM   1192  ND1 HIS A 156      10.906  28.223 -14.762  1.00 21.31           N  
ATOM   1193  CD2 HIS A 156      12.575  28.926 -15.966  1.00 19.35           C  
ATOM   1194  CE1 HIS A 156      11.098  29.497 -14.516  1.00 22.06           C  
ATOM   1195  NE2 HIS A 156      12.107  29.909 -15.247  1.00 20.83           N  
ATOM   1196  N   ILE A 157      12.269  24.382 -18.607  1.00 16.26           N  
ATOM   1197  CA  ILE A 157      12.567  23.011 -19.011  1.00 14.11           C  
ATOM   1198  C   ILE A 157      14.052  22.774 -18.792  1.00 15.69           C  
ATOM   1199  O   ILE A 157      14.877  23.639 -19.105  1.00 16.65           O  
ATOM   1200  CB  ILE A 157      12.230  22.783 -20.512  1.00 15.43           C  
ATOM   1201  CG1 ILE A 157      10.728  22.952 -20.754  1.00 14.39           C  
ATOM   1202  CG2 ILE A 157      12.691  21.389 -20.935  1.00 12.95           C  
ATOM   1203  CD1 ILE A 157      10.285  23.020 -22.241  1.00 24.03           C  
ATOM   1204  N   LEU A 158      14.374  21.609 -18.237  1.00 15.39           N  
ATOM   1205  CA  LEU A 158      15.741  21.184 -18.070  1.00 14.60           C  
ATOM   1206  C   LEU A 158      15.895  19.881 -18.827  1.00 15.66           C  
ATOM   1207  O   LEU A 158      15.123  18.939 -18.639  1.00 14.54           O  
ATOM   1208  CB  LEU A 158      16.066  20.948 -16.609  1.00 14.35           C  
ATOM   1209  CG  LEU A 158      17.448  20.452 -16.276  1.00 12.94           C  
ATOM   1210  CD1 LEU A 158      18.474  21.451 -16.727  1.00 10.90           C  
ATOM   1211  CD2 LEU A 158      17.542  20.231 -14.782  1.00 14.61           C  
ATOM   1212  N   LEU A 159      16.913  19.852 -19.682  1.00 16.64           N  
ATOM   1213  CA  LEU A 159      17.262  18.708 -20.498  1.00 13.05           C  
ATOM   1214  C   LEU A 159      18.397  18.011 -19.762  1.00 13.90           C  
ATOM   1215  O   LEU A 159      19.500  18.553 -19.604  1.00 12.68           O  
ATOM   1216  CB  LEU A 159      17.716  19.206 -21.875  1.00 14.48           C  
ATOM   1217  CG  LEU A 159      16.772  20.111 -22.681  1.00 13.52           C  
ATOM   1218  CD1 LEU A 159      17.447  20.572 -23.966  1.00 10.84           C  
ATOM   1219  CD2 LEU A 159      15.501  19.332 -22.993  1.00  8.17           C  
ATOM   1220  N   ALA A 160      18.128  16.814 -19.273  1.00 16.95           N  
ATOM   1221  CA  ALA A 160      19.112  16.066 -18.514  1.00 17.72           C  
ATOM   1222  C   ALA A 160      19.087  14.620 -18.969  1.00 17.13           C  
ATOM   1223  O   ALA A 160      19.243  13.705 -18.160  1.00 20.62           O  
ATOM   1224  CB  ALA A 160      18.761  16.172 -17.030  1.00 15.89           C  
ATOM   1225  N   SER A 161      18.971  14.394 -20.289  1.00 15.91           N  
ATOM   1226  CA  SER A 161      18.835  13.053 -20.862  1.00 14.32           C  
ATOM   1227  C   SER A 161      20.078  12.168 -20.919  1.00 12.25           C  
ATOM   1228  O   SER A 161      19.989  10.989 -21.258  1.00 14.03           O  
ATOM   1229  CB  SER A 161      18.218  13.218 -22.263  1.00 14.69           C  
ATOM   1230  OG  SER A 161      18.717  14.369 -22.945  1.00 19.16           O  
ATOM   1231  N   GLY A 162      21.263  12.658 -20.553  1.00 11.50           N  
ATOM   1232  CA  GLY A 162      22.441  11.807 -20.533  1.00 13.35           C  
ATOM   1233  C   GLY A 162      22.992  11.459 -21.905  1.00 17.45           C  
ATOM   1234  O   GLY A 162      22.829  12.198 -22.883  1.00 19.38           O  
ATOM   1235  N   SER A 163      23.744  10.383 -21.948  1.00 16.20           N  
ATOM   1236  CA  SER A 163      24.367   9.939 -23.159  1.00 14.62           C  
ATOM   1237  C   SER A 163      24.033   8.476 -23.393  1.00 17.17           C  
ATOM   1238  O   SER A 163      23.336   7.834 -22.599  1.00 16.35           O  
ATOM   1239  CB  SER A 163      25.865  10.195 -23.024  1.00 11.66           C  
ATOM   1240  OG  SER A 163      26.550   9.676 -21.892  1.00 19.08           O  
ATOM   1241  N   TRP A 164      24.530   7.917 -24.500  1.00 17.21           N  
ATOM   1242  CA  TRP A 164      24.233   6.536 -24.860  1.00 16.45           C  
ATOM   1243  C   TRP A 164      25.455   5.945 -25.550  1.00 15.05           C  
ATOM   1244  O   TRP A 164      26.219   6.747 -26.107  1.00 14.67           O  
ATOM   1245  CB  TRP A 164      23.006   6.566 -25.767  1.00 19.59           C  
ATOM   1246  CG  TRP A 164      22.284   5.233 -25.911  1.00 23.06           C  
ATOM   1247  CD1 TRP A 164      22.290   4.594 -27.119  1.00 23.26           C  
ATOM   1248  CD2 TRP A 164      21.571   4.550 -24.947  1.00 25.05           C  
ATOM   1249  NE1 TRP A 164      21.585   3.513 -26.928  1.00 26.36           N  
ATOM   1250  CE2 TRP A 164      21.138   3.428 -25.664  1.00 25.14           C  
ATOM   1251  CE3 TRP A 164      21.243   4.686 -23.598  1.00 17.43           C  
ATOM   1252  CZ2 TRP A 164      20.353   2.447 -25.048  1.00 20.76           C  
ATOM   1253  CZ3 TRP A 164      20.465   3.707 -22.983  1.00 16.37           C  
ATOM   1254  CH2 TRP A 164      20.029   2.592 -23.699  1.00 20.61           C  
ATOM   1255  N   PRO A 165      25.759   4.628 -25.527  1.00 17.24           N  
ATOM   1256  CA  PRO A 165      26.882   4.034 -26.245  1.00 17.80           C  
ATOM   1257  C   PRO A 165      26.838   4.406 -27.724  1.00 20.71           C  
ATOM   1258  O   PRO A 165      25.798   4.374 -28.389  1.00 20.80           O  
ATOM   1259  CB  PRO A 165      26.749   2.561 -26.060  1.00 13.66           C  
ATOM   1260  CG  PRO A 165      25.921   2.419 -24.819  1.00 14.11           C  
ATOM   1261  CD  PRO A 165      24.966   3.569 -24.908  1.00 11.36           C  
ATOM   1262  N   HIS A 166      27.981   4.803 -28.240  1.00 20.68           N  
ATOM   1263  CA  HIS A 166      28.107   5.127 -29.640  1.00 24.91           C  
ATOM   1264  C   HIS A 166      28.599   3.848 -30.306  1.00 23.65           C  
ATOM   1265  O   HIS A 166      29.714   3.438 -30.008  1.00 23.57           O  
ATOM   1266  CB  HIS A 166      29.124   6.272 -29.804  1.00 28.80           C  
ATOM   1267  CG  HIS A 166      29.604   6.515 -31.232  1.00 42.74           C  
ATOM   1268  ND1 HIS A 166      30.841   6.759 -31.639  1.00 50.08           N  
ATOM   1269  CD2 HIS A 166      28.819   6.490 -32.357  1.00 41.73           C  
ATOM   1270  CE1 HIS A 166      30.834   6.874 -32.944  1.00 48.29           C  
ATOM   1271  NE2 HIS A 166      29.604   6.710 -33.356  1.00 40.35           N  
ATOM   1272  N   MET A 167      27.813   3.235 -31.190  1.00 23.23           N  
ATOM   1273  CA  MET A 167      28.215   2.046 -31.949  1.00 26.07           C  
ATOM   1274  C   MET A 167      28.776   2.478 -33.320  1.00 26.04           C  
ATOM   1275  O   MET A 167      28.164   3.349 -33.946  1.00 25.86           O  
ATOM   1276  CB  MET A 167      26.992   1.141 -32.129  1.00 25.65           C  
ATOM   1277  CG  MET A 167      26.438   0.570 -30.823  1.00 29.42           C  
ATOM   1278  SD  MET A 167      27.660  -0.370 -29.869  1.00 28.82           S  
ATOM   1279  CE  MET A 167      27.026  -2.008 -30.094  1.00 20.69           C  
ATOM   1280  N   PRO A 168      29.943   2.056 -33.827  1.00 28.34           N  
ATOM   1281  CA  PRO A 168      30.503   2.530 -35.098  1.00 30.07           C  
ATOM   1282  C   PRO A 168      29.760   1.897 -36.256  1.00 32.41           C  
ATOM   1283  O   PRO A 168      29.234   0.790 -36.081  1.00 31.69           O  
ATOM   1284  CB  PRO A 168      31.950   2.135 -35.033  1.00 28.25           C  
ATOM   1285  CG  PRO A 168      31.881   0.826 -34.283  1.00 32.06           C  
ATOM   1286  CD  PRO A 168      30.841   1.097 -33.194  1.00 31.74           C  
ATOM   1287  N   ASN A 169      29.668   2.503 -37.448  1.00 38.01           N  
ATOM   1288  CA  ASN A 169      28.941   1.791 -38.496  1.00 40.63           C  
ATOM   1289  C   ASN A 169      29.943   0.961 -39.288  1.00 39.00           C  
ATOM   1290  O   ASN A 169      30.588   1.427 -40.232  1.00 39.99           O  
ATOM   1291  CB  ASN A 169      28.204   2.740 -39.451  1.00 46.19           C  
ATOM   1292  CG  ASN A 169      27.070   1.999 -40.172  1.00 62.44           C  
ATOM   1293  OD1 ASN A 169      26.398   1.141 -39.602  1.00 70.65           O  
ATOM   1294  ND2 ASN A 169      26.765   2.257 -41.441  1.00 60.45           N  
ATOM   1295  N   ILE A 170      30.194  -0.238 -38.762  1.00 33.87           N  
ATOM   1296  CA  ILE A 170      31.076  -1.208 -39.379  1.00 29.90           C  
ATOM   1297  C   ILE A 170      30.173  -2.400 -39.628  1.00 30.10           C  
ATOM   1298  O   ILE A 170      29.233  -2.666 -38.852  1.00 33.10           O  
ATOM   1299  CB  ILE A 170      32.285  -1.683 -38.483  1.00 29.66           C  
ATOM   1300  CG1 ILE A 170      31.869  -2.440 -37.232  1.00 28.84           C  
ATOM   1301  CG2 ILE A 170      33.079  -0.440 -38.117  1.00 31.84           C  
ATOM   1302  CD1 ILE A 170      33.005  -3.302 -36.665  1.00 35.17           C  
ATOM   1303  N   PRO A 171      30.337  -3.138 -40.718  1.00 28.37           N  
ATOM   1304  CA  PRO A 171      29.552  -4.324 -40.965  1.00 28.68           C  
ATOM   1305  C   PRO A 171      29.692  -5.316 -39.820  1.00 30.03           C  
ATOM   1306  O   PRO A 171      30.776  -5.595 -39.294  1.00 31.79           O  
ATOM   1307  CB  PRO A 171      30.064  -4.815 -42.295  1.00 26.00           C  
ATOM   1308  CG  PRO A 171      31.403  -4.159 -42.462  1.00 27.08           C  
ATOM   1309  CD  PRO A 171      31.173  -2.803 -41.858  1.00 26.53           C  
ATOM   1310  N   GLY A 172      28.527  -5.752 -39.378  1.00 29.20           N  
ATOM   1311  CA  GLY A 172      28.464  -6.745 -38.340  1.00 31.52           C  
ATOM   1312  C   GLY A 172      28.288  -6.158 -36.953  1.00 30.77           C  
ATOM   1313  O   GLY A 172      28.177  -6.927 -35.997  1.00 29.75           O  
ATOM   1314  N   ILE A 173      28.132  -4.844 -36.807  1.00 31.49           N  
ATOM   1315  CA  ILE A 173      27.933  -4.227 -35.508  1.00 31.37           C  
ATOM   1316  C   ILE A 173      26.783  -4.856 -34.718  1.00 33.58           C  
ATOM   1317  O   ILE A 173      26.823  -4.891 -33.490  1.00 38.39           O  
ATOM   1318  CB  ILE A 173      27.716  -2.700 -35.723  1.00 29.32           C  
ATOM   1319  CG1 ILE A 173      27.836  -1.980 -34.396  1.00 28.75           C  
ATOM   1320  CG2 ILE A 173      26.359  -2.433 -36.355  1.00 27.29           C  
ATOM   1321  CD1 ILE A 173      29.229  -2.153 -33.769  1.00 29.70           C  
ATOM   1322  N   GLU A 174      25.825  -5.518 -35.374  1.00 31.78           N  
ATOM   1323  CA  GLU A 174      24.690  -6.059 -34.636  1.00 31.55           C  
ATOM   1324  C   GLU A 174      25.043  -7.373 -33.938  1.00 30.80           C  
ATOM   1325  O   GLU A 174      24.200  -8.064 -33.375  1.00 31.72           O  
ATOM   1326  CB  GLU A 174      23.501  -6.264 -35.584  1.00 36.44           C  
ATOM   1327  CG  GLU A 174      23.684  -7.393 -36.617  1.00 44.14           C  
ATOM   1328  CD  GLU A 174      24.517  -7.034 -37.850  1.00 49.19           C  
ATOM   1329  OE1 GLU A 174      24.756  -5.845 -38.112  1.00 51.07           O  
ATOM   1330  OE2 GLU A 174      24.929  -7.951 -38.568  1.00 57.34           O  
ATOM   1331  N   HIS A 175      26.302  -7.793 -34.039  1.00 30.66           N  
ATOM   1332  CA  HIS A 175      26.798  -8.984 -33.372  1.00 31.17           C  
ATOM   1333  C   HIS A 175      27.625  -8.597 -32.155  1.00 31.81           C  
ATOM   1334  O   HIS A 175      28.204  -9.448 -31.467  1.00 32.41           O  
ATOM   1335  CB  HIS A 175      27.679  -9.809 -34.315  1.00 35.18           C  
ATOM   1336  CG  HIS A 175      26.941 -10.265 -35.570  1.00 39.72           C  
ATOM   1337  ND1 HIS A 175      25.804 -10.951 -35.579  1.00 40.93           N  
ATOM   1338  CD2 HIS A 175      27.285 -10.040 -36.883  1.00 35.99           C  
ATOM   1339  CE1 HIS A 175      25.434 -11.150 -36.815  1.00 39.67           C  
ATOM   1340  NE2 HIS A 175      26.333 -10.599 -37.589  1.00 39.21           N  
ATOM   1341  N   CYS A 176      27.728  -7.296 -31.937  1.00 30.50           N  
ATOM   1342  CA  CYS A 176      28.461  -6.749 -30.824  1.00 27.97           C  
ATOM   1343  C   CYS A 176      27.480  -6.196 -29.787  1.00 27.87           C  
ATOM   1344  O   CYS A 176      26.296  -5.991 -30.076  1.00 26.31           O  
ATOM   1345  CB  CYS A 176      29.382  -5.653 -31.337  1.00 23.62           C  
ATOM   1346  SG  CYS A 176      30.391  -6.087 -32.760  1.00 29.23           S  
ATOM   1347  N   ILE A 177      27.916  -6.099 -28.522  1.00 26.26           N  
ATOM   1348  CA  ILE A 177      27.112  -5.508 -27.458  1.00 20.07           C  
ATOM   1349  C   ILE A 177      27.816  -4.230 -27.013  1.00 20.68           C  
ATOM   1350  O   ILE A 177      28.920  -3.919 -27.482  1.00 19.18           O  
ATOM   1351  CB  ILE A 177      26.969  -6.481 -26.246  1.00 20.97           C  
ATOM   1352  CG1 ILE A 177      28.296  -6.792 -25.578  1.00 21.22           C  
ATOM   1353  CG2 ILE A 177      26.336  -7.769 -26.755  1.00 17.45           C  
ATOM   1354  CD1 ILE A 177      28.067  -7.412 -24.196  1.00 27.62           C  
ATOM   1355  N   SER A 178      27.190  -3.449 -26.140  1.00 22.29           N  
ATOM   1356  CA  SER A 178      27.812  -2.282 -25.516  1.00 19.61           C  
ATOM   1357  C   SER A 178      27.928  -2.594 -24.014  1.00 18.78           C  
ATOM   1358  O   SER A 178      27.580  -3.697 -23.574  1.00 20.02           O  
ATOM   1359  CB  SER A 178      26.933  -1.043 -25.751  1.00 17.58           C  
ATOM   1360  OG  SER A 178      25.643  -1.170 -25.153  1.00 19.25           O  
ATOM   1361  N   SER A 179      28.316  -1.628 -23.163  1.00 19.57           N  
ATOM   1362  CA  SER A 179      28.438  -1.857 -21.731  1.00 18.48           C  
ATOM   1363  C   SER A 179      27.087  -2.130 -21.111  1.00 19.16           C  
ATOM   1364  O   SER A 179      26.994  -2.917 -20.188  1.00 25.30           O  
ATOM   1365  CB  SER A 179      29.083  -0.657 -21.059  1.00 16.55           C  
ATOM   1366  OG  SER A 179      28.453   0.568 -21.401  1.00 12.39           O  
ATOM   1367  N   ASN A 180      26.009  -1.586 -21.676  1.00 18.64           N  
ATOM   1368  CA  ASN A 180      24.662  -1.824 -21.180  1.00 17.71           C  
ATOM   1369  C   ASN A 180      24.302  -3.288 -21.036  1.00 20.00           C  
ATOM   1370  O   ASN A 180      23.803  -3.711 -19.990  1.00 21.74           O  
ATOM   1371  CB  ASN A 180      23.643  -1.171 -22.101  1.00 13.23           C  
ATOM   1372  CG  ASN A 180      23.542   0.332 -21.972  1.00 17.97           C  
ATOM   1373  OD1 ASN A 180      23.096   1.023 -22.870  1.00 25.84           O  
ATOM   1374  ND2 ASN A 180      23.952   0.964 -20.905  1.00 12.60           N  
ATOM   1375  N   GLU A 181      24.603  -4.087 -22.060  1.00 19.27           N  
ATOM   1376  CA  GLU A 181      24.244  -5.499 -22.064  1.00 18.28           C  
ATOM   1377  C   GLU A 181      25.249  -6.269 -21.250  1.00 16.34           C  
ATOM   1378  O   GLU A 181      24.894  -7.286 -20.665  1.00 17.94           O  
ATOM   1379  CB  GLU A 181      24.226  -6.092 -23.482  1.00 16.59           C  
ATOM   1380  CG  GLU A 181      23.137  -5.565 -24.439  1.00 15.16           C  
ATOM   1381  CD  GLU A 181      23.376  -4.191 -25.063  1.00 19.55           C  
ATOM   1382  OE1 GLU A 181      24.498  -3.687 -25.068  1.00 23.71           O  
ATOM   1383  OE2 GLU A 181      22.415  -3.613 -25.556  1.00 29.06           O  
ATOM   1384  N   ALA A 182      26.502  -5.812 -21.196  1.00 14.80           N  
ATOM   1385  CA  ALA A 182      27.530  -6.453 -20.407  1.00 13.77           C  
ATOM   1386  C   ALA A 182      27.084  -6.589 -18.951  1.00 16.16           C  
ATOM   1387  O   ALA A 182      27.436  -7.572 -18.305  1.00 19.17           O  
ATOM   1388  CB  ALA A 182      28.793  -5.633 -20.467  1.00 13.53           C  
ATOM   1389  N   PHE A 183      26.242  -5.701 -18.404  1.00 16.46           N  
ATOM   1390  CA  PHE A 183      25.748  -5.825 -17.034  1.00 17.73           C  
ATOM   1391  C   PHE A 183      24.724  -6.944 -16.823  1.00 21.93           C  
ATOM   1392  O   PHE A 183      24.402  -7.308 -15.688  1.00 18.96           O  
ATOM   1393  CB  PHE A 183      25.116  -4.505 -16.582  1.00 12.90           C  
ATOM   1394  CG  PHE A 183      26.150  -3.428 -16.342  1.00 13.76           C  
ATOM   1395  CD1 PHE A 183      26.977  -3.477 -15.213  1.00 18.51           C  
ATOM   1396  CD2 PHE A 183      26.285  -2.388 -17.258  1.00 10.77           C  
ATOM   1397  CE1 PHE A 183      27.933  -2.475 -15.007  1.00 17.74           C  
ATOM   1398  CE2 PHE A 183      27.243  -1.391 -17.044  1.00 16.91           C  
ATOM   1399  CZ  PHE A 183      28.070  -1.432 -15.921  1.00 16.58           C  
ATOM   1400  N   TYR A 184      24.159  -7.527 -17.881  1.00 20.27           N  
ATOM   1401  CA  TYR A 184      23.142  -8.548 -17.731  1.00 18.28           C  
ATOM   1402  C   TYR A 184      23.580  -9.831 -18.395  1.00 18.01           C  
ATOM   1403  O   TYR A 184      22.730 -10.673 -18.672  1.00 22.89           O  
ATOM   1404  CB  TYR A 184      21.831  -8.052 -18.342  1.00 14.99           C  
ATOM   1405  CG  TYR A 184      21.353  -6.829 -17.594  1.00 14.85           C  
ATOM   1406  CD1 TYR A 184      20.571  -6.962 -16.453  1.00 16.01           C  
ATOM   1407  CD2 TYR A 184      21.771  -5.566 -18.013  1.00 16.63           C  
ATOM   1408  CE1 TYR A 184      20.212  -5.821 -15.720  1.00 21.22           C  
ATOM   1409  CE2 TYR A 184      21.425  -4.433 -17.287  1.00 14.91           C  
ATOM   1410  CZ  TYR A 184      20.650  -4.569 -16.146  1.00 15.04           C  
ATOM   1411  OH  TYR A 184      20.305  -3.441 -15.425  1.00 18.87           O  
ATOM   1412  N   LEU A 185      24.866 -10.058 -18.679  1.00 21.44           N  
ATOM   1413  CA  LEU A 185      25.251 -11.294 -19.343  1.00 25.01           C  
ATOM   1414  C   LEU A 185      24.948 -12.500 -18.472  1.00 30.73           C  
ATOM   1415  O   LEU A 185      25.228 -12.441 -17.271  1.00 33.43           O  
ATOM   1416  CB  LEU A 185      26.733 -11.320 -19.668  1.00 18.29           C  
ATOM   1417  CG  LEU A 185      27.234 -10.314 -20.678  1.00 20.82           C  
ATOM   1418  CD1 LEU A 185      28.744 -10.362 -20.686  1.00 13.78           C  
ATOM   1419  CD2 LEU A 185      26.641 -10.603 -22.045  1.00 13.38           C  
ATOM   1420  N   PRO A 186      24.393 -13.606 -18.997  1.00 32.93           N  
ATOM   1421  CA  PRO A 186      23.971 -14.762 -18.214  1.00 30.98           C  
ATOM   1422  C   PRO A 186      25.132 -15.487 -17.572  1.00 29.99           C  
ATOM   1423  O   PRO A 186      24.990 -16.065 -16.505  1.00 31.81           O  
ATOM   1424  CB  PRO A 186      23.229 -15.647 -19.177  1.00 33.98           C  
ATOM   1425  CG  PRO A 186      22.907 -14.739 -20.340  1.00 36.15           C  
ATOM   1426  CD  PRO A 186      24.127 -13.838 -20.411  1.00 39.04           C  
ATOM   1427  N   GLU A 187      26.284 -15.498 -18.224  1.00 29.98           N  
ATOM   1428  CA  GLU A 187      27.474 -16.185 -17.756  1.00 32.14           C  
ATOM   1429  C   GLU A 187      28.669 -15.477 -18.398  1.00 30.70           C  
ATOM   1430  O   GLU A 187      28.439 -14.749 -19.362  1.00 30.44           O  
ATOM   1431  CB  GLU A 187      27.380 -17.644 -18.184  1.00 42.65           C  
ATOM   1432  CG  GLU A 187      27.264 -17.787 -19.698  1.00 54.18           C  
ATOM   1433  CD  GLU A 187      26.912 -19.165 -20.230  1.00 68.23           C  
ATOM   1434  OE1 GLU A 187      26.739 -20.107 -19.451  1.00 75.07           O  
ATOM   1435  OE2 GLU A 187      26.808 -19.281 -21.453  1.00 81.12           O  
ATOM   1436  N   PRO A 188      29.929 -15.584 -17.957  1.00 31.81           N  
ATOM   1437  CA  PRO A 188      31.037 -14.812 -18.478  1.00 33.27           C  
ATOM   1438  C   PRO A 188      31.614 -15.361 -19.787  1.00 35.20           C  
ATOM   1439  O   PRO A 188      31.750 -16.578 -19.976  1.00 33.83           O  
ATOM   1440  CB  PRO A 188      32.018 -14.806 -17.328  1.00 36.65           C  
ATOM   1441  CG  PRO A 188      31.900 -16.225 -16.839  1.00 37.01           C  
ATOM   1442  CD  PRO A 188      30.401 -16.486 -16.909  1.00 32.35           C  
ATOM   1443  N   PRO A 189      31.990 -14.471 -20.714  1.00 35.55           N  
ATOM   1444  CA  PRO A 189      32.504 -14.830 -22.023  1.00 33.91           C  
ATOM   1445  C   PRO A 189      33.807 -15.593 -21.901  1.00 33.81           C  
ATOM   1446  O   PRO A 189      34.649 -15.269 -21.107  1.00 33.29           O  
ATOM   1447  CB  PRO A 189      32.680 -13.510 -22.742  1.00 38.20           C  
ATOM   1448  CG  PRO A 189      31.987 -12.485 -21.877  1.00 34.97           C  
ATOM   1449  CD  PRO A 189      32.152 -13.036 -20.490  1.00 34.53           C  
ATOM   1450  N   ARG A 190      34.029 -16.613 -22.709  1.00 32.65           N  
ATOM   1451  CA  ARG A 190      35.315 -17.296 -22.702  1.00 29.87           C  
ATOM   1452  C   ARG A 190      36.377 -16.473 -23.438  1.00 26.45           C  
ATOM   1453  O   ARG A 190      37.498 -16.296 -22.964  1.00 27.43           O  
ATOM   1454  CB  ARG A 190      35.133 -18.646 -23.355  1.00 37.51           C  
ATOM   1455  CG  ARG A 190      36.416 -19.436 -23.328  1.00 44.54           C  
ATOM   1456  CD  ARG A 190      36.334 -20.614 -24.253  1.00 54.65           C  
ATOM   1457  NE  ARG A 190      37.701 -21.054 -24.432  1.00 64.52           N  
ATOM   1458  CZ  ARG A 190      38.217 -21.320 -25.638  1.00 67.84           C  
ATOM   1459  NH1 ARG A 190      37.494 -21.218 -26.758  1.00 65.58           N  
ATOM   1460  NH2 ARG A 190      39.488 -21.710 -25.720  1.00 75.25           N  
ATOM   1461  N   ARG A 191      36.070 -16.038 -24.658  1.00 23.38           N  
ATOM   1462  CA  ARG A 191      36.965 -15.177 -25.408  1.00 20.92           C  
ATOM   1463  C   ARG A 191      36.157 -13.918 -25.577  1.00 19.06           C  
ATOM   1464  O   ARG A 191      35.039 -13.958 -26.106  1.00 19.56           O  
ATOM   1465  CB  ARG A 191      37.270 -15.718 -26.782  1.00 27.42           C  
ATOM   1466  CG  ARG A 191      38.453 -16.645 -26.983  1.00 22.82           C  
ATOM   1467  CD  ARG A 191      38.058 -18.091 -27.162  1.00 27.50           C  
ATOM   1468  NE  ARG A 191      36.817 -18.305 -27.896  1.00 33.82           N  
ATOM   1469  CZ  ARG A 191      36.736 -18.783 -29.150  1.00 42.70           C  
ATOM   1470  NH1 ARG A 191      37.807 -19.087 -29.884  1.00 47.06           N  
ATOM   1471  NH2 ARG A 191      35.532 -18.942 -29.697  1.00 38.23           N  
ATOM   1472  N   VAL A 192      36.653 -12.806 -25.095  1.00 19.67           N  
ATOM   1473  CA  VAL A 192      35.926 -11.568 -25.219  1.00 17.04           C  
ATOM   1474  C   VAL A 192      36.890 -10.558 -25.780  1.00 12.29           C  
ATOM   1475  O   VAL A 192      38.084 -10.584 -25.489  1.00 15.07           O  
ATOM   1476  CB  VAL A 192      35.362 -11.134 -23.811  1.00 24.32           C  
ATOM   1477  CG1 VAL A 192      36.477 -10.969 -22.790  1.00 22.11           C  
ATOM   1478  CG2 VAL A 192      34.605  -9.806 -23.949  1.00 15.98           C  
ATOM   1479  N   LEU A 193      36.394  -9.714 -26.659  1.00 13.45           N  
ATOM   1480  CA  LEU A 193      37.183  -8.620 -27.166  1.00 14.63           C  
ATOM   1481  C   LEU A 193      36.485  -7.361 -26.690  1.00 14.99           C  
ATOM   1482  O   LEU A 193      35.259  -7.287 -26.850  1.00 13.59           O  
ATOM   1483  CB  LEU A 193      37.194  -8.655 -28.681  1.00 17.79           C  
ATOM   1484  CG  LEU A 193      37.887  -7.526 -29.432  1.00 14.71           C  
ATOM   1485  CD1 LEU A 193      39.381  -7.527 -29.148  1.00  5.56           C  
ATOM   1486  CD2 LEU A 193      37.575  -7.691 -30.910  1.00 16.37           C  
ATOM   1487  N   THR A 194      37.165  -6.398 -26.072  1.00 15.85           N  
ATOM   1488  CA  THR A 194      36.572  -5.104 -25.796  1.00 17.86           C  
ATOM   1489  C   THR A 194      37.334  -4.183 -26.739  1.00 16.33           C  
ATOM   1490  O   THR A 194      38.556  -4.238 -26.905  1.00 17.71           O  
ATOM   1491  CB  THR A 194      36.736  -4.684 -24.278  1.00 21.90           C  
ATOM   1492  OG1 THR A 194      38.051  -4.965 -23.827  1.00 26.67           O  
ATOM   1493  CG2 THR A 194      35.811  -5.495 -23.384  1.00 21.54           C  
ATOM   1494  N   VAL A 195      36.556  -3.416 -27.489  1.00 17.27           N  
ATOM   1495  CA  VAL A 195      37.050  -2.501 -28.500  1.00 15.96           C  
ATOM   1496  C   VAL A 195      36.969  -1.114 -27.914  1.00 12.65           C  
ATOM   1497  O   VAL A 195      35.885  -0.628 -27.564  1.00 15.84           O  
ATOM   1498  CB  VAL A 195      36.159  -2.605 -29.772  1.00 16.74           C  
ATOM   1499  CG1 VAL A 195      36.660  -1.632 -30.822  1.00 15.43           C  
ATOM   1500  CG2 VAL A 195      36.152  -4.046 -30.289  1.00 13.99           C  
ATOM   1501  N   GLY A 196      38.093  -0.473 -27.808  1.00 13.33           N  
ATOM   1502  CA  GLY A 196      38.152   0.883 -27.331  1.00 14.69           C  
ATOM   1503  C   GLY A 196      39.317   0.977 -26.378  1.00 14.95           C  
ATOM   1504  O   GLY A 196      39.688   0.008 -25.715  1.00 16.08           O  
ATOM   1505  N   GLY A 197      39.929   2.139 -26.258  1.00 13.37           N  
ATOM   1506  CA  GLY A 197      41.003   2.278 -25.314  1.00 16.25           C  
ATOM   1507  C   GLY A 197      40.589   3.162 -24.148  1.00 17.02           C  
ATOM   1508  O   GLY A 197      41.471   3.591 -23.420  1.00 19.47           O  
ATOM   1509  N   GLY A 198      39.323   3.544 -23.983  1.00 15.60           N  
ATOM   1510  CA  GLY A 198      38.921   4.420 -22.893  1.00 13.98           C  
ATOM   1511  C   GLY A 198      38.653   3.688 -21.584  1.00 15.98           C  
ATOM   1512  O   GLY A 198      38.692   2.452 -21.537  1.00 14.95           O  
ATOM   1513  N   PHE A 199      38.219   4.420 -20.547  1.00 17.34           N  
ATOM   1514  CA  PHE A 199      38.050   3.818 -19.230  1.00 15.67           C  
ATOM   1515  C   PHE A 199      37.033   2.704 -19.185  1.00 12.54           C  
ATOM   1516  O   PHE A 199      37.333   1.693 -18.552  1.00 14.13           O  
ATOM   1517  CB  PHE A 199      37.683   4.890 -18.172  1.00 13.52           C  
ATOM   1518  CG  PHE A 199      36.255   5.415 -18.082  1.00 14.69           C  
ATOM   1519  CD1 PHE A 199      35.860   6.487 -18.870  1.00 18.98           C  
ATOM   1520  CD2 PHE A 199      35.332   4.821 -17.216  1.00 16.46           C  
ATOM   1521  CE1 PHE A 199      34.548   6.953 -18.800  1.00 18.32           C  
ATOM   1522  CE2 PHE A 199      34.019   5.293 -17.154  1.00 10.38           C  
ATOM   1523  CZ  PHE A 199      33.626   6.361 -17.943  1.00 16.35           C  
ATOM   1524  N   ILE A 200      35.900   2.773 -19.899  1.00 10.88           N  
ATOM   1525  CA  ILE A 200      34.898   1.704 -19.848  1.00  9.43           C  
ATOM   1526  C   ILE A 200      35.468   0.421 -20.425  1.00 14.57           C  
ATOM   1527  O   ILE A 200      35.255  -0.663 -19.879  1.00 18.82           O  
ATOM   1528  CB  ILE A 200      33.625   2.095 -20.634  1.00  8.34           C  
ATOM   1529  CG1 ILE A 200      33.013   3.302 -19.958  1.00  7.87           C  
ATOM   1530  CG2 ILE A 200      32.587   0.971 -20.647  1.00  9.19           C  
ATOM   1531  CD1 ILE A 200      31.951   4.078 -20.755  1.00 10.45           C  
ATOM   1532  N   SER A 201      36.240   0.503 -21.505  1.00 16.50           N  
ATOM   1533  CA  SER A 201      36.801  -0.696 -22.098  1.00 14.78           C  
ATOM   1534  C   SER A 201      37.838  -1.321 -21.155  1.00 13.25           C  
ATOM   1535  O   SER A 201      37.831  -2.536 -20.926  1.00 13.13           O  
ATOM   1536  CB  SER A 201      37.400  -0.288 -23.433  1.00 13.24           C  
ATOM   1537  OG  SER A 201      37.886  -1.424 -24.079  1.00 12.44           O  
ATOM   1538  N   VAL A 202      38.716  -0.491 -20.569  1.00 12.69           N  
ATOM   1539  CA  VAL A 202      39.738  -0.956 -19.638  1.00 12.57           C  
ATOM   1540  C   VAL A 202      39.134  -1.521 -18.343  1.00 13.22           C  
ATOM   1541  O   VAL A 202      39.578  -2.578 -17.893  1.00 15.62           O  
ATOM   1542  CB  VAL A 202      40.682   0.225 -19.368  1.00 13.39           C  
ATOM   1543  CG1 VAL A 202      41.704  -0.075 -18.283  1.00 17.70           C  
ATOM   1544  CG2 VAL A 202      41.475   0.473 -20.634  1.00 12.04           C  
ATOM   1545  N   GLU A 203      38.092  -0.918 -17.762  1.00 10.79           N  
ATOM   1546  CA  GLU A 203      37.475  -1.416 -16.543  1.00 10.79           C  
ATOM   1547  C   GLU A 203      36.832  -2.760 -16.758  1.00 11.38           C  
ATOM   1548  O   GLU A 203      37.048  -3.694 -15.982  1.00 16.09           O  
ATOM   1549  CB  GLU A 203      36.404  -0.452 -16.021  1.00  8.46           C  
ATOM   1550  CG  GLU A 203      37.089   0.788 -15.437  1.00  4.36           C  
ATOM   1551  CD  GLU A 203      36.218   1.965 -15.017  1.00  9.87           C  
ATOM   1552  OE1 GLU A 203      35.003   1.943 -15.187  1.00 13.22           O  
ATOM   1553  OE2 GLU A 203      36.770   2.940 -14.521  1.00 12.57           O  
ATOM   1554  N   PHE A 204      36.056  -2.908 -17.833  1.00 11.43           N  
ATOM   1555  CA  PHE A 204      35.427  -4.195 -18.111  1.00 10.59           C  
ATOM   1556  C   PHE A 204      36.422  -5.260 -18.503  1.00  9.89           C  
ATOM   1557  O   PHE A 204      36.177  -6.440 -18.267  1.00 12.14           O  
ATOM   1558  CB  PHE A 204      34.393  -4.077 -19.215  1.00 12.66           C  
ATOM   1559  CG  PHE A 204      33.006  -3.824 -18.655  1.00 15.88           C  
ATOM   1560  CD1 PHE A 204      32.259  -4.904 -18.171  1.00 16.91           C  
ATOM   1561  CD2 PHE A 204      32.479  -2.529 -18.621  1.00 18.96           C  
ATOM   1562  CE1 PHE A 204      30.982  -4.680 -17.659  1.00 16.44           C  
ATOM   1563  CE2 PHE A 204      31.199  -2.316 -18.106  1.00 17.49           C  
ATOM   1564  CZ  PHE A 204      30.455  -3.394 -17.626  1.00 17.86           C  
ATOM   1565  N   ALA A 205      37.566  -4.896 -19.057  1.00 11.69           N  
ATOM   1566  CA  ALA A 205      38.565  -5.890 -19.389  1.00 15.04           C  
ATOM   1567  C   ALA A 205      38.991  -6.548 -18.084  1.00 14.69           C  
ATOM   1568  O   ALA A 205      39.051  -7.780 -18.015  1.00 17.57           O  
ATOM   1569  CB  ALA A 205      39.787  -5.243 -20.052  1.00  9.68           C  
ATOM   1570  N   GLY A 206      39.214  -5.741 -17.038  1.00 18.35           N  
ATOM   1571  CA  GLY A 206      39.569  -6.213 -15.705  1.00 15.02           C  
ATOM   1572  C   GLY A 206      38.469  -7.091 -15.088  1.00 14.64           C  
ATOM   1573  O   GLY A 206      38.768  -8.138 -14.500  1.00 13.23           O  
ATOM   1574  N   ILE A 207      37.194  -6.727 -15.213  1.00 11.31           N  
ATOM   1575  CA  ILE A 207      36.093  -7.522 -14.720  1.00 12.20           C  
ATOM   1576  C   ILE A 207      36.080  -8.865 -15.431  1.00 17.97           C  
ATOM   1577  O   ILE A 207      36.177  -9.917 -14.791  1.00 21.49           O  
ATOM   1578  CB  ILE A 207      34.792  -6.758 -14.963  1.00 10.19           C  
ATOM   1579  CG1 ILE A 207      34.846  -5.525 -14.100  1.00  7.79           C  
ATOM   1580  CG2 ILE A 207      33.557  -7.592 -14.655  1.00  8.08           C  
ATOM   1581  CD1 ILE A 207      33.621  -4.613 -14.263  1.00  5.24           C  
ATOM   1582  N   PHE A 208      36.018  -8.876 -16.763  1.00 21.13           N  
ATOM   1583  CA  PHE A 208      35.990 -10.122 -17.519  1.00 18.18           C  
ATOM   1584  C   PHE A 208      37.191 -11.026 -17.243  1.00 18.72           C  
ATOM   1585  O   PHE A 208      37.063 -12.245 -17.193  1.00 17.79           O  
ATOM   1586  CB  PHE A 208      35.933  -9.809 -19.013  1.00 15.07           C  
ATOM   1587  CG  PHE A 208      34.599  -9.248 -19.483  1.00 15.76           C  
ATOM   1588  CD1 PHE A 208      33.402  -9.857 -19.104  1.00 12.20           C  
ATOM   1589  CD2 PHE A 208      34.577  -8.139 -20.329  1.00 10.82           C  
ATOM   1590  CE1 PHE A 208      32.188  -9.365 -19.581  1.00 17.73           C  
ATOM   1591  CE2 PHE A 208      33.357  -7.657 -20.798  1.00 10.30           C  
ATOM   1592  CZ  PHE A 208      32.164  -8.263 -20.428  1.00  9.46           C  
ATOM   1593  N   ASN A 209      38.374 -10.455 -17.024  1.00 16.08           N  
ATOM   1594  CA  ASN A 209      39.578 -11.212 -16.742  1.00 16.32           C  
ATOM   1595  C   ASN A 209      39.499 -11.996 -15.436  1.00 20.54           C  
ATOM   1596  O   ASN A 209      40.017 -13.097 -15.311  1.00 23.37           O  
ATOM   1597  CB  ASN A 209      40.736 -10.252 -16.681  1.00 16.71           C  
ATOM   1598  CG  ASN A 209      42.071 -10.954 -16.586  1.00 20.56           C  
ATOM   1599  OD1 ASN A 209      42.306 -11.889 -17.334  1.00 25.91           O  
ATOM   1600  ND2 ASN A 209      43.007 -10.565 -15.730  1.00 19.14           N  
ATOM   1601  N   ALA A 210      38.832 -11.459 -14.421  1.00 19.42           N  
ATOM   1602  CA  ALA A 210      38.754 -12.139 -13.144  1.00 18.95           C  
ATOM   1603  C   ALA A 210      37.696 -13.225 -13.090  1.00 20.74           C  
ATOM   1604  O   ALA A 210      37.789 -14.163 -12.300  1.00 20.79           O  
ATOM   1605  CB  ALA A 210      38.457 -11.125 -12.071  1.00 16.24           C  
ATOM   1606  N   TYR A 211      36.647 -13.079 -13.898  1.00 20.85           N  
ATOM   1607  CA  TYR A 211      35.555 -14.030 -13.933  1.00 21.52           C  
ATOM   1608  C   TYR A 211      35.574 -14.948 -15.141  1.00 24.69           C  
ATOM   1609  O   TYR A 211      34.638 -15.743 -15.287  1.00 29.23           O  
ATOM   1610  CB  TYR A 211      34.213 -13.296 -13.910  1.00 13.20           C  
ATOM   1611  CG  TYR A 211      33.909 -12.736 -12.543  1.00 20.48           C  
ATOM   1612  CD1 TYR A 211      33.243 -13.527 -11.604  1.00 14.89           C  
ATOM   1613  CD2 TYR A 211      34.348 -11.451 -12.217  1.00 16.22           C  
ATOM   1614  CE1 TYR A 211      33.018 -13.028 -10.320  1.00 19.27           C  
ATOM   1615  CE2 TYR A 211      34.129 -10.954 -10.938  1.00 19.07           C  
ATOM   1616  CZ  TYR A 211      33.468 -11.746 -10.002  1.00 19.56           C  
ATOM   1617  OH  TYR A 211      33.295 -11.248  -8.735  1.00 20.60           O  
ATOM   1618  N   LYS A 212      36.587 -14.869 -16.013  1.00 27.53           N  
ATOM   1619  CA  LYS A 212      36.656 -15.700 -17.211  1.00 29.38           C  
ATOM   1620  C   LYS A 212      36.697 -17.164 -16.827  1.00 34.59           C  
ATOM   1621  O   LYS A 212      37.133 -17.518 -15.726  1.00 39.57           O  
ATOM   1622  CB  LYS A 212      37.904 -15.360 -18.054  1.00 23.76           C  
ATOM   1623  CG  LYS A 212      39.227 -15.780 -17.487  1.00 23.75           C  
ATOM   1624  CD  LYS A 212      40.371 -15.104 -18.177  1.00 26.85           C  
ATOM   1625  CE  LYS A 212      41.525 -15.552 -17.322  1.00 26.39           C  
ATOM   1626  NZ  LYS A 212      42.698 -14.743 -17.575  1.00 40.81           N  
ATOM   1627  N   PRO A 213      36.198 -18.065 -17.671  1.00 40.31           N  
ATOM   1628  CA  PRO A 213      36.327 -19.495 -17.480  1.00 43.73           C  
ATOM   1629  C   PRO A 213      37.747 -19.944 -17.722  1.00 49.05           C  
ATOM   1630  O   PRO A 213      38.641 -19.189 -18.102  1.00 46.75           O  
ATOM   1631  CB  PRO A 213      35.359 -20.116 -18.450  1.00 44.50           C  
ATOM   1632  CG  PRO A 213      34.319 -19.040 -18.559  1.00 40.99           C  
ATOM   1633  CD  PRO A 213      35.178 -17.795 -18.666  1.00 42.09           C  
ATOM   1634  N   LYS A 214      37.845 -21.262 -17.592  1.00 55.48           N  
ATOM   1635  CA  LYS A 214      39.063 -22.043 -17.738  1.00 60.39           C  
ATOM   1636  C   LYS A 214      39.945 -21.628 -18.896  1.00 59.66           C  
ATOM   1637  O   LYS A 214      41.032 -21.036 -18.621  1.00 61.27           O  
ATOM   1638  CB  LYS A 214      38.740 -23.526 -17.939  1.00 69.49           C  
ATOM   1639  CG  LYS A 214      37.550 -24.162 -17.204  1.00 85.35           C  
ATOM   1640  CD  LYS A 214      36.209 -24.068 -17.960  1.00 89.31           C  
ATOM   1641  CE  LYS A 214      35.148 -24.760 -17.099  1.00 94.99           C  
ATOM   1642  NZ  LYS A 214      33.835 -24.772 -17.720  1.00 94.64           N  
ATOM   1643  N   ASP A 215      39.582 -21.885 -20.169  1.00 58.44           N  
ATOM   1644  CA  ASP A 215      40.660 -21.351 -20.955  1.00 57.09           C  
ATOM   1645  C   ASP A 215      40.124 -20.166 -21.799  1.00 51.64           C  
ATOM   1646  O   ASP A 215      40.391 -19.795 -22.949  1.00 51.30           O  
ATOM   1647  CB  ASP A 215      41.542 -22.716 -21.551  1.00 68.71           C  
ATOM   1648  CG  ASP A 215      42.272 -23.714 -20.509  1.00 79.50           C  
ATOM   1649  OD1 ASP A 215      43.345 -23.475 -19.885  1.00 86.62           O  
ATOM   1650  OD2 ASP A 215      41.730 -24.816 -20.332  1.00 83.18           O  
ATOM   1651  N   GLY A 216      39.833 -19.238 -20.848  1.00 44.65           N  
ATOM   1652  CA  GLY A 216      39.421 -17.860 -21.114  1.00 36.46           C  
ATOM   1653  C   GLY A 216      40.592 -16.958 -21.465  1.00 32.57           C  
ATOM   1654  O   GLY A 216      41.721 -17.148 -21.003  1.00 32.81           O  
ATOM   1655  N   GLN A 217      40.285 -15.939 -22.257  1.00 27.83           N  
ATOM   1656  CA  GLN A 217      41.251 -14.934 -22.660  1.00 26.52           C  
ATOM   1657  C   GLN A 217      40.464 -13.656 -22.892  1.00 26.84           C  
ATOM   1658  O   GLN A 217      39.365 -13.704 -23.449  1.00 27.89           O  
ATOM   1659  CB  GLN A 217      41.957 -15.345 -23.949  1.00 27.00           C  
ATOM   1660  CG  GLN A 217      43.073 -14.398 -24.392  1.00 30.70           C  
ATOM   1661  CD  GLN A 217      44.124 -14.101 -23.328  1.00 38.75           C  
ATOM   1662  OE1 GLN A 217      44.886 -14.961 -22.886  1.00 47.03           O  
ATOM   1663  NE2 GLN A 217      44.208 -12.861 -22.870  1.00 47.14           N  
ATOM   1664  N   VAL A 218      40.974 -12.532 -22.391  1.00 24.80           N  
ATOM   1665  CA  VAL A 218      40.375 -11.232 -22.608  1.00 23.44           C  
ATOM   1666  C   VAL A 218      41.365 -10.506 -23.500  1.00 22.48           C  
ATOM   1667  O   VAL A 218      42.574 -10.531 -23.245  1.00 20.92           O  
ATOM   1668  CB  VAL A 218      40.198 -10.461 -21.270  1.00 26.56           C  
ATOM   1669  CG1 VAL A 218      39.597  -9.065 -21.527  1.00 18.68           C  
ATOM   1670  CG2 VAL A 218      39.293 -11.279 -20.346  1.00 22.51           C  
ATOM   1671  N   THR A 219      40.834  -9.858 -24.528  1.00 20.97           N  
ATOM   1672  CA  THR A 219      41.615  -9.070 -25.453  1.00 20.40           C  
ATOM   1673  C   THR A 219      40.978  -7.694 -25.503  1.00 18.77           C  
ATOM   1674  O   THR A 219      39.750  -7.559 -25.556  1.00 22.07           O  
ATOM   1675  CB  THR A 219      41.581  -9.719 -26.842  1.00 15.07           C  
ATOM   1676  OG1 THR A 219      42.079 -11.037 -26.692  1.00 17.36           O  
ATOM   1677  CG2 THR A 219      42.410  -8.971 -27.861  1.00 21.91           C  
ATOM   1678  N   LEU A 220      41.811  -6.671 -25.492  1.00 18.12           N  
ATOM   1679  CA  LEU A 220      41.389  -5.283 -25.606  1.00 21.78           C  
ATOM   1680  C   LEU A 220      42.011  -4.833 -26.925  1.00 23.85           C  
ATOM   1681  O   LEU A 220      43.187  -5.152 -27.146  1.00 21.46           O  
ATOM   1682  CB  LEU A 220      41.979  -4.493 -24.431  1.00 20.55           C  
ATOM   1683  CG  LEU A 220      41.930  -2.987 -24.070  1.00 22.06           C  
ATOM   1684  CD1 LEU A 220      42.253  -2.068 -25.235  1.00 18.12           C  
ATOM   1685  CD2 LEU A 220      40.567  -2.704 -23.557  1.00 24.25           C  
ATOM   1686  N   CYS A 221      41.328  -4.145 -27.840  1.00 23.62           N  
ATOM   1687  CA  CYS A 221      42.010  -3.586 -28.994  1.00 23.06           C  
ATOM   1688  C   CYS A 221      41.641  -2.127 -29.064  1.00 21.98           C  
ATOM   1689  O   CYS A 221      40.561  -1.712 -28.633  1.00 22.49           O  
ATOM   1690  CB  CYS A 221      41.621  -4.274 -30.315  1.00 17.96           C  
ATOM   1691  SG  CYS A 221      39.914  -4.100 -30.838  1.00 26.60           S  
ATOM   1692  N   TYR A 222      42.611  -1.336 -29.468  1.00 21.28           N  
ATOM   1693  CA  TYR A 222      42.435   0.080 -29.612  1.00 19.69           C  
ATOM   1694  C   TYR A 222      43.104   0.412 -30.924  1.00 21.88           C  
ATOM   1695  O   TYR A 222      44.215  -0.048 -31.192  1.00 22.97           O  
ATOM   1696  CB  TYR A 222      43.124   0.817 -28.470  1.00 12.30           C  
ATOM   1697  CG  TYR A 222      43.079   2.332 -28.614  1.00 10.12           C  
ATOM   1698  CD1 TYR A 222      41.931   2.993 -29.076  1.00  5.98           C  
ATOM   1699  CD2 TYR A 222      44.227   3.057 -28.316  1.00  8.63           C  
ATOM   1700  CE1 TYR A 222      41.930   4.373 -29.252  1.00 11.23           C  
ATOM   1701  CE2 TYR A 222      44.232   4.440 -28.488  1.00 17.04           C  
ATOM   1702  CZ  TYR A 222      43.090   5.084 -28.956  1.00 14.77           C  
ATOM   1703  OH  TYR A 222      43.128   6.445 -29.141  1.00 29.17           O  
ATOM   1704  N   ARG A 223      42.474   1.272 -31.713  1.00 25.34           N  
ATOM   1705  CA  ARG A 223      43.024   1.638 -33.000  1.00 27.84           C  
ATOM   1706  C   ARG A 223      44.215   2.562 -32.895  1.00 26.13           C  
ATOM   1707  O   ARG A 223      45.018   2.589 -33.827  1.00 30.09           O  
ATOM   1708  CB  ARG A 223      41.946   2.288 -33.889  1.00 25.49           C  
ATOM   1709  CG  ARG A 223      41.381   3.627 -33.470  1.00 30.60           C  
ATOM   1710  CD  ARG A 223      40.175   3.957 -34.322  1.00 25.99           C  
ATOM   1711  NE  ARG A 223      39.618   5.234 -33.909  1.00 35.27           N  
ATOM   1712  CZ  ARG A 223      38.505   5.719 -34.468  1.00 38.18           C  
ATOM   1713  NH1 ARG A 223      37.846   5.066 -35.437  1.00 36.60           N  
ATOM   1714  NH2 ARG A 223      38.021   6.872 -34.020  1.00 44.08           N  
ATOM   1715  N   GLY A 224      44.354   3.335 -31.812  1.00 24.78           N  
ATOM   1716  CA  GLY A 224      45.498   4.225 -31.648  1.00 22.57           C  
ATOM   1717  C   GLY A 224      46.704   3.523 -31.037  1.00 22.75           C  
ATOM   1718  O   GLY A 224      46.726   2.309 -30.868  1.00 19.16           O  
ATOM   1719  N   GLU A 225      47.687   4.330 -30.635  1.00 26.89           N  
ATOM   1720  CA  GLU A 225      48.979   3.826 -30.171  1.00 32.22           C  
ATOM   1721  C   GLU A 225      49.022   3.205 -28.777  1.00 29.81           C  
ATOM   1722  O   GLU A 225      49.849   2.316 -28.544  1.00 30.10           O  
ATOM   1723  CB  GLU A 225      50.143   4.835 -29.975  1.00 40.33           C  
ATOM   1724  CG  GLU A 225      51.089   5.972 -30.457  1.00 59.40           C  
ATOM   1725  CD  GLU A 225      52.146   5.945 -31.567  1.00 72.20           C  
ATOM   1726  OE1 GLU A 225      52.313   4.931 -32.241  1.00 76.12           O  
ATOM   1727  OE2 GLU A 225      52.789   6.984 -31.761  1.00 81.74           O  
ATOM   1728  N   MET A 226      48.244   3.721 -27.819  1.00 29.46           N  
ATOM   1729  CA  MET A 226      48.248   3.256 -26.438  1.00 28.95           C  
ATOM   1730  C   MET A 226      46.890   3.574 -25.836  1.00 28.47           C  
ATOM   1731  O   MET A 226      46.220   4.535 -26.253  1.00 27.89           O  
ATOM   1732  CB  MET A 226      49.355   3.976 -25.670  1.00 26.61           C  
ATOM   1733  CG  MET A 226      49.796   3.322 -24.377  1.00 30.72           C  
ATOM   1734  SD  MET A 226      51.493   3.801 -23.959  1.00 37.65           S  
ATOM   1735  CE  MET A 226      51.245   5.531 -23.878  1.00 24.04           C  
ATOM   1736  N   ILE A 227      46.476   2.709 -24.900  1.00 26.36           N  
ATOM   1737  CA  ILE A 227      45.217   2.877 -24.182  1.00 22.73           C  
ATOM   1738  C   ILE A 227      45.200   4.179 -23.387  1.00 22.53           C  
ATOM   1739  O   ILE A 227      46.224   4.805 -23.126  1.00 21.23           O  
ATOM   1740  CB  ILE A 227      44.933   1.697 -23.186  1.00 22.18           C  
ATOM   1741  CG1 ILE A 227      46.052   1.513 -22.158  1.00 19.96           C  
ATOM   1742  CG2 ILE A 227      44.716   0.438 -24.011  1.00 18.05           C  
ATOM   1743  CD1 ILE A 227      45.723   0.488 -21.062  1.00 12.56           C  
ATOM   1744  N   LEU A 228      43.997   4.569 -23.005  1.00 22.85           N  
ATOM   1745  CA  LEU A 228      43.726   5.756 -22.222  1.00 22.92           C  
ATOM   1746  C   LEU A 228      44.309   7.063 -22.732  1.00 23.50           C  
ATOM   1747  O   LEU A 228      44.992   7.833 -22.038  1.00 24.16           O  
ATOM   1748  CB  LEU A 228      44.167   5.475 -20.767  1.00 17.42           C  
ATOM   1749  CG  LEU A 228      43.334   4.459 -19.996  1.00 13.88           C  
ATOM   1750  CD1 LEU A 228      43.854   4.394 -18.586  1.00 17.44           C  
ATOM   1751  CD2 LEU A 228      41.879   4.867 -19.939  1.00  6.29           C  
ATOM   1752  N   ARG A 229      43.965   7.366 -23.979  1.00 24.25           N  
ATOM   1753  CA  ARG A 229      44.312   8.629 -24.592  1.00 23.24           C  
ATOM   1754  C   ARG A 229      43.680   9.690 -23.702  1.00 23.49           C  
ATOM   1755  O   ARG A 229      42.531   9.552 -23.253  1.00 24.10           O  
ATOM   1756  CB  ARG A 229      43.721   8.702 -25.989  1.00 32.64           C  
ATOM   1757  CG  ARG A 229      44.028  10.002 -26.730  1.00 47.15           C  
ATOM   1758  CD  ARG A 229      43.241  10.150 -28.029  1.00 66.07           C  
ATOM   1759  NE  ARG A 229      41.806  10.198 -27.771  1.00 82.84           N  
ATOM   1760  CZ  ARG A 229      41.065  11.311 -27.888  1.00 87.15           C  
ATOM   1761  NH1 ARG A 229      41.584  12.486 -28.262  1.00 94.87           N  
ATOM   1762  NH2 ARG A 229      39.764  11.243 -27.595  1.00 94.77           N  
ATOM   1763  N   GLY A 230      44.466  10.712 -23.373  1.00 20.90           N  
ATOM   1764  CA  GLY A 230      43.958  11.788 -22.548  1.00 17.56           C  
ATOM   1765  C   GLY A 230      44.501  11.716 -21.135  1.00 20.03           C  
ATOM   1766  O   GLY A 230      44.431  12.691 -20.401  1.00 19.16           O  
ATOM   1767  N   PHE A 231      45.039  10.575 -20.729  1.00 18.90           N  
ATOM   1768  CA  PHE A 231      45.637  10.424 -19.426  1.00 20.00           C  
ATOM   1769  C   PHE A 231      47.142  10.629 -19.563  1.00 22.57           C  
ATOM   1770  O   PHE A 231      47.703  10.768 -20.657  1.00 26.14           O  
ATOM   1771  CB  PHE A 231      45.290   9.015 -18.879  1.00 14.84           C  
ATOM   1772  CG  PHE A 231      43.831   8.947 -18.455  1.00 18.66           C  
ATOM   1773  CD1 PHE A 231      42.813   8.786 -19.400  1.00 16.78           C  
ATOM   1774  CD2 PHE A 231      43.505   9.096 -17.106  1.00 17.38           C  
ATOM   1775  CE1 PHE A 231      41.474   8.772 -18.995  1.00 17.57           C  
ATOM   1776  CE2 PHE A 231      42.165   9.084 -16.710  1.00 16.32           C  
ATOM   1777  CZ  PHE A 231      41.147   8.925 -17.649  1.00 15.88           C  
ATOM   1778  N   ASP A 232      47.793  10.695 -18.405  1.00 21.94           N  
ATOM   1779  CA  ASP A 232      49.217  10.854 -18.321  1.00 21.66           C  
ATOM   1780  C   ASP A 232      49.923   9.701 -19.006  1.00 20.93           C  
ATOM   1781  O   ASP A 232      49.663   8.530 -18.725  1.00 23.93           O  
ATOM   1782  CB  ASP A 232      49.592  10.916 -16.859  1.00 20.50           C  
ATOM   1783  CG  ASP A 232      51.085  10.932 -16.608  1.00 23.78           C  
ATOM   1784  OD1 ASP A 232      51.723   9.890 -16.469  1.00 26.12           O  
ATOM   1785  OD2 ASP A 232      51.619  11.999 -16.538  1.00 19.62           O  
ATOM   1786  N   HIS A 233      50.937  10.042 -19.779  1.00 23.37           N  
ATOM   1787  CA  HIS A 233      51.651   9.062 -20.556  1.00 26.15           C  
ATOM   1788  C   HIS A 233      52.358   7.988 -19.744  1.00 23.18           C  
ATOM   1789  O   HIS A 233      52.361   6.835 -20.197  1.00 24.17           O  
ATOM   1790  CB  HIS A 233      52.634   9.798 -21.434  1.00 34.90           C  
ATOM   1791  CG  HIS A 233      53.010   8.982 -22.659  1.00 57.69           C  
ATOM   1792  ND1 HIS A 233      52.311   8.836 -23.783  1.00 62.52           N  
ATOM   1793  CD2 HIS A 233      54.177   8.269 -22.806  1.00 65.46           C  
ATOM   1794  CE1 HIS A 233      53.012   8.077 -24.595  1.00 71.86           C  
ATOM   1795  NE2 HIS A 233      54.125   7.738 -23.997  1.00 72.22           N  
ATOM   1796  N   THR A 234      52.926   8.282 -18.570  1.00 21.11           N  
ATOM   1797  CA  THR A 234      53.596   7.235 -17.793  1.00 22.21           C  
ATOM   1798  C   THR A 234      52.573   6.244 -17.264  1.00 21.33           C  
ATOM   1799  O   THR A 234      52.810   5.033 -17.256  1.00 24.63           O  
ATOM   1800  CB  THR A 234      54.350   7.812 -16.597  1.00 24.81           C  
ATOM   1801  OG1 THR A 234      54.995   8.971 -17.096  1.00 20.82           O  
ATOM   1802  CG2 THR A 234      55.329   6.829 -15.961  1.00 20.13           C  
ATOM   1803  N   LEU A 235      51.424   6.776 -16.840  1.00 20.89           N  
ATOM   1804  CA  LEU A 235      50.343   5.944 -16.328  1.00 22.54           C  
ATOM   1805  C   LEU A 235      49.831   5.071 -17.462  1.00 20.19           C  
ATOM   1806  O   LEU A 235      49.593   3.884 -17.230  1.00 23.76           O  
ATOM   1807  CB  LEU A 235      49.195   6.821 -15.783  1.00 21.05           C  
ATOM   1808  CG  LEU A 235      49.189   7.309 -14.352  1.00 13.73           C  
ATOM   1809  CD1 LEU A 235      50.502   7.961 -13.955  1.00 17.48           C  
ATOM   1810  CD2 LEU A 235      48.019   8.254 -14.238  1.00 10.88           C  
ATOM   1811  N   ARG A 236      49.703   5.604 -18.686  1.00 18.97           N  
ATOM   1812  CA  ARG A 236      49.309   4.790 -19.842  1.00 19.36           C  
ATOM   1813  C   ARG A 236      50.282   3.646 -20.124  1.00 16.86           C  
ATOM   1814  O   ARG A 236      49.886   2.478 -20.215  1.00 19.71           O  
ATOM   1815  CB  ARG A 236      49.206   5.674 -21.069  1.00 19.43           C  
ATOM   1816  CG  ARG A 236      48.140   6.748 -20.920  1.00 12.38           C  
ATOM   1817  CD  ARG A 236      48.306   7.716 -22.051  1.00 14.46           C  
ATOM   1818  NE  ARG A 236      47.840   7.091 -23.270  1.00 15.45           N  
ATOM   1819  CZ  ARG A 236      47.939   7.692 -24.456  1.00 21.51           C  
ATOM   1820  NH1 ARG A 236      48.487   8.895 -24.583  1.00 21.65           N  
ATOM   1821  NH2 ARG A 236      47.413   7.100 -25.529  1.00 22.61           N  
ATOM   1822  N   GLU A 237      51.584   3.923 -20.176  1.00 19.93           N  
ATOM   1823  CA  GLU A 237      52.571   2.879 -20.429  1.00 22.77           C  
ATOM   1824  C   GLU A 237      52.559   1.817 -19.347  1.00 23.81           C  
ATOM   1825  O   GLU A 237      52.505   0.610 -19.618  1.00 28.35           O  
ATOM   1826  CB  GLU A 237      53.968   3.437 -20.470  1.00 31.71           C  
ATOM   1827  CG  GLU A 237      54.189   4.495 -21.525  1.00 49.38           C  
ATOM   1828  CD  GLU A 237      55.568   5.117 -21.413  1.00 59.69           C  
ATOM   1829  OE1 GLU A 237      56.543   4.417 -21.697  1.00 71.72           O  
ATOM   1830  OE2 GLU A 237      55.666   6.286 -21.037  1.00 63.11           O  
ATOM   1831  N   GLU A 238      52.603   2.291 -18.094  1.00 25.22           N  
ATOM   1832  CA  GLU A 238      52.573   1.427 -16.928  1.00 20.14           C  
ATOM   1833  C   GLU A 238      51.344   0.554 -16.769  1.00 17.33           C  
ATOM   1834  O   GLU A 238      51.463  -0.648 -16.495  1.00 17.67           O  
ATOM   1835  CB  GLU A 238      52.739   2.263 -15.672  1.00 25.33           C  
ATOM   1836  CG  GLU A 238      54.189   2.341 -15.227  1.00 30.60           C  
ATOM   1837  CD  GLU A 238      54.872   0.983 -15.027  1.00 35.78           C  
ATOM   1838  OE1 GLU A 238      54.269   0.017 -14.526  1.00 33.45           O  
ATOM   1839  OE2 GLU A 238      56.039   0.908 -15.401  1.00 35.69           O  
ATOM   1840  N   LEU A 239      50.154   1.119 -16.969  1.00 18.17           N  
ATOM   1841  CA  LEU A 239      48.930   0.356 -16.858  1.00 16.82           C  
ATOM   1842  C   LEU A 239      48.924  -0.705 -17.927  1.00 18.47           C  
ATOM   1843  O   LEU A 239      48.555  -1.837 -17.617  1.00 20.91           O  
ATOM   1844  CB  LEU A 239      47.682   1.241 -17.017  1.00 12.06           C  
ATOM   1845  CG  LEU A 239      46.363   0.469 -16.834  1.00 15.83           C  
ATOM   1846  CD1 LEU A 239      46.296  -0.208 -15.465  1.00 12.57           C  
ATOM   1847  CD2 LEU A 239      45.221   1.423 -16.966  1.00 17.34           C  
ATOM   1848  N   THR A 240      49.377  -0.409 -19.148  1.00 20.93           N  
ATOM   1849  CA  THR A 240      49.455  -1.424 -20.194  1.00 19.30           C  
ATOM   1850  C   THR A 240      50.345  -2.560 -19.714  1.00 18.43           C  
ATOM   1851  O   THR A 240      49.951  -3.723 -19.798  1.00 15.99           O  
ATOM   1852  CB  THR A 240      50.013  -0.791 -21.484  1.00 21.80           C  
ATOM   1853  OG1 THR A 240      49.163   0.287 -21.856  1.00 19.49           O  
ATOM   1854  CG2 THR A 240      50.058  -1.799 -22.615  1.00 16.60           C  
ATOM   1855  N   LYS A 241      51.515  -2.257 -19.140  1.00 22.44           N  
ATOM   1856  CA  LYS A 241      52.385  -3.279 -18.572  1.00 22.94           C  
ATOM   1857  C   LYS A 241      51.687  -4.137 -17.524  1.00 25.33           C  
ATOM   1858  O   LYS A 241      51.701  -5.376 -17.598  1.00 27.70           O  
ATOM   1859  CB  LYS A 241      53.614  -2.619 -17.948  1.00 24.11           C  
ATOM   1860  CG  LYS A 241      54.675  -2.423 -19.009  1.00 32.87           C  
ATOM   1861  CD  LYS A 241      55.766  -1.405 -18.686  1.00 42.29           C  
ATOM   1862  CE  LYS A 241      56.682  -1.768 -17.519  1.00 54.41           C  
ATOM   1863  NZ  LYS A 241      57.800  -0.837 -17.447  1.00 55.85           N  
ATOM   1864  N   GLN A 242      50.988  -3.517 -16.575  1.00 25.97           N  
ATOM   1865  CA  GLN A 242      50.386  -4.271 -15.485  1.00 21.30           C  
ATOM   1866  C   GLN A 242      49.167  -5.081 -15.880  1.00 20.32           C  
ATOM   1867  O   GLN A 242      48.993  -6.198 -15.373  1.00 19.35           O  
ATOM   1868  CB  GLN A 242      50.077  -3.291 -14.373  1.00 19.39           C  
ATOM   1869  CG  GLN A 242      51.419  -2.903 -13.760  1.00 22.10           C  
ATOM   1870  CD  GLN A 242      51.339  -1.908 -12.621  1.00 19.39           C  
ATOM   1871  OE1 GLN A 242      50.484  -2.012 -11.751  1.00 26.08           O  
ATOM   1872  NE2 GLN A 242      52.193  -0.904 -12.539  1.00 18.25           N  
ATOM   1873  N   LEU A 243      48.363  -4.599 -16.833  1.00 21.36           N  
ATOM   1874  CA  LEU A 243      47.230  -5.345 -17.368  1.00 19.06           C  
ATOM   1875  C   LEU A 243      47.748  -6.535 -18.151  1.00 18.59           C  
ATOM   1876  O   LEU A 243      47.255  -7.654 -17.986  1.00 19.29           O  
ATOM   1877  CB  LEU A 243      46.378  -4.489 -18.309  1.00 20.03           C  
ATOM   1878  CG  LEU A 243      45.519  -3.349 -17.748  1.00 22.63           C  
ATOM   1879  CD1 LEU A 243      44.883  -2.605 -18.907  1.00 21.30           C  
ATOM   1880  CD2 LEU A 243      44.433  -3.885 -16.816  1.00 20.25           C  
ATOM   1881  N   THR A 244      48.782  -6.328 -18.961  1.00 23.34           N  
ATOM   1882  CA  THR A 244      49.382  -7.411 -19.733  1.00 27.11           C  
ATOM   1883  C   THR A 244      49.913  -8.438 -18.750  1.00 25.00           C  
ATOM   1884  O   THR A 244      49.609  -9.615 -18.863  1.00 26.31           O  
ATOM   1885  CB  THR A 244      50.529  -6.867 -20.613  1.00 26.11           C  
ATOM   1886  OG1 THR A 244      49.947  -5.936 -21.514  1.00 27.79           O  
ATOM   1887  CG2 THR A 244      51.258  -7.951 -21.384  1.00 34.62           C  
ATOM   1888  N   ALA A 245      50.630  -7.991 -17.714  1.00 26.31           N  
ATOM   1889  CA  ALA A 245      51.178  -8.896 -16.721  1.00 24.48           C  
ATOM   1890  C   ALA A 245      50.099  -9.725 -16.043  1.00 23.87           C  
ATOM   1891  O   ALA A 245      50.360 -10.824 -15.569  1.00 24.99           O  
ATOM   1892  CB  ALA A 245      51.927  -8.098 -15.670  1.00 25.12           C  
ATOM   1893  N   ASN A 246      48.850  -9.261 -16.018  1.00 23.39           N  
ATOM   1894  CA  ASN A 246      47.824 -10.050 -15.392  1.00 21.35           C  
ATOM   1895  C   ASN A 246      47.029 -10.864 -16.402  1.00 23.23           C  
ATOM   1896  O   ASN A 246      45.947 -11.357 -16.066  1.00 25.07           O  
ATOM   1897  CB  ASN A 246      46.902  -9.129 -14.580  1.00 21.38           C  
ATOM   1898  CG  ASN A 246      46.139  -9.866 -13.471  1.00 20.97           C  
ATOM   1899  OD1 ASN A 246      45.049  -9.476 -13.061  1.00 24.74           O  
ATOM   1900  ND2 ASN A 246      46.628 -10.956 -12.882  1.00 20.57           N  
ATOM   1901  N   GLY A 247      47.454 -11.012 -17.655  1.00 24.90           N  
ATOM   1902  CA  GLY A 247      46.781 -11.935 -18.568  1.00 24.42           C  
ATOM   1903  C   GLY A 247      45.907 -11.329 -19.657  1.00 26.27           C  
ATOM   1904  O   GLY A 247      45.405 -12.069 -20.501  1.00 24.86           O  
ATOM   1905  N   ILE A 248      45.703 -10.006 -19.682  1.00 27.86           N  
ATOM   1906  CA  ILE A 248      44.889  -9.334 -20.695  1.00 27.10           C  
ATOM   1907  C   ILE A 248      45.812  -9.104 -21.879  1.00 28.57           C  
ATOM   1908  O   ILE A 248      46.973  -8.701 -21.724  1.00 29.15           O  
ATOM   1909  CB  ILE A 248      44.365  -8.002 -20.107  1.00 26.88           C  
ATOM   1910  CG1 ILE A 248      43.465  -8.372 -18.925  1.00 25.01           C  
ATOM   1911  CG2 ILE A 248      43.604  -7.161 -21.135  1.00 26.18           C  
ATOM   1912  CD1 ILE A 248      43.028  -7.204 -18.020  1.00 20.05           C  
ATOM   1913  N   GLN A 249      45.336  -9.436 -23.078  1.00 30.15           N  
ATOM   1914  CA  GLN A 249      46.119  -9.215 -24.269  1.00 27.20           C  
ATOM   1915  C   GLN A 249      45.666  -7.889 -24.834  1.00 23.93           C  
ATOM   1916  O   GLN A 249      44.473  -7.681 -25.051  1.00 24.63           O  
ATOM   1917  CB  GLN A 249      45.862 -10.326 -25.236  1.00 30.65           C  
ATOM   1918  CG  GLN A 249      46.622 -10.059 -26.524  1.00 40.29           C  
ATOM   1919  CD  GLN A 249      46.416 -11.121 -27.583  1.00 45.28           C  
ATOM   1920  OE1 GLN A 249      45.349 -11.704 -27.754  1.00 45.79           O  
ATOM   1921  NE2 GLN A 249      47.475 -11.393 -28.336  1.00 54.90           N  
ATOM   1922  N   ILE A 250      46.584  -6.969 -25.047  1.00 21.72           N  
ATOM   1923  CA  ILE A 250      46.235  -5.678 -25.604  1.00 24.52           C  
ATOM   1924  C   ILE A 250      46.728  -5.570 -27.046  1.00 26.46           C  
ATOM   1925  O   ILE A 250      47.927  -5.723 -27.309  1.00 27.69           O  
ATOM   1926  CB  ILE A 250      46.851  -4.612 -24.678  1.00 22.48           C  
ATOM   1927  CG1 ILE A 250      46.130  -4.731 -23.332  1.00 21.21           C  
ATOM   1928  CG2 ILE A 250      46.733  -3.197 -25.273  1.00 18.54           C  
ATOM   1929  CD1 ILE A 250      46.783  -3.928 -22.210  1.00 23.27           C  
ATOM   1930  N   LEU A 251      45.826  -5.335 -27.993  1.00 25.16           N  
ATOM   1931  CA  LEU A 251      46.135  -5.174 -29.403  1.00 21.65           C  
ATOM   1932  C   LEU A 251      45.933  -3.711 -29.721  1.00 22.34           C  
ATOM   1933  O   LEU A 251      44.824  -3.210 -29.898  1.00 22.55           O  
ATOM   1934  CB  LEU A 251      45.200  -5.983 -30.270  1.00 21.12           C  
ATOM   1935  CG  LEU A 251      45.255  -7.483 -30.152  1.00 24.41           C  
ATOM   1936  CD1 LEU A 251      44.188  -8.084 -31.044  1.00 28.64           C  
ATOM   1937  CD2 LEU A 251      46.639  -7.970 -30.534  1.00 32.94           C  
ATOM   1938  N   THR A 252      47.016  -2.981 -29.665  1.00 21.29           N  
ATOM   1939  CA  THR A 252      47.013  -1.575 -30.011  1.00 27.22           C  
ATOM   1940  C   THR A 252      47.210  -1.453 -31.541  1.00 29.00           C  
ATOM   1941  O   THR A 252      47.678  -2.399 -32.189  1.00 28.26           O  
ATOM   1942  CB  THR A 252      48.135  -0.984 -29.130  1.00 24.75           C  
ATOM   1943  OG1 THR A 252      48.143   0.392 -29.359  1.00 42.33           O  
ATOM   1944  CG2 THR A 252      49.524  -1.488 -29.465  1.00 34.30           C  
ATOM   1945  N   LYS A 253      46.869  -0.327 -32.166  1.00 30.07           N  
ATOM   1946  CA  LYS A 253      46.946  -0.096 -33.611  1.00 29.72           C  
ATOM   1947  C   LYS A 253      46.275  -1.159 -34.461  1.00 28.18           C  
ATOM   1948  O   LYS A 253      46.670  -1.500 -35.579  1.00 31.33           O  
ATOM   1949  CB  LYS A 253      48.406   0.057 -34.042  1.00 28.56           C  
ATOM   1950  CG  LYS A 253      48.879   1.504 -34.044  1.00 32.60           C  
ATOM   1951  CD  LYS A 253      50.389   1.478 -34.050  1.00 35.56           C  
ATOM   1952  CE  LYS A 253      50.962   2.840 -34.375  1.00 44.80           C  
ATOM   1953  NZ  LYS A 253      52.403   2.829 -34.168  1.00 47.73           N  
ATOM   1954  N   GLU A 254      45.217  -1.715 -33.905  1.00 25.84           N  
ATOM   1955  CA  GLU A 254      44.414  -2.663 -34.616  1.00 23.81           C  
ATOM   1956  C   GLU A 254      43.054  -2.010 -34.680  1.00 24.72           C  
ATOM   1957  O   GLU A 254      42.623  -1.373 -33.717  1.00 26.40           O  
ATOM   1958  CB  GLU A 254      44.375  -3.970 -33.851  1.00 23.03           C  
ATOM   1959  CG  GLU A 254      45.669  -4.767 -33.985  1.00 26.91           C  
ATOM   1960  CD  GLU A 254      46.047  -5.191 -35.404  1.00 31.70           C  
ATOM   1961  OE1 GLU A 254      45.160  -5.476 -36.206  1.00 28.56           O  
ATOM   1962  OE2 GLU A 254      47.238  -5.251 -35.707  1.00 31.33           O  
ATOM   1963  N   ASN A 255      42.357  -2.142 -35.801  1.00 24.63           N  
ATOM   1964  CA  ASN A 255      41.075  -1.487 -35.980  1.00 25.22           C  
ATOM   1965  C   ASN A 255      40.107  -2.464 -36.640  1.00 27.89           C  
ATOM   1966  O   ASN A 255      40.454  -2.989 -37.705  1.00 31.50           O  
ATOM   1967  CB  ASN A 255      41.306  -0.259 -36.848  1.00 24.84           C  
ATOM   1968  CG  ASN A 255      40.108   0.654 -36.982  1.00 23.34           C  
ATOM   1969  OD1 ASN A 255      39.084   0.507 -36.322  1.00 27.08           O  
ATOM   1970  ND2 ASN A 255      40.194   1.659 -37.826  1.00 20.97           N  
ATOM   1971  N   PRO A 256      38.966  -2.849 -36.075  1.00 27.68           N  
ATOM   1972  CA  PRO A 256      38.031  -3.797 -36.679  1.00 27.12           C  
ATOM   1973  C   PRO A 256      37.465  -3.344 -38.029  1.00 27.13           C  
ATOM   1974  O   PRO A 256      37.046  -2.197 -38.165  1.00 25.51           O  
ATOM   1975  CB  PRO A 256      36.940  -3.980 -35.628  1.00 28.78           C  
ATOM   1976  CG  PRO A 256      37.562  -3.493 -34.331  1.00 27.75           C  
ATOM   1977  CD  PRO A 256      38.468  -2.359 -34.790  1.00 30.10           C  
ATOM   1978  N   ALA A 257      37.457  -4.232 -39.036  1.00 26.72           N  
ATOM   1979  CA  ALA A 257      36.891  -3.950 -40.359  1.00 26.23           C  
ATOM   1980  C   ALA A 257      35.479  -4.491 -40.462  1.00 24.53           C  
ATOM   1981  O   ALA A 257      34.592  -3.835 -41.007  1.00 28.32           O  
ATOM   1982  CB  ALA A 257      37.719  -4.602 -41.468  1.00 20.02           C  
ATOM   1983  N   LYS A 258      35.238  -5.686 -39.937  1.00 24.32           N  
ATOM   1984  CA  LYS A 258      33.912  -6.268 -39.954  1.00 26.40           C  
ATOM   1985  C   LYS A 258      33.857  -7.354 -38.902  1.00 28.05           C  
ATOM   1986  O   LYS A 258      34.904  -7.890 -38.506  1.00 26.96           O  
ATOM   1987  CB  LYS A 258      33.595  -6.884 -41.326  1.00 31.99           C  
ATOM   1988  CG  LYS A 258      34.472  -8.032 -41.779  1.00 30.20           C  
ATOM   1989  CD  LYS A 258      33.912  -8.519 -43.097  1.00 47.03           C  
ATOM   1990  CE  LYS A 258      34.669  -9.769 -43.514  1.00 47.11           C  
ATOM   1991  NZ  LYS A 258      36.023  -9.451 -43.913  1.00 50.32           N  
ATOM   1992  N   VAL A 259      32.641  -7.654 -38.459  1.00 27.31           N  
ATOM   1993  CA  VAL A 259      32.381  -8.708 -37.492  1.00 27.17           C  
ATOM   1994  C   VAL A 259      31.403  -9.675 -38.152  1.00 30.84           C  
ATOM   1995  O   VAL A 259      30.347  -9.268 -38.660  1.00 34.23           O  
ATOM   1996  CB  VAL A 259      31.722  -8.156 -36.191  1.00 23.28           C  
ATOM   1997  CG1 VAL A 259      31.446  -9.314 -35.242  1.00 21.34           C  
ATOM   1998  CG2 VAL A 259      32.629  -7.150 -35.503  1.00 19.39           C  
ATOM   1999  N   GLU A 260      31.681 -10.964 -38.193  1.00 31.46           N  
ATOM   2000  CA  GLU A 260      30.684 -11.852 -38.722  1.00 36.64           C  
ATOM   2001  C   GLU A 260      30.511 -13.040 -37.825  1.00 37.88           C  
ATOM   2002  O   GLU A 260      31.389 -13.421 -37.063  1.00 36.97           O  
ATOM   2003  CB  GLU A 260      31.061 -12.265 -40.141  1.00 47.27           C  
ATOM   2004  CG  GLU A 260      32.491 -12.646 -40.441  1.00 53.54           C  
ATOM   2005  CD  GLU A 260      32.893 -12.564 -41.918  1.00 63.57           C  
ATOM   2006  OE1 GLU A 260      32.174 -11.988 -42.745  1.00 62.94           O  
ATOM   2007  OE2 GLU A 260      33.966 -13.077 -42.243  1.00 67.73           O  
ATOM   2008  N   LEU A 261      29.276 -13.500 -37.859  1.00 40.38           N  
ATOM   2009  CA  LEU A 261      28.812 -14.574 -37.015  1.00 44.58           C  
ATOM   2010  C   LEU A 261      29.104 -15.925 -37.643  1.00 47.30           C  
ATOM   2011  O   LEU A 261      28.616 -16.231 -38.733  1.00 51.24           O  
ATOM   2012  CB  LEU A 261      27.316 -14.328 -36.799  1.00 41.42           C  
ATOM   2013  CG  LEU A 261      26.506 -15.226 -35.887  1.00 39.49           C  
ATOM   2014  CD1 LEU A 261      27.093 -15.239 -34.495  1.00 41.85           C  
ATOM   2015  CD2 LEU A 261      25.086 -14.712 -35.839  1.00 40.52           C  
ATOM   2016  N   ASN A 262      29.954 -16.701 -36.983  1.00 49.00           N  
ATOM   2017  CA  ASN A 262      30.292 -18.048 -37.393  1.00 49.84           C  
ATOM   2018  C   ASN A 262      29.157 -18.990 -37.057  1.00 53.43           C  
ATOM   2019  O   ASN A 262      28.443 -18.775 -36.079  1.00 54.11           O  
ATOM   2020  CB  ASN A 262      31.533 -18.516 -36.675  1.00 47.64           C  
ATOM   2021  CG  ASN A 262      32.803 -17.855 -37.180  1.00 55.24           C  
ATOM   2022  OD1 ASN A 262      32.870 -17.229 -38.239  1.00 58.02           O  
ATOM   2023  ND2 ASN A 262      33.897 -17.994 -36.443  1.00 56.65           N  
ATOM   2024  N   ALA A 263      29.011 -20.105 -37.781  1.00 57.67           N  
ATOM   2025  CA  ALA A 263      27.926 -21.073 -37.585  1.00 59.06           C  
ATOM   2026  C   ALA A 263      27.641 -21.549 -36.166  1.00 59.90           C  
ATOM   2027  O   ALA A 263      26.491 -21.790 -35.809  1.00 60.16           O  
ATOM   2028  CB  ALA A 263      28.178 -22.331 -38.398  1.00 60.72           C  
ATOM   2029  N   ASP A 264      28.691 -21.710 -35.351  1.00 59.82           N  
ATOM   2030  CA  ASP A 264      28.532 -22.143 -33.965  1.00 60.59           C  
ATOM   2031  C   ASP A 264      28.045 -21.044 -33.023  1.00 59.40           C  
ATOM   2032  O   ASP A 264      27.599 -21.304 -31.903  1.00 61.57           O  
ATOM   2033  CB  ASP A 264      29.873 -22.711 -33.456  1.00 61.56           C  
ATOM   2034  CG  ASP A 264      31.059 -21.752 -33.423  1.00 63.35           C  
ATOM   2035  OD1 ASP A 264      31.318 -21.065 -34.411  1.00 66.94           O  
ATOM   2036  OD2 ASP A 264      31.735 -21.701 -32.400  1.00 69.73           O  
ATOM   2037  N   GLY A 265      28.136 -19.795 -33.457  1.00 56.23           N  
ATOM   2038  CA  GLY A 265      27.731 -18.689 -32.616  1.00 51.38           C  
ATOM   2039  C   GLY A 265      28.903 -17.770 -32.328  1.00 46.38           C  
ATOM   2040  O   GLY A 265      28.667 -16.625 -31.953  1.00 47.14           O  
ATOM   2041  N   SER A 266      30.159 -18.201 -32.492  1.00 41.90           N  
ATOM   2042  CA  SER A 266      31.266 -17.308 -32.236  1.00 38.53           C  
ATOM   2043  C   SER A 266      31.295 -16.182 -33.253  1.00 36.68           C  
ATOM   2044  O   SER A 266      30.718 -16.291 -34.337  1.00 38.75           O  
ATOM   2045  CB  SER A 266      32.563 -18.095 -32.283  1.00 41.35           C  
ATOM   2046  OG  SER A 266      32.745 -18.915 -33.440  1.00 41.62           O  
ATOM   2047  N   LYS A 267      31.927 -15.082 -32.915  1.00 31.71           N  
ATOM   2048  CA  LYS A 267      32.064 -13.980 -33.825  1.00 28.60           C  
ATOM   2049  C   LYS A 267      33.499 -14.005 -34.287  1.00 28.86           C  
ATOM   2050  O   LYS A 267      34.427 -14.297 -33.528  1.00 30.70           O  
ATOM   2051  CB  LYS A 267      31.785 -12.677 -33.127  1.00 26.29           C  
ATOM   2052  CG  LYS A 267      30.332 -12.230 -33.135  1.00 32.40           C  
ATOM   2053  CD  LYS A 267      29.349 -13.105 -32.385  1.00 31.77           C  
ATOM   2054  CE  LYS A 267      29.746 -13.347 -30.938  1.00 36.95           C  
ATOM   2055  NZ  LYS A 267      28.605 -13.874 -30.219  1.00 38.39           N  
ATOM   2056  N   SER A 268      33.652 -13.666 -35.546  1.00 26.69           N  
ATOM   2057  CA  SER A 268      34.919 -13.658 -36.224  1.00 28.99           C  
ATOM   2058  C   SER A 268      35.164 -12.188 -36.516  1.00 26.78           C  
ATOM   2059  O   SER A 268      34.281 -11.549 -37.107  1.00 29.99           O  
ATOM   2060  CB  SER A 268      34.722 -14.496 -37.465  1.00 29.45           C  
ATOM   2061  OG  SER A 268      35.936 -14.882 -38.074  1.00 46.86           O  
ATOM   2062  N   VAL A 269      36.272 -11.594 -36.079  1.00 26.64           N  
ATOM   2063  CA  VAL A 269      36.538 -10.184 -36.301  1.00 25.87           C  
ATOM   2064  C   VAL A 269      37.714 -10.092 -37.248  1.00 27.14           C  
ATOM   2065  O   VAL A 269      38.774 -10.667 -36.965  1.00 27.70           O  
ATOM   2066  CB  VAL A 269      36.903  -9.439 -34.969  1.00 23.59           C  
ATOM   2067  CG1 VAL A 269      37.062  -7.934 -35.215  1.00 21.87           C  
ATOM   2068  CG2 VAL A 269      35.778  -9.592 -33.951  1.00 22.89           C  
ATOM   2069  N   THR A 270      37.546  -9.404 -38.370  1.00 28.65           N  
ATOM   2070  CA  THR A 270      38.666  -9.163 -39.253  1.00 26.52           C  
ATOM   2071  C   THR A 270      39.045  -7.729 -39.002  1.00 25.23           C  
ATOM   2072  O   THR A 270      38.195  -6.837 -38.953  1.00 27.20           O  
ATOM   2073  CB  THR A 270      38.297  -9.321 -40.732  1.00 26.75           C  
ATOM   2074  OG1 THR A 270      37.765 -10.638 -40.874  1.00 27.30           O  
ATOM   2075  CG2 THR A 270      39.499  -9.128 -41.659  1.00 22.14           C  
ATOM   2076  N   PHE A 271      40.316  -7.509 -38.777  1.00 25.00           N  
ATOM   2077  CA  PHE A 271      40.843  -6.189 -38.571  1.00 27.67           C  
ATOM   2078  C   PHE A 271      41.326  -5.687 -39.922  1.00 28.78           C  
ATOM   2079  O   PHE A 271      41.751  -6.466 -40.763  1.00 30.93           O  
ATOM   2080  CB  PHE A 271      42.014  -6.252 -37.571  1.00 27.70           C  
ATOM   2081  CG  PHE A 271      41.622  -6.758 -36.188  1.00 26.79           C  
ATOM   2082  CD1 PHE A 271      41.157  -5.858 -35.230  1.00 24.82           C  
ATOM   2083  CD2 PHE A 271      41.708  -8.117 -35.880  1.00 27.69           C  
ATOM   2084  CE1 PHE A 271      40.774  -6.320 -33.972  1.00 21.97           C  
ATOM   2085  CE2 PHE A 271      41.322  -8.573 -34.618  1.00 30.70           C  
ATOM   2086  CZ  PHE A 271      40.856  -7.675 -33.663  1.00 23.35           C  
ATOM   2087  N   GLU A 272      41.389  -4.373 -40.070  1.00 28.03           N  
ATOM   2088  CA  GLU A 272      41.922  -3.700 -41.230  1.00 26.63           C  
ATOM   2089  C   GLU A 272      43.326  -4.088 -41.644  1.00 29.76           C  
ATOM   2090  O   GLU A 272      43.853  -3.658 -42.664  1.00 37.43           O  
ATOM   2091  CB  GLU A 272      41.901  -2.214 -40.975  1.00 23.52           C  
ATOM   2092  CG  GLU A 272      40.541  -1.564 -41.085  1.00 23.98           C  
ATOM   2093  CD  GLU A 272      39.882  -1.558 -42.460  1.00 32.42           C  
ATOM   2094  OE1 GLU A 272      40.503  -1.825 -43.499  1.00 37.46           O  
ATOM   2095  OE2 GLU A 272      38.697  -1.256 -42.463  1.00 27.04           O  
ATOM   2096  N   SER A 273      44.054  -4.777 -40.787  1.00 30.19           N  
ATOM   2097  CA  SER A 273      45.392  -5.197 -41.144  1.00 31.75           C  
ATOM   2098  C   SER A 273      45.353  -6.593 -41.761  1.00 32.46           C  
ATOM   2099  O   SER A 273      46.404  -7.170 -42.040  1.00 32.85           O  
ATOM   2100  CB  SER A 273      46.226  -5.160 -39.879  1.00 27.61           C  
ATOM   2101  OG  SER A 273      45.510  -5.862 -38.871  1.00 33.85           O  
ATOM   2102  N   GLY A 274      44.171  -7.181 -41.942  1.00 33.45           N  
ATOM   2103  CA  GLY A 274      44.031  -8.531 -42.457  1.00 34.27           C  
ATOM   2104  C   GLY A 274      44.023  -9.559 -41.335  1.00 33.83           C  
ATOM   2105  O   GLY A 274      43.667 -10.723 -41.547  1.00 33.86           O  
ATOM   2106  N   LYS A 275      44.434  -9.158 -40.128  1.00 35.99           N  
ATOM   2107  CA  LYS A 275      44.440 -10.048 -38.978  1.00 37.30           C  
ATOM   2108  C   LYS A 275      42.990 -10.425 -38.678  1.00 35.43           C  
ATOM   2109  O   LYS A 275      42.102  -9.594 -38.849  1.00 35.43           O  
ATOM   2110  CB  LYS A 275      45.120  -9.286 -37.839  1.00 43.66           C  
ATOM   2111  CG  LYS A 275      45.442 -10.076 -36.575  1.00 50.73           C  
ATOM   2112  CD  LYS A 275      46.460  -9.330 -35.712  1.00 58.63           C  
ATOM   2113  CE  LYS A 275      46.662 -10.091 -34.402  1.00 62.30           C  
ATOM   2114  NZ  LYS A 275      47.764  -9.554 -33.619  1.00 60.38           N  
ATOM   2115  N   LYS A 276      42.699 -11.648 -38.269  1.00 34.07           N  
ATOM   2116  CA  LYS A 276      41.333 -12.092 -38.066  1.00 36.58           C  
ATOM   2117  C   LYS A 276      41.316 -12.925 -36.801  1.00 37.53           C  
ATOM   2118  O   LYS A 276      42.263 -13.699 -36.624  1.00 41.15           O  
ATOM   2119  CB  LYS A 276      40.912 -12.924 -39.259  1.00 39.32           C  
ATOM   2120  CG  LYS A 276      39.490 -13.444 -39.185  1.00 46.83           C  
ATOM   2121  CD  LYS A 276      39.250 -14.226 -40.452  1.00 54.98           C  
ATOM   2122  CE  LYS A 276      37.903 -14.917 -40.434  1.00 60.92           C  
ATOM   2123  NZ  LYS A 276      37.992 -16.256 -39.872  1.00 63.92           N  
ATOM   2124  N   MET A 277      40.327 -12.825 -35.901  1.00 34.35           N  
ATOM   2125  CA  MET A 277      40.300 -13.596 -34.658  1.00 31.02           C  
ATOM   2126  C   MET A 277      38.886 -13.966 -34.247  1.00 30.93           C  
ATOM   2127  O   MET A 277      37.942 -13.266 -34.616  1.00 31.00           O  
ATOM   2128  CB  MET A 277      40.929 -12.798 -33.513  1.00 32.70           C  
ATOM   2129  CG  MET A 277      42.445 -12.634 -33.508  1.00 32.09           C  
ATOM   2130  SD  MET A 277      43.033 -11.402 -32.318  1.00 45.73           S  
ATOM   2131  CE  MET A 277      43.160 -12.421 -30.871  1.00 37.78           C  
ATOM   2132  N   ASP A 278      38.691 -15.050 -33.492  1.00 30.35           N  
ATOM   2133  CA  ASP A 278      37.356 -15.428 -33.026  1.00 29.82           C  
ATOM   2134  C   ASP A 278      37.225 -15.186 -31.533  1.00 27.61           C  
ATOM   2135  O   ASP A 278      38.170 -15.407 -30.762  1.00 24.96           O  
ATOM   2136  CB  ASP A 278      37.053 -16.901 -33.251  1.00 35.36           C  
ATOM   2137  CG  ASP A 278      37.118 -17.341 -34.703  1.00 39.20           C  
ATOM   2138  OD1 ASP A 278      36.592 -16.662 -35.584  1.00 47.36           O  
ATOM   2139  OD2 ASP A 278      37.717 -18.381 -34.950  1.00 53.05           O  
ATOM   2140  N   PHE A 279      36.046 -14.728 -31.146  1.00 25.28           N  
ATOM   2141  CA  PHE A 279      35.685 -14.412 -29.785  1.00 23.40           C  
ATOM   2142  C   PHE A 279      34.275 -14.922 -29.566  1.00 25.82           C  
ATOM   2143  O   PHE A 279      33.532 -15.179 -30.521  1.00 28.32           O  
ATOM   2144  CB  PHE A 279      35.688 -12.904 -29.550  1.00 16.93           C  
ATOM   2145  CG  PHE A 279      37.030 -12.286 -29.878  1.00 14.02           C  
ATOM   2146  CD1 PHE A 279      38.069 -12.325 -28.950  1.00 11.70           C  
ATOM   2147  CD2 PHE A 279      37.226 -11.721 -31.139  1.00 18.61           C  
ATOM   2148  CE1 PHE A 279      39.320 -11.804 -29.287  1.00 12.13           C  
ATOM   2149  CE2 PHE A 279      38.479 -11.201 -31.470  1.00 18.54           C  
ATOM   2150  CZ  PHE A 279      39.529 -11.239 -30.544  1.00 15.31           C  
ATOM   2151  N   ASP A 280      33.861 -15.123 -28.321  1.00 26.49           N  
ATOM   2152  CA  ASP A 280      32.471 -15.459 -28.048  1.00 23.72           C  
ATOM   2153  C   ASP A 280      31.699 -14.175 -27.783  1.00 22.86           C  
ATOM   2154  O   ASP A 280      30.477 -14.158 -27.897  1.00 24.46           O  
ATOM   2155  CB  ASP A 280      32.380 -16.369 -26.838  1.00 28.56           C  
ATOM   2156  CG  ASP A 280      33.157 -17.662 -27.016  1.00 32.66           C  
ATOM   2157  OD1 ASP A 280      32.637 -18.595 -27.634  1.00 38.78           O  
ATOM   2158  OD2 ASP A 280      34.285 -17.717 -26.536  1.00 31.24           O  
ATOM   2159  N   LEU A 281      32.352 -13.073 -27.427  1.00 18.84           N  
ATOM   2160  CA  LEU A 281      31.622 -11.842 -27.197  1.00 20.03           C  
ATOM   2161  C   LEU A 281      32.480 -10.701 -27.679  1.00 18.42           C  
ATOM   2162  O   LEU A 281      33.708 -10.738 -27.502  1.00 20.51           O  
ATOM   2163  CB  LEU A 281      31.327 -11.653 -25.709  1.00 26.55           C  
ATOM   2164  CG  LEU A 281      30.396 -10.500 -25.361  1.00 22.31           C  
ATOM   2165  CD1 LEU A 281      28.964 -10.949 -25.451  1.00 26.82           C  
ATOM   2166  CD2 LEU A 281      30.658 -10.038 -23.954  1.00 23.95           C  
ATOM   2167  N   VAL A 282      31.879  -9.694 -28.301  1.00 17.54           N  
ATOM   2168  CA  VAL A 282      32.624  -8.552 -28.798  1.00 17.52           C  
ATOM   2169  C   VAL A 282      31.881  -7.387 -28.190  1.00 18.23           C  
ATOM   2170  O   VAL A 282      30.673  -7.258 -28.411  1.00 16.96           O  
ATOM   2171  CB  VAL A 282      32.581  -8.496 -30.353  1.00 20.79           C  
ATOM   2172  CG1 VAL A 282      33.286  -7.245 -30.857  1.00 17.38           C  
ATOM   2173  CG2 VAL A 282      33.270  -9.737 -30.934  1.00 16.13           C  
ATOM   2174  N   MET A 283      32.561  -6.561 -27.399  1.00 18.43           N  
ATOM   2175  CA  MET A 283      31.917  -5.443 -26.738  1.00 20.23           C  
ATOM   2176  C   MET A 283      32.450  -4.154 -27.320  1.00 16.94           C  
ATOM   2177  O   MET A 283      33.667  -3.969 -27.366  1.00 20.91           O  
ATOM   2178  CB  MET A 283      32.206  -5.475 -25.227  1.00 19.17           C  
ATOM   2179  CG  MET A 283      31.468  -4.381 -24.456  1.00 22.25           C  
ATOM   2180  SD  MET A 283      31.868  -4.266 -22.700  1.00 25.56           S  
ATOM   2181  CE  MET A 283      33.002  -2.913 -22.737  1.00 13.56           C  
ATOM   2182  N   MET A 284      31.604  -3.252 -27.790  1.00 18.96           N  
ATOM   2183  CA  MET A 284      32.050  -1.961 -28.293  1.00 21.72           C  
ATOM   2184  C   MET A 284      32.009  -0.990 -27.128  1.00 21.85           C  
ATOM   2185  O   MET A 284      30.993  -0.917 -26.428  1.00 23.96           O  
ATOM   2186  CB  MET A 284      31.126  -1.447 -29.392  1.00 24.82           C  
ATOM   2187  CG  MET A 284      31.261  -2.247 -30.670  1.00 25.08           C  
ATOM   2188  SD  MET A 284      32.799  -1.851 -31.526  1.00 33.86           S  
ATOM   2189  CE  MET A 284      32.875  -3.354 -32.455  1.00 24.24           C  
ATOM   2190  N   ALA A 285      33.116  -0.309 -26.845  1.00 20.05           N  
ATOM   2191  CA  ALA A 285      33.172   0.728 -25.828  1.00 19.35           C  
ATOM   2192  C   ALA A 285      34.067   1.816 -26.387  1.00 18.86           C  
ATOM   2193  O   ALA A 285      35.090   2.223 -25.823  1.00 20.49           O  
ATOM   2194  CB  ALA A 285      33.786   0.213 -24.555  1.00 19.83           C  
ATOM   2195  N   ILE A 286      33.650   2.311 -27.556  1.00 20.88           N  
ATOM   2196  CA  ILE A 286      34.430   3.312 -28.270  1.00 21.13           C  
ATOM   2197  C   ILE A 286      34.004   4.728 -27.943  1.00 23.96           C  
ATOM   2198  O   ILE A 286      34.696   5.680 -28.289  1.00 29.87           O  
ATOM   2199  CB  ILE A 286      34.347   3.035 -29.797  1.00 19.41           C  
ATOM   2200  CG1 ILE A 286      32.949   2.810 -30.341  1.00 22.19           C  
ATOM   2201  CG2 ILE A 286      35.167   1.789 -30.005  1.00 13.20           C  
ATOM   2202  CD1 ILE A 286      32.521   3.923 -31.307  1.00 26.32           C  
ATOM   2203  N   GLY A 287      32.899   4.960 -27.231  1.00 22.85           N  
ATOM   2204  CA  GLY A 287      32.560   6.327 -26.864  1.00 17.86           C  
ATOM   2205  C   GLY A 287      31.095   6.419 -26.557  1.00 18.63           C  
ATOM   2206  O   GLY A 287      30.371   5.439 -26.783  1.00 23.05           O  
ATOM   2207  N   ARG A 288      30.664   7.550 -26.029  1.00 16.17           N  
ATOM   2208  CA  ARG A 288      29.286   7.772 -25.651  1.00 17.65           C  
ATOM   2209  C   ARG A 288      28.848   9.095 -26.229  1.00 16.88           C  
ATOM   2210  O   ARG A 288      29.618  10.060 -26.201  1.00 20.67           O  
ATOM   2211  CB  ARG A 288      29.171   7.790 -24.126  1.00 17.87           C  
ATOM   2212  CG  ARG A 288      29.305   6.392 -23.526  1.00 20.61           C  
ATOM   2213  CD  ARG A 288      29.151   6.363 -22.021  1.00 21.59           C  
ATOM   2214  NE  ARG A 288      27.839   6.841 -21.600  1.00 18.80           N  
ATOM   2215  CZ  ARG A 288      26.739   6.084 -21.530  1.00 15.67           C  
ATOM   2216  NH1 ARG A 288      26.733   4.791 -21.847  1.00 13.21           N  
ATOM   2217  NH2 ARG A 288      25.612   6.656 -21.113  1.00 14.40           N  
ATOM   2218  N   SER A 289      27.609   9.187 -26.687  1.00 19.12           N  
ATOM   2219  CA  SER A 289      27.140  10.384 -27.370  1.00 20.44           C  
ATOM   2220  C   SER A 289      25.966  11.011 -26.641  1.00 16.04           C  
ATOM   2221  O   SER A 289      25.150  10.217 -26.163  1.00 16.51           O  
ATOM   2222  CB  SER A 289      26.675  10.036 -28.788  1.00 27.15           C  
ATOM   2223  OG  SER A 289      27.525   9.159 -29.548  1.00 42.20           O  
ATOM   2224  N   PRO A 290      25.782  12.340 -26.539  1.00 17.71           N  
ATOM   2225  CA  PRO A 290      24.596  12.995 -25.987  1.00 16.36           C  
ATOM   2226  C   PRO A 290      23.297  12.438 -26.526  1.00 20.95           C  
ATOM   2227  O   PRO A 290      23.246  12.139 -27.719  1.00 26.37           O  
ATOM   2228  CB  PRO A 290      24.806  14.447 -26.328  1.00 15.65           C  
ATOM   2229  CG  PRO A 290      26.301  14.610 -26.262  1.00 16.19           C  
ATOM   2230  CD  PRO A 290      26.752  13.346 -26.973  1.00 16.00           C  
ATOM   2231  N   ARG A 291      22.249  12.188 -25.736  1.00 23.25           N  
ATOM   2232  CA  ARG A 291      20.998  11.703 -26.282  1.00 21.49           C  
ATOM   2233  C   ARG A 291      20.103  12.869 -26.633  1.00 20.74           C  
ATOM   2234  O   ARG A 291      19.238  13.261 -25.855  1.00 26.93           O  
ATOM   2235  CB  ARG A 291      20.258  10.817 -25.300  1.00 21.21           C  
ATOM   2236  CG  ARG A 291      20.868   9.468 -25.124  1.00 18.68           C  
ATOM   2237  CD  ARG A 291      20.122   8.772 -24.016  1.00 24.05           C  
ATOM   2238  NE  ARG A 291      18.932   8.046 -24.416  1.00 27.60           N  
ATOM   2239  CZ  ARG A 291      18.427   7.103 -23.606  1.00 32.64           C  
ATOM   2240  NH1 ARG A 291      18.990   6.813 -22.427  1.00 28.83           N  
ATOM   2241  NH2 ARG A 291      17.358   6.406 -23.978  1.00 36.30           N  
ATOM   2242  N   THR A 292      20.211  13.433 -27.825  1.00 24.23           N  
ATOM   2243  CA  THR A 292      19.409  14.588 -28.183  1.00 21.52           C  
ATOM   2244  C   THR A 292      18.293  14.291 -29.178  1.00 24.45           C  
ATOM   2245  O   THR A 292      17.270  14.978 -29.205  1.00 25.73           O  
ATOM   2246  CB  THR A 292      20.376  15.630 -28.711  1.00 19.25           C  
ATOM   2247  OG1 THR A 292      21.149  14.987 -29.718  1.00 23.40           O  
ATOM   2248  CG2 THR A 292      21.301  16.165 -27.637  1.00 18.22           C  
ATOM   2249  N   LYS A 293      18.454  13.224 -29.959  1.00 29.12           N  
ATOM   2250  CA  LYS A 293      17.557  12.820 -31.042  1.00 31.89           C  
ATOM   2251  C   LYS A 293      16.063  12.819 -30.708  1.00 33.57           C  
ATOM   2252  O   LYS A 293      15.257  13.549 -31.294  1.00 37.96           O  
ATOM   2253  CB  LYS A 293      18.047  11.439 -31.486  1.00 35.99           C  
ATOM   2254  CG  LYS A 293      17.204  10.660 -32.483  1.00 52.95           C  
ATOM   2255  CD  LYS A 293      17.685   9.201 -32.550  1.00 64.93           C  
ATOM   2256  CE  LYS A 293      16.793   8.329 -33.503  1.00 70.31           C  
ATOM   2257  NZ  LYS A 293      15.582   7.619 -33.066  1.00 70.47           N  
ATOM   2258  N   ASP A 294      15.687  12.057 -29.686  1.00 32.69           N  
ATOM   2259  CA  ASP A 294      14.301  11.915 -29.278  1.00 29.53           C  
ATOM   2260  C   ASP A 294      13.715  13.166 -28.634  1.00 24.37           C  
ATOM   2261  O   ASP A 294      12.503  13.302 -28.497  1.00 25.54           O  
ATOM   2262  CB  ASP A 294      14.176  10.755 -28.292  1.00 32.56           C  
ATOM   2263  CG  ASP A 294      14.889   9.462 -28.672  1.00 33.99           C  
ATOM   2264  OD1 ASP A 294      14.782   9.012 -29.798  1.00 41.49           O  
ATOM   2265  OD2 ASP A 294      15.580   8.901 -27.822  1.00 45.53           O  
ATOM   2266  N   LEU A 295      14.528  14.152 -28.279  1.00 23.01           N  
ATOM   2267  CA  LEU A 295      14.014  15.306 -27.574  1.00 23.05           C  
ATOM   2268  C   LEU A 295      13.171  16.253 -28.416  1.00 24.13           C  
ATOM   2269  O   LEU A 295      12.357  17.003 -27.864  1.00 24.47           O  
ATOM   2270  CB  LEU A 295      15.184  16.057 -26.955  1.00 18.39           C  
ATOM   2271  CG  LEU A 295      15.994  15.349 -25.867  1.00 18.64           C  
ATOM   2272  CD1 LEU A 295      17.116  16.247 -25.384  1.00 17.99           C  
ATOM   2273  CD2 LEU A 295      15.094  15.023 -24.694  1.00 20.24           C  
ATOM   2274  N   GLN A 296      13.310  16.162 -29.754  1.00 24.42           N  
ATOM   2275  CA  GLN A 296      12.642  17.016 -30.740  1.00 22.24           C  
ATOM   2276  C   GLN A 296      12.948  18.481 -30.460  1.00 19.90           C  
ATOM   2277  O   GLN A 296      12.106  19.379 -30.413  1.00 20.05           O  
ATOM   2278  CB  GLN A 296      11.119  16.795 -30.735  1.00 21.15           C  
ATOM   2279  CG  GLN A 296      10.664  15.349 -30.964  1.00 26.36           C  
ATOM   2280  CD  GLN A 296      11.303  14.630 -32.151  1.00 37.79           C  
ATOM   2281  OE1 GLN A 296      11.514  15.140 -33.248  1.00 41.93           O  
ATOM   2282  NE2 GLN A 296      11.735  13.393 -31.943  1.00 34.72           N  
ATOM   2283  N   LEU A 297      14.252  18.743 -30.356  1.00 19.22           N  
ATOM   2284  CA  LEU A 297      14.758  20.053 -30.001  1.00 17.27           C  
ATOM   2285  C   LEU A 297      14.403  21.157 -30.974  1.00 20.47           C  
ATOM   2286  O   LEU A 297      14.319  22.347 -30.626  1.00 22.80           O  
ATOM   2287  CB  LEU A 297      16.261  19.965 -29.868  1.00 16.93           C  
ATOM   2288  CG  LEU A 297      16.826  19.110 -28.752  1.00 17.37           C  
ATOM   2289  CD1 LEU A 297      18.332  19.195 -28.765  1.00 15.38           C  
ATOM   2290  CD2 LEU A 297      16.300  19.600 -27.425  1.00 17.96           C  
ATOM   2291  N   GLN A 298      14.166  20.773 -32.231  1.00 22.13           N  
ATOM   2292  CA  GLN A 298      13.820  21.768 -33.232  1.00 24.31           C  
ATOM   2293  C   GLN A 298      12.453  22.400 -32.958  1.00 22.66           C  
ATOM   2294  O   GLN A 298      12.252  23.542 -33.351  1.00 27.43           O  
ATOM   2295  CB  GLN A 298      13.850  21.157 -34.646  1.00 23.32           C  
ATOM   2296  CG  GLN A 298      12.808  20.111 -35.014  1.00 30.08           C  
ATOM   2297  CD  GLN A 298      12.768  18.663 -34.270  1.00 33.86           C  
ATOM   2298  OE1 GLN A 298      13.831  18.328 -33.769  1.00 38.43           O  
ATOM   2299  NE2 GLN A 298      11.761  17.783 -34.263  1.00 33.56           N  
ATOM   2300  N   ASN A 299      11.552  21.793 -32.186  1.00 19.78           N  
ATOM   2301  CA  ASN A 299      10.284  22.430 -31.841  1.00 19.09           C  
ATOM   2302  C   ASN A 299      10.381  23.655 -30.940  1.00 20.42           C  
ATOM   2303  O   ASN A 299       9.424  24.400 -30.732  1.00 22.56           O  
ATOM   2304  CB  ASN A 299       9.400  21.409 -31.181  1.00 20.46           C  
ATOM   2305  CG  ASN A 299       8.954  20.360 -32.176  1.00 23.05           C  
ATOM   2306  OD1 ASN A 299       9.132  20.512 -33.383  1.00 29.43           O  
ATOM   2307  ND2 ASN A 299       8.389  19.241 -31.750  1.00 25.10           N  
ATOM   2308  N   ALA A 300      11.556  23.844 -30.351  1.00 21.63           N  
ATOM   2309  CA  ALA A 300      11.814  24.956 -29.462  1.00 18.52           C  
ATOM   2310  C   ALA A 300      12.980  25.771 -29.974  1.00 20.80           C  
ATOM   2311  O   ALA A 300      13.286  26.823 -29.414  1.00 27.18           O  
ATOM   2312  CB  ALA A 300      12.148  24.420 -28.090  1.00 19.28           C  
ATOM   2313  N   GLY A 301      13.709  25.292 -30.989  1.00 20.05           N  
ATOM   2314  CA  GLY A 301      14.815  26.046 -31.557  1.00 20.57           C  
ATOM   2315  C   GLY A 301      16.132  25.896 -30.821  1.00 22.66           C  
ATOM   2316  O   GLY A 301      16.997  26.773 -30.935  1.00 23.81           O  
ATOM   2317  N   VAL A 302      16.337  24.781 -30.112  1.00 23.31           N  
ATOM   2318  CA  VAL A 302      17.549  24.605 -29.318  1.00 20.07           C  
ATOM   2319  C   VAL A 302      18.705  24.139 -30.193  1.00 20.42           C  
ATOM   2320  O   VAL A 302      18.606  23.168 -30.950  1.00 21.49           O  
ATOM   2321  CB  VAL A 302      17.259  23.592 -28.182  1.00 20.61           C  
ATOM   2322  CG1 VAL A 302      18.506  23.392 -27.352  1.00 17.57           C  
ATOM   2323  CG2 VAL A 302      16.200  24.129 -27.230  1.00 15.32           C  
ATOM   2324  N   MET A 303      19.800  24.876 -30.091  1.00 22.96           N  
ATOM   2325  CA  MET A 303      20.993  24.592 -30.852  1.00 26.71           C  
ATOM   2326  C   MET A 303      21.788  23.458 -30.267  1.00 30.72           C  
ATOM   2327  O   MET A 303      21.953  23.310 -29.053  1.00 31.15           O  
ATOM   2328  CB  MET A 303      21.932  25.763 -30.898  1.00 27.58           C  
ATOM   2329  CG  MET A 303      21.620  26.808 -31.946  1.00 49.71           C  
ATOM   2330  SD  MET A 303      22.861  28.128 -31.925  1.00 63.94           S  
ATOM   2331  CE  MET A 303      24.298  27.166 -32.328  1.00 54.26           C  
ATOM   2332  N   ILE A 304      22.350  22.710 -31.202  1.00 32.18           N  
ATOM   2333  CA  ILE A 304      23.235  21.599 -30.925  1.00 34.47           C  
ATOM   2334  C   ILE A 304      24.620  21.968 -31.470  1.00 38.52           C  
ATOM   2335  O   ILE A 304      24.671  22.487 -32.587  1.00 39.35           O  
ATOM   2336  CB  ILE A 304      22.647  20.367 -31.624  1.00 33.31           C  
ATOM   2337  CG1 ILE A 304      21.303  20.030 -31.024  1.00 40.20           C  
ATOM   2338  CG2 ILE A 304      23.579  19.174 -31.466  1.00 44.45           C  
ATOM   2339  CD1 ILE A 304      20.559  19.005 -31.890  1.00 49.57           C  
ATOM   2340  N   LYS A 305      25.741  21.807 -30.755  1.00 42.07           N  
ATOM   2341  CA  LYS A 305      27.069  22.029 -31.312  1.00 47.11           C  
ATOM   2342  C   LYS A 305      27.873  20.817 -30.901  1.00 50.46           C  
ATOM   2343  O   LYS A 305      27.832  20.350 -29.764  1.00 50.62           O  
ATOM   2344  CB  LYS A 305      27.796  23.298 -30.788  1.00 55.26           C  
ATOM   2345  CG  LYS A 305      28.385  23.505 -29.384  1.00 59.34           C  
ATOM   2346  CD  LYS A 305      29.253  24.767 -29.521  1.00 71.60           C  
ATOM   2347  CE  LYS A 305      29.491  25.638 -28.261  1.00 78.79           C  
ATOM   2348  NZ  LYS A 305      30.607  25.261 -27.405  1.00 82.71           N  
ATOM   2349  N   ASN A 306      28.562  20.270 -31.895  1.00 52.86           N  
ATOM   2350  CA  ASN A 306      29.331  19.031 -31.815  1.00 55.52           C  
ATOM   2351  C   ASN A 306      28.762  17.942 -30.905  1.00 53.12           C  
ATOM   2352  O   ASN A 306      29.324  17.503 -29.905  1.00 52.86           O  
ATOM   2353  CB  ASN A 306      30.838  19.312 -31.430  1.00 63.61           C  
ATOM   2354  CG  ASN A 306      31.271  19.939 -30.098  1.00 70.40           C  
ATOM   2355  OD1 ASN A 306      31.775  21.064 -30.095  1.00 79.28           O  
ATOM   2356  ND2 ASN A 306      31.206  19.320 -28.924  1.00 77.29           N  
ATOM   2357  N   GLY A 307      27.547  17.550 -31.313  1.00 50.05           N  
ATOM   2358  CA  GLY A 307      26.824  16.440 -30.701  1.00 43.34           C  
ATOM   2359  C   GLY A 307      25.895  16.792 -29.545  1.00 38.13           C  
ATOM   2360  O   GLY A 307      24.780  16.272 -29.460  1.00 36.33           O  
ATOM   2361  N   GLY A 308      26.288  17.714 -28.683  1.00 34.02           N  
ATOM   2362  CA  GLY A 308      25.500  18.020 -27.512  1.00 30.81           C  
ATOM   2363  C   GLY A 308      24.763  19.331 -27.590  1.00 27.46           C  
ATOM   2364  O   GLY A 308      24.944  20.142 -28.500  1.00 26.98           O  
ATOM   2365  N   VAL A 309      23.880  19.520 -26.618  1.00 25.88           N  
ATOM   2366  CA  VAL A 309      23.100  20.739 -26.507  1.00 24.53           C  
ATOM   2367  C   VAL A 309      24.088  21.822 -26.123  1.00 27.90           C  
ATOM   2368  O   VAL A 309      24.891  21.654 -25.193  1.00 28.82           O  
ATOM   2369  CB  VAL A 309      22.009  20.605 -25.421  1.00 18.44           C  
ATOM   2370  CG1 VAL A 309      21.248  21.900 -25.275  1.00 13.90           C  
ATOM   2371  CG2 VAL A 309      21.032  19.513 -25.812  1.00 14.47           C  
ATOM   2372  N   GLN A 310      24.072  22.928 -26.867  1.00 28.83           N  
ATOM   2373  CA  GLN A 310      24.987  24.022 -26.614  1.00 25.30           C  
ATOM   2374  C   GLN A 310      24.535  24.819 -25.384  1.00 22.87           C  
ATOM   2375  O   GLN A 310      23.375  25.227 -25.315  1.00 23.86           O  
ATOM   2376  CB  GLN A 310      24.998  24.870 -27.858  1.00 32.22           C  
ATOM   2377  CG  GLN A 310      25.944  26.046 -27.781  1.00 42.41           C  
ATOM   2378  CD  GLN A 310      25.570  27.172 -28.733  1.00 52.48           C  
ATOM   2379  OE1 GLN A 310      26.275  27.594 -29.653  1.00 58.35           O  
ATOM   2380  NE2 GLN A 310      24.387  27.720 -28.472  1.00 55.07           N  
ATOM   2381  N   VAL A 311      25.365  25.060 -24.380  1.00 21.02           N  
ATOM   2382  CA  VAL A 311      24.976  25.815 -23.194  1.00 20.32           C  
ATOM   2383  C   VAL A 311      26.093  26.789 -22.940  1.00 20.85           C  
ATOM   2384  O   VAL A 311      27.199  26.626 -23.471  1.00 24.05           O  
ATOM   2385  CB  VAL A 311      24.820  24.944 -21.904  1.00 16.88           C  
ATOM   2386  CG1 VAL A 311      23.556  24.095 -22.015  1.00 11.54           C  
ATOM   2387  CG2 VAL A 311      26.038  24.055 -21.699  1.00 10.38           C  
ATOM   2388  N   ASP A 312      25.783  27.845 -22.200  1.00 23.56           N  
ATOM   2389  CA  ASP A 312      26.823  28.740 -21.738  1.00 25.03           C  
ATOM   2390  C   ASP A 312      27.340  28.191 -20.406  1.00 27.55           C  
ATOM   2391  O   ASP A 312      26.808  27.209 -19.886  1.00 30.35           O  
ATOM   2392  CB  ASP A 312      26.259  30.165 -21.545  1.00 23.71           C  
ATOM   2393  CG  ASP A 312      25.160  30.389 -20.506  1.00 26.56           C  
ATOM   2394  OD1 ASP A 312      24.785  29.468 -19.792  1.00 25.92           O  
ATOM   2395  OD2 ASP A 312      24.658  31.508 -20.412  1.00 30.20           O  
ATOM   2396  N   GLU A 313      28.216  28.928 -19.733  1.00 29.88           N  
ATOM   2397  CA  GLU A 313      28.747  28.519 -18.440  1.00 27.44           C  
ATOM   2398  C   GLU A 313      27.725  28.313 -17.346  1.00 24.97           C  
ATOM   2399  O   GLU A 313      27.995  27.631 -16.365  1.00 24.83           O  
ATOM   2400  CB  GLU A 313      29.708  29.535 -17.954  1.00 31.04           C  
ATOM   2401  CG  GLU A 313      30.947  29.621 -18.803  1.00 48.87           C  
ATOM   2402  CD  GLU A 313      31.748  30.873 -18.480  1.00 62.26           C  
ATOM   2403  OE1 GLU A 313      31.148  31.926 -18.208  1.00 67.97           O  
ATOM   2404  OE2 GLU A 313      32.979  30.785 -18.510  1.00 71.26           O  
ATOM   2405  N   TYR A 314      26.557  28.950 -17.470  1.00 22.15           N  
ATOM   2406  CA  TYR A 314      25.509  28.777 -16.477  1.00 20.43           C  
ATOM   2407  C   TYR A 314      24.500  27.720 -16.904  1.00 20.17           C  
ATOM   2408  O   TYR A 314      23.395  27.685 -16.359  1.00 20.65           O  
ATOM   2409  CB  TYR A 314      24.809  30.118 -16.252  1.00 20.67           C  
ATOM   2410  CG  TYR A 314      25.760  31.110 -15.618  1.00 24.09           C  
ATOM   2411  CD1 TYR A 314      26.693  31.790 -16.406  1.00 28.74           C  
ATOM   2412  CD2 TYR A 314      25.738  31.290 -14.236  1.00 22.23           C  
ATOM   2413  CE1 TYR A 314      27.622  32.650 -15.809  1.00 34.46           C  
ATOM   2414  CE2 TYR A 314      26.660  32.148 -13.636  1.00 24.88           C  
ATOM   2415  CZ  TYR A 314      27.598  32.822 -14.422  1.00 30.58           C  
ATOM   2416  OH  TYR A 314      28.515  33.664 -13.819  1.00 37.62           O  
ATOM   2417  N   SER A 315      24.833  26.915 -17.920  1.00 18.73           N  
ATOM   2418  CA  SER A 315      23.983  25.854 -18.443  1.00 19.17           C  
ATOM   2419  C   SER A 315      22.669  26.304 -19.086  1.00 20.43           C  
ATOM   2420  O   SER A 315      21.703  25.542 -19.219  1.00 23.89           O  
ATOM   2421  CB  SER A 315      23.702  24.850 -17.322  1.00 18.91           C  
ATOM   2422  OG  SER A 315      24.916  24.299 -16.818  1.00 23.95           O  
ATOM   2423  N   ARG A 316      22.635  27.560 -19.547  1.00 21.47           N  
ATOM   2424  CA  ARG A 316      21.484  28.108 -20.285  1.00 25.75           C  
ATOM   2425  C   ARG A 316      21.610  27.796 -21.778  1.00 25.98           C  
ATOM   2426  O   ARG A 316      22.736  27.949 -22.296  1.00 25.32           O  
ATOM   2427  CB  ARG A 316      21.415  29.617 -20.150  1.00 23.53           C  
ATOM   2428  CG  ARG A 316      21.249  30.209 -18.762  1.00 34.07           C  
ATOM   2429  CD  ARG A 316      21.445  31.707 -18.943  1.00 36.68           C  
ATOM   2430  NE  ARG A 316      21.648  32.385 -17.674  1.00 48.92           N  
ATOM   2431  CZ  ARG A 316      22.751  33.099 -17.408  1.00 51.86           C  
ATOM   2432  NH1 ARG A 316      23.740  33.234 -18.299  1.00 45.63           N  
ATOM   2433  NH2 ARG A 316      22.870  33.681 -16.208  1.00 53.86           N  
ATOM   2434  N   THR A 317      20.571  27.329 -22.488  1.00 26.22           N  
ATOM   2435  CA  THR A 317      20.720  27.090 -23.917  1.00 24.12           C  
ATOM   2436  C   THR A 317      20.565  28.439 -24.622  1.00 27.11           C  
ATOM   2437  O   THR A 317      20.452  29.512 -24.013  1.00 26.17           O  
ATOM   2438  CB  THR A 317      19.652  26.084 -24.473  1.00 22.73           C  
ATOM   2439  OG1 THR A 317      18.375  26.695 -24.381  1.00 21.47           O  
ATOM   2440  CG2 THR A 317      19.679  24.750 -23.737  1.00 18.79           C  
ATOM   2441  N   ASN A 318      20.553  28.425 -25.951  1.00 30.00           N  
ATOM   2442  CA  ASN A 318      20.318  29.634 -26.727  1.00 28.37           C  
ATOM   2443  C   ASN A 318      18.857  30.073 -26.589  1.00 26.51           C  
ATOM   2444  O   ASN A 318      18.509  31.179 -26.995  1.00 28.42           O  
ATOM   2445  CB  ASN A 318      20.651  29.372 -28.211  1.00 25.20           C  
ATOM   2446  CG  ASN A 318      19.762  28.322 -28.851  1.00 27.26           C  
ATOM   2447  OD1 ASN A 318      19.560  27.244 -28.287  1.00 31.20           O  
ATOM   2448  ND2 ASN A 318      19.175  28.563 -30.011  1.00 32.31           N  
ATOM   2449  N   VAL A 319      17.958  29.247 -26.061  1.00 26.05           N  
ATOM   2450  CA  VAL A 319      16.536  29.540 -25.950  1.00 24.64           C  
ATOM   2451  C   VAL A 319      16.232  29.806 -24.479  1.00 27.57           C  
ATOM   2452  O   VAL A 319      16.540  28.997 -23.600  1.00 27.89           O  
ATOM   2453  CB  VAL A 319      15.761  28.313 -26.509  1.00 20.33           C  
ATOM   2454  CG1 VAL A 319      14.274  28.474 -26.356  1.00 15.46           C  
ATOM   2455  CG2 VAL A 319      16.076  28.165 -27.995  1.00 20.12           C  
ATOM   2456  N   SER A 320      15.619  30.959 -24.201  1.00 27.52           N  
ATOM   2457  CA  SER A 320      15.300  31.310 -22.835  1.00 26.03           C  
ATOM   2458  C   SER A 320      14.345  30.321 -22.204  1.00 23.37           C  
ATOM   2459  O   SER A 320      13.481  29.741 -22.852  1.00 21.47           O  
ATOM   2460  CB  SER A 320      14.691  32.713 -22.749  1.00 31.63           C  
ATOM   2461  OG  SER A 320      13.467  32.953 -23.420  1.00 32.75           O  
ATOM   2462  N   ASN A 321      14.607  30.118 -20.912  1.00 22.16           N  
ATOM   2463  CA  ASN A 321      13.875  29.217 -20.030  1.00 21.27           C  
ATOM   2464  C   ASN A 321      14.065  27.744 -20.366  1.00 19.69           C  
ATOM   2465  O   ASN A 321      13.352  26.874 -19.854  1.00 19.92           O  
ATOM   2466  CB  ASN A 321      12.371  29.590 -20.030  1.00 23.20           C  
ATOM   2467  CG  ASN A 321      12.086  30.950 -19.392  1.00 29.29           C  
ATOM   2468  OD1 ASN A 321      12.939  31.603 -18.773  1.00 33.28           O  
ATOM   2469  ND2 ASN A 321      10.872  31.429 -19.527  1.00 33.50           N  
ATOM   2470  N   ILE A 322      15.065  27.400 -21.170  1.00 17.30           N  
ATOM   2471  CA  ILE A 322      15.397  26.019 -21.452  1.00 15.85           C  
ATOM   2472  C   ILE A 322      16.873  25.933 -21.111  1.00 19.14           C  
ATOM   2473  O   ILE A 322      17.689  26.794 -21.460  1.00 21.22           O  
ATOM   2474  CB  ILE A 322      15.151  25.673 -22.933  1.00 18.22           C  
ATOM   2475  CG1 ILE A 322      13.668  25.821 -23.235  1.00 13.74           C  
ATOM   2476  CG2 ILE A 322      15.632  24.249 -23.227  1.00 15.92           C  
ATOM   2477  CD1 ILE A 322      13.247  25.360 -24.631  1.00 20.37           C  
ATOM   2478  N   TYR A 323      17.204  24.894 -20.346  1.00 18.79           N  
ATOM   2479  CA  TYR A 323      18.543  24.695 -19.801  1.00 16.48           C  
ATOM   2480  C   TYR A 323      18.911  23.252 -20.034  1.00 13.22           C  
ATOM   2481  O   TYR A 323      18.043  22.402 -20.270  1.00 13.97           O  
ATOM   2482  CB  TYR A 323      18.576  24.938 -18.299  1.00 16.21           C  
ATOM   2483  CG  TYR A 323      17.757  26.137 -17.885  1.00 16.94           C  
ATOM   2484  CD1 TYR A 323      18.306  27.404 -18.059  1.00 15.36           C  
ATOM   2485  CD2 TYR A 323      16.454  25.961 -17.393  1.00 13.79           C  
ATOM   2486  CE1 TYR A 323      17.544  28.521 -17.756  1.00 16.36           C  
ATOM   2487  CE2 TYR A 323      15.692  27.085 -17.086  1.00 12.56           C  
ATOM   2488  CZ  TYR A 323      16.253  28.345 -17.281  1.00 13.41           C  
ATOM   2489  OH  TYR A 323      15.521  29.476 -17.011  1.00 23.40           O  
ATOM   2490  N   ALA A 324      20.184  22.941 -19.933  1.00 10.40           N  
ATOM   2491  CA  ALA A 324      20.625  21.583 -20.126  1.00 12.82           C  
ATOM   2492  C   ALA A 324      21.824  21.369 -19.231  1.00 12.35           C  
ATOM   2493  O   ALA A 324      22.642  22.281 -19.095  1.00 10.39           O  
ATOM   2494  CB  ALA A 324      21.034  21.372 -21.574  1.00 11.63           C  
ATOM   2495  N   ILE A 325      21.938  20.207 -18.577  1.00 15.60           N  
ATOM   2496  CA  ILE A 325      23.078  19.882 -17.724  1.00 12.20           C  
ATOM   2497  C   ILE A 325      23.465  18.437 -17.971  1.00 13.47           C  
ATOM   2498  O   ILE A 325      22.725  17.680 -18.607  1.00 16.89           O  
ATOM   2499  CB  ILE A 325      22.780  20.063 -16.162  1.00 14.77           C  
ATOM   2500  CG1 ILE A 325      21.479  19.475 -15.665  1.00  9.95           C  
ATOM   2501  CG2 ILE A 325      22.676  21.541 -15.888  1.00  7.56           C  
ATOM   2502  CD1 ILE A 325      21.550  18.014 -15.303  1.00 17.72           C  
ATOM   2503  N   GLY A 326      24.634  18.050 -17.470  1.00 12.09           N  
ATOM   2504  CA  GLY A 326      25.054  16.665 -17.510  1.00 10.93           C  
ATOM   2505  C   GLY A 326      25.643  16.261 -18.830  1.00 11.75           C  
ATOM   2506  O   GLY A 326      26.094  17.084 -19.605  1.00 17.67           O  
ATOM   2507  N   ASP A 327      25.662  14.972 -19.095  1.00 13.68           N  
ATOM   2508  CA  ASP A 327      26.216  14.401 -20.301  1.00 15.23           C  
ATOM   2509  C   ASP A 327      25.670  14.925 -21.622  1.00 18.22           C  
ATOM   2510  O   ASP A 327      26.424  14.928 -22.598  1.00 20.51           O  
ATOM   2511  CB  ASP A 327      26.024  12.893 -20.230  1.00  9.37           C  
ATOM   2512  CG  ASP A 327      26.962  12.165 -19.279  1.00 14.19           C  
ATOM   2513  OD1 ASP A 327      27.638  12.801 -18.469  1.00 13.05           O  
ATOM   2514  OD2 ASP A 327      27.016  10.942 -19.350  1.00  7.99           O  
ATOM   2515  N   VAL A 328      24.408  15.387 -21.686  1.00 17.01           N  
ATOM   2516  CA  VAL A 328      23.831  15.912 -22.904  1.00 14.71           C  
ATOM   2517  C   VAL A 328      24.559  17.196 -23.311  1.00 16.69           C  
ATOM   2518  O   VAL A 328      24.504  17.563 -24.478  1.00 16.96           O  
ATOM   2519  CB  VAL A 328      22.270  16.106 -22.655  1.00 15.48           C  
ATOM   2520  CG1 VAL A 328      21.908  17.428 -21.978  1.00  7.55           C  
ATOM   2521  CG2 VAL A 328      21.576  15.985 -24.012  1.00  9.92           C  
ATOM   2522  N   THR A 329      25.294  17.890 -22.445  1.00 17.25           N  
ATOM   2523  CA  THR A 329      25.982  19.108 -22.837  1.00 16.69           C  
ATOM   2524  C   THR A 329      27.390  18.844 -23.329  1.00 20.33           C  
ATOM   2525  O   THR A 329      28.121  19.767 -23.701  1.00 24.19           O  
ATOM   2526  CB  THR A 329      26.046  20.086 -21.665  1.00 16.67           C  
ATOM   2527  OG1 THR A 329      26.747  19.447 -20.614  1.00 18.54           O  
ATOM   2528  CG2 THR A 329      24.694  20.466 -21.159  1.00 13.81           C  
ATOM   2529  N   ASN A 330      27.813  17.580 -23.267  1.00 23.09           N  
ATOM   2530  CA  ASN A 330      29.122  17.111 -23.661  1.00 23.52           C  
ATOM   2531  C   ASN A 330      30.295  17.883 -23.050  1.00 27.63           C  
ATOM   2532  O   ASN A 330      31.357  17.980 -23.660  1.00 33.89           O  
ATOM   2533  CB  ASN A 330      29.203  17.113 -25.206  1.00 26.70           C  
ATOM   2534  CG  ASN A 330      30.168  16.080 -25.798  1.00 28.22           C  
ATOM   2535  OD1 ASN A 330      29.872  15.393 -26.779  1.00 39.33           O  
ATOM   2536  ND2 ASN A 330      31.359  15.848 -25.280  1.00 37.60           N  
ATOM   2537  N   ARG A 331      30.175  18.429 -21.833  1.00 26.65           N  
ATOM   2538  CA  ARG A 331      31.301  19.061 -21.163  1.00 23.35           C  
ATOM   2539  C   ARG A 331      32.112  17.995 -20.396  1.00 26.77           C  
ATOM   2540  O   ARG A 331      33.014  17.406 -20.976  1.00 28.49           O  
ATOM   2541  CB  ARG A 331      30.790  20.131 -20.202  1.00 22.21           C  
ATOM   2542  CG  ARG A 331      30.252  21.460 -20.733  1.00 21.30           C  
ATOM   2543  CD  ARG A 331      28.882  21.585 -20.100  1.00 21.35           C  
ATOM   2544  NE  ARG A 331      28.710  22.813 -19.372  1.00 21.25           N  
ATOM   2545  CZ  ARG A 331      27.642  23.058 -18.607  1.00 24.99           C  
ATOM   2546  NH1 ARG A 331      26.639  22.181 -18.454  1.00 16.05           N  
ATOM   2547  NH2 ARG A 331      27.618  24.227 -17.958  1.00 30.33           N  
ATOM   2548  N   VAL A 332      31.919  17.638 -19.111  1.00 25.61           N  
ATOM   2549  CA  VAL A 332      32.720  16.583 -18.480  1.00 21.32           C  
ATOM   2550  C   VAL A 332      31.704  15.527 -18.082  1.00 19.36           C  
ATOM   2551  O   VAL A 332      30.811  15.774 -17.274  1.00 22.08           O  
ATOM   2552  CB  VAL A 332      33.471  17.113 -17.228  1.00 22.74           C  
ATOM   2553  CG1 VAL A 332      34.307  15.995 -16.628  1.00 16.41           C  
ATOM   2554  CG2 VAL A 332      34.410  18.252 -17.595  1.00 16.47           C  
ATOM   2555  N   MET A 333      31.821  14.332 -18.659  1.00 18.59           N  
ATOM   2556  CA  MET A 333      30.849  13.274 -18.418  1.00 19.09           C  
ATOM   2557  C   MET A 333      31.113  12.422 -17.173  1.00 17.42           C  
ATOM   2558  O   MET A 333      31.530  11.261 -17.227  1.00 17.49           O  
ATOM   2559  CB  MET A 333      30.771  12.382 -19.666  1.00 13.01           C  
ATOM   2560  CG  MET A 333      30.249  13.054 -20.951  1.00 14.84           C  
ATOM   2561  SD  MET A 333      29.729  11.738 -22.085  1.00 28.82           S  
ATOM   2562  CE  MET A 333      29.117  12.658 -23.469  1.00 20.58           C  
ATOM   2563  N   LEU A 334      30.855  13.012 -16.017  1.00 19.16           N  
ATOM   2564  CA  LEU A 334      31.083  12.386 -14.722  1.00 17.58           C  
ATOM   2565  C   LEU A 334      29.893  12.710 -13.844  1.00 14.51           C  
ATOM   2566  O   LEU A 334      29.440  13.856 -13.876  1.00 18.42           O  
ATOM   2567  CB  LEU A 334      32.369  12.942 -14.085  1.00 15.28           C  
ATOM   2568  CG  LEU A 334      33.749  12.604 -14.677  1.00 12.26           C  
ATOM   2569  CD1 LEU A 334      34.798  13.442 -13.993  1.00 11.13           C  
ATOM   2570  CD2 LEU A 334      34.081  11.144 -14.486  1.00 10.26           C  
ATOM   2571  N   THR A 335      29.350  11.774 -13.058  1.00 16.10           N  
ATOM   2572  CA  THR A 335      28.219  12.052 -12.162  1.00 14.40           C  
ATOM   2573  C   THR A 335      28.397  13.258 -11.226  1.00 13.48           C  
ATOM   2574  O   THR A 335      27.463  14.073 -11.183  1.00 16.36           O  
ATOM   2575  CB  THR A 335      27.925  10.756 -11.347  1.00 15.63           C  
ATOM   2576  OG1 THR A 335      27.244   9.911 -12.256  1.00 16.35           O  
ATOM   2577  CG2 THR A 335      27.075  10.930 -10.103  1.00 13.22           C  
ATOM   2578  N   PRO A 336      29.486  13.491 -10.465  1.00 13.21           N  
ATOM   2579  CA  PRO A 336      29.589  14.623  -9.550  1.00 12.19           C  
ATOM   2580  C   PRO A 336      29.537  15.937 -10.285  1.00 13.61           C  
ATOM   2581  O   PRO A 336      29.041  16.930  -9.743  1.00 17.86           O  
ATOM   2582  CB  PRO A 336      30.887  14.421  -8.815  1.00 11.85           C  
ATOM   2583  CG  PRO A 336      31.064  12.941  -8.875  1.00 10.99           C  
ATOM   2584  CD  PRO A 336      30.665  12.633 -10.302  1.00 13.51           C  
ATOM   2585  N   VAL A 337      30.062  15.995 -11.513  1.00 17.90           N  
ATOM   2586  CA  VAL A 337      29.964  17.186 -12.356  1.00 15.64           C  
ATOM   2587  C   VAL A 337      28.499  17.468 -12.711  1.00 15.41           C  
ATOM   2588  O   VAL A 337      28.056  18.619 -12.576  1.00 18.74           O  
ATOM   2589  CB  VAL A 337      30.834  16.973 -13.625  1.00 15.51           C  
ATOM   2590  CG1 VAL A 337      30.680  18.101 -14.613  1.00 14.26           C  
ATOM   2591  CG2 VAL A 337      32.298  16.970 -13.208  1.00 14.66           C  
ATOM   2592  N   ALA A 338      27.706  16.457 -13.080  1.00 11.84           N  
ATOM   2593  CA  ALA A 338      26.300  16.634 -13.407  1.00 11.08           C  
ATOM   2594  C   ALA A 338      25.502  17.096 -12.196  1.00 15.64           C  
ATOM   2595  O   ALA A 338      24.633  17.969 -12.302  1.00 15.10           O  
ATOM   2596  CB  ALA A 338      25.700  15.315 -13.915  1.00  5.59           C  
ATOM   2597  N   ILE A 339      25.800  16.544 -11.014  1.00 16.68           N  
ATOM   2598  CA  ILE A 339      25.167  16.962  -9.774  1.00 13.00           C  
ATOM   2599  C   ILE A 339      25.477  18.416  -9.459  1.00 12.44           C  
ATOM   2600  O   ILE A 339      24.587  19.212  -9.195  1.00 15.41           O  
ATOM   2601  CB  ILE A 339      25.666  16.002  -8.693  1.00 15.13           C  
ATOM   2602  CG1 ILE A 339      24.992  14.668  -8.957  1.00 10.11           C  
ATOM   2603  CG2 ILE A 339      25.373  16.517  -7.286  1.00 12.03           C  
ATOM   2604  CD1 ILE A 339      25.471  13.518  -8.064  1.00 13.66           C  
ATOM   2605  N   ASN A 340      26.735  18.832  -9.557  1.00 14.62           N  
ATOM   2606  CA  ASN A 340      27.163  20.204  -9.269  1.00 12.75           C  
ATOM   2607  C   ASN A 340      26.502  21.217 -10.186  1.00 14.34           C  
ATOM   2608  O   ASN A 340      26.052  22.285  -9.754  1.00 20.27           O  
ATOM   2609  CB  ASN A 340      28.670  20.333  -9.432  1.00 17.63           C  
ATOM   2610  CG  ASN A 340      29.201  21.623  -8.833  1.00 20.63           C  
ATOM   2611  OD1 ASN A 340      29.002  22.707  -9.347  1.00 31.94           O  
ATOM   2612  ND2 ASN A 340      29.797  21.667  -7.650  1.00 32.17           N  
ATOM   2613  N   GLU A 341      26.498  20.914 -11.486  1.00 13.78           N  
ATOM   2614  CA  GLU A 341      25.801  21.726 -12.483  1.00 15.04           C  
ATOM   2615  C   GLU A 341      24.321  21.863 -12.197  1.00 14.79           C  
ATOM   2616  O   GLU A 341      23.760  22.950 -12.326  1.00 15.37           O  
ATOM   2617  CB  GLU A 341      25.901  21.143 -13.873  1.00 12.68           C  
ATOM   2618  CG  GLU A 341      27.307  21.128 -14.408  1.00 10.67           C  
ATOM   2619  CD  GLU A 341      27.450  20.466 -15.769  1.00 16.28           C  
ATOM   2620  OE1 GLU A 341      26.614  19.682 -16.185  1.00 17.05           O  
ATOM   2621  OE2 GLU A 341      28.414  20.729 -16.455  1.00 22.07           O  
ATOM   2622  N   ALA A 342      23.680  20.771 -11.794  1.00 14.90           N  
ATOM   2623  CA  ALA A 342      22.272  20.802 -11.454  1.00 13.81           C  
ATOM   2624  C   ALA A 342      21.962  21.756 -10.315  1.00 16.16           C  
ATOM   2625  O   ALA A 342      21.037  22.568 -10.389  1.00 20.28           O  
ATOM   2626  CB  ALA A 342      21.834  19.418 -11.061  1.00 15.01           C  
ATOM   2627  N   ALA A 343      22.769  21.720  -9.256  1.00 19.77           N  
ATOM   2628  CA  ALA A 343      22.567  22.575  -8.094  1.00 19.44           C  
ATOM   2629  C   ALA A 343      22.907  24.031  -8.411  1.00 18.02           C  
ATOM   2630  O   ALA A 343      22.190  24.932  -7.971  1.00 19.00           O  
ATOM   2631  CB  ALA A 343      23.438  22.075  -6.945  1.00 14.03           C  
ATOM   2632  N   ALA A 344      23.972  24.304  -9.177  1.00 18.36           N  
ATOM   2633  CA  ALA A 344      24.290  25.657  -9.640  1.00 18.99           C  
ATOM   2634  C   ALA A 344      23.171  26.251 -10.509  1.00 20.31           C  
ATOM   2635  O   ALA A 344      22.756  27.395 -10.304  1.00 24.10           O  
ATOM   2636  CB  ALA A 344      25.563  25.646 -10.472  1.00 13.38           C  
ATOM   2637  N   LEU A 345      22.626  25.452 -11.435  1.00 22.31           N  
ATOM   2638  CA  LEU A 345      21.543  25.848 -12.321  1.00 20.49           C  
ATOM   2639  C   LEU A 345      20.288  26.190 -11.538  1.00 20.85           C  
ATOM   2640  O   LEU A 345      19.703  27.250 -11.785  1.00 23.10           O  
ATOM   2641  CB  LEU A 345      21.274  24.706 -13.324  1.00 16.61           C  
ATOM   2642  CG  LEU A 345      20.319  24.820 -14.519  1.00 15.43           C  
ATOM   2643  CD1 LEU A 345      18.907  24.503 -14.084  1.00 21.14           C  
ATOM   2644  CD2 LEU A 345      20.423  26.205 -15.123  1.00 12.81           C  
ATOM   2645  N   VAL A 346      19.808  25.375 -10.598  1.00 21.33           N  
ATOM   2646  CA  VAL A 346      18.612  25.715  -9.834  1.00 21.22           C  
ATOM   2647  C   VAL A 346      18.810  26.962  -8.963  1.00 22.40           C  
ATOM   2648  O   VAL A 346      17.883  27.770  -8.831  1.00 23.52           O  
ATOM   2649  CB  VAL A 346      18.236  24.459  -9.037  1.00 22.74           C  
ATOM   2650  CG1 VAL A 346      17.166  24.709  -7.978  1.00 23.79           C  
ATOM   2651  CG2 VAL A 346      17.671  23.469 -10.051  1.00 14.79           C  
ATOM   2652  N   ASP A 347      20.009  27.194  -8.428  1.00 23.76           N  
ATOM   2653  CA  ASP A 347      20.312  28.415  -7.705  1.00 20.82           C  
ATOM   2654  C   ASP A 347      20.283  29.591  -8.656  1.00 21.75           C  
ATOM   2655  O   ASP A 347      19.600  30.541  -8.316  1.00 23.33           O  
ATOM   2656  CB  ASP A 347      21.691  28.332  -7.036  1.00 24.25           C  
ATOM   2657  CG  ASP A 347      21.754  27.474  -5.761  1.00 27.65           C  
ATOM   2658  OD1 ASP A 347      20.723  27.192  -5.147  1.00 26.70           O  
ATOM   2659  OD2 ASP A 347      22.852  27.072  -5.372  1.00 33.20           O  
ATOM   2660  N   THR A 348      20.908  29.567  -9.840  1.00 22.18           N  
ATOM   2661  CA  THR A 348      20.854  30.647 -10.825  1.00 21.57           C  
ATOM   2662  C   THR A 348      19.427  31.006 -11.235  1.00 22.04           C  
ATOM   2663  O   THR A 348      19.097  32.182 -11.333  1.00 26.47           O  
ATOM   2664  CB  THR A 348      21.667  30.253 -12.111  1.00 24.17           C  
ATOM   2665  OG1 THR A 348      23.021  30.172 -11.706  1.00 21.54           O  
ATOM   2666  CG2 THR A 348      21.574  31.246 -13.268  1.00 22.90           C  
ATOM   2667  N   VAL A 349      18.587  30.011 -11.517  1.00 24.27           N  
ATOM   2668  CA  VAL A 349      17.227  30.219 -11.996  1.00 23.05           C  
ATOM   2669  C   VAL A 349      16.213  30.542 -10.906  1.00 27.38           C  
ATOM   2670  O   VAL A 349      15.425  31.470 -11.065  1.00 29.72           O  
ATOM   2671  CB  VAL A 349      16.789  28.955 -12.789  1.00 20.40           C  
ATOM   2672  CG1 VAL A 349      15.352  29.006 -13.250  1.00 17.65           C  
ATOM   2673  CG2 VAL A 349      17.664  28.874 -14.016  1.00 21.14           C  
ATOM   2674  N   PHE A 350      16.123  29.775  -9.823  1.00 27.94           N  
ATOM   2675  CA  PHE A 350      15.137  30.078  -8.804  1.00 27.62           C  
ATOM   2676  C   PHE A 350      15.714  30.857  -7.646  1.00 30.57           C  
ATOM   2677  O   PHE A 350      14.961  31.434  -6.865  1.00 33.36           O  
ATOM   2678  CB  PHE A 350      14.525  28.783  -8.306  1.00 22.16           C  
ATOM   2679  CG  PHE A 350      13.845  28.039  -9.438  1.00 24.04           C  
ATOM   2680  CD1 PHE A 350      12.836  28.658 -10.184  1.00 24.90           C  
ATOM   2681  CD2 PHE A 350      14.253  26.742  -9.743  1.00 24.86           C  
ATOM   2682  CE1 PHE A 350      12.236  27.974 -11.240  1.00 27.07           C  
ATOM   2683  CE2 PHE A 350      13.647  26.064 -10.803  1.00 30.48           C  
ATOM   2684  CZ  PHE A 350      12.641  26.679 -11.551  1.00 26.19           C  
ATOM   2685  N   GLY A 351      17.023  30.850  -7.456  1.00 33.74           N  
ATOM   2686  CA  GLY A 351      17.638  31.573  -6.368  1.00 38.42           C  
ATOM   2687  C   GLY A 351      18.033  32.963  -6.810  1.00 44.86           C  
ATOM   2688  O   GLY A 351      17.887  33.389  -7.953  1.00 45.71           O  
ATOM   2689  N   THR A 352      18.536  33.664  -5.809  1.00 51.03           N  
ATOM   2690  CA  THR A 352      18.952  35.052  -5.940  1.00 58.15           C  
ATOM   2691  C   THR A 352      20.357  35.270  -6.486  1.00 59.57           C  
ATOM   2692  O   THR A 352      20.679  36.343  -7.006  1.00 61.79           O  
ATOM   2693  CB  THR A 352      18.779  35.722  -4.536  1.00 62.12           C  
ATOM   2694  OG1 THR A 352      19.093  34.742  -3.524  1.00 62.19           O  
ATOM   2695  CG2 THR A 352      17.353  36.261  -4.351  1.00 62.74           C  
ATOM   2696  N   THR A 353      21.226  34.273  -6.348  1.00 60.54           N  
ATOM   2697  CA  THR A 353      22.588  34.424  -6.813  1.00 58.94           C  
ATOM   2698  C   THR A 353      22.919  33.395  -7.893  1.00 55.99           C  
ATOM   2699  O   THR A 353      22.810  32.188  -7.642  1.00 56.41           O  
ATOM   2700  CB  THR A 353      23.515  34.291  -5.590  1.00 62.36           C  
ATOM   2701  OG1 THR A 353      22.945  35.050  -4.515  1.00 65.15           O  
ATOM   2702  CG2 THR A 353      24.917  34.802  -5.900  1.00 64.06           C  
ATOM   2703  N   PRO A 354      23.323  33.845  -9.094  1.00 52.81           N  
ATOM   2704  CA  PRO A 354      23.810  33.018 -10.195  1.00 50.85           C  
ATOM   2705  C   PRO A 354      25.053  32.241  -9.789  1.00 49.38           C  
ATOM   2706  O   PRO A 354      25.994  32.829  -9.249  1.00 50.83           O  
ATOM   2707  CB  PRO A 354      24.079  33.989 -11.318  1.00 50.30           C  
ATOM   2708  CG  PRO A 354      23.195  35.155 -10.977  1.00 51.20           C  
ATOM   2709  CD  PRO A 354      23.370  35.247  -9.475  1.00 53.05           C  
ATOM   2710  N   ARG A 355      25.094  30.949 -10.090  1.00 44.76           N  
ATOM   2711  CA  ARG A 355      26.161  30.064  -9.680  1.00 37.42           C  
ATOM   2712  C   ARG A 355      26.573  29.293 -10.925  1.00 36.00           C  
ATOM   2713  O   ARG A 355      25.712  28.980 -11.759  1.00 36.71           O  
ATOM   2714  CB  ARG A 355      25.579  29.163  -8.584  1.00 36.83           C  
ATOM   2715  CG  ARG A 355      26.601  28.659  -7.588  1.00 37.17           C  
ATOM   2716  CD  ARG A 355      26.021  27.890  -6.390  1.00 40.62           C  
ATOM   2717  NE  ARG A 355      25.710  26.462  -6.523  1.00 46.89           N  
ATOM   2718  CZ  ARG A 355      26.578  25.511  -6.934  1.00 59.79           C  
ATOM   2719  NH1 ARG A 355      27.849  25.755  -7.290  1.00 61.93           N  
ATOM   2720  NH2 ARG A 355      26.162  24.246  -6.990  1.00 62.34           N  
ATOM   2721  N   LYS A 356      27.865  29.050 -11.153  1.00 33.21           N  
ATOM   2722  CA  LYS A 356      28.316  28.171 -12.228  1.00 30.44           C  
ATOM   2723  C   LYS A 356      29.324  27.167 -11.712  1.00 27.61           C  
ATOM   2724  O   LYS A 356      30.002  27.405 -10.716  1.00 33.73           O  
ATOM   2725  CB  LYS A 356      28.979  28.931 -13.370  1.00 31.55           C  
ATOM   2726  CG  LYS A 356      29.945  30.028 -13.004  1.00 35.08           C  
ATOM   2727  CD  LYS A 356      30.672  30.404 -14.274  1.00 39.80           C  
ATOM   2728  CE  LYS A 356      31.382  31.727 -14.048  1.00 50.24           C  
ATOM   2729  NZ  LYS A 356      32.323  31.998 -15.118  1.00 55.08           N  
ATOM   2730  N   THR A 357      29.394  26.026 -12.370  1.00 24.68           N  
ATOM   2731  CA  THR A 357      30.334  24.970 -12.065  1.00 21.72           C  
ATOM   2732  C   THR A 357      31.695  25.240 -12.692  1.00 21.22           C  
ATOM   2733  O   THR A 357      31.848  25.590 -13.874  1.00 27.82           O  
ATOM   2734  CB  THR A 357      29.772  23.638 -12.604  1.00 16.50           C  
ATOM   2735  OG1 THR A 357      28.512  23.509 -11.987  1.00 21.95           O  
ATOM   2736  CG2 THR A 357      30.606  22.409 -12.318  1.00 18.75           C  
ATOM   2737  N   ASP A 358      32.724  24.982 -11.917  1.00 21.16           N  
ATOM   2738  CA  ASP A 358      34.086  25.006 -12.358  1.00 20.92           C  
ATOM   2739  C   ASP A 358      34.347  23.581 -12.785  1.00 20.06           C  
ATOM   2740  O   ASP A 358      34.170  22.612 -12.055  1.00 22.45           O  
ATOM   2741  CB  ASP A 358      35.039  25.357 -11.239  1.00 22.61           C  
ATOM   2742  CG  ASP A 358      36.485  25.512 -11.709  1.00 25.84           C  
ATOM   2743  OD1 ASP A 358      36.735  25.521 -12.912  1.00 30.96           O  
ATOM   2744  OD2 ASP A 358      37.372  25.639 -10.869  1.00 27.95           O  
ATOM   2745  N   HIS A 359      34.662  23.532 -14.075  1.00 17.21           N  
ATOM   2746  CA  HIS A 359      34.990  22.280 -14.716  1.00 14.69           C  
ATOM   2747  C   HIS A 359      36.484  22.074 -14.770  1.00 16.13           C  
ATOM   2748  O   HIS A 359      36.889  21.081 -15.360  1.00 23.25           O  
ATOM   2749  CB  HIS A 359      34.463  22.235 -16.138  1.00 14.79           C  
ATOM   2750  CG  HIS A 359      32.960  22.331 -16.198  1.00 15.90           C  
ATOM   2751  ND1 HIS A 359      32.125  23.379 -16.193  1.00 17.96           N  
ATOM   2752  CD2 HIS A 359      32.210  21.192 -16.197  1.00 14.08           C  
ATOM   2753  CE1 HIS A 359      30.890  22.920 -16.180  1.00 13.15           C  
ATOM   2754  NE2 HIS A 359      30.972  21.604 -16.184  1.00 15.79           N  
ATOM   2755  N   THR A 360      37.353  22.957 -14.282  1.00 15.83           N  
ATOM   2756  CA  THR A 360      38.784  22.685 -14.267  1.00 20.33           C  
ATOM   2757  C   THR A 360      39.108  21.958 -12.956  1.00 21.92           C  
ATOM   2758  O   THR A 360      38.298  21.979 -12.015  1.00 18.62           O  
ATOM   2759  CB  THR A 360      39.571  24.032 -14.384  1.00 21.64           C  
ATOM   2760  OG1 THR A 360      39.239  24.859 -13.283  1.00 25.54           O  
ATOM   2761  CG2 THR A 360      39.176  24.812 -15.617  1.00 22.90           C  
ATOM   2762  N   ARG A 361      40.280  21.293 -12.888  1.00 19.04           N  
ATOM   2763  CA  ARG A 361      40.776  20.648 -11.675  1.00 19.30           C  
ATOM   2764  C   ARG A 361      39.820  19.668 -11.001  1.00 21.73           C  
ATOM   2765  O   ARG A 361      39.826  19.487  -9.795  1.00 25.97           O  
ATOM   2766  CB  ARG A 361      41.197  21.710 -10.637  1.00 22.23           C  
ATOM   2767  CG  ARG A 361      42.361  22.593 -11.056  1.00 24.71           C  
ATOM   2768  CD  ARG A 361      41.911  24.049 -11.178  1.00 34.63           C  
ATOM   2769  NE  ARG A 361      41.904  24.797  -9.929  1.00 39.86           N  
ATOM   2770  CZ  ARG A 361      41.011  25.767  -9.639  1.00 41.20           C  
ATOM   2771  NH1 ARG A 361      40.042  26.127 -10.475  1.00 40.15           N  
ATOM   2772  NH2 ARG A 361      41.094  26.414  -8.472  1.00 38.25           N  
ATOM   2773  N   VAL A 362      39.016  18.967 -11.809  1.00 20.73           N  
ATOM   2774  CA  VAL A 362      38.087  17.962 -11.340  1.00 15.74           C  
ATOM   2775  C   VAL A 362      38.886  16.665 -11.221  1.00 17.90           C  
ATOM   2776  O   VAL A 362      39.515  16.232 -12.192  1.00 17.76           O  
ATOM   2777  CB  VAL A 362      36.939  17.818 -12.366  1.00 15.60           C  
ATOM   2778  CG1 VAL A 362      36.024  16.709 -11.911  1.00 21.19           C  
ATOM   2779  CG2 VAL A 362      36.149  19.118 -12.506  1.00 13.92           C  
ATOM   2780  N   ALA A 363      38.849  16.026 -10.062  1.00 13.92           N  
ATOM   2781  CA  ALA A 363      39.572  14.788  -9.835  1.00 14.30           C  
ATOM   2782  C   ALA A 363      38.703  13.636 -10.306  1.00 12.89           C  
ATOM   2783  O   ALA A 363      37.469  13.715 -10.220  1.00 13.04           O  
ATOM   2784  CB  ALA A 363      39.876  14.619  -8.345  1.00 12.19           C  
ATOM   2785  N   SER A 364      39.289  12.566 -10.818  1.00 10.36           N  
ATOM   2786  CA  SER A 364      38.513  11.450 -11.316  1.00 10.61           C  
ATOM   2787  C   SER A 364      39.342  10.198 -11.173  1.00  7.70           C  
ATOM   2788  O   SER A 364      40.528  10.281 -10.858  1.00 12.28           O  
ATOM   2789  CB  SER A 364      38.152  11.710 -12.775  1.00  7.70           C  
ATOM   2790  OG  SER A 364      39.252  11.627 -13.669  1.00 19.74           O  
ATOM   2791  N   ALA A 365      38.763   9.032 -11.399  1.00  8.95           N  
ATOM   2792  CA  ALA A 365      39.488   7.785 -11.235  1.00  9.39           C  
ATOM   2793  C   ALA A 365      39.171   6.849 -12.381  1.00 11.10           C  
ATOM   2794  O   ALA A 365      38.124   6.991 -13.014  1.00 13.36           O  
ATOM   2795  CB  ALA A 365      39.050   7.103  -9.972  1.00  9.00           C  
ATOM   2796  N   VAL A 366      40.044   5.902 -12.676  1.00 11.61           N  
ATOM   2797  CA  VAL A 366      39.735   4.832 -13.603  1.00 10.90           C  
ATOM   2798  C   VAL A 366      39.849   3.619 -12.677  1.00 12.00           C  
ATOM   2799  O   VAL A 366      40.892   3.385 -12.060  1.00 13.36           O  
ATOM   2800  CB  VAL A 366      40.775   4.693 -14.757  1.00  9.34           C  
ATOM   2801  CG1 VAL A 366      40.381   3.507 -15.636  1.00  7.51           C  
ATOM   2802  CG2 VAL A 366      40.823   5.957 -15.601  1.00  6.94           C  
ATOM   2803  N   PHE A 367      38.798   2.836 -12.523  1.00 12.30           N  
ATOM   2804  CA  PHE A 367      38.865   1.663 -11.683  1.00 12.94           C  
ATOM   2805  C   PHE A 367      39.399   0.473 -12.444  1.00 12.98           C  
ATOM   2806  O   PHE A 367      38.723  -0.546 -12.611  1.00 16.82           O  
ATOM   2807  CB  PHE A 367      37.460   1.363 -11.101  1.00 13.08           C  
ATOM   2808  CG  PHE A 367      37.085   2.400 -10.059  1.00  8.56           C  
ATOM   2809  CD1 PHE A 367      37.513   2.245  -8.742  1.00 16.42           C  
ATOM   2810  CD2 PHE A 367      36.350   3.519 -10.434  1.00 13.31           C  
ATOM   2811  CE1 PHE A 367      37.191   3.233  -7.809  1.00 24.27           C  
ATOM   2812  CE2 PHE A 367      36.032   4.501  -9.496  1.00 21.17           C  
ATOM   2813  CZ  PHE A 367      36.454   4.362  -8.181  1.00 14.71           C  
ATOM   2814  N   SER A 368      40.588   0.608 -13.012  1.00 14.09           N  
ATOM   2815  CA  SER A 368      41.238  -0.542 -13.610  1.00 15.54           C  
ATOM   2816  C   SER A 368      41.845  -1.303 -12.436  1.00 16.36           C  
ATOM   2817  O   SER A 368      41.783  -0.839 -11.297  1.00 15.91           O  
ATOM   2818  CB  SER A 368      42.335  -0.102 -14.579  1.00  7.97           C  
ATOM   2819  OG  SER A 368      42.819   1.177 -14.218  1.00 12.23           O  
ATOM   2820  N   ILE A 369      42.462  -2.456 -12.655  1.00 18.60           N  
ATOM   2821  CA  ILE A 369      43.125  -3.197 -11.595  1.00 18.28           C  
ATOM   2822  C   ILE A 369      44.576  -3.234 -12.072  1.00 21.41           C  
ATOM   2823  O   ILE A 369      44.838  -3.994 -13.008  1.00 25.84           O  
ATOM   2824  CB  ILE A 369      42.501  -4.619 -11.482  1.00 11.62           C  
ATOM   2825  CG1 ILE A 369      41.095  -4.526 -10.919  1.00 10.11           C  
ATOM   2826  CG2 ILE A 369      43.368  -5.488 -10.591  1.00  8.35           C  
ATOM   2827  CD1 ILE A 369      40.374  -5.863 -10.900  1.00 11.95           C  
ATOM   2828  N   PRO A 370      45.557  -2.459 -11.560  1.00 20.68           N  
ATOM   2829  CA  PRO A 370      45.452  -1.469 -10.491  1.00 16.17           C  
ATOM   2830  C   PRO A 370      44.795  -0.178 -10.957  1.00 17.05           C  
ATOM   2831  O   PRO A 370      44.796   0.099 -12.156  1.00 18.47           O  
ATOM   2832  CB  PRO A 370      46.870  -1.243 -10.040  1.00 14.21           C  
ATOM   2833  CG  PRO A 370      47.611  -2.391 -10.658  1.00 25.36           C  
ATOM   2834  CD  PRO A 370      46.940  -2.527 -11.999  1.00 16.07           C  
ATOM   2835  N   PRO A 371      44.221   0.626 -10.064  1.00 15.63           N  
ATOM   2836  CA  PRO A 371      43.478   1.809 -10.440  1.00  8.82           C  
ATOM   2837  C   PRO A 371      44.308   3.047 -10.701  1.00  9.88           C  
ATOM   2838  O   PRO A 371      45.493   3.105 -10.361  1.00 13.46           O  
ATOM   2839  CB  PRO A 371      42.513   1.946  -9.304  1.00 17.18           C  
ATOM   2840  CG  PRO A 371      43.337   1.530  -8.092  1.00  9.55           C  
ATOM   2841  CD  PRO A 371      44.018   0.308  -8.647  1.00 13.51           C  
ATOM   2842  N   ILE A 372      43.665   4.079 -11.245  1.00 11.04           N  
ATOM   2843  CA  ILE A 372      44.283   5.364 -11.533  1.00 11.56           C  
ATOM   2844  C   ILE A 372      43.514   6.437 -10.773  1.00  8.25           C  
ATOM   2845  O   ILE A 372      42.292   6.368 -10.682  1.00 11.08           O  
ATOM   2846  CB  ILE A 372      44.221   5.659 -13.069  1.00 13.87           C  
ATOM   2847  CG1 ILE A 372      45.273   4.814 -13.738  1.00  9.97           C  
ATOM   2848  CG2 ILE A 372      44.421   7.145 -13.393  1.00  5.52           C  
ATOM   2849  CD1 ILE A 372      45.291   4.919 -15.274  1.00 20.19           C  
ATOM   2850  N   GLY A 373      44.179   7.432 -10.210  1.00 10.44           N  
ATOM   2851  CA  GLY A 373      43.522   8.567  -9.599  1.00  7.09           C  
ATOM   2852  C   GLY A 373      44.157   9.771 -10.262  1.00 11.32           C  
ATOM   2853  O   GLY A 373      45.389   9.795 -10.331  1.00 14.47           O  
ATOM   2854  N   THR A 374      43.435  10.761 -10.788  1.00 10.88           N  
ATOM   2855  CA  THR A 374      44.039  11.876 -11.502  1.00 11.38           C  
ATOM   2856  C   THR A 374      43.303  13.198 -11.241  1.00 11.96           C  
ATOM   2857  O   THR A 374      42.086  13.222 -11.062  1.00 11.16           O  
ATOM   2858  CB  THR A 374      44.034  11.459 -12.991  1.00 12.42           C  
ATOM   2859  OG1 THR A 374      44.777  12.422 -13.728  1.00 15.14           O  
ATOM   2860  CG2 THR A 374      42.632  11.369 -13.556  1.00  7.16           C  
ATOM   2861  N   CYS A 375      44.020  14.305 -11.143  1.00  9.27           N  
ATOM   2862  CA  CYS A 375      43.418  15.607 -11.007  1.00 11.52           C  
ATOM   2863  C   CYS A 375      44.328  16.553 -11.792  1.00 16.20           C  
ATOM   2864  O   CYS A 375      45.566  16.398 -11.797  1.00 18.55           O  
ATOM   2865  CB  CYS A 375      43.380  16.032  -9.550  1.00 10.26           C  
ATOM   2866  SG  CYS A 375      42.438  17.563  -9.383  1.00 22.38           S  
ATOM   2867  N   GLY A 376      43.740  17.516 -12.499  1.00 18.27           N  
ATOM   2868  CA  GLY A 376      44.447  18.529 -13.264  1.00 16.89           C  
ATOM   2869  C   GLY A 376      45.048  18.055 -14.576  1.00 17.44           C  
ATOM   2870  O   GLY A 376      44.789  16.975 -15.116  1.00 19.22           O  
ATOM   2871  N   LEU A 377      45.936  18.920 -15.042  1.00 20.43           N  
ATOM   2872  CA  LEU A 377      46.612  18.813 -16.315  1.00 18.57           C  
ATOM   2873  C   LEU A 377      47.658  17.746 -16.459  1.00 18.76           C  
ATOM   2874  O   LEU A 377      48.382  17.401 -15.517  1.00 21.36           O  
ATOM   2875  CB  LEU A 377      47.238  20.163 -16.622  1.00 20.69           C  
ATOM   2876  CG  LEU A 377      46.517  21.252 -17.420  1.00 26.72           C  
ATOM   2877  CD1 LEU A 377      45.012  21.285 -17.183  1.00 24.47           C  
ATOM   2878  CD2 LEU A 377      47.202  22.552 -17.052  1.00 21.88           C  
ATOM   2879  N   ILE A 378      47.687  17.115 -17.631  1.00 21.37           N  
ATOM   2880  CA  ILE A 378      48.783  16.229 -18.002  1.00 22.37           C  
ATOM   2881  C   ILE A 378      49.843  17.133 -18.660  1.00 22.79           C  
ATOM   2882  O   ILE A 378      49.510  18.144 -19.289  1.00 24.56           O  
ATOM   2883  CB  ILE A 378      48.330  15.123 -18.998  1.00 20.30           C  
ATOM   2884  CG1 ILE A 378      47.775  15.658 -20.310  1.00 24.15           C  
ATOM   2885  CG2 ILE A 378      47.261  14.333 -18.297  1.00 24.15           C  
ATOM   2886  CD1 ILE A 378      47.590  14.567 -21.380  1.00 12.83           C  
ATOM   2887  N   GLU A 379      51.128  16.783 -18.611  1.00 25.74           N  
ATOM   2888  CA  GLU A 379      52.209  17.657 -19.056  1.00 28.96           C  
ATOM   2889  C   GLU A 379      52.163  18.157 -20.489  1.00 32.45           C  
ATOM   2890  O   GLU A 379      52.483  19.317 -20.704  1.00 32.87           O  
ATOM   2891  CB  GLU A 379      53.540  16.963 -18.824  1.00 24.74           C  
ATOM   2892  CG  GLU A 379      53.793  15.669 -19.571  1.00 20.62           C  
ATOM   2893  CD  GLU A 379      54.839  14.839 -18.863  1.00 29.91           C  
ATOM   2894  OE1 GLU A 379      54.627  14.438 -17.730  1.00 37.85           O  
ATOM   2895  OE2 GLU A 379      55.876  14.576 -19.435  1.00 33.59           O  
ATOM   2896  N   GLU A 380      51.703  17.338 -21.437  1.00 32.15           N  
ATOM   2897  CA  GLU A 380      51.619  17.740 -22.829  1.00 29.99           C  
ATOM   2898  C   GLU A 380      50.738  18.952 -22.990  1.00 30.18           C  
ATOM   2899  O   GLU A 380      51.051  19.758 -23.857  1.00 35.22           O  
ATOM   2900  CB  GLU A 380      51.024  16.671 -23.723  1.00 28.49           C  
ATOM   2901  CG  GLU A 380      51.766  15.347 -23.773  1.00 36.02           C  
ATOM   2902  CD  GLU A 380      51.338  14.261 -22.788  1.00 39.03           C  
ATOM   2903  OE1 GLU A 380      50.887  14.556 -21.684  1.00 35.60           O  
ATOM   2904  OE2 GLU A 380      51.465  13.089 -23.140  1.00 41.75           O  
ATOM   2905  N   VAL A 381      49.651  19.143 -22.219  1.00 26.99           N  
ATOM   2906  CA  VAL A 381      48.860  20.348 -22.434  1.00 26.71           C  
ATOM   2907  C   VAL A 381      49.386  21.433 -21.511  1.00 27.52           C  
ATOM   2908  O   VAL A 381      49.314  22.618 -21.851  1.00 32.17           O  
ATOM   2909  CB  VAL A 381      47.272  20.129 -22.227  1.00 19.87           C  
ATOM   2910  CG1 VAL A 381      47.008  18.658 -22.105  1.00 19.14           C  
ATOM   2911  CG2 VAL A 381      46.691  20.880 -21.049  1.00 23.72           C  
ATOM   2912  N   ALA A 382      49.984  21.087 -20.371  1.00 29.08           N  
ATOM   2913  CA  ALA A 382      50.482  22.120 -19.480  1.00 29.79           C  
ATOM   2914  C   ALA A 382      51.660  22.826 -20.118  1.00 29.28           C  
ATOM   2915  O   ALA A 382      51.701  24.058 -20.087  1.00 29.37           O  
ATOM   2916  CB  ALA A 382      50.969  21.563 -18.154  1.00 29.51           C  
ATOM   2917  N   SER A 383      52.548  22.073 -20.765  1.00 27.23           N  
ATOM   2918  CA  SER A 383      53.713  22.619 -21.429  1.00 33.69           C  
ATOM   2919  C   SER A 383      53.383  23.478 -22.631  1.00 36.20           C  
ATOM   2920  O   SER A 383      54.246  24.186 -23.144  1.00 43.19           O  
ATOM   2921  CB  SER A 383      54.631  21.499 -21.870  1.00 28.40           C  
ATOM   2922  OG  SER A 383      54.021  20.530 -22.704  1.00 36.87           O  
ATOM   2923  N   LYS A 384      52.157  23.374 -23.127  1.00 38.68           N  
ATOM   2924  CA  LYS A 384      51.719  24.240 -24.192  1.00 35.97           C  
ATOM   2925  C   LYS A 384      51.036  25.459 -23.616  1.00 35.14           C  
ATOM   2926  O   LYS A 384      50.837  26.442 -24.323  1.00 38.42           O  
ATOM   2927  CB  LYS A 384      50.774  23.487 -25.120  1.00 35.20           C  
ATOM   2928  CG  LYS A 384      51.555  22.478 -25.975  1.00 44.16           C  
ATOM   2929  CD  LYS A 384      50.890  22.239 -27.336  1.00 56.73           C  
ATOM   2930  CE  LYS A 384      49.634  21.375 -27.257  1.00 58.07           C  
ATOM   2931  NZ  LYS A 384      49.982  19.966 -27.228  1.00 64.75           N  
ATOM   2932  N   ARG A 385      50.629  25.461 -22.356  1.00 35.10           N  
ATOM   2933  CA  ARG A 385      49.996  26.643 -21.798  1.00 36.14           C  
ATOM   2934  C   ARG A 385      50.950  27.404 -20.903  1.00 37.88           C  
ATOM   2935  O   ARG A 385      50.682  28.550 -20.526  1.00 37.47           O  
ATOM   2936  CB  ARG A 385      48.780  26.294 -20.957  1.00 41.41           C  
ATOM   2937  CG  ARG A 385      47.697  25.545 -21.698  1.00 49.55           C  
ATOM   2938  CD  ARG A 385      46.487  25.408 -20.802  1.00 57.56           C  
ATOM   2939  NE  ARG A 385      45.509  24.524 -21.416  1.00 66.16           N  
ATOM   2940  CZ  ARG A 385      44.415  24.121 -20.763  1.00 69.17           C  
ATOM   2941  NH1 ARG A 385      44.151  24.514 -19.509  1.00 76.40           N  
ATOM   2942  NH2 ARG A 385      43.590  23.270 -21.371  1.00 77.04           N  
ATOM   2943  N   TYR A 386      52.054  26.786 -20.496  1.00 38.07           N  
ATOM   2944  CA  TYR A 386      52.973  27.390 -19.551  1.00 37.46           C  
ATOM   2945  C   TYR A 386      54.345  27.304 -20.159  1.00 36.96           C  
ATOM   2946  O   TYR A 386      54.687  26.309 -20.804  1.00 35.84           O  
ATOM   2947  CB  TYR A 386      52.951  26.632 -18.207  1.00 35.62           C  
ATOM   2948  CG  TYR A 386      51.636  26.823 -17.475  1.00 32.95           C  
ATOM   2949  CD1 TYR A 386      51.483  27.934 -16.648  1.00 33.17           C  
ATOM   2950  CD2 TYR A 386      50.575  25.931 -17.675  1.00 33.44           C  
ATOM   2951  CE1 TYR A 386      50.265  28.165 -16.020  1.00 30.19           C  
ATOM   2952  CE2 TYR A 386      49.348  26.159 -17.050  1.00 29.52           C  
ATOM   2953  CZ  TYR A 386      49.211  27.273 -16.231  1.00 33.95           C  
ATOM   2954  OH  TYR A 386      48.012  27.496 -15.592  1.00 40.35           O  
ATOM   2955  N   GLU A 387      55.122  28.371 -19.957  1.00 40.25           N  
ATOM   2956  CA  GLU A 387      56.470  28.401 -20.489  1.00 42.26           C  
ATOM   2957  C   GLU A 387      57.443  27.482 -19.765  1.00 40.46           C  
ATOM   2958  O   GLU A 387      58.313  26.920 -20.428  1.00 40.69           O  
ATOM   2959  CB  GLU A 387      56.981  29.831 -20.457  1.00 49.46           C  
ATOM   2960  CG  GLU A 387      58.357  29.982 -21.109  1.00 59.10           C  
ATOM   2961  CD  GLU A 387      58.566  31.340 -21.742  1.00 63.53           C  
ATOM   2962  OE1 GLU A 387      58.539  32.351 -21.053  1.00 72.36           O  
ATOM   2963  OE2 GLU A 387      58.763  31.401 -22.936  1.00 66.06           O  
ATOM   2964  N   VAL A 388      57.395  27.358 -18.437  1.00 37.22           N  
ATOM   2965  CA  VAL A 388      58.263  26.389 -17.784  1.00 36.73           C  
ATOM   2966  C   VAL A 388      57.446  25.518 -16.832  1.00 33.21           C  
ATOM   2967  O   VAL A 388      56.724  25.978 -15.938  1.00 31.31           O  
ATOM   2968  CB  VAL A 388      59.438  27.168 -17.079  1.00 37.69           C  
ATOM   2969  CG1 VAL A 388      58.968  28.180 -16.064  1.00 35.11           C  
ATOM   2970  CG2 VAL A 388      60.331  26.130 -16.422  1.00 35.94           C  
ATOM   2971  N   VAL A 389      57.534  24.223 -17.089  1.00 29.51           N  
ATOM   2972  CA  VAL A 389      56.804  23.210 -16.355  1.00 29.98           C  
ATOM   2973  C   VAL A 389      57.804  22.238 -15.732  1.00 30.33           C  
ATOM   2974  O   VAL A 389      58.765  21.841 -16.399  1.00 31.21           O  
ATOM   2975  CB  VAL A 389      55.827  22.491 -17.337  1.00 27.80           C  
ATOM   2976  CG1 VAL A 389      55.270  21.182 -16.791  1.00 26.61           C  
ATOM   2977  CG2 VAL A 389      54.637  23.406 -17.539  1.00 27.69           C  
ATOM   2978  N   ALA A 390      57.632  21.890 -14.451  1.00 27.35           N  
ATOM   2979  CA  ALA A 390      58.493  20.942 -13.758  1.00 20.67           C  
ATOM   2980  C   ALA A 390      57.698  19.663 -13.546  1.00 19.48           C  
ATOM   2981  O   ALA A 390      56.511  19.716 -13.198  1.00 17.21           O  
ATOM   2982  CB  ALA A 390      58.896  21.496 -12.406  1.00 20.39           C  
ATOM   2983  N   VAL A 391      58.295  18.507 -13.790  1.00 15.73           N  
ATOM   2984  CA  VAL A 391      57.619  17.247 -13.604  1.00 17.71           C  
ATOM   2985  C   VAL A 391      58.383  16.504 -12.526  1.00 20.28           C  
ATOM   2986  O   VAL A 391      59.597  16.334 -12.650  1.00 19.60           O  
ATOM   2987  CB  VAL A 391      57.627  16.444 -14.909  1.00 16.00           C  
ATOM   2988  CG1 VAL A 391      57.027  15.074 -14.681  1.00 19.66           C  
ATOM   2989  CG2 VAL A 391      56.805  17.165 -15.955  1.00 18.09           C  
ATOM   2990  N   TYR A 392      57.690  16.117 -11.454  1.00 22.51           N  
ATOM   2991  CA  TYR A 392      58.231  15.343 -10.337  1.00 17.87           C  
ATOM   2992  C   TYR A 392      57.649  13.972 -10.551  1.00 17.19           C  
ATOM   2993  O   TYR A 392      56.442  13.843 -10.746  1.00 20.32           O  
ATOM   2994  CB  TYR A 392      57.745  15.827  -8.992  1.00 20.14           C  
ATOM   2995  CG  TYR A 392      58.136  17.263  -8.731  1.00 16.87           C  
ATOM   2996  CD1 TYR A 392      57.468  18.282  -9.408  1.00 17.36           C  
ATOM   2997  CD2 TYR A 392      59.146  17.555  -7.819  1.00 16.35           C  
ATOM   2998  CE1 TYR A 392      57.804  19.605  -9.183  1.00 12.87           C  
ATOM   2999  CE2 TYR A 392      59.491  18.883  -7.584  1.00 13.30           C  
ATOM   3000  CZ  TYR A 392      58.812  19.893  -8.276  1.00 16.82           C  
ATOM   3001  OH  TYR A 392      59.112  21.233  -8.124  1.00 18.54           O  
ATOM   3002  N   LEU A 393      58.474  12.953 -10.571  1.00 17.27           N  
ATOM   3003  CA  LEU A 393      58.013  11.625 -10.852  1.00 21.77           C  
ATOM   3004  C   LEU A 393      58.602  10.715  -9.795  1.00 24.37           C  
ATOM   3005  O   LEU A 393      59.767  10.860  -9.435  1.00 25.75           O  
ATOM   3006  CB  LEU A 393      58.484  11.210 -12.243  1.00 21.66           C  
ATOM   3007  CG  LEU A 393      58.371   9.765 -12.705  1.00 20.57           C  
ATOM   3008  CD1 LEU A 393      56.931   9.280 -12.778  1.00 25.66           C  
ATOM   3009  CD2 LEU A 393      58.988   9.704 -14.081  1.00 29.66           C  
ATOM   3010  N   SER A 394      57.830   9.772  -9.291  1.00 26.34           N  
ATOM   3011  CA  SER A 394      58.318   8.842  -8.305  1.00 26.25           C  
ATOM   3012  C   SER A 394      57.636   7.518  -8.600  1.00 23.90           C  
ATOM   3013  O   SER A 394      56.421   7.503  -8.774  1.00 28.76           O  
ATOM   3014  CB  SER A 394      57.951   9.438  -6.958  1.00 26.87           C  
ATOM   3015  OG  SER A 394      58.296   8.606  -5.872  1.00 37.21           O  
ATOM   3016  N   SER A 395      58.323   6.415  -8.793  1.00 23.16           N  
ATOM   3017  CA  SER A 395      57.654   5.143  -8.949  1.00 30.57           C  
ATOM   3018  C   SER A 395      58.388   4.174  -8.050  1.00 34.18           C  
ATOM   3019  O   SER A 395      59.611   4.273  -7.916  1.00 36.40           O  
ATOM   3020  CB  SER A 395      57.697   4.682 -10.401  1.00 32.05           C  
ATOM   3021  OG  SER A 395      58.976   4.712 -11.015  1.00 48.28           O  
ATOM   3022  N   PHE A 396      57.686   3.258  -7.387  1.00 35.52           N  
ATOM   3023  CA  PHE A 396      58.295   2.356  -6.413  1.00 35.16           C  
ATOM   3024  C   PHE A 396      57.423   1.131  -6.255  1.00 36.23           C  
ATOM   3025  O   PHE A 396      56.219   1.244  -6.494  1.00 39.10           O  
ATOM   3026  CB  PHE A 396      58.426   3.052  -5.044  1.00 31.46           C  
ATOM   3027  CG  PHE A 396      57.135   3.659  -4.517  1.00 25.22           C  
ATOM   3028  CD1 PHE A 396      56.719   4.909  -4.981  1.00 27.99           C  
ATOM   3029  CD2 PHE A 396      56.360   2.966  -3.584  1.00 30.13           C  
ATOM   3030  CE1 PHE A 396      55.516   5.447  -4.536  1.00 32.45           C  
ATOM   3031  CE2 PHE A 396      55.154   3.511  -3.139  1.00 32.70           C  
ATOM   3032  CZ  PHE A 396      54.740   4.756  -3.606  1.00 29.96           C  
ATOM   3033  N   THR A 397      57.949  -0.022  -5.870  1.00 35.23           N  
ATOM   3034  CA  THR A 397      57.071  -1.149  -5.612  1.00 38.11           C  
ATOM   3035  C   THR A 397      56.691  -1.054  -4.142  1.00 38.75           C  
ATOM   3036  O   THR A 397      57.576  -0.944  -3.287  1.00 41.96           O  
ATOM   3037  CB  THR A 397      57.788  -2.450  -5.884  1.00 37.53           C  
ATOM   3038  OG1 THR A 397      58.508  -2.256  -7.102  1.00 45.61           O  
ATOM   3039  CG2 THR A 397      56.820  -3.628  -5.967  1.00 38.04           C  
ATOM   3040  N   PRO A 398      55.409  -1.001  -3.773  1.00 40.21           N  
ATOM   3041  CA  PRO A 398      54.982  -1.041  -2.384  1.00 41.53           C  
ATOM   3042  C   PRO A 398      55.570  -2.307  -1.750  1.00 43.53           C  
ATOM   3043  O   PRO A 398      55.581  -3.374  -2.391  1.00 43.45           O  
ATOM   3044  CB  PRO A 398      53.475  -1.008  -2.506  1.00 40.52           C  
ATOM   3045  CG  PRO A 398      53.257  -0.219  -3.776  1.00 39.12           C  
ATOM   3046  CD  PRO A 398      54.274  -0.875  -4.678  1.00 36.76           C  
ATOM   3047  N   LEU A 399      56.036  -2.262  -0.498  1.00 45.25           N  
ATOM   3048  CA  LEU A 399      56.664  -3.430   0.112  1.00 44.29           C  
ATOM   3049  C   LEU A 399      55.716  -4.621   0.160  1.00 40.65           C  
ATOM   3050  O   LEU A 399      56.102  -5.756  -0.111  1.00 39.77           O  
ATOM   3051  CB  LEU A 399      57.133  -3.066   1.509  1.00 51.87           C  
ATOM   3052  CG  LEU A 399      57.848  -4.116   2.364  1.00 55.29           C  
ATOM   3053  CD1 LEU A 399      59.085  -4.675   1.675  1.00 55.55           C  
ATOM   3054  CD2 LEU A 399      58.237  -3.450   3.665  1.00 57.11           C  
ATOM   3055  N   MET A 400      54.437  -4.321   0.371  1.00 34.52           N  
ATOM   3056  CA  MET A 400      53.395  -5.321   0.323  1.00 33.96           C  
ATOM   3057  C   MET A 400      53.474  -6.151  -0.951  1.00 32.67           C  
ATOM   3058  O   MET A 400      53.235  -7.356  -0.941  1.00 31.79           O  
ATOM   3059  CB  MET A 400      52.075  -4.628   0.373  1.00 35.40           C  
ATOM   3060  CG  MET A 400      50.917  -5.575   0.199  1.00 47.94           C  
ATOM   3061  SD  MET A 400      49.545  -4.614  -0.457  1.00 51.41           S  
ATOM   3062  CE  MET A 400      48.939  -3.849   1.024  1.00 66.48           C  
ATOM   3063  N   HIS A 401      53.768  -5.524  -2.089  1.00 31.12           N  
ATOM   3064  CA  HIS A 401      53.830  -6.258  -3.339  1.00 31.73           C  
ATOM   3065  C   HIS A 401      55.174  -6.859  -3.624  1.00 35.46           C  
ATOM   3066  O   HIS A 401      55.276  -7.758  -4.464  1.00 36.33           O  
ATOM   3067  CB  HIS A 401      53.416  -5.356  -4.470  1.00 24.78           C  
ATOM   3068  CG  HIS A 401      51.910  -5.294  -4.458  1.00 14.22           C  
ATOM   3069  ND1 HIS A 401      51.077  -6.326  -4.428  1.00 25.15           N  
ATOM   3070  CD2 HIS A 401      51.152  -4.155  -4.436  1.00 15.01           C  
ATOM   3071  CE1 HIS A 401      49.843  -5.873  -4.385  1.00 11.68           C  
ATOM   3072  NE2 HIS A 401      49.910  -4.572  -4.390  1.00 18.12           N  
ATOM   3073  N   LYS A 402      56.185  -6.382  -2.903  1.00 40.07           N  
ATOM   3074  CA  LYS A 402      57.481  -7.035  -2.962  1.00 44.55           C  
ATOM   3075  C   LYS A 402      57.300  -8.426  -2.330  1.00 45.01           C  
ATOM   3076  O   LYS A 402      57.884  -9.398  -2.813  1.00 48.68           O  
ATOM   3077  CB  LYS A 402      58.538  -6.271  -2.171  1.00 48.59           C  
ATOM   3078  CG  LYS A 402      58.895  -4.915  -2.766  1.00 58.86           C  
ATOM   3079  CD  LYS A 402      59.881  -4.184  -1.855  1.00 65.39           C  
ATOM   3080  CE  LYS A 402      60.261  -2.816  -2.416  1.00 66.34           C  
ATOM   3081  NZ  LYS A 402      61.150  -2.105  -1.515  1.00 63.08           N  
ATOM   3082  N   VAL A 403      56.418  -8.601  -1.322  1.00 42.40           N  
ATOM   3083  CA  VAL A 403      56.193  -9.886  -0.657  1.00 37.96           C  
ATOM   3084  C   VAL A 403      54.933 -10.597  -1.151  1.00 36.64           C  
ATOM   3085  O   VAL A 403      54.871 -11.828  -1.047  1.00 37.15           O  
ATOM   3086  CB  VAL A 403      56.177  -9.736   0.981  1.00 34.44           C  
ATOM   3087  CG1 VAL A 403      56.766  -8.359   1.371  1.00 34.41           C  
ATOM   3088  CG2 VAL A 403      54.797 -10.129   1.553  1.00 37.53           C  
ATOM   3089  N   SER A 404      53.948  -9.930  -1.756  1.00 37.24           N  
ATOM   3090  CA  SER A 404      52.754 -10.660  -2.144  1.00 34.57           C  
ATOM   3091  C   SER A 404      52.894 -11.501  -3.384  1.00 33.42           C  
ATOM   3092  O   SER A 404      52.025 -12.324  -3.671  1.00 32.30           O  
ATOM   3093  CB  SER A 404      51.607  -9.718  -2.370  1.00 34.14           C  
ATOM   3094  OG  SER A 404      51.680  -8.780  -3.463  1.00 28.41           O  
ATOM   3095  N   GLY A 405      53.955 -11.236  -4.145  1.00 33.65           N  
ATOM   3096  CA  GLY A 405      54.181 -11.924  -5.404  1.00 36.55           C  
ATOM   3097  C   GLY A 405      53.952 -11.003  -6.599  1.00 36.20           C  
ATOM   3098  O   GLY A 405      54.587 -11.160  -7.647  1.00 39.17           O  
ATOM   3099  N   SER A 406      53.086  -9.996  -6.471  1.00 32.48           N  
ATOM   3100  CA  SER A 406      52.837  -9.082  -7.565  1.00 31.40           C  
ATOM   3101  C   SER A 406      53.848  -7.947  -7.590  1.00 31.66           C  
ATOM   3102  O   SER A 406      53.514  -6.761  -7.441  1.00 30.81           O  
ATOM   3103  CB  SER A 406      51.424  -8.560  -7.416  1.00 23.33           C  
ATOM   3104  OG  SER A 406      50.542  -9.659  -7.278  1.00 27.17           O  
ATOM   3105  N   LYS A 407      55.105  -8.297  -7.855  1.00 31.78           N  
ATOM   3106  CA  LYS A 407      56.149  -7.292  -7.870  1.00 32.01           C  
ATOM   3107  C   LYS A 407      56.140  -6.409  -9.101  1.00 29.67           C  
ATOM   3108  O   LYS A 407      56.901  -5.448  -9.204  1.00 29.34           O  
ATOM   3109  CB  LYS A 407      57.530  -7.944  -7.718  1.00 39.29           C  
ATOM   3110  CG  LYS A 407      57.845  -9.245  -8.440  1.00 53.30           C  
ATOM   3111  CD  LYS A 407      57.928 -10.397  -7.424  1.00 66.81           C  
ATOM   3112  CE  LYS A 407      59.144 -10.258  -6.495  1.00 72.60           C  
ATOM   3113  NZ  LYS A 407      59.223 -11.358  -5.546  1.00 74.95           N  
ATOM   3114  N   TYR A 408      55.270  -6.725 -10.058  1.00 27.77           N  
ATOM   3115  CA  TYR A 408      55.035  -5.843 -11.197  1.00 26.47           C  
ATOM   3116  C   TYR A 408      54.103  -4.670 -10.862  1.00 25.71           C  
ATOM   3117  O   TYR A 408      53.815  -3.816 -11.701  1.00 24.71           O  
ATOM   3118  CB  TYR A 408      54.429  -6.633 -12.363  1.00 25.13           C  
ATOM   3119  CG  TYR A 408      53.144  -7.394 -12.066  1.00 23.68           C  
ATOM   3120  CD1 TYR A 408      53.225  -8.703 -11.588  1.00 20.78           C  
ATOM   3121  CD2 TYR A 408      51.894  -6.796 -12.273  1.00 18.17           C  
ATOM   3122  CE1 TYR A 408      52.055  -9.412 -11.318  1.00 20.54           C  
ATOM   3123  CE2 TYR A 408      50.723  -7.512 -12.003  1.00 15.33           C  
ATOM   3124  CZ  TYR A 408      50.814  -8.816 -11.527  1.00 23.19           C  
ATOM   3125  OH  TYR A 408      49.699  -9.573 -11.269  1.00 22.88           O  
ATOM   3126  N   LYS A 409      53.554  -4.642  -9.650  1.00 24.74           N  
ATOM   3127  CA  LYS A 409      52.638  -3.583  -9.281  1.00 21.64           C  
ATOM   3128  C   LYS A 409      53.373  -2.382  -8.733  1.00 21.96           C  
ATOM   3129  O   LYS A 409      53.402  -2.128  -7.524  1.00 23.71           O  
ATOM   3130  CB  LYS A 409      51.630  -4.114  -8.257  1.00 20.33           C  
ATOM   3131  CG  LYS A 409      50.610  -4.994  -8.933  1.00 18.42           C  
ATOM   3132  CD  LYS A 409      49.580  -5.462  -7.954  1.00 13.79           C  
ATOM   3133  CE  LYS A 409      48.529  -6.167  -8.764  1.00 19.06           C  
ATOM   3134  NZ  LYS A 409      47.578  -6.844  -7.911  1.00 17.68           N  
ATOM   3135  N   THR A 410      54.001  -1.673  -9.661  1.00 20.83           N  
ATOM   3136  CA  THR A 410      54.679  -0.421  -9.388  1.00 20.61           C  
ATOM   3137  C   THR A 410      53.663   0.683  -9.062  1.00 24.18           C  
ATOM   3138  O   THR A 410      52.654   0.805  -9.764  1.00 24.80           O  
ATOM   3139  CB  THR A 410      55.495  -0.093 -10.637  1.00 18.94           C  
ATOM   3140  OG1 THR A 410      56.375  -1.201 -10.757  1.00 32.45           O  
ATOM   3141  CG2 THR A 410      56.261   1.210 -10.607  1.00 18.70           C  
ATOM   3142  N   PHE A 411      53.901   1.482  -8.008  1.00 20.01           N  
ATOM   3143  CA  PHE A 411      53.078   2.627  -7.688  1.00 16.50           C  
ATOM   3144  C   PHE A 411      53.741   3.777  -8.422  1.00 17.19           C  
ATOM   3145  O   PHE A 411      54.964   3.897  -8.359  1.00 18.35           O  
ATOM   3146  CB  PHE A 411      53.089   2.928  -6.197  1.00 14.11           C  
ATOM   3147  CG  PHE A 411      52.014   3.942  -5.806  1.00 15.94           C  
ATOM   3148  CD1 PHE A 411      50.730   3.496  -5.504  1.00  9.73           C  
ATOM   3149  CD2 PHE A 411      52.290   5.318  -5.785  1.00 15.12           C  
ATOM   3150  CE1 PHE A 411      49.726   4.422  -5.192  1.00 15.34           C  
ATOM   3151  CE2 PHE A 411      51.285   6.235  -5.472  1.00 19.36           C  
ATOM   3152  CZ  PHE A 411      49.997   5.788  -5.175  1.00 17.28           C  
ATOM   3153  N   VAL A 412      53.012   4.626  -9.138  1.00 16.40           N  
ATOM   3154  CA  VAL A 412      53.579   5.738  -9.885  1.00 16.74           C  
ATOM   3155  C   VAL A 412      52.885   6.987  -9.362  1.00 15.44           C  
ATOM   3156  O   VAL A 412      51.649   7.020  -9.330  1.00 19.17           O  
ATOM   3157  CB  VAL A 412      53.298   5.585 -11.419  1.00 15.77           C  
ATOM   3158  CG1 VAL A 412      53.880   6.775 -12.160  1.00 24.63           C  
ATOM   3159  CG2 VAL A 412      53.932   4.315 -11.973  1.00 15.86           C  
ATOM   3160  N   ALA A 413      53.628   7.997  -8.930  1.00 13.09           N  
ATOM   3161  CA  ALA A 413      53.071   9.227  -8.437  1.00 13.10           C  
ATOM   3162  C   ALA A 413      53.745  10.288  -9.280  1.00 15.48           C  
ATOM   3163  O   ALA A 413      54.978  10.316  -9.389  1.00 16.99           O  
ATOM   3164  CB  ALA A 413      53.438   9.432  -6.968  1.00 10.67           C  
ATOM   3165  N   LYS A 414      52.963  11.163  -9.888  1.00 16.50           N  
ATOM   3166  CA  LYS A 414      53.528  12.200 -10.724  1.00 17.34           C  
ATOM   3167  C   LYS A 414      52.875  13.527 -10.429  1.00 15.61           C  
ATOM   3168  O   LYS A 414      51.646  13.623 -10.393  1.00 21.05           O  
ATOM   3169  CB  LYS A 414      53.303  11.777 -12.144  1.00 18.66           C  
ATOM   3170  CG  LYS A 414      54.166  12.477 -13.136  1.00 29.98           C  
ATOM   3171  CD  LYS A 414      54.251  11.477 -14.254  1.00 23.91           C  
ATOM   3172  CE  LYS A 414      54.722  12.247 -15.435  1.00 25.03           C  
ATOM   3173  NZ  LYS A 414      54.609  11.424 -16.609  1.00 20.93           N  
ATOM   3174  N   ILE A 415      53.649  14.565 -10.191  1.00 18.54           N  
ATOM   3175  CA  ILE A 415      53.118  15.891  -9.892  1.00 22.08           C  
ATOM   3176  C   ILE A 415      53.697  16.820 -10.961  1.00 21.81           C  
ATOM   3177  O   ILE A 415      54.904  16.764 -11.228  1.00 21.77           O  
ATOM   3178  CB  ILE A 415      53.570  16.371  -8.468  1.00 22.21           C  
ATOM   3179  CG1 ILE A 415      53.139  15.382  -7.370  1.00 20.20           C  
ATOM   3180  CG2 ILE A 415      52.956  17.745  -8.197  1.00 16.44           C  
ATOM   3181  CD1 ILE A 415      53.708  15.721  -5.971  1.00 16.53           C  
ATOM   3182  N   ILE A 416      52.902  17.643 -11.637  1.00 20.99           N  
ATOM   3183  CA  ILE A 416      53.489  18.554 -12.594  1.00 20.08           C  
ATOM   3184  C   ILE A 416      53.139  19.955 -12.090  1.00 18.49           C  
ATOM   3185  O   ILE A 416      52.036  20.192 -11.568  1.00 18.05           O  
ATOM   3186  CB  ILE A 416      52.953  18.222 -14.083  1.00 24.19           C  
ATOM   3187  CG1 ILE A 416      51.646  18.850 -14.347  1.00 24.79           C  
ATOM   3188  CG2 ILE A 416      52.787  16.713 -14.319  1.00 15.50           C  
ATOM   3189  CD1 ILE A 416      51.994  20.073 -15.210  1.00 29.78           C  
ATOM   3190  N   THR A 417      54.061  20.908 -12.141  1.00 19.81           N  
ATOM   3191  CA  THR A 417      53.788  22.259 -11.663  1.00 21.61           C  
ATOM   3192  C   THR A 417      54.130  23.352 -12.672  1.00 20.23           C  
ATOM   3193  O   THR A 417      54.860  23.145 -13.646  1.00 22.71           O  
ATOM   3194  CB  THR A 417      54.582  22.570 -10.350  1.00 19.25           C  
ATOM   3195  OG1 THR A 417      55.976  22.465 -10.636  1.00 26.08           O  
ATOM   3196  CG2 THR A 417      54.247  21.611  -9.229  1.00 18.19           C  
ATOM   3197  N   ASN A 418      53.592  24.545 -12.441  1.00 20.49           N  
ATOM   3198  CA  ASN A 418      54.013  25.713 -13.170  1.00 19.80           C  
ATOM   3199  C   ASN A 418      55.266  26.079 -12.395  1.00 23.17           C  
ATOM   3200  O   ASN A 418      55.189  26.638 -11.289  1.00 25.08           O  
ATOM   3201  CB  ASN A 418      52.991  26.830 -13.060  1.00 21.90           C  
ATOM   3202  CG  ASN A 418      53.524  28.176 -13.556  1.00 29.31           C  
ATOM   3203  OD1 ASN A 418      54.684  28.355 -13.928  1.00 30.04           O  
ATOM   3204  ND2 ASN A 418      52.720  29.223 -13.553  1.00 30.57           N  
ATOM   3205  N   HIS A 419      56.433  25.779 -12.951  1.00 25.55           N  
ATOM   3206  CA  HIS A 419      57.685  26.012 -12.270  1.00 28.42           C  
ATOM   3207  C   HIS A 419      57.967  27.469 -11.965  1.00 32.17           C  
ATOM   3208  O   HIS A 419      58.759  27.706 -11.063  1.00 33.89           O  
ATOM   3209  CB  HIS A 419      58.840  25.448 -13.092  1.00 33.39           C  
ATOM   3210  CG  HIS A 419      60.184  25.321 -12.362  1.00 40.03           C  
ATOM   3211  ND1 HIS A 419      60.419  24.869 -11.132  1.00 39.34           N  
ATOM   3212  CD2 HIS A 419      61.416  25.613 -12.909  1.00 42.20           C  
ATOM   3213  CE1 HIS A 419      61.701  24.862 -10.909  1.00 35.93           C  
ATOM   3214  NE2 HIS A 419      62.294  25.312 -11.987  1.00 43.96           N  
ATOM   3215  N   SER A 420      57.364  28.449 -12.625  1.00 35.55           N  
ATOM   3216  CA  SER A 420      57.632  29.840 -12.302  1.00 38.45           C  
ATOM   3217  C   SER A 420      57.141  30.218 -10.920  1.00 38.00           C  
ATOM   3218  O   SER A 420      57.662  31.157 -10.315  1.00 42.47           O  
ATOM   3219  CB  SER A 420      56.957  30.756 -13.293  1.00 40.12           C  
ATOM   3220  OG  SER A 420      57.279  30.393 -14.632  1.00 50.35           O  
ATOM   3221  N   ASP A 421      56.094  29.566 -10.405  1.00 37.41           N  
ATOM   3222  CA  ASP A 421      55.663  29.898  -9.057  1.00 33.63           C  
ATOM   3223  C   ASP A 421      55.403  28.693  -8.173  1.00 31.12           C  
ATOM   3224  O   ASP A 421      54.919  28.848  -7.059  1.00 32.49           O  
ATOM   3225  CB  ASP A 421      54.412  30.755  -9.122  1.00 32.12           C  
ATOM   3226  CG  ASP A 421      53.184  30.124  -9.752  1.00 36.35           C  
ATOM   3227  OD1 ASP A 421      53.248  29.026 -10.306  1.00 43.12           O  
ATOM   3228  OD2 ASP A 421      52.139  30.762  -9.687  1.00 49.99           O  
ATOM   3229  N   GLY A 422      55.653  27.485  -8.671  1.00 29.12           N  
ATOM   3230  CA  GLY A 422      55.483  26.291  -7.874  1.00 24.84           C  
ATOM   3231  C   GLY A 422      54.049  25.793  -7.766  1.00 23.32           C  
ATOM   3232  O   GLY A 422      53.839  24.783  -7.090  1.00 25.64           O  
ATOM   3233  N   THR A 423      53.051  26.401  -8.405  1.00 24.82           N  
ATOM   3234  CA  THR A 423      51.664  25.950  -8.372  1.00 23.41           C  
ATOM   3235  C   THR A 423      51.489  24.575  -8.988  1.00 24.53           C  
ATOM   3236  O   THR A 423      51.906  24.369 -10.140  1.00 24.96           O  
ATOM   3237  CB  THR A 423      50.781  26.931  -9.139  1.00 23.80           C  
ATOM   3238  OG1 THR A 423      51.034  28.217  -8.578  1.00 26.25           O  
ATOM   3239  CG2 THR A 423      49.301  26.584  -9.059  1.00 26.67           C  
ATOM   3240  N   VAL A 424      50.873  23.647  -8.258  1.00 25.59           N  
ATOM   3241  CA  VAL A 424      50.629  22.302  -8.759  1.00 23.36           C  
ATOM   3242  C   VAL A 424      49.467  22.370  -9.751  1.00 20.19           C  
ATOM   3243  O   VAL A 424      48.389  22.914  -9.508  1.00 21.38           O  
ATOM   3244  CB  VAL A 424      50.326  21.354  -7.561  1.00 23.84           C  
ATOM   3245  CG1 VAL A 424      49.992  19.955  -8.046  1.00 20.01           C  
ATOM   3246  CG2 VAL A 424      51.573  21.215  -6.701  1.00 20.40           C  
ATOM   3247  N   LEU A 425      49.800  21.871 -10.935  1.00 18.66           N  
ATOM   3248  CA  LEU A 425      48.907  21.890 -12.076  1.00 19.05           C  
ATOM   3249  C   LEU A 425      48.229  20.547 -12.306  1.00 17.68           C  
ATOM   3250  O   LEU A 425      47.148  20.493 -12.891  1.00 18.75           O  
ATOM   3251  CB  LEU A 425      49.709  22.286 -13.315  1.00 22.10           C  
ATOM   3252  CG  LEU A 425      49.786  23.694 -13.897  1.00 19.64           C  
ATOM   3253  CD1 LEU A 425      49.850  24.755 -12.838  1.00 19.94           C  
ATOM   3254  CD2 LEU A 425      51.000  23.713 -14.804  1.00 19.87           C  
ATOM   3255  N   GLY A 426      48.841  19.444 -11.900  1.00 16.34           N  
ATOM   3256  CA  GLY A 426      48.216  18.153 -12.040  1.00 16.22           C  
ATOM   3257  C   GLY A 426      48.939  17.154 -11.168  1.00 15.04           C  
ATOM   3258  O   GLY A 426      50.143  17.321 -10.926  1.00 15.63           O  
ATOM   3259  N   VAL A 427      48.188  16.159 -10.677  1.00 12.79           N  
ATOM   3260  CA  VAL A 427      48.713  15.054  -9.893  1.00 10.34           C  
ATOM   3261  C   VAL A 427      48.089  13.799 -10.505  1.00  9.71           C  
ATOM   3262  O   VAL A 427      46.887  13.751 -10.784  1.00 15.15           O  
ATOM   3263  CB  VAL A 427      48.320  15.214  -8.409  1.00 11.15           C  
ATOM   3264  CG1 VAL A 427      48.906  14.053  -7.619  1.00  6.88           C  
ATOM   3265  CG2 VAL A 427      48.910  16.500  -7.822  1.00  3.01           C  
ATOM   3266  N   HIS A 428      48.879  12.777 -10.823  1.00 10.32           N  
ATOM   3267  CA  HIS A 428      48.426  11.596 -11.548  1.00 11.07           C  
ATOM   3268  C   HIS A 428      48.972  10.383 -10.809  1.00 12.48           C  
ATOM   3269  O   HIS A 428      50.183  10.315 -10.579  1.00 14.62           O  
ATOM   3270  CB  HIS A 428      48.966  11.666 -13.008  1.00  6.11           C  
ATOM   3271  CG  HIS A 428      48.580  12.983 -13.688  1.00 10.79           C  
ATOM   3272  ND1 HIS A 428      47.374  13.390 -14.078  1.00 13.16           N  
ATOM   3273  CD2 HIS A 428      49.428  14.048 -13.882  1.00  8.04           C  
ATOM   3274  CE1 HIS A 428      47.431  14.638 -14.471  1.00 11.66           C  
ATOM   3275  NE2 HIS A 428      48.684  15.018 -14.348  1.00 12.50           N  
ATOM   3276  N   LEU A 429      48.140   9.423 -10.426  1.00 13.34           N  
ATOM   3277  CA  LEU A 429      48.584   8.294  -9.629  1.00 10.78           C  
ATOM   3278  C   LEU A 429      48.117   6.976 -10.197  1.00  8.01           C  
ATOM   3279  O   LEU A 429      46.965   6.857 -10.610  1.00 11.32           O  
ATOM   3280  CB  LEU A 429      48.038   8.382  -8.205  1.00 14.26           C  
ATOM   3281  CG  LEU A 429      48.111   9.674  -7.415  1.00 15.52           C  
ATOM   3282  CD1 LEU A 429      47.169   9.581  -6.241  1.00 11.08           C  
ATOM   3283  CD2 LEU A 429      49.519   9.930  -6.943  1.00 13.61           C  
ATOM   3284  N   LEU A 430      48.969   5.969 -10.207  1.00  7.92           N  
ATOM   3285  CA  LEU A 430      48.576   4.628 -10.599  1.00 10.45           C  
ATOM   3286  C   LEU A 430      48.940   3.742  -9.415  1.00 10.48           C  
ATOM   3287  O   LEU A 430      50.064   3.834  -8.914  1.00 10.64           O  
ATOM   3288  CB  LEU A 430      49.345   4.147 -11.848  1.00  6.48           C  
ATOM   3289  CG  LEU A 430      49.263   2.666 -12.266  1.00 13.00           C  
ATOM   3290  CD1 LEU A 430      47.850   2.261 -12.652  1.00 10.85           C  
ATOM   3291  CD2 LEU A 430      50.125   2.464 -13.476  1.00 19.24           C  
ATOM   3292  N   GLY A 431      48.037   2.894  -8.932  1.00  9.34           N  
ATOM   3293  CA  GLY A 431      48.367   1.953  -7.889  1.00 10.50           C  
ATOM   3294  C   GLY A 431      47.203   1.774  -6.951  1.00 14.36           C  
ATOM   3295  O   GLY A 431      46.185   2.474  -7.037  1.00 15.02           O  
ATOM   3296  N   ASP A 432      47.317   0.803  -6.046  1.00 14.19           N  
ATOM   3297  CA  ASP A 432      46.237   0.531  -5.116  1.00 14.78           C  
ATOM   3298  C   ASP A 432      45.779   1.739  -4.324  1.00 14.23           C  
ATOM   3299  O   ASP A 432      46.573   2.545  -3.859  1.00 17.15           O  
ATOM   3300  CB  ASP A 432      46.660  -0.555  -4.140  1.00 20.76           C  
ATOM   3301  CG  ASP A 432      46.844  -1.894  -4.794  1.00 31.91           C  
ATOM   3302  OD1 ASP A 432      46.159  -2.115  -5.765  1.00 38.28           O  
ATOM   3303  OD2 ASP A 432      47.656  -2.684  -4.340  1.00 36.83           O  
ATOM   3304  N   ASN A 433      44.466   1.898  -4.266  1.00 13.88           N  
ATOM   3305  CA  ASN A 433      43.822   2.981  -3.536  1.00 15.97           C  
ATOM   3306  C   ASN A 433      44.024   4.334  -4.143  1.00 16.60           C  
ATOM   3307  O   ASN A 433      43.517   5.277  -3.546  1.00 20.16           O  
ATOM   3308  CB  ASN A 433      44.289   3.065  -2.057  1.00 20.58           C  
ATOM   3309  CG  ASN A 433      44.046   1.744  -1.342  1.00 25.54           C  
ATOM   3310  OD1 ASN A 433      42.923   1.327  -1.557  1.00 27.93           O  
ATOM   3311  ND2 ASN A 433      44.924   0.898  -0.811  1.00 18.80           N  
ATOM   3312  N   ALA A 434      44.616   4.502  -5.335  1.00 17.78           N  
ATOM   3313  CA  ALA A 434      44.766   5.824  -5.940  1.00 13.25           C  
ATOM   3314  C   ALA A 434      43.457   6.619  -6.076  1.00 10.71           C  
ATOM   3315  O   ALA A 434      43.534   7.828  -5.843  1.00 14.91           O  
ATOM   3316  CB  ALA A 434      45.413   5.696  -7.325  1.00 11.06           C  
ATOM   3317  N   PRO A 435      42.228   6.109  -6.330  1.00  7.59           N  
ATOM   3318  CA  PRO A 435      40.973   6.841  -6.234  1.00  7.13           C  
ATOM   3319  C   PRO A 435      40.679   7.490  -4.884  1.00 10.20           C  
ATOM   3320  O   PRO A 435      40.082   8.567  -4.811  1.00 10.48           O  
ATOM   3321  CB  PRO A 435      39.916   5.834  -6.602  1.00  3.84           C  
ATOM   3322  CG  PRO A 435      40.638   4.892  -7.492  1.00  7.38           C  
ATOM   3323  CD  PRO A 435      41.941   4.750  -6.766  1.00  5.09           C  
ATOM   3324  N   GLU A 436      41.020   6.820  -3.783  1.00 11.54           N  
ATOM   3325  CA  GLU A 436      40.824   7.355  -2.441  1.00  9.82           C  
ATOM   3326  C   GLU A 436      41.866   8.419  -2.130  1.00 11.62           C  
ATOM   3327  O   GLU A 436      41.562   9.427  -1.492  1.00 14.46           O  
ATOM   3328  CB  GLU A 436      40.928   6.230  -1.417  1.00  9.28           C  
ATOM   3329  CG  GLU A 436      39.834   5.186  -1.517  1.00  5.08           C  
ATOM   3330  CD  GLU A 436      38.414   5.652  -1.231  1.00  5.82           C  
ATOM   3331  OE1 GLU A 436      38.207   6.752  -0.724  1.00 16.17           O  
ATOM   3332  OE2 GLU A 436      37.478   4.902  -1.507  1.00 15.21           O  
ATOM   3333  N   ILE A 437      43.103   8.258  -2.590  1.00 11.16           N  
ATOM   3334  CA  ILE A 437      44.155   9.237  -2.345  1.00 14.00           C  
ATOM   3335  C   ILE A 437      43.855  10.524  -3.118  1.00 16.42           C  
ATOM   3336  O   ILE A 437      44.015  11.628  -2.583  1.00 23.49           O  
ATOM   3337  CB  ILE A 437      45.519   8.618  -2.777  1.00 11.40           C  
ATOM   3338  CG1 ILE A 437      45.828   7.385  -1.931  1.00 11.20           C  
ATOM   3339  CG2 ILE A 437      46.638   9.631  -2.608  1.00 13.78           C  
ATOM   3340  CD1 ILE A 437      46.987   6.530  -2.508  1.00  6.65           C  
ATOM   3341  N   ILE A 438      43.360  10.443  -4.364  1.00 17.76           N  
ATOM   3342  CA  ILE A 438      43.206  11.646  -5.156  1.00 11.66           C  
ATOM   3343  C   ILE A 438      42.120  12.560  -4.627  1.00 14.32           C  
ATOM   3344  O   ILE A 438      42.205  13.768  -4.889  1.00 19.28           O  
ATOM   3345  CB  ILE A 438      42.959  11.263  -6.663  1.00 12.83           C  
ATOM   3346  CG1 ILE A 438      43.368  12.460  -7.519  1.00  6.63           C  
ATOM   3347  CG2 ILE A 438      41.505  10.929  -6.982  1.00  7.27           C  
ATOM   3348  CD1 ILE A 438      44.889  12.631  -7.661  1.00  3.00           C  
ATOM   3349  N   GLN A 439      41.145  12.141  -3.815  1.00 12.04           N  
ATOM   3350  CA  GLN A 439      40.127  13.090  -3.395  1.00 13.31           C  
ATOM   3351  C   GLN A 439      40.692  14.261  -2.600  1.00 14.42           C  
ATOM   3352  O   GLN A 439      40.368  15.407  -2.923  1.00 16.09           O  
ATOM   3353  CB  GLN A 439      39.070  12.395  -2.569  1.00  8.52           C  
ATOM   3354  CG  GLN A 439      37.966  13.350  -2.135  1.00 12.90           C  
ATOM   3355  CD  GLN A 439      37.092  13.834  -3.272  1.00 13.82           C  
ATOM   3356  OE1 GLN A 439      36.160  13.136  -3.641  1.00 15.62           O  
ATOM   3357  NE2 GLN A 439      37.309  14.980  -3.888  1.00 17.32           N  
ATOM   3358  N   GLY A 440      41.601  14.035  -1.645  1.00 14.90           N  
ATOM   3359  CA  GLY A 440      42.146  15.102  -0.818  1.00 11.77           C  
ATOM   3360  C   GLY A 440      42.998  16.022  -1.655  1.00 13.94           C  
ATOM   3361  O   GLY A 440      43.016  17.229  -1.430  1.00 17.07           O  
ATOM   3362  N   ILE A 441      43.678  15.464  -2.668  1.00 17.44           N  
ATOM   3363  CA  ILE A 441      44.497  16.227  -3.601  1.00 13.40           C  
ATOM   3364  C   ILE A 441      43.603  17.140  -4.424  1.00 15.59           C  
ATOM   3365  O   ILE A 441      43.975  18.282  -4.689  1.00 18.10           O  
ATOM   3366  CB  ILE A 441      45.279  15.258  -4.506  1.00 17.73           C  
ATOM   3367  CG1 ILE A 441      46.201  14.374  -3.676  1.00 16.61           C  
ATOM   3368  CG2 ILE A 441      46.106  16.052  -5.498  1.00 17.97           C  
ATOM   3369  CD1 ILE A 441      47.145  15.142  -2.721  1.00 15.33           C  
ATOM   3370  N   GLY A 442      42.399  16.708  -4.793  1.00 16.41           N  
ATOM   3371  CA  GLY A 442      41.462  17.564  -5.488  1.00 16.65           C  
ATOM   3372  C   GLY A 442      41.175  18.827  -4.689  1.00 19.04           C  
ATOM   3373  O   GLY A 442      41.123  19.925  -5.257  1.00 19.26           O  
ATOM   3374  N   ILE A 443      41.007  18.734  -3.357  1.00 20.98           N  
ATOM   3375  CA  ILE A 443      40.779  19.909  -2.509  1.00 16.22           C  
ATOM   3376  C   ILE A 443      42.045  20.762  -2.545  1.00 16.25           C  
ATOM   3377  O   ILE A 443      41.970  21.980  -2.659  1.00 19.96           O  
ATOM   3378  CB  ILE A 443      40.464  19.499  -1.037  1.00 19.72           C  
ATOM   3379  CG1 ILE A 443      39.321  18.479  -0.942  1.00 13.49           C  
ATOM   3380  CG2 ILE A 443      40.044  20.758  -0.274  1.00 12.55           C  
ATOM   3381  CD1 ILE A 443      39.129  17.903   0.472  1.00 12.63           C  
ATOM   3382  N   CYS A 444      43.244  20.195  -2.545  1.00 16.83           N  
ATOM   3383  CA  CYS A 444      44.455  20.990  -2.580  1.00 17.36           C  
ATOM   3384  C   CYS A 444      44.568  21.810  -3.858  1.00 21.45           C  
ATOM   3385  O   CYS A 444      44.969  22.984  -3.778  1.00 21.13           O  
ATOM   3386  CB  CYS A 444      45.685  20.103  -2.466  1.00 15.86           C  
ATOM   3387  SG  CYS A 444      45.889  19.349  -0.845  1.00 20.26           S  
ATOM   3388  N   LEU A 445      44.202  21.276  -5.041  1.00 22.88           N  
ATOM   3389  CA  LEU A 445      44.314  22.022  -6.287  1.00 20.62           C  
ATOM   3390  C   LEU A 445      43.309  23.144  -6.295  1.00 21.86           C  
ATOM   3391  O   LEU A 445      43.630  24.255  -6.708  1.00 21.73           O  
ATOM   3392  CB  LEU A 445      44.084  21.135  -7.503  1.00 19.98           C  
ATOM   3393  CG  LEU A 445      45.105  20.043  -7.834  1.00 22.73           C  
ATOM   3394  CD1 LEU A 445      45.388  20.140  -9.313  1.00 21.10           C  
ATOM   3395  CD2 LEU A 445      46.424  20.209  -7.100  1.00 18.56           C  
ATOM   3396  N   LYS A 446      42.130  22.915  -5.736  1.00 23.01           N  
ATOM   3397  CA  LYS A 446      41.161  23.978  -5.581  1.00 22.84           C  
ATOM   3398  C   LYS A 446      41.702  25.052  -4.648  1.00 24.67           C  
ATOM   3399  O   LYS A 446      41.373  26.225  -4.779  1.00 25.39           O  
ATOM   3400  CB  LYS A 446      39.898  23.378  -5.040  1.00 25.89           C  
ATOM   3401  CG  LYS A 446      38.916  23.079  -6.157  1.00 42.02           C  
ATOM   3402  CD  LYS A 446      38.048  24.309  -6.419  1.00 44.90           C  
ATOM   3403  CE  LYS A 446      36.854  24.480  -5.445  1.00 58.62           C  
ATOM   3404  NZ  LYS A 446      37.154  24.359  -4.019  1.00 51.39           N  
ATOM   3405  N   LEU A 447      42.572  24.697  -3.707  1.00 26.96           N  
ATOM   3406  CA  LEU A 447      43.188  25.673  -2.830  1.00 27.61           C  
ATOM   3407  C   LEU A 447      44.398  26.349  -3.448  1.00 28.92           C  
ATOM   3408  O   LEU A 447      44.956  27.261  -2.845  1.00 32.02           O  
ATOM   3409  CB  LEU A 447      43.607  25.007  -1.521  1.00 27.15           C  
ATOM   3410  CG  LEU A 447      42.484  24.524  -0.599  1.00 26.06           C  
ATOM   3411  CD1 LEU A 447      43.046  23.894   0.649  1.00 22.55           C  
ATOM   3412  CD2 LEU A 447      41.655  25.692  -0.182  1.00 19.71           C  
ATOM   3413  N   ASN A 448      44.818  25.976  -4.659  1.00 30.17           N  
ATOM   3414  CA  ASN A 448      45.998  26.517  -5.339  1.00 31.59           C  
ATOM   3415  C   ASN A 448      47.281  26.253  -4.570  1.00 29.88           C  
ATOM   3416  O   ASN A 448      48.138  27.099  -4.320  1.00 33.92           O  
ATOM   3417  CB  ASN A 448      45.850  28.028  -5.583  1.00 30.52           C  
ATOM   3418  CG  ASN A 448      44.731  28.292  -6.567  1.00 35.29           C  
ATOM   3419  OD1 ASN A 448      44.778  27.867  -7.723  1.00 44.71           O  
ATOM   3420  ND2 ASN A 448      43.682  28.981  -6.152  1.00 35.12           N  
ATOM   3421  N   ALA A 449      47.401  24.984  -4.190  1.00 29.15           N  
ATOM   3422  CA  ALA A 449      48.551  24.537  -3.448  1.00 23.75           C  
ATOM   3423  C   ALA A 449      49.790  24.585  -4.321  1.00 24.83           C  
ATOM   3424  O   ALA A 449      49.724  24.466  -5.545  1.00 24.44           O  
ATOM   3425  CB  ALA A 449      48.349  23.112  -2.982  1.00 23.41           C  
ATOM   3426  N   LYS A 450      50.940  24.775  -3.679  1.00 23.30           N  
ATOM   3427  CA  LYS A 450      52.218  24.777  -4.373  1.00 22.58           C  
ATOM   3428  C   LYS A 450      52.950  23.513  -3.998  1.00 22.31           C  
ATOM   3429  O   LYS A 450      52.642  22.922  -2.957  1.00 25.28           O  
ATOM   3430  CB  LYS A 450      53.071  25.968  -3.962  1.00 22.43           C  
ATOM   3431  CG  LYS A 450      52.277  27.230  -4.178  1.00 28.00           C  
ATOM   3432  CD  LYS A 450      53.035  28.529  -4.018  1.00 43.86           C  
ATOM   3433  CE  LYS A 450      52.004  29.668  -4.105  1.00 51.06           C  
ATOM   3434  NZ  LYS A 450      51.324  29.725  -5.393  1.00 61.49           N  
ATOM   3435  N   ILE A 451      53.962  23.108  -4.767  1.00 21.65           N  
ATOM   3436  CA  ILE A 451      54.749  21.926  -4.457  1.00 21.94           C  
ATOM   3437  C   ILE A 451      55.383  22.032  -3.071  1.00 23.21           C  
ATOM   3438  O   ILE A 451      55.491  21.019  -2.374  1.00 21.50           O  
ATOM   3439  CB  ILE A 451      55.822  21.726  -5.576  1.00 21.01           C  
ATOM   3440  CG1 ILE A 451      56.574  20.431  -5.312  1.00 22.07           C  
ATOM   3441  CG2 ILE A 451      56.792  22.893  -5.646  1.00 24.05           C  
ATOM   3442  CD1 ILE A 451      55.684  19.203  -5.540  1.00 24.85           C  
ATOM   3443  N   SER A 452      55.728  23.231  -2.587  1.00 23.16           N  
ATOM   3444  CA  SER A 452      56.284  23.330  -1.250  1.00 26.47           C  
ATOM   3445  C   SER A 452      55.267  22.986  -0.169  1.00 26.31           C  
ATOM   3446  O   SER A 452      55.630  22.412   0.860  1.00 30.04           O  
ATOM   3447  CB  SER A 452      56.855  24.738  -0.996  1.00 21.22           C  
ATOM   3448  OG  SER A 452      55.994  25.821  -1.315  1.00 30.22           O  
ATOM   3449  N   ASP A 453      53.981  23.262  -0.407  1.00 25.22           N  
ATOM   3450  CA  ASP A 453      52.938  22.923   0.541  1.00 22.31           C  
ATOM   3451  C   ASP A 453      52.770  21.406   0.592  1.00 21.88           C  
ATOM   3452  O   ASP A 453      52.352  20.860   1.607  1.00 22.90           O  
ATOM   3453  CB  ASP A 453      51.640  23.575   0.122  1.00 19.72           C  
ATOM   3454  CG  ASP A 453      51.674  25.092   0.051  1.00 23.27           C  
ATOM   3455  OD1 ASP A 453      52.236  25.753   0.923  1.00 39.32           O  
ATOM   3456  OD2 ASP A 453      51.103  25.625  -0.889  1.00 33.71           O  
ATOM   3457  N   PHE A 454      53.082  20.679  -0.480  1.00 20.49           N  
ATOM   3458  CA  PHE A 454      53.047  19.238  -0.434  1.00 17.47           C  
ATOM   3459  C   PHE A 454      54.264  18.805   0.356  1.00 22.17           C  
ATOM   3460  O   PHE A 454      54.078  18.199   1.408  1.00 24.08           O  
ATOM   3461  CB  PHE A 454      53.128  18.600  -1.817  1.00 20.30           C  
ATOM   3462  CG  PHE A 454      51.825  18.550  -2.609  1.00 17.05           C  
ATOM   3463  CD1 PHE A 454      50.959  19.645  -2.660  1.00 16.27           C  
ATOM   3464  CD2 PHE A 454      51.492  17.378  -3.292  1.00 20.11           C  
ATOM   3465  CE1 PHE A 454      49.768  19.560  -3.390  1.00 23.28           C  
ATOM   3466  CE2 PHE A 454      50.301  17.301  -4.019  1.00 18.58           C  
ATOM   3467  CZ  PHE A 454      49.434  18.391  -4.071  1.00 18.54           C  
ATOM   3468  N   TYR A 455      55.520  19.137   0.020  1.00 23.83           N  
ATOM   3469  CA  TYR A 455      56.600  18.547   0.789  1.00 27.72           C  
ATOM   3470  C   TYR A 455      56.869  19.081   2.185  1.00 26.47           C  
ATOM   3471  O   TYR A 455      57.651  18.490   2.935  1.00 27.71           O  
ATOM   3472  CB  TYR A 455      57.909  18.562  -0.038  1.00 30.77           C  
ATOM   3473  CG  TYR A 455      58.483  19.843  -0.624  1.00 35.54           C  
ATOM   3474  CD1 TYR A 455      58.957  20.870   0.196  1.00 33.12           C  
ATOM   3475  CD2 TYR A 455      58.583  19.953  -2.012  1.00 36.15           C  
ATOM   3476  CE1 TYR A 455      59.533  22.002  -0.368  1.00 32.78           C  
ATOM   3477  CE2 TYR A 455      59.161  21.083  -2.581  1.00 32.77           C  
ATOM   3478  CZ  TYR A 455      59.629  22.098  -1.753  1.00 37.53           C  
ATOM   3479  OH  TYR A 455      60.176  23.241  -2.310  1.00 49.94           O  
ATOM   3480  N   ASN A 456      56.194  20.161   2.557  1.00 23.84           N  
ATOM   3481  CA  ASN A 456      56.256  20.636   3.928  1.00 25.18           C  
ATOM   3482  C   ASN A 456      55.176  20.008   4.800  1.00 27.46           C  
ATOM   3483  O   ASN A 456      55.041  20.393   5.966  1.00 34.20           O  
ATOM   3484  CB  ASN A 456      56.081  22.137   4.016  1.00 23.30           C  
ATOM   3485  CG  ASN A 456      57.296  22.906   3.535  1.00 29.88           C  
ATOM   3486  OD1 ASN A 456      58.425  22.430   3.471  1.00 32.84           O  
ATOM   3487  ND2 ASN A 456      57.112  24.165   3.155  1.00 35.01           N  
ATOM   3488  N   THR A 457      54.311  19.127   4.287  1.00 25.86           N  
ATOM   3489  CA  THR A 457      53.367  18.396   5.106  1.00 19.30           C  
ATOM   3490  C   THR A 457      54.069  17.132   5.597  1.00 21.61           C  
ATOM   3491  O   THR A 457      54.817  16.473   4.866  1.00 24.43           O  
ATOM   3492  CB  THR A 457      52.128  18.081   4.245  1.00 16.73           C  
ATOM   3493  OG1 THR A 457      51.492  19.336   4.054  1.00 15.07           O  
ATOM   3494  CG2 THR A 457      51.114  17.129   4.885  1.00 11.11           C  
ATOM   3495  N   ILE A 458      53.872  16.744   6.855  1.00 21.23           N  
ATOM   3496  CA  ILE A 458      54.477  15.523   7.349  1.00 20.61           C  
ATOM   3497  C   ILE A 458      53.593  14.369   6.885  1.00 19.77           C  
ATOM   3498  O   ILE A 458      52.359  14.455   6.840  1.00 21.50           O  
ATOM   3499  CB  ILE A 458      54.579  15.701   8.874  1.00 26.26           C  
ATOM   3500  CG1 ILE A 458      55.717  16.686   9.135  1.00 29.78           C  
ATOM   3501  CG2 ILE A 458      54.832  14.389   9.590  1.00 21.33           C  
ATOM   3502  CD1 ILE A 458      55.717  17.308  10.549  1.00 31.57           C  
ATOM   3503  N   GLY A 459      54.265  13.320   6.444  1.00 17.72           N  
ATOM   3504  CA  GLY A 459      53.583  12.167   5.919  1.00 17.70           C  
ATOM   3505  C   GLY A 459      53.032  11.267   6.997  1.00 18.57           C  
ATOM   3506  O   GLY A 459      53.454  11.310   8.148  1.00 22.23           O  
ATOM   3507  N   VAL A 460      52.077  10.460   6.573  1.00 14.68           N  
ATOM   3508  CA  VAL A 460      51.465   9.446   7.398  1.00 15.52           C  
ATOM   3509  C   VAL A 460      52.265   8.208   6.999  1.00 18.22           C  
ATOM   3510  O   VAL A 460      52.271   7.805   5.838  1.00 19.24           O  
ATOM   3511  CB  VAL A 460      49.965   9.282   7.039  1.00 14.80           C  
ATOM   3512  CG1 VAL A 460      49.267   8.282   7.953  1.00 13.42           C  
ATOM   3513  CG2 VAL A 460      49.278  10.606   7.221  1.00 14.02           C  
ATOM   3514  N   HIS A 461      53.016   7.578   7.892  1.00 17.72           N  
ATOM   3515  CA  HIS A 461      53.837   6.428   7.564  1.00 20.35           C  
ATOM   3516  C   HIS A 461      53.276   5.142   8.185  1.00 20.13           C  
ATOM   3517  O   HIS A 461      52.909   5.184   9.359  1.00 23.82           O  
ATOM   3518  CB  HIS A 461      55.247   6.746   8.065  1.00 17.30           C  
ATOM   3519  CG  HIS A 461      56.323   5.762   7.626  1.00 22.34           C  
ATOM   3520  ND1 HIS A 461      56.704   5.427   6.400  1.00 25.35           N  
ATOM   3521  CD2 HIS A 461      57.068   5.008   8.491  1.00 19.79           C  
ATOM   3522  CE1 HIS A 461      57.631   4.506   6.479  1.00 17.85           C  
ATOM   3523  NE2 HIS A 461      57.833   4.268   7.738  1.00 23.10           N  
ATOM   3524  N   PRO A 462      53.226   3.966   7.552  1.00 17.61           N  
ATOM   3525  CA  PRO A 462      53.567   3.707   6.156  1.00 18.50           C  
ATOM   3526  C   PRO A 462      52.387   3.746   5.193  1.00 18.26           C  
ATOM   3527  O   PRO A 462      51.471   2.928   5.344  1.00 17.41           O  
ATOM   3528  CB  PRO A 462      54.245   2.350   6.209  1.00 18.24           C  
ATOM   3529  CG  PRO A 462      54.222   1.950   7.675  1.00 14.32           C  
ATOM   3530  CD  PRO A 462      53.030   2.695   8.218  1.00  9.93           C  
ATOM   3531  N   THR A 463      52.321   4.681   4.244  1.00 18.52           N  
ATOM   3532  CA  THR A 463      51.270   4.632   3.236  1.00 13.99           C  
ATOM   3533  C   THR A 463      51.891   4.879   1.876  1.00 15.43           C  
ATOM   3534  O   THR A 463      53.059   5.250   1.765  1.00 19.34           O  
ATOM   3535  CB  THR A 463      50.189   5.697   3.535  1.00 13.55           C  
ATOM   3536  OG1 THR A 463      50.808   6.959   3.387  1.00 12.09           O  
ATOM   3537  CG2 THR A 463      49.580   5.549   4.915  1.00 19.10           C  
ATOM   3538  N   SER A 464      51.116   4.659   0.812  1.00 15.99           N  
ATOM   3539  CA  SER A 464      51.554   5.046  -0.514  1.00 15.29           C  
ATOM   3540  C   SER A 464      51.412   6.550  -0.646  1.00 12.12           C  
ATOM   3541  O   SER A 464      52.299   7.227  -1.144  1.00 17.19           O  
ATOM   3542  CB  SER A 464      50.700   4.331  -1.556  1.00 15.93           C  
ATOM   3543  OG  SER A 464      51.099   2.971  -1.560  1.00 18.08           O  
ATOM   3544  N   ALA A 465      50.334   7.127  -0.117  1.00 11.61           N  
ATOM   3545  CA  ALA A 465      50.100   8.554  -0.251  1.00 10.87           C  
ATOM   3546  C   ALA A 465      51.197   9.443   0.307  1.00 11.46           C  
ATOM   3547  O   ALA A 465      51.422  10.511  -0.254  1.00 14.60           O  
ATOM   3548  CB  ALA A 465      48.781   8.927   0.430  1.00  5.47           C  
ATOM   3549  N   GLU A 466      51.970   9.060   1.323  1.00 14.06           N  
ATOM   3550  CA  GLU A 466      52.982   9.963   1.859  1.00 16.21           C  
ATOM   3551  C   GLU A 466      54.082  10.271   0.852  1.00 18.50           C  
ATOM   3552  O   GLU A 466      54.788  11.268   0.984  1.00 21.08           O  
ATOM   3553  CB  GLU A 466      53.586   9.369   3.125  1.00 14.50           C  
ATOM   3554  CG  GLU A 466      54.380   8.108   2.890  1.00 17.26           C  
ATOM   3555  CD  GLU A 466      55.074   7.541   4.110  1.00 21.34           C  
ATOM   3556  OE1 GLU A 466      55.590   8.298   4.932  1.00 25.64           O  
ATOM   3557  OE2 GLU A 466      55.105   6.324   4.218  1.00 20.23           O  
ATOM   3558  N   GLU A 467      54.208   9.471  -0.207  1.00 19.26           N  
ATOM   3559  CA  GLU A 467      55.150   9.722  -1.278  1.00 20.80           C  
ATOM   3560  C   GLU A 467      54.870  11.078  -1.897  1.00 19.76           C  
ATOM   3561  O   GLU A 467      55.810  11.767  -2.281  1.00 19.68           O  
ATOM   3562  CB  GLU A 467      55.018   8.655  -2.342  1.00 28.45           C  
ATOM   3563  CG  GLU A 467      56.239   8.546  -3.230  1.00 35.54           C  
ATOM   3564  CD  GLU A 467      57.497   8.192  -2.454  1.00 42.12           C  
ATOM   3565  OE1 GLU A 467      57.441   7.383  -1.515  1.00 50.43           O  
ATOM   3566  OE2 GLU A 467      58.537   8.752  -2.791  1.00 45.56           O  
ATOM   3567  N   LEU A 468      53.618  11.525  -1.957  1.00 18.33           N  
ATOM   3568  CA  LEU A 468      53.299  12.844  -2.484  1.00 20.19           C  
ATOM   3569  C   LEU A 468      53.892  13.975  -1.657  1.00 21.42           C  
ATOM   3570  O   LEU A 468      53.991  15.094  -2.141  1.00 25.31           O  
ATOM   3571  CB  LEU A 468      51.770  12.995  -2.571  1.00 20.32           C  
ATOM   3572  CG  LEU A 468      51.009  12.138  -3.606  1.00 19.74           C  
ATOM   3573  CD1 LEU A 468      49.527  12.266  -3.362  1.00 22.72           C  
ATOM   3574  CD2 LEU A 468      51.307  12.614  -5.031  1.00 17.64           C  
ATOM   3575  N   CYS A 469      54.298  13.702  -0.425  1.00 22.90           N  
ATOM   3576  CA  CYS A 469      54.929  14.685   0.436  1.00 22.61           C  
ATOM   3577  C   CYS A 469      56.439  14.525   0.413  1.00 21.07           C  
ATOM   3578  O   CYS A 469      57.147  15.281   1.073  1.00 23.33           O  
ATOM   3579  CB  CYS A 469      54.385  14.524   1.863  1.00 22.82           C  
ATOM   3580  SG  CYS A 469      52.581  14.749   1.862  1.00 27.03           S  
ATOM   3581  N   SER A 470      56.996  13.621  -0.392  1.00 23.48           N  
ATOM   3582  CA  SER A 470      58.436  13.397  -0.433  1.00 28.15           C  
ATOM   3583  C   SER A 470      59.103  13.887  -1.714  1.00 28.50           C  
ATOM   3584  O   SER A 470      60.301  13.682  -1.911  1.00 31.30           O  
ATOM   3585  CB  SER A 470      58.708  11.911  -0.275  1.00 24.11           C  
ATOM   3586  OG  SER A 470      57.844  11.306   0.686  1.00 44.77           O  
ATOM   3587  N   MET A 471      58.384  14.561  -2.616  1.00 30.38           N  
ATOM   3588  CA  MET A 471      58.915  14.978  -3.907  1.00 29.49           C  
ATOM   3589  C   MET A 471      59.377  16.436  -3.929  1.00 31.19           C  
ATOM   3590  O   MET A 471      58.590  17.366  -4.105  1.00 32.68           O  
ATOM   3591  CB  MET A 471      57.824  14.705  -4.933  1.00 28.10           C  
ATOM   3592  CG  MET A 471      57.739  13.219  -5.217  1.00 21.72           C  
ATOM   3593  SD  MET A 471      56.616  12.853  -6.581  1.00 39.21           S  
ATOM   3594  CE  MET A 471      55.386  12.052  -5.636  1.00 13.92           C  
ATOM   3595  N   ARG A 472      60.674  16.658  -3.731  1.00 31.94           N  
ATOM   3596  CA  ARG A 472      61.261  17.992  -3.632  1.00 34.00           C  
ATOM   3597  C   ARG A 472      61.973  18.480  -4.875  1.00 32.32           C  
ATOM   3598  O   ARG A 472      62.101  19.683  -5.066  1.00 34.93           O  
ATOM   3599  CB  ARG A 472      62.249  18.019  -2.459  1.00 32.78           C  
ATOM   3600  CG  ARG A 472      61.524  17.902  -1.128  1.00 47.26           C  
ATOM   3601  CD  ARG A 472      62.383  17.513   0.070  1.00 50.98           C  
ATOM   3602  NE  ARG A 472      61.782  16.365   0.748  1.00 66.97           N  
ATOM   3603  CZ  ARG A 472      60.810  16.465   1.674  1.00 70.09           C  
ATOM   3604  NH1 ARG A 472      60.312  17.642   2.061  1.00 71.60           N  
ATOM   3605  NH2 ARG A 472      60.303  15.352   2.212  1.00 74.76           N  
ATOM   3606  N   THR A 473      62.429  17.572  -5.725  1.00 35.91           N  
ATOM   3607  CA  THR A 473      63.253  17.911  -6.878  1.00 36.57           C  
ATOM   3608  C   THR A 473      62.621  17.425  -8.181  1.00 33.34           C  
ATOM   3609  O   THR A 473      62.269  16.239  -8.250  1.00 32.96           O  
ATOM   3610  CB  THR A 473      64.633  17.272  -6.598  1.00 38.86           C  
ATOM   3611  OG1 THR A 473      65.119  18.017  -5.488  1.00 38.69           O  
ATOM   3612  CG2 THR A 473      65.633  17.291  -7.744  1.00 34.90           C  
ATOM   3613  N   PRO A 474      62.442  18.280  -9.209  1.00 30.35           N  
ATOM   3614  CA  PRO A 474      61.937  17.881 -10.520  1.00 25.20           C  
ATOM   3615  C   PRO A 474      62.788  16.795 -11.161  1.00 25.53           C  
ATOM   3616  O   PRO A 474      63.990  16.737 -10.899  1.00 26.07           O  
ATOM   3617  CB  PRO A 474      61.923  19.161 -11.311  1.00 22.70           C  
ATOM   3618  CG  PRO A 474      61.882  20.260 -10.277  1.00 20.02           C  
ATOM   3619  CD  PRO A 474      62.794  19.702  -9.199  1.00 24.24           C  
ATOM   3620  N   SER A 475      62.184  15.878 -11.913  1.00 24.75           N  
ATOM   3621  CA  SER A 475      62.935  14.909 -12.685  1.00 27.89           C  
ATOM   3622  C   SER A 475      63.396  15.597 -13.974  1.00 27.47           C  
ATOM   3623  O   SER A 475      64.510  15.383 -14.445  1.00 30.72           O  
ATOM   3624  CB  SER A 475      62.066  13.721 -13.056  1.00 30.48           C  
ATOM   3625  OG  SER A 475      61.235  13.271 -11.992  1.00 42.95           O  
ATOM   3626  N   TYR A 476      62.524  16.386 -14.594  1.00 25.82           N  
ATOM   3627  CA  TYR A 476      62.855  17.099 -15.812  1.00 26.02           C  
ATOM   3628  C   TYR A 476      61.926  18.279 -15.919  1.00 26.39           C  
ATOM   3629  O   TYR A 476      61.150  18.532 -14.988  1.00 27.76           O  
ATOM   3630  CB  TYR A 476      62.714  16.198 -17.066  1.00 25.11           C  
ATOM   3631  CG  TYR A 476      61.393  15.493 -17.289  1.00 23.10           C  
ATOM   3632  CD1 TYR A 476      60.363  16.124 -17.984  1.00 21.93           C  
ATOM   3633  CD2 TYR A 476      61.234  14.190 -16.814  1.00 28.55           C  
ATOM   3634  CE1 TYR A 476      59.170  15.438 -18.206  1.00 23.38           C  
ATOM   3635  CE2 TYR A 476      60.042  13.502 -17.033  1.00 29.01           C  
ATOM   3636  CZ  TYR A 476      59.018  14.135 -17.732  1.00 25.82           C  
ATOM   3637  OH  TYR A 476      57.842  13.451 -17.964  1.00 30.94           O  
ATOM   3638  N   TYR A 477      62.034  19.010 -17.017  1.00 27.04           N  
ATOM   3639  CA  TYR A 477      61.284  20.224 -17.218  1.00 24.36           C  
ATOM   3640  C   TYR A 477      60.850  20.310 -18.666  1.00 26.09           C  
ATOM   3641  O   TYR A 477      61.347  19.570 -19.517  1.00 24.83           O  
ATOM   3642  CB  TYR A 477      62.136  21.433 -16.941  1.00 27.95           C  
ATOM   3643  CG  TYR A 477      62.793  21.490 -15.581  1.00 22.89           C  
ATOM   3644  CD1 TYR A 477      63.965  20.769 -15.325  1.00 25.03           C  
ATOM   3645  CD2 TYR A 477      62.222  22.302 -14.607  1.00 25.96           C  
ATOM   3646  CE1 TYR A 477      64.577  20.863 -14.077  1.00 26.37           C  
ATOM   3647  CE2 TYR A 477      62.830  22.401 -13.366  1.00 22.38           C  
ATOM   3648  CZ  TYR A 477      63.997  21.689 -13.116  1.00 21.50           C  
ATOM   3649  OH  TYR A 477      64.592  21.857 -11.890  1.00 36.06           O  
ATOM   3650  N   TYR A 478      59.925  21.225 -18.923  1.00 26.94           N  
ATOM   3651  CA  TYR A 478      59.450  21.597 -20.240  1.00 30.17           C  
ATOM   3652  C   TYR A 478      59.603  23.104 -20.356  1.00 32.89           C  
ATOM   3653  O   TYR A 478      58.907  23.833 -19.642  1.00 28.98           O  
ATOM   3654  CB  TYR A 478      57.971  21.322 -20.463  1.00 21.13           C  
ATOM   3655  CG  TYR A 478      57.742  19.874 -20.754  1.00 24.85           C  
ATOM   3656  CD1 TYR A 478      58.160  19.379 -21.984  1.00 26.58           C  
ATOM   3657  CD2 TYR A 478      57.188  19.040 -19.788  1.00 22.81           C  
ATOM   3658  CE1 TYR A 478      58.039  18.020 -22.255  1.00 29.28           C  
ATOM   3659  CE2 TYR A 478      57.068  17.683 -20.060  1.00 24.44           C  
ATOM   3660  CZ  TYR A 478      57.498  17.184 -21.288  1.00 25.32           C  
ATOM   3661  OH  TYR A 478      57.410  15.841 -21.563  1.00 34.86           O  
ATOM   3662  N   VAL A 479      60.510  23.604 -21.194  1.00 36.51           N  
ATOM   3663  CA  VAL A 479      60.636  25.047 -21.402  1.00 39.98           C  
ATOM   3664  C   VAL A 479      60.157  25.248 -22.823  1.00 38.92           C  
ATOM   3665  O   VAL A 479      60.706  24.619 -23.736  1.00 38.05           O  
ATOM   3666  CB  VAL A 479      62.093  25.494 -21.265  1.00 42.40           C  
ATOM   3667  CG1 VAL A 479      62.245  26.984 -21.557  1.00 38.04           C  
ATOM   3668  CG2 VAL A 479      62.547  25.186 -19.850  1.00 36.10           C  
ATOM   3669  N   LYS A 480      59.143  26.094 -23.014  1.00 40.21           N  
ATOM   3670  CA  LYS A 480      58.478  26.330 -24.299  1.00 44.73           C  
ATOM   3671  C   LYS A 480      58.218  25.017 -25.058  1.00 44.70           C  
ATOM   3672  O   LYS A 480      58.487  24.876 -26.256  1.00 48.90           O  
ATOM   3673  CB  LYS A 480      59.321  27.280 -25.208  1.00 48.34           C  
ATOM   3674  CG  LYS A 480      59.552  28.778 -24.873  1.00 53.40           C  
ATOM   3675  CD  LYS A 480      58.433  29.852 -25.251  1.00 64.21           C  
ATOM   3676  CE  LYS A 480      57.693  30.722 -26.315  1.00 71.47           C  
ATOM   3677  NZ  LYS A 480      57.277  31.871 -25.496  1.00 73.33           N  
ATOM   3678  N   GLY A 481      57.771  23.985 -24.350  1.00 40.61           N  
ATOM   3679  CA  GLY A 481      57.473  22.727 -24.996  1.00 33.65           C  
ATOM   3680  C   GLY A 481      58.651  21.786 -25.157  1.00 33.54           C  
ATOM   3681  O   GLY A 481      58.421  20.612 -25.460  1.00 36.25           O  
ATOM   3682  N   GLU A 482      59.914  22.136 -24.982  1.00 32.32           N  
ATOM   3683  CA  GLU A 482      60.945  21.121 -25.115  1.00 37.27           C  
ATOM   3684  C   GLU A 482      61.503  20.750 -23.754  1.00 36.65           C  
ATOM   3685  O   GLU A 482      61.641  21.566 -22.839  1.00 37.06           O  
ATOM   3686  CB  GLU A 482      62.039  21.626 -26.055  1.00 40.07           C  
ATOM   3687  CG  GLU A 482      62.559  23.012 -25.725  1.00 57.43           C  
ATOM   3688  CD  GLU A 482      62.998  23.858 -26.916  1.00 57.29           C  
ATOM   3689  OE1 GLU A 482      62.757  23.512 -28.076  1.00 60.91           O  
ATOM   3690  OE2 GLU A 482      63.599  24.890 -26.656  1.00 53.04           O  
ATOM   3691  N   LYS A 483      61.655  19.438 -23.626  1.00 37.09           N  
ATOM   3692  CA  LYS A 483      62.117  18.780 -22.424  1.00 41.48           C  
ATOM   3693  C   LYS A 483      63.564  19.111 -22.121  1.00 45.52           C  
ATOM   3694  O   LYS A 483      64.462  18.866 -22.936  1.00 46.58           O  
ATOM   3695  CB  LYS A 483      61.931  17.278 -22.605  1.00 39.91           C  
ATOM   3696  CG  LYS A 483      62.270  16.415 -21.405  1.00 45.31           C  
ATOM   3697  CD  LYS A 483      61.926  14.960 -21.710  1.00 51.54           C  
ATOM   3698  CE  LYS A 483      62.353  14.057 -20.557  1.00 54.25           C  
ATOM   3699  NZ  LYS A 483      63.797  13.944 -20.468  1.00 58.62           N  
ATOM   3700  N   MET A 484      63.807  19.685 -20.953  1.00 47.98           N  
ATOM   3701  CA  MET A 484      65.156  20.039 -20.561  1.00 47.47           C  
ATOM   3702  C   MET A 484      65.412  19.512 -19.174  1.00 48.10           C  
ATOM   3703  O   MET A 484      64.483  19.250 -18.407  1.00 47.48           O  
ATOM   3704  CB  MET A 484      65.341  21.541 -20.555  1.00 48.02           C  
ATOM   3705  CG  MET A 484      64.988  22.158 -21.889  1.00 49.80           C  
ATOM   3706  SD  MET A 484      66.200  23.385 -22.388  1.00 57.78           S  
ATOM   3707  CE  MET A 484      65.396  24.873 -21.904  1.00 33.70           C  
ATOM   3708  N   GLU A 485      66.679  19.344 -18.838  1.00 50.58           N  
ATOM   3709  CA  GLU A 485      67.104  18.844 -17.540  1.00 53.83           C  
ATOM   3710  C   GLU A 485      68.194  19.736 -16.962  1.00 55.47           C  
ATOM   3711  O   GLU A 485      68.869  20.452 -17.707  1.00 54.64           O  
ATOM   3712  CB  GLU A 485      67.669  17.444 -17.667  1.00 52.72           C  
ATOM   3713  CG  GLU A 485      66.733  16.443 -18.344  1.00 61.34           C  
ATOM   3714  CD  GLU A 485      67.300  15.050 -18.568  1.00 66.92           C  
ATOM   3715  OE1 GLU A 485      68.522  14.906 -18.671  1.00 65.14           O  
ATOM   3716  OE2 GLU A 485      66.506  14.110 -18.653  1.00 73.52           O  
ATOM   3717  N   LYS A 486      68.365  19.731 -15.637  1.00 59.83           N  
ATOM   3718  CA  LYS A 486      69.443  20.447 -14.944  1.00 63.83           C  
ATOM   3719  C   LYS A 486      70.699  19.595 -15.174  1.00 68.67           C  
ATOM   3720  O   LYS A 486      70.492  18.373 -15.218  1.00 69.90           O  
ATOM   3721  CB  LYS A 486      69.077  20.513 -13.477  1.00 57.98           C  
ATOM   3722  CG  LYS A 486      69.585  21.637 -12.593  1.00 60.02           C  
ATOM   3723  CD  LYS A 486      68.429  22.513 -12.076  1.00 57.79           C  
ATOM   3724  CE  LYS A 486      68.970  23.355 -10.908  1.00 66.31           C  
ATOM   3725  NZ  LYS A 486      68.057  24.329 -10.320  1.00 69.22           N  
ATOM   3726  N   PRO A 487      71.903  20.170 -15.438  1.00 72.11           N  
ATOM   3727  CA  PRO A 487      73.200  19.492 -15.635  1.00 74.07           C  
ATOM   3728  C   PRO A 487      73.940  18.942 -14.400  1.00 76.96           C  
ATOM   3729  CB  PRO A 487      74.034  20.527 -16.411  1.00 71.11           C  
ATOM   3730  CG  PRO A 487      73.522  21.827 -15.862  1.00 73.74           C  
ATOM   3731  CD  PRO A 487      72.034  21.541 -15.922  1.00 73.57           C  
TER    3732      PRO A 487                                                      
ATOM   3733  N   ILE B   5      87.909  15.447  15.600  1.00 67.47           N  
ATOM   3734  CA  ILE B   5      87.998  14.407  14.583  1.00 69.27           C  
ATOM   3735  C   ILE B   5      86.664  14.136  13.894  1.00 69.25           C  
ATOM   3736  O   ILE B   5      86.666  13.611  12.789  1.00 71.45           O  
ATOM   3737  CB  ILE B   5      88.540  13.077  15.199  1.00 67.80           C  
ATOM   3738  CG1 ILE B   5      87.633  12.592  16.322  1.00 66.60           C  
ATOM   3739  CG2 ILE B   5      89.985  13.306  15.639  1.00 70.64           C  
ATOM   3740  CD1 ILE B   5      87.964  11.245  16.972  1.00 53.86           C  
ATOM   3741  N   PHE B   6      85.542  14.460  14.527  1.00 66.81           N  
ATOM   3742  CA  PHE B   6      84.226  14.311  13.923  1.00 63.59           C  
ATOM   3743  C   PHE B   6      83.522  15.624  14.145  1.00 64.59           C  
ATOM   3744  O   PHE B   6      83.899  16.371  15.061  1.00 67.50           O  
ATOM   3745  CB  PHE B   6      83.443  13.189  14.593  1.00 58.06           C  
ATOM   3746  CG  PHE B   6      83.696  11.852  13.923  1.00 53.54           C  
ATOM   3747  CD1 PHE B   6      83.389  11.706  12.568  1.00 50.81           C  
ATOM   3748  CD2 PHE B   6      84.234  10.779  14.635  1.00 51.84           C  
ATOM   3749  CE1 PHE B   6      83.627  10.491  11.922  1.00 52.56           C  
ATOM   3750  CE2 PHE B   6      84.468   9.566  13.978  1.00 53.19           C  
ATOM   3751  CZ  PHE B   6      84.164   9.418  12.625  1.00 50.06           C  
ATOM   3752  N   ASP B   7      82.574  15.925  13.268  1.00 64.66           N  
ATOM   3753  CA  ASP B   7      81.798  17.151  13.360  1.00 64.45           C  
ATOM   3754  C   ASP B   7      80.478  16.932  14.071  1.00 60.91           C  
ATOM   3755  O   ASP B   7      79.985  17.811  14.791  1.00 59.14           O  
ATOM   3756  CB  ASP B   7      81.521  17.699  11.968  1.00 70.25           C  
ATOM   3757  CG  ASP B   7      82.781  18.170  11.263  1.00 75.50           C  
ATOM   3758  OD1 ASP B   7      83.477  17.341  10.670  1.00 75.61           O  
ATOM   3759  OD2 ASP B   7      83.053  19.370  11.322  1.00 76.18           O  
ATOM   3760  N   LEU B   8      79.915  15.748  13.851  1.00 57.29           N  
ATOM   3761  CA  LEU B   8      78.658  15.369  14.449  1.00 52.60           C  
ATOM   3762  C   LEU B   8      78.753  13.904  14.810  1.00 49.42           C  
ATOM   3763  O   LEU B   8      79.289  13.086  14.058  1.00 45.06           O  
ATOM   3764  CB  LEU B   8      77.510  15.584  13.457  1.00 55.93           C  
ATOM   3765  CG  LEU B   8      76.084  15.228  13.884  1.00 53.31           C  
ATOM   3766  CD1 LEU B   8      75.595  16.214  14.940  1.00 54.30           C  
ATOM   3767  CD2 LEU B   8      75.174  15.249  12.665  1.00 52.32           C  
ATOM   3768  N   VAL B   9      78.320  13.577  16.012  1.00 49.11           N  
ATOM   3769  CA  VAL B   9      78.183  12.190  16.418  1.00 47.80           C  
ATOM   3770  C   VAL B   9      76.703  12.086  16.740  1.00 46.14           C  
ATOM   3771  O   VAL B   9      76.122  12.964  17.395  1.00 47.68           O  
ATOM   3772  CB  VAL B   9      79.039  11.865  17.667  1.00 46.52           C  
ATOM   3773  CG1 VAL B   9      78.669  10.494  18.219  1.00 40.55           C  
ATOM   3774  CG2 VAL B   9      80.510  11.802  17.276  1.00 40.50           C  
ATOM   3775  N   VAL B  10      76.078  11.053  16.207  1.00 41.92           N  
ATOM   3776  CA  VAL B  10      74.672  10.807  16.420  1.00 38.24           C  
ATOM   3777  C   VAL B  10      74.620   9.535  17.249  1.00 35.64           C  
ATOM   3778  O   VAL B  10      75.197   8.505  16.869  1.00 32.79           O  
ATOM   3779  CB  VAL B  10      73.937  10.598  15.059  1.00 39.12           C  
ATOM   3780  CG1 VAL B  10      72.451  10.430  15.313  1.00 39.10           C  
ATOM   3781  CG2 VAL B  10      74.133  11.790  14.133  1.00 37.83           C  
ATOM   3782  N   ILE B  11      74.004   9.572  18.424  1.00 36.46           N  
ATOM   3783  CA  ILE B  11      73.800   8.349  19.181  1.00 37.38           C  
ATOM   3784  C   ILE B  11      72.391   7.903  18.774  1.00 35.49           C  
ATOM   3785  O   ILE B  11      71.384   8.528  19.141  1.00 33.45           O  
ATOM   3786  CB  ILE B  11      73.911   8.633  20.711  1.00 39.99           C  
ATOM   3787  CG1 ILE B  11      75.273   9.234  21.067  1.00 38.02           C  
ATOM   3788  CG2 ILE B  11      73.721   7.317  21.463  1.00 38.68           C  
ATOM   3789  CD1 ILE B  11      75.410   9.706  22.525  1.00 36.03           C  
ATOM   3790  N   GLY B  12      72.344   6.854  17.958  1.00 34.04           N  
ATOM   3791  CA  GLY B  12      71.082   6.317  17.483  1.00 33.67           C  
ATOM   3792  C   GLY B  12      70.973   6.373  15.972  1.00 32.03           C  
ATOM   3793  O   GLY B  12      70.925   7.434  15.356  1.00 34.74           O  
ATOM   3794  N   ALA B  13      70.951   5.210  15.336  1.00 30.05           N  
ATOM   3795  CA  ALA B  13      70.846   5.133  13.892  1.00 32.85           C  
ATOM   3796  C   ALA B  13      69.438   4.710  13.486  1.00 33.93           C  
ATOM   3797  O   ALA B  13      69.231   3.674  12.824  1.00 33.89           O  
ATOM   3798  CB  ALA B  13      71.856   4.120  13.358  1.00 27.83           C  
ATOM   3799  N   GLY B  14      68.448   5.497  13.917  1.00 32.88           N  
ATOM   3800  CA  GLY B  14      67.059   5.218  13.589  1.00 31.45           C  
ATOM   3801  C   GLY B  14      66.452   6.265  12.676  1.00 31.63           C  
ATOM   3802  O   GLY B  14      67.198   7.065  12.110  1.00 32.11           O  
ATOM   3803  N   SER B  15      65.115   6.353  12.621  1.00 31.31           N  
ATOM   3804  CA  SER B  15      64.411   7.300  11.755  1.00 31.98           C  
ATOM   3805  C   SER B  15      64.988   8.722  11.718  1.00 33.01           C  
ATOM   3806  O   SER B  15      65.301   9.261  10.649  1.00 34.17           O  
ATOM   3807  CB  SER B  15      62.958   7.411  12.174  1.00 20.28           C  
ATOM   3808  OG  SER B  15      62.349   6.160  12.427  1.00 30.18           O  
ATOM   3809  N   GLY B  16      65.178   9.321  12.904  1.00 34.48           N  
ATOM   3810  CA  GLY B  16      65.722  10.663  13.005  1.00 33.34           C  
ATOM   3811  C   GLY B  16      67.236  10.672  12.867  1.00 34.35           C  
ATOM   3812  O   GLY B  16      67.781  11.535  12.177  1.00 36.66           O  
ATOM   3813  N   GLY B  17      67.925   9.707  13.476  1.00 31.56           N  
ATOM   3814  CA  GLY B  17      69.381   9.657  13.464  1.00 31.86           C  
ATOM   3815  C   GLY B  17      70.001   9.529  12.081  1.00 32.56           C  
ATOM   3816  O   GLY B  17      70.858  10.331  11.685  1.00 32.04           O  
ATOM   3817  N   LEU B  18      69.567   8.500  11.346  1.00 33.40           N  
ATOM   3818  CA  LEU B  18      70.002   8.234   9.985  1.00 33.10           C  
ATOM   3819  C   LEU B  18      69.637   9.387   9.071  1.00 35.88           C  
ATOM   3820  O   LEU B  18      70.450   9.762   8.231  1.00 41.12           O  
ATOM   3821  CB  LEU B  18      69.356   6.983   9.435  1.00 30.91           C  
ATOM   3822  CG  LEU B  18      69.802   5.665  10.035  1.00 32.32           C  
ATOM   3823  CD1 LEU B  18      68.843   4.581   9.630  1.00 31.36           C  
ATOM   3824  CD2 LEU B  18      71.205   5.336   9.577  1.00 31.13           C  
ATOM   3825  N   GLU B  19      68.458   9.992   9.210  1.00 35.89           N  
ATOM   3826  CA  GLU B  19      68.085  11.156   8.425  1.00 36.26           C  
ATOM   3827  C   GLU B  19      69.065  12.293   8.669  1.00 38.50           C  
ATOM   3828  O   GLU B  19      69.662  12.775   7.711  1.00 40.96           O  
ATOM   3829  CB  GLU B  19      66.681  11.622   8.790  1.00 37.08           C  
ATOM   3830  CG  GLU B  19      66.190  12.901   8.113  1.00 38.55           C  
ATOM   3831  CD  GLU B  19      65.949  12.843   6.603  1.00 44.65           C  
ATOM   3832  OE1 GLU B  19      65.974  11.769   6.004  1.00 40.74           O  
ATOM   3833  OE2 GLU B  19      65.712  13.899   6.022  1.00 48.19           O  
ATOM   3834  N   ALA B  20      69.293  12.735   9.907  1.00 39.99           N  
ATOM   3835  CA  ALA B  20      70.234  13.809  10.207  1.00 39.40           C  
ATOM   3836  C   ALA B  20      71.667  13.515   9.767  1.00 38.11           C  
ATOM   3837  O   ALA B  20      72.349  14.371   9.200  1.00 37.06           O  
ATOM   3838  CB  ALA B  20      70.237  14.074  11.697  1.00 38.15           C  
ATOM   3839  N   ALA B  21      72.128  12.288   9.966  1.00 40.04           N  
ATOM   3840  CA  ALA B  21      73.453  11.883   9.546  1.00 42.80           C  
ATOM   3841  C   ALA B  21      73.612  12.019   8.038  1.00 44.94           C  
ATOM   3842  O   ALA B  21      74.556  12.654   7.568  1.00 46.77           O  
ATOM   3843  CB  ALA B  21      73.688  10.440   9.920  1.00 42.23           C  
ATOM   3844  N   TRP B  22      72.671  11.489   7.259  1.00 45.45           N  
ATOM   3845  CA  TRP B  22      72.746  11.551   5.817  1.00 47.59           C  
ATOM   3846  C   TRP B  22      72.691  12.998   5.370  1.00 50.55           C  
ATOM   3847  O   TRP B  22      73.559  13.482   4.648  1.00 52.54           O  
ATOM   3848  CB  TRP B  22      71.585  10.787   5.204  1.00 49.83           C  
ATOM   3849  CG  TRP B  22      71.514  10.888   3.685  1.00 62.35           C  
ATOM   3850  CD1 TRP B  22      70.680  11.784   3.054  1.00 63.87           C  
ATOM   3851  CD2 TRP B  22      72.229  10.125   2.806  1.00 65.73           C  
ATOM   3852  NE1 TRP B  22      70.875  11.588   1.773  1.00 64.54           N  
ATOM   3853  CE2 TRP B  22      71.785  10.620   1.571  1.00 68.02           C  
ATOM   3854  CE3 TRP B  22      73.182   9.112   2.874  1.00 69.36           C  
ATOM   3855  CZ2 TRP B  22      72.281  10.085   0.376  1.00 70.73           C  
ATOM   3856  CZ3 TRP B  22      73.672   8.585   1.679  1.00 73.23           C  
ATOM   3857  CH2 TRP B  22      73.236   9.065   0.439  1.00 67.92           C  
ATOM   3858  N   ASN B  23      71.672  13.710   5.819  1.00 50.11           N  
ATOM   3859  CA  ASN B  23      71.428  15.090   5.456  1.00 50.99           C  
ATOM   3860  C   ASN B  23      72.647  15.969   5.755  1.00 53.75           C  
ATOM   3861  O   ASN B  23      72.924  16.926   5.026  1.00 54.76           O  
ATOM   3862  CB  ASN B  23      70.215  15.531   6.243  1.00 52.55           C  
ATOM   3863  CG  ASN B  23      69.296  16.566   5.627  1.00 58.33           C  
ATOM   3864  OD1 ASN B  23      68.209  16.221   5.174  1.00 56.72           O  
ATOM   3865  ND2 ASN B  23      69.602  17.861   5.604  1.00 62.03           N  
ATOM   3866  N   ALA B  24      73.443  15.671   6.786  1.00 55.40           N  
ATOM   3867  CA  ALA B  24      74.627  16.457   7.119  1.00 57.00           C  
ATOM   3868  C   ALA B  24      75.827  16.142   6.235  1.00 57.99           C  
ATOM   3869  O   ALA B  24      76.378  17.051   5.599  1.00 58.62           O  
ATOM   3870  CB  ALA B  24      75.048  16.219   8.561  1.00 57.29           C  
ATOM   3871  N   ALA B  25      76.206  14.863   6.165  1.00 56.92           N  
ATOM   3872  CA  ALA B  25      77.318  14.378   5.358  1.00 58.49           C  
ATOM   3873  C   ALA B  25      77.149  14.645   3.864  1.00 60.44           C  
ATOM   3874  O   ALA B  25      78.098  15.005   3.167  1.00 63.03           O  
ATOM   3875  CB  ALA B  25      77.484  12.877   5.542  1.00 55.62           C  
ATOM   3876  N   THR B  26      75.933  14.514   3.351  1.00 60.76           N  
ATOM   3877  CA  THR B  26      75.647  14.794   1.963  1.00 59.82           C  
ATOM   3878  C   THR B  26      75.439  16.296   1.741  1.00 60.31           C  
ATOM   3879  O   THR B  26      76.279  16.928   1.106  1.00 62.40           O  
ATOM   3880  CB  THR B  26      74.422  13.929   1.606  1.00 55.94           C  
ATOM   3881  OG1 THR B  26      74.892  12.588   1.726  1.00 61.32           O  
ATOM   3882  CG2 THR B  26      73.837  14.166   0.228  1.00 59.30           C  
ATOM   3883  N   LEU B  27      74.416  16.962   2.283  1.00 61.30           N  
ATOM   3884  CA  LEU B  27      74.182  18.361   1.948  1.00 63.72           C  
ATOM   3885  C   LEU B  27      75.220  19.340   2.444  1.00 66.01           C  
ATOM   3886  O   LEU B  27      75.528  20.309   1.752  1.00 68.73           O  
ATOM   3887  CB  LEU B  27      72.861  18.887   2.484  1.00 63.90           C  
ATOM   3888  CG  LEU B  27      71.547  18.180   2.226  1.00 68.84           C  
ATOM   3889  CD1 LEU B  27      70.445  19.157   2.594  1.00 71.58           C  
ATOM   3890  CD2 LEU B  27      71.398  17.756   0.773  1.00 71.97           C  
ATOM   3891  N   TYR B  28      75.745  19.149   3.647  1.00 67.44           N  
ATOM   3892  CA  TYR B  28      76.683  20.119   4.177  1.00 68.61           C  
ATOM   3893  C   TYR B  28      78.091  19.586   4.250  1.00 70.03           C  
ATOM   3894  O   TYR B  28      78.969  20.224   4.826  1.00 70.31           O  
ATOM   3895  CB  TYR B  28      76.216  20.560   5.555  1.00 71.55           C  
ATOM   3896  CG  TYR B  28      74.852  21.218   5.470  1.00 70.69           C  
ATOM   3897  CD1 TYR B  28      74.693  22.409   4.765  1.00 69.40           C  
ATOM   3898  CD2 TYR B  28      73.756  20.609   6.078  1.00 75.62           C  
ATOM   3899  CE1 TYR B  28      73.430  22.990   4.666  1.00 76.22           C  
ATOM   3900  CE2 TYR B  28      72.491  21.186   5.983  1.00 76.17           C  
ATOM   3901  CZ  TYR B  28      72.337  22.373   5.276  1.00 75.91           C  
ATOM   3902  OH  TYR B  28      71.077  22.936   5.183  1.00 80.80           O  
ATOM   3903  N   LYS B  29      78.311  18.406   3.676  1.00 71.28           N  
ATOM   3904  CA  LYS B  29      79.591  17.711   3.625  1.00 73.94           C  
ATOM   3905  C   LYS B  29      80.441  17.729   4.900  1.00 74.63           C  
ATOM   3906  O   LYS B  29      81.675  17.660   4.862  1.00 77.65           O  
ATOM   3907  CB  LYS B  29      80.404  18.254   2.419  1.00 74.93           C  
ATOM   3908  CG  LYS B  29      79.805  18.026   1.021  1.00 81.54           C  
ATOM   3909  CD  LYS B  29      80.787  17.319   0.090  1.00 88.39           C  
ATOM   3910  CE  LYS B  29      80.609  15.813   0.243  1.00 87.79           C  
ATOM   3911  NZ  LYS B  29      81.676  15.076  -0.404  1.00 91.99           N  
ATOM   3912  N   LYS B  30      79.776  17.812   6.065  1.00 74.02           N  
ATOM   3913  CA  LYS B  30      80.444  17.714   7.356  1.00 72.21           C  
ATOM   3914  C   LYS B  30      80.450  16.248   7.760  1.00 70.16           C  
ATOM   3915  O   LYS B  30      79.513  15.509   7.479  1.00 71.56           O  
ATOM   3916  CB  LYS B  30      79.711  18.587   8.384  1.00 71.94           C  
ATOM   3917  CG  LYS B  30      80.151  20.013   8.076  1.00 78.76           C  
ATOM   3918  CD  LYS B  30      79.582  21.103   8.958  1.00 83.94           C  
ATOM   3919  CE  LYS B  30      80.086  22.471   8.481  1.00 85.54           C  
ATOM   3920  NZ  LYS B  30      79.552  23.564   9.279  1.00 89.69           N  
ATOM   3921  N   ARG B  31      81.525  15.838   8.425  1.00 69.48           N  
ATOM   3922  CA  ARG B  31      81.802  14.453   8.763  1.00 68.08           C  
ATOM   3923  C   ARG B  31      81.157  14.000  10.074  1.00 65.46           C  
ATOM   3924  O   ARG B  31      81.394  14.586  11.134  1.00 65.10           O  
ATOM   3925  CB  ARG B  31      83.291  14.382   8.801  1.00 73.95           C  
ATOM   3926  CG  ARG B  31      83.884  13.079   9.206  1.00 78.65           C  
ATOM   3927  CD  ARG B  31      85.350  13.399   9.345  1.00 87.65           C  
ATOM   3928  NE  ARG B  31      86.044  12.207   9.767  1.00 91.22           N  
ATOM   3929  CZ  ARG B  31      87.320  11.965   9.463  1.00 92.97           C  
ATOM   3930  NH1 ARG B  31      88.099  12.794   8.744  1.00 95.77           N  
ATOM   3931  NH2 ARG B  31      87.805  10.806   9.885  1.00 93.07           N  
ATOM   3932  N   VAL B  32      80.384  12.925  10.067  1.00 62.65           N  
ATOM   3933  CA  VAL B  32      79.577  12.440  11.190  1.00 58.07           C  
ATOM   3934  C   VAL B  32      79.777  10.943  11.397  1.00 53.03           C  
ATOM   3935  O   VAL B  32      79.990  10.174  10.443  1.00 50.78           O  
ATOM   3936  CB  VAL B  32      78.001  12.772  10.970  1.00 58.42           C  
ATOM   3937  CG1 VAL B  32      77.814  13.352   9.529  1.00 53.43           C  
ATOM   3938  CG2 VAL B  32      77.099  11.533  11.331  1.00 58.01           C  
ATOM   3939  N   ALA B  33      79.679  10.573  12.671  1.00 49.46           N  
ATOM   3940  CA  ALA B  33      79.736   9.194  13.105  1.00 48.23           C  
ATOM   3941  C   ALA B  33      78.394   8.860  13.734  1.00 48.02           C  
ATOM   3942  O   ALA B  33      77.824   9.744  14.388  1.00 49.14           O  
ATOM   3943  CB  ALA B  33      80.790   9.044  14.145  1.00 46.80           C  
ATOM   3944  N   VAL B  34      77.824   7.666  13.556  1.00 46.32           N  
ATOM   3945  CA  VAL B  34      76.573   7.290  14.200  1.00 45.85           C  
ATOM   3946  C   VAL B  34      76.822   5.956  14.879  1.00 43.61           C  
ATOM   3947  O   VAL B  34      77.588   5.117  14.391  1.00 41.38           O  
ATOM   3948  CB  VAL B  34      75.363   7.139  13.196  1.00 49.45           C  
ATOM   3949  CG1 VAL B  34      75.188   8.410  12.395  1.00 51.56           C  
ATOM   3950  CG2 VAL B  34      75.586   6.029  12.217  1.00 51.17           C  
ATOM   3951  N   ILE B  35      76.171   5.763  16.018  1.00 42.14           N  
ATOM   3952  CA  ILE B  35      76.367   4.596  16.867  1.00 38.91           C  
ATOM   3953  C   ILE B  35      75.058   3.836  16.980  1.00 37.31           C  
ATOM   3954  O   ILE B  35      73.995   4.463  17.076  1.00 35.88           O  
ATOM   3955  CB  ILE B  35      76.820   5.058  18.282  1.00 40.90           C  
ATOM   3956  CG1 ILE B  35      77.972   6.052  18.177  1.00 35.49           C  
ATOM   3957  CG2 ILE B  35      77.246   3.847  19.104  1.00 38.01           C  
ATOM   3958  CD1 ILE B  35      78.200   6.863  19.455  1.00 39.04           C  
ATOM   3959  N   ASP B  36      75.086   2.513  16.966  1.00 36.41           N  
ATOM   3960  CA  ASP B  36      73.910   1.713  17.265  1.00 38.24           C  
ATOM   3961  C   ASP B  36      74.376   0.339  17.730  1.00 36.62           C  
ATOM   3962  O   ASP B  36      75.430  -0.193  17.368  1.00 35.82           O  
ATOM   3963  CB  ASP B  36      72.984   1.527  16.049  1.00 38.02           C  
ATOM   3964  CG  ASP B  36      71.497   1.494  16.429  1.00 38.40           C  
ATOM   3965  OD1 ASP B  36      71.031   0.583  17.110  1.00 30.20           O  
ATOM   3966  OD2 ASP B  36      70.779   2.401  16.033  1.00 31.74           O  
ATOM   3967  N   VAL B  37      73.511  -0.256  18.535  1.00 37.30           N  
ATOM   3968  CA  VAL B  37      73.818  -1.488  19.223  1.00 36.32           C  
ATOM   3969  C   VAL B  37      73.793  -2.721  18.343  1.00 38.84           C  
ATOM   3970  O   VAL B  37      74.455  -3.695  18.695  1.00 42.81           O  
ATOM   3971  CB  VAL B  37      72.841  -1.645  20.432  1.00 32.96           C  
ATOM   3972  CG1 VAL B  37      72.855  -0.326  21.193  1.00 23.09           C  
ATOM   3973  CG2 VAL B  37      71.414  -1.985  20.013  1.00 34.38           C  
ATOM   3974  N   GLN B  38      73.078  -2.756  17.219  1.00 37.00           N  
ATOM   3975  CA  GLN B  38      73.038  -3.946  16.386  1.00 36.25           C  
ATOM   3976  C   GLN B  38      73.016  -3.518  14.936  1.00 37.96           C  
ATOM   3977  O   GLN B  38      72.549  -2.420  14.619  1.00 36.97           O  
ATOM   3978  CB  GLN B  38      71.793  -4.789  16.616  1.00 30.35           C  
ATOM   3979  CG  GLN B  38      71.716  -5.496  17.938  1.00 38.22           C  
ATOM   3980  CD  GLN B  38      70.630  -6.548  18.035  1.00 40.94           C  
ATOM   3981  OE1 GLN B  38      70.289  -6.966  19.133  1.00 46.03           O  
ATOM   3982  NE2 GLN B  38      70.027  -7.103  16.999  1.00 51.46           N  
ATOM   3983  N   MET B  39      73.527  -4.425  14.094  1.00 40.23           N  
ATOM   3984  CA  MET B  39      73.567  -4.297  12.636  1.00 40.32           C  
ATOM   3985  C   MET B  39      72.285  -4.824  12.008  1.00 39.29           C  
ATOM   3986  O   MET B  39      71.741  -4.257  11.072  1.00 41.28           O  
ATOM   3987  CB  MET B  39      74.687  -5.115  11.986  1.00 43.21           C  
ATOM   3988  CG  MET B  39      76.135  -4.849  12.351  1.00 49.37           C  
ATOM   3989  SD  MET B  39      76.641  -3.187  11.875  1.00 62.39           S  
ATOM   3990  CE  MET B  39      76.894  -3.407  10.141  1.00 53.19           C  
ATOM   3991  N   VAL B  40      71.825  -5.970  12.481  1.00 36.77           N  
ATOM   3992  CA  VAL B  40      70.650  -6.639  11.954  1.00 37.81           C  
ATOM   3993  C   VAL B  40      69.612  -6.687  13.064  1.00 37.72           C  
ATOM   3994  O   VAL B  40      69.955  -6.571  14.241  1.00 40.44           O  
ATOM   3995  CB  VAL B  40      71.140  -8.026  11.487  1.00 35.74           C  
ATOM   3996  CG1 VAL B  40      70.021  -9.021  11.268  1.00 42.10           C  
ATOM   3997  CG2 VAL B  40      71.869  -7.810  10.171  1.00 37.11           C  
ATOM   3998  N   HIS B  41      68.346  -6.792  12.693  1.00 37.09           N  
ATOM   3999  CA  HIS B  41      67.219  -6.874  13.613  1.00 34.62           C  
ATOM   4000  C   HIS B  41      67.184  -8.140  14.451  1.00 33.45           C  
ATOM   4001  O   HIS B  41      67.665  -9.194  14.028  1.00 33.38           O  
ATOM   4002  CB  HIS B  41      65.890  -6.817  12.846  1.00 33.51           C  
ATOM   4003  CG  HIS B  41      65.588  -8.069  12.013  1.00 32.64           C  
ATOM   4004  ND1 HIS B  41      64.696  -9.021  12.265  1.00 29.19           N  
ATOM   4005  CD2 HIS B  41      66.242  -8.423  10.848  1.00 31.51           C  
ATOM   4006  CE1 HIS B  41      64.779  -9.924  11.331  1.00 21.17           C  
ATOM   4007  NE2 HIS B  41      65.708  -9.555  10.488  1.00 24.99           N  
ATOM   4008  N   GLY B  42      66.447  -8.086  15.553  1.00 33.78           N  
ATOM   4009  CA  GLY B  42      66.208  -9.283  16.328  1.00 32.72           C  
ATOM   4010  C   GLY B  42      66.754  -9.236  17.734  1.00 32.33           C  
ATOM   4011  O   GLY B  42      67.433  -8.279  18.112  1.00 31.27           O  
ATOM   4012  N   PRO B  43      66.435 -10.240  18.553  1.00 32.90           N  
ATOM   4013  CA  PRO B  43      67.015 -10.429  19.883  1.00 36.40           C  
ATOM   4014  C   PRO B  43      68.538 -10.486  19.753  1.00 38.66           C  
ATOM   4015  O   PRO B  43      69.010 -11.081  18.778  1.00 41.46           O  
ATOM   4016  CB  PRO B  43      66.417 -11.720  20.378  1.00 34.86           C  
ATOM   4017  CG  PRO B  43      65.204 -11.934  19.504  1.00 36.75           C  
ATOM   4018  CD  PRO B  43      65.652 -11.404  18.159  1.00 32.52           C  
ATOM   4019  N   PRO B  44      69.373  -9.961  20.653  1.00 39.12           N  
ATOM   4020  CA  PRO B  44      69.005  -9.556  21.995  1.00 37.93           C  
ATOM   4021  C   PRO B  44      68.388  -8.179  22.186  1.00 36.94           C  
ATOM   4022  O   PRO B  44      67.492  -8.025  23.013  1.00 36.01           O  
ATOM   4023  CB  PRO B  44      70.304  -9.759  22.749  1.00 37.26           C  
ATOM   4024  CG  PRO B  44      71.352  -9.318  21.757  1.00 36.24           C  
ATOM   4025  CD  PRO B  44      70.827  -9.924  20.470  1.00 39.93           C  
ATOM   4026  N   PHE B  45      68.815  -7.180  21.426  1.00 36.39           N  
ATOM   4027  CA  PHE B  45      68.377  -5.810  21.641  1.00 38.64           C  
ATOM   4028  C   PHE B  45      67.235  -5.365  20.751  1.00 37.38           C  
ATOM   4029  O   PHE B  45      66.742  -4.250  20.921  1.00 39.25           O  
ATOM   4030  CB  PHE B  45      69.559  -4.850  21.452  1.00 45.44           C  
ATOM   4031  CG  PHE B  45      70.783  -5.230  22.283  1.00 54.93           C  
ATOM   4032  CD1 PHE B  45      70.632  -5.623  23.622  1.00 56.47           C  
ATOM   4033  CD2 PHE B  45      72.051  -5.245  21.692  1.00 55.75           C  
ATOM   4034  CE1 PHE B  45      71.743  -6.034  24.354  1.00 58.60           C  
ATOM   4035  CE2 PHE B  45      73.157  -5.658  22.436  1.00 58.96           C  
ATOM   4036  CZ  PHE B  45      73.005  -6.055  23.764  1.00 58.01           C  
ATOM   4037  N   PHE B  46      66.789  -6.206  19.813  1.00 36.49           N  
ATOM   4038  CA  PHE B  46      65.655  -5.975  18.918  1.00 36.36           C  
ATOM   4039  C   PHE B  46      65.803  -4.861  17.891  1.00 36.13           C  
ATOM   4040  O   PHE B  46      65.715  -5.124  16.683  1.00 34.02           O  
ATOM   4041  CB  PHE B  46      64.385  -5.743  19.759  1.00 32.55           C  
ATOM   4042  CG  PHE B  46      64.058  -6.971  20.590  1.00 28.68           C  
ATOM   4043  CD1 PHE B  46      63.482  -8.082  19.967  1.00 22.08           C  
ATOM   4044  CD2 PHE B  46      64.345  -6.982  21.956  1.00 25.72           C  
ATOM   4045  CE1 PHE B  46      63.217  -9.223  20.712  1.00 30.06           C  
ATOM   4046  CE2 PHE B  46      64.075  -8.131  22.688  1.00 27.60           C  
ATOM   4047  CZ  PHE B  46      63.504  -9.245  22.073  1.00 30.67           C  
ATOM   4048  N   SER B  47      65.949  -3.618  18.334  1.00 36.56           N  
ATOM   4049  CA  SER B  47      66.201  -2.517  17.434  1.00 40.73           C  
ATOM   4050  C   SER B  47      67.654  -2.625  16.973  1.00 41.55           C  
ATOM   4051  O   SER B  47      68.525  -3.136  17.684  1.00 42.27           O  
ATOM   4052  CB  SER B  47      65.977  -1.196  18.146  1.00 41.56           C  
ATOM   4053  OG  SER B  47      65.663  -0.181  17.194  1.00 47.37           O  
ATOM   4054  N   ALA B  48      67.913  -2.109  15.782  1.00 38.95           N  
ATOM   4055  CA  ALA B  48      69.195  -2.242  15.132  1.00 36.03           C  
ATOM   4056  C   ALA B  48      69.347  -1.046  14.217  1.00 36.13           C  
ATOM   4057  O   ALA B  48      68.626  -0.052  14.365  1.00 35.79           O  
ATOM   4058  CB  ALA B  48      69.193  -3.508  14.307  1.00 37.10           C  
ATOM   4059  N   LEU B  49      70.270  -1.135  13.257  1.00 37.34           N  
ATOM   4060  CA  LEU B  49      70.496  -0.132  12.220  1.00 38.67           C  
ATOM   4061  C   LEU B  49      69.191   0.001  11.424  1.00 37.52           C  
ATOM   4062  O   LEU B  49      68.598  -0.975  10.931  1.00 34.91           O  
ATOM   4063  CB  LEU B  49      71.672  -0.620  11.357  1.00 35.58           C  
ATOM   4064  CG  LEU B  49      72.365   0.262  10.334  1.00 37.65           C  
ATOM   4065  CD1 LEU B  49      72.781   1.568  10.957  1.00 33.26           C  
ATOM   4066  CD2 LEU B  49      73.599  -0.452   9.824  1.00 34.54           C  
ATOM   4067  N   GLY B  50      68.694   1.231  11.386  1.00 36.88           N  
ATOM   4068  CA  GLY B  50      67.398   1.484  10.788  1.00 34.28           C  
ATOM   4069  C   GLY B  50      66.448   2.030  11.841  1.00 33.01           C  
ATOM   4070  O   GLY B  50      65.599   2.866  11.527  1.00 30.73           O  
ATOM   4071  N   GLY B  51      66.574   1.572  13.100  1.00 29.24           N  
ATOM   4072  CA  GLY B  51      65.750   2.056  14.191  1.00 23.78           C  
ATOM   4073  C   GLY B  51      64.538   1.217  14.513  1.00 22.89           C  
ATOM   4074  O   GLY B  51      64.291   0.175  13.897  1.00 26.10           O  
ATOM   4075  N   THR B  52      63.752   1.682  15.480  1.00 22.24           N  
ATOM   4076  CA  THR B  52      62.530   1.000  15.909  1.00 24.70           C  
ATOM   4077  C   THR B  52      61.535   0.789  14.766  1.00 23.99           C  
ATOM   4078  O   THR B  52      61.005  -0.312  14.626  1.00 26.38           O  
ATOM   4079  CB  THR B  52      61.852   1.813  17.019  1.00 24.57           C  
ATOM   4080  OG1 THR B  52      62.871   2.056  17.980  1.00 29.40           O  
ATOM   4081  CG2 THR B  52      60.665   1.112  17.641  1.00 17.15           C  
ATOM   4082  N   CYS B  53      61.307   1.798  13.916  1.00 23.31           N  
ATOM   4083  CA  CYS B  53      60.358   1.706  12.816  1.00 22.44           C  
ATOM   4084  C   CYS B  53      60.696   0.605  11.833  1.00 20.45           C  
ATOM   4085  O   CYS B  53      59.832  -0.213  11.508  1.00 22.50           O  
ATOM   4086  CB  CYS B  53      60.297   3.031  12.073  1.00 27.03           C  
ATOM   4087  SG  CYS B  53      59.043   3.175  10.759  1.00 28.00           S  
ATOM   4088  N   VAL B  54      61.946   0.534  11.408  1.00 18.25           N  
ATOM   4089  CA  VAL B  54      62.345  -0.488  10.462  1.00 18.39           C  
ATOM   4090  C   VAL B  54      62.341  -1.859  11.103  1.00 20.31           C  
ATOM   4091  O   VAL B  54      61.835  -2.815  10.523  1.00 21.39           O  
ATOM   4092  CB  VAL B  54      63.750  -0.130   9.925  1.00 23.36           C  
ATOM   4093  CG1 VAL B  54      64.423  -1.295   9.208  1.00 21.22           C  
ATOM   4094  CG2 VAL B  54      63.576   1.028   8.954  1.00 20.53           C  
ATOM   4095  N   ASN B  55      62.855  -1.951  12.329  1.00 22.71           N  
ATOM   4096  CA  ASN B  55      63.085  -3.256  12.939  1.00 20.48           C  
ATOM   4097  C   ASN B  55      61.955  -3.868  13.735  1.00 21.83           C  
ATOM   4098  O   ASN B  55      61.653  -5.055  13.590  1.00 21.02           O  
ATOM   4099  CB  ASN B  55      64.335  -3.151  13.812  1.00 19.46           C  
ATOM   4100  CG  ASN B  55      65.558  -2.902  12.950  1.00 15.92           C  
ATOM   4101  OD1 ASN B  55      66.004  -3.815  12.276  1.00 25.97           O  
ATOM   4102  ND2 ASN B  55      66.191  -1.743  12.860  1.00 18.15           N  
ATOM   4103  N   VAL B  56      61.327  -3.074  14.612  1.00 22.70           N  
ATOM   4104  CA  VAL B  56      60.234  -3.546  15.462  1.00 21.70           C  
ATOM   4105  C   VAL B  56      59.118  -2.498  15.528  1.00 21.93           C  
ATOM   4106  O   VAL B  56      58.526  -2.278  16.584  1.00 23.52           O  
ATOM   4107  CB  VAL B  56      60.771  -3.878  16.917  1.00 20.05           C  
ATOM   4108  CG1 VAL B  56      61.397  -5.255  16.906  1.00 11.23           C  
ATOM   4109  CG2 VAL B  56      61.830  -2.873  17.394  1.00 17.14           C  
ATOM   4110  N   GLY B  57      58.771  -1.834  14.422  1.00 21.25           N  
ATOM   4111  CA  GLY B  57      57.782  -0.773  14.453  1.00 18.70           C  
ATOM   4112  C   GLY B  57      56.900  -0.778  13.225  1.00 18.28           C  
ATOM   4113  O   GLY B  57      56.369  -1.825  12.846  1.00 21.28           O  
ATOM   4114  N   CYS B  58      56.735   0.385  12.591  1.00 18.87           N  
ATOM   4115  CA  CYS B  58      55.941   0.586  11.377  1.00 16.91           C  
ATOM   4116  C   CYS B  58      56.049  -0.445  10.278  1.00 15.84           C  
ATOM   4117  O   CYS B  58      55.027  -0.998   9.873  1.00 14.49           O  
ATOM   4118  CB  CYS B  58      56.271   1.885  10.695  1.00 17.30           C  
ATOM   4119  SG  CYS B  58      57.220   3.106  11.625  1.00 26.26           S  
ATOM   4120  N   VAL B  59      57.265  -0.734   9.797  1.00 20.12           N  
ATOM   4121  CA  VAL B  59      57.441  -1.617   8.649  1.00 20.41           C  
ATOM   4122  C   VAL B  59      57.004  -3.047   8.954  1.00 20.21           C  
ATOM   4123  O   VAL B  59      56.023  -3.460   8.316  1.00 25.64           O  
ATOM   4124  CB  VAL B  59      58.930  -1.525   8.173  1.00 16.34           C  
ATOM   4125  CG1 VAL B  59      59.124  -2.392   6.956  1.00 17.04           C  
ATOM   4126  CG2 VAL B  59      59.294  -0.093   7.824  1.00 13.72           C  
ATOM   4127  N   PRO B  60      57.546  -3.855   9.885  1.00 20.45           N  
ATOM   4128  CA  PRO B  60      57.011  -5.176  10.182  1.00 18.17           C  
ATOM   4129  C   PRO B  60      55.538  -5.151  10.621  1.00 19.18           C  
ATOM   4130  O   PRO B  60      54.762  -6.038  10.231  1.00 23.26           O  
ATOM   4131  CB  PRO B  60      58.000  -5.708  11.218  1.00 16.60           C  
ATOM   4132  CG  PRO B  60      58.530  -4.499  11.902  1.00 15.87           C  
ATOM   4133  CD  PRO B  60      58.710  -3.572  10.728  1.00 13.86           C  
ATOM   4134  N   LYS B  61      55.110  -4.130  11.376  1.00 19.37           N  
ATOM   4135  CA  LYS B  61      53.720  -3.969  11.778  1.00 21.17           C  
ATOM   4136  C   LYS B  61      52.813  -3.911  10.550  1.00 20.20           C  
ATOM   4137  O   LYS B  61      51.806  -4.624  10.479  1.00 18.06           O  
ATOM   4138  CB  LYS B  61      53.596  -2.676  12.612  1.00 21.12           C  
ATOM   4139  CG  LYS B  61      52.235  -2.210  13.083  1.00 20.59           C  
ATOM   4140  CD  LYS B  61      51.412  -1.372  12.097  1.00 17.88           C  
ATOM   4141  CE  LYS B  61      51.944   0.026  11.962  1.00 15.66           C  
ATOM   4142  NZ  LYS B  61      51.708   0.774  13.179  1.00 16.35           N  
ATOM   4143  N   LYS B  62      53.143  -3.074   9.567  1.00 19.75           N  
ATOM   4144  CA  LYS B  62      52.326  -2.952   8.377  1.00 19.23           C  
ATOM   4145  C   LYS B  62      52.268  -4.279   7.618  1.00 18.62           C  
ATOM   4146  O   LYS B  62      51.169  -4.708   7.241  1.00 19.11           O  
ATOM   4147  CB  LYS B  62      52.913  -1.812   7.541  1.00 24.54           C  
ATOM   4148  CG  LYS B  62      52.121  -1.343   6.323  1.00 21.13           C  
ATOM   4149  CD  LYS B  62      50.705  -0.873   6.641  1.00 21.01           C  
ATOM   4150  CE  LYS B  62      49.963  -0.678   5.322  1.00 26.20           C  
ATOM   4151  NZ  LYS B  62      50.406   0.530   4.646  1.00 23.49           N  
ATOM   4152  N   LEU B  63      53.364  -5.031   7.447  1.00 16.68           N  
ATOM   4153  CA  LEU B  63      53.275  -6.316   6.762  1.00 16.25           C  
ATOM   4154  C   LEU B  63      52.330  -7.255   7.457  1.00 15.54           C  
ATOM   4155  O   LEU B  63      51.530  -7.926   6.803  1.00 19.42           O  
ATOM   4156  CB  LEU B  63      54.625  -7.044   6.669  1.00 15.99           C  
ATOM   4157  CG  LEU B  63      55.745  -6.385   5.870  1.00 23.78           C  
ATOM   4158  CD1 LEU B  63      56.904  -7.345   5.772  1.00 23.69           C  
ATOM   4159  CD2 LEU B  63      55.280  -6.058   4.455  1.00 24.40           C  
ATOM   4160  N   MET B  64      52.369  -7.263   8.786  1.00 15.77           N  
ATOM   4161  CA  MET B  64      51.548  -8.160   9.578  1.00 17.50           C  
ATOM   4162  C   MET B  64      50.083  -7.761   9.569  1.00 17.01           C  
ATOM   4163  O   MET B  64      49.211  -8.636   9.488  1.00 18.08           O  
ATOM   4164  CB  MET B  64      52.112  -8.199  11.009  1.00 24.98           C  
ATOM   4165  CG  MET B  64      53.414  -9.011  11.040  1.00 27.16           C  
ATOM   4166  SD  MET B  64      54.414  -8.877  12.540  1.00 28.50           S  
ATOM   4167  CE  MET B  64      53.552  -9.970  13.638  1.00 16.52           C  
ATOM   4168  N   VAL B  65      49.759  -6.463   9.601  1.00 16.95           N  
ATOM   4169  CA  VAL B  65      48.365  -6.028   9.546  1.00 20.19           C  
ATOM   4170  C   VAL B  65      47.789  -6.346   8.156  1.00 18.10           C  
ATOM   4171  O   VAL B  65      46.651  -6.816   8.076  1.00 15.44           O  
ATOM   4172  CB  VAL B  65      48.274  -4.509   9.872  1.00 20.88           C  
ATOM   4173  CG1 VAL B  65      46.848  -4.034   9.672  1.00 20.39           C  
ATOM   4174  CG2 VAL B  65      48.613  -4.249  11.337  1.00 18.36           C  
ATOM   4175  N   THR B  66      48.568  -6.211   7.075  1.00 19.42           N  
ATOM   4176  CA  THR B  66      48.144  -6.575   5.722  1.00 19.10           C  
ATOM   4177  C   THR B  66      47.816  -8.062   5.660  1.00 18.18           C  
ATOM   4178  O   THR B  66      46.771  -8.475   5.130  1.00 19.45           O  
ATOM   4179  CB  THR B  66      49.275  -6.225   4.743  1.00 20.71           C  
ATOM   4180  OG1 THR B  66      49.394  -4.815   4.825  1.00 23.31           O  
ATOM   4181  CG2 THR B  66      49.037  -6.669   3.315  1.00 11.40           C  
ATOM   4182  N   GLY B  67      48.688  -8.864   6.280  1.00 14.77           N  
ATOM   4183  CA  GLY B  67      48.469 -10.292   6.354  1.00 12.85           C  
ATOM   4184  C   GLY B  67      47.191 -10.564   7.110  1.00 13.69           C  
ATOM   4185  O   GLY B  67      46.391 -11.396   6.685  1.00 17.39           O  
ATOM   4186  N   ALA B  68      46.932  -9.823   8.193  1.00 16.54           N  
ATOM   4187  CA  ALA B  68      45.727 -10.032   8.978  1.00 13.72           C  
ATOM   4188  C   ALA B  68      44.489  -9.588   8.222  1.00 16.63           C  
ATOM   4189  O   ALA B  68      43.438 -10.232   8.351  1.00 16.31           O  
ATOM   4190  CB  ALA B  68      45.793  -9.256  10.291  1.00 14.97           C  
ATOM   4191  N   GLN B  69      44.550  -8.538   7.380  1.00 16.32           N  
ATOM   4192  CA  GLN B  69      43.365  -8.147   6.608  1.00 17.23           C  
ATOM   4193  C   GLN B  69      42.913  -9.202   5.610  1.00 17.91           C  
ATOM   4194  O   GLN B  69      41.729  -9.233   5.231  1.00 19.17           O  
ATOM   4195  CB  GLN B  69      43.615  -6.840   5.870  1.00 21.07           C  
ATOM   4196  CG  GLN B  69      43.499  -5.754   6.911  1.00 38.09           C  
ATOM   4197  CD  GLN B  69      43.944  -4.384   6.466  1.00 47.92           C  
ATOM   4198  OE1 GLN B  69      45.097  -4.147   6.103  1.00 52.52           O  
ATOM   4199  NE2 GLN B  69      43.025  -3.420   6.474  1.00 55.01           N  
ATOM   4200  N   TYR B  70      43.774 -10.133   5.170  1.00 17.84           N  
ATOM   4201  CA  TYR B  70      43.322 -11.204   4.304  1.00 16.38           C  
ATOM   4202  C   TYR B  70      42.253 -12.070   4.927  1.00 17.38           C  
ATOM   4203  O   TYR B  70      41.491 -12.653   4.159  1.00 24.91           O  
ATOM   4204  CB  TYR B  70      44.484 -12.077   3.886  1.00 13.00           C  
ATOM   4205  CG  TYR B  70      45.311 -11.345   2.845  1.00 17.15           C  
ATOM   4206  CD1 TYR B  70      44.775 -11.095   1.570  1.00 20.20           C  
ATOM   4207  CD2 TYR B  70      46.578 -10.888   3.168  1.00  9.60           C  
ATOM   4208  CE1 TYR B  70      45.510 -10.383   0.629  1.00 10.23           C  
ATOM   4209  CE2 TYR B  70      47.315 -10.173   2.226  1.00 15.88           C  
ATOM   4210  CZ  TYR B  70      46.774  -9.927   0.969  1.00  8.27           C  
ATOM   4211  OH  TYR B  70      47.476  -9.192   0.043  1.00 19.99           O  
ATOM   4212  N   MET B  71      42.064 -12.143   6.245  1.00 15.54           N  
ATOM   4213  CA  MET B  71      40.960 -12.913   6.801  1.00 15.88           C  
ATOM   4214  C   MET B  71      39.657 -12.239   6.411  1.00 14.18           C  
ATOM   4215  O   MET B  71      38.634 -12.890   6.189  1.00 20.55           O  
ATOM   4216  CB  MET B  71      41.058 -12.984   8.326  1.00 18.87           C  
ATOM   4217  CG  MET B  71      39.925 -13.746   9.035  1.00 29.12           C  
ATOM   4218  SD  MET B  71      40.150 -13.914  10.830  1.00 39.05           S  
ATOM   4219  CE  MET B  71      39.577 -12.373  11.477  1.00 27.05           C  
ATOM   4220  N   GLU B  72      39.717 -10.919   6.282  1.00 13.09           N  
ATOM   4221  CA  GLU B  72      38.577 -10.108   5.886  1.00 14.79           C  
ATOM   4222  C   GLU B  72      38.241 -10.347   4.425  1.00 13.92           C  
ATOM   4223  O   GLU B  72      37.103 -10.644   4.066  1.00 16.52           O  
ATOM   4224  CB  GLU B  72      38.886  -8.614   6.094  1.00 14.14           C  
ATOM   4225  CG  GLU B  72      39.274  -8.273   7.542  1.00 16.50           C  
ATOM   4226  CD  GLU B  72      38.237  -8.703   8.575  1.00 21.50           C  
ATOM   4227  OE1 GLU B  72      37.127  -8.179   8.559  1.00 21.98           O  
ATOM   4228  OE2 GLU B  72      38.522  -9.584   9.388  1.00 19.73           O  
ATOM   4229  N   HIS B  73      39.253 -10.246   3.559  1.00 14.23           N  
ATOM   4230  CA  HIS B  73      39.085 -10.441   2.126  1.00 13.91           C  
ATOM   4231  C   HIS B  73      38.557 -11.815   1.784  1.00 15.06           C  
ATOM   4232  O   HIS B  73      37.612 -11.943   1.004  1.00 17.88           O  
ATOM   4233  CB  HIS B  73      40.407 -10.249   1.395  1.00 10.78           C  
ATOM   4234  CG  HIS B  73      40.860  -8.808   1.463  1.00  9.17           C  
ATOM   4235  ND1 HIS B  73      40.038  -7.774   1.455  1.00 14.34           N  
ATOM   4236  CD2 HIS B  73      42.142  -8.309   1.549  1.00 14.30           C  
ATOM   4237  CE1 HIS B  73      40.732  -6.662   1.537  1.00 11.13           C  
ATOM   4238  NE2 HIS B  73      41.995  -7.005   1.590  1.00 17.22           N  
ATOM   4239  N   LEU B  74      39.172 -12.833   2.378  1.00 16.36           N  
ATOM   4240  CA  LEU B  74      38.784 -14.213   2.153  1.00 14.08           C  
ATOM   4241  C   LEU B  74      37.363 -14.480   2.613  1.00 18.68           C  
ATOM   4242  O   LEU B  74      36.620 -15.198   1.949  1.00 22.90           O  
ATOM   4243  CB  LEU B  74      39.778 -15.124   2.871  1.00 16.08           C  
ATOM   4244  CG  LEU B  74      41.020 -15.532   2.044  1.00 17.43           C  
ATOM   4245  CD1 LEU B  74      41.535 -14.367   1.229  1.00 24.93           C  
ATOM   4246  CD2 LEU B  74      42.151 -15.957   2.954  1.00 15.75           C  
ATOM   4247  N   ARG B  75      36.887 -13.907   3.711  1.00 18.82           N  
ATOM   4248  CA  ARG B  75      35.506 -14.102   4.136  1.00 18.21           C  
ATOM   4249  C   ARG B  75      34.520 -13.335   3.231  1.00 19.42           C  
ATOM   4250  O   ARG B  75      33.478 -13.836   2.786  1.00 20.16           O  
ATOM   4251  CB  ARG B  75      35.423 -13.629   5.599  1.00 19.18           C  
ATOM   4252  CG  ARG B  75      34.096 -13.790   6.333  1.00 20.02           C  
ATOM   4253  CD  ARG B  75      34.166 -13.099   7.704  1.00 23.75           C  
ATOM   4254  NE  ARG B  75      33.980 -11.658   7.643  1.00 27.53           N  
ATOM   4255  CZ  ARG B  75      34.828 -10.797   8.220  1.00 36.52           C  
ATOM   4256  NH1 ARG B  75      35.920 -11.191   8.909  1.00 36.00           N  
ATOM   4257  NH2 ARG B  75      34.570  -9.500   8.074  1.00 33.20           N  
ATOM   4258  N   GLU B  76      34.858 -12.074   2.969  1.00 18.94           N  
ATOM   4259  CA  GLU B  76      34.035 -11.167   2.192  1.00 18.02           C  
ATOM   4260  C   GLU B  76      33.984 -11.495   0.702  1.00 19.24           C  
ATOM   4261  O   GLU B  76      33.006 -11.129   0.042  1.00 18.29           O  
ATOM   4262  CB  GLU B  76      34.563  -9.755   2.405  1.00 16.77           C  
ATOM   4263  CG  GLU B  76      34.369  -9.271   3.846  1.00 16.26           C  
ATOM   4264  CD  GLU B  76      35.070  -7.978   4.226  1.00 22.16           C  
ATOM   4265  OE1 GLU B  76      35.997  -7.567   3.557  1.00 26.45           O  
ATOM   4266  OE2 GLU B  76      34.719  -7.356   5.214  1.00 23.18           O  
ATOM   4267  N   SER B  77      34.948 -12.241   0.138  1.00 17.88           N  
ATOM   4268  CA  SER B  77      34.953 -12.603  -1.275  1.00 17.78           C  
ATOM   4269  C   SER B  77      33.708 -13.379  -1.651  1.00 19.51           C  
ATOM   4270  O   SER B  77      33.174 -13.240  -2.757  1.00 26.24           O  
ATOM   4271  CB  SER B  77      36.186 -13.440  -1.612  1.00 14.08           C  
ATOM   4272  OG  SER B  77      36.236 -14.643  -0.882  1.00 16.96           O  
ATOM   4273  N   ALA B  78      33.174 -14.150  -0.709  1.00 17.69           N  
ATOM   4274  CA  ALA B  78      31.972 -14.917  -0.916  1.00 16.60           C  
ATOM   4275  C   ALA B  78      30.801 -14.065  -1.330  1.00 16.18           C  
ATOM   4276  O   ALA B  78      30.005 -14.519  -2.149  1.00 21.75           O  
ATOM   4277  CB  ALA B  78      31.558 -15.653   0.345  1.00 17.41           C  
ATOM   4278  N   GLY B  79      30.649 -12.830  -0.872  1.00 19.27           N  
ATOM   4279  CA  GLY B  79      29.493 -12.024  -1.251  1.00 20.23           C  
ATOM   4280  C   GLY B  79      29.551 -11.605  -2.716  1.00 20.70           C  
ATOM   4281  O   GLY B  79      28.554 -11.181  -3.283  1.00 22.47           O  
ATOM   4282  N   PHE B  80      30.715 -11.713  -3.349  1.00 20.14           N  
ATOM   4283  CA  PHE B  80      30.897 -11.311  -4.728  1.00 18.93           C  
ATOM   4284  C   PHE B  80      31.020 -12.530  -5.630  1.00 21.99           C  
ATOM   4285  O   PHE B  80      31.395 -12.423  -6.792  1.00 23.25           O  
ATOM   4286  CB  PHE B  80      32.141 -10.415  -4.799  1.00 15.75           C  
ATOM   4287  CG  PHE B  80      31.895  -9.039  -4.151  1.00 23.56           C  
ATOM   4288  CD1 PHE B  80      32.131  -8.836  -2.779  1.00 23.56           C  
ATOM   4289  CD2 PHE B  80      31.421  -7.968  -4.923  1.00 14.91           C  
ATOM   4290  CE1 PHE B  80      31.890  -7.590  -2.195  1.00 18.28           C  
ATOM   4291  CE2 PHE B  80      31.184  -6.724  -4.334  1.00 16.50           C  
ATOM   4292  CZ  PHE B  80      31.422  -6.534  -2.973  1.00 18.67           C  
ATOM   4293  N   GLY B  81      30.697 -13.727  -5.137  1.00 21.65           N  
ATOM   4294  CA  GLY B  81      30.708 -14.918  -5.964  1.00 20.95           C  
ATOM   4295  C   GLY B  81      31.970 -15.762  -5.927  1.00 24.03           C  
ATOM   4296  O   GLY B  81      32.055 -16.706  -6.707  1.00 27.00           O  
ATOM   4297  N   TRP B  82      32.973 -15.534  -5.092  1.00 22.37           N  
ATOM   4298  CA  TRP B  82      34.147 -16.392  -5.045  1.00 23.39           C  
ATOM   4299  C   TRP B  82      33.915 -17.529  -4.068  1.00 26.59           C  
ATOM   4300  O   TRP B  82      33.701 -17.285  -2.875  1.00 25.05           O  
ATOM   4301  CB  TRP B  82      35.317 -15.552  -4.623  1.00 22.33           C  
ATOM   4302  CG  TRP B  82      35.660 -14.549  -5.717  1.00 28.28           C  
ATOM   4303  CD1 TRP B  82      35.164 -13.262  -5.753  1.00 25.11           C  
ATOM   4304  CD2 TRP B  82      36.485 -14.825  -6.777  1.00 28.09           C  
ATOM   4305  NE1 TRP B  82      35.679 -12.733  -6.834  1.00 24.87           N  
ATOM   4306  CE2 TRP B  82      36.468 -13.613  -7.485  1.00 25.97           C  
ATOM   4307  CE3 TRP B  82      37.232 -15.920  -7.220  1.00 23.53           C  
ATOM   4308  CZ2 TRP B  82      37.213 -13.483  -8.658  1.00 26.43           C  
ATOM   4309  CZ3 TRP B  82      37.978 -15.786  -8.389  1.00 29.70           C  
ATOM   4310  CH2 TRP B  82      37.965 -14.580  -9.101  1.00 34.23           C  
ATOM   4311  N   GLU B  83      33.928 -18.757  -4.577  1.00 29.75           N  
ATOM   4312  CA  GLU B  83      33.723 -19.968  -3.805  1.00 30.80           C  
ATOM   4313  C   GLU B  83      35.003 -20.768  -3.770  1.00 31.22           C  
ATOM   4314  O   GLU B  83      35.739 -20.814  -4.759  1.00 29.79           O  
ATOM   4315  CB  GLU B  83      32.731 -20.907  -4.413  1.00 39.84           C  
ATOM   4316  CG  GLU B  83      31.289 -20.509  -4.621  1.00 55.98           C  
ATOM   4317  CD  GLU B  83      30.487 -21.635  -5.284  1.00 70.65           C  
ATOM   4318  OE1 GLU B  83      30.848 -22.093  -6.378  1.00 75.63           O  
ATOM   4319  OE2 GLU B  83      29.485 -22.050  -4.695  1.00 79.33           O  
ATOM   4320  N   PHE B  84      35.283 -21.389  -2.638  1.00 30.80           N  
ATOM   4321  CA  PHE B  84      36.375 -22.334  -2.520  1.00 34.59           C  
ATOM   4322  C   PHE B  84      36.072 -23.188  -1.305  1.00 34.58           C  
ATOM   4323  O   PHE B  84      35.136 -22.906  -0.537  1.00 34.02           O  
ATOM   4324  CB  PHE B  84      37.747 -21.644  -2.349  1.00 35.27           C  
ATOM   4325  CG  PHE B  84      38.006 -20.739  -1.150  1.00 38.03           C  
ATOM   4326  CD1 PHE B  84      37.720 -19.377  -1.237  1.00 39.11           C  
ATOM   4327  CD2 PHE B  84      38.594 -21.244   0.014  1.00 38.09           C  
ATOM   4328  CE1 PHE B  84      38.040 -18.520  -0.181  1.00 35.63           C  
ATOM   4329  CE2 PHE B  84      38.911 -20.380   1.067  1.00 42.48           C  
ATOM   4330  CZ  PHE B  84      38.631 -19.017   0.975  1.00 38.59           C  
ATOM   4331  N   ASP B  85      36.833 -24.268  -1.113  1.00 37.94           N  
ATOM   4332  CA  ASP B  85      36.578 -25.142   0.011  1.00 39.94           C  
ATOM   4333  C   ASP B  85      37.096 -24.452   1.257  1.00 39.33           C  
ATOM   4334  O   ASP B  85      38.233 -24.653   1.677  1.00 36.50           O  
ATOM   4335  CB  ASP B  85      37.285 -26.497  -0.160  1.00 44.81           C  
ATOM   4336  CG  ASP B  85      36.831 -27.576   0.835  1.00 49.41           C  
ATOM   4337  OD1 ASP B  85      35.827 -27.382   1.528  1.00 53.52           O  
ATOM   4338  OD2 ASP B  85      37.472 -28.628   0.908  1.00 54.59           O  
ATOM   4339  N   ARG B  86      36.236 -23.670   1.894  1.00 40.01           N  
ATOM   4340  CA  ARG B  86      36.655 -22.881   3.031  1.00 42.08           C  
ATOM   4341  C   ARG B  86      37.148 -23.672   4.242  1.00 44.37           C  
ATOM   4342  O   ARG B  86      37.862 -23.136   5.084  1.00 46.18           O  
ATOM   4343  CB  ARG B  86      35.487 -21.934   3.370  1.00 40.08           C  
ATOM   4344  CG  ARG B  86      35.530 -20.774   2.355  1.00 40.49           C  
ATOM   4345  CD  ARG B  86      34.605 -19.581   2.621  1.00 47.22           C  
ATOM   4346  NE  ARG B  86      34.959 -18.384   1.854  1.00 42.21           N  
ATOM   4347  CZ  ARG B  86      34.585 -18.188   0.585  1.00 44.91           C  
ATOM   4348  NH1 ARG B  86      33.854 -19.090  -0.063  1.00 49.81           N  
ATOM   4349  NH2 ARG B  86      34.951 -17.083  -0.066  1.00 41.47           N  
ATOM   4350  N   THR B  87      36.875 -24.975   4.307  1.00 44.47           N  
ATOM   4351  CA  THR B  87      37.382 -25.816   5.380  1.00 45.80           C  
ATOM   4352  C   THR B  87      38.870 -26.082   5.201  1.00 43.73           C  
ATOM   4353  O   THR B  87      39.498 -26.607   6.118  1.00 47.55           O  
ATOM   4354  CB  THR B  87      36.626 -27.154   5.405  1.00 47.28           C  
ATOM   4355  OG1 THR B  87      36.738 -27.666   4.084  1.00 52.72           O  
ATOM   4356  CG2 THR B  87      35.158 -27.032   5.803  1.00 48.80           C  
ATOM   4357  N   THR B  88      39.490 -25.802   4.062  1.00 40.74           N  
ATOM   4358  CA  THR B  88      40.914 -26.025   3.998  1.00 37.51           C  
ATOM   4359  C   THR B  88      41.687 -24.771   4.374  1.00 35.95           C  
ATOM   4360  O   THR B  88      42.917 -24.765   4.315  1.00 37.52           O  
ATOM   4361  CB  THR B  88      41.264 -26.526   2.576  1.00 43.05           C  
ATOM   4362  OG1 THR B  88      40.856 -25.558   1.615  1.00 36.60           O  
ATOM   4363  CG2 THR B  88      40.534 -27.829   2.261  1.00 44.21           C  
ATOM   4364  N   LEU B  89      41.012 -23.706   4.789  1.00 34.42           N  
ATOM   4365  CA  LEU B  89      41.702 -22.470   5.056  1.00 36.95           C  
ATOM   4366  C   LEU B  89      42.578 -22.543   6.304  1.00 37.51           C  
ATOM   4367  O   LEU B  89      42.138 -22.972   7.370  1.00 39.13           O  
ATOM   4368  CB  LEU B  89      40.629 -21.395   5.140  1.00 35.73           C  
ATOM   4369  CG  LEU B  89      41.067 -19.943   5.212  1.00 36.96           C  
ATOM   4370  CD1 LEU B  89      42.037 -19.627   4.088  1.00 30.21           C  
ATOM   4371  CD2 LEU B  89      39.836 -19.067   5.147  1.00 36.72           C  
ATOM   4372  N   ARG B  90      43.839 -22.146   6.180  1.00 36.92           N  
ATOM   4373  CA  ARG B  90      44.814 -22.162   7.246  1.00 39.03           C  
ATOM   4374  C   ARG B  90      45.602 -20.864   7.177  1.00 38.32           C  
ATOM   4375  O   ARG B  90      45.984 -20.436   6.090  1.00 39.82           O  
ATOM   4376  CB  ARG B  90      45.856 -23.268   7.098  1.00 47.60           C  
ATOM   4377  CG  ARG B  90      45.583 -24.776   6.989  1.00 62.89           C  
ATOM   4378  CD  ARG B  90      46.903 -25.619   6.713  1.00 74.55           C  
ATOM   4379  NE  ARG B  90      48.202 -24.958   6.442  1.00 82.11           N  
ATOM   4380  CZ  ARG B  90      48.798 -24.883   5.229  1.00 85.18           C  
ATOM   4381  NH1 ARG B  90      48.251 -25.411   4.128  1.00 79.31           N  
ATOM   4382  NH2 ARG B  90      49.948 -24.213   5.106  1.00 82.47           N  
ATOM   4383  N   ALA B  91      45.848 -20.204   8.308  1.00 37.38           N  
ATOM   4384  CA  ALA B  91      46.731 -19.045   8.374  1.00 36.18           C  
ATOM   4385  C   ALA B  91      48.049 -19.585   8.908  1.00 36.81           C  
ATOM   4386  O   ALA B  91      48.070 -20.267   9.931  1.00 41.08           O  
ATOM   4387  CB  ALA B  91      46.205 -18.015   9.346  1.00 31.02           C  
ATOM   4388  N   GLU B  92      49.173 -19.311   8.273  1.00 38.09           N  
ATOM   4389  CA  GLU B  92      50.445 -19.860   8.676  1.00 37.09           C  
ATOM   4390  C   GLU B  92      51.393 -18.778   9.177  1.00 36.83           C  
ATOM   4391  O   GLU B  92      52.216 -18.207   8.450  1.00 34.32           O  
ATOM   4392  CB  GLU B  92      51.001 -20.609   7.473  1.00 40.06           C  
ATOM   4393  CG  GLU B  92      52.179 -21.507   7.766  1.00 56.33           C  
ATOM   4394  CD  GLU B  92      51.955 -22.481   8.923  1.00 67.51           C  
ATOM   4395  OE1 GLU B  92      50.989 -23.262   8.890  1.00 68.43           O  
ATOM   4396  OE2 GLU B  92      52.766 -22.439   9.855  1.00 70.30           O  
ATOM   4397  N   TRP B  93      51.339 -18.587  10.497  1.00 34.96           N  
ATOM   4398  CA  TRP B  93      52.100 -17.573  11.194  1.00 30.83           C  
ATOM   4399  C   TRP B  93      53.572 -17.606  10.873  1.00 32.19           C  
ATOM   4400  O   TRP B  93      54.163 -16.542  10.669  1.00 31.64           O  
ATOM   4401  CB  TRP B  93      51.913 -17.731  12.700  1.00 31.90           C  
ATOM   4402  CG  TRP B  93      52.683 -16.752  13.604  1.00 33.56           C  
ATOM   4403  CD1 TRP B  93      53.891 -17.100  14.172  1.00 22.89           C  
ATOM   4404  CD2 TRP B  93      52.265 -15.495  13.989  1.00 28.07           C  
ATOM   4405  NE1 TRP B  93      54.223 -16.082  14.915  1.00 26.54           N  
ATOM   4406  CE2 TRP B  93      53.303 -15.107  14.842  1.00 26.84           C  
ATOM   4407  CE3 TRP B  93      51.188 -14.636  13.752  1.00 26.06           C  
ATOM   4408  CZ2 TRP B  93      53.272 -13.867  15.475  1.00 23.25           C  
ATOM   4409  CZ3 TRP B  93      51.160 -13.396  14.387  1.00 27.40           C  
ATOM   4410  CH2 TRP B  93      52.194 -13.011  15.237  1.00 23.05           C  
ATOM   4411  N   LYS B  94      54.218 -18.768  10.768  1.00 34.74           N  
ATOM   4412  CA  LYS B  94      55.644 -18.691  10.498  1.00 36.74           C  
ATOM   4413  C   LYS B  94      55.949 -18.307   9.049  1.00 32.62           C  
ATOM   4414  O   LYS B  94      57.029 -17.772   8.792  1.00 31.49           O  
ATOM   4415  CB  LYS B  94      56.309 -20.029  10.894  1.00 44.51           C  
ATOM   4416  CG  LYS B  94      57.860 -19.960  10.841  1.00 58.27           C  
ATOM   4417  CD  LYS B  94      58.516 -18.674  11.412  1.00 59.73           C  
ATOM   4418  CE  LYS B  94      59.902 -18.540  10.773  1.00 61.53           C  
ATOM   4419  NZ  LYS B  94      60.471 -17.210  10.905  1.00 63.17           N  
ATOM   4420  N   ASN B  95      55.040 -18.475   8.081  1.00 31.52           N  
ATOM   4421  CA  ASN B  95      55.327 -17.988   6.738  1.00 31.56           C  
ATOM   4422  C   ASN B  95      55.328 -16.464   6.826  1.00 29.75           C  
ATOM   4423  O   ASN B  95      56.273 -15.828   6.346  1.00 31.16           O  
ATOM   4424  CB  ASN B  95      54.274 -18.435   5.725  1.00 39.57           C  
ATOM   4425  CG  ASN B  95      54.601 -18.048   4.273  1.00 51.09           C  
ATOM   4426  OD1 ASN B  95      53.838 -18.363   3.368  1.00 59.47           O  
ATOM   4427  ND2 ASN B  95      55.686 -17.391   3.875  1.00 58.04           N  
ATOM   4428  N   LEU B  96      54.352 -15.872   7.520  1.00 24.99           N  
ATOM   4429  CA  LEU B  96      54.344 -14.436   7.729  1.00 24.94           C  
ATOM   4430  C   LEU B  96      55.610 -13.957   8.453  1.00 24.77           C  
ATOM   4431  O   LEU B  96      56.278 -13.037   7.975  1.00 26.09           O  
ATOM   4432  CB  LEU B  96      53.104 -14.064   8.531  1.00 21.58           C  
ATOM   4433  CG  LEU B  96      52.983 -12.606   8.959  1.00 24.41           C  
ATOM   4434  CD1 LEU B  96      52.703 -11.730   7.745  1.00 19.24           C  
ATOM   4435  CD2 LEU B  96      51.895 -12.484  10.003  1.00 15.49           C  
ATOM   4436  N   ILE B  97      56.031 -14.557   9.571  1.00 26.11           N  
ATOM   4437  CA  ILE B  97      57.228 -14.102  10.277  1.00 25.29           C  
ATOM   4438  C   ILE B  97      58.450 -14.238   9.379  1.00 23.99           C  
ATOM   4439  O   ILE B  97      59.240 -13.297   9.312  1.00 21.69           O  
ATOM   4440  CB  ILE B  97      57.388 -14.925  11.613  1.00 28.93           C  
ATOM   4441  CG1 ILE B  97      56.193 -14.661  12.534  1.00 24.25           C  
ATOM   4442  CG2 ILE B  97      58.667 -14.522  12.346  1.00 22.39           C  
ATOM   4443  CD1 ILE B  97      56.074 -13.193  13.000  1.00 26.15           C  
ATOM   4444  N   ALA B  98      58.583 -15.339   8.626  1.00 25.88           N  
ATOM   4445  CA  ALA B  98      59.688 -15.539   7.695  1.00 23.90           C  
ATOM   4446  C   ALA B  98      59.777 -14.459   6.622  1.00 24.71           C  
ATOM   4447  O   ALA B  98      60.862 -13.897   6.418  1.00 24.65           O  
ATOM   4448  CB  ALA B  98      59.537 -16.870   7.003  1.00 22.64           C  
ATOM   4449  N   VAL B  99      58.659 -14.085   5.959  1.00 26.23           N  
ATOM   4450  CA  VAL B  99      58.733 -13.033   4.945  1.00 24.66           C  
ATOM   4451  C   VAL B  99      59.019 -11.693   5.597  1.00 26.61           C  
ATOM   4452  O   VAL B  99      59.801 -10.909   5.051  1.00 28.37           O  
ATOM   4453  CB  VAL B  99      57.428 -12.891   4.082  1.00 25.72           C  
ATOM   4454  CG1 VAL B  99      57.087 -14.288   3.586  1.00 33.25           C  
ATOM   4455  CG2 VAL B  99      56.247 -12.286   4.815  1.00 25.72           C  
ATOM   4456  N   LYS B 100      58.463 -11.429   6.786  1.00 25.44           N  
ATOM   4457  CA  LYS B 100      58.727 -10.206   7.532  1.00 25.38           C  
ATOM   4458  C   LYS B 100      60.224 -10.109   7.835  1.00 24.19           C  
ATOM   4459  O   LYS B 100      60.872  -9.079   7.607  1.00 24.22           O  
ATOM   4460  CB  LYS B 100      57.857 -10.268   8.799  1.00 26.75           C  
ATOM   4461  CG  LYS B 100      57.878  -9.094   9.761  1.00 25.99           C  
ATOM   4462  CD  LYS B 100      59.050  -9.110  10.752  1.00 26.39           C  
ATOM   4463  CE  LYS B 100      58.914 -10.255  11.746  1.00 30.50           C  
ATOM   4464  NZ  LYS B 100      60.102 -10.340  12.571  1.00 27.63           N  
ATOM   4465  N   ASP B 101      60.824 -11.209   8.292  1.00 25.90           N  
ATOM   4466  CA  ASP B 101      62.230 -11.228   8.622  1.00 28.35           C  
ATOM   4467  C   ASP B 101      63.129 -10.884   7.469  1.00 30.57           C  
ATOM   4468  O   ASP B 101      64.098 -10.132   7.650  1.00 32.58           O  
ATOM   4469  CB  ASP B 101      62.633 -12.585   9.143  1.00 31.99           C  
ATOM   4470  CG  ASP B 101      62.246 -12.846  10.583  1.00 35.75           C  
ATOM   4471  OD1 ASP B 101      62.187 -11.903  11.372  1.00 36.08           O  
ATOM   4472  OD2 ASP B 101      62.024 -14.013  10.910  1.00 48.89           O  
ATOM   4473  N   GLU B 102      62.787 -11.426   6.303  1.00 32.91           N  
ATOM   4474  CA  GLU B 102      63.535 -11.177   5.092  1.00 32.95           C  
ATOM   4475  C   GLU B 102      63.360  -9.721   4.701  1.00 31.01           C  
ATOM   4476  O   GLU B 102      64.350  -9.040   4.443  1.00 34.02           O  
ATOM   4477  CB  GLU B 102      63.030 -12.066   3.980  1.00 39.67           C  
ATOM   4478  CG  GLU B 102      64.061 -12.193   2.867  1.00 53.81           C  
ATOM   4479  CD  GLU B 102      63.468 -12.239   1.463  1.00 67.37           C  
ATOM   4480  OE1 GLU B 102      62.507 -12.985   1.239  1.00 73.30           O  
ATOM   4481  OE2 GLU B 102      63.979 -11.517   0.596  1.00 72.04           O  
ATOM   4482  N   ALA B 103      62.138  -9.194   4.709  1.00 27.82           N  
ATOM   4483  CA  ALA B 103      61.900  -7.808   4.353  1.00 28.65           C  
ATOM   4484  C   ALA B 103      62.690  -6.863   5.241  1.00 29.93           C  
ATOM   4485  O   ALA B 103      63.314  -5.923   4.739  1.00 33.64           O  
ATOM   4486  CB  ALA B 103      60.422  -7.457   4.488  1.00 26.48           C  
ATOM   4487  N   VAL B 104      62.763  -7.129   6.554  1.00 29.05           N  
ATOM   4488  CA  VAL B 104      63.510  -6.250   7.454  1.00 29.78           C  
ATOM   4489  C   VAL B 104      65.008  -6.384   7.221  1.00 29.02           C  
ATOM   4490  O   VAL B 104      65.733  -5.386   7.145  1.00 27.81           O  
ATOM   4491  CB  VAL B 104      63.166  -6.575   8.937  1.00 29.49           C  
ATOM   4492  CG1 VAL B 104      63.952  -5.685   9.899  1.00 24.79           C  
ATOM   4493  CG2 VAL B 104      61.697  -6.251   9.189  1.00 24.25           C  
ATOM   4494  N   LEU B 105      65.489  -7.617   7.041  1.00 31.99           N  
ATOM   4495  CA  LEU B 105      66.906  -7.872   6.823  1.00 34.61           C  
ATOM   4496  C   LEU B 105      67.458  -7.112   5.636  1.00 32.19           C  
ATOM   4497  O   LEU B 105      68.508  -6.476   5.732  1.00 34.30           O  
ATOM   4498  CB  LEU B 105      67.138  -9.351   6.612  1.00 35.76           C  
ATOM   4499  CG  LEU B 105      68.569  -9.827   6.547  1.00 38.67           C  
ATOM   4500  CD1 LEU B 105      69.314  -9.447   7.805  1.00 32.13           C  
ATOM   4501  CD2 LEU B 105      68.562 -11.322   6.372  1.00 37.42           C  
ATOM   4502  N   ASN B 106      66.705  -7.086   4.549  1.00 32.55           N  
ATOM   4503  CA  ASN B 106      67.111  -6.368   3.358  1.00 35.13           C  
ATOM   4504  C   ASN B 106      67.211  -4.877   3.612  1.00 35.40           C  
ATOM   4505  O   ASN B 106      68.070  -4.206   3.024  1.00 37.20           O  
ATOM   4506  CB  ASN B 106      66.122  -6.622   2.226  1.00 38.18           C  
ATOM   4507  CG  ASN B 106      66.137  -8.065   1.708  1.00 48.30           C  
ATOM   4508  OD1 ASN B 106      67.073  -8.854   1.893  1.00 53.99           O  
ATOM   4509  ND2 ASN B 106      65.077  -8.493   1.017  1.00 49.91           N  
ATOM   4510  N   ILE B 107      66.410  -4.309   4.519  1.00 35.96           N  
ATOM   4511  CA  ILE B 107      66.496  -2.884   4.827  1.00 35.10           C  
ATOM   4512  C   ILE B 107      67.707  -2.638   5.728  1.00 36.42           C  
ATOM   4513  O   ILE B 107      68.392  -1.622   5.572  1.00 36.76           O  
ATOM   4514  CB  ILE B 107      65.194  -2.408   5.513  1.00 36.42           C  
ATOM   4515  CG1 ILE B 107      63.988  -2.697   4.631  1.00 38.47           C  
ATOM   4516  CG2 ILE B 107      65.253  -0.911   5.732  1.00 32.84           C  
ATOM   4517  CD1 ILE B 107      62.619  -2.432   5.298  1.00 45.27           C  
ATOM   4518  N   ASN B 108      68.037  -3.556   6.644  1.00 36.79           N  
ATOM   4519  CA  ASN B 108      69.239  -3.446   7.471  1.00 37.30           C  
ATOM   4520  C   ASN B 108      70.459  -3.455   6.550  1.00 37.87           C  
ATOM   4521  O   ASN B 108      71.260  -2.517   6.569  1.00 37.62           O  
ATOM   4522  CB  ASN B 108      69.385  -4.623   8.444  1.00 33.71           C  
ATOM   4523  CG  ASN B 108      68.317  -4.743   9.518  1.00 30.27           C  
ATOM   4524  OD1 ASN B 108      67.806  -5.837   9.789  1.00 26.73           O  
ATOM   4525  ND2 ASN B 108      67.947  -3.669  10.193  1.00 33.31           N  
ATOM   4526  N   LYS B 109      70.583  -4.462   5.670  1.00 37.52           N  
ATOM   4527  CA  LYS B 109      71.662  -4.571   4.680  1.00 39.53           C  
ATOM   4528  C   LYS B 109      71.825  -3.326   3.834  1.00 38.80           C  
ATOM   4529  O   LYS B 109      72.937  -2.848   3.614  1.00 41.85           O  
ATOM   4530  CB  LYS B 109      71.414  -5.731   3.728  1.00 40.00           C  
ATOM   4531  CG  LYS B 109      71.736  -7.082   4.328  1.00 48.24           C  
ATOM   4532  CD  LYS B 109      71.123  -8.189   3.491  1.00 51.95           C  
ATOM   4533  CE  LYS B 109      71.745  -9.500   3.953  1.00 62.65           C  
ATOM   4534  NZ  LYS B 109      71.029 -10.654   3.434  1.00 72.13           N  
ATOM   4535  N   SER B 110      70.694  -2.806   3.369  1.00 40.11           N  
ATOM   4536  CA  SER B 110      70.637  -1.587   2.600  1.00 40.86           C  
ATOM   4537  C   SER B 110      71.347  -0.472   3.361  1.00 41.50           C  
ATOM   4538  O   SER B 110      72.268   0.164   2.830  1.00 45.69           O  
ATOM   4539  CB  SER B 110      69.159  -1.316   2.367  1.00 42.58           C  
ATOM   4540  OG  SER B 110      68.791  -0.044   1.856  1.00 60.43           O  
ATOM   4541  N   TYR B 111      71.024  -0.292   4.643  1.00 40.92           N  
ATOM   4542  CA  TYR B 111      71.632   0.764   5.425  1.00 41.34           C  
ATOM   4543  C   TYR B 111      73.127   0.557   5.582  1.00 43.02           C  
ATOM   4544  O   TYR B 111      73.887   1.528   5.526  1.00 40.81           O  
ATOM   4545  CB  TYR B 111      70.942   0.845   6.792  1.00 40.30           C  
ATOM   4546  CG  TYR B 111      69.632   1.616   6.740  1.00 36.79           C  
ATOM   4547  CD1 TYR B 111      69.633   2.938   6.281  1.00 39.63           C  
ATOM   4548  CD2 TYR B 111      68.435   1.014   7.136  1.00 36.17           C  
ATOM   4549  CE1 TYR B 111      68.440   3.659   6.217  1.00 41.83           C  
ATOM   4550  CE2 TYR B 111      67.238   1.735   7.074  1.00 36.38           C  
ATOM   4551  CZ  TYR B 111      67.249   3.052   6.615  1.00 39.07           C  
ATOM   4552  OH  TYR B 111      66.076   3.777   6.536  1.00 45.83           O  
ATOM   4553  N   ASP B 112      73.583  -0.690   5.701  1.00 46.22           N  
ATOM   4554  CA  ASP B 112      75.002  -0.972   5.787  1.00 51.77           C  
ATOM   4555  C   ASP B 112      75.709  -0.478   4.538  1.00 53.45           C  
ATOM   4556  O   ASP B 112      76.705   0.242   4.640  1.00 51.32           O  
ATOM   4557  CB  ASP B 112      75.255  -2.475   5.938  1.00 60.37           C  
ATOM   4558  CG  ASP B 112      76.734  -2.867   5.956  1.00 67.84           C  
ATOM   4559  OD1 ASP B 112      77.534  -2.215   6.642  1.00 74.37           O  
ATOM   4560  OD2 ASP B 112      77.080  -3.828   5.266  1.00 77.61           O  
ATOM   4561  N   GLU B 113      75.202  -0.813   3.353  1.00 56.75           N  
ATOM   4562  CA  GLU B 113      75.798  -0.348   2.115  1.00 60.47           C  
ATOM   4563  C   GLU B 113      75.869   1.159   2.090  1.00 61.10           C  
ATOM   4564  O   GLU B 113      76.914   1.703   1.739  1.00 64.30           O  
ATOM   4565  CB  GLU B 113      74.997  -0.805   0.935  1.00 61.62           C  
ATOM   4566  CG  GLU B 113      75.278  -2.269   0.677  1.00 74.69           C  
ATOM   4567  CD  GLU B 113      74.177  -3.044  -0.040  1.00 81.00           C  
ATOM   4568  OE1 GLU B 113      73.249  -2.458  -0.610  1.00 86.61           O  
ATOM   4569  OE2 GLU B 113      74.257  -4.272  -0.014  1.00 85.17           O  
ATOM   4570  N   MET B 114      74.818   1.842   2.541  1.00 61.54           N  
ATOM   4571  CA  MET B 114      74.804   3.289   2.588  1.00 63.24           C  
ATOM   4572  C   MET B 114      76.011   3.824   3.353  1.00 64.69           C  
ATOM   4573  O   MET B 114      76.604   4.810   2.917  1.00 65.81           O  
ATOM   4574  CB  MET B 114      73.524   3.774   3.254  1.00 63.33           C  
ATOM   4575  CG  MET B 114      73.437   5.292   3.274  1.00 65.47           C  
ATOM   4576  SD  MET B 114      72.158   5.936   4.375  1.00 68.07           S  
ATOM   4577  CE  MET B 114      73.116   6.262   5.828  1.00 67.89           C  
ATOM   4578  N   PHE B 115      76.431   3.213   4.460  1.00 67.05           N  
ATOM   4579  CA  PHE B 115      77.631   3.679   5.140  1.00 70.92           C  
ATOM   4580  C   PHE B 115      78.873   3.342   4.329  1.00 73.55           C  
ATOM   4581  O   PHE B 115      79.656   4.238   4.039  1.00 73.12           O  
ATOM   4582  CB  PHE B 115      77.751   3.050   6.528  1.00 68.52           C  
ATOM   4583  CG  PHE B 115      76.765   3.687   7.486  1.00 62.55           C  
ATOM   4584  CD1 PHE B 115      77.046   4.938   8.039  1.00 55.72           C  
ATOM   4585  CD2 PHE B 115      75.563   3.038   7.770  1.00 57.06           C  
ATOM   4586  CE1 PHE B 115      76.118   5.541   8.879  1.00 52.50           C  
ATOM   4587  CE2 PHE B 115      74.640   3.649   8.613  1.00 56.74           C  
ATOM   4588  CZ  PHE B 115      74.915   4.898   9.162  1.00 56.69           C  
ATOM   4589  N   ARG B 116      79.009   2.092   3.855  1.00 76.45           N  
ATOM   4590  CA  ARG B 116      80.158   1.625   3.075  1.00 78.97           C  
ATOM   4591  C   ARG B 116      80.404   2.431   1.813  1.00 80.33           C  
ATOM   4592  O   ARG B 116      81.488   2.349   1.233  1.00 81.40           O  
ATOM   4593  CB  ARG B 116      79.998   0.168   2.624  1.00 76.02           C  
ATOM   4594  CG  ARG B 116      80.061  -0.857   3.741  1.00 80.39           C  
ATOM   4595  CD  ARG B 116      79.586  -2.241   3.303  1.00 83.28           C  
ATOM   4596  NE  ARG B 116      80.556  -2.995   2.510  1.00 92.87           N  
ATOM   4597  CZ  ARG B 116      80.485  -3.070   1.169  1.00 97.22           C  
ATOM   4598  NH1 ARG B 116      79.483  -2.433   0.525  1.00 97.92           N  
ATOM   4599  NH2 ARG B 116      81.451  -3.732   0.491  1.00 91.38           N  
ATOM   4600  N   ASP B 117      79.404   3.171   1.340  1.00 80.68           N  
ATOM   4601  CA  ASP B 117      79.537   3.917   0.111  1.00 82.12           C  
ATOM   4602  C   ASP B 117      79.462   5.436   0.265  1.00 82.66           C  
ATOM   4603  O   ASP B 117      79.885   6.136  -0.665  1.00 83.72           O  
ATOM   4604  CB  ASP B 117      78.459   3.418  -0.861  1.00 83.41           C  
ATOM   4605  CG  ASP B 117      78.406   1.896  -1.082  1.00 92.20           C  
ATOM   4606  OD1 ASP B 117      79.426   1.205  -0.969  1.00 93.14           O  
ATOM   4607  OD2 ASP B 117      77.318   1.392  -1.363  1.00 99.76           O  
ATOM   4608  N   THR B 118      78.953   6.057   1.370  1.00 83.79           N  
ATOM   4609  CA  THR B 118      78.912   7.481   1.458  1.00 84.80           C  
ATOM   4610  C   THR B 118      80.104   7.970   2.272  1.00 85.54           C  
ATOM   4611  O   THR B 118      80.195   7.787   3.482  1.00 85.60           O  
ATOM   4612  CB  THR B 118      77.546   7.794   2.082  1.00 83.91           C  
ATOM   4613  OG1 THR B 118      76.547   7.379   1.143  1.00 88.55           O  
ATOM   4614  CG2 THR B 118      77.339   9.254   2.381  1.00 84.57           C  
ATOM   4615  N   GLU B 119      81.003   8.744   1.672  1.00 86.40           N  
ATOM   4616  CA  GLU B 119      82.176   9.228   2.363  1.00 86.42           C  
ATOM   4617  C   GLU B 119      81.853  10.262   3.383  1.00 84.84           C  
ATOM   4618  O   GLU B 119      80.955  11.066   3.202  1.00 84.10           O  
ATOM   4619  CB  GLU B 119      83.246   9.635   1.300  1.00 90.01           C  
ATOM   4620  CG  GLU B 119      83.265  11.142   0.841  1.00 93.42           C  
ATOM   4621  CD  GLU B 119      84.543  11.643   0.347  1.00 95.36           C  
ATOM   4622  OE1 GLU B 119      85.690  11.116   0.596  1.00 95.78           O  
ATOM   4623  OE2 GLU B 119      84.475  12.561  -0.488  1.00 95.14           O  
ATOM   4624  N   GLY B 120      82.568  10.187   4.486  1.00 82.43           N  
ATOM   4625  CA  GLY B 120      82.350  11.103   5.596  1.00 80.22           C  
ATOM   4626  C   GLY B 120      81.279  10.652   6.651  1.00 78.45           C  
ATOM   4627  O   GLY B 120      80.926  11.445   7.626  1.00 76.77           O  
ATOM   4628  N   LEU B 121      80.761   9.421   6.470  1.00 76.94           N  
ATOM   4629  CA  LEU B 121      79.668   8.890   7.295  1.00 73.25           C  
ATOM   4630  C   LEU B 121      80.176   7.591   7.904  1.00 71.53           C  
ATOM   4631  O   LEU B 121      80.416   6.643   7.154  1.00 71.77           O  
ATOM   4632  CB  LEU B 121      78.486   8.654   6.361  1.00 71.11           C  
ATOM   4633  CG  LEU B 121      77.129   8.288   6.887  1.00 64.16           C  
ATOM   4634  CD1 LEU B 121      76.574   9.437   7.697  1.00 64.46           C  
ATOM   4635  CD2 LEU B 121      76.222   7.962   5.721  1.00 66.48           C  
ATOM   4636  N   GLU B 122      80.410   7.495   9.214  1.00 69.34           N  
ATOM   4637  CA  GLU B 122      80.953   6.275   9.797  1.00 67.17           C  
ATOM   4638  C   GLU B 122      80.067   5.676  10.873  1.00 62.91           C  
ATOM   4639  O   GLU B 122      79.596   6.393  11.756  1.00 60.95           O  
ATOM   4640  CB  GLU B 122      82.344   6.587  10.355  1.00 73.37           C  
ATOM   4641  CG  GLU B 122      83.396   6.596   9.242  1.00 84.46           C  
ATOM   4642  CD  GLU B 122      84.706   7.263   9.618  1.00 87.66           C  
ATOM   4643  OE1 GLU B 122      85.462   6.688  10.401  1.00 97.02           O  
ATOM   4644  OE2 GLU B 122      84.966   8.360   9.119  1.00 93.86           O  
ATOM   4645  N   PHE B 123      79.794   4.375  10.780  1.00 59.15           N  
ATOM   4646  CA  PHE B 123      78.970   3.674  11.749  1.00 56.39           C  
ATOM   4647  C   PHE B 123      79.863   3.016  12.785  1.00 56.27           C  
ATOM   4648  O   PHE B 123      80.857   2.398  12.396  1.00 56.05           O  
ATOM   4649  CB  PHE B 123      78.140   2.600  11.045  1.00 51.20           C  
ATOM   4650  CG  PHE B 123      77.264   1.761  11.975  1.00 49.33           C  
ATOM   4651  CD1 PHE B 123      76.156   2.337  12.604  1.00 44.21           C  
ATOM   4652  CD2 PHE B 123      77.579   0.416  12.215  1.00 45.18           C  
ATOM   4653  CE1 PHE B 123      75.371   1.565  13.462  1.00 42.13           C  
ATOM   4654  CE2 PHE B 123      76.785  -0.342  13.076  1.00 40.39           C  
ATOM   4655  CZ  PHE B 123      75.684   0.229  13.702  1.00 41.93           C  
ATOM   4656  N   PHE B 124      79.534   3.094  14.072  1.00 56.80           N  
ATOM   4657  CA  PHE B 124      80.268   2.412  15.129  1.00 57.19           C  
ATOM   4658  C   PHE B 124      79.287   1.529  15.884  1.00 56.14           C  
ATOM   4659  O   PHE B 124      78.240   2.006  16.342  1.00 59.33           O  
ATOM   4660  CB  PHE B 124      80.886   3.412  16.105  1.00 58.95           C  
ATOM   4661  CG  PHE B 124      81.975   4.240  15.448  1.00 57.97           C  
ATOM   4662  CD1 PHE B 124      83.238   3.677  15.240  1.00 58.29           C  
ATOM   4663  CD2 PHE B 124      81.705   5.542  15.027  1.00 56.54           C  
ATOM   4664  CE1 PHE B 124      84.229   4.422  14.607  1.00 54.64           C  
ATOM   4665  CE2 PHE B 124      82.707   6.276  14.395  1.00 55.60           C  
ATOM   4666  CZ  PHE B 124      83.965   5.722  14.182  1.00 56.81           C  
ATOM   4667  N   LEU B 125      79.577   0.228  15.968  1.00 53.36           N  
ATOM   4668  CA  LEU B 125      78.721  -0.708  16.683  1.00 50.50           C  
ATOM   4669  C   LEU B 125      79.015  -0.629  18.175  1.00 50.22           C  
ATOM   4670  O   LEU B 125      80.181  -0.693  18.575  1.00 51.49           O  
ATOM   4671  CB  LEU B 125      78.966  -2.142  16.201  1.00 45.62           C  
ATOM   4672  CG  LEU B 125      77.953  -3.177  16.687  1.00 44.56           C  
ATOM   4673  CD1 LEU B 125      76.662  -2.979  15.922  1.00 52.49           C  
ATOM   4674  CD2 LEU B 125      78.441  -4.585  16.444  1.00 46.62           C  
ATOM   4675  N   GLY B 126      77.986  -0.457  18.992  1.00 49.69           N  
ATOM   4676  CA  GLY B 126      78.143  -0.439  20.432  1.00 49.13           C  
ATOM   4677  C   GLY B 126      77.135   0.485  21.080  1.00 49.38           C  
ATOM   4678  O   GLY B 126      76.142   0.889  20.473  1.00 53.45           O  
ATOM   4679  N   TRP B 127      77.386   0.846  22.329  1.00 48.16           N  
ATOM   4680  CA  TRP B 127      76.511   1.718  23.090  1.00 47.99           C  
ATOM   4681  C   TRP B 127      77.197   3.055  23.276  1.00 48.20           C  
ATOM   4682  O   TRP B 127      78.304   3.101  23.811  1.00 50.52           O  
ATOM   4683  CB  TRP B 127      76.213   1.087  24.449  1.00 43.10           C  
ATOM   4684  CG  TRP B 127      75.441  -0.212  24.304  1.00 40.48           C  
ATOM   4685  CD1 TRP B 127      76.053  -1.380  23.931  1.00 37.97           C  
ATOM   4686  CD2 TRP B 127      74.096  -0.353  24.484  1.00 35.91           C  
ATOM   4687  NE1 TRP B 127      75.088  -2.264  23.871  1.00 43.64           N  
ATOM   4688  CE2 TRP B 127      73.912  -1.708  24.191  1.00 36.04           C  
ATOM   4689  CE3 TRP B 127      73.024   0.458  24.844  1.00 42.02           C  
ATOM   4690  CZ2 TRP B 127      72.643  -2.274  24.246  1.00 35.19           C  
ATOM   4691  CZ3 TRP B 127      71.748  -0.108  24.901  1.00 39.09           C  
ATOM   4692  CH2 TRP B 127      71.562  -1.465  24.606  1.00 39.29           C  
ATOM   4693  N   GLY B 128      76.625   4.142  22.781  1.00 47.53           N  
ATOM   4694  CA  GLY B 128      77.232   5.444  22.952  1.00 47.27           C  
ATOM   4695  C   GLY B 128      76.754   6.066  24.249  1.00 50.79           C  
ATOM   4696  O   GLY B 128      75.624   5.802  24.672  1.00 51.90           O  
ATOM   4697  N   SER B 129      77.592   6.884  24.870  1.00 53.68           N  
ATOM   4698  CA  SER B 129      77.263   7.619  26.075  1.00 52.81           C  
ATOM   4699  C   SER B 129      78.183   8.820  26.153  1.00 54.30           C  
ATOM   4700  O   SER B 129      79.244   8.854  25.515  1.00 52.75           O  
ATOM   4701  CB  SER B 129      77.451   6.742  27.308  1.00 53.82           C  
ATOM   4702  OG  SER B 129      78.693   6.046  27.364  1.00 60.17           O  
ATOM   4703  N   LEU B 130      77.764   9.846  26.877  1.00 56.36           N  
ATOM   4704  CA  LEU B 130      78.545  11.051  27.008  1.00 59.93           C  
ATOM   4705  C   LEU B 130      79.632  10.920  28.055  1.00 64.55           C  
ATOM   4706  O   LEU B 130      79.337  10.548  29.186  1.00 65.02           O  
ATOM   4707  CB  LEU B 130      77.619  12.196  27.365  1.00 59.30           C  
ATOM   4708  CG  LEU B 130      76.525  12.523  26.362  1.00 57.18           C  
ATOM   4709  CD1 LEU B 130      75.788  13.754  26.836  1.00 55.34           C  
ATOM   4710  CD2 LEU B 130      77.113  12.790  24.992  1.00 56.53           C  
ATOM   4711  N   GLU B 131      80.886  11.160  27.646  1.00 68.08           N  
ATOM   4712  CA  GLU B 131      82.014  11.224  28.565  1.00 70.33           C  
ATOM   4713  C   GLU B 131      82.054  12.672  29.024  1.00 70.55           C  
ATOM   4714  O   GLU B 131      82.320  12.962  30.187  1.00 71.68           O  
ATOM   4715  CB  GLU B 131      83.351  10.927  27.904  1.00 73.17           C  
ATOM   4716  CG  GLU B 131      84.389  10.523  28.950  1.00 82.34           C  
ATOM   4717  CD  GLU B 131      85.804  10.424  28.392  1.00 82.04           C  
ATOM   4718  OE1 GLU B 131      86.137   9.444  27.726  1.00 83.08           O  
ATOM   4719  OE2 GLU B 131      86.588  11.340  28.620  1.00 86.00           O  
ATOM   4720  N   SER B 132      81.833  13.613  28.115  1.00 70.99           N  
ATOM   4721  CA  SER B 132      81.772  15.024  28.446  1.00 71.23           C  
ATOM   4722  C   SER B 132      81.057  15.691  27.282  1.00 71.16           C  
ATOM   4723  O   SER B 132      80.721  15.023  26.298  1.00 70.94           O  
ATOM   4724  CB  SER B 132      83.182  15.615  28.585  1.00 74.36           C  
ATOM   4725  OG  SER B 132      83.893  15.784  27.346  1.00 78.40           O  
ATOM   4726  N   LYS B 133      80.921  17.021  27.325  1.00 69.59           N  
ATOM   4727  CA  LYS B 133      80.303  17.789  26.253  1.00 69.21           C  
ATOM   4728  C   LYS B 133      80.844  17.478  24.868  1.00 68.95           C  
ATOM   4729  O   LYS B 133      80.078  17.543  23.919  1.00 69.10           O  
ATOM   4730  CB  LYS B 133      80.486  19.285  26.459  1.00 70.01           C  
ATOM   4731  CG  LYS B 133      79.950  19.735  27.790  1.00 78.48           C  
ATOM   4732  CD  LYS B 133      80.043  21.237  27.975  1.00 80.66           C  
ATOM   4733  CE  LYS B 133      79.715  21.549  29.441  1.00 89.39           C  
ATOM   4734  NZ  LYS B 133      78.360  21.170  29.814  1.00 89.91           N  
ATOM   4735  N   ASN B 134      82.125  17.109  24.727  1.00 68.94           N  
ATOM   4736  CA  ASN B 134      82.706  16.914  23.402  1.00 65.83           C  
ATOM   4737  C   ASN B 134      83.230  15.527  23.143  1.00 62.25           C  
ATOM   4738  O   ASN B 134      83.856  15.273  22.107  1.00 62.64           O  
ATOM   4739  CB  ASN B 134      83.854  17.889  23.169  1.00 68.11           C  
ATOM   4740  CG  ASN B 134      83.387  19.330  23.072  1.00 74.80           C  
ATOM   4741  OD1 ASN B 134      83.448  20.080  24.053  1.00 77.65           O  
ATOM   4742  ND2 ASN B 134      82.903  19.791  21.921  1.00 72.41           N  
ATOM   4743  N   VAL B 135      83.025  14.591  24.060  1.00 60.33           N  
ATOM   4744  CA  VAL B 135      83.548  13.248  23.873  1.00 59.16           C  
ATOM   4745  C   VAL B 135      82.442  12.250  24.136  1.00 58.10           C  
ATOM   4746  O   VAL B 135      81.777  12.285  25.180  1.00 54.77           O  
ATOM   4747  CB  VAL B 135      84.712  12.937  24.841  1.00 60.84           C  
ATOM   4748  CG1 VAL B 135      85.258  11.557  24.500  1.00 56.43           C  
ATOM   4749  CG2 VAL B 135      85.826  13.971  24.734  1.00 65.50           C  
ATOM   4750  N   VAL B 136      82.283  11.354  23.173  1.00 57.36           N  
ATOM   4751  CA  VAL B 136      81.305  10.284  23.221  1.00 56.01           C  
ATOM   4752  C   VAL B 136      82.079   8.972  23.235  1.00 53.83           C  
ATOM   4753  O   VAL B 136      83.048   8.793  22.491  1.00 51.48           O  
ATOM   4754  CB  VAL B 136      80.379  10.364  21.977  1.00 54.74           C  
ATOM   4755  CG1 VAL B 136      79.420   9.187  21.939  1.00 57.73           C  
ATOM   4756  CG2 VAL B 136      79.572  11.652  22.032  1.00 52.49           C  
ATOM   4757  N   ASN B 137      81.702   8.034  24.086  1.00 54.44           N  
ATOM   4758  CA  ASN B 137      82.379   6.751  24.105  1.00 56.96           C  
ATOM   4759  C   ASN B 137      81.466   5.697  23.549  1.00 55.32           C  
ATOM   4760  O   ASN B 137      80.249   5.770  23.723  1.00 58.67           O  
ATOM   4761  CB  ASN B 137      82.754   6.290  25.501  1.00 62.27           C  
ATOM   4762  CG  ASN B 137      83.752   7.187  26.199  1.00 64.73           C  
ATOM   4763  OD1 ASN B 137      83.397   7.904  27.131  1.00 64.03           O  
ATOM   4764  ND2 ASN B 137      85.021   7.179  25.782  1.00 66.18           N  
ATOM   4765  N   VAL B 138      82.053   4.750  22.834  1.00 54.19           N  
ATOM   4766  CA  VAL B 138      81.326   3.626  22.283  1.00 51.97           C  
ATOM   4767  C   VAL B 138      81.815   2.525  23.203  1.00 52.80           C  
ATOM   4768  O   VAL B 138      82.982   2.138  23.142  1.00 54.77           O  
ATOM   4769  CB  VAL B 138      81.747   3.355  20.811  1.00 49.82           C  
ATOM   4770  CG1 VAL B 138      80.931   2.219  20.224  1.00 43.91           C  
ATOM   4771  CG2 VAL B 138      81.515   4.590  19.970  1.00 44.33           C  
ATOM   4772  N   ARG B 139      81.020   2.143  24.186  1.00 54.92           N  
ATOM   4773  CA  ARG B 139      81.366   1.036  25.048  1.00 57.08           C  
ATOM   4774  C   ARG B 139      80.760  -0.221  24.465  1.00 56.79           C  
ATOM   4775  O   ARG B 139      80.095  -0.191  23.432  1.00 57.80           O  
ATOM   4776  CB  ARG B 139      80.843   1.266  26.469  1.00 58.99           C  
ATOM   4777  CG  ARG B 139      81.818   2.147  27.216  1.00 68.87           C  
ATOM   4778  CD  ARG B 139      81.505   2.292  28.691  1.00 71.35           C  
ATOM   4779  NE  ARG B 139      82.641   2.972  29.293  1.00 81.58           N  
ATOM   4780  CZ  ARG B 139      82.541   3.983  30.165  1.00 88.80           C  
ATOM   4781  NH1 ARG B 139      81.373   4.477  30.584  1.00 93.73           N  
ATOM   4782  NH2 ARG B 139      83.661   4.548  30.607  1.00 91.22           N  
ATOM   4783  N   GLU B 140      80.898  -1.339  25.150  1.00 59.58           N  
ATOM   4784  CA  GLU B 140      80.505  -2.624  24.610  1.00 63.39           C  
ATOM   4785  C   GLU B 140      79.246  -3.193  25.265  1.00 64.84           C  
ATOM   4786  O   GLU B 140      78.759  -4.278  24.947  1.00 64.96           O  
ATOM   4787  CB  GLU B 140      81.744  -3.473  24.799  1.00 68.01           C  
ATOM   4788  CG  GLU B 140      81.940  -4.749  24.011  1.00 75.40           C  
ATOM   4789  CD  GLU B 140      83.292  -5.361  24.351  1.00 84.75           C  
ATOM   4790  OE1 GLU B 140      83.376  -6.105  25.333  1.00 86.76           O  
ATOM   4791  OE2 GLU B 140      84.261  -5.077  23.643  1.00 81.76           O  
ATOM   4792  N   SER B 141      78.683  -2.457  26.211  1.00 65.22           N  
ATOM   4793  CA  SER B 141      77.498  -2.870  26.939  1.00 67.49           C  
ATOM   4794  C   SER B 141      76.908  -1.584  27.485  1.00 68.65           C  
ATOM   4795  O   SER B 141      77.562  -0.541  27.487  1.00 69.68           O  
ATOM   4796  CB  SER B 141      77.906  -3.824  28.071  1.00 68.53           C  
ATOM   4797  OG  SER B 141      76.951  -3.986  29.120  1.00 79.44           O  
ATOM   4798  N   ALA B 142      75.664  -1.694  27.934  1.00 69.51           N  
ATOM   4799  CA  ALA B 142      74.941  -0.573  28.491  1.00 71.43           C  
ATOM   4800  C   ALA B 142      75.549  -0.136  29.818  1.00 73.66           C  
ATOM   4801  O   ALA B 142      75.400   1.015  30.230  1.00 73.26           O  
ATOM   4802  CB  ALA B 142      73.487  -0.979  28.694  1.00 70.54           C  
ATOM   4803  N   ASP B 143      76.238  -1.067  30.499  1.00 76.19           N  
ATOM   4804  CA  ASP B 143      76.883  -0.780  31.769  1.00 78.77           C  
ATOM   4805  C   ASP B 143      78.084   0.130  31.558  1.00 79.36           C  
ATOM   4806  O   ASP B 143      79.049  -0.305  30.917  1.00 78.50           O  
ATOM   4807  CB  ASP B 143      77.343  -2.092  32.438  1.00 79.38           C  
ATOM   4808  CG  ASP B 143      78.166  -1.939  33.722  1.00 80.90           C  
ATOM   4809  OD1 ASP B 143      77.853  -1.080  34.551  1.00 83.90           O  
ATOM   4810  OD2 ASP B 143      79.131  -2.686  33.889  1.00 81.88           O  
ATOM   4811  N   PRO B 144      78.138   1.322  32.176  1.00 80.58           N  
ATOM   4812  CA  PRO B 144      79.222   2.297  32.026  1.00 81.04           C  
ATOM   4813  C   PRO B 144      80.609   1.910  32.544  1.00 81.19           C  
ATOM   4814  O   PRO B 144      81.442   2.759  32.863  1.00 81.14           O  
ATOM   4815  CB  PRO B 144      78.649   3.539  32.695  1.00 81.15           C  
ATOM   4816  CG  PRO B 144      77.759   2.974  33.778  1.00 83.25           C  
ATOM   4817  CD  PRO B 144      77.065   1.866  33.009  1.00 81.17           C  
ATOM   4818  N   ALA B 145      80.860   0.621  32.690  1.00 81.63           N  
ATOM   4819  CA  ALA B 145      82.140   0.130  33.126  1.00 82.70           C  
ATOM   4820  C   ALA B 145      82.615  -0.869  32.085  1.00 83.63           C  
ATOM   4821  O   ALA B 145      83.625  -1.541  32.300  1.00 85.97           O  
ATOM   4822  CB  ALA B 145      81.974  -0.552  34.480  1.00 85.51           C  
ATOM   4823  N   SER B 146      81.916  -1.063  30.967  1.00 83.03           N  
ATOM   4824  CA  SER B 146      82.413  -2.006  29.992  1.00 81.89           C  
ATOM   4825  C   SER B 146      83.539  -1.378  29.175  1.00 82.25           C  
ATOM   4826  O   SER B 146      83.734  -0.156  29.146  1.00 84.00           O  
ATOM   4827  CB  SER B 146      81.255  -2.448  29.112  1.00 80.60           C  
ATOM   4828  OG  SER B 146      80.595  -1.408  28.407  1.00 76.51           O  
ATOM   4829  N   ALA B 147      84.306  -2.243  28.514  1.00 81.46           N  
ATOM   4830  CA  ALA B 147      85.424  -1.824  27.685  1.00 80.94           C  
ATOM   4831  C   ALA B 147      85.067  -0.781  26.635  1.00 79.36           C  
ATOM   4832  O   ALA B 147      84.174  -1.000  25.808  1.00 81.16           O  
ATOM   4833  CB  ALA B 147      86.004  -3.033  26.968  1.00 81.86           C  
ATOM   4834  N   VAL B 148      85.738   0.368  26.702  1.00 77.38           N  
ATOM   4835  CA  VAL B 148      85.540   1.419  25.724  1.00 76.70           C  
ATOM   4836  C   VAL B 148      86.183   0.901  24.447  1.00 77.71           C  
ATOM   4837  O   VAL B 148      87.386   0.641  24.375  1.00 78.87           O  
ATOM   4838  CB  VAL B 148      86.215   2.734  26.167  1.00 73.28           C  
ATOM   4839  CG1 VAL B 148      85.978   3.811  25.127  1.00 74.79           C  
ATOM   4840  CG2 VAL B 148      85.612   3.227  27.465  1.00 73.41           C  
ATOM   4841  N   LYS B 149      85.285   0.685  23.498  1.00 77.40           N  
ATOM   4842  CA  LYS B 149      85.587   0.185  22.179  1.00 75.47           C  
ATOM   4843  C   LYS B 149      86.131   1.340  21.331  1.00 76.10           C  
ATOM   4844  O   LYS B 149      87.123   1.169  20.625  1.00 77.79           O  
ATOM   4845  CB  LYS B 149      84.275  -0.402  21.682  1.00 71.66           C  
ATOM   4846  CG  LYS B 149      84.306  -1.387  20.547  1.00 72.08           C  
ATOM   4847  CD  LYS B 149      82.902  -1.980  20.427  1.00 70.94           C  
ATOM   4848  CE  LYS B 149      82.800  -2.895  19.214  1.00 76.16           C  
ATOM   4849  NZ  LYS B 149      82.855  -2.131  17.978  1.00 75.94           N  
ATOM   4850  N   GLU B 150      85.538   2.538  21.349  1.00 75.35           N  
ATOM   4851  CA  GLU B 150      86.029   3.685  20.585  1.00 76.57           C  
ATOM   4852  C   GLU B 150      85.804   4.936  21.426  1.00 77.21           C  
ATOM   4853  O   GLU B 150      84.912   4.935  22.279  1.00 78.64           O  
ATOM   4854  CB  GLU B 150      85.261   3.882  19.275  1.00 80.10           C  
ATOM   4855  CG  GLU B 150      85.303   2.826  18.160  1.00 85.06           C  
ATOM   4856  CD  GLU B 150      86.506   2.832  17.211  1.00 85.25           C  
ATOM   4857  OE1 GLU B 150      87.260   3.810  17.171  1.00 87.02           O  
ATOM   4858  OE2 GLU B 150      86.674   1.845  16.489  1.00 89.81           O  
ATOM   4859  N   ARG B 151      86.566   6.015  21.261  1.00 78.36           N  
ATOM   4860  CA  ARG B 151      86.366   7.273  21.982  1.00 78.24           C  
ATOM   4861  C   ARG B 151      86.306   8.283  20.845  1.00 78.27           C  
ATOM   4862  O   ARG B 151      87.235   8.341  20.034  1.00 79.78           O  
ATOM   4863  CB  ARG B 151      87.554   7.583  22.895  1.00 78.29           C  
ATOM   4864  CG  ARG B 151      87.298   8.767  23.811  1.00 76.67           C  
ATOM   4865  CD  ARG B 151      88.542   9.196  24.581  1.00 75.91           C  
ATOM   4866  NE  ARG B 151      88.889  10.578  24.269  1.00 74.09           N  
ATOM   4867  CZ  ARG B 151      89.060  11.512  25.213  1.00 76.65           C  
ATOM   4868  NH1 ARG B 151      88.922  11.225  26.510  1.00 78.61           N  
ATOM   4869  NH2 ARG B 151      89.367  12.762  24.856  1.00 74.91           N  
ATOM   4870  N   LEU B 152      85.219   9.039  20.737  1.00 76.23           N  
ATOM   4871  CA  LEU B 152      85.001   9.950  19.627  1.00 72.83           C  
ATOM   4872  C   LEU B 152      84.924  11.384  20.108  1.00 71.81           C  
ATOM   4873  O   LEU B 152      84.094  11.725  20.953  1.00 72.20           O  
ATOM   4874  CB  LEU B 152      83.693   9.591  18.915  1.00 70.80           C  
ATOM   4875  CG  LEU B 152      83.519   8.457  17.892  1.00 69.03           C  
ATOM   4876  CD1 LEU B 152      84.123   7.148  18.337  1.00 67.24           C  
ATOM   4877  CD2 LEU B 152      82.029   8.248  17.718  1.00 65.22           C  
ATOM   4878  N   GLU B 153      85.805  12.240  19.609  1.00 71.56           N  
ATOM   4879  CA  GLU B 153      85.756  13.646  19.955  1.00 72.76           C  
ATOM   4880  C   GLU B 153      85.061  14.377  18.829  1.00 71.12           C  
ATOM   4881  O   GLU B 153      85.491  14.343  17.658  1.00 73.00           O  
ATOM   4882  CB  GLU B 153      87.145  14.232  20.119  1.00 78.35           C  
ATOM   4883  CG  GLU B 153      87.830  13.748  21.384  1.00 87.93           C  
ATOM   4884  CD  GLU B 153      89.222  14.317  21.601  1.00 92.27           C  
ATOM   4885  OE1 GLU B 153      89.394  15.533  21.496  1.00 87.26           O  
ATOM   4886  OE2 GLU B 153      90.128  13.535  21.887  1.00 96.57           O  
ATOM   4887  N   THR B 154      84.028  15.100  19.196  1.00 69.55           N  
ATOM   4888  CA  THR B 154      83.223  15.776  18.221  1.00 66.98           C  
ATOM   4889  C   THR B 154      82.929  17.214  18.603  1.00 66.44           C  
ATOM   4890  O   THR B 154      82.973  17.676  19.749  1.00 66.01           O  
ATOM   4891  CB  THR B 154      81.933  14.935  18.042  1.00 64.76           C  
ATOM   4892  OG1 THR B 154      81.211  15.501  16.951  1.00 64.75           O  
ATOM   4893  CG2 THR B 154      81.082  14.891  19.299  1.00 63.42           C  
ATOM   4894  N   GLU B 155      82.667  17.906  17.511  1.00 67.30           N  
ATOM   4895  CA  GLU B 155      82.280  19.287  17.524  1.00 67.34           C  
ATOM   4896  C   GLU B 155      80.778  19.383  17.785  1.00 64.52           C  
ATOM   4897  O   GLU B 155      80.309  20.494  18.050  1.00 64.46           O  
ATOM   4898  CB  GLU B 155      82.683  19.887  16.165  1.00 76.43           C  
ATOM   4899  CG  GLU B 155      82.301  21.340  15.826  1.00 86.92           C  
ATOM   4900  CD  GLU B 155      82.954  22.476  16.615  1.00 92.97           C  
ATOM   4901  OE1 GLU B 155      83.768  22.232  17.512  1.00 96.44           O  
ATOM   4902  OE2 GLU B 155      82.642  23.630  16.310  1.00 99.97           O  
ATOM   4903  N   HIS B 156      79.945  18.338  17.696  1.00 59.98           N  
ATOM   4904  CA  HIS B 156      78.508  18.413  17.979  1.00 54.04           C  
ATOM   4905  C   HIS B 156      77.989  17.027  18.302  1.00 51.25           C  
ATOM   4906  O   HIS B 156      78.500  16.035  17.761  1.00 51.60           O  
ATOM   4907  CB  HIS B 156      77.671  18.904  16.788  1.00 53.83           C  
ATOM   4908  CG  HIS B 156      77.992  20.302  16.295  1.00 52.50           C  
ATOM   4909  ND1 HIS B 156      77.652  21.464  16.832  1.00 54.47           N  
ATOM   4910  CD2 HIS B 156      78.778  20.569  15.202  1.00 51.83           C  
ATOM   4911  CE1 HIS B 156      78.195  22.418  16.123  1.00 53.25           C  
ATOM   4912  NE2 HIS B 156      78.873  21.868  15.143  1.00 51.92           N  
ATOM   4913  N   ILE B 157      76.969  16.911  19.147  1.00 50.23           N  
ATOM   4914  CA  ILE B 157      76.354  15.621  19.460  1.00 48.21           C  
ATOM   4915  C   ILE B 157      74.844  15.714  19.256  1.00 45.72           C  
ATOM   4916  O   ILE B 157      74.219  16.725  19.603  1.00 43.07           O  
ATOM   4917  CB  ILE B 157      76.643  15.203  20.934  1.00 52.16           C  
ATOM   4918  CG1 ILE B 157      78.138  15.088  21.148  1.00 53.15           C  
ATOM   4919  CG2 ILE B 157      76.021  13.839  21.248  1.00 52.31           C  
ATOM   4920  CD1 ILE B 157      78.576  15.130  22.612  1.00 56.14           C  
ATOM   4921  N   LEU B 158      74.262  14.680  18.650  1.00 44.15           N  
ATOM   4922  CA  LEU B 158      72.824  14.573  18.508  1.00 41.92           C  
ATOM   4923  C   LEU B 158      72.421  13.275  19.193  1.00 39.35           C  
ATOM   4924  O   LEU B 158      73.014  12.211  18.980  1.00 37.52           O  
ATOM   4925  CB  LEU B 158      72.402  14.534  17.022  1.00 40.19           C  
ATOM   4926  CG  LEU B 158      70.906  14.354  16.682  1.00 35.59           C  
ATOM   4927  CD1 LEU B 158      70.094  15.539  17.138  1.00 28.35           C  
ATOM   4928  CD2 LEU B 158      70.733  14.264  15.194  1.00 37.69           C  
ATOM   4929  N   LEU B 159      71.428  13.376  20.064  1.00 38.64           N  
ATOM   4930  CA  LEU B 159      70.890  12.238  20.784  1.00 37.51           C  
ATOM   4931  C   LEU B 159      69.637  11.836  20.023  1.00 35.72           C  
ATOM   4932  O   LEU B 159      68.764  12.675  19.755  1.00 35.25           O  
ATOM   4933  CB  LEU B 159      70.537  12.651  22.209  1.00 36.64           C  
ATOM   4934  CG  LEU B 159      71.586  13.431  23.007  1.00 33.90           C  
ATOM   4935  CD1 LEU B 159      70.938  13.983  24.263  1.00 27.78           C  
ATOM   4936  CD2 LEU B 159      72.782  12.538  23.301  1.00 28.59           C  
ATOM   4937  N   ALA B 160      69.556  10.569  19.646  1.00 33.56           N  
ATOM   4938  CA  ALA B 160      68.424  10.056  18.901  1.00 31.64           C  
ATOM   4939  C   ALA B 160      68.175   8.600  19.292  1.00 29.98           C  
ATOM   4940  O   ALA B 160      67.910   7.739  18.450  1.00 34.33           O  
ATOM   4941  CB  ALA B 160      68.748  10.184  17.417  1.00 29.03           C  
ATOM   4942  N   SER B 161      68.193   8.330  20.603  1.00 29.82           N  
ATOM   4943  CA  SER B 161      68.078   6.978  21.162  1.00 26.90           C  
ATOM   4944  C   SER B 161      66.699   6.338  21.166  1.00 24.63           C  
ATOM   4945  O   SER B 161      66.558   5.134  21.368  1.00 26.32           O  
ATOM   4946  CB  SER B 161      68.628   6.981  22.597  1.00 25.78           C  
ATOM   4947  OG  SER B 161      68.445   8.237  23.249  1.00 23.77           O  
ATOM   4948  N   GLY B 162      65.677   7.152  20.906  1.00 20.98           N  
ATOM   4949  CA  GLY B 162      64.317   6.669  20.834  1.00 21.39           C  
ATOM   4950  C   GLY B 162      63.660   6.414  22.173  1.00 24.06           C  
ATOM   4951  O   GLY B 162      63.887   7.121  23.167  1.00 24.37           O  
ATOM   4952  N   SER B 163      62.768   5.439  22.167  1.00 23.53           N  
ATOM   4953  CA  SER B 163      62.054   5.068  23.358  1.00 20.91           C  
ATOM   4954  C   SER B 163      62.106   3.558  23.508  1.00 20.09           C  
ATOM   4955  O   SER B 163      62.693   2.859  22.678  1.00 19.53           O  
ATOM   4956  CB  SER B 163      60.606   5.613  23.260  1.00 21.87           C  
ATOM   4957  OG  SER B 163      59.915   5.251  22.078  1.00 27.56           O  
ATOM   4958  N   TRP B 164      61.511   3.023  24.566  1.00 18.38           N  
ATOM   4959  CA  TRP B 164      61.562   1.602  24.840  1.00 17.53           C  
ATOM   4960  C   TRP B 164      60.258   1.256  25.549  1.00 16.36           C  
ATOM   4961  O   TRP B 164      59.694   2.168  26.171  1.00 18.16           O  
ATOM   4962  CB  TRP B 164      62.805   1.380  25.706  1.00 20.98           C  
ATOM   4963  CG  TRP B 164      63.220  -0.080  25.820  1.00 28.88           C  
ATOM   4964  CD1 TRP B 164      63.076  -0.764  27.000  1.00 33.80           C  
ATOM   4965  CD2 TRP B 164      63.734  -0.859  24.813  1.00 31.37           C  
ATOM   4966  NE1 TRP B 164      63.487  -1.976  26.742  1.00 32.44           N  
ATOM   4967  CE2 TRP B 164      63.887  -2.087  25.466  1.00 28.75           C  
ATOM   4968  CE3 TRP B 164      64.078  -0.725  23.464  1.00 29.18           C  
ATOM   4969  CZ2 TRP B 164      64.393  -3.197  24.792  1.00 28.37           C  
ATOM   4970  CZ3 TRP B 164      64.584  -1.837  22.792  1.00 29.65           C  
ATOM   4971  CH2 TRP B 164      64.737  -3.064  23.448  1.00 28.55           C  
ATOM   4972  N   PRO B 165      59.669   0.050  25.510  1.00 17.21           N  
ATOM   4973  CA  PRO B 165      58.402  -0.249  26.170  1.00 19.28           C  
ATOM   4974  C   PRO B 165      58.461  -0.018  27.675  1.00 20.95           C  
ATOM   4975  O   PRO B 165      59.516  -0.206  28.274  1.00 23.19           O  
ATOM   4976  CB  PRO B 165      58.132  -1.686  25.821  1.00 18.03           C  
ATOM   4977  CG  PRO B 165      58.970  -1.958  24.607  1.00 14.52           C  
ATOM   4978  CD  PRO B 165      60.206  -1.154  24.887  1.00 14.16           C  
ATOM   4979  N   HIS B 166      57.379   0.370  28.337  1.00 23.47           N  
ATOM   4980  CA  HIS B 166      57.391   0.516  29.782  1.00 23.28           C  
ATOM   4981  C   HIS B 166      56.668  -0.687  30.357  1.00 24.58           C  
ATOM   4982  O   HIS B 166      55.482  -0.872  30.084  1.00 25.97           O  
ATOM   4983  CB  HIS B 166      56.677   1.795  30.187  1.00 24.15           C  
ATOM   4984  CG  HIS B 166      56.416   1.898  31.683  1.00 25.64           C  
ATOM   4985  ND1 HIS B 166      57.246   2.079  32.701  1.00 24.85           N  
ATOM   4986  CD2 HIS B 166      55.156   1.816  32.211  1.00 26.82           C  
ATOM   4987  CE1 HIS B 166      56.546   2.117  33.799  1.00 22.49           C  
ATOM   4988  NE2 HIS B 166      55.301   1.954  33.493  1.00 28.70           N  
ATOM   4989  N   MET B 167      57.362  -1.513  31.139  1.00 26.67           N  
ATOM   4990  CA  MET B 167      56.755  -2.671  31.795  1.00 29.37           C  
ATOM   4991  C   MET B 167      56.369  -2.282  33.214  1.00 26.89           C  
ATOM   4992  O   MET B 167      57.188  -1.663  33.907  1.00 29.01           O  
ATOM   4993  CB  MET B 167      57.741  -3.835  31.841  1.00 30.10           C  
ATOM   4994  CG  MET B 167      58.120  -4.377  30.465  1.00 30.72           C  
ATOM   4995  SD  MET B 167      56.748  -5.204  29.622  1.00 30.04           S  
ATOM   4996  CE  MET B 167      56.454  -3.952  28.426  1.00 37.11           C  
ATOM   4997  N   PRO B 168      55.152  -2.488  33.707  1.00 25.40           N  
ATOM   4998  CA  PRO B 168      54.765  -2.178  35.075  1.00 26.60           C  
ATOM   4999  C   PRO B 168      55.421  -3.102  36.107  1.00 27.40           C  
ATOM   5000  O   PRO B 168      55.678  -4.272  35.843  1.00 26.71           O  
ATOM   5001  CB  PRO B 168      53.264  -2.273  35.019  1.00 24.14           C  
ATOM   5002  CG  PRO B 168      53.056  -3.377  34.025  1.00 24.59           C  
ATOM   5003  CD  PRO B 168      54.011  -2.951  32.931  1.00 28.31           C  
ATOM   5004  N   ASN B 169      55.677  -2.617  37.313  1.00 28.64           N  
ATOM   5005  CA  ASN B 169      56.321  -3.409  38.354  1.00 28.85           C  
ATOM   5006  C   ASN B 169      55.192  -4.133  39.055  1.00 27.69           C  
ATOM   5007  O   ASN B 169      54.567  -3.608  39.971  1.00 29.98           O  
ATOM   5008  CB  ASN B 169      57.074  -2.503  39.340  1.00 31.98           C  
ATOM   5009  CG  ASN B 169      57.636  -3.238  40.548  1.00 32.24           C  
ATOM   5010  OD1 ASN B 169      58.426  -4.168  40.405  1.00 33.18           O  
ATOM   5011  ND2 ASN B 169      57.287  -2.840  41.756  1.00 34.59           N  
ATOM   5012  N   ILE B 170      54.750  -5.250  38.513  1.00 25.89           N  
ATOM   5013  CA  ILE B 170      53.727  -6.034  39.166  1.00 24.60           C  
ATOM   5014  C   ILE B 170      54.355  -7.394  39.378  1.00 27.06           C  
ATOM   5015  O   ILE B 170      55.325  -7.748  38.684  1.00 27.31           O  
ATOM   5016  CB  ILE B 170      52.440  -6.196  38.312  1.00 20.24           C  
ATOM   5017  CG1 ILE B 170      52.709  -6.857  36.977  1.00 18.29           C  
ATOM   5018  CG2 ILE B 170      51.820  -4.822  38.175  1.00 20.51           C  
ATOM   5019  CD1 ILE B 170      51.420  -7.460  36.404  1.00 22.30           C  
ATOM   5020  N   PRO B 171      53.885  -8.196  40.335  1.00 27.94           N  
ATOM   5021  CA  PRO B 171      54.308  -9.576  40.471  1.00 30.01           C  
ATOM   5022  C   PRO B 171      54.042 -10.427  39.231  1.00 31.78           C  
ATOM   5023  O   PRO B 171      52.917 -10.525  38.733  1.00 33.36           O  
ATOM   5024  CB  PRO B 171      53.582 -10.031  41.721  1.00 32.04           C  
ATOM   5025  CG  PRO B 171      52.433  -9.073  41.886  1.00 31.03           C  
ATOM   5026  CD  PRO B 171      53.020  -7.771  41.426  1.00 25.91           C  
ATOM   5027  N   GLY B 172      55.131 -10.981  38.691  1.00 31.24           N  
ATOM   5028  CA  GLY B 172      55.049 -11.860  37.538  1.00 31.82           C  
ATOM   5029  C   GLY B 172      55.270 -11.202  36.180  1.00 32.88           C  
ATOM   5030  O   GLY B 172      55.143 -11.875  35.151  1.00 32.61           O  
ATOM   5031  N   ILE B 173      55.723  -9.946  36.137  1.00 32.37           N  
ATOM   5032  CA  ILE B 173      55.973  -9.240  34.892  1.00 32.74           C  
ATOM   5033  C   ILE B 173      57.037  -9.921  34.030  1.00 34.71           C  
ATOM   5034  O   ILE B 173      57.137  -9.635  32.838  1.00 37.13           O  
ATOM   5035  CB  ILE B 173      56.360  -7.756  35.240  1.00 35.08           C  
ATOM   5036  CG1 ILE B 173      56.320  -6.894  33.973  1.00 28.07           C  
ATOM   5037  CG2 ILE B 173      57.756  -7.678  35.855  1.00 32.43           C  
ATOM   5038  CD1 ILE B 173      54.915  -6.764  33.354  1.00 24.36           C  
ATOM   5039  N   GLU B 174      57.823 -10.866  34.573  1.00 36.04           N  
ATOM   5040  CA  GLU B 174      58.797 -11.603  33.772  1.00 36.24           C  
ATOM   5041  C   GLU B 174      58.139 -12.689  32.922  1.00 34.26           C  
ATOM   5042  O   GLU B 174      58.789 -13.359  32.123  1.00 35.23           O  
ATOM   5043  CB  GLU B 174      59.873 -12.250  34.668  1.00 44.50           C  
ATOM   5044  CG  GLU B 174      59.507 -13.375  35.653  1.00 53.75           C  
ATOM   5045  CD  GLU B 174      58.858 -12.952  36.966  1.00 60.39           C  
ATOM   5046  OE1 GLU B 174      58.968 -11.786  37.364  1.00 64.07           O  
ATOM   5047  OE2 GLU B 174      58.246 -13.817  37.596  1.00 63.59           O  
ATOM   5048  N   HIS B 175      56.846 -12.947  33.132  1.00 34.12           N  
ATOM   5049  CA  HIS B 175      56.079 -13.877  32.312  1.00 33.99           C  
ATOM   5050  C   HIS B 175      55.323 -13.170  31.193  1.00 33.65           C  
ATOM   5051  O   HIS B 175      54.539 -13.795  30.482  1.00 35.05           O  
ATOM   5052  CB  HIS B 175      55.070 -14.614  33.160  1.00 37.16           C  
ATOM   5053  CG  HIS B 175      55.748 -15.346  34.287  1.00 41.34           C  
ATOM   5054  ND1 HIS B 175      56.817 -16.137  34.237  1.00 38.45           N  
ATOM   5055  CD2 HIS B 175      55.334 -15.237  35.584  1.00 37.90           C  
ATOM   5056  CE1 HIS B 175      57.078 -16.511  35.456  1.00 39.56           C  
ATOM   5057  NE2 HIS B 175      56.181 -15.966  36.249  1.00 42.63           N  
ATOM   5058  N   CYS B 176      55.551 -11.869  31.056  1.00 32.87           N  
ATOM   5059  CA  CYS B 176      54.911 -11.017  30.076  1.00 30.16           C  
ATOM   5060  C   CYS B 176      55.911 -10.613  29.002  1.00 30.18           C  
ATOM   5061  O   CYS B 176      57.120 -10.725  29.213  1.00 31.01           O  
ATOM   5062  CB  CYS B 176      54.386  -9.796  30.791  1.00 27.75           C  
ATOM   5063  SG  CYS B 176      53.193 -10.237  32.071  1.00 26.36           S  
ATOM   5064  N   ILE B 177      55.452 -10.212  27.813  1.00 28.55           N  
ATOM   5065  CA  ILE B 177      56.356  -9.716  26.777  1.00 23.65           C  
ATOM   5066  C   ILE B 177      55.932  -8.304  26.443  1.00 19.69           C  
ATOM   5067  O   ILE B 177      54.899  -7.843  26.937  1.00 20.72           O  
ATOM   5068  CB  ILE B 177      56.291 -10.560  25.469  1.00 26.60           C  
ATOM   5069  CG1 ILE B 177      54.880 -10.591  24.894  1.00 22.32           C  
ATOM   5070  CG2 ILE B 177      56.769 -11.971  25.775  1.00 28.98           C  
ATOM   5071  CD1 ILE B 177      54.833 -11.031  23.429  1.00 20.37           C  
ATOM   5072  N   SER B 178      56.750  -7.606  25.663  1.00 20.25           N  
ATOM   5073  CA  SER B 178      56.379  -6.328  25.077  1.00 21.73           C  
ATOM   5074  C   SER B 178      56.102  -6.565  23.583  1.00 22.27           C  
ATOM   5075  O   SER B 178      56.148  -7.708  23.104  1.00 24.20           O  
ATOM   5076  CB  SER B 178      57.522  -5.343  25.240  1.00 17.22           C  
ATOM   5077  OG  SER B 178      58.712  -5.775  24.576  1.00 22.52           O  
ATOM   5078  N   SER B 179      55.918  -5.512  22.785  1.00 23.77           N  
ATOM   5079  CA  SER B 179      55.697  -5.646  21.358  1.00 22.62           C  
ATOM   5080  C   SER B 179      56.953  -6.164  20.682  1.00 21.68           C  
ATOM   5081  O   SER B 179      56.866  -6.963  19.759  1.00 28.69           O  
ATOM   5082  CB  SER B 179      55.295  -4.304  20.787  1.00 20.33           C  
ATOM   5083  OG  SER B 179      56.200  -3.283  21.151  1.00 18.14           O  
ATOM   5084  N   ASN B 180      58.149  -5.814  21.175  1.00 23.27           N  
ATOM   5085  CA  ASN B 180      59.419  -6.328  20.657  1.00 20.21           C  
ATOM   5086  C   ASN B 180      59.470  -7.842  20.482  1.00 20.38           C  
ATOM   5087  O   ASN B 180      59.782  -8.349  19.406  1.00 22.89           O  
ATOM   5088  CB  ASN B 180      60.562  -5.964  21.572  1.00 19.56           C  
ATOM   5089  CG  ASN B 180      61.001  -4.515  21.560  1.00 24.09           C  
ATOM   5090  OD1 ASN B 180      61.419  -3.988  22.580  1.00 30.60           O  
ATOM   5091  ND2 ASN B 180      60.915  -3.765  20.475  1.00 28.98           N  
ATOM   5092  N   GLU B 181      59.126  -8.594  21.520  1.00 17.51           N  
ATOM   5093  CA  GLU B 181      59.149 -10.031  21.405  1.00 16.63           C  
ATOM   5094  C   GLU B 181      57.970 -10.479  20.596  1.00 18.40           C  
ATOM   5095  O   GLU B 181      58.088 -11.537  19.988  1.00 22.65           O  
ATOM   5096  CB  GLU B 181      59.045 -10.761  22.732  1.00 18.37           C  
ATOM   5097  CG  GLU B 181      60.178 -10.485  23.701  1.00 24.69           C  
ATOM   5098  CD  GLU B 181      60.167  -9.126  24.393  1.00 33.50           C  
ATOM   5099  OE1 GLU B 181      59.148  -8.457  24.398  1.00 37.98           O  
ATOM   5100  OE2 GLU B 181      61.186  -8.723  24.937  1.00 43.46           O  
ATOM   5101  N   ALA B 182      56.832  -9.769  20.541  1.00 17.05           N  
ATOM   5102  CA  ALA B 182      55.708 -10.192  19.724  1.00 13.82           C  
ATOM   5103  C   ALA B 182      56.099 -10.347  18.244  1.00 17.25           C  
ATOM   5104  O   ALA B 182      55.542 -11.176  17.531  1.00 15.62           O  
ATOM   5105  CB  ALA B 182      54.603  -9.174  19.849  1.00 12.25           C  
ATOM   5106  N   PHE B 183      57.113  -9.625  17.756  1.00 20.18           N  
ATOM   5107  CA  PHE B 183      57.595  -9.746  16.383  1.00 21.46           C  
ATOM   5108  C   PHE B 183      58.386 -11.016  16.126  1.00 25.81           C  
ATOM   5109  O   PHE B 183      58.730 -11.321  14.981  1.00 25.35           O  
ATOM   5110  CB  PHE B 183      58.499  -8.567  15.996  1.00 17.95           C  
ATOM   5111  CG  PHE B 183      57.690  -7.299  15.776  1.00 23.04           C  
ATOM   5112  CD1 PHE B 183      56.798  -7.220  14.703  1.00 22.51           C  
ATOM   5113  CD2 PHE B 183      57.810  -6.220  16.660  1.00 26.78           C  
ATOM   5114  CE1 PHE B 183      56.031  -6.064  14.520  1.00 21.64           C  
ATOM   5115  CE2 PHE B 183      57.038  -5.071  16.466  1.00 23.74           C  
ATOM   5116  CZ  PHE B 183      56.150  -4.991  15.398  1.00 23.37           C  
ATOM   5117  N   TYR B 184      58.720 -11.798  17.147  1.00 25.93           N  
ATOM   5118  CA  TYR B 184      59.564 -12.953  16.952  1.00 23.45           C  
ATOM   5119  C   TYR B 184      58.910 -14.216  17.449  1.00 22.82           C  
ATOM   5120  O   TYR B 184      59.529 -15.280  17.399  1.00 28.66           O  
ATOM   5121  CB  TYR B 184      60.900 -12.672  17.652  1.00 22.87           C  
ATOM   5122  CG  TYR B 184      61.642 -11.553  16.928  1.00 24.16           C  
ATOM   5123  CD1 TYR B 184      62.309 -11.832  15.732  1.00 24.33           C  
ATOM   5124  CD2 TYR B 184      61.597 -10.238  17.398  1.00 23.44           C  
ATOM   5125  CE1 TYR B 184      62.911 -10.804  15.005  1.00 26.38           C  
ATOM   5126  CE2 TYR B 184      62.202  -9.206  16.671  1.00 24.21           C  
ATOM   5127  CZ  TYR B 184      62.852  -9.497  15.476  1.00 22.48           C  
ATOM   5128  OH  TYR B 184      63.438  -8.491  14.733  1.00 22.01           O  
ATOM   5129  N   LEU B 185      57.641 -14.159  17.854  1.00 20.06           N  
ATOM   5130  CA  LEU B 185      56.972 -15.329  18.385  1.00 24.59           C  
ATOM   5131  C   LEU B 185      57.044 -16.467  17.392  1.00 29.34           C  
ATOM   5132  O   LEU B 185      56.777 -16.264  16.211  1.00 33.97           O  
ATOM   5133  CB  LEU B 185      55.503 -15.087  18.679  1.00 22.47           C  
ATOM   5134  CG  LEU B 185      55.089 -14.081  19.730  1.00 25.72           C  
ATOM   5135  CD1 LEU B 185      53.582 -13.978  19.694  1.00 27.35           C  
ATOM   5136  CD2 LEU B 185      55.544 -14.504  21.115  1.00 22.62           C  
ATOM   5137  N   PRO B 186      57.451 -17.658  17.814  1.00 33.28           N  
ATOM   5138  CA  PRO B 186      57.554 -18.838  16.964  1.00 34.50           C  
ATOM   5139  C   PRO B 186      56.219 -19.356  16.457  1.00 32.90           C  
ATOM   5140  O   PRO B 186      56.166 -19.958  15.388  1.00 33.36           O  
ATOM   5141  CB  PRO B 186      58.289 -19.842  17.823  1.00 37.38           C  
ATOM   5142  CG  PRO B 186      59.045 -18.967  18.798  1.00 40.03           C  
ATOM   5143  CD  PRO B 186      58.014 -17.916  19.131  1.00 32.65           C  
ATOM   5144  N   GLU B 187      55.143 -19.220  17.228  1.00 34.08           N  
ATOM   5145  CA  GLU B 187      53.831 -19.632  16.772  1.00 35.91           C  
ATOM   5146  C   GLU B 187      52.734 -18.798  17.431  1.00 36.25           C  
ATOM   5147  O   GLU B 187      53.031 -18.134  18.442  1.00 34.74           O  
ATOM   5148  CB  GLU B 187      53.676 -21.130  17.043  1.00 40.52           C  
ATOM   5149  CG  GLU B 187      53.939 -21.794  18.376  1.00 64.23           C  
ATOM   5150  CD  GLU B 187      54.101 -23.304  18.159  1.00 78.44           C  
ATOM   5151  OE1 GLU B 187      53.104 -23.986  17.886  1.00 89.77           O  
ATOM   5152  OE2 GLU B 187      55.233 -23.797  18.242  1.00 92.01           O  
ATOM   5153  N   PRO B 188      51.511 -18.671  16.855  1.00 33.84           N  
ATOM   5154  CA  PRO B 188      50.505 -17.727  17.315  1.00 33.02           C  
ATOM   5155  C   PRO B 188      49.859 -18.216  18.612  1.00 32.22           C  
ATOM   5156  O   PRO B 188      49.519 -19.392  18.714  1.00 35.18           O  
ATOM   5157  CB  PRO B 188      49.552 -17.615  16.132  1.00 29.54           C  
ATOM   5158  CG  PRO B 188      49.529 -19.005  15.560  1.00 27.14           C  
ATOM   5159  CD  PRO B 188      50.990 -19.425  15.709  1.00 28.98           C  
ATOM   5160  N   PRO B 189      49.682 -17.396  19.655  1.00 31.97           N  
ATOM   5161  CA  PRO B 189      49.074 -17.799  20.920  1.00 30.28           C  
ATOM   5162  C   PRO B 189      47.644 -18.253  20.732  1.00 31.73           C  
ATOM   5163  O   PRO B 189      46.974 -17.742  19.839  1.00 33.55           O  
ATOM   5164  CB  PRO B 189      49.160 -16.589  21.796  1.00 31.19           C  
ATOM   5165  CG  PRO B 189      50.340 -15.855  21.202  1.00 38.44           C  
ATOM   5166  CD  PRO B 189      50.131 -16.012  19.714  1.00 33.89           C  
ATOM   5167  N   ARG B 190      47.168 -19.206  21.535  1.00 31.68           N  
ATOM   5168  CA  ARG B 190      45.775 -19.599  21.484  1.00 28.97           C  
ATOM   5169  C   ARG B 190      44.968 -18.577  22.289  1.00 29.22           C  
ATOM   5170  O   ARG B 190      43.924 -18.118  21.837  1.00 31.18           O  
ATOM   5171  CB  ARG B 190      45.611 -20.981  22.079  1.00 30.62           C  
ATOM   5172  CG  ARG B 190      44.199 -21.518  21.903  1.00 44.14           C  
ATOM   5173  CD  ARG B 190      44.052 -22.881  22.560  1.00 53.14           C  
ATOM   5174  NE  ARG B 190      43.569 -22.779  23.929  1.00 60.15           N  
ATOM   5175  CZ  ARG B 190      42.274 -22.959  24.230  1.00 60.34           C  
ATOM   5176  NH1 ARG B 190      41.360 -23.240  23.303  1.00 63.12           N  
ATOM   5177  NH2 ARG B 190      41.873 -22.856  25.491  1.00 64.53           N  
ATOM   5178  N   ARG B 191      45.382 -18.193  23.496  1.00 25.64           N  
ATOM   5179  CA  ARG B 191      44.641 -17.202  24.269  1.00 22.82           C  
ATOM   5180  C   ARG B 191      45.682 -16.134  24.496  1.00 22.96           C  
ATOM   5181  O   ARG B 191      46.737 -16.456  25.052  1.00 23.68           O  
ATOM   5182  CB  ARG B 191      44.179 -17.764  25.609  1.00 22.77           C  
ATOM   5183  CG  ARG B 191      43.392 -19.045  25.417  1.00 32.58           C  
ATOM   5184  CD  ARG B 191      42.765 -19.629  26.673  1.00 41.14           C  
ATOM   5185  NE  ARG B 191      43.635 -20.015  27.792  1.00 52.92           N  
ATOM   5186  CZ  ARG B 191      44.558 -20.992  27.788  1.00 49.44           C  
ATOM   5187  NH1 ARG B 191      44.833 -21.719  26.712  1.00 55.23           N  
ATOM   5188  NH2 ARG B 191      45.256 -21.227  28.896  1.00 46.94           N  
ATOM   5189  N   VAL B 192      45.518 -14.909  24.025  1.00 21.94           N  
ATOM   5190  CA  VAL B 192      46.492 -13.857  24.252  1.00 21.16           C  
ATOM   5191  C   VAL B 192      45.757 -12.679  24.858  1.00 18.74           C  
ATOM   5192  O   VAL B 192      44.593 -12.420  24.533  1.00 20.97           O  
ATOM   5193  CB  VAL B 192      47.212 -13.475  22.903  1.00 21.58           C  
ATOM   5194  CG1 VAL B 192      46.220 -13.194  21.813  1.00 28.37           C  
ATOM   5195  CG2 VAL B 192      48.047 -12.217  23.087  1.00 26.84           C  
ATOM   5196  N   LEU B 193      46.394 -12.053  25.845  1.00 19.12           N  
ATOM   5197  CA  LEU B 193      45.891 -10.858  26.505  1.00 19.08           C  
ATOM   5198  C   LEU B 193      46.857  -9.780  26.078  1.00 18.79           C  
ATOM   5199  O   LEU B 193      48.071  -9.934  26.249  1.00 16.27           O  
ATOM   5200  CB  LEU B 193      45.946 -10.918  28.045  1.00 13.71           C  
ATOM   5201  CG  LEU B 193      45.583  -9.673  28.844  1.00 10.05           C  
ATOM   5202  CD1 LEU B 193      44.094  -9.420  28.712  1.00 10.29           C  
ATOM   5203  CD2 LEU B 193      45.975  -9.851  30.295  1.00 13.14           C  
ATOM   5204  N   THR B 194      46.305  -8.703  25.549  1.00 18.51           N  
ATOM   5205  CA  THR B 194      47.098  -7.574  25.134  1.00 21.09           C  
ATOM   5206  C   THR B 194      46.638  -6.482  26.097  1.00 16.18           C  
ATOM   5207  O   THR B 194      45.446  -6.230  26.278  1.00 18.96           O  
ATOM   5208  CB  THR B 194      46.767  -7.431  23.599  1.00 19.82           C  
ATOM   5209  OG1 THR B 194      47.935  -6.845  23.064  1.00 31.33           O  
ATOM   5210  CG2 THR B 194      45.596  -6.590  23.216  1.00 11.20           C  
ATOM   5211  N   VAL B 195      47.577  -5.912  26.840  1.00 15.21           N  
ATOM   5212  CA  VAL B 195      47.275  -4.969  27.896  1.00 15.11           C  
ATOM   5213  C   VAL B 195      47.568  -3.574  27.406  1.00 12.66           C  
ATOM   5214  O   VAL B 195      48.710  -3.255  27.073  1.00 16.54           O  
ATOM   5215  CB  VAL B 195      48.138  -5.259  29.164  1.00 15.70           C  
ATOM   5216  CG1 VAL B 195      47.612  -4.422  30.293  1.00 11.13           C  
ATOM   5217  CG2 VAL B 195      48.098  -6.716  29.561  1.00 13.67           C  
ATOM   5218  N   GLY B 196      46.587  -2.697  27.439  1.00 10.47           N  
ATOM   5219  CA  GLY B 196      46.787  -1.337  26.990  1.00 11.56           C  
ATOM   5220  C   GLY B 196      45.661  -0.948  26.050  1.00 14.74           C  
ATOM   5221  O   GLY B 196      44.990  -1.791  25.451  1.00 14.55           O  
ATOM   5222  N   GLY B 197      45.439   0.349  25.890  1.00 13.23           N  
ATOM   5223  CA  GLY B 197      44.380   0.797  25.006  1.00 15.66           C  
ATOM   5224  C   GLY B 197      44.907   1.627  23.849  1.00 15.23           C  
ATOM   5225  O   GLY B 197      44.097   2.223  23.151  1.00 17.61           O  
ATOM   5226  N   GLY B 198      46.217   1.768  23.656  1.00 15.95           N  
ATOM   5227  CA  GLY B 198      46.767   2.564  22.577  1.00 14.73           C  
ATOM   5228  C   GLY B 198      46.887   1.789  21.289  1.00 15.95           C  
ATOM   5229  O   GLY B 198      46.604   0.595  21.236  1.00 17.81           O  
ATOM   5230  N   PHE B 199      47.427   2.458  20.272  1.00 18.00           N  
ATOM   5231  CA  PHE B 199      47.515   1.889  18.931  1.00 15.80           C  
ATOM   5232  C   PHE B 199      48.272   0.579  18.884  1.00 15.57           C  
ATOM   5233  O   PHE B 199      47.771  -0.328  18.231  1.00 15.06           O  
ATOM   5234  CB  PHE B 199      48.163   2.909  17.951  1.00 13.29           C  
ATOM   5235  CG  PHE B 199      49.679   3.123  17.947  1.00 12.32           C  
ATOM   5236  CD1 PHE B 199      50.290   3.994  18.852  1.00 18.82           C  
ATOM   5237  CD2 PHE B 199      50.464   2.466  17.005  1.00  9.93           C  
ATOM   5238  CE1 PHE B 199      51.672   4.204  18.808  1.00 17.50           C  
ATOM   5239  CE2 PHE B 199      51.840   2.683  16.972  1.00 12.94           C  
ATOM   5240  CZ  PHE B 199      52.451   3.550  17.868  1.00 17.03           C  
ATOM   5241  N   ILE B 200      49.386   0.387  19.597  1.00 13.21           N  
ATOM   5242  CA  ILE B 200      50.133  -0.871  19.531  1.00 15.12           C  
ATOM   5243  C   ILE B 200      49.301  -2.044  20.037  1.00 15.53           C  
ATOM   5244  O   ILE B 200      49.294  -3.128  19.445  1.00 19.08           O  
ATOM   5245  CB  ILE B 200      51.443  -0.724  20.348  1.00 13.44           C  
ATOM   5246  CG1 ILE B 200      52.332   0.311  19.700  1.00 16.21           C  
ATOM   5247  CG2 ILE B 200      52.215  -2.024  20.379  1.00 18.18           C  
ATOM   5248  CD1 ILE B 200      53.548   0.758  20.531  1.00 20.66           C  
ATOM   5249  N   SER B 201      48.538  -1.834  21.106  1.00 19.45           N  
ATOM   5250  CA  SER B 201      47.681  -2.865  21.680  1.00 18.36           C  
ATOM   5251  C   SER B 201      46.566  -3.241  20.699  1.00 14.92           C  
ATOM   5252  O   SER B 201      46.380  -4.416  20.356  1.00 18.78           O  
ATOM   5253  CB  SER B 201      47.105  -2.317  22.984  1.00 19.69           C  
ATOM   5254  OG  SER B 201      46.541  -3.356  23.752  1.00 26.29           O  
ATOM   5255  N   VAL B 202      45.847  -2.226  20.197  1.00 14.27           N  
ATOM   5256  CA  VAL B 202      44.760  -2.375  19.230  1.00 12.86           C  
ATOM   5257  C   VAL B 202      45.218  -3.072  17.925  1.00 13.80           C  
ATOM   5258  O   VAL B 202      44.577  -3.987  17.400  1.00 11.90           O  
ATOM   5259  CB  VAL B 202      44.203  -0.934  19.008  1.00 15.73           C  
ATOM   5260  CG1 VAL B 202      43.198  -0.859  17.882  1.00 16.10           C  
ATOM   5261  CG2 VAL B 202      43.455  -0.514  20.265  1.00 14.14           C  
ATOM   5262  N   GLU B 203      46.376  -2.681  17.403  1.00 14.05           N  
ATOM   5263  CA  GLU B 203      46.934  -3.252  16.189  1.00 15.40           C  
ATOM   5264  C   GLU B 203      47.329  -4.694  16.386  1.00 15.73           C  
ATOM   5265  O   GLU B 203      46.958  -5.540  15.554  1.00 20.38           O  
ATOM   5266  CB  GLU B 203      48.159  -2.464  15.742  1.00 13.30           C  
ATOM   5267  CG  GLU B 203      47.729  -1.116  15.199  1.00  7.34           C  
ATOM   5268  CD  GLU B 203      48.842  -0.165  14.822  1.00 13.13           C  
ATOM   5269  OE1 GLU B 203      50.012  -0.472  15.014  1.00 14.22           O  
ATOM   5270  OE2 GLU B 203      48.537   0.912  14.332  1.00 10.79           O  
ATOM   5271  N   PHE B 204      48.033  -5.041  17.473  1.00 15.99           N  
ATOM   5272  CA  PHE B 204      48.388  -6.428  17.707  1.00 12.99           C  
ATOM   5273  C   PHE B 204      47.180  -7.254  18.033  1.00 11.61           C  
ATOM   5274  O   PHE B 204      47.139  -8.409  17.631  1.00 17.17           O  
ATOM   5275  CB  PHE B 204      49.404  -6.551  18.821  1.00 12.82           C  
ATOM   5276  CG  PHE B 204      50.807  -6.420  18.246  1.00  7.94           C  
ATOM   5277  CD1 PHE B 204      51.402  -7.536  17.656  1.00 14.26           C  
ATOM   5278  CD2 PHE B 204      51.491  -5.208  18.290  1.00 10.89           C  
ATOM   5279  CE1 PHE B 204      52.687  -7.447  17.123  1.00 11.46           C  
ATOM   5280  CE2 PHE B 204      52.779  -5.123  17.753  1.00 14.78           C  
ATOM   5281  CZ  PHE B 204      53.371  -6.238  17.165  1.00 16.37           C  
ATOM   5282  N   ALA B 205      46.147  -6.726  18.674  1.00 11.88           N  
ATOM   5283  CA  ALA B 205      44.925  -7.476  18.884  1.00 11.08           C  
ATOM   5284  C   ALA B 205      44.360  -7.914  17.526  1.00 14.03           C  
ATOM   5285  O   ALA B 205      43.997  -9.079  17.349  1.00 18.54           O  
ATOM   5286  CB  ALA B 205      43.928  -6.588  19.603  1.00  6.86           C  
ATOM   5287  N   GLY B 206      44.343  -7.057  16.492  1.00 15.48           N  
ATOM   5288  CA  GLY B 206      43.875  -7.407  15.154  1.00 11.16           C  
ATOM   5289  C   GLY B 206      44.748  -8.469  14.479  1.00 11.77           C  
ATOM   5290  O   GLY B 206      44.216  -9.401  13.869  1.00 16.29           O  
ATOM   5291  N   ILE B 207      46.072  -8.352  14.608  1.00  8.99           N  
ATOM   5292  CA  ILE B 207      47.045  -9.290  14.074  1.00 12.08           C  
ATOM   5293  C   ILE B 207      46.871 -10.674  14.686  1.00 16.21           C  
ATOM   5294  O   ILE B 207      46.805 -11.668  13.959  1.00 20.96           O  
ATOM   5295  CB  ILE B 207      48.468  -8.774  14.354  1.00 10.02           C  
ATOM   5296  CG1 ILE B 207      48.694  -7.482  13.612  1.00  9.50           C  
ATOM   5297  CG2 ILE B 207      49.497  -9.807  13.921  1.00 15.57           C  
ATOM   5298  CD1 ILE B 207      50.037  -6.772  13.917  1.00 10.35           C  
ATOM   5299  N   PHE B 208      46.754 -10.783  16.011  1.00 19.39           N  
ATOM   5300  CA  PHE B 208      46.611 -12.065  16.690  1.00 12.62           C  
ATOM   5301  C   PHE B 208      45.245 -12.649  16.408  1.00 14.74           C  
ATOM   5302  O   PHE B 208      45.089 -13.856  16.232  1.00 17.19           O  
ATOM   5303  CB  PHE B 208      46.776 -11.900  18.206  1.00 17.67           C  
ATOM   5304  CG  PHE B 208      48.184 -11.547  18.686  1.00 15.10           C  
ATOM   5305  CD1 PHE B 208      49.289 -12.249  18.203  1.00 14.12           C  
ATOM   5306  CD2 PHE B 208      48.363 -10.521  19.616  1.00 16.71           C  
ATOM   5307  CE1 PHE B 208      50.570 -11.913  18.645  1.00 17.03           C  
ATOM   5308  CE2 PHE B 208      49.646 -10.192  20.053  1.00 13.23           C  
ATOM   5309  CZ  PHE B 208      50.743 -10.889  19.571  1.00 10.62           C  
ATOM   5310  N   ASN B 209      44.214 -11.810  16.322  1.00 12.88           N  
ATOM   5311  CA  ASN B 209      42.878 -12.293  16.010  1.00 13.77           C  
ATOM   5312  C   ASN B 209      42.822 -13.022  14.673  1.00 18.18           C  
ATOM   5313  O   ASN B 209      42.087 -13.990  14.506  1.00 23.10           O  
ATOM   5314  CB  ASN B 209      41.901 -11.141  15.965  1.00 11.51           C  
ATOM   5315  CG  ASN B 209      40.464 -11.613  15.812  1.00 15.39           C  
ATOM   5316  OD1 ASN B 209      40.049 -12.561  16.462  1.00 19.27           O  
ATOM   5317  ND2 ASN B 209      39.629 -10.982  14.981  1.00 16.07           N  
ATOM   5318  N   ALA B 210      43.610 -12.598  13.684  1.00 18.68           N  
ATOM   5319  CA  ALA B 210      43.549 -13.222  12.377  1.00 17.73           C  
ATOM   5320  C   ALA B 210      44.356 -14.508  12.309  1.00 19.31           C  
ATOM   5321  O   ALA B 210      43.978 -15.446  11.629  1.00 19.93           O  
ATOM   5322  CB  ALA B 210      44.059 -12.228  11.353  1.00 13.18           C  
ATOM   5323  N   TYR B 211      45.486 -14.590  12.995  1.00 20.83           N  
ATOM   5324  CA  TYR B 211      46.303 -15.786  12.933  1.00 21.62           C  
ATOM   5325  C   TYR B 211      46.117 -16.730  14.104  1.00 24.99           C  
ATOM   5326  O   TYR B 211      46.912 -17.655  14.284  1.00 28.24           O  
ATOM   5327  CB  TYR B 211      47.758 -15.369  12.834  1.00 21.22           C  
ATOM   5328  CG  TYR B 211      48.100 -14.792  11.475  1.00 24.30           C  
ATOM   5329  CD1 TYR B 211      47.876 -13.441  11.216  1.00 22.00           C  
ATOM   5330  CD2 TYR B 211      48.628 -15.627  10.489  1.00 23.30           C  
ATOM   5331  CE1 TYR B 211      48.182 -12.921   9.966  1.00 22.05           C  
ATOM   5332  CE2 TYR B 211      48.935 -15.116   9.233  1.00 23.23           C  
ATOM   5333  CZ  TYR B 211      48.710 -13.764   8.985  1.00 24.57           C  
ATOM   5334  OH  TYR B 211      49.032 -13.235   7.758  1.00 23.97           O  
ATOM   5335  N   LYS B 212      45.092 -16.533  14.924  1.00 27.35           N  
ATOM   5336  CA  LYS B 212      44.858 -17.377  16.088  1.00 30.23           C  
ATOM   5337  C   LYS B 212      44.427 -18.776  15.672  1.00 33.01           C  
ATOM   5338  O   LYS B 212      43.750 -18.920  14.643  1.00 34.36           O  
ATOM   5339  CB  LYS B 212      43.773 -16.761  16.997  1.00 23.18           C  
ATOM   5340  CG  LYS B 212      42.353 -16.788  16.473  1.00 19.80           C  
ATOM   5341  CD  LYS B 212      41.482 -16.018  17.423  1.00 21.12           C  
ATOM   5342  CE  LYS B 212      40.036 -16.258  17.059  1.00 23.66           C  
ATOM   5343  NZ  LYS B 212      39.665 -15.467  15.903  1.00 30.08           N  
ATOM   5344  N   PRO B 213      44.770 -19.837  16.424  1.00 36.26           N  
ATOM   5345  CA  PRO B 213      44.283 -21.198  16.201  1.00 37.59           C  
ATOM   5346  C   PRO B 213      42.764 -21.322  16.248  1.00 40.82           C  
ATOM   5347  O   PRO B 213      42.039 -20.398  16.622  1.00 41.14           O  
ATOM   5348  CB  PRO B 213      44.960 -22.013  17.269  1.00 37.72           C  
ATOM   5349  CG  PRO B 213      46.205 -21.223  17.594  1.00 37.30           C  
ATOM   5350  CD  PRO B 213      45.686 -19.798  17.563  1.00 33.84           C  
ATOM   5351  N   LYS B 214      42.275 -22.522  15.945  1.00 45.80           N  
ATOM   5352  CA  LYS B 214      40.846 -22.809  15.920  1.00 51.24           C  
ATOM   5353  C   LYS B 214      40.062 -22.387  17.153  1.00 50.92           C  
ATOM   5354  O   LYS B 214      39.002 -21.782  16.996  1.00 53.61           O  
ATOM   5355  CB  LYS B 214      40.627 -24.311  15.692  1.00 57.90           C  
ATOM   5356  CG  LYS B 214      41.270 -25.259  16.717  1.00 69.14           C  
ATOM   5357  CD  LYS B 214      40.964 -26.725  16.428  1.00 77.11           C  
ATOM   5358  CE  LYS B 214      39.474 -27.055  16.547  1.00 80.52           C  
ATOM   5359  NZ  LYS B 214      39.240 -28.437  16.167  1.00 87.86           N  
ATOM   5360  N   ASP B 215      40.535 -22.657  18.374  1.00 47.79           N  
ATOM   5361  CA  ASP B 215      39.783 -22.255  19.551  1.00 47.01           C  
ATOM   5362  C   ASP B 215      40.469 -21.105  20.280  1.00 43.43           C  
ATOM   5363  O   ASP B 215      40.545 -21.065  21.509  1.00 45.83           O  
ATOM   5364  CB  ASP B 215      39.628 -23.473  20.470  1.00 56.76           C  
ATOM   5365  CG  ASP B 215      38.841 -24.633  19.870  1.00 60.17           C  
ATOM   5366  OD1 ASP B 215      37.664 -24.462  19.545  1.00 70.87           O  
ATOM   5367  OD2 ASP B 215      39.408 -25.718  19.731  1.00 73.94           O  
ATOM   5368  N   GLY B 216      41.027 -20.178  19.512  1.00 35.76           N  
ATOM   5369  CA  GLY B 216      41.741 -19.061  20.086  1.00 27.24           C  
ATOM   5370  C   GLY B 216      40.828 -17.936  20.523  1.00 26.04           C  
ATOM   5371  O   GLY B 216      39.677 -17.847  20.099  1.00 26.74           O  
ATOM   5372  N   GLN B 217      41.313 -17.029  21.344  1.00 26.35           N  
ATOM   5373  CA  GLN B 217      40.558 -15.884  21.787  1.00 25.06           C  
ATOM   5374  C   GLN B 217      41.590 -14.811  22.051  1.00 24.92           C  
ATOM   5375  O   GLN B 217      42.667 -15.098  22.565  1.00 29.51           O  
ATOM   5376  CB  GLN B 217      39.809 -16.205  23.067  1.00 23.80           C  
ATOM   5377  CG  GLN B 217      38.992 -15.057  23.648  1.00 32.81           C  
ATOM   5378  CD  GLN B 217      37.908 -14.580  22.706  1.00 34.19           C  
ATOM   5379  OE1 GLN B 217      36.960 -15.295  22.418  1.00 45.06           O  
ATOM   5380  NE2 GLN B 217      38.012 -13.371  22.178  1.00 38.42           N  
ATOM   5381  N   VAL B 218      41.302 -13.576  21.657  1.00 27.15           N  
ATOM   5382  CA  VAL B 218      42.171 -12.445  21.909  1.00 21.73           C  
ATOM   5383  C   VAL B 218      41.350 -11.583  22.855  1.00 19.60           C  
ATOM   5384  O   VAL B 218      40.135 -11.400  22.644  1.00 19.31           O  
ATOM   5385  CB  VAL B 218      42.491 -11.710  20.578  1.00 20.19           C  
ATOM   5386  CG1 VAL B 218      43.398 -10.514  20.879  1.00 17.23           C  
ATOM   5387  CG2 VAL B 218      43.193 -12.643  19.596  1.00 12.92           C  
ATOM   5388  N   THR B 219      41.975 -11.164  23.950  1.00 20.80           N  
ATOM   5389  CA  THR B 219      41.372 -10.244  24.903  1.00 18.87           C  
ATOM   5390  C   THR B 219      42.275  -9.016  24.973  1.00 16.25           C  
ATOM   5391  O   THR B 219      43.507  -9.111  25.042  1.00 15.62           O  
ATOM   5392  CB  THR B 219      41.270 -10.854  26.327  1.00 22.32           C  
ATOM   5393  OG1 THR B 219      40.590 -12.109  26.248  1.00 22.73           O  
ATOM   5394  CG2 THR B 219      40.473  -9.959  27.257  1.00 16.80           C  
ATOM   5395  N   LEU B 220      41.676  -7.848  24.937  1.00 13.60           N  
ATOM   5396  CA  LEU B 220      42.397  -6.611  25.066  1.00 20.48           C  
ATOM   5397  C   LEU B 220      41.895  -6.025  26.370  1.00 20.53           C  
ATOM   5398  O   LEU B 220      40.677  -6.015  26.576  1.00 19.92           O  
ATOM   5399  CB  LEU B 220      42.054  -5.689  23.895  1.00 22.00           C  
ATOM   5400  CG  LEU B 220      42.676  -4.304  23.771  1.00 25.04           C  
ATOM   5401  CD1 LEU B 220      42.583  -3.896  22.319  1.00 27.99           C  
ATOM   5402  CD2 LEU B 220      41.960  -3.273  24.639  1.00 25.62           C  
ATOM   5403  N   CYS B 221      42.733  -5.539  27.271  1.00 21.33           N  
ATOM   5404  CA  CYS B 221      42.165  -4.899  28.439  1.00 23.61           C  
ATOM   5405  C   CYS B 221      42.778  -3.547  28.616  1.00 18.84           C  
ATOM   5406  O   CYS B 221      43.949  -3.329  28.294  1.00 21.10           O  
ATOM   5407  CB  CYS B 221      42.386  -5.715  29.732  1.00 29.32           C  
ATOM   5408  SG  CYS B 221      44.081  -5.768  30.329  1.00 30.16           S  
ATOM   5409  N   TYR B 222      41.992  -2.616  29.107  1.00 16.86           N  
ATOM   5410  CA  TYR B 222      42.479  -1.284  29.321  1.00 17.33           C  
ATOM   5411  C   TYR B 222      41.942  -0.853  30.688  1.00 20.93           C  
ATOM   5412  O   TYR B 222      40.830  -1.232  31.060  1.00 22.70           O  
ATOM   5413  CB  TYR B 222      41.960  -0.461  28.145  1.00 11.40           C  
ATOM   5414  CG  TYR B 222      42.281   1.012  28.256  1.00 15.30           C  
ATOM   5415  CD1 TYR B 222      43.563   1.477  28.598  1.00 18.11           C  
ATOM   5416  CD2 TYR B 222      41.233   1.908  28.072  1.00 15.67           C  
ATOM   5417  CE1 TYR B 222      43.789   2.848  28.771  1.00 18.75           C  
ATOM   5418  CE2 TYR B 222      41.458   3.270  28.242  1.00 21.85           C  
ATOM   5419  CZ  TYR B 222      42.723   3.732  28.594  1.00 21.19           C  
ATOM   5420  OH  TYR B 222      42.889   5.082  28.812  1.00 30.02           O  
ATOM   5421  N   ARG B 223      42.710  -0.082  31.461  1.00 21.97           N  
ATOM   5422  CA  ARG B 223      42.291   0.395  32.773  1.00 25.50           C  
ATOM   5423  C   ARG B 223      41.308   1.559  32.689  1.00 26.40           C  
ATOM   5424  O   ARG B 223      40.569   1.817  33.640  1.00 28.86           O  
ATOM   5425  CB  ARG B 223      43.523   0.811  33.593  1.00 25.10           C  
ATOM   5426  CG  ARG B 223      44.330   2.006  33.093  1.00 35.95           C  
ATOM   5427  CD  ARG B 223      45.452   2.444  34.037  1.00 41.03           C  
ATOM   5428  NE  ARG B 223      44.887   2.766  35.336  1.00 47.09           N  
ATOM   5429  CZ  ARG B 223      45.405   2.282  36.467  1.00 49.99           C  
ATOM   5430  NH1 ARG B 223      46.481   1.496  36.473  1.00 45.55           N  
ATOM   5431  NH2 ARG B 223      44.763   2.510  37.606  1.00 46.28           N  
ATOM   5432  N   GLY B 224      41.270   2.312  31.587  1.00 25.96           N  
ATOM   5433  CA  GLY B 224      40.306   3.398  31.439  1.00 21.60           C  
ATOM   5434  C   GLY B 224      38.976   2.869  30.928  1.00 23.00           C  
ATOM   5435  O   GLY B 224      38.780   1.654  30.822  1.00 25.21           O  
ATOM   5436  N   GLU B 225      38.050   3.727  30.530  1.00 24.77           N  
ATOM   5437  CA  GLU B 225      36.753   3.217  30.129  1.00 29.80           C  
ATOM   5438  C   GLU B 225      36.523   2.964  28.646  1.00 29.55           C  
ATOM   5439  O   GLU B 225      35.526   2.333  28.286  1.00 29.08           O  
ATOM   5440  CB  GLU B 225      35.673   4.154  30.695  1.00 38.66           C  
ATOM   5441  CG  GLU B 225      35.884   5.667  30.630  1.00 55.45           C  
ATOM   5442  CD  GLU B 225      35.106   6.397  31.726  1.00 67.46           C  
ATOM   5443  OE1 GLU B 225      35.582   6.436  32.867  1.00 72.24           O  
ATOM   5444  OE2 GLU B 225      34.028   6.925  31.441  1.00 74.44           O  
ATOM   5445  N   MET B 226      37.426   3.365  27.754  1.00 29.07           N  
ATOM   5446  CA  MET B 226      37.265   3.112  26.331  1.00 23.33           C  
ATOM   5447  C   MET B 226      38.649   3.162  25.717  1.00 22.71           C  
ATOM   5448  O   MET B 226      39.467   3.976  26.150  1.00 20.13           O  
ATOM   5449  CB  MET B 226      36.372   4.178  25.732  1.00 23.21           C  
ATOM   5450  CG  MET B 226      35.990   3.890  24.301  1.00 26.74           C  
ATOM   5451  SD  MET B 226      34.340   4.534  23.963  1.00 35.97           S  
ATOM   5452  CE  MET B 226      34.604   6.259  24.269  1.00 22.92           C  
ATOM   5453  N   ILE B 227      38.974   2.249  24.792  1.00 23.76           N  
ATOM   5454  CA  ILE B 227      40.253   2.240  24.093  1.00 20.74           C  
ATOM   5455  C   ILE B 227      40.506   3.556  23.387  1.00 20.71           C  
ATOM   5456  O   ILE B 227      39.605   4.346  23.127  1.00 23.66           O  
ATOM   5457  CB  ILE B 227      40.355   1.099  23.014  1.00 20.44           C  
ATOM   5458  CG1 ILE B 227      39.260   1.144  21.945  1.00 23.06           C  
ATOM   5459  CG2 ILE B 227      40.303  -0.201  23.768  1.00 20.76           C  
ATOM   5460  CD1 ILE B 227      39.498   0.204  20.735  1.00 19.12           C  
ATOM   5461  N   LEU B 228      41.785   3.729  23.087  1.00 18.85           N  
ATOM   5462  CA  LEU B 228      42.297   4.860  22.363  1.00 20.59           C  
ATOM   5463  C   LEU B 228      41.986   6.250  22.903  1.00 23.82           C  
ATOM   5464  O   LEU B 228      41.407   7.093  22.214  1.00 25.99           O  
ATOM   5465  CB  LEU B 228      41.834   4.732  20.889  1.00 16.34           C  
ATOM   5466  CG  LEU B 228      42.335   3.569  20.024  1.00 15.99           C  
ATOM   5467  CD1 LEU B 228      41.614   3.625  18.696  1.00 13.30           C  
ATOM   5468  CD2 LEU B 228      43.837   3.645  19.807  1.00  6.88           C  
ATOM   5469  N   ARG B 229      42.441   6.539  24.126  1.00 27.22           N  
ATOM   5470  CA  ARG B 229      42.293   7.867  24.678  1.00 28.63           C  
ATOM   5471  C   ARG B 229      43.231   8.766  23.868  1.00 25.86           C  
ATOM   5472  O   ARG B 229      44.298   8.388  23.383  1.00 25.87           O  
ATOM   5473  CB  ARG B 229      42.595   7.725  26.195  1.00 38.39           C  
ATOM   5474  CG  ARG B 229      43.758   8.495  26.782  1.00 56.36           C  
ATOM   5475  CD  ARG B 229      44.038   8.446  28.286  1.00 68.88           C  
ATOM   5476  NE  ARG B 229      45.469   8.663  28.235  1.00 85.20           N  
ATOM   5477  CZ  ARG B 229      46.335   7.677  28.496  1.00 86.43           C  
ATOM   5478  NH1 ARG B 229      45.997   6.542  29.115  1.00 88.19           N  
ATOM   5479  NH2 ARG B 229      47.631   7.901  28.366  1.00 87.56           N  
ATOM   5480  N   GLY B 230      42.665   9.929  23.558  1.00 23.43           N  
ATOM   5481  CA  GLY B 230      43.302  10.928  22.715  1.00 23.18           C  
ATOM   5482  C   GLY B 230      42.665  10.948  21.329  1.00 24.68           C  
ATOM   5483  O   GLY B 230      42.893  11.863  20.531  1.00 24.83           O  
ATOM   5484  N   PHE B 231      41.894   9.919  21.004  1.00 22.92           N  
ATOM   5485  CA  PHE B 231      41.210   9.901  19.733  1.00 21.66           C  
ATOM   5486  C   PHE B 231      39.777  10.368  19.918  1.00 23.83           C  
ATOM   5487  O   PHE B 231      39.267  10.529  21.035  1.00 26.53           O  
ATOM   5488  CB  PHE B 231      41.248   8.485  19.132  1.00 17.13           C  
ATOM   5489  CG  PHE B 231      42.653   8.129  18.660  1.00 17.17           C  
ATOM   5490  CD1 PHE B 231      43.638   7.782  19.587  1.00 14.11           C  
ATOM   5491  CD2 PHE B 231      42.971   8.192  17.300  1.00 18.71           C  
ATOM   5492  CE1 PHE B 231      44.930   7.495  19.163  1.00 12.77           C  
ATOM   5493  CE2 PHE B 231      44.269   7.905  16.875  1.00 16.90           C  
ATOM   5494  CZ  PHE B 231      45.250   7.563  17.812  1.00 22.37           C  
ATOM   5495  N   ASP B 232      39.141  10.626  18.778  1.00 22.74           N  
ATOM   5496  CA  ASP B 232      37.769  11.058  18.710  1.00 20.61           C  
ATOM   5497  C   ASP B 232      36.870  10.019  19.346  1.00 18.37           C  
ATOM   5498  O   ASP B 232      36.927   8.849  18.981  1.00 20.56           O  
ATOM   5499  CB  ASP B 232      37.448  11.285  17.236  1.00 25.09           C  
ATOM   5500  CG  ASP B 232      36.006  11.618  16.941  1.00 21.90           C  
ATOM   5501  OD1 ASP B 232      35.172  10.720  16.900  1.00 33.77           O  
ATOM   5502  OD2 ASP B 232      35.717  12.768  16.721  1.00 29.76           O  
ATOM   5503  N   HIS B 233      35.971  10.439  20.246  1.00 20.87           N  
ATOM   5504  CA  HIS B 233      35.101   9.520  20.972  1.00 19.37           C  
ATOM   5505  C   HIS B 233      34.167   8.757  20.043  1.00 19.16           C  
ATOM   5506  O   HIS B 233      33.860   7.607  20.332  1.00 23.24           O  
ATOM   5507  CB  HIS B 233      34.274  10.283  22.041  1.00 20.86           C  
ATOM   5508  CG  HIS B 233      33.183  11.237  21.521  1.00 35.37           C  
ATOM   5509  ND1 HIS B 233      31.919  10.896  21.270  1.00 44.61           N  
ATOM   5510  CD2 HIS B 233      33.264  12.585  21.234  1.00 38.59           C  
ATOM   5511  CE1 HIS B 233      31.242  11.947  20.850  1.00 39.60           C  
ATOM   5512  NE2 HIS B 233      32.079  12.962  20.835  1.00 44.23           N  
ATOM   5513  N   THR B 234      33.666   9.287  18.912  1.00 20.63           N  
ATOM   5514  CA  THR B 234      32.815   8.510  17.991  1.00 15.64           C  
ATOM   5515  C   THR B 234      33.647   7.381  17.405  1.00 14.14           C  
ATOM   5516  O   THR B 234      33.207   6.239  17.362  1.00 18.37           O  
ATOM   5517  CB  THR B 234      32.293   9.393  16.844  1.00 22.68           C  
ATOM   5518  OG1 THR B 234      31.709  10.539  17.476  1.00 23.46           O  
ATOM   5519  CG2 THR B 234      31.301   8.683  15.936  1.00 10.52           C  
ATOM   5520  N   LEU B 235      34.881   7.682  16.991  1.00 13.73           N  
ATOM   5521  CA  LEU B 235      35.785   6.681  16.454  1.00 12.48           C  
ATOM   5522  C   LEU B 235      36.104   5.636  17.509  1.00 14.79           C  
ATOM   5523  O   LEU B 235      36.097   4.449  17.188  1.00 18.02           O  
ATOM   5524  CB  LEU B 235      37.080   7.340  15.976  1.00 12.49           C  
ATOM   5525  CG  LEU B 235      37.210   7.771  14.518  1.00 13.80           C  
ATOM   5526  CD1 LEU B 235      36.091   8.682  14.078  1.00 13.83           C  
ATOM   5527  CD2 LEU B 235      38.524   8.480  14.387  1.00 14.54           C  
ATOM   5528  N   ARG B 236      36.307   6.026  18.772  1.00 16.30           N  
ATOM   5529  CA  ARG B 236      36.592   5.083  19.849  1.00 15.95           C  
ATOM   5530  C   ARG B 236      35.437   4.142  20.077  1.00 13.24           C  
ATOM   5531  O   ARG B 236      35.581   2.920  20.183  1.00 14.85           O  
ATOM   5532  CB  ARG B 236      36.867   5.815  21.145  1.00 16.05           C  
ATOM   5533  CG  ARG B 236      38.125   6.661  21.065  1.00 17.63           C  
ATOM   5534  CD  ARG B 236      38.167   7.642  22.224  1.00 17.62           C  
ATOM   5535  NE  ARG B 236      38.577   6.945  23.423  1.00 18.49           N  
ATOM   5536  CZ  ARG B 236      38.589   7.507  24.626  1.00 19.57           C  
ATOM   5537  NH1 ARG B 236      38.220   8.762  24.831  1.00 26.12           N  
ATOM   5538  NH2 ARG B 236      39.026   6.783  25.640  1.00 19.48           N  
ATOM   5539  N   GLU B 237      34.239   4.706  20.080  1.00 14.76           N  
ATOM   5540  CA  GLU B 237      33.043   3.916  20.276  1.00 17.04           C  
ATOM   5541  C   GLU B 237      32.754   2.919  19.173  1.00 18.59           C  
ATOM   5542  O   GLU B 237      32.376   1.770  19.468  1.00 19.15           O  
ATOM   5543  CB  GLU B 237      31.864   4.804  20.384  1.00 18.49           C  
ATOM   5544  CG  GLU B 237      31.776   5.556  21.681  1.00 33.07           C  
ATOM   5545  CD  GLU B 237      30.685   6.610  21.636  1.00 43.38           C  
ATOM   5546  OE1 GLU B 237      29.573   6.285  21.228  1.00 49.03           O  
ATOM   5547  OE2 GLU B 237      30.949   7.757  22.008  1.00 50.96           O  
ATOM   5548  N   GLU B 238      32.859   3.412  17.936  1.00 19.43           N  
ATOM   5549  CA  GLU B 238      32.628   2.625  16.746  1.00 15.48           C  
ATOM   5550  C   GLU B 238      33.677   1.579  16.498  1.00 12.66           C  
ATOM   5551  O   GLU B 238      33.323   0.467  16.115  1.00 13.61           O  
ATOM   5552  CB  GLU B 238      32.553   3.516  15.534  1.00 21.38           C  
ATOM   5553  CG  GLU B 238      31.151   4.035  15.315  1.00 31.95           C  
ATOM   5554  CD  GLU B 238      30.087   2.952  15.117  1.00 39.97           C  
ATOM   5555  OE1 GLU B 238      30.356   1.869  14.556  1.00 37.46           O  
ATOM   5556  OE2 GLU B 238      28.966   3.225  15.543  1.00 44.73           O  
ATOM   5557  N   LEU B 239      34.954   1.871  16.734  1.00 11.86           N  
ATOM   5558  CA  LEU B 239      35.981   0.871  16.568  1.00 12.89           C  
ATOM   5559  C   LEU B 239      35.767  -0.201  17.621  1.00 17.46           C  
ATOM   5560  O   LEU B 239      35.902  -1.382  17.268  1.00 21.75           O  
ATOM   5561  CB  LEU B 239      37.386   1.473  16.723  1.00 13.78           C  
ATOM   5562  CG  LEU B 239      38.536   0.486  16.492  1.00 14.03           C  
ATOM   5563  CD1 LEU B 239      38.430  -0.054  15.075  1.00  8.56           C  
ATOM   5564  CD2 LEU B 239      39.872   1.149  16.756  1.00 12.19           C  
ATOM   5565  N   THR B 240      35.377   0.114  18.868  1.00 16.68           N  
ATOM   5566  CA  THR B 240      35.129  -0.912  19.870  1.00 15.11           C  
ATOM   5567  C   THR B 240      34.083  -1.900  19.374  1.00 12.10           C  
ATOM   5568  O   THR B 240      34.320  -3.105  19.435  1.00 15.40           O  
ATOM   5569  CB  THR B 240      34.690  -0.222  21.183  1.00 13.92           C  
ATOM   5570  OG1 THR B 240      35.793   0.560  21.637  1.00 13.49           O  
ATOM   5571  CG2 THR B 240      34.319  -1.211  22.277  1.00 21.75           C  
ATOM   5572  N   LYS B 241      32.979  -1.429  18.801  1.00 15.02           N  
ATOM   5573  CA  LYS B 241      31.932  -2.297  18.285  1.00 13.40           C  
ATOM   5574  C   LYS B 241      32.361  -3.157  17.122  1.00 16.23           C  
ATOM   5575  O   LYS B 241      31.900  -4.291  16.990  1.00 18.80           O  
ATOM   5576  CB  LYS B 241      30.757  -1.465  17.845  1.00 15.47           C  
ATOM   5577  CG  LYS B 241      30.045  -0.930  19.050  1.00 27.10           C  
ATOM   5578  CD  LYS B 241      29.398   0.415  18.831  1.00 29.14           C  
ATOM   5579  CE  LYS B 241      28.393   0.364  17.723  1.00 37.93           C  
ATOM   5580  NZ  LYS B 241      27.653   1.608  17.715  1.00 49.77           N  
ATOM   5581  N   GLN B 242      33.236  -2.646  16.255  1.00 16.62           N  
ATOM   5582  CA  GLN B 242      33.684  -3.427  15.124  1.00 15.12           C  
ATOM   5583  C   GLN B 242      34.746  -4.414  15.561  1.00 15.19           C  
ATOM   5584  O   GLN B 242      34.756  -5.540  15.055  1.00 15.16           O  
ATOM   5585  CB  GLN B 242      34.213  -2.495  14.030  1.00 15.83           C  
ATOM   5586  CG  GLN B 242      32.988  -1.751  13.491  1.00 15.66           C  
ATOM   5587  CD  GLN B 242      33.256  -0.796  12.348  1.00 14.50           C  
ATOM   5588  OE1 GLN B 242      34.010  -1.115  11.452  1.00 22.70           O  
ATOM   5589  NE2 GLN B 242      32.672   0.395  12.294  1.00 10.58           N  
ATOM   5590  N   LEU B 243      35.603  -4.083  16.539  1.00 14.68           N  
ATOM   5591  CA  LEU B 243      36.557  -5.064  17.045  1.00 15.12           C  
ATOM   5592  C   LEU B 243      35.831  -6.169  17.794  1.00 16.59           C  
ATOM   5593  O   LEU B 243      36.153  -7.344  17.583  1.00 17.59           O  
ATOM   5594  CB  LEU B 243      37.562  -4.440  17.987  1.00 12.89           C  
ATOM   5595  CG  LEU B 243      38.625  -3.525  17.414  1.00 14.67           C  
ATOM   5596  CD1 LEU B 243      39.522  -3.112  18.546  1.00 12.18           C  
ATOM   5597  CD2 LEU B 243      39.486  -4.216  16.379  1.00 13.20           C  
ATOM   5598  N   THR B 244      34.816  -5.874  18.612  1.00 16.42           N  
ATOM   5599  CA  THR B 244      34.091  -6.937  19.291  1.00 20.53           C  
ATOM   5600  C   THR B 244      33.281  -7.712  18.256  1.00 21.55           C  
ATOM   5601  O   THR B 244      33.136  -8.924  18.386  1.00 22.02           O  
ATOM   5602  CB  THR B 244      33.145  -6.379  20.378  1.00 17.63           C  
ATOM   5603  OG1 THR B 244      32.320  -5.421  19.752  1.00 32.99           O  
ATOM   5604  CG2 THR B 244      33.872  -5.700  21.517  1.00 22.25           C  
ATOM   5605  N   ALA B 245      32.770  -7.078  17.190  1.00 20.85           N  
ATOM   5606  CA  ALA B 245      32.075  -7.807  16.129  1.00 17.28           C  
ATOM   5607  C   ALA B 245      33.013  -8.769  15.413  1.00 15.55           C  
ATOM   5608  O   ALA B 245      32.588  -9.795  14.904  1.00 15.55           O  
ATOM   5609  CB  ALA B 245      31.520  -6.858  15.086  1.00 19.02           C  
ATOM   5610  N   ASN B 246      34.320  -8.542  15.407  1.00 13.76           N  
ATOM   5611  CA  ASN B 246      35.201  -9.478  14.751  1.00 14.77           C  
ATOM   5612  C   ASN B 246      35.798 -10.475  15.730  1.00 17.74           C  
ATOM   5613  O   ASN B 246      36.835 -11.089  15.450  1.00 17.24           O  
ATOM   5614  CB  ASN B 246      36.304  -8.715  14.051  1.00 14.40           C  
ATOM   5615  CG  ASN B 246      36.960  -9.467  12.904  1.00 17.04           C  
ATOM   5616  OD1 ASN B 246      38.070  -9.131  12.467  1.00 23.58           O  
ATOM   5617  ND2 ASN B 246      36.347 -10.492  12.325  1.00 24.66           N  
ATOM   5618  N   GLY B 247      35.175 -10.670  16.900  1.00 21.47           N  
ATOM   5619  CA  GLY B 247      35.584 -11.689  17.863  1.00 18.76           C  
ATOM   5620  C   GLY B 247      36.649 -11.310  18.880  1.00 18.80           C  
ATOM   5621  O   GLY B 247      37.112 -12.210  19.580  1.00 23.95           O  
ATOM   5622  N   ILE B 248      37.096 -10.064  19.012  1.00 16.78           N  
ATOM   5623  CA  ILE B 248      38.056  -9.685  20.046  1.00 17.64           C  
ATOM   5624  C   ILE B 248      37.318  -9.337  21.340  1.00 19.94           C  
ATOM   5625  O   ILE B 248      36.297  -8.627  21.301  1.00 20.31           O  
ATOM   5626  CB  ILE B 248      38.870  -8.475  19.541  1.00 19.29           C  
ATOM   5627  CG1 ILE B 248      39.708  -8.946  18.362  1.00 11.72           C  
ATOM   5628  CG2 ILE B 248      39.758  -7.875  20.651  1.00 12.32           C  
ATOM   5629  CD1 ILE B 248      40.363  -7.799  17.573  1.00 19.05           C  
ATOM   5630  N   GLN B 249      37.730  -9.820  22.520  1.00 20.49           N  
ATOM   5631  CA  GLN B 249      37.044  -9.417  23.750  1.00 19.19           C  
ATOM   5632  C   GLN B 249      37.733  -8.186  24.282  1.00 17.10           C  
ATOM   5633  O   GLN B 249      38.957  -8.187  24.422  1.00 20.19           O  
ATOM   5634  CB  GLN B 249      37.153 -10.346  24.916  1.00 27.59           C  
ATOM   5635  CG  GLN B 249      36.636 -11.742  25.065  1.00 39.99           C  
ATOM   5636  CD  GLN B 249      36.990 -12.084  26.509  1.00 46.56           C  
ATOM   5637  OE1 GLN B 249      36.340 -11.641  27.454  1.00 47.86           O  
ATOM   5638  NE2 GLN B 249      38.089 -12.776  26.802  1.00 49.11           N  
ATOM   5639  N   ILE B 250      36.994  -7.154  24.634  1.00 19.59           N  
ATOM   5640  CA  ILE B 250      37.588  -5.944  25.180  1.00 24.91           C  
ATOM   5641  C   ILE B 250      37.082  -5.829  26.612  1.00 24.81           C  
ATOM   5642  O   ILE B 250      35.868  -5.804  26.840  1.00 22.32           O  
ATOM   5643  CB  ILE B 250      37.154  -4.713  24.327  1.00 24.37           C  
ATOM   5644  CG1 ILE B 250      37.699  -4.874  22.908  1.00 22.39           C  
ATOM   5645  CG2 ILE B 250      37.647  -3.413  24.973  1.00 24.38           C  
ATOM   5646  CD1 ILE B 250      37.287  -3.777  21.912  1.00 24.50           C  
ATOM   5647  N   LEU B 251      38.016  -5.776  27.554  1.00 25.37           N  
ATOM   5648  CA  LEU B 251      37.730  -5.626  28.976  1.00 24.59           C  
ATOM   5649  C   LEU B 251      38.226  -4.255  29.387  1.00 24.00           C  
ATOM   5650  O   LEU B 251      39.438  -4.014  29.452  1.00 25.52           O  
ATOM   5651  CB  LEU B 251      38.469  -6.689  29.805  1.00 26.77           C  
ATOM   5652  CG  LEU B 251      38.242  -8.192  29.571  1.00 29.47           C  
ATOM   5653  CD1 LEU B 251      39.168  -9.009  30.455  1.00 19.27           C  
ATOM   5654  CD2 LEU B 251      36.795  -8.533  29.875  1.00 29.87           C  
ATOM   5655  N   THR B 252      37.335  -3.304  29.562  1.00 25.49           N  
ATOM   5656  CA  THR B 252      37.736  -1.986  30.014  1.00 29.94           C  
ATOM   5657  C   THR B 252      37.597  -1.910  31.525  1.00 30.91           C  
ATOM   5658  O   THR B 252      36.955  -2.760  32.151  1.00 29.45           O  
ATOM   5659  CB  THR B 252      36.870  -0.973  29.264  1.00 32.44           C  
ATOM   5660  OG1 THR B 252      35.530  -1.462  29.219  1.00 33.78           O  
ATOM   5661  CG2 THR B 252      37.430  -0.753  27.864  1.00 28.12           C  
ATOM   5662  N   LYS B 253      38.230  -0.886  32.103  1.00 31.32           N  
ATOM   5663  CA  LYS B 253      38.312  -0.713  33.537  1.00 34.71           C  
ATOM   5664  C   LYS B 253      38.893  -1.959  34.210  1.00 34.82           C  
ATOM   5665  O   LYS B 253      38.562  -2.277  35.350  1.00 38.43           O  
ATOM   5666  CB  LYS B 253      36.905  -0.363  34.086  1.00 38.41           C  
ATOM   5667  CG  LYS B 253      36.454   1.092  33.839  1.00 43.13           C  
ATOM   5668  CD  LYS B 253      35.160   1.320  34.624  1.00 56.81           C  
ATOM   5669  CE  LYS B 253      34.432   2.655  34.388  1.00 67.28           C  
ATOM   5670  NZ  LYS B 253      33.181   2.756  35.137  1.00 75.20           N  
ATOM   5671  N   GLU B 254      39.806  -2.674  33.541  1.00 33.63           N  
ATOM   5672  CA  GLU B 254      40.463  -3.857  34.079  1.00 29.22           C  
ATOM   5673  C   GLU B 254      41.948  -3.665  33.903  1.00 30.49           C  
ATOM   5674  O   GLU B 254      42.374  -3.158  32.863  1.00 34.66           O  
ATOM   5675  CB  GLU B 254      40.060  -5.116  33.335  1.00 25.71           C  
ATOM   5676  CG  GLU B 254      38.607  -5.536  33.536  1.00 30.62           C  
ATOM   5677  CD  GLU B 254      38.217  -6.115  34.898  1.00 35.80           C  
ATOM   5678  OE1 GLU B 254      39.063  -6.224  35.794  1.00 29.82           O  
ATOM   5679  OE2 GLU B 254      37.048  -6.473  35.056  1.00 36.41           O  
ATOM   5680  N   ASN B 255      42.742  -4.049  34.899  1.00 29.41           N  
ATOM   5681  CA  ASN B 255      44.179  -3.848  34.857  1.00 29.46           C  
ATOM   5682  C   ASN B 255      44.797  -5.002  35.616  1.00 30.06           C  
ATOM   5683  O   ASN B 255      44.334  -5.291  36.728  1.00 32.26           O  
ATOM   5684  CB  ASN B 255      44.537  -2.525  35.525  1.00 30.42           C  
ATOM   5685  CG  ASN B 255      45.988  -2.129  35.317  1.00 32.93           C  
ATOM   5686  OD1 ASN B 255      46.637  -2.496  34.347  1.00 43.03           O  
ATOM   5687  ND2 ASN B 255      46.598  -1.348  36.194  1.00 45.08           N  
ATOM   5688  N   PRO B 256      45.755  -5.749  35.073  1.00 30.42           N  
ATOM   5689  CA  PRO B 256      46.448  -6.852  35.729  1.00 31.04           C  
ATOM   5690  C   PRO B 256      47.188  -6.468  36.998  1.00 31.02           C  
ATOM   5691  O   PRO B 256      47.935  -5.485  37.038  1.00 31.06           O  
ATOM   5692  CB  PRO B 256      47.387  -7.389  34.690  1.00 31.49           C  
ATOM   5693  CG  PRO B 256      46.741  -6.981  33.401  1.00 31.44           C  
ATOM   5694  CD  PRO B 256      46.264  -5.586  33.721  1.00 26.95           C  
ATOM   5695  N   ALA B 257      46.941  -7.276  38.023  1.00 32.55           N  
ATOM   5696  CA  ALA B 257      47.548  -7.122  39.335  1.00 30.75           C  
ATOM   5697  C   ALA B 257      48.735  -8.054  39.412  1.00 29.47           C  
ATOM   5698  O   ALA B 257      49.810  -7.644  39.842  1.00 30.91           O  
ATOM   5699  CB  ALA B 257      46.571  -7.505  40.435  1.00 31.97           C  
ATOM   5700  N   LYS B 258      48.574  -9.310  39.016  1.00 29.55           N  
ATOM   5701  CA  LYS B 258      49.696 -10.231  39.020  1.00 31.30           C  
ATOM   5702  C   LYS B 258      49.520 -11.278  37.952  1.00 29.06           C  
ATOM   5703  O   LYS B 258      48.390 -11.517  37.522  1.00 29.86           O  
ATOM   5704  CB  LYS B 258      49.855 -10.953  40.362  1.00 32.00           C  
ATOM   5705  CG  LYS B 258      48.643 -11.606  40.963  1.00 41.42           C  
ATOM   5706  CD  LYS B 258      49.178 -12.730  41.818  1.00 51.69           C  
ATOM   5707  CE  LYS B 258      48.090 -13.218  42.755  1.00 55.66           C  
ATOM   5708  NZ  LYS B 258      48.576 -14.398  43.443  1.00 67.43           N  
ATOM   5709  N   VAL B 259      50.646 -11.846  37.540  1.00 28.27           N  
ATOM   5710  CA  VAL B 259      50.734 -12.865  36.516  1.00 32.98           C  
ATOM   5711  C   VAL B 259      51.573 -13.967  37.135  1.00 36.78           C  
ATOM   5712  O   VAL B 259      52.721 -13.730  37.537  1.00 36.56           O  
ATOM   5713  CB  VAL B 259      51.467 -12.350  35.241  1.00 34.19           C  
ATOM   5714  CG1 VAL B 259      51.595 -13.477  34.235  1.00 29.17           C  
ATOM   5715  CG2 VAL B 259      50.703 -11.198  34.611  1.00 30.38           C  
ATOM   5716  N   GLU B 260      51.073 -15.188  37.221  1.00 38.79           N  
ATOM   5717  CA  GLU B 260      51.888 -16.275  37.727  1.00 45.28           C  
ATOM   5718  C   GLU B 260      51.755 -17.414  36.758  1.00 44.34           C  
ATOM   5719  O   GLU B 260      50.657 -17.581  36.225  1.00 45.72           O  
ATOM   5720  CB  GLU B 260      51.419 -16.681  39.124  1.00 52.30           C  
ATOM   5721  CG  GLU B 260      49.962 -17.068  39.348  1.00 59.64           C  
ATOM   5722  CD  GLU B 260      49.521 -16.770  40.776  1.00 67.54           C  
ATOM   5723  OE1 GLU B 260      50.189 -17.206  41.715  1.00 69.04           O  
ATOM   5724  OE2 GLU B 260      48.514 -16.086  40.953  1.00 76.49           O  
ATOM   5725  N   LEU B 261      52.823 -18.150  36.434  1.00 45.28           N  
ATOM   5726  CA  LEU B 261      52.592 -19.189  35.458  1.00 49.38           C  
ATOM   5727  C   LEU B 261      52.130 -20.469  36.083  1.00 50.34           C  
ATOM   5728  O   LEU B 261      52.547 -20.855  37.168  1.00 53.09           O  
ATOM   5729  CB  LEU B 261      53.817 -19.496  34.591  1.00 47.97           C  
ATOM   5730  CG  LEU B 261      55.250 -19.712  34.980  1.00 48.94           C  
ATOM   5731  CD1 LEU B 261      55.501 -20.930  35.847  1.00 61.47           C  
ATOM   5732  CD2 LEU B 261      55.958 -19.947  33.670  1.00 50.60           C  
ATOM   5733  N   ASN B 262      51.134 -21.014  35.416  1.00 52.35           N  
ATOM   5734  CA  ASN B 262      50.533 -22.265  35.778  1.00 52.97           C  
ATOM   5735  C   ASN B 262      51.460 -23.373  35.342  1.00 56.65           C  
ATOM   5736  O   ASN B 262      52.410 -23.206  34.570  1.00 55.43           O  
ATOM   5737  CB  ASN B 262      49.224 -22.498  35.067  1.00 53.88           C  
ATOM   5738  CG  ASN B 262      48.090 -21.592  35.484  1.00 58.65           C  
ATOM   5739  OD1 ASN B 262      47.990 -20.453  35.051  1.00 61.88           O  
ATOM   5740  ND2 ASN B 262      47.157 -22.062  36.305  1.00 65.33           N  
ATOM   5741  N   ALA B 263      51.049 -24.566  35.775  1.00 60.84           N  
ATOM   5742  CA  ALA B 263      51.729 -25.815  35.460  1.00 63.51           C  
ATOM   5743  C   ALA B 263      51.954 -26.031  33.958  1.00 64.27           C  
ATOM   5744  O   ALA B 263      53.050 -26.385  33.527  1.00 65.15           O  
ATOM   5745  CB  ALA B 263      50.897 -26.964  36.017  1.00 65.27           C  
ATOM   5746  N   ASP B 264      50.923 -25.740  33.146  1.00 62.87           N  
ATOM   5747  CA  ASP B 264      50.989 -25.912  31.695  1.00 59.58           C  
ATOM   5748  C   ASP B 264      52.062 -25.078  31.019  1.00 59.56           C  
ATOM   5749  O   ASP B 264      52.496 -25.387  29.907  1.00 61.95           O  
ATOM   5750  CB  ASP B 264      49.745 -25.482  30.965  1.00 58.10           C  
ATOM   5751  CG  ASP B 264      48.413 -25.890  31.535  1.00 62.71           C  
ATOM   5752  OD1 ASP B 264      48.103 -25.494  32.656  1.00 69.31           O  
ATOM   5753  OD2 ASP B 264      47.673 -26.572  30.832  1.00 69.99           O  
ATOM   5754  N   GLY B 265      52.413 -23.968  31.664  1.00 57.28           N  
ATOM   5755  CA  GLY B 265      53.258 -22.971  31.036  1.00 52.82           C  
ATOM   5756  C   GLY B 265      52.371 -21.779  30.697  1.00 47.95           C  
ATOM   5757  O   GLY B 265      52.875 -20.731  30.305  1.00 48.24           O  
ATOM   5758  N   SER B 266      51.048 -21.959  30.827  1.00 43.48           N  
ATOM   5759  CA  SER B 266      50.083 -20.893  30.671  1.00 43.33           C  
ATOM   5760  C   SER B 266      50.256 -19.929  31.835  1.00 43.28           C  
ATOM   5761  O   SER B 266      50.994 -20.224  32.780  1.00 45.50           O  
ATOM   5762  CB  SER B 266      48.671 -21.464  30.672  1.00 36.59           C  
ATOM   5763  OG  SER B 266      48.472 -22.428  31.688  1.00 44.87           O  
ATOM   5764  N   LYS B 267      49.585 -18.788  31.786  1.00 41.27           N  
ATOM   5765  CA  LYS B 267      49.700 -17.747  32.782  1.00 35.39           C  
ATOM   5766  C   LYS B 267      48.341 -17.487  33.392  1.00 32.74           C  
ATOM   5767  O   LYS B 267      47.347 -17.362  32.665  1.00 34.60           O  
ATOM   5768  CB  LYS B 267      50.205 -16.486  32.114  1.00 30.41           C  
ATOM   5769  CG  LYS B 267      51.699 -16.268  32.090  1.00 33.18           C  
ATOM   5770  CD  LYS B 267      52.584 -17.210  31.300  1.00 39.92           C  
ATOM   5771  CE  LYS B 267      52.397 -17.064  29.809  1.00 45.11           C  
ATOM   5772  NZ  LYS B 267      53.517 -17.680  29.122  1.00 47.78           N  
ATOM   5773  N   SER B 268      48.264 -17.413  34.708  1.00 30.36           N  
ATOM   5774  CA  SER B 268      47.020 -17.043  35.344  1.00 31.69           C  
ATOM   5775  C   SER B 268      47.236 -15.573  35.610  1.00 29.90           C  
ATOM   5776  O   SER B 268      48.330 -15.164  36.040  1.00 34.97           O  
ATOM   5777  CB  SER B 268      46.838 -17.787  36.650  1.00 29.47           C  
ATOM   5778  OG  SER B 268      45.479 -18.102  36.956  1.00 38.97           O  
ATOM   5779  N   VAL B 269      46.241 -14.777  35.249  1.00 27.02           N  
ATOM   5780  CA  VAL B 269      46.321 -13.349  35.450  1.00 28.75           C  
ATOM   5781  C   VAL B 269      45.215 -12.998  36.404  1.00 30.22           C  
ATOM   5782  O   VAL B 269      44.035 -13.315  36.184  1.00 32.05           O  
ATOM   5783  CB  VAL B 269      46.114 -12.553  34.139  1.00 25.26           C  
ATOM   5784  CG1 VAL B 269      46.214 -11.048  34.384  1.00 21.12           C  
ATOM   5785  CG2 VAL B 269      47.197 -12.933  33.152  1.00 28.12           C  
ATOM   5786  N   THR B 270      45.613 -12.334  37.473  1.00 31.35           N  
ATOM   5787  CA  THR B 270      44.627 -11.875  38.415  1.00 33.15           C  
ATOM   5788  C   THR B 270      44.616 -10.371  38.195  1.00 31.12           C  
ATOM   5789  O   THR B 270      45.653  -9.688  38.156  1.00 32.79           O  
ATOM   5790  CB  THR B 270      45.042 -12.267  39.867  1.00 34.84           C  
ATOM   5791  OG1 THR B 270      45.304 -13.678  39.953  1.00 36.70           O  
ATOM   5792  CG2 THR B 270      43.912 -11.904  40.829  1.00 32.56           C  
ATOM   5793  N   PHE B 271      43.412  -9.879  37.974  1.00 28.18           N  
ATOM   5794  CA  PHE B 271      43.135  -8.484  37.735  1.00 30.71           C  
ATOM   5795  C   PHE B 271      42.911  -7.790  39.067  1.00 35.62           C  
ATOM   5796  O   PHE B 271      42.562  -8.432  40.065  1.00 35.61           O  
ATOM   5797  CB  PHE B 271      41.888  -8.368  36.839  1.00 30.08           C  
ATOM   5798  CG  PHE B 271      42.129  -8.876  35.418  1.00 28.13           C  
ATOM   5799  CD1 PHE B 271      42.750  -8.039  34.482  1.00 26.49           C  
ATOM   5800  CD2 PHE B 271      41.776 -10.178  35.059  1.00 26.48           C  
ATOM   5801  CE1 PHE B 271      43.024  -8.509  33.200  1.00 19.94           C  
ATOM   5802  CE2 PHE B 271      42.057 -10.637  33.769  1.00 29.77           C  
ATOM   5803  CZ  PHE B 271      42.680  -9.807  32.843  1.00 22.29           C  
ATOM   5804  N   GLU B 272      43.113  -6.471  39.115  1.00 37.20           N  
ATOM   5805  CA  GLU B 272      42.902  -5.700  40.330  1.00 38.62           C  
ATOM   5806  C   GLU B 272      41.504  -5.893  40.897  1.00 40.06           C  
ATOM   5807  O   GLU B 272      41.320  -5.884  42.106  1.00 45.57           O  
ATOM   5808  CB  GLU B 272      43.116  -4.214  40.073  1.00 36.65           C  
ATOM   5809  CG  GLU B 272      44.585  -3.825  39.886  1.00 41.96           C  
ATOM   5810  CD  GLU B 272      44.873  -2.337  39.671  1.00 42.08           C  
ATOM   5811  OE1 GLU B 272      44.029  -1.487  39.968  1.00 52.32           O  
ATOM   5812  OE2 GLU B 272      45.961  -2.019  39.204  1.00 43.75           O  
ATOM   5813  N   SER B 273      40.529  -6.163  40.041  1.00 39.24           N  
ATOM   5814  CA  SER B 273      39.152  -6.355  40.447  1.00 39.60           C  
ATOM   5815  C   SER B 273      38.919  -7.666  41.175  1.00 40.04           C  
ATOM   5816  O   SER B 273      37.832  -7.892  41.701  1.00 43.75           O  
ATOM   5817  CB  SER B 273      38.274  -6.325  39.213  1.00 42.30           C  
ATOM   5818  OG  SER B 273      38.757  -7.324  38.315  1.00 37.18           O  
ATOM   5819  N   GLY B 274      39.880  -8.577  41.144  1.00 36.95           N  
ATOM   5820  CA  GLY B 274      39.651  -9.897  41.690  1.00 36.35           C  
ATOM   5821  C   GLY B 274      39.396 -10.890  40.563  1.00 37.69           C  
ATOM   5822  O   GLY B 274      39.514 -12.102  40.778  1.00 37.68           O  
ATOM   5823  N   LYS B 275      39.046 -10.433  39.344  1.00 38.48           N  
ATOM   5824  CA  LYS B 275      38.847 -11.325  38.203  1.00 35.53           C  
ATOM   5825  C   LYS B 275      40.101 -12.130  37.941  1.00 32.81           C  
ATOM   5826  O   LYS B 275      41.208 -11.617  38.104  1.00 33.62           O  
ATOM   5827  CB  LYS B 275      38.542 -10.552  36.941  1.00 44.24           C  
ATOM   5828  CG  LYS B 275      37.177  -9.875  36.896  1.00 54.66           C  
ATOM   5829  CD  LYS B 275      36.312 -10.945  36.180  1.00 72.29           C  
ATOM   5830  CE  LYS B 275      34.862 -10.763  35.651  1.00 76.44           C  
ATOM   5831  NZ  LYS B 275      34.825 -10.835  34.193  1.00 77.76           N  
ATOM   5832  N   LYS B 276      39.944 -13.368  37.529  1.00 33.36           N  
ATOM   5833  CA  LYS B 276      41.090 -14.209  37.261  1.00 34.47           C  
ATOM   5834  C   LYS B 276      40.818 -14.896  35.931  1.00 35.01           C  
ATOM   5835  O   LYS B 276      39.666 -15.292  35.687  1.00 35.46           O  
ATOM   5836  CB  LYS B 276      41.199 -15.174  38.409  1.00 37.96           C  
ATOM   5837  CG  LYS B 276      42.539 -15.840  38.476  1.00 48.45           C  
ATOM   5838  CD  LYS B 276      42.619 -16.364  39.884  1.00 63.52           C  
ATOM   5839  CE  LYS B 276      43.881 -17.162  40.049  1.00 67.25           C  
ATOM   5840  NZ  LYS B 276      43.712 -18.481  39.468  1.00 73.81           N  
ATOM   5841  N   MET B 277      41.813 -15.002  35.041  1.00 31.82           N  
ATOM   5842  CA  MET B 277      41.654 -15.584  33.714  1.00 30.87           C  
ATOM   5843  C   MET B 277      42.993 -16.114  33.280  1.00 29.82           C  
ATOM   5844  O   MET B 277      44.025 -15.575  33.685  1.00 30.15           O  
ATOM   5845  CB  MET B 277      41.234 -14.565  32.657  1.00 33.16           C  
ATOM   5846  CG  MET B 277      39.757 -14.161  32.631  1.00 50.95           C  
ATOM   5847  SD  MET B 277      39.334 -12.818  31.481  1.00 55.85           S  
ATOM   5848  CE  MET B 277      39.281 -13.817  30.018  1.00 54.71           C  
ATOM   5849  N   ASP B 278      42.997 -17.163  32.462  1.00 29.33           N  
ATOM   5850  CA  ASP B 278      44.253 -17.736  31.986  1.00 31.20           C  
ATOM   5851  C   ASP B 278      44.502 -17.411  30.529  1.00 27.65           C  
ATOM   5852  O   ASP B 278      43.564 -17.397  29.719  1.00 25.29           O  
ATOM   5853  CB  ASP B 278      44.287 -19.262  32.071  1.00 42.02           C  
ATOM   5854  CG  ASP B 278      44.021 -19.854  33.442  1.00 46.11           C  
ATOM   5855  OD1 ASP B 278      44.820 -19.630  34.353  1.00 47.01           O  
ATOM   5856  OD2 ASP B 278      43.009 -20.540  33.572  1.00 51.42           O  
ATOM   5857  N   PHE B 279      45.758 -17.199  30.184  1.00 24.79           N  
ATOM   5858  CA  PHE B 279      46.155 -16.877  28.833  1.00 26.11           C  
ATOM   5859  C   PHE B 279      47.415 -17.654  28.526  1.00 28.24           C  
ATOM   5860  O   PHE B 279      48.080 -18.142  29.438  1.00 25.95           O  
ATOM   5861  CB  PHE B 279      46.450 -15.383  28.691  1.00 23.69           C  
ATOM   5862  CG  PHE B 279      45.245 -14.534  29.022  1.00 23.79           C  
ATOM   5863  CD1 PHE B 279      44.217 -14.374  28.085  1.00 24.73           C  
ATOM   5864  CD2 PHE B 279      45.155 -13.948  30.281  1.00 23.62           C  
ATOM   5865  CE1 PHE B 279      43.092 -13.618  28.422  1.00 21.59           C  
ATOM   5866  CE2 PHE B 279      44.023 -13.192  30.609  1.00 24.54           C  
ATOM   5867  CZ  PHE B 279      42.992 -13.028  29.684  1.00 22.56           C  
ATOM   5868  N   ASP B 280      47.738 -17.835  27.251  1.00 27.06           N  
ATOM   5869  CA  ASP B 280      48.986 -18.465  26.882  1.00 26.51           C  
ATOM   5870  C   ASP B 280      50.042 -17.396  26.656  1.00 27.23           C  
ATOM   5871  O   ASP B 280      51.226 -17.726  26.637  1.00 28.54           O  
ATOM   5872  CB  ASP B 280      48.813 -19.279  25.609  1.00 29.00           C  
ATOM   5873  CG  ASP B 280      47.754 -20.352  25.775  1.00 34.93           C  
ATOM   5874  OD1 ASP B 280      48.000 -21.350  26.451  1.00 46.79           O  
ATOM   5875  OD2 ASP B 280      46.667 -20.176  25.237  1.00 40.92           O  
ATOM   5876  N   LEU B 281      49.679 -16.122  26.494  1.00 25.14           N  
ATOM   5877  CA  LEU B 281      50.658 -15.077  26.219  1.00 24.39           C  
ATOM   5878  C   LEU B 281      50.093 -13.793  26.786  1.00 22.71           C  
ATOM   5879  O   LEU B 281      48.881 -13.574  26.717  1.00 23.21           O  
ATOM   5880  CB  LEU B 281      50.850 -14.992  24.697  1.00 28.38           C  
ATOM   5881  CG  LEU B 281      51.964 -14.256  23.929  1.00 26.16           C  
ATOM   5882  CD1 LEU B 281      51.581 -12.818  23.657  1.00 30.51           C  
ATOM   5883  CD2 LEU B 281      53.246 -14.398  24.706  1.00 29.12           C  
ATOM   5884  N   VAL B 282      50.915 -12.947  27.394  1.00 21.17           N  
ATOM   5885  CA  VAL B 282      50.435 -11.691  27.933  1.00 19.04           C  
ATOM   5886  C   VAL B 282      51.394 -10.636  27.414  1.00 22.04           C  
ATOM   5887  O   VAL B 282      52.603 -10.682  27.684  1.00 21.01           O  
ATOM   5888  CB  VAL B 282      50.454 -11.708  29.471  1.00 20.61           C  
ATOM   5889  CG1 VAL B 282      49.915 -10.377  29.990  1.00 18.74           C  
ATOM   5890  CG2 VAL B 282      49.587 -12.844  30.009  1.00 14.94           C  
ATOM   5891  N   MET B 283      50.888  -9.704  26.619  1.00 22.61           N  
ATOM   5892  CA  MET B 283      51.719  -8.662  26.038  1.00 22.48           C  
ATOM   5893  C   MET B 283      51.386  -7.351  26.723  1.00 18.50           C  
ATOM   5894  O   MET B 283      50.215  -6.982  26.823  1.00 20.36           O  
ATOM   5895  CB  MET B 283      51.453  -8.559  24.517  1.00 24.49           C  
ATOM   5896  CG  MET B 283      52.435  -7.625  23.812  1.00 25.23           C  
ATOM   5897  SD  MET B 283      52.113  -7.309  22.062  1.00 24.31           S  
ATOM   5898  CE  MET B 283      51.134  -5.850  22.240  1.00 21.05           C  
ATOM   5899  N   MET B 284      52.372  -6.655  27.259  1.00 17.67           N  
ATOM   5900  CA  MET B 284      52.144  -5.371  27.882  1.00 20.20           C  
ATOM   5901  C   MET B 284      52.376  -4.296  26.825  1.00 21.95           C  
ATOM   5902  O   MET B 284      53.475  -4.161  26.267  1.00 17.55           O  
ATOM   5903  CB  MET B 284      53.116  -5.191  29.051  1.00 22.98           C  
ATOM   5904  CG  MET B 284      52.809  -5.998  30.305  1.00 24.67           C  
ATOM   5905  SD  MET B 284      51.399  -5.373  31.255  1.00 32.72           S  
ATOM   5906  CE  MET B 284      50.924  -6.878  32.066  1.00 32.08           C  
ATOM   5907  N   ALA B 285      51.366  -3.510  26.469  1.00 21.66           N  
ATOM   5908  CA  ALA B 285      51.555  -2.436  25.511  1.00 23.67           C  
ATOM   5909  C   ALA B 285      50.989  -1.196  26.158  1.00 24.37           C  
ATOM   5910  O   ALA B 285      50.124  -0.467  25.679  1.00 27.73           O  
ATOM   5911  CB  ALA B 285      50.809  -2.762  24.232  1.00 28.43           C  
ATOM   5912  N   ILE B 286      51.552  -0.978  27.331  1.00 25.74           N  
ATOM   5913  CA  ILE B 286      51.085   0.080  28.203  1.00 23.31           C  
ATOM   5914  C   ILE B 286      51.713   1.406  27.841  1.00 20.22           C  
ATOM   5915  O   ILE B 286      51.071   2.434  28.007  1.00 24.94           O  
ATOM   5916  CB  ILE B 286      51.378  -0.416  29.669  1.00 26.64           C  
ATOM   5917  CG1 ILE B 286      50.210  -1.302  30.053  1.00 23.40           C  
ATOM   5918  CG2 ILE B 286      51.543   0.696  30.688  1.00 31.01           C  
ATOM   5919  CD1 ILE B 286      50.399  -2.001  31.409  1.00 38.55           C  
ATOM   5920  N   GLY B 287      52.937   1.489  27.344  1.00 16.95           N  
ATOM   5921  CA  GLY B 287      53.487   2.786  27.026  1.00 15.26           C  
ATOM   5922  C   GLY B 287      54.921   2.621  26.624  1.00 15.07           C  
ATOM   5923  O   GLY B 287      55.433   1.501  26.698  1.00 19.33           O  
ATOM   5924  N   ARG B 288      55.518   3.695  26.127  1.00 17.52           N  
ATOM   5925  CA  ARG B 288      56.915   3.741  25.718  1.00 21.68           C  
ATOM   5926  C   ARG B 288      57.587   4.920  26.399  1.00 21.80           C  
ATOM   5927  O   ARG B 288      57.013   6.011  26.416  1.00 22.93           O  
ATOM   5928  CB  ARG B 288      57.027   3.912  24.204  1.00 21.64           C  
ATOM   5929  CG  ARG B 288      56.579   2.626  23.525  1.00 20.75           C  
ATOM   5930  CD  ARG B 288      56.752   2.638  22.028  1.00 22.26           C  
ATOM   5931  NE  ARG B 288      58.137   2.808  21.593  1.00 22.68           N  
ATOM   5932  CZ  ARG B 288      59.037   1.825  21.467  1.00 19.88           C  
ATOM   5933  NH1 ARG B 288      58.757   0.550  21.753  1.00 14.14           N  
ATOM   5934  NH2 ARG B 288      60.241   2.125  20.972  1.00 18.33           N  
ATOM   5935  N   SER B 289      58.790   4.747  26.923  1.00 24.29           N  
ATOM   5936  CA  SER B 289      59.485   5.808  27.641  1.00 26.71           C  
ATOM   5937  C   SER B 289      60.731   6.214  26.880  1.00 25.73           C  
ATOM   5938  O   SER B 289      61.357   5.309  26.326  1.00 27.77           O  
ATOM   5939  CB  SER B 289      59.881   5.307  29.027  1.00 29.52           C  
ATOM   5940  OG  SER B 289      58.795   4.662  29.704  1.00 38.31           O  
ATOM   5941  N   PRO B 290      61.147   7.484  26.796  1.00 26.11           N  
ATOM   5942  CA  PRO B 290      62.427   7.902  26.218  1.00 27.11           C  
ATOM   5943  C   PRO B 290      63.598   7.137  26.807  1.00 31.24           C  
ATOM   5944  O   PRO B 290      63.647   6.990  28.037  1.00 36.17           O  
ATOM   5945  CB  PRO B 290      62.505   9.356  26.512  1.00 25.28           C  
ATOM   5946  CG  PRO B 290      61.060   9.796  26.574  1.00 26.95           C  
ATOM   5947  CD  PRO B 290      60.381   8.631  27.273  1.00 26.47           C  
ATOM   5948  N   ARG B 291      64.518   6.559  26.037  1.00 32.98           N  
ATOM   5949  CA  ARG B 291      65.636   5.919  26.680  1.00 36.66           C  
ATOM   5950  C   ARG B 291      66.882   6.778  26.759  1.00 40.42           C  
ATOM   5951  O   ARG B 291      67.717   6.954  25.875  1.00 40.35           O  
ATOM   5952  CB  ARG B 291      65.950   4.598  26.013  1.00 34.97           C  
ATOM   5953  CG  ARG B 291      66.220   4.379  24.579  1.00 36.55           C  
ATOM   5954  CD  ARG B 291      66.452   2.897  24.708  1.00 38.32           C  
ATOM   5955  NE  ARG B 291      66.834   2.271  23.467  1.00 42.27           N  
ATOM   5956  CZ  ARG B 291      67.217   0.994  23.415  1.00 44.94           C  
ATOM   5957  NH1 ARG B 291      67.279   0.193  24.481  1.00 48.04           N  
ATOM   5958  NH2 ARG B 291      67.546   0.490  22.237  1.00 55.89           N  
ATOM   5959  N   THR B 292      66.868   7.377  27.939  1.00 43.49           N  
ATOM   5960  CA  THR B 292      67.879   8.308  28.403  1.00 45.73           C  
ATOM   5961  C   THR B 292      68.969   7.747  29.317  1.00 46.81           C  
ATOM   5962  O   THR B 292      70.107   8.222  29.260  1.00 46.35           O  
ATOM   5963  CB  THR B 292      67.151   9.453  29.105  1.00 43.82           C  
ATOM   5964  OG1 THR B 292      66.127   8.866  29.910  1.00 48.46           O  
ATOM   5965  CG2 THR B 292      66.552  10.427  28.124  1.00 45.04           C  
ATOM   5966  N   LYS B 293      68.670   6.711  30.122  1.00 49.78           N  
ATOM   5967  CA  LYS B 293      69.575   6.230  31.162  1.00 51.60           C  
ATOM   5968  C   LYS B 293      70.991   5.883  30.739  1.00 52.20           C  
ATOM   5969  O   LYS B 293      71.921   6.400  31.347  1.00 54.23           O  
ATOM   5970  CB  LYS B 293      68.978   4.997  31.889  1.00 54.24           C  
ATOM   5971  CG  LYS B 293      69.105   3.607  31.282  1.00 60.39           C  
ATOM   5972  CD  LYS B 293      68.493   2.532  32.172  1.00 73.61           C  
ATOM   5973  CE  LYS B 293      69.070   1.157  31.812  1.00 74.84           C  
ATOM   5974  NZ  LYS B 293      68.827   0.765  30.432  1.00 81.68           N  
ATOM   5975  N   ASP B 294      71.193   5.117  29.665  1.00 51.37           N  
ATOM   5976  CA  ASP B 294      72.525   4.725  29.246  1.00 52.30           C  
ATOM   5977  C   ASP B 294      73.317   5.841  28.598  1.00 52.33           C  
ATOM   5978  O   ASP B 294      74.529   5.717  28.421  1.00 57.11           O  
ATOM   5979  CB  ASP B 294      72.439   3.574  28.269  1.00 54.54           C  
ATOM   5980  CG  ASP B 294      71.680   2.387  28.825  1.00 59.00           C  
ATOM   5981  OD1 ASP B 294      72.007   1.951  29.931  1.00 68.78           O  
ATOM   5982  OD2 ASP B 294      70.764   1.910  28.151  1.00 62.16           O  
ATOM   5983  N   LEU B 295      72.678   6.956  28.234  1.00 49.42           N  
ATOM   5984  CA  LEU B 295      73.382   8.056  27.590  1.00 49.56           C  
ATOM   5985  C   LEU B 295      74.348   8.783  28.521  1.00 50.84           C  
ATOM   5986  O   LEU B 295      75.223   9.514  28.057  1.00 47.66           O  
ATOM   5987  CB  LEU B 295      72.393   9.083  27.043  1.00 46.13           C  
ATOM   5988  CG  LEU B 295      71.406   8.708  25.953  1.00 39.39           C  
ATOM   5989  CD1 LEU B 295      70.576   9.940  25.621  1.00 39.24           C  
ATOM   5990  CD2 LEU B 295      72.132   8.194  24.725  1.00 40.79           C  
ATOM   5991  N   GLN B 296      74.183   8.595  29.836  1.00 53.76           N  
ATOM   5992  CA  GLN B 296      74.980   9.223  30.879  1.00 55.55           C  
ATOM   5993  C   GLN B 296      74.926  10.730  30.727  1.00 56.04           C  
ATOM   5994  O   GLN B 296      75.904  11.473  30.810  1.00 56.95           O  
ATOM   5995  CB  GLN B 296      76.430   8.721  30.808  1.00 56.41           C  
ATOM   5996  CG  GLN B 296      76.584   7.242  31.117  1.00 67.64           C  
ATOM   5997  CD  GLN B 296      76.112   6.919  32.523  1.00 76.98           C  
ATOM   5998  OE1 GLN B 296      76.764   7.008  33.564  1.00 80.68           O  
ATOM   5999  NE2 GLN B 296      74.904   6.367  32.543  1.00 81.57           N  
ATOM   6000  N   LEU B 297      73.699  11.224  30.581  1.00 57.05           N  
ATOM   6001  CA  LEU B 297      73.458  12.642  30.354  1.00 57.78           C  
ATOM   6002  C   LEU B 297      74.014  13.594  31.414  1.00 58.54           C  
ATOM   6003  O   LEU B 297      74.361  14.753  31.130  1.00 60.46           O  
ATOM   6004  CB  LEU B 297      71.951  12.828  30.193  1.00 54.23           C  
ATOM   6005  CG  LEU B 297      71.321  12.230  28.938  1.00 46.80           C  
ATOM   6006  CD1 LEU B 297      69.832  12.442  28.984  1.00 45.70           C  
ATOM   6007  CD2 LEU B 297      71.886  12.888  27.697  1.00 37.01           C  
ATOM   6008  N   GLN B 298      74.182  13.071  32.638  1.00 58.83           N  
ATOM   6009  CA  GLN B 298      74.729  13.851  33.728  1.00 58.73           C  
ATOM   6010  C   GLN B 298      76.194  14.212  33.434  1.00 56.19           C  
ATOM   6011  O   GLN B 298      76.592  15.337  33.696  1.00 54.51           O  
ATOM   6012  CB  GLN B 298      74.550  13.045  35.043  1.00 60.60           C  
ATOM   6013  CG  GLN B 298      75.500  11.933  35.492  1.00 65.98           C  
ATOM   6014  CD  GLN B 298      75.296  10.517  34.973  1.00 70.56           C  
ATOM   6015  OE1 GLN B 298      74.444   9.752  35.397  1.00 71.00           O  
ATOM   6016  NE2 GLN B 298      76.305  10.001  34.281  1.00 79.31           N  
ATOM   6017  N   ASN B 299      76.990  13.385  32.755  1.00 55.95           N  
ATOM   6018  CA  ASN B 299      78.378  13.675  32.391  1.00 56.79           C  
ATOM   6019  C   ASN B 299      78.555  14.896  31.498  1.00 58.66           C  
ATOM   6020  O   ASN B 299      79.682  15.299  31.205  1.00 63.05           O  
ATOM   6021  CB  ASN B 299      79.012  12.470  31.675  1.00 59.00           C  
ATOM   6022  CG  ASN B 299      79.209  11.284  32.564  1.00 64.76           C  
ATOM   6023  OD1 ASN B 299      78.841  11.146  33.731  1.00 64.94           O  
ATOM   6024  ND2 ASN B 299      79.313  10.173  31.840  1.00 68.51           N  
ATOM   6025  N   ALA B 300      77.485  15.513  30.993  1.00 57.07           N  
ATOM   6026  CA  ALA B 300      77.614  16.727  30.209  1.00 53.18           C  
ATOM   6027  C   ALA B 300      76.566  17.725  30.651  1.00 51.17           C  
ATOM   6028  O   ALA B 300      76.487  18.825  30.117  1.00 50.92           O  
ATOM   6029  CB  ALA B 300      77.418  16.434  28.733  1.00 57.88           C  
ATOM   6030  N   GLY B 301      75.736  17.372  31.624  1.00 49.79           N  
ATOM   6031  CA  GLY B 301      74.746  18.302  32.138  1.00 51.47           C  
ATOM   6032  C   GLY B 301      73.551  18.492  31.219  1.00 51.82           C  
ATOM   6033  O   GLY B 301      72.937  19.564  31.167  1.00 52.41           O  
ATOM   6034  N   VAL B 302      73.175  17.467  30.457  1.00 51.62           N  
ATOM   6035  CA  VAL B 302      72.006  17.611  29.616  1.00 50.50           C  
ATOM   6036  C   VAL B 302      70.809  17.409  30.541  1.00 50.95           C  
ATOM   6037  O   VAL B 302      70.757  16.477  31.343  1.00 48.35           O  
ATOM   6038  CB  VAL B 302      72.080  16.576  28.487  1.00 51.20           C  
ATOM   6039  CG1 VAL B 302      70.915  16.786  27.538  1.00 52.97           C  
ATOM   6040  CG2 VAL B 302      73.375  16.746  27.693  1.00 52.31           C  
ATOM   6041  N   MET B 303      69.869  18.343  30.472  1.00 53.84           N  
ATOM   6042  CA  MET B 303      68.697  18.350  31.333  1.00 57.72           C  
ATOM   6043  C   MET B 303      67.539  17.551  30.769  1.00 59.37           C  
ATOM   6044  O   MET B 303      67.207  17.738  29.594  1.00 58.73           O  
ATOM   6045  CB  MET B 303      68.308  19.789  31.525  1.00 60.65           C  
ATOM   6046  CG  MET B 303      67.125  20.032  32.419  1.00 70.19           C  
ATOM   6047  SD  MET B 303      67.488  21.486  33.421  1.00 81.87           S  
ATOM   6048  CE  MET B 303      68.310  20.600  34.723  1.00 83.11           C  
ATOM   6049  N   ILE B 304      66.951  16.629  31.535  1.00 59.69           N  
ATOM   6050  CA  ILE B 304      65.752  15.923  31.097  1.00 60.09           C  
ATOM   6051  C   ILE B 304      64.596  16.544  31.865  1.00 60.32           C  
ATOM   6052  O   ILE B 304      64.824  17.156  32.908  1.00 61.61           O  
ATOM   6053  CB  ILE B 304      65.793  14.379  31.391  1.00 59.57           C  
ATOM   6054  CG1 ILE B 304      65.678  14.017  32.860  1.00 62.16           C  
ATOM   6055  CG2 ILE B 304      67.104  13.864  30.844  1.00 58.59           C  
ATOM   6056  CD1 ILE B 304      64.400  13.195  33.162  1.00 69.72           C  
ATOM   6057  N   LYS B 305      63.368  16.475  31.374  1.00 62.93           N  
ATOM   6058  CA  LYS B 305      62.257  16.996  32.126  1.00 65.45           C  
ATOM   6059  C   LYS B 305      61.353  15.798  32.334  1.00 66.82           C  
ATOM   6060  O   LYS B 305      61.734  14.922  33.110  1.00 69.81           O  
ATOM   6061  CB  LYS B 305      61.576  18.116  31.339  1.00 67.78           C  
ATOM   6062  CG  LYS B 305      60.541  18.803  32.214  1.00 70.86           C  
ATOM   6063  CD  LYS B 305      60.060  20.113  31.618  1.00 78.97           C  
ATOM   6064  CE  LYS B 305      58.797  20.513  32.375  1.00 83.16           C  
ATOM   6065  NZ  LYS B 305      58.327  21.831  31.983  1.00 85.27           N  
ATOM   6066  N   ASN B 306      60.223  15.598  31.647  1.00 66.43           N  
ATOM   6067  CA  ASN B 306      59.336  14.487  31.989  1.00 65.16           C  
ATOM   6068  C   ASN B 306      59.773  13.244  31.264  1.00 61.69           C  
ATOM   6069  O   ASN B 306      59.317  12.925  30.163  1.00 63.96           O  
ATOM   6070  CB  ASN B 306      57.879  14.800  31.620  1.00 71.89           C  
ATOM   6071  CG  ASN B 306      57.265  15.832  32.555  1.00 80.02           C  
ATOM   6072  OD1 ASN B 306      57.351  15.739  33.781  1.00 88.18           O  
ATOM   6073  ND2 ASN B 306      56.671  16.895  32.015  1.00 85.52           N  
ATOM   6074  N   GLY B 307      60.811  12.636  31.824  1.00 58.93           N  
ATOM   6075  CA  GLY B 307      61.380  11.400  31.315  1.00 54.34           C  
ATOM   6076  C   GLY B 307      62.251  11.553  30.074  1.00 51.51           C  
ATOM   6077  O   GLY B 307      63.202  10.785  29.894  1.00 51.89           O  
ATOM   6078  N   GLY B 308      61.929  12.507  29.204  1.00 46.68           N  
ATOM   6079  CA  GLY B 308      62.696  12.726  28.005  1.00 43.77           C  
ATOM   6080  C   GLY B 308      63.528  13.972  28.141  1.00 41.33           C  
ATOM   6081  O   GLY B 308      63.323  14.789  29.041  1.00 41.91           O  
ATOM   6082  N   VAL B 309      64.486  14.069  27.235  1.00 39.00           N  
ATOM   6083  CA  VAL B 309      65.419  15.172  27.145  1.00 37.36           C  
ATOM   6084  C   VAL B 309      64.709  16.483  26.869  1.00 39.01           C  
ATOM   6085  O   VAL B 309      63.929  16.565  25.926  1.00 40.89           O  
ATOM   6086  CB  VAL B 309      66.435  14.896  26.019  1.00 36.04           C  
ATOM   6087  CG1 VAL B 309      67.422  16.035  25.937  1.00 33.26           C  
ATOM   6088  CG2 VAL B 309      67.206  13.621  26.283  1.00 27.84           C  
ATOM   6089  N   GLN B 310      64.992  17.520  27.642  1.00 41.78           N  
ATOM   6090  CA  GLN B 310      64.378  18.811  27.434  1.00 45.57           C  
ATOM   6091  C   GLN B 310      65.099  19.473  26.266  1.00 46.14           C  
ATOM   6092  O   GLN B 310      66.336  19.564  26.258  1.00 48.96           O  
ATOM   6093  CB  GLN B 310      64.527  19.640  28.701  1.00 51.30           C  
ATOM   6094  CG  GLN B 310      63.712  20.928  28.751  1.00 61.05           C  
ATOM   6095  CD  GLN B 310      63.998  21.784  29.986  1.00 63.72           C  
ATOM   6096  OE1 GLN B 310      65.145  22.059  30.338  1.00 62.72           O  
ATOM   6097  NE2 GLN B 310      62.976  22.268  30.692  1.00 67.19           N  
ATOM   6098  N   VAL B 311      64.339  19.902  25.261  1.00 45.99           N  
ATOM   6099  CA  VAL B 311      64.838  20.586  24.072  1.00 41.19           C  
ATOM   6100  C   VAL B 311      63.974  21.818  23.862  1.00 42.36           C  
ATOM   6101  O   VAL B 311      62.836  21.873  24.343  1.00 40.38           O  
ATOM   6102  CB  VAL B 311      64.754  19.718  22.776  1.00 37.74           C  
ATOM   6103  CG1 VAL B 311      65.752  18.587  22.870  1.00 34.41           C  
ATOM   6104  CG2 VAL B 311      63.347  19.158  22.571  1.00 33.48           C  
ATOM   6105  N   ASP B 312      64.490  22.863  23.223  1.00 44.68           N  
ATOM   6106  CA  ASP B 312      63.672  24.016  22.891  1.00 46.61           C  
ATOM   6107  C   ASP B 312      63.043  23.724  21.535  1.00 48.85           C  
ATOM   6108  O   ASP B 312      63.448  22.763  20.873  1.00 48.41           O  
ATOM   6109  CB  ASP B 312      64.547  25.269  22.824  1.00 45.71           C  
ATOM   6110  CG  ASP B 312      65.642  25.313  21.763  1.00 45.33           C  
ATOM   6111  OD1 ASP B 312      66.021  24.299  21.183  1.00 49.15           O  
ATOM   6112  OD2 ASP B 312      66.134  26.403  21.516  1.00 57.46           O  
ATOM   6113  N   GLU B 313      62.185  24.591  20.997  1.00 51.52           N  
ATOM   6114  CA  GLU B 313      61.527  24.309  19.726  1.00 52.16           C  
ATOM   6115  C   GLU B 313      62.448  24.087  18.525  1.00 50.04           C  
ATOM   6116  O   GLU B 313      61.979  23.645  17.481  1.00 52.71           O  
ATOM   6117  CB  GLU B 313      60.514  25.432  19.415  1.00 58.09           C  
ATOM   6118  CG  GLU B 313      60.976  26.834  18.997  1.00 76.16           C  
ATOM   6119  CD  GLU B 313      61.533  27.808  20.041  1.00 86.11           C  
ATOM   6120  OE1 GLU B 313      61.522  27.530  21.243  1.00 91.87           O  
ATOM   6121  OE2 GLU B 313      61.977  28.880  19.630  1.00 90.23           O  
ATOM   6122  N   TYR B 314      63.758  24.346  18.643  1.00 47.67           N  
ATOM   6123  CA  TYR B 314      64.709  24.030  17.588  1.00 46.56           C  
ATOM   6124  C   TYR B 314      65.532  22.786  17.921  1.00 45.63           C  
ATOM   6125  O   TYR B 314      66.615  22.592  17.369  1.00 46.06           O  
ATOM   6126  CB  TYR B 314      65.646  25.218  17.357  1.00 45.12           C  
ATOM   6127  CG  TYR B 314      64.961  26.396  16.686  1.00 49.32           C  
ATOM   6128  CD1 TYR B 314      64.902  26.470  15.290  1.00 49.58           C  
ATOM   6129  CD2 TYR B 314      64.389  27.405  17.468  1.00 52.78           C  
ATOM   6130  CE1 TYR B 314      64.271  27.555  14.676  1.00 50.92           C  
ATOM   6131  CE2 TYR B 314      63.757  28.491  16.858  1.00 52.70           C  
ATOM   6132  CZ  TYR B 314      63.705  28.556  15.466  1.00 56.78           C  
ATOM   6133  OH  TYR B 314      63.093  29.639  14.873  1.00 61.80           O  
ATOM   6134  N   SER B 315      65.064  21.933  18.832  1.00 46.87           N  
ATOM   6135  CA  SER B 315      65.716  20.688  19.261  1.00 48.47           C  
ATOM   6136  C   SER B 315      67.087  20.786  19.935  1.00 47.82           C  
ATOM   6137  O   SER B 315      67.791  19.789  20.130  1.00 44.76           O  
ATOM   6138  CB  SER B 315      65.808  19.723  18.063  1.00 48.56           C  
ATOM   6139  OG  SER B 315      64.510  19.331  17.612  1.00 47.88           O  
ATOM   6140  N   ARG B 316      67.494  21.993  20.336  1.00 50.82           N  
ATOM   6141  CA  ARG B 316      68.728  22.183  21.099  1.00 55.13           C  
ATOM   6142  C   ARG B 316      68.382  21.918  22.549  1.00 56.09           C  
ATOM   6143  O   ARG B 316      67.263  22.275  22.950  1.00 54.41           O  
ATOM   6144  CB  ARG B 316      69.257  23.602  21.063  1.00 59.53           C  
ATOM   6145  CG  ARG B 316      69.541  24.203  19.714  1.00 63.35           C  
ATOM   6146  CD  ARG B 316      70.265  25.510  19.969  1.00 66.99           C  
ATOM   6147  NE  ARG B 316      70.069  26.383  18.831  1.00 69.34           N  
ATOM   6148  CZ  ARG B 316      69.018  27.205  18.763  1.00 69.56           C  
ATOM   6149  NH1 ARG B 316      68.111  27.261  19.739  1.00 69.54           N  
ATOM   6150  NH2 ARG B 316      68.864  27.972  17.687  1.00 71.67           N  
ATOM   6151  N   THR B 317      69.279  21.296  23.315  1.00 57.61           N  
ATOM   6152  CA  THR B 317      69.000  21.055  24.716  1.00 61.30           C  
ATOM   6153  C   THR B 317      69.508  22.277  25.490  1.00 63.56           C  
ATOM   6154  O   THR B 317      69.407  23.412  25.022  1.00 65.61           O  
ATOM   6155  CB  THR B 317      69.704  19.731  25.167  1.00 60.25           C  
ATOM   6156  OG1 THR B 317      71.102  19.994  25.279  1.00 61.76           O  
ATOM   6157  CG2 THR B 317      69.459  18.584  24.209  1.00 60.57           C  
ATOM   6158  N   ASN B 318      70.083  22.110  26.685  1.00 66.73           N  
ATOM   6159  CA  ASN B 318      70.613  23.242  27.433  1.00 68.20           C  
ATOM   6160  C   ASN B 318      72.144  23.337  27.376  1.00 68.10           C  
ATOM   6161  O   ASN B 318      72.757  24.269  27.896  1.00 67.82           O  
ATOM   6162  CB  ASN B 318      70.118  23.143  28.887  1.00 69.72           C  
ATOM   6163  CG  ASN B 318      70.716  22.028  29.744  1.00 68.97           C  
ATOM   6164  OD1 ASN B 318      70.650  20.859  29.400  1.00 79.79           O  
ATOM   6165  ND2 ASN B 318      71.647  22.333  30.646  1.00 66.71           N  
ATOM   6166  N   VAL B 319      72.796  22.376  26.722  1.00 67.61           N  
ATOM   6167  CA  VAL B 319      74.239  22.389  26.538  1.00 66.80           C  
ATOM   6168  C   VAL B 319      74.353  22.668  25.044  1.00 68.45           C  
ATOM   6169  O   VAL B 319      73.972  21.829  24.230  1.00 69.66           O  
ATOM   6170  CB  VAL B 319      74.814  21.018  26.906  1.00 63.82           C  
ATOM   6171  CG1 VAL B 319      76.309  21.000  26.681  1.00 63.99           C  
ATOM   6172  CG2 VAL B 319      74.503  20.718  28.350  1.00 61.50           C  
ATOM   6173  N   SER B 320      74.956  23.774  24.622  1.00 69.96           N  
ATOM   6174  CA  SER B 320      74.920  24.220  23.229  1.00 70.11           C  
ATOM   6175  C   SER B 320      75.562  23.316  22.183  1.00 68.77           C  
ATOM   6176  O   SER B 320      75.421  23.496  20.970  1.00 69.15           O  
ATOM   6177  CB  SER B 320      75.560  25.607  23.167  1.00 72.19           C  
ATOM   6178  OG  SER B 320      75.129  26.460  24.229  1.00 79.68           O  
ATOM   6179  N   ASN B 321      76.311  22.335  22.657  1.00 66.09           N  
ATOM   6180  CA  ASN B 321      76.973  21.407  21.773  1.00 61.59           C  
ATOM   6181  C   ASN B 321      76.057  20.245  21.357  1.00 58.10           C  
ATOM   6182  O   ASN B 321      76.197  19.665  20.273  1.00 56.16           O  
ATOM   6183  CB  ASN B 321      78.210  20.945  22.524  1.00 57.83           C  
ATOM   6184  CG  ASN B 321      79.119  20.167  21.603  1.00 58.50           C  
ATOM   6185  OD1 ASN B 321      79.564  20.633  20.573  1.00 65.93           O  
ATOM   6186  ND2 ASN B 321      79.477  18.942  21.944  1.00 64.92           N  
ATOM   6187  N   ILE B 322      75.072  19.969  22.217  1.00 54.55           N  
ATOM   6188  CA  ILE B 322      74.213  18.798  22.129  1.00 52.15           C  
ATOM   6189  C   ILE B 322      72.763  19.146  21.841  1.00 48.71           C  
ATOM   6190  O   ILE B 322      72.145  20.029  22.440  1.00 46.69           O  
ATOM   6191  CB  ILE B 322      74.339  18.003  23.471  1.00 53.10           C  
ATOM   6192  CG1 ILE B 322      75.816  17.668  23.754  1.00 57.39           C  
ATOM   6193  CG2 ILE B 322      73.541  16.705  23.390  1.00 51.75           C  
ATOM   6194  CD1 ILE B 322      76.184  17.185  25.172  1.00 57.78           C  
ATOM   6195  N   TYR B 323      72.210  18.352  20.939  1.00 47.31           N  
ATOM   6196  CA  TYR B 323      70.837  18.502  20.484  1.00 44.33           C  
ATOM   6197  C   TYR B 323      70.168  17.141  20.600  1.00 40.65           C  
ATOM   6198  O   TYR B 323      70.853  16.110  20.650  1.00 39.72           O  
ATOM   6199  CB  TYR B 323      70.772  18.933  19.016  1.00 42.57           C  
ATOM   6200  CG  TYR B 323      71.898  19.852  18.587  1.00 42.09           C  
ATOM   6201  CD1 TYR B 323      71.853  21.217  18.883  1.00 39.66           C  
ATOM   6202  CD2 TYR B 323      72.992  19.298  17.921  1.00 40.98           C  
ATOM   6203  CE1 TYR B 323      72.917  22.043  18.514  1.00 43.10           C  
ATOM   6204  CE2 TYR B 323      74.054  20.116  17.553  1.00 45.14           C  
ATOM   6205  CZ  TYR B 323      74.011  21.475  17.847  1.00 43.39           C  
ATOM   6206  OH  TYR B 323      75.096  22.226  17.419  1.00 48.25           O  
ATOM   6207  N   ALA B 324      68.843  17.089  20.641  1.00 37.67           N  
ATOM   6208  CA  ALA B 324      68.138  15.821  20.700  1.00 36.56           C  
ATOM   6209  C   ALA B 324      66.865  15.898  19.864  1.00 34.66           C  
ATOM   6210  O   ALA B 324      66.167  16.919  19.838  1.00 29.68           O  
ATOM   6211  CB  ALA B 324      67.750  15.477  22.141  1.00 36.15           C  
ATOM   6212  N   ILE B 325      66.577  14.834  19.114  1.00 32.84           N  
ATOM   6213  CA  ILE B 325      65.363  14.742  18.310  1.00 32.06           C  
ATOM   6214  C   ILE B 325      64.737  13.352  18.456  1.00 30.09           C  
ATOM   6215  O   ILE B 325      65.327  12.407  19.009  1.00 28.14           O  
ATOM   6216  CB  ILE B 325      65.653  15.051  16.763  1.00 28.89           C  
ATOM   6217  CG1 ILE B 325      66.772  14.225  16.173  1.00 29.10           C  
ATOM   6218  CG2 ILE B 325      66.102  16.483  16.616  1.00 24.13           C  
ATOM   6219  CD1 ILE B 325      66.333  12.898  15.565  1.00 28.63           C  
ATOM   6220  N   GLY B 326      63.499  13.209  17.976  1.00 28.35           N  
ATOM   6221  CA  GLY B 326      62.809  11.930  17.951  1.00 26.30           C  
ATOM   6222  C   GLY B 326      62.060  11.597  19.231  1.00 25.00           C  
ATOM   6223  O   GLY B 326      61.677  12.469  19.996  1.00 26.83           O  
ATOM   6224  N   ASP B 327      61.883  10.320  19.499  1.00 23.26           N  
ATOM   6225  CA  ASP B 327      61.154   9.858  20.659  1.00 24.46           C  
ATOM   6226  C   ASP B 327      61.741  10.240  21.994  1.00 24.03           C  
ATOM   6227  O   ASP B 327      60.980  10.508  22.920  1.00 25.11           O  
ATOM   6228  CB  ASP B 327      61.035   8.364  20.562  1.00 23.33           C  
ATOM   6229  CG  ASP B 327      60.028   7.883  19.535  1.00 23.14           C  
ATOM   6230  OD1 ASP B 327      59.569   8.653  18.692  1.00 21.95           O  
ATOM   6231  OD2 ASP B 327      59.692   6.707  19.577  1.00 17.57           O  
ATOM   6232  N   VAL B 328      63.069  10.351  22.066  1.00 26.72           N  
ATOM   6233  CA  VAL B 328      63.745  10.745  23.288  1.00 25.40           C  
ATOM   6234  C   VAL B 328      63.318  12.140  23.752  1.00 28.90           C  
ATOM   6235  O   VAL B 328      63.473  12.446  24.934  1.00 31.44           O  
ATOM   6236  CB  VAL B 328      65.295  10.639  23.046  1.00 26.77           C  
ATOM   6237  CG1 VAL B 328      65.904  11.858  22.333  1.00 18.33           C  
ATOM   6238  CG2 VAL B 328      65.916  10.396  24.414  1.00 23.64           C  
ATOM   6239  N   THR B 329      62.765  13.004  22.892  1.00 29.62           N  
ATOM   6240  CA  THR B 329      62.298  14.319  23.311  1.00 28.79           C  
ATOM   6241  C   THR B 329      60.860  14.277  23.789  1.00 30.55           C  
ATOM   6242  O   THR B 329      60.338  15.246  24.348  1.00 32.47           O  
ATOM   6243  CB  THR B 329      62.408  15.329  22.163  1.00 30.06           C  
ATOM   6244  OG1 THR B 329      61.723  14.814  21.035  1.00 36.58           O  
ATOM   6245  CG2 THR B 329      63.824  15.527  21.724  1.00 33.88           C  
ATOM   6246  N   ASN B 330      60.188  13.153  23.519  1.00 31.99           N  
ATOM   6247  CA  ASN B 330      58.823  12.916  23.949  1.00 34.82           C  
ATOM   6248  C   ASN B 330      57.817  13.992  23.520  1.00 36.42           C  
ATOM   6249  O   ASN B 330      57.035  14.523  24.316  1.00 40.11           O  
ATOM   6250  CB  ASN B 330      58.883  12.762  25.457  1.00 38.75           C  
ATOM   6251  CG  ASN B 330      57.682  12.119  26.120  1.00 45.08           C  
ATOM   6252  OD1 ASN B 330      56.770  11.553  25.514  1.00 47.11           O  
ATOM   6253  ND2 ASN B 330      57.725  12.150  27.447  1.00 50.42           N  
ATOM   6254  N   ARG B 331      57.862  14.393  22.244  1.00 37.12           N  
ATOM   6255  CA  ARG B 331      56.906  15.361  21.725  1.00 36.54           C  
ATOM   6256  C   ARG B 331      55.869  14.551  20.960  1.00 35.38           C  
ATOM   6257  O   ARG B 331      54.860  14.173  21.559  1.00 37.78           O  
ATOM   6258  CB  ARG B 331      57.584  16.370  20.789  1.00 35.18           C  
ATOM   6259  CG  ARG B 331      58.544  17.370  21.406  1.00 35.22           C  
ATOM   6260  CD  ARG B 331      59.823  17.318  20.586  1.00 31.06           C  
ATOM   6261  NE  ARG B 331      60.289  18.626  20.168  1.00 29.95           N  
ATOM   6262  CZ  ARG B 331      61.429  18.771  19.487  1.00 32.66           C  
ATOM   6263  NH1 ARG B 331      62.198  17.723  19.164  1.00 22.74           N  
ATOM   6264  NH2 ARG B 331      61.795  19.999  19.120  1.00 31.75           N  
ATOM   6265  N   VAL B 332      56.037  14.228  19.667  1.00 34.05           N  
ATOM   6266  CA  VAL B 332      55.099  13.385  18.921  1.00 33.19           C  
ATOM   6267  C   VAL B 332      55.961  12.197  18.510  1.00 28.46           C  
ATOM   6268  O   VAL B 332      56.988  12.323  17.836  1.00 33.71           O  
ATOM   6269  CB  VAL B 332      54.530  14.120  17.661  1.00 32.34           C  
ATOM   6270  CG1 VAL B 332      53.501  13.214  17.017  1.00 29.90           C  
ATOM   6271  CG2 VAL B 332      53.837  15.436  18.015  1.00 27.04           C  
ATOM   6272  N   MET B 333      55.580  11.024  18.982  1.00 23.85           N  
ATOM   6273  CA  MET B 333      56.381   9.841  18.712  1.00 22.63           C  
ATOM   6274  C   MET B 333      55.949   9.148  17.439  1.00 20.56           C  
ATOM   6275  O   MET B 333      55.247   8.133  17.459  1.00 18.84           O  
ATOM   6276  CB  MET B 333      56.299   8.842  19.884  1.00 22.61           C  
ATOM   6277  CG  MET B 333      56.945   9.303  21.196  1.00 25.17           C  
ATOM   6278  SD  MET B 333      57.154   7.967  22.413  1.00 32.56           S  
ATOM   6279  CE  MET B 333      57.728   8.910  23.794  1.00 27.53           C  
ATOM   6280  N   LEU B 334      56.339   9.718  16.300  1.00 20.50           N  
ATOM   6281  CA  LEU B 334      56.029   9.167  14.986  1.00 19.94           C  
ATOM   6282  C   LEU B 334      57.268   9.258  14.090  1.00 15.67           C  
ATOM   6283  O   LEU B 334      57.950  10.280  14.145  1.00 17.83           O  
ATOM   6284  CB  LEU B 334      54.840   9.958  14.400  1.00 13.14           C  
ATOM   6285  CG  LEU B 334      53.464   9.809  15.086  1.00 11.40           C  
ATOM   6286  CD1 LEU B 334      52.493  10.817  14.531  1.00 14.07           C  
ATOM   6287  CD2 LEU B 334      52.904   8.434  14.843  1.00  4.74           C  
ATOM   6288  N   THR B 335      57.632   8.250  13.271  1.00 19.22           N  
ATOM   6289  CA  THR B 335      58.761   8.331  12.335  1.00 20.02           C  
ATOM   6290  C   THR B 335      58.805   9.621  11.495  1.00 20.15           C  
ATOM   6291  O   THR B 335      59.848  10.283  11.507  1.00 23.33           O  
ATOM   6292  CB  THR B 335      58.699   7.093  11.429  1.00 21.54           C  
ATOM   6293  OG1 THR B 335      59.138   6.026  12.247  1.00 20.81           O  
ATOM   6294  CG2 THR B 335      59.548   7.158  10.176  1.00 22.84           C  
ATOM   6295  N   PRO B 336      57.754  10.092  10.797  1.00 20.66           N  
ATOM   6296  CA  PRO B 336      57.819  11.286   9.964  1.00 19.00           C  
ATOM   6297  C   PRO B 336      58.171  12.520  10.773  1.00 21.43           C  
ATOM   6298  O   PRO B 336      58.882  13.399  10.283  1.00 23.85           O  
ATOM   6299  CB  PRO B 336      56.457  11.350   9.326  1.00 20.11           C  
ATOM   6300  CG  PRO B 336      55.951   9.934   9.355  1.00 20.80           C  
ATOM   6301  CD  PRO B 336      56.404   9.518  10.727  1.00 15.91           C  
ATOM   6302  N   VAL B 337      57.707  12.606  12.030  1.00 20.61           N  
ATOM   6303  CA  VAL B 337      58.046  13.737  12.893  1.00 22.68           C  
ATOM   6304  C   VAL B 337      59.546  13.647  13.231  1.00 22.85           C  
ATOM   6305  O   VAL B 337      60.250  14.660  13.137  1.00 23.91           O  
ATOM   6306  CB  VAL B 337      57.140  13.706  14.176  1.00 20.65           C  
ATOM   6307  CG1 VAL B 337      57.523  14.821  15.138  1.00 23.88           C  
ATOM   6308  CG2 VAL B 337      55.697  14.005  13.819  1.00 17.00           C  
ATOM   6309  N   ALA B 338      60.110  12.473  13.543  1.00 20.73           N  
ATOM   6310  CA  ALA B 338      61.534  12.344  13.841  1.00 19.15           C  
ATOM   6311  C   ALA B 338      62.406  12.726  12.648  1.00 23.14           C  
ATOM   6312  O   ALA B 338      63.422  13.413  12.799  1.00 28.11           O  
ATOM   6313  CB  ALA B 338      61.875  10.910  14.226  1.00 13.86           C  
ATOM   6314  N   ILE B 339      62.015  12.296  11.445  1.00 24.20           N  
ATOM   6315  CA  ILE B 339      62.702  12.626  10.211  1.00 23.18           C  
ATOM   6316  C   ILE B 339      62.610  14.136   9.976  1.00 25.30           C  
ATOM   6317  O   ILE B 339      63.605  14.793   9.635  1.00 28.95           O  
ATOM   6318  CB  ILE B 339      62.028  11.776   9.089  1.00 21.27           C  
ATOM   6319  CG1 ILE B 339      62.523  10.361   9.227  1.00 16.55           C  
ATOM   6320  CG2 ILE B 339      62.341  12.271   7.690  1.00 20.48           C  
ATOM   6321  CD1 ILE B 339      61.846   9.399   8.238  1.00 20.14           C  
ATOM   6322  N   ASN B 340      61.454  14.750  10.219  1.00 26.72           N  
ATOM   6323  CA  ASN B 340      61.284  16.177   9.986  1.00 30.74           C  
ATOM   6324  C   ASN B 340      62.174  16.999  10.896  1.00 32.33           C  
ATOM   6325  O   ASN B 340      62.846  17.933  10.453  1.00 33.02           O  
ATOM   6326  CB  ASN B 340      59.851  16.619  10.229  1.00 34.69           C  
ATOM   6327  CG  ASN B 340      59.557  17.944   9.540  1.00 37.41           C  
ATOM   6328  OD1 ASN B 340      58.978  17.926   8.464  1.00 42.74           O  
ATOM   6329  ND2 ASN B 340      59.888  19.135  10.041  1.00 38.27           N  
ATOM   6330  N   GLU B 341      62.185  16.648  12.186  1.00 33.61           N  
ATOM   6331  CA  GLU B 341      63.001  17.313  13.188  1.00 31.34           C  
ATOM   6332  C   GLU B 341      64.481  17.179  12.892  1.00 31.63           C  
ATOM   6333  O   GLU B 341      65.232  18.135  13.092  1.00 29.73           O  
ATOM   6334  CB  GLU B 341      62.740  16.729  14.554  1.00 28.72           C  
ATOM   6335  CG  GLU B 341      61.416  17.080  15.196  1.00 21.89           C  
ATOM   6336  CD  GLU B 341      61.134  16.316  16.483  1.00 23.58           C  
ATOM   6337  OE1 GLU B 341      61.841  15.385  16.836  1.00 23.45           O  
ATOM   6338  OE2 GLU B 341      60.188  16.650  17.168  1.00 28.96           O  
ATOM   6339  N   ALA B 342      64.891  15.995  12.423  1.00 31.44           N  
ATOM   6340  CA  ALA B 342      66.270  15.737  12.042  1.00 34.26           C  
ATOM   6341  C   ALA B 342      66.705  16.659  10.906  1.00 37.46           C  
ATOM   6342  O   ALA B 342      67.764  17.284  11.000  1.00 40.73           O  
ATOM   6343  CB  ALA B 342      66.427  14.305  11.583  1.00 29.04           C  
ATOM   6344  N   ALA B 343      65.909  16.819   9.842  1.00 39.28           N  
ATOM   6345  CA  ALA B 343      66.256  17.734   8.763  1.00 37.89           C  
ATOM   6346  C   ALA B 343      66.269  19.181   9.271  1.00 39.03           C  
ATOM   6347  O   ALA B 343      67.202  19.944   8.996  1.00 41.27           O  
ATOM   6348  CB  ALA B 343      65.241  17.594   7.641  1.00 32.48           C  
ATOM   6349  N   ALA B 344      65.293  19.576  10.091  1.00 39.13           N  
ATOM   6350  CA  ALA B 344      65.227  20.915  10.661  1.00 39.49           C  
ATOM   6351  C   ALA B 344      66.401  21.208  11.591  1.00 43.00           C  
ATOM   6352  O   ALA B 344      66.882  22.344  11.613  1.00 45.54           O  
ATOM   6353  CB  ALA B 344      63.925  21.086  11.443  1.00 32.84           C  
ATOM   6354  N   LEU B 345      66.926  20.215  12.329  1.00 44.47           N  
ATOM   6355  CA  LEU B 345      68.095  20.424  13.185  1.00 45.62           C  
ATOM   6356  C   LEU B 345      69.351  20.579  12.328  1.00 45.58           C  
ATOM   6357  O   LEU B 345      70.111  21.528  12.545  1.00 43.62           O  
ATOM   6358  CB  LEU B 345      68.293  19.238  14.175  1.00 42.14           C  
ATOM   6359  CG  LEU B 345      69.332  19.252  15.334  1.00 39.73           C  
ATOM   6360  CD1 LEU B 345      70.732  18.884  14.853  1.00 34.95           C  
ATOM   6361  CD2 LEU B 345      69.279  20.624  15.991  1.00 34.67           C  
ATOM   6362  N   VAL B 346      69.628  19.705  11.349  1.00 45.62           N  
ATOM   6363  CA  VAL B 346      70.818  19.838  10.525  1.00 44.12           C  
ATOM   6364  C   VAL B 346      70.787  21.150   9.749  1.00 47.58           C  
ATOM   6365  O   VAL B 346      71.848  21.740   9.547  1.00 50.37           O  
ATOM   6366  CB  VAL B 346      70.906  18.609   9.609  1.00 41.31           C  
ATOM   6367  CG1 VAL B 346      72.020  18.708   8.585  1.00 40.41           C  
ATOM   6368  CG2 VAL B 346      71.264  17.426  10.490  1.00 33.08           C  
ATOM   6369  N   ASP B 347      69.626  21.681   9.378  1.00 49.09           N  
ATOM   6370  CA  ASP B 347      69.549  22.984   8.737  1.00 52.71           C  
ATOM   6371  C   ASP B 347      69.869  24.112   9.709  1.00 55.48           C  
ATOM   6372  O   ASP B 347      70.773  24.891   9.424  1.00 56.40           O  
ATOM   6373  CB  ASP B 347      68.160  23.169   8.146  1.00 53.91           C  
ATOM   6374  CG  ASP B 347      68.055  22.692   6.701  1.00 52.51           C  
ATOM   6375  OD1 ASP B 347      68.597  21.641   6.330  1.00 50.54           O  
ATOM   6376  OD2 ASP B 347      67.412  23.401   5.933  1.00 59.62           O  
ATOM   6377  N   THR B 348      69.231  24.210  10.874  1.00 58.31           N  
ATOM   6378  CA  THR B 348      69.545  25.211  11.896  1.00 60.55           C  
ATOM   6379  C   THR B 348      71.012  25.177  12.379  1.00 62.27           C  
ATOM   6380  O   THR B 348      71.512  26.157  12.934  1.00 63.64           O  
ATOM   6381  CB  THR B 348      68.569  24.980  13.095  1.00 59.81           C  
ATOM   6382  OG1 THR B 348      67.260  25.071  12.550  1.00 53.82           O  
ATOM   6383  CG2 THR B 348      68.728  25.975  14.241  1.00 59.31           C  
ATOM   6384  N   VAL B 349      71.715  24.044  12.259  1.00 62.89           N  
ATOM   6385  CA  VAL B 349      73.074  23.928  12.768  1.00 63.41           C  
ATOM   6386  C   VAL B 349      74.131  24.140  11.696  1.00 65.03           C  
ATOM   6387  O   VAL B 349      75.058  24.933  11.846  1.00 64.49           O  
ATOM   6388  CB  VAL B 349      73.273  22.521  13.434  1.00 62.04           C  
ATOM   6389  CG1 VAL B 349      74.693  22.331  13.934  1.00 55.84           C  
ATOM   6390  CG2 VAL B 349      72.378  22.413  14.650  1.00 60.55           C  
ATOM   6391  N   PHE B 350      74.049  23.355  10.635  1.00 67.31           N  
ATOM   6392  CA  PHE B 350      75.052  23.416   9.595  1.00 68.93           C  
ATOM   6393  C   PHE B 350      74.587  24.213   8.394  1.00 68.87           C  
ATOM   6394  O   PHE B 350      75.310  24.309   7.404  1.00 69.61           O  
ATOM   6395  CB  PHE B 350      75.411  21.999   9.165  1.00 73.41           C  
ATOM   6396  CG  PHE B 350      75.902  21.091  10.281  1.00 78.11           C  
ATOM   6397  CD1 PHE B 350      76.966  21.471  11.098  1.00 74.83           C  
ATOM   6398  CD2 PHE B 350      75.286  19.851  10.464  1.00 82.08           C  
ATOM   6399  CE1 PHE B 350      77.418  20.604  12.090  1.00 81.06           C  
ATOM   6400  CE2 PHE B 350      75.746  18.990  11.463  1.00 84.85           C  
ATOM   6401  CZ  PHE B 350      76.811  19.364  12.278  1.00 78.85           C  
ATOM   6402  N   GLY B 351      73.381  24.753   8.423  1.00 69.51           N  
ATOM   6403  CA  GLY B 351      72.862  25.514   7.314  1.00 70.67           C  
ATOM   6404  C   GLY B 351      72.760  26.946   7.736  1.00 72.66           C  
ATOM   6405  O   GLY B 351      73.230  27.347   8.802  1.00 71.42           O  
ATOM   6406  N   THR B 352      72.104  27.688   6.854  1.00 75.70           N  
ATOM   6407  CA  THR B 352      72.049  29.117   7.083  1.00 79.29           C  
ATOM   6408  C   THR B 352      70.782  29.511   7.813  1.00 79.76           C  
ATOM   6409  O   THR B 352      70.780  30.313   8.750  1.00 81.28           O  
ATOM   6410  CB  THR B 352      72.169  29.862   5.715  1.00 81.16           C  
ATOM   6411  OG1 THR B 352      72.124  31.262   5.965  1.00 83.50           O  
ATOM   6412  CG2 THR B 352      71.047  29.504   4.746  1.00 79.94           C  
ATOM   6413  N   THR B 353      69.669  28.959   7.379  1.00 79.12           N  
ATOM   6414  CA  THR B 353      68.448  29.379   8.000  1.00 78.23           C  
ATOM   6415  C   THR B 353      67.944  28.280   8.951  1.00 74.37           C  
ATOM   6416  O   THR B 353      68.008  27.082   8.646  1.00 73.42           O  
ATOM   6417  CB  THR B 353      67.572  29.834   6.751  1.00 82.47           C  
ATOM   6418  OG1 THR B 353      66.352  30.371   7.236  1.00 89.03           O  
ATOM   6419  CG2 THR B 353      67.290  28.723   5.759  1.00 84.12           C  
ATOM   6420  N   PRO B 354      67.579  28.673  10.183  1.00 72.52           N  
ATOM   6421  CA  PRO B 354      67.000  27.824  11.209  1.00 70.68           C  
ATOM   6422  C   PRO B 354      65.602  27.428  10.802  1.00 69.48           C  
ATOM   6423  O   PRO B 354      64.784  28.269  10.405  1.00 70.80           O  
ATOM   6424  CB  PRO B 354      67.003  28.646  12.471  1.00 73.61           C  
ATOM   6425  CG  PRO B 354      67.914  29.800  12.156  1.00 74.56           C  
ATOM   6426  CD  PRO B 354      67.682  30.034  10.683  1.00 71.42           C  
ATOM   6427  N   ARG B 355      65.366  26.133  10.847  1.00 66.84           N  
ATOM   6428  CA  ARG B 355      64.079  25.570  10.544  1.00 60.79           C  
ATOM   6429  C   ARG B 355      63.687  24.854  11.834  1.00 55.65           C  
ATOM   6430  O   ARG B 355      64.539  24.399  12.600  1.00 51.99           O  
ATOM   6431  CB  ARG B 355      64.252  24.614   9.378  1.00 64.37           C  
ATOM   6432  CG  ARG B 355      62.981  24.464   8.563  1.00 68.02           C  
ATOM   6433  CD  ARG B 355      62.918  23.096   7.913  1.00 72.42           C  
ATOM   6434  NE  ARG B 355      64.073  22.808   7.081  1.00 74.69           N  
ATOM   6435  CZ  ARG B 355      64.349  21.559   6.689  1.00 80.03           C  
ATOM   6436  NH1 ARG B 355      63.591  20.519   7.044  1.00 84.39           N  
ATOM   6437  NH2 ARG B 355      65.384  21.339   5.886  1.00 84.70           N  
ATOM   6438  N   LYS B 356      62.397  24.829  12.141  1.00 52.89           N  
ATOM   6439  CA  LYS B 356      61.877  24.074  13.270  1.00 50.11           C  
ATOM   6440  C   LYS B 356      60.641  23.326  12.777  1.00 47.89           C  
ATOM   6441  O   LYS B 356      59.957  23.778  11.850  1.00 49.65           O  
ATOM   6442  CB  LYS B 356      61.498  25.002  14.432  1.00 46.95           C  
ATOM   6443  CG  LYS B 356      60.447  26.050  14.135  1.00 49.19           C  
ATOM   6444  CD  LYS B 356      60.021  26.778  15.385  1.00 44.66           C  
ATOM   6445  CE  LYS B 356      58.940  27.750  14.959  1.00 54.82           C  
ATOM   6446  NZ  LYS B 356      59.171  29.071  15.511  1.00 57.47           N  
ATOM   6447  N   THR B 357      60.376  22.142  13.315  1.00 43.63           N  
ATOM   6448  CA  THR B 357      59.211  21.356  12.957  1.00 37.99           C  
ATOM   6449  C   THR B 357      57.922  21.904  13.549  1.00 36.70           C  
ATOM   6450  O   THR B 357      57.816  22.234  14.741  1.00 38.38           O  
ATOM   6451  CB  THR B 357      59.396  19.905  13.438  1.00 33.53           C  
ATOM   6452  OG1 THR B 357      60.579  19.456  12.806  1.00 37.39           O  
ATOM   6453  CG2 THR B 357      58.260  18.957  13.097  1.00 29.85           C  
ATOM   6454  N   ASP B 358      56.896  21.918  12.710  1.00 35.61           N  
ATOM   6455  CA  ASP B 358      55.565  22.215  13.186  1.00 33.05           C  
ATOM   6456  C   ASP B 358      54.999  20.869  13.645  1.00 32.43           C  
ATOM   6457  O   ASP B 358      55.021  19.846  12.967  1.00 32.30           O  
ATOM   6458  CB  ASP B 358      54.734  22.826  12.051  1.00 33.76           C  
ATOM   6459  CG  ASP B 358      53.330  23.283  12.430  1.00 33.35           C  
ATOM   6460  OD1 ASP B 358      52.953  23.209  13.592  1.00 34.05           O  
ATOM   6461  OD2 ASP B 358      52.606  23.713  11.543  1.00 42.05           O  
ATOM   6462  N   HIS B 359      54.631  20.845  14.918  1.00 31.72           N  
ATOM   6463  CA  HIS B 359      54.102  19.640  15.516  1.00 30.36           C  
ATOM   6464  C   HIS B 359      52.601  19.631  15.502  1.00 31.46           C  
ATOM   6465  O   HIS B 359      52.037  18.673  15.991  1.00 35.35           O  
ATOM   6466  CB  HIS B 359      54.583  19.516  16.964  1.00 31.60           C  
ATOM   6467  CG  HIS B 359      56.079  19.274  17.035  1.00 28.86           C  
ATOM   6468  ND1 HIS B 359      57.100  20.117  17.144  1.00 27.03           N  
ATOM   6469  CD2 HIS B 359      56.599  18.018  16.922  1.00 29.30           C  
ATOM   6470  CE1 HIS B 359      58.207  19.430  17.093  1.00 19.31           C  
ATOM   6471  NE2 HIS B 359      57.889  18.167  16.959  1.00 22.64           N  
ATOM   6472  N   THR B 360      51.934  20.688  15.068  1.00 28.68           N  
ATOM   6473  CA  THR B 360      50.485  20.654  15.057  1.00 28.65           C  
ATOM   6474  C   THR B 360      49.985  20.133  13.718  1.00 27.87           C  
ATOM   6475  O   THR B 360      50.744  20.110  12.751  1.00 30.15           O  
ATOM   6476  CB  THR B 360      49.963  22.062  15.332  1.00 28.98           C  
ATOM   6477  OG1 THR B 360      50.504  22.912  14.341  1.00 29.50           O  
ATOM   6478  CG2 THR B 360      50.354  22.555  16.716  1.00 30.17           C  
ATOM   6479  N   ARG B 361      48.720  19.693  13.649  1.00 24.65           N  
ATOM   6480  CA  ARG B 361      48.093  19.221  12.427  1.00 22.58           C  
ATOM   6481  C   ARG B 361      48.850  18.108  11.721  1.00 23.37           C  
ATOM   6482  O   ARG B 361      48.844  18.002  10.495  1.00 26.87           O  
ATOM   6483  CB  ARG B 361      47.899  20.424  11.499  1.00 21.15           C  
ATOM   6484  CG  ARG B 361      46.975  21.452  12.146  1.00 25.31           C  
ATOM   6485  CD  ARG B 361      47.092  22.785  11.450  1.00 29.55           C  
ATOM   6486  NE  ARG B 361      48.453  23.298  11.473  1.00 36.77           N  
ATOM   6487  CZ  ARG B 361      48.843  24.306  10.679  1.00 38.59           C  
ATOM   6488  NH1 ARG B 361      48.025  24.911   9.810  1.00 36.65           N  
ATOM   6489  NH2 ARG B 361      50.098  24.723  10.750  1.00 38.80           N  
ATOM   6490  N   VAL B 362      49.500  17.220  12.476  1.00 22.34           N  
ATOM   6491  CA  VAL B 362      50.222  16.089  11.897  1.00 19.31           C  
ATOM   6492  C   VAL B 362      49.163  15.013  11.708  1.00 20.28           C  
ATOM   6493  O   VAL B 362      48.401  14.726  12.631  1.00 21.38           O  
ATOM   6494  CB  VAL B 362      51.328  15.609  12.868  1.00 20.89           C  
ATOM   6495  CG1 VAL B 362      52.050  14.401  12.313  1.00 19.81           C  
ATOM   6496  CG2 VAL B 362      52.349  16.720  13.064  1.00 23.34           C  
ATOM   6497  N   ALA B 363      49.061  14.456  10.511  1.00 16.74           N  
ATOM   6498  CA  ALA B 363      48.101  13.401  10.263  1.00 15.51           C  
ATOM   6499  C   ALA B 363      48.728  12.099  10.717  1.00 17.41           C  
ATOM   6500  O   ALA B 363      49.955  11.931  10.701  1.00 15.00           O  
ATOM   6501  CB  ALA B 363      47.794  13.298   8.788  1.00 14.96           C  
ATOM   6502  N   SER B 364      47.901  11.168  11.150  1.00 12.84           N  
ATOM   6503  CA  SER B 364      48.421   9.888  11.565  1.00 13.79           C  
ATOM   6504  C   SER B 364      47.326   8.858  11.384  1.00 11.60           C  
ATOM   6505  O   SER B 364      46.185   9.187  11.059  1.00 16.14           O  
ATOM   6506  CB  SER B 364      48.895   9.992  13.033  1.00 11.16           C  
ATOM   6507  OG  SER B 364      47.879  10.184  14.007  1.00 17.15           O  
ATOM   6508  N   ALA B 365      47.661   7.600  11.611  1.00 12.20           N  
ATOM   6509  CA  ALA B 365      46.756   6.494  11.407  1.00 13.04           C  
ATOM   6510  C   ALA B 365      46.926   5.486  12.524  1.00 11.37           C  
ATOM   6511  O   ALA B 365      47.975   5.453  13.180  1.00 11.33           O  
ATOM   6512  CB  ALA B 365      47.095   5.806  10.109  1.00  6.33           C  
ATOM   6513  N   VAL B 366      45.902   4.676  12.715  1.00 12.05           N  
ATOM   6514  CA  VAL B 366      45.960   3.515  13.591  1.00 14.47           C  
ATOM   6515  C   VAL B 366      45.643   2.414  12.579  1.00 14.17           C  
ATOM   6516  O   VAL B 366      44.618   2.460  11.887  1.00 16.01           O  
ATOM   6517  CB  VAL B 366      44.853   3.510  14.718  1.00 16.23           C  
ATOM   6518  CG1 VAL B 366      44.915   2.255  15.597  1.00  7.99           C  
ATOM   6519  CG2 VAL B 366      45.070   4.688  15.628  1.00 14.97           C  
ATOM   6520  N   PHE B 367      46.520   1.433  12.436  1.00 16.05           N  
ATOM   6521  CA  PHE B 367      46.248   0.304  11.559  1.00 15.55           C  
ATOM   6522  C   PHE B 367      45.500  -0.857  12.211  1.00 13.74           C  
ATOM   6523  O   PHE B 367      45.951  -1.997  12.252  1.00 18.65           O  
ATOM   6524  CB  PHE B 367      47.577  -0.193  10.939  1.00  9.97           C  
ATOM   6525  CG  PHE B 367      48.093   0.809   9.911  1.00 13.24           C  
ATOM   6526  CD1 PHE B 367      47.625   0.755   8.593  1.00 17.38           C  
ATOM   6527  CD2 PHE B 367      49.013   1.794  10.274  1.00 13.54           C  
ATOM   6528  CE1 PHE B 367      48.072   1.692   7.661  1.00 12.94           C  
ATOM   6529  CE2 PHE B 367      49.459   2.733   9.332  1.00 16.11           C  
ATOM   6530  CZ  PHE B 367      48.989   2.676   8.022  1.00 12.38           C  
ATOM   6531  N   SER B 368      44.365  -0.532  12.803  1.00 11.72           N  
ATOM   6532  CA  SER B 368      43.438  -1.533  13.274  1.00 10.45           C  
ATOM   6533  C   SER B 368      42.687  -2.085  12.079  1.00 15.21           C  
ATOM   6534  O   SER B 368      42.838  -1.621  10.952  1.00 18.53           O  
ATOM   6535  CB  SER B 368      42.463  -0.906  14.216  1.00 11.37           C  
ATOM   6536  OG  SER B 368      42.200   0.422  13.783  1.00 10.48           O  
ATOM   6537  N   ILE B 369      41.867  -3.115  12.244  1.00 18.37           N  
ATOM   6538  CA  ILE B 369      41.002  -3.593  11.176  1.00 16.08           C  
ATOM   6539  C   ILE B 369      39.568  -3.308  11.666  1.00 18.16           C  
ATOM   6540  O   ILE B 369      39.130  -4.029  12.568  1.00 16.51           O  
ATOM   6541  CB  ILE B 369      41.300  -5.091  10.989  1.00 18.03           C  
ATOM   6542  CG1 ILE B 369      42.745  -5.266  10.550  1.00 11.00           C  
ATOM   6543  CG2 ILE B 369      40.318  -5.692   9.994  1.00 14.06           C  
ATOM   6544  CD1 ILE B 369      43.240  -6.699  10.746  1.00 13.44           C  
ATOM   6545  N   PRO B 370      38.778  -2.318  11.206  1.00 18.11           N  
ATOM   6546  CA  PRO B 370      39.108  -1.298  10.196  1.00 17.29           C  
ATOM   6547  C   PRO B 370      40.050  -0.201  10.693  1.00 16.93           C  
ATOM   6548  O   PRO B 370      40.102  -0.008  11.916  1.00 20.50           O  
ATOM   6549  CB  PRO B 370      37.756  -0.780   9.785  1.00 18.27           C  
ATOM   6550  CG  PRO B 370      37.065  -0.747  11.124  1.00 22.09           C  
ATOM   6551  CD  PRO B 370      37.410  -2.118  11.666  1.00 18.95           C  
ATOM   6552  N   PRO B 371      40.829   0.502   9.857  1.00 12.69           N  
ATOM   6553  CA  PRO B 371      41.813   1.484  10.312  1.00  8.94           C  
ATOM   6554  C   PRO B 371      41.222   2.839  10.624  1.00  9.56           C  
ATOM   6555  O   PRO B 371      40.065   3.115  10.275  1.00  8.79           O  
ATOM   6556  CB  PRO B 371      42.822   1.510   9.188  1.00 12.01           C  
ATOM   6557  CG  PRO B 371      41.956   1.301   7.974  1.00  9.96           C  
ATOM   6558  CD  PRO B 371      41.030   0.202   8.450  1.00 12.85           C  
ATOM   6559  N   ILE B 372      42.035   3.693  11.248  1.00  9.63           N  
ATOM   6560  CA  ILE B 372      41.667   5.075  11.569  1.00 10.52           C  
ATOM   6561  C   ILE B 372      42.659   6.007  10.875  1.00  8.55           C  
ATOM   6562  O   ILE B 372      43.846   5.676  10.776  1.00  7.99           O  
ATOM   6563  CB  ILE B 372      41.719   5.330  13.126  1.00 13.34           C  
ATOM   6564  CG1 ILE B 372      40.482   4.708  13.723  1.00 10.97           C  
ATOM   6565  CG2 ILE B 372      41.790   6.822  13.505  1.00  5.59           C  
ATOM   6566  CD1 ILE B 372      40.548   4.795  15.244  1.00 20.19           C  
ATOM   6567  N   GLY B 373      42.203   7.152  10.389  1.00  5.92           N  
ATOM   6568  CA  GLY B 373      43.082   8.188   9.873  1.00  4.81           C  
ATOM   6569  C   GLY B 373      42.663   9.464  10.583  1.00  5.35           C  
ATOM   6570  O   GLY B 373      41.458   9.695  10.738  1.00  6.47           O  
ATOM   6571  N   THR B 374      43.543  10.335  11.038  1.00  8.35           N  
ATOM   6572  CA  THR B 374      43.110  11.477  11.823  1.00 10.33           C  
ATOM   6573  C   THR B 374      44.101  12.604  11.623  1.00  9.43           C  
ATOM   6574  O   THR B 374      45.301  12.359  11.463  1.00  8.85           O  
ATOM   6575  CB  THR B 374      43.017  10.997  13.313  1.00 13.78           C  
ATOM   6576  OG1 THR B 374      42.495  12.075  14.100  1.00 13.26           O  
ATOM   6577  CG2 THR B 374      44.353  10.590  13.891  1.00  8.45           C  
ATOM   6578  N   CYS B 375      43.612  13.836  11.611  1.00 11.05           N  
ATOM   6579  CA  CYS B 375      44.456  15.009  11.518  1.00 14.72           C  
ATOM   6580  C   CYS B 375      43.763  16.113  12.302  1.00 14.57           C  
ATOM   6581  O   CYS B 375      42.542  16.295  12.193  1.00 16.26           O  
ATOM   6582  CB  CYS B 375      44.607  15.421  10.055  1.00 17.95           C  
ATOM   6583  SG  CYS B 375      45.859  16.718   9.860  1.00 26.45           S  
ATOM   6584  N   GLY B 376      44.472  16.831  13.161  1.00 16.73           N  
ATOM   6585  CA  GLY B 376      43.841  17.979  13.774  1.00 19.52           C  
ATOM   6586  C   GLY B 376      43.284  17.655  15.147  1.00 23.41           C  
ATOM   6587  O   GLY B 376      43.574  16.613  15.729  1.00 25.49           O  
ATOM   6588  N   LEU B 377      42.473  18.567  15.664  1.00 24.00           N  
ATOM   6589  CA  LEU B 377      41.902  18.478  16.992  1.00 18.03           C  
ATOM   6590  C   LEU B 377      40.665  17.632  17.074  1.00 19.03           C  
ATOM   6591  O   LEU B 377      39.920  17.464  16.105  1.00 20.40           O  
ATOM   6592  CB  LEU B 377      41.515  19.873  17.519  1.00 21.74           C  
ATOM   6593  CG  LEU B 377      42.601  20.962  17.421  1.00 19.41           C  
ATOM   6594  CD1 LEU B 377      42.061  22.295  17.873  1.00 17.72           C  
ATOM   6595  CD2 LEU B 377      43.780  20.606  18.311  1.00 18.57           C  
ATOM   6596  N   ILE B 378      40.451  17.082  18.265  1.00 19.03           N  
ATOM   6597  CA  ILE B 378      39.212  16.403  18.592  1.00 17.74           C  
ATOM   6598  C   ILE B 378      38.377  17.468  19.300  1.00 21.49           C  
ATOM   6599  O   ILE B 378      38.883  18.473  19.830  1.00 22.03           O  
ATOM   6600  CB  ILE B 378      39.410  15.151  19.517  1.00 16.81           C  
ATOM   6601  CG1 ILE B 378      40.006  15.503  20.862  1.00 17.80           C  
ATOM   6602  CG2 ILE B 378      40.356  14.177  18.844  1.00 16.18           C  
ATOM   6603  CD1 ILE B 378      39.991  14.302  21.832  1.00 12.31           C  
ATOM   6604  N   GLU B 379      37.062  17.339  19.189  1.00 23.74           N  
ATOM   6605  CA  GLU B 379      36.157  18.358  19.653  1.00 25.55           C  
ATOM   6606  C   GLU B 379      36.317  18.709  21.114  1.00 30.28           C  
ATOM   6607  O   GLU B 379      36.097  19.858  21.482  1.00 33.99           O  
ATOM   6608  CB  GLU B 379      34.742  17.907  19.358  1.00 23.60           C  
ATOM   6609  CG  GLU B 379      34.162  16.718  20.098  1.00 18.96           C  
ATOM   6610  CD  GLU B 379      32.987  16.147  19.342  1.00 23.61           C  
ATOM   6611  OE1 GLU B 379      33.199  15.670  18.243  1.00 32.28           O  
ATOM   6612  OE2 GLU B 379      31.882  16.151  19.842  1.00 32.52           O  
ATOM   6613  N   GLU B 380      36.785  17.766  21.933  1.00 31.19           N  
ATOM   6614  CA  GLU B 380      36.962  18.045  23.356  1.00 31.29           C  
ATOM   6615  C   GLU B 380      38.012  19.121  23.586  1.00 29.42           C  
ATOM   6616  O   GLU B 380      37.816  19.993  24.437  1.00 32.80           O  
ATOM   6617  CB  GLU B 380      37.392  16.808  24.158  1.00 34.24           C  
ATOM   6618  CG  GLU B 380      36.310  15.741  24.353  1.00 43.63           C  
ATOM   6619  CD  GLU B 380      36.194  14.682  23.256  1.00 46.31           C  
ATOM   6620  OE1 GLU B 380      36.666  14.875  22.136  1.00 46.59           O  
ATOM   6621  OE2 GLU B 380      35.624  13.632  23.535  1.00 47.37           O  
ATOM   6622  N   VAL B 381      39.120  19.132  22.832  1.00 25.68           N  
ATOM   6623  CA  VAL B 381      40.097  20.200  23.024  1.00 29.00           C  
ATOM   6624  C   VAL B 381      39.668  21.368  22.133  1.00 29.77           C  
ATOM   6625  O   VAL B 381      39.963  22.513  22.487  1.00 34.88           O  
ATOM   6626  CB  VAL B 381      41.628  19.733  22.727  1.00 21.58           C  
ATOM   6627  CG1 VAL B 381      41.654  18.194  22.668  1.00 25.04           C  
ATOM   6628  CG2 VAL B 381      42.246  20.548  21.582  1.00 22.11           C  
ATOM   6629  N   ALA B 382      38.940  21.154  21.032  1.00 31.05           N  
ATOM   6630  CA  ALA B 382      38.536  22.267  20.193  1.00 31.22           C  
ATOM   6631  C   ALA B 382      37.572  23.164  20.951  1.00 32.62           C  
ATOM   6632  O   ALA B 382      37.756  24.382  20.931  1.00 33.17           O  
ATOM   6633  CB  ALA B 382      37.838  21.787  18.936  1.00 29.73           C  
ATOM   6634  N   SER B 383      36.599  22.611  21.669  1.00 32.46           N  
ATOM   6635  CA  SER B 383      35.651  23.419  22.397  1.00 38.20           C  
ATOM   6636  C   SER B 383      36.299  24.098  23.592  1.00 42.65           C  
ATOM   6637  O   SER B 383      35.757  25.055  24.135  1.00 48.85           O  
ATOM   6638  CB  SER B 383      34.485  22.557  22.855  1.00 34.23           C  
ATOM   6639  OG  SER B 383      34.860  21.346  23.484  1.00 37.13           O  
ATOM   6640  N   LYS B 384      37.456  23.631  24.045  1.00 44.74           N  
ATOM   6641  CA  LYS B 384      38.125  24.301  25.134  1.00 44.64           C  
ATOM   6642  C   LYS B 384      38.871  25.483  24.539  1.00 41.46           C  
ATOM   6643  O   LYS B 384      38.976  26.516  25.186  1.00 44.45           O  
ATOM   6644  CB  LYS B 384      39.066  23.300  25.816  1.00 54.30           C  
ATOM   6645  CG  LYS B 384      39.926  23.910  26.918  1.00 70.26           C  
ATOM   6646  CD  LYS B 384      39.726  23.271  28.298  1.00 78.24           C  
ATOM   6647  CE  LYS B 384      39.416  24.327  29.391  1.00 83.39           C  
ATOM   6648  NZ  LYS B 384      40.498  25.275  29.625  1.00 81.03           N  
ATOM   6649  N   ARG B 385      39.405  25.394  23.322  1.00 39.02           N  
ATOM   6650  CA  ARG B 385      40.171  26.488  22.754  1.00 38.46           C  
ATOM   6651  C   ARG B 385      39.384  27.463  21.887  1.00 40.72           C  
ATOM   6652  O   ARG B 385      39.936  28.503  21.492  1.00 40.47           O  
ATOM   6653  CB  ARG B 385      41.310  26.004  21.872  1.00 44.86           C  
ATOM   6654  CG  ARG B 385      42.277  24.954  22.366  1.00 51.42           C  
ATOM   6655  CD  ARG B 385      43.518  25.104  21.490  1.00 62.97           C  
ATOM   6656  NE  ARG B 385      44.224  23.864  21.190  1.00 73.57           N  
ATOM   6657  CZ  ARG B 385      44.883  23.109  22.085  1.00 76.08           C  
ATOM   6658  NH1 ARG B 385      44.964  23.419  23.386  1.00 86.61           N  
ATOM   6659  NH2 ARG B 385      45.490  22.002  21.651  1.00 79.55           N  
ATOM   6660  N   TYR B 386      38.138  27.180  21.489  1.00 38.52           N  
ATOM   6661  CA  TYR B 386      37.390  28.063  20.605  1.00 34.66           C  
ATOM   6662  C   TYR B 386      36.009  28.308  21.156  1.00 36.33           C  
ATOM   6663  O   TYR B 386      35.433  27.413  21.764  1.00 37.33           O  
ATOM   6664  CB  TYR B 386      37.275  27.447  19.198  1.00 35.55           C  
ATOM   6665  CG  TYR B 386      38.630  27.323  18.517  1.00 25.26           C  
ATOM   6666  CD1 TYR B 386      39.153  28.384  17.779  1.00 25.66           C  
ATOM   6667  CD2 TYR B 386      39.372  26.161  18.703  1.00 24.79           C  
ATOM   6668  CE1 TYR B 386      40.427  28.280  17.230  1.00 28.44           C  
ATOM   6669  CE2 TYR B 386      40.648  26.054  18.163  1.00 28.01           C  
ATOM   6670  CZ  TYR B 386      41.164  27.113  17.432  1.00 30.44           C  
ATOM   6671  OH  TYR B 386      42.435  26.988  16.911  1.00 42.30           O  
ATOM   6672  N   GLU B 387      35.443  29.503  20.947  1.00 39.33           N  
ATOM   6673  CA  GLU B 387      34.129  29.812  21.485  1.00 39.47           C  
ATOM   6674  C   GLU B 387      32.990  29.042  20.821  1.00 37.19           C  
ATOM   6675  O   GLU B 387      32.109  28.564  21.544  1.00 35.62           O  
ATOM   6676  CB  GLU B 387      33.886  31.329  21.368  1.00 51.10           C  
ATOM   6677  CG  GLU B 387      32.611  31.818  22.091  1.00 63.16           C  
ATOM   6678  CD  GLU B 387      32.411  33.335  22.203  1.00 70.18           C  
ATOM   6679  OE1 GLU B 387      32.032  33.983  21.224  1.00 72.89           O  
ATOM   6680  OE2 GLU B 387      32.621  33.868  23.290  1.00 68.21           O  
ATOM   6681  N   VAL B 388      32.906  28.980  19.487  1.00 32.54           N  
ATOM   6682  CA  VAL B 388      31.864  28.178  18.856  1.00 30.76           C  
ATOM   6683  C   VAL B 388      32.520  27.245  17.835  1.00 28.81           C  
ATOM   6684  O   VAL B 388      33.308  27.627  16.966  1.00 25.43           O  
ATOM   6685  CB  VAL B 388      30.775  29.153  18.245  1.00 32.78           C  
ATOM   6686  CG1 VAL B 388      31.412  30.252  17.425  1.00 30.87           C  
ATOM   6687  CG2 VAL B 388      29.801  28.356  17.381  1.00 29.52           C  
ATOM   6688  N   VAL B 389      32.197  25.969  17.981  1.00 27.80           N  
ATOM   6689  CA  VAL B 389      32.763  24.871  17.210  1.00 24.54           C  
ATOM   6690  C   VAL B 389      31.623  24.140  16.505  1.00 23.68           C  
ATOM   6691  O   VAL B 389      30.586  23.905  17.142  1.00 25.88           O  
ATOM   6692  CB  VAL B 389      33.536  23.958  18.215  1.00 22.24           C  
ATOM   6693  CG1 VAL B 389      33.824  22.565  17.686  1.00 24.10           C  
ATOM   6694  CG2 VAL B 389      34.882  24.600  18.458  1.00 19.07           C  
ATOM   6695  N   ALA B 390      31.746  23.841  15.205  1.00 20.09           N  
ATOM   6696  CA  ALA B 390      30.752  23.065  14.460  1.00 16.58           C  
ATOM   6697  C   ALA B 390      31.273  21.634  14.278  1.00 15.66           C  
ATOM   6698  O   ALA B 390      32.472  21.430  14.041  1.00 15.85           O  
ATOM   6699  CB  ALA B 390      30.535  23.671  13.089  1.00 15.81           C  
ATOM   6700  N   VAL B 391      30.426  20.623  14.451  1.00 13.73           N  
ATOM   6701  CA  VAL B 391      30.811  19.236  14.267  1.00 14.32           C  
ATOM   6702  C   VAL B 391      29.970  18.726  13.116  1.00 15.41           C  
ATOM   6703  O   VAL B 391      28.759  18.899  13.150  1.00 16.59           O  
ATOM   6704  CB  VAL B 391      30.513  18.421  15.529  1.00 15.74           C  
ATOM   6705  CG1 VAL B 391      30.824  16.951  15.286  1.00 13.70           C  
ATOM   6706  CG2 VAL B 391      31.374  18.931  16.678  1.00 16.80           C  
ATOM   6707  N   TYR B 392      30.591  18.158  12.078  1.00 17.03           N  
ATOM   6708  CA  TYR B 392      29.946  17.589  10.898  1.00 14.24           C  
ATOM   6709  C   TYR B 392      30.261  16.118  11.021  1.00 13.70           C  
ATOM   6710  O   TYR B 392      31.419  15.717  11.061  1.00 14.13           O  
ATOM   6711  CB  TYR B 392      30.560  18.073   9.598  1.00 14.61           C  
ATOM   6712  CG  TYR B 392      30.515  19.572   9.453  1.00 16.97           C  
ATOM   6713  CD1 TYR B 392      31.342  20.420  10.210  1.00 16.59           C  
ATOM   6714  CD2 TYR B 392      29.597  20.096   8.561  1.00 13.36           C  
ATOM   6715  CE1 TYR B 392      31.237  21.807  10.075  1.00 16.60           C  
ATOM   6716  CE2 TYR B 392      29.496  21.473   8.422  1.00 20.28           C  
ATOM   6717  CZ  TYR B 392      30.304  22.316   9.168  1.00 17.87           C  
ATOM   6718  OH  TYR B 392      30.132  23.664   8.944  1.00 16.94           O  
ATOM   6719  N   LEU B 393      29.246  15.286  11.133  1.00 16.40           N  
ATOM   6720  CA  LEU B 393      29.447  13.869  11.313  1.00 17.62           C  
ATOM   6721  C   LEU B 393      28.685  13.139  10.233  1.00 20.41           C  
ATOM   6722  O   LEU B 393      27.521  13.460   9.977  1.00 19.65           O  
ATOM   6723  CB  LEU B 393      28.941  13.472  12.708  1.00 20.61           C  
ATOM   6724  CG  LEU B 393      29.012  12.059  13.325  1.00 23.11           C  
ATOM   6725  CD1 LEU B 393      27.757  11.288  12.998  1.00 32.29           C  
ATOM   6726  CD2 LEU B 393      30.274  11.361  12.856  1.00 20.23           C  
ATOM   6727  N   SER B 394      29.310  12.146   9.627  1.00 19.83           N  
ATOM   6728  CA  SER B 394      28.660  11.317   8.645  1.00 20.35           C  
ATOM   6729  C   SER B 394      29.028   9.879   8.949  1.00 19.63           C  
ATOM   6730  O   SER B 394      30.203   9.600   9.190  1.00 21.32           O  
ATOM   6731  CB  SER B 394      29.143  11.716   7.260  1.00 23.30           C  
ATOM   6732  OG  SER B 394      28.387  10.995   6.304  1.00 29.75           O  
ATOM   6733  N   SER B 395      28.083   8.961   9.016  1.00 19.33           N  
ATOM   6734  CA  SER B 395      28.423   7.566   9.202  1.00 26.30           C  
ATOM   6735  C   SER B 395      27.466   6.769   8.339  1.00 28.09           C  
ATOM   6736  O   SER B 395      26.260   7.032   8.307  1.00 29.86           O  
ATOM   6737  CB  SER B 395      28.299   7.188  10.681  1.00 28.64           C  
ATOM   6738  OG  SER B 395      27.060   7.582  11.244  1.00 39.95           O  
ATOM   6739  N   PHE B 396      27.985   5.802   7.592  1.00 28.42           N  
ATOM   6740  CA  PHE B 396      27.195   5.049   6.628  1.00 26.62           C  
ATOM   6741  C   PHE B 396      27.883   3.698   6.442  1.00 26.62           C  
ATOM   6742  O   PHE B 396      29.086   3.591   6.698  1.00 22.14           O  
ATOM   6743  CB  PHE B 396      27.134   5.860   5.292  1.00 24.42           C  
ATOM   6744  CG  PHE B 396      28.495   6.227   4.699  1.00 22.68           C  
ATOM   6745  CD1 PHE B 396      29.253   7.262   5.254  1.00 19.05           C  
ATOM   6746  CD2 PHE B 396      29.031   5.468   3.650  1.00 26.53           C  
ATOM   6747  CE1 PHE B 396      30.545   7.515   4.784  1.00 23.15           C  
ATOM   6748  CE2 PHE B 396      30.329   5.728   3.180  1.00 29.60           C  
ATOM   6749  CZ  PHE B 396      31.086   6.753   3.746  1.00 24.37           C  
ATOM   6750  N   THR B 397      27.171   2.636   6.072  1.00 29.67           N  
ATOM   6751  CA  THR B 397      27.789   1.350   5.735  1.00 28.98           C  
ATOM   6752  C   THR B 397      28.150   1.547   4.264  1.00 28.60           C  
ATOM   6753  O   THR B 397      27.237   1.833   3.481  1.00 28.21           O  
ATOM   6754  CB  THR B 397      26.793   0.162   5.847  1.00 32.80           C  
ATOM   6755  OG1 THR B 397      26.096   0.337   7.081  1.00 42.46           O  
ATOM   6756  CG2 THR B 397      27.472  -1.204   5.804  1.00 26.39           C  
ATOM   6757  N   PRO B 398      29.396   1.462   3.804  1.00 25.96           N  
ATOM   6758  CA  PRO B 398      29.721   1.469   2.390  1.00 28.27           C  
ATOM   6759  C   PRO B 398      28.984   0.335   1.675  1.00 33.09           C  
ATOM   6760  O   PRO B 398      28.902  -0.799   2.187  1.00 34.59           O  
ATOM   6761  CB  PRO B 398      31.213   1.319   2.359  1.00 25.71           C  
ATOM   6762  CG  PRO B 398      31.642   1.858   3.699  1.00 28.28           C  
ATOM   6763  CD  PRO B 398      30.583   1.286   4.614  1.00 22.15           C  
ATOM   6764  N   LEU B 399      28.532   0.585   0.439  1.00 35.98           N  
ATOM   6765  CA  LEU B 399      27.764  -0.381  -0.339  1.00 33.73           C  
ATOM   6766  C   LEU B 399      28.521  -1.673  -0.545  1.00 28.25           C  
ATOM   6767  O   LEU B 399      27.879  -2.727  -0.485  1.00 30.63           O  
ATOM   6768  CB  LEU B 399      27.374   0.172  -1.731  1.00 41.10           C  
ATOM   6769  CG  LEU B 399      26.502  -0.727  -2.639  1.00 45.31           C  
ATOM   6770  CD1 LEU B 399      25.159  -1.027  -1.963  1.00 42.91           C  
ATOM   6771  CD2 LEU B 399      26.313  -0.045  -3.981  1.00 41.97           C  
ATOM   6772  N   MET B 400      29.857  -1.638  -0.672  1.00 22.89           N  
ATOM   6773  CA  MET B 400      30.572  -2.884  -0.841  1.00 24.36           C  
ATOM   6774  C   MET B 400      30.385  -3.744   0.399  1.00 24.20           C  
ATOM   6775  O   MET B 400      30.378  -4.965   0.301  1.00 25.63           O  
ATOM   6776  CB  MET B 400      32.073  -2.675  -1.056  1.00 31.80           C  
ATOM   6777  CG  MET B 400      32.933  -2.268   0.127  1.00 37.33           C  
ATOM   6778  SD  MET B 400      34.696  -2.640  -0.079  1.00 45.87           S  
ATOM   6779  CE  MET B 400      34.667  -4.417  -0.010  1.00 32.98           C  
ATOM   6780  N   HIS B 401      30.200  -3.142   1.585  1.00 20.11           N  
ATOM   6781  CA  HIS B 401      30.033  -3.925   2.782  1.00 18.91           C  
ATOM   6782  C   HIS B 401      28.619  -4.341   3.030  1.00 20.41           C  
ATOM   6783  O   HIS B 401      28.397  -5.231   3.838  1.00 21.29           O  
ATOM   6784  CB  HIS B 401      30.567  -3.164   3.940  1.00 13.24           C  
ATOM   6785  CG  HIS B 401      32.060  -3.394   3.933  1.00 10.33           C  
ATOM   6786  ND1 HIS B 401      32.742  -4.524   3.728  1.00 15.18           N  
ATOM   6787  CD2 HIS B 401      32.965  -2.393   4.124  1.00  6.04           C  
ATOM   6788  CE1 HIS B 401      34.021  -4.255   3.784  1.00  7.94           C  
ATOM   6789  NE2 HIS B 401      34.137  -2.968   4.021  1.00 17.36           N  
ATOM   6790  N   LYS B 402      27.665  -3.776   2.313  1.00 22.24           N  
ATOM   6791  CA  LYS B 402      26.311  -4.293   2.341  1.00 27.40           C  
ATOM   6792  C   LYS B 402      26.313  -5.599   1.549  1.00 31.05           C  
ATOM   6793  O   LYS B 402      25.724  -6.601   1.952  1.00 38.55           O  
ATOM   6794  CB  LYS B 402      25.369  -3.321   1.691  1.00 32.09           C  
ATOM   6795  CG  LYS B 402      24.755  -2.343   2.673  1.00 37.12           C  
ATOM   6796  CD  LYS B 402      24.161  -1.117   1.979  1.00 45.32           C  
ATOM   6797  CE  LYS B 402      23.333  -0.331   3.008  1.00 52.73           C  
ATOM   6798  NZ  LYS B 402      23.121   1.054   2.621  1.00 53.10           N  
ATOM   6799  N   VAL B 403      27.017  -5.606   0.417  1.00 29.14           N  
ATOM   6800  CA  VAL B 403      27.203  -6.787  -0.412  1.00 25.87           C  
ATOM   6801  C   VAL B 403      28.222  -7.796   0.147  1.00 24.57           C  
ATOM   6802  O   VAL B 403      28.020  -9.005   0.013  1.00 24.44           O  
ATOM   6803  CB  VAL B 403      27.592  -6.264  -1.836  1.00 26.82           C  
ATOM   6804  CG1 VAL B 403      27.975  -7.397  -2.772  1.00 29.53           C  
ATOM   6805  CG2 VAL B 403      26.386  -5.553  -2.442  1.00 23.57           C  
ATOM   6806  N   SER B 404      29.314  -7.400   0.802  1.00 24.25           N  
ATOM   6807  CA  SER B 404      30.270  -8.379   1.275  1.00 23.49           C  
ATOM   6808  C   SER B 404      29.835  -9.235   2.454  1.00 25.68           C  
ATOM   6809  O   SER B 404      30.471 -10.251   2.739  1.00 30.15           O  
ATOM   6810  CB  SER B 404      31.568  -7.693   1.647  1.00 24.47           C  
ATOM   6811  OG  SER B 404      31.613  -6.779   2.754  1.00 26.01           O  
ATOM   6812  N   GLY B 405      28.776  -8.841   3.164  1.00 27.85           N  
ATOM   6813  CA  GLY B 405      28.326  -9.548   4.347  1.00 23.75           C  
ATOM   6814  C   GLY B 405      28.714  -8.774   5.599  1.00 23.06           C  
ATOM   6815  O   GLY B 405      27.996  -8.812   6.592  1.00 27.18           O  
ATOM   6816  N   SER B 406      29.794  -7.999   5.601  1.00 21.55           N  
ATOM   6817  CA  SER B 406      30.223  -7.248   6.771  1.00 19.43           C  
ATOM   6818  C   SER B 406      29.425  -5.978   7.002  1.00 17.78           C  
ATOM   6819  O   SER B 406      29.951  -4.863   7.034  1.00 16.52           O  
ATOM   6820  CB  SER B 406      31.698  -6.928   6.613  1.00 15.45           C  
ATOM   6821  OG  SER B 406      32.351  -8.150   6.302  1.00 21.79           O  
ATOM   6822  N   LYS B 407      28.148  -6.162   7.309  1.00 20.78           N  
ATOM   6823  CA  LYS B 407      27.219  -5.054   7.457  1.00 25.85           C  
ATOM   6824  C   LYS B 407      27.452  -4.170   8.675  1.00 26.06           C  
ATOM   6825  O   LYS B 407      26.889  -3.078   8.783  1.00 27.69           O  
ATOM   6826  CB  LYS B 407      25.802  -5.604   7.484  1.00 30.15           C  
ATOM   6827  CG  LYS B 407      25.425  -6.191   6.135  1.00 42.98           C  
ATOM   6828  CD  LYS B 407      23.927  -6.410   6.052  1.00 49.49           C  
ATOM   6829  CE  LYS B 407      23.581  -6.845   4.636  1.00 54.78           C  
ATOM   6830  NZ  LYS B 407      22.335  -6.219   4.227  1.00 52.70           N  
ATOM   6831  N   TYR B 408      28.296  -4.658   9.592  1.00 23.82           N  
ATOM   6832  CA  TYR B 408      28.671  -3.912  10.782  1.00 18.68           C  
ATOM   6833  C   TYR B 408      29.795  -2.916  10.522  1.00 20.33           C  
ATOM   6834  O   TYR B 408      30.151  -2.124  11.402  1.00 20.91           O  
ATOM   6835  CB  TYR B 408      29.088  -4.908  11.878  1.00 14.26           C  
ATOM   6836  CG  TYR B 408      30.271  -5.793  11.525  1.00 12.31           C  
ATOM   6837  CD1 TYR B 408      30.084  -6.998  10.838  1.00 17.08           C  
ATOM   6838  CD2 TYR B 408      31.559  -5.383  11.868  1.00 12.33           C  
ATOM   6839  CE1 TYR B 408      31.185  -7.782  10.494  1.00 10.18           C  
ATOM   6840  CE2 TYR B 408      32.662  -6.160  11.528  1.00 12.99           C  
ATOM   6841  CZ  TYR B 408      32.459  -7.350  10.842  1.00 11.73           C  
ATOM   6842  OH  TYR B 408      33.551  -8.111  10.483  1.00 14.91           O  
ATOM   6843  N   LYS B 409      30.427  -2.972   9.342  1.00 20.23           N  
ATOM   6844  CA  LYS B 409      31.516  -2.047   9.056  1.00 18.70           C  
ATOM   6845  C   LYS B 409      31.029  -0.657   8.659  1.00 19.96           C  
ATOM   6846  O   LYS B 409      30.894  -0.315   7.483  1.00 23.39           O  
ATOM   6847  CB  LYS B 409      32.405  -2.660   7.966  1.00 17.00           C  
ATOM   6848  CG  LYS B 409      33.248  -3.792   8.538  1.00 13.99           C  
ATOM   6849  CD  LYS B 409      34.235  -4.373   7.545  1.00 10.86           C  
ATOM   6850  CE  LYS B 409      35.047  -5.440   8.245  1.00 15.95           C  
ATOM   6851  NZ  LYS B 409      36.087  -5.934   7.372  1.00 12.42           N  
ATOM   6852  N   THR B 410      30.688   0.144   9.655  1.00 17.72           N  
ATOM   6853  CA  THR B 410      30.310   1.530   9.450  1.00 17.16           C  
ATOM   6854  C   THR B 410      31.528   2.393   9.187  1.00 18.36           C  
ATOM   6855  O   THR B 410      32.528   2.332   9.914  1.00 18.93           O  
ATOM   6856  CB  THR B 410      29.608   2.058  10.683  1.00 19.29           C  
ATOM   6857  OG1 THR B 410      28.635   1.066  10.977  1.00 29.10           O  
ATOM   6858  CG2 THR B 410      28.931   3.409  10.516  1.00 13.86           C  
ATOM   6859  N   PHE B 411      31.440   3.213   8.149  1.00 17.90           N  
ATOM   6860  CA  PHE B 411      32.479   4.166   7.817  1.00 15.51           C  
ATOM   6861  C   PHE B 411      32.070   5.409   8.569  1.00 12.82           C  
ATOM   6862  O   PHE B 411      30.891   5.762   8.525  1.00 12.92           O  
ATOM   6863  CB  PHE B 411      32.503   4.479   6.314  1.00 13.82           C  
ATOM   6864  CG  PHE B 411      33.718   5.312   5.916  1.00 11.38           C  
ATOM   6865  CD1 PHE B 411      33.710   6.703   6.025  1.00 14.99           C  
ATOM   6866  CD2 PHE B 411      34.870   4.667   5.474  1.00 13.15           C  
ATOM   6867  CE1 PHE B 411      34.852   7.438   5.708  1.00 11.49           C  
ATOM   6868  CE2 PHE B 411      36.011   5.407   5.157  1.00 14.36           C  
ATOM   6869  CZ  PHE B 411      35.998   6.792   5.274  1.00 15.71           C  
ATOM   6870  N   VAL B 412      32.969   6.078   9.276  1.00 11.22           N  
ATOM   6871  CA  VAL B 412      32.631   7.298   9.997  1.00 12.34           C  
ATOM   6872  C   VAL B 412      33.557   8.403   9.480  1.00 10.50           C  
ATOM   6873  O   VAL B 412      34.770   8.200   9.347  1.00 11.75           O  
ATOM   6874  CB  VAL B 412      32.838   7.100  11.533  1.00 16.59           C  
ATOM   6875  CG1 VAL B 412      32.604   8.417  12.253  1.00 13.00           C  
ATOM   6876  CG2 VAL B 412      31.862   6.094  12.100  1.00 12.68           C  
ATOM   6877  N   ALA B 413      33.018   9.565   9.165  1.00  9.37           N  
ATOM   6878  CA  ALA B 413      33.812  10.689   8.721  1.00 14.44           C  
ATOM   6879  C   ALA B 413      33.324  11.829   9.585  1.00 16.25           C  
ATOM   6880  O   ALA B 413      32.106  12.025   9.730  1.00 15.19           O  
ATOM   6881  CB  ALA B 413      33.534  11.055   7.263  1.00 14.21           C  
ATOM   6882  N   LYS B 414      34.257  12.593  10.146  1.00 16.05           N  
ATOM   6883  CA  LYS B 414      33.893  13.658  11.064  1.00 16.54           C  
ATOM   6884  C   LYS B 414      34.821  14.834  10.914  1.00 11.90           C  
ATOM   6885  O   LYS B 414      36.038  14.671  10.996  1.00 12.49           O  
ATOM   6886  CB  LYS B 414      33.945  13.054  12.451  1.00 19.24           C  
ATOM   6887  CG  LYS B 414      33.509  13.922  13.585  1.00 27.91           C  
ATOM   6888  CD  LYS B 414      33.214  12.938  14.685  1.00 25.98           C  
ATOM   6889  CE  LYS B 414      32.922  13.813  15.855  1.00 24.25           C  
ATOM   6890  NZ  LYS B 414      32.755  13.035  17.057  1.00 20.71           N  
ATOM   6891  N   ILE B 415      34.260  16.002  10.663  1.00 14.30           N  
ATOM   6892  CA  ILE B 415      35.035  17.200  10.463  1.00 14.56           C  
ATOM   6893  C   ILE B 415      34.635  18.179  11.559  1.00 13.89           C  
ATOM   6894  O   ILE B 415      33.456  18.319  11.881  1.00 16.14           O  
ATOM   6895  CB  ILE B 415      34.733  17.820   9.073  1.00 16.00           C  
ATOM   6896  CG1 ILE B 415      35.032  16.866   7.921  1.00 13.40           C  
ATOM   6897  CG2 ILE B 415      35.617  19.052   8.927  1.00 19.95           C  
ATOM   6898  CD1 ILE B 415      34.700  17.480   6.542  1.00 16.64           C  
ATOM   6899  N   ILE B 416      35.573  18.905  12.132  1.00 14.16           N  
ATOM   6900  CA  ILE B 416      35.327  19.817  13.230  1.00 16.32           C  
ATOM   6901  C   ILE B 416      35.817  21.162  12.783  1.00 15.91           C  
ATOM   6902  O   ILE B 416      36.954  21.252  12.301  1.00 14.90           O  
ATOM   6903  CB  ILE B 416      36.103  19.254  14.442  1.00 17.84           C  
ATOM   6904  CG1 ILE B 416      35.242  18.117  14.968  1.00 17.96           C  
ATOM   6905  CG2 ILE B 416      36.387  20.285  15.525  1.00 18.16           C  
ATOM   6906  CD1 ILE B 416      36.039  17.048  15.663  1.00 32.56           C  
ATOM   6907  N   THR B 417      35.027  22.213  12.914  1.00 18.43           N  
ATOM   6908  CA  THR B 417      35.525  23.523  12.518  1.00 20.31           C  
ATOM   6909  C   THR B 417      35.386  24.583  13.600  1.00 19.57           C  
ATOM   6910  O   THR B 417      34.664  24.437  14.592  1.00 21.98           O  
ATOM   6911  CB  THR B 417      34.797  24.060  11.247  1.00 19.02           C  
ATOM   6912  OG1 THR B 417      33.445  24.277  11.638  1.00 20.59           O  
ATOM   6913  CG2 THR B 417      34.878  23.135  10.043  1.00 14.44           C  
ATOM   6914  N   ASN B 418      36.105  25.683  13.398  1.00 23.58           N  
ATOM   6915  CA  ASN B 418      35.911  26.890  14.174  1.00 22.25           C  
ATOM   6916  C   ASN B 418      34.774  27.522  13.392  1.00 22.15           C  
ATOM   6917  O   ASN B 418      34.947  28.019  12.272  1.00 23.60           O  
ATOM   6918  CB  ASN B 418      37.120  27.788  14.128  1.00 20.87           C  
ATOM   6919  CG  ASN B 418      36.838  29.179  14.675  1.00 28.31           C  
ATOM   6920  OD1 ASN B 418      35.754  29.567  15.117  1.00 33.25           O  
ATOM   6921  ND2 ASN B 418      37.846  30.025  14.606  1.00 39.14           N  
ATOM   6922  N   HIS B 419      33.578  27.474  13.945  1.00 21.83           N  
ATOM   6923  CA  HIS B 419      32.411  27.944  13.245  1.00 25.59           C  
ATOM   6924  C   HIS B 419      32.400  29.436  13.011  1.00 29.25           C  
ATOM   6925  O   HIS B 419      31.612  29.865  12.181  1.00 32.63           O  
ATOM   6926  CB  HIS B 419      31.154  27.552  14.005  1.00 22.67           C  
ATOM   6927  CG  HIS B 419      29.850  27.755  13.236  1.00 26.57           C  
ATOM   6928  ND1 HIS B 419      28.844  28.556  13.558  1.00 32.85           N  
ATOM   6929  CD2 HIS B 419      29.493  27.125  12.067  1.00 24.38           C  
ATOM   6930  CE1 HIS B 419      27.910  28.443  12.650  1.00 26.02           C  
ATOM   6931  NE2 HIS B 419      28.314  27.575  11.757  1.00 27.37           N  
ATOM   6932  N   SER B 420      33.210  30.247  13.666  1.00 30.74           N  
ATOM   6933  CA  SER B 420      33.213  31.677  13.421  1.00 33.63           C  
ATOM   6934  C   SER B 420      33.736  31.993  12.026  1.00 32.67           C  
ATOM   6935  O   SER B 420      33.263  32.937  11.395  1.00 36.76           O  
ATOM   6936  CB  SER B 420      34.077  32.345  14.482  1.00 36.30           C  
ATOM   6937  OG  SER B 420      33.749  31.812  15.768  1.00 50.95           O  
ATOM   6938  N   ASP B 421      34.695  31.216  11.501  1.00 29.96           N  
ATOM   6939  CA  ASP B 421      35.244  31.503  10.184  1.00 29.76           C  
ATOM   6940  C   ASP B 421      35.262  30.330   9.211  1.00 28.67           C  
ATOM   6941  O   ASP B 421      35.677  30.463   8.058  1.00 31.68           O  
ATOM   6942  CB  ASP B 421      36.663  32.050  10.350  1.00 27.92           C  
ATOM   6943  CG  ASP B 421      37.705  31.131  10.962  1.00 31.42           C  
ATOM   6944  OD1 ASP B 421      37.383  30.035  11.416  1.00 43.50           O  
ATOM   6945  OD2 ASP B 421      38.869  31.518  10.983  1.00 46.34           O  
ATOM   6946  N   GLY B 422      34.862  29.153   9.681  1.00 25.16           N  
ATOM   6947  CA  GLY B 422      34.820  27.984   8.837  1.00 20.42           C  
ATOM   6948  C   GLY B 422      36.095  27.169   8.830  1.00 24.07           C  
ATOM   6949  O   GLY B 422      36.028  26.108   8.204  1.00 27.77           O  
ATOM   6950  N   THR B 423      37.219  27.532   9.477  1.00 23.19           N  
ATOM   6951  CA  THR B 423      38.463  26.760   9.436  1.00 20.33           C  
ATOM   6952  C   THR B 423      38.312  25.365  10.010  1.00 20.35           C  
ATOM   6953  O   THR B 423      37.747  25.171  11.091  1.00 21.79           O  
ATOM   6954  CB  THR B 423      39.585  27.437  10.223  1.00 23.86           C  
ATOM   6955  OG1 THR B 423      39.450  28.820   9.954  1.00 27.47           O  
ATOM   6956  CG2 THR B 423      40.985  26.964   9.838  1.00 26.28           C  
ATOM   6957  N   VAL B 424      38.815  24.381   9.274  1.00 20.29           N  
ATOM   6958  CA  VAL B 424      38.723  22.999   9.668  1.00 18.93           C  
ATOM   6959  C   VAL B 424      39.806  22.804  10.716  1.00 20.54           C  
ATOM   6960  O   VAL B 424      40.989  23.056  10.485  1.00 22.40           O  
ATOM   6961  CB  VAL B 424      38.922  22.102   8.412  1.00 13.63           C  
ATOM   6962  CG1 VAL B 424      38.985  20.625   8.773  1.00 10.89           C  
ATOM   6963  CG2 VAL B 424      37.715  22.257   7.513  1.00  9.69           C  
ATOM   6964  N   LEU B 425      39.370  22.432  11.915  1.00 21.06           N  
ATOM   6965  CA  LEU B 425      40.297  22.201  13.005  1.00 19.11           C  
ATOM   6966  C   LEU B 425      40.699  20.741  13.063  1.00 21.45           C  
ATOM   6967  O   LEU B 425      41.776  20.434  13.596  1.00 19.20           O  
ATOM   6968  CB  LEU B 425      39.652  22.622  14.319  1.00 20.88           C  
ATOM   6969  CG  LEU B 425      39.212  24.084  14.440  1.00 16.84           C  
ATOM   6970  CD1 LEU B 425      38.543  24.213  15.772  1.00 14.53           C  
ATOM   6971  CD2 LEU B 425      40.372  25.068  14.326  1.00 14.43           C  
ATOM   6972  N   GLY B 426      39.891  19.812  12.529  1.00 18.30           N  
ATOM   6973  CA  GLY B 426      40.268  18.412  12.542  1.00 13.87           C  
ATOM   6974  C   GLY B 426      39.317  17.610  11.699  1.00 12.40           C  
ATOM   6975  O   GLY B 426      38.172  18.007  11.516  1.00 14.88           O  
ATOM   6976  N   VAL B 427      39.810  16.492  11.190  1.00 12.27           N  
ATOM   6977  CA  VAL B 427      39.092  15.537  10.353  1.00 11.00           C  
ATOM   6978  C   VAL B 427      39.493  14.172  10.911  1.00  9.21           C  
ATOM   6979  O   VAL B 427      40.681  13.930  11.157  1.00 10.25           O  
ATOM   6980  CB  VAL B 427      39.524  15.626   8.853  1.00  7.93           C  
ATOM   6981  CG1 VAL B 427      38.669  14.667   8.037  1.00  3.18           C  
ATOM   6982  CG2 VAL B 427      39.311  17.027   8.301  1.00  6.24           C  
ATOM   6983  N   HIS B 428      38.540  13.294  11.196  1.00  8.13           N  
ATOM   6984  CA  HIS B 428      38.796  11.997  11.834  1.00 10.84           C  
ATOM   6985  C   HIS B 428      38.030  10.943  11.048  1.00 13.29           C  
ATOM   6986  O   HIS B 428      36.826  11.121  10.814  1.00 13.27           O  
ATOM   6987  CB  HIS B 428      38.294  12.025  13.302  1.00  8.60           C  
ATOM   6988  CG  HIS B 428      38.839  13.219  14.090  1.00 14.13           C  
ATOM   6989  ND1 HIS B 428      40.091  13.415  14.492  1.00 12.03           N  
ATOM   6990  CD2 HIS B 428      38.127  14.356  14.401  1.00  7.77           C  
ATOM   6991  CE1 HIS B 428      40.183  14.614  15.011  1.00  9.21           C  
ATOM   6992  NE2 HIS B 428      38.992  15.165  14.949  1.00 10.12           N  
ATOM   6993  N   LEU B 429      38.657   9.849  10.648  1.00 12.89           N  
ATOM   6994  CA  LEU B 429      38.005   8.859   9.798  1.00 10.62           C  
ATOM   6995  C   LEU B 429      38.180   7.464  10.370  1.00  9.96           C  
ATOM   6996  O   LEU B 429      39.261   7.170  10.890  1.00  9.37           O  
ATOM   6997  CB  LEU B 429      38.637   8.859   8.416  1.00 11.86           C  
ATOM   6998  CG  LEU B 429      38.784  10.164   7.662  1.00 12.66           C  
ATOM   6999  CD1 LEU B 429      39.664   9.917   6.471  1.00  7.34           C  
ATOM   7000  CD2 LEU B 429      37.431  10.695   7.251  1.00 10.18           C  
ATOM   7001  N   LEU B 430      37.171   6.603  10.246  1.00  8.46           N  
ATOM   7002  CA  LEU B 430      37.258   5.198  10.602  1.00  7.79           C  
ATOM   7003  C   LEU B 430      36.707   4.463   9.395  1.00  7.93           C  
ATOM   7004  O   LEU B 430      35.599   4.757   8.945  1.00 10.57           O  
ATOM   7005  CB  LEU B 430      36.386   4.803  11.805  1.00  7.48           C  
ATOM   7006  CG  LEU B 430      36.266   3.299  12.144  1.00 11.00           C  
ATOM   7007  CD1 LEU B 430      37.569   2.767  12.665  1.00 12.67           C  
ATOM   7008  CD2 LEU B 430      35.286   3.081  13.269  1.00 13.41           C  
ATOM   7009  N   GLY B 431      37.428   3.493   8.873  1.00  9.33           N  
ATOM   7010  CA  GLY B 431      36.960   2.731   7.737  1.00  9.35           C  
ATOM   7011  C   GLY B 431      38.120   2.370   6.839  1.00  7.65           C  
ATOM   7012  O   GLY B 431      39.243   2.848   7.003  1.00 10.98           O  
ATOM   7013  N   ASP B 432      37.867   1.519   5.857  1.00 12.48           N  
ATOM   7014  CA  ASP B 432      38.928   1.061   4.991  1.00 10.10           C  
ATOM   7015  C   ASP B 432      39.521   2.187   4.205  1.00  9.81           C  
ATOM   7016  O   ASP B 432      38.843   3.071   3.706  1.00 14.00           O  
ATOM   7017  CB  ASP B 432      38.429   0.034   4.016  1.00 13.17           C  
ATOM   7018  CG  ASP B 432      38.112  -1.292   4.664  1.00 22.99           C  
ATOM   7019  OD1 ASP B 432      38.979  -1.854   5.334  1.00 37.34           O  
ATOM   7020  OD2 ASP B 432      37.008  -1.778   4.462  1.00 28.25           O  
ATOM   7021  N   ASN B 433      40.838   2.135   4.172  1.00 10.82           N  
ATOM   7022  CA  ASN B 433      41.717   3.063   3.492  1.00 14.66           C  
ATOM   7023  C   ASN B 433      41.812   4.401   4.138  1.00 15.60           C  
ATOM   7024  O   ASN B 433      42.510   5.275   3.607  1.00 18.33           O  
ATOM   7025  CB  ASN B 433      41.317   3.306   2.033  1.00 16.91           C  
ATOM   7026  CG  ASN B 433      41.323   1.987   1.325  1.00 23.01           C  
ATOM   7027  OD1 ASN B 433      40.349   1.533   0.747  1.00 26.05           O  
ATOM   7028  ND2 ASN B 433      42.374   1.236   1.384  1.00 23.16           N  
ATOM   7029  N   ALA B 434      41.258   4.567   5.338  1.00 17.49           N  
ATOM   7030  CA  ALA B 434      41.341   5.854   6.009  1.00 12.79           C  
ATOM   7031  C   ALA B 434      42.769   6.353   6.146  1.00  9.81           C  
ATOM   7032  O   ALA B 434      42.940   7.550   5.932  1.00 16.17           O  
ATOM   7033  CB  ALA B 434      40.703   5.765   7.388  1.00  9.46           C  
ATOM   7034  N   PRO B 435      43.853   5.588   6.371  1.00 11.89           N  
ATOM   7035  CA  PRO B 435      45.221   6.104   6.362  1.00 12.21           C  
ATOM   7036  C   PRO B 435      45.627   6.747   5.042  1.00 13.49           C  
ATOM   7037  O   PRO B 435      46.392   7.710   5.034  1.00 15.43           O  
ATOM   7038  CB  PRO B 435      46.091   4.917   6.701  1.00  5.84           C  
ATOM   7039  CG  PRO B 435      45.186   4.021   7.498  1.00 12.73           C  
ATOM   7040  CD  PRO B 435      43.858   4.189   6.797  1.00  7.05           C  
ATOM   7041  N   GLU B 436      45.147   6.214   3.913  1.00 16.16           N  
ATOM   7042  CA  GLU B 436      45.445   6.753   2.587  1.00 12.94           C  
ATOM   7043  C   GLU B 436      44.690   8.044   2.309  1.00 12.38           C  
ATOM   7044  O   GLU B 436      45.283   8.999   1.808  1.00 14.38           O  
ATOM   7045  CB  GLU B 436      45.105   5.701   1.519  1.00  9.06           C  
ATOM   7046  CG  GLU B 436      46.030   4.494   1.567  1.00  3.05           C  
ATOM   7047  CD  GLU B 436      47.475   4.762   1.200  1.00 10.19           C  
ATOM   7048  OE1 GLU B 436      47.825   5.853   0.777  1.00 17.85           O  
ATOM   7049  OE2 GLU B 436      48.287   3.860   1.331  1.00 17.58           O  
ATOM   7050  N   ILE B 437      43.425   8.104   2.740  1.00 10.80           N  
ATOM   7051  CA  ILE B 437      42.592   9.286   2.566  1.00 11.30           C  
ATOM   7052  C   ILE B 437      43.074  10.469   3.405  1.00 13.61           C  
ATOM   7053  O   ILE B 437      42.943  11.631   2.996  1.00 17.74           O  
ATOM   7054  CB  ILE B 437      41.137   8.955   2.948  1.00  6.68           C  
ATOM   7055  CG1 ILE B 437      40.602   7.820   2.098  1.00  5.00           C  
ATOM   7056  CG2 ILE B 437      40.278  10.196   2.781  1.00 11.03           C  
ATOM   7057  CD1 ILE B 437      39.267   7.202   2.604  1.00  4.37           C  
ATOM   7058  N   ILE B 438      43.635  10.242   4.594  1.00 16.01           N  
ATOM   7059  CA  ILE B 438      43.955  11.370   5.454  1.00 14.17           C  
ATOM   7060  C   ILE B 438      45.188  12.134   4.995  1.00 15.15           C  
ATOM   7061  O   ILE B 438      45.310  13.322   5.322  1.00 18.42           O  
ATOM   7062  CB  ILE B 438      44.104  10.871   6.953  1.00 10.38           C  
ATOM   7063  CG1 ILE B 438      43.928  12.068   7.875  1.00  8.09           C  
ATOM   7064  CG2 ILE B 438      45.451  10.232   7.242  1.00  8.88           C  
ATOM   7065  CD1 ILE B 438      42.496  12.644   7.870  1.00  7.30           C  
ATOM   7066  N   GLN B 439      46.094  11.574   4.191  1.00 15.74           N  
ATOM   7067  CA  GLN B 439      47.282  12.317   3.793  1.00 14.99           C  
ATOM   7068  C   GLN B 439      46.978  13.607   3.021  1.00 16.39           C  
ATOM   7069  O   GLN B 439      47.555  14.663   3.316  1.00 16.51           O  
ATOM   7070  CB  GLN B 439      48.173  11.404   2.974  1.00 11.82           C  
ATOM   7071  CG  GLN B 439      49.484  12.084   2.572  1.00 14.53           C  
ATOM   7072  CD  GLN B 439      50.418  12.368   3.725  1.00 12.08           C  
ATOM   7073  OE1 GLN B 439      51.219  11.516   4.086  1.00 15.63           O  
ATOM   7074  NE2 GLN B 439      50.387  13.522   4.366  1.00 18.43           N  
ATOM   7075  N   GLY B 440      46.015  13.596   2.097  1.00 16.30           N  
ATOM   7076  CA  GLY B 440      45.667  14.777   1.335  1.00 12.80           C  
ATOM   7077  C   GLY B 440      45.031  15.799   2.248  1.00 14.59           C  
ATOM   7078  O   GLY B 440      45.278  17.002   2.160  1.00 20.23           O  
ATOM   7079  N   ILE B 441      44.237  15.315   3.194  1.00 15.39           N  
ATOM   7080  CA  ILE B 441      43.573  16.157   4.174  1.00 16.90           C  
ATOM   7081  C   ILE B 441      44.601  16.844   5.072  1.00 16.16           C  
ATOM   7082  O   ILE B 441      44.449  18.027   5.384  1.00 22.09           O  
ATOM   7083  CB  ILE B 441      42.586  15.269   4.975  1.00 18.93           C  
ATOM   7084  CG1 ILE B 441      41.613  14.526   4.048  1.00 18.65           C  
ATOM   7085  CG2 ILE B 441      41.787  16.146   5.903  1.00 20.30           C  
ATOM   7086  CD1 ILE B 441      40.824  15.414   3.073  1.00 14.22           C  
ATOM   7087  N   GLY B 442      45.701  16.191   5.438  1.00 17.17           N  
ATOM   7088  CA  GLY B 442      46.771  16.827   6.197  1.00 17.51           C  
ATOM   7089  C   GLY B 442      47.334  18.028   5.446  1.00 19.72           C  
ATOM   7090  O   GLY B 442      47.619  19.074   6.029  1.00 20.48           O  
ATOM   7091  N   ILE B 443      47.481  17.955   4.120  1.00 19.26           N  
ATOM   7092  CA  ILE B 443      47.938  19.083   3.314  1.00 17.66           C  
ATOM   7093  C   ILE B 443      46.898  20.198   3.373  1.00 20.03           C  
ATOM   7094  O   ILE B 443      47.237  21.369   3.539  1.00 20.78           O  
ATOM   7095  CB  ILE B 443      48.144  18.643   1.855  1.00 19.91           C  
ATOM   7096  CG1 ILE B 443      49.034  17.403   1.747  1.00 18.33           C  
ATOM   7097  CG2 ILE B 443      48.785  19.816   1.124  1.00 18.72           C  
ATOM   7098  CD1 ILE B 443      49.209  16.776   0.349  1.00 15.34           C  
ATOM   7099  N   CYS B 444      45.607  19.879   3.298  1.00 17.46           N  
ATOM   7100  CA  CYS B 444      44.549  20.865   3.385  1.00 15.16           C  
ATOM   7101  C   CYS B 444      44.581  21.659   4.676  1.00 17.99           C  
ATOM   7102  O   CYS B 444      44.413  22.877   4.654  1.00 19.00           O  
ATOM   7103  CB  CYS B 444      43.195  20.213   3.309  1.00 19.04           C  
ATOM   7104  SG  CYS B 444      42.782  19.554   1.693  1.00 23.73           S  
ATOM   7105  N   LEU B 445      44.782  21.029   5.832  1.00 19.87           N  
ATOM   7106  CA  LEU B 445      44.815  21.745   7.092  1.00 17.94           C  
ATOM   7107  C   LEU B 445      46.064  22.607   7.171  1.00 18.72           C  
ATOM   7108  O   LEU B 445      46.034  23.742   7.661  1.00 21.49           O  
ATOM   7109  CB  LEU B 445      44.776  20.761   8.247  1.00 17.56           C  
ATOM   7110  CG  LEU B 445      43.394  20.392   8.756  1.00 22.49           C  
ATOM   7111  CD1 LEU B 445      42.620  19.625   7.715  1.00 24.56           C  
ATOM   7112  CD2 LEU B 445      43.546  19.525   9.980  1.00 21.51           C  
ATOM   7113  N   LYS B 446      47.173  22.162   6.604  1.00 20.39           N  
ATOM   7114  CA  LYS B 446      48.387  22.951   6.560  1.00 24.15           C  
ATOM   7115  C   LYS B 446      48.181  24.202   5.681  1.00 26.52           C  
ATOM   7116  O   LYS B 446      48.878  25.201   5.820  1.00 30.58           O  
ATOM   7117  CB  LYS B 446      49.451  22.010   6.036  1.00 26.09           C  
ATOM   7118  CG  LYS B 446      50.855  22.236   6.529  1.00 36.36           C  
ATOM   7119  CD  LYS B 446      50.941  22.020   8.037  1.00 41.95           C  
ATOM   7120  CE  LYS B 446      52.330  22.450   8.491  1.00 36.76           C  
ATOM   7121  NZ  LYS B 446      53.333  21.514   8.025  1.00 50.06           N  
ATOM   7122  N   LEU B 447      47.198  24.176   4.771  1.00 27.98           N  
ATOM   7123  CA  LEU B 447      46.819  25.296   3.912  1.00 27.58           C  
ATOM   7124  C   LEU B 447      45.640  26.075   4.481  1.00 28.27           C  
ATOM   7125  O   LEU B 447      45.033  26.916   3.810  1.00 28.67           O  
ATOM   7126  CB  LEU B 447      46.429  24.801   2.523  1.00 27.18           C  
ATOM   7127  CG  LEU B 447      47.556  24.333   1.634  1.00 24.55           C  
ATOM   7128  CD1 LEU B 447      47.009  23.640   0.400  1.00 26.76           C  
ATOM   7129  CD2 LEU B 447      48.388  25.533   1.267  1.00 28.09           C  
ATOM   7130  N   ASN B 448      45.273  25.765   5.723  1.00 26.01           N  
ATOM   7131  CA  ASN B 448      44.197  26.422   6.443  1.00 26.56           C  
ATOM   7132  C   ASN B 448      42.861  26.382   5.737  1.00 25.65           C  
ATOM   7133  O   ASN B 448      42.107  27.364   5.701  1.00 28.11           O  
ATOM   7134  CB  ASN B 448      44.533  27.896   6.735  1.00 32.03           C  
ATOM   7135  CG  ASN B 448      45.815  28.057   7.521  1.00 36.18           C  
ATOM   7136  OD1 ASN B 448      46.743  28.749   7.111  1.00 50.38           O  
ATOM   7137  ND2 ASN B 448      45.966  27.402   8.664  1.00 40.25           N  
ATOM   7138  N   ALA B 449      42.521  25.223   5.177  1.00 22.86           N  
ATOM   7139  CA  ALA B 449      41.242  25.086   4.512  1.00 20.29           C  
ATOM   7140  C   ALA B 449      40.034  25.285   5.424  1.00 20.85           C  
ATOM   7141  O   ALA B 449      40.068  25.031   6.628  1.00 21.43           O  
ATOM   7142  CB  ALA B 449      41.115  23.719   3.902  1.00 17.27           C  
ATOM   7143  N   LYS B 450      38.958  25.747   4.808  1.00 18.89           N  
ATOM   7144  CA  LYS B 450      37.681  26.005   5.435  1.00 18.78           C  
ATOM   7145  C   LYS B 450      36.736  24.938   4.948  1.00 18.67           C  
ATOM   7146  O   LYS B 450      36.961  24.358   3.886  1.00 21.05           O  
ATOM   7147  CB  LYS B 450      37.138  27.361   5.012  1.00 19.76           C  
ATOM   7148  CG  LYS B 450      37.994  28.419   5.628  1.00 25.72           C  
ATOM   7149  CD  LYS B 450      37.659  29.760   5.061  1.00 39.25           C  
ATOM   7150  CE  LYS B 450      38.621  30.787   5.653  1.00 47.34           C  
ATOM   7151  NZ  LYS B 450      40.020  30.454   5.404  1.00 53.69           N  
ATOM   7152  N   ILE B 451      35.621  24.729   5.640  1.00 20.63           N  
ATOM   7153  CA  ILE B 451      34.675  23.701   5.247  1.00 20.47           C  
ATOM   7154  C   ILE B 451      34.068  23.981   3.881  1.00 18.60           C  
ATOM   7155  O   ILE B 451      33.756  23.038   3.162  1.00 20.42           O  
ATOM   7156  CB  ILE B 451      33.598  23.572   6.377  1.00 19.38           C  
ATOM   7157  CG1 ILE B 451      32.642  22.440   6.047  1.00 12.87           C  
ATOM   7158  CG2 ILE B 451      32.864  24.884   6.580  1.00 16.66           C  
ATOM   7159  CD1 ILE B 451      33.347  21.082   6.182  1.00 16.22           C  
ATOM   7160  N   SER B 452      33.968  25.240   3.445  1.00 20.11           N  
ATOM   7161  CA  SER B 452      33.456  25.546   2.120  1.00 19.68           C  
ATOM   7162  C   SER B 452      34.420  25.057   1.060  1.00 17.91           C  
ATOM   7163  O   SER B 452      33.989  24.680  -0.028  1.00 18.39           O  
ATOM   7164  CB  SER B 452      33.235  27.052   1.957  1.00 22.04           C  
ATOM   7165  OG  SER B 452      34.415  27.791   2.273  1.00 29.14           O  
ATOM   7166  N   ASP B 453      35.720  25.037   1.358  1.00 17.85           N  
ATOM   7167  CA  ASP B 453      36.707  24.506   0.436  1.00 17.73           C  
ATOM   7168  C   ASP B 453      36.500  23.018   0.253  1.00 20.96           C  
ATOM   7169  O   ASP B 453      36.699  22.511  -0.842  1.00 23.91           O  
ATOM   7170  CB  ASP B 453      38.098  24.731   0.954  1.00 21.03           C  
ATOM   7171  CG  ASP B 453      38.467  26.195   1.014  1.00 27.09           C  
ATOM   7172  OD1 ASP B 453      38.188  26.932   0.071  1.00 37.52           O  
ATOM   7173  OD2 ASP B 453      39.061  26.598   2.002  1.00 32.90           O  
ATOM   7174  N   PHE B 454      36.086  22.306   1.301  1.00 19.64           N  
ATOM   7175  CA  PHE B 454      35.800  20.892   1.180  1.00 15.57           C  
ATOM   7176  C   PHE B 454      34.534  20.710   0.357  1.00 17.39           C  
ATOM   7177  O   PHE B 454      34.593  20.024  -0.667  1.00 15.43           O  
ATOM   7178  CB  PHE B 454      35.598  20.263   2.553  1.00 15.33           C  
ATOM   7179  CG  PHE B 454      36.888  19.919   3.275  1.00 15.22           C  
ATOM   7180  CD1 PHE B 454      37.949  20.832   3.342  1.00 12.90           C  
ATOM   7181  CD2 PHE B 454      37.018  18.650   3.835  1.00 13.64           C  
ATOM   7182  CE1 PHE B 454      39.120  20.475   3.997  1.00 12.35           C  
ATOM   7183  CE2 PHE B 454      38.199  18.307   4.489  1.00 13.82           C  
ATOM   7184  CZ  PHE B 454      39.253  19.211   4.558  1.00 11.30           C  
ATOM   7185  N   TYR B 455      33.399  21.355   0.673  1.00 15.20           N  
ATOM   7186  CA  TYR B 455      32.224  21.015  -0.093  1.00 16.98           C  
ATOM   7187  C   TYR B 455      32.101  21.703  -1.426  1.00 16.63           C  
ATOM   7188  O   TYR B 455      31.100  21.496  -2.102  1.00 22.15           O  
ATOM   7189  CB  TYR B 455      30.934  21.241   0.733  1.00 21.74           C  
ATOM   7190  CG  TYR B 455      30.616  22.610   1.299  1.00 28.22           C  
ATOM   7191  CD1 TYR B 455      30.307  23.682   0.470  1.00 29.33           C  
ATOM   7192  CD2 TYR B 455      30.620  22.775   2.676  1.00 32.73           C  
ATOM   7193  CE1 TYR B 455      30.005  24.924   1.016  1.00 31.29           C  
ATOM   7194  CE2 TYR B 455      30.316  24.015   3.234  1.00 37.94           C  
ATOM   7195  CZ  TYR B 455      30.015  25.083   2.395  1.00 35.00           C  
ATOM   7196  OH  TYR B 455      29.781  26.332   2.928  1.00 39.33           O  
ATOM   7197  N   ASN B 456      33.049  22.552  -1.808  1.00 16.15           N  
ATOM   7198  CA  ASN B 456      33.011  23.122  -3.145  1.00 18.57           C  
ATOM   7199  C   ASN B 456      33.915  22.365  -4.081  1.00 18.96           C  
ATOM   7200  O   ASN B 456      34.042  22.698  -5.262  1.00 23.88           O  
ATOM   7201  CB  ASN B 456      33.439  24.576  -3.155  1.00 18.27           C  
ATOM   7202  CG  ASN B 456      32.317  25.453  -2.611  1.00 29.21           C  
ATOM   7203  OD1 ASN B 456      31.131  25.270  -2.874  1.00 35.49           O  
ATOM   7204  ND2 ASN B 456      32.597  26.459  -1.789  1.00 33.18           N  
ATOM   7205  N   THR B 457      34.622  21.366  -3.560  1.00 18.45           N  
ATOM   7206  CA  THR B 457      35.429  20.502  -4.383  1.00 16.37           C  
ATOM   7207  C   THR B 457      34.512  19.415  -4.917  1.00 16.94           C  
ATOM   7208  O   THR B 457      33.698  18.870  -4.179  1.00 17.36           O  
ATOM   7209  CB  THR B 457      36.541  19.878  -3.556  1.00 11.79           C  
ATOM   7210  OG1 THR B 457      37.393  20.942  -3.175  1.00 15.62           O  
ATOM   7211  CG2 THR B 457      37.351  18.848  -4.320  1.00 15.22           C  
ATOM   7212  N   ILE B 458      34.648  19.042  -6.183  1.00 18.23           N  
ATOM   7213  CA  ILE B 458      33.850  17.955  -6.733  1.00 17.82           C  
ATOM   7214  C   ILE B 458      34.434  16.604  -6.296  1.00 13.14           C  
ATOM   7215  O   ILE B 458      35.649  16.406  -6.190  1.00 17.16           O  
ATOM   7216  CB  ILE B 458      33.822  18.203  -8.281  1.00 18.92           C  
ATOM   7217  CG1 ILE B 458      32.957  19.422  -8.567  1.00 10.80           C  
ATOM   7218  CG2 ILE B 458      33.221  17.042  -9.030  1.00 16.53           C  
ATOM   7219  CD1 ILE B 458      33.143  19.916 -10.000  1.00 22.67           C  
ATOM   7220  N   GLY B 459      33.527  15.692  -5.969  1.00 13.77           N  
ATOM   7221  CA  GLY B 459      33.881  14.380  -5.474  1.00 13.33           C  
ATOM   7222  C   GLY B 459      34.239  13.410  -6.571  1.00 13.41           C  
ATOM   7223  O   GLY B 459      33.772  13.530  -7.696  1.00 15.29           O  
ATOM   7224  N   VAL B 460      35.096  12.454  -6.223  1.00 16.00           N  
ATOM   7225  CA  VAL B 460      35.525  11.348  -7.054  1.00 12.69           C  
ATOM   7226  C   VAL B 460      34.479  10.297  -6.692  1.00 12.40           C  
ATOM   7227  O   VAL B 460      34.353   9.917  -5.536  1.00 12.56           O  
ATOM   7228  CB  VAL B 460      36.954  10.872  -6.649  1.00 14.77           C  
ATOM   7229  CG1 VAL B 460      37.418   9.745  -7.570  1.00 12.56           C  
ATOM   7230  CG2 VAL B 460      37.938  12.018  -6.763  1.00 13.71           C  
ATOM   7231  N   HIS B 461      33.676   9.820  -7.635  1.00 12.38           N  
ATOM   7232  CA  HIS B 461      32.597   8.894  -7.382  1.00 10.33           C  
ATOM   7233  C   HIS B 461      32.814   7.583  -8.109  1.00 10.82           C  
ATOM   7234  O   HIS B 461      33.088   7.657  -9.298  1.00 15.03           O  
ATOM   7235  CB  HIS B 461      31.318   9.581  -7.839  1.00  9.33           C  
ATOM   7236  CG  HIS B 461      30.048   8.814  -7.563  1.00  9.94           C  
ATOM   7237  ND1 HIS B 461      29.552   8.462  -6.386  1.00 12.48           N  
ATOM   7238  CD2 HIS B 461      29.217   8.341  -8.536  1.00 14.12           C  
ATOM   7239  CE1 HIS B 461      28.452   7.792  -6.593  1.00 12.48           C  
ATOM   7240  NE2 HIS B 461      28.273   7.730  -7.884  1.00 20.74           N  
ATOM   7241  N   PRO B 462      32.630   6.382  -7.555  1.00 14.53           N  
ATOM   7242  CA  PRO B 462      32.317   6.116  -6.154  1.00 12.26           C  
ATOM   7243  C   PRO B 462      33.540   5.869  -5.277  1.00 14.13           C  
ATOM   7244  O   PRO B 462      34.379   5.031  -5.610  1.00 12.87           O  
ATOM   7245  CB  PRO B 462      31.389   4.917  -6.197  1.00 10.06           C  
ATOM   7246  CG  PRO B 462      31.186   4.620  -7.654  1.00 11.70           C  
ATOM   7247  CD  PRO B 462      32.456   5.145  -8.303  1.00 10.71           C  
ATOM   7248  N   THR B 463      33.706   6.658  -4.217  1.00 14.47           N  
ATOM   7249  CA  THR B 463      34.765   6.438  -3.254  1.00 11.75           C  
ATOM   7250  C   THR B 463      34.170   6.732  -1.872  1.00 15.52           C  
ATOM   7251  O   THR B 463      33.036   7.238  -1.763  1.00 21.18           O  
ATOM   7252  CB  THR B 463      35.985   7.369  -3.525  1.00  5.83           C  
ATOM   7253  OG1 THR B 463      35.547   8.698  -3.322  1.00 11.96           O  
ATOM   7254  CG2 THR B 463      36.595   7.175  -4.902  1.00 14.54           C  
ATOM   7255  N   SER B 464      34.887   6.388  -0.785  1.00 15.40           N  
ATOM   7256  CA  SER B 464      34.476   6.756   0.572  1.00 12.29           C  
ATOM   7257  C   SER B 464      34.886   8.189   0.787  1.00  9.21           C  
ATOM   7258  O   SER B 464      34.126   8.972   1.336  1.00 15.26           O  
ATOM   7259  CB  SER B 464      35.173   5.913   1.628  1.00  7.70           C  
ATOM   7260  OG  SER B 464      34.810   4.586   1.331  1.00 12.09           O  
ATOM   7261  N   ALA B 465      36.057   8.554   0.254  1.00  8.97           N  
ATOM   7262  CA  ALA B 465      36.598   9.876   0.472  1.00  8.01           C  
ATOM   7263  C   ALA B 465      35.732  11.028  -0.004  1.00  9.36           C  
ATOM   7264  O   ALA B 465      35.766  12.109   0.590  1.00 12.85           O  
ATOM   7265  CB  ALA B 465      37.955   9.933  -0.197  1.00  3.46           C  
ATOM   7266  N   GLU B 466      34.880  10.828  -1.004  1.00  9.93           N  
ATOM   7267  CA  GLU B 466      34.026  11.895  -1.495  1.00  9.70           C  
ATOM   7268  C   GLU B 466      33.025  12.327  -0.437  1.00 14.35           C  
ATOM   7269  O   GLU B 466      32.462  13.428  -0.532  1.00 15.34           O  
ATOM   7270  CB  GLU B 466      33.254  11.460  -2.751  1.00 11.59           C  
ATOM   7271  CG  GLU B 466      32.289  10.306  -2.523  1.00 10.86           C  
ATOM   7272  CD  GLU B 466      31.443   9.919  -3.721  1.00 14.96           C  
ATOM   7273  OE1 GLU B 466      30.958  10.802  -4.419  1.00 15.48           O  
ATOM   7274  OE2 GLU B 466      31.264   8.725  -3.939  1.00 20.12           O  
ATOM   7275  N   GLU B 467      32.785  11.528   0.613  1.00 14.05           N  
ATOM   7276  CA  GLU B 467      31.896  11.936   1.690  1.00 12.09           C  
ATOM   7277  C   GLU B 467      32.365  13.213   2.338  1.00 13.58           C  
ATOM   7278  O   GLU B 467      31.553  14.045   2.729  1.00 15.94           O  
ATOM   7279  CB  GLU B 467      31.814  10.880   2.752  1.00 14.38           C  
ATOM   7280  CG  GLU B 467      30.682   9.964   2.377  1.00 27.10           C  
ATOM   7281  CD  GLU B 467      29.308  10.616   2.475  1.00 34.83           C  
ATOM   7282  OE1 GLU B 467      29.040  11.326   3.447  1.00 34.80           O  
ATOM   7283  OE2 GLU B 467      28.506  10.416   1.563  1.00 44.48           O  
ATOM   7284  N   LEU B 468      33.675  13.421   2.377  1.00 12.44           N  
ATOM   7285  CA  LEU B 468      34.238  14.612   2.960  1.00 15.41           C  
ATOM   7286  C   LEU B 468      33.888  15.858   2.172  1.00 17.26           C  
ATOM   7287  O   LEU B 468      33.910  16.944   2.742  1.00 21.92           O  
ATOM   7288  CB  LEU B 468      35.761  14.408   3.069  1.00 13.25           C  
ATOM   7289  CG  LEU B 468      36.226  13.289   4.012  1.00 17.28           C  
ATOM   7290  CD1 LEU B 468      37.718  13.072   3.869  1.00 13.59           C  
ATOM   7291  CD2 LEU B 468      35.882  13.667   5.455  1.00 18.41           C  
ATOM   7292  N   CYS B 469      33.531  15.726   0.903  1.00 16.01           N  
ATOM   7293  CA  CYS B 469      33.127  16.851   0.073  1.00 18.55           C  
ATOM   7294  C   CYS B 469      31.621  16.954   0.071  1.00 17.13           C  
ATOM   7295  O   CYS B 469      31.053  17.760  -0.650  1.00 19.61           O  
ATOM   7296  CB  CYS B 469      33.599  16.667  -1.368  1.00 16.33           C  
ATOM   7297  SG  CYS B 469      35.393  16.521  -1.357  1.00 18.94           S  
ATOM   7298  N   SER B 470      30.927  16.164   0.875  1.00 19.69           N  
ATOM   7299  CA  SER B 470      29.487  16.201   0.837  1.00 21.88           C  
ATOM   7300  C   SER B 470      28.900  16.569   2.191  1.00 24.62           C  
ATOM   7301  O   SER B 470      27.707  16.364   2.412  1.00 24.73           O  
ATOM   7302  CB  SER B 470      29.019  14.836   0.379  1.00 23.27           C  
ATOM   7303  OG  SER B 470      29.686  14.377  -0.804  1.00 35.69           O  
ATOM   7304  N   MET B 471      29.702  17.089   3.125  1.00 26.16           N  
ATOM   7305  CA  MET B 471      29.261  17.460   4.466  1.00 23.38           C  
ATOM   7306  C   MET B 471      29.108  18.968   4.515  1.00 22.83           C  
ATOM   7307  O   MET B 471      30.065  19.731   4.602  1.00 23.67           O  
ATOM   7308  CB  MET B 471      30.291  16.998   5.458  1.00 25.41           C  
ATOM   7309  CG  MET B 471      30.128  15.518   5.665  1.00 24.82           C  
ATOM   7310  SD  MET B 471      31.266  14.906   6.928  1.00 34.26           S  
ATOM   7311  CE  MET B 471      32.098  13.848   5.826  1.00 17.56           C  
ATOM   7312  N   ARG B 472      27.875  19.422   4.504  1.00 23.20           N  
ATOM   7313  CA  ARG B 472      27.616  20.830   4.319  1.00 25.63           C  
ATOM   7314  C   ARG B 472      26.966  21.494   5.521  1.00 26.11           C  
ATOM   7315  O   ARG B 472      27.153  22.683   5.737  1.00 28.31           O  
ATOM   7316  CB  ARG B 472      26.760  20.894   3.056  1.00 28.18           C  
ATOM   7317  CG  ARG B 472      26.760  22.159   2.219  1.00 44.70           C  
ATOM   7318  CD  ARG B 472      26.219  21.815   0.828  1.00 51.49           C  
ATOM   7319  NE  ARG B 472      27.161  21.021   0.050  1.00 66.16           N  
ATOM   7320  CZ  ARG B 472      27.546  21.386  -1.184  1.00 71.05           C  
ATOM   7321  NH1 ARG B 472      27.091  22.501  -1.766  1.00 74.31           N  
ATOM   7322  NH2 ARG B 472      28.415  20.622  -1.849  1.00 72.97           N  
ATOM   7323  N   THR B 473      26.276  20.711   6.348  1.00 27.59           N  
ATOM   7324  CA  THR B 473      25.473  21.199   7.468  1.00 29.42           C  
ATOM   7325  C   THR B 473      25.962  20.555   8.764  1.00 27.49           C  
ATOM   7326  O   THR B 473      26.049  19.325   8.781  1.00 28.93           O  
ATOM   7327  CB  THR B 473      23.999  20.815   7.220  1.00 33.08           C  
ATOM   7328  OG1 THR B 473      23.721  21.183   5.871  1.00 38.37           O  
ATOM   7329  CG2 THR B 473      23.026  21.487   8.184  1.00 35.41           C  
ATOM   7330  N   PRO B 474      26.309  21.282   9.840  1.00 24.84           N  
ATOM   7331  CA  PRO B 474      26.798  20.701  11.084  1.00 20.17           C  
ATOM   7332  C   PRO B 474      25.764  19.810  11.738  1.00 19.89           C  
ATOM   7333  O   PRO B 474      24.573  19.999  11.505  1.00 21.13           O  
ATOM   7334  CB  PRO B 474      27.165  21.884  11.918  1.00 17.84           C  
ATOM   7335  CG  PRO B 474      27.313  23.019  10.942  1.00 20.54           C  
ATOM   7336  CD  PRO B 474      26.227  22.735   9.936  1.00 16.94           C  
ATOM   7337  N   SER B 475      26.154  18.794  12.489  1.00 21.94           N  
ATOM   7338  CA  SER B 475      25.187  18.006  13.235  1.00 26.47           C  
ATOM   7339  C   SER B 475      24.830  18.698  14.554  1.00 24.00           C  
ATOM   7340  O   SER B 475      23.699  18.626  15.032  1.00 27.78           O  
ATOM   7341  CB  SER B 475      25.736  16.641  13.583  1.00 29.26           C  
ATOM   7342  OG  SER B 475      26.528  16.020  12.585  1.00 37.15           O  
ATOM   7343  N   TYR B 476      25.812  19.274  15.236  1.00 20.89           N  
ATOM   7344  CA  TYR B 476      25.592  19.995  16.477  1.00 21.20           C  
ATOM   7345  C   TYR B 476      26.770  20.927  16.626  1.00 21.14           C  
ATOM   7346  O   TYR B 476      27.695  20.908  15.799  1.00 21.39           O  
ATOM   7347  CB  TYR B 476      25.503  19.045  17.694  1.00 17.07           C  
ATOM   7348  CG  TYR B 476      26.646  18.062  17.884  1.00 18.59           C  
ATOM   7349  CD1 TYR B 476      26.602  16.835  17.218  1.00 19.08           C  
ATOM   7350  CD2 TYR B 476      27.737  18.393  18.687  1.00 17.25           C  
ATOM   7351  CE1 TYR B 476      27.658  15.942  17.343  1.00 20.87           C  
ATOM   7352  CE2 TYR B 476      28.792  17.500  18.818  1.00 21.91           C  
ATOM   7353  CZ  TYR B 476      28.744  16.285  18.137  1.00 20.05           C  
ATOM   7354  OH  TYR B 476      29.801  15.408  18.216  1.00 23.55           O  
ATOM   7355  N   TYR B 477      26.744  21.761  17.649  1.00 23.66           N  
ATOM   7356  CA  TYR B 477      27.753  22.781  17.849  1.00 23.36           C  
ATOM   7357  C   TYR B 477      28.187  22.751  19.304  1.00 26.23           C  
ATOM   7358  O   TYR B 477      27.534  22.116  20.140  1.00 26.28           O  
ATOM   7359  CB  TYR B 477      27.176  24.154  17.558  1.00 20.78           C  
ATOM   7360  CG  TYR B 477      26.506  24.349  16.206  1.00 20.59           C  
ATOM   7361  CD1 TYR B 477      25.198  23.905  15.992  1.00 18.93           C  
ATOM   7362  CD2 TYR B 477      27.209  24.985  15.180  1.00 16.71           C  
ATOM   7363  CE1 TYR B 477      24.592  24.094  14.743  1.00 21.60           C  
ATOM   7364  CE2 TYR B 477      26.606  25.178  13.943  1.00 16.49           C  
ATOM   7365  CZ  TYR B 477      25.307  24.731  13.726  1.00 21.09           C  
ATOM   7366  OH  TYR B 477      24.764  24.921  12.468  1.00 26.19           O  
ATOM   7367  N   TYR B 478      29.283  23.421  19.629  1.00 25.86           N  
ATOM   7368  CA  TYR B 478      29.717  23.595  20.998  1.00 30.78           C  
ATOM   7369  C   TYR B 478      29.822  25.085  21.200  1.00 33.55           C  
ATOM   7370  O   TYR B 478      30.698  25.698  20.586  1.00 34.36           O  
ATOM   7371  CB  TYR B 478      31.090  23.024  21.268  1.00 34.45           C  
ATOM   7372  CG  TYR B 478      31.048  21.540  21.510  1.00 37.70           C  
ATOM   7373  CD1 TYR B 478      30.539  21.066  22.715  1.00 36.98           C  
ATOM   7374  CD2 TYR B 478      31.511  20.665  20.532  1.00 38.00           C  
ATOM   7375  CE1 TYR B 478      30.486  19.700  22.950  1.00 36.12           C  
ATOM   7376  CE2 TYR B 478      31.459  19.297  20.766  1.00 29.52           C  
ATOM   7377  CZ  TYR B 478      30.948  18.826  21.971  1.00 36.25           C  
ATOM   7378  OH  TYR B 478      30.901  17.463  22.198  1.00 36.84           O  
ATOM   7379  N   VAL B 479      28.954  25.699  22.000  1.00 35.60           N  
ATOM   7380  CA  VAL B 479      29.017  27.133  22.256  1.00 37.75           C  
ATOM   7381  C   VAL B 479      29.461  27.315  23.696  1.00 38.89           C  
ATOM   7382  O   VAL B 479      28.746  26.941  24.635  1.00 36.56           O  
ATOM   7383  CB  VAL B 479      27.636  27.743  22.022  1.00 38.61           C  
ATOM   7384  CG1 VAL B 479      27.698  29.235  22.287  1.00 39.46           C  
ATOM   7385  CG2 VAL B 479      27.194  27.482  20.588  1.00 37.43           C  
ATOM   7386  N   LYS B 480      30.665  27.866  23.866  1.00 41.31           N  
ATOM   7387  CA  LYS B 480      31.306  28.046  25.161  1.00 48.35           C  
ATOM   7388  C   LYS B 480      31.383  26.729  25.938  1.00 50.57           C  
ATOM   7389  O   LYS B 480      31.198  26.669  27.159  1.00 54.68           O  
ATOM   7390  CB  LYS B 480      30.549  29.105  25.993  1.00 56.04           C  
ATOM   7391  CG  LYS B 480      30.892  30.569  25.717  1.00 59.72           C  
ATOM   7392  CD  LYS B 480      32.308  30.864  26.195  1.00 69.59           C  
ATOM   7393  CE  LYS B 480      32.611  32.347  26.075  1.00 66.46           C  
ATOM   7394  NZ  LYS B 480      34.002  32.636  26.386  1.00 74.34           N  
ATOM   7395  N   GLY B 481      31.650  25.645  25.210  1.00 48.61           N  
ATOM   7396  CA  GLY B 481      31.719  24.305  25.776  1.00 43.94           C  
ATOM   7397  C   GLY B 481      30.369  23.600  25.909  1.00 43.97           C  
ATOM   7398  O   GLY B 481      30.312  22.388  26.112  1.00 45.13           O  
ATOM   7399  N   GLU B 482      29.242  24.285  25.767  1.00 45.60           N  
ATOM   7400  CA  GLU B 482      27.928  23.673  25.901  1.00 48.19           C  
ATOM   7401  C   GLU B 482      27.550  23.087  24.541  1.00 45.90           C  
ATOM   7402  O   GLU B 482      27.756  23.754  23.525  1.00 43.50           O  
ATOM   7403  CB  GLU B 482      26.907  24.737  26.307  1.00 54.74           C  
ATOM   7404  CG  GLU B 482      27.311  25.673  27.459  1.00 67.84           C  
ATOM   7405  CD  GLU B 482      26.589  27.025  27.466  1.00 72.25           C  
ATOM   7406  OE1 GLU B 482      25.522  27.133  28.075  1.00 67.43           O  
ATOM   7407  OE2 GLU B 482      27.096  27.975  26.860  1.00 68.69           O  
ATOM   7408  N   LYS B 483      27.056  21.851  24.448  1.00 44.79           N  
ATOM   7409  CA  LYS B 483      26.602  21.307  23.180  1.00 43.78           C  
ATOM   7410  C   LYS B 483      25.266  21.949  22.883  1.00 44.99           C  
ATOM   7411  O   LYS B 483      24.376  21.982  23.738  1.00 45.61           O  
ATOM   7412  CB  LYS B 483      26.429  19.790  23.256  1.00 42.42           C  
ATOM   7413  CG  LYS B 483      25.843  19.180  21.989  1.00 44.56           C  
ATOM   7414  CD  LYS B 483      25.935  17.669  21.978  1.00 49.84           C  
ATOM   7415  CE  LYS B 483      24.753  17.145  21.169  1.00 59.54           C  
ATOM   7416  NZ  LYS B 483      24.769  15.697  21.087  1.00 66.76           N  
ATOM   7417  N   MET B 484      25.128  22.499  21.693  1.00 46.78           N  
ATOM   7418  CA  MET B 484      23.867  23.066  21.279  1.00 45.69           C  
ATOM   7419  C   MET B 484      23.541  22.627  19.869  1.00 45.04           C  
ATOM   7420  O   MET B 484      24.403  22.200  19.099  1.00 44.13           O  
ATOM   7421  CB  MET B 484      23.939  24.592  21.377  1.00 47.89           C  
ATOM   7422  CG  MET B 484      23.498  25.090  22.749  1.00 50.96           C  
ATOM   7423  SD  MET B 484      24.074  26.751  23.154  1.00 46.68           S  
ATOM   7424  CE  MET B 484      23.694  27.777  21.767  1.00 50.93           C  
ATOM   7425  N   GLU B 485      22.265  22.697  19.535  1.00 47.66           N  
ATOM   7426  CA  GLU B 485      21.765  22.303  18.238  1.00 51.99           C  
ATOM   7427  C   GLU B 485      20.838  23.370  17.698  1.00 54.48           C  
ATOM   7428  O   GLU B 485      20.214  24.124  18.448  1.00 56.63           O  
ATOM   7429  CB  GLU B 485      20.980  21.006  18.332  1.00 48.98           C  
ATOM   7430  CG  GLU B 485      21.773  19.805  18.878  1.00 63.30           C  
ATOM   7431  CD  GLU B 485      20.973  18.521  19.105  1.00 65.19           C  
ATOM   7432  OE1 GLU B 485      19.738  18.557  19.035  1.00 75.38           O  
ATOM   7433  OE2 GLU B 485      21.582  17.476  19.369  1.00 65.04           O  
ATOM   7434  N   LYS B 486      20.794  23.453  16.374  1.00 56.65           N  
ATOM   7435  CA  LYS B 486      19.827  24.291  15.683  1.00 59.18           C  
ATOM   7436  C   LYS B 486      18.469  23.599  15.828  1.00 62.86           C  
ATOM   7437  O   LYS B 486      18.468  22.372  15.774  1.00 66.22           O  
ATOM   7438  CB  LYS B 486      20.156  24.396  14.215  1.00 54.75           C  
ATOM   7439  CG  LYS B 486      21.190  25.449  13.889  1.00 57.74           C  
ATOM   7440  CD  LYS B 486      20.907  26.015  12.505  1.00 59.25           C  
ATOM   7441  CE  LYS B 486      22.012  26.947  12.027  1.00 60.35           C  
ATOM   7442  NZ  LYS B 486      21.584  27.752  10.894  1.00 63.48           N  
ATOM   7443  N   PRO B 487      17.310  24.202  16.052  1.00 67.19           N  
ATOM   7444  CA  PRO B 487      16.043  23.516  16.337  1.00 70.68           C  
ATOM   7445  C   PRO B 487      15.316  22.762  15.221  1.00 74.21           C  
ATOM   7446  CB  PRO B 487      15.219  24.615  16.952  1.00 71.25           C  
ATOM   7447  CG  PRO B 487      15.705  25.832  16.220  1.00 71.35           C  
ATOM   7448  CD  PRO B 487      17.193  25.626  16.236  1.00 66.33           C  
TER    7449      PRO B 487                                                      
HETATM 7450  PA  FAD A 492      22.006  10.175 -16.670  1.00 21.95           P  
HETATM 7451  O1A FAD A 492      22.574   9.460 -17.827  1.00 21.22           O  
HETATM 7452  O2A FAD A 492      22.344   9.720 -15.310  1.00 25.96           O  
HETATM 7453  O5B FAD A 492      20.430  10.207 -16.769  1.00 18.78           O  
HETATM 7454  C5B FAD A 492      19.781  10.235 -18.027  1.00 15.82           C  
HETATM 7455  C4B FAD A 492      18.334   9.642 -17.958  1.00 14.00           C  
HETATM 7456  O4B FAD A 492      17.591  10.062 -19.091  1.00 14.34           O  
HETATM 7457  C3B FAD A 492      18.295   8.138 -17.920  1.00 15.96           C  
HETATM 7458  O3B FAD A 492      18.110   7.214 -16.880  1.00  8.62           O  
HETATM 7459  C2B FAD A 492      17.348   7.671 -19.091  1.00 15.28           C  
HETATM 7460  O2B FAD A 492      16.671   6.622 -19.259  1.00 14.42           O  
HETATM 7461  C1B FAD A 492      16.734   8.997 -19.519  1.00 15.95           C  
HETATM 7462  N9A FAD A 492      16.144   9.547 -20.722  1.00 15.97           N  
HETATM 7463  C8A FAD A 492      16.845   9.730 -21.868  1.00 17.66           C  
HETATM 7464  N7A FAD A 492      16.164  10.278 -22.822  1.00 19.11           N  
HETATM 7465  C5A FAD A 492      14.908  10.425 -22.294  1.00 14.77           C  
HETATM 7466  C6A FAD A 492      13.728  10.944 -22.823  1.00 17.20           C  
HETATM 7467  N6A FAD A 492      13.639  11.432 -24.051  1.00 16.47           N  
HETATM 7468  N1A FAD A 492      12.662  10.947 -22.023  1.00 23.12           N  
HETATM 7469  C2A FAD A 492      12.783  10.532 -20.769  1.00 19.84           C  
HETATM 7470  N3A FAD A 492      13.847  10.044 -20.156  1.00 17.84           N  
HETATM 7471  C4A FAD A 492      14.897  10.031 -20.991  1.00 15.43           C  
HETATM 7472  N1  FAD A 492      30.855   8.587 -13.747  1.00 14.16           N  
HETATM 7473  C2  FAD A 492      31.538   8.793 -12.536  1.00 11.66           C  
HETATM 7474  O2  FAD A 492      31.495   9.873 -11.957  1.00 10.96           O  
HETATM 7475  N3  FAD A 492      32.179   7.727 -11.965  1.00 10.44           N  
HETATM 7476  C4  FAD A 492      32.161   6.448 -12.484  1.00 14.75           C  
HETATM 7477  O4  FAD A 492      32.622   5.522 -11.838  1.00 14.48           O  
HETATM 7478  C4X FAD A 492      31.472   6.281 -13.813  1.00 10.48           C  
HETATM 7479  N5  FAD A 492      31.380   5.084 -14.386  1.00  9.04           N  
HETATM 7480  C5X FAD A 492      30.650   4.898 -15.483  1.00  8.47           C  
HETATM 7481  C6  FAD A 492      30.673   3.656 -16.142  1.00  8.50           C  
HETATM 7482  C7  FAD A 492      29.895   3.409 -17.214  1.00 10.98           C  
HETATM 7483  C7M FAD A 492      29.758   1.973 -17.772  1.00  3.00           C  
HETATM 7484  C8  FAD A 492      29.114   4.490 -17.765  1.00  8.41           C  
HETATM 7485  C8M FAD A 492      28.089   4.241 -18.858  1.00  9.33           C  
HETATM 7486  C9  FAD A 492      29.197   5.718 -17.230  1.00 11.27           C  
HETATM 7487  C9A FAD A 492      29.937   5.975 -16.061  1.00 11.14           C  
HETATM 7488  N10 FAD A 492      30.013   7.212 -15.480  1.00 14.26           N  
HETATM 7489  C10 FAD A 492      30.791   7.399 -14.368  1.00  9.75           C  
HETATM 7490  C1' FAD A 492      29.225   8.369 -16.052  1.00  3.00           C  
HETATM 7491  C2' FAD A 492      28.025   8.836 -15.365  1.00  5.21           C  
HETATM 7492  O2' FAD A 492      27.204   7.692 -15.294  1.00  9.04           O  
HETATM 7493  C3' FAD A 492      27.314   9.887 -16.125  1.00  8.34           C  
HETATM 7494  O3' FAD A 492      28.244  10.957 -16.285  1.00  9.51           O  
HETATM 7495  C4' FAD A 492      26.121  10.438 -15.421  1.00  8.52           C  
HETATM 7496  O4' FAD A 492      25.135   9.412 -15.316  1.00 11.36           O  
HETATM 7497  C5' FAD A 492      25.454  11.533 -16.200  1.00 11.71           C  
HETATM 7498  O5' FAD A 492      24.319  12.068 -15.522  1.00 18.11           O  
HETATM 7499  P   FAD A 492      23.203  12.790 -16.387  1.00 11.56           P  
HETATM 7500  O1P FAD A 492      22.281  13.448 -15.436  1.00 15.25           O  
HETATM 7501  O2P FAD A 492      23.895  13.628 -17.376  1.00 15.80           O  
HETATM 7502  O3P FAD A 492      22.430  11.623 -17.113  1.00 13.68           O  
HETATM 7503  C1  MAE A 500      38.731   2.038 -31.474  1.00 34.26           C  
HETATM 7504  O1  MAE A 500      38.842   3.163 -31.004  1.00 39.86           O  
HETATM 7505  O2  MAE A 500      39.584   1.299 -31.019  1.00 31.46           O  
HETATM 7506  C2  MAE A 500      37.839   1.609 -32.516  1.00 38.67           C  
HETATM 7507  C3  MAE A 500      36.819   2.234 -33.222  1.00 37.97           C  
HETATM 7508  C4  MAE A 500      36.181   3.522 -33.120  1.00 39.05           C  
HETATM 7509  O3  MAE A 500      35.177   3.784 -33.796  1.00 35.15           O  
HETATM 7510  O4  MAE A 500      36.490   4.432 -32.358  1.00 38.44           O  
HETATM 7511  C1  MAE A 501      40.282  -5.084 -44.395  1.00 74.91           C  
HETATM 7512  O1  MAE A 501      40.454  -6.232 -43.949  1.00 69.22           O  
HETATM 7513  O2  MAE A 501      41.307  -4.412 -44.515  1.00 79.18           O  
HETATM 7514  C2  MAE A 501      39.060  -4.478 -44.837  1.00 70.66           C  
HETATM 7515  C3  MAE A 501      37.782  -4.968 -45.034  1.00 67.57           C  
HETATM 7516  C4  MAE A 501      37.246  -6.265 -44.797  1.00 69.08           C  
HETATM 7517  O3  MAE A 501      37.856  -7.223 -44.319  1.00 67.93           O  
HETATM 7518  O4  MAE A 501      36.040  -6.446 -44.991  1.00 69.52           O  
HETATM 7519  PA  FAD B 492      64.378   5.069  16.714  1.00 26.09           P  
HETATM 7520  O1A FAD B 492      63.772   4.501  17.941  1.00 22.59           O  
HETATM 7521  O2A FAD B 492      63.961   4.492  15.408  1.00 31.71           O  
HETATM 7522  O5B FAD B 492      65.962   4.830  16.817  1.00 26.20           O  
HETATM 7523  C5B FAD B 492      66.562   4.610  18.097  1.00 24.00           C  
HETATM 7524  C4B FAD B 492      67.977   4.096  17.941  1.00 22.54           C  
HETATM 7525  O4B FAD B 492      68.736   4.336  19.116  1.00 26.26           O  
HETATM 7526  C3B FAD B 492      67.732   2.660  17.929  1.00 25.75           C  
HETATM 7527  O3B FAD B 492      67.822   1.658  16.824  1.00 29.10           O  
HETATM 7528  C2B FAD B 492      68.374   2.113  19.217  1.00 27.35           C  
HETATM 7529  O2B FAD B 492      68.955   0.810  19.228  1.00 26.85           O  
HETATM 7530  C1B FAD B 492      69.435   3.142  19.480  1.00 26.43           C  
HETATM 7531  N9A FAD B 492      70.019   3.140  20.829  1.00 35.39           N  
HETATM 7532  C8A FAD B 492      69.411   3.534  21.989  1.00 36.31           C  
HETATM 7533  N7A FAD B 492      70.229   3.910  22.923  1.00 39.15           N  
HETATM 7534  C5A FAD B 492      71.473   3.754  22.352  1.00 38.90           C  
HETATM 7535  C6A FAD B 492      72.755   4.023  22.824  1.00 39.43           C  
HETATM 7536  N6A FAD B 492      72.968   4.631  23.983  1.00 38.92           N  
HETATM 7537  N1A FAD B 492      73.776   3.653  22.048  1.00 42.09           N  
HETATM 7538  C2A FAD B 492      73.535   3.164  20.836  1.00 37.78           C  
HETATM 7539  N3A FAD B 492      72.376   2.906  20.253  1.00 40.95           N  
HETATM 7540  C4A FAD B 492      71.363   3.236  21.092  1.00 38.94           C  
HETATM 7541  N1  FAD B 492      55.495   5.441  13.822  1.00 18.89           N  
HETATM 7542  C2  FAD B 492      54.836   5.821  12.645  1.00 14.77           C  
HETATM 7543  O2  FAD B 492      55.055   6.897  12.097  1.00 20.85           O  
HETATM 7544  N3  FAD B 492      53.966   4.944  12.078  1.00 15.13           N  
HETATM 7545  C4  FAD B 492      53.712   3.694  12.585  1.00 14.51           C  
HETATM 7546  O4  FAD B 492      52.961   2.921  12.015  1.00 19.71           O  
HETATM 7547  C4X FAD B 492      54.432   3.328  13.829  1.00 13.40           C  
HETATM 7548  N5  FAD B 492      54.271   2.125  14.340  1.00 20.53           N  
HETATM 7549  C5X FAD B 492      54.917   1.754  15.422  1.00 16.32           C  
HETATM 7550  C6  FAD B 492      54.669   0.488  15.970  1.00 20.63           C  
HETATM 7551  C7  FAD B 492      55.393   0.021  17.005  1.00 14.90           C  
HETATM 7552  C7M FAD B 492      55.218  -1.427  17.489  1.00 10.49           C  
HETATM 7553  C8  FAD B 492      56.382   0.876  17.595  1.00 14.95           C  
HETATM 7554  C8M FAD B 492      57.234   0.361  18.721  1.00 11.81           C  
HETATM 7555  C9  FAD B 492      56.573   2.125  17.134  1.00 18.12           C  
HETATM 7556  C9A FAD B 492      55.852   2.623  16.033  1.00 19.43           C  
HETATM 7557  N10 FAD B 492      56.049   3.875  15.498  1.00 18.86           N  
HETATM 7558  C10 FAD B 492      55.333   4.254  14.402  1.00 11.96           C  
HETATM 7559  C1' FAD B 492      56.909   4.883  16.247  1.00 11.91           C  
HETATM 7560  C2' FAD B 492      58.214   5.120  15.536  1.00 15.60           C  
HETATM 7561  O2' FAD B 492      58.849   3.850  15.369  1.00 22.46           O  
HETATM 7562  C3' FAD B 492      59.152   5.999  16.264  1.00 17.76           C  
HETATM 7563  O3' FAD B 492      58.459   7.244  16.488  1.00 20.35           O  
HETATM 7564  C4' FAD B 492      60.425   6.275  15.488  1.00 17.79           C  
HETATM 7565  O4' FAD B 492      61.207   5.083  15.334  1.00 18.15           O  
HETATM 7566  C5' FAD B 492      61.286   7.206  16.268  1.00 19.19           C  
HETATM 7567  O5' FAD B 492      62.532   7.440  15.635  1.00 26.13           O  
HETATM 7568  P   FAD B 492      63.729   7.869  16.602  1.00 21.91           P  
HETATM 7569  O1P FAD B 492      64.779   8.418  15.720  1.00 24.66           O  
HETATM 7570  O2P FAD B 492      63.171   8.782  17.611  1.00 20.86           O  
HETATM 7571  O3P FAD B 492      64.239   6.541  17.263  1.00 17.35           O  
HETATM 7572  O   HOH A 502      19.546  13.352 -15.199  1.00 12.14           O  
HETATM 7573  O   HOH A 503      20.219  24.324  -5.927  1.00 35.07           O  
HETATM 7574  O   HOH A 504      21.302  12.683  -7.923  1.00 35.43           O  
HETATM 7575  O   HOH A 505       8.693  29.404 -12.063  1.00 34.79           O  
HETATM 7576  O   HOH A 506      17.496   4.711 -20.961  1.00 31.50           O  
HETATM 7577  O   HOH A 507      22.034   5.587 -20.228  1.00 31.86           O  
HETATM 7578  O   HOH A 508      23.961   3.761 -21.352  1.00 32.05           O  
HETATM 7579  O   HOH A 509      32.956   0.697 -16.693  1.00 24.49           O  
HETATM 7580  O   HOH A 510      41.503  -8.456 -13.708  1.00 19.40           O  
HETATM 7581  O   HOH A 511      46.869  -6.012 -13.034  1.00 24.06           O  
HETATM 7582  O   HOH A 512      16.295  -6.636  -9.777  1.00 43.39           O  
HETATM 7583  O   HOH A 513      22.526  14.974 -19.342  1.00 15.89           O  
HETATM 7584  O   HOH A 514      24.704   9.320 -19.522  1.00 11.02           O  
HETATM 7585  O   HOH A 515      28.723   8.812 -19.694  1.00 18.83           O  
HETATM 7586  O   HOH A 516      31.346   8.530 -19.214  1.00 25.33           O  
HETATM 7587  O   HOH A 517      30.905   3.186 -24.780  1.00 19.39           O  
HETATM 7588  O   HOH A 518      30.659   2.146 -27.754  1.00 25.72           O  
HETATM 7589  O   HOH A 519      40.477 -13.226 -26.380  1.00 32.69           O  
HETATM 7590  O   HOH A 520      41.721 -15.331 -27.575  1.00 39.10           O  
HETATM 7591  O   HOH A 521      38.324   7.350 -21.040  1.00 15.37           O  
HETATM 7592  O   HOH A 522      35.657   4.323 -22.734  1.00 29.71           O  
HETATM 7593  O   HOH A 523      41.265  -3.384 -15.474  1.00 21.78           O  
HETATM 7594  O   HOH A 524      38.957  -3.168 -13.960  1.00 11.42           O  
HETATM 7595  O   HOH A 525      35.719   5.339 -13.414  1.00 18.81           O  
HETATM 7596  O   HOH A 526      35.940   9.181 -11.561  1.00 18.37           O  
HETATM 7597  O   HOH A 527      42.769 -12.682 -20.065  1.00 25.61           O  
HETATM 7598  O   HOH A 528      46.752   7.824 -29.650  1.00 36.57           O  
HETATM 7599  O   HOH A 529      48.243   0.368 -24.573  1.00 30.43           O  
HETATM 7600  O   HOH A 530      46.945  12.126 -24.148  1.00 40.14           O  
HETATM 7601  O   HOH A 531      52.009  14.480 -17.123  1.00 38.38           O  
HETATM 7602  O   HOH A 532      36.276   0.001 -36.249  1.00 28.71           O  
HETATM 7603  O   HOH A 533      37.061   0.018 -40.378  1.00 24.89           O  
HETATM 7604  O   HOH A 534      25.202  24.656 -14.087  1.00 28.39           O  
HETATM 7605  O   HOH A 535      24.191  27.379 -13.680  1.00 25.79           O  
HETATM 7606  O   HOH A 536      27.896  25.303 -14.815  1.00 22.50           O  
HETATM 7607  O   HOH A 537      27.905  15.124 -16.682  1.00 19.16           O  
HETATM 7608  O   HOH A 538      29.309  18.286 -17.852  1.00 31.17           O  
HETATM 7609  O   HOH A 539      34.711  13.103 -10.537  1.00 15.83           O  
HETATM 7610  O   HOH A 540      36.173  22.172  -9.946  1.00 23.61           O  
HETATM 7611  O   HOH A 541      37.760  17.243  -7.934  1.00 17.44           O  
HETATM 7612  O   HOH A 542      50.116  -0.352  -9.527  1.00 20.40           O  
HETATM 7613  O   HOH A 543      49.553  -1.306  -6.726  1.00 45.72           O  
HETATM 7614  O   HOH A 544      58.649  23.602  -9.421  1.00 30.71           O  
HETATM 7615  O   HOH A 545      50.005  29.323 -12.175  1.00 46.22           O  
HETATM 7616  O   HOH A 546      47.289  23.872  -7.088  1.00 23.62           O  
HETATM 7617  O   HOH A 547      37.490   3.129  -3.779  1.00 29.01           O  
HETATM 7618  O   HOH A 548      42.002  11.827   0.069  1.00 19.91           O  
HETATM 7619  O   HOH A 549      39.189  19.477  -7.240  1.00 23.20           O  
HETATM 7620  O   HOH A 550      56.277  16.305  -2.203  1.00 24.18           O  
HETATM 7621  O   HOH A 551      53.047   8.173  10.616  1.00 16.70           O  
HETATM 7622  O   HOH A 552      51.151 -15.121  -3.877  1.00 50.39           O  
HETATM 7623  O   HOH A 553      21.897  -0.853 -25.504  1.00 33.29           O  
HETATM 7624  O   HOH A 554      16.600  32.008 -19.757  1.00 43.73           O  
HETATM 7625  O   HOH A 555      41.086  17.436 -13.747  1.00 30.67           O  
HETATM 7626  O   HOH A 556      38.570  18.818 -15.225  1.00 34.27           O  
HETATM 7627  O   HOH A 557      52.314  18.679   8.360  1.00 29.13           O  
HETATM 7628  O   HOH A 558      22.785  -3.162 -13.952  1.00 22.59           O  
HETATM 7629  O   HOH A 559      26.303   1.182 -19.707  1.00 15.65           O  
HETATM 7630  O   HOH A 560      41.548  -9.124 -10.955  1.00 29.27           O  
HETATM 7631  O   HOH A 561      45.172 -14.564 -10.495  1.00 47.34           O  
HETATM 7632  O   HOH A 562      47.582  -7.900 -11.379  1.00 23.79           O  
HETATM 7633  O   HOH A 563      43.789  -6.585 -14.293  1.00 23.29           O  
HETATM 7634  O   HOH A 564      45.697  -7.809  -1.869  1.00 20.52           O  
HETATM 7635  O   HOH A 565       8.769  10.392 -27.677  1.00 31.65           O  
HETATM 7636  O   HOH A 566      10.753  11.651 -30.085  1.00 38.68           O  
HETATM 7637  O   HOH A 567       8.542  29.525 -21.033  1.00 37.03           O  
HETATM 7638  O   HOH A 568      20.933   8.330 -21.002  1.00 18.30           O  
HETATM 7639  O   HOH A 569      28.906   2.933 -22.590  1.00 16.95           O  
HETATM 7640  O   HOH A 570      29.358 -10.419 -29.077  1.00 26.09           O  
HETATM 7641  O   HOH A 571      10.255  33.761 -17.287  1.00 42.75           O  
HETATM 7642  O   HOH A 572      33.842  10.614 -10.512  1.00 16.59           O  
HETATM 7643  O   HOH A 573      45.421  23.047 -13.013  1.00 51.69           O  
HETATM 7644  O   HOH A 574      24.027   9.491  -9.179  1.00 29.05           O  
HETATM 7645  O   HOH A 575      21.241   9.356  -9.242  1.00 27.17           O  
HETATM 7646  O   HOH A 576       8.822   1.002 -19.745  1.00 68.74           O  
HETATM 7647  O   HOH A 577      10.662  -0.800 -20.219  1.00 49.02           O  
HETATM 7648  O   HOH A 578      16.719  -8.563  -7.754  1.00 59.58           O  
HETATM 7649  O   HOH A 579      32.137   3.393  -2.919  1.00 28.46           O  
HETATM 7650  O   HOH A 580      29.361   1.426  -4.836  1.00 44.88           O  
HETATM 7651  O   HOH A 581      40.327  -0.958  -8.621  1.00 26.82           O  
HETATM 7652  O   HOH A 582      45.873  -4.386  -7.155  1.00 33.45           O  
HETATM 7653  O   HOH A 583      43.418 -16.484  -7.477  1.00 38.27           O  
HETATM 7654  O   HOH A 584      44.805 -18.288  -6.277  1.00 43.08           O  
HETATM 7655  O   HOH A 585      22.701  -6.645  -2.832  1.00 42.76           O  
HETATM 7656  O   HOH A 586      21.994  -0.562  -2.416  1.00 32.66           O  
HETATM 7657  O   HOH A 587       5.037  10.721  -8.563  1.00 38.29           O  
HETATM 7658  O   HOH A 588       7.361   3.976 -21.162  1.00 54.05           O  
HETATM 7659  O   HOH A 589      29.786   0.659 -24.445  1.00 25.79           O  
HETATM 7660  O   HOH A 590      34.636  -0.696 -41.940  1.00 29.81           O  
HETATM 7661  O   HOH A 591      23.299  -9.177 -22.044  1.00 34.34           O  
HETATM 7662  O   HOH A 592      20.463  -7.650 -22.355  1.00 47.91           O  
HETATM 7663  O   HOH A 593      21.284 -12.197 -15.909  1.00 62.01           O  
HETATM 7664  O   HOH A 594      35.318 -13.558 -19.278  1.00 35.15           O  
HETATM 7665  O   HOH A 595      40.279 -16.458 -13.999  1.00 49.67           O  
HETATM 7666  O   HOH A 596      49.257  11.039 -23.068  1.00 30.52           O  
HETATM 7667  O   HOH A 597      47.882  10.303 -27.790  1.00 50.11           O  
HETATM 7668  O   HOH A 598      55.286  -2.916 -14.102  1.00 38.34           O  
HETATM 7669  O   HOH A 599      49.293  -7.660 -24.330  1.00 56.44           O  
HETATM 7670  O   HOH A 600      46.762 -13.498 -13.816  1.00 54.23           O  
HETATM 7671  O   HOH A 601      40.622 -18.503 -30.435  1.00 43.94           O  
HETATM 7672  O   HOH A 602      40.673   7.250 -22.852  1.00 34.71           O  
HETATM 7673  O   HOH A 603      43.994  13.240 -17.296  1.00 27.02           O  
HETATM 7674  O   HOH A 604      43.110  14.666 -14.920  1.00 27.62           O  
HETATM 7675  O   HOH A 605      39.896  14.327 -14.465  1.00 31.54           O  
HETATM 7676  O   HOH A 606      35.844   7.288 -22.565  1.00 43.98           O  
HETATM 7677  O   HOH A 607      42.166   5.942 -25.703  1.00 35.94           O  
HETATM 7678  O   HOH A 608      32.892   4.770 -23.889  1.00 33.12           O  
HETATM 7679  O   HOH A 609      28.954  16.527 -19.924  1.00 31.93           O  
HETATM 7680  O   HOH A 610      29.464  17.147  -6.738  1.00 41.20           O  
HETATM 7681  O   HOH A 611      28.205  14.867  -5.737  1.00 48.18           O  
HETATM 7682  O   HOH A 612      32.330  23.907  -9.161  1.00 41.55           O  
HETATM 7683  O   HOH A 613      42.830  21.627 -14.797  1.00 38.40           O  
HETATM 7684  O   HOH A 614      43.520  -3.109  -7.244  1.00 41.15           O  
HETATM 7685  O   HOH A 615      42.060  -0.486  -5.283  1.00 53.05           O  
HETATM 7686  O   HOH A 616      45.000  17.510 -19.332  1.00 29.71           O  
HETATM 7687  O   HOH A 617      49.125   1.426  -2.713  1.00 32.91           O  
HETATM 7688  O   HOH A 618      61.735  29.439 -10.585  1.00 45.38           O  
HETATM 7689  O   HOH A 619      60.804  22.307  -6.156  1.00 58.08           O  
HETATM 7690  O   HOH A 620      66.171  18.933 -11.308  1.00 40.67           O  
HETATM 7691  O   HOH A 621       7.419  12.283 -26.279  1.00 29.29           O  
HETATM 7692  O   HOH A 622       3.371  30.820 -17.594  1.00 33.03           O  
HETATM 7693  O   HOH A 623      39.590   0.702  -6.084  1.00 45.24           O  
HETATM 7694  O   HOH A 624      72.405  23.774 -12.829  1.00 57.73           O  
HETATM 7695  O   HOH A 625       5.539  29.725 -20.689  1.00 36.11           O  
HETATM 7696  O   HOH A 626      38.220  -6.495  -3.428  1.00 27.28           O  
HETATM 7697  O   HOH A 627      22.635   2.400  -1.842  1.00 47.50           O  
HETATM 7698  O   HOH A 628      21.981  -3.552  -0.968  1.00 49.56           O  
HETATM 7699  O   HOH A 629      41.254 -17.350  -9.834  1.00 56.37           O  
HETATM 7700  O   HOH A 630      57.108 -14.296  -0.388  1.00 59.11           O  
HETATM 7701  O   HOH A 631      21.932 -13.642 -11.985  1.00 45.49           O  
HETATM 7702  O   HOH A 632      19.802 -11.558 -11.512  1.00 46.84           O  
HETATM 7703  O   HOH A 633       4.595  20.764 -32.254  1.00 50.06           O  
HETATM 7704  O   HOH A 634       6.734  15.757 -29.431  1.00 64.24           O  
HETATM 7705  O   HOH A 635      23.110 -10.169 -24.572  1.00 63.27           O  
HETATM 7706  O   HOH A 636      37.952  10.006 -19.515  1.00 67.39           O  
HETATM 7707  O   HOH A 637      32.434   9.007 -21.488  1.00 44.04           O  
HETATM 7708  O   HOH A 638      42.287 -18.243 -27.296  1.00 61.65           O  
HETATM 7709  O   HOH A 639      49.308   8.620 -35.013  1.00 58.57           O  
HETATM 7710  O   HOH A 640      43.654  15.443 -20.798  1.00 50.92           O  
HETATM 7711  O   HOH A 641      41.048  12.520 -17.882  1.00 44.33           O  
HETATM 7712  O   HOH A 642      46.359  11.402 -15.994  1.00 23.84           O  
HETATM 7713  O   HOH A 643      53.929  -0.622 -22.114  1.00 51.53           O  
HETATM 7714  O   HOH A 644      54.513  -6.824 -18.248  1.00 39.07           O  
HETATM 7715  O   HOH A 645      34.251  -8.848 -47.016  1.00 49.25           O  
HETATM 7716  O   HOH A 646      34.628 -15.471 -40.913  1.00 49.57           O  
HETATM 7717  O   HOH A 647      38.688 -12.845 -43.207  1.00 63.97           O  
HETATM 7718  O   HOH A 648      43.235  -0.724 -44.000  1.00 52.94           O  
HETATM 7719  O   HOH A 649      48.515  -6.774 -33.229  1.00 50.77           O  
HETATM 7720  O   HOH A 650      27.514 -15.018 -26.074  1.00 53.78           O  
HETATM 7721  O   HOH A 651      31.229  12.603 -26.336  1.00 68.10           O  
HETATM 7722  O   HOH A 652      19.317  31.651 -30.767  1.00 52.31           O  
HETATM 7723  O   HOH A 653      41.641  23.032 -18.287  1.00 73.69           O  
HETATM 7724  O   HOH A 654      57.379  12.323   5.822  1.00 64.09           O  
HETATM 7725  O   HOH A 655      58.374   8.572   6.228  1.00 38.84           O  
HETATM 7726  O   HOH A 656      -0.891  18.722 -15.922  1.00 55.30           O  
HETATM 7727  O   HOH A 657      40.356  -4.421  -2.176  1.00 58.53           O  
HETATM 7728  O   HOH A 658       8.547  26.873 -29.556  1.00 23.86           O  
HETATM 7729  O   HOH A 659      16.300  10.993 -25.532  1.00 33.47           O  
HETATM 7730  O   HOH A 660      34.298  10.653 -18.564  1.00 52.31           O  
HETATM 7731  O   HOH A 661      20.667  10.373 -29.523  1.00 46.19           O  
HETATM 7732  O   HOH A 662      28.491  19.441  -5.609  1.00 66.51           O  
HETATM 7733  O   HOH A 663      10.924  33.150 -27.883  1.00 42.25           O  
HETATM 7734  O   HOH A 664       0.623  20.781 -16.830  1.00 45.53           O  
HETATM 7735  O   HOH A 665      24.652   7.029 -29.456  1.00 42.61           O  
HETATM 7736  O   HOH A 666      22.919   9.102 -28.739  1.00 37.58           O  
HETATM 7737  O   HOH A 667      23.597  13.407 -30.677  1.00 47.46           O  
HETATM 7738  O   HOH A 668      17.334  -4.416 -26.869  1.00 80.31           O  
HETATM 7739  O   HOH A 669      51.021  -3.042 -26.080  1.00 51.88           O  
HETATM 7740  O   HOH A 670      53.048  -4.323 -22.821  1.00 65.95           O  
HETATM 7741  O   HOH A 671      49.120 -11.695 -21.521  1.00 56.07           O  
HETATM 7742  O   HOH A 672      18.295  29.967 -21.476  1.00 38.89           O  
HETATM 7743  O   HOH A 673      13.120  34.988 -25.499  1.00 47.92           O  
HETATM 7744  O   HOH A 674      10.853  29.100 -29.769  1.00 47.83           O  
HETATM 7745  O   HOH A 675      12.581  31.152 -29.018  1.00 48.84           O  
HETATM 7746  O   HOH A 676      14.632  32.596 -27.411  1.00 39.00           O  
HETATM 7747  O   HOH A 677      25.050 -11.305 -25.750  1.00 82.86           O  
HETATM 7748  O   HOH A 678      49.673 -12.410 -11.701  1.00 55.64           O  
HETATM 7749  O   HOH A 679      14.501  15.408 -33.921  1.00 52.37           O  
HETATM 7750  O   HOH A 680      16.115  16.754 -31.303  1.00 32.54           O  
HETATM 7751  O   HOH A 681      31.182  26.596 -16.657  1.00 36.05           O  
HETATM 7752  O   HOH A 682      50.218  28.315  -0.987  1.00 61.05           O  
HETATM 7753  O   HOH A 683      34.600   7.816 -14.736  1.00 40.88           O  
HETATM 7754  O   HOH A 684      18.879  13.440  -5.457  1.00 55.79           O  
HETATM 7755  O   HOH A 685       4.643  27.776  -2.122  1.00 66.41           O  
HETATM 7756  O   HOH A 686      16.613  -7.430 -15.725  1.00 49.01           O  
HETATM 7757  O   HOH A 687      18.851  -1.008 -26.579  1.00 52.79           O  
HETATM 7758  O   HOH A 688      18.606 -10.692  -7.573  1.00 47.21           O  
HETATM 7759  O   HOH A 689       3.990  28.217 -19.338  1.00 33.97           O  
HETATM 7760  O   HOH A 690      23.883  -2.481 -28.225  1.00 52.53           O  
HETATM 7761  O   HOH A 691      18.002  17.849 -33.852  1.00 74.48           O  
HETATM 7762  O   HOH A 692      57.736  15.705   4.066  1.00 46.62           O  
HETATM 7763  O   HOH A 693      21.052  16.404  -2.412  1.00 68.38           O  
HETATM 7764  O   HOH A 694      22.932  21.365  -2.946  1.00 58.35           O  
HETATM 7765  O   HOH A 695       7.157  29.914  -1.589  1.00 57.83           O  
HETATM 7766  O   HOH A 696      18.392  -9.820 -19.629  1.00 71.84           O  
HETATM 7767  O   HOH A 697      36.616   7.453 -25.436  1.00 71.26           O  
HETATM 7768  O   HOH A 698      53.275  11.524 -24.904  1.00 59.23           O  
HETATM 7769  O   HOH A 699      50.722 -10.252 -24.258  1.00 66.79           O  
HETATM 7770  O   HOH A 700      44.513  -0.831 -39.100  1.00 47.35           O  
HETATM 7771  O   HOH A 701      35.231 -11.243 -40.038  1.00 40.54           O  
HETATM 7772  O   HOH A 702      18.304  21.326 -33.426  1.00 64.80           O  
HETATM 7773  O   HOH A 703      26.768  14.240  -3.356  1.00 66.72           O  
HETATM 7774  O   HOH A 704      68.769  18.905  -9.249  1.00 79.83           O  
HETATM 7775  O   HOH A 705      60.605   3.589   7.874  1.00 42.19           O  
HETATM 7776  O   HOH A 706      32.366  -1.098  -3.621  1.00 57.14           O  
HETATM 7777  O   HOH A 707      27.439  12.956 -31.625  1.00 59.62           O  
HETATM 7778  O   HOH A 708      15.407  -8.450  -5.065  1.00 69.73           O  
HETATM 7779  O   HOH A 709      40.806  27.764 -16.731  1.00 60.25           O  
HETATM 7780  O   HOH A 710      37.589  11.905 -16.848  1.00 67.00           O  
HETATM 7781  O   HOH A 711      37.620  15.692 -15.833  1.00 48.29           O  
HETATM 7782  O   HOH A 712      75.755  23.308 -13.326  1.00 59.14           O  
HETATM 7783  O   HOH A 713      21.937 -15.869  -6.340  1.00 73.01           O  
HETATM 7784  O   HOH A 714      51.661  12.718 -19.684  1.00 28.78           O  
HETATM 7785  O   HOH A 715      16.720  32.140 -16.947  1.00 64.17           O  
HETATM 7786  O   HOH A 716       2.011  21.006  -4.988  1.00 70.76           O  
HETATM 7787  O   HOH A 717      44.423 -17.209  -9.900  1.00 80.74           O  
HETATM 7788  O   HOH A 718      30.156 -18.348 -13.640  1.00 53.78           O  
HETATM 7789  O   HOH A 719       8.693  19.915  -1.365  1.00 60.92           O  
HETATM 7790  O   HOH A 720       2.665  26.293 -21.351  1.00 47.02           O  
HETATM 7791  O   HOH A 721      24.125   0.202 -39.080  1.00 67.07           O  
HETATM 7792  O   HOH A 722      24.191  -3.707 -30.869  1.00 63.58           O  
HETATM 7793  O   HOH A 723      21.599   0.485 -36.110  1.00 74.97           O  
HETATM 7794  O   HOH A 724      20.382   0.657 -28.466  1.00 58.85           O  
HETATM 7795  O   HOH A 725      18.982 -11.272 -23.741  1.00 68.13           O  
HETATM 7796  O   HOH A 726      21.069 -15.807 -23.747  1.00 72.94           O  
HETATM 7797  O   HOH A 727      27.561 -14.896 -22.522  1.00 49.09           O  
HETATM 7798  O   HOH A 728      38.700   4.176 -27.976  1.00 33.63           O  
HETATM 7799  O   HOH A 729      46.968   7.885 -32.763  1.00 61.67           O  
HETATM 7800  O   HOH A 730      22.293 -18.814 -21.274  1.00 68.69           O  
HETATM 7801  O   HOH A 731      49.102  11.510 -33.588  1.00 49.52           O  
HETATM 7802  O   HOH A 732      55.068  11.223 -20.493  1.00 33.26           O  
HETATM 7803  O   HOH A 733      55.027  13.545 -23.316  1.00 57.22           O  
HETATM 7804  O   HOH A 734      54.263  -9.478 -18.691  1.00 51.67           O  
HETATM 7805  O   HOH A 735      38.342  -4.888 -47.854  1.00 46.25           O  
HETATM 7806  O   HOH A 736      43.993 -13.715 -44.718  1.00 84.26           O  
HETATM 7807  O   HOH A 737      30.227  25.854 -22.452  1.00 61.61           O  
HETATM 7808  O   HOH A 738      16.476  37.311  -8.004  1.00 63.66           O  
HETATM 7809  O   HOH A 739      50.562  32.387  -6.786  1.00 72.08           O  
HETATM 7810  O   HOH A 740      18.407 -12.474 -14.265  1.00 84.70           O  
HETATM 7811  O   HOH A 741      12.953   7.246 -34.533  1.00 69.47           O  
HETATM 7812  O   HOH A 742      52.719 -12.048 -14.429  1.00 52.33           O  
HETATM 7813  O   HOH A 743      54.015   0.113 -25.240  1.00 58.36           O  
HETATM 7814  O   HOH A 744      34.927  33.333 -17.568  1.00 46.40           O  
HETATM 7815  O   HOH A 745      45.276  -2.285  -0.884  1.00 51.81           O  
HETATM 7816  O   HOH A 746      34.956   7.512 -32.620  1.00 72.36           O  
HETATM 7817  O   HOH A 747      54.409  -6.316 -21.099  1.00 53.84           O  
HETATM 7818  O   HOH A 748      31.267  21.569 -24.655  1.00 56.49           O  
HETATM 7819  O   HOH A 749       6.775   7.472  -8.030  1.00 52.60           O  
HETATM 7820  O   HOH A 750       2.440  25.985 -26.549  1.00 47.98           O  
HETATM 7821  O   HOH B 493      37.494  -7.041   1.405  1.00 30.40           O  
HETATM 7822  O   HOH B 494      25.839 -10.950  -1.011  1.00 54.62           O  
HETATM 7823  O   HOH B 495      45.206  11.725   0.358  1.00 16.47           O  
HETATM 7824  O   HOH B 496      36.524  20.604  -7.590  1.00 14.58           O  
HETATM 7825  O   HOH B 497      52.536  10.783  10.949  1.00 16.47           O  
HETATM 7826  O   HOH B 498      50.054   2.999  13.387  1.00 22.78           O  
HETATM 7827  O   HOH B 499      51.947  -2.134  16.437  1.00 18.55           O  
HETATM 7828  O   HOH B 500      67.290   7.924  15.618  1.00 30.51           O  
HETATM 7829  O   HOH B 501      60.981  -7.780  13.383  1.00 20.79           O  
HETATM 7830  O   HOH B 502      61.060  -1.153  21.324  1.00 26.63           O  
HETATM 7831  O   HOH B 503      64.994   2.605  21.072  1.00 32.16           O  
HETATM 7832  O   HOH B 504      61.563   4.426  19.645  1.00 21.64           O  
HETATM 7833  O   HOH B 505      64.858   9.747  19.796  1.00 23.77           O  
HETATM 7834  O   HOH B 506      45.309  -7.087   2.671  1.00 33.27           O  
HETATM 7835  O   HOH B 507      41.345  -9.948  10.247  1.00 19.48           O  
HETATM 7836  O   HOH B 508      44.141  -1.878   8.502  1.00 17.84           O  
HETATM 7837  O   HOH B 509      35.995  -7.223  10.965  1.00 24.33           O  
HETATM 7838  O   HOH B 510      56.273  -0.869  22.259  1.00 18.11           O  
HETATM 7839  O   HOH B 511      53.513 -14.325  27.896  1.00 24.15           O  
HETATM 7840  O   HOH B 512      49.857  -5.466  42.057  1.00 50.51           O  
HETATM 7841  O   HOH B 513      47.229 -15.469  17.854  1.00 28.87           O  
HETATM 7842  O   HOH B 514      57.786   4.697  19.574  1.00 18.99           O  
HETATM 7843  O   HOH B 515      50.252  15.810   8.381  1.00 22.77           O  
HETATM 7844  O   HOH B 516      61.413  21.167  15.754  1.00 27.34           O  
HETATM 7845  O   HOH B 517      49.432  18.479   7.974  1.00 27.78           O  
HETATM 7846  O   HOH B 518      43.169  12.005  17.507  1.00 30.70           O  
HETATM 7847  O   HOH B 519      40.711  11.168  16.185  1.00 13.08           O  
HETATM 7848  O   HOH B 520      45.119  -4.584  13.519  1.00 19.63           O  
HETATM 7849  O   HOH B 521      42.790  -4.061  14.952  1.00 18.01           O  
HETATM 7850  O   HOH B 522      34.751   0.734   9.181  1.00 23.73           O  
HETATM 7851  O   HOH B 523      37.534  11.437  23.216  1.00 41.65           O  
HETATM 7852  O   HOH B 524      31.965  18.628   3.088  1.00 18.50           O  
HETATM 7853  O   HOH B 525      29.487  -1.958  14.273  1.00 22.26           O  
HETATM 7854  O   HOH B 526      37.451  -5.359   4.854  1.00 38.27           O  
HETATM 7855  O   HOH B 527      39.560 -13.423  19.637  1.00 30.87           O  
HETATM 7856  O   HOH B 528      42.168  -0.121   4.914  1.00 27.29           O  
HETATM 7857  O   HOH B 529      62.088   5.061   9.500  1.00 41.56           O  
HETATM 7858  O   HOH B 530      32.006 -16.220   3.657  1.00 30.58           O  
HETATM 7859  O   HOH B 531      58.418  -3.076  19.371  1.00 23.27           O  
HETATM 7860  O   HOH B 532      44.457   4.481  25.297  1.00 37.99           O  
HETATM 7861  O   HOH B 533      45.749  -0.356  30.770  1.00 39.40           O  
HETATM 7862  O   HOH B 534      33.104  28.072   5.315  1.00 33.06           O  
HETATM 7863  O   HOH B 535      30.780  18.509  -4.013  1.00 42.72           O  
HETATM 7864  O   HOH B 536      25.642   7.486  -7.831  1.00 29.86           O  
HETATM 7865  O   HOH B 537      41.380  -9.259  13.065  1.00 23.49           O  
HETATM 7866  O   HOH B 538      54.631  -0.521  24.378  1.00 24.99           O  
HETATM 7867  O   HOH B 539      55.119  -3.216  24.159  1.00 28.44           O  
HETATM 7868  O   HOH B 540      54.350  -1.952  27.750  1.00 22.69           O  
HETATM 7869  O   HOH B 541      47.709   5.277  20.815  1.00 34.77           O  
HETATM 7870  O   HOH B 542      36.815   0.570  24.449  1.00 32.30           O  
HETATM 7871  O   HOH B 543      55.845 -23.958  33.343  1.00 42.29           O  
HETATM 7872  O   HOH B 544      51.876   8.253  18.799  1.00 49.43           O  
HETATM 7873  O   HOH B 545      55.170   5.403  19.752  1.00 35.53           O  
HETATM 7874  O   HOH B 546      43.080  17.107  19.905  1.00 37.67           O  
HETATM 7875  O   HOH B 547      48.011   2.108   3.473  1.00 24.17           O  
HETATM 7876  O   HOH B 548      42.353  23.999   8.194  1.00 24.06           O  
HETATM 7877  O   HOH B 549      44.149  -4.815   1.768  1.00 70.79           O  
HETATM 7878  O   HOH B 550      50.418   7.186  11.817  1.00 28.43           O  
HETATM 7879  O   HOH B 551      51.433   5.256  14.608  1.00 49.12           O  
HETATM 7880  O   HOH B 552      37.884   2.509   0.280  1.00 33.29           O  
HETATM 7881  O   HOH B 553      36.095   2.710   3.120  1.00 38.16           O  
HETATM 7882  O   HOH B 554      35.382  -0.453   6.390  1.00 47.47           O  
HETATM 7883  O   HOH B 555      47.648   1.373   0.113  1.00 38.30           O  
HETATM 7884  O   HOH B 556      64.770   4.697   8.885  1.00 56.35           O  
HETATM 7885  O   HOH B 557      63.122   0.678  20.186  1.00 54.35           O  
HETATM 7886  O   HOH B 558      36.928  -5.670  13.020  1.00 34.54           O  
HETATM 7887  O   HOH B 559      39.789  -7.037  14.130  1.00 51.58           O  
HETATM 7888  O   HOH B 560      66.439 -12.587   9.232  1.00 51.01           O  
HETATM 7889  O   HOH B 561      62.710  -4.865   1.859  1.00 48.16           O  
HETATM 7890  O   HOH B 562      39.795 -16.716  26.579  1.00 43.74           O  
HETATM 7891  O   HOH B 563      46.878   2.308  27.935  1.00 43.39           O  
HETATM 7892  O   HOH B 564      50.456   1.904  22.279  1.00 37.52           O  
HETATM 7893  O   HOH B 565      45.534   5.974  22.960  1.00 27.08           O  
HETATM 7894  O   HOH B 566      52.650   1.715  23.865  1.00 26.29           O  
HETATM 7895  O   HOH B 567      39.252   7.062  29.347  1.00 42.58           O  
HETATM 7896  O   HOH B 568      40.628  11.394  24.747  1.00 57.39           O  
HETATM 7897  O   HOH B 569      49.274   7.907  20.431  1.00 75.68           O  
HETATM 7898  O   HOH B 570      44.955  13.820  15.343  1.00 39.97           O  
HETATM 7899  O   HOH B 571      40.939  -0.041  36.596  1.00 47.66           O  
HETATM 7900  O   HOH B 572      49.428  -2.568  35.281  1.00 67.70           O  
HETATM 7901  O   HOH B 573      45.442 -24.330  30.037  1.00 63.92           O  
HETATM 7902  O   HOH B 574      44.671  25.421   9.921  1.00 45.73           O  
HETATM 7903  O   HOH B 575      44.223  22.385  13.830  1.00 37.40           O  
HETATM 7904  O   HOH B 576      46.987  16.565  14.576  1.00 32.94           O  
HETATM 7905  O   HOH B 577      47.450  12.684  14.925  1.00 45.01           O  
HETATM 7906  O   HOH B 578      31.449  25.652  10.468  1.00 34.03           O  
HETATM 7907  O   HOH B 579      40.953  29.174   2.432  1.00 41.15           O  
HETATM 7908  O   HOH B 580      34.734  28.373  -1.641  1.00 48.47           O  
HETATM 7909  O   HOH B 581      32.016   3.607  -0.024  1.00 59.64           O  
HETATM 7910  O   HOH B 582      45.277   1.970   4.583  1.00 28.37           O  
HETATM 7911  O   HOH B 583      25.768  27.010  11.001  1.00 49.34           O  
HETATM 7912  O   HOH B 584      26.236  10.270  -6.258  1.00 32.00           O  
HETATM 7913  O   HOH B 585      28.373  12.068  -6.321  1.00 40.82           O  
HETATM 7914  O   HOH B 586      26.562   6.559  -0.420  1.00 79.80           O  
HETATM 7915  O   HOH B 587      52.588  20.057  10.697  1.00 30.06           O  
HETATM 7916  O   HOH B 588      75.225  -6.447  18.412  1.00 52.12           O  
HETATM 7917  O   HOH B 589      44.986  -0.398   5.909  1.00 45.32           O  
HETATM 7918  O   HOH B 590      23.740  -1.844   8.130  1.00 48.20           O  
HETATM 7919  O   HOH B 591      50.166   4.784  22.720  1.00 51.63           O  
HETATM 7920  O   HOH B 592      58.641  14.668  18.712  1.00 35.36           O  
HETATM 7921  O   HOH B 593      40.908 -17.081  28.925  1.00 39.86           O  
HETATM 7922  O   HOH B 594      36.929 -14.674  15.950  1.00 55.02           O  
HETATM 7923  O   HOH B 595      59.562 -14.093  21.493  1.00 52.19           O  
HETATM 7924  O   HOH B 596      59.427  -3.832  35.301  1.00 56.12           O  
HETATM 7925  O   HOH B 597      63.290  -3.804  29.019  1.00 52.50           O  
HETATM 7926  O   HOH B 598      60.125  -6.940  27.839  1.00 65.37           O  
HETATM 7927  O   HOH B 599      54.031   6.490  25.150  1.00 46.01           O  
HETATM 7928  O   HOH B 600      64.117  20.244  15.167  1.00 36.20           O  
HETATM 7929  O   HOH B 601      52.683  18.609  19.953  1.00 60.82           O  
HETATM 7930  O   HOH B 602      44.536   0.219   2.329  1.00 45.69           O  
HETATM 7931  O   HOH B 603      23.098  22.609  11.807  1.00 44.48           O  
HETATM 7932  O   HOH B 604      39.305 -20.730   8.967  1.00 59.82           O  
HETATM 7933  O   HOH B 605      79.983  -0.335   9.136  1.00 82.65           O  
HETATM 7934  O   HOH B 606      52.246   7.053  21.228  1.00 64.68           O  
HETATM 7935  O   HOH B 607      58.131 -17.392  31.523  1.00 59.02           O  
HETATM 7936  O   HOH B 608      51.617  26.126   7.456  1.00 84.94           O  
HETATM 7937  O   HOH B 609      61.213  -8.427   0.572  1.00 48.75           O  
HETATM 7938  O   HOH B 610      85.585  25.489  16.638  1.00 79.38           O  
HETATM 7939  O   HOH B 611      65.737  22.235  14.576  1.00 41.13           O  
HETATM 7940  O   HOH B 612      28.853   3.821  -0.251  1.00 47.02           O  
HETATM 7941  O   HOH B 613      22.029  17.119   6.556  1.00 50.97           O  
HETATM 7942  O   HOH B 614      24.703 -13.625  -1.823  1.00 80.64           O  
HETATM 7943  O   HOH B 615      27.183 -14.160   3.967  1.00 78.80           O  
HETATM 7944  O   HOH B 616      22.476  24.729   9.227  1.00 46.76           O  
HETATM 7945  O   HOH B 617      38.244  -3.871   7.337  1.00 41.83           O  
HETATM 7946  O   HOH B 618      59.784   0.171   3.252  1.00 49.80           O  
HETATM 7947  O   HOH B 619      37.320 -18.900  18.291  1.00 64.47           O  
HETATM 7948  O   HOH B 620      27.810   7.906  14.638  1.00 75.82           O  
HETATM 7949  O   HOH B 621      28.444  12.123  -2.119  1.00 63.18           O  
HETATM 7950  O   HOH B 622      84.916  19.133   8.110  1.00 58.20           O  
HETATM 7951  O   HOH B 623      60.143   2.278  31.791  1.00 49.34           O  
HETATM 7952  O   HOH B 624      62.711 -14.809  13.711  1.00 73.11           O  
HETATM 7953  O   HOH B 625      38.702 -19.697  24.575  1.00 73.36           O  
HETATM 7954  O   HOH B 626      48.969  -7.186  44.909  1.00 68.01           O  
HETATM 7955  O   HOH B 627      53.298   4.583  22.675  1.00 52.79           O  
HETATM 7956  O   HOH B 628      61.121  17.613  26.330  1.00 61.01           O  
HETATM 7957  O   HOH B 629      47.899  20.730  19.851  1.00 61.86           O  
HETATM 7958  O   HOH B 630      26.752  15.202   7.709  1.00 61.87           O  
HETATM 7959  O   HOH B 631      31.506  31.757   8.371  1.00 65.32           O  
HETATM 7960  O   HOH B 632      58.653  21.151   6.910  1.00 46.38           O  
HETATM 7961  O   HOH B 633      63.410   4.409  32.173  1.00 75.57           O  
HETATM 7962  O   HOH B 634      60.876 -13.553  26.043  1.00 67.77           O  
HETATM 7963  O   HOH B 635      53.028  10.448  20.539  1.00 47.69           O  
HETATM 7964  O   HOH B 636      42.597 -18.509  36.705  1.00 54.27           O  
HETATM 7965  O   HOH B 637      50.122  17.094  15.698  1.00 40.80           O  
HETATM 7966  O   HOH B 638      26.708  16.655  10.174  1.00 36.12           O  
HETATM 7967  O   HOH B 639      64.561  -6.447  27.182  1.00 70.27           O  
HETATM 7968  O   HOH B 640      63.805 -10.034  25.608  1.00 61.29           O  
HETATM 7969  O   HOH B 641      38.201  10.535  27.693  1.00 65.48           O  
HETATM 7970  O   HOH B 642      36.495  12.267  26.542  1.00 75.81           O  
HETATM 7971  O   HOH B 643      44.642  14.566  22.016  1.00 68.99           O  
HETATM 7972  O   HOH B 644      28.698  10.241  18.521  1.00 54.48           O  
HETATM 7973  O   HOH B 645      32.430  20.463  27.001  1.00 82.02           O  
HETATM 7974  O   HOH B 646      17.010  18.203  17.576  1.00 79.60           O  
HETATM 7975  O   HOH B 647      63.179   2.858   5.443  1.00 55.64           O  
HETATM 7976  O   HOH B 648      65.145   8.909   5.473  1.00 68.11           O  
HETATM 7977  O   HOH B 649      38.116 -17.253  11.458  1.00 66.25           O  
HETATM 7978  O   HOH B 650      35.799 -16.924  16.756  1.00 97.02           O  
HETATM 7979  O   HOH B 651      77.314   2.067  28.378  1.00 46.19           O  
HETATM 7980  O   HOH B 652      61.331  -7.620  37.502  1.00 81.60           O  
HETATM 7981  O   HOH B 653      47.649 -24.090  19.890  1.00 49.40           O  
HETATM 7982  O   HOH B 654      27.930 -14.385   1.358  1.00 57.19           O  
HETATM 7983  O   HOH B 655      88.350   8.184  15.973  1.00 58.12           O  
HETATM 7984  O   HOH B 656      34.769  -4.875  31.396  1.00 58.32           O  
HETATM 7985  O   HOH B 657      40.979  -4.849  37.177  1.00 47.53           O  
HETATM 7986  O   HOH B 658      29.696 -17.386  -3.403  1.00 48.88           O  
HETATM 7987  O   HOH B 659      52.904   0.998   2.996  1.00 62.81           O  
HETATM 7988  O   HOH B 660      47.208   9.350  21.733  1.00 57.44           O  
HETATM 7989  O   HOH B 661      29.007   5.552  18.554  1.00 52.93           O  
HETATM 7990  O   HOH B 662      34.392  27.749  25.322  1.00 52.81           O  
CONECT  370  402                                                                
CONECT  402  370                                                                
CONECT 4087 4119                                                                
CONECT 4119 4087                                                                
CONECT 7450 7451 7452 7453 7502                                                 
CONECT 7451 7450                                                                
CONECT 7452 7450                                                                
CONECT 7453 7450 7454                                                           
CONECT 7454 7453 7455                                                           
CONECT 7455 7454 7456 7457                                                      
CONECT 7456 7455 7461                                                           
CONECT 7457 7455 7458 7459                                                      
CONECT 7458 7457                                                                
CONECT 7459 7457 7460 7461                                                      
CONECT 7460 7459                                                                
CONECT 7461 7456 7459 7462                                                      
CONECT 7462 7461 7463 7471                                                      
CONECT 7463 7462 7464                                                           
CONECT 7464 7463 7465                                                           
CONECT 7465 7464 7466 7471                                                      
CONECT 7466 7465 7467 7468                                                      
CONECT 7467 7466                                                                
CONECT 7468 7466 7469                                                           
CONECT 7469 7468 7470                                                           
CONECT 7470 7469 7471                                                           
CONECT 7471 7462 7465 7470                                                      
CONECT 7472 7473 7489                                                           
CONECT 7473 7472 7474 7475                                                      
CONECT 7474 7473                                                                
CONECT 7475 7473 7476                                                           
CONECT 7476 7475 7477 7478                                                      
CONECT 7477 7476                                                                
CONECT 7478 7476 7479 7489                                                      
CONECT 7479 7478 7480                                                           
CONECT 7480 7479 7481 7487                                                      
CONECT 7481 7480 7482                                                           
CONECT 7482 7481 7483 7484                                                      
CONECT 7483 7482                                                                
CONECT 7484 7482 7485 7486                                                      
CONECT 7485 7484                                                                
CONECT 7486 7484 7487                                                           
CONECT 7487 7480 7486 7488                                                      
CONECT 7488 7487 7489 7490                                                      
CONECT 7489 7472 7478 7488                                                      
CONECT 7490 7488 7491                                                           
CONECT 7491 7490 7492 7493                                                      
CONECT 7492 7491                                                                
CONECT 7493 7491 7494 7495                                                      
CONECT 7494 7493                                                                
CONECT 7495 7493 7496 7497                                                      
CONECT 7496 7495                                                                
CONECT 7497 7495 7498                                                           
CONECT 7498 7497 7499                                                           
CONECT 7499 7498 7500 7501 7502                                                 
CONECT 7500 7499                                                                
CONECT 7501 7499                                                                
CONECT 7502 7450 7499                                                           
CONECT 7503 7504 7505 7506                                                      
CONECT 7504 7503                                                                
CONECT 7505 7503                                                                
CONECT 7506 7503 7507                                                           
CONECT 7507 7506 7508                                                           
CONECT 7508 7507 7509 7510                                                      
CONECT 7509 7508                                                                
CONECT 7510 7508                                                                
CONECT 7511 7512 7513 7514                                                      
CONECT 7512 7511                                                                
CONECT 7513 7511                                                                
CONECT 7514 7511 7515                                                           
CONECT 7515 7514 7516                                                           
CONECT 7516 7515 7517 7518                                                      
CONECT 7517 7516                                                                
CONECT 7518 7516                                                                
CONECT 7519 7520 7521 7522 7571                                                 
CONECT 7520 7519                                                                
CONECT 7521 7519                                                                
CONECT 7522 7519 7523                                                           
CONECT 7523 7522 7524                                                           
CONECT 7524 7523 7525 7526                                                      
CONECT 7525 7524 7530                                                           
CONECT 7526 7524 7527 7528                                                      
CONECT 7527 7526                                                                
CONECT 7528 7526 7529 7530                                                      
CONECT 7529 7528                                                                
CONECT 7530 7525 7528 7531                                                      
CONECT 7531 7530 7532 7540                                                      
CONECT 7532 7531 7533                                                           
CONECT 7533 7532 7534                                                           
CONECT 7534 7533 7535 7540                                                      
CONECT 7535 7534 7536 7537                                                      
CONECT 7536 7535                                                                
CONECT 7537 7535 7538                                                           
CONECT 7538 7537 7539                                                           
CONECT 7539 7538 7540                                                           
CONECT 7540 7531 7534 7539                                                      
CONECT 7541 7542 7558                                                           
CONECT 7542 7541 7543 7544                                                      
CONECT 7543 7542                                                                
CONECT 7544 7542 7545                                                           
CONECT 7545 7544 7546 7547                                                      
CONECT 7546 7545                                                                
CONECT 7547 7545 7548 7558                                                      
CONECT 7548 7547 7549                                                           
CONECT 7549 7548 7550 7556                                                      
CONECT 7550 7549 7551                                                           
CONECT 7551 7550 7552 7553                                                      
CONECT 7552 7551                                                                
CONECT 7553 7551 7554 7555                                                      
CONECT 7554 7553                                                                
CONECT 7555 7553 7556                                                           
CONECT 7556 7549 7555 7557                                                      
CONECT 7557 7556 7558 7559                                                      
CONECT 7558 7541 7547 7557                                                      
CONECT 7559 7557 7560                                                           
CONECT 7560 7559 7561 7562                                                      
CONECT 7561 7560                                                                
CONECT 7562 7560 7563 7564                                                      
CONECT 7563 7562                                                                
CONECT 7564 7562 7565 7566                                                      
CONECT 7565 7564                                                                
CONECT 7566 7564 7567                                                           
CONECT 7567 7566 7568                                                           
CONECT 7568 7567 7569 7570 7571                                                 
CONECT 7569 7568                                                                
CONECT 7570 7568                                                                
CONECT 7571 7519 7568                                                           
MASTER      436    0    4   36   48    0   22    6 7988    2  126   76          
END                                                                             


A second structure was input as follows:


HEADER    OXIDOREDUCTASE                          24-JUN-08   3DK8              
TITLE     CATALYTIC CYCLE OF HUMAN GLUTATHIONE REDUCTASE NEAR 1 A RESOLUTION    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE REDUCTASE;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 45 TO 522;                                    
COMPND   5 SYNONYM: GRASE, GR;                                                  
COMPND   6 EC: 1.8.1.7;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GSR, GLUR, GRD1;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FLAVOENZYME, GLUTATHIONE, NICOTINAMIDE, ALTERNATIVE INITIATION, FAD,  
KEYWDS   2 FLAVOPROTEIN, MITOCHONDRION, NADP, OXIDOREDUCTASE, PHOSPHOPROTEIN,   
KEYWDS   3 REDOX-ACTIVE CENTER, TRANSIT PEPTIDE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.S.BERKHOLZ,H.R.FABER,S.N.SAVVIDES,P.A.KARPLUS                       
REVDAT   6   25-OCT-17 3DK8    1       REMARK                                   
REVDAT   5   25-DEC-13 3DK8    1       AUTHOR                                   
REVDAT   4   13-JUL-11 3DK8    1       VERSN                                    
REVDAT   3   24-FEB-09 3DK8    1       VERSN                                    
REVDAT   2   16-SEP-08 3DK8    1       JRNL                                     
REVDAT   1   05-AUG-08 3DK8    0                                                
JRNL        AUTH   D.S.BERKHOLZ,H.R.FABER,S.N.SAVVIDES,P.A.KARPLUS              
JRNL        TITL   CATALYTIC CYCLE OF HUMAN GLUTATHIONE REDUCTASE NEAR 1 A      
JRNL        TITL 2 RESOLUTION.                                                  
JRNL        REF    J.MOL.BIOL.                   V. 382   371 2008              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   18638483                                                     
JRNL        DOI    10.1016/J.JMB.2008.06.083                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELX                                                
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.1                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.124                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.157                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 4.900                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 7671                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 155146                 
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.120                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.153                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 4.900                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 6891                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 139319                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 3496                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 117                                           
REMARK   3   SOLVENT ATOMS      : 839                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL                    
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL                    
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL                    
REMARK   3   NUMBER OF RESTRAINTS                     : NULL                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.016                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.033                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.029                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.088                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.103                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.035                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.006                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.053                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.099                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3DK8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000048141.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 250008                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 30.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 64.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 3DK9                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3% AMMONIUM SULFATE, 0.1 M POTASSIUM     
REMARK 280  PHOSPHATE AND 0.1% BETA-OCTYL GLUCOSIDE, PH 7.0, VAPOR DIFFUSION,   
REMARK 280  HANGING DROP, TEMPERATURE 298K, PH 7.00                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -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        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       60.01550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.14050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       60.01550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.14050            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14960 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 36490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -129.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       75.65275            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       71.29664            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CE   MET A  79  LIES ON A SPECIAL POSITION.                          
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     ALA A     1                                                      
REMARK 465     CYS A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     GLN A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     PRO A    12                                                      
REMARK 465     PRO A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     GLY A    16                                                      
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  93    CG   CD   CE   NZ                                   
REMARK 470     LYS A 296    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O2   GOL A   604     O    HOH A  1051              0.47            
REMARK 500   O1   GOL A   604     O    HOH A  1035              0.87            
REMARK 500   C2   GOL A   604     O    HOH A  1051              0.98            
REMARK 500   C1   GOL A   604     O    HOH A  1035              2.05            
REMARK 500   C1   GOL A   604     O    HOH A  1051              2.07            
REMARK 500   C3   GOL A   604     O    HOH A  1051              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  22   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG A  37   CD  -  NE  -  CZ  ANGL. DEV. =  23.9 DEGREES          
REMARK 500    ARG A  37   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    HIS A  75   CE1 -  NE2 -  CD2 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    GLU A  77   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    HIS A  82   CA  -  CB  -  CG  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ARG A 103   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 189   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A 218   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 224   CD  -  NE  -  CZ  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ARG A 224   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 224   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    GLU A 239   OE1 -  CD  -  OE2 ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    ARG A 272   CD  -  NE  -  CZ  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ARG A 272   CD  -  NE  -  CZ  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    ARG A 272   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    MET A 276   CA  -  CB  -  CG  ANGL. DEV. =  12.4 DEGREES          
REMARK 500    MET A 406   CG  -  SD  -  CE  ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    CYS A 417   N   -  CA  -  CB  ANGL. DEV. =  19.2 DEGREES          
REMARK 500    CYS A 417   CA  -  CB  -  SG  ANGL. DEV. = -16.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  52     -121.83   -128.07                                   
REMARK 500    VAL A  61       26.81   -142.42                                   
REMARK 500    CYS A  90       52.09    -98.65                                   
REMARK 500    GLU A  91       70.53    -55.39                                   
REMARK 500    GLU A  91       73.18    166.39                                   
REMARK 500    HIS A 219     -147.63   -125.67                                   
REMARK 500    ALA A 336       72.32     56.71                                   
REMARK 500    ASN A 425     -178.72     64.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     GSH A  482                                                       
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     GOL A   602                                                      
REMARK 615     GOL A   604                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 580                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 582                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 605                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3DJG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3DJJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3DK4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3DK9   RELATED DB: PDB                                   
DBREF  3DK8 A   18   478  UNP    P00390   GSHR_HUMAN      45    522             
SEQRES   1 A  478  ALA CYS ARG GLN GLU PRO GLN PRO GLN GLY PRO PRO PRO          
SEQRES   2 A  478  ALA ALA GLY ALA VAL ALA SER TYR ASP TYR LEU VAL ILE          
SEQRES   3 A  478  GLY GLY GLY SER GLY GLY LEU ALA SER ALA ARG ARG ALA          
SEQRES   4 A  478  ALA GLU LEU GLY ALA ARG ALA ALA VAL VAL GLU SER HIS          
SEQRES   5 A  478  LYS LEU GLY GLY THR CYS VAL ASN VAL GLY CYS VAL PRO          
SEQRES   6 A  478  LYS LYS VAL MET TRP ASN THR ALA VAL HIS SER GLU PHE          
SEQRES   7 A  478  MET HIS ASP HIS ALA ASP TYR GLY PHE PRO SER CYS GLU          
SEQRES   8 A  478  GLY LYS PHE ASN TRP ARG VAL ILE LYS GLU LYS ARG ASP          
SEQRES   9 A  478  ALA TYR VAL SER ARG LEU ASN ALA ILE TYR GLN ASN ASN          
SEQRES  10 A  478  LEU THR LYS SER HIS ILE GLU ILE ILE ARG GLY HIS ALA          
SEQRES  11 A  478  ALA PHE THR SER ASP PRO LYS PRO THR ILE GLU VAL SER          
SEQRES  12 A  478  GLY LYS LYS TYR THR ALA PRO HIS ILE LEU ILE ALA THR          
SEQRES  13 A  478  GLY GLY MET PRO SER THR PRO HIS GLU SER GLN ILE PRO          
SEQRES  14 A  478  GLY ALA SER LEU GLY ILE THR SER ASP GLY PHE PHE GLN          
SEQRES  15 A  478  LEU GLU GLU LEU PRO GLY ARG SER VAL ILE VAL GLY ALA          
SEQRES  16 A  478  GLY TYR ILE ALA VAL GLU MET ALA GLY ILE LEU SER ALA          
SEQRES  17 A  478  LEU GLY SER LYS THR SER LEU MET ILE ARG HIS ASP LYS          
SEQRES  18 A  478  VAL LEU ARG SER PHE ASP SER MET ILE SER THR ASN CYS          
SEQRES  19 A  478  THR GLU GLU LEU GLU ASN ALA GLY VAL GLU VAL LEU LYS          
SEQRES  20 A  478  PHE SER GLN VAL LYS GLU VAL LYS LYS THR LEU SER GLY          
SEQRES  21 A  478  LEU GLU VAL SER MET VAL THR ALA VAL PRO GLY ARG LEU          
SEQRES  22 A  478  PRO VAL MET THR MET ILE PRO ASP VAL ASP CYS LEU LEU          
SEQRES  23 A  478  TRP ALA ILE GLY ARG VAL PRO ASN THR LYS ASP LEU SER          
SEQRES  24 A  478  LEU ASN LYS LEU GLY ILE GLN THR ASP ASP LYS GLY HIS          
SEQRES  25 A  478  ILE ILE VAL ASP GLU PHE GLN ASN THR ASN VAL LYS GLY          
SEQRES  26 A  478  ILE TYR ALA VAL GLY ASP VAL CYS GLY LYS ALA LEU LEU          
SEQRES  27 A  478  THR PRO VAL ALA ILE ALA ALA GLY ARG LYS LEU ALA HIS          
SEQRES  28 A  478  ARG LEU PHE GLU TYR LYS GLU ASP SER LYS LEU ASP TYR          
SEQRES  29 A  478  ASN ASN ILE PRO THR VAL VAL PHE SER HIS PRO PRO ILE          
SEQRES  30 A  478  GLY THR VAL GLY LEU THR GLU ASP GLU ALA ILE HIS LYS          
SEQRES  31 A  478  TYR GLY ILE GLU ASN VAL LYS THR TYR SER THR SER PHE          
SEQRES  32 A  478  THR PRO MET TYR HIS ALA VAL THR LYS ARG LYS THR LYS          
SEQRES  33 A  478  CYS VAL MET LYS MET VAL CYS ALA ASN LYS GLU GLU LYS          
SEQRES  34 A  478  VAL VAL GLY ILE HIS MET GLN GLY LEU GLY CYS ASP GLU          
SEQRES  35 A  478  MET LEU GLN GLY PHE ALA VAL ALA VAL LYS MET GLY ALA          
SEQRES  36 A  478  THR LYS ALA ASP PHE ASP ASN THR VAL ALA ILE HIS PRO          
SEQRES  37 A  478  THR SER SER GLU GLU LEU VAL THR LEU ARG                      
HET    SO4  A 580       5                                                       
HET    SO4  A 582       5                                                       
HET    FAD  A 479      53                                                       
HET    GSH  A 481      22                                                       
HET    GSH  A 482      10                                                       
HET    GOL  A 602       6                                                       
HET    GOL  A 603       6                                                       
HET    GOL  A 604       6                                                       
HET    GOL  A 605       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     GSH GLUTATHIONE                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  FAD    C27 H33 N9 O15 P2                                            
FORMUL   5  GSH    2(C10 H17 N3 O6 S)                                           
FORMUL   7  GOL    4(C3 H8 O3)                                                  
FORMUL  11  HOH   *839(H2 O)                                                    
HELIX    1   1 GLY A   29  LEU A   42  1                                  14    
HELIX    2   2 GLY A   55  VAL A   61  1                                   7    
HELIX    3   3 GLY A   62  HIS A   80  1                                  19    
HELIX    4   4 ASN A   95  SER A  121  1                                  27    
HELIX    5   5 GLY A  170  GLY A  174  5                                   5    
HELIX    6   6 THR A  176  PHE A  181  1                                   6    
HELIX    7   7 GLY A  196  LEU A  209  1                                  14    
HELIX    8   8 ASP A  227  ALA A  241  1                                  15    
HELIX    9   9 SER A  299  LEU A  303  5                                   5    
HELIX   10  10 GLY A  330  GLY A  334  5                                   5    
HELIX   11  11 LEU A  338  GLU A  355  1                                  18    
HELIX   12  12 THR A  383  GLY A  392  1                                  10    
HELIX   13  13 PRO A  405  THR A  411  5                                   7    
HELIX   14  14 GLY A  439  MET A  453  1                                  15    
HELIX   15  15 THR A  456  ASN A  462  1                                   7    
HELIX   16  16 SER A  470  THR A  476  5                                   7    
SHEET    1   A 4 VAL A  18  SER A  20  0                                        
SHEET    2   A 4 LYS A 145  THR A 148  1  O  THR A 148   N  ALA A  19           
SHEET    3   A 4 THR A 139  VAL A 142 -1  N  ILE A 140   O  TYR A 147           
SHEET    4   A 4 ALA A 130  PHE A 132 -1  N  ALA A 131   O  GLU A 141           
SHEET    1   B 5 GLU A 124  ARG A 127  0                                        
SHEET    2   B 5 ALA A  46  GLU A  50  1  N  VAL A  48   O  ILE A 126           
SHEET    3   B 5 TYR A  23  ILE A  26  1  N  VAL A  25   O  VAL A  49           
SHEET    4   B 5 ILE A 152  ILE A 154  1  O  LEU A 153   N  ILE A  26           
SHEET    5   B 5 ILE A 326  ALA A 328  1  O  TYR A 327   N  ILE A 154           
SHEET    1   C 2 GLY A 158  PRO A 160  0                                        
SHEET    2   C 2 ARG A 291  PRO A 293 -1  O  VAL A 292   N  MET A 159           
SHEET    1   D 4 GLU A 244  LEU A 246  0                                        
SHEET    2   D 4 LYS A 212  MET A 216  1  N  LEU A 215   O  LEU A 246           
SHEET    3   D 4 ARG A 189  VAL A 193  1  N  ILE A 192   O  MET A 216           
SHEET    4   D 4 CYS A 284  TRP A 287  1  O  LEU A 286   N  VAL A 193           
SHEET    1   E 3 SER A 249  LYS A 256  0                                        
SHEET    2   E 3 LEU A 261  THR A 267 -1  O  SER A 264   N  LYS A 252           
SHEET    3   E 3 VAL A 275  VAL A 282 -1  O  ILE A 279   N  VAL A 263           
SHEET    1   F 5 THR A 369  VAL A 371  0                                        
SHEET    2   F 5 ILE A 377  GLY A 381 -1  O  ILE A 377   N  VAL A 371           
SHEET    3   F 5 LYS A 429  GLN A 436 -1  O  MET A 435   N  GLY A 378           
SHEET    4   F 5 CYS A 417  ALA A 424 -1  N  VAL A 422   O  GLY A 432           
SHEET    5   F 5 VAL A 396  PHE A 403 -1  N  TYR A 399   O  MET A 421           
LINK         SG  CYS A  58                 SG2BGSH A 481     1555   1555  2.03  
CISPEP   1 HIS A  374    PRO A  375          0         0.86                     
CISPEP   2 HIS A  467    PRO A  468          0       -10.54                     
SITE     1 AC1  9 ALA A 195  ARG A 218  HIS A 219  ARG A 224                    
SITE     2 AC1  9 HOH A1023  HOH A1113  HOH A1296  HOH A2125                    
SITE     3 AC1  9 HOH A3004                                                     
SITE     1 AC2  9 ARG A 218  HIS A 219  THR A 257  LEU A 258                    
SITE     2 AC2  9 HOH A1321  HOH A1360  HOH A1407  HOH A1640                    
SITE     3 AC2  9 HOH A3004                                                     
SITE     1 AC3 40 GLY A  27  GLY A  29  SER A  30  GLY A  31                    
SITE     2 AC3 40 GLU A  50  SER A  51  GLY A  56  THR A  57                    
SITE     3 AC3 40 CYS A  58  GLY A  62  CYS A  63  LYS A  66                    
SITE     4 AC3 40 GLY A 128  HIS A 129  ALA A 130  ALA A 155                    
SITE     5 AC3 40 THR A 156  GLY A 157  TYR A 197  ARG A 291                    
SITE     6 AC3 40 ASN A 294  LEU A 298  GLY A 330  ASP A 331                    
SITE     7 AC3 40 LEU A 337  LEU A 338  THR A 339  PRO A 340                    
SITE     8 AC3 40 HIS A 467  PRO A 468  HOH A1001  HOH A1002                    
SITE     9 AC3 40 HOH A1007  HOH A1024  HOH A1063  HOH A1080                    
SITE    10 AC3 40 HOH A1084  HOH A1243  HOH A1269  HOH A1425                    
SITE     1 AC4 21 SER A  30  ARG A  37  CYS A  58  VAL A  59                    
SITE     2 AC4 21 VAL A  64  TYR A 114  THR A 339  ILE A 343                    
SITE     3 AC4 21 ARG A 347  HIS A 467  THR A 476  HOH A1058                    
SITE     4 AC4 21 HOH A1149  HOH A1191  HOH A1192  HOH A1655                    
SITE     5 AC4 21 HOH A1744  HOH A2795  HOH A2800  HOH A3101                    
SITE     6 AC4 21 HOH A3301                                                     
SITE     1 AC5 11 PRO A 405  MET A 406  THR A 469  GLU A 472                    
SITE     2 AC5 11 GLU A 473  HOH A1019  HOH A1061  HOH A1199                    
SITE     3 AC5 11 HOH A1655  HOH A2800  HOH A3305                               
SITE     1 AC6  8 ASN A 320  LYS A 324  GLY A 325  TYR A 327                    
SITE     2 AC6  8 ARG A 352  HOH A1069  HOH A1285  HOH A1445                    
SITE     1 AC7  8 GLU A 101  LYS A 102  ALA A 105  HIS A 122                    
SITE     2 AC7  8 HOH A1068  HOH A1152  HOH A1639  HOH A1798                    
CRYST1  120.031   62.281   83.980  90.00 121.90  90.00 C 1 2 1       4          
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      0.008331  0.000000  0.005186        0.00000                         
SCALE2      0.000000  0.016056  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014026        0.00000                         
ATOM      1  N   ALA A  17     -13.673  26.736  18.805  1.00 58.09           N  
ANISOU    1  N   ALA A  17     3864   9877   8331  -1674  -2871   1773       N  
ATOM      2  CA  ALA A  17     -13.227  27.367  20.042  1.00 50.73           C  
ANISOU    2  CA  ALA A  17     2587   8860   7828  -1334  -1417   1482       C  
ATOM      3  C   ALA A  17     -11.696  27.351  20.108  1.00 39.84           C  
ANISOU    3  C   ALA A  17     2414   7366   5360  -1053   -244     -2       C  
ATOM      4  O   ALA A  17     -11.086  26.459  19.538  1.00 53.51           O  
ANISOU    4  O   ALA A  17     4214   7805   8312  -1097   -238  -2023       O  
ATOM      5  CB  ALA A  17     -13.798  26.665  21.261  1.00 57.24           C  
ANISOU    5  CB  ALA A  17     2613  10546   8589  -2466     40    929       C  
ATOM      6  N   VAL A  18     -11.107  28.323  20.772  1.00 35.54           N  
ANISOU    6  N   VAL A  18     1867   7726   3912    268   -644   -509       N  
ATOM      7  CA  VAL A  18      -9.677  28.416  20.833  1.00 27.43           C  
ANISOU    7  CA  VAL A  18     1839   5830   2754    287    -85   -509       C  
ATOM      8  C   VAL A  18      -9.241  28.715  22.283  1.00 22.27           C  
ANISOU    8  C   VAL A  18     1273   4591   2598   -282    344   -199       C  
ATOM      9  O   VAL A  18      -9.683  29.658  22.898  1.00 29.15           O  
ANISOU    9  O   VAL A  18     2325   6058   2693   1274    157   -574       O  
ATOM     10  CB AVAL A  18      -9.062  29.486  19.913  0.57 26.63           C  
ANISOU   10  CB AVAL A  18     2634   5296   2188   1272    346   -539       C  
ATOM     11  CB BVAL A  18      -9.061  29.465  19.884  0.43 28.54           C  
ANISOU   11  CB BVAL A  18     2557   5876   2410   1091    -26    -51       C  
ATOM     12  CG1AVAL A  18      -7.544  29.448  20.015  0.57 18.90           C  
ANISOU   12  CG1AVAL A  18     2615   2949   1617    543    282   -666       C  
ATOM     13  CG1BVAL A  18      -9.087  30.873  20.458  0.43 28.93           C  
ANISOU   13  CG1BVAL A  18     3420   5538   2033   1428    360    509       C  
ATOM     14  CG2AVAL A  18      -9.544  29.261  18.491  0.57 27.67           C  
ANISOU   14  CG2AVAL A  18     3293   4404   2815   2276   -860   -389       C  
ATOM     15  CG2BVAL A  18      -7.616  29.098  19.533  0.43 24.29           C  
ANISOU   15  CG2BVAL A  18     2014   5364   1853   -262   -238  -1534       C  
ATOM     16  N   ALA A  19      -8.382  27.843  22.770  1.00 20.07           N  
ANISOU   16  N   ALA A  19     1801   3575   2251   -663    168   -358       N  
ATOM     17  CA  ALA A  19      -7.867  28.095  24.122  1.00 17.09           C  
ANISOU   17  CA  ALA A  19     1452   2992   2049   -453    512   -393       C  
ATOM     18  C   ALA A  19      -6.668  29.046  24.100  1.00 14.57           C  
ANISOU   18  C   ALA A  19     1326   2392   1817   -152    362   -133       C  
ATOM     19  O   ALA A  19      -5.774  28.807  23.257  1.00 18.01           O  
ANISOU   19  O   ALA A  19     1863   2974   2005   -666    847   -723       O  
ATOM     20  CB  ALA A  19      -7.476  26.755  24.693  1.00 19.22           C  
ANISOU   20  CB  ALA A  19     1984   2820   2500   -895    429    -62       C  
ATOM     21  N   SER A  20      -6.644  30.014  24.983  1.00 14.07           N  
ANISOU   21  N   SER A  20     1207   2494   1646    -26    226   -145       N  
ATOM     22  CA  SER A  20      -5.566  31.029  25.016  1.00 13.98           C  
ANISOU   22  CA  SER A  20     1235   2485   1592    -15    280   -263       C  
ATOM     23  C   SER A  20      -4.690  30.813  26.219  1.00 15.20           C  
ANISOU   23  C   SER A  20     1230   2946   1599   -156    248   -147       C  
ATOM     24  O   SER A  20      -5.159  30.535  27.320  1.00 16.06           O  
ANISOU   24  O   SER A  20     1044   3380   1681    -15    398    -58       O  
ATOM     25  CB ASER A  20      -6.269  32.360  25.031  0.61 16.15           C  
ANISOU   25  CB ASER A  20     1909   2407   1821    128    148   -329       C  
ATOM     26  CB BSER A  20      -6.067  32.457  24.981  0.39 14.97           C  
ANISOU   26  CB BSER A  20     1163   2492   2033     54    774    -96       C  
ATOM     27  OG ASER A  20      -7.023  32.693  23.871  0.61 18.17           O  
ANISOU   27  OG ASER A  20     2598   2530   1776    281     13    -20       O  
ATOM     28  OG BSER A  20      -4.961  33.364  24.864  0.39 22.78           O  
ANISOU   28  OG BSER A  20     2500   2908   3248   -921   1254   -682       O  
ATOM     29  N   TYR A  21      -3.379  31.013  26.003  1.00 14.97           N  
ANISOU   29  N   TYR A  21     1151   3026   1512     -9    404   -369       N  
ATOM     30  CA  TYR A  21      -2.311  30.931  26.944  1.00 15.03           C  
ANISOU   30  CA  TYR A  21     1164   2813   1734    206    357   -505       C  
ATOM     31  C   TYR A  21      -1.430  32.172  26.847  1.00 14.60           C  
ANISOU   31  C   TYR A  21      876   2563   2108    446     74   -418       C  
ATOM     32  O   TYR A  21      -1.497  32.883  25.838  1.00 16.13           O  
ANISOU   32  O   TYR A  21     1213   2633   2283    194     27   -360       O  
ATOM     33  CB  TYR A  21      -1.428  29.653  26.709  1.00 15.30           C  
ANISOU   33  CB  TYR A  21     1247   2631   1937    105    459   -663       C  
ATOM     34  CG  TYR A  21      -2.236  28.393  26.889  1.00 16.82           C  
ANISOU   34  CG  TYR A  21     1386   2782   2224   -118    790   -896       C  
ATOM     35  CD1 TYR A  21      -3.089  27.928  25.895  1.00 21.63           C  
ANISOU   35  CD1 TYR A  21     2260   3513   2445   -636    696  -1325       C  
ATOM     36  CD2 TYR A  21      -2.190  27.700  28.101  1.00 16.66           C  
ANISOU   36  CD2 TYR A  21     1204   2355   2770     84    664   -679       C  
ATOM     37  CE1 TYR A  21      -3.835  26.794  26.070  1.00 26.54           C  
ANISOU   37  CE1 TYR A  21     3038   3179   3866   -762    176  -1366       C  
ATOM     38  CE2 TYR A  21      -2.950  26.538  28.296  1.00 19.86           C  
ANISOU   38  CE2 TYR A  21     1635   2320   3592    108   1023   -586       C  
ATOM     39  CZ  TYR A  21      -3.762  26.108  27.261  1.00 22.73           C  
ANISOU   39  CZ  TYR A  21     1762   2543   4330   -292    798  -1161       C  
ATOM     40  OH  TYR A  21      -4.550  24.994  27.388  1.00 30.19           O  
ANISOU   40  OH  TYR A  21     1991   2927   6550   -528    789   -717       O  
ATOM     41  N   ASP A  22      -0.606  32.427  27.853  1.00 14.75           N  
ANISOU   41  N   ASP A  22      961   2543   2100    463    207   -614       N  
ATOM     42  CA  ASP A  22       0.436  33.422  27.676  1.00 15.74           C  
ANISOU   42  CA  ASP A  22     1243   2066   2673    454   -144   -388       C  
ATOM     43  C   ASP A  22       1.586  32.967  26.802  1.00 15.29           C  
ANISOU   43  C   ASP A  22     1150   1761   2899    304    187   -107       C  
ATOM     44  O   ASP A  22       2.228  33.749  26.135  1.00 16.42           O  
ANISOU   44  O   ASP A  22     1333   1665   3240    244     25     81       O  
ATOM     45  CB AASP A  22       1.146  33.850  28.954  0.29 12.62           C  
ANISOU   45  CB AASP A  22      717   1748   2329    468      1    322       C  
ATOM     46  CB BASP A  22       0.929  33.820  29.071  0.71 20.34           C  
ANISOU   46  CB BASP A  22     2725   2004   2998    573   -698   -917       C  
ATOM     47  CG AASP A  22       0.308  34.756  29.801  0.29 10.62           C  
ANISOU   47  CG AASP A  22      872   1242   1919   -107    487    537       C  
ATOM     48  CG BASP A  22      -0.112  34.333  30.039  0.71 23.43           C  
ANISOU   48  CG BASP A  22     2958   2995   2950   1458  -1185  -1368       C  
ATOM     49  OD1AASP A  22       0.247  34.477  31.010  0.29 10.88           O  
ANISOU   49  OD1AASP A  22      593   1445   2098     26    363    908       O  
ATOM     50  OD1BASP A  22      -0.110  33.971  31.230  0.71 22.74           O  
ANISOU   50  OD1BASP A  22     3051   2640   2950   1172   -813  -1535       O  
ATOM     51  OD2AASP A  22      -0.325  35.727  29.368  0.29 11.60           O  
ANISOU   51  OD2AASP A  22     1805   1470   1131    533    648    272       O  
ATOM     52  OD2BASP A  22      -0.994  35.097  29.574  0.71 29.85           O  
ANISOU   52  OD2BASP A  22     3820   3099   4421   1998  -1472  -1150       O  
ATOM     53  N   TYR A  23       1.857  31.638  26.865  1.00 13.16           N  
ANISOU   53  N   TYR A  23     1002   1664   2335    170    251    -78       N  
ATOM     54  CA  TYR A  23       3.039  31.088  26.216  1.00 12.13           C  
ANISOU   54  CA  TYR A  23      950   1614   2043    185    234     11       C  
ATOM     55  C   TYR A  23       2.696  29.675  25.724  1.00 11.11           C  
ANISOU   55  C   TYR A  23      871   1588   1760    184    168     84       C  
ATOM     56  O   TYR A  23       2.320  28.841  26.543  1.00 12.46           O  
ANISOU   56  O   TYR A  23     1386   1687   1663     89    292     73       O  
ATOM     57  CB  TYR A  23       4.229  31.002  27.138  1.00 11.18           C  
ANISOU   57  CB  TYR A  23     1031   1534   1683    215    254    -89       C  
ATOM     58  CG  TYR A  23       5.623  30.913  26.588  1.00 10.43           C  
ANISOU   58  CG  TYR A  23     1046   1407   1509    213    233    -80       C  
ATOM     59  CD1 TYR A  23       5.966  31.484  25.382  1.00 11.59           C  
ANISOU   59  CD1 TYR A  23     1070   1669   1665    278    183    168       C  
ATOM     60  CD2 TYR A  23       6.641  30.300  27.321  1.00 10.49           C  
ANISOU   60  CD2 TYR A  23     1070   1576   1339    177    298    -70       C  
ATOM     61  CE1 TYR A  23       7.271  31.414  24.898  1.00 10.96           C  
ANISOU   61  CE1 TYR A  23     1054   1716   1397    253    183    -10       C  
ATOM     62  CE2 TYR A  23       7.951  30.271  26.865  1.00 10.36           C  
ANISOU   62  CE2 TYR A  23     1072   1544   1320    213    152    -93       C  
ATOM     63  CZ  TYR A  23       8.256  30.827  25.653  1.00 10.36           C  
ANISOU   63  CZ  TYR A  23     1031   1446   1457    176    325     -5       C  
ATOM     64  OH  TYR A  23       9.550  30.868  25.137  1.00 11.51           O  
ANISOU   64  OH  TYR A  23      979   1786   1607    171    279    -10       O  
ATOM     65  N   LEU A  24       2.870  29.421  24.442  1.00 11.39           N  
ANISOU   65  N   LEU A  24      972   1613   1744    186    313    129       N  
ATOM     66  CA  LEU A  24       2.708  28.104  23.858  1.00 11.97           C  
ANISOU   66  CA  LEU A  24      922   1650   1976     77    176    -41       C  
ATOM     67  C   LEU A  24       4.057  27.662  23.343  1.00 10.27           C  
ANISOU   67  C   LEU A  24     1065   1558   1278     49    138      0       C  
ATOM     68  O   LEU A  24       4.644  28.390  22.540  1.00 12.21           O  
ANISOU   68  O   LEU A  24     1367   1685   1588    178    434    238       O  
ATOM     69  CB  LEU A  24       1.701  28.115  22.695  1.00 15.51           C  
ANISOU   69  CB  LEU A  24     1314   2515   2063    -29   -154    487       C  
ATOM     70  CG  LEU A  24       0.239  28.127  22.985  1.00 17.56           C  
ANISOU   70  CG  LEU A  24     1404   3099   2170    360    -17    -95       C  
ATOM     71  CD1 LEU A  24      -0.427  28.206  21.592  1.00 22.81           C  
ANISOU   71  CD1 LEU A  24     1564   4595   2509   -846   -491   1048       C  
ATOM     72  CD2 LEU A  24      -0.158  26.839  23.675  1.00 32.95           C  
ANISOU   72  CD2 LEU A  24     3358   6657   2504  -2905   -705   1952       C  
ATOM     73  N   VAL A  25       4.513  26.507  23.784  1.00 10.86           N  
ANISOU   73  N   VAL A  25      957   1645   1524    125    188    111       N  
ATOM     74  CA  VAL A  25       5.817  25.953  23.400  1.00 10.36           C  
ANISOU   74  CA  VAL A  25     1037   1487   1412     54    252    -27       C  
ATOM     75  C   VAL A  25       5.606  24.686  22.612  1.00 10.22           C  
ANISOU   75  C   VAL A  25      968   1495   1421     58    207     12       C  
ATOM     76  O   VAL A  25       4.980  23.737  23.092  1.00 11.79           O  
ANISOU   76  O   VAL A  25     1424   1533   1524      1    359    -41       O  
ATOM     77  CB  VAL A  25       6.636  25.727  24.670  1.00 10.63           C  
ANISOU   77  CB  VAL A  25     1009   1564   1468     46    154     78       C  
ATOM     78  CG1 VAL A  25       7.941  25.001  24.322  1.00 11.96           C  
ANISOU   78  CG1 VAL A  25     1051   1749   1744    170    117    -25       C  
ATOM     79  CG2 VAL A  25       6.902  27.013  25.399  1.00 11.33           C  
ANISOU   79  CG2 VAL A  25     1346   1659   1299     33    239     27       C  
ATOM     80  N   ILE A  26       6.140  24.640  21.386  1.00 10.72           N  
ANISOU   80  N   ILE A  26     1003   1582   1489    -15    252    -75       N  
ATOM     81  CA  ILE A  26       6.018  23.480  20.509  1.00 10.47           C  
ANISOU   81  CA  ILE A  26     1064   1486   1426    -53    206    -46       C  
ATOM     82  C   ILE A  26       7.317  22.691  20.608  1.00 10.18           C  
ANISOU   82  C   ILE A  26     1100   1466   1303    -51    183   -105       C  
ATOM     83  O   ILE A  26       8.347  23.100  20.094  1.00 11.35           O  
ANISOU   83  O   ILE A  26     1066   1596   1651    -41    296     31       O  
ATOM     84  CB  ILE A  26       5.736  23.863  19.055  1.00 11.92           C  
ANISOU   84  CB  ILE A  26     1221   1794   1513     58    165     42       C  
ATOM     85  CG1 ILE A  26       4.587  24.842  18.897  1.00 13.81           C  
ANISOU   85  CG1 ILE A  26     1229   2132   1887    200    160    157       C  
ATOM     86  CG2 ILE A  26       5.477  22.599  18.249  1.00 12.97           C  
ANISOU   86  CG2 ILE A  26     1167   2272   1488    -25    269   -316       C  
ATOM     87  CD1 ILE A  26       4.482  25.459  17.523  1.00 19.18           C  
ANISOU   87  CD1 ILE A  26     1857   3392   2040    742     26    499       C  
ATOM     88  N   GLY A  27       7.237  21.560  21.313  1.00 10.57           N  
ANISOU   88  N   GLY A  27     1068   1484   1464     64    272    -23       N  
ATOM     89  CA  GLY A  27       8.370  20.682  21.531  1.00 11.29           C  
ANISOU   89  CA  GLY A  27     1157   1528   1605    101    165     43       C  
ATOM     90  C   GLY A  27       8.717  20.632  22.996  1.00 10.64           C  
ANISOU   90  C   GLY A  27     1042   1512   1489    -51    186    -58       C  
ATOM     91  O   GLY A  27       8.977  21.665  23.635  1.00 12.58           O  
ANISOU   91  O   GLY A  27     1514   1592   1672    -26    243    -47       O  
ATOM     92  N   GLY A  28       8.823  19.441  23.561  1.00 11.36           N  
ANISOU   92  N   GLY A  28     1263   1565   1488     44    226    -20       N  
ATOM     93  CA  GLY A  28       9.146  19.182  24.942  1.00 11.40           C  
ANISOU   93  CA  GLY A  28     1083   1714   1533    -69    246     99       C  
ATOM     94  C   GLY A  28      10.520  18.549  25.142  1.00 10.18           C  
ANISOU   94  C   GLY A  28     1073   1386   1408    -77    258    -17       C  
ATOM     95  O   GLY A  28      10.694  17.648  25.960  1.00 11.34           O  
ANISOU   95  O   GLY A  28     1317   1588   1406    -37    273     93       O  
ATOM     96  N   GLY A  29      11.515  19.041  24.399  1.00 11.39           N  
ANISOU   96  N   GLY A  29     1070   1663   1595     30    174    239       N  
ATOM     97  CA  GLY A  29      12.902  18.749  24.576  1.00 10.63           C  
ANISOU   97  CA  GLY A  29     1001   1605   1431    121    226     -8       C  
ATOM     98  C   GLY A  29      13.589  19.812  25.378  1.00  9.83           C  
ANISOU   98  C   GLY A  29     1107   1370   1258    158    239     21       C  
ATOM     99  O   GLY A  29      12.970  20.598  26.130  1.00 11.01           O  
ANISOU   99  O   GLY A  29     1087   1666   1430     97    346    -46       O  
ATOM    100  N   SER A  30      14.916  19.862  25.321  1.00 10.64           N  
ANISOU  100  N   SER A  30     1010   1629   1403     52    254   -111       N  
ATOM    101  CA  SER A  30      15.680  20.723  26.197  1.00 11.86           C  
ANISOU  101  CA  SER A  30     1382   1448   1677     76     82   -159       C  
ATOM    102  C   SER A  30      15.258  22.164  26.158  1.00 10.24           C  
ANISOU  102  C   SER A  30      952   1507   1434     54    225   -137       C  
ATOM    103  O   SER A  30      15.062  22.818  27.208  1.00 11.46           O  
ANISOU  103  O   SER A  30     1210   1714   1431     57    196   -235       O  
ATOM    104  CB  SER A  30      17.201  20.612  25.763  1.00 16.24           C  
ANISOU  104  CB  SER A  30     1062   1730   3377    402   -667   -810       C  
ATOM    105  OG  SER A  30      17.679  19.291  25.972  1.00 18.11           O  
ANISOU  105  OG  SER A  30     1600   2107   3174    438    -15    202       O  
ATOM    106  N   GLY A  31      15.183  22.723  24.957  1.00 10.79           N  
ANISOU  106  N   GLY A  31     1097   1588   1416    139    353   -101       N  
ATOM    107  CA  GLY A  31      14.864  24.117  24.803  1.00 11.16           C  
ANISOU  107  CA  GLY A  31     1255   1589   1396     -3    453    -24       C  
ATOM    108  C   GLY A  31      13.435  24.474  25.220  1.00  9.82           C  
ANISOU  108  C   GLY A  31     1118   1398   1214     88    239     63       C  
ATOM    109  O   GLY A  31      13.214  25.458  25.949  1.00 10.79           O  
ANISOU  109  O   GLY A  31     1147   1551   1402     -3    349   -159       O  
ATOM    110  N   GLY A  32      12.486  23.652  24.814  1.00  9.92           N  
ANISOU  110  N   GLY A  32     1069   1384   1318    189    306   -137       N  
ATOM    111  CA  GLY A  32      11.082  23.924  25.146  1.00 10.32           C  
ANISOU  111  CA  GLY A  32     1017   1546   1359    199    246   -114       C  
ATOM    112  C   GLY A  32      10.779  23.762  26.599  1.00 10.15           C  
ANISOU  112  C   GLY A  32      974   1565   1317    -42    252   -104       C  
ATOM    113  O   GLY A  32      10.110  24.598  27.235  1.00 10.73           O  
ANISOU  113  O   GLY A  32     1016   1673   1387    147    199   -253       O  
ATOM    114  N   LEU A  33      11.288  22.675  27.204  1.00 10.01           N  
ANISOU  114  N   LEU A  33      980   1598   1227    120    355   -163       N  
ATOM    115  CA  LEU A  33      11.112  22.456  28.635  1.00 10.05           C  
ANISOU  115  CA  LEU A  33      923   1679   1217    -30    272   -130       C  
ATOM    116  C   LEU A  33      11.677  23.602  29.424  1.00  9.74           C  
ANISOU  116  C   LEU A  33      961   1520   1218     85    119    -41       C  
ATOM    117  O   LEU A  33      11.060  24.155  30.362  1.00 10.54           O  
ANISOU  117  O   LEU A  33     1129   1593   1281     88    372    -89       O  
ATOM    118  CB  LEU A  33      11.719  21.132  29.103  1.00 11.49           C  
ANISOU  118  CB  LEU A  33     1381   1630   1356    -65    333    -64       C  
ATOM    119  CG  LEU A  33      11.138  19.828  28.575  1.00 12.32           C  
ANISOU  119  CG  LEU A  33     1544   1664   1474   -184    570     17       C  
ATOM    120  CD1 LEU A  33      12.019  18.658  28.969  1.00 13.26           C  
ANISOU  120  CD1 LEU A  33     1862   1631   1545   -182    310     43       C  
ATOM    121  CD2 LEU A  33       9.723  19.650  29.091  1.00 18.26           C  
ANISOU  121  CD2 LEU A  33     1582   2408   2947   -491    850   -508       C  
ATOM    122  N   ALA A  34      12.921  23.984  29.128  1.00  9.72           N  
ANISOU  122  N   ALA A  34      940   1493   1259     87    350    -85       N  
ATOM    123  CA  ALA A  34      13.578  24.998  29.929  1.00  9.81           C  
ANISOU  123  CA  ALA A  34     1011   1431   1285    143    158    -27       C  
ATOM    124  C   ALA A  34      12.858  26.334  29.759  1.00  9.34           C  
ANISOU  124  C   ALA A  34      858   1448   1243     82    286     52       C  
ATOM    125  O   ALA A  34      12.688  27.096  30.752  1.00  9.68           O  
ANISOU  125  O   ALA A  34      970   1496   1212    101    219    -64       O  
ATOM    126  CB  ALA A  34      15.037  25.143  29.544  1.00 12.36           C  
ANISOU  126  CB  ALA A  34      956   1720   2022    194    236   -409       C  
ATOM    127  N   SER A  35      12.467  26.703  28.557  1.00  9.33           N  
ANISOU  127  N   SER A  35      944   1430   1172    112    289    130       N  
ATOM    128  CA  SER A  35      11.838  27.990  28.354  1.00  9.43           C  
ANISOU  128  CA  SER A  35      844   1462   1277     61    224     -5       C  
ATOM    129  C   SER A  35      10.446  28.026  29.064  1.00  9.33           C  
ANISOU  129  C   SER A  35      915   1401   1228     77    238    -81       C  
ATOM    130  O   SER A  35      10.112  28.999  29.743  1.00  9.68           O  
ANISOU  130  O   SER A  35      992   1414   1272     69    350    -21       O  
ATOM    131  CB  SER A  35      11.675  28.295  26.885  1.00 10.37           C  
ANISOU  131  CB  SER A  35     1120   1600   1219    213    332    174       C  
ATOM    132  OG  SER A  35      11.437  29.678  26.677  1.00 10.39           O  
ANISOU  132  OG  SER A  35     1038   1499   1410    134    306     62       O  
ATOM    133  N   ALA A  36       9.682  26.953  28.911  1.00  9.40           N  
ANISOU  133  N   ALA A  36      831   1503   1238     86    341   -200       N  
ATOM    134  CA  ALA A  36       8.342  26.903  29.562  1.00  9.47           C  
ANISOU  134  CA  ALA A  36      968   1456   1173     31    346    -54       C  
ATOM    135  C   ALA A  36       8.472  26.980  31.075  1.00  9.60           C  
ANISOU  135  C   ALA A  36      948   1416   1284    -62    388    -59       C  
ATOM    136  O   ALA A  36       7.695  27.685  31.742  1.00 10.01           O  
ANISOU  136  O   ALA A  36     1013   1483   1308     18    465    -40       O  
ATOM    137  CB  ALA A  36       7.634  25.629  29.150  1.00 10.57           C  
ANISOU  137  CB  ALA A  36      948   1719   1350   -125    354   -123       C  
ATOM    138  N   ARG A  37       9.424  26.245  31.646  1.00  9.48           N  
ANISOU  138  N   ARG A  37      905   1498   1197    -42    344    -16       N  
ATOM    139  CA  ARG A  37       9.575  26.233  33.112  1.00  9.80           C  
ANISOU  139  CA  ARG A  37      975   1486   1262    -49    385     -5       C  
ATOM    140  C   ARG A  37       9.971  27.611  33.629  1.00 10.00           C  
ANISOU  140  C   ARG A  37     1031   1540   1228     89    281   -117       C  
ATOM    141  O   ARG A  37       9.453  28.065  34.653  1.00 10.32           O  
ANISOU  141  O   ARG A  37     1111   1523   1285     59    377    -87       O  
ATOM    142  CB AARG A  37      10.586  25.166  33.492  0.45 12.25           C  
ANISOU  142  CB AARG A  37     1459   1518   1677     75   -196   -111       C  
ATOM    143  CB BARG A  37      10.539  25.158  33.580  0.55  9.81           C  
ANISOU  143  CB BARG A  37      971   1569   1187    -46    494    152       C  
ATOM    144  CG AARG A  37       9.883  23.809  33.399  0.45 13.72           C  
ANISOU  144  CG AARG A  37     1504   1516   2192     86    115   -159       C  
ATOM    145  CG BARG A  37      10.025  23.764  33.250  0.55 12.06           C  
ANISOU  145  CG BARG A  37     1115   1541   1925    -78    503    201       C  
ATOM    146  CD AARG A  37       9.395  23.426  34.799  0.45 19.74           C  
ANISOU  146  CD AARG A  37     2911   2048   2540   -114    336    454       C  
ATOM    147  CD BARG A  37      10.997  22.639  33.574  0.55 12.27           C  
ANISOU  147  CD BARG A  37      998   1592   2074    -83    121    -32       C  
ATOM    148  NE AARG A  37      10.390  22.780  35.558  0.45 20.83           N  
ANISOU  148  NE AARG A  37     3379   2036   2497    308    330    364       N  
ATOM    149  NE BARG A  37      11.297  22.576  34.984  0.55 12.58           N  
ANISOU  149  NE BARG A  37     1565   1417   1796    148    715    137       N  
ATOM    150  CZ AARG A  37      10.776  22.350  36.725  0.45 16.73           C  
ANISOU  150  CZ AARG A  37     1832   2199   2326    -64    695    314       C  
ATOM    151  CZ BARG A  37      12.291  21.842  35.503  0.55 12.40           C  
ANISOU  151  CZ BARG A  37     1252   1630   1828    -41    594    260       C  
ATOM    152  NH1AARG A  37       9.964  22.571  37.744  0.45 24.02           N  
ANISOU  152  NH1AARG A  37     2722   3760   2645   1027    937   -284       N  
ATOM    153  NH1BARG A  37      13.083  21.118  34.721  0.55 17.62           N  
ANISOU  153  NH1BARG A  37     1637   1810   3247    389   1551    640       N  
ATOM    154  NH2AARG A  37      11.956  21.710  36.844  0.45 15.72           N  
ANISOU  154  NH2AARG A  37     1126   2251   2595   -661    573    -41       N  
ATOM    155  NH2BARG A  37      12.509  21.813  36.808  0.55 19.69           N  
ANISOU  155  NH2BARG A  37     2073   3434   1975   -851    250    770       N  
ATOM    156  N   ARG A  38      10.868  28.316  32.917  1.00  9.47           N  
ANISOU  156  N   ARG A  38      894   1446   1259     91    371    -94       N  
ATOM    157  CA  ARG A  38      11.249  29.645  33.389  1.00 10.01           C  
ANISOU  157  CA  ARG A  38     1045   1492   1266     74    312    -57       C  
ATOM    158  C   ARG A  38      10.106  30.633  33.209  1.00  9.88           C  
ANISOU  158  C   ARG A  38     1011   1419   1325     65    295    -70       C  
ATOM    159  O   ARG A  38       9.867  31.457  34.111  1.00 10.73           O  
ANISOU  159  O   ARG A  38     1151   1534   1392     89    325   -162       O  
ATOM    160  CB  ARG A  38      12.538  30.125  32.689  1.00 10.28           C  
ANISOU  160  CB  ARG A  38     1015   1503   1386     76    321    -82       C  
ATOM    161  CG  ARG A  38      13.090  31.396  33.216  1.00 11.28           C  
ANISOU  161  CG  ARG A  38      972   1640   1672    -15    260   -135       C  
ATOM    162  CD  ARG A  38      13.376  31.406  34.741  1.00 12.03           C  
ANISOU  162  CD  ARG A  38     1265   1754   1552    -22    316   -376       C  
ATOM    163  NE  ARG A  38      14.266  30.346  35.090  1.00 12.36           N  
ANISOU  163  NE  ARG A  38     1369   1800   1528   -130    188    -28       N  
ATOM    164  CZ  ARG A  38      15.572  30.311  34.945  1.00 12.47           C  
ANISOU  164  CZ  ARG A  38     1419   1595   1725     -7    127   -198       C  
ATOM    165  NH1 ARG A  38      16.270  29.231  35.254  1.00 14.37           N  
ANISOU  165  NH1 ARG A  38     1787   1839   1835    281     28   -111       N  
ATOM    166  NH2 ARG A  38      16.210  31.371  34.501  1.00 14.19           N  
ANISOU  166  NH2 ARG A  38     1181   1871   2341     54    144    248       N  
ATOM    167  N   ALA A  39       9.362  30.556  32.103  1.00  9.89           N  
ANISOU  167  N   ALA A  39      914   1501   1342    -29    347    -17       N  
ATOM    168  CA  ALA A  39       8.227  31.440  31.904  1.00  9.90           C  
ANISOU  168  CA  ALA A  39     1038   1388   1334    128    385    -19       C  
ATOM    169  C   ALA A  39       7.197  31.234  33.024  1.00 10.57           C  
ANISOU  169  C   ALA A  39     1053   1486   1477    107    410    -24       C  
ATOM    170  O   ALA A  39       6.650  32.201  33.571  1.00 10.32           O  
ANISOU  170  O   ALA A  39     1119   1464   1339    162    404    -84       O  
ATOM    171  CB  ALA A  39       7.573  31.119  30.562  1.00 10.89           C  
ANISOU  171  CB  ALA A  39     1205   1542   1391    181    223    -22       C  
ATOM    172  N   ALA A  40       6.921  29.982  33.397  1.00 10.30           N  
ANISOU  172  N   ALA A  40     1129   1507   1277    123    499    -13       N  
ATOM    173  CA  ALA A  40       5.953  29.693  34.468  1.00 10.97           C  
ANISOU  173  CA  ALA A  40     1015   1556   1596     79    480    -61       C  
ATOM    174  C   ALA A  40       6.431  30.264  35.788  1.00 10.70           C  
ANISOU  174  C   ALA A  40     1165   1426   1475     86    525     10       C  
ATOM    175  O   ALA A  40       5.597  30.753  36.590  1.00 11.54           O  
ANISOU  175  O   ALA A  40     1209   1661   1516     37    574    -50       O  
ATOM    176  CB  ALA A  40       5.722  28.196  34.533  1.00 11.92           C  
ANISOU  176  CB  ALA A  40     1468   1569   1493    -95    635    -26       C  
ATOM    177  N   GLU A  41       7.723  30.190  36.091  1.00 11.32           N  
ANISOU  177  N   GLU A  41     1218   1795   1289    260    458    147       N  
ATOM    178  CA  GLU A  41       8.229  30.843  37.291  1.00 12.33           C  
ANISOU  178  CA  GLU A  41     1432   2042   1212    182    396    160       C  
ATOM    179  C   GLU A  41       7.910  32.311  37.323  1.00 11.88           C  
ANISOU  179  C   GLU A  41     1282   1998   1235    -79    275     90       C  
ATOM    180  O   GLU A  41       7.708  32.862  38.445  1.00 14.61           O  
ANISOU  180  O   GLU A  41     2107   2175   1269    146    426    -12       O  
ATOM    181  CB AGLU A  41       9.759  30.788  37.441  0.48 13.82           C  
ANISOU  181  CB AGLU A  41     1435   2464   1352    197    265    286       C  
ATOM    182  CB BGLU A  41       9.731  30.504  37.444  0.52 14.54           C  
ANISOU  182  CB BGLU A  41     1387   2329   1809     93    181     63       C  
ATOM    183  CG AGLU A  41      10.320  29.439  37.747  0.48 12.33           C  
ANISOU  183  CG AGLU A  41     1156   2398   1129    249    411     76       C  
ATOM    184  CG BGLU A  41      10.438  31.062  38.654  0.52 17.53           C  
ANISOU  184  CG BGLU A  41     1585   3097   1979    132    132   -320       C  
ATOM    185  CD AGLU A  41      11.791  29.486  38.117  0.48 17.83           C  
ANISOU  185  CD AGLU A  41     1082   3035   2658    418    319   -119       C  
ATOM    186  CD BGLU A  41      11.950  30.899  38.563  0.52 23.74           C  
ANISOU  186  CD BGLU A  41     1628   3417   3977    765   -806   -512       C  
ATOM    187  OE1AGLU A  41      12.470  30.521  37.934  0.48 21.41           O  
ANISOU  187  OE1AGLU A  41     1094   3365   3674    207    -76    223       O  
ATOM    188  OE1BGLU A  41      12.358  29.776  38.215  0.52 27.64           O  
ANISOU  188  OE1BGLU A  41     2716   3646   4138   1493   -617   -144       O  
ATOM    189  OE2AGLU A  41      12.260  28.420  38.597  0.48 18.54           O  
ANISOU  189  OE2AGLU A  41     1083   3413   2548    449     96    161       O  
ATOM    190  OE2BGLU A  41      12.690  31.876  38.768  0.52 32.00           O  
ANISOU  190  OE2BGLU A  41     1560   4790   5808     31   -430  -1552       O  
ATOM    191  N   LEU A  42       7.886  32.994  36.228  1.00 11.22           N  
ANISOU  191  N   LEU A  42     1267   1733   1265   -143    301     54       N  
ATOM    192  CA  LEU A  42       7.572  34.393  36.090  1.00 11.67           C  
ANISOU  192  CA  LEU A  42     1488   1591   1356   -207    286    -83       C  
ATOM    193  C   LEU A  42       6.078  34.677  36.001  1.00 12.02           C  
ANISOU  193  C   LEU A  42     1513   1647   1408     50    582   -142       C  
ATOM    194  O   LEU A  42       5.653  35.828  35.884  1.00 14.73           O  
ANISOU  194  O   LEU A  42     1954   1574   2067     35    798     -3       O  
ATOM    195  CB  LEU A  42       8.327  34.937  34.894  1.00 12.74           C  
ANISOU  195  CB  LEU A  42     1385   2047   1409   -394    224    207       C  
ATOM    196  CG  LEU A  42       9.838  34.867  34.993  1.00 14.25           C  
ANISOU  196  CG  LEU A  42     1420   2395   1598   -327    129    276       C  
ATOM    197  CD1 LEU A  42      10.553  35.048  33.669  1.00 13.97           C  
ANISOU  197  CD1 LEU A  42     1471   2008   1829   -270    365     43       C  
ATOM    198  CD2 LEU A  42      10.320  35.925  35.999  1.00 24.04           C  
ANISOU  198  CD2 LEU A  42     2482   4784   1866  -1952    422   -562       C  
ATOM    199  N   GLY A  43       5.248  33.642  36.116  1.00 11.62           N  
ANISOU  199  N   GLY A  43     1203   1617   1595     73    362   -162       N  
ATOM    200  CA  GLY A  43       3.790  33.781  36.161  1.00 11.96           C  
ANISOU  200  CA  GLY A  43     1271   1715   1559    144    320   -133       C  
ATOM    201  C   GLY A  43       3.063  33.444  34.917  1.00 11.00           C  
ANISOU  201  C   GLY A  43     1183   1519   1475    133    421    -39       C  
ATOM    202  O   GLY A  43       1.835  33.492  34.893  1.00 12.20           O  
ANISOU  202  O   GLY A  43     1059   1765   1811     41    460   -246       O  
ATOM    203  N   ALA A  44       3.778  33.165  33.824  1.00 11.19           N  
ANISOU  203  N   ALA A  44     1045   1722   1484    146    391   -106       N  
ATOM    204  CA  ALA A  44       3.091  32.858  32.556  1.00 11.77           C  
ANISOU  204  CA  ALA A  44      994   1729   1750    130    209   -397       C  
ATOM    205  C   ALA A  44       2.208  31.632  32.699  1.00 12.42           C  
ANISOU  205  C   ALA A  44      869   1850   2000    254    365   -414       C  
ATOM    206  O   ALA A  44       2.666  30.632  33.274  1.00 13.35           O  
ANISOU  206  O   ALA A  44     1262   1873   1939    214    479   -220       O  
ATOM    207  CB  ALA A  44       4.118  32.642  31.461  1.00 12.14           C  
ANISOU  207  CB  ALA A  44     1312   1857   1445    173    272    -86       C  
ATOM    208  N   ARG A  45       1.063  31.664  32.093  1.00 13.49           N  
ANISOU  208  N   ARG A  45     1000   2084   2040     -6    281   -573       N  
ATOM    209  CA  ARG A  45       0.159  30.580  31.794  1.00 14.32           C  
ANISOU  209  CA  ARG A  45     1079   2063   2297   -128    465   -650       C  
ATOM    210  C   ARG A  45       0.628  29.875  30.513  1.00 12.80           C  
ANISOU  210  C   ARG A  45     1132   1826   1906      6    163   -413       C  
ATOM    211  O   ARG A  45       0.503  30.398  29.431  1.00 15.49           O  
ANISOU  211  O   ARG A  45     1463   2269   2152    521    -47   -298       O  
ATOM    212  CB  ARG A  45      -1.236  31.165  31.571  1.00 16.20           C  
ANISOU  212  CB  ARG A  45     1056   2547   2553     -4    313   -753       C  
ATOM    213  CG  ARG A  45      -1.814  31.910  32.770  1.00 15.59           C  
ANISOU  213  CG  ARG A  45     1461   2439   2023    291    418   -156       C  
ATOM    214  CD  ARG A  45      -2.973  32.925  32.511  1.00 16.37           C  
ANISOU  214  CD  ARG A  45     1607   2443   2170    314    493   -340       C  
ATOM    215  NE  ARG A  45      -2.491  34.124  31.842  1.00 18.72           N  
ANISOU  215  NE  ARG A  45     2117   2359   2636    622    426    -94       N  
ATOM    216  CZ  ARG A  45      -3.253  35.185  31.533  1.00 20.06           C  
ANISOU  216  CZ  ARG A  45     2166   2983   2472   1020    698    228       C  
ATOM    217  NH1 ARG A  45      -4.525  35.223  31.857  1.00 21.76           N  
ANISOU  217  NH1 ARG A  45     2048   3408   2813    912    454    -49       N  
ATOM    218  NH2 ARG A  45      -2.755  36.273  30.900  1.00 21.82           N  
ANISOU  218  NH2 ARG A  45     2161   3095   3035    637   -264    701       N  
ATOM    219  N   ALA A  46       1.326  28.729  30.748  1.00 13.69           N  
ANISOU  219  N   ALA A  46     1359   1866   1976    146    455   -267       N  
ATOM    220  CA  ALA A  46       2.058  28.094  29.665  1.00 12.42           C  
ANISOU  220  CA  ALA A  46     1374   1686   1660    152    269   -218       C  
ATOM    221  C   ALA A  46       1.542  26.691  29.374  1.00 11.07           C  
ANISOU  221  C   ALA A  46     1078   1619   1507    316    295    -20       C  
ATOM    222  O   ALA A  46       1.017  25.989  30.226  1.00 12.15           O  
ANISOU  222  O   ALA A  46     1346   1777   1494    142    489      4       O  
ATOM    223  CB  ALA A  46       3.557  27.975  30.001  1.00 14.73           C  
ANISOU  223  CB  ALA A  46     1224   1968   2405    -15    529   -280       C  
ATOM    224  N   ALA A  47       1.803  26.258  28.139  1.00 11.42           N  
ANISOU  224  N   ALA A  47     1297   1575   1467    121    455    -14       N  
ATOM    225  CA  ALA A  47       1.539  24.895  27.705  1.00 11.75           C  
ANISOU  225  CA  ALA A  47     1109   1705   1651     -2    358   -133       C  
ATOM    226  C   ALA A  47       2.704  24.431  26.826  1.00 11.26           C  
ANISOU  226  C   ALA A  47     1172   1556   1549     26    291    -37       C  
ATOM    227  O   ALA A  47       3.225  25.251  26.049  1.00 12.10           O  
ANISOU  227  O   ALA A  47     1429   1593   1576     30    560     -3       O  
ATOM    228  CB  ALA A  47       0.216  24.774  26.976  1.00 13.29           C  
ANISOU  228  CB  ALA A  47     1107   1983   1960    175    311   -142       C  
ATOM    229  N   VAL A  48       3.036  23.157  26.915  1.00 10.79           N  
ANISOU  229  N   VAL A  48     1128   1632   1338     33    439     -7       N  
ATOM    230  CA  VAL A  48       4.024  22.475  26.075  1.00 10.64           C  
ANISOU  230  CA  VAL A  48     1162   1445   1437    -19    382    -74       C  
ATOM    231  C   VAL A  48       3.329  21.418  25.222  1.00 10.83           C  
ANISOU  231  C   VAL A  48      947   1662   1507    -82    436    -93       C  
ATOM    232  O   VAL A  48       2.617  20.578  25.792  1.00 12.17           O  
ANISOU  232  O   VAL A  48     1220   1827   1577   -260    402   -193       O  
ATOM    233  CB  VAL A  48       5.121  21.832  26.930  1.00 11.14           C  
ANISOU  233  CB  VAL A  48     1185   1554   1494     59    358    -96       C  
ATOM    234  CG1 VAL A  48       6.027  20.928  26.099  1.00 12.62           C  
ANISOU  234  CG1 VAL A  48     1342   1738   1715    187    443   -109       C  
ATOM    235  CG2 VAL A  48       5.942  22.869  27.658  1.00 12.13           C  
ANISOU  235  CG2 VAL A  48     1280   1750   1580   -112    253    -52       C  
ATOM    236  N   VAL A  49       3.545  21.467  23.933  1.00 11.10           N  
ANISOU  236  N   VAL A  49     1159   1531   1526    -80    289    -48       N  
ATOM    237  CA  VAL A  49       3.047  20.438  22.999  1.00 11.09           C  
ANISOU  237  CA  VAL A  49     1126   1553   1534    -93    305    -89       C  
ATOM    238  C   VAL A  49       4.157  19.458  22.749  1.00 11.48           C  
ANISOU  238  C   VAL A  49     1009   1720   1633    -95    300   -237       C  
ATOM    239  O   VAL A  49       5.291  19.852  22.409  1.00 12.35           O  
ANISOU  239  O   VAL A  49     1181   1712   1800    -81    361   -267       O  
ATOM    240  CB  VAL A  49       2.546  21.058  21.689  1.00 12.44           C  
ANISOU  240  CB  VAL A  49     1309   1836   1583    -59    197   -127       C  
ATOM    241  CG1 VAL A  49       1.804  20.017  20.908  1.00 13.69           C  
ANISOU  241  CG1 VAL A  49     1224   2152   1825    -89    -34   -239       C  
ATOM    242  CG2 VAL A  49       1.677  22.286  21.879  1.00 15.12           C  
ANISOU  242  CG2 VAL A  49     1738   2006   2002    246     79    -97       C  
ATOM    243  N   GLU A  50       3.867  18.168  22.844  1.00 11.63           N  
ANISOU  243  N   GLU A  50     1041   1653   1724    -97    258   -295       N  
ATOM    244  CA  GLU A  50       4.884  17.126  22.625  1.00 11.90           C  
ANISOU  244  CA  GLU A  50     1243   1605   1675    -39    281   -180       C  
ATOM    245  C   GLU A  50       4.208  15.936  21.918  1.00 11.74           C  
ANISOU  245  C   GLU A  50     1145   1624   1693      8    200   -209       C  
ATOM    246  O   GLU A  50       3.249  15.367  22.435  1.00 13.13           O  
ANISOU  246  O   GLU A  50     1300   1907   1782   -155    262   -137       O  
ATOM    247  CB  GLU A  50       5.566  16.687  23.873  1.00 12.82           C  
ANISOU  247  CB  GLU A  50     1150   1914   1808    -92    207    -87       C  
ATOM    248  CG  GLU A  50       6.556  15.514  23.769  1.00 13.09           C  
ANISOU  248  CG  GLU A  50     1252   1821   1899   -112    134   -127       C  
ATOM    249  CD  GLU A  50       7.586  15.741  22.684  1.00 12.99           C  
ANISOU  249  CD  GLU A  50     1303   1806   1827   -229    293   -247       C  
ATOM    250  OE1 GLU A  50       8.377  16.731  22.831  1.00 13.42           O  
ANISOU  250  OE1 GLU A  50     1314   1700   2086   -117    163   -235       O  
ATOM    251  OE2 GLU A  50       7.706  14.902  21.757  1.00 13.74           O  
ANISOU  251  OE2 GLU A  50     1338   1689   2195   -180    304   -319       O  
ATOM    252  N   SER A  51       4.762  15.547  20.758  1.00 12.06           N  
ANISOU  252  N   SER A  51     1185   1788   1611    -28     85   -280       N  
ATOM    253  CA  SER A  51       4.193  14.443  20.000  1.00 13.16           C  
ANISOU  253  CA  SER A  51     1264   1929   1806     50     64   -408       C  
ATOM    254  C   SER A  51       4.718  13.081  20.389  1.00 13.02           C  
ANISOU  254  C   SER A  51     1126   1778   2044   -118     47   -386       C  
ATOM    255  O   SER A  51       4.082  12.068  20.064  1.00 15.26           O  
ANISOU  255  O   SER A  51     1497   1997   2304   -135   -140   -478       O  
ATOM    256  CB  SER A  51       4.500  14.687  18.522  1.00 14.75           C  
ANISOU  256  CB  SER A  51     1738   2056   1810    -57     97   -476       C  
ATOM    257  OG  SER A  51       5.899  14.803  18.314  1.00 16.13           O  
ANISOU  257  OG  SER A  51     1780   2287   2061     55    425   -281       O  
ATOM    258  N   HIS A  52       5.869  13.028  21.042  1.00 13.05           N  
ANISOU  258  N   HIS A  52     1236   1675   2049    -98     60   -307       N  
ATOM    259  CA  HIS A  52       6.550  11.795  21.414  1.00 13.69           C  
ANISOU  259  CA  HIS A  52     1267   1659   2276   -237    -46   -164       C  
ATOM    260  C   HIS A  52       6.878  11.821  22.891  1.00 14.57           C  
ANISOU  260  C   HIS A  52     1473   1918   2144    -44     72   -142       C  
ATOM    261  O   HIS A  52       5.963  11.876  23.710  1.00 17.97           O  
ANISOU  261  O   HIS A  52     1430   2997   2402    163     73    261       O  
ATOM    262  CB  HIS A  52       7.748  11.584  20.479  1.00 15.77           C  
ANISOU  262  CB  HIS A  52     1736   1980   2277    264    234   -251       C  
ATOM    263  CG  HIS A  52       7.322  11.291  19.063  1.00 20.14           C  
ANISOU  263  CG  HIS A  52     2449   2781   2421    257    100   -472       C  
ATOM    264  ND1 HIS A  52       6.910  12.283  18.164  1.00 21.65           N  
ANISOU  264  ND1 HIS A  52     2910   2958   2357    695    -53   -532       N  
ATOM    265  CD2 HIS A  52       7.230  10.118  18.394  1.00 30.14           C  
ANISOU  265  CD2 HIS A  52     5466   3074   2911   1551   -758  -1098       C  
ATOM    266  CE1 HIS A  52       6.601  11.716  17.005  1.00 21.24           C  
ANISOU  266  CE1 HIS A  52     2618   3045   2407    200    145   -580       C  
ATOM    267  NE2 HIS A  52       6.780  10.386  17.102  1.00 32.02           N  
ANISOU  267  NE2 HIS A  52     5678   3220   3268   1279  -1372  -1027       N  
ATOM    268  N   LYS A  53       8.129  11.700  23.282  1.00 15.59           N  
ANISOU  268  N   LYS A  53     1315   2518   2091   -260     55   -373       N  
ATOM    269  CA  LYS A  53       8.487  11.571  24.683  1.00 14.84           C  
ANISOU  269  CA  LYS A  53     1474   2044   2119    -99    122   -300       C  
ATOM    270  C   LYS A  53       9.153  12.824  25.209  1.00 13.78           C  
ANISOU  270  C   LYS A  53     1435   1990   1811   -145    146   -120       C  
ATOM    271  O   LYS A  53      10.067  13.443  24.633  1.00 13.92           O  
ANISOU  271  O   LYS A  53     1306   1902   2082    -62    211    -35       O  
ATOM    272  CB  LYS A  53       9.467  10.401  24.887  1.00 17.35           C  
ANISOU  272  CB  LYS A  53     1814   2130   2650    123   -213   -549       C  
ATOM    273  CG  LYS A  53       8.726   9.045  24.668  1.00 20.63           C  
ANISOU  273  CG  LYS A  53     2256   2133   3451     46   -784   -350       C  
ATOM    274  CD  LYS A  53       9.616   7.897  25.127  1.00 24.10           C  
ANISOU  274  CD  LYS A  53     2197   2324   4635     47   -538      1       C  
ATOM    275  CE  LYS A  53       8.916   6.544  24.882  1.00 26.82           C  
ANISOU  275  CE  LYS A  53     3498   2140   4552    -21   -791   -178       C  
ATOM    276  NZ  LYS A  53       9.897   5.410  24.913  1.00 29.11           N  
ANISOU  276  NZ  LYS A  53     4269   2625   4168    600   -368   -345       N  
ATOM    277  N   LEU A  54       8.651  13.267  26.366  1.00 14.44           N  
ANISOU  277  N   LEU A  54     1475   2141   1869   -130    265   -154       N  
ATOM    278  CA  LEU A  54       9.256  14.405  27.032  1.00 12.70           C  
ANISOU  278  CA  LEU A  54     1473   1745   1608     95    240    147       C  
ATOM    279  C   LEU A  54      10.721  14.126  27.302  1.00 12.75           C  
ANISOU  279  C   LEU A  54     1427   1637   1780     95    189    236       C  
ATOM    280  O   LEU A  54      11.158  13.014  27.576  1.00 14.40           O  
ANISOU  280  O   LEU A  54     1683   1534   2253     36    127    261       O  
ATOM    281  CB  LEU A  54       8.506  14.717  28.347  1.00 14.34           C  
ANISOU  281  CB  LEU A  54     1661   2069   1718     -6    433     -3       C  
ATOM    282  CG  LEU A  54       7.102  15.275  28.155  1.00 14.62           C  
ANISOU  282  CG  LEU A  54     1739   2084   1731     42    510     67       C  
ATOM    283  CD1 LEU A  54       6.367  15.330  29.492  1.00 18.69           C  
ANISOU  283  CD1 LEU A  54     2086   2892   2125    548    903    299       C  
ATOM    284  CD2 LEU A  54       7.102  16.627  27.484  1.00 14.85           C  
ANISOU  284  CD2 LEU A  54     1591   2002   2047    -39    333    -53       C  
ATOM    285  N   GLY A  55      11.493  15.228  27.207  1.00 12.31           N  
ANISOU  285  N   GLY A  55     1313   1475   1889    171    272    -11       N  
ATOM    286  CA  GLY A  55      12.928  15.147  27.256  1.00 12.17           C  
ANISOU  286  CA  GLY A  55     1311   1612   1700    217    156     10       C  
ATOM    287  C   GLY A  55      13.608  15.191  25.918  1.00 11.67           C  
ANISOU  287  C   GLY A  55     1101   1584   1750    100    133     43       C  
ATOM    288  O   GLY A  55      14.841  15.423  25.821  1.00 12.98           O  
ANISOU  288  O   GLY A  55     1375   1671   1886   -156    153     12       O  
ATOM    289  N   GLY A  56      12.873  14.960  24.863  1.00 11.86           N  
ANISOU  289  N   GLY A  56     1125   1640   1742     70    205     -8       N  
ATOM    290  CA  GLY A  56      13.363  15.115  23.527  1.00 12.15           C  
ANISOU  290  CA  GLY A  56     1161   1688   1766    105    162    170       C  
ATOM    291  C   GLY A  56      14.602  14.305  23.236  1.00 10.56           C  
ANISOU  291  C   GLY A  56     1190   1374   1447     69    109     83       C  
ATOM    292  O   GLY A  56      14.786  13.204  23.716  1.00 11.69           O  
ANISOU  292  O   GLY A  56     1227   1445   1769     43    205    161       O  
ATOM    293  N   THR A  57      15.461  14.894  22.410  1.00 11.69           N  
ANISOU  293  N   THR A  57     1225   1473   1745    146    250    297       N  
ATOM    294  CA  THR A  57      16.662  14.192  21.965  1.00 11.79           C  
ANISOU  294  CA  THR A  57     1193   1451   1833     -3    327    201       C  
ATOM    295  C   THR A  57      17.600  13.937  23.130  1.00 11.97           C  
ANISOU  295  C   THR A  57     1237   1581   1729    172    453    334       C  
ATOM    296  O   THR A  57      18.134  12.824  23.210  1.00 12.82           O  
ANISOU  296  O   THR A  57     1304   1683   1885    313    507    374       O  
ATOM    297  CB  THR A  57      17.289  15.000  20.800  1.00 13.36           C  
ANISOU  297  CB  THR A  57     1612   1843   1621     96    418    222       C  
ATOM    298  OG1 THR A  57      16.301  15.015  19.755  1.00 14.85           O  
ANISOU  298  OG1 THR A  57     1845   2058   1738     13    219    136       O  
ATOM    299  CG2 THR A  57      18.589  14.375  20.329  1.00 14.76           C  
ANISOU  299  CG2 THR A  57     1535   2151   1920    -70    575     47       C  
ATOM    300  N   CYS A  58      17.777  14.917  24.005  1.00 12.60           N  
ANISOU  300  N   CYS A  58     1201   1566   2023     65     89    372       N  
ATOM    301  CA  CYS A  58      18.702  14.838  25.119  1.00 13.59           C  
ANISOU  301  CA  CYS A  58     1371   1743   2051    -76     13    488       C  
ATOM    302  C   CYS A  58      18.444  13.557  25.933  1.00 11.25           C  
ANISOU  302  C   CYS A  58     1021   1633   1622   -125    -11    248       C  
ATOM    303  O   CYS A  58      19.355  12.763  26.213  1.00 13.92           O  
ANISOU  303  O   CYS A  58     1054   1868   2366    -19    155    492       O  
ATOM    304  CB  CYS A  58      18.586  16.089  26.025  1.00 16.77           C  
ANISOU  304  CB  CYS A  58     1297   1557   3518   -234   -470    -42       C  
ATOM    305  SG  CYS A  58      19.650  16.191  27.449  1.00 15.40           S  
ANISOU  305  SG  CYS A  58     1356   2266   2230     50    242     50       S  
ATOM    306  N   VAL A  59      17.210  13.382  26.344  1.00 10.94           N  
ANISOU  306  N   VAL A  59      979   1447   1729     -8     23    120       N  
ATOM    307  CA  VAL A  59      16.904  12.261  27.256  1.00 10.15           C  
ANISOU  307  CA  VAL A  59     1051   1460   1344     61     16     64       C  
ATOM    308  C   VAL A  59      16.830  10.974  26.479  1.00  9.70           C  
ANISOU  308  C   VAL A  59      866   1496   1323    -18    171      6       C  
ATOM    309  O   VAL A  59      17.255   9.920  26.982  1.00 10.75           O  
ANISOU  309  O   VAL A  59     1033   1544   1509     49    225     69       O  
ATOM    310  CB  VAL A  59      15.551  12.541  27.955  1.00 11.76           C  
ANISOU  310  CB  VAL A  59     1082   1862   1525     56    148   -235       C  
ATOM    311  CG1 VAL A  59      15.008  11.285  28.623  1.00 13.17           C  
ANISOU  311  CG1 VAL A  59     1574   1997   1433    348    534     90       C  
ATOM    312  CG2 VAL A  59      15.690  13.728  28.922  1.00 13.84           C  
ANISOU  312  CG2 VAL A  59     1578   2090   1592    373    -32   -402       C  
ATOM    313  N   ASN A  60      16.204  10.960  25.288  1.00 10.09           N  
ANISOU  313  N   ASN A  60     1091   1470   1271     53    174    -15       N  
ATOM    314  CA  ASN A  60      15.761   9.715  24.692  1.00 10.18           C  
ANISOU  314  CA  ASN A  60     1024   1431   1412    -64    242      1       C  
ATOM    315  C   ASN A  60      16.770   9.136  23.689  1.00 10.88           C  
ANISOU  315  C   ASN A  60     1114   1420   1598      3    318    -28       C  
ATOM    316  O   ASN A  60      16.897   7.902  23.646  1.00 12.24           O  
ANISOU  316  O   ASN A  60     1284   1545   1820     -4    346    -64       O  
ATOM    317  CB  ASN A  60      14.399   9.932  24.002  1.00 10.02           C  
ANISOU  317  CB  ASN A  60     1055   1437   1316    -53    279     16       C  
ATOM    318  CG  ASN A  60      13.339  10.272  25.019  1.00 10.73           C  
ANISOU  318  CG  ASN A  60     1064   1631   1382    109    271     99       C  
ATOM    319  OD1 ASN A  60      12.873   9.387  25.756  1.00 11.41           O  
ANISOU  319  OD1 ASN A  60     1196   1618   1521     56    381     96       O  
ATOM    320  ND2 ASN A  60      12.975  11.521  25.134  1.00 12.01           N  
ANISOU  320  ND2 ASN A  60     1051   1658   1855     92    362    102       N  
ATOM    321  N   VAL A  61      17.429   9.925  22.872  1.00 10.82           N  
ANISOU  321  N   VAL A  61     1214   1578   1319    -69    366   -129       N  
ATOM    322  CA  VAL A  61      18.255   9.403  21.762  1.00 11.24           C  
ANISOU  322  CA  VAL A  61     1255   1643   1373    -58    259   -313       C  
ATOM    323  C   VAL A  61      19.525  10.236  21.582  1.00 11.12           C  
ANISOU  323  C   VAL A  61     1171   1532   1521     53    309   -188       C  
ATOM    324  O   VAL A  61      20.097  10.258  20.478  1.00 13.75           O  
ANISOU  324  O   VAL A  61     1260   2367   1598   -183    390   -355       O  
ATOM    325  CB  VAL A  61      17.442   9.318  20.439  1.00 12.75           C  
ANISOU  325  CB  VAL A  61     1471   1874   1498   -193    228   -317       C  
ATOM    326  CG1 VAL A  61      16.369   8.252  20.544  1.00 14.54           C  
ANISOU  326  CG1 VAL A  61     1486   2234   1803   -521    148   -239       C  
ATOM    327  CG2 VAL A  61      16.903  10.660  20.023  1.00 13.25           C  
ANISOU  327  CG2 VAL A  61     1545   2102   1387    128    280    -41       C  
ATOM    328  N   GLY A  62      20.024  10.880  22.616  1.00 10.64           N  
ANISOU  328  N   GLY A  62     1098   1480   1466    -81    317    -57       N  
ATOM    329  CA  GLY A  62      21.101  11.808  22.534  1.00 11.34           C  
ANISOU  329  CA  GLY A  62     1037   1638   1635      3    157     21       C  
ATOM    330  C   GLY A  62      22.014  11.728  23.734  1.00 10.50           C  
ANISOU  330  C   GLY A  62      978   1667   1345     68    283      3       C  
ATOM    331  O   GLY A  62      22.495  10.674  24.095  1.00 11.64           O  
ANISOU  331  O   GLY A  62     1108   1629   1686    168    224    105       O  
ATOM    332  N   CYS A  63      22.239  12.891  24.340  1.00 11.08           N  
ANISOU  332  N   CYS A  63     1021   1658   1529     11    202     49       N  
ATOM    333  CA  CYS A  63      23.169  13.127  25.436  1.00 11.46           C  
ANISOU  333  CA  CYS A  63     1111   1772   1471   -114    259     46       C  
ATOM    334  C   CYS A  63      23.179  11.986  26.450  1.00  9.98           C  
ANISOU  334  C   CYS A  63     1001   1540   1249     17    189   -182       C  
ATOM    335  O   CYS A  63      24.230  11.440  26.757  1.00 10.98           O  
ANISOU  335  O   CYS A  63      992   1610   1568    165    194   -166       O  
ATOM    336  CB  CYS A  63      22.806  14.429  26.187  1.00 14.47           C  
ANISOU  336  CB  CYS A  63     1757   1527   2214    -50    249   -168       C  
ATOM    337  SG  CYS A  63      22.536  15.849  25.127  1.00 13.71           S  
ANISOU  337  SG  CYS A  63     1503   1810   1896     90    337     27       S  
ATOM    338  N   VAL A  64      22.023  11.671  27.057  1.00 10.67           N  
ANISOU  338  N   VAL A  64      993   1560   1500    168    290     47       N  
ATOM    339  CA  VAL A  64      21.974  10.786  28.195  1.00 11.40           C  
ANISOU  339  CA  VAL A  64     1183   1738   1411    232    345     57       C  
ATOM    340  C   VAL A  64      22.308   9.350  27.787  1.00 10.22           C  
ANISOU  340  C   VAL A  64      958   1563   1363    136    450    164       C  
ATOM    341  O   VAL A  64      23.251   8.752  28.346  1.00 10.79           O  
ANISOU  341  O   VAL A  64      994   1707   1398    199    362     27       O  
ATOM    342  CB  VAL A  64      20.605  10.886  28.900  1.00 14.19           C  
ANISOU  342  CB  VAL A  64     1437   2155   1797    589    658    300       C  
ATOM    343  CG1 VAL A  64      20.515   9.784  29.940  1.00 19.00           C  
ANISOU  343  CG1 VAL A  64     2156   3174   1888   1094   1256    905       C  
ATOM    344  CG2 VAL A  64      20.456  12.251  29.542  1.00 16.85           C  
ANISOU  344  CG2 VAL A  64     1801   2740   1861    842    553   -208       C  
ATOM    345  N   PRO A  65      21.601   8.710  26.842  1.00 10.75           N  
ANISOU  345  N   PRO A  65      925   1546   1614     87    284    154       N  
ATOM    346  CA  PRO A  65      21.966   7.333  26.518  1.00 11.24           C  
ANISOU  346  CA  PRO A  65      895   1581   1793     33    298    116       C  
ATOM    347  C   PRO A  65      23.364   7.249  25.904  1.00  9.97           C  
ANISOU  347  C   PRO A  65      986   1489   1313     59    185     40       C  
ATOM    348  O   PRO A  65      24.046   6.229  26.113  1.00 10.40           O  
ANISOU  348  O   PRO A  65      959   1491   1501      4    228     54       O  
ATOM    349  CB  PRO A  65      20.835   6.842  25.609  1.00 12.39           C  
ANISOU  349  CB  PRO A  65     1090   1695   1924    -85    208    145       C  
ATOM    350  CG  PRO A  65      20.301   8.104  25.010  1.00 12.23           C  
ANISOU  350  CG  PRO A  65     1100   1820   1726    -80     83    269       C  
ATOM    351  CD  PRO A  65      20.377   9.147  26.108  1.00 11.79           C  
ANISOU  351  CD  PRO A  65      913   1876   1691    132    294    204       C  
ATOM    352  N   LYS A  66      23.779   8.259  25.179  1.00 10.10           N  
ANISOU  352  N   LYS A  66      962   1447   1430      3    220    110       N  
ATOM    353  CA  LYS A  66      25.181   8.266  24.672  1.00 10.08           C  
ANISOU  353  CA  LYS A  66      997   1613   1218    200    293    -72       C  
ATOM    354  C   LYS A  66      26.127   8.194  25.844  1.00  9.61           C  
ANISOU  354  C   LYS A  66      942   1354   1356     -2    233     92       C  
ATOM    355  O   LYS A  66      27.116   7.416  25.817  1.00  9.98           O  
ANISOU  355  O   LYS A  66      960   1517   1316     94    292     29       O  
ATOM    356  CB  LYS A  66      25.393   9.504  23.822  1.00 10.97           C  
ANISOU  356  CB  LYS A  66      968   1614   1587    112    221    131       C  
ATOM    357  CG  LYS A  66      26.818   9.671  23.280  1.00 12.99           C  
ANISOU  357  CG  LYS A  66     1327   1927   1682    140    504    239       C  
ATOM    358  CD  LYS A  66      27.860  10.324  24.162  1.00 14.52           C  
ANISOU  358  CD  LYS A  66     1070   2341   2108     41    372    311       C  
ATOM    359  CE  LYS A  66      27.603  11.694  24.751  1.00 16.29           C  
ANISOU  359  CE  LYS A  66     1433   2448   2308   -288    454    -52       C  
ATOM    360  NZ  LYS A  66      27.480  12.681  23.620  1.00 15.93           N  
ANISOU  360  NZ  LYS A  66     1490   2109   2455    360    354   -198       N  
ATOM    361  N   LYS A  67      25.944   9.019  26.868  1.00  9.87           N  
ANISOU  361  N   LYS A  67      850   1552   1348     71    174     40       N  
ATOM    362  CA  LYS A  67      26.864   9.037  27.973  1.00 10.16           C  
ANISOU  362  CA  LYS A  67      858   1613   1389    123    199     18       C  
ATOM    363  C   LYS A  67      26.916   7.752  28.763  1.00  9.55           C  
ANISOU  363  C   LYS A  67      904   1577   1149     38    220   -123       C  
ATOM    364  O   LYS A  67      27.977   7.283  29.195  1.00 10.08           O  
ANISOU  364  O   LYS A  67      905   1572   1355    110    235    -40       O  
ATOM    365  CB  LYS A  67      26.583  10.229  28.901  1.00 10.70           C  
ANISOU  365  CB  LYS A  67      992   1652   1420    -36    347    -88       C  
ATOM    366  CG  LYS A  67      27.617  10.416  30.008  1.00 10.72           C  
ANISOU  366  CG  LYS A  67      939   1526   1607    -67    274    -49       C  
ATOM    367  CD  LYS A  67      28.942  10.948  29.523  1.00 11.56           C  
ANISOU  367  CD  LYS A  67     1072   1828   1491   -284    331   -106       C  
ATOM    368  CE  LYS A  67      29.949  11.182  30.626  1.00 11.49           C  
ANISOU  368  CE  LYS A  67      989   1811   1565   -131    216   -185       C  
ATOM    369  NZ  LYS A  67      29.606  12.267  31.574  1.00 12.78           N  
ANISOU  369  NZ  LYS A  67     1272   1898   1687    -41    231   -236       N  
ATOM    370  N   VAL A  68      25.736   7.092  28.896  1.00  9.80           N  
ANISOU  370  N   VAL A  68      942   1539   1242     85    213    -31       N  
ATOM    371  CA  VAL A  68      25.723   5.786  29.539  1.00  9.98           C  
ANISOU  371  CA  VAL A  68      969   1519   1305     32    279    -50       C  
ATOM    372  C   VAL A  68      26.607   4.823  28.739  1.00  9.54           C  
ANISOU  372  C   VAL A  68      940   1384   1300    -97    273     10       C  
ATOM    373  O   VAL A  68      27.409   4.033  29.282  1.00 10.11           O  
ANISOU  373  O   VAL A  68     1038   1444   1361     58    252     68       O  
ATOM    374  CB  VAL A  68      24.290   5.215  29.689  1.00 10.52           C  
ANISOU  374  CB  VAL A  68     1016   1719   1263    -38    229    -11       C  
ATOM    375  CG1 VAL A  68      24.331   3.790  30.226  1.00 12.11           C  
ANISOU  375  CG1 VAL A  68     1080   1855   1666   -158    304    170       C  
ATOM    376  CG2 VAL A  68      23.499   6.112  30.634  1.00 12.15           C  
ANISOU  376  CG2 VAL A  68     1102   2110   1403     71    507     88       C  
ATOM    377  N   MET A  69      26.466   4.843  27.408  1.00  9.87           N  
ANISOU  377  N   MET A  69      926   1493   1331      8    290    -36       N  
ATOM    378  CA  MET A  69      27.263   3.956  26.559  1.00 10.43           C  
ANISOU  378  CA  MET A  69     1125   1385   1451    -15    361   -151       C  
ATOM    379  C   MET A  69      28.728   4.334  26.568  1.00  9.86           C  
ANISOU  379  C   MET A  69      986   1478   1281     96    342     72       C  
ATOM    380  O   MET A  69      29.612   3.440  26.537  1.00 10.05           O  
ANISOU  380  O   MET A  69     1075   1376   1368    112    305     44       O  
ATOM    381  CB  MET A  69      26.724   3.938  25.151  1.00 10.96           C  
ANISOU  381  CB  MET A  69     1093   1574   1496    118    279    -17       C  
ATOM    382  CG  MET A  69      25.331   3.346  25.025  1.00 11.81           C  
ANISOU  382  CG  MET A  69     1129   1700   1656      1    193    -35       C  
ATOM    383  SD  MET A  69      25.106   1.724  25.773  1.00 13.61           S  
ANISOU  383  SD  MET A  69     1257   1682   2232   -115    262    -44       S  
ATOM    384  CE  MET A  69      26.046   0.720  24.620  1.00 20.69           C  
ANISOU  384  CE  MET A  69     1965   1729   4166   -104    869   -648       C  
ATOM    385  N   TRP A  70      29.065   5.616  26.706  1.00 10.21           N  
ANISOU  385  N   TRP A  70      941   1451   1489    106    257    -58       N  
ATOM    386  CA  TRP A  70      30.461   6.048  26.832  1.00 10.12           C  
ANISOU  386  CA  TRP A  70      975   1542   1327     62    299    138       C  
ATOM    387  C   TRP A  70      31.048   5.508  28.126  1.00 10.16           C  
ANISOU  387  C   TRP A  70     1007   1494   1360      3    313    112       C  
ATOM    388  O   TRP A  70      32.175   4.990  28.154  1.00 10.73           O  
ANISOU  388  O   TRP A  70      969   1607   1500    122    290    140       O  
ATOM    389  CB  TRP A  70      30.563   7.558  26.715  1.00 10.41           C  
ANISOU  389  CB  TRP A  70      960   1521   1474    101    217     -3       C  
ATOM    390  CG  TRP A  70      31.973   8.070  26.751  1.00 11.27           C  
ANISOU  390  CG  TRP A  70     1059   1609   1615    -85    410     25       C  
ATOM    391  CD1 TRP A  70      32.861   8.070  25.704  1.00 11.73           C  
ANISOU  391  CD1 TRP A  70     1091   1745   1623    -26    439    131       C  
ATOM    392  CD2 TRP A  70      32.654   8.648  27.891  1.00 11.73           C  
ANISOU  392  CD2 TRP A  70      943   1864   1650   -149    406      5       C  
ATOM    393  NE1 TRP A  70      34.046   8.622  26.127  1.00 12.12           N  
ANISOU  393  NE1 TRP A  70      899   2148   1558     -3    395    182       N  
ATOM    394  CE2 TRP A  70      33.946   8.982  27.423  1.00 11.89           C  
ANISOU  394  CE2 TRP A  70     1024   1826   1669   -147    412    114       C  
ATOM    395  CE3 TRP A  70      32.342   8.925  29.191  1.00 13.32           C  
ANISOU  395  CE3 TRP A  70     1029   2283   1749   -215    467   -322       C  
ATOM    396  CZ2 TRP A  70      34.902   9.586  28.255  1.00 15.77           C  
ANISOU  396  CZ2 TRP A  70     1104   2848   2041   -358    315   -245       C  
ATOM    397  CZ3 TRP A  70      33.268   9.519  30.010  1.00 17.48           C  
ANISOU  397  CZ3 TRP A  70     1385   3371   1883   -614    393   -547       C  
ATOM    398  CH2 TRP A  70      34.521   9.837  29.564  1.00 16.94           C  
ANISOU  398  CH2 TRP A  70     1225   3196   2015   -470    234   -365       C  
ATOM    399  N   ASN A  71      30.317   5.645  29.236  1.00 10.10           N  
ANISOU  399  N   ASN A  71     1038   1531   1270     32    261    -24       N  
ATOM    400  CA  ASN A  71      30.767   5.095  30.500  1.00 10.51           C  
ANISOU  400  CA  ASN A  71     1047   1649   1299    -37    373     49       C  
ATOM    401  C   ASN A  71      31.043   3.606  30.427  1.00 10.18           C  
ANISOU  401  C   ASN A  71      973   1626   1268     63    387    150       C  
ATOM    402  O   ASN A  71      32.003   3.072  30.997  1.00 12.14           O  
ANISOU  402  O   ASN A  71     1163   2074   1377    242    325     49       O  
ATOM    403  CB  ASN A  71      29.791   5.414  31.625  1.00 10.33           C  
ANISOU  403  CB  ASN A  71     1101   1647   1176    -70    244    -15       C  
ATOM    404  CG  ASN A  71      29.812   6.843  32.064  1.00 11.44           C  
ANISOU  404  CG  ASN A  71     1243   1706   1398   -339    350   -253       C  
ATOM    405  OD1 ASN A  71      30.811   7.514  31.979  1.00 16.11           O  
ANISOU  405  OD1 ASN A  71     1524   2476   2120   -758    793   -749       O  
ATOM    406  ND2 ASN A  71      28.665   7.320  32.572  1.00 11.62           N  
ANISOU  406  ND2 ASN A  71     1334   1630   1452    -72    414    -20       N  
ATOM    407  N   THR A  72      30.205   2.902  29.665  1.00 10.47           N  
ANISOU  407  N   THR A  72     1102   1446   1431     65    318    139       N  
ATOM    408  CA  THR A  72      30.374   1.458  29.460  1.00 10.80           C  
ANISOU  408  CA  THR A  72     1192   1506   1407    112    386     89       C  
ATOM    409  C   THR A  72      31.669   1.177  28.686  1.00 11.25           C  
ANISOU  409  C   THR A  72     1199   1604   1473    167    273    179       C  
ATOM    410  O   THR A  72      32.458   0.306  29.021  1.00 12.20           O  
ANISOU  410  O   THR A  72     1321   1785   1531    367    394    398       O  
ATOM    411  CB  THR A  72      29.164   0.892  28.718  1.00 11.00           C  
ANISOU  411  CB  THR A  72     1246   1521   1413     37    423     50       C  
ATOM    412  OG1 THR A  72      27.945   1.233  29.409  1.00 11.75           O  
ANISOU  412  OG1 THR A  72     1180   1695   1589    -54    403     47       O  
ATOM    413  CG2 THR A  72      29.168  -0.624  28.598  1.00 12.63           C  
ANISOU  413  CG2 THR A  72     1522   1573   1705     20    336     32       C  
ATOM    414  N   ALA A  73      31.882   1.950  27.614  1.00 10.71           N  
ANISOU  414  N   ALA A  73     1138   1492   1441    183    338    214       N  
ATOM    415  CA  ALA A  73      33.103   1.840  26.799  1.00 11.78           C  
ANISOU  415  CA  ALA A  73     1294   1631   1551     54    438    124       C  
ATOM    416  C   ALA A  73      34.330   2.166  27.606  1.00 12.27           C  
ANISOU  416  C   ALA A  73     1154   1813   1695    216    361    122       C  
ATOM    417  O   ALA A  73      35.388   1.488  27.492  1.00 13.66           O  
ANISOU  417  O   ALA A  73     1313   2230   1648    520    559    324       O  
ATOM    418  CB  ALA A  73      32.964   2.768  25.614  1.00 11.56           C  
ANISOU  418  CB  ALA A  73     1222   1780   1391    139    480     88       C  
ATOM    419  N  AVAL A  74      34.336   3.244  28.383  0.52 12.43           N  
ANISOU  419  N  AVAL A  74      954   2320   1450    267    357    -70       N  
ATOM    420  N  BVAL A  74      34.227   3.045  28.588  0.47 11.95           N  
ANISOU  420  N  BVAL A  74      918   1935   1687    139    231     95       N  
ATOM    421  CA AVAL A  74      35.425   3.728  29.223  0.52 12.73           C  
ANISOU  421  CA AVAL A  74     1320   2165   1352     -6    291    128       C  
ATOM    422  CA BVAL A  74      35.383   3.166  29.493  0.47 12.18           C  
ANISOU  422  CA BVAL A  74      839   2186   1601     79    309    307       C  
ATOM    423  C  AVAL A  74      35.852   2.666  30.237  0.52 11.66           C  
ANISOU  423  C  AVAL A  74      929   2049   1453    147    363     32       C  
ATOM    424  C  BVAL A  74      35.616   1.904  30.322  0.47 13.25           C  
ANISOU  424  C  BVAL A  74      966   2347   1721    -89    227    449       C  
ATOM    425  O  AVAL A  74      37.023   2.390  30.460  0.52 12.04           O  
ANISOU  425  O  AVAL A  74      847   1903   1824    -13    295   -125       O  
ATOM    426  O  BVAL A  74      36.785   1.581  30.560  0.47 13.13           O  
ANISOU  426  O  BVAL A  74      958   1887   2146     37    332    448       O  
ATOM    427  CB AVAL A  74      35.084   5.025  30.002  0.52 13.92           C  
ANISOU  427  CB AVAL A  74     1208   2304   1776    602   -325    -25       C  
ATOM    428  CB BVAL A  74      35.263   4.427  30.348  0.47 13.90           C  
ANISOU  428  CB BVAL A  74     1049   2433   1797     -4     96     15       C  
ATOM    429  CG1AVAL A  74      36.069   5.288  31.141  0.52 15.42           C  
ANISOU  429  CG1AVAL A  74      788   3322   1748    193    183   -610       C  
ATOM    430  CG1BVAL A  74      36.535   4.752  31.133  0.47 26.26           C  
ANISOU  430  CG1BVAL A  74     2370   3078   4529   1156  -2015  -1119       C  
ATOM    431  CG2AVAL A  74      35.029   6.217  29.053  0.52 14.95           C  
ANISOU  431  CG2AVAL A  74     1409   2123   2147   -257    202     71       C  
ATOM    432  CG2BVAL A  74      35.020   5.625  29.449  0.47 14.79           C  
ANISOU  432  CG2BVAL A  74      650   2208   2763    215     92    147       C  
ATOM    433  N  AHIS A  75      34.854   2.064  30.858  0.52 12.27           N  
ANISOU  433  N  AHIS A  75     1010   2134   1520    -14    345    105       N  
ATOM    434  N  BHIS A  75      34.587   1.174  30.727  0.47 12.56           N  
ANISOU  434  N  BHIS A  75      945   1875   1953     70    258    319       N  
ATOM    435  CA AHIS A  75      35.058   0.973  31.785  0.52 13.89           C  
ANISOU  435  CA AHIS A  75     1127   2106   2046   -225     70    246       C  
ATOM    436  CA BHIS A  75      34.787  -0.071  31.447  0.47 12.58           C  
ANISOU  436  CA BHIS A  75     1259   1720   1801    200    353    157       C  
ATOM    437  C  AHIS A  75      35.799  -0.142  31.072  0.52 13.69           C  
ANISOU  437  C  AHIS A  75     1167   2167   1865    -13    203    605       C  
ATOM    438  C  BHIS A  75      35.546  -1.094  30.595  0.47 13.97           C  
ANISOU  438  C  BHIS A  75     1196   2215   1897    445    209    -44       C  
ATOM    439  O  AHIS A  75      36.795  -0.704  31.558  0.52 14.86           O  
ANISOU  439  O  AHIS A  75     1150   2314   2181    -25     38    616       O  
ATOM    440  O  BHIS A  75      36.301  -1.875  31.176  0.47 13.86           O  
ANISOU  440  O  BHIS A  75     1092   2116   2059    405    278     56       O  
ATOM    441  CB AHIS A  75      33.689   0.577  32.357  0.52 14.14           C  
ANISOU  441  CB AHIS A  75     1475   2246   1652   -269    373    170       C  
ATOM    442  CB BHIS A  75      33.468  -0.677  31.938  0.47 11.34           C  
ANISOU  442  CB BHIS A  75     1256   1565   1487    161    227    198       C  
ATOM    443  CG AHIS A  75      33.860  -0.597  33.241  0.52 14.77           C  
ANISOU  443  CG AHIS A  75     1446   2180   1987   -266    181    198       C  
ATOM    444  CG BHIS A  75      33.131  -0.354  33.339  0.47 10.24           C  
ANISOU  444  CG BHIS A  75      940   1477   1475     45     32     66       C  
ATOM    445  ND1AHIS A  75      34.254  -0.480  34.569  0.52 14.50           N  
ANISOU  445  ND1AHIS A  75     1321   2165   2024    -66     18    307       N  
ATOM    446  ND1BHIS A  75      33.537  -1.207  34.340  0.47 10.93           N  
ANISOU  446  ND1BHIS A  75     1139   1619   1394     33    402    197       N  
ATOM    447  CD2AHIS A  75      33.752  -1.898  32.944  0.52 17.20           C  
ANISOU  447  CD2AHIS A  75     2198   2215   2123   -709     60    333       C  
ATOM    448  CD2BHIS A  75      32.476   0.722  33.889  0.47 11.27           C  
ANISOU  448  CD2BHIS A  75      879   1620   1782    -85    346    -48       C  
ATOM    449  CE1AHIS A  75      34.361  -1.704  35.086  0.52 15.04           C  
ANISOU  449  CE1AHIS A  75     1831   1945   1940     27    502    121       C  
ATOM    450  CE1BHIS A  75      33.154  -0.668  35.480  0.47 11.76           C  
ANISOU  450  CE1BHIS A  75     1304   1709   1456   -309    388    -74       C  
ATOM    451  NE2AHIS A  75      34.038  -2.521  34.118  0.52 16.63           N  
ANISOU  451  NE2AHIS A  75     1964   2275   2077   -382    114    270       N  
ATOM    452  NE2BHIS A  75      32.495   0.489  35.233  0.47 13.03           N  
ANISOU  452  NE2BHIS A  75     1574   1707   1670   -128    282   -245       N  
ATOM    453  N  ASER A  76      35.330  -0.491  29.865  0.52 13.48           N  
ANISOU  453  N  ASER A  76     1249   1776   2095    102     81    402       N  
ATOM    454  N  BSER A  76      35.368  -1.113  29.274  0.47 14.58           N  
ANISOU  454  N  BSER A  76     1958   1707   1876    235    131   -129       N  
ATOM    455  CA ASER A  76      35.984  -1.599  29.144  0.52 15.15           C  
ANISOU  455  CA ASER A  76     1664   1562   2529    143    167    415       C  
ATOM    456  CA BSER A  76      36.249  -1.968  28.471  0.47 16.99           C  
ANISOU  456  CA BSER A  76     2385   1946   2124    200    527   -245       C  
ATOM    457  C  ASER A  76      37.436  -1.306  28.852  0.52 15.22           C  
ANISOU  457  C  ASER A  76     1582   1538   2662    416    199     47       C  
ATOM    458  C  BSER A  76      37.698  -1.564  28.606  0.47 18.20           C  
ANISOU  458  C  BSER A  76     2263   2247   2404    480    590    -54       C  
ATOM    459  O  ASER A  76      38.367  -2.100  29.084  0.52 16.14           O  
ANISOU  459  O  ASER A  76     1798   2123   2211    823    171   -147       O  
ATOM    460  O  BSER A  76      38.586  -2.420  28.493  0.47 20.44           O  
ANISOU  460  O  BSER A  76     2687   3057   2023   1014    844   -481       O  
ATOM    461  CB ASER A  76      35.222  -1.821  27.843  0.52 16.58           C  
ANISOU  461  CB ASER A  76     1701   1789   2811    361     53   -136       C  
ATOM    462  CB BSER A  76      35.772  -1.879  27.020  0.47 19.99           C  
ANISOU  462  CB BSER A  76     3445   2017   2134    -12    210   -581       C  
ATOM    463  OG ASER A  76      35.557  -2.899  27.018  0.52 23.15           O  
ANISOU  463  OG ASER A  76     3380   1977   3439   -302    909   -554       O  
ATOM    464  OG BSER A  76      36.256  -0.684  26.415  0.47 22.39           O  
ANISOU  464  OG BSER A  76     3058   2876   2575    306    625    384       O  
ATOM    465  N  AGLU A  77      37.686  -0.102  28.318  0.52 13.32           N  
ANISOU  465  N  AGLU A  77     1350   1901   1812    237    319    111       N  
ATOM    466  N  BGLU A  77      38.058  -0.304  28.859  0.47 16.46           N  
ANISOU  466  N  BGLU A  77     1658   2363   2234    202    370    385       N  
ATOM    467  CA AGLU A  77      39.059   0.313  28.008  0.52 16.14           C  
ANISOU  467  CA AGLU A  77     1378   2614   2139    131    400     92       C  
ATOM    468  CA BGLU A  77      39.495  -0.070  29.030  0.47 18.55           C  
ANISOU  468  CA BGLU A  77     1427   3120   2503    510    648    353       C  
ATOM    469  C  AGLU A  77      39.933   0.251  29.239  0.52 14.14           C  
ANISOU  469  C  AGLU A  77     1017   2054   2299    224    459    266       C  
ATOM    470  C  BGLU A  77      40.029  -0.342  30.415  0.47 18.30           C  
ANISOU  470  C  BGLU A  77     1573   2870   2510    -27    326     96       C  
ATOM    471  O  AGLU A  77      41.051  -0.300  29.215  0.52 16.58           O  
ANISOU  471  O  AGLU A  77     1296   2173   2829    578    485    284       O  
ATOM    472  O  BGLU A  77      41.178  -0.720  30.579  0.47 17.99           O  
ANISOU  472  O  BGLU A  77     1649   2359   2826     64    206    -13       O  
ATOM    473  CB AGLU A  77      38.978   1.707  27.366  0.52 16.81           C  
ANISOU  473  CB AGLU A  77     1039   3253   2094     39    633    805       C  
ATOM    474  CB BGLU A  77      39.783   1.397  28.698  0.47 22.41           C  
ANISOU  474  CB BGLU A  77     2095   3665   2756   -687     58    654       C  
ATOM    475  CG AGLU A  77      38.366   1.543  25.994  0.52 22.76           C  
ANISOU  475  CG AGLU A  77     2147   4614   1886    172    622    656       C  
ATOM    476  CG BGLU A  77      39.984   1.418  27.166  0.47 30.05           C  
ANISOU  476  CG BGLU A  77     3800   5004   2615   -968   -373   1227       C  
ATOM    477  CD AGLU A  77      39.128   0.659  25.027  0.52 31.60           C  
ANISOU  477  CD AGLU A  77     3115   6397   2497    811    770   -229       C  
ATOM    478  CD BGLU A  77      39.964   2.852  26.812  0.47 28.39           C  
ANISOU  478  CD BGLU A  77     3282   4858   2646  -1424   -317    971       C  
ATOM    479  OE1AGLU A  77      38.879  -0.557  24.886  0.52 36.19           O  
ANISOU  479  OE1AGLU A  77     3677   6706   3369    511   1681  -1381       O  
ATOM    480  OE1BGLU A  77      39.757   3.364  25.697  0.47 73.71           O  
ANISOU  480  OE1BGLU A  77    15311   7538   5158  -3381  -2999   4050       O  
ATOM    481  OE2AGLU A  77      40.035   1.175  24.344  0.52 40.27           O  
ANISOU  481  OE2AGLU A  77     4451   6412   4439   1427   2665    116       O  
ATOM    482  OE2BGLU A  77      40.242   3.668  27.747  0.47 45.96           O  
ANISOU  482  OE2BGLU A  77     5710   6452   5300   -900   1274  -2081       O  
ATOM    483  N  APHE A  78      39.466   0.773  30.358  0.52 13.90           N  
ANISOU  483  N  APHE A  78     1090   2117   2074    351    335    475       N  
ATOM    484  N  BPHE A  78      39.177  -0.129  31.416  0.47 19.49           N  
ANISOU  484  N  BPHE A  78     2156   2868   2381    906    294    233       N  
ATOM    485  CA APHE A  78      40.317   0.753  31.559  0.52 15.84           C  
ANISOU  485  CA APHE A  78     1408   2329   2280    355     27    465       C  
ATOM    486  CA BPHE A  78      39.506  -0.590  32.764  0.47 19.36           C  
ANISOU  486  CA BPHE A  78     2165   2947   2244   1026    232   -117       C  
ATOM    487  C  APHE A  78      40.575  -0.664  32.019  0.52 13.53           C  
ANISOU  487  C  APHE A  78     1072   2378   1689    399    452    358       C  
ATOM    488  C  BPHE A  78      39.900  -2.047  32.677  0.47 19.14           C  
ANISOU  488  C  BPHE A  78     2553   2979   1741   1157    -65   -126       C  
ATOM    489  O  APHE A  78      41.620  -0.920  32.612  0.52 13.65           O  
ANISOU  489  O  APHE A  78     1109   2014   2065    402    269    222       O  
ATOM    490  O  BPHE A  78      40.903  -2.464  33.244  0.47 18.98           O  
ANISOU  490  O  BPHE A  78     2079   3120   2014    960     92   -101       O  
ATOM    491  CB APHE A  78      39.640   1.538  32.670  0.52 17.71           C  
ANISOU  491  CB APHE A  78     2338   2091   2299    385    -28    246       C  
ATOM    492  CB BPHE A  78      38.333  -0.403  33.741  0.47 22.68           C  
ANISOU  492  CB BPHE A  78     2684   3261   2674   1168    815    267       C  
ATOM    493  CG APHE A  78      39.936   3.038  32.753  0.52 20.06           C  
ANISOU  493  CG APHE A  78     1659   2085   3878    349   -542    211       C  
ATOM    494  CG BPHE A  78      37.852   1.022  33.917  0.47 25.23           C  
ANISOU  494  CG BPHE A  78     2341   3402   3841    883    721   -905       C  
ATOM    495  CD1APHE A  78      38.856   3.897  32.902  0.52 19.18           C  
ANISOU  495  CD1APHE A  78     1523   2245   3519    148    -10   -462       C  
ATOM    496  CD1BPHE A  78      36.531   1.382  34.091  0.47 31.03           C  
ANISOU  496  CD1BPHE A  78     2570   4706   4515   1487    297  -1964       C  
ATOM    497  CD2APHE A  78      41.219   3.580  32.689  0.52 21.88           C  
ANISOU  497  CD2APHE A  78     1653   2606   4055    334    528   1115       C  
ATOM    498  CD2BPHE A  78      38.807   2.036  33.891  0.47 26.33           C  
ANISOU  498  CD2BPHE A  78     3605   3689   2710    164   1121   -616       C  
ATOM    499  CE1APHE A  78      39.024   5.261  32.994  0.52 22.33           C  
ANISOU  499  CE1APHE A  78     1780   2342   4363    297   -308  -1248       C  
ATOM    500  CE1BPHE A  78      36.190   2.723  34.162  0.47 31.71           C  
ANISOU  500  CE1BPHE A  78     2072   4746   5229   1437    152  -1959       C  
ATOM    501  CE2APHE A  78      41.379   4.966  32.781  0.52 25.68           C  
ANISOU  501  CE2APHE A  78     1628   2867   5263   -168   -254    412       C  
ATOM    502  CE2BPHE A  78      38.466   3.355  33.995  0.47 27.85           C  
ANISOU  502  CE2BPHE A  78     2839   3702   4040    228   -299   -537       C  
ATOM    503  CZ APHE A  78      40.293   5.810  32.931  0.52 23.56           C  
ANISOU  503  CZ APHE A  78     2247   2259   4448   -133     34     93       C  
ATOM    504  CZ BPHE A  78      37.136   3.706  34.165  0.47 35.91           C  
ANISOU  504  CZ BPHE A  78     3095   5036   5513    773   -373  -1284       C  
ATOM    505  N  AMET A  79      39.643  -1.583  31.847  0.52 15.34           N  
ANISOU  505  N  AMET A  79     1129   2252   2448    424     44    569       N  
ATOM    506  N  BMET A  79      39.115  -2.826  31.943  0.47 16.77           N  
ANISOU  506  N  BMET A  79     1751   2778   1845    865    427    165       N  
ATOM    507  CA AMET A  79      39.836  -2.946  32.383  0.52 16.99           C  
ANISOU  507  CA AMET A  79     1604   2329   2521    426     38    627       C  
ATOM    508  CA BMET A  79      39.341  -4.254  31.780  0.47 18.17           C  
ANISOU  508  CA BMET A  79     1979   2751   2174    939    348    163       C  
ATOM    509  C  AMET A  79      40.927  -3.669  31.613  0.52 16.97           C  
ANISOU  509  C  AMET A  79     1852   2057   2537    350    -91     91       C  
ATOM    510  C  BMET A  79      40.738  -4.469  31.204  0.47 17.90           C  
ANISOU  510  C  BMET A  79     2169   2675   1956    934    550    -43       C  
ATOM    511  O  AMET A  79      41.538  -4.627  32.146  0.52 17.02           O  
ANISOU  511  O  AMET A  79     1574   1906   2987    182   -184    126       O  
ATOM    512  O  BMET A  79      41.443  -5.351  31.729  0.47 14.58           O  
ANISOU  512  O  BMET A  79     1335   2527   1678    204    255     98       O  
ATOM    513  CB AMET A  79      38.547  -3.751  32.470  0.52 20.10           C  
ANISOU  513  CB AMET A  79     2036   2570   3031     91    240    931       C  
ATOM    514  CB BMET A  79      38.229  -4.921  30.980  0.47 24.31           C  
ANISOU  514  CB BMET A  79     2313   3076   3849    769    -25   -527       C  
ATOM    515  CG AMET A  79      37.593  -3.207  33.536  0.52 23.51           C  
ANISOU  515  CG AMET A  79     1929   3616   3388    514    523   1255       C  
ATOM    516  CG BMET A  79      38.399  -6.435  30.742  0.47 27.21           C  
ANISOU  516  CG BMET A  79     2524   2960   4853    712   -301   -299       C  
ATOM    517  SD AMET A  79      38.211  -3.235  35.243  0.52 24.73           S  
ANISOU  517  SD AMET A  79     2404   3784   3209    198    605    515       S  
ATOM    518  SD BMET A  79      37.156  -7.073  29.608  0.47 58.58           S  
ANISOU  518  SD BMET A  79     4494   3343  14422     53  -4685  -1700       S  
ATOM    519  CE AMET A  79      37.828  -4.945  35.649  0.52 85.07           C  
ANISOU  519  CE AMET A  79    27909   2082   2332      0   -856      0       C  
ATOM    520  CE BMET A  79      36.534  -5.548  28.901  0.47 50.27           C  
ANISOU  520  CE BMET A  79     2164   9752   7184   -353    189   5512       C  
ATOM    521  N  AHIS A  80      41.305  -3.125  30.447  0.52 17.63           N  
ANISOU  521  N  AHIS A  80     2220   2498   1979    519   -210   -274       N  
ATOM    522  N  BHIS A  80      41.161  -3.687  30.211  0.47 16.96           N  
ANISOU  522  N  BHIS A  80     1665   2698   2081    906     97    199       N  
ATOM    523  CA AHIS A  80      42.419  -3.594  29.632  0.52 18.25           C  
ANISOU  523  CA AHIS A  80     2282   2382   2269    574    -62    -43       C  
ATOM    524  CA BHIS A  80      42.492  -3.926  29.629  0.47 16.50           C  
ANISOU  524  CA BHIS A  80     1694   2502   2075    516    200    -15       C  
ATOM    525  C  AHIS A  80      43.738  -3.405  30.380  0.52 17.61           C  
ANISOU  525  C  AHIS A  80     2212   2427   2053    627    116   -401       C  
ATOM    526  C  BHIS A  80      43.658  -3.588  30.541  0.47 13.31           C  
ANISOU  526  C  BHIS A  80     1523   1595   1938    411    421    102       C  
ATOM    527  O  AHIS A  80      44.775  -3.951  30.036  0.52 17.20           O  
ANISOU  527  O  AHIS A  80     2239   2472   1825    621     79   -580       O  
ATOM    528  O  BHIS A  80      44.685  -4.277  30.413  0.47 15.11           O  
ANISOU  528  O  BHIS A  80     2011   1974   1757   1007      7    113       O  
ATOM    529  CB AHIS A  80      42.559  -2.884  28.287  0.52 22.36           C  
ANISOU  529  CB AHIS A  80     2949   3398   2149   1014    131    113       C  
ATOM    530  CB BHIS A  80      42.698  -3.194  28.286  0.47 21.04           C  
ANISOU  530  CB BHIS A  80     2998   3371   1625   1163    488   -124       C  
ATOM    531  CG AHIS A  80      41.778  -3.374  27.130  0.52 29.14           C  
ANISOU  531  CG AHIS A  80     4058   4810   2203   1380   -186   -538       C  
ATOM    532  CG BHIS A  80      41.599  -3.442  27.318  0.47 25.71           C  
ANISOU  532  CG BHIS A  80     3348   4706   1714   1205    272   -476       C  
ATOM    533  ND1AHIS A  80      42.025  -4.568  26.495  0.52 31.28           N  
ANISOU  533  ND1AHIS A  80     4021   5535   2328   1426     92  -1154       N  
ATOM    534  ND1BHIS A  80      40.959  -4.647  27.169  0.47 28.03           N  
ANISOU  534  ND1BHIS A  80     2931   5334   2384    741    218   -559       N  
ATOM    535  CD2AHIS A  80      40.739  -2.792  26.477  0.52 29.46           C  
ANISOU  535  CD2AHIS A  80     4038   5311   1845   1276   -248   -488       C  
ATOM    536  CD2BHIS A  80      41.032  -2.592  26.428  0.47 28.48           C  
ANISOU  536  CD2BHIS A  80     3459   5420   1943   1502    -26   -408       C  
ATOM    537  CE1AHIS A  80      41.151  -4.694  25.505  0.52 34.36           C  
ANISOU  537  CE1AHIS A  80     4481   5868   2705   1401   -321  -1240       C  
ATOM    538  CE1BHIS A  80      40.034  -4.531  26.231  0.47 33.26           C  
ANISOU  538  CE1BHIS A  80     4153   5865   2620   1056   -527   -995       C  
ATOM    539  NE2AHIS A  80      40.361  -3.633  25.465  0.52 31.54           N  
ANISOU  539  NE2AHIS A  80     3692   6058   2234   1255     79  -1137       N  
ATOM    540  NE2BHIS A  80      40.061  -3.293  25.760  0.47 28.99           N  
ANISOU  540  NE2BHIS A  80     2595   5826   2595   1903    212  -1008       N  
ATOM    541  N   ASP A  81      43.651  -2.609  31.442  1.00 15.37           N  
ANISOU  541  N   ASP A  81     2074   1984   1784    654    406    -13       N  
ATOM    542  CA  ASP A  81      44.747  -2.244  32.299  1.00 15.50           C  
ANISOU  542  CA  ASP A  81     2327   1843   1719    543    298   -114       C  
ATOM    543  C   ASP A  81      44.747  -2.978  33.648  1.00 15.74           C  
ANISOU  543  C   ASP A  81     2002   2066   1914    860    401    116       C  
ATOM    544  O   ASP A  81      45.633  -2.728  34.483  1.00 16.63           O  
ANISOU  544  O   ASP A  81     2302   2243   1772    777    369     39       O  
ATOM    545  CB  ASP A  81      44.671  -0.727  32.564  1.00 18.30           C  
ANISOU  545  CB  ASP A  81     3266   1790   1897    488    619    -36       C  
ATOM    546  CG  ASP A  81      44.700   0.128  31.329  1.00 14.32           C  
ANISOU  546  CG  ASP A  81     1801   1925   1715    445    248    -91       C  
ATOM    547  OD1 ASP A  81      44.205   1.294  31.448  1.00 14.96           O  
ANISOU  547  OD1 ASP A  81     1947   1811   1928    283    435    -55       O  
ATOM    548  OD2 ASP A  81      45.161  -0.310  30.253  1.00 15.21           O  
ANISOU  548  OD2 ASP A  81     1819   2186   1773    499    274   -156       O  
ATOM    549  N   HIS A  82      43.808  -3.869  33.863  1.00 16.59           N  
ANISOU  549  N   HIS A  82     1797   2615   1892    789    602    254       N  
ATOM    550  CA  HIS A  82      43.594  -4.460  35.185  1.00 17.28           C  
ANISOU  550  CA  HIS A  82     1641   3112   1811    677    439    336       C  
ATOM    551  C   HIS A  82      44.797  -5.291  35.642  1.00 16.69           C  
ANISOU  551  C   HIS A  82     1935   2378   2027    623    231     73       C  
ATOM    552  O   HIS A  82      45.258  -5.126  36.777  1.00 17.33           O  
ANISOU  552  O   HIS A  82     2162   2477   1945    801    240    245       O  
ATOM    553  CB AHIS A  82      42.371  -5.408  35.100  0.52 19.50           C  
ANISOU  553  CB AHIS A  82     1797   3293   2319    533    419    624       C  
ATOM    554  CB BHIS A  82      42.215  -5.086  35.249  0.47 17.64           C  
ANISOU  554  CB BHIS A  82     1902   2887   1915    399    332    349       C  
ATOM    555  CG AHIS A  82      41.690  -6.053  36.272  0.52 18.12           C  
ANISOU  555  CG AHIS A  82     2186   2352   2346    479    477    357       C  
ATOM    556  CG BHIS A  82      41.633  -5.010  36.634  0.47 14.55           C  
ANISOU  556  CG BHIS A  82     1632   1632   2263    350    430    172       C  
ATOM    557  ND1AHIS A  82      41.372  -7.385  36.512  0.52 21.61           N  
ANISOU  557  ND1AHIS A  82     3292   2366   2554     -8     69     -5       N  
ATOM    558  ND1BHIS A  82      41.366  -3.959  37.456  0.47 14.37           N  
ANISOU  558  ND1BHIS A  82     1068   1975   2418     68    516    -25       N  
ATOM    559  CD2AHIS A  82      41.222  -5.430  37.389  0.52 16.37           C  
ANISOU  559  CD2AHIS A  82     1529   2304   2387   -180    402     84       C  
ATOM    560  CD2BHIS A  82      41.194  -6.105  37.302  0.47 17.04           C  
ANISOU  560  CD2BHIS A  82     2340   1982   2153   -426    369     35       C  
ATOM    561  CE1AHIS A  82      40.780  -7.495  37.679  0.52 20.81           C  
ANISOU  561  CE1AHIS A  82     2891   2231   2786    -81      8    605       C  
ATOM    562  CE1BHIS A  82      40.802  -4.397  38.586  0.47 15.05           C  
ANISOU  562  CE1BHIS A  82     1243   2073   2403   -194    550    -59       C  
ATOM    563  NE2AHIS A  82      40.648  -6.307  38.263  0.52 20.10           N  
ANISOU  563  NE2AHIS A  82     2364   2732   2542   -288    654    227       N  
ATOM    564  NE2BHIS A  82      40.708  -5.703  38.525  0.47 15.35           N  
ANISOU  564  NE2BHIS A  82     1373   2068   2393    -25    429    103       N  
ATOM    565  N   ALA A  83      45.373  -6.096  34.768  1.00 17.28           N  
ANISOU  565  N   ALA A  83     2060   2292   2215    667    145     32       N  
ATOM    566  CA  ALA A  83      46.556  -6.877  35.117  1.00 16.69           C  
ANISOU  566  CA  ALA A  83     2062   1731   2548    491     78    -17       C  
ATOM    567  C   ALA A  83      47.737  -5.931  35.389  1.00 15.15           C  
ANISOU  567  C   ALA A  83     1990   1904   1864    481    362     70       C  
ATOM    568  O   ALA A  83      48.544  -6.219  36.269  1.00 15.77           O  
ANISOU  568  O   ALA A  83     2014   1852   2124    558    198      1       O  
ATOM    569  CB  ALA A  83      46.842  -7.904  34.012  1.00 21.24           C  
ANISOU  569  CB  ALA A  83     2827   1969   3275    620     76   -530       C  
ATOM    570  N   ASP A  84      47.859  -4.859  34.599  1.00 15.28           N  
ANISOU  570  N   ASP A  84     1838   1939   2029    562    508    120       N  
ATOM    571  CA  ASP A  84      49.000  -3.953  34.834  1.00 14.52           C  
ANISOU  571  CA  ASP A  84     1600   2112   1803    643    512    210       C  
ATOM    572  C   ASP A  84      48.947  -3.327  36.226  1.00 15.80           C  
ANISOU  572  C   ASP A  84     2341   1869   1795    529    493    199       C  
ATOM    573  O   ASP A  84      49.961  -3.017  36.820  1.00 18.19           O  
ANISOU  573  O   ASP A  84     2714   2337   1860     -3    532      4       O  
ATOM    574  CB  ASP A  84      49.048  -2.864  33.801  1.00 16.09           C  
ANISOU  574  CB  ASP A  84     2138   2106   1869    416    484    253       C  
ATOM    575  CG  ASP A  84      49.536  -3.309  32.433  1.00 18.63           C  
ANISOU  575  CG  ASP A  84     2310   2794   1975    774    646    248       C  
ATOM    576  OD1 ASP A  84      49.254  -2.636  31.445  1.00 19.09           O  
ANISOU  576  OD1 ASP A  84     2396   2913   1944    538    664    308       O  
ATOM    577  OD2 ASP A  84      50.226  -4.369  32.365  1.00 27.84           O  
ANISOU  577  OD2 ASP A  84     4181   3967   2431   2301   1355    588       O  
ATOM    578  N   TYR A  85      47.737  -3.108  36.739  1.00 15.50           N  
ANISOU  578  N   TYR A  85     2600   1605   1684    472    696     83       N  
ATOM    579  CA  TYR A  85      47.525  -2.554  38.070  1.00 15.97           C  
ANISOU  579  CA  TYR A  85     2897   1448   1724    332    716      6       C  
ATOM    580  C   TYR A  85      47.497  -3.590  39.194  1.00 16.56           C  
ANISOU  580  C   TYR A  85     2819   1621   1852    332    813    142       C  
ATOM    581  O   TYR A  85      47.212  -3.240  40.312  1.00 21.84           O  
ANISOU  581  O   TYR A  85     4810   1805   1682    774    595    161       O  
ATOM    582  CB  TYR A  85      46.280  -1.643  38.043  1.00 16.50           C  
ANISOU  582  CB  TYR A  85     2998   1582   1689    410    844     89       C  
ATOM    583  CG  TYR A  85      46.606  -0.199  37.769  1.00 14.88           C  
ANISOU  583  CG  TYR A  85     2492   1550   1613    375    686     18       C  
ATOM    584  CD1 TYR A  85      46.451   0.372  36.511  1.00 16.67           C  
ANISOU  584  CD1 TYR A  85     3383   1419   1534    240    567   -113       C  
ATOM    585  CD2 TYR A  85      47.072   0.655  38.768  1.00 14.04           C  
ANISOU  585  CD2 TYR A  85     2277   1554   1504    527    569    154       C  
ATOM    586  CE1 TYR A  85      46.737   1.696  36.208  1.00 14.79           C  
ANISOU  586  CE1 TYR A  85     2609   1371   1638    323    185     -4       C  
ATOM    587  CE2 TYR A  85      47.378   1.951  38.518  1.00 14.51           C  
ANISOU  587  CE2 TYR A  85     2670   1413   1431    613    439     38       C  
ATOM    588  CZ  TYR A  85      47.203   2.489  37.238  1.00 14.26           C  
ANISOU  588  CZ  TYR A  85     2709   1306   1402    626    401    -62       C  
ATOM    589  OH  TYR A  85      47.538   3.808  37.048  1.00 13.40           O  
ANISOU  589  OH  TYR A  85     2122   1482   1486    331    193    -26       O  
ATOM    590  N   GLY A  86      47.853  -4.838  38.897  1.00 14.14           N  
ANISOU  590  N   GLY A  86     2067   1531   1776    242    465    239       N  
ATOM    591  CA  GLY A  86      48.077  -5.812  39.931  1.00 14.85           C  
ANISOU  591  CA  GLY A  86     2022   1576   2043    119    187    265       C  
ATOM    592  C   GLY A  86      46.925  -6.785  40.128  1.00 15.20           C  
ANISOU  592  C   GLY A  86     1955   1651   2170    129    417    332       C  
ATOM    593  O   GLY A  86      47.009  -7.552  41.100  1.00 17.03           O  
ANISOU  593  O   GLY A  86     2556   1901   2014     62    337    365       O  
ATOM    594  N   PHE A  87      45.927  -6.807  39.325  1.00 17.25           N  
ANISOU  594  N   PHE A  87     1753   2330   2469    -30    420    581       N  
ATOM    595  CA  PHE A  87      44.790  -7.697  39.545  1.00 21.41           C  
ANISOU  595  CA  PHE A  87     2337   3384   2413   -812    649    443       C  
ATOM    596  C   PHE A  87      44.812  -8.813  38.534  1.00 24.88           C  
ANISOU  596  C   PHE A  87     3083   3245   3126   -856    255    178       C  
ATOM    597  O   PHE A  87      45.389  -8.651  37.439  1.00 29.07           O  
ANISOU  597  O   PHE A  87     5020   3085   2942  -1570    609   -395       O  
ATOM    598  CB  PHE A  87      43.511  -6.860  39.416  1.00 25.11           C  
ANISOU  598  CB  PHE A  87     1816   4895   2830   -635     96   -708       C  
ATOM    599  CG  PHE A  87      43.384  -5.672  40.371  1.00 25.80           C  
ANISOU  599  CG  PHE A  87     1315   5506   2983   -204    109  -1075       C  
ATOM    600  CD1 PHE A  87      42.663  -5.876  41.552  1.00 29.69           C  
ANISOU  600  CD1 PHE A  87     1475   6674   3131    224    289   -948       C  
ATOM    601  CD2 PHE A  87      43.973  -4.452  40.112  1.00 24.63           C  
ANISOU  601  CD2 PHE A  87     1753   4513   3091    775   -321   -866       C  
ATOM    602  CE1 PHE A  87      42.522  -4.835  42.449  1.00 32.14           C  
ANISOU  602  CE1 PHE A  87     1696   7291   3224    336    532  -1239       C  
ATOM    603  CE2 PHE A  87      43.844  -3.402  41.021  1.00 25.88           C  
ANISOU  603  CE2 PHE A  87     1557   5016   3261    949   -265  -1102       C  
ATOM    604  CZ  PHE A  87      43.168  -3.616  42.207  1.00 32.19           C  
ANISOU  604  CZ  PHE A  87     1965   6786   3481    570    145  -1537       C  
ATOM    605  N  APRO A  88      44.316  -9.999  38.846  0.50 26.40           N  
ANISOU  605  N  APRO A  88     3484   3338   3210   -900    -67    473       N  
ATOM    606  N  BPRO A  88      44.070  -9.879  38.786  0.50 28.36           N  
ANISOU  606  N  BPRO A  88     4206   3422   3148  -1297   -305    718       N  
ATOM    607  CA APRO A  88      44.125 -10.997  37.785  0.50 27.98           C  
ANISOU  607  CA APRO A  88     3830   3080   3720   -658   -337    293       C  
ATOM    608  CA BPRO A  88      43.854 -10.948  37.804  0.50 31.19           C  
ANISOU  608  CA BPRO A  88     4771   3375   3705  -1413   -609    548       C  
ATOM    609  C  APRO A  88      43.182 -10.437  36.719  0.50 27.91           C  
ANISOU  609  C  APRO A  88     4350   2969   3285   -164   -256   -117       C  
ATOM    610  C  BPRO A  88      43.510 -10.434  36.407  0.50 31.56           C  
ANISOU  610  C  BPRO A  88     5209   3240   3542   -510   -715     76       C  
ATOM    611  O  APRO A  88      42.138  -9.893  37.044  0.50 26.88           O  
ANISOU  611  O  APRO A  88     2948   4103   3163  -1133    -13    792       O  
ATOM    612  O  BPRO A  88      42.691  -9.521  36.365  0.50 30.74           O  
ANISOU  612  O  BPRO A  88     3118   4840   3723   -553   -545     90       O  
ATOM    613  CB APRO A  88      43.472 -12.189  38.488  0.50 32.14           C  
ANISOU  613  CB APRO A  88     4066   3584   4561  -1321  -1202    870       C  
ATOM    614  CB BPRO A  88      42.597 -11.652  38.337  0.50 36.42           C  
ANISOU  614  CB BPRO A  88     4581   4766   4492  -2091  -1183    800       C  
ATOM    615  CG APRO A  88      43.850 -12.036  39.924  0.50 26.13           C  
ANISOU  615  CG APRO A  88     1878   3647   4402   -986   -858   1173       C  
ATOM    616  CG BPRO A  88      42.679 -11.474  39.812  0.50 34.53           C  
ANISOU  616  CG BPRO A  88     4252   4558   4308  -2082   -663   1235       C  
ATOM    617  CD APRO A  88      43.939 -10.550  40.155  0.50 29.82           C  
ANISOU  617  CD APRO A  88     4238   3663   3430   -763   -273   1012       C  
ATOM    618  CD BPRO A  88      43.333 -10.146  40.037  0.50 31.60           C  
ANISOU  618  CD BPRO A  88     4181   4222   3604  -1695    -23    877       C  
ATOM    619  N  ASER A  89      43.588 -10.615  35.467  0.50 32.27           N  
ANISOU  619  N  ASER A  89     5005   3920   3335   -101     20   -101       N  
ATOM    620  N  BSER A  89      44.141 -11.032  35.397  0.50 36.73           N  
ANISOU  620  N  BSER A  89     7495   2835   3624    511  -1208   -532       N  
ATOM    621  CA ASER A  89      42.853 -10.132  34.319  0.50 37.33           C  
ANISOU  621  CA ASER A  89     5425   5533   3227    655   -432   -750       C  
ATOM    622  CA BSER A  89      43.991 -10.650  33.995  0.50 39.85           C  
ANISOU  622  CA BSER A  89     6469   5132   3540     -1   -800   -202       C  
ATOM    623  C  ASER A  89      41.409 -10.609  34.381  0.50 37.87           C  
ANISOU  623  C  ASER A  89     4722   6340   3325   1646    349  -1235       C  
ATOM    624  C  BSER A  89      42.568 -10.922  33.499  0.50 43.23           C  
ANISOU  624  C  BSER A  89     6227   6348   3852    403   -800   -280       C  
ATOM    625  O  ASER A  89      41.092 -11.634  34.951  0.50 36.09           O  
ANISOU  625  O  ASER A  89     3065   6651   3997   1663    -15   -797       O  
ATOM    626  O  BSER A  89      41.954 -11.913  33.895  0.50 46.75           O  
ANISOU  626  O  BSER A  89     6945   5778   5039   -398  -2989   -334       O  
ATOM    627  CB ASER A  89      43.425 -10.615  32.980  0.50 37.34           C  
ANISOU  627  CB ASER A  89     4721   6186   3282    238    345     -3       C  
ATOM    628  CB BSER A  89      44.985 -11.389  33.099  0.50 43.35           C  
ANISOU  628  CB BSER A  89     6295   5712   4463   -285    318    353       C  
ATOM    629  OG ASER A  89      44.655  -9.967  32.734  0.50 43.66           O  
ANISOU  629  OG ASER A  89     6931   5354   4302  -1444    490   1277       O  
ATOM    630  OG BSER A  89      46.156 -10.648  32.823  0.50 50.45           O  
ANISOU  630  OG BSER A  89     6025   5993   7152   -567   -225     46       O  
ATOM    631  N  ACYS A  90      40.618  -9.780  33.735  0.50 44.37           N  
ANISOU  631  N  ACYS A  90     5469   6925   4467   1521   -214   -353       N  
ATOM    632  N  BCYS A  90      42.090 -10.029  32.639  0.50 43.05           N  
ANISOU  632  N  BCYS A  90     5551   6899   3905   1020    112     64       N  
ATOM    633  CA ACYS A  90      39.195  -9.925  33.635  0.50 51.21           C  
ANISOU  633  CA ACYS A  90     5400   8046   6012   2160   -798  -1169       C  
ATOM    634  CA BCYS A  90      40.707 -10.082  32.161  0.50 52.21           C  
ANISOU  634  CA BCYS A  90     6032   8201   5606   1704   -906   -690       C  
ATOM    635  C  ACYS A  90      38.683 -10.552  32.348  0.50 53.01           C  
ANISOU  635  C  ACYS A  90     5333   8472   6337   1843   -665  -1585       C  
ATOM    636  C  BCYS A  90      40.570  -9.648  30.704  0.50 56.61           C  
ANISOU  636  C  BCYS A  90     6232  10091   5184   1565  -1283  -1266       C  
ATOM    637  O  ACYS A  90      37.805  -9.925  31.751  0.50 57.58           O  
ANISOU  637  O  ACYS A  90     5187  11080   5610   4119   -460  -3773       O  
ATOM    638  O  BCYS A  90      41.432  -8.937  30.175  0.50 56.61           O  
ANISOU  638  O  BCYS A  90     5567  13061   2882   1260   -755  -2001       O  
ATOM    639  CB ACYS A  90      38.575  -8.504  33.739  0.50 54.76           C  
ANISOU  639  CB ACYS A  90     6110   8131   6564   2420  -1360  -1404       C  
ATOM    640  CB BCYS A  90      39.847  -9.196  33.073  0.50 49.25           C  
ANISOU  640  CB BCYS A  90     5028   8082   5601    717   -217   -431       C  
ATOM    641  SG ACYS A  90      37.465  -8.546  35.156  0.50 48.22           S  
ANISOU  641  SG ACYS A  90     6967   5357   5995   2862  -1372  -1057       S  
ATOM    642  SG BCYS A  90      38.294  -9.903  33.661  0.50 62.23           S  
ANISOU  642  SG BCYS A  90     4391   9964   9289   -665   -901  -1674       S  
ATOM    643  N  AGLU A  91      39.205 -11.705  31.968  0.50 46.87           N  
ANISOU  643  N  AGLU A  91     4172   7629   6008   1098   -652   -965       N  
ATOM    644  N  BGLU A  91      39.505 -10.063  30.033  0.50 60.69           N  
ANISOU  644  N  BGLU A  91     6229  10655   6178   1428  -1465  -1659       N  
ATOM    645  CA AGLU A  91      38.887 -12.318  30.683  0.50 49.91           C  
ANISOU  645  CA AGLU A  91     4429   8315   6221   2621  -1290  -1389       C  
ATOM    646  CA BGLU A  91      39.102  -9.633  28.701  0.50 58.14           C  
ANISOU  646  CA BGLU A  91     4373  11166   6552    207  -1526   -964       C  
ATOM    647  C  AGLU A  91      37.393 -12.532  30.442  0.50 50.93           C  
ANISOU  647  C  AGLU A  91     4612   8749   5992   1910  -1255  -1446       C  
ATOM    648  C  BGLU A  91      38.027 -10.557  28.116  0.50 56.23           C  
ANISOU  648  C  BGLU A  91     4018  10558   6787    577   -778  -1724       C  
ATOM    649  O  AGLU A  91      36.923 -13.670  30.398  0.50 60.04           O  
ANISOU  649  O  AGLU A  91     7055   9560   6199    273  -2268    220       O  
ATOM    650  O  BGLU A  91      38.331 -11.334  27.208  0.50 61.87           O  
ANISOU  650  O  BGLU A  91     4938  12611   5960   -888    806  -2065       O  
ATOM    651  CB AGLU A  91      39.659 -13.634  30.485  0.50 55.91           C  
ANISOU  651  CB AGLU A  91     5683   8071   7489   2824  -2451  -1791       C  
ATOM    652  CB BGLU A  91      40.269  -9.574  27.710  0.50 62.06           C  
ANISOU  652  CB BGLU A  91     4516  11940   7126   -300  -1248   -633       C  
ATOM    653  CG AGLU A  91      39.785 -14.640  31.599  0.50 49.12           C  
ANISOU  653  CG AGLU A  91     3255   8788   6622   3401  -2267  -2037       C  
ATOM    654  CG BGLU A  91      39.864  -9.137  26.310  0.50 65.43           C  
ANISOU  654  CG BGLU A  91     5689  12201   6971  -1166  -1221   -426       C  
ATOM    655  CD AGLU A  91      38.519 -15.428  31.864  0.50 54.94           C  
ANISOU  655  CD AGLU A  91     5172   8816   6887   1709  -2373  -2587       C  
ATOM    656  CD BGLU A  91      40.555  -9.914  25.205  0.50 64.95           C  
ANISOU  656  CD BGLU A  91     5068  12504   7104  -1638   -988   -541       C  
ATOM    657  OE1AGLU A  91      38.494 -16.650  31.630  0.50 62.42           O  
ANISOU  657  OE1AGLU A  91     9106   9122   5489   1231  -2948  -3219       O  
ATOM    658  OE1BGLU A  91      41.676 -10.422  25.413  0.50 59.90           O  
ANISOU  658  OE1BGLU A  91     3643  11864   7251  -3215   -655   -631       O  
ATOM    659  OE2AGLU A  91      37.516 -14.816  32.295  0.50 53.93           O  
ANISOU  659  OE2AGLU A  91     4309   9528   6653    505  -1262  -2265       O  
ATOM    660  OE2BGLU A  91      39.949 -10.012  24.111  0.50 70.50           O  
ANISOU  660  OE2BGLU A  91     5738  13833   7215   -348  -1314  -1001       O  
ATOM    661  N  AGLY A  92      36.589 -11.482  30.226  0.50 51.16           N  
ANISOU  661  N  AGLY A  92     3804  10052   5583   2761   -239  -1890       N  
ATOM    662  N  BGLY A  92      36.809 -10.434  28.649  0.50 53.88           N  
ANISOU  662  N  BGLY A  92     3895   9576   7000   1125  -1033  -1950       N  
ATOM    663  CA AGLY A  92      35.163 -11.570  30.044  0.50 52.28           C  
ANISOU  663  CA AGLY A  92     4035   9986   5843   1684   -664  -1142       C  
ATOM    664  CA BGLY A  92      35.664 -11.272  28.363  0.50 49.97           C  
ANISOU  664  CA BGLY A  92     3658   9016   6312   1384   -927  -1612       C  
ATOM    665  C  AGLY A  92      34.387 -10.885  28.969  0.50 50.44           C  
ANISOU  665  C  AGLY A  92     4258   8914   5995   1491  -1252  -1786       C  
ATOM    666  C  BGLY A  92      34.535 -10.607  27.608  0.50 48.23           C  
ANISOU  666  C  BGLY A  92     3985   8198   6141   1548  -1001  -2073       C  
ATOM    667  O  AGLY A  92      34.465  -9.664  28.748  0.50 55.29           O  
ANISOU  667  O  AGLY A  92     5851   8725   6434   1259  -2891  -2269       O  
ATOM    668  O  BGLY A  92      34.546  -9.397  27.361  0.50 43.13           O  
ANISOU  668  O  BGLY A  92     3394   7848   5144   2047    532  -2980       O  
ATOM    669  N  ALYS A  93      33.530 -11.598  28.209  0.50 43.38           N  
ANISOU  669  N  ALYS A  93     3310   7759   5414   2450    -88  -2730       N  
ATOM    670  N  BLYS A  93      33.548 -11.439  27.242  0.50 43.19           N  
ANISOU  670  N  BLYS A  93     3275   7597   5536   2396   -397  -3144       N  
ATOM    671  CA ALYS A  93      32.825 -10.911  27.124  0.50 38.66           C  
ANISOU  671  CA ALYS A  93     2912   6687   5088   1711   -130  -3038       C  
ATOM    672  CA BLYS A  93      32.460 -10.994  26.399  0.50 40.63           C  
ANISOU  672  CA BLYS A  93     3409   6532   5494   2343   -338  -3030       C  
ATOM    673  C  ALYS A  93      31.689  -9.990  27.559  0.50 33.27           C  
ANISOU  673  C  ALYS A  93     2593   5163   4885    979      0  -2776       C  
ATOM    674  C  BLYS A  93      31.463 -10.153  27.204  0.50 32.64           C  
ANISOU  674  C  BLYS A  93     2693   4997   4712   1135    -38  -2521       C  
ATOM    675  O  ALYS A  93      30.923 -10.202  28.487  0.50 30.66           O  
ANISOU  675  O  ALYS A  93     3319   4963   3369   1864   -496  -2403       O  
ATOM    676  O  BLYS A  93      30.720 -10.606  28.061  0.50 32.53           O  
ANISOU  676  O  BLYS A  93     4085   4638   3636   1217   -418  -1935       O  
ATOM    677  CB ALYS A  93      32.244 -11.921  26.118  0.50 42.79           C  
ANISOU  677  CB ALYS A  93     5374   5553   5331   2182   -498  -3048       C  
ATOM    678  CB BLYS A  93      31.692 -12.124  25.713  0.50 39.97           C  
ANISOU  678  CB BLYS A  93     4440   6427   4319   2700   -625  -3185       C  
ATOM    679  N   PHE A  94      31.549  -8.900  26.816  1.00 31.21           N  
ANISOU  679  N   PHE A  94     2210   4972   4678    140    621  -2808       N  
ATOM    680  CA  PHE A  94      30.507  -7.930  27.144  1.00 25.00           C  
ANISOU  680  CA  PHE A  94     2108   3715   3676   -442   1195  -1726       C  
ATOM    681  C   PHE A  94      29.158  -8.472  26.740  1.00 22.60           C  
ANISOU  681  C   PHE A  94     2218   2854   3514   -248    680  -1369       C  
ATOM    682  O   PHE A  94      29.079  -9.146  25.734  1.00 24.11           O  
ANISOU  682  O   PHE A  94     2915   3215   3029   -577   1028  -1186       O  
ATOM    683  CB  PHE A  94      30.825  -6.694  26.337  1.00 29.20           C  
ANISOU  683  CB  PHE A  94     3161   4346   3586  -1295   2080  -1747       C  
ATOM    684  CG  PHE A  94      29.853  -5.589  26.442  1.00 23.96           C  
ANISOU  684  CG  PHE A  94     3030   3392   2680  -1717   1179   -940       C  
ATOM    685  CD1 PHE A  94      29.583  -4.997  27.692  1.00 18.67           C  
ANISOU  685  CD1 PHE A  94     2705   2074   2313   -847    540   -379       C  
ATOM    686  CD2 PHE A  94      29.193  -5.169  25.338  1.00 28.90           C  
ANISOU  686  CD2 PHE A  94     4904   4001   2075  -2332   1063   -512       C  
ATOM    687  CE1 PHE A  94      28.650  -4.010  27.735  1.00 17.31           C  
ANISOU  687  CE1 PHE A  94     2411   2135   2032   -895     62    171       C  
ATOM    688  CE2 PHE A  94      28.277  -4.149  25.391  1.00 26.29           C  
ANISOU  688  CE2 PHE A  94     3948   4009   2032  -2690   -106     91       C  
ATOM    689  CZ  PHE A  94      28.022  -3.563  26.611  1.00 23.57           C  
ANISOU  689  CZ  PHE A  94     4012   2640   2303  -1306   -685    233       C  
ATOM    690  N   ASN A  95      28.144  -8.127  27.529  1.00 16.33           N  
ANISOU  690  N   ASN A  95     1948   1961   2296    -81    384   -201       N  
ATOM    691  CA  ASN A  95      26.772  -8.469  27.183  1.00 16.12           C  
ANISOU  691  CA  ASN A  95     2039   1769   2317      0     95     18       C  
ATOM    692  C   ASN A  95      25.966  -7.191  26.945  1.00 15.02           C  
ANISOU  692  C   ASN A  95     1921   1704   2081    -96    456    -73       C  
ATOM    693  O   ASN A  95      25.504  -6.568  27.933  1.00 15.67           O  
ANISOU  693  O   ASN A  95     2110   1864   1980   -139    593   -115       O  
ATOM    694  CB  ASN A  95      26.181  -9.314  28.288  1.00 18.33           C  
ANISOU  694  CB  ASN A  95     1947   2008   3009    147    431    424       C  
ATOM    695  CG  ASN A  95      24.846  -9.897  27.890  1.00 24.01           C  
ANISOU  695  CG  ASN A  95     2124   2400   4599   -140    266    593       C  
ATOM    696  OD1 ASN A  95      24.166  -9.364  27.019  1.00 34.86           O  
ANISOU  696  OD1 ASN A  95     2977   2549   7719   -720  -1898   1249       O  
ATOM    697  ND2 ASN A  95      24.459 -10.995  28.511  1.00 30.52           N  
ANISOU  697  ND2 ASN A  95     3019   2352   6225   -511    331    832       N  
ATOM    698  N   TRP A  96      25.813  -6.798  25.716  1.00 15.18           N  
ANISOU  698  N   TRP A  96     2223   1581   1962    105    486   -104       N  
ATOM    699  CA  TRP A  96      25.094  -5.589  25.332  1.00 15.25           C  
ANISOU  699  CA  TRP A  96     1979   1785   2031    200    555   -147       C  
ATOM    700  C   TRP A  96      23.709  -5.510  25.923  1.00 15.16           C  
ANISOU  700  C   TRP A  96     2116   1650   1994     -3    680   -121       C  
ATOM    701  O   TRP A  96      23.250  -4.443  26.317  1.00 15.39           O  
ANISOU  701  O   TRP A  96     2028   1690   2128     18    761   -268       O  
ATOM    702  CB  TRP A  96      25.032  -5.564  23.775  1.00 16.53           C  
ANISOU  702  CB  TRP A  96     2220   2084   1979    375    666      5       C  
ATOM    703  CG  TRP A  96      24.374  -4.406  23.140  1.00 15.75           C  
ANISOU  703  CG  TRP A  96     1962   2054   1970    400    428   -178       C  
ATOM    704  CD1 TRP A  96      23.031  -4.175  23.020  1.00 17.08           C  
ANISOU  704  CD1 TRP A  96     2072   1962   2456    102    147   -142       C  
ATOM    705  CD2 TRP A  96      25.033  -3.289  22.506  1.00 16.19           C  
ANISOU  705  CD2 TRP A  96     1919   2102   2132    439    288    -64       C  
ATOM    706  NE1 TRP A  96      22.825  -3.003  22.378  1.00 17.37           N  
ANISOU  706  NE1 TRP A  96     1906   2170   2525    126     34    121       N  
ATOM    707  CE2 TRP A  96      24.048  -2.412  22.033  1.00 16.22           C  
ANISOU  707  CE2 TRP A  96     1842   2154   2167    165    -10     13       C  
ATOM    708  CE3 TRP A  96      26.367  -2.969  22.316  1.00 18.89           C  
ANISOU  708  CE3 TRP A  96     1939   2882   2355    415    603    432       C  
ATOM    709  CZ2 TRP A  96      24.372  -1.235  21.372  1.00 17.87           C  
ANISOU  709  CZ2 TRP A  96     2000   2273   2518    250    303    183       C  
ATOM    710  CZ3 TRP A  96      26.686  -1.805  21.658  1.00 18.68           C  
ANISOU  710  CZ3 TRP A  96     2122   2772   2205    323    359    361       C  
ATOM    711  CH2 TRP A  96      25.694  -0.916  21.174  1.00 18.29           C  
ANISOU  711  CH2 TRP A  96     2048   2577   2325     79    190    223       C  
ATOM    712  N   ARG A  97      22.967  -6.644  25.956  1.00 16.61           N  
ANISOU  712  N   ARG A  97     1880   1715   2717     87    433   -363       N  
ATOM    713  CA  ARG A  97      21.585  -6.609  26.474  1.00 18.12           C  
ANISOU  713  CA  ARG A  97     2007   1826   3050   -282    603   -707       C  
ATOM    714  C   ARG A  97      21.521  -6.116  27.916  1.00 15.79           C  
ANISOU  714  C   ARG A  97     1800   1411   2790    -41    652    -81       C  
ATOM    715  O   ARG A  97      20.553  -5.438  28.280  1.00 17.20           O  
ANISOU  715  O   ARG A  97     1708   1863   2964    -49    799   -372       O  
ATOM    716  CB  ARG A  97      20.995  -8.027  26.387  1.00 23.62           C  
ANISOU  716  CB  ARG A  97     2737   2255   3985   -836   1171   -973       C  
ATOM    717  CG  ARG A  97      19.585  -8.113  25.840  1.00 42.77           C  
ANISOU  717  CG  ARG A  97     4492   4384   7376  -2841  -1397    937       C  
ATOM    718  CD  ARG A  97      19.188  -9.515  25.345  1.00 59.16           C  
ANISOU  718  CD  ARG A  97     8575   5483   8420  -5059  -2627    869       C  
ATOM    719  NE  ARG A  97      17.983  -9.401  24.505  1.00 71.59           N  
ANISOU  719  NE  ARG A  97    10565   6970   9665  -5343  -4527    911       N  
ATOM    720  CZ  ARG A  97      17.948  -9.162  23.206  1.00 75.28           C  
ANISOU  720  CZ  ARG A  97     9774   8883   9945  -6308  -4277   1885       C  
ATOM    721  NH1 ARG A  97      19.074  -9.006  22.515  1.00 83.57           N  
ANISOU  721  NH1 ARG A  97     8692  12862  10197    698  -3246   1316       N  
ATOM    722  NH2 ARG A  97      16.818  -9.062  22.525  1.00 76.44           N  
ANISOU  722  NH2 ARG A  97     9179  10136   9728  -6786  -3609   3957       N  
ATOM    723  N   VAL A  98      22.520  -6.434  28.740  1.00 16.21           N  
ANISOU  723  N   VAL A  98     1906   1591   2662    196    814   -104       N  
ATOM    724  CA  VAL A  98      22.492  -6.027  30.152  1.00 16.90           C  
ANISOU  724  CA  VAL A  98     2172   1757   2494    224    839    121       C  
ATOM    725  C   VAL A  98      22.441  -4.495  30.255  1.00 16.00           C  
ANISOU  725  C   VAL A  98     2027   1757   2296     99    859    -43       C  
ATOM    726  O   VAL A  98      21.597  -3.935  30.964  1.00 16.05           O  
ANISOU  726  O   VAL A  98     1731   2034   2335   -248    822   -511       O  
ATOM    727  CB  VAL A  98      23.705  -6.615  30.885  1.00 19.20           C  
ANISOU  727  CB  VAL A  98     2566   2198   2531    465    779    295       C  
ATOM    728  CG1 VAL A  98      23.888  -6.005  32.266  1.00 20.35           C  
ANISOU  728  CG1 VAL A  98     2333   2639   2759    259    464    111       C  
ATOM    729  CG2 VAL A  98      23.610  -8.148  31.046  1.00 24.33           C  
ANISOU  729  CG2 VAL A  98     3669   2133   3445    824    292    256       C  
ATOM    730  N   ILE A  99      23.341  -3.834  29.555  1.00 14.56           N  
ANISOU  730  N   ILE A  99     1593   1669   2269    209    666    -13       N  
ATOM    731  CA  ILE A  99      23.369  -2.398  29.675  1.00 14.96           C  
ANISOU  731  CA  ILE A  99     1271   1702   2710    109    498   -186       C  
ATOM    732  C   ILE A  99      22.250  -1.762  28.880  1.00 12.93           C  
ANISOU  732  C   ILE A  99     1428   1335   2149   -126    612   -121       C  
ATOM    733  O   ILE A  99      21.728  -0.722  29.315  1.00 14.00           O  
ANISOU  733  O   ILE A  99     1312   1544   2465    -33    452   -283       O  
ATOM    734  CB AILE A  99      24.768  -1.882  29.268  0.47 16.09           C  
ANISOU  734  CB AILE A  99     1452   1997   2663   -109    558   -267       C  
ATOM    735  CB BILE A  99      24.750  -1.855  29.230  0.53 15.65           C  
ANISOU  735  CB BILE A  99     1493   1734   2718    243    658    674       C  
ATOM    736  CG1AILE A  99      25.638  -1.880  30.534  0.47 18.85           C  
ANISOU  736  CG1AILE A  99     1079   2920   3163    187    319    947       C  
ATOM    737  CG1BILE A  99      24.840  -0.368  29.638  0.53 17.68           C  
ANISOU  737  CG1BILE A  99     1399   2383   2936   -338    850   -486       C  
ATOM    738  CG2AILE A  99      24.677  -0.528  28.591  0.47 13.75           C  
ANISOU  738  CG2AILE A  99     1178   2576   1470    -27    545    -15       C  
ATOM    739  CG2BILE A  99      25.063  -2.075  27.775  0.53 22.02           C  
ANISOU  739  CG2BILE A  99     1731   3277   3360   -221   1171  -1034       C  
ATOM    740  CD1AILE A  99      25.269  -0.747  31.488  0.47 19.02           C  
ANISOU  740  CD1AILE A  99     1750   3832   1645   -364   -262    619       C  
ATOM    741  CD1BILE A  99      24.718  -0.149  31.136  0.53 18.89           C  
ANISOU  741  CD1BILE A  99     2198   2631   2348   -259  -1027    476       C  
ATOM    742  N   LYS A 100      21.807  -2.325  27.774  1.00 13.85           N  
ANISOU  742  N   LYS A 100     1544   1435   2284      7    633   -188       N  
ATOM    743  CA  LYS A 100      20.677  -1.771  27.030  1.00 14.16           C  
ANISOU  743  CA  LYS A 100     1760   1501   2121    115    531    -62       C  
ATOM    744  C   LYS A 100      19.453  -1.666  27.946  1.00 13.28           C  
ANISOU  744  C   LYS A 100     1550   1586   1911    150    284   -100       C  
ATOM    745  O   LYS A 100      18.760  -0.636  27.948  1.00 13.93           O  
ANISOU  745  O   LYS A 100     1703   1679   1909    288    396    -25       O  
ATOM    746  CB  LYS A 100      20.302  -2.583  25.799  1.00 18.64           C  
ANISOU  746  CB  LYS A 100     2407   2375   2301    154    417   -494       C  
ATOM    747  CG  LYS A 100      18.955  -2.217  25.174  1.00 26.39           C  
ANISOU  747  CG  LYS A 100     2218   4811   2997     35     38   -527       C  
ATOM    748  CD  LYS A 100      18.848  -2.274  23.713  1.00 35.11           C  
ANISOU  748  CD  LYS A 100     2728   7427   3185   1210   -172   -186       C  
ATOM    749  CE  LYS A 100      17.728  -1.375  23.202  1.00 23.44           C  
ANISOU  749  CE  LYS A 100     1943   4515   2447     49    555   -413       C  
ATOM    750  NZ  LYS A 100      16.359  -1.679  23.733  1.00 18.91           N  
ANISOU  750  NZ  LYS A 100     2280   2555   2350   -148    800   -623       N  
ATOM    751  N   GLU A 101      19.181  -2.735  28.694  1.00 13.13           N  
ANISOU  751  N   GLU A 101     1347   1538   2103     94    337   -176       N  
ATOM    752  CA  GLU A 101      17.982  -2.721  29.536  1.00 13.72           C  
ANISOU  752  CA  GLU A 101     1515   1604   2095    -94    293   -179       C  
ATOM    753  C   GLU A 101      18.116  -1.638  30.615  1.00 11.81           C  
ANISOU  753  C   GLU A 101     1232   1506   1750   -110    337     21       C  
ATOM    754  O   GLU A 101      17.143  -0.952  30.930  1.00 12.62           O  
ANISOU  754  O   GLU A 101     1204   1551   2038    -82    368     46       O  
ATOM    755  CB AGLU A 101      17.713  -4.074  30.158  0.57 16.55           C  
ANISOU  755  CB AGLU A 101     1787   1649   2852   -425    314    -90       C  
ATOM    756  CB BGLU A 101      17.845  -4.110  30.135  0.43 15.95           C  
ANISOU  756  CB BGLU A 101     1749   1549   2760   -100    688   -196       C  
ATOM    757  CG AGLU A 101      17.488  -5.220  29.246  0.57 18.70           C  
ANISOU  757  CG AGLU A 101     1603   1833   3668   -272    583   -621       C  
ATOM    758  CG BGLU A 101      16.840  -4.142  31.234  0.43 21.21           C  
ANISOU  758  CG BGLU A 101     1380   3073   3604   -411    966    481       C  
ATOM    759  CD AGLU A 101      17.669  -6.621  29.787  0.57 26.82           C  
ANISOU  759  CD AGLU A 101     3687   1775   4729    -31    236   -589       C  
ATOM    760  CD BGLU A 101      17.103  -3.907  32.692  0.43 30.02           C  
ANISOU  760  CD BGLU A 101     5425   3200   2782   -737   1775   1539       C  
ATOM    761  OE1AGLU A 101      18.020  -6.806  30.968  0.57 25.33           O  
ANISOU  761  OE1AGLU A 101     2918   1889   4817   -221    520     62       O  
ATOM    762  OE1BGLU A 101      16.331  -3.086  33.265  0.43 38.50           O  
ANISOU  762  OE1BGLU A 101     8426   2715   3487    -99   2112    925       O  
ATOM    763  OE2AGLU A 101      17.442  -7.540  28.960  0.57 35.26           O  
ANISOU  763  OE2AGLU A 101     5956   1799   5640   -874   -103   -729       O  
ATOM    764  OE2BGLU A 101      18.047  -4.477  33.248  0.43 32.03           O  
ANISOU  764  OE2BGLU A 101     3130   5879   3161  -2087    246   -450       O  
ATOM    765  N   LYS A 102      19.289  -1.531  31.219  1.00 12.02           N  
ANISOU  765  N   LYS A 102     1276   1404   1885    -30    308     77       N  
ATOM    766  CA  LYS A 102      19.498  -0.549  32.294  1.00 11.32           C  
ANISOU  766  CA  LYS A 102     1198   1526   1578    117    365    113       C  
ATOM    767  C   LYS A 102      19.417   0.880  31.757  1.00 10.67           C  
ANISOU  767  C   LYS A 102     1097   1489   1470    -33    283     86       C  
ATOM    768  O   LYS A 102      18.904   1.779  32.419  1.00 11.51           O  
ANISOU  768  O   LYS A 102     1254   1609   1512    -12    377    -27       O  
ATOM    769  CB  LYS A 102      20.804  -0.792  33.014  1.00 11.92           C  
ANISOU  769  CB  LYS A 102     1176   1694   1660     73    360    100       C  
ATOM    770  CG  LYS A 102      20.839  -2.123  33.766  1.00 13.83           C  
ANISOU  770  CG  LYS A 102     1724   1723   1810     -4     27    155       C  
ATOM    771  CD  LYS A 102      22.152  -2.378  34.459  1.00 14.47           C  
ANISOU  771  CD  LYS A 102     1459   2253   1787     35    153    112       C  
ATOM    772  CE  LYS A 102      22.214  -3.806  35.031  1.00 18.59           C  
ANISOU  772  CE  LYS A 102     2281   2316   2465    700     84    262       C  
ATOM    773  NZ  LYS A 102      23.406  -3.933  35.889  1.00 26.83           N  
ANISOU  773  NZ  LYS A 102     2420   4869   2906   1120     52   1012       N  
ATOM    774  N   ARG A 103      19.959   1.091  30.574  1.00 10.85           N  
ANISOU  774  N   ARG A 103     1131   1428   1565     36    403    134       N  
ATOM    775  CA  ARG A 103      19.915   2.382  29.898  1.00 10.67           C  
ANISOU  775  CA  ARG A 103     1196   1516   1343     65    282     85       C  
ATOM    776  C   ARG A 103      18.488   2.782  29.617  1.00 10.07           C  
ANISOU  776  C   ARG A 103     1121   1358   1347    -36    293    128       C  
ATOM    777  O   ARG A 103      18.063   3.900  29.879  1.00 10.92           O  
ANISOU  777  O   ARG A 103     1213   1376   1559     42    447     18       O  
ATOM    778  CB  ARG A 103      20.772   2.304  28.623  1.00 11.57           C  
ANISOU  778  CB  ARG A 103     1032   1542   1822     32    490    153       C  
ATOM    779  CG  ARG A 103      21.070   3.621  27.953  1.00 11.27           C  
ANISOU  779  CG  ARG A 103     1185   1462   1635    -79    419     83       C  
ATOM    780  CD  ARG A 103      21.759   3.425  26.621  1.00 11.42           C  
ANISOU  780  CD  ARG A 103     1200   1442   1696    -84    417    -56       C  
ATOM    781  NE  ARG A 103      20.744   3.008  25.644  1.00 12.81           N  
ANISOU  781  NE  ARG A 103     1284   1873   1710   -135    311    -10       N  
ATOM    782  CZ  ARG A 103      20.887   2.134  24.643  1.00 13.44           C  
ANISOU  782  CZ  ARG A 103     1397   1966   1746   -303    417    -71       C  
ATOM    783  NH1 ARG A 103      19.859   1.905  23.867  1.00 14.68           N  
ANISOU  783  NH1 ARG A 103     1476   2400   1703   -195    365   -215       N  
ATOM    784  NH2 ARG A 103      22.002   1.492  24.374  1.00 15.14           N  
ANISOU  784  NH2 ARG A 103     1261   2560   1931   -360    404   -520       N  
ATOM    785  N   ASP A 104      17.713   1.838  29.073  1.00 10.75           N  
ANISOU  785  N   ASP A 104     1214   1361   1508    -66    323    -10       N  
ATOM    786  CA  ASP A 104      16.309   2.111  28.781  1.00 11.04           C  
ANISOU  786  CA  ASP A 104     1217   1564   1413    -53    336     52       C  
ATOM    787  C   ASP A 104      15.541   2.432  30.053  1.00 10.32           C  
ANISOU  787  C   ASP A 104     1130   1359   1433   -148    232    -64       C  
ATOM    788  O   ASP A 104      14.657   3.329  30.011  1.00 11.25           O  
ANISOU  788  O   ASP A 104     1117   1486   1673    -60    312    -15       O  
ATOM    789  CB  ASP A 104      15.665   0.909  28.108  1.00 11.71           C  
ANISOU  789  CB  ASP A 104     1262   1559   1629     61    316   -197       C  
ATOM    790  CG  ASP A 104      16.007   0.637  26.645  1.00 13.29           C  
ANISOU  790  CG  ASP A 104     1419   2023   1608   -176    376   -111       C  
ATOM    791  OD1 ASP A 104      16.576   1.525  25.996  1.00 15.56           O  
ANISOU  791  OD1 ASP A 104     1888   2198   1827   -237    608     58       O  
ATOM    792  OD2 ASP A 104      15.642  -0.475  26.165  1.00 15.90           O  
ANISOU  792  OD2 ASP A 104     1903   2252   1885   -355    598   -443       O  
ATOM    793  N   ALA A 105      15.827   1.755  31.142  1.00 11.14           N  
ANISOU  793  N   ALA A 105     1338   1456   1439     -8    454     58       N  
ATOM    794  CA  ALA A 105      15.132   2.046  32.421  1.00 10.57           C  
ANISOU  794  CA  ALA A 105     1143   1461   1411    -51    399    -50       C  
ATOM    795  C   ALA A 105      15.454   3.447  32.870  1.00 10.72           C  
ANISOU  795  C   ALA A 105     1170   1407   1497    -80    313    -18       C  
ATOM    796  O   ALA A 105      14.560   4.188  33.359  1.00 11.06           O  
ANISOU  796  O   ALA A 105     1133   1439   1630     11    520    194       O  
ATOM    797  CB  ALA A 105      15.515   0.998  33.448  1.00 11.84           C  
ANISOU  797  CB  ALA A 105     1516   1468   1515    -85    527    153       C  
ATOM    798  N   TYR A 106      16.705   3.881  32.761  1.00 10.02           N  
ANISOU  798  N   TYR A 106     1078   1445   1285    -41    343    -88       N  
ATOM    799  CA  TYR A 106      17.099   5.246  33.140  1.00  9.97           C  
ANISOU  799  CA  TYR A 106     1018   1395   1375      1    320   -111       C  
ATOM    800  C   TYR A 106      16.357   6.293  32.312  1.00 10.22           C  
ANISOU  800  C   TYR A 106      983   1395   1506   -129    288    -68       C  
ATOM    801  O   TYR A 106      15.818   7.241  32.844  1.00 10.43           O  
ANISOU  801  O   TYR A 106     1055   1398   1510    -28    446     31       O  
ATOM    802  CB  TYR A 106      18.621   5.403  33.061  1.00 10.73           C  
ANISOU  802  CB  TYR A 106     1032   1690   1355    -25    311    -19       C  
ATOM    803  CG  TYR A 106      19.174   6.707  33.477  1.00 10.73           C  
ANISOU  803  CG  TYR A 106      951   1669   1458    -21    250     57       C  
ATOM    804  CD1 TYR A 106      18.670   7.473  34.534  1.00 11.80           C  
ANISOU  804  CD1 TYR A 106     1207   1692   1586   -136    351   -120       C  
ATOM    805  CD2 TYR A 106      20.258   7.260  32.832  1.00 12.16           C  
ANISOU  805  CD2 TYR A 106     1090   1883   1646    -85    370    125       C  
ATOM    806  CE1 TYR A 106      19.233   8.684  34.906  1.00 13.72           C  
ANISOU  806  CE1 TYR A 106     1263   1805   2145   -197    221   -294       C  
ATOM    807  CE2 TYR A 106      20.833   8.422  33.206  1.00 14.10           C  
ANISOU  807  CE2 TYR A 106     1203   2268   1886   -376    188    200       C  
ATOM    808  CZ  TYR A 106      20.313   9.153  34.223  1.00 13.74           C  
ANISOU  808  CZ  TYR A 106     1329   1818   2072   -312    -30     30       C  
ATOM    809  OH  TYR A 106      20.924  10.354  34.574  1.00 17.28           O  
ANISOU  809  OH  TYR A 106     1944   2020   2602   -757   -256    169       O  
ATOM    810  N   VAL A 107      16.272   6.051  31.007  1.00 10.28           N  
ANISOU  810  N   VAL A 107     1103   1331   1473     -8    330    -12       N  
ATOM    811  CA  VAL A 107      15.528   6.951  30.136  1.00 10.12           C  
ANISOU  811  CA  VAL A 107     1055   1362   1427     -1    362    -39       C  
ATOM    812  C   VAL A 107      14.085   7.075  30.613  1.00 10.54           C  
ANISOU  812  C   VAL A 107     1057   1509   1437      4    250   -114       C  
ATOM    813  O   VAL A 107      13.518   8.159  30.668  1.00 10.69           O  
ANISOU  813  O   VAL A 107     1180   1469   1412    106    412     74       O  
ATOM    814  CB  VAL A 107      15.663   6.510  28.689  1.00 11.29           C  
ANISOU  814  CB  VAL A 107     1441   1382   1468    107    515     63       C  
ATOM    815  CG1 VAL A 107      14.719   7.300  27.782  1.00 11.88           C  
ANISOU  815  CG1 VAL A 107     1459   1665   1390     98    402     13       C  
ATOM    816  CG2 VAL A 107      17.101   6.677  28.188  1.00 12.42           C  
ANISOU  816  CG2 VAL A 107     1467   1569   1684    119    643    279       C  
ATOM    817  N   SER A 108      13.466   5.920  30.937  1.00 10.61           N  
ANISOU  817  N   SER A 108     1092   1494   1446    -27    370     88       N  
ATOM    818  CA  SER A 108      12.091   5.945  31.450  1.00 10.76           C  
ANISOU  818  CA  SER A 108     1038   1526   1524     95    327     68       C  
ATOM    819  C   SER A 108      11.956   6.730  32.745  1.00 10.27           C  
ANISOU  819  C   SER A 108     1066   1279   1555    -20    376    122       C  
ATOM    820  O   SER A 108      10.974   7.460  32.914  1.00 10.88           O  
ANISOU  820  O   SER A 108      925   1451   1759    -43    399     12       O  
ATOM    821  CB  SER A 108      11.588   4.510  31.646  1.00 12.57           C  
ANISOU  821  CB  SER A 108     1158   1627   1992   -231    323   -286       C  
ATOM    822  OG  SER A 108      11.442   3.824  30.466  1.00 16.02           O  
ANISOU  822  OG  SER A 108     1756   2110   2222   -459    528   -491       O  
ATOM    823  N   ARG A 109      12.917   6.589  33.665  1.00 10.31           N  
ANISOU  823  N   ARG A 109     1031   1359   1527     19    383     74       N  
ATOM    824  CA  ARG A 109      12.898   7.379  34.884  1.00 10.36           C  
ANISOU  824  CA  ARG A 109      948   1448   1538     86    465     78       C  
ATOM    825  C   ARG A 109      12.935   8.860  34.581  1.00 10.78           C  
ANISOU  825  C   ARG A 109     1130   1416   1550    -48    434     86       C  
ATOM    826  O   ARG A 109      12.231   9.677  35.207  1.00 11.00           O  
ANISOU  826  O   ARG A 109     1217   1503   1460    -24    581     37       O  
ATOM    827  CB  ARG A 109      14.035   7.003  35.811  1.00 10.45           C  
ANISOU  827  CB  ARG A 109     1141   1460   1371     26    479     39       C  
ATOM    828  CG  ARG A 109      13.929   5.602  36.374  1.00 10.93           C  
ANISOU  828  CG  ARG A 109     1165   1543   1446     81    439    205       C  
ATOM    829  CD  ARG A 109      14.889   5.300  37.509  1.00 11.58           C  
ANISOU  829  CD  ARG A 109     1325   1629   1443    141    390     96       C  
ATOM    830  NE  ARG A 109      16.294   5.368  37.225  1.00 12.19           N  
ANISOU  830  NE  ARG A 109     1228   1784   1618    -97    313    -23       N  
ATOM    831  CZ  ARG A 109      17.029   4.420  36.706  1.00 11.43           C  
ANISOU  831  CZ  ARG A 109     1111   1770   1460    -70    260     73       C  
ATOM    832  NH1 ARG A 109      18.346   4.585  36.531  1.00 13.88           N  
ANISOU  832  NH1 ARG A 109     1044   2179   2051    -68    250    159       N  
ATOM    833  NH2 ARG A 109      16.513   3.303  36.267  1.00 11.51           N  
ANISOU  833  NH2 ARG A 109     1103   1815   1456    -21    346     73       N  
ATOM    834  N   LEU A 110      13.774   9.258  33.597  1.00 10.63           N  
ANISOU  834  N   LEU A 110     1109   1342   1589     30    560     20       N  
ATOM    835  CA  LEU A 110      13.861  10.656  33.202  1.00 10.41           C  
ANISOU  835  CA  LEU A 110     1139   1409   1409    -97    403     61       C  
ATOM    836  C   LEU A 110      12.594  11.165  32.542  1.00 10.14           C  
ANISOU  836  C   LEU A 110     1152   1416   1284    -14    473     68       C  
ATOM    837  O   LEU A 110      12.169  12.304  32.766  1.00 11.21           O  
ANISOU  837  O   LEU A 110     1216   1402   1641    -22    494     63       O  
ATOM    838  CB  LEU A 110      15.108  10.870  32.365  1.00 10.72           C  
ANISOU  838  CB  LEU A 110     1089   1469   1516    -82    462     62       C  
ATOM    839  CG  LEU A 110      16.459  10.668  33.058  1.00 11.30           C  
ANISOU  839  CG  LEU A 110     1149   1639   1505     15    460     86       C  
ATOM    840  CD1 LEU A 110      17.567  10.849  32.023  1.00 14.61           C  
ANISOU  840  CD1 LEU A 110     1183   2633   1734    -35    452     30       C  
ATOM    841  CD2 LEU A 110      16.640  11.605  34.214  1.00 14.64           C  
ANISOU  841  CD2 LEU A 110     1234   2386   1942     -7    253   -411       C  
ATOM    842  N   ASN A 111      11.960  10.337  31.720  1.00 10.61           N  
ANISOU  842  N   ASN A 111     1117   1401   1513     92    347     44       N  
ATOM    843  CA  ASN A 111      10.686  10.751  31.137  1.00 10.78           C  
ANISOU  843  CA  ASN A 111     1121   1486   1488     76    338      9       C  
ATOM    844  C   ASN A 111       9.692  11.098  32.242  1.00 10.86           C  
ANISOU  844  C   ASN A 111     1091   1471   1563      2    396     65       C  
ATOM    845  O   ASN A 111       8.956  12.084  32.134  1.00 11.82           O  
ANISOU  845  O   ASN A 111     1200   1641   1649    177    365     15       O  
ATOM    846  CB  ASN A 111      10.100   9.649  30.260  1.00 11.54           C  
ANISOU  846  CB  ASN A 111     1227   1652   1504     11    310      5       C  
ATOM    847  CG  ASN A 111      10.827   9.215  29.044  1.00 11.43           C  
ANISOU  847  CG  ASN A 111     1183   1709   1452     92    305    -35       C  
ATOM    848  OD1 ASN A 111      10.798   8.012  28.718  1.00 13.86           O  
ANISOU  848  OD1 ASN A 111     1416   1882   1968    -54    400   -242       O  
ATOM    849  ND2 ASN A 111      11.471  10.075  28.308  1.00 13.02           N  
ANISOU  849  ND2 ASN A 111     1283   2046   1617   -148    572   -208       N  
ATOM    850  N   ALA A 112       9.647  10.280  33.282  1.00 10.77           N  
ANISOU  850  N   ALA A 112     1131   1392   1569     16    403    -24       N  
ATOM    851  CA  ALA A 112       8.722  10.508  34.400  1.00 10.60           C  
ANISOU  851  CA  ALA A 112     1156   1485   1387    -15    373     -5       C  
ATOM    852  C   ALA A 112       9.083  11.778  35.168  1.00 10.11           C  
ANISOU  852  C   ALA A 112     1009   1474   1358     53    368     36       C  
ATOM    853  O   ALA A 112       8.178  12.527  35.568  1.00 11.27           O  
ANISOU  853  O   ALA A 112     1112   1515   1654     39    510    -23       O  
ATOM    854  CB  ALA A 112       8.675   9.309  35.314  1.00 11.59           C  
ANISOU  854  CB  ALA A 112     1216   1561   1625    -50    398    100       C  
ATOM    855  N   ILE A 113      10.356  12.040  35.379  1.00 10.15           N  
ANISOU  855  N   ILE A 113      954   1391   1512     60    347    -68       N  
ATOM    856  CA  ILE A 113      10.805  13.231  36.065  1.00 10.78           C  
ANISOU  856  CA  ILE A 113     1294   1506   1294     46    328    -53       C  
ATOM    857  C   ILE A 113      10.410  14.466  35.277  1.00 10.76           C  
ANISOU  857  C   ILE A 113     1288   1424   1378    -76    332     72       C  
ATOM    858  O   ILE A 113       9.897  15.439  35.881  1.00 11.71           O  
ANISOU  858  O   ILE A 113     1416   1519   1516     46    430     14       O  
ATOM    859  CB  ILE A 113      12.313  13.174  36.367  1.00 11.58           C  
ANISOU  859  CB  ILE A 113     1284   1532   1583   -112    101      7       C  
ATOM    860  CG1 ILE A 113      12.620  12.168  37.502  1.00 12.19           C  
ANISOU  860  CG1 ILE A 113     1317   1757   1556     27    250     61       C  
ATOM    861  CG2 ILE A 113      12.930  14.540  36.644  1.00 13.84           C  
ANISOU  861  CG2 ILE A 113     1477   1679   2103   -220     51     76       C  
ATOM    862  CD1 ILE A 113      14.019  11.673  37.573  1.00 15.23           C  
ANISOU  862  CD1 ILE A 113     1305   2257   2223     17      6    477       C  
ATOM    863  N   TYR A 114      10.646  14.515  33.975  1.00 11.56           N  
ANISOU  863  N   TYR A 114     1401   1520   1471    136    489    151       N  
ATOM    864  CA  TYR A 114      10.303  15.728  33.251  1.00 12.39           C  
ANISOU  864  CA  TYR A 114     1595   1662   1450    -33    330    306       C  
ATOM    865  C   TYR A 114       8.816  15.962  33.133  1.00 11.95           C  
ANISOU  865  C   TYR A 114     1577   1467   1498    136    358    162       C  
ATOM    866  O   TYR A 114       8.372  17.109  33.132  1.00 13.20           O  
ANISOU  866  O   TYR A 114     1807   1460   1750    113    482    246       O  
ATOM    867  CB  TYR A 114      11.057  15.752  31.853  1.00 13.07           C  
ANISOU  867  CB  TYR A 114     1828   1630   1508    -37    515     68       C  
ATOM    868  CG  TYR A 114      12.508  16.085  32.115  1.00 13.73           C  
ANISOU  868  CG  TYR A 114     1859   1682   1677   -139    552    201       C  
ATOM    869  CD1 TYR A 114      13.507  15.134  32.049  1.00 17.06           C  
ANISOU  869  CD1 TYR A 114     1807   1845   2830   -112    801    220       C  
ATOM    870  CD2 TYR A 114      12.931  17.371  32.540  1.00 15.62           C  
ANISOU  870  CD2 TYR A 114     1895   1912   2127   -241    613   -116       C  
ATOM    871  CE1 TYR A 114      14.821  15.416  32.304  1.00 18.69           C  
ANISOU  871  CE1 TYR A 114     1806   2393   2901    -50    886    290       C  
ATOM    872  CE2 TYR A 114      14.255  17.665  32.839  1.00 17.55           C  
ANISOU  872  CE2 TYR A 114     1890   2434   2345   -491    770   -336       C  
ATOM    873  CZ  TYR A 114      15.216  16.683  32.721  1.00 19.62           C  
ANISOU  873  CZ  TYR A 114     1739   2790   2924   -332    485     90       C  
ATOM    874  OH  TYR A 114      16.570  16.924  33.018  1.00 24.11           O  
ANISOU  874  OH  TYR A 114     1795   3826   3538   -457    233    660       O  
ATOM    875  N   GLN A 115       8.028  14.892  33.031  1.00 12.05           N  
ANISOU  875  N   GLN A 115     1525   1354   1701    243    177     92       N  
ATOM    876  CA  GLN A 115       6.571  15.057  33.113  1.00 12.95           C  
ANISOU  876  CA  GLN A 115     1518   1580   1821    236     15     66       C  
ATOM    877  C   GLN A 115       6.173  15.719  34.429  1.00 12.24           C  
ANISOU  877  C   GLN A 115     1381   1329   1941    135    217     86       C  
ATOM    878  O   GLN A 115       5.403  16.670  34.453  1.00 13.46           O  
ANISOU  878  O   GLN A 115     1366   1496   2250    205    258     60       O  
ATOM    879  CB  GLN A 115       5.861  13.703  32.908  1.00 13.38           C  
ANISOU  879  CB  GLN A 115     1701   1786   1597    -36     16     11       C  
ATOM    880  CG  GLN A 115       4.356  13.806  32.968  1.00 18.37           C  
ANISOU  880  CG  GLN A 115     1622   2413   2943     -6      0    -90       C  
ATOM    881  CD  GLN A 115       3.767  12.434  32.637  1.00 24.14           C  
ANISOU  881  CD  GLN A 115     2729   3141   3301  -1206   -627    197       C  
ATOM    882  OE1 GLN A 115       3.337  12.194  31.523  1.00 30.98           O  
ANISOU  882  OE1 GLN A 115     4731   3333   3708  -1117  -1427    162       O  
ATOM    883  NE2 GLN A 115       3.834  11.505  33.592  1.00 25.64           N  
ANISOU  883  NE2 GLN A 115     3662   2904   3177  -1051   -355     -3       N  
ATOM    884  N   ASN A 116       6.745  15.220  35.527  1.00 11.38           N  
ANISOU  884  N   ASN A 116     1276   1326   1722    203    407     47       N  
ATOM    885  CA  ASN A 116       6.440  15.787  36.827  1.00 11.99           C  
ANISOU  885  CA  ASN A 116     1340   1455   1759    -27    578     47       C  
ATOM    886  C   ASN A 116       6.917  17.224  36.949  1.00 11.43           C  
ANISOU  886  C   ASN A 116     1470   1454   1421    123    449     21       C  
ATOM    887  O   ASN A 116       6.252  18.042  37.582  1.00 12.46           O  
ANISOU  887  O   ASN A 116     1623   1513   1600    132    601    -58       O  
ATOM    888  CB  ASN A 116       7.043  14.916  37.893  1.00 14.19           C  
ANISOU  888  CB  ASN A 116     2217   1454   1722     76    654    175       C  
ATOM    889  CG  ASN A 116       6.678  15.384  39.288  1.00 15.78           C  
ANISOU  889  CG  ASN A 116     2874   1352   1769    -20    917    225       C  
ATOM    890  OD1 ASN A 116       7.550  15.655  40.133  1.00 22.56           O  
ANISOU  890  OD1 ASN A 116     4315   2295   1961   -626    352      1       O  
ATOM    891  ND2 ASN A 116       5.387  15.487  39.558  1.00 18.70           N  
ANISOU  891  ND2 ASN A 116     3358   1790   1956    586   1425    477       N  
ATOM    892  N   ASN A 117       8.063  17.552  36.368  1.00 11.60           N  
ANISOU  892  N   ASN A 117     1317   1380   1711     65    410      7       N  
ATOM    893  CA  ASN A 117       8.525  18.953  36.423  1.00 12.35           C  
ANISOU  893  CA  ASN A 117     1480   1543   1671    -39    280     39       C  
ATOM    894  C   ASN A 117       7.557  19.896  35.798  1.00 12.56           C  
ANISOU  894  C   ASN A 117     1500   1415   1856     91    325     20       C  
ATOM    895  O   ASN A 117       7.323  20.991  36.327  1.00 14.86           O  
ANISOU  895  O   ASN A 117     2303   1428   1914     51     74   -138       O  
ATOM    896  CB  ASN A 117       9.925  19.035  35.783  1.00 12.15           C  
ANISOU  896  CB  ASN A 117     1353   1401   1861    -80    233     34       C  
ATOM    897  CG  ASN A 117      11.090  18.389  36.494  1.00 13.94           C  
ANISOU  897  CG  ASN A 117     1576   1743   1976      2    133    207       C  
ATOM    898  OD1 ASN A 117      12.202  18.189  35.933  1.00 17.89           O  
ANISOU  898  OD1 ASN A 117     1621   2253   2922     58    526    147       O  
ATOM    899  ND2 ASN A 117      10.898  18.080  37.734  1.00 13.87           N  
ANISOU  899  ND2 ASN A 117     1298   1973   2000     55     -8    113       N  
ATOM    900  N   LEU A 118       6.943  19.478  34.682  1.00 11.86           N  
ANISOU  900  N   LEU A 118     1573   1246   1687    210    325     63       N  
ATOM    901  CA  LEU A 118       5.914  20.332  34.076  1.00 12.36           C  
ANISOU  901  CA  LEU A 118     1814   1406   1476    387    421    178       C  
ATOM    902  C   LEU A 118       4.664  20.399  34.941  1.00 12.51           C  
ANISOU  902  C   LEU A 118     1751   1542   1462    376    335     58       C  
ATOM    903  O   LEU A 118       4.142  21.486  35.174  1.00 14.15           O  
ANISOU  903  O   LEU A 118     1923   1649   1805    460    455     97       O  
ATOM    904  CB  LEU A 118       5.560  19.808  32.687  1.00 11.83           C  
ANISOU  904  CB  LEU A 118     1450   1412   1634    192    418     89       C  
ATOM    905  CG  LEU A 118       6.698  19.975  31.622  1.00 12.26           C  
ANISOU  905  CG  LEU A 118     1547   1634   1477    131    461     11       C  
ATOM    906  CD1 LEU A 118       6.140  19.500  30.290  1.00 14.01           C  
ANISOU  906  CD1 LEU A 118     1489   2191   1643   -273    493   -175       C  
ATOM    907  CD2 LEU A 118       7.286  21.360  31.559  1.00 13.71           C  
ANISOU  907  CD2 LEU A 118     1518   1618   2073     23    515     -6       C  
ATOM    908  N   THR A 119       4.147  19.253  35.409  1.00 14.51           N  
ANISOU  908  N   THR A 119     1841   1668   2002    508    817    270       N  
ATOM    909  CA  THR A 119       2.938  19.201  36.219  1.00 18.40           C  
ANISOU  909  CA  THR A 119     1964   2561   2468    505   1211     61       C  
ATOM    910  C   THR A 119       3.099  20.031  37.466  1.00 17.89           C  
ANISOU  910  C   THR A 119     2690   2327   1779   1040   1159    698       C  
ATOM    911  O   THR A 119       2.174  20.767  37.858  1.00 20.71           O  
ANISOU  911  O   THR A 119     3185   2512   2171   1369   1419    512       O  
ATOM    912  CB  THR A 119       2.615  17.683  36.521  1.00 23.18           C  
ANISOU  912  CB  THR A 119     2301   3065   3443   -447   1508    193       C  
ATOM    913  OG1 THR A 119       2.352  17.151  35.228  1.00 26.72           O  
ANISOU  913  OG1 THR A 119     2449   3395   4309   -775   1337   -536       O  
ATOM    914  CG2 THR A 119       1.417  17.690  37.414  1.00 26.99           C  
ANISOU  914  CG2 THR A 119     2537   3052   4668    243   2011    311       C  
ATOM    915  N   LYS A 120       4.212  19.932  38.164  1.00 20.29           N  
ANISOU  915  N   LYS A 120     3324   2741   1643   1357    723    590       N  
ATOM    916  CA  LYS A 120       4.456  20.645  39.418  1.00 24.91           C  
ANISOU  916  CA  LYS A 120     4300   3413   1752   1915    587    220       C  
ATOM    917  C   LYS A 120       4.530  22.138  39.203  1.00 24.50           C  
ANISOU  917  C   LYS A 120     4139   3215   1956   2359    287   -234       C  
ATOM    918  O   LYS A 120       4.267  22.890  40.127  1.00 29.70           O  
ANISOU  918  O   LYS A 120     5174   4192   1919   2687   -164   -855       O  
ATOM    919  CB  LYS A 120       5.764  20.112  40.054  1.00 34.50           C  
ANISOU  919  CB  LYS A 120     6838   3332   2940   3033  -1634   -735       C  
ATOM    920  CG  LYS A 120       5.468  19.086  41.154  1.00 54.11           C  
ANISOU  920  CG  LYS A 120    10119   5346   5093   2309  -2813   1596       C  
ATOM    921  CD  LYS A 120       6.436  19.450  42.290  1.00 62.10           C  
ANISOU  921  CD  LYS A 120    12875   5350   5368   1512  -4105   2117       C  
ATOM    922  CE  LYS A 120       7.863  19.058  41.903  1.00 68.49           C  
ANISOU  922  CE  LYS A 120    11806   3307  10908   2102  -6432   1010       C  
ATOM    923  NZ  LYS A 120       8.648  18.413  43.001  1.00109.88           N  
ANISOU  923  NZ  LYS A 120    19890   6409  15451   5551 -12129   -135       N  
ATOM    924  N   SER A 121       4.908  22.527  37.984  1.00 21.66           N  
ANISOU  924  N   SER A 121     3940   2569   1720   1630   -219   -290       N  
ATOM    925  CA  SER A 121       4.974  23.935  37.587  1.00 21.52           C  
ANISOU  925  CA  SER A 121     3689   2477   2012   1425   -762   -636       C  
ATOM    926  C   SER A 121       3.633  24.378  37.044  1.00 17.68           C  
ANISOU  926  C   SER A 121     2936   2179   1604   1144     81   -274       C  
ATOM    927  O   SER A 121       3.493  25.518  36.595  1.00 18.65           O  
ANISOU  927  O   SER A 121     2691   2226   2170   1018    234   -103       O  
ATOM    928  CB  SER A 121       6.105  24.163  36.610  1.00 23.32           C  
ANISOU  928  CB  SER A 121     2428   2134   4300    405   -797   -505       C  
ATOM    929  OG  SER A 121       7.458  24.009  36.959  1.00 33.32           O  
ANISOU  929  OG  SER A 121     2977   3640   6043   1153  -1736  -1679       O  
ATOM    930  N   HIS A 122       2.612  23.561  36.975  1.00 17.73           N  
ANISOU  930  N   HIS A 122     2910   2202   1623   1164    555     33       N  
ATOM    931  CA  HIS A 122       1.312  23.910  36.435  1.00 16.66           C  
ANISOU  931  CA  HIS A 122     2487   2007   1837    823    762    280       C  
ATOM    932  C   HIS A 122       1.385  24.300  34.983  1.00 14.72           C  
ANISOU  932  C   HIS A 122     1758   1930   1903    631    679    333       C  
ATOM    933  O   HIS A 122       0.637  25.148  34.514  1.00 17.05           O  
ANISOU  933  O   HIS A 122     1920   2529   2030   1027    564    236       O  
ATOM    934  CB  HIS A 122       0.621  25.045  37.292  1.00 23.69           C  
ANISOU  934  CB  HIS A 122     3112   3614   2276   1727   1069    -48       C  
ATOM    935  CG  HIS A 122       0.795  24.720  38.755  1.00 31.20           C  
ANISOU  935  CG  HIS A 122     4679   4963   2211   2666   1633    -36       C  
ATOM    936  ND1 HIS A 122       1.447  25.490  39.680  1.00 35.68           N  
ANISOU  936  ND1 HIS A 122     5054   6501   2001   2596    990    -97       N  
ATOM    937  CD2 HIS A 122       0.403  23.603  39.401  1.00 38.80           C  
ANISOU  937  CD2 HIS A 122     5951   6392   2400   2017   2030    885       C  
ATOM    938  CE1 HIS A 122       1.442  24.878  40.849  1.00 37.99           C  
ANISOU  938  CE1 HIS A 122     4958   7246   2229   3441   1541    249       C  
ATOM    939  NE2 HIS A 122       0.802  23.724  40.709  1.00 48.44           N  
ANISOU  939  NE2 HIS A 122     7867   7941   2596   1852   1392   1050       N  
ATOM    940  N   ILE A 123       2.241  23.616  34.245  1.00 12.28           N  
ANISOU  940  N   ILE A 123     1305   1616   1746    242    418     57       N  
ATOM    941  CA  ILE A 123       2.369  23.769  32.794  1.00 11.78           C  
ANISOU  941  CA  ILE A 123     1122   1680   1673     36    251    194       C  
ATOM    942  C   ILE A 123       1.535  22.684  32.167  1.00 12.06           C  
ANISOU  942  C   ILE A 123     1190   1761   1630    -18    479    105       C  
ATOM    943  O   ILE A 123       1.777  21.524  32.432  1.00 14.67           O  
ANISOU  943  O   ILE A 123     1556   1791   2228   -103    173    223       O  
ATOM    944  CB  ILE A 123       3.827  23.730  32.350  1.00 11.12           C  
ANISOU  944  CB  ILE A 123     1122   1522   1582    111    347     81       C  
ATOM    945  CG1 ILE A 123       4.621  24.877  33.018  1.00 12.26           C  
ANISOU  945  CG1 ILE A 123     1212   1583   1864     75    315    102       C  
ATOM    946  CG2 ILE A 123       3.935  23.735  30.844  1.00 12.77           C  
ANISOU  946  CG2 ILE A 123     1266   1940   1646    197    260    226       C  
ATOM    947  CD1 ILE A 123       6.133  24.690  32.965  1.00 15.31           C  
ANISOU  947  CD1 ILE A 123     1220   1787   2811    -92    189   -254       C  
ATOM    948  N   GLU A 124       0.582  23.059  31.309  1.00 12.83           N  
ANISOU  948  N   GLU A 124     1095   1863   1918     90    376   -120       N  
ATOM    949  CA  GLU A 124      -0.227  22.053  30.630  1.00 13.05           C  
ANISOU  949  CA  GLU A 124     1224   2005   1730    -96    544   -154       C  
ATOM    950  C   GLU A 124       0.583  21.269  29.634  1.00 12.90           C  
ANISOU  950  C   GLU A 124     1119   1846   1935    -18    512    -82       C  
ATOM    951  O   GLU A 124       1.357  21.893  28.906  1.00 13.68           O  
ANISOU  951  O   GLU A 124     1508   1878   1812    -80    649    -17       O  
ATOM    952  CB  GLU A 124      -1.405  22.777  29.941  1.00 15.37           C  
ANISOU  952  CB  GLU A 124     1096   2482   2263    197    412   -433       C  
ATOM    953  CG  GLU A 124      -2.367  21.848  29.237  1.00 21.78           C  
ANISOU  953  CG  GLU A 124     1820   3584   2871   -552      5   -356       C  
ATOM    954  CD  GLU A 124      -3.662  22.464  28.774  1.00 27.43           C  
ANISOU  954  CD  GLU A 124     1441   5030   3950     18    -58  -1279       C  
ATOM    955  OE1 GLU A 124      -4.378  21.735  28.026  1.00 34.15           O  
ANISOU  955  OE1 GLU A 124     2037   6066   4873    384   -508  -2271       O  
ATOM    956  OE2 GLU A 124      -3.943  23.619  29.185  1.00 33.21           O  
ANISOU  956  OE2 GLU A 124     1757   5017   5846    135    -50  -1693       O  
ATOM    957  N   ILE A 125       0.377  19.969  29.551  1.00 12.91           N  
ANISOU  957  N   ILE A 125     1304   1883   1718   -296    488   -119       N  
ATOM    958  CA  ILE A 125       0.998  19.155  28.541  1.00 13.11           C  
ANISOU  958  CA  ILE A 125     1142   1916   1925   -240    350   -275       C  
ATOM    959  C   ILE A 125      -0.069  18.794  27.504  1.00 13.65           C  
ANISOU  959  C   ILE A 125      943   2272   1970   -177    379   -331       C  
ATOM    960  O   ILE A 125      -1.073  18.169  27.825  1.00 16.12           O  
ANISOU  960  O   ILE A 125     1344   2614   2167   -650    378   -183       O  
ATOM    961  CB  ILE A 125       1.587  17.877  29.149  1.00 14.22           C  
ANISOU  961  CB  ILE A 125     1323   1856   2223   -332    322   -147       C  
ATOM    962  CG1 ILE A 125       2.555  18.167  30.281  1.00 15.66           C  
ANISOU  962  CG1 ILE A 125     1647   1968   2335   -158     93      0       C  
ATOM    963  CG2 ILE A 125       2.209  16.968  28.071  1.00 17.43           C  
ANISOU  963  CG2 ILE A 125     1976   2238   2410    324    155   -294       C  
ATOM    964  CD1 ILE A 125       3.054  16.994  31.118  1.00 17.75           C  
ANISOU  964  CD1 ILE A 125     1761   2053   2929    298     78     89       C  
ATOM    965  N   ILE A 126       0.187  19.178  26.264  1.00 13.49           N  
ANISOU  965  N   ILE A 126     1087   2169   1870   -296    412   -460       N  
ATOM    966  CA  ILE A 126      -0.684  18.875  25.140  1.00 14.10           C  
ANISOU  966  CA  ILE A 126     1148   2232   1976   -233    291   -332       C  
ATOM    967  C   ILE A 126      -0.021  17.782  24.319  1.00 13.78           C  
ANISOU  967  C   ILE A 126     1328   2119   1790   -426    261   -364       C  
ATOM    968  O   ILE A 126       1.046  17.998  23.757  1.00 14.49           O  
ANISOU  968  O   ILE A 126     1299   2100   2108   -354    511   -180       O  
ATOM    969  CB  ILE A 126      -0.975  20.137  24.311  1.00 14.34           C  
ANISOU  969  CB  ILE A 126     1124   2333   1990   -110    353   -333       C  
ATOM    970  CG1 ILE A 126      -1.548  21.278  25.136  1.00 16.10           C  
ANISOU  970  CG1 ILE A 126     1319   2422   2375    190    282   -278       C  
ATOM    971  CG2 ILE A 126      -1.872  19.795  23.120  1.00 17.03           C  
ANISOU  971  CG2 ILE A 126     1491   2568   2411   -268    -81   -118       C  
ATOM    972  CD1 ILE A 126      -1.581  22.651  24.473  1.00 19.58           C  
ANISOU  972  CD1 ILE A 126     1655   2394   3392    270   -244   -200       C  
ATOM    973  N   ARG A 127      -0.598  16.595  24.280  1.00 14.83           N  
ANISOU  973  N   ARG A 127     1391   2098   2147   -463    498   -293       N  
ATOM    974  CA  ARG A 127       0.000  15.457  23.619  1.00 15.68           C  
ANISOU  974  CA  ARG A 127     1626   2097   2235   -571    540   -499       C  
ATOM    975  C   ARG A 127      -0.446  15.398  22.183  1.00 16.58           C  
ANISOU  975  C   ARG A 127     1420   2531   2351   -567    426   -602       C  
ATOM    976  O   ARG A 127      -1.649  15.258  21.883  1.00 23.25           O  
ANISOU  976  O   ARG A 127     1412   4672   2751   -723    378   -756       O  
ATOM    977  CB  ARG A 127      -0.406  14.183  24.355  1.00 22.25           C  
ANISOU  977  CB  ARG A 127     3612   2018   2824   -617    869   -359       C  
ATOM    978  CG  ARG A 127      -0.012  14.250  25.826  1.00 27.70           C  
ANISOU  978  CG  ARG A 127     4969   2363   3193    240     21    397       C  
ATOM    979  CD  ARG A 127       1.258  13.518  26.047  1.00 31.88           C  
ANISOU  979  CD  ARG A 127     3403   5256   3456    373    -51  -2438       C  
ATOM    980  NE  ARG A 127       1.854  13.387  27.338  1.00 28.78           N  
ANISOU  980  NE  ARG A 127     3565   4097   3273    879    637   -687       N  
ATOM    981  CZ  ARG A 127       3.156  13.078  27.561  1.00 22.62           C  
ANISOU  981  CZ  ARG A 127     3329   2700   2565    107    772   -156       C  
ATOM    982  NH1 ARG A 127       4.002  12.880  26.595  1.00 23.37           N  
ANISOU  982  NH1 ARG A 127     3148   3128   2604    -17    886    490       N  
ATOM    983  NH2 ARG A 127       3.642  12.986  28.806  1.00 26.74           N  
ANISOU  983  NH2 ARG A 127     4337   3298   2526   -762    452    476       N  
ATOM    984  N   GLY A 128       0.428  15.473  21.217  1.00 14.40           N  
ANISOU  984  N   GLY A 128     1248   2162   2062   -285    128   -257       N  
ATOM    985  CA  GLY A 128       0.104  15.348  19.832  1.00 15.35           C  
ANISOU  985  CA  GLY A 128     1292   2380   2160   -308     62   -286       C  
ATOM    986  C   GLY A 128       1.062  16.219  19.018  1.00 13.81           C  
ANISOU  986  C   GLY A 128     1351   1925   1970    -62      4   -266       C  
ATOM    987  O   GLY A 128       1.994  16.839  19.535  1.00 14.24           O  
ANISOU  987  O   GLY A 128     1356   2002   2052   -141    210   -248       O  
ATOM    988  N   HIS A 129       0.828  16.214  17.692  1.00 15.33           N  
ANISOU  988  N   HIS A 129     1456   2320   2050    -65    -48   -220       N  
ATOM    989  CA  HIS A 129       1.604  16.970  16.727  1.00 15.31           C  
ANISOU  989  CA  HIS A 129     1617   2279   1919     14     64   -353       C  
ATOM    990  C   HIS A 129       0.982  18.309  16.418  1.00 14.19           C  
ANISOU  990  C   HIS A 129     1274   2369   1747     23    -70   -237       C  
ATOM    991  O   HIS A 129      -0.167  18.405  15.968  1.00 16.14           O  
ANISOU  991  O   HIS A 129     1303   2693   2136    -19    -95   -349       O  
ATOM    992  CB  HIS A 129       1.743  16.127  15.439  1.00 16.97           C  
ANISOU  992  CB  HIS A 129     1688   2678   2083     89     35   -612       C  
ATOM    993  CG  HIS A 129       2.513  16.865  14.391  1.00 17.74           C  
ANISOU  993  CG  HIS A 129     2054   2587   2101    243    260   -607       C  
ATOM    994  ND1 HIS A 129       1.969  17.696  13.461  1.00 21.25           N  
ANISOU  994  ND1 HIS A 129     2925   2909   2240    595    397   -463       N  
ATOM    995  CD2 HIS A 129       3.860  16.883  14.162  1.00 20.03           C  
ANISOU  995  CD2 HIS A 129     2160   3644   1805   -285    312   -606       C  
ATOM    996  CE1 HIS A 129       2.898  18.231  12.651  1.00 22.12           C  
ANISOU  996  CE1 HIS A 129     3537   3077   1791     71    417   -662       C  
ATOM    997  NE2 HIS A 129       4.069  17.735  13.079  1.00 23.24           N  
ANISOU  997  NE2 HIS A 129     3066   3814   1951   -312    551   -515       N  
ATOM    998  N   ALA A 130       1.699  19.392  16.683  1.00 13.13           N  
ANISOU  998  N   ALA A 130     1076   2365   1547    157     68   -134       N  
ATOM    999  CA  ALA A 130       1.262  20.757  16.389  1.00 13.55           C  
ANISOU  999  CA  ALA A 130     1277   2280   1592    160    142   -243       C  
ATOM   1000  C   ALA A 130       1.584  21.177  14.964  1.00 13.10           C  
ANISOU 1000  C   ALA A 130     1108   2298   1569     49    -21   -204       C  
ATOM   1001  O   ALA A 130       2.694  20.854  14.474  1.00 15.00           O  
ANISOU 1001  O   ALA A 130     1211   2683   1806    179    233     71       O  
ATOM   1002  CB  ALA A 130       1.884  21.793  17.317  1.00 13.64           C  
ANISOU 1002  CB  ALA A 130     1292   2461   1429     36    136   -151       C  
ATOM   1003  N   ALA A 131       0.702  21.910  14.346  1.00 14.61           N  
ANISOU 1003  N   ALA A 131     1233   2760   1557    190      3   -115       N  
ATOM   1004  CA  ALA A 131       0.948  22.683  13.143  1.00 15.27           C  
ANISOU 1004  CA  ALA A 131     1428   2853   1520    325     27    -35       C  
ATOM   1005  C   ALA A 131       0.268  24.022  13.212  1.00 14.84           C  
ANISOU 1005  C   ALA A 131     1296   2778   1563    224    128   -133       C  
ATOM   1006  O   ALA A 131      -0.788  24.145  13.834  1.00 16.86           O  
ANISOU 1006  O   ALA A 131     1539   3066   1800    455    312    119       O  
ATOM   1007  CB  ALA A 131       0.511  21.930  11.873  1.00 17.07           C  
ANISOU 1007  CB  ALA A 131     2312   2628   1547    285     66    -76       C  
ATOM   1008  N   PHE A 132       0.837  25.033  12.568  1.00 14.71           N  
ANISOU 1008  N   PHE A 132     1313   2841   1438    469    178      4       N  
ATOM   1009  CA  PHE A 132       0.177  26.320  12.504  1.00 15.92           C  
ANISOU 1009  CA  PHE A 132     1373   2862   1812    475    123     48       C  
ATOM   1010  C   PHE A 132      -1.048  26.296  11.605  1.00 17.03           C  
ANISOU 1010  C   PHE A 132     1625   3199   1648    606    -33    152       C  
ATOM   1011  O   PHE A 132      -1.122  25.515  10.659  1.00 19.19           O  
ANISOU 1011  O   PHE A 132     1846   3659   1785    429   -124    -35       O  
ATOM   1012  CB  PHE A 132       1.175  27.397  11.977  1.00 16.88           C  
ANISOU 1012  CB  PHE A 132     1809   2793   1813    366    174     14       C  
ATOM   1013  CG  PHE A 132       2.272  27.694  13.005  1.00 14.44           C  
ANISOU 1013  CG  PHE A 132     1729   2237   1521    294    241    226       C  
ATOM   1014  CD1 PHE A 132       3.533  27.142  12.938  1.00 14.96           C  
ANISOU 1014  CD1 PHE A 132     1699   2352   1635    172    177    -89       C  
ATOM   1015  CD2 PHE A 132       1.996  28.578  14.072  1.00 15.48           C  
ANISOU 1015  CD2 PHE A 132     2003   2302   1577    511    243    292       C  
ATOM   1016  CE1 PHE A 132       4.478  27.434  13.883  1.00 15.79           C  
ANISOU 1016  CE1 PHE A 132     1862   2397   1740    318    -43   -195       C  
ATOM   1017  CE2 PHE A 132       2.962  28.829  15.045  1.00 16.86           C  
ANISOU 1017  CE2 PHE A 132     2225   2535   1646    569    140    -14       C  
ATOM   1018  CZ  PHE A 132       4.208  28.268  14.958  1.00 16.02           C  
ANISOU 1018  CZ  PHE A 132     2145   2508   1433    612     38    -32       C  
ATOM   1019  N   THR A 133      -1.974  27.168  11.921  1.00 19.45           N  
ANISOU 1019  N   THR A 133     1692   3755   1941    960     61    323       N  
ATOM   1020  CA  THR A 133      -3.126  27.406  11.036  1.00 22.64           C  
ANISOU 1020  CA  THR A 133     1864   4549   2188   1062    -70    777       C  
ATOM   1021  C   THR A 133      -2.979  28.710  10.284  1.00 24.65           C  
ANISOU 1021  C   THR A 133     2310   4889   2167   1307    206   1028       C  
ATOM   1022  O   THR A 133      -2.046  29.466  10.569  1.00 26.39           O  
ANISOU 1022  O   THR A 133     2690   4500   2836   1079    726    751       O  
ATOM   1023  CB  THR A 133      -4.448  27.463  11.838  1.00 22.81           C  
ANISOU 1023  CB  THR A 133     1774   4290   2603    625     28    246       C  
ATOM   1024  OG1 THR A 133      -4.492  28.737  12.474  1.00 24.56           O  
ANISOU 1024  OG1 THR A 133     2219   4405   2707    680     50    101       O  
ATOM   1025  CG2 THR A 133      -4.564  26.378  12.892  1.00 24.84           C  
ANISOU 1025  CG2 THR A 133     1866   4541   3030    203    174    495       C  
ATOM   1026  N   SER A 134      -3.947  28.938   9.391  1.00 30.10           N  
ANISOU 1026  N   SER A 134     2856   5948   2631   2011    -70   1312       N  
ATOM   1027  CA  SER A 134      -3.888  30.174   8.620  1.00 35.87           C  
ANISOU 1027  CA  SER A 134     5076   5886   2666   2508   -282   1244       C  
ATOM   1028  C   SER A 134      -4.521  31.402   9.285  1.00 39.61           C  
ANISOU 1028  C   SER A 134     5273   6279   3497   3066   -160   1200       C  
ATOM   1029  O   SER A 134      -4.604  32.480   8.648  1.00 41.71           O  
ANISOU 1029  O   SER A 134     6190   6060   3598   2968   -123   1075       O  
ATOM   1030  CB ASER A 134      -4.583  30.015   7.245  0.73 45.69           C  
ANISOU 1030  CB ASER A 134     7286   7488   2587   2523   -830   1493       C  
ATOM   1031  CB BSER A 134      -4.514  29.944   7.229  0.27 41.30           C  
ANISOU 1031  CB BSER A 134     5982   7212   2500   1940   -362   1568       C  
ATOM   1032  OG ASER A 134      -5.889  29.489   7.421  0.73 57.81           O  
ANISOU 1032  OG ASER A 134     6571  10254   5140   2213  -2792   1905       O  
ATOM   1033  OG BSER A 134      -3.702  29.034   6.491  0.27 30.79           O  
ANISOU 1033  OG BSER A 134     2556   6840   2302   -783    304   1149       O  
ATOM   1034  N   ASP A 135      -4.958  31.267  10.514  1.00 33.04           N  
ANISOU 1034  N   ASP A 135     2949   5691   3915   2281      9    937       N  
ATOM   1035  CA  ASP A 135      -5.510  32.381  11.275  1.00 35.46           C  
ANISOU 1035  CA  ASP A 135     3243   5864   4366   2344   -386    408       C  
ATOM   1036  C   ASP A 135      -4.476  33.498  11.350  1.00 43.69           C  
ANISOU 1036  C   ASP A 135     5487   5543   5571   1523  -2140   1591       C  
ATOM   1037  O   ASP A 135      -3.302  33.266  11.698  1.00 40.06           O  
ANISOU 1037  O   ASP A 135     4242   4843   6134    759   -361   2609       O  
ATOM   1038  CB  ASP A 135      -5.983  31.905  12.659  1.00 40.10           C  
ANISOU 1038  CB  ASP A 135     3772   6869   4596   3113    438    444       C  
ATOM   1039  CG  ASP A 135      -6.966  30.745  12.469  1.00 48.93           C  
ANISOU 1039  CG  ASP A 135     3127   8449   7015   2099   -515   2811       C  
ATOM   1040  OD1 ASP A 135      -6.854  29.665  13.084  1.00 43.93           O  
ANISOU 1040  OD1 ASP A 135     5123   7598   3971   2302    284   1235       O  
ATOM   1041  OD2 ASP A 135      -7.907  30.932  11.642  1.00 70.44           O  
ANISOU 1041  OD2 ASP A 135     6798   7776  12189   2799  -4906   1632       O  
ATOM   1042  N   PRO A 136      -4.858  34.714  10.967  1.00 51.95           N  
ANISOU 1042  N   PRO A 136     7333   5683   6723   2046  -3164   1372       N  
ATOM   1043  CA  PRO A 136      -3.864  35.808  10.993  1.00 48.38           C  
ANISOU 1043  CA  PRO A 136     7594   5694   5093   1808  -1058   2637       C  
ATOM   1044  C   PRO A 136      -3.232  35.978  12.362  1.00 39.02           C  
ANISOU 1044  C   PRO A 136     3242   5864   5720   1557   -532   2074       C  
ATOM   1045  O   PRO A 136      -2.026  36.211  12.452  1.00 53.31           O  
ANISOU 1045  O   PRO A 136     3446   5965  10845    874   -443   2488       O  
ATOM   1046  CB  PRO A 136      -4.698  37.044  10.620  1.00 63.12           C  
ANISOU 1046  CB  PRO A 136    10231   6059   7694   2218  -3742   2822       C  
ATOM   1047  CG  PRO A 136      -5.727  36.456   9.699  1.00 67.03           C  
ANISOU 1047  CG  PRO A 136    10260   6561   8646   2260  -4108   2514       C  
ATOM   1048  CD  PRO A 136      -6.142  35.213  10.453  1.00 58.85           C  
ANISOU 1048  CD  PRO A 136     7837   6614   7909   2833  -3106   2099       C  
ATOM   1049  N   LYS A 137      -4.049  35.811  13.394  1.00 37.43           N  
ANISOU 1049  N   LYS A 137     4051   4934   5236   2511    -23    411       N  
ATOM   1050  CA  LYS A 137      -3.482  35.680  14.726  1.00 31.22           C  
ANISOU 1050  CA  LYS A 137     2859   3567   5438   1408    -86    394       C  
ATOM   1051  C   LYS A 137      -2.842  34.298  14.956  1.00 24.34           C  
ANISOU 1051  C   LYS A 137     1765   3266   4215    867    619    174       C  
ATOM   1052  O   LYS A 137      -3.602  33.305  14.837  1.00 27.76           O  
ANISOU 1052  O   LYS A 137     2340   3674   4532    380   -546   1179       O  
ATOM   1053  CB  LYS A 137      -4.557  35.821  15.786  1.00 37.81           C  
ANISOU 1053  CB  LYS A 137     4373   4680   5312   2696    276  -1015       C  
ATOM   1054  CG  LYS A 137      -4.035  35.695  17.211  1.00 51.49           C  
ANISOU 1054  CG  LYS A 137     8890   5577   5097   2444   -354   -928       C  
ATOM   1055  CD  LYS A 137      -5.109  36.076  18.228  1.00 58.32           C  
ANISOU 1055  CD  LYS A 137     9335   8051   4774   2496     83   -306       C  
ATOM   1056  CE  LYS A 137      -5.315  34.989  19.275  1.00 71.80           C  
ANISOU 1056  CE  LYS A 137    12863   9872   4547   1649   -226    454       C  
ATOM   1057  NZ  LYS A 137      -6.459  35.281  20.193  1.00 87.19           N  
ANISOU 1057  NZ  LYS A 137    15626  14624   2879    755   1064   -553       N  
ATOM   1058  N   PRO A 138      -1.553  34.250  15.232  1.00 22.96           N  
ANISOU 1058  N   PRO A 138     2094   3084   3545    705    -94    239       N  
ATOM   1059  CA  PRO A 138      -0.902  32.939  15.293  1.00 19.77           C  
ANISOU 1059  CA  PRO A 138     1810   2971   2732    603    330    -55       C  
ATOM   1060  C   PRO A 138      -1.574  31.951  16.241  1.00 19.25           C  
ANISOU 1060  C   PRO A 138     1620   3117   2580    577    268     41       C  
ATOM   1061  O   PRO A 138      -1.808  32.241  17.412  1.00 19.54           O  
ANISOU 1061  O   PRO A 138     1725   3009   2691    555    276   -160       O  
ATOM   1062  CB  PRO A 138       0.514  33.278  15.746  1.00 20.65           C  
ANISOU 1062  CB  PRO A 138     1844   3025   2975    414    230    214       C  
ATOM   1063  CG  PRO A 138       0.750  34.657  15.214  1.00 23.65           C  
ANISOU 1063  CG  PRO A 138     2191   3092   3702    393    209    469       C  
ATOM   1064  CD  PRO A 138      -0.576  35.350  15.410  1.00 25.06           C  
ANISOU 1064  CD  PRO A 138     2371   2952   4198    530    181    329       C  
ATOM   1065  N   THR A 139      -1.874  30.800  15.680  1.00 18.20           N  
ANISOU 1065  N   THR A 139     1781   2984   2149    725    457    265       N  
ATOM   1066  CA  THR A 139      -2.698  29.748  16.298  1.00 18.01           C  
ANISOU 1066  CA  THR A 139     1712   2987   2146    631    521    136       C  
ATOM   1067  C   THR A 139      -2.146  28.431  15.795  1.00 16.68           C  
ANISOU 1067  C   THR A 139     1866   3002   1469    731    222     56       C  
ATOM   1068  O   THR A 139      -1.692  28.308  14.635  1.00 19.96           O  
ANISOU 1068  O   THR A 139     2382   3552   1648    801    631    187       O  
ATOM   1069  CB  THR A 139      -4.166  29.921  15.842  1.00 21.66           C  
ANISOU 1069  CB  THR A 139     1782   3423   3024    836    181    248       C  
ATOM   1070  OG1 THR A 139      -4.599  31.223  16.223  1.00 23.99           O  
ANISOU 1070  OG1 THR A 139     1905   3524   3688    873    -44   -107       O  
ATOM   1071  CG2 THR A 139      -5.161  28.929  16.393  1.00 21.86           C  
ANISOU 1071  CG2 THR A 139     1788   3733   2783    320   -229   -181       C  
ATOM   1072  N   ILE A 140      -2.171  27.433  16.634  1.00 14.78           N  
ANISOU 1072  N   ILE A 140     1346   2827   1441    457    177   -114       N  
ATOM   1073  CA  ILE A 140      -1.775  26.083  16.283  1.00 15.05           C  
ANISOU 1073  CA  ILE A 140     1324   2778   1618    338    218   -229       C  
ATOM   1074  C   ILE A 140      -2.994  25.148  16.468  1.00 15.64           C  
ANISOU 1074  C   ILE A 140     1330   2855   1757    394    244   -208       C  
ATOM   1075  O   ILE A 140      -3.908  25.476  17.201  1.00 17.55           O  
ANISOU 1075  O   ILE A 140     1483   3163   2023    290    445   -500       O  
ATOM   1076  CB  ILE A 140      -0.588  25.557  17.112  1.00 15.94           C  
ANISOU 1076  CB  ILE A 140     1298   2735   2024    333    221    110       C  
ATOM   1077  CG1 ILE A 140      -0.912  25.486  18.577  1.00 18.30           C  
ANISOU 1077  CG1 ILE A 140     1461   3486   2006    550    177    435       C  
ATOM   1078  CG2 ILE A 140       0.636  26.419  16.833  1.00 17.63           C  
ANISOU 1078  CG2 ILE A 140     1382   2944   2373    175     39    371       C  
ATOM   1079  CD1 ILE A 140       0.149  24.792  19.459  1.00 22.28           C  
ANISOU 1079  CD1 ILE A 140     2598   3589   2280   1515    -47    174       C  
ATOM   1080  N   GLU A 141      -2.920  24.026  15.771  1.00 16.14           N  
ANISOU 1080  N   GLU A 141     1587   2770   1776    337    306   -258       N  
ATOM   1081  CA  GLU A 141      -3.903  22.947  15.910  1.00 16.33           C  
ANISOU 1081  CA  GLU A 141     1475   3032   1698    282    185   -322       C  
ATOM   1082  C   GLU A 141      -3.157  21.674  16.307  1.00 14.98           C  
ANISOU 1082  C   GLU A 141     1419   2598   1673     69     86   -637       C  
ATOM   1083  O   GLU A 141      -2.081  21.369  15.750  1.00 16.14           O  
ANISOU 1083  O   GLU A 141     1436   2873   1824    264    210   -422       O  
ATOM   1084  CB  GLU A 141      -4.740  22.797  14.631  1.00 21.53           C  
ANISOU 1084  CB  GLU A 141     1895   3920   2366    182   -453   -134       C  
ATOM   1085  CG  GLU A 141      -5.818  21.754  14.768  1.00 30.56           C  
ANISOU 1085  CG  GLU A 141     1948   6515   3149  -1099   -265   -454       C  
ATOM   1086  CD  GLU A 141      -6.667  21.635  13.524  1.00 43.87           C  
ANISOU 1086  CD  GLU A 141     2972   9604   4091  -1835  -1219   -669       C  
ATOM   1087  OE1 GLU A 141      -6.237  21.738  12.352  1.00 58.12           O  
ANISOU 1087  OE1 GLU A 141     4526  13943   3613  -1054  -1552   -149       O  
ATOM   1088  OE2 GLU A 141      -7.863  21.425  13.786  1.00 64.21           O  
ANISOU 1088  OE2 GLU A 141     3028  15144   6226  -3146  -1516   -914       O  
ATOM   1089  N   VAL A 142      -3.700  20.940  17.264  1.00 16.08           N  
ANISOU 1089  N   VAL A 142     1290   2736   2085     34    212   -475       N  
ATOM   1090  CA  VAL A 142      -3.191  19.683  17.753  1.00 16.37           C  
ANISOU 1090  CA  VAL A 142     1572   2413   2236   -111    282   -559       C  
ATOM   1091  C   VAL A 142      -4.406  18.746  17.859  1.00 20.49           C  
ANISOU 1091  C   VAL A 142     1537   2664   3585   -186    496   -811       C  
ATOM   1092  O   VAL A 142      -5.334  19.080  18.629  1.00 20.47           O  
ANISOU 1092  O   VAL A 142     1504   3027   3248   -121    459   -528       O  
ATOM   1093  CB  VAL A 142      -2.488  19.788  19.101  1.00 16.33           C  
ANISOU 1093  CB  VAL A 142     1550   2562   2092    132    426   -358       C  
ATOM   1094  CG1 VAL A 142      -1.854  18.428  19.450  1.00 18.75           C  
ANISOU 1094  CG1 VAL A 142     1962   2876   2287    519    542   -335       C  
ATOM   1095  CG2 VAL A 142      -1.478  20.903  19.115  1.00 15.96           C  
ANISOU 1095  CG2 VAL A 142     1217   3002   1843     -4    170   -132       C  
ATOM   1096  N   SER A 143      -4.436  17.656  17.117  1.00 22.05           N  
ANISOU 1096  N   SER A 143     1637   2595   4144   -184    244   -949       N  
ATOM   1097  CA  SER A 143      -5.546  16.701  17.206  1.00 24.69           C  
ANISOU 1097  CA  SER A 143     1771   3229   4379   -554    364  -1154       C  
ATOM   1098  C   SER A 143      -6.907  17.416  17.038  1.00 25.92           C  
ANISOU 1098  C   SER A 143     1651   3289   4908   -540    446  -1595       C  
ATOM   1099  O   SER A 143      -7.854  17.076  17.718  1.00 30.88           O  
ANISOU 1099  O   SER A 143     2018   3732   5983   -724   1104  -1927       O  
ATOM   1100  CB  SER A 143      -5.464  15.877  18.484  1.00 31.92           C  
ANISOU 1100  CB  SER A 143     3300   3293   5534   -198   1171   -152       C  
ATOM   1101  OG  SER A 143      -4.192  15.255  18.623  1.00 44.76           O  
ANISOU 1101  OG  SER A 143     3388   4269   9348   -376    349   2291       O  
ATOM   1102  N   GLY A 144      -6.995  18.379  16.116  1.00 26.41           N  
ANISOU 1102  N   GLY A 144     1686   3640   4708   -184   -187  -1656       N  
ATOM   1103  CA  GLY A 144      -8.233  19.018  15.781  1.00 28.53           C  
ANISOU 1103  CA  GLY A 144     1734   4616   4490    109   -346  -2218       C  
ATOM   1104  C   GLY A 144      -8.655  20.094  16.768  1.00 27.25           C  
ANISOU 1104  C   GLY A 144     1674   4514   4164    225   -373  -1959       C  
ATOM   1105  O   GLY A 144      -9.765  20.648  16.646  1.00 41.28           O  
ANISOU 1105  O   GLY A 144     1979   7466   6242   1352  -1135  -4113       O  
ATOM   1106  N   LYS A 145      -7.856  20.411  17.784  1.00 22.47           N  
ANISOU 1106  N   LYS A 145     1300   3762   3475   -339    204  -1307       N  
ATOM   1107  CA  LYS A 145      -8.170  21.420  18.765  1.00 20.67           C  
ANISOU 1107  CA  LYS A 145     1141   3508   3205   -124    101   -970       C  
ATOM   1108  C   LYS A 145      -7.208  22.587  18.541  1.00 18.79           C  
ANISOU 1108  C   LYS A 145     1205   3254   2681     37    150   -732       C  
ATOM   1109  O   LYS A 145      -6.014  22.362  18.275  1.00 18.03           O  
ANISOU 1109  O   LYS A 145     1217   3119   2515    -73    215   -748       O  
ATOM   1110  CB ALYS A 145      -8.072  20.965  20.220  0.57 22.32           C  
ANISOU 1110  CB ALYS A 145     1668   3541   3271   -419    518   -720       C  
ATOM   1111  CB BLYS A 145      -8.118  20.908  20.202  0.43 20.74           C  
ANISOU 1111  CB BLYS A 145     1272   3278   3329   -622    332   -812       C  
ATOM   1112  CG ALYS A 145      -8.864  19.754  20.645  0.57 26.08           C  
ANISOU 1112  CG ALYS A 145     2289   3105   4515   -362   -548    -82       C  
ATOM   1113  CG BLYS A 145      -8.372  22.032  21.198  0.43 27.10           C  
ANISOU 1113  CG BLYS A 145     3759   3450   3089   -343   -460   -975       C  
ATOM   1114  CD ALYS A 145      -8.163  18.996  21.762  0.57 48.12           C  
ANISOU 1114  CD ALYS A 145     7441   5369   5472  -1324  -2759   1408       C  
ATOM   1115  CD BLYS A 145      -8.757  21.438  22.543  0.43 29.80           C  
ANISOU 1115  CD BLYS A 145     3792   4229   3300   -540    396  -1156       C  
ATOM   1116  CE ALYS A 145      -8.671  19.456  23.122  0.57 54.91           C  
ANISOU 1116  CE ALYS A 145     9755   5967   5142   -140  -3445   1090       C  
ATOM   1117  CE BLYS A 145      -8.598  22.457  23.668  0.43 38.03           C  
ANISOU 1117  CE BLYS A 145     6543   4844   3061  -1112   -378  -1108       C  
ATOM   1118  NZ ALYS A 145      -8.321  18.514  24.230  0.57 67.39           N  
ANISOU 1118  NZ ALYS A 145    13194   7311   5099  -1981  -5514   1601       N  
ATOM   1119  NZ BLYS A 145      -9.818  22.484  24.525  0.43 50.38           N  
ANISOU 1119  NZ BLYS A 145     7429   6534   5177   2250    777  -2663       N  
ATOM   1120  N   LYS A 146      -7.688  23.829  18.693  1.00 20.06           N  
ANISOU 1120  N   LYS A 146     1000   3489   3132    -14    116  -1198       N  
ATOM   1121  CA  LYS A 146      -6.870  25.003  18.418  1.00 18.29           C  
ANISOU 1121  CA  LYS A 146     1238   3092   2620    210    -23  -1021       C  
ATOM   1122  C   LYS A 146      -6.444  25.718  19.690  1.00 16.25           C  
ANISOU 1122  C   LYS A 146     1078   2863   2234    217    300   -746       C  
ATOM   1123  O   LYS A 146      -7.153  25.787  20.700  1.00 17.48           O  
ANISOU 1123  O   LYS A 146     1091   3286   2264    -88    287   -597       O  
ATOM   1124  CB  LYS A 146      -7.613  26.007  17.539  1.00 21.93           C  
ANISOU 1124  CB  LYS A 146     1564   3959   2810    324   -456   -826       C  
ATOM   1125  CG  LYS A 146      -7.940  25.485  16.139  1.00 26.93           C  
ANISOU 1125  CG  LYS A 146     2098   5008   3125    111   -973  -1165       C  
ATOM   1126  CD  LYS A 146      -8.541  26.603  15.268  1.00 40.46           C  
ANISOU 1126  CD  LYS A 146     3646   7440   4288    813  -2304    -66       C  
ATOM   1127  CE  LYS A 146      -8.586  26.026  13.845  1.00 53.33           C  
ANISOU 1127  CE  LYS A 146     6979   9034   4251    124  -3268   -238       C  
ATOM   1128  NZ  LYS A 146      -8.688  27.100  12.810  1.00 70.70           N  
ANISOU 1128  NZ  LYS A 146    10224  11827   4812   1981  -3348   1284       N  
ATOM   1129  N   TYR A 147      -5.209  26.273  19.672  1.00 14.33           N  
ANISOU 1129  N   TYR A 147     1052   2596   1797    203    133   -460       N  
ATOM   1130  CA  TYR A 147      -4.598  26.925  20.786  1.00 13.58           C  
ANISOU 1130  CA  TYR A 147     1164   2493   1503    173    378   -408       C  
ATOM   1131  C   TYR A 147      -3.908  28.198  20.323  1.00 13.87           C  
ANISOU 1131  C   TYR A 147     1020   2678   1571     23    292   -321       C  
ATOM   1132  O   TYR A 147      -3.334  28.170  19.219  1.00 14.95           O  
ANISOU 1132  O   TYR A 147     1387   2655   1639     55    371   -237       O  
ATOM   1133  CB  TYR A 147      -3.559  26.020  21.432  1.00 14.97           C  
ANISOU 1133  CB  TYR A 147     1086   2679   1922     -6     89   -259       C  
ATOM   1134  CG  TYR A 147      -4.050  24.669  21.877  1.00 14.71           C  
ANISOU 1134  CG  TYR A 147     1053   2536   2002    138    248   -221       C  
ATOM   1135  CD1 TYR A 147      -4.492  24.429  23.169  1.00 16.38           C  
ANISOU 1135  CD1 TYR A 147     1320   2874   2031   -128    378   -362       C  
ATOM   1136  CD2 TYR A 147      -4.101  23.603  20.981  1.00 15.60           C  
ANISOU 1136  CD2 TYR A 147     1123   2737   2069   -104    310   -339       C  
ATOM   1137  CE1 TYR A 147      -4.958  23.167  23.551  1.00 17.31           C  
ANISOU 1137  CE1 TYR A 147     1605   3010   1964   -172    467   -241       C  
ATOM   1138  CE2 TYR A 147      -4.584  22.349  21.381  1.00 15.69           C  
ANISOU 1138  CE2 TYR A 147     1244   2574   2143     86    371   -440       C  
ATOM   1139  CZ  TYR A 147      -4.998  22.126  22.660  1.00 16.56           C  
ANISOU 1139  CZ  TYR A 147     1266   2769   2256   -230    248   -171       C  
ATOM   1140  OH  TYR A 147      -5.462  20.902  23.086  1.00 19.77           O  
ANISOU 1140  OH  TYR A 147     1784   2745   2983    -99    426    125       O  
ATOM   1141  N   THR A 148      -3.923  29.268  21.087  1.00 15.48           N  
ANISOU 1141  N   THR A 148     1289   2889   1703   -370    415   -499       N  
ATOM   1142  CA  THR A 148      -3.280  30.506  20.698  1.00 16.46           C  
ANISOU 1142  CA  THR A 148     1772   2763   1717   -269    539   -522       C  
ATOM   1143  C   THR A 148      -2.585  31.125  21.904  1.00 15.00           C  
ANISOU 1143  C   THR A 148     1479   2506   1715   -247    542   -355       C  
ATOM   1144  O   THR A 148      -2.894  30.782  23.067  1.00 16.53           O  
ANISOU 1144  O   THR A 148     1540   3039   1700   -420    564   -345       O  
ATOM   1145  CB  THR A 148      -4.274  31.480  20.056  1.00 18.46           C  
ANISOU 1145  CB  THR A 148     1970   3118   1925   -295    280   -221       C  
ATOM   1146  OG1 THR A 148      -3.532  32.556  19.493  1.00 21.00           O  
ANISOU 1146  OG1 THR A 148     2740   3124   2115   -496    405   -131       O  
ATOM   1147  CG2 THR A 148      -5.183  32.051  21.125  1.00 19.09           C  
ANISOU 1147  CG2 THR A 148     1912   3293   2046    130    209   -135       C  
ATOM   1148  N   ALA A 149      -1.646  32.013  21.619  1.00 14.34           N  
ANISOU 1148  N   ALA A 149     1267   2345   1838     -9    486   -195       N  
ATOM   1149  CA  ALA A 149      -0.950  32.799  22.622  1.00 13.58           C  
ANISOU 1149  CA  ALA A 149     1064   2104   1992    273    356   -230       C  
ATOM   1150  C   ALA A 149      -0.315  33.995  21.927  1.00 12.96           C  
ANISOU 1150  C   ALA A 149      870   2097   1959    400    128    -37       C  
ATOM   1151  O   ALA A 149       0.027  33.887  20.731  1.00 14.65           O  
ANISOU 1151  O   ALA A 149     1273   2270   2023    285    342    -93       O  
ATOM   1152  CB  ALA A 149       0.147  32.009  23.329  1.00 13.88           C  
ANISOU 1152  CB  ALA A 149     1194   1946   2135    324    434    -18       C  
ATOM   1153  N   PRO A 150      -0.029  35.064  22.684  1.00 13.98           N  
ANISOU 1153  N   PRO A 150     1263   2007   2043    440    237    -87       N  
ATOM   1154  CA  PRO A 150       0.738  36.161  22.101  1.00 14.87           C  
ANISOU 1154  CA  PRO A 150     1373   1901   2375    533    282      8       C  
ATOM   1155  C   PRO A 150       2.207  35.824  21.897  1.00 13.70           C  
ANISOU 1155  C   PRO A 150     1395   1809   2001    531    337    168       C  
ATOM   1156  O   PRO A 150       2.937  36.602  21.250  1.00 14.63           O  
ANISOU 1156  O   PRO A 150     1611   1849   2100    501    384    357       O  
ATOM   1157  CB  PRO A 150       0.596  37.262  23.139  1.00 16.74           C  
ANISOU 1157  CB  PRO A 150     1464   2096   2800    369    440   -389       C  
ATOM   1158  CG  PRO A 150       0.280  36.577  24.395  1.00 20.84           C  
ANISOU 1158  CG  PRO A 150     3110   2299   2508     30    392   -491       C  
ATOM   1159  CD  PRO A 150      -0.525  35.333  24.049  1.00 15.55           C  
ANISOU 1159  CD  PRO A 150     1601   2134   2173    550    354   -169       C  
ATOM   1160  N   HIS A 151       2.661  34.728  22.462  1.00 11.80           N  
ANISOU 1160  N   HIS A 151     1115   1561   1808    204    215     75       N  
ATOM   1161  CA  HIS A 151       4.021  34.269  22.357  1.00 11.55           C  
ANISOU 1161  CA  HIS A 151     1133   1737   1518    326    320     48       C  
ATOM   1162  C   HIS A 151       4.045  32.759  22.079  1.00 11.22           C  
ANISOU 1162  C   HIS A 151     1139   1715   1409    279    124     83       C  
ATOM   1163  O   HIS A 151       3.569  31.998  22.943  1.00 11.68           O  
ANISOU 1163  O   HIS A 151     1218   1756   1465    248    288     32       O  
ATOM   1164  CB  HIS A 151       4.769  34.583  23.654  1.00 11.74           C  
ANISOU 1164  CB  HIS A 151     1117   1690   1652    197    317      8       C  
ATOM   1165  CG  HIS A 151       4.781  36.038  24.033  1.00 12.21           C  
ANISOU 1165  CG  HIS A 151     1170   1740   1729    289    284    -68       C  
ATOM   1166  ND1 HIS A 151       5.454  36.995  23.385  1.00 13.59           N  
ANISOU 1166  ND1 HIS A 151     1467   1634   2063    155    400   -129       N  
ATOM   1167  CD2 HIS A 151       4.117  36.593  25.073  1.00 14.65           C  
ANISOU 1167  CD2 HIS A 151     1860   1989   1717    336    328   -174       C  
ATOM   1168  CE1 HIS A 151       5.203  38.170  23.993  1.00 14.24           C  
ANISOU 1168  CE1 HIS A 151     1646   1767   1997    364    394   -181       C  
ATOM   1169  NE2 HIS A 151       4.405  37.957  25.043  1.00 15.19           N  
ANISOU 1169  NE2 HIS A 151     1662   1964   2147    270    412   -316       N  
ATOM   1170  N   ILE A 152       4.578  32.348  20.959  1.00 10.97           N  
ANISOU 1170  N   ILE A 152     1109   1559   1499    258    183     48       N  
ATOM   1171  CA  ILE A 152       4.684  30.950  20.584  1.00 10.63           C  
ANISOU 1171  CA  ILE A 152     1068   1557   1413    107    252     82       C  
ATOM   1172  C   ILE A 152       6.140  30.641  20.268  1.00  9.95           C  
ANISOU 1172  C   ILE A 152     1124   1492   1164    196    180     60       C  
ATOM   1173  O   ILE A 152       6.718  31.276  19.401  1.00 11.49           O  
ANISOU 1173  O   ILE A 152     1121   1820   1425    157    240    300       O  
ATOM   1174  CB  ILE A 152       3.768  30.594  19.364  1.00 11.70           C  
ANISOU 1174  CB  ILE A 152     1059   1827   1560     75    221      6       C  
ATOM   1175  CG1 ILE A 152       2.298  30.943  19.673  1.00 13.50           C  
ANISOU 1175  CG1 ILE A 152      992   2111   2028    190     69     35       C  
ATOM   1176  CG2 ILE A 152       3.952  29.161  18.991  1.00 12.31           C  
ANISOU 1176  CG2 ILE A 152     1318   1819   1543    101    232   -153       C  
ATOM   1177  CD1 ILE A 152       1.337  30.725  18.548  1.00 15.37           C  
ANISOU 1177  CD1 ILE A 152     1196   2762   1883    477     55    -57       C  
ATOM   1178  N   LEU A 153       6.680  29.659  20.970  1.00 10.64           N  
ANISOU 1178  N   LEU A 153     1030   1651   1360    228    280    232       N  
ATOM   1179  CA  LEU A 153       8.063  29.206  20.770  1.00 10.10           C  
ANISOU 1179  CA  LEU A 153      941   1526   1370    157    164     42       C  
ATOM   1180  C   LEU A 153       8.079  27.918  19.996  1.00 10.18           C  
ANISOU 1180  C   LEU A 153     1037   1525   1307    235    153    149       C  
ATOM   1181  O   LEU A 153       7.426  26.923  20.377  1.00 11.49           O  
ANISOU 1181  O   LEU A 153     1267   1577   1522     89    238    115       O  
ATOM   1182  CB  LEU A 153       8.719  28.988  22.170  1.00 10.43           C  
ANISOU 1182  CB  LEU A 153     1106   1588   1268    182    267    164       C  
ATOM   1183  CG  LEU A 153      10.124  28.348  22.053  1.00 10.17           C  
ANISOU 1183  CG  LEU A 153      958   1528   1379     37    106    168       C  
ATOM   1184  CD1 LEU A 153      11.089  29.247  21.272  1.00  9.99           C  
ANISOU 1184  CD1 LEU A 153     1115   1494   1189     32    210     67       C  
ATOM   1185  CD2 LEU A 153      10.654  28.014  23.431  1.00 10.60           C  
ANISOU 1185  CD2 LEU A 153     1284   1498   1245    140    225    100       C  
ATOM   1186  N   ILE A 154       8.813  27.898  18.886  1.00 10.15           N  
ANISOU 1186  N   ILE A 154     1088   1455   1314    105    227     40       N  
ATOM   1187  CA  ILE A 154       9.083  26.696  18.097  1.00 10.50           C  
ANISOU 1187  CA  ILE A 154     1150   1483   1358    171    104    -33       C  
ATOM   1188  C   ILE A 154      10.393  26.115  18.579  1.00 10.00           C  
ANISOU 1188  C   ILE A 154     1067   1513   1220    198    246     -8       C  
ATOM   1189  O   ILE A 154      11.471  26.732  18.460  1.00 10.52           O  
ANISOU 1189  O   ILE A 154     1085   1538   1374     99    176     97       O  
ATOM   1190  CB  ILE A 154       9.152  27.000  16.591  1.00 11.76           C  
ANISOU 1190  CB  ILE A 154     1478   1675   1316    320     25    -22       C  
ATOM   1191  CG1 ILE A 154       7.897  27.721  16.091  1.00 13.28           C  
ANISOU 1191  CG1 ILE A 154     1642   1787   1619    248   -279     74       C  
ATOM   1192  CG2 ILE A 154       9.377  25.701  15.849  1.00 14.06           C  
ANISOU 1192  CG2 ILE A 154     2143   1837   1362    227     41   -209       C  
ATOM   1193  CD1 ILE A 154       8.062  28.331  14.706  1.00 15.95           C  
ANISOU 1193  CD1 ILE A 154     2303   2139   1618    370   -405    121       C  
ATOM   1194  N   ALA A 155      10.320  24.920  19.190  1.00  9.78           N  
ANISOU 1194  N   ALA A 155      989   1509   1218    139    239     92       N  
ATOM   1195  CA  ALA A 155      11.489  24.230  19.764  1.00  9.56           C  
ANISOU 1195  CA  ALA A 155      999   1373   1260    128    284    -62       C  
ATOM   1196  C   ALA A 155      11.407  22.748  19.404  1.00  9.54           C  
ANISOU 1196  C   ALA A 155      997   1410   1220    126    296   -105       C  
ATOM   1197  O   ALA A 155      11.488  21.869  20.240  1.00 10.13           O  
ANISOU 1197  O   ALA A 155     1080   1455   1314    119    194     14       O  
ATOM   1198  CB  ALA A 155      11.547  24.460  21.257  1.00 11.41           C  
ANISOU 1198  CB  ALA A 155     1606   1432   1296    191     86   -113       C  
ATOM   1199  N   THR A 156      11.281  22.469  18.090  1.00  9.91           N  
ANISOU 1199  N   THR A 156     1056   1482   1226    128    272   -127       N  
ATOM   1200  CA  THR A 156      10.974  21.157  17.592  1.00 10.36           C  
ANISOU 1200  CA  THR A 156     1033   1602   1302    111    128   -214       C  
ATOM   1201  C   THR A 156      12.195  20.313  17.246  1.00  9.60           C  
ANISOU 1201  C   THR A 156     1046   1517   1086     23    292   -223       C  
ATOM   1202  O   THR A 156      12.040  19.178  16.813  1.00 10.83           O  
ANISOU 1202  O   THR A 156     1159   1560   1396     71    262   -252       O  
ATOM   1203  CB  THR A 156      10.053  21.263  16.354  1.00 11.16           C  
ANISOU 1203  CB  THR A 156     1008   1947   1287     45    260   -140       C  
ATOM   1204  OG1 THR A 156      10.653  22.187  15.450  1.00 11.90           O  
ANISOU 1204  OG1 THR A 156     1382   1785   1353    118    181    -23       O  
ATOM   1205  CG2 THR A 156       8.663  21.763  16.798  1.00 11.81           C  
ANISOU 1205  CG2 THR A 156     1151   1873   1463    218     50   -300       C  
ATOM   1206  N   GLY A 157      13.401  20.837  17.418  1.00  9.75           N  
ANISOU 1206  N   GLY A 157     1016   1452   1236    112    217    -49       N  
ATOM   1207  CA  GLY A 157      14.590  20.063  17.218  1.00 10.82           C  
ANISOU 1207  CA  GLY A 157     1098   1746   1268    205    353   -151       C  
ATOM   1208  C   GLY A 157      14.838  19.635  15.786  1.00 10.50           C  
ANISOU 1208  C   GLY A 157     1027   1628   1333    167    210   -124       C  
ATOM   1209  O   GLY A 157      14.395  20.286  14.859  1.00 11.72           O  
ANISOU 1209  O   GLY A 157     1330   1866   1258    384    308    -27       O  
ATOM   1210  N   GLY A 158      15.577  18.539  15.668  1.00 11.67           N  
ANISOU 1210  N   GLY A 158     1345   1652   1437    282    271   -173       N  
ATOM   1211  CA  GLY A 158      15.969  17.980  14.370  1.00 12.77           C  
ANISOU 1211  CA  GLY A 158     1601   1704   1548    188    421   -306       C  
ATOM   1212  C   GLY A 158      15.998  16.464  14.453  1.00 11.84           C  
ANISOU 1212  C   GLY A 158     1248   1754   1499    211    363   -159       C  
ATOM   1213  O   GLY A 158      15.468  15.852  15.388  1.00 12.91           O  
ANISOU 1213  O   GLY A 158     1495   1768   1643    101    479   -249       O  
ATOM   1214  N   MET A 159      16.611  15.861  13.430  1.00 12.79           N  
ANISOU 1214  N   MET A 159     1695   1679   1487    270    406   -233       N  
ATOM   1215  CA  MET A 159      16.665  14.428  13.308  1.00 13.15           C  
ANISOU 1215  CA  MET A 159     1664   1692   1639     18    453   -300       C  
ATOM   1216  C   MET A 159      17.882  14.099  12.463  1.00 11.88           C  
ANISOU 1216  C   MET A 159     1599   1595   1321    206    311   -270       C  
ATOM   1217  O   MET A 159      18.456  14.953  11.764  1.00 13.71           O  
ANISOU 1217  O   MET A 159     1829   1763   1618    329    472    -16       O  
ATOM   1218  CB AMET A 159      15.456  13.869  12.552  0.50 17.73           C  
ANISOU 1218  CB AMET A 159     1647   2372   2718   -399    364   -348       C  
ATOM   1219  CB BMET A 159      15.393  13.829  12.712  0.50 14.90           C  
ANISOU 1219  CB BMET A 159     1561   1805   2296    168    228   -188       C  
ATOM   1220  CG AMET A 159      14.119  14.527  12.595  0.50 26.07           C  
ANISOU 1220  CG AMET A 159     2098   3440   4368    375   -556   -992       C  
ATOM   1221  CG BMET A 159      15.207  14.430  11.320  0.50 14.91           C  
ANISOU 1221  CG BMET A 159     1515   2157   1995    515    225   -439       C  
ATOM   1222  SD AMET A 159      13.693  15.811  11.367  0.50 36.77           S  
ANISOU 1222  SD AMET A 159     5683   4786   3501   3123   -591  -1509       S  
ATOM   1223  SD BMET A 159      13.661  13.922  10.569  0.50 30.47           S  
ANISOU 1223  SD BMET A 159     2883   5655   3040   -320   -805  -1264       S  
ATOM   1224  CE AMET A 159      12.354  14.932  10.591  0.50 40.40           C  
ANISOU 1224  CE AMET A 159     1525   9643   4184   1823    520   1388       C  
ATOM   1225  CE BMET A 159      13.172  15.568   9.970  0.50 39.71           C  
ANISOU 1225  CE BMET A 159     2219  10112   2756   2814   1281   2800       C  
ATOM   1226  N   PRO A 160      18.351  12.826  12.475  1.00 12.06           N  
ANISOU 1226  N   PRO A 160     1557   1684   1342    196    241   -147       N  
ATOM   1227  CA  PRO A 160      19.538  12.504  11.670  1.00 12.92           C  
ANISOU 1227  CA  PRO A 160     1630   1824   1457    325    335   -289       C  
ATOM   1228  C   PRO A 160      19.271  12.603  10.181  1.00 13.40           C  
ANISOU 1228  C   PRO A 160     1475   2082   1533    311    327   -336       C  
ATOM   1229  O   PRO A 160      18.169  12.236   9.754  1.00 15.18           O  
ANISOU 1229  O   PRO A 160     1628   2487   1652    168     52   -455       O  
ATOM   1230  CB  PRO A 160      19.856  11.067  12.044  1.00 14.60           C  
ANISOU 1230  CB  PRO A 160     1953   1828   1765    309    350   -277       C  
ATOM   1231  CG  PRO A 160      19.155  10.821  13.350  1.00 15.02           C  
ANISOU 1231  CG  PRO A 160     1972   1740   1995    335    465    -47       C  
ATOM   1232  CD  PRO A 160      17.916  11.701  13.290  1.00 14.34           C  
ANISOU 1232  CD  PRO A 160     1876   1786   1787    235    403     56       C  
ATOM   1233  N   SER A 161      20.292  13.032   9.434  1.00 14.75           N  
ANISOU 1233  N   SER A 161     1659   2517   1428    377    502   -321       N  
ATOM   1234  CA  SER A 161      20.238  12.955   7.996  1.00 16.77           C  
ANISOU 1234  CA  SER A 161     1900   3050   1421    758    401   -388       C  
ATOM   1235  C   SER A 161      20.565  11.581   7.434  1.00 15.68           C  
ANISOU 1235  C   SER A 161     1652   2890   1415    399    146   -417       C  
ATOM   1236  O   SER A 161      21.464  10.881   7.922  1.00 15.97           O  
ANISOU 1236  O   SER A 161     1811   2549   1709    255    -59   -368       O  
ATOM   1237  CB ASER A 161      21.238  13.945   7.362  0.55 25.24           C  
ANISOU 1237  CB ASER A 161     5071   3249   1270   -621    524    -11       C  
ATOM   1238  CB BSER A 161      21.410  13.836   7.507  0.45 19.31           C  
ANISOU 1238  CB BSER A 161     3325   2407   1604    605   1176   -212       C  
ATOM   1239  OG ASER A 161      20.992  15.281   7.801  0.55 29.69           O  
ANISOU 1239  OG ASER A 161     5738   3305   2238     15   1277    304       O  
ATOM   1240  OG BSER A 161      21.248  14.046   6.144  0.45 21.73           O  
ANISOU 1240  OG BSER A 161     2782   3801   1674     12    727   -367       O  
ATOM   1241  N   THR A 162      19.891  11.123   6.393  1.00 19.25           N  
ANISOU 1241  N   THR A 162     1833   3716   1765    893   -185   -876       N  
ATOM   1242  CA  THR A 162      20.257   9.939   5.662  1.00 19.76           C  
ANISOU 1242  CA  THR A 162     2306   3680   1523    760     75   -823       C  
ATOM   1243  C   THR A 162      20.350  10.272   4.165  1.00 17.53           C  
ANISOU 1243  C   THR A 162     2214   2731   1717    681     90   -474       C  
ATOM   1244  O   THR A 162      19.596  11.080   3.657  1.00 23.63           O  
ANISOU 1244  O   THR A 162     2956   4321   1703   1893   -281   -904       O  
ATOM   1245  CB ATHR A 162      19.313   8.738   5.828  0.44 20.64           C  
ANISOU 1245  CB ATHR A 162     2948   3281   1612    934    733   -387       C  
ATOM   1246  CB BTHR A 162      19.175   8.841   5.806  0.56 23.18           C  
ANISOU 1246  CB BTHR A 162     3537   3261   2011    485    200    109       C  
ATOM   1247  OG1ATHR A 162      18.034   9.171   5.379  0.44 27.23           O  
ANISOU 1247  OG1ATHR A 162     3428   3590   3329   -565  -1347    618       O  
ATOM   1248  OG1BTHR A 162      19.036   8.539   7.208  0.56 32.03           O  
ANISOU 1248  OG1BTHR A 162     4496   5829   1846   -599    -33     86       O  
ATOM   1249  CG2ATHR A 162      19.238   8.291   7.273  0.44 22.87           C  
ANISOU 1249  CG2ATHR A 162     2137   4978   1573   1386    645   -118       C  
ATOM   1250  CG2BTHR A 162      19.464   7.537   5.055  0.56 25.51           C  
ANISOU 1250  CG2BTHR A 162     3502   3407   2785    574   -363   -258       C  
ATOM   1251  N   PRO A 163      21.270   9.673   3.447  1.00 15.45           N  
ANISOU 1251  N   PRO A 163     2063   2245   1562    368    159   -535       N  
ATOM   1252  CA  PRO A 163      21.351   9.890   2.016  1.00 15.26           C  
ANISOU 1252  CA  PRO A 163     2118   2006   1675    167    183   -286       C  
ATOM   1253  C   PRO A 163      20.061   9.442   1.328  1.00 17.39           C  
ANISOU 1253  C   PRO A 163     2116   2789   1702    453     55   -465       C  
ATOM   1254  O   PRO A 163      19.404   8.494   1.682  1.00 19.87           O  
ANISOU 1254  O   PRO A 163     2160   3615   1774   -341    -14   -525       O  
ATOM   1255  CB  PRO A 163      22.479   8.958   1.559  1.00 16.88           C  
ANISOU 1255  CB  PRO A 163     2055   2593   1768    189    387   -569       C  
ATOM   1256  CG  PRO A 163      23.320   8.823   2.796  1.00 16.94           C  
ANISOU 1256  CG  PRO A 163     2240   2396   1799    475    360   -270       C  
ATOM   1257  CD  PRO A 163      22.339   8.752   3.901  1.00 15.39           C  
ANISOU 1257  CD  PRO A 163     1973   2176   1698    315    245   -346       C  
ATOM   1258  N   HIS A 164      19.753  10.148   0.222  1.00 19.43           N  
ANISOU 1258  N   HIS A 164     2673   2893   1817    745   -205   -591       N  
ATOM   1259  CA  HIS A 164      18.655   9.722  -0.640  1.00 24.30           C  
ANISOU 1259  CA  HIS A 164     3280   3955   2000   1140   -634  -1299       C  
ATOM   1260  C   HIS A 164      19.080   8.551  -1.517  1.00 19.90           C  
ANISOU 1260  C   HIS A 164     2576   3038   1946    629   -295   -714       C  
ATOM   1261  O   HIS A 164      20.252   8.495  -1.941  1.00 20.69           O  
ANISOU 1261  O   HIS A 164     2595   3322   1943    658   -285   -695       O  
ATOM   1262  CB  HIS A 164      18.185  10.850  -1.560  1.00 41.24           C  
ANISOU 1262  CB  HIS A 164     6414   4689   4566   3436  -3034  -1664       C  
ATOM   1263  CG  HIS A 164      17.483  11.963  -0.889  1.00 54.63           C  
ANISOU 1263  CG  HIS A 164     8821   6043   5894   4665  -2827  -2539       C  
ATOM   1264  ND1 HIS A 164      18.171  13.097  -0.509  1.00 61.38           N  
ANISOU 1264  ND1 HIS A 164    10370   5863   7089   4855  -3260  -3386       N  
ATOM   1265  CD2 HIS A 164      16.182  12.143  -0.554  1.00 60.54           C  
ANISOU 1265  CD2 HIS A 164     9700   7341   5963   5100  -1311  -2982       C  
ATOM   1266  CE1 HIS A 164      17.326  13.933   0.058  1.00 64.87           C  
ANISOU 1266  CE1 HIS A 164    11647   6231   6771   5596  -2595  -2784       C  
ATOM   1267  NE2 HIS A 164      16.122  13.382   0.041  1.00 65.97           N  
ANISOU 1267  NE2 HIS A 164    11610   7264   6190   5357  -1227  -2917       N  
ATOM   1268  N   GLU A 165      18.139   7.674  -1.821  1.00 22.06           N  
ANISOU 1268  N   GLU A 165     2654   3753   1974    442   -282   -955       N  
ATOM   1269  CA  GLU A 165      18.403   6.541  -2.682  1.00 21.38           C  
ANISOU 1269  CA  GLU A 165     3017   3103   2003     49   -245   -628       C  
ATOM   1270  C   GLU A 165      18.885   6.948  -4.070  1.00 20.98           C  
ANISOU 1270  C   GLU A 165     3208   2971   1794    499   -287   -720       C  
ATOM   1271  O   GLU A 165      19.604   6.175  -4.666  1.00 23.11           O  
ANISOU 1271  O   GLU A 165     2917   3530   2335    673   -132   -793       O  
ATOM   1272  CB AGLU A 165      17.153   5.677  -2.923  0.56 25.21           C  
ANISOU 1272  CB AGLU A 165     2997   3800   2782   -117   -379   -758       C  
ATOM   1273  CB BGLU A 165      17.099   5.750  -2.859  0.44 25.32           C  
ANISOU 1273  CB BGLU A 165     2882   3705   3033     -6   -338   -780       C  
ATOM   1274  CG AGLU A 165      16.547   5.117  -1.644  0.56 23.70           C  
ANISOU 1274  CG AGLU A 165     2116   3798   3092    247   -116   -658       C  
ATOM   1275  CG BGLU A 165      17.155   4.813  -4.044  0.44 30.42           C  
ANISOU 1275  CG BGLU A 165     3708   4252   3599   -430   -797  -1393       C  
ATOM   1276  CD AGLU A 165      17.418   4.037  -1.012  0.56 21.04           C  
ANISOU 1276  CD AGLU A 165     1413   4281   2300    214   -264   -883       C  
ATOM   1277  CD BGLU A 165      17.634   3.427  -3.649  0.44 30.13           C  
ANISOU 1277  CD BGLU A 165     3761   4784   2903    770   -398  -1886       C  
ATOM   1278  OE1AGLU A 165      17.917   3.180  -1.777  0.56 19.25           O  
ANISOU 1278  OE1AGLU A 165     1482   3575   2259   -177    214   -464       O  
ATOM   1279  OE1BGLU A 165      18.079   3.217  -2.506  0.44 35.91           O  
ANISOU 1279  OE1BGLU A 165     4465   5695   3485   1403  -1258  -1988       O  
ATOM   1280  OE2AGLU A 165      17.563   4.044   0.229  0.56 28.83           O  
ANISOU 1280  OE2AGLU A 165     3096   5553   2304    814   -208   -955       O  
ATOM   1281  OE2BGLU A 165      17.510   2.566  -4.540  0.44 28.22           O  
ANISOU 1281  OE2BGLU A 165     3263   4650   2808   -107    364  -1755       O  
ATOM   1282  N   SER A 166      18.402   8.075  -4.559  1.00 22.13           N  
ANISOU 1282  N   SER A 166     3102   3215   2093    536   -585   -520       N  
ATOM   1283  CA  SER A 166      18.816   8.507  -5.887  1.00 24.28           C  
ANISOU 1283  CA  SER A 166     3508   3368   2350    825   -388   -227       C  
ATOM   1284  C   SER A 166      20.301   8.809  -5.921  1.00 24.36           C  
ANISOU 1284  C   SER A 166     3754   3379   2124    442   -263   -119       C  
ATOM   1285  O   SER A 166      20.887   8.710  -7.002  1.00 26.45           O  
ANISOU 1285  O   SER A 166     3827   3899   2323    151   -180   -472       O  
ATOM   1286  CB  SER A 166      17.980   9.748  -6.287  1.00 29.48           C  
ANISOU 1286  CB  SER A 166     4618   3541   3044   1151  -1012   -113       C  
ATOM   1287  OG  SER A 166      18.204  10.769  -5.285  1.00 50.64           O  
ANISOU 1287  OG  SER A 166     8339   5016   5886   3656  -3494  -2402       O  
ATOM   1288  N   GLN A 167      20.846   9.145  -4.752  1.00 23.49           N  
ANISOU 1288  N   GLN A 167     3381   3258   2284    823   -293   -361       N  
ATOM   1289  CA  GLN A 167      22.280   9.446  -4.648  1.00 23.90           C  
ANISOU 1289  CA  GLN A 167     3662   2690   2729    166   -236    227       C  
ATOM   1290  C   GLN A 167      23.121   8.214  -4.312  1.00 19.89           C  
ANISOU 1290  C   GLN A 167     2908   2645   2004    110    156    -50       C  
ATOM   1291  O   GLN A 167      24.177   7.913  -4.884  1.00 25.17           O  
ANISOU 1291  O   GLN A 167     3621   3395   2548    239    875    119       O  
ATOM   1292  CB AGLN A 167      22.534  10.536  -3.600  0.60 28.27           C  
ANISOU 1292  CB AGLN A 167     4166   2520   4054    405   -664   -293       C  
ATOM   1293  CB BGLN A 167      22.515  10.553  -3.605  0.40 26.24           C  
ANISOU 1293  CB BGLN A 167     4202   2227   3542     74   -330    125       C  
ATOM   1294  CG AGLN A 167      21.929  11.873  -3.961  0.60 35.35           C  
ANISOU 1294  CG AGLN A 167     6747   2655   4030    729  -1270    189       C  
ATOM   1295  CG BGLN A 167      24.001  10.825  -3.521  0.40 26.81           C  
ANISOU 1295  CG BGLN A 167     4143   2044   4000    312   -475   -233       C  
ATOM   1296  CD AGLN A 167      22.262  12.338  -5.362  0.60 38.23           C  
ANISOU 1296  CD AGLN A 167     6091   3841   4592    754   -413    605       C  
ATOM   1297  CD BGLN A 167      24.482  11.692  -2.388  0.40 29.31           C  
ANISOU 1297  CD BGLN A 167     4155   2482   4498   -593    519   -885       C  
ATOM   1298  OE1AGLN A 167      23.398  12.428  -5.825  0.60 43.53           O  
ANISOU 1298  OE1AGLN A 167     5949   4468   6121   2432     50    889       O  
ATOM   1299  OE1BGLN A 167      25.290  12.580  -2.670  0.40 35.83           O  
ANISOU 1299  OE1BGLN A 167     2951   4505   6156  -1302    110   -551       O  
ATOM   1300  NE2AGLN A 167      21.197  12.652  -6.085  0.60 37.81           N  
ANISOU 1300  NE2AGLN A 167     5574   5060   3731   1346    842   1837       N  
ATOM   1301  NE2BGLN A 167      24.030  11.429  -1.166  0.40 25.03           N  
ANISOU 1301  NE2BGLN A 167     2388   3086   4037    751   -333   -495       N  
ATOM   1302  N   ILE A 168      22.639   7.459  -3.335  1.00 18.45           N  
ANISOU 1302  N   ILE A 168     2667   2538   1805    333    133   -164       N  
ATOM   1303  CA  ILE A 168      23.336   6.300  -2.770  1.00 16.63           C  
ANISOU 1303  CA  ILE A 168     2081   2498   1739    312    275   -268       C  
ATOM   1304  C   ILE A 168      22.315   5.184  -2.703  1.00 17.93           C  
ANISOU 1304  C   ILE A 168     2473   2443   1896    143    313   -531       C  
ATOM   1305  O   ILE A 168      21.596   5.058  -1.695  1.00 17.71           O  
ANISOU 1305  O   ILE A 168     2216   2572   1943    134    260   -283       O  
ATOM   1306  CB  ILE A 168      24.035   6.539  -1.425  1.00 16.68           C  
ANISOU 1306  CB  ILE A 168     2045   2448   1846    214    255   -213       C  
ATOM   1307  CG1 ILE A 168      25.053   7.691  -1.482  1.00 19.57           C  
ANISOU 1307  CG1 ILE A 168     2290   3123   2021   -238    337   -394       C  
ATOM   1308  CG2 ILE A 168      24.681   5.239  -0.952  1.00 18.03           C  
ANISOU 1308  CG2 ILE A 168     2494   2864   1492    583    146   -307       C  
ATOM   1309  CD1 ILE A 168      25.754   7.932  -0.150  1.00 19.19           C  
ANISOU 1309  CD1 ILE A 168     1939   3222   2132   -228    390   -505       C  
ATOM   1310  N   PRO A 169      22.210   4.378  -3.751  1.00 18.19           N  
ANISOU 1310  N   PRO A 169     2295   2801   1817    221     44   -430       N  
ATOM   1311  CA  PRO A 169      21.229   3.274  -3.705  1.00 18.94           C  
ANISOU 1311  CA  PRO A 169     2377   2852   1969    113   -198   -700       C  
ATOM   1312  C   PRO A 169      21.546   2.330  -2.549  1.00 18.01           C  
ANISOU 1312  C   PRO A 169     2115   2640   2089     64     98   -652       C  
ATOM   1313  O   PRO A 169      22.680   1.924  -2.319  1.00 17.98           O  
ANISOU 1313  O   PRO A 169     2144   2595   2094     33    217   -351       O  
ATOM   1314  CB  PRO A 169      21.340   2.627  -5.081  1.00 22.47           C  
ANISOU 1314  CB  PRO A 169     3077   3412   2048     63     -9   -885       C  
ATOM   1315  CG  PRO A 169      22.496   3.242  -5.765  1.00 24.35           C  
ANISOU 1315  CG  PRO A 169     3586   3234   2432     96    491   -877       C  
ATOM   1316  CD  PRO A 169      22.914   4.456  -5.041  1.00 19.28           C  
ANISOU 1316  CD  PRO A 169     2508   3184   1632    407     16   -529       C  
ATOM   1317  N   GLY A 170      20.501   1.929  -1.800  1.00 18.98           N  
ANISOU 1317  N   GLY A 170     1985   3142   2084   -131    -45   -707       N  
ATOM   1318  CA  GLY A 170      20.618   1.064  -0.648  1.00 19.20           C  
ANISOU 1318  CA  GLY A 170     2470   2666   2159   -268    223   -762       C  
ATOM   1319  C   GLY A 170      20.904   1.809   0.653  1.00 16.85           C  
ANISOU 1319  C   GLY A 170     1920   2438   2043     14    189   -674       C  
ATOM   1320  O   GLY A 170      21.067   1.190   1.705  1.00 17.44           O  
ANISOU 1320  O   GLY A 170     2197   2363   2066   -186    302   -581       O  
ATOM   1321  N   ALA A 171      20.969   3.165   0.615  1.00 16.78           N  
ANISOU 1321  N   ALA A 171     2006   2512   1859   -163    130   -570       N  
ATOM   1322  CA  ALA A 171      21.290   3.886   1.839  1.00 16.72           C  
ANISOU 1322  CA  ALA A 171     2052   2345   1957   -160    371   -650       C  
ATOM   1323  C   ALA A 171      20.297   3.579   2.961  1.00 16.23           C  
ANISOU 1323  C   ALA A 171     1782   2409   1974   -249    225   -774       C  
ATOM   1324  O   ALA A 171      20.677   3.612   4.140  1.00 16.23           O  
ANISOU 1324  O   ALA A 171     1850   2402   1914   -362    332   -786       O  
ATOM   1325  CB  ALA A 171      21.405   5.399   1.623  1.00 19.97           C  
ANISOU 1325  CB  ALA A 171     2656   2365   2566   -375    341   -487       C  
ATOM   1326  N   SER A 172      19.034   3.269   2.599  1.00 17.89           N  
ANISOU 1326  N   SER A 172     1639   2858   2302    -20    207   -767       N  
ATOM   1327  CA  SER A 172      18.033   2.948   3.656  1.00 19.13           C  
ANISOU 1327  CA  SER A 172     1782   3115   2373    -92    452   -988       C  
ATOM   1328  C   SER A 172      18.347   1.685   4.419  1.00 19.02           C  
ANISOU 1328  C   SER A 172     2073   2810   2343   -505    471  -1087       C  
ATOM   1329  O   SER A 172      17.689   1.477   5.458  1.00 20.40           O  
ANISOU 1329  O   SER A 172     1883   3284   2586   -221    493   -836       O  
ATOM   1330  CB  SER A 172      16.648   2.851   3.014  1.00 24.08           C  
ANISOU 1330  CB  SER A 172     1704   4768   2677    -67    542   -862       C  
ATOM   1331  OG  SER A 172      16.550   1.667   2.205  1.00 30.04           O  
ANISOU 1331  OG  SER A 172     2666   5633   3114  -1343    226  -1454       O  
ATOM   1332  N   LEU A 173      19.291   0.868   3.980  1.00 18.14           N  
ANISOU 1332  N   LEU A 173     2037   2791   2065   -320    271  -1020       N  
ATOM   1333  CA  LEU A 173      19.738  -0.310   4.724  1.00 18.51           C  
ANISOU 1333  CA  LEU A 173     2362   2567   2104   -588    775   -759       C  
ATOM   1334  C   LEU A 173      20.631   0.033   5.943  1.00 17.82           C  
ANISOU 1334  C   LEU A 173     2742   2313   1718   -178    742   -469       C  
ATOM   1335  O   LEU A 173      20.815  -0.797   6.844  1.00 21.21           O  
ANISOU 1335  O   LEU A 173     3381   2636   2043     70    980   -200       O  
ATOM   1336  CB  LEU A 173      20.503  -1.275   3.777  1.00 20.66           C  
ANISOU 1336  CB  LEU A 173     2923   2369   2556   -502    741  -1058       C  
ATOM   1337  CG  LEU A 173      19.674  -1.890   2.696  1.00 21.62           C  
ANISOU 1337  CG  LEU A 173     3244   2674   2298   -834    882   -888       C  
ATOM   1338  CD1 LEU A 173      20.562  -2.475   1.602  1.00 20.27           C  
ANISOU 1338  CD1 LEU A 173     2716   2692   2293   -590    490   -934       C  
ATOM   1339  CD2 LEU A 173      18.754  -2.977   3.253  1.00 29.24           C  
ANISOU 1339  CD2 LEU A 173     3832   4111   3169  -1966   1198  -1002       C  
ATOM   1340  N   GLY A 174      21.144   1.239   5.930  1.00 16.34           N  
ANISOU 1340  N   GLY A 174     2288   2274   1645    -21    428   -754       N  
ATOM   1341  CA  GLY A 174      21.882   1.773   7.055  1.00 16.61           C  
ANISOU 1341  CA  GLY A 174     1958   2732   1620    236    300   -669       C  
ATOM   1342  C   GLY A 174      20.911   2.271   8.142  1.00 16.62           C  
ANISOU 1342  C   GLY A 174     1788   2821   1705     67    308   -816       C  
ATOM   1343  O   GLY A 174      19.706   2.385   7.943  1.00 23.39           O  
ANISOU 1343  O   GLY A 174     1850   4715   2323    489    141  -1775       O  
ATOM   1344  N   ILE A 175      21.492   2.569   9.276  1.00 13.58           N  
ANISOU 1344  N   ILE A 175     1690   1832   1639    -13    442   -480       N  
ATOM   1345  CA  ILE A 175      20.824   3.128  10.420  1.00 12.50           C  
ANISOU 1345  CA  ILE A 175     1407   1823   1520   -163    321   -381       C  
ATOM   1346  C   ILE A 175      21.456   4.507  10.717  1.00 11.71           C  
ANISOU 1346  C   ILE A 175     1339   1613   1498    112    289   -255       C  
ATOM   1347  O   ILE A 175      22.460   4.870  10.117  1.00 13.34           O  
ANISOU 1347  O   ILE A 175     1403   1798   1867    -96    400   -351       O  
ATOM   1348  CB  ILE A 175      20.811   2.215  11.660  1.00 13.81           C  
ANISOU 1348  CB  ILE A 175     1719   1794   1736   -248    445   -248       C  
ATOM   1349  CG1 ILE A 175      22.222   1.935  12.221  1.00 13.89           C  
ANISOU 1349  CG1 ILE A 175     1702   1824   1749    137    498    -80       C  
ATOM   1350  CG2 ILE A 175      20.058   0.927  11.420  1.00 17.51           C  
ANISOU 1350  CG2 ILE A 175     2153   1949   2550   -560    548   -257       C  
ATOM   1351  CD1 ILE A 175      22.233   1.445  13.637  1.00 16.88           C  
ANISOU 1351  CD1 ILE A 175     2410   2301   1702    348    750     58       C  
ATOM   1352  N   THR A 176      20.868   5.207  11.661  1.00 11.94           N  
ANISOU 1352  N   THR A 176     1333   1691   1515    -41    330   -314       N  
ATOM   1353  CA  THR A 176      21.411   6.447  12.172  1.00 12.14           C  
ANISOU 1353  CA  THR A 176     1559   1617   1439    -87    447   -275       C  
ATOM   1354  C   THR A 176      21.607   6.317  13.684  1.00 12.28           C  
ANISOU 1354  C   THR A 176     1371   1891   1405   -163    374   -255       C  
ATOM   1355  O   THR A 176      21.365   5.224  14.265  1.00 12.53           O  
ANISOU 1355  O   THR A 176     1389   1776   1594   -136    441   -178       O  
ATOM   1356  CB  THR A 176      20.504   7.644  11.895  1.00 13.72           C  
ANISOU 1356  CB  THR A 176     1784   1892   1536    273    373   -310       C  
ATOM   1357  OG1 THR A 176      19.301   7.433  12.704  1.00 15.21           O  
ANISOU 1357  OG1 THR A 176     1781   2154   1845    367    487   -403       O  
ATOM   1358  CG2 THR A 176      20.175   7.748  10.414  1.00 15.81           C  
ANISOU 1358  CG2 THR A 176     2707   1711   1591    325    285   -214       C  
ATOM   1359  N   SER A 177      21.995   7.407  14.349  1.00 12.05           N  
ANISOU 1359  N   SER A 177     1405   1761   1411    -37    337   -320       N  
ATOM   1360  CA  SER A 177      22.078   7.369  15.810  1.00 12.03           C  
ANISOU 1360  CA  SER A 177     1448   1663   1459    -70    390   -251       C  
ATOM   1361  C   SER A 177      20.779   6.941  16.460  1.00 12.35           C  
ANISOU 1361  C   SER A 177     1432   1653   1607     -7    334   -171       C  
ATOM   1362  O   SER A 177      20.798   6.300  17.526  1.00 13.53           O  
ANISOU 1362  O   SER A 177     1573   1941   1627   -126    221     -8       O  
ATOM   1363  CB  SER A 177      22.579   8.711  16.356  1.00 12.89           C  
ANISOU 1363  CB  SER A 177     1797   1681   1421   -197    330   -183       C  
ATOM   1364  OG  SER A 177      21.731   9.778  15.973  1.00 13.08           O  
ANISOU 1364  OG  SER A 177     1878   1618   1472    -32    492   -216       O  
ATOM   1365  N   ASP A 178      19.643   7.258  15.854  1.00 12.27           N  
ANISOU 1365  N   ASP A 178     1386   1768   1509     40    400    -90       N  
ATOM   1366  CA  ASP A 178      18.374   6.788  16.436  1.00 13.18           C  
ANISOU 1366  CA  ASP A 178     1468   1912   1627    -85    360    -81       C  
ATOM   1367  C   ASP A 178      18.335   5.263  16.491  1.00 12.51           C  
ANISOU 1367  C   ASP A 178     1196   1918   1641    -76    378    -21       C  
ATOM   1368  O   ASP A 178      17.969   4.635  17.481  1.00 14.04           O  
ANISOU 1368  O   ASP A 178     1451   2122   1760   -231    445     47       O  
ATOM   1369  CB  ASP A 178      17.203   7.340  15.634  1.00 15.27           C  
ANISOU 1369  CB  ASP A 178     1428   2253   2122    243    441    145       C  
ATOM   1370  CG  ASP A 178      16.893   8.787  15.836  1.00 17.02           C  
ANISOU 1370  CG  ASP A 178     2165   2405   1897    530    658    -58       C  
ATOM   1371  OD1 ASP A 178      17.489   9.471  16.740  1.00 19.78           O  
ANISOU 1371  OD1 ASP A 178     2526   2663   2326    308    712   -414       O  
ATOM   1372  OD2 ASP A 178      16.056   9.338  15.057  1.00 22.50           O  
ANISOU 1372  OD2 ASP A 178     2525   2397   3628    517   -153    178       O  
ATOM   1373  N   GLY A 179      18.696   4.621  15.354  1.00 14.31           N  
ANISOU 1373  N   GLY A 179     1955   1847   1634     13    314    -74       N  
ATOM   1374  CA  GLY A 179      18.733   3.183  15.332  1.00 14.22           C  
ANISOU 1374  CA  GLY A 179     1715   1828   1860   -187    359     -8       C  
ATOM   1375  C   GLY A 179      19.791   2.601  16.230  1.00 13.16           C  
ANISOU 1375  C   GLY A 179     1652   1653   1697   -139    289   -262       C  
ATOM   1376  O   GLY A 179      19.637   1.475  16.722  1.00 13.80           O  
ANISOU 1376  O   GLY A 179     1772   1751   1720   -140    309   -199       O  
ATOM   1377  N   PHE A 180      20.893   3.299  16.469  1.00 12.79           N  
ANISOU 1377  N   PHE A 180     1671   1607   1583    -28    338    -70       N  
ATOM   1378  CA  PHE A 180      21.922   2.858  17.388  1.00 12.92           C  
ANISOU 1378  CA  PHE A 180     1431   1834   1643    -71    416   -126       C  
ATOM   1379  C   PHE A 180      21.300   2.571  18.763  1.00 12.16           C  
ANISOU 1379  C   PHE A 180     1537   1513   1573    -60    343    -92       C  
ATOM   1380  O   PHE A 180      21.587   1.567  19.384  1.00 13.28           O  
ANISOU 1380  O   PHE A 180     1605   1647   1792     59    405    -45       O  
ATOM   1381  CB  PHE A 180      23.003   3.936  17.509  1.00 13.95           C  
ANISOU 1381  CB  PHE A 180     1482   1973   1845    -62    364    -28       C  
ATOM   1382  CG  PHE A 180      24.094   3.628  18.521  1.00 13.78           C  
ANISOU 1382  CG  PHE A 180     1347   1808   2080    196    291     39       C  
ATOM   1383  CD1 PHE A 180      24.004   4.211  19.775  1.00 16.64           C  
ANISOU 1383  CD1 PHE A 180     1818   2211   2292    429   -102   -282       C  
ATOM   1384  CD2 PHE A 180      25.154   2.786  18.223  1.00 17.83           C  
ANISOU 1384  CD2 PHE A 180     1639   2390   2745    476    487   -118       C  
ATOM   1385  CE1 PHE A 180      24.978   4.002  20.737  1.00 21.22           C  
ANISOU 1385  CE1 PHE A 180     2194   3483   2386    930   -305   -190       C  
ATOM   1386  CE2 PHE A 180      26.138   2.560  19.156  1.00 21.81           C  
ANISOU 1386  CE2 PHE A 180     2176   3476   2634   1423    605    688       C  
ATOM   1387  CZ  PHE A 180      26.035   3.179  20.388  1.00 22.27           C  
ANISOU 1387  CZ  PHE A 180     1832   3990   2641    923    197    396       C  
ATOM   1388  N   PHE A 181      20.407   3.453  19.220  1.00 11.90           N  
ANISOU 1388  N   PHE A 181     1448   1597   1478    -39    270   -160       N  
ATOM   1389  CA  PHE A 181      19.786   3.313  20.505  1.00 12.26           C  
ANISOU 1389  CA  PHE A 181     1425   1803   1431    -50    296   -286       C  
ATOM   1390  C   PHE A 181      18.638   2.286  20.515  1.00 12.88           C  
ANISOU 1390  C   PHE A 181     1603   1750   1541   -140    260   -108       C  
ATOM   1391  O   PHE A 181      18.070   2.008  21.594  1.00 15.53           O  
ANISOU 1391  O   PHE A 181     1865   2387   1650   -417    347    -78       O  
ATOM   1392  CB  PHE A 181      19.313   4.667  21.072  1.00 13.37           C  
ANISOU 1392  CB  PHE A 181     1588   1736   1754    -10    371   -300       C  
ATOM   1393  CG  PHE A 181      20.513   5.572  21.356  1.00 12.63           C  
ANISOU 1393  CG  PHE A 181     1591   1847   1360   -110    434   -284       C  
ATOM   1394  CD1 PHE A 181      21.431   5.173  22.349  1.00 14.39           C  
ANISOU 1394  CD1 PHE A 181     1926   2168   1374   -197    193   -332       C  
ATOM   1395  CD2 PHE A 181      20.758   6.730  20.661  1.00 13.18           C  
ANISOU 1395  CD2 PHE A 181     1601   1860   1547    -18    601   -237       C  
ATOM   1396  CE1 PHE A 181      22.506   5.981  22.630  1.00 14.46           C  
ANISOU 1396  CE1 PHE A 181     1904   2280   1309   -283    184   -224       C  
ATOM   1397  CE2 PHE A 181      21.842   7.539  20.936  1.00 14.33           C  
ANISOU 1397  CE2 PHE A 181     1904   1835   1708   -166    459   -151       C  
ATOM   1398  CZ  PHE A 181      22.757   7.116  21.906  1.00 14.99           C  
ANISOU 1398  CZ  PHE A 181     1905   2098   1695   -157    362   -275       C  
ATOM   1399  N   GLN A 182      18.334   1.700  19.374  1.00 13.01           N  
ANISOU 1399  N   GLN A 182     1396   1782   1765   -190    231   -330       N  
ATOM   1400  CA  GLN A 182      17.411   0.572  19.318  1.00 14.20           C  
ANISOU 1400  CA  GLN A 182     1339   1913   2143   -168    337   -362       C  
ATOM   1401  C   GLN A 182      18.152  -0.759  19.205  1.00 14.57           C  
ANISOU 1401  C   GLN A 182     1485   1801   2248   -174    219   -124       C  
ATOM   1402  O   GLN A 182      17.530  -1.819  19.362  1.00 16.41           O  
ANISOU 1402  O   GLN A 182     1806   1926   2502   -264    290    -27       O  
ATOM   1403  CB AGLN A 182      16.444   0.702  18.131  0.58 16.56           C  
ANISOU 1403  CB AGLN A 182     1526   1903   2864    -13   -206   -684       C  
ATOM   1404  CB BGLN A 182      16.482   0.661  18.108  0.42 16.65           C  
ANISOU 1404  CB BGLN A 182     1421   1922   2984   -434   -241     33       C  
ATOM   1405  CG AGLN A 182      15.564   1.927  18.276  0.58 15.28           C  
ANISOU 1405  CG AGLN A 182      950   2053   2802   -128    265   -581       C  
ATOM   1406  CG BGLN A 182      15.403   1.712  18.098  0.42 21.72           C  
ANISOU 1406  CG BGLN A 182     2322   2430   3501    272   -603   -337       C  
ATOM   1407  CD AGLN A 182      14.694   2.217  17.083  0.58 24.95           C  
ANISOU 1407  CD AGLN A 182     2219   3457   3803    817   -903   -994       C  
ATOM   1408  CD BGLN A 182      14.377   1.588  19.194  0.42 22.37           C  
ANISOU 1408  CD BGLN A 182     1687   2609   4204    147   -445   -917       C  
ATOM   1409  OE1AGLN A 182      14.881   1.779  15.949  0.58 40.11           O  
ANISOU 1409  OE1AGLN A 182     5144   5956   4142   2657  -2413  -2431       O  
ATOM   1410  OE1BGLN A 182      13.552   0.677  19.220  0.42 32.06           O  
ANISOU 1410  OE1BGLN A 182     2239   3067   6875   -389    454  -1400       O  
ATOM   1411  NE2AGLN A 182      13.638   2.992  17.332  0.58 37.25           N  
ANISOU 1411  NE2AGLN A 182     2295   7213   4646   2265   -269   -192       N  
ATOM   1412  NE2BGLN A 182      14.344   2.504  20.139  0.42 32.96           N  
ANISOU 1412  NE2BGLN A 182     3703   4809   4013   -876   -185  -1916       N  
ATOM   1413  N   LEU A 183      19.449  -0.772  18.913  1.00 13.60           N  
ANISOU 1413  N   LEU A 183     1547   1875   1744     24    365     69       N  
ATOM   1414  CA  LEU A 183      20.189  -2.039  18.807  1.00 13.94           C  
ANISOU 1414  CA  LEU A 183     1608   1714   1974    -49    199     33       C  
ATOM   1415  C   LEU A 183      20.061  -2.908  20.068  1.00 14.03           C  
ANISOU 1415  C   LEU A 183     1503   1741   2087     35    477     70       C  
ATOM   1416  O   LEU A 183      20.251  -2.382  21.154  1.00 14.39           O  
ANISOU 1416  O   LEU A 183     1605   1980   1881    131    432    151       O  
ATOM   1417  CB  LEU A 183      21.660  -1.783  18.575  1.00 13.79           C  
ANISOU 1417  CB  LEU A 183     1636   1786   1819      5    520    -67       C  
ATOM   1418  CG  LEU A 183      22.073  -1.188  17.236  1.00 15.03           C  
ANISOU 1418  CG  LEU A 183     2056   1678   1977     96    562     31       C  
ATOM   1419  CD1 LEU A 183      23.553  -0.794  17.284  1.00 16.39           C  
ANISOU 1419  CD1 LEU A 183     1830   2078   2320    384    899    588       C  
ATOM   1420  CD2 LEU A 183      21.823  -2.195  16.120  1.00 19.98           C  
ANISOU 1420  CD2 LEU A 183     3437   2280   1872     92    957   -368       C  
ATOM   1421  N   GLU A 184      19.802  -4.185  19.893  1.00 15.66           N  
ANISOU 1421  N   GLU A 184     1721   1782   2447   -118    355    170       N  
ATOM   1422  CA  GLU A 184      19.611  -5.101  21.013  1.00 16.54           C  
ANISOU 1422  CA  GLU A 184     1974   1777   2533   -145    491    226       C  
ATOM   1423  C   GLU A 184      20.810  -6.006  21.203  1.00 15.88           C  
ANISOU 1423  C   GLU A 184     1868   1910   2254   -105    467    197       C  
ATOM   1424  O   GLU A 184      20.859  -6.729  22.176  1.00 19.89           O  
ANISOU 1424  O   GLU A 184     2302   2453   2801    -58    576    786       O  
ATOM   1425  CB AGLU A 184      18.364  -5.956  20.840  0.57 23.24           C  
ANISOU 1425  CB AGLU A 184     1824   2755   4252   -443     71   1339       C  
ATOM   1426  CB BGLU A 184      18.305  -5.869  20.832  0.43 22.44           C  
ANISOU 1426  CB BGLU A 184     1830   2612   4086   -355    273   1113       C  
ATOM   1427  CG AGLU A 184      17.015  -5.255  20.849  0.57 25.85           C  
ANISOU 1427  CG AGLU A 184     2016   2870   4937   -155    185   1150       C  
ATOM   1428  CG BGLU A 184      17.124  -4.901  20.914  0.43 26.14           C  
ANISOU 1428  CG BGLU A 184     2118   2446   5369   -151   -274   1159       C  
ATOM   1429  CD AGLU A 184      16.455  -5.036  22.235  0.57 29.96           C  
ANISOU 1429  CD AGLU A 184     2414   3813   5157    -37    411    772       C  
ATOM   1430  CD BGLU A 184      15.781  -5.580  20.961  0.43 28.60           C  
ANISOU 1430  CD BGLU A 184     1894   3372   5601   -186    279    429       C  
ATOM   1431  OE1AGLU A 184      17.155  -4.938  23.258  0.57 39.90           O  
ANISOU 1431  OE1AGLU A 184     3730   5995   5435   -907     56   -828       O  
ATOM   1432  OE1BGLU A 184      15.757  -6.796  20.699  0.43 40.01           O  
ANISOU 1432  OE1BGLU A 184     3106   3245   8852  -1049    271    380       O  
ATOM   1433  OE2AGLU A 184      15.200  -4.960  22.305  0.57 43.28           O  
ANISOU 1433  OE2AGLU A 184     2645   7382   6416   1002    847     76       O  
ATOM   1434  OE2BGLU A 184      14.772  -4.920  21.273  0.43 41.54           O  
ANISOU 1434  OE2BGLU A 184     2021   6503   7260    910   -554  -1236       O  
ATOM   1435  N   GLU A 185      21.782  -5.970  20.295  1.00 16.26           N  
ANISOU 1435  N   GLU A 185     1970   1942   2267   -176    567   -169       N  
ATOM   1436  CA  GLU A 185      23.006  -6.766  20.371  1.00 16.40           C  
ANISOU 1436  CA  GLU A 185     2103   1729   2401    -89    704    -14       C  
ATOM   1437  C   GLU A 185      24.179  -5.947  19.807  1.00 14.78           C  
ANISOU 1437  C   GLU A 185     1919   1431   2266    112    595     -4       C  
ATOM   1438  O   GLU A 185      23.977  -5.049  19.027  1.00 15.76           O  
ANISOU 1438  O   GLU A 185     1995   1845   2149    -89    434    148       O  
ATOM   1439  CB  GLU A 185      22.862  -8.052  19.561  1.00 22.98           C  
ANISOU 1439  CB  GLU A 185     2483   1704   4543   -194    460   -563       C  
ATOM   1440  CG  GLU A 185      21.723  -8.931  20.031  1.00 31.09           C  
ANISOU 1440  CG  GLU A 185     4414   2587   4811  -1366   1016   -395       C  
ATOM   1441  CD  GLU A 185      21.992  -9.516  21.424  1.00 37.93           C  
ANISOU 1441  CD  GLU A 185     4177   4052   6182  -1574    143   1178       C  
ATOM   1442  OE1 GLU A 185      23.049  -9.207  22.018  1.00 49.09           O  
ANISOU 1442  OE1 GLU A 185     3575   9128   5948  -1140    451   -241       O  
ATOM   1443  OE2 GLU A 185      21.130 -10.284  21.896  1.00 57.02           O  
ANISOU 1443  OE2 GLU A 185     5849   8229   7588  -3166    677   3263       O  
ATOM   1444  N   LEU A 186      25.371  -6.299  20.209  1.00 15.61           N  
ANISOU 1444  N   LEU A 186     1965   2023   1944     81    628    187       N  
ATOM   1445  CA  LEU A 186      26.590  -5.689  19.646  1.00 14.62           C  
ANISOU 1445  CA  LEU A 186     1866   1947   1743     46    650    -90       C  
ATOM   1446  C   LEU A 186      26.777  -6.118  18.206  1.00 14.78           C  
ANISOU 1446  C   LEU A 186     1961   1868   1787    -43    538   -190       C  
ATOM   1447  O   LEU A 186      26.867  -7.337  17.953  1.00 16.88           O  
ANISOU 1447  O   LEU A 186     2520   1850   2044     64    887   -109       O  
ATOM   1448  CB  LEU A 186      27.771  -6.180  20.455  1.00 17.66           C  
ANISOU 1448  CB  LEU A 186     1938   3011   1759     20    585    178       C  
ATOM   1449  CG  LEU A 186      29.147  -5.684  19.996  1.00 18.15           C  
ANISOU 1449  CG  LEU A 186     1904   2842   2151    -70    397    257       C  
ATOM   1450  CD1 LEU A 186      29.333  -4.213  20.277  1.00 18.72           C  
ANISOU 1450  CD1 LEU A 186     1906   3086   2121    -89    818   -261       C  
ATOM   1451  CD2 LEU A 186      30.224  -6.507  20.683  1.00 23.38           C  
ANISOU 1451  CD2 LEU A 186     1958   3647   3278     21    139    867       C  
ATOM   1452  N   PRO A 187      26.860  -5.212  17.234  1.00 13.88           N  
ANISOU 1452  N   PRO A 187     1909   1700   1664     11    415   -337       N  
ATOM   1453  CA  PRO A 187      27.175  -5.655  15.872  1.00 14.30           C  
ANISOU 1453  CA  PRO A 187     1891   1819   1724      8    380   -288       C  
ATOM   1454  C   PRO A 187      28.576  -6.243  15.805  1.00 14.46           C  
ANISOU 1454  C   PRO A 187     1920   1677   1897    -25    630   -140       C  
ATOM   1455  O   PRO A 187      29.528  -5.640  16.328  1.00 15.17           O  
ANISOU 1455  O   PRO A 187     1846   1939   1979   -129    652   -249       O  
ATOM   1456  CB  PRO A 187      27.055  -4.375  15.043  1.00 14.99           C  
ANISOU 1456  CB  PRO A 187     2021   1895   1779     51    489   -157       C  
ATOM   1457  CG  PRO A 187      26.381  -3.359  15.906  1.00 17.56           C  
ANISOU 1457  CG  PRO A 187     3099   1701   1870      7    682   -176       C  
ATOM   1458  CD  PRO A 187      26.642  -3.760  17.298  1.00 15.22           C  
ANISOU 1458  CD  PRO A 187     2097   1769   1916    176    762   -203       C  
ATOM   1459  N   GLY A 188      28.748  -7.303  15.053  1.00 14.88           N  
ANISOU 1459  N   GLY A 188     2029   1798   1824     41    543   -107       N  
ATOM   1460  CA  GLY A 188      30.087  -7.844  14.930  1.00 15.87           C  
ANISOU 1460  CA  GLY A 188     2225   1671   2134    142    915     25       C  
ATOM   1461  C   GLY A 188      31.025  -6.968  14.142  1.00 14.20           C  
ANISOU 1461  C   GLY A 188     1998   1528   1870    168    633    -52       C  
ATOM   1462  O   GLY A 188      32.219  -6.839  14.482  1.00 15.34           O  
ANISOU 1462  O   GLY A 188     2058   1916   1855     58    457     46       O  
ATOM   1463  N   ARG A 189      30.519  -6.345  13.096  1.00 13.86           N  
ANISOU 1463  N   ARG A 189     1944   1492   1831     46    605    -71       N  
ATOM   1464  CA  ARG A 189      31.240  -5.505  12.141  1.00 14.00           C  
ANISOU 1464  CA  ARG A 189     2203   1531   1587    100    502    -86       C  
ATOM   1465  C   ARG A 189      30.459  -4.213  11.903  1.00 12.32           C  
ANISOU 1465  C   ARG A 189     1638   1542   1502   -106    630    -25       C  
ATOM   1466  O   ARG A 189      29.301  -4.358  11.448  1.00 13.91           O  
ANISOU 1466  O   ARG A 189     1780   1705   1799   -202    379   -333       O  
ATOM   1467  CB  ARG A 189      31.506  -6.290  10.837  1.00 14.52           C  
ANISOU 1467  CB  ARG A 189     2154   1625   1738    -24    540   -245       C  
ATOM   1468  CG  ARG A 189      32.216  -5.509   9.761  1.00 15.62           C  
ANISOU 1468  CG  ARG A 189     2164   2068   1703     44    666   -322       C  
ATOM   1469  CD  ARG A 189      33.723  -5.493   9.971  1.00 16.34           C  
ANISOU 1469  CD  ARG A 189     2164   2083   1962    -52    520   -168       C  
ATOM   1470  NE  ARG A 189      34.403  -4.828   8.868  1.00 16.55           N  
ANISOU 1470  NE  ARG A 189     2288   2017   1983    123    753   -258       N  
ATOM   1471  CZ  ARG A 189      34.835  -3.595   8.849  1.00 14.90           C  
ANISOU 1471  CZ  ARG A 189     1983   1961   1717    243    528    -82       C  
ATOM   1472  NH1 ARG A 189      35.459  -3.136   7.761  1.00 17.78           N  
ANISOU 1472  NH1 ARG A 189     2664   2259   1833    -93    684    -94       N  
ATOM   1473  NH2 ARG A 189      34.677  -2.747   9.833  1.00 16.09           N  
ANISOU 1473  NH2 ARG A 189     2370   1893   1849    143    744    -66       N  
ATOM   1474  N   SER A 190      31.094  -3.107  12.206  1.00 12.40           N  
ANISOU 1474  N   SER A 190     1681   1452   1579    -22    416   -204       N  
ATOM   1475  CA  SER A 190      30.430  -1.795  12.061  1.00 12.79           C  
ANISOU 1475  CA  SER A 190     1632   1555   1672    164    284    -48       C  
ATOM   1476  C   SER A 190      31.199  -0.865  11.118  1.00 11.98           C  
ANISOU 1476  C   SER A 190     1552   1474   1525    270    398   -169       C  
ATOM   1477  O   SER A 190      32.435  -0.810  11.218  1.00 13.49           O  
ANISOU 1477  O   SER A 190     1542   1886   1699    295    468     86       O  
ATOM   1478  CB  SER A 190      30.309  -1.113  13.436  1.00 14.67           C  
ANISOU 1478  CB  SER A 190     2226   1569   1778    413    891     13       C  
ATOM   1479  OG  SER A 190      29.545  -1.889  14.342  1.00 14.68           O  
ANISOU 1479  OG  SER A 190     1818   1793   1968    -43    636    -58       O  
ATOM   1480  N   VAL A 191      30.458  -0.139  10.310  1.00 11.56           N  
ANISOU 1480  N   VAL A 191     1526   1470   1397    166    365   -143       N  
ATOM   1481  CA  VAL A 191      31.030   0.920   9.476  1.00 11.93           C  
ANISOU 1481  CA  VAL A 191     1562   1493   1479    100    414   -128       C  
ATOM   1482  C   VAL A 191      30.222   2.200   9.794  1.00 11.26           C  
ANISOU 1482  C   VAL A 191     1356   1499   1424    -37    352   -111       C  
ATOM   1483  O   VAL A 191      29.021   2.212   9.581  1.00 12.53           O  
ANISOU 1483  O   VAL A 191     1360   1613   1789     67    296   -201       O  
ATOM   1484  CB  VAL A 191      30.972   0.591   7.987  1.00 12.59           C  
ANISOU 1484  CB  VAL A 191     1709   1581   1494    157    512   -175       C  
ATOM   1485  CG1 VAL A 191      31.480   1.777   7.147  1.00 13.67           C  
ANISOU 1485  CG1 VAL A 191     1799   1829   1566     99    445     53       C  
ATOM   1486  CG2 VAL A 191      31.814  -0.669   7.699  1.00 14.51           C  
ANISOU 1486  CG2 VAL A 191     1950   1752   1810    256    681   -257       C  
ATOM   1487  N   ILE A 192      30.890   3.202  10.332  1.00 10.89           N  
ANISOU 1487  N   ILE A 192     1323   1557   1256    113    270   -167       N  
ATOM   1488  CA  ILE A 192      30.316   4.486  10.686  1.00 11.41           C  
ANISOU 1488  CA  ILE A 192     1382   1524   1431     63    297   -192       C  
ATOM   1489  C   ILE A 192      30.761   5.451   9.606  1.00 11.22           C  
ANISOU 1489  C   ILE A 192     1302   1478   1481      2    254   -204       C  
ATOM   1490  O   ILE A 192      31.951   5.544   9.328  1.00 12.55           O  
ANISOU 1490  O   ILE A 192     1281   1855   1631     85    334     56       O  
ATOM   1491  CB  ILE A 192      30.713   4.989  12.075  1.00 11.67           C  
ANISOU 1491  CB  ILE A 192     1297   1643   1493    -54    197   -238       C  
ATOM   1492  CG1 ILE A 192      30.273   4.024  13.156  1.00 14.54           C  
ANISOU 1492  CG1 ILE A 192     1802   2157   1565   -157    326     19       C  
ATOM   1493  CG2 ILE A 192      30.099   6.356  12.336  1.00 13.25           C  
ANISOU 1493  CG2 ILE A 192     1660   1817   1556     61    415   -460       C  
ATOM   1494  CD1 ILE A 192      31.076   2.819  13.384  1.00 19.44           C  
ANISOU 1494  CD1 ILE A 192     3328   2109   1950    368    472    229       C  
ATOM   1495  N   VAL A 193      29.806   6.188   9.011  1.00 10.98           N  
ANISOU 1495  N   VAL A 193     1243   1527   1402   -116    336   -176       N  
ATOM   1496  CA  VAL A 193      30.097   7.159   7.968  1.00 11.16           C  
ANISOU 1496  CA  VAL A 193     1292   1564   1384    -38    324   -138       C  
ATOM   1497  C   VAL A 193      29.955   8.557   8.541  1.00 10.70           C  
ANISOU 1497  C   VAL A 193     1338   1525   1203     62    228    -74       C  
ATOM   1498  O   VAL A 193      28.816   8.938   8.925  1.00 12.14           O  
ANISOU 1498  O   VAL A 193     1328   1662   1623     51    480    -56       O  
ATOM   1499  CB  VAL A 193      29.209   6.927   6.720  1.00 11.60           C  
ANISOU 1499  CB  VAL A 193     1350   1649   1408   -176    323   -233       C  
ATOM   1500  CG1 VAL A 193      29.613   7.929   5.636  1.00 13.11           C  
ANISOU 1500  CG1 VAL A 193     1519   1927   1534   -133    176    -35       C  
ATOM   1501  CG2 VAL A 193      29.319   5.521   6.200  1.00 13.51           C  
ANISOU 1501  CG2 VAL A 193     1778   1718   1638    -57    461   -388       C  
ATOM   1502  N   GLY A 194      30.998   9.349   8.529  1.00 11.79           N  
ANISOU 1502  N   GLY A 194     1266   1653   1560     15    340   -317       N  
ATOM   1503  CA  GLY A 194      30.981  10.712   9.011  1.00 12.71           C  
ANISOU 1503  CA  GLY A 194     1402   1781   1647    -68    259   -336       C  
ATOM   1504  C   GLY A 194      32.227  11.073   9.737  1.00 11.43           C  
ANISOU 1504  C   GLY A 194     1255   1654   1434    -18    264   -178       C  
ATOM   1505  O   GLY A 194      32.988  10.203  10.145  1.00 12.85           O  
ANISOU 1505  O   GLY A 194     1491   1731   1662     30    229     10       O  
ATOM   1506  N   ALA A 195      32.455  12.359   9.963  1.00 12.36           N  
ANISOU 1506  N   ALA A 195     1464   1645   1586     -5    199   -205       N  
ATOM   1507  CA  ALA A 195      33.675  12.825  10.538  1.00 12.01           C  
ANISOU 1507  CA  ALA A 195     1334   1771   1456   -128    382   -207       C  
ATOM   1508  C   ALA A 195      33.459  13.848  11.660  1.00 11.93           C  
ANISOU 1508  C   ALA A 195     1289   1834   1412   -157    285   -193       C  
ATOM   1509  O   ALA A 195      34.395  14.467  12.125  1.00 14.76           O  
ANISOU 1509  O   ALA A 195     1181   2423   2005   -192    319   -752       O  
ATOM   1510  CB  ALA A 195      34.613  13.371   9.477  1.00 14.27           C  
ANISOU 1510  CB  ALA A 195     1602   2253   1567   -121    619   -205       C  
ATOM   1511  N   GLY A 196      32.194  14.077  12.064  1.00 11.82           N  
ANISOU 1511  N   GLY A 196     1220   1820   1452   -167    243   -237       N  
ATOM   1512  CA  GLY A 196      31.872  14.952  13.153  1.00 12.05           C  
ANISOU 1512  CA  GLY A 196     1519   1612   1446    -50    308    -67       C  
ATOM   1513  C   GLY A 196      31.785  14.261  14.475  1.00 11.03           C  
ANISOU 1513  C   GLY A 196     1125   1650   1418     -1    222    -87       C  
ATOM   1514  O   GLY A 196      32.109  13.075  14.620  1.00 12.24           O  
ANISOU 1514  O   GLY A 196     1358   1647   1645    163    554     69       O  
ATOM   1515  N   TYR A 197      31.385  15.011  15.495  1.00 10.92           N  
ANISOU 1515  N   TYR A 197     1169   1550   1430     14    314    -91       N  
ATOM   1516  CA  TYR A 197      31.485  14.434  16.847  1.00 11.50           C  
ANISOU 1516  CA  TYR A 197     1170   1801   1399     84    192    -51       C  
ATOM   1517  C   TYR A 197      30.617  13.216  17.044  1.00 10.81           C  
ANISOU 1517  C   TYR A 197     1191   1721   1196    132    277   -130       C  
ATOM   1518  O   TYR A 197      31.015  12.298  17.768  1.00 11.55           O  
ANISOU 1518  O   TYR A 197     1311   1670   1409    223    262    -90       O  
ATOM   1519  CB  TYR A 197      31.244  15.485  17.933  1.00 12.45           C  
ANISOU 1519  CB  TYR A 197     1616   1711   1404    174     17   -117       C  
ATOM   1520  CG  TYR A 197      29.794  15.740  18.300  1.00 13.22           C  
ANISOU 1520  CG  TYR A 197     1844   1845   1335    296    347    -80       C  
ATOM   1521  CD1 TYR A 197      29.240  15.091  19.397  1.00 16.85           C  
ANISOU 1521  CD1 TYR A 197     2439   2543   1420    537    715    117       C  
ATOM   1522  CD2 TYR A 197      29.003  16.607  17.609  1.00 14.20           C  
ANISOU 1522  CD2 TYR A 197     1607   2037   1753    397    595     84       C  
ATOM   1523  CE1 TYR A 197      27.937  15.283  19.781  1.00 18.66           C  
ANISOU 1523  CE1 TYR A 197     2662   2379   2048    561   1043    165       C  
ATOM   1524  CE2 TYR A 197      27.673  16.831  17.975  1.00 17.22           C  
ANISOU 1524  CE2 TYR A 197     1663   2443   2438    377    944    418       C  
ATOM   1525  CZ  TYR A 197      27.165  16.142  19.076  1.00 18.07           C  
ANISOU 1525  CZ  TYR A 197     2154   2143   2567    454   1219    357       C  
ATOM   1526  OH  TYR A 197      25.884  16.344  19.480  1.00 22.56           O  
ANISOU 1526  OH  TYR A 197     2386   2972   3215    580   1696    450       O  
ATOM   1527  N   ILE A 198      29.419  13.182  16.464  1.00 11.33           N  
ANISOU 1527  N   ILE A 198     1158   1807   1339     51    276     23       N  
ATOM   1528  CA  ILE A 198      28.558  12.006  16.660  1.00 11.57           C  
ANISOU 1528  CA  ILE A 198     1191   1818   1387     18    384     32       C  
ATOM   1529  C   ILE A 198      29.195  10.776  16.049  1.00 10.93           C  
ANISOU 1529  C   ILE A 198     1125   1725   1301    -80    126     43       C  
ATOM   1530  O   ILE A 198      29.206   9.702  16.661  1.00 12.22           O  
ANISOU 1530  O   ILE A 198     1342   1719   1582    -35    173    150       O  
ATOM   1531  CB  ILE A 198      27.120  12.305  16.128  1.00 14.07           C  
ANISOU 1531  CB  ILE A 198     1082   1959   2304    -42    334    234       C  
ATOM   1532  CG1 ILE A 198      26.407  13.393  16.985  1.00 15.55           C  
ANISOU 1532  CG1 ILE A 198     1300   2254   2353    250    390    258       C  
ATOM   1533  CG2 ILE A 198      26.295  11.119  16.048  1.00 16.97           C  
ANISOU 1533  CG2 ILE A 198     1306   2446   2695   -185     83    -39       C  
ATOM   1534  CD1 ILE A 198      25.107  13.922  16.420  1.00 18.12           C  
ANISOU 1534  CD1 ILE A 198     1411   2726   2748    477    478    650       C  
ATOM   1535  N   ALA A 199      29.746  10.902  14.831  1.00 11.54           N  
ANISOU 1535  N   ALA A 199     1352   1629   1402     49    252      2       N  
ATOM   1536  CA  ALA A 199      30.420   9.772  14.190  1.00 12.09           C  
ANISOU 1536  CA  ALA A 199     1427   1730   1436    -18    189   -165       C  
ATOM   1537  C   ALA A 199      31.578   9.273  15.039  1.00 11.29           C  
ANISOU 1537  C   ALA A 199     1398   1568   1323     74    382   -191       C  
ATOM   1538  O   ALA A 199      31.787   8.084  15.236  1.00 11.78           O  
ANISOU 1538  O   ALA A 199     1611   1589   1277     37    373   -125       O  
ATOM   1539  CB  ALA A 199      30.904  10.206  12.810  1.00 12.95           C  
ANISOU 1539  CB  ALA A 199     1672   1845   1405    -53    265   -143       C  
ATOM   1540  N   VAL A 200      32.398  10.222  15.561  1.00 11.16           N  
ANISOU 1540  N   VAL A 200     1293   1616   1331     69    307    -55       N  
ATOM   1541  CA  VAL A 200      33.556   9.866  16.383  1.00 10.61           C  
ANISOU 1541  CA  VAL A 200     1156   1556   1320    136    438      6       C  
ATOM   1542  C   VAL A 200      33.120   9.110  17.617  1.00 10.32           C  
ANISOU 1542  C   VAL A 200     1085   1535   1300      1    297    -35       C  
ATOM   1543  O   VAL A 200      33.715   8.107  18.023  1.00 11.41           O  
ANISOU 1543  O   VAL A 200     1194   1529   1611    111    271     94       O  
ATOM   1544  CB  VAL A 200      34.374  11.132  16.704  1.00 10.87           C  
ANISOU 1544  CB  VAL A 200     1251   1505   1375    120    412     -4       C  
ATOM   1545  CG1 VAL A 200      35.393  10.882  17.774  1.00 12.47           C  
ANISOU 1545  CG1 VAL A 200     1195   1806   1738      5    266    -24       C  
ATOM   1546  CG2 VAL A 200      35.050  11.693  15.427  1.00 12.08           C  
ANISOU 1546  CG2 VAL A 200     1231   1761   1598    -39    539    -22       C  
ATOM   1547  N   GLU A 201      32.069   9.647  18.294  1.00 10.81           N  
ANISOU 1547  N   GLU A 201     1172   1668   1266     55    343    -37       N  
ATOM   1548  CA  GLU A 201      31.630   9.046  19.541  1.00 10.98           C  
ANISOU 1548  CA  GLU A 201     1210   1644   1319    108    321     60       C  
ATOM   1549  C   GLU A 201      31.075   7.656  19.284  1.00 10.83           C  
ANISOU 1549  C   GLU A 201     1140   1640   1335    102    360     46       C  
ATOM   1550  O   GLU A 201      31.356   6.694  20.043  1.00 11.76           O  
ANISOU 1550  O   GLU A 201     1395   1686   1388    148    290    214       O  
ATOM   1551  CB  GLU A 201      30.576   9.938  20.221  1.00 11.86           C  
ANISOU 1551  CB  GLU A 201     1332   1800   1374     70    413   -119       C  
ATOM   1552  CG  GLU A 201      31.138  11.220  20.789  1.00 11.97           C  
ANISOU 1552  CG  GLU A 201     1312   1890   1346     80    338   -117       C  
ATOM   1553  CD  GLU A 201      30.147  12.163  21.463  1.00 12.60           C  
ANISOU 1553  CD  GLU A 201     1170   1955   1663     60    230   -230       C  
ATOM   1554  OE1 GLU A 201      30.586  13.162  22.110  1.00 13.13           O  
ANISOU 1554  OE1 GLU A 201     1168   1891   1932     92     34   -332       O  
ATOM   1555  OE2 GLU A 201      28.924  11.878  21.363  1.00 14.90           O  
ANISOU 1555  OE2 GLU A 201     1226   2056   2380    -45    247   -318       O  
ATOM   1556  N   MET A 202      30.250   7.489  18.252  1.00 11.06           N  
ANISOU 1556  N   MET A 202     1234   1593   1376    116    305    108       N  
ATOM   1557  CA  MET A 202      29.651   6.182  18.000  1.00 12.29           C  
ANISOU 1557  CA  MET A 202     1286   1670   1713     72    332   -149       C  
ATOM   1558  C   MET A 202      30.745   5.157  17.615  1.00 11.25           C  
ANISOU 1558  C   MET A 202     1529   1598   1147     96    296     10       C  
ATOM   1559  O   MET A 202      30.689   4.017  18.095  1.00 11.98           O  
ANISOU 1559  O   MET A 202     1350   1619   1582     -3    265     34       O  
ATOM   1560  CB AMET A 202      28.712   6.392  16.800  0.52 11.19           C  
ANISOU 1560  CB AMET A 202     1161   1407   1684     14    510    -69       C  
ATOM   1561  CB BMET A 202      28.489   6.063  17.110  0.48 15.87           C  
ANISOU 1561  CB BMET A 202     1478   2049   2503   -295     31    204       C  
ATOM   1562  CG AMET A 202      27.455   7.177  17.080  0.52 11.50           C  
ANISOU 1562  CG AMET A 202      995   1338   2038   -129    458    -38       C  
ATOM   1563  CG BMET A 202      27.225   6.721  17.747  0.48 19.22           C  
ANISOU 1563  CG BMET A 202     1332   2586   3384    -10    163    606       C  
ATOM   1564  SD AMET A 202      26.300   6.290  18.087  0.52 16.02           S  
ANISOU 1564  SD AMET A 202     1557   2065   2465   -199    990    -44       S  
ATOM   1565  SD BMET A 202      25.802   6.673  16.590  0.48 23.09           S  
ANISOU 1565  SD BMET A 202     1808   3502   3462   -255   -115   1234       S  
ATOM   1566  CE AMET A 202      25.404   7.585  18.939  0.52 20.61           C  
ANISOU 1566  CE AMET A 202     2363   2472   2997    -40   1540   -271       C  
ATOM   1567  CE BMET A 202      26.505   7.836  15.561  0.48 45.96           C  
ANISOU 1567  CE BMET A 202     2548   7259   7655    421    -98   5839       C  
ATOM   1568  N   ALA A 203      31.697   5.548  16.765  1.00 11.44           N  
ANISOU 1568  N   ALA A 203     1493   1432   1423    191    406     20       N  
ATOM   1569  CA  ALA A 203      32.757   4.616  16.409  1.00 11.82           C  
ANISOU 1569  CA  ALA A 203     1538   1463   1488    226    386     48       C  
ATOM   1570  C   ALA A 203      33.568   4.181  17.604  1.00 11.47           C  
ANISOU 1570  C   ALA A 203     1233   1528   1599     85    404     65       C  
ATOM   1571  O   ALA A 203      33.935   3.010  17.749  1.00 12.59           O  
ANISOU 1571  O   ALA A 203     1588   1563   1632    177    292     43       O  
ATOM   1572  CB  ALA A 203      33.625   5.239  15.286  1.00 13.89           C  
ANISOU 1572  CB  ALA A 203     1894   1641   1743    163    746     67       C  
ATOM   1573  N   GLY A 204      33.896   5.134  18.485  1.00 12.04           N  
ANISOU 1573  N   GLY A 204     1447   1524   1604     86    276     52       N  
ATOM   1574  CA  GLY A 204      34.701   4.816  19.656  1.00 13.82           C  
ANISOU 1574  CA  GLY A 204     1617   1817   1816     -7     90     90       C  
ATOM   1575  C   GLY A 204      33.974   3.895  20.616  1.00 12.10           C  
ANISOU 1575  C   GLY A 204     1572   1609   1415    148     31    -36       C  
ATOM   1576  O   GLY A 204      34.646   3.008  21.186  1.00 13.98           O  
ANISOU 1576  O   GLY A 204     1603   1748   1962    161   -125     37       O  
ATOM   1577  N   ILE A 205      32.659   4.094  20.813  1.00 12.71           N  
ANISOU 1577  N   ILE A 205     1608   1715   1506    194    251   -131       N  
ATOM   1578  CA  ILE A 205      31.886   3.197  21.690  1.00 12.09           C  
ANISOU 1578  CA  ILE A 205     1691   1628   1276    227    167   -113       C  
ATOM   1579  C   ILE A 205      31.816   1.799  21.081  1.00 11.59           C  
ANISOU 1579  C   ILE A 205     1463   1649   1290    151    475    -61       C  
ATOM   1580  O   ILE A 205      32.090   0.810  21.787  1.00 12.55           O  
ANISOU 1580  O   ILE A 205     1590   1609   1571    180    499    124       O  
ATOM   1581  CB  ILE A 205      30.494   3.803  21.943  1.00 13.45           C  
ANISOU 1581  CB  ILE A 205     1857   1898   1357    457    373     -7       C  
ATOM   1582  CG1 ILE A 205      30.560   5.045  22.839  1.00 15.30           C  
ANISOU 1582  CG1 ILE A 205     2438   2177   1199    658    394   -133       C  
ATOM   1583  CG2 ILE A 205      29.582   2.742  22.526  1.00 16.18           C  
ANISOU 1583  CG2 ILE A 205     2077   2314   1756    364    756    169       C  
ATOM   1584  CD1 ILE A 205      29.335   5.921  22.785  1.00 18.44           C  
ANISOU 1584  CD1 ILE A 205     3078   1982   1946   1036   1065    371       C  
ATOM   1585  N   LEU A 206      31.453   1.724  19.807  1.00 11.69           N  
ANISOU 1585  N   LEU A 206     1479   1615   1346     39    453   -100       N  
ATOM   1586  CA  LEU A 206      31.310   0.390  19.205  1.00 11.89           C  
ANISOU 1586  CA  LEU A 206     1521   1549   1448     19    439   -108       C  
ATOM   1587  C   LEU A 206      32.613  -0.363  19.195  1.00 12.51           C  
ANISOU 1587  C   LEU A 206     1604   1647   1503    105    354    -19       C  
ATOM   1588  O   LEU A 206      32.655  -1.588  19.514  1.00 13.61           O  
ANISOU 1588  O   LEU A 206     1814   1594   1763    222    405     -2       O  
ATOM   1589  CB  LEU A 206      30.754   0.527  17.786  1.00 12.89           C  
ANISOU 1589  CB  LEU A 206     1635   1675   1590    120    301   -144       C  
ATOM   1590  CG  LEU A 206      29.253   0.786  17.727  1.00 13.13           C  
ANISOU 1590  CG  LEU A 206     1465   1847   1676    -88    382     42       C  
ATOM   1591  CD1 LEU A 206      28.837   1.312  16.355  1.00 15.46           C  
ANISOU 1591  CD1 LEU A 206     1991   2228   1654    259    146    -66       C  
ATOM   1592  CD2 LEU A 206      28.461  -0.473  18.072  1.00 15.89           C  
ANISOU 1592  CD2 LEU A 206     1816   1987   2235   -297    260    -60       C  
ATOM   1593  N   SER A 207      33.724   0.319  18.907  1.00 11.71           N  
ANISOU 1593  N   SER A 207     1460   1641   1348    167    376    -64       N  
ATOM   1594  CA  SER A 207      35.018  -0.374  18.897  1.00 12.64           C  
ANISOU 1594  CA  SER A 207     1671   1712   1421    239    502     31       C  
ATOM   1595  C   SER A 207      35.447  -0.815  20.276  1.00 12.56           C  
ANISOU 1595  C   SER A 207     1600   1612   1559    225    323    125       C  
ATOM   1596  O   SER A 207      35.935  -1.922  20.508  1.00 13.98           O  
ANISOU 1596  O   SER A 207     1892   1765   1657    453    584    163       O  
ATOM   1597  CB  SER A 207      36.064   0.565  18.264  1.00 13.36           C  
ANISOU 1597  CB  SER A 207     1513   1900   1663    252    491    131       C  
ATOM   1598  OG  SER A 207      37.265  -0.164  18.069  1.00 15.56           O  
ANISOU 1598  OG  SER A 207     1552   2243   2117    304    578    -20       O  
ATOM   1599  N   ALA A 208      35.290   0.076  21.280  1.00 12.34           N  
ANISOU 1599  N   ALA A 208     1560   1655   1475    181    330     60       N  
ATOM   1600  CA  ALA A 208      35.688  -0.266  22.654  1.00 13.35           C  
ANISOU 1600  CA  ALA A 208     1534   1921   1616    342    315    104       C  
ATOM   1601  C   ALA A 208      34.957  -1.496  23.139  1.00 13.45           C  
ANISOU 1601  C   ALA A 208     1800   1820   1492    436    455    123       C  
ATOM   1602  O   ALA A 208      35.478  -2.330  23.874  1.00 16.95           O  
ANISOU 1602  O   ALA A 208     2326   2160   1955    558    325    490       O  
ATOM   1603  CB  ALA A 208      35.455   0.927  23.572  1.00 14.11           C  
ANISOU 1603  CB  ALA A 208     1841   2096   1424    141    359    -21       C  
ATOM   1604  N   LEU A 209      33.668  -1.644  22.738  1.00 13.48           N  
ANISOU 1604  N   LEU A 209     1774   1981   1366    120    524      3       N  
ATOM   1605  CA  LEU A 209      32.810  -2.728  23.208  1.00 14.18           C  
ANISOU 1605  CA  LEU A 209     2072   1735   1582    146    490     76       C  
ATOM   1606  C   LEU A 209      32.965  -3.990  22.410  1.00 15.30           C  
ANISOU 1606  C   LEU A 209     2208   1814   1793    221    439     66       C  
ATOM   1607  O   LEU A 209      32.346  -5.016  22.772  1.00 18.92           O  
ANISOU 1607  O   LEU A 209     3327   1743   2118     71    978      7       O  
ATOM   1608  CB  LEU A 209      31.362  -2.265  23.274  1.00 14.36           C  
ANISOU 1608  CB  LEU A 209     1886   1849   1722   -143    562    -85       C  
ATOM   1609  CG  LEU A 209      31.120  -1.136  24.262  1.00 15.12           C  
ANISOU 1609  CG  LEU A 209     1902   1991   1850   -147    756   -224       C  
ATOM   1610  CD1 LEU A 209      29.675  -0.726  24.148  1.00 17.77           C  
ANISOU 1610  CD1 LEU A 209     2045   1923   2784    172    823    382       C  
ATOM   1611  CD2 LEU A 209      31.435  -1.536  25.689  1.00 16.38           C  
ANISOU 1611  CD2 LEU A 209     2195   2230   1799   -308    709   -140       C  
ATOM   1612  N   GLY A 210      33.820  -3.978  21.393  1.00 14.28           N  
ANISOU 1612  N   GLY A 210     2337   1605   1486    410    374    103       N  
ATOM   1613  CA  GLY A 210      34.269  -5.201  20.685  1.00 15.35           C  
ANISOU 1613  CA  GLY A 210     2131   1834   1869    391    195    -97       C  
ATOM   1614  C   GLY A 210      33.851  -5.301  19.254  1.00 14.51           C  
ANISOU 1614  C   GLY A 210     2093   1760   1659    320    533   -107       C  
ATOM   1615  O   GLY A 210      34.168  -6.344  18.624  1.00 19.06           O  
ANISOU 1615  O   GLY A 210     3394   1968   1882    959    310   -165       O  
ATOM   1616  N   SER A 211      33.142  -4.340  18.680  1.00 13.57           N  
ANISOU 1616  N   SER A 211     1864   1622   1671    185    423     -9       N  
ATOM   1617  CA  SER A 211      32.833  -4.438  17.251  1.00 13.95           C  
ANISOU 1617  CA  SER A 211     1906   1651   1741    300    410   -118       C  
ATOM   1618  C   SER A 211      34.074  -4.169  16.415  1.00 13.01           C  
ANISOU 1618  C   SER A 211     1899   1387   1656    289    399    -92       C  
ATOM   1619  O   SER A 211      34.888  -3.296  16.789  1.00 14.00           O  
ANISOU 1619  O   SER A 211     1917   1720   1681    116    461   -221       O  
ATOM   1620  CB  SER A 211      31.741  -3.420  16.900  1.00 13.56           C  
ANISOU 1620  CB  SER A 211     1833   1561   1758    262    326   -216       C  
ATOM   1621  OG  SER A 211      31.214  -3.675  15.604  1.00 15.00           O  
ANISOU 1621  OG  SER A 211     2135   1961   1605    354    344    -75       O  
ATOM   1622  N   LYS A 212      34.227  -4.864  15.298  1.00 13.68           N  
ANISOU 1622  N   LYS A 212     1919   1573   1705    170    461   -104       N  
ATOM   1623  CA  LYS A 212      35.309  -4.584  14.337  1.00 14.17           C  
ANISOU 1623  CA  LYS A 212     2072   1552   1760    270    627     -9       C  
ATOM   1624  C   LYS A 212      34.856  -3.366  13.521  1.00 12.48           C  
ANISOU 1624  C   LYS A 212     1576   1592   1575    273    538   -140       C  
ATOM   1625  O   LYS A 212      33.934  -3.465  12.720  1.00 13.36           O  
ANISOU 1625  O   LYS A 212     1700   1746   1631     81    454   -275       O  
ATOM   1626  CB ALYS A 212      35.675  -5.739  13.420  0.38 17.74           C  
ANISOU 1626  CB ALYS A 212     2917   1981   1843   1092    523    -90       C  
ATOM   1627  CB BLYS A 212      35.497  -5.779  13.400  0.62 14.29           C  
ANISOU 1627  CB BLYS A 212     1818   1579   2033    487    523    -58       C  
ATOM   1628  CG ALYS A 212      37.032  -5.671  12.743  0.38 20.75           C  
ANISOU 1628  CG ALYS A 212     3493   2276   2113    998   1124    -68       C  
ATOM   1629  CG BLYS A 212      36.537  -5.566  12.306  0.62 17.34           C  
ANISOU 1629  CG BLYS A 212     2134   2225   2231    585    788   -114       C  
ATOM   1630  CD ALYS A 212      38.098  -4.890  13.460  0.38 29.38           C  
ANISOU 1630  CD ALYS A 212     3221   4024   3919    270    577    292       C  
ATOM   1631  CD BLYS A 212      36.859  -6.853  11.566  0.62 24.61           C  
ANISOU 1631  CD BLYS A 212     3374   2969   3008    513   1442   -875       C  
ATOM   1632  CE ALYS A 212      38.595  -5.413  14.782  0.38 40.38           C  
ANISOU 1632  CE ALYS A 212     6449   4583   4309   1299  -1371   -769       C  
ATOM   1633  CE BLYS A 212      37.144  -6.647  10.086  0.62 34.28           C  
ANISOU 1633  CE BLYS A 212     6107   3932   2986   1765   1648   -795       C  
ATOM   1634  NZ ALYS A 212      38.568  -4.450  15.925  0.38 35.48           N  
ANISOU 1634  NZ ALYS A 212     6813   1510   5159    715  -2483    -58       N  
ATOM   1635  NZ BLYS A 212      37.084  -7.937   9.310  0.62 37.47           N  
ANISOU 1635  NZ BLYS A 212     8026   3611   2600   1172   1870   -436       N  
ATOM   1636  N   THR A 213      35.440  -2.225  13.830  1.00 12.53           N  
ANISOU 1636  N   THR A 213     1625   1599   1537    142    502    -27       N  
ATOM   1637  CA  THR A 213      34.846  -0.958  13.463  1.00 12.18           C  
ANISOU 1637  CA  THR A 213     1636   1534   1456    123    380    -55       C  
ATOM   1638  C   THR A 213      35.719  -0.179  12.475  1.00 12.57           C  
ANISOU 1638  C   THR A 213     1551   1701   1524    143    466    -65       C  
ATOM   1639  O   THR A 213      36.948  -0.072  12.681  1.00 14.00           O  
ANISOU 1639  O   THR A 213     1562   1878   1880    151    347    107       O  
ATOM   1640  CB  THR A 213      34.688  -0.125  14.754  1.00 12.83           C  
ANISOU 1640  CB  THR A 213     1754   1654   1467    146    492    -48       C  
ATOM   1641  OG1 THR A 213      33.864  -0.813  15.709  1.00 14.78           O  
ANISOU 1641  OG1 THR A 213     1876   2075   1665      6    693   -118       O  
ATOM   1642  CG2 THR A 213      34.032   1.212  14.484  1.00 14.16           C  
ANISOU 1642  CG2 THR A 213     1975   1728   1677    315    219   -244       C  
ATOM   1643  N   SER A 214      35.079   0.390  11.481  1.00 12.46           N  
ANISOU 1643  N   SER A 214     1581   1514   1640    114    422     48       N  
ATOM   1644  CA  SER A 214      35.676   1.332  10.552  1.00 12.61           C  
ANISOU 1644  CA  SER A 214     1579   1654   1560    168    487    -54       C  
ATOM   1645  C   SER A 214      34.903   2.665  10.621  1.00 11.76           C  
ANISOU 1645  C   SER A 214     1378   1612   1477    138    413     29       C  
ATOM   1646  O   SER A 214      33.676   2.662  10.802  1.00 14.20           O  
ANISOU 1646  O   SER A 214     1355   1871   2171     88    412     97       O  
ATOM   1647  CB  SER A 214      35.613   0.862   9.110  1.00 14.14           C  
ANISOU 1647  CB  SER A 214     1921   1815   1636    147    692   -104       C  
ATOM   1648  OG  SER A 214      36.186  -0.440   8.992  1.00 15.91           O  
ANISOU 1648  OG  SER A 214     2152   1948   1944    295    729   -239       O  
ATOM   1649  N   LEU A 215      35.608   3.761  10.446  1.00 11.88           N  
ANISOU 1649  N   LEU A 215     1190   1650   1675    162    416     35       N  
ATOM   1650  CA  LEU A 215      35.051   5.102  10.391  1.00 11.54           C  
ANISOU 1650  CA  LEU A 215     1124   1644   1617     71    335     57       C  
ATOM   1651  C   LEU A 215      35.453   5.673   9.032  1.00 11.69           C  
ANISOU 1651  C   LEU A 215     1286   1583   1572    164    395    -20       C  
ATOM   1652  O   LEU A 215      36.660   5.831   8.748  1.00 13.24           O  
ANISOU 1652  O   LEU A 215     1320   2140   1571    245    499    104       O  
ATOM   1653  CB  LEU A 215      35.611   5.919  11.533  1.00 12.12           C  
ANISOU 1653  CB  LEU A 215     1261   1829   1514    156    369    -92       C  
ATOM   1654  CG  LEU A 215      35.142   7.367  11.620  1.00 12.72           C  
ANISOU 1654  CG  LEU A 215     1568   1739   1526    152    500      4       C  
ATOM   1655  CD1 LEU A 215      33.644   7.467  11.824  1.00 14.26           C  
ANISOU 1655  CD1 LEU A 215     1481   1894   2043    372    407    191       C  
ATOM   1656  CD2 LEU A 215      35.917   8.121  12.672  1.00 15.70           C  
ANISOU 1656  CD2 LEU A 215     1722   2145   2098    -70    455   -442       C  
ATOM   1657  N   MET A 216      34.469   5.970   8.204  1.00 11.93           N  
ANISOU 1657  N   MET A 216     1339   1719   1473    155    450     28       N  
ATOM   1658  CA  MET A 216      34.707   6.429   6.832  1.00 11.94           C  
ANISOU 1658  CA  MET A 216     1450   1692   1395     50    570   -126       C  
ATOM   1659  C   MET A 216      34.541   7.930   6.730  1.00 11.61           C  
ANISOU 1659  C   MET A 216     1294   1723   1395    102    358     22       C  
ATOM   1660  O   MET A 216      33.447   8.435   6.989  1.00 13.13           O  
ANISOU 1660  O   MET A 216     1272   1782   1933    176    495    164       O  
ATOM   1661  CB  MET A 216      33.727   5.715   5.902  1.00 12.75           C  
ANISOU 1661  CB  MET A 216     1508   1823   1515     26    567   -228       C  
ATOM   1662  CG  MET A 216      34.141   5.890   4.434  1.00 13.89           C  
ANISOU 1662  CG  MET A 216     1751   1984   1543   -154    457   -203       C  
ATOM   1663  SD  MET A 216      32.916   5.288   3.261  1.00 15.18           S  
ANISOU 1663  SD  MET A 216     1942   2270   1556   -159    456   -106       S  
ATOM   1664  CE  MET A 216      32.729   3.612   3.854  1.00 14.30           C  
ANISOU 1664  CE  MET A 216     1769   2001   1662   -109     29   -149       C  
ATOM   1665  N   ILE A 217      35.608   8.604   6.340  1.00 11.50           N  
ANISOU 1665  N   ILE A 217     1354   1795   1219     86    488    -49       N  
ATOM   1666  CA  ILE A 217      35.666  10.066   6.353  1.00 11.98           C  
ANISOU 1666  CA  ILE A 217     1441   1765   1346    -35    503    -27       C  
ATOM   1667  C   ILE A 217      36.071  10.565   4.976  1.00 11.41           C  
ANISOU 1667  C   ILE A 217     1431   1655   1250     -5    475    -75       C  
ATOM   1668  O   ILE A 217      36.829   9.921   4.244  1.00 12.60           O  
ANISOU 1668  O   ILE A 217     1730   1741   1315     65    610   -154       O  
ATOM   1669  CB  ILE A 217      36.623  10.571   7.458  1.00 11.95           C  
ANISOU 1669  CB  ILE A 217     1408   1797   1337     64    497   -159       C  
ATOM   1670  CG1 ILE A 217      38.080  10.210   7.223  1.00 11.77           C  
ANISOU 1670  CG1 ILE A 217     1446   1805   1222   -101    487   -115       C  
ATOM   1671  CG2 ILE A 217      36.164  10.034   8.813  1.00 13.55           C  
ANISOU 1671  CG2 ILE A 217     1340   2346   1464   -139    547    -24       C  
ATOM   1672  CD1 ILE A 217      38.995  10.854   8.221  1.00 13.63           C  
ANISOU 1672  CD1 ILE A 217     1398   2119   1663     52    257   -326       C  
ATOM   1673  N   ARG A 218      35.586  11.754   4.615  1.00 11.99           N  
ANISOU 1673  N   ARG A 218     1633   1897   1025    172    366    -98       N  
ATOM   1674  CA  ARG A 218      35.786  12.309   3.291  1.00 12.24           C  
ANISOU 1674  CA  ARG A 218     1659   1819   1172     42    323     -5       C  
ATOM   1675  C   ARG A 218      37.194  12.862   3.071  1.00 11.80           C  
ANISOU 1675  C   ARG A 218     1645   1667   1171     95    333   -117       C  
ATOM   1676  O   ARG A 218      37.607  12.971   1.902  1.00 12.89           O  
ANISOU 1676  O   ARG A 218     1772   1871   1256    -12    453   -176       O  
ATOM   1677  CB  ARG A 218      34.726  13.368   2.998  1.00 13.46           C  
ANISOU 1677  CB  ARG A 218     1589   1888   1638     57    120     94       C  
ATOM   1678  CG  ARG A 218      33.327  12.836   2.833  1.00 14.40           C  
ANISOU 1678  CG  ARG A 218     1634   2122   1716    -39    342    143       C  
ATOM   1679  CD  ARG A 218      32.311  13.985   2.758  1.00 16.68           C  
ANISOU 1679  CD  ARG A 218     1529   2617   2193    145    435    394       C  
ATOM   1680  NE  ARG A 218      32.421  14.763   1.536  1.00 17.81           N  
ANISOU 1680  NE  ARG A 218     1794   2606   2367    350    184    551       N  
ATOM   1681  CZ  ARG A 218      31.842  14.504   0.366  1.00 23.28           C  
ANISOU 1681  CZ  ARG A 218     3311   2848   2687    386   -616    655       C  
ATOM   1682  NH1 ARG A 218      31.103  13.406   0.250  1.00 23.65           N  
ANISOU 1682  NH1 ARG A 218     2641   3464   2880    293   -343    -36       N  
ATOM   1683  NH2 ARG A 218      31.993  15.275  -0.718  1.00 25.58           N  
ANISOU 1683  NH2 ARG A 218     2867   4193   2660    928     27   1031       N  
ATOM   1684  N   HIS A 219      37.927  13.200   4.113  1.00 12.76           N  
ANISOU 1684  N   HIS A 219     1603   1976   1270   -192    369   -107       N  
ATOM   1685  CA  HIS A 219      39.243  13.792   3.998  1.00 12.87           C  
ANISOU 1685  CA  HIS A 219     1551   1923   1417    -59    440   -162       C  
ATOM   1686  C   HIS A 219      40.212  12.949   4.807  1.00 12.37           C  
ANISOU 1686  C   HIS A 219     1586   2023   1091    -19    528   -335       C  
ATOM   1687  O   HIS A 219      40.063  11.718   4.868  1.00 13.08           O  
ANISOU 1687  O   HIS A 219     1545   2023   1403    -25    471   -169       O  
ATOM   1688  CB  HIS A 219      39.201  15.281   4.369  1.00 13.54           C  
ANISOU 1688  CB  HIS A 219     1791   1962   1393   -274    189    -14       C  
ATOM   1689  CG  HIS A 219      38.270  16.096   3.581  1.00 14.72           C  
ANISOU 1689  CG  HIS A 219     2291   1765   1538    -35    224   -167       C  
ATOM   1690  ND1 HIS A 219      38.648  16.858   2.509  1.00 21.05           N  
ANISOU 1690  ND1 HIS A 219     2891   2947   2160    202    365    821       N  
ATOM   1691  CD2 HIS A 219      36.927  16.228   3.722  1.00 16.27           C  
ANISOU 1691  CD2 HIS A 219     2288   1964   1931    276     68    -12       C  
ATOM   1692  CE1 HIS A 219      37.580  17.485   1.999  1.00 21.27           C  
ANISOU 1692  CE1 HIS A 219     3149   3144   1790    679    416    373       C  
ATOM   1693  NE2 HIS A 219      36.549  17.086   2.730  1.00 19.22           N  
ANISOU 1693  NE2 HIS A 219     2855   2395   2051    322     72    339       N  
ATOM   1694  N   ASP A 220      41.244  13.565   5.395  1.00 12.79           N  
ANISOU 1694  N   ASP A 220     1668   1978   1212    -17    382   -296       N  
ATOM   1695  CA  ASP A 220      42.325  12.849   6.066  1.00 14.43           C  
ANISOU 1695  CA  ASP A 220     1384   2625   1475     39    450   -251       C  
ATOM   1696  C   ASP A 220      42.148  12.711   7.582  1.00 12.41           C  
ANISOU 1696  C   ASP A 220     1263   2071   1380    -24    437   -228       C  
ATOM   1697  O   ASP A 220      42.786  11.847   8.190  1.00 14.74           O  
ANISOU 1697  O   ASP A 220     1602   2407   1594    284    483   -217       O  
ATOM   1698  CB  ASP A 220      43.691  13.559   5.811  1.00 18.82           C  
ANISOU 1698  CB  ASP A 220     1564   4000   1586   -383    675     -2       C  
ATOM   1699  CG  ASP A 220      43.713  15.034   6.202  1.00 22.50           C  
ANISOU 1699  CG  ASP A 220     2593   3870   2084  -1297    481    209       C  
ATOM   1700  OD1 ASP A 220      44.798  15.555   6.542  1.00 28.97           O  
ANISOU 1700  OD1 ASP A 220     3000   5414   2593  -2016    554   -196       O  
ATOM   1701  OD2 ASP A 220      42.651  15.726   6.198  1.00 24.42           O  
ANISOU 1701  OD2 ASP A 220     3323   2971   2986  -1030    102   -168       O  
ATOM   1702  N   LYS A 221      41.315  13.555   8.188  1.00 12.56           N  
ANISOU 1702  N   LYS A 221     1386   2040   1347    170    378   -110       N  
ATOM   1703  CA  LYS A 221      41.188  13.690   9.626  1.00 12.36           C  
ANISOU 1703  CA  LYS A 221     1297   2094   1306     30    436   -215       C  
ATOM   1704  C   LYS A 221      39.738  13.873   9.999  1.00 11.33           C  
ANISOU 1704  C   LYS A 221     1278   1671   1357     41    359   -156       C  
ATOM   1705  O   LYS A 221      38.949  14.432   9.213  1.00 11.75           O  
ANISOU 1705  O   LYS A 221     1458   1758   1247     79    487    -10       O  
ATOM   1706  CB  LYS A 221      42.026  14.854  10.120  1.00 13.80           C  
ANISOU 1706  CB  LYS A 221     1440   2293   1510   -212    523   -331       C  
ATOM   1707  CG  LYS A 221      43.522  14.629   9.994  1.00 14.18           C  
ANISOU 1707  CG  LYS A 221     1442   2374   1571   -135    481   -296       C  
ATOM   1708  CD  LYS A 221      44.378  15.813  10.246  1.00 16.36           C  
ANISOU 1708  CD  LYS A 221     1653   2735   1826   -399    424   -499       C  
ATOM   1709  CE  LYS A 221      45.855  15.504  10.090  1.00 19.78           C  
ANISOU 1709  CE  LYS A 221     1585   3998   1932   -702    839   -658       C  
ATOM   1710  NZ  LYS A 221      46.629  16.741  10.216  1.00 22.23           N  
ANISOU 1710  NZ  LYS A 221     1984   4079   2383   -987    948   -596       N  
ATOM   1711  N   VAL A 222      39.399  13.528  11.229  1.00 11.81           N  
ANISOU 1711  N   VAL A 222     1313   1967   1207     83    379    -57       N  
ATOM   1712  CA  VAL A 222      38.105  13.826  11.819  1.00 11.68           C  
ANISOU 1712  CA  VAL A 222     1154   1948   1334    -68    303   -194       C  
ATOM   1713  C   VAL A 222      38.101  15.220  12.433  1.00 11.20           C  
ANISOU 1713  C   VAL A 222     1188   1915   1152      1    282   -159       C  
ATOM   1714  O   VAL A 222      39.134  15.881  12.646  1.00 12.24           O  
ANISOU 1714  O   VAL A 222     1193   1999   1457   -144    414   -162       O  
ATOM   1715  CB  VAL A 222      37.744  12.778  12.913  1.00 12.40           C  
ANISOU 1715  CB  VAL A 222     1404   1943   1365   -121    547   -269       C  
ATOM   1716  CG1 VAL A 222      37.656  11.408  12.335  1.00 15.76           C  
ANISOU 1716  CG1 VAL A 222     2314   1867   1808   -215    772   -250       C  
ATOM   1717  CG2 VAL A 222      38.670  12.857  14.129  1.00 12.88           C  
ANISOU 1717  CG2 VAL A 222     1289   2072   1532    144    447     78       C  
ATOM   1718  N   LEU A 223      36.899  15.716  12.742  1.00 11.48           N  
ANISOU 1718  N   LEU A 223     1159   1895   1306    -93    323   -171       N  
ATOM   1719  CA  LEU A 223      36.733  16.954  13.534  1.00 11.63           C  
ANISOU 1719  CA  LEU A 223     1264   1773   1382    -39    517    -73       C  
ATOM   1720  C   LEU A 223      37.473  18.115  12.898  1.00 11.91           C  
ANISOU 1720  C   LEU A 223     1287   1811   1429    -11    385    -17       C  
ATOM   1721  O   LEU A 223      38.157  18.901  13.551  1.00 12.91           O  
ANISOU 1721  O   LEU A 223     1471   1711   1721   -105    260     -4       O  
ATOM   1722  CB  LEU A 223      37.130  16.767  15.004  1.00 11.90           C  
ANISOU 1722  CB  LEU A 223     1346   1768   1406    101    460   -129       C  
ATOM   1723  CG  LEU A 223      36.374  15.662  15.754  1.00 12.17           C  
ANISOU 1723  CG  LEU A 223     1299   1790   1534    -61    357    -62       C  
ATOM   1724  CD1 LEU A 223      36.860  15.666  17.211  1.00 13.86           C  
ANISOU 1724  CD1 LEU A 223     1418   2270   1580    -17    386    119       C  
ATOM   1725  CD2 LEU A 223      34.888  15.788  15.688  1.00 13.21           C  
ANISOU 1725  CD2 LEU A 223     1231   2174   1616    198    375    205       C  
ATOM   1726  N   ARG A 224      37.342  18.268  11.579  1.00 12.89           N  
ANISOU 1726  N   ARG A 224     1788   1678   1433    -23    421    119       N  
ATOM   1727  CA  ARG A 224      38.068  19.297  10.854  1.00 14.14           C  
ANISOU 1727  CA  ARG A 224     1997   1809   1565   -162    637     -6       C  
ATOM   1728  C   ARG A 224      37.652  20.706  11.246  1.00 15.02           C  
ANISOU 1728  C   ARG A 224     2330   1735   1643    -99    495    -23       C  
ATOM   1729  O   ARG A 224      38.465  21.616  11.004  1.00 18.36           O  
ANISOU 1729  O   ARG A 224     2870   1868   2238   -331    803    -79       O  
ATOM   1730  CB  ARG A 224      37.944  19.050   9.338  1.00 15.86           C  
ANISOU 1730  CB  ARG A 224     2568   2022   1435      7    628     66       C  
ATOM   1731  CG  ARG A 224      38.683  17.745   8.956  1.00 17.13           C  
ANISOU 1731  CG  ARG A 224     2575   2039   1896   -132    741   -262       C  
ATOM   1732  CD  ARG A 224      38.819  17.528   7.499  1.00 22.91           C  
ANISOU 1732  CD  ARG A 224     3782   2833   2091    209   1282   -447       C  
ATOM   1733  NE  ARG A 224      37.752  18.018   6.716  1.00 33.06           N  
ANISOU 1733  NE  ARG A 224     6637   3953   1970   1235    -32   -457       N  
ATOM   1734  CZ  ARG A 224      37.685  18.829   5.695  1.00 27.82           C  
ANISOU 1734  CZ  ARG A 224     5377   2821   2373    464    535   -560       C  
ATOM   1735  NH1 ARG A 224      36.478  19.073   5.200  1.00 37.44           N  
ANISOU 1735  NH1 ARG A 224     6036   4115   4073    223   -604    759       N  
ATOM   1736  NH2 ARG A 224      38.747  19.403   5.141  1.00 39.27           N  
ANISOU 1736  NH2 ARG A 224     6501   4855   3563  -1227   1335  -1721       N  
ATOM   1737  N   SER A 225      36.484  20.904  11.829  1.00 14.95           N  
ANISOU 1737  N   SER A 225     2207   2016   1457    130    244    -73       N  
ATOM   1738  CA  SER A 225      36.126  22.241  12.287  1.00 15.62           C  
ANISOU 1738  CA  SER A 225     2234   2117   1582    252    169   -119       C  
ATOM   1739  C   SER A 225      36.752  22.615  13.635  1.00 14.84           C  
ANISOU 1739  C   SER A 225     2099   2012   1527    360    152   -187       C  
ATOM   1740  O   SER A 225      36.652  23.767  14.046  1.00 18.23           O  
ANISOU 1740  O   SER A 225     2929   1904   2093    271    -55   -151       O  
ATOM   1741  CB  SER A 225      34.601  22.378  12.440  1.00 18.41           C  
ANISOU 1741  CB  SER A 225     2156   2568   2268    444   -190   -117       C  
ATOM   1742  OG  SER A 225      34.103  21.435  13.395  1.00 22.50           O  
ANISOU 1742  OG  SER A 225     2258   3860   2431    494    604    225       O  
ATOM   1743  N   PHE A 226      37.353  21.639  14.305  1.00 12.80           N  
ANISOU 1743  N   PHE A 226     1584   1773   1505    -11    343   -111       N  
ATOM   1744  CA  PHE A 226      38.025  21.892  15.584  1.00 12.55           C  
ANISOU 1744  CA  PHE A 226     1508   1697   1564    -48    297      6       C  
ATOM   1745  C   PHE A 226      39.439  22.373  15.312  1.00 13.33           C  
ANISOU 1745  C   PHE A 226     1586   1901   1576   -134    348     22       C  
ATOM   1746  O   PHE A 226      39.894  22.435  14.161  1.00 14.55           O  
ANISOU 1746  O   PHE A 226     1659   2225   1645   -238    452     75       O  
ATOM   1747  CB  PHE A 226      38.055  20.625  16.415  1.00 13.17           C  
ANISOU 1747  CB  PHE A 226     1622   1841   1541   -132    337     29       C  
ATOM   1748  CG  PHE A 226      36.716  20.213  17.017  1.00 13.54           C  
ANISOU 1748  CG  PHE A 226     1880   1760   1506   -270    487    -68       C  
ATOM   1749  CD1 PHE A 226      35.619  19.930  16.275  1.00 14.60           C  
ANISOU 1749  CD1 PHE A 226     1653   2245   1647    -90    501   -109       C  
ATOM   1750  CD2 PHE A 226      36.638  20.128  18.425  1.00 15.54           C  
ANISOU 1750  CD2 PHE A 226     2238   2206   1462   -320    488     41       C  
ATOM   1751  CE1 PHE A 226      34.422  19.521  16.848  1.00 15.05           C  
ANISOU 1751  CE1 PHE A 226     1736   2108   1872    -16    682    -22       C  
ATOM   1752  CE2 PHE A 226      35.441  19.749  19.021  1.00 17.77           C  
ANISOU 1752  CE2 PHE A 226     2594   2482   1674   -550    744    -91       C  
ATOM   1753  CZ  PHE A 226      34.324  19.470  18.222  1.00 15.49           C  
ANISOU 1753  CZ  PHE A 226     1998   1966   1920    -28    800    126       C  
ATOM   1754  N   ASP A 227      40.131  22.827  16.366  1.00 13.68           N  
ANISOU 1754  N   ASP A 227     1644   1748   1806   -224    335   -154       N  
ATOM   1755  CA  ASP A 227      41.509  23.243  16.187  1.00 13.66           C  
ANISOU 1755  CA  ASP A 227     1641   1861   1688   -227    287     56       C  
ATOM   1756  C   ASP A 227      42.304  22.132  15.517  1.00 14.03           C  
ANISOU 1756  C   ASP A 227     1537   2015   1777   -160    362    100       C  
ATOM   1757  O   ASP A 227      42.096  20.939  15.834  1.00 14.00           O  
ANISOU 1757  O   ASP A 227     1527   1961   1831    -93    411     72       O  
ATOM   1758  CB  ASP A 227      42.114  23.595  17.552  1.00 13.93           C  
ANISOU 1758  CB  ASP A 227     1539   1978   1776   -155    223     43       C  
ATOM   1759  CG  ASP A 227      43.501  24.188  17.415  1.00 15.04           C  
ANISOU 1759  CG  ASP A 227     1553   2085   2077   -212    224    -67       C  
ATOM   1760  OD1 ASP A 227      43.612  25.434  17.297  1.00 18.94           O  
ANISOU 1760  OD1 ASP A 227     1863   2140   3195   -335    228    141       O  
ATOM   1761  OD2 ASP A 227      44.475  23.447  17.457  1.00 15.78           O  
ANISOU 1761  OD2 ASP A 227     1553   2292   2150   -184    206   -147       O  
ATOM   1762  N   SER A 228      43.250  22.544  14.661  1.00 14.84           N  
ANISOU 1762  N   SER A 228     1583   2142   1913   -243    515     19       N  
ATOM   1763  CA  SER A 228      44.044  21.551  13.975  1.00 16.18           C  
ANISOU 1763  CA  SER A 228     2286   2091   1771   -213    812     90       C  
ATOM   1764  C   SER A 228      44.719  20.514  14.885  1.00 14.84           C  
ANISOU 1764  C   SER A 228     1488   2165   1983   -273    722     27       C  
ATOM   1765  O   SER A 228      44.875  19.365  14.483  1.00 15.41           O  
ANISOU 1765  O   SER A 228     1600   2255   2000   -156    577   -115       O  
ATOM   1766  CB  SER A 228      45.124  22.220  13.094  1.00 19.01           C  
ANISOU 1766  CB  SER A 228     1925   2723   2574     34    994    530       C  
ATOM   1767  OG  SER A 228      46.010  22.978  13.867  1.00 24.65           O  
ANISOU 1767  OG  SER A 228     2100   3508   3758   -493    718    364       O  
ATOM   1768  N   MET A 229      45.175  20.954  16.069  1.00 15.75           N  
ANISOU 1768  N   MET A 229     1772   2083   2129   -361    492    -18       N  
ATOM   1769  CA  MET A 229      45.814  19.998  16.981  1.00 15.79           C  
ANISOU 1769  CA  MET A 229     1642   2030   2330   -329    170   -197       C  
ATOM   1770  C   MET A 229      44.864  18.880  17.426  1.00 14.36           C  
ANISOU 1770  C   MET A 229     1583   1918   1955   -167     71    -97       C  
ATOM   1771  O   MET A 229      45.268  17.707  17.542  1.00 16.13           O  
ANISOU 1771  O   MET A 229     1960   1978   2191    -86    285    -46       O  
ATOM   1772  CB  MET A 229      46.330  20.713  18.268  1.00 16.99           C  
ANISOU 1772  CB  MET A 229     1775   1917   2765   -139   -106   -384       C  
ATOM   1773  CG  MET A 229      46.858  19.711  19.385  1.00 23.54           C  
ANISOU 1773  CG  MET A 229     2883   2553   3506   1354  -1465  -1006       C  
ATOM   1774  SD  MET A 229      47.223  20.695  20.891  1.00 21.60           S  
ANISOU 1774  SD  MET A 229     3012   2414   2780     -2   -425   -162       S  
ATOM   1775  CE  MET A 229      45.507  20.708  21.486  1.00 23.93           C  
ANISOU 1775  CE  MET A 229     3431   2892   2767  -1226    193   -183       C  
ATOM   1776  N   ILE A 230      43.608  19.252  17.687  1.00 13.90           N  
ANISOU 1776  N   ILE A 230     1581   1742   1958   -251    147   -113       N  
ATOM   1777  CA  ILE A 230      42.585  18.303  18.082  1.00 14.09           C  
ANISOU 1777  CA  ILE A 230     1861   1798   1694   -218    509   -163       C  
ATOM   1778  C   ILE A 230      42.218  17.389  16.915  1.00 12.61           C  
ANISOU 1778  C   ILE A 230     1241   1713   1836    -84    380   -140       C  
ATOM   1779  O   ILE A 230      42.078  16.175  17.099  1.00 13.32           O  
ANISOU 1779  O   ILE A 230     1413   1825   1824   -205    621   -195       O  
ATOM   1780  CB AILE A 230      41.288  19.043  18.514  0.28 16.17           C  
ANISOU 1780  CB AILE A 230     2049   2473   1623     19    746   -197       C  
ATOM   1781  CB BILE A 230      41.366  19.046  18.681  0.71 13.98           C  
ANISOU 1781  CB BILE A 230     2125   1744   1442   -118    670     82       C  
ATOM   1782  CG1AILE A 230      41.283  19.756  19.872  0.28 15.73           C  
ANISOU 1782  CG1AILE A 230     2237   2146   1595    204    478    -85       C  
ATOM   1783  CG1BILE A 230      41.808  19.849  19.921  0.71 15.96           C  
ANISOU 1783  CG1BILE A 230     2452   1978   1633    -27    466   -161       C  
ATOM   1784  CG2AILE A 230      40.106  18.069  18.440  0.28 14.29           C  
ANISOU 1784  CG2AILE A 230     1888   2050   1493    308   1227   -475       C  
ATOM   1785  CG2BILE A 230      40.175  18.140  18.972  0.71 14.83           C  
ANISOU 1785  CG2BILE A 230     1992   2175   1467   -167    745     76       C  
ATOM   1786  CD1AILE A 230      39.983  20.506  20.176  0.28 13.89           C  
ANISOU 1786  CD1AILE A 230     1797   1476   2004   -527    898   -103       C  
ATOM   1787  CD1BILE A 230      42.342  18.976  21.037  0.71 17.12           C  
ANISOU 1787  CD1BILE A 230     2486   2247   1771   -293    121    -66       C  
ATOM   1788  N   SER A 231      42.022  17.975  15.731  1.00 12.89           N  
ANISOU 1788  N   SER A 231     1255   1912   1732    -34    350   -140       N  
ATOM   1789  CA  SER A 231      41.716  17.131  14.593  1.00 12.88           C  
ANISOU 1789  CA  SER A 231     1324   1944   1628    -62    618    -27       C  
ATOM   1790  C   SER A 231      42.777  16.066  14.369  1.00 12.89           C  
ANISOU 1790  C   SER A 231     1293   2074   1531   -154    419   -251       C  
ATOM   1791  O   SER A 231      42.472  14.876  14.159  1.00 13.62           O  
ANISOU 1791  O   SER A 231     1410   2042   1721    -40    440   -360       O  
ATOM   1792  CB  SER A 231      41.496  18.061  13.372  1.00 14.23           C  
ANISOU 1792  CB  SER A 231     1594   2288   1526   -189    556     34       C  
ATOM   1793  OG  SER A 231      41.324  17.341  12.189  1.00 14.82           O  
ANISOU 1793  OG  SER A 231     1583   2298   1749   -149    458   -118       O  
ATOM   1794  N   THR A 232      44.053  16.468  14.398  1.00 12.81           N  
ANISOU 1794  N   THR A 232     1312   2203   1353   -134    436     47       N  
ATOM   1795  CA  THR A 232      45.151  15.511  14.238  1.00 13.06           C  
ANISOU 1795  CA  THR A 232     1271   2267   1422   -121    468   -206       C  
ATOM   1796  C   THR A 232      45.163  14.468  15.368  1.00 12.85           C  
ANISOU 1796  C   THR A 232     1246   2121   1517    -54    361   -198       C  
ATOM   1797  O   THR A 232      45.233  13.256  15.115  1.00 13.86           O  
ANISOU 1797  O   THR A 232     1348   2099   1818     54    518   -325       O  
ATOM   1798  CB  THR A 232      46.461  16.268  14.205  1.00 13.97           C  
ANISOU 1798  CB  THR A 232     1310   2342   1654   -161    490    -92       C  
ATOM   1799  OG1 THR A 232      46.461  17.144  13.073  1.00 15.62           O  
ANISOU 1799  OG1 THR A 232     1460   2708   1768   -243    617     41       O  
AT