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***  STRUCTURAL PROTEIN 03-JUN-07 2V26  ***

elNémo ID: 22021014344621848

Job options:

ID        	=	 22021014344621848
JOBID     	=	 STRUCTURAL PROTEIN 03-JUN-07 2V26
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    STRUCTURAL PROTEIN                      03-JUN-07   2V26              
TITLE     MYOSIN VI (MD) PRE-POWERSTROKE STATE (MG.ADP.VO4)                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOSIN VI;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: DOMAIN MOTOR, RESIDUES 5-377,379-789;                      
COMPND   5 SYNONYM: UNCONVENTIONAL MYOSIN VI;                                   
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    CALMODULIN-BINDING, NUCLEOTIDE-BINDING, MYOSIN, MEMBRANE,             
KEYWDS   2 VANADATE, MYOSIN VI, TRANSPORT, PRE- POWERSTROKE,                    
KEYWDS   3 TRANSITION STATE, PROTEIN TRANSPORT, ACTIN-BINDING, MOTOR            
KEYWDS   4 PROTEIN, NUCLEAR PROTEIN, ENDOCYTOSIS, ATP-BINDING, COILED           
KEYWDS   5 COIL, DOMAIN MOTOR, GOLGI APPARATUS, PHOSPHORYLATION,                
KEYWDS   6 MOLECULAR MOTOR, STRUCTURAL PROTEIN                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.MENETREY,P.LLINAS,M.MUKHERJEA,H.L.SWEENEY,A.HOUDUSSE                
REVDAT   2   24-FEB-09 2V26    1       VERSN                                    
REVDAT   1   20-NOV-07 2V26    0                                                
JRNL        AUTH   J.MENETREY,P.LLINAS,M.MUKHERJEA,H.L.SWEENEY,                 
JRNL        AUTH 2 A.HOUDUSSE                                                   
JRNL        TITL   THE STRUCTURAL BASIS FOR THE LARGE POWERSTROKE OF            
JRNL        TITL 2 MYOSIN VI.                                                   
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 131   300 2007              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   17956731                                                     
JRNL        DOI    10.1016/J.CELL.2007.08.027                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 68.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 81037                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 9071                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.79                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5939                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2600                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 643                          
REMARK   3   BIN FREE R VALUE                    : 0.3050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6058                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 71                                      
REMARK   3   SOLVENT ATOMS            : 536                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.20000                                             
REMARK   3    B22 (A**2) : 0.77000                                              
REMARK   3    B33 (A**2) : -0.57000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.128         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.118         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.122         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6252 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8429 ; 1.062 ; 1.968       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   760 ; 5.036 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   309 ;35.161 ;24.175       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1126 ;12.493 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    39 ;14.632 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   919 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4700 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3011 ; 0.186 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4323 ; 0.299 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.097 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    54 ; 0.145 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.068 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3872 ; 0.517 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6044 ; 0.832 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2669 ; 1.355 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2376 ; 2.113 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2V26 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  04-JUN-07.                 
REMARK 100 THE PDBE ID CODE IS EBI-32777.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0080                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 90108                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.75                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.0                                
REMARK 200  R MERGE                    (I) : 0.11                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 4.00                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.0                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.41                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.90                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 2BKH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.8                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):2.37                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3-4% PEG 8000, 50MM MES PH 6.75,         
REMARK 280   100MM SAM, 1MM TCEP                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       46.75600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.48800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.92250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.48800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       46.75600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.92250            
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 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU A    34                                                      
REMARK 465     ASN A    35                                                      
REMARK 465     GLN A    36                                                      
REMARK 465     LYS A    37                                                      
REMARK 465     THR A   174                                                      
REMARK 465     GLY A   175                                                      
REMARK 465     GLN A   176                                                      
REMARK 465     ASP A   177                                                      
REMARK 465     ILE A   178                                                      
REMARK 465     ASP A   179                                                      
REMARK 465     LEU A   396                                                      
REMARK 465     THR A   397                                                      
REMARK 465     THR A   398                                                      
REMARK 465     ALA A   399                                                      
REMARK 465     GLY A   400                                                      
REMARK 465     GLY A   401                                                      
REMARK 465     ALA A   402                                                      
REMARK 465     LYS A   403                                                      
REMARK 465     GLY A   404                                                      
REMARK 465     THR A   405                                                      
REMARK 465     VAL A   406                                                      
REMARK 465     GLU A   622                                                      
REMARK 465     SER A   623                                                      
REMARK 465     SER A   624                                                      
REMARK 465     THR A   625                                                      
REMARK 465     ASN A   626                                                      
REMARK 465     ASN A   627                                                      
REMARK 465     ASN A   628                                                      
REMARK 465     LYS A   629                                                      
REMARK 465     ASP A   630                                                      
REMARK 465     THR A   631                                                      
REMARK 465     LYS A   632                                                      
REMARK 465     GLN A   633                                                      
REMARK 465     LYS A   634                                                      
REMARK 465     ALA A   635                                                      
REMARK 465     GLY A   636                                                      
REMARK 465     LYS A   637                                                      
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 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    ALA A  91     -119.72     52.75                                   
REMARK 500    LYS A 105      -18.21     78.89                                   
REMARK 500    ASN A 244     -176.40    -69.52                                   
REMARK 500    SER A 467     -161.82   -122.29                                   
REMARK 500    LEU A 522      -48.35     69.99                                   
REMARK 500    ASP A 553       -4.66     76.92                                   
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 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             VO4 A1791   V                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A1789   O2B                                                    
REMARK 620 2 VO4 A1791   O2   85.4                                              
REMARK 620 3 VO4 A1791   O4   86.3 119.5                                        
REMARK 620 4 VO4 A1791   O1  178.6  95.8  93.7                                  
REMARK 620 5 VO4 A1791   O3   83.2 119.1 119.2  95.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1801  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 158   OG1                                                    
REMARK 620 2 SER A 204   OG   82.3                                              
REMARK 620 3 ADP A1789   O1B  91.3 172.1                                        
REMARK 620 4 VO4 A1791   O2  170.8  88.6  97.9                                  
REMARK 620 5 HOH A2527   O    86.5  82.9  92.2  93.4                            
REMARK 620 6 HOH A2314   O    84.5  87.6  96.3  94.1 167.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A1789                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 A1791                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1792                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1793                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1794                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1795                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1796                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1797                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1798                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1799                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1800                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2BKH   RELATED DB: PDB                                   
REMARK 900  MYOSIN VI NUCLEOTIDE-FREE (MD) CRYSTAL                              
REMARK 900  STRUCTURE                                                           
REMARK 900 RELATED ID: 2BKI   RELATED DB: PDB                                   
REMARK 900  MYOSIN VI NUCLEOTIDE-FREE (LONG.S1) CRYSTAL                         
REMARK 900   STRUCTURE.                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE AUTHORS STATE THAT THE ORIGINAL SEQUENCE (UNIPROT                
REMARK 999 Q29122) OF MYOSIN VI FROM PIG WAS MOST LIKELY                        
REMARK 999 INCORRECT BECAUSE THE CHANGES THAT ARE IN THEIR CLONE                
REMARK 999 (LYS DELETION AND THE 6 MUTATIONS) ARE CONSERVED ACROSS              
REMARK 999 THE MYOSIN VI FAMILY.                                                
DBREF  2V26 A    5   377  UNP    Q29122   MYO6_PIG         5    377             
DBREF  2V26 A  378   788  UNP    Q29122   MYO6_PIG       379    789             
SEQADV 2V26 VAL A  547  UNP  Q29122    GLY   548 CONFLICT                       
SEQADV 2V26 ARG A  572  UNP  Q29122    ALA   573 CONFLICT                       
SEQADV 2V26 ASP A  573  UNP  Q29122    TYR   574 CONFLICT                       
SEQADV 2V26 LEU A  714  UNP  Q29122    VAL   715 CONFLICT                       
SEQADV 2V26 TYR A  721  UNP  Q29122    SER   722 CONFLICT                       
SEQADV 2V26 MET A  722  UNP  Q29122    LEU   723 CONFLICT                       
SEQRES   1 A  784  LYS PRO VAL TRP ALA PRO HIS PRO THR ASP GLY PHE GLN          
SEQRES   2 A  784  VAL GLY ASN ILE VAL ASP ILE GLY PRO ASP SER LEU THR          
SEQRES   3 A  784  ILE GLU PRO LEU ASN GLN LYS GLY LYS THR PHE LEU ALA          
SEQRES   4 A  784  LEU ILE ASN GLN VAL PHE PRO ALA GLU GLU ASP SER LYS          
SEQRES   5 A  784  LYS ASP VAL GLU ASP ASN CYS SER LEU MET TYR LEU ASN          
SEQRES   6 A  784  GLU ALA THR LEU LEU HIS ASN ILE LYS VAL ARG TYR SER          
SEQRES   7 A  784  LYS ASP ARG ILE TYR THR TYR VAL ALA ASN ILE LEU ILE          
SEQRES   8 A  784  ALA VAL ASN PRO TYR PHE ASP ILE PRO LYS ILE TYR SER          
SEQRES   9 A  784  SER GLU THR ILE LYS SER TYR GLN GLY LYS SER LEU GLY          
SEQRES  10 A  784  THR MET PRO PRO HIS VAL PHE ALA ILE ALA ASP LYS ALA          
SEQRES  11 A  784  PHE ARG ASP MET LYS VAL LEU LYS LEU SER GLN SER ILE          
SEQRES  12 A  784  ILE VAL SER GLY GLU SER GLY ALA GLY LYS THR GLU ASN          
SEQRES  13 A  784  THR LYS PHE VAL LEU ARG TYR LEU THR GLU SER TYR GLY          
SEQRES  14 A  784  THR GLY GLN ASP ILE ASP ASP ARG ILE VAL GLU ALA ASN          
SEQRES  15 A  784  PRO LEU LEU GLU ALA PHE GLY ASN ALA LYS THR VAL ARG          
SEQRES  16 A  784  ASN ASN ASN SER SER ARG PHE GLY LYS PHE VAL GLU ILE          
SEQRES  17 A  784  HIS PHE ASN GLU LYS SER SER VAL VAL GLY GLY PHE VAL          
SEQRES  18 A  784  SER HIS TYR LEU LEU GLU LYS SER ARG ILE CYS VAL GLN          
SEQRES  19 A  784  GLY LYS GLU GLU ARG ASN TYR HIS ILE PHE TYR ARG LEU          
SEQRES  20 A  784  CYS ALA GLY ALA SER GLU ASP ILE ARG GLU ARG LEU HIS          
SEQRES  21 A  784  LEU SER SER PRO ASP ASN PHE ARG TYR LEU ASN ARG GLY          
SEQRES  22 A  784  CYS THR ARG TYR PHE ALA ASN LYS GLU THR ASP LYS GLN          
SEQRES  23 A  784  ILE LEU GLN ASN ARG LYS SER PRO GLU TYR LEU LYS ALA          
SEQRES  24 A  784  GLY SER LEU LYS ASP PRO LEU LEU ASP ASP HIS GLY ASP          
SEQRES  25 A  784  PHE ILE ARG MET CYS THR ALA MET LYS LYS ILE GLY LEU          
SEQRES  26 A  784  ASP ASP GLU GLU LYS LEU ASP LEU PHE ARG VAL VAL ALA          
SEQRES  27 A  784  GLY VAL LEU HIS LEU GLY ASN ILE ASP PHE GLU GLU ALA          
SEQRES  28 A  784  GLY SER THR SER GLY GLY CYS ASN LEU LYS ASN LYS SER          
SEQRES  29 A  784  THR GLN ALA LEU GLU TYR CYS ALA GLU LEU LEU GLY LEU          
SEQRES  30 A  784  ASP GLN ASP ASP LEU ARG VAL SER LEU THR THR ARG VAL          
SEQRES  31 A  784  MET LEU THR THR ALA GLY GLY ALA LYS GLY THR VAL ILE          
SEQRES  32 A  784  LYS VAL PRO LEU LYS VAL GLU GLN ALA ASN ASN ALA ARG          
SEQRES  33 A  784  ASP ALA LEU ALA LYS THR VAL TYR SER HIS LEU PHE ASP          
SEQRES  34 A  784  HIS VAL VAL ASN ARG VAL ASN GLN CYS PHE PRO PHE GLU          
SEQRES  35 A  784  THR SER SER TYR PHE ILE GLY VAL LEU ASP ILE ALA GLY          
SEQRES  36 A  784  PHE GLU TYR PHE GLU HIS ASN SER PHE GLU GLN PHE CYS          
SEQRES  37 A  784  ILE ASN TYR CYS ASN GLU LYS LEU GLN GLN PHE PHE ASN          
SEQRES  38 A  784  GLU ARG ILE LEU LYS GLU GLU GLN GLU LEU TYR GLN LYS          
SEQRES  39 A  784  GLU GLY LEU GLY VAL ASN GLU VAL HIS TYR VAL ASP ASN          
SEQRES  40 A  784  GLN ASP CYS ILE ASP LEU ILE GLU ALA ARG LEU VAL GLY          
SEQRES  41 A  784  ILE LEU ASP ILE LEU ASP GLU GLU ASN ARG LEU PRO GLN          
SEQRES  42 A  784  PRO SER ASP GLN HIS PHE THR SER ALA VAL HIS GLN LYS          
SEQRES  43 A  784  HIS LYS ASP HIS PHE ARG LEU SER ILE PRO ARG LYS SER          
SEQRES  44 A  784  LYS LEU ALA ILE HIS ARG ASN ILE ARG ASP ASP GLU GLY          
SEQRES  45 A  784  PHE ILE ILE ARG HIS PHE ALA GLY ALA VAL CYS TYR GLU          
SEQRES  46 A  784  THR THR GLN PHE VAL GLU LYS ASN ASN ASP ALA LEU HIS          
SEQRES  47 A  784  MET SER LEU GLU SER LEU ILE CYS GLU SER ARG ASP LYS          
SEQRES  48 A  784  PHE ILE ARG GLU LEU PHE GLU SER SER THR ASN ASN ASN          
SEQRES  49 A  784  LYS ASP THR LYS GLN LYS ALA GLY LYS LEU SER PHE ILE          
SEQRES  50 A  784  SER VAL GLY ASN LYS PHE LYS THR GLN LEU ASN LEU LEU          
SEQRES  51 A  784  LEU ASP LYS LEU ARG SER THR GLY ALA SER PHE ILE ARG          
SEQRES  52 A  784  CYS ILE LYS PRO ASN LEU LYS MET THR SER HIS HIS PHE          
SEQRES  53 A  784  GLU GLY ALA GLN ILE LEU SER GLN LEU GLN CYS SER GLY          
SEQRES  54 A  784  MET VAL SER VAL LEU ASP LEU MET GLN GLY GLY PHE PRO          
SEQRES  55 A  784  SER ARG ALA SER PHE HIS GLU LEU TYR ASN MET TYR LYS          
SEQRES  56 A  784  LYS TYR MET PRO ASP LYS LEU ALA ARG LEU ASP PRO ARG          
SEQRES  57 A  784  LEU PHE CYS LYS ALA LEU PHE LYS ALA LEU GLY LEU ASN          
SEQRES  58 A  784  GLU ILE ASP TYR LYS PHE GLY LEU THR LYS VAL PHE PHE          
SEQRES  59 A  784  ARG PRO GLY LYS PHE ALA GLU PHE ASP GLN ILE MET LYS          
SEQRES  60 A  784  SER ASP PRO ASP HIS LEU ALA GLU LEU VAL LYS ARG VAL          
SEQRES  61 A  784  ASN HIS TRP LEU                                              
HET    ADP  A1789      27                                                       
HET     MG  A1801       1                                                       
HET    VO4  A1791       5                                                       
HET    EDO  A1792       4                                                       
HET    EDO  A1793       4                                                       
HET    EDO  A1794       4                                                       
HET    EDO  A1795       4                                                       
HET    EDO  A1796       4                                                       
HET    EDO  A1797       4                                                       
HET    EDO  A1798       4                                                       
HET    SO4  A1799       5                                                       
HET    SO4  A1800       5                                                       
HETNAM     VO4 VANADATE ION                                                     
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  VO4    O4 V 3-                                                      
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   4  ADP    C10 H15 N5 O10 P2                                            
FORMUL   5  EDO    7(C2 H6 O2)                                                  
FORMUL   6   MG    MG 2+                                                        
FORMUL   7  HOH   *536(H2 O1)                                                   
HELIX    1   1 ASN A   46  VAL A   48  5                                   3    
HELIX    2   2 ASN A   62  LEU A   65  5                                   4    
HELIX    3   3 ASN A   69  LYS A   83  1                                  15    
HELIX    4   4 SER A  108  GLN A  116  1                                   9    
HELIX    5   5 HIS A  126  LYS A  142  1                                  17    
HELIX    6   6 GLY A  156  GLY A  173  1                                  18    
HELIX    7   7 ASP A  180  ALA A  185  1                                   6    
HELIX    8   8 ALA A  185  GLY A  193  1                                   9    
HELIX    9   9 LYS A  232  CYS A  236  5                                   5    
HELIX   10  10 TYR A  245  ALA A  255  1                                  11    
HELIX   11  11 SER A  256  LEU A  263  1                                   8    
HELIX   12  12 SER A  267  ASN A  270  5                                   4    
HELIX   13  13 PHE A  271  ARG A  276  1                                   6    
HELIX   14  14 ASN A  284  LYS A  289  1                                   6    
HELIX   15  15 LEU A  292  LYS A  296  5                                   5    
HELIX   16  16 SER A  297  GLY A  304  1                                   8    
HELIX   17  17 ASP A  312  GLY A  328  1                                  17    
HELIX   18  18 ASP A  330  ASN A  349  1                                  20    
HELIX   19  19 SER A  368  GLY A  380  1                                  13    
HELIX   20  20 ASP A  382  THR A  391  1                                  10    
HELIX   21  21 LYS A  412  GLN A  441  1                                  30    
HELIX   22  22 SER A  467  LEU A  489  1                                  23    
HELIX   23  23 LYS A  490  GLU A  499  1                                  10    
HELIX   24  24 ASN A  511  ALA A  520  1                                  10    
HELIX   25  25 GLY A  524  LEU A  535  1                                  12    
HELIX   26  26 SER A  539  HIS A  551  1                                  13    
HELIX   27  27 ILE A  559  SER A  563  5                                   5    
HELIX   28  28 LEU A  565  ARG A  569  5                                   5    
HELIX   29  29 GLN A  592  ASN A  597  1                                   6    
HELIX   30  30 HIS A  602  GLU A  611  1                                  10    
HELIX   31  31 ASP A  614  PHE A  621  1                                   8    
HELIX   32  32 SER A  642  SER A  660  1                                  19    
HELIX   33  33 GLU A  681  SER A  692  1                                  12    
HELIX   34  34 GLY A  693  GLN A  702  1                                  10    
HELIX   35  35 PHE A  711  LYS A  719  1                                   9    
HELIX   36  36 LYS A  720  MET A  722  5                                   3    
HELIX   37  37 PRO A  723  ARG A  728  1                                   6    
HELIX   38  38 ASP A  730  LEU A  742  1                                  13    
HELIX   39  39 ASN A  745  ILE A  747  5                                   3    
HELIX   40  40 LYS A  762  LYS A  771  1                                  10    
HELIX   41  41 ASP A  773  LEU A  788  1                                  16    
SHEET    1  AA 5 PHE A  41  LEU A  44  0                                        
SHEET    2  AA 5 SER A  28  GLU A  32 -1  O  LEU A  29   N  ALA A  43           
SHEET    3  AA 5 GLY A  15  ILE A  24 -1  O  ASN A  20   N  GLU A  32           
SHEET    4  AA 5 VAL A   7  HIS A  11 -1  O  VAL A   7   N  GLY A  19           
SHEET    5  AA 5 PHE A  49  PRO A  50 -1  O  PHE A  49   N  TRP A   8           
SHEET    1  AB 7 TYR A  87  VAL A  90  0                                        
SHEET    2  AB 7 ILE A  93  VAL A  97 -1  O  ILE A  93   N  VAL A  90           
SHEET    3  AB 7 GLY A 662  ILE A 669  1  O  PHE A 665   N  LEU A  94           
SHEET    4  AB 7 GLN A 145  SER A 150  1  O  SER A 146   N  SER A 664           
SHEET    5  AB 7 TYR A 450  ASP A 456  1  O  PHE A 451   N  GLN A 145           
SHEET    6  AB 7 GLY A 207  PHE A 214 -1  O  LYS A 208   N  ASP A 456           
SHEET    7  AB 7 VAL A 220  TYR A 228 -1  N  VAL A 221   O  HIS A 213           
SHEET    1  AC 2 ASN A 194  ALA A 195  0                                        
SHEET    2  AC 2 SER A 203  SER A 204 -1  O  SER A 203   N  ALA A 195           
SHEET    1  AD 2 PHE A 352  GLU A 354  0                                        
SHEET    2  AD 2 CYS A 362  LEU A 364 -1  O  ASN A 363   N  GLU A 353           
SHEET    1  AE 2 THR A 392  VAL A 394  0                                        
SHEET    2  AE 2 LYS A 408  PRO A 410 -1  O  VAL A 409   N  ARG A 393           
SHEET    1  AF 3 LEU A 557  SER A 558  0                                        
SHEET    2  AF 3 GLY A 576  HIS A 581 -1  O  ILE A 578   N  SER A 558           
SHEET    3  AF 3 GLY A 584  GLU A 589 -1  O  GLY A 584   N  HIS A 581           
SHEET    1  AG 3 SER A 707  SER A 710  0                                        
SHEET    2  AG 3 LYS A 755  PHE A 758 -1  O  VAL A 756   N  ALA A 709           
SHEET    3  AG 3 TYR A 749  PHE A 751 -1  O  LYS A 750   N  PHE A 757           
LINK         O2  VO4 A1791                MG    MG A1801     1555   1555  1.79  
LINK         V   VO4 A1791                 O2B ADP A1789     1555   1555  2.16  
LINK        MG    MG A1801                 O   HOH A2527     1555   1555  2.16  
LINK        MG    MG A1801                 OG  SER A 204     1555   1555  2.22  
LINK        MG    MG A1801                 O1B ADP A1789     1555   1555  2.06  
LINK        MG    MG A1801                 O   HOH A2314     1555   1555  2.15  
LINK        MG    MG A1801                 OG1 THR A 158     1555   1555  2.10  
SITE     1 AC1 23 ASN A  98  PRO A  99  TYR A 100  PHE A 101                    
SITE     2 AC1 23 ASP A 102  TYR A 107  GLY A 154  ALA A 155                    
SITE     3 AC1 23 GLY A 156  LYS A 157  THR A 158  GLU A 159                    
SITE     4 AC1 23 PHE A 163  ASN A 200  LEU A 310  VO4 A1791                    
SITE     5 AC1 23  MG A1801  HOH A2524  HOH A2525  HOH A2526                    
SITE     6 AC1 23 HOH A2527  HOH A2528  HOH A2529                               
SITE     1 AC2  6 THR A 158  SER A 204  ADP A1789  VO4 A1791                    
SITE     2 AC2  6 HOH A2314  HOH A2527                                          
SITE     1 AC3 13 SER A 153  GLY A 154  LYS A 157  ASN A 200                    
SITE     2 AC3 13 SER A 203  SER A 204  ALA A 458  GLY A 459                    
SITE     3 AC3 13 ADP A1789   MG A1801  HOH A2314  HOH A2315                    
SITE     4 AC3 13 HOH A2527                                                     
SITE     1 AC4  5 HIS A 227  TYR A 228  LEU A 229  GLN A 650                    
SITE     2 AC4  5 HOH A2530                                                     
SITE     1 AC5  5 PHE A 206  GLY A 207  ALA A 458  CYS A 476                    
SITE     2 AC5  5 EDO A1798                                                     
SITE     1 AC6  7 GLU A 152  ARG A 199  GLU A 461  TYR A 462                    
SITE     2 AC6  7 LYS A 670  LEU A 673  HOH A2531                               
SITE     1 AC7  6 ASP A  84  ARG A  85  ILE A  86  TYR A  87                    
SITE     2 AC7  6 ILE A 106  HOH A2134                                          
SITE     1 AC8  6 TRP A   8  HIS A  75  LYS A  78  HOH A2017                    
SITE     2 AC8  6 HOH A2532  HOH A2533                                          
SITE     1 AC9  7 TYR A 462  ASN A 466  LEU A 565  HIS A 568                    
SITE     2 AC9  7 ALA A 585  VAL A 586  CYS A 587                               
SITE     1 BC1  8 ARG A 205  PHE A 206  LEU A 229  GLU A 231                    
SITE     2 BC1  8 ILE A 473  PHE A 647  EDO A1793  HOH A2534                    
SITE     1 BC2  6 LYS A  83  ARG A  85  SER A 256  GLU A 257                    
SITE     2 BC2  6 HOH A2535  HOH A2536                                          
SITE     1 BC3  2 ARG A 521  LYS A 782                                          
CRYST1   93.512   93.845  100.976  90.00  90.00  90.00 P 21 21 21    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      0.010694  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010656  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009903        0.00000                         
ATOM      1  N   LYS A   5      -6.475  16.224 -21.125  1.00 26.13           N  
ATOM      2  CA  LYS A   5      -6.945  15.269 -20.078  1.00 25.92           C  
ATOM      3  C   LYS A   5      -6.415  15.653 -18.698  1.00 25.29           C  
ATOM      4  O   LYS A   5      -5.228  15.955 -18.555  1.00 25.58           O  
ATOM      5  CB  LYS A   5      -6.501  13.842 -20.406  1.00 26.15           C  
ATOM      6  CG  LYS A   5      -7.213  13.201 -21.587  1.00 27.88           C  
ATOM      7  CD  LYS A   5      -6.597  11.845 -21.899  1.00 29.78           C  
ATOM      8  CE  LYS A   5      -7.081  11.296 -23.235  1.00 31.92           C  
ATOM      9  NZ  LYS A   5      -6.637  12.128 -24.398  1.00 33.33           N  
ATOM     10  N   PRO A   6      -7.289  15.626 -17.674  1.00 24.53           N  
ATOM     11  CA  PRO A   6      -6.833  15.878 -16.300  1.00 23.55           C  
ATOM     12  C   PRO A   6      -5.754  14.892 -15.838  1.00 22.34           C  
ATOM     13  O   PRO A   6      -5.743  13.733 -16.257  1.00 22.18           O  
ATOM     14  CB  PRO A   6      -8.109  15.715 -15.460  1.00 23.76           C  
ATOM     15  CG  PRO A   6      -9.073  14.980 -16.331  1.00 24.45           C  
ATOM     16  CD  PRO A   6      -8.741  15.378 -17.734  1.00 24.58           C  
ATOM     17  N   VAL A   7      -4.850  15.369 -14.985  1.00 20.79           N  
ATOM     18  CA  VAL A   7      -3.759  14.554 -14.445  1.00 19.11           C  
ATOM     19  C   VAL A   7      -3.702  14.723 -12.923  1.00 18.13           C  
ATOM     20  O   VAL A   7      -4.357  15.612 -12.375  1.00 17.81           O  
ATOM     21  CB  VAL A   7      -2.387  14.945 -15.054  1.00 19.30           C  
ATOM     22  CG1 VAL A   7      -2.314  14.567 -16.538  1.00 19.20           C  
ATOM     23  CG2 VAL A   7      -2.107  16.443 -14.857  1.00 18.38           C  
ATOM     24  N   TRP A   8      -2.934  13.862 -12.256  1.00 17.07           N  
ATOM     25  CA  TRP A   8      -2.675  13.992 -10.817  1.00 15.87           C  
ATOM     26  C   TRP A   8      -1.305  14.612 -10.579  1.00 15.69           C  
ATOM     27  O   TRP A   8      -0.301  14.125 -11.101  1.00 15.74           O  
ATOM     28  CB  TRP A   8      -2.712  12.625 -10.124  1.00 15.24           C  
ATOM     29  CG  TRP A   8      -4.059  11.994 -10.060  1.00 14.36           C  
ATOM     30  CD1 TRP A   8      -4.476  10.875 -10.731  1.00 14.14           C  
ATOM     31  CD2 TRP A   8      -5.168  12.422  -9.266  1.00 13.43           C  
ATOM     32  NE1 TRP A   8      -5.778  10.592 -10.411  1.00 13.65           N  
ATOM     33  CE2 TRP A   8      -6.233  11.530  -9.521  1.00 13.48           C  
ATOM     34  CE3 TRP A   8      -5.372  13.486  -8.375  1.00 14.20           C  
ATOM     35  CZ2 TRP A   8      -7.483  11.661  -8.909  1.00 14.00           C  
ATOM     36  CZ3 TRP A   8      -6.616  13.616  -7.763  1.00 13.99           C  
ATOM     37  CH2 TRP A   8      -7.655  12.706  -8.034  1.00 14.60           C  
ATOM     38  N   ALA A   9      -1.267  15.676  -9.780  1.00 15.27           N  
ATOM     39  CA  ALA A   9      -0.014  16.307  -9.382  1.00 15.22           C  
ATOM     40  C   ALA A   9       0.019  16.470  -7.858  1.00 15.05           C  
ATOM     41  O   ALA A   9      -1.037  16.471  -7.228  1.00 14.80           O  
ATOM     42  CB  ALA A   9       0.147  17.658 -10.082  1.00 15.11           C  
ATOM     43  N   PRO A  10       1.225  16.600  -7.267  1.00 15.09           N  
ATOM     44  CA  PRO A  10       1.363  16.645  -5.802  1.00 15.41           C  
ATOM     45  C   PRO A  10       0.531  17.727  -5.116  1.00 15.54           C  
ATOM     46  O   PRO A  10       0.382  18.840  -5.638  1.00 15.72           O  
ATOM     47  CB  PRO A  10       2.851  16.941  -5.595  1.00 15.63           C  
ATOM     48  CG  PRO A  10       3.514  16.437  -6.823  1.00 15.82           C  
ATOM     49  CD  PRO A  10       2.538  16.702  -7.934  1.00 15.01           C  
ATOM     50  N   HIS A  11       0.000  17.379  -3.948  1.00 15.33           N  
ATOM     51  CA  HIS A  11      -0.663  18.315  -3.056  1.00 15.46           C  
ATOM     52  C   HIS A  11      -0.175  17.965  -1.652  1.00 15.47           C  
ATOM     53  O   HIS A  11      -0.129  16.782  -1.293  1.00 15.35           O  
ATOM     54  CB  HIS A  11      -2.183  18.183  -3.159  1.00 15.57           C  
ATOM     55  CG  HIS A  11      -2.933  19.221  -2.385  1.00 16.18           C  
ATOM     56  ND1 HIS A  11      -3.116  19.145  -1.021  1.00 16.25           N  
ATOM     57  CD2 HIS A  11      -3.547  20.360  -2.783  1.00 16.96           C  
ATOM     58  CE1 HIS A  11      -3.811  20.190  -0.612  1.00 17.69           C  
ATOM     59  NE2 HIS A  11      -4.087  20.944  -1.661  1.00 17.52           N  
ATOM     60  N   PRO A  12       0.202  18.984  -0.855  1.00 15.72           N  
ATOM     61  CA  PRO A  12       0.894  18.704   0.411  1.00 15.92           C  
ATOM     62  C   PRO A  12       0.050  18.038   1.500  1.00 16.17           C  
ATOM     63  O   PRO A  12       0.611  17.401   2.393  1.00 16.47           O  
ATOM     64  CB  PRO A  12       1.378  20.087   0.864  1.00 16.06           C  
ATOM     65  CG  PRO A  12       0.448  21.048   0.229  1.00 16.17           C  
ATOM     66  CD  PRO A  12       0.025  20.434  -1.079  1.00 15.80           C  
ATOM     67  N   THR A  13      -1.271  18.177   1.440  1.00 15.98           N  
ATOM     68  CA  THR A  13      -2.128  17.547   2.449  1.00 16.36           C  
ATOM     69  C   THR A  13      -3.051  16.476   1.875  1.00 15.73           C  
ATOM     70  O   THR A  13      -3.452  15.554   2.590  1.00 15.49           O  
ATOM     71  CB  THR A  13      -2.943  18.581   3.267  1.00 16.81           C  
ATOM     72  OG1 THR A  13      -3.810  19.308   2.396  1.00 18.30           O  
ATOM     73  CG2 THR A  13      -2.014  19.557   3.992  1.00 17.59           C  
ATOM     74  N   ASP A  14      -3.387  16.605   0.594  1.00 15.01           N  
ATOM     75  CA  ASP A  14      -4.218  15.615  -0.095  1.00 14.78           C  
ATOM     76  C   ASP A  14      -3.401  14.510  -0.766  1.00 13.97           C  
ATOM     77  O   ASP A  14      -3.961  13.515  -1.234  1.00 13.88           O  
ATOM     78  CB  ASP A  14      -5.122  16.297  -1.128  1.00 15.39           C  
ATOM     79  CG  ASP A  14      -6.188  17.167  -0.489  1.00 17.14           C  
ATOM     80  OD1 ASP A  14      -6.612  18.142  -1.138  1.00 18.36           O  
ATOM     81  OD2 ASP A  14      -6.598  16.881   0.658  1.00 18.58           O  
ATOM     82  N   GLY A  15      -2.084  14.690  -0.813  1.00 13.43           N  
ATOM     83  CA  GLY A  15      -1.190  13.753  -1.487  1.00 13.12           C  
ATOM     84  C   GLY A  15      -1.094  14.104  -2.960  1.00 12.98           C  
ATOM     85  O   GLY A  15      -0.009  14.427  -3.463  1.00 12.85           O  
ATOM     86  N   PHE A  16      -2.239  14.043  -3.637  1.00 12.93           N  
ATOM     87  CA  PHE A  16      -2.368  14.468  -5.032  1.00 13.50           C  
ATOM     88  C   PHE A  16      -3.615  15.320  -5.243  1.00 13.94           C  
ATOM     89  O   PHE A  16      -4.589  15.204  -4.499  1.00 13.57           O  
ATOM     90  CB  PHE A  16      -2.405  13.258  -5.975  1.00 13.32           C  
ATOM     91  CG  PHE A  16      -1.109  12.507  -6.044  1.00 13.39           C  
ATOM     92  CD1 PHE A  16      -0.913  11.362  -5.278  1.00 13.57           C  
ATOM     93  CD2 PHE A  16      -0.075  12.944  -6.875  1.00 12.67           C  
ATOM     94  CE1 PHE A  16       0.286  10.659  -5.342  1.00 12.95           C  
ATOM     95  CE2 PHE A  16       1.131  12.253  -6.940  1.00 12.53           C  
ATOM     96  CZ  PHE A  16       1.316  11.105  -6.171  1.00 13.66           C  
ATOM     97  N   GLN A  17      -3.573  16.170  -6.271  1.00 14.50           N  
ATOM     98  CA  GLN A  17      -4.721  16.976  -6.684  1.00 15.71           C  
ATOM     99  C   GLN A  17      -4.924  16.885  -8.199  1.00 16.25           C  
ATOM    100  O   GLN A  17      -3.970  16.624  -8.931  1.00 16.32           O  
ATOM    101  CB  GLN A  17      -4.538  18.443  -6.266  1.00 15.47           C  
ATOM    102  CG  GLN A  17      -3.283  19.121  -6.827  1.00 15.93           C  
ATOM    103  CD  GLN A  17      -3.135  20.555  -6.344  1.00 16.00           C  
ATOM    104  OE1 GLN A  17      -4.055  21.365  -6.486  1.00 16.97           O  
ATOM    105  NE2 GLN A  17      -1.980  20.871  -5.762  1.00 16.04           N  
ATOM    106  N   VAL A  18      -6.162  17.108  -8.647  1.00 17.68           N  
ATOM    107  CA  VAL A  18      -6.517  17.100 -10.074  1.00 19.15           C  
ATOM    108  C   VAL A  18      -6.112  18.418 -10.717  1.00 19.38           C  
ATOM    109  O   VAL A  18      -6.315  19.491 -10.142  1.00 19.84           O  
ATOM    110  CB  VAL A  18      -8.053  16.946 -10.315  1.00 19.19           C  
ATOM    111  CG1 VAL A  18      -8.357  16.845 -11.814  1.00 19.84           C  
ATOM    112  CG2 VAL A  18      -8.609  15.746  -9.599  1.00 20.24           C  
ATOM    113  N   GLY A  19      -5.553  18.329 -11.918  1.00 20.11           N  
ATOM    114  CA  GLY A  19      -5.234  19.519 -12.699  1.00 20.97           C  
ATOM    115  C   GLY A  19      -5.059  19.222 -14.172  1.00 21.42           C  
ATOM    116  O   GLY A  19      -5.189  18.076 -14.603  1.00 21.25           O  
ATOM    117  N   ASN A  20      -4.774  20.270 -14.940  1.00 21.96           N  
ATOM    118  CA  ASN A  20      -4.419  20.137 -16.345  1.00 22.69           C  
ATOM    119  C   ASN A  20      -3.003  20.648 -16.581  1.00 22.73           C  
ATOM    120  O   ASN A  20      -2.592  21.647 -15.986  1.00 22.93           O  
ATOM    121  CB  ASN A  20      -5.407  20.907 -17.227  1.00 22.92           C  
ATOM    122  CG  ASN A  20      -6.789  20.281 -17.242  1.00 23.88           C  
ATOM    123  OD1 ASN A  20      -7.691  20.739 -16.548  1.00 26.59           O  
ATOM    124  ND2 ASN A  20      -6.957  19.226 -18.027  1.00 25.52           N  
ATOM    125  N   ILE A  21      -2.254  19.960 -17.438  1.00 23.11           N  
ATOM    126  CA  ILE A  21      -0.927  20.438 -17.823  1.00 23.28           C  
ATOM    127  C   ILE A  21      -1.109  21.546 -18.852  1.00 23.62           C  
ATOM    128  O   ILE A  21      -1.686  21.324 -19.920  1.00 23.81           O  
ATOM    129  CB  ILE A  21      -0.018  19.323 -18.402  1.00 23.34           C  
ATOM    130  CG1 ILE A  21       0.068  18.127 -17.444  1.00 23.23           C  
ATOM    131  CG2 ILE A  21       1.377  19.884 -18.679  1.00 23.20           C  
ATOM    132  CD1 ILE A  21       0.513  16.824 -18.104  1.00 23.17           C  
ATOM    133  N   VAL A  22      -0.639  22.741 -18.518  1.00 23.86           N  
ATOM    134  CA  VAL A  22      -0.793  23.885 -19.415  1.00 24.23           C  
ATOM    135  C   VAL A  22       0.522  24.264 -20.102  1.00 24.55           C  
ATOM    136  O   VAL A  22       0.512  24.915 -21.155  1.00 24.68           O  
ATOM    137  CB  VAL A  22      -1.453  25.109 -18.712  1.00 24.20           C  
ATOM    138  CG1 VAL A  22      -2.880  24.767 -18.279  1.00 24.62           C  
ATOM    139  CG2 VAL A  22      -0.621  25.591 -17.526  1.00 24.14           C  
ATOM    140  N   ASP A  23       1.641  23.843 -19.513  1.00 24.68           N  
ATOM    141  CA  ASP A  23       2.966  24.147 -20.054  1.00 24.85           C  
ATOM    142  C   ASP A  23       4.035  23.144 -19.613  1.00 24.80           C  
ATOM    143  O   ASP A  23       3.843  22.379 -18.665  1.00 24.57           O  
ATOM    144  CB  ASP A  23       3.386  25.568 -19.667  1.00 25.07           C  
ATOM    145  CG  ASP A  23       4.334  26.199 -20.677  1.00 26.01           C  
ATOM    146  OD1 ASP A  23       4.865  27.287 -20.372  1.00 27.16           O  
ATOM    147  OD2 ASP A  23       4.549  25.618 -21.764  1.00 26.40           O  
ATOM    148  N   ILE A  24       5.165  23.165 -20.315  1.00 24.63           N  
ATOM    149  CA  ILE A  24       6.283  22.270 -20.038  1.00 24.56           C  
ATOM    150  C   ILE A  24       7.609  23.040 -20.039  1.00 24.94           C  
ATOM    151  O   ILE A  24       7.827  23.930 -20.867  1.00 24.80           O  
ATOM    152  CB  ILE A  24       6.299  21.059 -21.035  1.00 24.49           C  
ATOM    153  CG1 ILE A  24       7.414  20.059 -20.693  1.00 24.26           C  
ATOM    154  CG2 ILE A  24       6.383  21.529 -22.497  1.00 24.18           C  
ATOM    155  CD1 ILE A  24       7.290  18.720 -21.415  1.00 23.97           C  
ATOM    156  N   GLY A  25       8.471  22.705 -19.084  1.00 25.27           N  
ATOM    157  CA  GLY A  25       9.803  23.296 -18.976  1.00 25.96           C  
ATOM    158  C   GLY A  25      10.854  22.211 -18.819  1.00 26.38           C  
ATOM    159  O   GLY A  25      10.512  21.027 -18.759  1.00 26.34           O  
ATOM    160  N   PRO A  26      12.142  22.601 -18.756  1.00 27.09           N  
ATOM    161  CA  PRO A  26      13.241  21.638 -18.628  1.00 27.73           C  
ATOM    162  C   PRO A  26      13.038  20.582 -17.536  1.00 28.59           C  
ATOM    163  O   PRO A  26      13.194  19.391 -17.808  1.00 28.96           O  
ATOM    164  CB  PRO A  26      14.447  22.529 -18.318  1.00 27.69           C  
ATOM    165  CG  PRO A  26      14.134  23.801 -19.011  1.00 27.25           C  
ATOM    166  CD  PRO A  26      12.647  23.986 -18.836  1.00 27.07           C  
ATOM    167  N   ASP A  27      12.677  20.998 -16.324  1.00 29.36           N  
ATOM    168  CA  ASP A  27      12.504  20.030 -15.237  1.00 30.12           C  
ATOM    169  C   ASP A  27      11.079  20.004 -14.670  1.00 29.87           C  
ATOM    170  O   ASP A  27      10.817  19.347 -13.659  1.00 30.23           O  
ATOM    171  CB  ASP A  27      13.540  20.267 -14.122  1.00 30.57           C  
ATOM    172  CG  ASP A  27      13.817  19.010 -13.291  1.00 31.94           C  
ATOM    173  OD1 ASP A  27      13.492  17.888 -13.752  1.00 33.75           O  
ATOM    174  OD2 ASP A  27      14.367  19.142 -12.173  1.00 33.69           O  
ATOM    175  N   SER A  28      10.154  20.695 -15.334  1.00 29.50           N  
ATOM    176  CA  SER A  28       8.818  20.866 -14.776  1.00 28.76           C  
ATOM    177  C   SER A  28       7.660  20.738 -15.763  1.00 28.24           C  
ATOM    178  O   SER A  28       7.825  20.872 -16.983  1.00 28.09           O  
ATOM    179  CB  SER A  28       8.721  22.209 -14.037  1.00 29.10           C  
ATOM    180  OG  SER A  28       8.651  23.297 -14.945  1.00 29.34           O  
ATOM    181  N   LEU A  29       6.489  20.449 -15.200  1.00 27.14           N  
ATOM    182  CA  LEU A  29       5.218  20.636 -15.871  1.00 26.36           C  
ATOM    183  C   LEU A  29       4.456  21.707 -15.103  1.00 26.16           C  
ATOM    184  O   LEU A  29       4.488  21.738 -13.868  1.00 26.13           O  
ATOM    185  CB  LEU A  29       4.411  19.335 -15.900  1.00 26.17           C  
ATOM    186  CG  LEU A  29       4.958  18.158 -16.714  1.00 25.79           C  
ATOM    187  CD1 LEU A  29       4.064  16.942 -16.547  1.00 25.48           C  
ATOM    188  CD2 LEU A  29       5.096  18.517 -18.189  1.00 25.19           C  
ATOM    189  N   THR A  30       3.786  22.592 -15.833  1.00 25.63           N  
ATOM    190  CA  THR A  30       2.955  23.608 -15.210  1.00 25.34           C  
ATOM    191  C   THR A  30       1.524  23.092 -15.140  1.00 25.03           C  
ATOM    192  O   THR A  30       0.927  22.726 -16.156  1.00 24.54           O  
ATOM    193  CB  THR A  30       3.038  24.960 -15.953  1.00 25.57           C  
ATOM    194  OG1 THR A  30       4.398  25.401 -15.976  1.00 25.43           O  
ATOM    195  CG2 THR A  30       2.208  26.012 -15.245  1.00 25.53           C  
ATOM    196  N   ILE A  31       1.000  23.041 -13.921  1.00 24.85           N  
ATOM    197  CA  ILE A  31      -0.312  22.469 -13.662  1.00 25.07           C  
ATOM    198  C   ILE A  31      -1.286  23.567 -13.262  1.00 25.37           C  
ATOM    199  O   ILE A  31      -0.988  24.384 -12.387  1.00 25.14           O  
ATOM    200  CB  ILE A  31      -0.264  21.383 -12.539  1.00 24.80           C  
ATOM    201  CG1 ILE A  31       0.850  20.353 -12.790  1.00 24.91           C  
ATOM    202  CG2 ILE A  31      -1.631  20.705 -12.366  1.00 24.59           C  
ATOM    203  CD1 ILE A  31       0.712  19.534 -14.077  1.00 24.24           C  
ATOM    204  N   GLU A  32      -2.434  23.587 -13.930  1.00 26.01           N  
ATOM    205  CA  GLU A  32      -3.552  24.424 -13.528  1.00 27.04           C  
ATOM    206  C   GLU A  32      -4.516  23.571 -12.701  1.00 27.12           C  
ATOM    207  O   GLU A  32      -5.106  22.626 -13.226  1.00 27.09           O  
ATOM    208  CB  GLU A  32      -4.257  25.002 -14.756  1.00 26.94           C  
ATOM    209  CG  GLU A  32      -5.375  25.984 -14.439  1.00 27.77           C  
ATOM    210  CD  GLU A  32      -6.095  26.459 -15.686  1.00 28.00           C  
ATOM    211  OE1 GLU A  32      -5.946  27.649 -16.036  1.00 30.33           O  
ATOM    212  OE2 GLU A  32      -6.800  25.645 -16.322  1.00 29.79           O  
ATOM    213  N   PRO A  33      -4.676  23.901 -11.403  1.00 27.57           N  
ATOM    214  CA  PRO A  33      -5.554  23.150 -10.499  1.00 27.85           C  
ATOM    215  C   PRO A  33      -7.003  23.104 -10.983  1.00 28.05           C  
ATOM    216  O   PRO A  33      -7.488  24.078 -11.568  1.00 28.45           O  
ATOM    217  CB  PRO A  33      -5.467  23.940  -9.188  1.00 27.82           C  
ATOM    218  CG  PRO A  33      -4.183  24.677  -9.269  1.00 28.06           C  
ATOM    219  CD  PRO A  33      -4.023  25.027 -10.712  1.00 27.72           C  
ATOM    220  N   GLY A  38      -6.510  30.045 -14.368  1.00 33.44           N  
ATOM    221  CA  GLY A  38      -5.511  31.109 -14.350  1.00 33.23           C  
ATOM    222  C   GLY A  38      -4.356  30.862 -13.397  1.00 33.16           C  
ATOM    223  O   GLY A  38      -3.251  31.370 -13.609  1.00 33.36           O  
ATOM    224  N   LYS A  39      -4.613  30.084 -12.346  1.00 32.83           N  
ATOM    225  CA  LYS A  39      -3.604  29.775 -11.330  1.00 32.35           C  
ATOM    226  C   LYS A  39      -2.742  28.599 -11.773  1.00 31.85           C  
ATOM    227  O   LYS A  39      -3.220  27.704 -12.474  1.00 31.98           O  
ATOM    228  CB  LYS A  39      -4.262  29.467  -9.979  1.00 32.53           C  
ATOM    229  CG  LYS A  39      -4.841  30.684  -9.252  1.00 32.98           C  
ATOM    230  CD  LYS A  39      -6.276  30.981  -9.679  1.00 33.93           C  
ATOM    231  CE  LYS A  39      -6.785  32.282  -9.072  1.00 34.23           C  
ATOM    232  NZ  LYS A  39      -6.060  33.472  -9.594  1.00 34.56           N  
ATOM    233  N   THR A  40      -1.474  28.611 -11.366  1.00 31.01           N  
ATOM    234  CA  THR A  40      -0.520  27.571 -11.751  1.00 30.11           C  
ATOM    235  C   THR A  40       0.441  27.201 -10.623  1.00 29.25           C  
ATOM    236  O   THR A  40       0.759  28.025  -9.759  1.00 29.04           O  
ATOM    237  CB  THR A  40       0.338  27.991 -12.977  1.00 30.30           C  
ATOM    238  OG1 THR A  40       1.064  29.190 -12.672  1.00 30.94           O  
ATOM    239  CG2 THR A  40      -0.521  28.206 -14.227  1.00 30.50           C  
ATOM    240  N   PHE A  41       0.898  25.953 -10.642  1.00 28.06           N  
ATOM    241  CA  PHE A  41       2.022  25.523  -9.818  1.00 26.93           C  
ATOM    242  C   PHE A  41       2.919  24.572 -10.611  1.00 26.43           C  
ATOM    243  O   PHE A  41       2.479  23.956 -11.587  1.00 26.12           O  
ATOM    244  CB  PHE A  41       1.556  24.901  -8.489  1.00 26.89           C  
ATOM    245  CG  PHE A  41       0.802  23.600  -8.638  1.00 26.31           C  
ATOM    246  CD1 PHE A  41       1.460  22.379  -8.490  1.00 25.86           C  
ATOM    247  CD2 PHE A  41      -0.568  23.595  -8.895  1.00 25.92           C  
ATOM    248  CE1 PHE A  41       0.771  21.174  -8.612  1.00 25.14           C  
ATOM    249  CE2 PHE A  41      -1.266  22.394  -9.021  1.00 25.65           C  
ATOM    250  CZ  PHE A  41      -0.593  21.181  -8.880  1.00 26.00           C  
ATOM    251  N   LEU A  42       4.177  24.472 -10.195  1.00 25.84           N  
ATOM    252  CA  LEU A  42       5.141  23.619 -10.881  1.00 25.44           C  
ATOM    253  C   LEU A  42       5.262  22.249 -10.221  1.00 25.12           C  
ATOM    254  O   LEU A  42       5.230  22.121  -8.994  1.00 24.89           O  
ATOM    255  CB  LEU A  42       6.514  24.298 -10.957  1.00 25.54           C  
ATOM    256  CG  LEU A  42       6.616  25.627 -11.719  1.00 25.68           C  
ATOM    257  CD1 LEU A  42       7.926  26.315 -11.392  1.00 26.57           C  
ATOM    258  CD2 LEU A  42       6.478  25.426 -13.224  1.00 26.28           C  
ATOM    259  N   ALA A  43       5.395  21.227 -11.058  1.00 24.69           N  
ATOM    260  CA  ALA A  43       5.624  19.870 -10.593  1.00 24.54           C  
ATOM    261  C   ALA A  43       6.701  19.224 -11.453  1.00 24.52           C  
ATOM    262  O   ALA A  43       6.839  19.554 -12.631  1.00 24.43           O  
ATOM    263  CB  ALA A  43       4.342  19.069 -10.659  1.00 24.40           C  
ATOM    264  N   LEU A  44       7.468  18.316 -10.859  1.00 24.40           N  
ATOM    265  CA  LEU A  44       8.425  17.518 -11.613  1.00 24.60           C  
ATOM    266  C   LEU A  44       7.676  16.579 -12.552  1.00 24.59           C  
ATOM    267  O   LEU A  44       6.605  16.073 -12.206  1.00 24.27           O  
ATOM    268  CB  LEU A  44       9.319  16.707 -10.668  1.00 24.86           C  
ATOM    269  CG  LEU A  44      10.252  17.473  -9.720  1.00 25.25           C  
ATOM    270  CD1 LEU A  44      10.934  16.511  -8.760  1.00 25.86           C  
ATOM    271  CD2 LEU A  44      11.293  18.291 -10.483  1.00 25.92           C  
ATOM    272  N   ILE A  45       8.240  16.352 -13.736  1.00 24.66           N  
ATOM    273  CA  ILE A  45       7.620  15.473 -14.727  1.00 24.99           C  
ATOM    274  C   ILE A  45       7.279  14.102 -14.125  1.00 24.87           C  
ATOM    275  O   ILE A  45       6.178  13.589 -14.337  1.00 24.84           O  
ATOM    276  CB  ILE A  45       8.476  15.357 -16.021  1.00 25.08           C  
ATOM    277  CG1 ILE A  45       8.582  16.726 -16.705  1.00 25.65           C  
ATOM    278  CG2 ILE A  45       7.873  14.339 -16.993  1.00 25.54           C  
ATOM    279  CD1 ILE A  45       9.744  16.856 -17.683  1.00 26.72           C  
ATOM    280  N   ASN A  46       8.196  13.540 -13.337  1.00 24.92           N  
ATOM    281  CA  ASN A  46       7.970  12.229 -12.713  1.00 25.08           C  
ATOM    282  C   ASN A  46       6.991  12.212 -11.523  1.00 24.79           C  
ATOM    283  O   ASN A  46       6.698  11.152 -10.968  1.00 25.12           O  
ATOM    284  CB  ASN A  46       9.304  11.544 -12.357  1.00 25.50           C  
ATOM    285  CG  ASN A  46      10.037  12.215 -11.199  1.00 26.44           C  
ATOM    286  OD1 ASN A  46       9.671  13.301 -10.745  1.00 28.03           O  
ATOM    287  ND2 ASN A  46      11.091  11.560 -10.718  1.00 28.30           N  
ATOM    288  N   GLN A  47       6.483  13.385 -11.147  1.00 24.23           N  
ATOM    289  CA  GLN A  47       5.527  13.501 -10.040  1.00 23.82           C  
ATOM    290  C   GLN A  47       4.094  13.712 -10.536  1.00 22.47           C  
ATOM    291  O   GLN A  47       3.172  13.908  -9.740  1.00 22.14           O  
ATOM    292  CB  GLN A  47       5.936  14.634  -9.094  1.00 23.95           C  
ATOM    293  CG  GLN A  47       7.210  14.365  -8.297  1.00 25.26           C  
ATOM    294  CD  GLN A  47       7.707  15.588  -7.538  1.00 25.70           C  
ATOM    295  OE1 GLN A  47       7.409  16.735  -7.897  1.00 29.09           O  
ATOM    296  NE2 GLN A  47       8.484  15.347  -6.488  1.00 28.31           N  
ATOM    297  N   VAL A  48       3.919  13.665 -11.855  1.00 21.38           N  
ATOM    298  CA  VAL A  48       2.615  13.853 -12.483  1.00 20.32           C  
ATOM    299  C   VAL A  48       2.151  12.541 -13.125  1.00 19.88           C  
ATOM    300  O   VAL A  48       2.887  11.926 -13.904  1.00 19.61           O  
ATOM    301  CB  VAL A  48       2.656  15.003 -13.526  1.00 20.50           C  
ATOM    302  CG1 VAL A  48       1.296  15.222 -14.155  1.00 20.09           C  
ATOM    303  CG2 VAL A  48       3.147  16.297 -12.876  1.00 20.31           C  
ATOM    304  N   PHE A  49       0.929  12.128 -12.791  1.00 19.02           N  
ATOM    305  CA  PHE A  49       0.397  10.828 -13.202  1.00 18.29           C  
ATOM    306  C   PHE A  49      -0.909  10.965 -13.980  1.00 18.10           C  
ATOM    307  O   PHE A  49      -1.693  11.878 -13.715  1.00 17.86           O  
ATOM    308  CB  PHE A  49       0.158   9.943 -11.966  1.00 18.18           C  
ATOM    309  CG  PHE A  49       1.403   9.637 -11.186  1.00 17.56           C  
ATOM    310  CD1 PHE A  49       1.789  10.442 -10.119  1.00 17.35           C  
ATOM    311  CD2 PHE A  49       2.194   8.538 -11.517  1.00 17.91           C  
ATOM    312  CE1 PHE A  49       2.941  10.165  -9.395  1.00 16.86           C  
ATOM    313  CE2 PHE A  49       3.349   8.249 -10.800  1.00 17.80           C  
ATOM    314  CZ  PHE A  49       3.725   9.064  -9.736  1.00 17.62           C  
ATOM    315  N   PRO A  50      -1.158  10.043 -14.932  1.00 17.88           N  
ATOM    316  CA  PRO A  50      -2.447  10.034 -15.616  1.00 17.91           C  
ATOM    317  C   PRO A  50      -3.551   9.680 -14.630  1.00 18.01           C  
ATOM    318  O   PRO A  50      -3.300   8.958 -13.657  1.00 17.81           O  
ATOM    319  CB  PRO A  50      -2.290   8.929 -16.666  1.00 17.69           C  
ATOM    320  CG  PRO A  50      -1.204   8.061 -16.154  1.00 18.15           C  
ATOM    321  CD  PRO A  50      -0.270   8.967 -15.410  1.00 17.74           C  
ATOM    322  N   ALA A  51      -4.745  10.208 -14.879  1.00 18.31           N  
ATOM    323  CA  ALA A  51      -5.900   9.984 -14.021  1.00 18.77           C  
ATOM    324  C   ALA A  51      -6.943   9.130 -14.735  1.00 19.24           C  
ATOM    325  O   ALA A  51      -6.987   9.096 -15.970  1.00 19.06           O  
ATOM    326  CB  ALA A  51      -6.503  11.315 -13.592  1.00 18.77           C  
ATOM    327  N   GLU A  52      -7.764   8.428 -13.955  1.00 19.60           N  
ATOM    328  CA  GLU A  52      -8.911   7.706 -14.498  1.00 20.35           C  
ATOM    329  C   GLU A  52      -9.909   8.706 -15.068  1.00 21.15           C  
ATOM    330  O   GLU A  52     -10.164   9.754 -14.467  1.00 20.84           O  
ATOM    331  CB  GLU A  52      -9.587   6.847 -13.423  1.00 20.20           C  
ATOM    332  CG  GLU A  52      -8.684   5.782 -12.800  1.00 20.10           C  
ATOM    333  CD  GLU A  52      -8.189   4.758 -13.803  1.00 19.29           C  
ATOM    334  OE1 GLU A  52      -9.016   3.974 -14.316  1.00 20.74           O  
ATOM    335  OE2 GLU A  52      -6.971   4.730 -14.069  1.00 19.44           O  
ATOM    336  N   GLU A  53     -10.466   8.371 -16.229  1.00 22.09           N  
ATOM    337  CA  GLU A  53     -11.370   9.268 -16.958  1.00 23.66           C  
ATOM    338  C   GLU A  53     -12.643   9.623 -16.182  1.00 23.46           C  
ATOM    339  O   GLU A  53     -13.131  10.757 -16.258  1.00 23.84           O  
ATOM    340  CB  GLU A  53     -11.707   8.667 -18.331  1.00 23.38           C  
ATOM    341  CG  GLU A  53     -10.510   8.625 -19.286  1.00 25.31           C  
ATOM    342  CD  GLU A  53     -10.716   7.718 -20.495  1.00 25.62           C  
ATOM    343  OE1 GLU A  53     -11.484   6.731 -20.406  1.00 28.40           O  
ATOM    344  OE2 GLU A  53     -10.091   7.991 -21.541  1.00 28.92           O  
ATOM    345  N   ASP A  54     -13.173   8.654 -15.441  1.00 23.62           N  
ATOM    346  CA  ASP A  54     -14.346   8.869 -14.598  1.00 23.72           C  
ATOM    347  C   ASP A  54     -13.868   9.020 -13.154  1.00 23.65           C  
ATOM    348  O   ASP A  54     -13.272   8.102 -12.581  1.00 23.64           O  
ATOM    349  CB  ASP A  54     -15.335   7.707 -14.753  1.00 24.00           C  
ATOM    350  CG  ASP A  54     -16.681   7.958 -14.066  1.00 24.97           C  
ATOM    351  OD1 ASP A  54     -16.751   8.708 -13.063  1.00 24.81           O  
ATOM    352  OD2 ASP A  54     -17.683   7.371 -14.531  1.00 26.37           O  
ATOM    353  N   SER A  55     -14.120  10.192 -12.584  1.00 23.15           N  
ATOM    354  CA  SER A  55     -13.605  10.537 -11.263  1.00 22.80           C  
ATOM    355  C   SER A  55     -14.550  10.133 -10.129  1.00 22.30           C  
ATOM    356  O   SER A  55     -14.165  10.181  -8.957  1.00 21.97           O  
ATOM    357  CB  SER A  55     -13.323  12.039 -11.188  1.00 22.83           C  
ATOM    358  OG  SER A  55     -14.533  12.778 -11.185  1.00 23.72           O  
ATOM    359  N   LYS A  56     -15.772   9.736 -10.486  1.00 21.82           N  
ATOM    360  CA  LYS A  56     -16.837   9.459  -9.511  1.00 21.72           C  
ATOM    361  C   LYS A  56     -17.085   7.968  -9.290  1.00 21.33           C  
ATOM    362  O   LYS A  56     -17.524   7.560  -8.207  1.00 20.99           O  
ATOM    363  CB  LYS A  56     -18.140  10.137  -9.941  1.00 21.93           C  
ATOM    364  CG  LYS A  56     -18.081  11.656  -9.928  1.00 23.24           C  
ATOM    365  CD  LYS A  56     -19.292  12.255 -10.623  1.00 26.12           C  
ATOM    366  CE  LYS A  56     -19.152  13.760 -10.772  1.00 27.58           C  
ATOM    367  NZ  LYS A  56     -20.246  14.319 -11.617  1.00 28.77           N  
ATOM    368  N   LYS A  57     -16.834   7.184 -10.339  1.00 21.02           N  
ATOM    369  CA  LYS A  57     -16.814   5.720 -10.301  1.00 20.60           C  
ATOM    370  C   LYS A  57     -15.709   5.226  -9.372  1.00 19.33           C  
ATOM    371  O   LYS A  57     -14.807   5.983  -9.010  1.00 19.11           O  
ATOM    372  CB  LYS A  57     -16.517   5.162 -11.706  1.00 20.91           C  
ATOM    373  CG  LYS A  57     -15.085   5.502 -12.212  1.00 22.43           C  
ATOM    374  CD  LYS A  57     -14.504   4.510 -13.231  1.00 22.29           C  
ATOM    375  CE  LYS A  57     -13.560   3.495 -12.581  1.00 24.96           C  
ATOM    376  NZ  LYS A  57     -12.134   3.955 -12.466  1.00 25.35           N  
ATOM    377  N   ASP A  58     -15.773   3.946  -9.022  1.00 17.63           N  
ATOM    378  CA  ASP A  58     -14.643   3.269  -8.395  1.00 16.32           C  
ATOM    379  C   ASP A  58     -14.554   1.823  -8.873  1.00 15.40           C  
ATOM    380  O   ASP A  58     -15.513   1.282  -9.438  1.00 14.98           O  
ATOM    381  CB  ASP A  58     -14.700   3.368  -6.858  1.00 16.45           C  
ATOM    382  CG  ASP A  58     -15.933   2.703  -6.258  1.00 17.36           C  
ATOM    383  OD1 ASP A  58     -16.800   3.433  -5.741  1.00 19.70           O  
ATOM    384  OD2 ASP A  58     -16.029   1.460  -6.280  1.00 17.86           O  
ATOM    385  N   VAL A  59     -13.390   1.217  -8.672  1.00 13.98           N  
ATOM    386  CA  VAL A  59     -13.201  -0.197  -8.974  1.00 13.39           C  
ATOM    387  C   VAL A  59     -12.904  -0.982  -7.702  1.00 13.10           C  
ATOM    388  O   VAL A  59     -12.237  -0.488  -6.787  1.00 12.76           O  
ATOM    389  CB  VAL A  59     -12.100  -0.441 -10.037  1.00 13.00           C  
ATOM    390  CG1 VAL A  59     -12.542   0.099 -11.401  1.00 13.89           C  
ATOM    391  CG2 VAL A  59     -10.758   0.172  -9.613  1.00 12.91           C  
ATOM    392  N   GLU A  60     -13.413  -2.205  -7.656  1.00 12.62           N  
ATOM    393  CA  GLU A  60     -13.237  -3.076  -6.498  1.00 12.84           C  
ATOM    394  C   GLU A  60     -11.812  -3.618  -6.381  1.00 12.58           C  
ATOM    395  O   GLU A  60     -11.326  -3.842  -5.273  1.00 12.74           O  
ATOM    396  CB  GLU A  60     -14.267  -4.208  -6.532  1.00 12.47           C  
ATOM    397  CG  GLU A  60     -15.701  -3.695  -6.334  1.00 12.65           C  
ATOM    398  CD  GLU A  60     -16.746  -4.789  -6.284  1.00 13.55           C  
ATOM    399  OE1 GLU A  60     -16.556  -5.838  -6.931  1.00 16.17           O  
ATOM    400  OE2 GLU A  60     -17.776  -4.588  -5.597  1.00 15.13           O  
ATOM    401  N   ASP A  61     -11.155  -3.817  -7.524  1.00 12.63           N  
ATOM    402  CA  ASP A  61      -9.759  -4.251  -7.571  1.00 12.77           C  
ATOM    403  C   ASP A  61      -8.943  -3.165  -8.255  1.00 12.94           C  
ATOM    404  O   ASP A  61      -9.211  -2.800  -9.411  1.00 12.43           O  
ATOM    405  CB  ASP A  61      -9.629  -5.589  -8.313  1.00 13.27           C  
ATOM    406  CG  ASP A  61      -8.180  -6.096  -8.411  1.00 13.58           C  
ATOM    407  OD1 ASP A  61      -7.259  -5.528  -7.779  1.00 13.00           O  
ATOM    408  OD2 ASP A  61      -7.961  -7.089  -9.143  1.00 16.71           O  
ATOM    409  N   ASN A  62      -7.954  -2.637  -7.541  1.00 12.44           N  
ATOM    410  CA  ASN A  62      -7.102  -1.589  -8.105  1.00 12.93           C  
ATOM    411  C   ASN A  62      -6.387  -2.026  -9.387  1.00 13.34           C  
ATOM    412  O   ASN A  62      -6.006  -1.192 -10.206  1.00 13.02           O  
ATOM    413  CB  ASN A  62      -6.122  -1.066  -7.056  1.00 12.84           C  
ATOM    414  CG  ASN A  62      -6.819  -0.264  -5.976  1.00 12.55           C  
ATOM    415  OD1 ASN A  62      -7.321   0.839  -6.230  1.00 11.49           O  
ATOM    416  ND2 ASN A  62      -6.865  -0.814  -4.764  1.00 12.50           N  
ATOM    417  N   CYS A  63      -6.239  -3.340  -9.569  1.00 13.75           N  
ATOM    418  CA  CYS A  63      -5.698  -3.894 -10.814  1.00 15.19           C  
ATOM    419  C   CYS A  63      -6.584  -3.616 -12.039  1.00 15.30           C  
ATOM    420  O   CYS A  63      -6.124  -3.760 -13.177  1.00 15.98           O  
ATOM    421  CB  CYS A  63      -5.444  -5.397 -10.672  1.00 15.44           C  
ATOM    422  SG  CYS A  63      -4.170  -5.807  -9.473  1.00 18.78           S  
ATOM    423  N   SER A  64      -7.833  -3.213 -11.795  1.00 15.28           N  
ATOM    424  CA  SER A  64      -8.807  -2.890 -12.851  1.00 15.75           C  
ATOM    425  C   SER A  64      -8.696  -1.452 -13.361  1.00 15.68           C  
ATOM    426  O   SER A  64      -9.351  -1.091 -14.347  1.00 15.94           O  
ATOM    427  CB  SER A  64     -10.237  -3.118 -12.361  1.00 15.52           C  
ATOM    428  OG  SER A  64     -10.489  -4.488 -12.117  1.00 17.39           O  
ATOM    429  N   LEU A  65      -7.893  -0.629 -12.685  1.00 15.51           N  
ATOM    430  CA  LEU A  65      -7.706   0.764 -13.101  1.00 15.54           C  
ATOM    431  C   LEU A  65      -7.062   0.814 -14.484  1.00 15.94           C  
ATOM    432  O   LEU A  65      -6.268  -0.059 -14.830  1.00 15.82           O  
ATOM    433  CB  LEU A  65      -6.834   1.529 -12.100  1.00 15.54           C  
ATOM    434  CG  LEU A  65      -7.359   1.790 -10.680  1.00 14.21           C  
ATOM    435  CD1 LEU A  65      -6.202   2.140  -9.753  1.00 14.45           C  
ATOM    436  CD2 LEU A  65      -8.434   2.875 -10.642  1.00 13.07           C  
ATOM    437  N   MET A  66      -7.412   1.826 -15.272  1.00 16.42           N  
ATOM    438  CA  MET A  66      -6.773   2.029 -16.573  1.00 17.53           C  
ATOM    439  C   MET A  66      -5.292   2.356 -16.396  1.00 16.70           C  
ATOM    440  O   MET A  66      -4.438   1.846 -17.124  1.00 16.58           O  
ATOM    441  CB  MET A  66      -7.472   3.140 -17.362  1.00 17.36           C  
ATOM    442  CG  MET A  66      -6.826   3.406 -18.713  1.00 19.31           C  
ATOM    443  SD  MET A  66      -7.654   4.689 -19.661  1.00 21.33           S  
ATOM    444  CE  MET A  66      -9.088   3.811 -20.279  1.00 21.79           C  
ATOM    445  N   TYR A  67      -5.000   3.206 -15.413  1.00 16.26           N  
ATOM    446  CA  TYR A  67      -3.632   3.560 -15.075  1.00 15.86           C  
ATOM    447  C   TYR A  67      -3.368   3.112 -13.653  1.00 15.53           C  
ATOM    448  O   TYR A  67      -4.087   3.511 -12.731  1.00 15.16           O  
ATOM    449  CB  TYR A  67      -3.416   5.068 -15.207  1.00 16.34           C  
ATOM    450  CG  TYR A  67      -3.889   5.624 -16.529  1.00 16.64           C  
ATOM    451  CD1 TYR A  67      -3.152   5.420 -17.693  1.00 17.81           C  
ATOM    452  CD2 TYR A  67      -5.080   6.351 -16.616  1.00 17.57           C  
ATOM    453  CE1 TYR A  67      -3.584   5.929 -18.916  1.00 18.06           C  
ATOM    454  CE2 TYR A  67      -5.520   6.865 -17.835  1.00 17.38           C  
ATOM    455  CZ  TYR A  67      -4.765   6.647 -18.978  1.00 17.59           C  
ATOM    456  OH  TYR A  67      -5.191   7.145 -20.189  1.00 18.50           O  
ATOM    457  N   LEU A  68      -2.363   2.255 -13.498  1.00 15.12           N  
ATOM    458  CA  LEU A  68      -1.947   1.764 -12.181  1.00 15.01           C  
ATOM    459  C   LEU A  68      -0.772   2.583 -11.669  1.00 14.36           C  
ATOM    460  O   LEU A  68       0.357   2.434 -12.140  1.00 14.43           O  
ATOM    461  CB  LEU A  68      -1.594   0.269 -12.233  1.00 14.96           C  
ATOM    462  CG  LEU A  68      -2.717  -0.766 -12.036  1.00 15.84           C  
ATOM    463  CD1 LEU A  68      -3.718  -0.744 -13.173  1.00 15.92           C  
ATOM    464  CD2 LEU A  68      -2.128  -2.157 -11.895  1.00 15.56           C  
ATOM    465  N   ASN A  69      -1.053   3.466 -10.711  1.00 13.81           N  
ATOM    466  CA  ASN A  69      -0.022   4.292 -10.084  1.00 13.29           C  
ATOM    467  C   ASN A  69      -0.484   4.767  -8.710  1.00 13.06           C  
ATOM    468  O   ASN A  69      -1.653   4.608  -8.363  1.00 12.86           O  
ATOM    469  CB  ASN A  69       0.375   5.477 -10.986  1.00 13.28           C  
ATOM    470  CG  ASN A  69      -0.767   6.450 -11.222  1.00 13.32           C  
ATOM    471  OD1 ASN A  69      -1.284   7.064 -10.284  1.00 12.34           O  
ATOM    472  ND2 ASN A  69      -1.155   6.610 -12.486  1.00 13.06           N  
ATOM    473  N   GLU A  70       0.424   5.351  -7.934  1.00 12.93           N  
ATOM    474  CA  GLU A  70       0.095   5.703  -6.547  1.00 13.36           C  
ATOM    475  C   GLU A  70      -1.047   6.716  -6.447  1.00 12.43           C  
ATOM    476  O   GLU A  70      -1.838   6.675  -5.500  1.00 12.31           O  
ATOM    477  CB  GLU A  70       1.336   6.173  -5.773  1.00 13.30           C  
ATOM    478  CG  GLU A  70       2.043   7.401  -6.340  1.00 14.59           C  
ATOM    479  CD  GLU A  70       3.260   7.810  -5.522  1.00 16.16           C  
ATOM    480  OE1 GLU A  70       3.898   8.820  -5.888  1.00 21.12           O  
ATOM    481  OE2 GLU A  70       3.582   7.131  -4.518  1.00 21.06           O  
ATOM    482  N   ALA A  71      -1.137   7.613  -7.429  1.00 11.65           N  
ATOM    483  CA  ALA A  71      -2.182   8.636  -7.441  1.00 11.17           C  
ATOM    484  C   ALA A  71      -3.572   8.054  -7.718  1.00 10.99           C  
ATOM    485  O   ALA A  71      -4.538   8.406  -7.048  1.00 10.71           O  
ATOM    486  CB  ALA A  71      -1.840   9.749  -8.429  1.00 11.38           C  
ATOM    487  N   THR A  72      -3.666   7.151  -8.693  1.00 10.67           N  
ATOM    488  CA  THR A  72      -4.951   6.525  -9.019  1.00 10.40           C  
ATOM    489  C   THR A  72      -5.375   5.558  -7.916  1.00 10.42           C  
ATOM    490  O   THR A  72      -6.562   5.431  -7.617  1.00 10.70           O  
ATOM    491  CB  THR A  72      -4.927   5.826 -10.394  1.00 10.49           C  
ATOM    492  OG1 THR A  72      -3.842   4.893 -10.442  1.00 10.26           O  
ATOM    493  CG2 THR A  72      -4.747   6.869 -11.509  1.00 11.00           C  
ATOM    494  N   LEU A  73      -4.391   4.898  -7.309  1.00 10.22           N  
ATOM    495  CA  LEU A  73      -4.616   4.025  -6.161  1.00 10.40           C  
ATOM    496  C   LEU A  73      -5.223   4.838  -5.019  1.00  9.95           C  
ATOM    497  O   LEU A  73      -6.248   4.460  -4.460  1.00  9.47           O  
ATOM    498  CB  LEU A  73      -3.292   3.391  -5.713  1.00 10.24           C  
ATOM    499  CG  LEU A  73      -3.287   2.571  -4.422  1.00 10.83           C  
ATOM    500  CD1 LEU A  73      -4.214   1.368  -4.550  1.00 12.17           C  
ATOM    501  CD2 LEU A  73      -1.865   2.126  -4.099  1.00 10.96           C  
ATOM    502  N   LEU A  74      -4.588   5.960  -4.693  1.00  9.99           N  
ATOM    503  CA  LEU A  74      -5.063   6.823  -3.619  1.00  9.91           C  
ATOM    504  C   LEU A  74      -6.489   7.297  -3.881  1.00  9.93           C  
ATOM    505  O   LEU A  74      -7.341   7.231  -2.999  1.00  9.98           O  
ATOM    506  CB  LEU A  74      -4.127   8.023  -3.446  1.00  9.72           C  
ATOM    507  CG  LEU A  74      -4.465   8.976  -2.297  1.00  9.58           C  
ATOM    508  CD1 LEU A  74      -4.298   8.303  -0.931  1.00 10.48           C  
ATOM    509  CD2 LEU A  74      -3.610  10.240  -2.394  1.00 10.23           C  
ATOM    510  N   HIS A  75      -6.748   7.751  -5.105  1.00  9.98           N  
ATOM    511  CA  HIS A  75      -8.058   8.283  -5.446  1.00 10.16           C  
ATOM    512  C   HIS A  75      -9.146   7.219  -5.380  1.00  9.77           C  
ATOM    513  O   HIS A  75     -10.237   7.483  -4.896  1.00  9.34           O  
ATOM    514  CB  HIS A  75      -8.047   8.922  -6.834  1.00 10.44           C  
ATOM    515  CG  HIS A  75      -9.385   9.441  -7.258  1.00 11.62           C  
ATOM    516  ND1 HIS A  75      -9.956  10.563  -6.699  1.00 13.24           N  
ATOM    517  CD2 HIS A  75     -10.270   8.985  -8.176  1.00 13.44           C  
ATOM    518  CE1 HIS A  75     -11.136  10.778  -7.255  1.00 14.09           C  
ATOM    519  NE2 HIS A  75     -11.349   9.835  -8.155  1.00 13.67           N  
ATOM    520  N   ASN A  76      -8.842   6.019  -5.866  1.00  9.66           N  
ATOM    521  CA  ASN A  76      -9.820   4.942  -5.889  1.00  9.93           C  
ATOM    522  C   ASN A  76     -10.237   4.569  -4.472  1.00  9.92           C  
ATOM    523  O   ASN A  76     -11.426   4.440  -4.181  1.00  9.48           O  
ATOM    524  CB  ASN A  76      -9.275   3.726  -6.639  1.00 10.29           C  
ATOM    525  CG  ASN A  76     -10.351   2.713  -6.948  1.00 10.62           C  
ATOM    526  OD1 ASN A  76     -11.338   3.030  -7.618  1.00 12.01           O  
ATOM    527  ND2 ASN A  76     -10.177   1.488  -6.451  1.00 10.79           N  
ATOM    528  N   ILE A  77      -9.242   4.414  -3.599  1.00 10.02           N  
ATOM    529  C   ILE A  77     -10.314   5.270  -1.551  1.00 10.37           C  
ATOM    530  O   ILE A  77     -11.215   5.007  -0.745  1.00  9.81           O  
ATOM    531  CA AILE A  77      -9.486   4.146  -2.183  0.50 10.32           C  
ATOM    532  CB AILE A  77      -8.149   3.912  -1.415  0.50 10.56           C  
ATOM    533  CG1AILE A  77      -7.527   2.581  -1.850  0.50 11.16           C  
ATOM    534  CG2AILE A  77      -8.364   3.929   0.097  0.50 11.31           C  
ATOM    535  CD1AILE A  77      -6.055   2.438  -1.502  0.50 12.07           C  
ATOM    537  CB BILE A  77      -8.099   4.017  -1.417  0.50 10.50           C  
ATOM    538  CG1BILE A  77      -7.288   2.834  -1.966  0.50 11.11           C  
ATOM    539  CG2BILE A  77      -8.294   3.914   0.097  0.50 11.30           C  
ATOM    540  CD1BILE A  77      -8.021   1.509  -1.986  0.50 11.11           C  
ATOM    541  N   LYS A  78     -10.025   6.514  -1.939  1.00 10.51           N  
ATOM    542  CA  LYS A  78     -10.724   7.691  -1.420  1.00 10.77           C  
ATOM    543  C   LYS A  78     -12.197   7.719  -1.822  1.00 10.59           C  
ATOM    544  O   LYS A  78     -13.074   7.996  -0.997  1.00 10.46           O  
ATOM    545  CB  LYS A  78     -10.020   8.975  -1.880  1.00 10.73           C  
ATOM    546  CG  LYS A  78     -10.563  10.253  -1.239  1.00 11.43           C  
ATOM    547  CD  LYS A  78      -9.704  11.461  -1.622  1.00 12.70           C  
ATOM    548  CE  LYS A  78     -10.185  12.730  -0.949  1.00 16.29           C  
ATOM    549  NZ  LYS A  78      -9.244  13.866  -1.197  1.00 18.23           N  
ATOM    550  N   VAL A  79     -12.460   7.437  -3.094  1.00 10.77           N  
ATOM    551  CA  VAL A  79     -13.825   7.431  -3.601  1.00 10.87           C  
ATOM    552  C   VAL A  79     -14.617   6.355  -2.872  1.00 10.51           C  
ATOM    553  O   VAL A  79     -15.713   6.609  -2.364  1.00 11.04           O  
ATOM    554  CB  VAL A  79     -13.862   7.216  -5.133  1.00 10.88           C  
ATOM    555  CG1 VAL A  79     -15.287   6.952  -5.596  1.00 11.22           C  
ATOM    556  CG2 VAL A  79     -13.299   8.430  -5.843  1.00 11.30           C  
ATOM    557  N   ARG A  80     -14.033   5.164  -2.784  1.00 10.24           N  
ATOM    558  CA  ARG A  80     -14.667   4.054  -2.087  1.00 10.06           C  
ATOM    559  C   ARG A  80     -14.963   4.402  -0.626  1.00  9.99           C  
ATOM    560  O   ARG A  80     -16.079   4.202  -0.154  1.00 10.09           O  
ATOM    561  CB  ARG A  80     -13.828   2.783  -2.223  1.00  9.61           C  
ATOM    562  CG  ARG A  80     -13.883   2.206  -3.642  1.00  9.75           C  
ATOM    563  CD  ARG A  80     -13.119   0.905  -3.801  1.00  9.86           C  
ATOM    564  NE  ARG A  80     -13.663  -0.188  -2.990  1.00 10.12           N  
ATOM    565  CZ  ARG A  80     -14.781  -0.864  -3.260  1.00 11.32           C  
ATOM    566  NH1 ARG A  80     -15.174  -1.842  -2.449  1.00  9.99           N  
ATOM    567  NH2 ARG A  80     -15.514  -0.570  -4.334  1.00 10.88           N  
ATOM    568  N   TYR A  81     -13.981   4.978   0.063  1.00 10.22           N  
ATOM    569  CA  TYR A  81     -14.159   5.391   1.456  1.00 10.59           C  
ATOM    570  C   TYR A  81     -15.327   6.369   1.631  1.00 10.91           C  
ATOM    571  O   TYR A  81     -16.055   6.296   2.618  1.00 11.19           O  
ATOM    572  CB  TYR A  81     -12.879   6.024   1.982  1.00 10.56           C  
ATOM    573  CG  TYR A  81     -12.810   6.171   3.487  1.00 10.69           C  
ATOM    574  CD1 TYR A  81     -12.698   5.046   4.308  1.00 11.84           C  
ATOM    575  CD2 TYR A  81     -12.823   7.436   4.087  1.00 11.17           C  
ATOM    576  CE1 TYR A  81     -12.618   5.167   5.693  1.00 11.66           C  
ATOM    577  CE2 TYR A  81     -12.734   7.569   5.477  1.00 10.79           C  
ATOM    578  CZ  TYR A  81     -12.629   6.430   6.269  1.00 10.86           C  
ATOM    579  OH  TYR A  81     -12.538   6.548   7.640  1.00 10.88           O  
ATOM    580  N   SER A  82     -15.504   7.268   0.664  1.00 11.57           N  
ATOM    581  CA  SER A  82     -16.575   8.272   0.715  1.00 12.22           C  
ATOM    582  C   SER A  82     -17.964   7.642   0.552  1.00 12.48           C  
ATOM    583  O   SER A  82     -18.978   8.249   0.924  1.00 12.99           O  
ATOM    584  CB  SER A  82     -16.358   9.357  -0.349  1.00 12.28           C  
ATOM    585  OG  SER A  82     -16.683   8.887  -1.650  1.00 12.75           O  
ATOM    586  N   LYS A  83     -17.993   6.435  -0.011  1.00 12.43           N  
ATOM    587  CA  LYS A  83     -19.216   5.648  -0.170  1.00 12.64           C  
ATOM    588  C   LYS A  83     -19.312   4.557   0.907  1.00 12.81           C  
ATOM    589  O   LYS A  83     -20.083   3.602   0.778  1.00 12.93           O  
ATOM    590  CB  LYS A  83     -19.259   5.014  -1.564  1.00 12.77           C  
ATOM    591  CG  LYS A  83     -19.168   6.003  -2.716  1.00 13.32           C  
ATOM    592  CD  LYS A  83     -18.963   5.278  -4.037  1.00 13.87           C  
ATOM    593  CE  LYS A  83     -18.890   6.251  -5.208  1.00 15.43           C  
ATOM    594  NZ  LYS A  83     -18.524   5.567  -6.477  1.00 15.26           N  
ATOM    595  N   ASP A  84     -18.523   4.711   1.970  1.00 12.62           N  
ATOM    596  CA  ASP A  84     -18.472   3.739   3.074  1.00 12.65           C  
ATOM    597  C   ASP A  84     -18.078   2.336   2.617  1.00 12.35           C  
ATOM    598  O   ASP A  84     -18.551   1.329   3.166  1.00 12.83           O  
ATOM    599  CB  ASP A  84     -19.794   3.716   3.862  1.00 13.12           C  
ATOM    600  CG  ASP A  84     -20.053   5.016   4.596  1.00 14.58           C  
ATOM    601  OD1 ASP A  84     -19.079   5.748   4.860  1.00 14.91           O  
ATOM    602  OD2 ASP A  84     -21.228   5.314   4.906  1.00 15.52           O  
ATOM    603  N   ARG A  85     -17.217   2.283   1.605  1.00 11.49           N  
ATOM    604  CA  ARG A  85     -16.609   1.031   1.168  1.00 11.21           C  
ATOM    605  C   ARG A  85     -15.168   1.046   1.635  1.00 10.96           C  
ATOM    606  O   ARG A  85     -14.296   1.626   0.983  1.00 11.08           O  
ATOM    607  CB  ARG A  85     -16.697   0.872  -0.349  1.00 11.46           C  
ATOM    608  CG  ARG A  85     -18.122   0.825  -0.840  1.00 11.92           C  
ATOM    609  CD  ARG A  85     -18.230   1.049  -2.338  1.00 13.22           C  
ATOM    610  NE  ARG A  85     -19.635   1.259  -2.687  1.00 14.93           N  
ATOM    611  CZ  ARG A  85     -20.076   1.667  -3.874  1.00 15.14           C  
ATOM    612  NH1 ARG A  85     -19.234   1.915  -4.873  1.00 13.65           N  
ATOM    613  NH2 ARG A  85     -21.380   1.829  -4.053  1.00 16.66           N  
ATOM    614  N   ILE A  86     -14.932   0.424   2.787  1.00 10.64           N  
ATOM    615  CA  ILE A  86     -13.623   0.476   3.428  1.00 10.26           C  
ATOM    616  C   ILE A  86     -12.627  -0.554   2.893  1.00  9.83           C  
ATOM    617  O   ILE A  86     -11.423  -0.434   3.148  1.00 10.10           O  
ATOM    618  CB  ILE A  86     -13.734   0.360   4.979  1.00  9.87           C  
ATOM    619  CG1 ILE A  86     -14.218  -1.032   5.410  1.00 11.07           C  
ATOM    620  CG2 ILE A  86     -14.630   1.483   5.532  1.00 10.71           C  
ATOM    621  CD1 ILE A  86     -14.087  -1.283   6.931  1.00 10.17           C  
ATOM    622  N   TYR A  87     -13.136  -1.557   2.171  1.00  9.14           N  
ATOM    623  CA  TYR A  87     -12.314  -2.637   1.626  1.00  8.88           C  
ATOM    624  C   TYR A  87     -12.134  -2.528   0.113  1.00  9.05           C  
ATOM    625  O   TYR A  87     -13.113  -2.350  -0.628  1.00  9.35           O  
ATOM    626  CB  TYR A  87     -12.931  -4.001   1.950  1.00  8.87           C  
ATOM    627  CG  TYR A  87     -13.122  -4.283   3.425  1.00  8.58           C  
ATOM    628  CD1 TYR A  87     -14.386  -4.565   3.941  1.00  9.77           C  
ATOM    629  CD2 TYR A  87     -12.039  -4.300   4.291  1.00  9.73           C  
ATOM    630  CE1 TYR A  87     -14.572  -4.842   5.294  1.00  9.70           C  
ATOM    631  CE2 TYR A  87     -12.207  -4.565   5.649  1.00  9.88           C  
ATOM    632  CZ  TYR A  87     -13.475  -4.838   6.144  1.00  9.67           C  
ATOM    633  OH  TYR A  87     -13.636  -5.103   7.486  1.00  8.64           O  
ATOM    634  N   THR A  88     -10.882  -2.654  -0.326  1.00  8.84           N  
ATOM    635  CA  THR A  88     -10.526  -2.654  -1.750  1.00  9.24           C  
ATOM    636  C   THR A  88      -9.353  -3.615  -1.973  1.00  9.39           C  
ATOM    637  O   THR A  88      -8.452  -3.707  -1.142  1.00  9.89           O  
ATOM    638  CB  THR A  88     -10.111  -1.239  -2.233  1.00  8.69           C  
ATOM    639  OG1 THR A  88     -11.011  -0.251  -1.717  1.00  9.11           O  
ATOM    640  CG2 THR A  88     -10.102  -1.151  -3.770  1.00  8.64           C  
ATOM    641  N   TYR A  89      -9.365  -4.325  -3.097  1.00 10.10           N  
ATOM    642  CA  TYR A  89      -8.287  -5.259  -3.419  1.00 10.56           C  
ATOM    643  C   TYR A  89      -7.139  -4.617  -4.191  1.00 10.89           C  
ATOM    644  O   TYR A  89      -7.322  -3.633  -4.909  1.00 11.55           O  
ATOM    645  CB  TYR A  89      -8.806  -6.419  -4.267  1.00 10.64           C  
ATOM    646  CG  TYR A  89      -9.784  -7.339  -3.581  1.00 10.86           C  
ATOM    647  CD1 TYR A  89     -11.050  -7.544  -4.111  1.00 11.01           C  
ATOM    648  CD2 TYR A  89      -9.435  -8.014  -2.408  1.00 11.02           C  
ATOM    649  CE1 TYR A  89     -11.959  -8.398  -3.493  1.00 11.40           C  
ATOM    650  CE2 TYR A  89     -10.329  -8.864  -1.778  1.00 11.69           C  
ATOM    651  CZ  TYR A  89     -11.591  -9.050  -2.327  1.00 11.30           C  
ATOM    652  OH  TYR A  89     -12.487  -9.883  -1.707  1.00 11.38           O  
ATOM    653  N   VAL A  90      -5.956  -5.193  -4.018  1.00 11.19           N  
ATOM    654  CA  VAL A  90      -4.925  -5.178  -5.045  1.00 11.60           C  
ATOM    655  C   VAL A  90      -4.697  -6.666  -5.296  1.00 11.80           C  
ATOM    656  O   VAL A  90      -3.985  -7.330  -4.538  1.00 11.83           O  
ATOM    657  CB  VAL A  90      -3.620  -4.487  -4.588  1.00 11.64           C  
ATOM    658  CG1 VAL A  90      -2.550  -4.580  -5.684  1.00 12.17           C  
ATOM    659  CG2 VAL A  90      -3.874  -3.025  -4.224  1.00 11.55           C  
ATOM    660  N   ALA A  91      -5.336  -7.186  -6.343  1.00 12.06           N  
ATOM    661  CA  ALA A  91      -5.417  -8.633  -6.591  1.00 12.30           C  
ATOM    662  C   ALA A  91      -5.944  -9.367  -5.352  1.00 12.60           C  
ATOM    663  O   ALA A  91      -7.058  -9.096  -4.913  1.00 12.93           O  
ATOM    664  CB  ALA A  91      -4.064  -9.205  -7.052  1.00 12.33           C  
ATOM    665  N   ASN A  92      -5.151 -10.283  -4.800  1.00 12.24           N  
ATOM    666  CA  ASN A  92      -5.553 -11.044  -3.605  1.00 12.47           C  
ATOM    667  C   ASN A  92      -5.111 -10.463  -2.254  1.00 11.97           C  
ATOM    668  O   ASN A  92      -5.246 -11.118  -1.211  1.00 11.70           O  
ATOM    669  CB  ASN A  92      -5.171 -12.536  -3.721  1.00 13.07           C  
ATOM    670  CG  ASN A  92      -3.699 -12.773  -4.075  1.00 15.40           C  
ATOM    671  OD1 ASN A  92      -3.258 -13.926  -4.131  1.00 20.50           O  
ATOM    672  ND2 ASN A  92      -2.946 -11.711  -4.319  1.00 16.09           N  
ATOM    673  N   ILE A  93      -4.601  -9.233  -2.275  1.00 11.07           N  
ATOM    674  CA  ILE A  93      -4.275  -8.516  -1.034  1.00 11.01           C  
ATOM    675  C   ILE A  93      -5.389  -7.510  -0.747  1.00 10.38           C  
ATOM    676  O   ILE A  93      -5.860  -6.839  -1.657  1.00 10.43           O  
ATOM    677  CB  ILE A  93      -2.904  -7.800  -1.130  1.00 10.90           C  
ATOM    678  CG1 ILE A  93      -1.781  -8.836  -1.320  1.00 12.33           C  
ATOM    679  CG2 ILE A  93      -2.656  -6.933   0.116  1.00 11.75           C  
ATOM    680  CD1 ILE A  93      -0.508  -8.267  -1.911  1.00 14.27           C  
ATOM    681  N   LEU A  94      -5.826  -7.428   0.509  1.00  9.99           N  
ATOM    682  CA  LEU A  94      -6.916  -6.528   0.879  1.00  9.74           C  
ATOM    683  C   LEU A  94      -6.415  -5.271   1.582  1.00  9.60           C  
ATOM    684  O   LEU A  94      -5.598  -5.347   2.502  1.00  9.41           O  
ATOM    685  CB  LEU A  94      -7.930  -7.241   1.781  1.00 10.07           C  
ATOM    686  CG  LEU A  94      -9.222  -6.497   2.139  1.00 11.41           C  
ATOM    687  CD1 LEU A  94     -10.132  -6.295   0.926  1.00 11.65           C  
ATOM    688  CD2 LEU A  94      -9.947  -7.265   3.215  1.00 12.53           C  
ATOM    689  N   ILE A  95      -6.933  -4.126   1.146  1.00  9.44           N  
ATOM    690  CA  ILE A  95      -6.715  -2.845   1.822  1.00  9.71           C  
ATOM    691  C   ILE A  95      -7.980  -2.477   2.594  1.00  9.58           C  
ATOM    692  O   ILE A  95      -9.078  -2.481   2.031  1.00  9.37           O  
ATOM    693  CB  ILE A  95      -6.355  -1.731   0.818  1.00 10.11           C  
ATOM    694  CG1 ILE A  95      -5.044  -2.080   0.097  1.00 10.43           C  
ATOM    695  CG2 ILE A  95      -6.273  -0.366   1.514  1.00  9.39           C  
ATOM    696  CD1 ILE A  95      -4.668  -1.119  -1.030  1.00 10.49           C  
ATOM    697  N   ALA A  96      -7.815  -2.178   3.881  1.00  9.12           N  
ATOM    698  CA  ALA A  96      -8.938  -1.817   4.757  1.00  9.15           C  
ATOM    699  C   ALA A  96      -8.711  -0.470   5.439  1.00  9.21           C  
ATOM    700  O   ALA A  96      -7.808  -0.340   6.273  1.00  9.33           O  
ATOM    701  CB  ALA A  96      -9.147  -2.903   5.817  1.00  8.97           C  
ATOM    702  N   VAL A  97      -9.525   0.527   5.102  1.00  9.22           N  
ATOM    703  CA  VAL A  97      -9.383   1.847   5.711  1.00  9.65           C  
ATOM    704  C   VAL A  97     -10.368   1.996   6.871  1.00  9.29           C  
ATOM    705  O   VAL A  97     -11.582   1.902   6.682  1.00  9.60           O  
ATOM    706  CB  VAL A  97      -9.600   2.993   4.697  1.00  9.86           C  
ATOM    707  CG1 VAL A  97      -9.278   4.326   5.345  1.00 10.09           C  
ATOM    708  CG2 VAL A  97      -8.740   2.790   3.448  1.00  9.86           C  
ATOM    709  N   ASN A  98      -9.836   2.224   8.069  1.00  9.21           N  
ATOM    710  CA  ASN A  98     -10.653   2.351   9.275  1.00  9.60           C  
ATOM    711  C   ASN A  98     -11.759   3.401   9.087  1.00  9.99           C  
ATOM    712  O   ASN A  98     -11.452   4.561   8.817  1.00  9.67           O  
ATOM    713  CB  ASN A  98      -9.744   2.736  10.447  1.00  9.14           C  
ATOM    714  CG  ASN A  98     -10.436   2.658  11.795  1.00 10.11           C  
ATOM    715  OD1 ASN A  98     -11.659   2.582  11.888  1.00  9.05           O  
ATOM    716  ND2 ASN A  98      -9.641   2.684  12.856  1.00  9.50           N  
ATOM    717  N   PRO A  99     -13.046   2.990   9.197  1.00 10.40           N  
ATOM    718  CA  PRO A  99     -14.166   3.946   9.074  1.00 10.72           C  
ATOM    719  C   PRO A  99     -14.401   4.827  10.308  1.00 10.85           C  
ATOM    720  O   PRO A  99     -15.027   5.891  10.193  1.00 10.83           O  
ATOM    721  CB  PRO A  99     -15.376   3.034   8.860  1.00 10.48           C  
ATOM    722  CG  PRO A  99     -15.025   1.775   9.592  1.00 11.18           C  
ATOM    723  CD  PRO A  99     -13.525   1.606   9.407  1.00 10.70           C  
ATOM    724  N   TYR A 100     -13.921   4.374  11.469  1.00 11.02           N  
ATOM    725  CA  TYR A 100     -14.143   5.051  12.762  1.00 11.34           C  
ATOM    726  C   TYR A 100     -15.631   5.266  13.114  1.00 12.04           C  
ATOM    727  O   TYR A 100     -15.984   6.153  13.919  1.00 12.10           O  
ATOM    728  CB  TYR A 100     -13.342   6.357  12.857  1.00 11.36           C  
ATOM    729  CG  TYR A 100     -11.900   6.171  13.298  1.00 11.22           C  
ATOM    730  CD1 TYR A 100     -10.843   6.615  12.501  1.00 11.00           C  
ATOM    731  CD2 TYR A 100     -11.596   5.551  14.515  1.00 10.88           C  
ATOM    732  CE1 TYR A 100      -9.511   6.462  12.910  1.00 10.26           C  
ATOM    733  CE2 TYR A 100     -10.269   5.384  14.932  1.00 10.84           C  
ATOM    734  CZ  TYR A 100      -9.238   5.837  14.123  1.00 10.84           C  
ATOM    735  OH  TYR A 100      -7.937   5.681  14.530  1.00 11.05           O  
ATOM    736  N   PHE A 101     -16.483   4.446  12.501  1.00 12.68           N  
ATOM    737  CA  PHE A 101     -17.886   4.292  12.896  1.00 13.61           C  
ATOM    738  C   PHE A 101     -18.424   2.947  12.415  1.00 13.99           C  
ATOM    739  O   PHE A 101     -17.822   2.298  11.553  1.00 13.62           O  
ATOM    740  CB  PHE A 101     -18.753   5.462  12.397  1.00 13.56           C  
ATOM    741  CG  PHE A 101     -19.210   5.335  10.964  1.00 14.08           C  
ATOM    742  CD1 PHE A 101     -20.519   4.965  10.675  1.00 14.39           C  
ATOM    743  CD2 PHE A 101     -18.340   5.605   9.909  1.00 13.70           C  
ATOM    744  CE1 PHE A 101     -20.958   4.860   9.356  1.00 14.12           C  
ATOM    745  CE2 PHE A 101     -18.767   5.495   8.589  1.00 14.49           C  
ATOM    746  CZ  PHE A 101     -20.077   5.122   8.313  1.00 14.14           C  
ATOM    747  N   ASP A 102     -19.552   2.526  12.981  1.00 15.00           N  
ATOM    748  CA  ASP A 102     -20.155   1.253  12.613  1.00 16.04           C  
ATOM    749  C   ASP A 102     -21.006   1.387  11.358  1.00 16.32           C  
ATOM    750  O   ASP A 102     -22.069   2.027  11.370  1.00 16.25           O  
ATOM    751  CB  ASP A 102     -20.972   0.678  13.776  1.00 16.48           C  
ATOM    752  CG  ASP A 102     -20.098   0.196  14.919  1.00 18.59           C  
ATOM    753  OD1 ASP A 102     -20.370   0.574  16.083  1.00 21.64           O  
ATOM    754  OD2 ASP A 102     -19.128  -0.547  14.654  1.00 19.95           O  
ATOM    755  N   ILE A 103     -20.512   0.803  10.269  1.00 16.60           N  
ATOM    756  CA  ILE A 103     -21.230   0.789   8.999  1.00 16.97           C  
ATOM    757  C   ILE A 103     -22.312  -0.281   9.088  1.00 17.46           C  
ATOM    758  O   ILE A 103     -22.007  -1.447   9.345  1.00 17.19           O  
ATOM    759  CB  ILE A 103     -20.283   0.516   7.803  1.00 16.81           C  
ATOM    760  CG1 ILE A 103     -19.219   1.614   7.702  1.00 16.41           C  
ATOM    761  CG2 ILE A 103     -21.076   0.418   6.488  1.00 16.74           C  
ATOM    762  CD1 ILE A 103     -18.094   1.307   6.720  1.00 16.73           C  
ATOM    763  N   PRO A 104     -23.585   0.114   8.882  1.00 18.14           N  
ATOM    764  CA  PRO A 104     -24.690  -0.825   9.097  1.00 18.73           C  
ATOM    765  C   PRO A 104     -24.583  -2.068   8.223  1.00 18.93           C  
ATOM    766  O   PRO A 104     -24.219  -1.968   7.047  1.00 19.22           O  
ATOM    767  CB  PRO A 104     -25.929  -0.011   8.695  1.00 18.89           C  
ATOM    768  CG  PRO A 104     -25.522   1.407   8.838  1.00 18.96           C  
ATOM    769  CD  PRO A 104     -24.070   1.438   8.447  1.00 18.34           C  
ATOM    770  N   LYS A 105     -24.866  -3.227   8.818  1.00 19.22           N  
ATOM    771  CA  LYS A 105     -25.157  -4.469   8.085  1.00 19.43           C  
ATOM    772  C   LYS A 105     -23.956  -5.241   7.522  1.00 18.75           C  
ATOM    773  O   LYS A 105     -24.087  -6.428   7.212  1.00 18.49           O  
ATOM    774  CB  LYS A 105     -26.172  -4.219   6.950  1.00 19.98           C  
ATOM    775  CG  LYS A 105     -27.513  -3.635   7.383  1.00 22.64           C  
ATOM    776  CD  LYS A 105     -28.250  -3.071   6.177  1.00 26.04           C  
ATOM    777  CE  LYS A 105     -29.558  -2.404   6.569  1.00 27.60           C  
ATOM    778  NZ  LYS A 105     -30.422  -2.190   5.371  1.00 29.68           N  
ATOM    779  N   ILE A 106     -22.796  -4.594   7.394  1.00 18.11           N  
ATOM    780  CA  ILE A 106     -21.701  -5.196   6.614  1.00 17.38           C  
ATOM    781  C   ILE A 106     -21.014  -6.396   7.280  1.00 16.87           C  
ATOM    782  O   ILE A 106     -20.237  -7.098   6.629  1.00 16.62           O  
ATOM    783  CB  ILE A 106     -20.649  -4.157   6.104  1.00 17.64           C  
ATOM    784  CG1 ILE A 106     -19.867  -3.528   7.262  1.00 17.30           C  
ATOM    785  CG2 ILE A 106     -21.315  -3.100   5.209  1.00 17.95           C  
ATOM    786  CD1 ILE A 106     -18.587  -2.792   6.825  1.00 17.25           C  
ATOM    787  N   TYR A 107     -21.306  -6.627   8.562  1.00 16.13           N  
ATOM    788  CA  TYR A 107     -20.789  -7.800   9.275  1.00 15.88           C  
ATOM    789  C   TYR A 107     -21.905  -8.716   9.777  1.00 16.07           C  
ATOM    790  O   TYR A 107     -21.674  -9.569  10.631  1.00 16.25           O  
ATOM    791  CB  TYR A 107     -19.868  -7.379  10.431  1.00 15.59           C  
ATOM    792  CG  TYR A 107     -18.756  -6.454   9.993  1.00 14.85           C  
ATOM    793  CD1 TYR A 107     -18.750  -5.113  10.376  1.00 15.54           C  
ATOM    794  CD2 TYR A 107     -17.723  -6.911   9.173  1.00 14.44           C  
ATOM    795  CE1 TYR A 107     -17.735  -4.250   9.970  1.00 15.20           C  
ATOM    796  CE2 TYR A 107     -16.701  -6.052   8.753  1.00 13.90           C  
ATOM    797  CZ  TYR A 107     -16.716  -4.726   9.157  1.00 14.61           C  
ATOM    798  OH  TYR A 107     -15.717  -3.863   8.752  1.00 14.93           O  
ATOM    799  N   SER A 108     -23.107  -8.548   9.223  1.00 16.25           N  
ATOM    800  CA  SER A 108     -24.271  -9.343   9.631  1.00 16.67           C  
ATOM    801  C   SER A 108     -24.116 -10.827   9.291  1.00 16.95           C  
ATOM    802  O   SER A 108     -23.306 -11.198   8.436  1.00 16.37           O  
ATOM    803  CB  SER A 108     -25.535  -8.805   8.963  1.00 16.70           C  
ATOM    804  OG  SER A 108     -25.518  -9.080   7.574  1.00 17.54           O  
ATOM    805  N   SER A 109     -24.914 -11.663   9.952  1.00 17.24           N  
ATOM    806  CA  SER A 109     -24.963 -13.094   9.658  1.00 17.94           C  
ATOM    807  C   SER A 109     -25.389 -13.361   8.209  1.00 17.99           C  
ATOM    808  O   SER A 109     -24.925 -14.322   7.595  1.00 18.12           O  
ATOM    809  CB  SER A 109     -25.903 -13.818  10.632  1.00 18.07           C  
ATOM    810  OG  SER A 109     -25.310 -13.948  11.913  1.00 19.59           O  
ATOM    811  N   GLU A 110     -26.265 -12.507   7.676  1.00 18.49           N  
ATOM    812  CA  GLU A 110     -26.679 -12.576   6.269  1.00 19.34           C  
ATOM    813  C   GLU A 110     -25.490 -12.350   5.334  1.00 18.15           C  
ATOM    814  O   GLU A 110     -25.307 -13.078   4.354  1.00 18.36           O  
ATOM    815  CB  GLU A 110     -27.780 -11.552   5.974  1.00 19.65           C  
ATOM    816  CG  GLU A 110     -28.318 -11.603   4.548  1.00 21.64           C  
ATOM    817  CD  GLU A 110     -29.508 -10.683   4.307  1.00 22.24           C  
ATOM    818  OE1 GLU A 110     -30.309 -10.996   3.397  1.00 26.17           O  
ATOM    819  OE2 GLU A 110     -29.645  -9.651   5.009  1.00 26.70           O  
ATOM    820  N   THR A 111     -24.693 -11.332   5.646  1.00 17.01           N  
ATOM    821  CA  THR A 111     -23.493 -11.014   4.876  1.00 15.96           C  
ATOM    822  C   THR A 111     -22.488 -12.168   4.942  1.00 15.34           C  
ATOM    823  O   THR A 111     -21.948 -12.586   3.916  1.00 14.95           O  
ATOM    824  CB  THR A 111     -22.867  -9.680   5.345  1.00 15.98           C  
ATOM    825  OG1 THR A 111     -23.855  -8.643   5.263  1.00 16.14           O  
ATOM    826  CG2 THR A 111     -21.670  -9.302   4.473  1.00 15.25           C  
ATOM    827  N   ILE A 112     -22.271 -12.700   6.145  1.00 14.94           N  
ATOM    828  CA  ILE A 112     -21.400 -13.864   6.335  1.00 14.55           C  
ATOM    829  C   ILE A 112     -21.803 -15.011   5.401  1.00 14.88           C  
ATOM    830  O   ILE A 112     -20.969 -15.557   4.680  1.00 14.67           O  
ATOM    831  CB  ILE A 112     -21.385 -14.347   7.819  1.00 14.40           C  
ATOM    832  CG1 ILE A 112     -20.648 -13.333   8.702  1.00 13.96           C  
ATOM    833  CG2 ILE A 112     -20.736 -15.722   7.932  1.00 14.04           C  
ATOM    834  CD1 ILE A 112     -20.603 -13.690  10.196  1.00 14.22           C  
ATOM    835  N   LYS A 113     -23.089 -15.356   5.403  1.00 15.53           N  
ATOM    836  CA  LYS A 113     -23.597 -16.433   4.552  1.00 16.12           C  
ATOM    837  C   LYS A 113     -23.316 -16.178   3.070  1.00 15.78           C  
ATOM    838  O   LYS A 113     -22.947 -17.100   2.343  1.00 16.17           O  
ATOM    839  CB  LYS A 113     -25.095 -16.660   4.793  1.00 16.44           C  
ATOM    840  CG  LYS A 113     -25.384 -17.298   6.144  1.00 19.41           C  
ATOM    841  CD  LYS A 113     -26.811 -17.830   6.240  1.00 22.99           C  
ATOM    842  CE  LYS A 113     -27.189 -18.125   7.687  1.00 25.51           C  
ATOM    843  NZ  LYS A 113     -27.550 -16.882   8.430  1.00 28.22           N  
ATOM    844  N   SER A 114     -23.451 -14.920   2.654  1.00 15.70           N  
ATOM    845  CA  SER A 114     -23.307 -14.522   1.249  1.00 15.59           C  
ATOM    846  C   SER A 114     -21.881 -14.642   0.701  1.00 15.19           C  
ATOM    847  O   SER A 114     -21.689 -14.654  -0.519  1.00 15.23           O  
ATOM    848  CB  SER A 114     -23.840 -13.102   1.029  1.00 15.79           C  
ATOM    849  OG  SER A 114     -22.946 -12.120   1.531  1.00 17.04           O  
ATOM    850  N   TYR A 115     -20.891 -14.704   1.596  1.00 14.42           N  
ATOM    851  CA  TYR A 115     -19.486 -14.853   1.194  1.00 14.32           C  
ATOM    852  C   TYR A 115     -19.003 -16.303   1.133  1.00 14.40           C  
ATOM    853  O   TYR A 115     -17.919 -16.582   0.614  1.00 14.41           O  
ATOM    854  CB  TYR A 115     -18.563 -13.992   2.085  1.00 13.81           C  
ATOM    855  CG  TYR A 115     -18.509 -12.563   1.606  1.00 13.12           C  
ATOM    856  CD1 TYR A 115     -17.526 -12.148   0.702  1.00 12.62           C  
ATOM    857  CD2 TYR A 115     -19.467 -11.636   2.015  1.00 11.87           C  
ATOM    858  CE1 TYR A 115     -17.492 -10.835   0.234  1.00 11.79           C  
ATOM    859  CE2 TYR A 115     -19.450 -10.326   1.549  1.00 12.29           C  
ATOM    860  CZ  TYR A 115     -18.465  -9.933   0.658  1.00 12.14           C  
ATOM    861  OH  TYR A 115     -18.452  -8.640   0.200  1.00 13.62           O  
ATOM    862  N   GLN A 116     -19.805 -17.230   1.651  1.00 14.55           N  
ATOM    863  CA  GLN A 116     -19.370 -18.629   1.749  1.00 15.14           C  
ATOM    864  C   GLN A 116     -19.194 -19.301   0.382  1.00 15.08           C  
ATOM    865  O   GLN A 116     -20.124 -19.347  -0.427  1.00 15.06           O  
ATOM    866  CB  GLN A 116     -20.314 -19.427   2.654  1.00 15.13           C  
ATOM    867  CG  GLN A 116     -20.262 -18.974   4.108  1.00 15.70           C  
ATOM    868  CD  GLN A 116     -21.389 -19.525   4.972  1.00 16.47           C  
ATOM    869  OE1 GLN A 116     -21.486 -19.194   6.157  1.00 18.26           O  
ATOM    870  NE2 GLN A 116     -22.245 -20.356   4.387  1.00 16.60           N  
ATOM    871  N   GLY A 117     -17.983 -19.789   0.130  1.00 14.99           N  
ATOM    872  CA  GLY A 117     -17.649 -20.482  -1.116  1.00 15.16           C  
ATOM    873  C   GLY A 117     -17.517 -19.605  -2.351  1.00 15.33           C  
ATOM    874  O   GLY A 117     -17.410 -20.122  -3.469  1.00 15.84           O  
ATOM    875  N   LYS A 118     -17.510 -18.285  -2.167  1.00 14.78           N  
ATOM    876  CA  LYS A 118     -17.405 -17.362  -3.304  1.00 14.83           C  
ATOM    877  C   LYS A 118     -15.955 -17.020  -3.608  1.00 14.46           C  
ATOM    878  O   LYS A 118     -15.210 -16.592  -2.725  1.00 14.45           O  
ATOM    879  CB  LYS A 118     -18.203 -16.075  -3.055  1.00 14.83           C  
ATOM    880  CG  LYS A 118     -19.650 -16.290  -2.649  1.00 16.54           C  
ATOM    881  CD  LYS A 118     -20.520 -16.748  -3.812  1.00 18.75           C  
ATOM    882  CE  LYS A 118     -21.938 -17.034  -3.337  1.00 20.43           C  
ATOM    883  NZ  LYS A 118     -22.649 -15.791  -2.903  1.00 21.19           N  
ATOM    884  N   SER A 119     -15.560 -17.215  -4.864  1.00 13.75           N  
ATOM    885  CA  SER A 119     -14.233 -16.821  -5.331  1.00 13.53           C  
ATOM    886  C   SER A 119     -14.005 -15.320  -5.156  1.00 13.27           C  
ATOM    887  O   SER A 119     -14.956 -14.537  -5.157  1.00 13.03           O  
ATOM    888  CB  SER A 119     -14.065 -17.186  -6.806  1.00 13.51           C  
ATOM    889  OG  SER A 119     -14.212 -18.584  -6.999  1.00 14.14           O  
ATOM    890  N   LEU A 120     -12.742 -14.929  -5.009  1.00 13.59           N  
ATOM    891  CA  LEU A 120     -12.372 -13.513  -4.966  1.00 14.02           C  
ATOM    892  C   LEU A 120     -12.878 -12.819  -6.221  1.00 14.20           C  
ATOM    893  O   LEU A 120     -12.720 -13.340  -7.322  1.00 14.21           O  
ATOM    894  CB  LEU A 120     -10.850 -13.349  -4.882  1.00 13.88           C  
ATOM    895  CG  LEU A 120     -10.128 -13.717  -3.590  1.00 15.10           C  
ATOM    896  CD1 LEU A 120      -8.629 -13.656  -3.822  1.00 15.53           C  
ATOM    897  CD2 LEU A 120     -10.532 -12.784  -2.447  1.00 14.80           C  
ATOM    898  N   GLY A 121     -13.504 -11.658  -6.040  1.00 14.38           N  
ATOM    899  CA  GLY A 121     -13.996 -10.860  -7.155  1.00 14.91           C  
ATOM    900  C   GLY A 121     -15.438 -11.137  -7.545  1.00 15.14           C  
ATOM    901  O   GLY A 121     -16.024 -10.383  -8.324  1.00 15.67           O  
ATOM    902  N   THR A 122     -16.016 -12.213  -7.012  1.00 14.67           N  
ATOM    903  CA  THR A 122     -17.422 -12.554  -7.295  1.00 14.73           C  
ATOM    904  C   THR A 122     -18.382 -11.903  -6.290  1.00 14.62           C  
ATOM    905  O   THR A 122     -19.599 -11.946  -6.454  1.00 14.48           O  
ATOM    906  CB  THR A 122     -17.651 -14.086  -7.354  1.00 14.81           C  
ATOM    907  OG1 THR A 122     -17.499 -14.660  -6.049  1.00 15.60           O  
ATOM    908  CG2 THR A 122     -16.663 -14.737  -8.311  1.00 14.87           C  
ATOM    909  N   MET A 123     -17.801 -11.321  -5.244  1.00 14.25           N  
ATOM    910  CA  MET A 123     -18.502 -10.558  -4.221  1.00 13.88           C  
ATOM    911  C   MET A 123     -17.669  -9.291  -4.018  1.00 13.50           C  
ATOM    912  O   MET A 123     -16.475  -9.296  -4.340  1.00 13.73           O  
ATOM    913  CB  MET A 123     -18.549 -11.333  -2.899  1.00 13.96           C  
ATOM    914  CG  MET A 123     -19.405 -12.593  -2.894  1.00 14.50           C  
ATOM    915  SD  MET A 123     -21.152 -12.266  -3.201  1.00 16.34           S  
ATOM    916  CE  MET A 123     -21.672 -11.517  -1.657  1.00 16.24           C  
ATOM    917  N   PRO A 124     -18.278  -8.208  -3.487  1.00 13.10           N  
ATOM    918  CA  PRO A 124     -17.484  -7.009  -3.185  1.00 12.59           C  
ATOM    919  C   PRO A 124     -16.333  -7.301  -2.219  1.00 11.96           C  
ATOM    920  O   PRO A 124     -16.407  -8.259  -1.437  1.00 11.53           O  
ATOM    921  CB  PRO A 124     -18.505  -6.064  -2.540  1.00 12.91           C  
ATOM    922  CG  PRO A 124     -19.824  -6.506  -3.113  1.00 13.29           C  
ATOM    923  CD  PRO A 124     -19.702  -8.004  -3.163  1.00 13.12           C  
ATOM    924  N   PRO A 125     -15.261  -6.492  -2.282  1.00 11.23           N  
ATOM    925  CA  PRO A 125     -14.119  -6.706  -1.397  1.00 10.67           C  
ATOM    926  C   PRO A 125     -14.545  -6.715   0.066  1.00 10.19           C  
ATOM    927  O   PRO A 125     -15.367  -5.895   0.482  1.00  9.99           O  
ATOM    928  CB  PRO A 125     -13.225  -5.497  -1.685  1.00 11.02           C  
ATOM    929  CG  PRO A 125     -13.562  -5.125  -3.094  1.00 11.03           C  
ATOM    930  CD  PRO A 125     -15.049  -5.341  -3.176  1.00 11.15           C  
ATOM    931  N   HIS A 126     -13.989  -7.644   0.832  1.00  9.86           N  
ATOM    932  CA  HIS A 126     -14.375  -7.809   2.225  1.00  9.64           C  
ATOM    933  C   HIS A 126     -13.386  -8.717   2.936  1.00  9.59           C  
ATOM    934  O   HIS A 126     -12.816  -9.637   2.337  1.00  9.50           O  
ATOM    935  CB  HIS A 126     -15.779  -8.427   2.297  1.00  9.85           C  
ATOM    936  CG  HIS A 126     -16.530  -8.114   3.554  1.00 10.74           C  
ATOM    937  ND1 HIS A 126     -16.164  -8.610   4.787  1.00 11.46           N  
ATOM    938  CD2 HIS A 126     -17.657  -7.390   3.762  1.00 11.58           C  
ATOM    939  CE1 HIS A 126     -17.017  -8.185   5.703  1.00 11.52           C  
ATOM    940  NE2 HIS A 126     -17.935  -7.447   5.106  1.00 11.45           N  
ATOM    941  N   VAL A 127     -13.189  -8.449   4.221  1.00  9.72           N  
ATOM    942  C   VAL A 127     -12.918 -10.765   5.033  1.00  9.91           C  
ATOM    943  O   VAL A 127     -12.142 -11.710   5.099  1.00  9.78           O  
ATOM    944  CA AVAL A 127     -12.403  -9.317   5.089  0.50  9.74           C  
ATOM    945  CB AVAL A 127     -12.382  -8.764   6.544  0.50  9.88           C  
ATOM    946  CG1AVAL A 127     -13.755  -8.852   7.206  0.50 10.19           C  
ATOM    947  CG2AVAL A 127     -11.337  -9.461   7.368  0.50  9.42           C  
ATOM    949  CB BVAL A 127     -12.269  -8.839   6.521  0.50 10.01           C  
ATOM    950  CG1BVAL A 127     -11.201  -7.770   6.609  0.50 10.19           C  
ATOM    951  CG2BVAL A 127     -13.611  -8.331   7.050  0.50 10.19           C  
ATOM    952  N   PHE A 128     -14.237 -10.920   4.901  1.00 10.37           N  
ATOM    953  CA  PHE A 128     -14.859 -12.252   4.804  1.00 10.49           C  
ATOM    954  C   PHE A 128     -14.341 -13.039   3.589  1.00 10.64           C  
ATOM    955  O   PHE A 128     -14.156 -14.259   3.658  1.00 10.36           O  
ATOM    956  CB  PHE A 128     -16.391 -12.155   4.726  1.00 10.70           C  
ATOM    957  CG  PHE A 128     -17.062 -11.612   5.976  1.00 10.87           C  
ATOM    958  CD1 PHE A 128     -16.402 -11.571   7.212  1.00 11.03           C  
ATOM    959  CD2 PHE A 128     -18.383 -11.175   5.917  1.00 11.70           C  
ATOM    960  CE1 PHE A 128     -17.044 -11.072   8.356  1.00 11.12           C  
ATOM    961  CE2 PHE A 128     -19.031 -10.680   7.048  1.00 12.06           C  
ATOM    962  CZ  PHE A 128     -18.360 -10.626   8.271  1.00 11.99           C  
ATOM    963  N   ALA A 129     -14.121 -12.334   2.482  1.00 10.69           N  
ATOM    964  CA  ALA A 129     -13.596 -12.947   1.265  1.00 11.07           C  
ATOM    965  C   ALA A 129     -12.153 -13.431   1.436  1.00 10.98           C  
ATOM    966  O   ALA A 129     -11.779 -14.473   0.900  1.00 11.08           O  
ATOM    967  CB  ALA A 129     -13.707 -11.988   0.099  1.00 11.33           C  
ATOM    968  N   ILE A 130     -11.347 -12.673   2.181  1.00 11.07           N  
ATOM    969  CA  ILE A 130      -9.980 -13.100   2.500  1.00 11.03           C  
ATOM    970  C   ILE A 130     -10.017 -14.362   3.368  1.00 11.33           C  
ATOM    971  O   ILE A 130      -9.262 -15.311   3.133  1.00 11.41           O  
ATOM    972  CB  ILE A 130      -9.179 -11.970   3.196  1.00 11.14           C  
ATOM    973  CG1 ILE A 130      -8.993 -10.779   2.241  1.00 10.82           C  
ATOM    974  CG2 ILE A 130      -7.836 -12.483   3.744  1.00 11.39           C  
ATOM    975  CD1 ILE A 130      -8.213 -11.086   0.935  1.00 11.97           C  
ATOM    976  N   ALA A 131     -10.916 -14.363   4.351  1.00 11.38           N  
ATOM    977  CA  ALA A 131     -11.128 -15.512   5.234  1.00 11.79           C  
ATOM    978  C   ALA A 131     -11.557 -16.749   4.449  1.00 12.08           C  
ATOM    979  O   ALA A 131     -11.030 -17.841   4.665  1.00 11.74           O  
ATOM    980  CB  ALA A 131     -12.156 -15.179   6.289  1.00 12.11           C  
ATOM    981  N   ASP A 132     -12.507 -16.572   3.534  1.00 12.56           N  
ATOM    982  CA  ASP A 132     -12.987 -17.693   2.725  1.00 13.71           C  
ATOM    983  C   ASP A 132     -11.908 -18.217   1.772  1.00 13.86           C  
ATOM    984  O   ASP A 132     -11.812 -19.425   1.538  1.00 13.99           O  
ATOM    985  CB  ASP A 132     -14.251 -17.321   1.952  1.00 14.00           C  
ATOM    986  CG  ASP A 132     -15.111 -18.534   1.645  1.00 15.78           C  
ATOM    987  OD1 ASP A 132     -15.792 -19.018   2.571  1.00 17.42           O  
ATOM    988  OD2 ASP A 132     -15.089 -19.006   0.494  1.00 19.22           O  
ATOM    989  N   LYS A 133     -11.096 -17.306   1.237  1.00 14.03           N  
ATOM    990  CA  LYS A 133      -9.990 -17.676   0.361  1.00 14.75           C  
ATOM    991  C   LYS A 133      -8.960 -18.511   1.117  1.00 14.51           C  
ATOM    992  O   LYS A 133      -8.450 -19.495   0.585  1.00 14.63           O  
ATOM    993  CB  LYS A 133      -9.349 -16.429  -0.252  1.00 14.98           C  
ATOM    994  CG  LYS A 133      -8.104 -16.682  -1.099  1.00 17.89           C  
ATOM    995  CD  LYS A 133      -8.425 -17.309  -2.445  1.00 21.93           C  
ATOM    996  CE  LYS A 133      -7.340 -16.970  -3.472  1.00 23.28           C  
ATOM    997  NZ  LYS A 133      -5.947 -17.104  -2.938  1.00 24.94           N  
ATOM    998  N   ALA A 134      -8.671 -18.125   2.362  1.00 14.33           N  
ATOM    999  CA  ALA A 134      -7.770 -18.911   3.214  1.00 14.35           C  
ATOM   1000  C   ALA A 134      -8.320 -20.322   3.438  1.00 14.52           C  
ATOM   1001  O   ALA A 134      -7.589 -21.310   3.337  1.00 14.32           O  
ATOM   1002  CB  ALA A 134      -7.541 -18.212   4.543  1.00 14.53           C  
ATOM   1003  N   PHE A 135      -9.613 -20.399   3.738  1.00 14.79           N  
ATOM   1004  CA  PHE A 135     -10.298 -21.675   3.921  1.00 15.60           C  
ATOM   1005  C   PHE A 135     -10.207 -22.542   2.661  1.00 16.15           C  
ATOM   1006  O   PHE A 135      -9.859 -23.720   2.742  1.00 15.78           O  
ATOM   1007  CB  PHE A 135     -11.760 -21.441   4.326  1.00 15.74           C  
ATOM   1008  CG  PHE A 135     -12.533 -22.709   4.562  1.00 16.21           C  
ATOM   1009  CD1 PHE A 135     -12.343 -23.451   5.726  1.00 16.23           C  
ATOM   1010  CD2 PHE A 135     -13.444 -23.164   3.615  1.00 17.03           C  
ATOM   1011  CE1 PHE A 135     -13.059 -24.632   5.949  1.00 16.33           C  
ATOM   1012  CE2 PHE A 135     -14.161 -24.342   3.825  1.00 18.23           C  
ATOM   1013  CZ  PHE A 135     -13.967 -25.073   4.991  1.00 16.85           C  
ATOM   1014  N   ARG A 136     -10.511 -21.943   1.510  1.00 17.00           N  
ATOM   1015  CA  ARG A 136     -10.445 -22.622   0.209  1.00 18.52           C  
ATOM   1016  C   ARG A 136      -9.042 -23.146  -0.092  1.00 18.37           C  
ATOM   1017  O   ARG A 136      -8.878 -24.296  -0.510  1.00 18.31           O  
ATOM   1018  CB  ARG A 136     -10.905 -21.667  -0.899  1.00 18.35           C  
ATOM   1019  CG  ARG A 136     -10.879 -22.229  -2.327  1.00 20.03           C  
ATOM   1020  CD  ARG A 136     -11.324 -21.165  -3.342  1.00 20.78           C  
ATOM   1021  NE  ARG A 136     -12.606 -20.593  -2.940  1.00 25.53           N  
ATOM   1022  CZ  ARG A 136     -12.803 -19.339  -2.532  1.00 26.89           C  
ATOM   1023  NH1 ARG A 136     -14.020 -18.966  -2.170  1.00 28.30           N  
ATOM   1024  NH2 ARG A 136     -11.810 -18.454  -2.501  1.00 27.22           N  
ATOM   1025  N   ASP A 137      -8.033 -22.304   0.128  1.00 18.33           N  
ATOM   1026  CA  ASP A 137      -6.644 -22.708  -0.084  1.00 18.64           C  
ATOM   1027  C   ASP A 137      -6.227 -23.837   0.853  1.00 18.55           C  
ATOM   1028  O   ASP A 137      -5.523 -24.756   0.437  1.00 18.43           O  
ATOM   1029  CB  ASP A 137      -5.699 -21.516   0.061  1.00 18.82           C  
ATOM   1030  CG  ASP A 137      -5.795 -20.545  -1.105  1.00 20.19           C  
ATOM   1031  OD1 ASP A 137      -5.362 -19.389  -0.939  1.00 22.01           O  
ATOM   1032  OD2 ASP A 137      -6.305 -20.926  -2.183  1.00 22.11           O  
ATOM   1033  N   MET A 138      -6.676 -23.770   2.108  1.00 18.55           N  
ATOM   1034  CA  MET A 138      -6.402 -24.813   3.089  1.00 19.03           C  
ATOM   1035  C   MET A 138      -6.935 -26.160   2.596  1.00 19.69           C  
ATOM   1036  O   MET A 138      -6.229 -27.165   2.653  1.00 19.59           O  
ATOM   1037  CB  MET A 138      -7.019 -24.455   4.444  1.00 18.57           C  
ATOM   1038  CG  MET A 138      -6.705 -25.443   5.557  1.00 18.87           C  
ATOM   1039  SD  MET A 138      -7.779 -25.268   6.994  1.00 18.86           S  
ATOM   1040  CE  MET A 138      -9.335 -25.909   6.365  1.00 19.58           C  
ATOM   1041  N   LYS A 139      -8.175 -26.152   2.105  1.00 20.50           N  
ATOM   1042  CA  LYS A 139      -8.833 -27.339   1.541  1.00 21.76           C  
ATOM   1043  C   LYS A 139      -8.167 -27.861   0.268  1.00 21.81           C  
ATOM   1044  O   LYS A 139      -7.911 -29.062   0.145  1.00 22.20           O  
ATOM   1045  CB  LYS A 139     -10.294 -27.020   1.221  1.00 22.00           C  
ATOM   1046  CG  LYS A 139     -11.283 -27.291   2.326  1.00 24.05           C  
ATOM   1047  CD  LYS A 139     -12.696 -27.037   1.805  1.00 26.55           C  
ATOM   1048  CE  LYS A 139     -13.730 -27.853   2.554  1.00 28.39           C  
ATOM   1049  NZ  LYS A 139     -15.121 -27.501   2.144  1.00 30.06           N  
ATOM   1050  N   VAL A 140      -7.912 -26.964  -0.680  1.00 22.16           N  
ATOM   1051  CA  VAL A 140      -7.406 -27.346  -2.003  1.00 22.27           C  
ATOM   1052  C   VAL A 140      -5.927 -27.747  -1.967  1.00 22.28           C  
ATOM   1053  O   VAL A 140      -5.535 -28.752  -2.573  1.00 22.38           O  
ATOM   1054  CB  VAL A 140      -7.661 -26.231  -3.064  1.00 22.42           C  
ATOM   1055  CG1 VAL A 140      -7.035 -26.586  -4.417  1.00 22.93           C  
ATOM   1056  CG2 VAL A 140      -9.152 -25.986  -3.233  1.00 22.52           C  
ATOM   1057  N   LEU A 141      -5.116 -26.975  -1.245  1.00 21.79           N  
ATOM   1058  CA  LEU A 141      -3.671 -27.201  -1.215  1.00 21.75           C  
ATOM   1059  C   LEU A 141      -3.204 -28.107  -0.072  1.00 21.26           C  
ATOM   1060  O   LEU A 141      -2.046 -28.536  -0.052  1.00 21.47           O  
ATOM   1061  CB  LEU A 141      -2.914 -25.866  -1.191  1.00 21.91           C  
ATOM   1062  CG  LEU A 141      -3.165 -24.908  -2.359  1.00 23.07           C  
ATOM   1063  CD1 LEU A 141      -2.581 -23.543  -2.060  1.00 23.79           C  
ATOM   1064  CD2 LEU A 141      -2.604 -25.466  -3.674  1.00 24.41           C  
ATOM   1065  N   LYS A 142      -4.110 -28.409   0.858  1.00 20.75           N  
ATOM   1066  CA  LYS A 142      -3.803 -29.225   2.043  1.00 20.34           C  
ATOM   1067  C   LYS A 142      -2.622 -28.614   2.803  1.00 19.58           C  
ATOM   1068  O   LYS A 142      -1.608 -29.268   3.076  1.00 19.42           O  
ATOM   1069  CB  LYS A 142      -3.555 -30.695   1.663  1.00 20.89           C  
ATOM   1070  CG  LYS A 142      -4.545 -31.235   0.636  1.00 22.74           C  
ATOM   1071  CD  LYS A 142      -5.158 -32.560   1.068  1.00 26.60           C  
ATOM   1072  CE  LYS A 142      -6.589 -32.368   1.578  1.00 28.46           C  
ATOM   1073  NZ  LYS A 142      -6.699 -31.354   2.672  1.00 30.83           N  
ATOM   1074  N   LEU A 143      -2.775 -27.335   3.125  1.00 18.54           N  
ATOM   1075  CA  LEU A 143      -1.712 -26.537   3.708  1.00 17.96           C  
ATOM   1076  C   LEU A 143      -2.340 -25.561   4.692  1.00 16.80           C  
ATOM   1077  O   LEU A 143      -3.289 -24.859   4.350  1.00 15.85           O  
ATOM   1078  CB  LEU A 143      -0.972 -25.776   2.598  1.00 18.20           C  
ATOM   1079  CG  LEU A 143       0.136 -24.761   2.919  1.00 19.09           C  
ATOM   1080  CD1 LEU A 143       1.333 -25.443   3.563  1.00 20.18           C  
ATOM   1081  CD2 LEU A 143       0.561 -24.006   1.671  1.00 18.83           C  
ATOM   1082  N   SER A 144      -1.817 -25.529   5.914  1.00 16.07           N  
ATOM   1083  CA  SER A 144      -2.277 -24.555   6.902  1.00 15.30           C  
ATOM   1084  C   SER A 144      -2.039 -23.140   6.385  1.00 14.81           C  
ATOM   1085  O   SER A 144      -1.157 -22.916   5.548  1.00 14.86           O  
ATOM   1086  CB  SER A 144      -1.598 -24.783   8.248  1.00 15.60           C  
ATOM   1087  OG  SER A 144      -2.126 -25.945   8.868  1.00 15.34           O  
ATOM   1088  N   GLN A 145      -2.846 -22.200   6.871  1.00 14.18           N  
ATOM   1089  CA  GLN A 145      -2.867 -20.847   6.325  1.00 13.43           C  
ATOM   1090  C   GLN A 145      -2.721 -19.794   7.411  1.00 12.73           C  
ATOM   1091  O   GLN A 145      -3.187 -19.981   8.538  1.00 12.84           O  
ATOM   1092  CB  GLN A 145      -4.169 -20.599   5.553  1.00 13.65           C  
ATOM   1093  CG  GLN A 145      -4.408 -21.545   4.377  1.00 14.71           C  
ATOM   1094  CD  GLN A 145      -3.490 -21.281   3.208  1.00 15.50           C  
ATOM   1095  OE1 GLN A 145      -3.298 -20.133   2.794  1.00 17.05           O  
ATOM   1096  NE2 GLN A 145      -2.921 -22.347   2.655  1.00 17.33           N  
ATOM   1097  N   SER A 146      -2.068 -18.692   7.061  1.00 12.16           N  
ATOM   1098  C   SER A 146      -2.585 -16.309   7.276  1.00 11.97           C  
ATOM   1099  O   SER A 146      -2.392 -16.087   6.076  1.00 12.03           O  
ATOM   1100  CA ASER A 146      -1.998 -17.541   7.949  0.50 11.97           C  
ATOM   1101  CB ASER A 146      -0.560 -17.267   8.392  0.50 12.05           C  
ATOM   1102  OG ASER A 146       0.240 -16.853   7.301  0.50 11.60           O  
ATOM   1104  CB BSER A 146      -0.529 -17.263   8.343  0.50 12.15           C  
ATOM   1105  OG BSER A 146       0.023 -18.359   9.057  0.50 12.26           O  
ATOM   1106  N   ILE A 147      -3.315 -15.524   8.060  1.00 11.41           N  
ATOM   1107  CA  ILE A 147      -3.845 -14.252   7.598  1.00 10.86           C  
ATOM   1108  C   ILE A 147      -3.153 -13.197   8.445  1.00 10.69           C  
ATOM   1109  O   ILE A 147      -3.305 -13.178   9.676  1.00 10.56           O  
ATOM   1110  CB  ILE A 147      -5.379 -14.181   7.732  1.00 10.99           C  
ATOM   1111  CG1 ILE A 147      -6.028 -15.246   6.830  1.00 11.23           C  
ATOM   1112  CG2 ILE A 147      -5.888 -12.775   7.392  1.00 11.01           C  
ATOM   1113  CD1 ILE A 147      -7.492 -15.526   7.136  1.00 11.22           C  
ATOM   1114  N   ILE A 148      -2.368 -12.356   7.777  1.00 10.52           N  
ATOM   1115  C   ILE A 148      -2.277  -9.993   8.341  1.00 10.58           C  
ATOM   1116  O   ILE A 148      -2.500  -9.485   7.245  1.00 10.36           O  
ATOM   1117  CA AILE A 148      -1.569 -11.335   8.455  0.50 10.57           C  
ATOM   1118  CB AILE A 148      -0.116 -11.243   7.896  0.50 10.75           C  
ATOM   1119  CG1AILE A 148       0.641 -12.558   8.099  0.50 11.34           C  
ATOM   1120  CG2AILE A 148       0.663 -10.099   8.554  0.50 10.75           C  
ATOM   1121  CD1AILE A 148       0.663 -13.438   6.876  0.50 12.08           C  
ATOM   1123  CB BILE A 148      -0.137 -11.238   7.821  0.50 10.69           C  
ATOM   1124  CG1BILE A 148       0.506 -12.628   7.674  0.50 11.21           C  
ATOM   1125  CG2BILE A 148       0.756 -10.277   8.625  0.50 10.61           C  
ATOM   1126  CD1BILE A 148       0.640 -13.415   8.975  0.50 11.55           C  
ATOM   1127  N   VAL A 149      -2.637  -9.429   9.489  1.00 10.22           N  
ATOM   1128  CA  VAL A 149      -3.375  -8.171   9.510  1.00 10.30           C  
ATOM   1129  C   VAL A 149      -2.415  -7.093  10.019  1.00 10.67           C  
ATOM   1130  O   VAL A 149      -2.116  -7.044  11.214  1.00 11.37           O  
ATOM   1131  CB  VAL A 149      -4.657  -8.281  10.365  1.00 10.48           C  
ATOM   1132  CG1 VAL A 149      -5.564  -7.092  10.131  1.00 10.30           C  
ATOM   1133  CG2 VAL A 149      -5.418  -9.573  10.033  1.00 11.17           C  
ATOM   1134  N   SER A 150      -1.926  -6.259   9.099  1.00 10.20           N  
ATOM   1135  C   SER A 150      -1.382  -3.848   9.421  1.00 10.14           C  
ATOM   1136  O   SER A 150      -2.479  -3.559   8.925  1.00 10.62           O  
ATOM   1137  CA ASER A 150      -0.873  -5.284   9.408  0.50 10.33           C  
ATOM   1138  CB ASER A 150       0.261  -5.394   8.390  0.50 10.26           C  
ATOM   1139  OG ASER A 150      -0.174  -4.924   7.127  0.50 11.49           O  
ATOM   1141  CB BSER A 150       0.294  -5.414   8.414  0.50 10.07           C  
ATOM   1142  OG BSER A 150       0.830  -6.729   8.396  0.50 10.32           O  
ATOM   1143  N   GLY A 151      -0.567  -2.947   9.966  1.00 10.11           N  
ATOM   1144  CA  GLY A 151      -0.918  -1.531  10.034  1.00 10.22           C  
ATOM   1145  C   GLY A 151      -0.436  -0.874  11.310  1.00 10.32           C  
ATOM   1146  O   GLY A 151      -0.110  -1.549  12.292  1.00 10.62           O  
ATOM   1147  N   GLU A 152      -0.394   0.455  11.299  1.00  9.85           N  
ATOM   1148  CA  GLU A 152       0.034   1.212  12.469  1.00 10.25           C  
ATOM   1149  C   GLU A 152      -1.037   1.189  13.559  1.00  9.34           C  
ATOM   1150  O   GLU A 152      -2.165   0.725  13.337  1.00  8.65           O  
ATOM   1151  CB  GLU A 152       0.403   2.654  12.079  1.00 10.32           C  
ATOM   1152  CG  GLU A 152      -0.776   3.524  11.686  1.00 11.80           C  
ATOM   1153  CD  GLU A 152      -0.359   4.951  11.373  1.00 12.95           C  
ATOM   1154  OE1 GLU A 152      -0.509   5.354  10.211  1.00 17.42           O  
ATOM   1155  OE2 GLU A 152       0.140   5.660  12.280  1.00 16.26           O  
ATOM   1156  N   SER A 153      -0.665   1.660  14.744  1.00  8.74           N  
ATOM   1157  CA  SER A 153      -1.593   1.740  15.853  1.00  8.86           C  
ATOM   1158  C   SER A 153      -2.874   2.481  15.472  1.00  8.48           C  
ATOM   1159  O   SER A 153      -2.829   3.600  14.942  1.00  9.05           O  
ATOM   1160  CB  SER A 153      -0.925   2.396  17.062  1.00  8.59           C  
ATOM   1161  OG  SER A 153      -1.858   2.567  18.106  1.00  9.73           O  
ATOM   1162  N   GLY A 154      -4.009   1.842  15.754  1.00  8.61           N  
ATOM   1163  CA  GLY A 154      -5.326   2.409  15.480  1.00  8.38           C  
ATOM   1164  C   GLY A 154      -5.844   2.207  14.062  1.00  8.35           C  
ATOM   1165  O   GLY A 154      -6.890   2.747  13.712  1.00  8.90           O  
ATOM   1166  N   ALA A 155      -5.116   1.446  13.246  1.00  8.19           N  
ATOM   1167  CA  ALA A 155      -5.497   1.241  11.840  1.00  7.99           C  
ATOM   1168  C   ALA A 155      -6.702   0.316  11.651  1.00  8.16           C  
ATOM   1169  O   ALA A 155      -7.398   0.413  10.633  1.00  8.45           O  
ATOM   1170  CB  ALA A 155      -4.310   0.744  11.027  1.00  7.87           C  
ATOM   1171  N   GLY A 156      -6.923  -0.592  12.605  1.00  8.01           N  
ATOM   1172  CA  GLY A 156      -8.052  -1.525  12.553  1.00  7.80           C  
ATOM   1173  C   GLY A 156      -7.707  -3.009  12.521  1.00  7.53           C  
ATOM   1174  O   GLY A 156      -8.557  -3.831  12.162  1.00  7.93           O  
ATOM   1175  N   LYS A 157      -6.485  -3.363  12.929  1.00  7.57           N  
ATOM   1176  CA  LYS A 157      -6.025  -4.762  12.908  1.00  7.51           C  
ATOM   1177  C   LYS A 157      -6.862  -5.666  13.803  1.00  7.73           C  
ATOM   1178  O   LYS A 157      -7.285  -6.755  13.396  1.00  7.89           O  
ATOM   1179  CB  LYS A 157      -4.549  -4.867  13.316  1.00  7.38           C  
ATOM   1180  CG  LYS A 157      -3.591  -4.092  12.427  1.00  7.04           C  
ATOM   1181  CD  LYS A 157      -2.153  -4.281  12.887  1.00  7.81           C  
ATOM   1182  CE  LYS A 157      -1.895  -3.654  14.267  1.00  7.00           C  
ATOM   1183  NZ  LYS A 157      -2.134  -2.167  14.264  1.00  6.80           N  
ATOM   1184  N   THR A 158      -7.093  -5.217  15.028  1.00  7.60           N  
ATOM   1185  CA  THR A 158      -7.835  -6.015  16.004  1.00  7.72           C  
ATOM   1186  C   THR A 158      -9.288  -6.208  15.581  1.00  7.82           C  
ATOM   1187  O   THR A 158      -9.813  -7.332  15.629  1.00  7.84           O  
ATOM   1188  CB  THR A 158      -7.707  -5.399  17.406  1.00  7.39           C  
ATOM   1189  OG1 THR A 158      -6.358  -5.586  17.852  1.00  7.44           O  
ATOM   1190  CG2 THR A 158      -8.678  -6.040  18.414  1.00  8.25           C  
ATOM   1191  N   GLU A 159      -9.928  -5.135  15.129  1.00  8.09           N  
ATOM   1192  CA  GLU A 159     -11.294  -5.262  14.632  1.00  8.84           C  
ATOM   1193  C   GLU A 159     -11.394  -6.268  13.478  1.00  8.87           C  
ATOM   1194  O   GLU A 159     -12.269  -7.142  13.482  1.00  9.01           O  
ATOM   1195  CB  GLU A 159     -11.895  -3.901  14.267  1.00  8.95           C  
ATOM   1196  CG  GLU A 159     -12.180  -3.019  15.492  1.00 10.48           C  
ATOM   1197  CD  GLU A 159     -12.909  -3.758  16.609  1.00 12.73           C  
ATOM   1198  OE1 GLU A 159     -14.055  -4.205  16.380  1.00 13.49           O  
ATOM   1199  OE2 GLU A 159     -12.333  -3.901  17.716  1.00 13.44           O  
ATOM   1200  N   ASN A 160     -10.482  -6.170  12.511  1.00  8.99           N  
ATOM   1201  CA  ASN A 160     -10.508  -7.085  11.371  1.00  9.23           C  
ATOM   1202  C   ASN A 160     -10.165  -8.531  11.714  1.00  9.26           C  
ATOM   1203  O   ASN A 160     -10.728  -9.463  11.133  1.00  9.05           O  
ATOM   1204  CB  ASN A 160      -9.664  -6.541  10.226  1.00  9.37           C  
ATOM   1205  CG  ASN A 160     -10.359  -5.404   9.518  1.00 10.14           C  
ATOM   1206  OD1 ASN A 160     -11.272  -5.626   8.725  1.00 11.91           O  
ATOM   1207  ND2 ASN A 160      -9.964  -4.179   9.831  1.00 10.19           N  
ATOM   1208  N   THR A 161      -9.271  -8.712  12.683  1.00  9.04           N  
ATOM   1209  CA  THR A 161      -8.996 -10.040  13.237  1.00  9.78           C  
ATOM   1210  C   THR A 161     -10.283 -10.654  13.794  1.00  9.94           C  
ATOM   1211  O   THR A 161     -10.606 -11.807  13.504  1.00 10.15           O  
ATOM   1212  CB  THR A 161      -7.902  -9.951  14.325  1.00  9.66           C  
ATOM   1213  OG1 THR A 161      -6.696  -9.481  13.717  1.00 10.77           O  
ATOM   1214  CG2 THR A 161      -7.639 -11.320  14.982  1.00 10.22           C  
ATOM   1215  N   LYS A 162     -11.033  -9.868  14.561  1.00 10.02           N  
ATOM   1216  CA  LYS A 162     -12.301 -10.339  15.112  1.00 10.62           C  
ATOM   1217  C   LYS A 162     -13.312 -10.709  14.018  1.00 10.63           C  
ATOM   1218  O   LYS A 162     -14.021 -11.716  14.148  1.00 10.71           O  
ATOM   1219  CB  LYS A 162     -12.879  -9.324  16.099  1.00 10.98           C  
ATOM   1220  CG  LYS A 162     -12.119  -9.297  17.422  1.00 11.87           C  
ATOM   1221  CD  LYS A 162     -12.799  -8.427  18.450  1.00 15.09           C  
ATOM   1222  CE  LYS A 162     -12.468  -6.968  18.232  1.00 14.99           C  
ATOM   1223  NZ  LYS A 162     -12.805  -6.151  19.434  1.00 14.84           N  
ATOM   1224  N   PHE A 163     -13.354  -9.933  12.934  1.00 10.80           N  
ATOM   1225  CA  PHE A 163     -14.264 -10.245  11.816  1.00 11.21           C  
ATOM   1226  C   PHE A 163     -13.896 -11.566  11.150  1.00 11.39           C  
ATOM   1227  O   PHE A 163     -14.778 -12.364  10.816  1.00 11.57           O  
ATOM   1228  CB  PHE A 163     -14.278  -9.142  10.747  1.00 11.40           C  
ATOM   1229  CG  PHE A 163     -14.625  -7.774  11.264  1.00 12.18           C  
ATOM   1230  CD1 PHE A 163     -13.926  -6.662  10.804  1.00 13.36           C  
ATOM   1231  CD2 PHE A 163     -15.640  -7.588  12.201  1.00 13.22           C  
ATOM   1232  CE1 PHE A 163     -14.221  -5.387  11.268  1.00 13.38           C  
ATOM   1233  CE2 PHE A 163     -15.948  -6.308  12.671  1.00 15.19           C  
ATOM   1234  CZ  PHE A 163     -15.238  -5.208  12.205  1.00 14.04           C  
ATOM   1235  N   VAL A 164     -12.597 -11.780  10.930  1.00 11.21           N  
ATOM   1236  CA  VAL A 164     -12.109 -13.033  10.337  1.00 11.47           C  
ATOM   1237  C   VAL A 164     -12.488 -14.225  11.216  1.00 12.06           C  
ATOM   1238  O   VAL A 164     -12.999 -15.232  10.721  1.00 11.51           O  
ATOM   1239  CB  VAL A 164     -10.568 -13.017  10.093  1.00 11.39           C  
ATOM   1240  CG1 VAL A 164     -10.061 -14.407   9.723  1.00 11.08           C  
ATOM   1241  CG2 VAL A 164     -10.199 -12.021   9.000  1.00 10.58           C  
ATOM   1242  N   LEU A 165     -12.250 -14.098  12.522  1.00 12.31           N  
ATOM   1243  CA  LEU A 165     -12.555 -15.186  13.457  1.00 13.26           C  
ATOM   1244  C   LEU A 165     -14.045 -15.488  13.510  1.00 13.59           C  
ATOM   1245  O   LEU A 165     -14.438 -16.661  13.541  1.00 13.76           O  
ATOM   1246  CB  LEU A 165     -12.006 -14.882  14.854  1.00 13.03           C  
ATOM   1247  CG  LEU A 165     -10.480 -14.718  14.941  1.00 14.10           C  
ATOM   1248  CD1 LEU A 165     -10.073 -14.219  16.324  1.00 15.64           C  
ATOM   1249  CD2 LEU A 165      -9.735 -15.998  14.572  1.00 15.60           C  
ATOM   1250  N   ARG A 166     -14.866 -14.435  13.504  1.00 14.06           N  
ATOM   1251  CA  ARG A 166     -16.321 -14.585  13.493  1.00 15.36           C  
ATOM   1252  C   ARG A 166     -16.767 -15.280  12.213  1.00 14.81           C  
ATOM   1253  O   ARG A 166     -17.567 -16.212  12.261  1.00 15.00           O  
ATOM   1254  CB  ARG A 166     -17.026 -13.233  13.642  1.00 15.32           C  
ATOM   1255  CG  ARG A 166     -18.546 -13.333  13.810  1.00 17.29           C  
ATOM   1256  CD  ARG A 166     -19.181 -11.983  14.123  1.00 18.13           C  
ATOM   1257  NE  ARG A 166     -18.801 -11.454  15.438  1.00 24.21           N  
ATOM   1258  CZ  ARG A 166     -19.613 -11.384  16.495  1.00 25.69           C  
ATOM   1259  NH1 ARG A 166     -20.866 -11.819  16.416  1.00 27.52           N  
ATOM   1260  NH2 ARG A 166     -19.171 -10.877  17.640  1.00 26.24           N  
ATOM   1261  N   TYR A 167     -16.227 -14.841  11.078  1.00 14.18           N  
ATOM   1262  CA  TYR A 167     -16.583 -15.439   9.794  1.00 14.30           C  
ATOM   1263  C   TYR A 167     -16.320 -16.945   9.741  1.00 14.42           C  
ATOM   1264  O   TYR A 167     -17.190 -17.722   9.322  1.00 14.67           O  
ATOM   1265  CB  TYR A 167     -15.858 -14.753   8.631  1.00 13.93           C  
ATOM   1266  CG  TYR A 167     -16.193 -15.407   7.316  1.00 14.01           C  
ATOM   1267  CD1 TYR A 167     -17.361 -15.065   6.631  1.00 14.49           C  
ATOM   1268  CD2 TYR A 167     -15.381 -16.412   6.785  1.00 13.61           C  
ATOM   1269  CE1 TYR A 167     -17.697 -15.685   5.431  1.00 13.84           C  
ATOM   1270  CE2 TYR A 167     -15.709 -17.041   5.578  1.00 13.83           C  
ATOM   1271  CZ  TYR A 167     -16.870 -16.668   4.918  1.00 13.97           C  
ATOM   1272  OH  TYR A 167     -17.211 -17.278   3.735  1.00 15.32           O  
ATOM   1273  N   LEU A 168     -15.123 -17.349  10.156  1.00 14.39           N  
ATOM   1274  CA  LEU A 168     -14.690 -18.740  10.027  1.00 14.90           C  
ATOM   1275  C   LEU A 168     -15.446 -19.674  10.968  1.00 15.42           C  
ATOM   1276  O   LEU A 168     -15.826 -20.781  10.576  1.00 15.51           O  
ATOM   1277  CB  LEU A 168     -13.179 -18.865  10.242  1.00 14.80           C  
ATOM   1278  CG  LEU A 168     -12.251 -18.295   9.158  1.00 14.43           C  
ATOM   1279  CD1 LEU A 168     -10.805 -18.231   9.639  1.00 15.79           C  
ATOM   1280  CD2 LEU A 168     -12.358 -19.085   7.854  1.00 15.57           C  
ATOM   1281  N   THR A 169     -15.655 -19.228  12.205  1.00 16.03           N  
ATOM   1282  CA  THR A 169     -16.345 -20.050  13.205  1.00 16.83           C  
ATOM   1283  C   THR A 169     -17.850 -20.144  12.944  1.00 17.56           C  
ATOM   1284  O   THR A 169     -18.459 -21.185  13.196  1.00 17.83           O  
ATOM   1285  CB  THR A 169     -16.078 -19.561  14.641  1.00 16.67           C  
ATOM   1286  OG1 THR A 169     -16.498 -18.197  14.776  1.00 16.33           O  
ATOM   1287  CG2 THR A 169     -14.591 -19.672  14.963  1.00 17.09           C  
ATOM   1288  N   GLU A 170     -18.442 -19.067  12.432  1.00 17.83           N  
ATOM   1289  CA  GLU A 170     -19.865 -19.069  12.075  1.00 18.80           C  
ATOM   1290  C   GLU A 170     -20.135 -19.894  10.811  1.00 18.92           C  
ATOM   1291  O   GLU A 170     -21.156 -20.585  10.721  1.00 19.09           O  
ATOM   1292  CB  GLU A 170     -20.398 -17.640  11.923  1.00 18.61           C  
ATOM   1293  CG  GLU A 170     -21.906 -17.557  11.721  1.00 20.00           C  
ATOM   1294  CD  GLU A 170     -22.490 -16.185  12.023  1.00 19.81           C  
ATOM   1295  OE1 GLU A 170     -23.481 -15.827  11.361  1.00 22.48           O  
ATOM   1296  OE2 GLU A 170     -21.982 -15.472  12.917  1.00 21.85           O  
ATOM   1297  N   SER A 171     -19.214 -19.831   9.850  1.00 19.00           N  
ATOM   1298  CA  SER A 171     -19.387 -20.516   8.568  1.00 19.34           C  
ATOM   1299  C   SER A 171     -19.073 -22.008   8.626  1.00 20.15           C  
ATOM   1300  O   SER A 171     -19.787 -22.816   8.031  1.00 20.24           O  
ATOM   1301  CB  SER A 171     -18.528 -19.864   7.480  1.00 19.09           C  
ATOM   1302  OG  SER A 171     -18.847 -18.494   7.339  1.00 17.31           O  
ATOM   1303  N   TYR A 172     -18.004 -22.366   9.333  1.00 21.06           N  
ATOM   1304  CA  TYR A 172     -17.452 -23.719   9.236  1.00 22.27           C  
ATOM   1305  C   TYR A 172     -17.330 -24.447  10.576  1.00 22.85           C  
ATOM   1306  O   TYR A 172     -16.684 -25.496  10.671  1.00 22.92           O  
ATOM   1307  CB  TYR A 172     -16.127 -23.688   8.459  1.00 22.48           C  
ATOM   1308  CG  TYR A 172     -16.278 -23.038   7.095  1.00 23.16           C  
ATOM   1309  CD1 TYR A 172     -15.590 -21.866   6.771  1.00 23.41           C  
ATOM   1310  CD2 TYR A 172     -17.146 -23.577   6.142  1.00 23.54           C  
ATOM   1311  CE1 TYR A 172     -15.748 -21.262   5.514  1.00 23.31           C  
ATOM   1312  CE2 TYR A 172     -17.316 -22.981   4.896  1.00 23.64           C  
ATOM   1313  CZ  TYR A 172     -16.617 -21.830   4.586  1.00 23.55           C  
ATOM   1314  OH  TYR A 172     -16.796 -21.258   3.346  1.00 23.89           O  
ATOM   1315  N   GLY A 173     -17.988 -23.899  11.594  1.00 23.63           N  
ATOM   1316  CA  GLY A 173     -18.025 -24.501  12.925  1.00 24.57           C  
ATOM   1317  C   GLY A 173     -19.208 -25.433  13.104  1.00 25.15           C  
ATOM   1318  O   GLY A 173     -20.177 -25.382  12.340  1.00 26.22           O  
ATOM   1319  N   ASP A 180     -17.707 -20.303  18.044  1.00 28.14           N  
ATOM   1320  CA  ASP A 180     -18.426 -19.264  18.775  1.00 27.90           C  
ATOM   1321  C   ASP A 180     -17.760 -18.874  20.102  1.00 27.09           C  
ATOM   1322  O   ASP A 180     -17.735 -17.696  20.457  1.00 26.89           O  
ATOM   1323  CB  ASP A 180     -19.873 -19.682  19.015  1.00 28.50           C  
ATOM   1324  CG  ASP A 180     -20.719 -18.557  19.570  1.00 29.51           C  
ATOM   1325  OD1 ASP A 180     -21.208 -17.721  18.777  1.00 31.71           O  
ATOM   1326  OD2 ASP A 180     -20.908 -18.520  20.802  1.00 31.42           O  
ATOM   1327  N   ARG A 181     -17.240 -19.857  20.838  1.00 26.25           N  
ATOM   1328  CA  ARG A 181     -16.513 -19.568  22.077  1.00 25.45           C  
ATOM   1329  C   ARG A 181     -15.199 -18.841  21.796  1.00 24.90           C  
ATOM   1330  O   ARG A 181     -14.737 -18.047  22.617  1.00 24.35           O  
ATOM   1331  CB  ARG A 181     -16.272 -20.837  22.899  1.00 25.67           C  
ATOM   1332  CG  ARG A 181     -17.528 -21.357  23.593  1.00 26.16           C  
ATOM   1333  CD  ARG A 181     -17.203 -22.328  24.721  1.00 27.86           C  
ATOM   1334  NE  ARG A 181     -16.587 -23.557  24.229  1.00 28.86           N  
ATOM   1335  CZ  ARG A 181     -17.256 -24.650  23.868  1.00 29.78           C  
ATOM   1336  NH1 ARG A 181     -18.582 -24.684  23.942  1.00 30.18           N  
ATOM   1337  NH2 ARG A 181     -16.592 -25.713  23.433  1.00 29.95           N  
ATOM   1338  N   ILE A 182     -14.615 -19.113  20.629  1.00 24.14           N  
ATOM   1339  CA  ILE A 182     -13.441 -18.379  20.146  1.00 24.01           C  
ATOM   1340  C   ILE A 182     -13.764 -16.884  20.021  1.00 23.70           C  
ATOM   1341  O   ILE A 182     -12.957 -16.025  20.394  1.00 23.66           O  
ATOM   1342  CB  ILE A 182     -12.928 -18.957  18.797  1.00 23.94           C  
ATOM   1343  CG1 ILE A 182     -12.264 -20.322  19.026  1.00 24.58           C  
ATOM   1344  CG2 ILE A 182     -11.950 -17.990  18.130  1.00 24.40           C  
ATOM   1345  CD1 ILE A 182     -12.239 -21.248  17.816  1.00 24.64           C  
ATOM   1346  N   VAL A 183     -14.958 -16.593  19.508  1.00 23.24           N  
ATOM   1347  CA  VAL A 183     -15.463 -15.228  19.384  1.00 23.07           C  
ATOM   1348  C   VAL A 183     -15.801 -14.648  20.760  1.00 23.00           C  
ATOM   1349  O   VAL A 183     -15.415 -13.524  21.087  1.00 21.99           O  
ATOM   1350  CB  VAL A 183     -16.722 -15.192  18.472  1.00 23.21           C  
ATOM   1351  CG1 VAL A 183     -17.379 -13.810  18.473  1.00 23.46           C  
ATOM   1352  CG2 VAL A 183     -16.367 -15.627  17.061  1.00 23.12           C  
ATOM   1353  N   GLU A 184     -16.510 -15.438  21.563  1.00 23.20           N  
ATOM   1354  CA  GLU A 184     -17.036 -14.978  22.848  1.00 23.68           C  
ATOM   1355  C   GLU A 184     -15.952 -14.683  23.886  1.00 23.15           C  
ATOM   1356  O   GLU A 184     -16.173 -13.895  24.802  1.00 22.97           O  
ATOM   1357  CB  GLU A 184     -18.050 -15.986  23.401  1.00 24.09           C  
ATOM   1358  CG  GLU A 184     -19.415 -15.957  22.701  1.00 26.44           C  
ATOM   1359  CD  GLU A 184     -20.216 -14.694  22.997  1.00 29.46           C  
ATOM   1360  OE1 GLU A 184     -20.110 -14.156  24.121  1.00 31.25           O  
ATOM   1361  OE2 GLU A 184     -20.961 -14.241  22.100  1.00 31.76           O  
ATOM   1362  N   ALA A 185     -14.785 -15.308  23.731  1.00 22.85           N  
ATOM   1363  CA  ALA A 185     -13.685 -15.150  24.686  1.00 22.64           C  
ATOM   1364  C   ALA A 185     -12.956 -13.814  24.554  1.00 22.52           C  
ATOM   1365  O   ALA A 185     -12.193 -13.428  25.443  1.00 22.60           O  
ATOM   1366  CB  ALA A 185     -12.702 -16.306  24.553  1.00 22.73           C  
ATOM   1367  N   ASN A 186     -13.198 -13.106  23.454  1.00 22.06           N  
ATOM   1368  CA  ASN A 186     -12.455 -11.880  23.149  1.00 21.92           C  
ATOM   1369  C   ASN A 186     -12.513 -10.744  24.192  1.00 21.05           C  
ATOM   1370  O   ASN A 186     -11.469 -10.154  24.501  1.00 21.03           O  
ATOM   1371  CB  ASN A 186     -12.811 -11.352  21.760  1.00 22.62           C  
ATOM   1372  CG  ASN A 186     -11.653 -10.651  21.111  1.00 24.52           C  
ATOM   1373  OD1 ASN A 186     -10.744 -11.292  20.579  1.00 27.56           O  
ATOM   1374  ND2 ASN A 186     -11.660  -9.325  21.166  1.00 26.40           N  
ATOM   1375  N   PRO A 187     -13.717 -10.419  24.724  1.00 20.02           N  
ATOM   1376  CA  PRO A 187     -13.814  -9.428  25.803  1.00 19.36           C  
ATOM   1377  C   PRO A 187     -12.884  -9.697  26.991  1.00 18.59           C  
ATOM   1378  O   PRO A 187     -12.441  -8.755  27.646  1.00 18.46           O  
ATOM   1379  CB  PRO A 187     -15.277  -9.538  26.247  1.00 19.46           C  
ATOM   1380  CG  PRO A 187     -15.994  -9.966  25.019  1.00 19.75           C  
ATOM   1381  CD  PRO A 187     -15.056 -10.912  24.332  1.00 20.01           C  
ATOM   1382  N   LEU A 188     -12.593 -10.967  27.259  1.00 17.69           N  
ATOM   1383  CA  LEU A 188     -11.697 -11.335  28.352  1.00 17.20           C  
ATOM   1384  C   LEU A 188     -10.244 -10.959  28.046  1.00 16.12           C  
ATOM   1385  O   LEU A 188      -9.559 -10.360  28.880  1.00 15.78           O  
ATOM   1386  CB  LEU A 188     -11.827 -12.833  28.658  1.00 17.49           C  
ATOM   1387  CG  LEU A 188     -11.098 -13.445  29.851  1.00 18.49           C  
ATOM   1388  CD1 LEU A 188     -11.357 -12.650  31.113  1.00 20.08           C  
ATOM   1389  CD2 LEU A 188     -11.529 -14.902  30.026  1.00 18.19           C  
ATOM   1390  N   LEU A 189      -9.778 -11.301  26.847  1.00 15.14           N  
ATOM   1391  CA  LEU A 189      -8.414 -10.966  26.441  1.00 14.39           C  
ATOM   1392  C   LEU A 189      -8.224  -9.450  26.402  1.00 13.82           C  
ATOM   1393  O   LEU A 189      -7.232  -8.931  26.919  1.00 13.55           O  
ATOM   1394  CB  LEU A 189      -8.079 -11.577  25.074  1.00 14.73           C  
ATOM   1395  CG  LEU A 189      -8.041 -13.105  24.973  1.00 15.77           C  
ATOM   1396  CD1 LEU A 189      -7.662 -13.516  23.562  1.00 17.04           C  
ATOM   1397  CD2 LEU A 189      -7.065 -13.683  25.981  1.00 16.96           C  
ATOM   1398  N   GLU A 190      -9.187  -8.748  25.807  1.00 13.22           N  
ATOM   1399  CA  GLU A 190      -9.112  -7.285  25.697  1.00 13.24           C  
ATOM   1400  C   GLU A 190      -9.150  -6.581  27.053  1.00 12.59           C  
ATOM   1401  O   GLU A 190      -8.518  -5.540  27.232  1.00 11.90           O  
ATOM   1402  CB  GLU A 190     -10.212  -6.741  24.772  1.00 13.76           C  
ATOM   1403  CG  GLU A 190     -10.077  -7.255  23.351  1.00 15.79           C  
ATOM   1404  CD  GLU A 190     -10.778  -6.400  22.306  1.00 18.46           C  
ATOM   1405  OE1 GLU A 190     -11.519  -5.461  22.665  1.00 19.17           O  
ATOM   1406  OE2 GLU A 190     -10.573  -6.683  21.107  1.00 19.76           O  
ATOM   1407  N   ALA A 191      -9.884  -7.147  28.010  1.00 11.89           N  
ATOM   1408  CA  ALA A 191      -9.924  -6.556  29.345  1.00 11.45           C  
ATOM   1409  C   ALA A 191      -8.526  -6.543  29.970  1.00 10.80           C  
ATOM   1410  O   ALA A 191      -8.133  -5.561  30.592  1.00 10.71           O  
ATOM   1411  CB  ALA A 191     -10.899  -7.301  30.234  1.00 11.51           C  
ATOM   1412  N   PHE A 192      -7.778  -7.628  29.775  1.00 10.44           N  
ATOM   1413  CA  PHE A 192      -6.494  -7.807  30.458  1.00 10.40           C  
ATOM   1414  C   PHE A 192      -5.296  -7.328  29.646  1.00  9.97           C  
ATOM   1415  O   PHE A 192      -4.240  -7.031  30.208  1.00 10.06           O  
ATOM   1416  CB  PHE A 192      -6.313  -9.267  30.891  1.00 10.51           C  
ATOM   1417  CG  PHE A 192      -7.174  -9.652  32.061  1.00 11.48           C  
ATOM   1418  CD1 PHE A 192      -8.469 -10.131  31.859  1.00 12.19           C  
ATOM   1419  CD2 PHE A 192      -6.704  -9.502  33.368  1.00 12.08           C  
ATOM   1420  CE1 PHE A 192      -9.283 -10.468  32.943  1.00 11.85           C  
ATOM   1421  CE2 PHE A 192      -7.515  -9.840  34.461  1.00 12.22           C  
ATOM   1422  CZ  PHE A 192      -8.800 -10.320  34.245  1.00 11.76           C  
ATOM   1423  N   GLY A 193      -5.473  -7.230  28.330  1.00  9.50           N  
ATOM   1424  CA  GLY A 193      -4.358  -6.906  27.439  1.00  9.58           C  
ATOM   1425  C   GLY A 193      -4.458  -5.646  26.600  1.00  9.45           C  
ATOM   1426  O   GLY A 193      -3.509  -5.320  25.881  1.00  9.60           O  
ATOM   1427  N   ASN A 194      -5.596  -4.950  26.670  1.00  9.39           N  
ATOM   1428  CA  ASN A 194      -5.813  -3.711  25.908  1.00  9.31           C  
ATOM   1429  C   ASN A 194      -5.910  -2.501  26.833  1.00  9.68           C  
ATOM   1430  O   ASN A 194      -6.321  -2.630  28.003  1.00  9.15           O  
ATOM   1431  CB  ASN A 194      -7.079  -3.791  25.020  1.00  9.14           C  
ATOM   1432  CG  ASN A 194      -6.882  -4.634  23.752  1.00 10.10           C  
ATOM   1433  OD1 ASN A 194      -7.277  -4.223  22.655  1.00 11.91           O  
ATOM   1434  ND2 ASN A 194      -6.298  -5.810  23.899  1.00  8.98           N  
ATOM   1435  N   ALA A 195      -5.533  -1.335  26.309  1.00  9.77           N  
ATOM   1436  CA  ALA A 195      -5.530  -0.094  27.089  1.00  9.97           C  
ATOM   1437  C   ALA A 195      -5.678   1.151  26.224  1.00 10.43           C  
ATOM   1438  O   ALA A 195      -5.351   1.136  25.042  1.00 10.08           O  
ATOM   1439  CB  ALA A 195      -4.256   0.001  27.921  1.00 10.44           C  
ATOM   1440  N   LYS A 196      -6.162   2.230  26.833  1.00 10.42           N  
ATOM   1441  CA  LYS A 196      -6.197   3.529  26.174  1.00 10.75           C  
ATOM   1442  C   LYS A 196      -4.791   4.120  26.001  1.00 10.81           C  
ATOM   1443  O   LYS A 196      -4.079   4.372  26.983  1.00 10.59           O  
ATOM   1444  CB  LYS A 196      -7.096   4.500  26.951  1.00 11.12           C  
ATOM   1445  CG  LYS A 196      -7.210   5.889  26.320  1.00 11.31           C  
ATOM   1446  CD  LYS A 196      -7.729   6.914  27.331  1.00 13.53           C  
ATOM   1447  CE  LYS A 196      -8.175   8.205  26.644  1.00 14.27           C  
ATOM   1448  NZ  LYS A 196      -7.061   8.962  26.006  1.00 15.28           N  
ATOM   1449  N   THR A 197      -4.395   4.313  24.745  1.00 10.66           N  
ATOM   1450  CA  THR A 197      -3.245   5.157  24.406  1.00 11.13           C  
ATOM   1451  C   THR A 197      -3.759   6.367  23.627  1.00 11.60           C  
ATOM   1452  O   THR A 197      -4.926   6.397  23.226  1.00 11.72           O  
ATOM   1453  CB  THR A 197      -2.190   4.424  23.542  1.00 11.21           C  
ATOM   1454  OG1 THR A 197      -2.681   4.303  22.200  1.00 10.63           O  
ATOM   1455  CG2 THR A 197      -1.859   3.042  24.114  1.00 11.82           C  
ATOM   1456  N   VAL A 198      -2.900   7.357  23.394  1.00 11.84           N  
ATOM   1457  CA  VAL A 198      -3.346   8.529  22.642  1.00 12.53           C  
ATOM   1458  C   VAL A 198      -3.620   8.205  21.166  1.00 11.93           C  
ATOM   1459  O   VAL A 198      -4.286   8.986  20.483  1.00 12.03           O  
ATOM   1460  CB  VAL A 198      -2.420   9.779  22.792  1.00 12.96           C  
ATOM   1461  CG1 VAL A 198      -2.105  10.058  24.264  1.00 14.31           C  
ATOM   1462  CG2 VAL A 198      -1.168   9.647  21.976  1.00 13.78           C  
ATOM   1463  N   ARG A 199      -3.117   7.063  20.683  1.00 11.24           N  
ATOM   1464  CA  ARG A 199      -3.372   6.639  19.292  1.00 10.84           C  
ATOM   1465  C   ARG A 199      -4.613   5.761  19.129  1.00 10.45           C  
ATOM   1466  O   ARG A 199      -5.185   5.675  18.040  1.00 10.15           O  
ATOM   1467  CB  ARG A 199      -2.164   5.919  18.681  1.00 11.08           C  
ATOM   1468  CG  ARG A 199      -0.855   6.693  18.704  1.00 11.98           C  
ATOM   1469  CD  ARG A 199      -0.967   8.040  18.021  1.00 12.71           C  
ATOM   1470  NE  ARG A 199       0.301   8.765  18.062  1.00 13.32           N  
ATOM   1471  CZ  ARG A 199       0.435  10.071  17.845  1.00 15.30           C  
ATOM   1472  NH1 ARG A 199       1.642  10.630  17.902  1.00 15.55           N  
ATOM   1473  NH2 ARG A 199      -0.629  10.824  17.573  1.00 16.06           N  
ATOM   1474  N   ASN A 200      -5.018   5.097  20.210  1.00  9.91           N  
ATOM   1475  CA  ASN A 200      -6.093   4.116  20.153  1.00  9.32           C  
ATOM   1476  C   ASN A 200      -6.674   3.892  21.543  1.00  9.33           C  
ATOM   1477  O   ASN A 200      -5.974   3.437  22.454  1.00  9.06           O  
ATOM   1478  CB  ASN A 200      -5.553   2.794  19.579  1.00  9.70           C  
ATOM   1479  CG  ASN A 200      -6.640   1.765  19.308  1.00  9.35           C  
ATOM   1480  OD1 ASN A 200      -7.809   1.956  19.648  1.00  9.03           O  
ATOM   1481  ND2 ASN A 200      -6.240   0.640  18.705  1.00  9.60           N  
ATOM   1482  N   ASN A 201      -7.955   4.220  21.692  1.00  9.45           N  
ATOM   1483  CA  ASN A 201      -8.683   4.012  22.945  1.00  9.51           C  
ATOM   1484  C   ASN A 201      -8.694   2.542  23.372  1.00  9.51           C  
ATOM   1485  O   ASN A 201      -8.784   2.236  24.567  1.00  9.87           O  
ATOM   1486  CB  ASN A 201     -10.121   4.519  22.806  1.00  9.96           C  
ATOM   1487  CG  ASN A 201     -10.213   6.040  22.789  1.00 10.79           C  
ATOM   1488  OD1 ASN A 201      -9.405   6.730  23.405  1.00 12.47           O  
ATOM   1489  ND2 ASN A 201     -11.222   6.562  22.097  1.00 13.62           N  
ATOM   1490  N   ASN A 202      -8.603   1.648  22.388  1.00  9.20           N  
ATOM   1491  CA  ASN A 202      -8.589   0.215  22.624  1.00  9.36           C  
ATOM   1492  C   ASN A 202      -7.298  -0.452  22.128  1.00  9.41           C  
ATOM   1493  O   ASN A 202      -7.333  -1.506  21.497  1.00  9.53           O  
ATOM   1494  CB  ASN A 202      -9.817  -0.445  21.981  1.00  9.84           C  
ATOM   1495  CG  ASN A 202     -10.069  -1.855  22.508  1.00  9.59           C  
ATOM   1496  OD1 ASN A 202      -9.782  -2.155  23.670  1.00 11.57           O  
ATOM   1497  ND2 ASN A 202     -10.607  -2.720  21.658  1.00  9.89           N  
ATOM   1498  N   SER A 203      -6.158   0.167  22.426  1.00  9.43           N  
ATOM   1499  CA  SER A 203      -4.869  -0.324  21.945  1.00  9.35           C  
ATOM   1500  C   SER A 203      -4.513  -1.707  22.500  1.00  9.47           C  
ATOM   1501  O   SER A 203      -4.582  -1.934  23.711  1.00  9.91           O  
ATOM   1502  CB  SER A 203      -3.763   0.683  22.288  1.00  9.34           C  
ATOM   1503  OG  SER A 203      -2.526   0.317  21.700  1.00  9.17           O  
ATOM   1504  N   SER A 204      -4.128  -2.618  21.607  1.00  9.23           N  
ATOM   1505  CA  SER A 204      -3.586  -3.926  22.008  1.00  9.38           C  
ATOM   1506  C   SER A 204      -2.157  -3.743  22.520  1.00  9.35           C  
ATOM   1507  O   SER A 204      -1.280  -3.263  21.783  1.00  9.46           O  
ATOM   1508  CB  SER A 204      -3.564  -4.908  20.828  1.00  9.75           C  
ATOM   1509  OG  SER A 204      -4.810  -4.979  20.157  1.00  9.77           O  
ATOM   1510  N   ARG A 205      -1.917  -4.132  23.772  1.00  9.13           N  
ATOM   1511  CA  ARG A 205      -0.568  -4.054  24.355  1.00  9.11           C  
ATOM   1512  C   ARG A 205       0.088  -5.437  24.471  1.00  9.15           C  
ATOM   1513  O   ARG A 205       0.958  -5.678  25.321  1.00  8.81           O  
ATOM   1514  CB  ARG A 205      -0.573  -3.310  25.700  1.00  9.04           C  
ATOM   1515  CG  ARG A 205      -1.375  -1.999  25.714  1.00  9.00           C  
ATOM   1516  CD  ARG A 205      -1.050  -1.088  24.530  1.00  8.75           C  
ATOM   1517  NE  ARG A 205       0.317  -0.570  24.584  1.00 10.34           N  
ATOM   1518  CZ  ARG A 205       0.902   0.099  23.594  1.00 10.99           C  
ATOM   1519  NH1 ARG A 205       0.244   0.343  22.462  1.00  9.60           N  
ATOM   1520  NH2 ARG A 205       2.147   0.532  23.738  1.00 10.51           N  
ATOM   1521  N   PHE A 206      -0.341  -6.331  23.588  1.00  9.16           N  
ATOM   1522  CA  PHE A 206       0.259  -7.645  23.415  1.00  9.59           C  
ATOM   1523  C   PHE A 206      -0.001  -8.071  21.980  1.00 10.12           C  
ATOM   1524  O   PHE A 206      -0.887  -7.521  21.312  1.00 10.39           O  
ATOM   1525  CB  PHE A 206      -0.339  -8.662  24.404  1.00  9.29           C  
ATOM   1526  CG  PHE A 206      -1.769  -9.044  24.100  1.00  9.00           C  
ATOM   1527  CD1 PHE A 206      -2.076 -10.297  23.567  1.00  9.36           C  
ATOM   1528  CD2 PHE A 206      -2.809  -8.145  24.340  1.00  8.33           C  
ATOM   1529  CE1 PHE A 206      -3.407 -10.641  23.278  1.00  8.78           C  
ATOM   1530  CE2 PHE A 206      -4.131  -8.480  24.056  1.00 10.45           C  
ATOM   1531  CZ  PHE A 206      -4.431  -9.726  23.527  1.00  9.14           C  
ATOM   1532  N   GLY A 207       0.759  -9.048  21.510  1.00 10.38           N  
ATOM   1533  CA  GLY A 207       0.524  -9.613  20.187  1.00 10.33           C  
ATOM   1534  C   GLY A 207      -0.165 -10.953  20.324  1.00 11.07           C  
ATOM   1535  O   GLY A 207      -0.048 -11.617  21.356  1.00 10.91           O  
ATOM   1536  N   LYS A 208      -0.885 -11.356  19.285  1.00 11.28           N  
ATOM   1537  CA  LYS A 208      -1.515 -12.667  19.289  1.00 12.09           C  
ATOM   1538  C   LYS A 208      -1.562 -13.313  17.910  1.00 11.92           C  
ATOM   1539  O   LYS A 208      -1.663 -12.635  16.882  1.00 11.23           O  
ATOM   1540  CB  LYS A 208      -2.917 -12.606  19.916  1.00 12.25           C  
ATOM   1541  CG  LYS A 208      -3.955 -11.872  19.098  1.00 13.30           C  
ATOM   1542  CD  LYS A 208      -5.310 -11.866  19.783  1.00 13.56           C  
ATOM   1543  CE  LYS A 208      -6.359 -11.323  18.835  1.00 16.13           C  
ATOM   1544  NZ  LYS A 208      -7.716 -11.397  19.438  1.00 20.16           N  
ATOM   1545  N   PHE A 209      -1.463 -14.637  17.917  1.00 12.03           N  
ATOM   1546  CA  PHE A 209      -1.698 -15.449  16.739  1.00 12.39           C  
ATOM   1547  C   PHE A 209      -2.802 -16.419  17.141  1.00 12.68           C  
ATOM   1548  O   PHE A 209      -2.593 -17.273  18.002  1.00 12.96           O  
ATOM   1549  CB  PHE A 209      -0.425 -16.196  16.339  1.00 12.54           C  
ATOM   1550  CG  PHE A 209      -0.507 -16.867  14.989  1.00 12.84           C  
ATOM   1551  CD1 PHE A 209      -0.783 -16.126  13.844  1.00 13.83           C  
ATOM   1552  CD2 PHE A 209      -0.283 -18.234  14.863  1.00 13.91           C  
ATOM   1553  CE1 PHE A 209      -0.858 -16.739  12.594  1.00 13.97           C  
ATOM   1554  CE2 PHE A 209      -0.349 -18.855  13.618  1.00 13.60           C  
ATOM   1555  CZ  PHE A 209      -0.639 -18.109  12.482  1.00 14.02           C  
ATOM   1556  N   VAL A 210      -3.983 -16.245  16.554  1.00 12.51           N  
ATOM   1557  CA  VAL A 210      -5.146 -17.068  16.889  1.00 12.96           C  
ATOM   1558  C   VAL A 210      -5.346 -18.125  15.806  1.00 13.40           C  
ATOM   1559  O   VAL A 210      -5.630 -17.795  14.647  1.00 12.99           O  
ATOM   1560  CB  VAL A 210      -6.439 -16.222  17.060  1.00 13.00           C  
ATOM   1561  CG1 VAL A 210      -7.612 -17.100  17.501  1.00 13.07           C  
ATOM   1562  CG2 VAL A 210      -6.218 -15.100  18.059  1.00 13.11           C  
ATOM   1563  N   GLU A 211      -5.187 -19.389  16.197  1.00 13.82           N  
ATOM   1564  CA  GLU A 211      -5.346 -20.516  15.280  1.00 14.78           C  
ATOM   1565  C   GLU A 211      -6.717 -21.164  15.424  1.00 14.78           C  
ATOM   1566  O   GLU A 211      -7.131 -21.513  16.533  1.00 14.52           O  
ATOM   1567  CB  GLU A 211      -4.266 -21.576  15.522  1.00 14.90           C  
ATOM   1568  CG  GLU A 211      -2.841 -21.131  15.206  1.00 15.70           C  
ATOM   1569  CD  GLU A 211      -1.783 -22.081  15.760  1.00 16.37           C  
ATOM   1570  OE1 GLU A 211      -2.081 -23.282  15.947  1.00 18.17           O  
ATOM   1571  OE2 GLU A 211      -0.646 -21.624  16.009  1.00 18.63           O  
ATOM   1572  N   ILE A 212      -7.416 -21.287  14.300  1.00 14.87           N  
ATOM   1573  C   ILE A 212      -8.301 -23.399  13.598  1.00 15.55           C  
ATOM   1574  O   ILE A 212      -7.815 -23.449  12.464  1.00 15.04           O  
ATOM   1575  CA AILE A 212      -8.648 -22.066  14.245  0.50 15.11           C  
ATOM   1576  CB AILE A 212      -9.786 -21.346  13.475  0.50 15.16           C  
ATOM   1577  CG1AILE A 212     -10.184 -20.048  14.191  0.50 15.03           C  
ATOM   1578  CG2AILE A 212     -11.004 -22.273  13.322  0.50 15.08           C  
ATOM   1579  CD1AILE A 212     -11.127 -19.155  13.393  0.50 14.92           C  
ATOM   1581  CB BILE A 212      -9.730 -21.345  13.353  0.50 15.23           C  
ATOM   1582  CG1BILE A 212      -9.918 -19.882  13.786  0.50 15.27           C  
ATOM   1583  CG2BILE A 212     -11.058 -22.126  13.364  0.50 15.21           C  
ATOM   1584  CD1BILE A 212     -10.376 -19.696  15.218  0.50 15.09           C  
ATOM   1585  N   HIS A 213      -8.532 -24.475  14.341  1.00 15.86           N  
ATOM   1586  CA  HIS A 213      -8.129 -25.797  13.894  1.00 16.78           C  
ATOM   1587  C   HIS A 213      -9.278 -26.586  13.288  1.00 17.46           C  
ATOM   1588  O   HIS A 213     -10.411 -26.523  13.765  1.00 17.28           O  
ATOM   1589  CB  HIS A 213      -7.447 -26.558  15.030  1.00 16.57           C  
ATOM   1590  CG  HIS A 213      -6.031 -26.131  15.259  1.00 16.81           C  
ATOM   1591  ND1 HIS A 213      -4.950 -26.905  14.893  1.00 16.85           N  
ATOM   1592  CD2 HIS A 213      -5.518 -24.999  15.798  1.00 16.59           C  
ATOM   1593  CE1 HIS A 213      -3.833 -26.273  15.205  1.00 16.94           C  
ATOM   1594  NE2 HIS A 213      -4.150 -25.112  15.752  1.00 16.84           N  
ATOM   1595  N   PHE A 214      -8.953 -27.321  12.226  1.00 18.79           N  
ATOM   1596  CA  PHE A 214      -9.932 -28.040  11.421  1.00 19.88           C  
ATOM   1597  C   PHE A 214      -9.615 -29.526  11.347  1.00 21.04           C  
ATOM   1598  O   PHE A 214      -8.447 -29.925  11.409  1.00 21.42           O  
ATOM   1599  CB  PHE A 214      -9.955 -27.482   9.996  1.00 19.50           C  
ATOM   1600  CG  PHE A 214     -10.443 -26.064   9.899  1.00 18.92           C  
ATOM   1601  CD1 PHE A 214      -9.581 -24.996  10.146  1.00 18.15           C  
ATOM   1602  CD2 PHE A 214     -11.760 -25.797   9.548  1.00 17.91           C  
ATOM   1603  CE1 PHE A 214     -10.027 -23.682  10.050  1.00 18.06           C  
ATOM   1604  CE2 PHE A 214     -12.220 -24.483   9.448  1.00 18.59           C  
ATOM   1605  CZ  PHE A 214     -11.348 -23.423   9.702  1.00 18.39           C  
ATOM   1606  N   ASN A 215     -10.662 -30.333  11.194  1.00 22.54           N  
ATOM   1607  CA  ASN A 215     -10.502 -31.758  10.910  1.00 24.19           C  
ATOM   1608  C   ASN A 215     -10.375 -32.051   9.413  1.00 25.02           C  
ATOM   1609  O   ASN A 215     -10.284 -31.133   8.592  1.00 24.84           O  
ATOM   1610  CB  ASN A 215     -11.623 -32.597  11.562  1.00 24.25           C  
ATOM   1611  CG  ASN A 215     -13.031 -32.214  11.087  1.00 25.21           C  
ATOM   1612  OD1 ASN A 215     -13.230 -31.703   9.981  1.00 25.73           O  
ATOM   1613  ND2 ASN A 215     -14.020 -32.488  11.934  1.00 26.21           N  
ATOM   1614  N   GLU A 216     -10.367 -33.340   9.075  1.00 26.23           N  
ATOM   1615  CA  GLU A 216     -10.240 -33.816   7.696  1.00 27.33           C  
ATOM   1616  C   GLU A 216     -11.433 -33.440   6.818  1.00 27.61           C  
ATOM   1617  O   GLU A 216     -11.301 -33.345   5.597  1.00 27.97           O  
ATOM   1618  CB  GLU A 216     -10.012 -35.338   7.675  1.00 27.62           C  
ATOM   1619  CG  GLU A 216     -11.032 -36.174   8.479  1.00 29.42           C  
ATOM   1620  CD  GLU A 216     -10.901 -36.010   9.993  1.00 31.83           C  
ATOM   1621  OE1 GLU A 216      -9.797 -35.670  10.477  1.00 33.28           O  
ATOM   1622  OE2 GLU A 216     -11.908 -36.224  10.703  1.00 32.81           O  
ATOM   1623  N   LYS A 217     -12.590 -33.231   7.447  1.00 27.94           N  
ATOM   1624  CA  LYS A 217     -13.793 -32.766   6.758  1.00 28.25           C  
ATOM   1625  C   LYS A 217     -13.826 -31.239   6.652  1.00 28.06           C  
ATOM   1626  O   LYS A 217     -14.797 -30.667   6.148  1.00 28.19           O  
ATOM   1627  CB  LYS A 217     -15.056 -33.261   7.473  1.00 28.51           C  
ATOM   1628  CG  LYS A 217     -15.284 -34.766   7.405  1.00 29.77           C  
ATOM   1629  CD  LYS A 217     -16.762 -35.101   7.571  1.00 31.65           C  
ATOM   1630  CE  LYS A 217     -17.018 -36.603   7.478  1.00 33.15           C  
ATOM   1631  NZ  LYS A 217     -16.713 -37.313   8.756  1.00 33.96           N  
ATOM   1632  N   SER A 218     -12.761 -30.598   7.136  1.00 27.76           N  
ATOM   1633  CA  SER A 218     -12.629 -29.135   7.164  1.00 27.41           C  
ATOM   1634  C   SER A 218     -13.715 -28.463   8.008  1.00 26.84           C  
ATOM   1635  O   SER A 218     -14.288 -27.438   7.622  1.00 27.01           O  
ATOM   1636  CB  SER A 218     -12.579 -28.554   5.748  1.00 27.43           C  
ATOM   1637  OG  SER A 218     -11.550 -29.163   4.996  1.00 28.13           O  
ATOM   1638  N   SER A 219     -13.989 -29.061   9.163  1.00 26.07           N  
ATOM   1639  CA  SER A 219     -14.908 -28.496  10.141  1.00 25.40           C  
ATOM   1640  C   SER A 219     -14.119 -28.114  11.396  1.00 24.46           C  
ATOM   1641  O   SER A 219     -13.179 -28.814  11.777  1.00 24.38           O  
ATOM   1642  CB  SER A 219     -16.010 -29.505  10.477  1.00 25.56           C  
ATOM   1643  OG  SER A 219     -17.006 -28.922  11.296  1.00 26.79           O  
ATOM   1644  N   VAL A 220     -14.499 -27.002  12.021  1.00 23.71           N  
ATOM   1645  CA  VAL A 220     -13.797 -26.484  13.208  1.00 22.77           C  
ATOM   1646  C   VAL A 220     -13.875 -27.464  14.383  1.00 22.37           C  
ATOM   1647  O   VAL A 220     -14.966 -27.892  14.772  1.00 22.43           O  
ATOM   1648  CB  VAL A 220     -14.352 -25.097  13.642  1.00 23.01           C  
ATOM   1649  CG1 VAL A 220     -13.652 -24.590  14.904  1.00 22.57           C  
ATOM   1650  CG2 VAL A 220     -14.217 -24.081  12.511  1.00 22.50           C  
ATOM   1651  N   VAL A 221     -12.714 -27.815  14.934  1.00 21.51           N  
ATOM   1652  CA  VAL A 221     -12.637 -28.705  16.102  1.00 20.67           C  
ATOM   1653  C   VAL A 221     -12.261 -27.973  17.393  1.00 20.03           C  
ATOM   1654  O   VAL A 221     -12.550 -28.444  18.498  1.00 19.97           O  
ATOM   1655  CB  VAL A 221     -11.672 -29.904  15.874  1.00 20.53           C  
ATOM   1656  CG1 VAL A 221     -12.183 -30.796  14.746  1.00 20.68           C  
ATOM   1657  CG2 VAL A 221     -10.235 -29.437  15.608  1.00 20.64           C  
ATOM   1658  N   GLY A 222     -11.623 -26.814  17.247  1.00 19.12           N  
ATOM   1659  CA  GLY A 222     -11.168 -26.040  18.393  1.00 18.06           C  
ATOM   1660  C   GLY A 222     -10.266 -24.903  17.963  1.00 17.21           C  
ATOM   1661  O   GLY A 222     -10.171 -24.586  16.773  1.00 16.66           O  
ATOM   1662  N   GLY A 223      -9.604 -24.289  18.935  1.00 16.75           N  
ATOM   1663  CA  GLY A 223      -8.734 -23.153  18.658  1.00 16.29           C  
ATOM   1664  C   GLY A 223      -7.549 -23.070  19.597  1.00 16.03           C  
ATOM   1665  O   GLY A 223      -7.479 -23.781  20.602  1.00 15.78           O  
ATOM   1666  N   PHE A 224      -6.604 -22.200  19.260  1.00 15.53           N  
ATOM   1667  CA  PHE A 224      -5.479 -21.937  20.141  1.00 15.23           C  
ATOM   1668  C   PHE A 224      -4.979 -20.519  19.952  1.00 15.12           C  
ATOM   1669  O   PHE A 224      -4.678 -20.103  18.829  1.00 15.08           O  
ATOM   1670  CB  PHE A 224      -4.335 -22.918  19.908  1.00 15.32           C  
ATOM   1671  CG  PHE A 224      -3.286 -22.880  20.984  1.00 15.62           C  
ATOM   1672  CD1 PHE A 224      -3.426 -23.651  22.136  1.00 16.97           C  
ATOM   1673  CD2 PHE A 224      -2.168 -22.059  20.858  1.00 15.59           C  
ATOM   1674  CE1 PHE A 224      -2.459 -23.610  23.137  1.00 16.83           C  
ATOM   1675  CE2 PHE A 224      -1.198 -22.014  21.854  1.00 16.56           C  
ATOM   1676  CZ  PHE A 224      -1.348 -22.793  22.996  1.00 16.75           C  
ATOM   1677  N   VAL A 225      -4.896 -19.794  21.062  1.00 14.69           N  
ATOM   1678  CA  VAL A 225      -4.383 -18.432  21.064  1.00 14.49           C  
ATOM   1679  C   VAL A 225      -2.962 -18.432  21.620  1.00 14.61           C  
ATOM   1680  O   VAL A 225      -2.744 -18.813  22.775  1.00 14.36           O  
ATOM   1681  CB  VAL A 225      -5.262 -17.476  21.910  1.00 14.22           C  
ATOM   1682  CG1 VAL A 225      -4.707 -16.042  21.852  1.00 14.38           C  
ATOM   1683  CG2 VAL A 225      -6.714 -17.510  21.448  1.00 14.70           C  
ATOM   1684  N   SER A 226      -2.002 -18.033  20.786  1.00 14.71           N  
ATOM   1685  CA  SER A 226      -0.646 -17.754  21.245  1.00 14.97           C  
ATOM   1686  C   SER A 226      -0.558 -16.267  21.524  1.00 15.14           C  
ATOM   1687  O   SER A 226      -0.982 -15.453  20.703  1.00 15.04           O  
ATOM   1688  CB  SER A 226       0.400 -18.149  20.195  1.00 15.05           C  
ATOM   1689  OG  SER A 226       0.424 -19.554  19.995  1.00 16.19           O  
ATOM   1690  N   HIS A 227      -0.038 -15.913  22.693  1.00 15.21           N  
ATOM   1691  CA  HIS A 227       0.083 -14.506  23.067  1.00 15.27           C  
ATOM   1692  C   HIS A 227       1.541 -14.130  23.274  1.00 15.72           C  
ATOM   1693  O   HIS A 227       2.363 -14.964  23.689  1.00 15.97           O  
ATOM   1694  CB  HIS A 227      -0.742 -14.207  24.320  1.00 15.43           C  
ATOM   1695  CG  HIS A 227      -0.162 -14.785  25.570  1.00 15.48           C  
ATOM   1696  ND1 HIS A 227      -0.209 -16.132  25.853  1.00 15.31           N  
ATOM   1697  CD2 HIS A 227       0.483 -14.203  26.608  1.00 16.44           C  
ATOM   1698  CE1 HIS A 227       0.384 -16.357  27.013  1.00 16.30           C  
ATOM   1699  NE2 HIS A 227       0.815 -15.203  27.490  1.00 16.98           N  
ATOM   1700  N   TYR A 228       1.851 -12.870  22.988  1.00 15.48           N  
ATOM   1701  CA  TYR A 228       3.226 -12.403  22.936  1.00 15.81           C  
ATOM   1702  C   TYR A 228       3.415 -11.045  23.590  1.00 15.24           C  
ATOM   1703  O   TYR A 228       2.671 -10.101  23.325  1.00 14.73           O  
ATOM   1704  CB  TYR A 228       3.708 -12.316  21.480  1.00 16.64           C  
ATOM   1705  CG  TYR A 228       3.645 -13.620  20.724  1.00 17.92           C  
ATOM   1706  CD1 TYR A 228       2.552 -13.926  19.912  1.00 18.82           C  
ATOM   1707  CD2 TYR A 228       4.677 -14.558  20.823  1.00 19.12           C  
ATOM   1708  CE1 TYR A 228       2.486 -15.132  19.224  1.00 19.56           C  
ATOM   1709  CE2 TYR A 228       4.621 -15.764  20.132  1.00 19.76           C  
ATOM   1710  CZ  TYR A 228       3.525 -16.041  19.337  1.00 19.20           C  
ATOM   1711  OH  TYR A 228       3.460 -17.233  18.655  1.00 19.57           O  
ATOM   1712  N   LEU A 229       4.425 -10.966  24.449  1.00 14.49           N  
ATOM   1713  CA  LEU A 229       5.074  -9.701  24.778  1.00 14.06           C  
ATOM   1714  C   LEU A 229       4.121  -8.636  25.346  1.00 13.43           C  
ATOM   1715  O   LEU A 229       4.017  -7.516  24.830  1.00 13.62           O  
ATOM   1716  CB  LEU A 229       5.852  -9.195  23.546  1.00 14.61           C  
ATOM   1717  CG  LEU A 229       6.789 -10.263  22.935  1.00 15.10           C  
ATOM   1718  CD1 LEU A 229       7.049 -10.054  21.433  1.00 15.86           C  
ATOM   1719  CD2 LEU A 229       8.102 -10.355  23.711  1.00 15.12           C  
ATOM   1720  N   LEU A 230       3.411  -9.005  26.411  1.00 12.53           N  
ATOM   1721  CA  LEU A 230       2.591  -8.042  27.143  1.00 12.06           C  
ATOM   1722  C   LEU A 230       3.447  -6.867  27.622  1.00 12.29           C  
ATOM   1723  O   LEU A 230       4.565  -7.064  28.111  1.00 12.08           O  
ATOM   1724  CB  LEU A 230       1.915  -8.714  28.346  1.00 11.78           C  
ATOM   1725  CG  LEU A 230       0.947  -7.853  29.163  1.00 11.26           C  
ATOM   1726  CD1 LEU A 230      -0.345  -7.581  28.378  1.00 10.52           C  
ATOM   1727  CD2 LEU A 230       0.649  -8.540  30.495  1.00 11.40           C  
ATOM   1728  N   GLU A 231       2.914  -5.657  27.478  1.00 12.49           N  
ATOM   1729  CA  GLU A 231       3.585  -4.434  27.932  1.00 13.43           C  
ATOM   1730  C   GLU A 231       3.523  -4.311  29.457  1.00 13.97           C  
ATOM   1731  O   GLU A 231       2.514  -3.880  30.020  1.00 14.14           O  
ATOM   1732  CB  GLU A 231       2.949  -3.213  27.267  1.00 12.96           C  
ATOM   1733  CG  GLU A 231       3.693  -1.899  27.511  1.00 13.24           C  
ATOM   1734  CD  GLU A 231       3.080  -0.732  26.754  1.00 14.42           C  
ATOM   1735  OE1 GLU A 231       1.875  -0.454  26.924  1.00 14.47           O  
ATOM   1736  OE2 GLU A 231       3.814  -0.084  25.984  1.00 16.59           O  
ATOM   1737  N   LYS A 232       4.615  -4.678  30.122  1.00 14.94           N  
ATOM   1738  CA  LYS A 232       4.611  -4.757  31.587  1.00 15.60           C  
ATOM   1739  C   LYS A 232       4.691  -3.411  32.311  1.00 15.28           C  
ATOM   1740  O   LYS A 232       4.131  -3.254  33.400  1.00 15.12           O  
ATOM   1741  CB  LYS A 232       5.672  -5.756  32.082  1.00 15.72           C  
ATOM   1742  CG  LYS A 232       5.350  -7.209  31.702  1.00 15.91           C  
ATOM   1743  CD  LYS A 232       6.406  -8.193  32.206  1.00 17.46           C  
ATOM   1744  CE  LYS A 232       6.312  -9.514  31.454  1.00 19.62           C  
ATOM   1745  NZ  LYS A 232       7.336 -10.492  31.906  1.00 22.28           N  
ATOM   1746  N   SER A 233       5.351  -2.428  31.703  1.00 15.06           N  
ATOM   1747  CA  SER A 233       5.501  -1.111  32.323  1.00 15.25           C  
ATOM   1748  C   SER A 233       4.164  -0.432  32.616  1.00 14.76           C  
ATOM   1749  O   SER A 233       4.039   0.296  33.607  1.00 14.97           O  
ATOM   1750  CB  SER A 233       6.358  -0.198  31.450  1.00 15.79           C  
ATOM   1751  OG  SER A 233       5.747  -0.007  30.186  1.00 16.44           O  
ATOM   1752  N   ARG A 234       3.169  -0.693  31.761  1.00 14.02           N  
ATOM   1753  CA  ARG A 234       1.842  -0.078  31.870  1.00 13.41           C  
ATOM   1754  C   ARG A 234       1.131  -0.449  33.169  1.00 13.24           C  
ATOM   1755  O   ARG A 234       0.302   0.309  33.668  1.00 13.33           O  
ATOM   1756  CB  ARG A 234       0.966  -0.480  30.683  1.00 13.21           C  
ATOM   1757  CG  ARG A 234      -0.413   0.199  30.649  1.00 12.49           C  
ATOM   1758  CD  ARG A 234      -1.053   0.069  29.284  1.00 12.24           C  
ATOM   1759  NE  ARG A 234      -0.188   0.635  28.259  1.00 11.25           N  
ATOM   1760  CZ  ARG A 234      -0.264   1.882  27.796  1.00 11.12           C  
ATOM   1761  NH1 ARG A 234       0.594   2.287  26.864  1.00 11.68           N  
ATOM   1762  NH2 ARG A 234      -1.205   2.712  28.231  1.00 11.49           N  
ATOM   1763  N   ILE A 235       1.454  -1.626  33.694  1.00 13.19           N  
ATOM   1764  CA  ILE A 235       0.864  -2.113  34.942  1.00 13.45           C  
ATOM   1765  C   ILE A 235       1.051  -1.118  36.093  1.00 13.62           C  
ATOM   1766  O   ILE A 235       0.163  -0.973  36.938  1.00 13.62           O  
ATOM   1767  CB  ILE A 235       1.421  -3.518  35.305  1.00 13.37           C  
ATOM   1768  CG1 ILE A 235       1.179  -4.492  34.136  1.00 13.39           C  
ATOM   1769  CG2 ILE A 235       0.815  -4.038  36.624  1.00 13.36           C  
ATOM   1770  CD1 ILE A 235       2.044  -5.731  34.158  1.00 12.52           C  
ATOM   1771  N   CYS A 236       2.186  -0.417  36.100  1.00 13.96           N  
ATOM   1772  CA  CYS A 236       2.548   0.456  37.221  1.00 14.65           C  
ATOM   1773  C   CYS A 236       2.405   1.957  36.956  1.00 14.91           C  
ATOM   1774  O   CYS A 236       2.067   2.717  37.864  1.00 15.46           O  
ATOM   1775  CB  CYS A 236       3.964   0.133  37.713  1.00 14.43           C  
ATOM   1776  SG  CYS A 236       4.195  -1.577  38.201  1.00 16.12           S  
ATOM   1777  N   VAL A 237       2.650   2.388  35.719  1.00 14.63           N  
ATOM   1778  CA  VAL A 237       2.600   3.814  35.398  1.00 15.18           C  
ATOM   1779  C   VAL A 237       2.122   4.081  33.967  1.00 14.95           C  
ATOM   1780  O   VAL A 237       2.362   3.279  33.065  1.00 14.55           O  
ATOM   1781  CB  VAL A 237       3.972   4.511  35.667  1.00 15.24           C  
ATOM   1782  CG1 VAL A 237       5.031   4.078  34.635  1.00 16.28           C  
ATOM   1783  CG2 VAL A 237       3.826   6.042  35.727  1.00 16.36           C  
ATOM   1784  N   GLN A 238       1.428   5.207  33.795  1.00 15.04           N  
ATOM   1785  CA  GLN A 238       0.957   5.674  32.488  1.00 15.70           C  
ATOM   1786  C   GLN A 238       1.080   7.193  32.392  1.00 16.35           C  
ATOM   1787  O   GLN A 238       1.160   7.882  33.413  1.00 16.97           O  
ATOM   1788  CB  GLN A 238      -0.511   5.283  32.249  1.00 15.38           C  
ATOM   1789  CG  GLN A 238      -0.924   3.882  32.740  1.00 14.10           C  
ATOM   1790  CD  GLN A 238      -1.163   3.825  34.244  1.00 14.59           C  
ATOM   1791  OE1 GLN A 238      -1.649   4.782  34.850  1.00 13.66           O  
ATOM   1792  NE2 GLN A 238      -0.821   2.694  34.850  1.00 13.95           N  
ATOM   1793  N   GLY A 239       1.079   7.706  31.161  1.00 17.07           N  
ATOM   1794  CA  GLY A 239       0.993   9.147  30.911  1.00 17.77           C  
ATOM   1795  C   GLY A 239      -0.414   9.661  31.176  1.00 18.08           C  
ATOM   1796  O   GLY A 239      -1.377   8.883  31.201  1.00 18.46           O  
ATOM   1797  N   LYS A 240      -0.543  10.973  31.360  1.00 18.51           N  
ATOM   1798  CA  LYS A 240      -1.818  11.589  31.754  1.00 18.69           C  
ATOM   1799  C   LYS A 240      -2.990  11.426  30.776  1.00 18.47           C  
ATOM   1800  O   LYS A 240      -4.150  11.563  31.171  1.00 18.14           O  
ATOM   1801  CB  LYS A 240      -1.624  13.070  32.084  1.00 19.28           C  
ATOM   1802  CG  LYS A 240      -1.073  13.299  33.466  1.00 21.38           C  
ATOM   1803  CD  LYS A 240      -1.591  14.602  34.049  1.00 24.45           C  
ATOM   1804  CE  LYS A 240      -1.238  14.727  35.528  1.00 25.90           C  
ATOM   1805  NZ  LYS A 240       0.229  14.624  35.761  1.00 27.91           N  
ATOM   1806  N   GLU A 241      -2.687  11.149  29.509  1.00 17.94           N  
ATOM   1807  CA  GLU A 241      -3.725  10.920  28.508  1.00 18.09           C  
ATOM   1808  C   GLU A 241      -3.984   9.430  28.274  1.00 17.02           C  
ATOM   1809  O   GLU A 241      -4.788   9.060  27.416  1.00 17.18           O  
ATOM   1810  CB  GLU A 241      -3.357  11.592  27.181  1.00 18.65           C  
ATOM   1811  CG  GLU A 241      -3.619  13.091  27.123  1.00 22.24           C  
ATOM   1812  CD  GLU A 241      -3.814  13.580  25.700  1.00 26.42           C  
ATOM   1813  OE1 GLU A 241      -4.979  13.807  25.310  1.00 29.24           O  
ATOM   1814  OE2 GLU A 241      -2.811  13.710  24.960  1.00 29.06           O  
ATOM   1815  N   GLU A 242      -3.304   8.578  29.032  1.00 15.69           N  
ATOM   1816  CA  GLU A 242      -3.400   7.133  28.815  1.00 14.55           C  
ATOM   1817  C   GLU A 242      -3.923   6.428  30.061  1.00 13.76           C  
ATOM   1818  O   GLU A 242      -4.036   7.044  31.124  1.00 13.98           O  
ATOM   1819  CB  GLU A 242      -2.050   6.568  28.366  1.00 14.73           C  
ATOM   1820  CG  GLU A 242      -1.548   7.201  27.052  1.00 15.28           C  
ATOM   1821  CD  GLU A 242      -0.572   6.332  26.282  1.00 17.71           C  
ATOM   1822  OE1 GLU A 242      -0.131   5.282  26.814  1.00 16.28           O  
ATOM   1823  OE2 GLU A 242      -0.247   6.711  25.128  1.00 17.53           O  
ATOM   1824  N   ARG A 243      -4.268   5.150  29.920  1.00 12.73           N  
ATOM   1825  CA  ARG A 243      -4.758   4.369  31.053  1.00 11.46           C  
ATOM   1826  C   ARG A 243      -4.017   3.055  31.201  1.00 11.00           C  
ATOM   1827  O   ARG A 243      -3.336   2.600  30.278  1.00 10.20           O  
ATOM   1828  CB  ARG A 243      -6.253   4.070  30.919  1.00 11.73           C  
ATOM   1829  CG  ARG A 243      -7.138   5.277  30.709  1.00 11.30           C  
ATOM   1830  CD  ARG A 243      -8.571   4.981  31.124  1.00 13.25           C  
ATOM   1831  NE  ARG A 243      -9.092   3.736  30.560  1.00 11.93           N  
ATOM   1832  CZ  ARG A 243     -10.358   3.342  30.658  1.00 13.18           C  
ATOM   1833  NH1 ARG A 243     -11.254   4.112  31.268  1.00 11.80           N  
ATOM   1834  NH2 ARG A 243     -10.735   2.183  30.135  1.00 11.83           N  
ATOM   1835  N   ASN A 244      -4.161   2.452  32.380  1.00 10.36           N  
ATOM   1836  CA  ASN A 244      -3.740   1.072  32.602  1.00 10.10           C  
ATOM   1837  C   ASN A 244      -4.682   0.156  31.816  1.00  9.76           C  
ATOM   1838  O   ASN A 244      -5.565   0.644  31.094  1.00 10.23           O  
ATOM   1839  CB  ASN A 244      -3.802   0.765  34.098  1.00  9.72           C  
ATOM   1840  CG  ASN A 244      -2.809  -0.292  34.528  1.00  9.84           C  
ATOM   1841  OD1 ASN A 244      -2.543  -1.254  33.803  1.00  8.96           O  
ATOM   1842  ND2 ASN A 244      -2.260  -0.124  35.735  1.00  9.66           N  
ATOM   1843  N   TYR A 245      -4.509  -1.156  31.947  1.00  9.68           N  
ATOM   1844  CA  TYR A 245      -5.385  -2.123  31.262  1.00  9.62           C  
ATOM   1845  C   TYR A 245      -6.861  -1.933  31.605  1.00  9.57           C  
ATOM   1846  O   TYR A 245      -7.201  -1.555  32.727  1.00  9.94           O  
ATOM   1847  CB  TYR A 245      -4.906  -3.555  31.512  1.00  9.58           C  
ATOM   1848  CG  TYR A 245      -3.558  -3.756  30.866  1.00  9.58           C  
ATOM   1849  CD1 TYR A 245      -2.384  -3.766  31.623  1.00  9.27           C  
ATOM   1850  CD2 TYR A 245      -3.456  -3.859  29.482  1.00  9.21           C  
ATOM   1851  CE1 TYR A 245      -1.132  -3.913  31.001  1.00 10.61           C  
ATOM   1852  CE2 TYR A 245      -2.227  -4.002  28.859  1.00 10.75           C  
ATOM   1853  CZ  TYR A 245      -1.071  -4.032  29.615  1.00  9.86           C  
ATOM   1854  OH  TYR A 245       0.132  -4.173  28.964  1.00  8.99           O  
ATOM   1855  N   HIS A 246      -7.728  -2.165  30.617  1.00  9.27           N  
ATOM   1856  CA  HIS A 246      -9.167  -1.914  30.771  1.00  9.35           C  
ATOM   1857  C   HIS A 246      -9.753  -2.523  32.039  1.00  9.41           C  
ATOM   1858  O   HIS A 246     -10.607  -1.915  32.693  1.00  9.18           O  
ATOM   1859  CB  HIS A 246      -9.952  -2.443  29.564  1.00  9.53           C  
ATOM   1860  CG  HIS A 246      -9.672  -1.726  28.279  1.00  9.92           C  
ATOM   1861  ND1 HIS A 246      -9.424  -0.370  28.211  1.00 10.03           N  
ATOM   1862  CD2 HIS A 246      -9.655  -2.175  27.001  1.00  9.81           C  
ATOM   1863  CE1 HIS A 246      -9.232  -0.024  26.950  1.00 10.91           C  
ATOM   1864  NE2 HIS A 246      -9.370  -1.100  26.196  1.00 10.01           N  
ATOM   1865  N   ILE A 247      -9.288  -3.722  32.384  1.00  9.51           N  
ATOM   1866  CA  ILE A 247      -9.864  -4.476  33.500  1.00 10.10           C  
ATOM   1867  C   ILE A 247      -9.956  -3.652  34.789  1.00 10.40           C  
ATOM   1868  O   ILE A 247     -10.964  -3.709  35.496  1.00 10.35           O  
ATOM   1869  CB  ILE A 247      -9.133  -5.834  33.732  1.00 10.13           C  
ATOM   1870  CG1 ILE A 247      -9.802  -6.644  34.857  1.00 10.94           C  
ATOM   1871  CG2 ILE A 247      -7.633  -5.629  34.005  1.00  9.78           C  
ATOM   1872  CD1 ILE A 247     -11.280  -6.971  34.617  1.00 11.43           C  
ATOM   1873  N   PHE A 248      -8.925  -2.864  35.078  1.00 10.53           N  
ATOM   1874  CA  PHE A 248      -8.933  -2.023  36.277  1.00 11.04           C  
ATOM   1875  C   PHE A 248     -10.143  -1.086  36.297  1.00 11.55           C  
ATOM   1876  O   PHE A 248     -10.795  -0.927  37.329  1.00 11.80           O  
ATOM   1877  CB  PHE A 248      -7.628  -1.239  36.407  1.00 10.78           C  
ATOM   1878  CG  PHE A 248      -6.419  -2.109  36.595  1.00 10.68           C  
ATOM   1879  CD1 PHE A 248      -6.142  -2.681  37.831  1.00  9.96           C  
ATOM   1880  CD2 PHE A 248      -5.554  -2.360  35.534  1.00  9.95           C  
ATOM   1881  CE1 PHE A 248      -5.017  -3.496  38.016  1.00 10.52           C  
ATOM   1882  CE2 PHE A 248      -4.424  -3.178  35.705  1.00 10.25           C  
ATOM   1883  CZ  PHE A 248      -4.158  -3.745  36.953  1.00 10.43           C  
ATOM   1884  N   TYR A 249     -10.464  -0.512  35.139  1.00 11.86           N  
ATOM   1885  CA  TYR A 249     -11.527   0.489  35.033  1.00 12.47           C  
ATOM   1886  C   TYR A 249     -12.895  -0.170  34.921  1.00 12.94           C  
ATOM   1887  O   TYR A 249     -13.880   0.329  35.474  1.00 13.30           O  
ATOM   1888  CB  TYR A 249     -11.240   1.446  33.871  1.00 12.38           C  
ATOM   1889  CG  TYR A 249      -9.847   2.002  33.982  1.00 12.30           C  
ATOM   1890  CD1 TYR A 249      -8.768   1.326  33.408  1.00 12.77           C  
ATOM   1891  CD2 TYR A 249      -9.590   3.156  34.719  1.00 12.61           C  
ATOM   1892  CE1 TYR A 249      -7.477   1.797  33.539  1.00 12.86           C  
ATOM   1893  CE2 TYR A 249      -8.289   3.639  34.862  1.00 12.57           C  
ATOM   1894  CZ  TYR A 249      -7.245   2.951  34.263  1.00 12.77           C  
ATOM   1895  OH  TYR A 249      -5.958   3.400  34.370  1.00 12.22           O  
ATOM   1896  N   ARG A 250     -12.944  -1.307  34.232  1.00 13.07           N  
ATOM   1897  CA  ARG A 250     -14.172  -2.089  34.130  1.00 13.42           C  
ATOM   1898  C   ARG A 250     -14.599  -2.592  35.508  1.00 14.02           C  
ATOM   1899  O   ARG A 250     -15.769  -2.480  35.884  1.00 14.01           O  
ATOM   1900  CB  ARG A 250     -13.988  -3.247  33.154  1.00 13.66           C  
ATOM   1901  CG  ARG A 250     -13.812  -2.789  31.709  1.00 13.51           C  
ATOM   1902  CD  ARG A 250     -13.730  -3.975  30.761  1.00 15.71           C  
ATOM   1903  NE  ARG A 250     -13.407  -3.542  29.403  1.00 16.83           N  
ATOM   1904  CZ  ARG A 250     -13.219  -4.363  28.370  1.00 17.62           C  
ATOM   1905  NH1 ARG A 250     -13.344  -5.678  28.512  1.00 17.77           N  
ATOM   1906  NH2 ARG A 250     -12.920  -3.860  27.185  1.00 18.39           N  
ATOM   1907  N   LEU A 251     -13.635  -3.104  36.267  1.00 14.05           N  
ATOM   1908  CA  LEU A 251     -13.897  -3.585  37.622  1.00 14.63           C  
ATOM   1909  C   LEU A 251     -14.343  -2.461  38.559  1.00 15.02           C  
ATOM   1910  O   LEU A 251     -15.326  -2.618  39.288  1.00 15.19           O  
ATOM   1911  CB  LEU A 251     -12.661  -4.297  38.181  1.00 14.60           C  
ATOM   1912  CG  LEU A 251     -12.791  -5.009  39.530  1.00 14.27           C  
ATOM   1913  CD1 LEU A 251     -13.898  -6.074  39.512  1.00 14.87           C  
ATOM   1914  CD2 LEU A 251     -11.447  -5.619  39.930  1.00 15.19           C  
ATOM   1915  N   CYS A 252     -13.638  -1.328  38.535  1.00 15.23           N  
ATOM   1916  CA  CYS A 252     -13.978  -0.204  39.413  1.00 15.94           C  
ATOM   1917  C   CYS A 252     -15.346   0.396  39.070  1.00 16.11           C  
ATOM   1918  O   CYS A 252     -16.109   0.750  39.970  1.00 16.20           O  
ATOM   1919  CB  CYS A 252     -12.893   0.882  39.398  1.00 16.00           C  
ATOM   1920  SG  CYS A 252     -11.373   0.492  40.328  1.00 17.72           S  
ATOM   1921  N   ALA A 253     -15.656   0.490  37.778  1.00 15.77           N  
ATOM   1922  CA  ALA A 253     -16.927   1.072  37.322  1.00 15.93           C  
ATOM   1923  C   ALA A 253     -18.120   0.139  37.515  1.00 15.94           C  
ATOM   1924  O   ALA A 253     -19.230   0.595  37.818  1.00 16.15           O  
ATOM   1925  CB  ALA A 253     -16.832   1.493  35.859  1.00 15.91           C  
ATOM   1926  N   GLY A 254     -17.888  -1.161  37.345  1.00 15.66           N  
ATOM   1927  CA  GLY A 254     -18.982  -2.117  37.206  1.00 15.94           C  
ATOM   1928  C   GLY A 254     -19.234  -3.092  38.338  1.00 16.02           C  
ATOM   1929  O   GLY A 254     -20.340  -3.628  38.449  1.00 16.33           O  
ATOM   1930  N   ALA A 255     -18.224  -3.342  39.169  1.00 15.92           N  
ATOM   1931  CA  ALA A 255     -18.346  -4.325  40.247  1.00 16.02           C  
ATOM   1932  C   ALA A 255     -19.496  -3.970  41.179  1.00 16.01           C  
ATOM   1933  O   ALA A 255     -19.780  -2.793  41.406  1.00 15.92           O  
ATOM   1934  CB  ALA A 255     -17.053  -4.430  41.043  1.00 16.18           C  
ATOM   1935  N   SER A 256     -20.152  -4.998  41.705  1.00 16.14           N  
ATOM   1936  CA  SER A 256     -21.181  -4.812  42.726  1.00 16.39           C  
ATOM   1937  C   SER A 256     -20.552  -4.212  43.978  1.00 16.53           C  
ATOM   1938  O   SER A 256     -19.336  -4.310  44.183  1.00 16.06           O  
ATOM   1939  CB  SER A 256     -21.825  -6.152  43.072  1.00 16.23           C  
ATOM   1940  OG  SER A 256     -20.892  -7.012  43.700  1.00 16.93           O  
ATOM   1941  N   GLU A 257     -21.376  -3.591  44.818  1.00 16.81           N  
ATOM   1942  CA  GLU A 257     -20.888  -3.063  46.087  1.00 17.66           C  
ATOM   1943  C   GLU A 257     -20.304  -4.159  46.972  1.00 17.93           C  
ATOM   1944  O   GLU A 257     -19.336  -3.921  47.693  1.00 18.01           O  
ATOM   1945  CB  GLU A 257     -21.986  -2.293  46.823  1.00 17.74           C  
ATOM   1946  CG  GLU A 257     -22.184  -0.877  46.315  1.00 18.96           C  
ATOM   1947  CD  GLU A 257     -21.052   0.049  46.715  1.00 21.43           C  
ATOM   1948  OE1 GLU A 257     -20.109   0.209  45.916  1.00 20.66           O  
ATOM   1949  OE2 GLU A 257     -21.095   0.606  47.837  1.00 23.44           O  
ATOM   1950  N   ASP A 258     -20.881  -5.358  46.912  1.00 18.55           N  
ATOM   1951  CA  ASP A 258     -20.342  -6.496  47.658  1.00 19.33           C  
ATOM   1952  C   ASP A 258     -18.914  -6.824  47.216  1.00 19.41           C  
ATOM   1953  O   ASP A 258     -18.031  -7.017  48.055  1.00 19.41           O  
ATOM   1954  CB  ASP A 258     -21.235  -7.732  47.520  1.00 19.64           C  
ATOM   1955  CG  ASP A 258     -20.822  -8.853  48.459  1.00 21.16           C  
ATOM   1956  OD1 ASP A 258     -20.533  -9.963  47.972  1.00 23.36           O  
ATOM   1957  OD2 ASP A 258     -20.775  -8.623  49.685  1.00 23.95           O  
ATOM   1958  N   ILE A 259     -18.694  -6.876  45.903  1.00 19.36           N  
ATOM   1959  CA  ILE A 259     -17.358  -7.149  45.362  1.00 19.44           C  
ATOM   1960  C   ILE A 259     -16.396  -6.004  45.678  1.00 19.53           C  
ATOM   1961  O   ILE A 259     -15.265  -6.245  46.106  1.00 19.40           O  
ATOM   1962  CB  ILE A 259     -17.394  -7.457  43.843  1.00 19.39           C  
ATOM   1963  CG1 ILE A 259     -17.976  -8.857  43.610  1.00 19.29           C  
ATOM   1964  CG2 ILE A 259     -15.984  -7.342  43.222  1.00 19.47           C  
ATOM   1965  CD1 ILE A 259     -18.349  -9.145  42.171  1.00 19.72           C  
ATOM   1966  N   ARG A 260     -16.854  -4.768  45.492  1.00 19.70           N  
ATOM   1967  CA  ARG A 260     -16.051  -3.595  45.832  1.00 20.46           C  
ATOM   1968  C   ARG A 260     -15.578  -3.626  47.290  1.00 20.59           C  
ATOM   1969  O   ARG A 260     -14.411  -3.352  47.571  1.00 20.35           O  
ATOM   1970  CB  ARG A 260     -16.814  -2.298  45.562  1.00 20.47           C  
ATOM   1971  CG  ARG A 260     -15.944  -1.060  45.736  1.00 22.36           C  
ATOM   1972  CD  ARG A 260     -16.743   0.197  46.003  1.00 25.36           C  
ATOM   1973  NE  ARG A 260     -17.676   0.061  47.122  1.00 27.92           N  
ATOM   1974  CZ  ARG A 260     -17.347   0.124  48.410  1.00 29.22           C  
ATOM   1975  NH1 ARG A 260     -18.293  -0.005  49.329  1.00 30.15           N  
ATOM   1976  NH2 ARG A 260     -16.085   0.308  48.786  1.00 30.42           N  
ATOM   1977  N   GLU A 261     -16.491  -3.957  48.203  1.00 20.89           N  
ATOM   1978  CA  GLU A 261     -16.171  -4.042  49.630  1.00 21.69           C  
ATOM   1979  C   GLU A 261     -15.146  -5.131  49.941  1.00 21.08           C  
ATOM   1980  O   GLU A 261     -14.165  -4.879  50.646  1.00 21.20           O  
ATOM   1981  CB  GLU A 261     -17.441  -4.262  50.467  1.00 21.65           C  
ATOM   1982  CG  GLU A 261     -18.327  -3.030  50.595  1.00 23.70           C  
ATOM   1983  CD  GLU A 261     -19.740  -3.342  51.084  1.00 23.88           C  
ATOM   1984  OE1 GLU A 261     -20.117  -4.533  51.161  1.00 27.53           O  
ATOM   1985  OE2 GLU A 261     -20.483  -2.383  51.382  1.00 28.00           O  
ATOM   1986  N   ARG A 262     -15.382  -6.334  49.419  1.00 20.78           N  
ATOM   1987  CA  ARG A 262     -14.504  -7.483  49.660  1.00 20.89           C  
ATOM   1988  C   ARG A 262     -13.094  -7.244  49.125  1.00 20.32           C  
ATOM   1989  O   ARG A 262     -12.118  -7.742  49.685  1.00 19.97           O  
ATOM   1990  CB  ARG A 262     -15.070  -8.745  49.007  1.00 21.27           C  
ATOM   1991  CG  ARG A 262     -16.273  -9.368  49.699  1.00 23.93           C  
ATOM   1992  CD  ARG A 262     -16.661 -10.634  48.956  1.00 28.17           C  
ATOM   1993  NE  ARG A 262     -17.871 -11.268  49.473  1.00 31.59           N  
ATOM   1994  CZ  ARG A 262     -18.306 -12.465  49.087  1.00 33.14           C  
ATOM   1995  NH1 ARG A 262     -17.626 -13.167  48.184  1.00 34.00           N  
ATOM   1996  NH2 ARG A 262     -19.419 -12.971  49.607  1.00 33.76           N  
ATOM   1997  N   LEU A 263     -13.004  -6.487  48.035  1.00 19.61           N  
ATOM   1998  CA  LEU A 263     -11.723  -6.221  47.380  1.00 19.37           C  
ATOM   1999  C   LEU A 263     -11.127  -4.877  47.776  1.00 19.47           C  
ATOM   2000  O   LEU A 263     -10.044  -4.508  47.302  1.00 18.94           O  
ATOM   2001  CB  LEU A 263     -11.883  -6.309  45.862  1.00 19.20           C  
ATOM   2002  CG  LEU A 263     -12.328  -7.666  45.306  1.00 18.79           C  
ATOM   2003  CD1 LEU A 263     -12.316  -7.633  43.787  1.00 18.13           C  
ATOM   2004  CD2 LEU A 263     -11.465  -8.817  45.825  1.00 18.87           C  
ATOM   2005  N   HIS A 264     -11.846  -4.157  48.641  1.00 19.68           N  
ATOM   2006  CA  HIS A 264     -11.440  -2.837  49.146  1.00 20.31           C  
ATOM   2007  C   HIS A 264     -11.169  -1.836  48.023  1.00 20.29           C  
ATOM   2008  O   HIS A 264     -10.213  -1.053  48.072  1.00 20.46           O  
ATOM   2009  CB  HIS A 264     -10.247  -2.963  50.102  1.00 20.56           C  
ATOM   2010  CG  HIS A 264     -10.400  -4.064  51.103  1.00 22.42           C  
ATOM   2011  ND1 HIS A 264     -11.162  -3.930  52.245  1.00 24.16           N  
ATOM   2012  CD2 HIS A 264      -9.914  -5.328  51.121  1.00 22.88           C  
ATOM   2013  CE1 HIS A 264     -11.130  -5.061  52.927  1.00 24.22           C  
ATOM   2014  NE2 HIS A 264     -10.374  -5.923  52.270  1.00 24.82           N  
ATOM   2015  N   LEU A 265     -12.030  -1.863  47.012  1.00 20.05           N  
ATOM   2016  CA  LEU A 265     -11.874  -0.990  45.867  1.00 20.28           C  
ATOM   2017  C   LEU A 265     -12.503   0.379  46.105  1.00 20.19           C  
ATOM   2018  O   LEU A 265     -13.295   0.567  47.040  1.00 20.33           O  
ATOM   2019  CB  LEU A 265     -12.413  -1.661  44.595  1.00 20.32           C  
ATOM   2020  CG  LEU A 265     -11.669  -2.931  44.158  1.00 21.46           C  
ATOM   2021  CD1 LEU A 265     -12.351  -3.558  42.960  1.00 22.40           C  
ATOM   2022  CD2 LEU A 265     -10.194  -2.656  43.857  1.00 22.51           C  
ATOM   2023  N   SER A 266     -12.108   1.335  45.269  1.00 20.05           N  
ATOM   2024  CA  SER A 266     -12.602   2.708  45.318  1.00 20.05           C  
ATOM   2025  C   SER A 266     -12.331   3.374  43.967  1.00 19.78           C  
ATOM   2026  O   SER A 266     -11.885   2.704  43.026  1.00 19.92           O  
ATOM   2027  CB  SER A 266     -11.965   3.489  46.481  1.00 20.18           C  
ATOM   2028  OG  SER A 266     -10.552   3.383  46.489  1.00 20.70           O  
ATOM   2029  N   SER A 267     -12.614   4.671  43.856  1.00 19.27           N  
ATOM   2030  CA  SER A 267     -12.356   5.410  42.617  1.00 19.25           C  
ATOM   2031  C   SER A 267     -10.864   5.347  42.233  1.00 18.67           C  
ATOM   2032  O   SER A 267     -10.007   5.300  43.113  1.00 18.67           O  
ATOM   2033  CB  SER A 267     -12.854   6.858  42.718  1.00 19.37           C  
ATOM   2034  OG  SER A 267     -12.269   7.554  43.807  1.00 20.79           O  
ATOM   2035  N   PRO A 268     -10.559   5.311  40.919  1.00 18.26           N  
ATOM   2036  CA  PRO A 268      -9.192   5.106  40.408  1.00 18.01           C  
ATOM   2037  C   PRO A 268      -8.122   6.063  40.941  1.00 17.72           C  
ATOM   2038  O   PRO A 268      -6.946   5.696  40.994  1.00 17.59           O  
ATOM   2039  CB  PRO A 268      -9.355   5.299  38.895  1.00 18.09           C  
ATOM   2040  CG  PRO A 268     -10.757   4.916  38.630  1.00 18.30           C  
ATOM   2041  CD  PRO A 268     -11.533   5.414  39.815  1.00 18.48           C  
ATOM   2042  N   ASP A 269      -8.519   7.276  41.317  1.00 17.50           N  
ATOM   2043  CA  ASP A 269      -7.578   8.258  41.868  1.00 17.67           C  
ATOM   2044  C   ASP A 269      -6.958   7.819  43.200  1.00 17.40           C  
ATOM   2045  O   ASP A 269      -5.977   8.411  43.650  1.00 17.82           O  
ATOM   2046  CB  ASP A 269      -8.251   9.622  42.028  1.00 17.98           C  
ATOM   2047  CG  ASP A 269      -9.465   9.566  42.924  1.00 19.01           C  
ATOM   2048  OD1 ASP A 269      -9.461  10.236  43.982  1.00 20.76           O  
ATOM   2049  OD2 ASP A 269     -10.421   8.839  42.581  1.00 19.93           O  
ATOM   2050  N   ASN A 270      -7.526   6.781  43.817  1.00 17.08           N  
ATOM   2051  CA  ASN A 270      -7.019   6.259  45.090  1.00 16.66           C  
ATOM   2052  C   ASN A 270      -5.879   5.251  44.932  1.00 16.28           C  
ATOM   2053  O   ASN A 270      -5.353   4.740  45.929  1.00 15.72           O  
ATOM   2054  CB  ASN A 270      -8.159   5.648  45.911  1.00 17.13           C  
ATOM   2055  CG  ASN A 270      -9.120   6.696  46.440  1.00 18.52           C  
ATOM   2056  OD1 ASN A 270      -8.777   7.479  47.328  1.00 20.49           O  
ATOM   2057  ND2 ASN A 270     -10.330   6.716  45.897  1.00 19.58           N  
ATOM   2058  N   PHE A 271      -5.491   4.980  43.685  1.00 15.46           N  
ATOM   2059  CA  PHE A 271      -4.474   3.969  43.398  1.00 15.23           C  
ATOM   2060  C   PHE A 271      -3.311   4.525  42.589  1.00 15.06           C  
ATOM   2061  O   PHE A 271      -3.508   5.043  41.487  1.00 14.79           O  
ATOM   2062  CB  PHE A 271      -5.106   2.768  42.681  1.00 15.04           C  
ATOM   2063  CG  PHE A 271      -6.165   2.077  43.494  1.00 15.41           C  
ATOM   2064  CD1 PHE A 271      -7.516   2.344  43.274  1.00 16.32           C  
ATOM   2065  CD2 PHE A 271      -5.810   1.178  44.496  1.00 15.60           C  
ATOM   2066  CE1 PHE A 271      -8.499   1.714  44.035  1.00 16.32           C  
ATOM   2067  CE2 PHE A 271      -6.781   0.543  45.264  1.00 15.47           C  
ATOM   2068  CZ  PHE A 271      -8.130   0.814  45.035  1.00 15.89           C  
ATOM   2069  N   ARG A 272      -2.103   4.406  43.145  1.00 14.88           N  
ATOM   2070  CA  ARG A 272      -0.870   4.828  42.463  1.00 15.38           C  
ATOM   2071  C   ARG A 272      -0.744   4.221  41.062  1.00 14.45           C  
ATOM   2072  O   ARG A 272      -0.314   4.897  40.124  1.00 14.47           O  
ATOM   2073  CB  ARG A 272       0.365   4.476  43.305  1.00 15.30           C  
ATOM   2074  CG  ARG A 272       1.705   4.765  42.627  1.00 16.84           C  
ATOM   2075  CD  ARG A 272       2.889   4.588  43.569  1.00 17.46           C  
ATOM   2076  NE  ARG A 272       2.985   5.697  44.517  1.00 22.63           N  
ATOM   2077  CZ  ARG A 272       2.581   5.650  45.784  1.00 23.98           C  
ATOM   2078  NH1 ARG A 272       2.715   6.722  46.555  1.00 25.69           N  
ATOM   2079  NH2 ARG A 272       2.051   4.538  46.289  1.00 24.21           N  
ATOM   2080  N   TYR A 273      -1.127   2.953  40.920  1.00 13.81           N  
ATOM   2081  CA  TYR A 273      -1.011   2.270  39.621  1.00 13.25           C  
ATOM   2082  C   TYR A 273      -2.025   2.761  38.580  1.00 13.21           C  
ATOM   2083  O   TYR A 273      -1.944   2.379  37.407  1.00 12.87           O  
ATOM   2084  CB  TYR A 273      -1.071   0.745  39.776  1.00 13.03           C  
ATOM   2085  CG  TYR A 273       0.162   0.112  40.399  1.00 12.59           C  
ATOM   2086  CD1 TYR A 273       1.360   0.824  40.540  1.00 13.22           C  
ATOM   2087  CD2 TYR A 273       0.138  -1.218  40.809  1.00 13.55           C  
ATOM   2088  CE1 TYR A 273       2.498   0.224  41.105  1.00 12.12           C  
ATOM   2089  CE2 TYR A 273       1.262  -1.822  41.369  1.00 12.57           C  
ATOM   2090  CZ  TYR A 273       2.436  -1.100  41.508  1.00 12.72           C  
ATOM   2091  OH  TYR A 273       3.523  -1.719  42.069  1.00 12.56           O  
ATOM   2092  N   LEU A 274      -2.954   3.615  39.007  1.00 12.90           N  
ATOM   2093  CA  LEU A 274      -3.933   4.221  38.107  1.00 13.40           C  
ATOM   2094  C   LEU A 274      -3.870   5.749  38.053  1.00 14.05           C  
ATOM   2095  O   LEU A 274      -4.245   6.347  37.046  1.00 14.16           O  
ATOM   2096  CB  LEU A 274      -5.355   3.794  38.493  1.00 13.20           C  
ATOM   2097  CG  LEU A 274      -5.693   2.307  38.622  1.00 12.71           C  
ATOM   2098  CD1 LEU A 274      -7.155   2.132  39.016  1.00 12.70           C  
ATOM   2099  CD2 LEU A 274      -5.400   1.561  37.327  1.00 12.47           C  
ATOM   2100  N   ASN A 275      -3.401   6.386  39.126  1.00 14.60           N  
ATOM   2101  CA  ASN A 275      -3.653   7.826  39.300  1.00 15.34           C  
ATOM   2102  C   ASN A 275      -2.661   8.816  38.654  1.00 15.94           C  
ATOM   2103  O   ASN A 275      -2.873  10.032  38.721  1.00 16.33           O  
ATOM   2104  CB  ASN A 275      -3.952   8.169  40.776  1.00 15.04           C  
ATOM   2105  CG  ASN A 275      -2.735   8.046  41.676  1.00 15.14           C  
ATOM   2106  OD1 ASN A 275      -1.596   8.035  41.209  1.00 14.74           O  
ATOM   2107  ND2 ASN A 275      -2.973   7.959  42.989  1.00 14.42           N  
ATOM   2108  N   ARG A 276      -1.598   8.300  38.034  1.00 16.60           N  
ATOM   2109  CA  ARG A 276      -0.722   9.114  37.174  1.00 17.48           C  
ATOM   2110  C   ARG A 276      -1.280   9.166  35.756  1.00 17.65           C  
ATOM   2111  O   ARG A 276      -0.950  10.066  34.976  1.00 17.81           O  
ATOM   2112  CB  ARG A 276       0.705   8.560  37.133  1.00 17.84           C  
ATOM   2113  CG  ARG A 276       1.640   9.061  38.236  1.00 20.04           C  
ATOM   2114  CD  ARG A 276       1.437   8.324  39.556  1.00 22.58           C  
ATOM   2115  NE  ARG A 276       1.595   6.873  39.432  1.00 24.22           N  
ATOM   2116  CZ  ARG A 276       2.762   6.232  39.444  1.00 25.16           C  
ATOM   2117  NH1 ARG A 276       3.905   6.902  39.567  1.00 26.05           N  
ATOM   2118  NH2 ARG A 276       2.786   4.912  39.327  1.00 25.31           N  
ATOM   2119  N   GLY A 277      -2.111   8.183  35.422  1.00 17.60           N  
ATOM   2120  CA  GLY A 277      -2.782   8.149  34.127  1.00 17.41           C  
ATOM   2121  C   GLY A 277      -4.107   8.882  34.158  1.00 17.48           C  
ATOM   2122  O   GLY A 277      -4.452   9.548  35.144  1.00 17.71           O  
ATOM   2123  N   CYS A 278      -4.850   8.767  33.066  1.00 17.40           N  
ATOM   2124  CA  CYS A 278      -6.202   9.284  33.005  1.00 17.26           C  
ATOM   2125  C   CYS A 278      -7.124   8.386  33.830  1.00 16.86           C  
ATOM   2126  O   CYS A 278      -7.151   7.168  33.636  1.00 16.73           O  
ATOM   2127  CB  CYS A 278      -6.674   9.341  31.555  1.00 17.42           C  
ATOM   2128  SG  CYS A 278      -8.350   9.951  31.382  1.00 18.94           S  
ATOM   2129  N   THR A 279      -7.868   8.986  34.756  1.00 16.77           N  
ATOM   2130  CA  THR A 279      -8.738   8.213  35.651  1.00 17.16           C  
ATOM   2131  C   THR A 279     -10.219   8.275  35.263  1.00 16.94           C  
ATOM   2132  O   THR A 279     -11.082   7.814  36.011  1.00 17.01           O  
ATOM   2133  CB  THR A 279      -8.582   8.650  37.129  1.00 17.26           C  
ATOM   2134  OG1 THR A 279      -8.971  10.023  37.271  1.00 18.18           O  
ATOM   2135  CG2 THR A 279      -7.143   8.461  37.603  1.00 17.86           C  
ATOM   2136  N   ARG A 280     -10.500   8.840  34.092  1.00 16.93           N  
ATOM   2137  CA  ARG A 280     -11.866   8.958  33.591  1.00 16.77           C  
ATOM   2138  C   ARG A 280     -12.328   7.645  32.957  1.00 16.58           C  
ATOM   2139  O   ARG A 280     -11.526   6.915  32.367  1.00 16.59           O  
ATOM   2140  CB  ARG A 280     -11.962  10.095  32.567  1.00 17.10           C  
ATOM   2141  CG  ARG A 280     -11.588  11.478  33.109  1.00 17.86           C  
ATOM   2142  CD  ARG A 280     -11.143  12.416  31.989  1.00 19.41           C  
ATOM   2143  NE  ARG A 280     -12.225  12.753  31.066  1.00 20.87           N  
ATOM   2144  CZ  ARG A 280     -12.072  13.445  29.938  1.00 21.21           C  
ATOM   2145  NH1 ARG A 280     -13.122  13.694  29.171  1.00 22.96           N  
ATOM   2146  NH2 ARG A 280     -10.875  13.882  29.569  1.00 21.77           N  
ATOM   2147  N   TYR A 281     -13.617   7.348  33.093  1.00 16.24           N  
ATOM   2148  CA  TYR A 281     -14.213   6.184  32.457  1.00 16.01           C  
ATOM   2149  C   TYR A 281     -14.704   6.520  31.057  1.00 16.04           C  
ATOM   2150  O   TYR A 281     -15.070   7.665  30.777  1.00 15.78           O  
ATOM   2151  CB  TYR A 281     -15.407   5.666  33.266  1.00 16.07           C  
ATOM   2152  CG  TYR A 281     -15.089   5.211  34.673  1.00 15.58           C  
ATOM   2153  CD1 TYR A 281     -14.208   4.149  34.908  1.00 15.82           C  
ATOM   2154  CD2 TYR A 281     -15.700   5.819  35.771  1.00 15.89           C  
ATOM   2155  CE1 TYR A 281     -13.923   3.722  36.203  1.00 15.52           C  
ATOM   2156  CE2 TYR A 281     -15.423   5.398  37.071  1.00 15.63           C  
ATOM   2157  CZ  TYR A 281     -14.536   4.347  37.277  1.00 15.99           C  
ATOM   2158  OH  TYR A 281     -14.252   3.921  38.556  1.00 15.69           O  
ATOM   2159  N   PHE A 282     -14.717   5.515  30.183  1.00 16.25           N  
ATOM   2160  CA  PHE A 282     -15.497   5.602  28.951  1.00 16.68           C  
ATOM   2161  C   PHE A 282     -16.954   5.387  29.332  1.00 17.14           C  
ATOM   2162  O   PHE A 282     -17.306   4.363  29.917  1.00 17.14           O  
ATOM   2163  CB  PHE A 282     -15.064   4.546  27.931  1.00 16.33           C  
ATOM   2164  CG  PHE A 282     -13.713   4.802  27.331  1.00 15.51           C  
ATOM   2165  CD1 PHE A 282     -12.585   4.162  27.833  1.00 15.06           C  
ATOM   2166  CD2 PHE A 282     -13.566   5.684  26.262  1.00 15.02           C  
ATOM   2167  CE1 PHE A 282     -11.333   4.392  27.278  1.00 14.65           C  
ATOM   2168  CE2 PHE A 282     -12.317   5.927  25.706  1.00 14.35           C  
ATOM   2169  CZ  PHE A 282     -11.194   5.279  26.221  1.00 15.58           C  
ATOM   2170  N   ALA A 283     -17.787   6.378  29.029  1.00 18.13           N  
ATOM   2171  CA  ALA A 283     -19.217   6.306  29.314  1.00 19.09           C  
ATOM   2172  C   ALA A 283     -19.972   7.283  28.427  1.00 19.84           C  
ATOM   2173  O   ALA A 283     -19.378   8.195  27.850  1.00 19.89           O  
ATOM   2174  CB  ALA A 283     -19.496   6.601  30.795  1.00 19.05           C  
ATOM   2175  N   ASN A 284     -21.275   7.064  28.296  1.00 20.99           N  
ATOM   2176  CA  ASN A 284     -22.152   8.054  27.679  1.00 22.28           C  
ATOM   2177  C   ASN A 284     -23.175   8.539  28.705  1.00 23.14           C  
ATOM   2178  O   ASN A 284     -23.095   8.166  29.877  1.00 22.83           O  
ATOM   2179  CB  ASN A 284     -22.809   7.506  26.399  1.00 22.38           C  
ATOM   2180  CG  ASN A 284     -23.659   6.268  26.643  1.00 22.53           C  
ATOM   2181  OD1 ASN A 284     -24.276   6.110  27.698  1.00 22.63           O  
ATOM   2182  ND2 ASN A 284     -23.705   5.385  25.650  1.00 22.66           N  
ATOM   2183  N   LYS A 285     -24.126   9.363  28.270  1.00 24.27           N  
ATOM   2184  CA  LYS A 285     -25.166   9.891  29.158  1.00 25.48           C  
ATOM   2185  C   LYS A 285     -25.866   8.806  29.975  1.00 25.75           C  
ATOM   2186  O   LYS A 285     -26.036   8.946  31.190  1.00 26.00           O  
ATOM   2187  CB  LYS A 285     -26.203  10.685  28.355  1.00 25.80           C  
ATOM   2188  CG  LYS A 285     -25.745  12.074  27.950  1.00 27.68           C  
ATOM   2189  CD  LYS A 285     -26.870  12.850  27.282  1.00 30.57           C  
ATOM   2190  CE  LYS A 285     -26.438  14.272  26.957  1.00 32.09           C  
ATOM   2191  NZ  LYS A 285     -27.502  15.024  26.230  1.00 33.16           N  
ATOM   2192  N   GLU A 286     -26.248   7.722  29.302  1.00 26.05           N  
ATOM   2193  CA  GLU A 286     -27.016   6.643  29.919  1.00 26.61           C  
ATOM   2194  C   GLU A 286     -26.181   5.812  30.897  1.00 25.85           C  
ATOM   2195  O   GLU A 286     -26.580   5.617  32.049  1.00 25.77           O  
ATOM   2196  CB  GLU A 286     -27.648   5.751  28.841  1.00 26.60           C  
ATOM   2197  CG  GLU A 286     -28.570   6.506  27.872  1.00 28.27           C  
ATOM   2198  CD  GLU A 286     -28.852   5.750  26.577  1.00 28.80           C  
ATOM   2199  OE1 GLU A 286     -28.044   4.872  26.191  1.00 32.37           O  
ATOM   2200  OE2 GLU A 286     -29.885   6.049  25.931  1.00 32.75           O  
ATOM   2201  N   THR A 287     -25.020   5.342  30.443  1.00 25.30           N  
ATOM   2202  CA  THR A 287     -24.184   4.443  31.247  1.00 24.72           C  
ATOM   2203  C   THR A 287     -23.519   5.128  32.443  1.00 24.61           C  
ATOM   2204  O   THR A 287     -23.223   4.478  33.445  1.00 24.46           O  
ATOM   2205  CB  THR A 287     -23.122   3.712  30.396  1.00 24.58           C  
ATOM   2206  OG1 THR A 287     -22.283   4.671  29.743  1.00 23.95           O  
ATOM   2207  CG2 THR A 287     -23.790   2.816  29.355  1.00 24.50           C  
ATOM   2208  N   ASP A 288     -23.297   6.436  32.337  1.00 24.60           N  
ATOM   2209  CA  ASP A 288     -22.796   7.233  33.459  1.00 24.97           C  
ATOM   2210  C   ASP A 288     -23.702   7.095  34.689  1.00 25.01           C  
ATOM   2211  O   ASP A 288     -23.220   7.024  35.820  1.00 24.75           O  
ATOM   2212  CB  ASP A 288     -22.650   8.704  33.055  1.00 24.96           C  
ATOM   2213  CG  ASP A 288     -22.396   9.619  34.245  1.00 25.85           C  
ATOM   2214  OD1 ASP A 288     -23.285  10.439  34.560  1.00 26.82           O  
ATOM   2215  OD2 ASP A 288     -21.324   9.506  34.875  1.00 25.89           O  
ATOM   2216  N   LYS A 289     -25.011   7.030  34.445  1.00 25.14           N  
ATOM   2217  CA  LYS A 289     -26.014   6.895  35.505  1.00 25.27           C  
ATOM   2218  C   LYS A 289     -25.962   5.539  36.206  1.00 25.31           C  
ATOM   2219  O   LYS A 289     -26.453   5.398  37.329  1.00 25.42           O  
ATOM   2220  CB  LYS A 289     -27.417   7.138  34.938  1.00 25.50           C  
ATOM   2221  CG  LYS A 289     -27.628   8.546  34.408  1.00 26.33           C  
ATOM   2222  CD  LYS A 289     -29.033   8.728  33.855  1.00 27.82           C  
ATOM   2223  CE  LYS A 289     -29.164  10.059  33.134  1.00 28.37           C  
ATOM   2224  NZ  LYS A 289     -30.543  10.265  32.602  1.00 29.14           N  
ATOM   2225  N   GLN A 290     -25.367   4.552  35.538  1.00 24.91           N  
ATOM   2226  CA  GLN A 290     -25.242   3.198  36.073  1.00 24.98           C  
ATOM   2227  C   GLN A 290     -23.993   3.029  36.940  1.00 24.38           C  
ATOM   2228  O   GLN A 290     -23.868   2.043  37.667  1.00 24.51           O  
ATOM   2229  CB  GLN A 290     -25.228   2.176  34.934  1.00 24.89           C  
ATOM   2230  CG  GLN A 290     -26.554   2.035  34.209  1.00 25.73           C  
ATOM   2231  CD  GLN A 290     -26.489   1.042  33.070  1.00 26.17           C  
ATOM   2232  OE1 GLN A 290     -27.023  -0.062  33.164  1.00 28.97           O  
ATOM   2233  NE2 GLN A 290     -25.826   1.427  31.985  1.00 27.42           N  
ATOM   2234  N   ILE A 291     -23.070   3.984  36.849  1.00 23.79           N  
ATOM   2235  CA  ILE A 291     -21.858   3.964  37.668  1.00 23.52           C  
ATOM   2236  C   ILE A 291     -22.130   4.682  38.988  1.00 23.51           C  
ATOM   2237  O   ILE A 291     -22.559   5.840  38.994  1.00 23.32           O  
ATOM   2238  CB  ILE A 291     -20.644   4.607  36.942  1.00 23.44           C  
ATOM   2239  CG1 ILE A 291     -20.428   3.957  35.568  1.00 23.29           C  
ATOM   2240  CG2 ILE A 291     -19.378   4.499  37.802  1.00 23.24           C  
ATOM   2241  CD1 ILE A 291     -19.481   4.728  34.654  1.00 23.04           C  
ATOM   2242  N   LEU A 292     -21.890   3.981  40.096  1.00 23.55           N  
ATOM   2243  CA  LEU A 292     -22.092   4.540  41.432  1.00 23.76           C  
ATOM   2244  C   LEU A 292     -21.147   5.705  41.698  1.00 23.80           C  
ATOM   2245  O   LEU A 292     -20.013   5.725  41.213  1.00 23.83           O  
ATOM   2246  CB  LEU A 292     -21.923   3.468  42.512  1.00 23.76           C  
ATOM   2247  CG  LEU A 292     -23.018   2.404  42.644  1.00 24.43           C  
ATOM   2248  CD1 LEU A 292     -22.526   1.257  43.503  1.00 24.96           C  
ATOM   2249  CD2 LEU A 292     -24.314   2.988  43.214  1.00 25.86           C  
ATOM   2250  N   GLN A 293     -21.638   6.670  42.472  1.00 23.74           N  
ATOM   2251  CA  GLN A 293     -20.902   7.884  42.821  1.00 23.77           C  
ATOM   2252  C   GLN A 293     -19.512   7.595  43.390  1.00 22.87           C  
ATOM   2253  O   GLN A 293     -18.549   8.281  43.046  1.00 22.69           O  
ATOM   2254  CB  GLN A 293     -21.717   8.724  43.819  1.00 23.88           C  
ATOM   2255  CG  GLN A 293     -23.120   9.099  43.324  1.00 25.04           C  
ATOM   2256  CD  GLN A 293     -24.039   9.629  44.426  1.00 25.26           C  
ATOM   2257  OE1 GLN A 293     -24.557  10.741  44.330  1.00 27.54           O  
ATOM   2258  NE2 GLN A 293     -24.243   8.834  45.470  1.00 27.45           N  
ATOM   2259  N   ASN A 294     -19.418   6.570  44.243  1.00 22.18           N  
ATOM   2260  CA  ASN A 294     -18.166   6.222  44.928  1.00 21.59           C  
ATOM   2261  C   ASN A 294     -17.083   5.597  44.030  1.00 20.97           C  
ATOM   2262  O   ASN A 294     -16.003   5.235  44.508  1.00 20.94           O  
ATOM   2263  CB  ASN A 294     -18.431   5.351  46.175  1.00 21.67           C  
ATOM   2264  CG  ASN A 294     -18.935   3.939  45.841  1.00 22.22           C  
ATOM   2265  OD1 ASN A 294     -19.055   3.548  44.678  1.00 21.88           O  
ATOM   2266  ND2 ASN A 294     -19.230   3.168  46.884  1.00 22.77           N  
ATOM   2267  N   ARG A 295     -17.380   5.479  42.738  1.00 20.48           N  
ATOM   2268  CA  ARG A 295     -16.434   4.923  41.769  1.00 19.89           C  
ATOM   2269  C   ARG A 295     -15.777   6.017  40.932  1.00 19.84           C  
ATOM   2270  O   ARG A 295     -14.813   5.759  40.208  1.00 19.57           O  
ATOM   2271  CB  ARG A 295     -17.129   3.927  40.828  1.00 19.77           C  
ATOM   2272  CG  ARG A 295     -18.095   2.953  41.488  1.00 19.12           C  
ATOM   2273  CD  ARG A 295     -17.430   2.086  42.548  1.00 19.49           C  
ATOM   2274  NE  ARG A 295     -18.400   1.194  43.183  1.00 19.09           N  
ATOM   2275  CZ  ARG A 295     -18.700  -0.022  42.737  1.00 19.24           C  
ATOM   2276  NH1 ARG A 295     -18.105  -0.502  41.650  1.00 18.89           N  
ATOM   2277  NH2 ARG A 295     -19.596  -0.761  43.373  1.00 19.50           N  
ATOM   2278  N   LYS A 296     -16.301   7.235  41.032  1.00 19.78           N  
ATOM   2279  CA  LYS A 296     -15.895   8.330  40.153  1.00 19.94           C  
ATOM   2280  C   LYS A 296     -14.815   9.215  40.766  1.00 19.97           C  
ATOM   2281  O   LYS A 296     -14.931   9.653  41.914  1.00 20.09           O  
ATOM   2282  CB  LYS A 296     -17.118   9.151  39.737  1.00 20.00           C  
ATOM   2283  CG  LYS A 296     -18.133   8.331  38.928  1.00 20.42           C  
ATOM   2284  CD  LYS A 296     -19.462   9.041  38.752  1.00 22.96           C  
ATOM   2285  CE  LYS A 296     -20.390   8.183  37.905  1.00 23.50           C  
ATOM   2286  NZ  LYS A 296     -21.735   8.779  37.691  1.00 24.64           N  
ATOM   2287  N   SER A 297     -13.764   9.468  39.990  1.00 20.07           N  
ATOM   2288  CA  SER A 297     -12.635  10.288  40.433  1.00 20.35           C  
ATOM   2289  C   SER A 297     -12.960  11.778  40.304  1.00 20.69           C  
ATOM   2290  O   SER A 297     -13.830  12.148  39.517  1.00 20.83           O  
ATOM   2291  CB  SER A 297     -11.390   9.965  39.602  1.00 20.20           C  
ATOM   2292  OG  SER A 297     -11.530  10.443  38.276  1.00 19.89           O  
ATOM   2293  N   PRO A 298     -12.257  12.639  41.069  1.00 21.26           N  
ATOM   2294  CA  PRO A 298     -12.378  14.085  40.884  1.00 21.67           C  
ATOM   2295  C   PRO A 298     -12.211  14.522  39.423  1.00 22.11           C  
ATOM   2296  O   PRO A 298     -12.931  15.414  38.977  1.00 22.49           O  
ATOM   2297  CB  PRO A 298     -11.239  14.638  41.745  1.00 21.67           C  
ATOM   2298  CG  PRO A 298     -11.120  13.656  42.842  1.00 21.75           C  
ATOM   2299  CD  PRO A 298     -11.332  12.319  42.174  1.00 21.44           C  
ATOM   2300  N   GLU A 299     -11.280  13.893  38.699  1.00 22.41           N  
ATOM   2301  CA  GLU A 299     -11.044  14.185  37.277  1.00 23.02           C  
ATOM   2302  C   GLU A 299     -12.294  13.882  36.447  1.00 22.58           C  
ATOM   2303  O   GLU A 299     -12.687  14.683  35.597  1.00 23.07           O  
ATOM   2304  CB  GLU A 299      -9.834  13.393  36.739  1.00 22.91           C  
ATOM   2305  CG  GLU A 299      -9.428  13.729  35.291  1.00 24.15           C  
ATOM   2306  CD  GLU A 299      -8.434  12.734  34.663  1.00 24.38           C  
ATOM   2307  OE1 GLU A 299      -7.989  11.776  35.334  1.00 25.94           O  
ATOM   2308  OE2 GLU A 299      -8.093  12.920  33.473  1.00 27.57           O  
ATOM   2309  N   TYR A 300     -12.910  12.728  36.704  1.00 22.34           N  
ATOM   2310  CA  TYR A 300     -14.138  12.321  36.022  1.00 22.25           C  
ATOM   2311  C   TYR A 300     -15.298  13.275  36.318  1.00 22.42           C  
ATOM   2312  O   TYR A 300     -16.065  13.621  35.425  1.00 22.29           O  
ATOM   2313  CB  TYR A 300     -14.521  10.891  36.414  1.00 22.12           C  
ATOM   2314  CG  TYR A 300     -15.724  10.347  35.672  1.00 21.99           C  
ATOM   2315  CD1 TYR A 300     -15.585   9.745  34.422  1.00 21.74           C  
ATOM   2316  CD2 TYR A 300     -17.004  10.429  36.223  1.00 22.10           C  
ATOM   2317  CE1 TYR A 300     -16.691   9.241  33.741  1.00 21.57           C  
ATOM   2318  CE2 TYR A 300     -18.115   9.930  35.547  1.00 22.11           C  
ATOM   2319  CZ  TYR A 300     -17.951   9.336  34.309  1.00 22.14           C  
ATOM   2320  OH  TYR A 300     -19.049   8.839  33.639  1.00 22.44           O  
ATOM   2321  N   LEU A 301     -15.421  13.692  37.575  1.00 22.64           N  
ATOM   2322  CA  LEU A 301     -16.516  14.575  37.983  1.00 23.37           C  
ATOM   2323  C   LEU A 301     -16.387  15.974  37.378  1.00 23.67           C  
ATOM   2324  O   LEU A 301     -17.393  16.630  37.092  1.00 23.91           O  
ATOM   2325  CB  LEU A 301     -16.612  14.644  39.514  1.00 23.30           C  
ATOM   2326  CG  LEU A 301     -17.005  13.347  40.235  1.00 23.64           C  
ATOM   2327  CD1 LEU A 301     -16.723  13.436  41.733  1.00 23.76           C  
ATOM   2328  CD2 LEU A 301     -18.463  12.966  39.974  1.00 24.38           C  
ATOM   2329  N   LYS A 302     -15.148  16.407  37.164  1.00 24.00           N  
ATOM   2330  CA  LYS A 302     -14.862  17.723  36.597  1.00 24.37           C  
ATOM   2331  C   LYS A 302     -14.932  17.740  35.068  1.00 24.21           C  
ATOM   2332  O   LYS A 302     -15.589  18.608  34.486  1.00 24.36           O  
ATOM   2333  CB  LYS A 302     -13.491  18.210  37.072  1.00 24.40           C  
ATOM   2334  CG  LYS A 302     -13.101  19.608  36.593  1.00 25.36           C  
ATOM   2335  CD  LYS A 302     -11.629  19.898  36.870  1.00 25.61           C  
ATOM   2336  CE  LYS A 302     -11.386  20.346  38.308  1.00 28.18           C  
ATOM   2337  NZ  LYS A 302     -11.669  21.802  38.509  1.00 29.62           N  
ATOM   2338  N   ALA A 303     -14.249  16.789  34.428  1.00 23.76           N  
ATOM   2339  CA  ALA A 303     -14.112  16.777  32.964  1.00 23.40           C  
ATOM   2340  C   ALA A 303     -15.171  15.950  32.234  1.00 22.99           C  
ATOM   2341  O   ALA A 303     -15.351  16.097  31.023  1.00 23.18           O  
ATOM   2342  CB  ALA A 303     -12.708  16.324  32.565  1.00 23.54           C  
ATOM   2343  N   GLY A 304     -15.864  15.083  32.967  1.00 22.45           N  
ATOM   2344  CA  GLY A 304     -16.843  14.180  32.368  1.00 21.77           C  
ATOM   2345  C   GLY A 304     -16.182  12.931  31.808  1.00 21.18           C  
ATOM   2346  O   GLY A 304     -14.983  12.711  31.996  1.00 21.21           O  
ATOM   2347  N   SER A 305     -16.962  12.120  31.104  1.00 20.90           N  
ATOM   2348  CA  SER A 305     -16.479  10.835  30.612  1.00 20.39           C  
ATOM   2349  C   SER A 305     -15.622  10.956  29.357  1.00 20.14           C  
ATOM   2350  O   SER A 305     -15.629  11.983  28.666  1.00 19.89           O  
ATOM   2351  CB  SER A 305     -17.656   9.889  30.351  1.00 20.61           C  
ATOM   2352  OG  SER A 305     -18.432  10.334  29.253  1.00 20.76           O  
ATOM   2353  N   LEU A 306     -14.879   9.891  29.079  1.00 19.70           N  
ATOM   2354  CA  LEU A 306     -14.203   9.734  27.804  1.00 19.72           C  
ATOM   2355  C   LEU A 306     -15.215   9.199  26.797  1.00 19.81           C  
ATOM   2356  O   LEU A 306     -16.121   8.445  27.159  1.00 19.24           O  
ATOM   2357  CB  LEU A 306     -13.038   8.754  27.932  1.00 19.62           C  
ATOM   2358  CG  LEU A 306     -11.913   9.067  28.918  1.00 19.21           C  
ATOM   2359  CD1 LEU A 306     -11.019   7.845  29.076  1.00 19.47           C  
ATOM   2360  CD2 LEU A 306     -11.111  10.280  28.460  1.00 18.66           C  
ATOM   2361  N   LYS A 307     -15.057   9.600  25.538  1.00 20.15           N  
ATOM   2362  CA  LYS A 307     -16.019   9.253  24.499  1.00 20.47           C  
ATOM   2363  C   LYS A 307     -15.423   8.269  23.496  1.00 20.60           C  
ATOM   2364  O   LYS A 307     -14.296   8.451  23.025  1.00 20.29           O  
ATOM   2365  CB  LYS A 307     -16.508  10.514  23.767  1.00 20.72           C  
ATOM   2366  CG  LYS A 307     -16.839  11.711  24.666  1.00 21.66           C  
ATOM   2367  CD  LYS A 307     -18.041  11.445  25.558  1.00 23.61           C  
ATOM   2368  CE  LYS A 307     -18.385  12.672  26.392  1.00 24.35           C  
ATOM   2369  NZ  LYS A 307     -19.466  12.362  27.364  1.00 25.74           N  
ATOM   2370  N   ASP A 308     -16.189   7.228  23.180  1.00 20.93           N  
ATOM   2371  CA  ASP A 308     -15.805   6.252  22.160  1.00 21.49           C  
ATOM   2372  C   ASP A 308     -17.054   5.572  21.598  1.00 22.03           C  
ATOM   2373  O   ASP A 308     -18.024   5.367  22.334  1.00 22.25           O  
ATOM   2374  CB  ASP A 308     -14.855   5.201  22.751  1.00 21.28           C  
ATOM   2375  CG  ASP A 308     -14.157   4.369  21.681  1.00 21.48           C  
ATOM   2376  OD1 ASP A 308     -14.545   3.204  21.491  1.00 22.07           O  
ATOM   2377  OD2 ASP A 308     -13.235   4.884  21.018  1.00 21.07           O  
ATOM   2378  N   PRO A 309     -17.048   5.243  20.289  1.00 22.46           N  
ATOM   2379  CA  PRO A 309     -18.157   4.476  19.709  1.00 23.00           C  
ATOM   2380  C   PRO A 309     -18.207   3.022  20.191  1.00 23.31           C  
ATOM   2381  O   PRO A 309     -19.290   2.440  20.261  1.00 24.09           O  
ATOM   2382  CB  PRO A 309     -17.874   4.514  18.199  1.00 22.94           C  
ATOM   2383  CG  PRO A 309     -16.808   5.534  18.002  1.00 22.89           C  
ATOM   2384  CD  PRO A 309     -16.037   5.594  19.275  1.00 22.40           C  
ATOM   2385  N   LEU A 310     -17.050   2.444  20.511  1.00 23.35           N  
ATOM   2386  CA  LEU A 310     -16.977   1.040  20.926  1.00 23.03           C  
ATOM   2387  C   LEU A 310     -16.981   0.876  22.452  1.00 22.41           C  
ATOM   2388  O   LEU A 310     -17.809   0.147  23.000  1.00 22.94           O  
ATOM   2389  CB  LEU A 310     -15.750   0.350  20.303  1.00 23.24           C  
ATOM   2390  CG  LEU A 310     -15.479  -1.144  20.557  1.00 23.41           C  
ATOM   2391  CD1 LEU A 310     -16.614  -2.051  20.066  1.00 24.66           C  
ATOM   2392  CD2 LEU A 310     -14.152  -1.563  19.924  1.00 23.31           C  
ATOM   2393  N   LEU A 311     -16.074   1.578  23.126  1.00 21.34           N  
ATOM   2394  CA  LEU A 311     -15.777   1.328  24.538  1.00 19.81           C  
ATOM   2395  C   LEU A 311     -16.712   2.002  25.528  1.00 19.01           C  
ATOM   2396  O   LEU A 311     -17.111   3.149  25.339  1.00 18.45           O  
ATOM   2397  CB  LEU A 311     -14.349   1.760  24.859  1.00 19.96           C  
ATOM   2398  CG  LEU A 311     -13.177   1.052  24.187  1.00 20.49           C  
ATOM   2399  CD1 LEU A 311     -11.900   1.707  24.667  1.00 20.78           C  
ATOM   2400  CD2 LEU A 311     -13.168  -0.445  24.483  1.00 21.25           C  
ATOM   2401  N   ASP A 312     -17.012   1.276  26.604  1.00 17.93           N  
ATOM   2402  CA  ASP A 312     -17.827   1.763  27.707  1.00 17.13           C  
ATOM   2403  C   ASP A 312     -17.506   0.903  28.922  1.00 16.37           C  
ATOM   2404  O   ASP A 312     -17.855  -0.269  28.951  1.00 16.19           O  
ATOM   2405  CB  ASP A 312     -19.308   1.627  27.357  1.00 17.56           C  
ATOM   2406  CG  ASP A 312     -20.200   2.299  28.364  1.00 17.82           C  
ATOM   2407  OD1 ASP A 312     -20.540   3.480  28.135  1.00 19.72           O  
ATOM   2408  OD2 ASP A 312     -20.536   1.661  29.386  1.00 18.06           O  
ATOM   2409  N   ASP A 313     -16.848   1.479  29.925  1.00 15.82           N  
ATOM   2410  CA  ASP A 313     -16.309   0.671  31.027  1.00 15.01           C  
ATOM   2411  C   ASP A 313     -17.359  -0.152  31.781  1.00 14.93           C  
ATOM   2412  O   ASP A 313     -17.146  -1.339  32.046  1.00 14.76           O  
ATOM   2413  CB  ASP A 313     -15.455   1.520  31.974  1.00 14.79           C  
ATOM   2414  CG  ASP A 313     -14.181   2.031  31.309  1.00 14.28           C  
ATOM   2415  OD1 ASP A 313     -13.532   1.264  30.557  1.00 13.95           O  
ATOM   2416  OD2 ASP A 313     -13.820   3.198  31.545  1.00 12.74           O  
ATOM   2417  N   HIS A 314     -18.492   0.467  32.103  1.00 15.09           N  
ATOM   2418  CA  HIS A 314     -19.573  -0.233  32.802  1.00 15.32           C  
ATOM   2419  C   HIS A 314     -20.222  -1.309  31.922  1.00 14.98           C  
ATOM   2420  O   HIS A 314     -20.360  -2.465  32.343  1.00 14.97           O  
ATOM   2421  CB  HIS A 314     -20.624   0.758  33.320  1.00 15.67           C  
ATOM   2422  CG  HIS A 314     -21.625   0.134  34.238  1.00 16.68           C  
ATOM   2423  ND1 HIS A 314     -22.732  -0.545  33.777  1.00 18.44           N  
ATOM   2424  CD2 HIS A 314     -21.673   0.062  35.589  1.00 17.80           C  
ATOM   2425  CE1 HIS A 314     -23.426  -0.998  34.806  1.00 18.56           C  
ATOM   2426  NE2 HIS A 314     -22.804  -0.645  35.917  1.00 18.16           N  
ATOM   2427  N   GLY A 315     -20.611  -0.923  30.708  1.00 14.95           N  
ATOM   2428  CA  GLY A 315     -21.177  -1.849  29.728  1.00 15.10           C  
ATOM   2429  C   GLY A 315     -20.247  -3.006  29.399  1.00 14.94           C  
ATOM   2430  O   GLY A 315     -20.695  -4.144  29.279  1.00 15.23           O  
ATOM   2431  N   ASP A 316     -18.954  -2.711  29.256  1.00 14.95           N  
ATOM   2432  CA  ASP A 316     -17.943  -3.735  28.952  1.00 14.78           C  
ATOM   2433  C   ASP A 316     -17.689  -4.681  30.130  1.00 14.50           C  
ATOM   2434  O   ASP A 316     -17.408  -5.855  29.923  1.00 14.38           O  
ATOM   2435  CB  ASP A 316     -16.626  -3.107  28.460  1.00 15.08           C  
ATOM   2436  CG  ASP A 316     -16.760  -2.435  27.091  1.00 16.37           C  
ATOM   2437  OD1 ASP A 316     -17.655  -2.814  26.304  1.00 16.93           O  
ATOM   2438  OD2 ASP A 316     -15.960  -1.516  26.802  1.00 16.40           O  
ATOM   2439  N   PHE A 317     -17.791  -4.179  31.358  1.00 14.49           N  
ATOM   2440  CA  PHE A 317     -17.718  -5.061  32.527  1.00 14.59           C  
ATOM   2441  C   PHE A 317     -18.837  -6.104  32.461  1.00 14.49           C  
ATOM   2442  O   PHE A 317     -18.584  -7.302  32.595  1.00 13.90           O  
ATOM   2443  CB  PHE A 317     -17.797  -4.278  33.843  1.00 14.42           C  
ATOM   2444  CG  PHE A 317     -17.713  -5.153  35.073  1.00 14.76           C  
ATOM   2445  CD1 PHE A 317     -16.485  -5.667  35.498  1.00 14.90           C  
ATOM   2446  CD2 PHE A 317     -18.861  -5.480  35.798  1.00 15.27           C  
ATOM   2447  CE1 PHE A 317     -16.399  -6.480  36.628  1.00 15.35           C  
ATOM   2448  CE2 PHE A 317     -18.782  -6.295  36.937  1.00 15.21           C  
ATOM   2449  CZ  PHE A 317     -17.546  -6.794  37.346  1.00 14.86           C  
ATOM   2450  N   ILE A 318     -20.064  -5.635  32.231  1.00 15.12           N  
ATOM   2451  CA  ILE A 318     -21.230  -6.519  32.109  1.00 16.20           C  
ATOM   2452  C   ILE A 318     -21.024  -7.526  30.975  1.00 16.30           C  
ATOM   2453  O   ILE A 318     -21.210  -8.733  31.163  1.00 16.44           O  
ATOM   2454  CB  ILE A 318     -22.549  -5.713  31.898  1.00 16.22           C  
ATOM   2455  CG1 ILE A 318     -22.829  -4.817  33.113  1.00 16.45           C  
ATOM   2456  CG2 ILE A 318     -23.728  -6.657  31.604  1.00 17.12           C  
ATOM   2457  CD1 ILE A 318     -24.025  -3.885  32.947  1.00 17.23           C  
ATOM   2458  N   ARG A 319     -20.622  -7.025  29.809  1.00 16.81           N  
ATOM   2459  CA  ARG A 319     -20.411  -7.870  28.633  1.00 17.58           C  
ATOM   2460  C   ARG A 319     -19.302  -8.892  28.861  1.00 17.10           C  
ATOM   2461  O   ARG A 319     -19.409 -10.043  28.426  1.00 17.14           O  
ATOM   2462  CB  ARG A 319     -20.125  -7.018  27.393  1.00 17.68           C  
ATOM   2463  CG  ARG A 319     -21.379  -6.443  26.743  1.00 19.00           C  
ATOM   2464  CD  ARG A 319     -21.049  -5.694  25.453  1.00 19.27           C  
ATOM   2465  NE  ARG A 319     -20.409  -4.406  25.715  1.00 22.56           N  
ATOM   2466  CZ  ARG A 319     -21.063  -3.259  25.896  1.00 22.86           C  
ATOM   2467  NH1 ARG A 319     -22.390  -3.226  25.839  1.00 24.03           N  
ATOM   2468  NH2 ARG A 319     -20.387  -2.143  26.135  1.00 22.98           N  
ATOM   2469  N   MET A 320     -18.249  -8.469  29.561  1.00 16.68           N  
ATOM   2470  CA  MET A 320     -17.136  -9.353  29.900  1.00 16.70           C  
ATOM   2471  C   MET A 320     -17.590 -10.484  30.820  1.00 16.40           C  
ATOM   2472  O   MET A 320     -17.238 -11.641  30.607  1.00 16.58           O  
ATOM   2473  CB  MET A 320     -16.005  -8.559  30.551  1.00 16.63           C  
ATOM   2474  CG  MET A 320     -14.794  -9.385  30.953  1.00 16.57           C  
ATOM   2475  SD  MET A 320     -13.697  -8.467  32.055  1.00 17.15           S  
ATOM   2476  CE  MET A 320     -14.711  -8.319  33.533  1.00 17.95           C  
ATOM   2477  N   CYS A 321     -18.376 -10.143  31.837  1.00 16.57           N  
ATOM   2478  CA  CYS A 321     -18.898 -11.139  32.774  1.00 16.90           C  
ATOM   2479  C   CYS A 321     -19.842 -12.132  32.097  1.00 17.25           C  
ATOM   2480  O   CYS A 321     -19.815 -13.329  32.409  1.00 17.06           O  
ATOM   2481  CB  CYS A 321     -19.572 -10.454  33.963  1.00 17.05           C  
ATOM   2482  SG  CYS A 321     -18.395  -9.619  35.045  1.00 17.88           S  
ATOM   2483  N   THR A 322     -20.653 -11.635  31.163  1.00 17.74           N  
ATOM   2484  CA  THR A 322     -21.518 -12.492  30.348  1.00 18.50           C  
ATOM   2485  C   THR A 322     -20.660 -13.442  29.511  1.00 18.63           C  
ATOM   2486  O   THR A 322     -20.911 -14.651  29.486  1.00 18.58           O  
ATOM   2487  CB  THR A 322     -22.470 -11.665  29.448  1.00 18.57           C  
ATOM   2488  OG1 THR A 322     -23.304 -10.837  30.268  1.00 19.28           O  
ATOM   2489  CG2 THR A 322     -23.361 -12.576  28.609  1.00 19.24           C  
ATOM   2490  N   ALA A 323     -19.644 -12.883  28.853  1.00 18.93           N  
ATOM   2491  CA  ALA A 323     -18.681 -13.648  28.059  1.00 19.53           C  
ATOM   2492  C   ALA A 323     -18.007 -14.752  28.875  1.00 19.98           C  
ATOM   2493  O   ALA A 323     -17.912 -15.890  28.416  1.00 19.86           O  
ATOM   2494  CB  ALA A 323     -17.632 -12.717  27.449  1.00 19.61           C  
ATOM   2495  N   MET A 324     -17.552 -14.411  30.083  1.00 20.55           N  
ATOM   2496  CA  MET A 324     -16.913 -15.381  30.978  1.00 21.61           C  
ATOM   2497  C   MET A 324     -17.841 -16.563  31.273  1.00 21.61           C  
ATOM   2498  O   MET A 324     -17.414 -17.720  31.241  1.00 21.58           O  
ATOM   2499  CB  MET A 324     -16.481 -14.718  32.292  1.00 21.54           C  
ATOM   2500  CG  MET A 324     -15.290 -13.765  32.194  1.00 22.11           C  
ATOM   2501  SD  MET A 324     -14.972 -13.035  33.815  1.00 23.76           S  
ATOM   2502  CE  MET A 324     -13.589 -11.948  33.495  1.00 23.64           C  
ATOM   2503  N   LYS A 325     -19.108 -16.259  31.547  1.00 22.00           N  
ATOM   2504  CA  LYS A 325     -20.113 -17.280  31.843  1.00 22.71           C  
ATOM   2505  C   LYS A 325     -20.401 -18.172  30.638  1.00 22.82           C  
ATOM   2506  O   LYS A 325     -20.451 -19.399  30.770  1.00 22.91           O  
ATOM   2507  CB  LYS A 325     -21.409 -16.638  32.346  1.00 23.04           C  
ATOM   2508  CG  LYS A 325     -21.361 -16.178  33.788  1.00 24.80           C  
ATOM   2509  CD  LYS A 325     -22.731 -15.690  34.246  1.00 28.08           C  
ATOM   2510  CE  LYS A 325     -22.689 -15.155  35.669  1.00 29.47           C  
ATOM   2511  NZ  LYS A 325     -23.900 -14.342  35.984  1.00 31.04           N  
ATOM   2512  N   LYS A 326     -20.572 -17.557  29.470  1.00 22.88           N  
ATOM   2513  CA  LYS A 326     -20.893 -18.297  28.248  1.00 23.33           C  
ATOM   2514  C   LYS A 326     -19.811 -19.305  27.864  1.00 23.15           C  
ATOM   2515  O   LYS A 326     -20.122 -20.405  27.403  1.00 23.51           O  
ATOM   2516  CB  LYS A 326     -21.172 -17.349  27.077  1.00 23.36           C  
ATOM   2517  CG  LYS A 326     -22.461 -16.551  27.211  1.00 24.98           C  
ATOM   2518  CD  LYS A 326     -23.282 -16.623  25.930  1.00 27.21           C  
ATOM   2519  CE  LYS A 326     -24.240 -15.449  25.796  1.00 27.63           C  
ATOM   2520  NZ  LYS A 326     -23.651 -14.362  24.973  1.00 28.62           N  
ATOM   2521  N   ILE A 327     -18.549 -18.932  28.070  1.00 22.81           N  
ATOM   2522  CA  ILE A 327     -17.418 -19.776  27.669  1.00 22.68           C  
ATOM   2523  C   ILE A 327     -17.034 -20.819  28.729  1.00 22.72           C  
ATOM   2524  O   ILE A 327     -16.171 -21.669  28.489  1.00 22.43           O  
ATOM   2525  CB  ILE A 327     -16.176 -18.942  27.225  1.00 22.58           C  
ATOM   2526  CG1 ILE A 327     -15.519 -18.230  28.415  1.00 22.71           C  
ATOM   2527  CG2 ILE A 327     -16.559 -17.969  26.107  1.00 22.48           C  
ATOM   2528  CD1 ILE A 327     -14.222 -17.503  28.067  1.00 22.72           C  
ATOM   2529  N   GLY A 328     -17.668 -20.746  29.897  1.00 22.91           N  
ATOM   2530  CA  GLY A 328     -17.513 -21.787  30.913  1.00 23.21           C  
ATOM   2531  C   GLY A 328     -16.736 -21.444  32.174  1.00 23.55           C  
ATOM   2532  O   GLY A 328     -16.420 -22.337  32.963  1.00 23.48           O  
ATOM   2533  N   LEU A 329     -16.416 -20.167  32.377  1.00 23.79           N  
ATOM   2534  CA  LEU A 329     -15.779 -19.756  33.632  1.00 24.22           C  
ATOM   2535  C   LEU A 329     -16.831 -19.663  34.724  1.00 24.68           C  
ATOM   2536  O   LEU A 329     -17.852 -18.993  34.550  1.00 24.88           O  
ATOM   2537  CB  LEU A 329     -15.048 -18.414  33.491  1.00 24.16           C  
ATOM   2538  CG  LEU A 329     -13.596 -18.442  33.015  1.00 24.01           C  
ATOM   2539  CD1 LEU A 329     -13.522 -18.650  31.514  1.00 24.43           C  
ATOM   2540  CD2 LEU A 329     -12.883 -17.153  33.409  1.00 24.09           C  
ATOM   2541  N   ASP A 330     -16.592 -20.344  35.842  1.00 25.07           N  
ATOM   2542  CA  ASP A 330     -17.531 -20.278  36.956  1.00 25.36           C  
ATOM   2543  C   ASP A 330     -17.281 -19.033  37.802  1.00 25.39           C  
ATOM   2544  O   ASP A 330     -16.265 -18.351  37.628  1.00 25.11           O  
ATOM   2545  CB  ASP A 330     -17.538 -21.575  37.789  1.00 25.89           C  
ATOM   2546  CG  ASP A 330     -16.213 -21.864  38.476  1.00 26.71           C  
ATOM   2547  OD1 ASP A 330     -15.491 -20.919  38.857  1.00 27.65           O  
ATOM   2548  OD2 ASP A 330     -15.905 -23.062  38.669  1.00 28.59           O  
ATOM   2549  N   ASP A 331     -18.214 -18.737  38.702  1.00 25.31           N  
ATOM   2550  CA  ASP A 331     -18.156 -17.517  39.503  1.00 25.36           C  
ATOM   2551  C   ASP A 331     -16.917 -17.453  40.402  1.00 24.85           C  
ATOM   2552  O   ASP A 331     -16.385 -16.367  40.644  1.00 24.76           O  
ATOM   2553  CB  ASP A 331     -19.449 -17.333  40.310  1.00 26.01           C  
ATOM   2554  CG  ASP A 331     -20.658 -17.012  39.425  1.00 27.51           C  
ATOM   2555  OD1 ASP A 331     -20.476 -16.712  38.221  1.00 28.93           O  
ATOM   2556  OD2 ASP A 331     -21.798 -17.062  39.939  1.00 30.01           O  
ATOM   2557  N   GLU A 332     -16.453 -18.613  40.872  1.00 24.28           N  
ATOM   2558  CA  GLU A 332     -15.226 -18.691  41.673  1.00 24.11           C  
ATOM   2559  C   GLU A 332     -14.017 -18.210  40.872  1.00 23.17           C  
ATOM   2560  O   GLU A 332     -13.223 -17.404  41.364  1.00 23.07           O  
ATOM   2561  CB  GLU A 332     -14.983 -20.113  42.195  1.00 24.25           C  
ATOM   2562  CG  GLU A 332     -13.738 -20.242  43.079  1.00 25.38           C  
ATOM   2563  CD  GLU A 332     -13.517 -21.644  43.616  1.00 25.61           C  
ATOM   2564  OE1 GLU A 332     -12.340 -22.044  43.748  1.00 27.98           O  
ATOM   2565  OE2 GLU A 332     -14.507 -22.345  43.915  1.00 28.36           O  
ATOM   2566  N   GLU A 333     -13.901 -18.702  39.638  1.00 22.20           N  
ATOM   2567  CA  GLU A 333     -12.833 -18.305  38.720  1.00 21.56           C  
ATOM   2568  C   GLU A 333     -12.863 -16.801  38.477  1.00 20.66           C  
ATOM   2569  O   GLU A 333     -11.832 -16.137  38.548  1.00 20.36           O  
ATOM   2570  CB  GLU A 333     -12.966 -19.033  37.383  1.00 21.78           C  
ATOM   2571  CG  GLU A 333     -12.852 -20.541  37.456  1.00 23.41           C  
ATOM   2572  CD  GLU A 333     -12.718 -21.165  36.085  1.00 25.42           C  
ATOM   2573  OE1 GLU A 333     -11.651 -20.975  35.468  1.00 25.87           O  
ATOM   2574  OE2 GLU A 333     -13.669 -21.842  35.628  1.00 25.37           O  
ATOM   2575  N   LYS A 334     -14.055 -16.278  38.197  1.00 19.67           N  
ATOM   2576  CA  LYS A 334     -14.259 -14.844  37.993  1.00 19.12           C  
ATOM   2577  C   LYS A 334     -13.753 -14.023  39.186  1.00 18.47           C  
ATOM   2578  O   LYS A 334     -13.005 -13.055  39.018  1.00 17.67           O  
ATOM   2579  CB  LYS A 334     -15.741 -14.564  37.721  1.00 19.16           C  
ATOM   2580  CG  LYS A 334     -16.099 -13.097  37.512  1.00 19.62           C  
ATOM   2581  CD  LYS A 334     -17.517 -12.923  36.955  1.00 20.57           C  
ATOM   2582  CE  LYS A 334     -18.603 -13.366  37.938  1.00 22.59           C  
ATOM   2583  NZ  LYS A 334     -19.978 -13.316  37.331  1.00 23.50           N  
ATOM   2584  N   LEU A 335     -14.156 -14.426  40.389  1.00 17.74           N  
ATOM   2585  CA  LEU A 335     -13.771 -13.710  41.604  1.00 17.66           C  
ATOM   2586  C   LEU A 335     -12.272 -13.824  41.892  1.00 17.03           C  
ATOM   2587  O   LEU A 335     -11.659 -12.866  42.370  1.00 16.72           O  
ATOM   2588  CB  LEU A 335     -14.616 -14.161  42.802  1.00 18.07           C  
ATOM   2589  CG  LEU A 335     -16.118 -13.848  42.705  1.00 19.40           C  
ATOM   2590  CD1 LEU A 335     -16.872 -14.333  43.937  1.00 21.14           C  
ATOM   2591  CD2 LEU A 335     -16.382 -12.363  42.466  1.00 20.52           C  
ATOM   2592  N   ASP A 336     -11.692 -14.983  41.572  1.00 16.65           N  
ATOM   2593  CA  ASP A 336     -10.244 -15.188  41.677  1.00 16.34           C  
ATOM   2594  C   ASP A 336      -9.502 -14.167  40.812  1.00 15.60           C  
ATOM   2595  O   ASP A 336      -8.561 -13.520  41.272  1.00 15.65           O  
ATOM   2596  CB  ASP A 336      -9.849 -16.612  41.257  1.00 16.75           C  
ATOM   2597  CG  ASP A 336     -10.146 -17.663  42.326  1.00 18.14           C  
ATOM   2598  OD1 ASP A 336     -10.402 -17.306  43.499  1.00 19.58           O  
ATOM   2599  OD2 ASP A 336     -10.105 -18.866  41.983  1.00 19.62           O  
ATOM   2600  N   LEU A 337      -9.941 -14.017  39.564  1.00 14.71           N  
ATOM   2601  CA  LEU A 337      -9.337 -13.040  38.655  1.00 13.96           C  
ATOM   2602  C   LEU A 337      -9.410 -11.634  39.230  1.00 13.61           C  
ATOM   2603  O   LEU A 337      -8.405 -10.921  39.276  1.00 13.11           O  
ATOM   2604  CB  LEU A 337     -10.009 -13.083  37.278  1.00 13.80           C  
ATOM   2605  CG  LEU A 337      -9.872 -14.361  36.442  1.00 13.60           C  
ATOM   2606  CD1 LEU A 337     -10.722 -14.210  35.196  1.00 14.13           C  
ATOM   2607  CD2 LEU A 337      -8.421 -14.633  36.074  1.00 13.01           C  
ATOM   2608  N   PHE A 338     -10.600 -11.241  39.680  1.00 13.52           N  
ATOM   2609  CA  PHE A 338     -10.811  -9.907  40.234  1.00 13.71           C  
ATOM   2610  C   PHE A 338      -9.950  -9.673  41.474  1.00 13.73           C  
ATOM   2611  O   PHE A 338      -9.428  -8.578  41.671  1.00 13.51           O  
ATOM   2612  CB  PHE A 338     -12.285  -9.673  40.585  1.00 14.17           C  
ATOM   2613  CG  PHE A 338     -13.214  -9.660  39.394  1.00 14.33           C  
ATOM   2614  CD1 PHE A 338     -14.592  -9.762  39.586  1.00 14.64           C  
ATOM   2615  CD2 PHE A 338     -12.724  -9.565  38.090  1.00 14.20           C  
ATOM   2616  CE1 PHE A 338     -15.464  -9.744  38.505  1.00 15.25           C  
ATOM   2617  CE2 PHE A 338     -13.592  -9.552  36.997  1.00 15.30           C  
ATOM   2618  CZ  PHE A 338     -14.963  -9.642  37.207  1.00 15.06           C  
ATOM   2619  N   ARG A 339      -9.809 -10.716  42.291  1.00 13.83           N  
ATOM   2620  CA  ARG A 339      -9.050 -10.651  43.540  1.00 14.29           C  
ATOM   2621  C   ARG A 339      -7.582 -10.320  43.278  1.00 13.68           C  
ATOM   2622  O   ARG A 339      -7.008  -9.457  43.948  1.00 13.71           O  
ATOM   2623  CB  ARG A 339      -9.186 -11.969  44.309  1.00 14.42           C  
ATOM   2624  CG  ARG A 339      -8.448 -12.023  45.639  1.00 15.72           C  
ATOM   2625  CD  ARG A 339      -8.906 -13.223  46.479  1.00 15.80           C  
ATOM   2626  NE  ARG A 339      -8.857 -14.490  45.740  1.00 19.06           N  
ATOM   2627  CZ  ARG A 339      -7.757 -15.218  45.555  1.00 20.38           C  
ATOM   2628  NH1 ARG A 339      -6.586 -14.814  46.045  1.00 21.62           N  
ATOM   2629  NH2 ARG A 339      -7.826 -16.354  44.870  1.00 22.01           N  
ATOM   2630  N   VAL A 340      -6.987 -10.998  42.299  1.00 13.18           N  
ATOM   2631  CA  VAL A 340      -5.587 -10.751  41.933  1.00 12.75           C  
ATOM   2632  C   VAL A 340      -5.415  -9.325  41.371  1.00 12.18           C  
ATOM   2633  O   VAL A 340      -4.458  -8.636  41.706  1.00 11.77           O  
ATOM   2634  CB  VAL A 340      -5.037 -11.832  40.964  1.00 12.81           C  
ATOM   2635  CG1 VAL A 340      -3.591 -11.527  40.555  1.00 12.96           C  
ATOM   2636  CG2 VAL A 340      -5.113 -13.217  41.606  1.00 13.49           C  
ATOM   2637  N   VAL A 341      -6.354  -8.885  40.536  1.00 12.12           N  
ATOM   2638  CA  VAL A 341      -6.342  -7.517  40.010  1.00 11.79           C  
ATOM   2639  C   VAL A 341      -6.318  -6.487  41.155  1.00 11.82           C  
ATOM   2640  O   VAL A 341      -5.469  -5.586  41.181  1.00 11.37           O  
ATOM   2641  CB  VAL A 341      -7.542  -7.280  39.047  1.00 11.89           C  
ATOM   2642  CG1 VAL A 341      -7.697  -5.807  38.705  1.00 11.18           C  
ATOM   2643  CG2 VAL A 341      -7.372  -8.117  37.779  1.00 11.63           C  
ATOM   2644  N   ALA A 342      -7.229  -6.648  42.115  1.00 11.57           N  
ATOM   2645  CA  ALA A 342      -7.281  -5.777  43.284  1.00 12.07           C  
ATOM   2646  C   ALA A 342      -6.014  -5.884  44.147  1.00 11.73           C  
ATOM   2647  O   ALA A 342      -5.548  -4.880  44.696  1.00 12.41           O  
ATOM   2648  CB  ALA A 342      -8.524  -6.082  44.111  1.00 11.90           C  
ATOM   2649  N   GLY A 343      -5.461  -7.091  44.244  1.00 12.07           N  
ATOM   2650  CA  GLY A 343      -4.221  -7.329  44.995  1.00 11.92           C  
ATOM   2651  C   GLY A 343      -3.063  -6.535  44.417  1.00 11.84           C  
ATOM   2652  O   GLY A 343      -2.275  -5.937  45.152  1.00 11.77           O  
ATOM   2653  N   VAL A 344      -2.970  -6.519  43.090  1.00 11.54           N  
ATOM   2654  CA  VAL A 344      -1.964  -5.711  42.390  1.00 11.46           C  
ATOM   2655  C   VAL A 344      -2.160  -4.211  42.662  1.00 11.30           C  
ATOM   2656  O   VAL A 344      -1.192  -3.478  42.893  1.00 11.21           O  
ATOM   2657  CB  VAL A 344      -1.964  -6.021  40.868  1.00 11.21           C  
ATOM   2658  CG1 VAL A 344      -1.126  -5.003  40.091  1.00 12.11           C  
ATOM   2659  CG2 VAL A 344      -1.439  -7.428  40.618  1.00 11.82           C  
ATOM   2660  N   LEU A 345      -3.412  -3.754  42.646  1.00 11.52           N  
ATOM   2661  CA  LEU A 345      -3.714  -2.361  42.973  1.00 11.85           C  
ATOM   2662  C   LEU A 345      -3.258  -1.967  44.385  1.00 12.11           C  
ATOM   2663  O   LEU A 345      -2.594  -0.946  44.556  1.00 12.92           O  
ATOM   2664  CB  LEU A 345      -5.200  -2.050  42.781  1.00 11.64           C  
ATOM   2665  CG  LEU A 345      -5.683  -1.878  41.335  1.00 11.34           C  
ATOM   2666  CD1 LEU A 345      -7.190  -1.630  41.302  1.00 11.19           C  
ATOM   2667  CD2 LEU A 345      -4.933  -0.744  40.637  1.00 10.91           C  
ATOM   2668  N   HIS A 346      -3.598  -2.776  45.385  1.00 12.94           N  
ATOM   2669  CA  HIS A 346      -3.180  -2.482  46.760  1.00 13.31           C  
ATOM   2670  C   HIS A 346      -1.665  -2.566  46.949  1.00 13.41           C  
ATOM   2671  O   HIS A 346      -1.083  -1.783  47.704  1.00 13.73           O  
ATOM   2672  CB  HIS A 346      -3.934  -3.362  47.759  1.00 13.71           C  
ATOM   2673  CG  HIS A 346      -5.406  -3.087  47.790  1.00 13.22           C  
ATOM   2674  ND1 HIS A 346      -5.923  -1.871  48.179  1.00 14.26           N  
ATOM   2675  CD2 HIS A 346      -6.468  -3.866  47.476  1.00 13.61           C  
ATOM   2676  CE1 HIS A 346      -7.241  -1.910  48.093  1.00 13.84           C  
ATOM   2677  NE2 HIS A 346      -7.597  -3.110  47.673  1.00 12.64           N  
ATOM   2678  N   LEU A 347      -1.033  -3.505  46.253  1.00 13.53           N  
ATOM   2679  CA  LEU A 347       0.431  -3.598  46.231  1.00 13.92           C  
ATOM   2680  C   LEU A 347       1.065  -2.261  45.863  1.00 14.10           C  
ATOM   2681  O   LEU A 347       2.013  -1.823  46.517  1.00 14.37           O  
ATOM   2682  CB  LEU A 347       0.904  -4.692  45.269  1.00 13.78           C  
ATOM   2683  CG  LEU A 347       2.410  -4.945  45.128  1.00 13.70           C  
ATOM   2684  CD1 LEU A 347       3.109  -5.082  46.496  1.00 14.39           C  
ATOM   2685  CD2 LEU A 347       2.655  -6.180  44.278  1.00 13.93           C  
ATOM   2686  N   GLY A 348       0.526  -1.615  44.827  1.00 13.96           N  
ATOM   2687  CA  GLY A 348       1.051  -0.339  44.341  1.00 14.25           C  
ATOM   2688  C   GLY A 348       0.915   0.812  45.311  1.00 14.73           C  
ATOM   2689  O   GLY A 348       1.645   1.796  45.213  1.00 14.94           O  
ATOM   2690  N   ASN A 349      -0.025   0.684  46.247  1.00 14.88           N  
ATOM   2691  CA  ASN A 349      -0.272   1.723  47.237  1.00 15.50           C  
ATOM   2692  C   ASN A 349       0.687   1.684  48.427  1.00 15.89           C  
ATOM   2693  O   ASN A 349       0.671   2.594  49.258  1.00 16.36           O  
ATOM   2694  CB  ASN A 349      -1.726   1.686  47.710  1.00 15.30           C  
ATOM   2695  CG  ASN A 349      -2.668   2.388  46.748  1.00 15.21           C  
ATOM   2696  OD1 ASN A 349      -2.235   2.988  45.764  1.00 14.70           O  
ATOM   2697  ND2 ASN A 349      -3.961   2.331  47.039  1.00 14.59           N  
ATOM   2698  N   ILE A 350       1.508   0.637  48.503  1.00 16.14           N  
ATOM   2699  CA  ILE A 350       2.520   0.517  49.563  1.00 16.83           C  
ATOM   2700  C   ILE A 350       3.690   1.477  49.314  1.00 17.48           C  
ATOM   2701  O   ILE A 350       4.340   1.416  48.266  1.00 17.50           O  
ATOM   2702  CB  ILE A 350       3.032  -0.937  49.716  1.00 16.79           C  
ATOM   2703  CG1 ILE A 350       1.886  -1.871  50.129  1.00 16.72           C  
ATOM   2704  CG2 ILE A 350       4.180  -1.005  50.727  1.00 16.64           C  
ATOM   2705  CD1 ILE A 350       2.234  -3.341  50.114  1.00 16.95           C  
ATOM   2706  N   ASP A 351       3.931   2.359  50.286  1.00 18.06           N  
ATOM   2707  CA  ASP A 351       4.953   3.406  50.210  1.00 18.95           C  
ATOM   2708  C   ASP A 351       6.062   3.138  51.216  1.00 18.92           C  
ATOM   2709  O   ASP A 351       5.817   2.534  52.261  1.00 18.74           O  
ATOM   2710  CB  ASP A 351       4.353   4.768  50.561  1.00 19.55           C  
ATOM   2711  CG  ASP A 351       3.356   5.262  49.536  1.00 21.91           C  
ATOM   2712  OD1 ASP A 351       3.510   4.927  48.349  1.00 24.64           O  
ATOM   2713  OD2 ASP A 351       2.434   6.012  49.923  1.00 25.59           O  
ATOM   2714  N   PHE A 352       7.262   3.635  50.917  1.00 19.01           N  
ATOM   2715  CA  PHE A 352       8.429   3.436  51.783  1.00 19.03           C  
ATOM   2716  C   PHE A 352       9.084   4.757  52.181  1.00 19.64           C  
ATOM   2717  O   PHE A 352       8.968   5.763  51.477  1.00 19.69           O  
ATOM   2718  CB  PHE A 352       9.459   2.518  51.109  1.00 18.70           C  
ATOM   2719  CG  PHE A 352       8.862   1.271  50.517  1.00 17.95           C  
ATOM   2720  CD1 PHE A 352       8.522   1.223  49.165  1.00 18.02           C  
ATOM   2721  CD2 PHE A 352       8.625   0.152  51.307  1.00 17.19           C  
ATOM   2722  CE1 PHE A 352       7.960   0.075  48.612  1.00 17.00           C  
ATOM   2723  CE2 PHE A 352       8.062  -1.000  50.763  1.00 17.45           C  
ATOM   2724  CZ  PHE A 352       7.728  -1.036  49.409  1.00 17.25           C  
ATOM   2725  N   GLU A 353       9.774   4.740  53.320  1.00 19.97           N  
ATOM   2726  CA  GLU A 353      10.480   5.919  53.815  1.00 20.72           C  
ATOM   2727  C   GLU A 353      11.842   5.536  54.380  1.00 20.56           C  
ATOM   2728  O   GLU A 353      12.053   4.393  54.770  1.00 19.81           O  
ATOM   2729  CB  GLU A 353       9.647   6.658  54.869  1.00 20.53           C  
ATOM   2730  CG  GLU A 353       9.375   5.883  56.159  1.00 21.89           C  
ATOM   2731  CD  GLU A 353       8.461   6.636  57.116  1.00 22.33           C  
ATOM   2732  OE1 GLU A 353       8.574   6.422  58.341  1.00 24.93           O  
ATOM   2733  OE2 GLU A 353       7.629   7.442  56.646  1.00 25.20           O  
ATOM   2734  N   GLU A 354      12.753   6.506  54.411  1.00 20.97           N  
ATOM   2735  CA  GLU A 354      14.081   6.332  54.998  1.00 21.51           C  
ATOM   2736  C   GLU A 354      13.978   5.889  56.453  1.00 20.95           C  
ATOM   2737  O   GLU A 354      13.230   6.480  57.236  1.00 21.18           O  
ATOM   2738  CB  GLU A 354      14.859   7.650  54.935  1.00 21.87           C  
ATOM   2739  CG  GLU A 354      14.896   8.303  53.562  1.00 24.72           C  
ATOM   2740  CD  GLU A 354      16.126   7.932  52.758  1.00 28.50           C  
ATOM   2741  OE1 GLU A 354      16.883   8.858  52.385  1.00 30.42           O  
ATOM   2742  OE2 GLU A 354      16.342   6.727  52.503  1.00 30.69           O  
ATOM   2743  N   ALA A 355      14.720   4.842  56.801  1.00 20.85           N  
ATOM   2744  CA  ALA A 355      14.771   4.356  58.179  1.00 20.70           C  
ATOM   2745  C   ALA A 355      15.784   5.139  59.010  1.00 20.69           C  
ATOM   2746  O   ALA A 355      15.688   5.185  60.239  1.00 20.59           O  
ATOM   2747  CB  ALA A 355      15.103   2.871  58.207  1.00 20.64           C  
ATOM   2748  N   GLY A 356      16.762   5.741  58.336  1.00 20.64           N  
ATOM   2749  CA  GLY A 356      17.870   6.393  59.026  1.00 21.09           C  
ATOM   2750  C   GLY A 356      18.840   5.356  59.563  1.00 21.20           C  
ATOM   2751  O   GLY A 356      18.929   4.251  59.034  1.00 21.51           O  
ATOM   2752  N   SER A 357      19.536   5.696  60.642  1.00 21.58           N  
ATOM   2753  CA  SER A 357      20.665   4.899  61.122  1.00 21.91           C  
ATOM   2754  C   SER A 357      20.309   3.605  61.865  1.00 21.83           C  
ATOM   2755  O   SER A 357      21.199   2.890  62.335  1.00 21.67           O  
ATOM   2756  CB  SER A 357      21.581   5.772  61.979  1.00 22.07           C  
ATOM   2757  OG  SER A 357      22.072   6.857  61.218  1.00 24.13           O  
ATOM   2758  N   THR A 358      19.018   3.296  61.962  1.00 21.46           N  
ATOM   2759  CA  THR A 358      18.582   2.043  62.585  1.00 21.31           C  
ATOM   2760  C   THR A 358      19.043   0.841  61.757  1.00 21.58           C  
ATOM   2761  O   THR A 358      19.897   0.065  62.194  1.00 21.14           O  
ATOM   2762  CB  THR A 358      17.053   1.996  62.778  1.00 21.22           C  
ATOM   2763  OG1 THR A 358      16.405   2.241  61.520  1.00 20.81           O  
ATOM   2764  CG2 THR A 358      16.613   3.037  63.797  1.00 21.09           C  
ATOM   2765  N   SER A 359      18.487   0.707  60.557  1.00 22.14           N  
ATOM   2766  CA  SER A 359      18.852  -0.374  59.645  1.00 22.58           C  
ATOM   2767  C   SER A 359      19.713   0.127  58.491  1.00 22.74           C  
ATOM   2768  O   SER A 359      20.398  -0.664  57.842  1.00 23.45           O  
ATOM   2769  CB  SER A 359      17.593  -1.024  59.075  1.00 22.61           C  
ATOM   2770  OG  SER A 359      16.866  -0.085  58.303  1.00 23.03           O  
ATOM   2771  N   GLY A 360      19.665   1.435  58.238  1.00 22.87           N  
ATOM   2772  CA  GLY A 360      20.294   2.040  57.062  1.00 22.87           C  
ATOM   2773  C   GLY A 360      19.451   1.911  55.800  1.00 22.86           C  
ATOM   2774  O   GLY A 360      19.817   2.435  54.742  1.00 23.61           O  
ATOM   2775  N   GLY A 361      18.320   1.217  55.914  1.00 22.18           N  
ATOM   2776  CA  GLY A 361      17.456   0.935  54.766  1.00 21.50           C  
ATOM   2777  C   GLY A 361      16.178   1.747  54.757  1.00 20.82           C  
ATOM   2778  O   GLY A 361      16.209   2.978  54.797  1.00 20.77           O  
ATOM   2779  N   CYS A 362      15.047   1.052  54.704  1.00 20.46           N  
ATOM   2780  CA  CYS A 362      13.748   1.712  54.654  1.00 20.28           C  
ATOM   2781  C   CYS A 362      12.691   0.968  55.464  1.00 20.04           C  
ATOM   2782  O   CYS A 362      12.850  -0.214  55.773  1.00 19.94           O  
ATOM   2783  CB  CYS A 362      13.285   1.878  53.201  1.00 20.11           C  
ATOM   2784  SG  CYS A 362      12.842   0.341  52.366  1.00 20.92           S  
ATOM   2785  N   ASN A 363      11.628   1.690  55.815  1.00 19.88           N  
ATOM   2786  CA  ASN A 363      10.435   1.122  56.431  1.00 20.05           C  
ATOM   2787  C   ASN A 363       9.227   1.442  55.563  1.00 20.11           C  
ATOM   2788  O   ASN A 363       9.263   2.385  54.771  1.00 19.84           O  
ATOM   2789  CB  ASN A 363      10.196   1.721  57.825  1.00 20.08           C  
ATOM   2790  CG  ASN A 363      11.373   1.529  58.764  1.00 20.57           C  
ATOM   2791  OD1 ASN A 363      11.767   2.454  59.477  1.00 22.02           O  
ATOM   2792  ND2 ASN A 363      11.935   0.330  58.774  1.00 20.23           N  
ATOM   2793  N   LEU A 364       8.161   0.661  55.711  1.00 20.47           N  
ATOM   2794  CA  LEU A 364       6.868   1.039  55.143  1.00 21.09           C  
ATOM   2795  C   LEU A 364       6.360   2.275  55.873  1.00 21.57           C  
ATOM   2796  O   LEU A 364       6.502   2.374  57.097  1.00 21.66           O  
ATOM   2797  CB  LEU A 364       5.849  -0.093  55.294  1.00 21.08           C  
ATOM   2798  CG  LEU A 364       5.655  -1.084  54.144  1.00 21.50           C  
ATOM   2799  CD1 LEU A 364       6.853  -2.007  53.982  1.00 22.08           C  
ATOM   2800  CD2 LEU A 364       4.391  -1.894  54.382  1.00 21.33           C  
ATOM   2801  N   LYS A 365       5.782   3.220  55.133  1.00 22.08           N  
ATOM   2802  CA  LYS A 365       5.149   4.383  55.757  1.00 22.91           C  
ATOM   2803  C   LYS A 365       3.967   3.912  56.601  1.00 23.24           C  
ATOM   2804  O   LYS A 365       3.315   2.925  56.253  1.00 23.07           O  
ATOM   2805  CB  LYS A 365       4.670   5.393  54.705  1.00 23.13           C  
ATOM   2806  CG  LYS A 365       5.774   6.022  53.866  1.00 23.79           C  
ATOM   2807  CD  LYS A 365       5.260   7.223  53.088  1.00 25.67           C  
ATOM   2808  CE  LYS A 365       6.365   7.835  52.236  1.00 26.69           C  
ATOM   2809  NZ  LYS A 365       5.933   9.080  51.537  1.00 27.70           N  
ATOM   2810  N   ASN A 366       3.698   4.606  57.709  1.00 24.00           N  
ATOM   2811  CA  ASN A 366       2.525   4.307  58.544  1.00 24.84           C  
ATOM   2812  C   ASN A 366       1.209   4.352  57.761  1.00 24.62           C  
ATOM   2813  O   ASN A 366       0.311   3.538  58.002  1.00 24.84           O  
ATOM   2814  CB  ASN A 366       2.458   5.239  59.761  1.00 25.38           C  
ATOM   2815  CG  ASN A 366       3.524   4.926  60.800  1.00 27.37           C  
ATOM   2816  OD1 ASN A 366       3.871   3.763  61.029  1.00 29.88           O  
ATOM   2817  ND2 ASN A 366       4.041   5.968  61.448  1.00 29.16           N  
ATOM   2818  N   LYS A 367       1.124   5.292  56.819  1.00 24.60           N  
ATOM   2819  CA  LYS A 367      -0.014   5.441  55.905  1.00 24.79           C  
ATOM   2820  C   LYS A 367      -0.322   4.180  55.093  1.00 23.99           C  
ATOM   2821  O   LYS A 367      -1.467   3.969  54.683  1.00 24.04           O  
ATOM   2822  CB  LYS A 367       0.251   6.577  54.911  1.00 24.96           C  
ATOM   2823  CG  LYS A 367       0.084   7.992  55.441  1.00 26.19           C  
ATOM   2824  CD  LYS A 367       0.443   8.999  54.345  1.00 26.33           C  
ATOM   2825  CE  LYS A 367       0.641  10.410  54.894  1.00 28.96           C  
ATOM   2826  NZ  LYS A 367      -0.649  11.117  55.155  1.00 30.29           N  
ATOM   2827  N   SER A 368       0.704   3.361  54.854  1.00 23.11           N  
ATOM   2828  CA  SER A 368       0.603   2.181  53.987  1.00 22.31           C  
ATOM   2829  C   SER A 368       0.139   0.906  54.694  1.00 22.06           C  
ATOM   2830  O   SER A 368       0.112  -0.168  54.084  1.00 21.48           O  
ATOM   2831  CB  SER A 368       1.949   1.918  53.300  1.00 22.15           C  
ATOM   2832  OG  SER A 368       2.364   3.041  52.547  1.00 21.30           O  
ATOM   2833  N   THR A 369      -0.218   1.023  55.974  1.00 21.87           N  
ATOM   2834  CA  THR A 369      -0.638  -0.130  56.771  1.00 21.86           C  
ATOM   2835  C   THR A 369      -1.839  -0.860  56.153  1.00 21.46           C  
ATOM   2836  O   THR A 369      -1.819  -2.086  56.026  1.00 21.39           O  
ATOM   2837  CB  THR A 369      -0.920   0.282  58.242  1.00 22.08           C  
ATOM   2838  OG1 THR A 369       0.292   0.770  58.832  1.00 22.63           O  
ATOM   2839  CG2 THR A 369      -1.430  -0.899  59.060  1.00 22.83           C  
ATOM   2840  N   GLN A 370      -2.861  -0.103  55.754  1.00 21.29           N  
ATOM   2841  CA  GLN A 370      -4.059  -0.682  55.139  1.00 21.42           C  
ATOM   2842  C   GLN A 370      -3.727  -1.381  53.823  1.00 20.29           C  
ATOM   2843  O   GLN A 370      -4.161  -2.509  53.588  1.00 20.06           O  
ATOM   2844  CB  GLN A 370      -5.123   0.387  54.905  1.00 21.60           C  
ATOM   2845  CG  GLN A 370      -5.875   0.822  56.157  1.00 23.58           C  
ATOM   2846  CD  GLN A 370      -6.914   1.892  55.865  1.00 23.66           C  
ATOM   2847  OE1 GLN A 370      -7.500   1.929  54.778  1.00 27.70           O  
ATOM   2848  NE2 GLN A 370      -7.147   2.770  56.835  1.00 27.11           N  
ATOM   2849  N   ALA A 371      -2.943  -0.706  52.982  1.00 19.35           N  
ATOM   2850  CA  ALA A 371      -2.522  -1.254  51.689  1.00 18.47           C  
ATOM   2851  C   ALA A 371      -1.790  -2.581  51.855  1.00 18.03           C  
ATOM   2852  O   ALA A 371      -2.018  -3.519  51.095  1.00 17.56           O  
ATOM   2853  CB  ALA A 371      -1.659  -0.259  50.945  1.00 18.45           C  
ATOM   2854  N   LEU A 372      -0.916  -2.653  52.859  1.00 17.54           N  
ATOM   2855  CA  LEU A 372      -0.201  -3.885  53.182  1.00 17.45           C  
ATOM   2856  C   LEU A 372      -1.162  -5.002  53.590  1.00 17.46           C  
ATOM   2857  O   LEU A 372      -1.015  -6.141  53.140  1.00 17.00           O  
ATOM   2858  CB  LEU A 372       0.820  -3.640  54.299  1.00 17.47           C  
ATOM   2859  CG  LEU A 372       1.559  -4.870  54.838  1.00 17.63           C  
ATOM   2860  CD1 LEU A 372       2.584  -5.392  53.842  1.00 18.07           C  
ATOM   2861  CD2 LEU A 372       2.225  -4.533  56.159  1.00 18.41           C  
ATOM   2862  N   GLU A 373      -2.124  -4.658  54.448  1.00 17.82           N  
ATOM   2863  CA  GLU A 373      -3.145  -5.591  54.926  1.00 18.69           C  
ATOM   2864  C   GLU A 373      -3.987  -6.138  53.773  1.00 17.84           C  
ATOM   2865  O   GLU A 373      -4.142  -7.350  53.637  1.00 17.70           O  
ATOM   2866  CB  GLU A 373      -4.053  -4.908  55.958  1.00 18.54           C  
ATOM   2867  CG  GLU A 373      -5.142  -5.819  56.531  1.00 20.84           C  
ATOM   2868  CD  GLU A 373      -6.173  -5.082  57.374  1.00 21.27           C  
ATOM   2869  OE1 GLU A 373      -7.368  -5.451  57.301  1.00 24.97           O  
ATOM   2870  OE2 GLU A 373      -5.800  -4.136  58.107  1.00 26.03           O  
ATOM   2871  N   TYR A 374      -4.511  -5.236  52.948  1.00 17.74           N  
ATOM   2872  CA  TYR A 374      -5.379  -5.611  51.823  1.00 17.73           C  
ATOM   2873  C   TYR A 374      -4.639  -6.441  50.775  1.00 17.35           C  
ATOM   2874  O   TYR A 374      -5.146  -7.463  50.312  1.00 16.68           O  
ATOM   2875  CB  TYR A 374      -5.999  -4.374  51.166  1.00 18.28           C  
ATOM   2876  CG  TYR A 374      -6.885  -3.530  52.064  1.00 19.27           C  
ATOM   2877  CD1 TYR A 374      -7.114  -2.184  51.777  1.00 19.88           C  
ATOM   2878  CD2 TYR A 374      -7.495  -4.075  53.203  1.00 20.04           C  
ATOM   2879  CE1 TYR A 374      -7.935  -1.401  52.593  1.00 20.36           C  
ATOM   2880  CE2 TYR A 374      -8.304  -3.300  54.026  1.00 20.24           C  
ATOM   2881  CZ  TYR A 374      -8.520  -1.971  53.717  1.00 20.29           C  
ATOM   2882  OH  TYR A 374      -9.328  -1.217  54.542  1.00 21.81           O  
ATOM   2883  N   CYS A 375      -3.439  -5.993  50.412  1.00 16.79           N  
ATOM   2884  CA  CYS A 375      -2.607  -6.709  49.448  1.00 16.32           C  
ATOM   2885  C   CYS A 375      -2.296  -8.121  49.929  1.00 16.34           C  
ATOM   2886  O   CYS A 375      -2.482  -9.089  49.192  1.00 16.23           O  
ATOM   2887  CB  CYS A 375      -1.309  -5.943  49.181  1.00 16.28           C  
ATOM   2888  SG  CYS A 375      -0.186  -6.808  48.067  1.00 16.74           S  
ATOM   2889  N   ALA A 376      -1.840  -8.234  51.177  1.00 16.35           N  
ATOM   2890  CA  ALA A 376      -1.499  -9.526  51.754  1.00 16.80           C  
ATOM   2891  C   ALA A 376      -2.708 -10.454  51.778  1.00 16.88           C  
ATOM   2892  O   ALA A 376      -2.599 -11.627  51.432  1.00 17.12           O  
ATOM   2893  CB  ALA A 376      -0.926  -9.354  53.153  1.00 16.58           C  
ATOM   2894  N   GLU A 377      -3.858  -9.915  52.173  1.00 17.41           N  
ATOM   2895  CA  GLU A 377      -5.079 -10.707  52.263  1.00 17.91           C  
ATOM   2896  C   GLU A 377      -5.433 -11.286  50.897  1.00 17.64           C  
ATOM   2897  O   GLU A 377      -5.646 -12.491  50.760  1.00 17.56           O  
ATOM   2898  CB  GLU A 377      -6.230  -9.857  52.798  1.00 18.32           C  
ATOM   2899  CG  GLU A 377      -7.575 -10.582  52.846  1.00 20.66           C  
ATOM   2900  CD  GLU A 377      -8.761  -9.629  52.784  1.00 24.35           C  
ATOM   2901  OE1 GLU A 377      -9.895 -10.117  52.616  1.00 26.47           O  
ATOM   2902  OE2 GLU A 377      -8.567  -8.397  52.900  1.00 26.57           O  
ATOM   2903  N   LEU A 378      -5.455 -10.416  49.891  1.00 17.48           N  
ATOM   2904  CA  LEU A 378      -5.892 -10.793  48.548  1.00 17.50           C  
ATOM   2905  C   LEU A 378      -4.925 -11.727  47.828  1.00 17.52           C  
ATOM   2906  O   LEU A 378      -5.351 -12.553  47.021  1.00 17.56           O  
ATOM   2907  CB  LEU A 378      -6.194  -9.547  47.710  1.00 17.58           C  
ATOM   2908  CG  LEU A 378      -7.320  -8.657  48.255  1.00 17.69           C  
ATOM   2909  CD1 LEU A 378      -7.498  -7.419  47.397  1.00 19.02           C  
ATOM   2910  CD2 LEU A 378      -8.645  -9.420  48.384  1.00 19.03           C  
ATOM   2911  N   LEU A 379      -3.633 -11.601  48.131  1.00 17.14           N  
ATOM   2912  CA  LEU A 379      -2.602 -12.422  47.502  1.00 16.95           C  
ATOM   2913  C   LEU A 379      -2.210 -13.676  48.301  1.00 17.01           C  
ATOM   2914  O   LEU A 379      -1.333 -14.430  47.879  1.00 17.03           O  
ATOM   2915  CB  LEU A 379      -1.366 -11.579  47.140  1.00 16.85           C  
ATOM   2916  CG  LEU A 379      -1.559 -10.419  46.150  1.00 16.52           C  
ATOM   2917  CD1 LEU A 379      -0.233  -9.724  45.876  1.00 16.39           C  
ATOM   2918  CD2 LEU A 379      -2.210 -10.868  44.829  1.00 17.13           C  
ATOM   2919  N   GLY A 380      -2.888 -13.909  49.426  1.00 17.35           N  
ATOM   2920  CA  GLY A 380      -2.656 -15.102  50.251  1.00 17.75           C  
ATOM   2921  C   GLY A 380      -1.296 -15.102  50.925  1.00 18.07           C  
ATOM   2922  O   GLY A 380      -0.667 -16.157  51.093  1.00 18.48           O  
ATOM   2923  N   LEU A 381      -0.845 -13.912  51.306  1.00 18.32           N  
ATOM   2924  CA  LEU A 381       0.479 -13.730  51.897  1.00 18.74           C  
ATOM   2925  C   LEU A 381       0.395 -13.279  53.347  1.00 19.09           C  
ATOM   2926  O   LEU A 381      -0.533 -12.570  53.738  1.00 18.98           O  
ATOM   2927  CB  LEU A 381       1.286 -12.698  51.100  1.00 18.38           C  
ATOM   2928  CG  LEU A 381       1.442 -12.862  49.586  1.00 17.83           C  
ATOM   2929  CD1 LEU A 381       2.217 -11.668  49.019  1.00 17.64           C  
ATOM   2930  CD2 LEU A 381       2.123 -14.181  49.224  1.00 17.43           C  
ATOM   2931  N   ASP A 382       1.379 -13.699  54.137  1.00 19.97           N  
ATOM   2932  CA  ASP A 382       1.580 -13.167  55.477  1.00 20.74           C  
ATOM   2933  C   ASP A 382       2.066 -11.719  55.360  1.00 20.84           C  
ATOM   2934  O   ASP A 382       3.007 -11.440  54.606  1.00 20.88           O  
ATOM   2935  CB  ASP A 382       2.617 -14.010  56.227  1.00 21.05           C  
ATOM   2936  CG  ASP A 382       2.892 -13.491  57.618  1.00 22.40           C  
ATOM   2937  OD1 ASP A 382       3.909 -12.788  57.793  1.00 23.96           O  
ATOM   2938  OD2 ASP A 382       2.087 -13.773  58.532  1.00 23.76           O  
ATOM   2939  N   GLN A 383       1.421 -10.815  56.099  1.00 20.89           N  
ATOM   2940  CA  GLN A 383       1.764  -9.388  56.099  1.00 21.45           C  
ATOM   2941  C   GLN A 383       3.244  -9.109  56.368  1.00 21.35           C  
ATOM   2942  O   GLN A 383       3.850  -8.255  55.714  1.00 21.04           O  
ATOM   2943  CB  GLN A 383       0.925  -8.626  57.128  1.00 21.42           C  
ATOM   2944  CG  GLN A 383      -0.524  -8.409  56.732  1.00 22.39           C  
ATOM   2945  CD  GLN A 383      -1.254  -7.471  57.672  1.00 22.65           C  
ATOM   2946  OE1 GLN A 383      -2.407  -7.710  58.029  1.00 25.28           O  
ATOM   2947  NE2 GLN A 383      -0.587  -6.394  58.077  1.00 25.33           N  
ATOM   2948  N   ASP A 384       3.813  -9.816  57.343  1.00 21.22           N  
ATOM   2949  CA  ASP A 384       5.217  -9.622  57.685  1.00 21.09           C  
ATOM   2950  C   ASP A 384       6.141 -10.152  56.589  1.00 20.51           C  
ATOM   2951  O   ASP A 384       7.148  -9.515  56.280  1.00 20.11           O  
ATOM   2952  CB  ASP A 384       5.561 -10.252  59.035  1.00 21.77           C  
ATOM   2953  CG  ASP A 384       6.941  -9.851  59.527  1.00 23.46           C  
ATOM   2954  OD1 ASP A 384       7.148  -8.652  59.820  1.00 26.20           O  
ATOM   2955  OD2 ASP A 384       7.818 -10.735  59.617  1.00 26.47           O  
ATOM   2956  N   ASP A 385       5.793 -11.301  56.006  1.00 19.88           N  
ATOM   2957  CA  ASP A 385       6.530 -11.858  54.864  1.00 19.77           C  
ATOM   2958  C   ASP A 385       6.594 -10.854  53.710  1.00 19.20           C  
ATOM   2959  O   ASP A 385       7.646 -10.664  53.098  1.00 18.67           O  
ATOM   2960  CB  ASP A 385       5.888 -13.161  54.369  1.00 19.81           C  
ATOM   2961  CG  ASP A 385       6.230 -14.368  55.234  1.00 21.18           C  
ATOM   2962  OD1 ASP A 385       7.102 -14.265  56.128  1.00 21.74           O  
ATOM   2963  OD2 ASP A 385       5.624 -15.437  55.001  1.00 21.97           O  
ATOM   2964  N   LEU A 386       5.463 -10.215  53.420  1.00 18.91           N  
ATOM   2965  CA  LEU A 386       5.406  -9.203  52.359  1.00 18.65           C  
ATOM   2966  C   LEU A 386       6.261  -7.979  52.709  1.00 18.56           C  
ATOM   2967  O   LEU A 386       7.045  -7.509  51.884  1.00 18.17           O  
ATOM   2968  CB  LEU A 386       3.956  -8.798  52.072  1.00 18.64           C  
ATOM   2969  CG  LEU A 386       3.694  -7.741  50.990  1.00 18.33           C  
ATOM   2970  CD1 LEU A 386       4.286  -8.148  49.640  1.00 16.62           C  
ATOM   2971  CD2 LEU A 386       2.210  -7.479  50.864  1.00 18.70           C  
ATOM   2972  N   ARG A 387       6.109  -7.482  53.934  1.00 18.55           N  
ATOM   2973  CA  ARG A 387       6.909  -6.363  54.445  1.00 18.98           C  
ATOM   2974  C   ARG A 387       8.407  -6.625  54.311  1.00 18.42           C  
ATOM   2975  O   ARG A 387       9.150  -5.784  53.796  1.00 18.20           O  
ATOM   2976  CB  ARG A 387       6.558  -6.088  55.914  1.00 18.75           C  
ATOM   2977  CG  ARG A 387       7.341  -4.942  56.547  1.00 20.27           C  
ATOM   2978  CD  ARG A 387       7.161  -4.909  58.056  1.00 20.68           C  
ATOM   2979  NE  ARG A 387       5.752  -4.880  58.444  1.00 24.75           N  
ATOM   2980  CZ  ARG A 387       5.048  -3.770  58.644  1.00 26.19           C  
ATOM   2981  NH1 ARG A 387       3.773  -3.856  58.995  1.00 27.79           N  
ATOM   2982  NH2 ARG A 387       5.611  -2.575  58.501  1.00 27.68           N  
ATOM   2983  N   VAL A 388       8.838  -7.795  54.779  1.00 18.21           N  
ATOM   2984  CA  VAL A 388      10.249  -8.178  54.764  1.00 18.14           C  
ATOM   2985  C   VAL A 388      10.774  -8.323  53.331  1.00 18.11           C  
ATOM   2986  O   VAL A 388      11.873  -7.856  53.011  1.00 17.92           O  
ATOM   2987  CB  VAL A 388      10.475  -9.482  55.579  1.00 18.30           C  
ATOM   2988  CG1 VAL A 388      11.836 -10.108  55.282  1.00 18.51           C  
ATOM   2989  CG2 VAL A 388      10.310  -9.205  57.074  1.00 18.75           C  
ATOM   2990  N   SER A 389       9.974  -8.955  52.476  1.00 17.90           N  
ATOM   2991  CA  SER A 389      10.361  -9.193  51.084  1.00 17.99           C  
ATOM   2992  C   SER A 389      10.480  -7.899  50.276  1.00 17.60           C  
ATOM   2993  O   SER A 389      11.232  -7.843  49.299  1.00 17.63           O  
ATOM   2994  CB  SER A 389       9.373 -10.146  50.413  1.00 18.02           C  
ATOM   2995  OG  SER A 389       9.428 -11.438  51.003  1.00 19.38           O  
ATOM   2996  N   LEU A 390       9.737  -6.870  50.680  1.00 17.12           N  
ATOM   2997  CA  LEU A 390       9.746  -5.581  49.979  1.00 17.07           C  
ATOM   2998  C   LEU A 390      10.841  -4.626  50.455  1.00 17.14           C  
ATOM   2999  O   LEU A 390      11.173  -3.669  49.760  1.00 16.84           O  
ATOM   3000  CB  LEU A 390       8.386  -4.885  50.092  1.00 16.83           C  
ATOM   3001  CG  LEU A 390       7.191  -5.487  49.345  1.00 16.73           C  
ATOM   3002  CD1 LEU A 390       5.951  -4.666  49.642  1.00 16.91           C  
ATOM   3003  CD2 LEU A 390       7.453  -5.559  47.842  1.00 17.82           C  
ATOM   3004  N   THR A 391      11.393  -4.888  51.637  1.00 17.32           N  
ATOM   3005  CA  THR A 391      12.315  -3.947  52.279  1.00 18.05           C  
ATOM   3006  C   THR A 391      13.694  -4.540  52.601  1.00 18.72           C  
ATOM   3007  O   THR A 391      14.580  -3.827  53.087  1.00 18.53           O  
ATOM   3008  CB  THR A 391      11.708  -3.368  53.581  1.00 17.74           C  
ATOM   3009  OG1 THR A 391      11.413  -4.439  54.483  1.00 17.40           O  
ATOM   3010  CG2 THR A 391      10.430  -2.580  53.291  1.00 17.94           C  
ATOM   3011  N   THR A 392      13.864  -5.836  52.344  1.00 19.98           N  
ATOM   3012  CA  THR A 392      15.133  -6.536  52.588  1.00 21.42           C  
ATOM   3013  C   THR A 392      15.393  -7.593  51.519  1.00 22.81           C  
ATOM   3014  O   THR A 392      14.466  -8.038  50.833  1.00 22.91           O  
ATOM   3015  CB  THR A 392      15.168  -7.266  53.961  1.00 21.35           C  
ATOM   3016  OG1 THR A 392      14.359  -8.449  53.903  1.00 21.10           O  
ATOM   3017  CG2 THR A 392      14.699  -6.368  55.108  1.00 21.12           C  
ATOM   3018  N   ARG A 393      16.653  -8.007  51.402  1.00 24.28           N  
ATOM   3019  CA  ARG A 393      17.036  -9.093  50.501  1.00 26.04           C  
ATOM   3020  C   ARG A 393      18.245  -9.864  51.030  1.00 26.89           C  
ATOM   3021  O   ARG A 393      19.246  -9.266  51.412  1.00 27.13           O  
ATOM   3022  CB  ARG A 393      17.325  -8.551  49.099  1.00 26.06           C  
ATOM   3023  CG  ARG A 393      17.597  -9.636  48.062  1.00 27.51           C  
ATOM   3024  CD  ARG A 393      17.379  -9.135  46.645  1.00 29.01           C  
ATOM   3025  NE  ARG A 393      15.981  -8.783  46.398  1.00 30.79           N  
ATOM   3026  CZ  ARG A 393      15.555  -7.567  46.063  1.00 31.95           C  
ATOM   3027  NH1 ARG A 393      16.417  -6.564  45.915  1.00 33.36           N  
ATOM   3028  NH2 ARG A 393      14.264  -7.355  45.862  1.00 31.46           N  
ATOM   3029  N   VAL A 394      18.134 -11.190  51.059  1.00 28.22           N  
ATOM   3030  CA  VAL A 394      19.270 -12.055  51.376  1.00 29.41           C  
ATOM   3031  C   VAL A 394      20.181 -12.091  50.149  1.00 30.17           C  
ATOM   3032  O   VAL A 394      19.739 -12.442  49.052  1.00 30.35           O  
ATOM   3033  CB  VAL A 394      18.820 -13.486  51.784  1.00 29.40           C  
ATOM   3034  CG1 VAL A 394      20.026 -14.389  52.049  1.00 29.67           C  
ATOM   3035  CG2 VAL A 394      17.920 -13.437  53.014  1.00 29.54           C  
ATOM   3036  N   MET A 395      21.441 -11.700  50.332  1.00 30.94           N  
ATOM   3037  CA  MET A 395      22.391 -11.614  49.220  1.00 31.99           C  
ATOM   3038  C   MET A 395      23.822 -11.971  49.635  1.00 31.95           C  
ATOM   3039  O   MET A 395      24.269 -11.633  50.734  1.00 32.21           O  
ATOM   3040  CB  MET A 395      22.332 -10.225  48.565  1.00 31.96           C  
ATOM   3041  CG  MET A 395      23.010  -9.109  49.354  1.00 32.43           C  
ATOM   3042  SD  MET A 395      22.553  -7.436  48.859  1.00 33.65           S  
ATOM   3043  CE  MET A 395      22.926  -7.456  47.100  1.00 34.43           C  
ATOM   3044  N   ILE A 407      23.895 -12.810  53.540  1.00 27.99           N  
ATOM   3045  CA  ILE A 407      23.373 -11.877  54.539  1.00 27.98           C  
ATOM   3046  C   ILE A 407      22.061 -11.222  54.091  1.00 27.44           C  
ATOM   3047  O   ILE A 407      21.914 -10.837  52.930  1.00 27.77           O  
ATOM   3048  CB  ILE A 407      24.426 -10.787  54.919  1.00 27.96           C  
ATOM   3049  CG1 ILE A 407      23.930  -9.947  56.102  1.00 28.17           C  
ATOM   3050  CG2 ILE A 407      24.797  -9.921  53.700  1.00 28.71           C  
ATOM   3051  CD1 ILE A 407      24.927  -8.924  56.613  1.00 28.37           C  
ATOM   3052  N   LYS A 408      21.118 -11.113  55.026  1.00 27.04           N  
ATOM   3053  CA  LYS A 408      19.889 -10.349  54.826  1.00 26.45           C  
ATOM   3054  C   LYS A 408      20.183  -8.854  54.992  1.00 25.89           C  
ATOM   3055  O   LYS A 408      20.426  -8.376  56.108  1.00 25.70           O  
ATOM   3056  CB  LYS A 408      18.816 -10.816  55.814  1.00 26.48           C  
ATOM   3057  CG  LYS A 408      17.471 -10.116  55.702  1.00 26.66           C  
ATOM   3058  CD  LYS A 408      16.497 -10.701  56.719  1.00 27.01           C  
ATOM   3059  CE  LYS A 408      15.348  -9.757  57.014  1.00 27.69           C  
ATOM   3060  NZ  LYS A 408      14.484 -10.289  58.108  1.00 28.53           N  
ATOM   3061  N   VAL A 409      20.162  -8.137  53.869  1.00 25.22           N  
ATOM   3062  CA  VAL A 409      20.521  -6.715  53.804  1.00 24.77           C  
ATOM   3063  C   VAL A 409      19.275  -5.841  53.628  1.00 24.27           C  
ATOM   3064  O   VAL A 409      18.360  -6.217  52.891  1.00 24.23           O  
ATOM   3065  CB  VAL A 409      21.527  -6.444  52.639  1.00 24.82           C  
ATOM   3066  CG1 VAL A 409      20.864  -6.624  51.288  1.00 25.13           C  
ATOM   3067  CG2 VAL A 409      22.127  -5.051  52.730  1.00 25.30           C  
ATOM   3068  N   PRO A 410      19.227  -4.678  54.312  1.00 23.82           N  
ATOM   3069  CA  PRO A 410      18.123  -3.747  54.088  1.00 23.38           C  
ATOM   3070  C   PRO A 410      18.201  -3.090  52.716  1.00 22.91           C  
ATOM   3071  O   PRO A 410      19.295  -2.774  52.237  1.00 22.92           O  
ATOM   3072  CB  PRO A 410      18.327  -2.688  55.178  1.00 23.24           C  
ATOM   3073  CG  PRO A 410      19.252  -3.316  56.173  1.00 23.59           C  
ATOM   3074  CD  PRO A 410      20.148  -4.170  55.343  1.00 23.80           C  
ATOM   3075  N   LEU A 411      17.045  -2.893  52.091  1.00 22.31           N  
ATOM   3076  CA  LEU A 411      16.977  -2.184  50.818  1.00 21.80           C  
ATOM   3077  C   LEU A 411      16.756  -0.693  51.040  1.00 21.70           C  
ATOM   3078  O   LEU A 411      16.130  -0.289  52.021  1.00 21.43           O  
ATOM   3079  CB  LEU A 411      15.851  -2.749  49.941  1.00 21.60           C  
ATOM   3080  CG  LEU A 411      15.969  -4.209  49.480  1.00 21.40           C  
ATOM   3081  CD1 LEU A 411      14.691  -4.654  48.770  1.00 21.23           C  
ATOM   3082  CD2 LEU A 411      17.195  -4.421  48.589  1.00 21.85           C  
ATOM   3083  N   LYS A 412      17.275   0.116  50.120  1.00 21.73           N  
ATOM   3084  CA  LYS A 412      17.007   1.547  50.100  1.00 22.02           C  
ATOM   3085  C   LYS A 412      15.594   1.778  49.557  1.00 21.70           C  
ATOM   3086  O   LYS A 412      15.011   0.881  48.940  1.00 21.39           O  
ATOM   3087  CB  LYS A 412      18.035   2.275  49.221  1.00 22.42           C  
ATOM   3088  CG  LYS A 412      19.514   1.941  49.489  1.00 24.20           C  
ATOM   3089  CD  LYS A 412      19.965   2.329  50.896  1.00 26.41           C  
ATOM   3090  CE  LYS A 412      20.217   1.097  51.767  1.00 28.09           C  
ATOM   3091  NZ  LYS A 412      21.538   0.445  51.490  1.00 28.37           N  
ATOM   3092  N   VAL A 413      15.054   2.973  49.785  1.00 21.78           N  
ATOM   3093  CA  VAL A 413      13.703   3.329  49.325  1.00 21.80           C  
ATOM   3094  C   VAL A 413      13.494   3.018  47.836  1.00 22.04           C  
ATOM   3095  O   VAL A 413      12.474   2.430  47.462  1.00 21.69           O  
ATOM   3096  CB  VAL A 413      13.358   4.818  49.628  1.00 21.82           C  
ATOM   3097  CG1 VAL A 413      12.071   5.246  48.925  1.00 21.98           C  
ATOM   3098  CG2 VAL A 413      13.233   5.048  51.130  1.00 21.95           C  
ATOM   3099  N   GLU A 414      14.459   3.398  46.997  1.00 22.25           N  
ATOM   3100  CA  GLU A 414      14.349   3.168  45.550  1.00 22.85           C  
ATOM   3101  C   GLU A 414      14.297   1.681  45.197  1.00 22.03           C  
ATOM   3102  O   GLU A 414      13.548   1.277  44.301  1.00 22.14           O  
ATOM   3103  CB  GLU A 414      15.482   3.863  44.786  1.00 22.90           C  
ATOM   3104  CG  GLU A 414      15.354   5.383  44.731  1.00 24.63           C  
ATOM   3105  CD  GLU A 414      16.337   6.028  43.763  1.00 25.05           C  
ATOM   3106  OE1 GLU A 414      16.134   5.901  42.534  1.00 29.17           O  
ATOM   3107  OE2 GLU A 414      17.304   6.676  44.231  1.00 28.31           O  
ATOM   3108  N   GLN A 415      15.080   0.875  45.910  1.00 21.24           N  
ATOM   3109  CA  GLN A 415      15.112  -0.571  45.693  1.00 20.85           C  
ATOM   3110  C   GLN A 415      13.802  -1.210  46.155  1.00 19.99           C  
ATOM   3111  O   GLN A 415      13.337  -2.189  45.565  1.00 19.78           O  
ATOM   3112  CB  GLN A 415      16.301  -1.209  46.417  1.00 20.91           C  
ATOM   3113  CG  GLN A 415      17.667  -0.818  45.853  1.00 21.73           C  
ATOM   3114  CD  GLN A 415      18.824  -1.446  46.615  1.00 22.05           C  
ATOM   3115  OE1 GLN A 415      19.687  -2.096  46.025  1.00 25.39           O  
ATOM   3116  NE2 GLN A 415      18.845  -1.256  47.929  1.00 21.50           N  
ATOM   3117  N   ALA A 416      13.217  -0.647  47.213  1.00 19.06           N  
ATOM   3118  CA  ALA A 416      11.926  -1.107  47.722  1.00 18.40           C  
ATOM   3119  C   ALA A 416      10.823  -0.810  46.707  1.00 18.07           C  
ATOM   3120  O   ALA A 416       9.987  -1.675  46.416  1.00 17.66           O  
ATOM   3121  CB  ALA A 416      11.617  -0.458  49.053  1.00 18.14           C  
ATOM   3122  N   ASN A 417      10.832   0.410  46.171  1.00 18.04           N  
ATOM   3123  CA  ASN A 417       9.946   0.779  45.065  1.00 18.26           C  
ATOM   3124  C   ASN A 417      10.066  -0.206  43.907  1.00 18.07           C  
ATOM   3125  O   ASN A 417       9.056  -0.648  43.354  1.00 17.51           O  
ATOM   3126  CB  ASN A 417      10.245   2.199  44.568  1.00 18.68           C  
ATOM   3127  CG  ASN A 417       9.775   3.280  45.531  1.00 19.71           C  
ATOM   3128  OD1 ASN A 417       8.863   3.074  46.333  1.00 20.60           O  
ATOM   3129  ND2 ASN A 417      10.397   4.454  45.441  1.00 21.27           N  
ATOM   3130  N   ASN A 418      11.305  -0.552  43.551  1.00 17.99           N  
ATOM   3131  CA  ASN A 418      11.561  -1.496  42.462  1.00 17.81           C  
ATOM   3132  C   ASN A 418      11.069  -2.905  42.760  1.00 17.38           C  
ATOM   3133  O   ASN A 418      10.538  -3.573  41.877  1.00 17.26           O  
ATOM   3134  CB  ASN A 418      13.046  -1.508  42.081  1.00 18.35           C  
ATOM   3135  CG  ASN A 418      13.479  -0.231  41.384  1.00 19.46           C  
ATOM   3136  OD1 ASN A 418      12.653   0.523  40.870  1.00 21.84           O  
ATOM   3137  ND2 ASN A 418      14.787   0.012  41.354  1.00 21.77           N  
ATOM   3138  N   ALA A 419      11.240  -3.344  44.007  1.00 16.47           N  
ATOM   3139  CA  ALA A 419      10.767  -4.653  44.443  1.00 15.98           C  
ATOM   3140  C   ALA A 419       9.246  -4.744  44.338  1.00 15.47           C  
ATOM   3141  O   ALA A 419       8.707  -5.718  43.790  1.00 15.45           O  
ATOM   3142  CB  ALA A 419      11.225  -4.929  45.876  1.00 16.05           C  
ATOM   3143  N   ARG A 420       8.572  -3.718  44.857  1.00 15.07           N  
ATOM   3144  CA  ARG A 420       7.115  -3.607  44.806  1.00 14.63           C  
ATOM   3145  C   ARG A 420       6.634  -3.699  43.361  1.00 14.54           C  
ATOM   3146  O   ARG A 420       5.802  -4.547  43.031  1.00 14.49           O  
ATOM   3147  CB  ARG A 420       6.673  -2.290  45.448  1.00 14.54           C  
ATOM   3148  CG  ARG A 420       5.163  -2.004  45.424  1.00 14.46           C  
ATOM   3149  CD  ARG A 420       4.890  -0.524  45.664  1.00 15.43           C  
ATOM   3150  NE  ARG A 420       5.457   0.307  44.602  1.00 16.42           N  
ATOM   3151  CZ  ARG A 420       5.860   1.563  44.753  1.00 17.41           C  
ATOM   3152  NH1 ARG A 420       6.370   2.214  43.716  1.00 18.52           N  
ATOM   3153  NH2 ARG A 420       5.772   2.172  45.935  1.00 17.45           N  
ATOM   3154  N   ASP A 421       7.189  -2.846  42.504  1.00 14.27           N  
ATOM   3155  CA  ASP A 421       6.774  -2.781  41.098  1.00 14.29           C  
ATOM   3156  C   ASP A 421       7.098  -4.060  40.321  1.00 13.95           C  
ATOM   3157  O   ASP A 421       6.299  -4.498  39.491  1.00 13.76           O  
ATOM   3158  CB  ASP A 421       7.386  -1.556  40.409  1.00 14.59           C  
ATOM   3159  CG  ASP A 421       6.839  -0.233  40.947  1.00 15.47           C  
ATOM   3160  OD1 ASP A 421       5.838  -0.225  41.697  1.00 16.58           O  
ATOM   3161  OD2 ASP A 421       7.411   0.818  40.602  1.00 16.40           O  
ATOM   3162  N   ALA A 422       8.260  -4.659  40.596  1.00 13.62           N  
ATOM   3163  CA  ALA A 422       8.659  -5.913  39.951  1.00 13.44           C  
ATOM   3164  C   ALA A 422       7.703  -7.043  40.312  1.00 13.58           C  
ATOM   3165  O   ALA A 422       7.326  -7.836  39.452  1.00 13.49           O  
ATOM   3166  CB  ALA A 422      10.105  -6.288  40.314  1.00 13.64           C  
ATOM   3167  N   LEU A 423       7.309  -7.106  41.585  1.00 13.18           N  
ATOM   3168  CA  LEU A 423       6.319  -8.085  42.032  1.00 13.23           C  
ATOM   3169  C   LEU A 423       4.965  -7.845  41.348  1.00 13.11           C  
ATOM   3170  O   LEU A 423       4.340  -8.789  40.847  1.00 13.18           O  
ATOM   3171  CB  LEU A 423       6.180  -8.067  43.560  1.00 13.40           C  
ATOM   3172  CG  LEU A 423       5.188  -9.050  44.204  1.00 13.55           C  
ATOM   3173  CD1 LEU A 423       5.549 -10.510  43.914  1.00 13.86           C  
ATOM   3174  CD2 LEU A 423       5.088  -8.800  45.708  1.00 13.60           C  
ATOM   3175  N   ALA A 424       4.542  -6.586  41.300  1.00 12.89           N  
ATOM   3176  CA  ALA A 424       3.277  -6.216  40.657  1.00 12.65           C  
ATOM   3177  C   ALA A 424       3.239  -6.655  39.195  1.00 12.86           C  
ATOM   3178  O   ALA A 424       2.264  -7.266  38.747  1.00 12.51           O  
ATOM   3179  CB  ALA A 424       3.045  -4.727  40.772  1.00 12.78           C  
ATOM   3180  N   LYS A 425       4.309  -6.349  38.465  1.00 12.91           N  
ATOM   3181  CA  LYS A 425       4.405  -6.696  37.048  1.00 13.27           C  
ATOM   3182  C   LYS A 425       4.390  -8.202  36.816  1.00 13.32           C  
ATOM   3183  O   LYS A 425       3.692  -8.679  35.928  1.00 13.85           O  
ATOM   3184  CB  LYS A 425       5.648  -6.063  36.421  1.00 13.09           C  
ATOM   3185  CG  LYS A 425       5.552  -4.567  36.241  1.00 13.80           C  
ATOM   3186  CD  LYS A 425       6.900  -4.016  35.819  1.00 15.90           C  
ATOM   3187  CE  LYS A 425       6.928  -2.505  35.879  1.00 17.43           C  
ATOM   3188  NZ  LYS A 425       8.249  -2.014  35.386  1.00 19.82           N  
ATOM   3189  N   THR A 426       5.132  -8.949  37.631  1.00 13.40           N  
ATOM   3190  CA  THR A 426       5.177 -10.405  37.503  1.00 13.69           C  
ATOM   3191  C   THR A 426       3.823 -11.041  37.868  1.00 12.87           C  
ATOM   3192  O   THR A 426       3.375 -11.970  37.201  1.00 12.86           O  
ATOM   3193  CB  THR A 426       6.355 -11.025  38.299  1.00 14.00           C  
ATOM   3194  OG1 THR A 426       7.581 -10.384  37.907  1.00 17.29           O  
ATOM   3195  CG2 THR A 426       6.478 -12.514  38.019  1.00 13.76           C  
ATOM   3196  N   VAL A 427       3.162 -10.527  38.902  1.00 12.38           N  
ATOM   3197  CA  VAL A 427       1.841 -11.045  39.277  1.00 11.63           C  
ATOM   3198  C   VAL A 427       0.838 -10.826  38.135  1.00 11.31           C  
ATOM   3199  O   VAL A 427       0.186 -11.774  37.679  1.00 10.70           O  
ATOM   3200  CB  VAL A 427       1.328 -10.443  40.610  1.00 12.03           C  
ATOM   3201  CG1 VAL A 427      -0.144 -10.793  40.831  1.00 11.66           C  
ATOM   3202  CG2 VAL A 427       2.168 -10.964  41.788  1.00 11.86           C  
ATOM   3203  N   TYR A 428       0.748  -9.588  37.655  1.00 10.91           N  
ATOM   3204  CA  TYR A 428      -0.203  -9.272  36.585  1.00 11.03           C  
ATOM   3205  C   TYR A 428       0.110 -10.055  35.298  1.00 11.44           C  
ATOM   3206  O   TYR A 428      -0.797 -10.594  34.655  1.00 11.23           O  
ATOM   3207  CB  TYR A 428      -0.262  -7.766  36.309  1.00 10.99           C  
ATOM   3208  CG  TYR A 428      -1.401  -7.421  35.373  1.00 10.61           C  
ATOM   3209  CD1 TYR A 428      -2.680  -7.181  35.868  1.00 10.48           C  
ATOM   3210  CD2 TYR A 428      -1.208  -7.394  33.987  1.00 10.98           C  
ATOM   3211  CE1 TYR A 428      -3.735  -6.892  35.013  1.00 10.11           C  
ATOM   3212  CE2 TYR A 428      -2.259  -7.107  33.120  1.00  9.88           C  
ATOM   3213  CZ  TYR A 428      -3.521  -6.859  33.645  1.00 11.16           C  
ATOM   3214  OH  TYR A 428      -4.578  -6.570  32.811  1.00 10.88           O  
ATOM   3215  N   SER A 429       1.391 -10.128  34.941  1.00 11.87           N  
ATOM   3216  CA  SER A 429       1.809 -10.850  33.737  1.00 12.58           C  
ATOM   3217  C   SER A 429       1.448 -12.330  33.793  1.00 12.70           C  
ATOM   3218  O   SER A 429       0.950 -12.899  32.814  1.00 12.82           O  
ATOM   3219  CB  SER A 429       3.307 -10.673  33.473  1.00 12.68           C  
ATOM   3220  OG  SER A 429       3.638 -11.202  32.195  1.00 14.64           O  
ATOM   3221  N   HIS A 430       1.693 -12.959  34.940  1.00 13.08           N  
ATOM   3222  CA  HIS A 430       1.291 -14.354  35.124  1.00 13.18           C  
ATOM   3223  C   HIS A 430      -0.235 -14.529  35.147  1.00 12.80           C  
ATOM   3224  O   HIS A 430      -0.752 -15.568  34.726  1.00 12.68           O  
ATOM   3225  CB  HIS A 430       1.953 -14.953  36.368  1.00 13.69           C  
ATOM   3226  CG  HIS A 430       3.397 -15.287  36.165  1.00 16.02           C  
ATOM   3227  ND1 HIS A 430       3.837 -16.566  35.897  1.00 18.63           N  
ATOM   3228  CD2 HIS A 430       4.498 -14.501  36.151  1.00 17.49           C  
ATOM   3229  CE1 HIS A 430       5.151 -16.556  35.754  1.00 19.28           C  
ATOM   3230  NE2 HIS A 430       5.577 -15.314  35.901  1.00 19.14           N  
ATOM   3231  N   LEU A 431      -0.946 -13.507  35.624  1.00 12.23           N  
ATOM   3232  CA  LEU A 431      -2.408 -13.501  35.564  1.00 11.81           C  
ATOM   3233  C   LEU A 431      -2.878 -13.480  34.111  1.00 11.41           C  
ATOM   3234  O   LEU A 431      -3.797 -14.215  33.742  1.00 11.40           O  
ATOM   3235  CB  LEU A 431      -2.991 -12.306  36.327  1.00 11.84           C  
ATOM   3236  CG  LEU A 431      -4.519 -12.209  36.448  1.00 12.11           C  
ATOM   3237  CD1 LEU A 431      -5.092 -13.372  37.238  1.00 13.64           C  
ATOM   3238  CD2 LEU A 431      -4.892 -10.894  37.098  1.00 11.78           C  
ATOM   3239  N   PHE A 432      -2.242 -12.641  33.297  1.00 10.99           N  
ATOM   3240  CA  PHE A 432      -2.549 -12.584  31.865  1.00 11.02           C  
ATOM   3241  C   PHE A 432      -2.267 -13.934  31.189  1.00 11.01           C  
ATOM   3242  O   PHE A 432      -3.088 -14.434  30.418  1.00 10.58           O  
ATOM   3243  CB  PHE A 432      -1.781 -11.446  31.181  1.00 10.98           C  
ATOM   3244  CG  PHE A 432      -2.185 -11.222  29.740  1.00 11.11           C  
ATOM   3245  CD1 PHE A 432      -1.260 -11.378  28.716  1.00 11.28           C  
ATOM   3246  CD2 PHE A 432      -3.497 -10.880  29.418  1.00 12.78           C  
ATOM   3247  CE1 PHE A 432      -1.630 -11.178  27.379  1.00 12.17           C  
ATOM   3248  CE2 PHE A 432      -3.887 -10.682  28.075  1.00 12.28           C  
ATOM   3249  CZ  PHE A 432      -2.947 -10.829  27.060  1.00 11.94           C  
ATOM   3250  N   ASP A 433      -1.113 -14.528  31.499  1.00 11.33           N  
ATOM   3251  CA  ASP A 433      -0.788 -15.870  31.011  1.00 11.76           C  
ATOM   3252  C   ASP A 433      -1.901 -16.858  31.359  1.00 12.05           C  
ATOM   3253  O   ASP A 433      -2.295 -17.680  30.525  1.00 12.10           O  
ATOM   3254  CB  ASP A 433       0.530 -16.372  31.606  1.00 12.24           C  
ATOM   3255  CG  ASP A 433       1.739 -15.589  31.134  1.00 13.01           C  
ATOM   3256  OD1 ASP A 433       1.645 -14.844  30.135  1.00 14.98           O  
ATOM   3257  OD2 ASP A 433       2.802 -15.726  31.777  1.00 14.84           O  
ATOM   3258  N   HIS A 434      -2.402 -16.780  32.594  1.00 12.24           N  
ATOM   3259  CA  HIS A 434      -3.484 -17.657  33.033  1.00 12.37           C  
ATOM   3260  C   HIS A 434      -4.759 -17.419  32.231  1.00 12.02           C  
ATOM   3261  O   HIS A 434      -5.430 -18.369  31.845  1.00 11.80           O  
ATOM   3262  CB  HIS A 434      -3.802 -17.471  34.518  1.00 12.72           C  
ATOM   3263  CG  HIS A 434      -4.992 -18.259  34.968  1.00 14.20           C  
ATOM   3264  ND1 HIS A 434      -6.246 -17.704  35.106  1.00 16.85           N  
ATOM   3265  CD2 HIS A 434      -5.129 -19.573  35.264  1.00 15.97           C  
ATOM   3266  CE1 HIS A 434      -7.100 -18.636  35.488  1.00 15.97           C  
ATOM   3267  NE2 HIS A 434      -6.446 -19.778  35.598  1.00 16.82           N  
ATOM   3268  N   VAL A 435      -5.092 -16.147  32.013  1.00 11.71           N  
ATOM   3269  CA  VAL A 435      -6.289 -15.786  31.253  1.00 11.53           C  
ATOM   3270  C   VAL A 435      -6.238 -16.389  29.842  1.00 11.71           C  
ATOM   3271  O   VAL A 435      -7.217 -16.986  29.388  1.00 11.11           O  
ATOM   3272  CB  VAL A 435      -6.510 -14.249  31.232  1.00 11.55           C  
ATOM   3273  CG1 VAL A 435      -7.573 -13.857  30.207  1.00 11.90           C  
ATOM   3274  CG2 VAL A 435      -6.908 -13.760  32.616  1.00 11.39           C  
ATOM   3275  N   VAL A 436      -5.091 -16.268  29.173  1.00 11.70           N  
ATOM   3276  CA  VAL A 436      -4.952 -16.804  27.811  1.00 12.11           C  
ATOM   3277  C   VAL A 436      -5.043 -18.331  27.826  1.00 12.58           C  
ATOM   3278  O   VAL A 436      -5.717 -18.924  26.988  1.00 13.14           O  
ATOM   3279  CB  VAL A 436      -3.658 -16.333  27.109  1.00 12.05           C  
ATOM   3280  CG1 VAL A 436      -3.613 -16.852  25.663  1.00 11.63           C  
ATOM   3281  CG2 VAL A 436      -3.577 -14.809  27.104  1.00 11.64           C  
ATOM   3282  N   ASN A 437      -4.362 -18.959  28.782  1.00 13.40           N  
ATOM   3283  CA  ASN A 437      -4.462 -20.407  28.972  1.00 14.34           C  
ATOM   3284  C   ASN A 437      -5.899 -20.848  29.252  1.00 14.53           C  
ATOM   3285  O   ASN A 437      -6.367 -21.844  28.690  1.00 14.89           O  
ATOM   3286  CB  ASN A 437      -3.533 -20.872  30.101  1.00 14.66           C  
ATOM   3287  CG  ASN A 437      -3.477 -22.391  30.231  1.00 15.73           C  
ATOM   3288  OD1 ASN A 437      -3.676 -22.937  31.321  1.00 18.59           O  
ATOM   3289  ND2 ASN A 437      -3.215 -23.077  29.125  1.00 14.83           N  
ATOM   3290  N   ARG A 438      -6.594 -20.107  30.114  1.00 14.70           N  
ATOM   3291  CA  ARG A 438      -7.981 -20.430  30.465  1.00 14.97           C  
ATOM   3292  C   ARG A 438      -8.890 -20.342  29.238  1.00 15.17           C  
ATOM   3293  O   ARG A 438      -9.773 -21.179  29.048  1.00 15.51           O  
ATOM   3294  CB  ARG A 438      -8.491 -19.525  31.592  1.00 14.86           C  
ATOM   3295  CG  ARG A 438      -9.901 -19.849  32.083  1.00 14.84           C  
ATOM   3296  CD  ARG A 438     -10.015 -21.290  32.572  1.00 15.30           C  
ATOM   3297  NE  ARG A 438     -11.380 -21.640  32.963  1.00 15.81           N  
ATOM   3298  CZ  ARG A 438     -12.294 -22.153  32.143  1.00 15.98           C  
ATOM   3299  NH1 ARG A 438     -13.501 -22.451  32.601  1.00 15.49           N  
ATOM   3300  NH2 ARG A 438     -12.008 -22.371  30.866  1.00 16.07           N  
ATOM   3301  N   VAL A 439      -8.646 -19.338  28.401  1.00 15.46           N  
ATOM   3302  CA  VAL A 439      -9.372 -19.176  27.142  1.00 15.50           C  
ATOM   3303  C   VAL A 439      -9.152 -20.392  26.232  1.00 15.70           C  
ATOM   3304  O   VAL A 439     -10.115 -20.972  25.731  1.00 15.59           O  
ATOM   3305  CB  VAL A 439      -9.016 -17.819  26.460  1.00 15.74           C  
ATOM   3306  CG1 VAL A 439      -9.367 -17.814  24.984  1.00 15.66           C  
ATOM   3307  CG2 VAL A 439      -9.733 -16.679  27.173  1.00 16.07           C  
ATOM   3308  N   ASN A 440      -7.896 -20.803  26.062  1.00 15.66           N  
ATOM   3309  CA  ASN A 440      -7.563 -21.992  25.278  1.00 15.93           C  
ATOM   3310  C   ASN A 440      -8.246 -23.249  25.807  1.00 16.21           C  
ATOM   3311  O   ASN A 440      -8.606 -24.136  25.037  1.00 16.39           O  
ATOM   3312  CB  ASN A 440      -6.050 -22.193  25.204  1.00 15.90           C  
ATOM   3313  CG  ASN A 440      -5.367 -21.140  24.339  1.00 15.92           C  
ATOM   3314  OD1 ASN A 440      -5.970 -20.597  23.406  1.00 14.35           O  
ATOM   3315  ND2 ASN A 440      -4.112 -20.849  24.647  1.00 15.25           N  
ATOM   3316  N   GLN A 441      -8.449 -23.299  27.121  1.00 16.59           N  
ATOM   3317  CA  GLN A 441      -9.137 -24.429  27.745  1.00 16.85           C  
ATOM   3318  C   GLN A 441     -10.637 -24.475  27.459  1.00 17.19           C  
ATOM   3319  O   GLN A 441     -11.273 -25.493  27.744  1.00 17.54           O  
ATOM   3320  CB  GLN A 441      -8.891 -24.453  29.257  1.00 16.88           C  
ATOM   3321  CG  GLN A 441      -7.468 -24.832  29.641  1.00 16.73           C  
ATOM   3322  CD  GLN A 441      -7.215 -24.722  31.130  1.00 17.50           C  
ATOM   3323  OE1 GLN A 441      -7.804 -23.885  31.818  1.00 16.87           O  
ATOM   3324  NE2 GLN A 441      -6.326 -25.569  31.638  1.00 18.83           N  
ATOM   3325  N   CYS A 442     -11.201 -23.394  26.904  1.00 17.28           N  
ATOM   3326  C   CYS A 442     -12.911 -23.967  25.197  1.00 17.78           C  
ATOM   3327  O   CYS A 442     -14.036 -24.377  24.914  1.00 17.96           O  
ATOM   3328  CA ACYS A 442     -12.625 -23.324  26.547  0.70 17.71           C  
ATOM   3329  CB ACYS A 442     -13.102 -21.870  26.502  0.70 17.67           C  
ATOM   3330  SG ACYS A 442     -13.002 -20.991  28.061  0.70 18.42           S  
ATOM   3332  CB BCYS A 442     -13.273 -22.028  26.811  0.30 17.58           C  
ATOM   3333  SG BCYS A 442     -12.992 -20.813  25.524  0.30 17.50           S  
ATOM   3334  N   PHE A 443     -11.887 -24.019  24.349  1.00 17.92           N  
ATOM   3335  CA  PHE A 443     -12.025 -24.637  23.028  1.00 18.29           C  
ATOM   3336  C   PHE A 443     -10.890 -25.617  22.674  1.00 18.85           C  
ATOM   3337  O   PHE A 443     -10.268 -25.501  21.610  1.00 18.84           O  
ATOM   3338  CB  PHE A 443     -12.254 -23.578  21.929  1.00 17.92           C  
ATOM   3339  CG  PHE A 443     -11.438 -22.323  22.093  1.00 17.48           C  
ATOM   3340  CD1 PHE A 443     -10.057 -22.341  21.915  1.00 17.49           C  
ATOM   3341  CD2 PHE A 443     -12.054 -21.111  22.398  1.00 18.11           C  
ATOM   3342  CE1 PHE A 443      -9.296 -21.182  22.051  1.00 16.33           C  
ATOM   3343  CE2 PHE A 443     -11.296 -19.941  22.538  1.00 17.64           C  
ATOM   3344  CZ  PHE A 443      -9.920 -19.980  22.357  1.00 16.89           C  
ATOM   3345  N   PRO A 444     -10.648 -26.617  23.549  1.00 19.41           N  
ATOM   3346  CA  PRO A 444      -9.541 -27.537  23.334  1.00 19.99           C  
ATOM   3347  C   PRO A 444      -9.871 -28.603  22.291  1.00 20.58           C  
ATOM   3348  O   PRO A 444     -11.043 -28.907  22.052  1.00 20.64           O  
ATOM   3349  CB  PRO A 444      -9.358 -28.184  24.710  1.00 19.90           C  
ATOM   3350  CG  PRO A 444     -10.712 -28.181  25.303  1.00 19.43           C  
ATOM   3351  CD  PRO A 444     -11.417 -26.962  24.761  1.00 19.57           C  
ATOM   3352  N   PHE A 445      -8.831 -29.159  21.682  1.00 21.32           N  
ATOM   3353  CA  PHE A 445      -8.986 -30.221  20.692  1.00 22.27           C  
ATOM   3354  C   PHE A 445      -7.859 -31.231  20.847  1.00 22.80           C  
ATOM   3355  O   PHE A 445      -6.725 -30.863  21.156  1.00 23.25           O  
ATOM   3356  CB  PHE A 445      -9.023 -29.644  19.266  1.00 21.91           C  
ATOM   3357  CG  PHE A 445      -7.797 -28.851  18.895  1.00 22.08           C  
ATOM   3358  CD1 PHE A 445      -6.750 -29.449  18.197  1.00 21.50           C  
ATOM   3359  CD2 PHE A 445      -7.690 -27.504  19.239  1.00 21.54           C  
ATOM   3360  CE1 PHE A 445      -5.611 -28.726  17.855  1.00 22.42           C  
ATOM   3361  CE2 PHE A 445      -6.555 -26.768  18.898  1.00 21.72           C  
ATOM   3362  CZ  PHE A 445      -5.512 -27.381  18.209  1.00 21.99           C  
ATOM   3363  N   GLU A 446      -8.168 -32.505  20.639  1.00 23.78           N  
ATOM   3364  CA  GLU A 446      -7.149 -33.542  20.746  1.00 24.76           C  
ATOM   3365  C   GLU A 446      -6.259 -33.573  19.504  1.00 24.49           C  
ATOM   3366  O   GLU A 446      -5.036 -33.674  19.612  1.00 24.78           O  
ATOM   3367  CB  GLU A 446      -7.785 -34.910  20.990  1.00 24.74           C  
ATOM   3368  CG  GLU A 446      -6.768 -36.018  21.202  1.00 26.20           C  
ATOM   3369  CD  GLU A 446      -7.399 -37.371  21.457  1.00 26.56           C  
ATOM   3370  OE1 GLU A 446      -6.660 -38.290  21.873  1.00 29.85           O  
ATOM   3371  OE2 GLU A 446      -8.622 -37.523  21.242  1.00 29.82           O  
ATOM   3372  N   THR A 447      -6.874 -33.479  18.329  1.00 24.33           N  
ATOM   3373  CA  THR A 447      -6.123 -33.536  17.077  1.00 24.00           C  
ATOM   3374  C   THR A 447      -6.746 -32.649  16.001  1.00 23.36           C  
ATOM   3375  O   THR A 447      -7.920 -32.285  16.088  1.00 23.33           O  
ATOM   3376  CB  THR A 447      -5.975 -35.001  16.563  1.00 24.17           C  
ATOM   3377  OG1 THR A 447      -5.026 -35.047  15.490  1.00 25.64           O  
ATOM   3378  CG2 THR A 447      -7.310 -35.563  16.088  1.00 24.49           C  
ATOM   3379  N   SER A 448      -5.946 -32.311  14.992  1.00 22.77           N  
ATOM   3380  CA  SER A 448      -6.404 -31.508  13.862  1.00 22.20           C  
ATOM   3381  C   SER A 448      -5.583 -31.812  12.613  1.00 21.98           C  
ATOM   3382  O   SER A 448      -4.450 -32.299  12.708  1.00 22.20           O  
ATOM   3383  CB  SER A 448      -6.299 -30.017  14.192  1.00 22.01           C  
ATOM   3384  OG  SER A 448      -4.946 -29.642  14.397  1.00 21.36           O  
ATOM   3385  N   SER A 449      -6.159 -31.503  11.453  1.00 21.43           N  
ATOM   3386  CA  SER A 449      -5.496 -31.697  10.168  1.00 21.09           C  
ATOM   3387  C   SER A 449      -4.735 -30.441   9.731  1.00 20.67           C  
ATOM   3388  O   SER A 449      -3.574 -30.518   9.319  1.00 20.31           O  
ATOM   3389  CB  SER A 449      -6.513 -32.105   9.097  1.00 21.42           C  
ATOM   3390  OG  SER A 449      -7.241 -33.262   9.487  1.00 22.53           O  
ATOM   3391  N   TYR A 450      -5.401 -29.290   9.824  1.00 19.95           N  
ATOM   3392  CA  TYR A 450      -4.807 -28.006   9.453  1.00 19.10           C  
ATOM   3393  C   TYR A 450      -5.405 -26.901  10.302  1.00 17.86           C  
ATOM   3394  O   TYR A 450      -6.411 -27.099  10.987  1.00 17.17           O  
ATOM   3395  CB  TYR A 450      -5.061 -27.673   7.978  1.00 20.22           C  
ATOM   3396  CG  TYR A 450      -4.858 -28.825   7.028  1.00 21.58           C  
ATOM   3397  CD1 TYR A 450      -5.940 -29.593   6.608  1.00 23.26           C  
ATOM   3398  CD2 TYR A 450      -3.589 -29.151   6.555  1.00 22.98           C  
ATOM   3399  CE1 TYR A 450      -5.773 -30.660   5.745  1.00 24.28           C  
ATOM   3400  CE2 TYR A 450      -3.406 -30.227   5.683  1.00 23.90           C  
ATOM   3401  CZ  TYR A 450      -4.507 -30.974   5.286  1.00 23.79           C  
ATOM   3402  OH  TYR A 450      -4.357 -32.037   4.424  1.00 24.60           O  
ATOM   3403  N   PHE A 451      -4.789 -25.728  10.230  1.00 16.38           N  
ATOM   3404  CA  PHE A 451      -5.317 -24.562  10.910  1.00 15.17           C  
ATOM   3405  C   PHE A 451      -5.300 -23.355   9.989  1.00 14.27           C  
ATOM   3406  O   PHE A 451      -4.559 -23.318   8.999  1.00 13.46           O  
ATOM   3407  CB  PHE A 451      -4.523 -24.268  12.194  1.00 15.59           C  
ATOM   3408  CG  PHE A 451      -3.107 -23.809  11.951  1.00 15.86           C  
ATOM   3409  CD1 PHE A 451      -2.827 -22.467  11.693  1.00 16.40           C  
ATOM   3410  CD2 PHE A 451      -2.049 -24.713  12.002  1.00 16.42           C  
ATOM   3411  CE1 PHE A 451      -1.520 -22.035  11.468  1.00 16.81           C  
ATOM   3412  CE2 PHE A 451      -0.736 -24.293  11.783  1.00 16.62           C  
ATOM   3413  CZ  PHE A 451      -0.471 -22.949  11.512  1.00 16.95           C  
ATOM   3414  N   ILE A 452      -6.143 -22.385  10.315  1.00 13.42           N  
ATOM   3415  CA  ILE A 452      -6.040 -21.044   9.759  1.00 13.04           C  
ATOM   3416  C   ILE A 452      -5.730 -20.148  10.947  1.00 12.61           C  
ATOM   3417  O   ILE A 452      -6.491 -20.116  11.917  1.00 12.87           O  
ATOM   3418  CB  ILE A 452      -7.341 -20.580   9.091  1.00 12.82           C  
ATOM   3419  CG1 ILE A 452      -7.720 -21.515   7.937  1.00 13.02           C  
ATOM   3420  CG2 ILE A 452      -7.218 -19.110   8.609  1.00 13.30           C  
ATOM   3421  CD1 ILE A 452      -9.119 -21.277   7.396  1.00 12.82           C  
ATOM   3422  N   GLY A 453      -4.604 -19.446  10.873  1.00 12.24           N  
ATOM   3423  CA  GLY A 453      -4.164 -18.576  11.958  1.00 12.17           C  
ATOM   3424  C   GLY A 453      -4.267 -17.121  11.551  1.00 12.11           C  
ATOM   3425  O   GLY A 453      -4.020 -16.782  10.397  1.00 12.25           O  
ATOM   3426  N   VAL A 454      -4.664 -16.266  12.489  1.00 11.76           N  
ATOM   3427  CA  VAL A 454      -4.749 -14.830  12.228  1.00 11.76           C  
ATOM   3428  C   VAL A 454      -3.788 -14.098  13.155  1.00 11.60           C  
ATOM   3429  O   VAL A 454      -3.837 -14.272  14.380  1.00 11.14           O  
ATOM   3430  CB  VAL A 454      -6.180 -14.277  12.409  1.00 11.88           C  
ATOM   3431  CG1 VAL A 454      -6.278 -12.880  11.813  1.00 12.78           C  
ATOM   3432  CG2 VAL A 454      -7.215 -15.205  11.754  1.00 12.66           C  
ATOM   3433  N   LEU A 455      -2.911 -13.293  12.557  1.00 11.44           N  
ATOM   3434  CA  LEU A 455      -1.888 -12.577  13.305  1.00 11.52           C  
ATOM   3435  C   LEU A 455      -2.285 -11.128  13.526  1.00 11.51           C  
ATOM   3436  O   LEU A 455      -2.545 -10.391  12.567  1.00 11.39           O  
ATOM   3437  CB  LEU A 455      -0.530 -12.650  12.595  1.00 11.45           C  
ATOM   3438  CG  LEU A 455       0.630 -11.943  13.306  1.00 11.22           C  
ATOM   3439  CD1 LEU A 455       0.966 -12.620  14.637  1.00 11.34           C  
ATOM   3440  CD2 LEU A 455       1.853 -11.884  12.415  1.00 12.09           C  
ATOM   3441  N   ASP A 456      -2.295 -10.741  14.800  1.00 11.54           N  
ATOM   3442  CA  ASP A 456      -2.683  -9.412  15.252  1.00 11.96           C  
ATOM   3443  C   ASP A 456      -1.648  -8.928  16.278  1.00 12.22           C  
ATOM   3444  O   ASP A 456      -1.733  -9.266  17.460  1.00 12.05           O  
ATOM   3445  CB  ASP A 456      -4.088  -9.477  15.882  1.00 12.34           C  
ATOM   3446  CG  ASP A 456      -4.607  -8.117  16.329  1.00 12.90           C  
ATOM   3447  OD1 ASP A 456      -5.495  -8.079  17.209  1.00 15.23           O  
ATOM   3448  OD2 ASP A 456      -4.132  -7.091  15.806  1.00 15.07           O  
ATOM   3449  N   ILE A 457      -0.675  -8.143  15.818  1.00 12.39           N  
ATOM   3450  CA  ILE A 457       0.377  -7.598  16.696  1.00 13.30           C  
ATOM   3451  C   ILE A 457       0.060  -6.158  17.120  1.00 13.06           C  
ATOM   3452  O   ILE A 457      -0.843  -5.525  16.562  1.00 13.42           O  
ATOM   3453  CB  ILE A 457       1.793  -7.663  16.037  1.00 13.85           C  
ATOM   3454  CG1 ILE A 457       1.850  -6.791  14.770  1.00 14.61           C  
ATOM   3455  CG2 ILE A 457       2.201  -9.128  15.773  1.00 13.99           C  
ATOM   3456  CD1 ILE A 457       3.241  -6.339  14.357  1.00 14.49           C  
ATOM   3457  N   ALA A 458       0.778  -5.645  18.118  1.00 12.15           N  
ATOM   3458  CA  ALA A 458       0.722  -4.211  18.399  1.00 11.26           C  
ATOM   3459  C   ALA A 458       1.420  -3.496  17.234  1.00 10.82           C  
ATOM   3460  O   ALA A 458       2.520  -3.879  16.841  1.00 10.86           O  
ATOM   3461  CB  ALA A 458       1.395  -3.886  19.724  1.00 11.07           C  
ATOM   3462  N   GLY A 459       0.762  -2.488  16.666  1.00  9.90           N  
ATOM   3463  CA  GLY A 459       1.246  -1.846  15.444  1.00  9.38           C  
ATOM   3464  C   GLY A 459       2.175  -0.671  15.680  1.00  9.31           C  
ATOM   3465  O   GLY A 459       2.268  -0.140  16.789  1.00  9.26           O  
ATOM   3466  N   PHE A 460       2.845  -0.263  14.608  1.00  8.77           N  
ATOM   3467  CA  PHE A 460       3.789   0.850  14.614  1.00  9.03           C  
ATOM   3468  C   PHE A 460       3.200   2.064  15.341  1.00  9.00           C  
ATOM   3469  O   PHE A 460       2.073   2.479  15.063  1.00  8.72           O  
ATOM   3470  CB  PHE A 460       4.134   1.198  13.167  1.00  9.14           C  
ATOM   3471  CG  PHE A 460       5.185   2.259  13.025  1.00  9.76           C  
ATOM   3472  CD1 PHE A 460       6.533   1.944  13.155  1.00 11.54           C  
ATOM   3473  CD2 PHE A 460       4.820   3.572  12.750  1.00 11.11           C  
ATOM   3474  CE1 PHE A 460       7.512   2.936  13.019  1.00 11.86           C  
ATOM   3475  CE2 PHE A 460       5.791   4.571  12.606  1.00 12.04           C  
ATOM   3476  CZ  PHE A 460       7.131   4.250  12.742  1.00 11.30           C  
ATOM   3477  N   GLU A 461       3.950   2.621  16.286  1.00  8.83           N  
ATOM   3478  CA  GLU A 461       3.454   3.764  17.057  1.00  9.23           C  
ATOM   3479  C   GLU A 461       4.593   4.691  17.457  1.00  9.82           C  
ATOM   3480  O   GLU A 461       5.728   4.247  17.643  1.00  9.16           O  
ATOM   3481  CB  GLU A 461       2.677   3.291  18.306  1.00  9.24           C  
ATOM   3482  CG  GLU A 461       3.516   2.526  19.360  1.00  9.21           C  
ATOM   3483  CD  GLU A 461       2.736   2.197  20.642  1.00  9.76           C  
ATOM   3484  OE1 GLU A 461       3.348   2.197  21.741  1.00 11.67           O  
ATOM   3485  OE2 GLU A 461       1.516   1.946  20.558  1.00 10.37           O  
ATOM   3486  N   TYR A 462       4.283   5.977  17.578  1.00 10.29           N  
ATOM   3487  CA  TYR A 462       5.213   6.934  18.173  1.00 11.66           C  
ATOM   3488  C   TYR A 462       4.461   8.103  18.801  1.00 11.61           C  
ATOM   3489  O   TYR A 462       3.302   8.374  18.451  1.00 11.42           O  
ATOM   3490  CB  TYR A 462       6.286   7.416  17.181  1.00 12.99           C  
ATOM   3491  CG  TYR A 462       5.790   8.302  16.051  1.00 15.13           C  
ATOM   3492  CD1 TYR A 462       5.423   9.634  16.281  1.00 16.03           C  
ATOM   3493  CD2 TYR A 462       5.707   7.814  14.747  1.00 17.60           C  
ATOM   3494  CE1 TYR A 462       4.971  10.448  15.238  1.00 17.87           C  
ATOM   3495  CE2 TYR A 462       5.262   8.622  13.698  1.00 18.29           C  
ATOM   3496  CZ  TYR A 462       4.896   9.934  13.951  1.00 17.04           C  
ATOM   3497  OH  TYR A 462       4.458  10.734  12.916  1.00 18.57           O  
ATOM   3498  N   PHE A 463       5.142   8.770  19.730  1.00 11.91           N  
ATOM   3499  CA  PHE A 463       4.574   9.821  20.568  1.00 12.80           C  
ATOM   3500  C   PHE A 463       5.594  10.938  20.712  1.00 13.21           C  
ATOM   3501  O   PHE A 463       6.683  10.870  20.139  1.00 12.99           O  
ATOM   3502  CB  PHE A 463       4.238   9.240  21.949  1.00 12.94           C  
ATOM   3503  CG  PHE A 463       3.380   8.007  21.889  1.00 13.88           C  
ATOM   3504  CD1 PHE A 463       3.957   6.742  21.815  1.00 14.74           C  
ATOM   3505  CD2 PHE A 463       1.989   8.113  21.868  1.00 14.17           C  
ATOM   3506  CE1 PHE A 463       3.161   5.599  21.735  1.00 15.41           C  
ATOM   3507  CE2 PHE A 463       1.186   6.973  21.791  1.00 14.07           C  
ATOM   3508  CZ  PHE A 463       1.773   5.715  21.723  1.00 14.30           C  
ATOM   3509  N   GLU A 464       5.249  11.961  21.492  1.00 13.95           N  
ATOM   3510  CA  GLU A 464       6.198  13.020  21.816  1.00 15.16           C  
ATOM   3511  C   GLU A 464       7.441  12.460  22.511  1.00 14.15           C  
ATOM   3512  O   GLU A 464       8.550  12.931  22.278  1.00 14.78           O  
ATOM   3513  CB  GLU A 464       5.537  14.090  22.684  1.00 15.14           C  
ATOM   3514  CG  GLU A 464       4.586  15.006  21.912  1.00 17.63           C  
ATOM   3515  CD  GLU A 464       4.161  16.226  22.711  1.00 18.61           C  
ATOM   3516  OE1 GLU A 464       4.046  16.130  23.954  1.00 24.03           O  
ATOM   3517  OE2 GLU A 464       3.935  17.287  22.092  1.00 24.58           O  
ATOM   3518  N   HIS A 465       7.243  11.443  23.344  1.00 13.34           N  
ATOM   3519  CA  HIS A 465       8.330  10.777  24.056  1.00 12.64           C  
ATOM   3520  C   HIS A 465       8.243   9.273  23.829  1.00 12.07           C  
ATOM   3521  O   HIS A 465       7.269   8.639  24.226  1.00 12.13           O  
ATOM   3522  CB  HIS A 465       8.265  11.094  25.550  1.00 13.12           C  
ATOM   3523  CG  HIS A 465       8.297  12.561  25.841  1.00 13.41           C  
ATOM   3524  ND1 HIS A 465       9.471  13.279  25.901  1.00 14.52           N  
ATOM   3525  CD2 HIS A 465       7.299  13.452  26.046  1.00 15.76           C  
ATOM   3526  CE1 HIS A 465       9.196  14.548  26.145  1.00 15.80           C  
ATOM   3527  NE2 HIS A 465       7.886  14.679  26.242  1.00 16.00           N  
ATOM   3528  N   ASN A 466       9.271   8.725  23.192  1.00 10.93           N  
ATOM   3529  CA  ASN A 466       9.331   7.306  22.858  1.00 10.39           C  
ATOM   3530  C   ASN A 466      10.383   6.568  23.662  1.00 10.07           C  
ATOM   3531  O   ASN A 466      11.532   7.010  23.746  1.00 10.43           O  
ATOM   3532  CB  ASN A 466       9.630   7.161  21.370  1.00 10.03           C  
ATOM   3533  CG  ASN A 466       8.596   7.841  20.521  1.00  9.98           C  
ATOM   3534  OD1 ASN A 466       7.411   7.514  20.602  1.00  9.23           O  
ATOM   3535  ND2 ASN A 466       9.025   8.811  19.720  1.00  9.26           N  
ATOM   3536  N   SER A 467       9.993   5.431  24.231  1.00  9.68           N  
ATOM   3537  CA  SER A 467      10.880   4.663  25.084  1.00  9.40           C  
ATOM   3538  C   SER A 467      11.051   3.244  24.546  1.00  9.23           C  
ATOM   3539  O   SER A 467      10.763   2.973  23.372  1.00  8.65           O  
ATOM   3540  CB  SER A 467      10.345   4.655  26.523  1.00  9.57           C  
ATOM   3541  OG  SER A 467      11.344   4.282  27.457  1.00 10.81           O  
ATOM   3542  N   PHE A 468      11.518   2.353  25.413  1.00  8.85           N  
ATOM   3543  CA  PHE A 468      11.866   0.983  25.027  1.00  9.04           C  
ATOM   3544  C   PHE A 468      10.653   0.198  24.523  1.00  8.88           C  
ATOM   3545  O   PHE A 468      10.777  -0.635  23.618  1.00  9.04           O  
ATOM   3546  CB  PHE A 468      12.534   0.263  26.198  1.00  9.67           C  
ATOM   3547  CG  PHE A 468      13.211  -1.030  25.819  1.00  9.72           C  
ATOM   3548  CD1 PHE A 468      14.189  -1.061  24.829  1.00 11.52           C  
ATOM   3549  CD2 PHE A 468      12.879  -2.214  26.472  1.00 11.67           C  
ATOM   3550  CE1 PHE A 468      14.821  -2.264  24.486  1.00 12.38           C  
ATOM   3551  CE2 PHE A 468      13.503  -3.415  26.138  1.00 12.33           C  
ATOM   3552  CZ  PHE A 468      14.480  -3.439  25.146  1.00 11.70           C  
ATOM   3553  N   GLU A 469       9.485   0.484  25.095  1.00  8.42           N  
ATOM   3554  CA  GLU A 469       8.233  -0.157  24.666  1.00  8.57           C  
ATOM   3555  C   GLU A 469       7.974   0.131  23.191  1.00  8.20           C  
ATOM   3556  O   GLU A 469       7.692  -0.782  22.415  1.00  8.16           O  
ATOM   3557  CB  GLU A 469       7.052   0.326  25.519  1.00  8.97           C  
ATOM   3558  CG  GLU A 469       7.121  -0.095  26.985  1.00 10.24           C  
ATOM   3559  CD  GLU A 469       7.963   0.837  27.867  1.00 12.58           C  
ATOM   3560  OE1 GLU A 469       8.546   1.822  27.374  1.00 12.16           O  
ATOM   3561  OE2 GLU A 469       8.038   0.574  29.083  1.00 13.39           O  
ATOM   3562  N   GLN A 470       8.111   1.398  22.794  1.00  7.70           N  
ATOM   3563  CA  GLN A 470       7.927   1.772  21.384  1.00  7.57           C  
ATOM   3564  C   GLN A 470       9.006   1.137  20.510  1.00  7.58           C  
ATOM   3565  O   GLN A 470       8.732   0.702  19.401  1.00  7.22           O  
ATOM   3566  CB  GLN A 470       7.941   3.292  21.204  1.00  7.80           C  
ATOM   3567  CG  GLN A 470       6.670   3.987  21.699  1.00  8.56           C  
ATOM   3568  CD  GLN A 470       6.464   3.822  23.191  1.00 10.03           C  
ATOM   3569  OE1 GLN A 470       7.330   4.187  23.991  1.00 10.23           O  
ATOM   3570  NE2 GLN A 470       5.318   3.268  23.575  1.00 10.30           N  
ATOM   3571  N   PHE A 471      10.230   1.084  21.026  1.00  7.59           N  
ATOM   3572  CA  PHE A 471      11.355   0.523  20.277  1.00  7.99           C  
ATOM   3573  C   PHE A 471      11.076  -0.947  19.960  1.00  8.11           C  
ATOM   3574  O   PHE A 471      11.218  -1.386  18.814  1.00  8.27           O  
ATOM   3575  CB  PHE A 471      12.645   0.669  21.085  1.00  8.56           C  
ATOM   3576  CG  PHE A 471      13.873   0.159  20.379  1.00  8.79           C  
ATOM   3577  CD1 PHE A 471      14.534   0.945  19.444  1.00 10.04           C  
ATOM   3578  CD2 PHE A 471      14.375  -1.105  20.669  1.00 10.78           C  
ATOM   3579  CE1 PHE A 471      15.680   0.483  18.797  1.00 11.45           C  
ATOM   3580  CE2 PHE A 471      15.520  -1.583  20.032  1.00 10.77           C  
ATOM   3581  CZ  PHE A 471      16.171  -0.788  19.090  1.00 10.67           C  
ATOM   3582  N   CYS A 472      10.645  -1.688  20.975  1.00  8.03           N  
ATOM   3583  CA  CYS A 472      10.298  -3.098  20.805  1.00  8.16           C  
ATOM   3584  C   CYS A 472       9.101  -3.302  19.862  1.00  7.90           C  
ATOM   3585  O   CYS A 472       9.151  -4.152  18.965  1.00  7.72           O  
ATOM   3586  CB  CYS A 472      10.060  -3.743  22.168  1.00  8.30           C  
ATOM   3587  SG  CYS A 472      11.566  -3.900  23.150  1.00 10.78           S  
ATOM   3588  N   ILE A 473       8.040  -2.515  20.045  1.00  7.29           N  
ATOM   3589  CA  ILE A 473       6.867  -2.594  19.164  1.00  7.56           C  
ATOM   3590  C   ILE A 473       7.263  -2.317  17.711  1.00  7.17           C  
ATOM   3591  O   ILE A 473       6.912  -3.074  16.791  1.00  7.57           O  
ATOM   3592  CB  ILE A 473       5.746  -1.628  19.609  1.00  7.20           C  
ATOM   3593  CG1 ILE A 473       5.108  -2.131  20.910  1.00  8.06           C  
ATOM   3594  CG2 ILE A 473       4.681  -1.484  18.511  1.00  7.82           C  
ATOM   3595  CD1 ILE A 473       4.225  -1.117  21.596  1.00  8.53           C  
ATOM   3596  N   ASN A 474       8.034  -1.256  17.507  1.00  6.86           N  
ATOM   3597  CA  ASN A 474       8.418  -0.876  16.146  1.00  7.57           C  
ATOM   3598  C   ASN A 474       9.365  -1.877  15.474  1.00  7.97           C  
ATOM   3599  O   ASN A 474       9.273  -2.112  14.262  1.00  8.01           O  
ATOM   3600  CB  ASN A 474       8.908   0.574  16.117  1.00  7.52           C  
ATOM   3601  CG  ASN A 474       7.784   1.554  16.452  1.00  7.07           C  
ATOM   3602  OD1 ASN A 474       6.605   1.210  16.343  1.00  6.97           O  
ATOM   3603  ND2 ASN A 474       8.141   2.764  16.880  1.00  6.98           N  
ATOM   3604  N   TYR A 475      10.229  -2.495  16.277  1.00  8.03           N  
ATOM   3605  CA  TYR A 475      11.084  -3.592  15.822  1.00  8.85           C  
ATOM   3606  C   TYR A 475      10.239  -4.769  15.308  1.00  9.12           C  
ATOM   3607  O   TYR A 475      10.502  -5.299  14.226  1.00  9.07           O  
ATOM   3608  CB  TYR A 475      12.021  -4.007  16.959  1.00  9.20           C  
ATOM   3609  CG  TYR A 475      12.651  -5.378  16.846  1.00  9.35           C  
ATOM   3610  CD1 TYR A 475      13.468  -5.715  15.762  1.00  9.34           C  
ATOM   3611  CD2 TYR A 475      12.461  -6.327  17.856  1.00 10.71           C  
ATOM   3612  CE1 TYR A 475      14.065  -6.981  15.677  1.00 10.37           C  
ATOM   3613  CE2 TYR A 475      13.053  -7.593  17.779  1.00 10.53           C  
ATOM   3614  CZ  TYR A 475      13.849  -7.907  16.688  1.00 11.35           C  
ATOM   3615  OH  TYR A 475      14.429  -9.157  16.612  1.00 12.04           O  
ATOM   3616  N   CYS A 476       9.215  -5.157  16.064  1.00  9.15           N  
ATOM   3617  C   CYS A 476       7.673  -5.898  14.295  1.00  9.33           C  
ATOM   3618  O   CYS A 476       7.591  -6.742  13.399  1.00  9.04           O  
ATOM   3619  CA ACYS A 476       8.327  -6.241  15.626  0.50  9.69           C  
ATOM   3620  CB ACYS A 476       7.260  -6.539  16.673  0.50  9.77           C  
ATOM   3621  SG ACYS A 476       7.930  -7.076  18.250  0.50 13.05           S  
ATOM   3623  CB BCYS A 476       7.256  -6.475  16.703  0.50  9.48           C  
ATOM   3624  SG BCYS A 476       6.047  -7.719  16.275  0.50 11.08           S  
ATOM   3625  N   ASN A 477       7.222  -4.652  14.162  1.00  9.40           N  
ATOM   3626  CA  ASN A 477       6.611  -4.196  12.915  1.00 10.15           C  
ATOM   3627  C   ASN A 477       7.592  -4.221  11.728  1.00 10.32           C  
ATOM   3628  O   ASN A 477       7.192  -4.546  10.602  1.00 10.66           O  
ATOM   3629  CB  ASN A 477       5.969  -2.820  13.098  1.00 10.38           C  
ATOM   3630  CG  ASN A 477       4.612  -2.893  13.796  1.00 11.23           C  
ATOM   3631  OD1 ASN A 477       3.563  -2.795  13.148  1.00 13.62           O  
ATOM   3632  ND2 ASN A 477       4.623  -3.073  15.121  1.00 10.14           N  
ATOM   3633  N   GLU A 478       8.866  -3.898  11.984  1.00 10.72           N  
ATOM   3634  CA  GLU A 478       9.940  -4.049  10.978  1.00 11.51           C  
ATOM   3635  C   GLU A 478      10.016  -5.491  10.496  1.00 11.88           C  
ATOM   3636  O   GLU A 478      10.079  -5.758   9.290  1.00 11.71           O  
ATOM   3637  CB  GLU A 478      11.328  -3.741  11.562  1.00 12.05           C  
ATOM   3638  CG  GLU A 478      11.698  -2.319  11.802  1.00 14.80           C  
ATOM   3639  CD  GLU A 478      11.656  -1.405  10.581  1.00 15.71           C  
ATOM   3640  OE1 GLU A 478      11.325  -0.253  10.815  1.00 14.91           O  
ATOM   3641  OE2 GLU A 478      11.939  -1.786   9.418  1.00 16.97           O  
ATOM   3642  N   LYS A 479      10.031  -6.414  11.455  1.00 11.90           N  
ATOM   3643  CA  LYS A 479      10.179  -7.842  11.162  1.00 12.42           C  
ATOM   3644  C   LYS A 479       9.010  -8.332  10.315  1.00 12.46           C  
ATOM   3645  O   LYS A 479       9.202  -9.076   9.346  1.00 12.63           O  
ATOM   3646  CB  LYS A 479      10.288  -8.655  12.457  1.00 12.79           C  
ATOM   3647  CG  LYS A 479      11.540  -8.355  13.296  1.00 14.42           C  
ATOM   3648  CD  LYS A 479      12.756  -9.172  12.861  1.00 16.99           C  
ATOM   3649  CE  LYS A 479      12.711 -10.602  13.403  1.00 17.12           C  
ATOM   3650  NZ  LYS A 479      13.926 -11.384  13.025  1.00 17.98           N  
ATOM   3651  N   LEU A 480       7.804  -7.899  10.669  1.00 12.12           N  
ATOM   3652  CA  LEU A 480       6.615  -8.308   9.917  1.00 12.60           C  
ATOM   3653  C   LEU A 480       6.572  -7.726   8.504  1.00 12.50           C  
ATOM   3654  O   LEU A 480       6.174  -8.412   7.556  1.00 11.92           O  
ATOM   3655  CB  LEU A 480       5.328  -8.017  10.693  1.00 13.12           C  
ATOM   3656  CG  LEU A 480       4.809  -9.205  11.519  1.00 14.17           C  
ATOM   3657  CD1 LEU A 480       4.443 -10.382  10.609  1.00 15.27           C  
ATOM   3658  CD2 LEU A 480       5.800  -9.645  12.601  1.00 15.58           C  
ATOM   3659  N   GLN A 481       7.004  -6.475   8.351  1.00 11.81           N  
ATOM   3660  CA  GLN A 481       7.115  -5.885   7.014  1.00 12.06           C  
ATOM   3661  C   GLN A 481       8.130  -6.643   6.162  1.00 12.02           C  
ATOM   3662  O   GLN A 481       7.935  -6.819   4.954  1.00 12.18           O  
ATOM   3663  CB  GLN A 481       7.490  -4.399   7.082  1.00 11.89           C  
ATOM   3664  CG  GLN A 481       7.535  -3.705   5.711  1.00 11.98           C  
ATOM   3665  CD  GLN A 481       6.184  -3.669   4.997  1.00 12.78           C  
ATOM   3666  OE1 GLN A 481       5.137  -3.467   5.615  1.00 13.17           O  
ATOM   3667  NE2 GLN A 481       6.209  -3.869   3.683  1.00 12.80           N  
ATOM   3668  N   GLN A 482       9.207  -7.098   6.796  1.00 12.30           N  
ATOM   3669  CA  GLN A 482      10.230  -7.865   6.093  1.00 12.70           C  
ATOM   3670  C   GLN A 482       9.661  -9.189   5.572  1.00 12.52           C  
ATOM   3671  O   GLN A 482       9.988  -9.617   4.460  1.00 12.34           O  
ATOM   3672  CB  GLN A 482      11.454  -8.073   6.999  1.00 13.12           C  
ATOM   3673  CG  GLN A 482      12.531  -9.057   6.499  1.00 15.38           C  
ATOM   3674  CD  GLN A 482      13.069  -8.761   5.111  1.00 18.23           C  
ATOM   3675  OE1 GLN A 482      13.455  -9.683   4.389  1.00 19.35           O  
ATOM   3676  NE2 GLN A 482      13.107  -7.486   4.728  1.00 19.64           N  
ATOM   3677  N   PHE A 483       8.785  -9.810   6.360  1.00 12.56           N  
ATOM   3678  CA  PHE A 483       8.124 -11.046   5.936  1.00 12.85           C  
ATOM   3679  C   PHE A 483       7.253 -10.809   4.700  1.00 12.76           C  
ATOM   3680  O   PHE A 483       7.254 -11.627   3.763  1.00 12.98           O  
ATOM   3681  CB  PHE A 483       7.306 -11.668   7.076  1.00 13.38           C  
ATOM   3682  CG  PHE A 483       6.501 -12.875   6.657  1.00 14.45           C  
ATOM   3683  CD1 PHE A 483       5.122 -12.785   6.497  1.00 15.53           C  
ATOM   3684  CD2 PHE A 483       7.126 -14.093   6.407  1.00 15.61           C  
ATOM   3685  CE1 PHE A 483       4.374 -13.895   6.099  1.00 15.94           C  
ATOM   3686  CE2 PHE A 483       6.381 -15.209   6.012  1.00 16.76           C  
ATOM   3687  CZ  PHE A 483       5.008 -15.104   5.860  1.00 15.54           C  
ATOM   3688  N   PHE A 484       6.518  -9.699   4.697  1.00 12.29           N  
ATOM   3689  CA  PHE A 484       5.736  -9.303   3.521  1.00 12.31           C  
ATOM   3690  C   PHE A 484       6.638  -9.078   2.312  1.00 12.38           C  
ATOM   3691  O   PHE A 484       6.360  -9.600   1.233  1.00 12.34           O  
ATOM   3692  CB  PHE A 484       4.913  -8.037   3.784  1.00 12.77           C  
ATOM   3693  CG  PHE A 484       4.192  -7.524   2.557  1.00 13.12           C  
ATOM   3694  CD1 PHE A 484       2.951  -8.042   2.198  1.00 15.13           C  
ATOM   3695  CD2 PHE A 484       4.770  -6.542   1.749  1.00 14.02           C  
ATOM   3696  CE1 PHE A 484       2.281  -7.574   1.058  1.00 15.87           C  
ATOM   3697  CE2 PHE A 484       4.112  -6.070   0.608  1.00 14.84           C  
ATOM   3698  CZ  PHE A 484       2.867  -6.591   0.264  1.00 15.67           C  
ATOM   3699  N   ASN A 485       7.702  -8.291   2.494  1.00 12.41           N  
ATOM   3700  CA  ASN A 485       8.660  -8.017   1.414  1.00 13.02           C  
ATOM   3701  C   ASN A 485       9.236  -9.307   0.812  1.00 13.54           C  
ATOM   3702  O   ASN A 485       9.331  -9.455  -0.417  1.00 13.20           O  
ATOM   3703  CB  ASN A 485       9.805  -7.123   1.914  1.00 13.02           C  
ATOM   3704  CG  ASN A 485       9.364  -5.694   2.219  1.00 13.14           C  
ATOM   3705  OD1 ASN A 485       8.256  -5.276   1.891  1.00 13.56           O  
ATOM   3706  ND2 ASN A 485      10.254  -4.935   2.862  1.00 14.72           N  
ATOM   3707  N   GLU A 486       9.598 -10.231   1.699  1.00 14.22           N  
ATOM   3708  CA  GLU A 486      10.172 -11.527   1.345  1.00 15.95           C  
ATOM   3709  C   GLU A 486       9.171 -12.384   0.568  1.00 15.68           C  
ATOM   3710  O   GLU A 486       9.490 -12.905  -0.503  1.00 15.23           O  
ATOM   3711  CB  GLU A 486      10.646 -12.224   2.630  1.00 15.93           C  
ATOM   3712  CG  GLU A 486      10.849 -13.747   2.583  1.00 18.37           C  
ATOM   3713  CD  GLU A 486      11.024 -14.344   3.983  1.00 18.92           C  
ATOM   3714  OE1 GLU A 486      11.919 -13.885   4.724  1.00 23.89           O  
ATOM   3715  OE2 GLU A 486      10.267 -15.269   4.349  1.00 22.52           O  
ATOM   3716  N   ARG A 487       7.956 -12.508   1.101  1.00 15.56           N  
ATOM   3717  CA  ARG A 487       6.932 -13.359   0.495  1.00 16.29           C  
ATOM   3718  C   ARG A 487       6.310 -12.768  -0.786  1.00 16.41           C  
ATOM   3719  O   ARG A 487       6.104 -13.496  -1.769  1.00 17.42           O  
ATOM   3720  CB  ARG A 487       5.859 -13.710   1.543  1.00 16.26           C  
ATOM   3721  CG  ARG A 487       4.806 -14.735   1.108  1.00 17.34           C  
ATOM   3722  CD  ARG A 487       5.391 -16.118   0.803  1.00 17.48           C  
ATOM   3723  NE  ARG A 487       5.901 -16.821   1.982  1.00 18.10           N  
ATOM   3724  CZ  ARG A 487       5.169 -17.589   2.789  1.00 18.95           C  
ATOM   3725  NH1 ARG A 487       3.868 -17.749   2.582  1.00 18.53           N  
ATOM   3726  NH2 ARG A 487       5.740 -18.189   3.824  1.00 20.15           N  
ATOM   3727  N   ILE A 488       6.041 -11.461  -0.788  1.00 16.38           N  
ATOM   3728  CA  ILE A 488       5.243 -10.825  -1.855  1.00 16.45           C  
ATOM   3729  C   ILE A 488       6.039 -10.072  -2.925  1.00 16.67           C  
ATOM   3730  O   ILE A 488       5.620 -10.018  -4.089  1.00 17.50           O  
ATOM   3731  CB  ILE A 488       4.133  -9.900  -1.271  1.00 16.48           C  
ATOM   3732  CG1 ILE A 488       3.183 -10.704  -0.375  1.00 16.62           C  
ATOM   3733  CG2 ILE A 488       3.334  -9.188  -2.378  1.00 16.60           C  
ATOM   3734  CD1 ILE A 488       2.549 -11.927  -1.055  1.00 17.33           C  
ATOM   3735  N   LEU A 489       7.151  -9.462  -2.532  1.00 15.80           N  
ATOM   3736  CA  LEU A 489       7.942  -8.677  -3.476  1.00 15.79           C  
ATOM   3737  C   LEU A 489       9.174  -9.415  -3.982  1.00 15.89           C  
ATOM   3738  O   LEU A 489       9.560  -9.241  -5.143  1.00 16.53           O  
ATOM   3739  CB  LEU A 489       8.319  -7.311  -2.886  1.00 15.31           C  
ATOM   3740  CG  LEU A 489       7.174  -6.312  -2.688  1.00 15.76           C  
ATOM   3741  CD1 LEU A 489       7.634  -5.111  -1.878  1.00 14.91           C  
ATOM   3742  CD2 LEU A 489       6.581  -5.864  -4.028  1.00 15.89           C  
ATOM   3743  N   LYS A 490       9.792 -10.228  -3.125  1.00 15.75           N  
ATOM   3744  CA  LYS A 490      10.990 -10.975  -3.516  1.00 16.13           C  
ATOM   3745  C   LYS A 490      10.636 -12.329  -4.132  1.00 16.00           C  
ATOM   3746  O   LYS A 490      10.915 -12.571  -5.309  1.00 16.03           O  
ATOM   3747  CB  LYS A 490      11.942 -11.172  -2.334  1.00 16.13           C  
ATOM   3748  CG  LYS A 490      13.350 -11.627  -2.754  1.00 18.15           C  
ATOM   3749  CD  LYS A 490      14.001 -12.485  -1.680  1.00 22.09           C  
ATOM   3750  CE  LYS A 490      14.285 -11.692  -0.430  1.00 24.52           C  
ATOM   3751  NZ  LYS A 490      14.113 -12.534   0.797  1.00 27.45           N  
ATOM   3752  N   GLU A 491      10.018 -13.204  -3.337  1.00 16.00           N  
ATOM   3753  CA  GLU A 491       9.716 -14.571  -3.787  1.00 16.09           C  
ATOM   3754  C   GLU A 491       8.783 -14.621  -4.998  1.00 15.59           C  
ATOM   3755  O   GLU A 491       8.903 -15.513  -5.836  1.00 15.15           O  
ATOM   3756  CB  GLU A 491       9.155 -15.410  -2.638  1.00 16.12           C  
ATOM   3757  CG  GLU A 491      10.203 -15.807  -1.606  1.00 17.06           C  
ATOM   3758  CD  GLU A 491       9.612 -16.504  -0.385  1.00 17.69           C  
ATOM   3759  OE1 GLU A 491      10.355 -16.689   0.604  1.00 21.26           O  
ATOM   3760  OE2 GLU A 491       8.417 -16.860  -0.407  1.00 20.12           O  
ATOM   3761  N   GLU A 492       7.863 -13.664  -5.090  1.00 15.18           N  
ATOM   3762  CA  GLU A 492       6.951 -13.590  -6.226  1.00 15.49           C  
ATOM   3763  C   GLU A 492       7.735 -13.371  -7.522  1.00 15.31           C  
ATOM   3764  O   GLU A 492       7.487 -14.031  -8.534  1.00 15.14           O  
ATOM   3765  CB  GLU A 492       5.927 -12.471  -6.012  1.00 15.57           C  
ATOM   3766  CG  GLU A 492       4.819 -12.411  -7.041  1.00 17.16           C  
ATOM   3767  CD  GLU A 492       3.711 -13.442  -6.817  1.00 18.88           C  
ATOM   3768  OE1 GLU A 492       2.730 -13.415  -7.592  1.00 20.16           O  
ATOM   3769  OE2 GLU A 492       3.805 -14.262  -5.878  1.00 19.16           O  
ATOM   3770  N   GLN A 493       8.695 -12.450  -7.479  1.00 15.22           N  
ATOM   3771  CA  GLN A 493       9.500 -12.135  -8.660  1.00 15.22           C  
ATOM   3772  C   GLN A 493      10.491 -13.248  -8.997  1.00 15.40           C  
ATOM   3773  O   GLN A 493      10.771 -13.502 -10.173  1.00 15.16           O  
ATOM   3774  CB  GLN A 493      10.193 -10.786  -8.491  1.00 15.13           C  
ATOM   3775  CG  GLN A 493       9.189  -9.650  -8.324  1.00 14.41           C  
ATOM   3776  CD  GLN A 493       9.800  -8.282  -8.507  1.00 15.36           C  
ATOM   3777  OE1 GLN A 493      10.090  -7.871  -9.626  1.00 13.40           O  
ATOM   3778  NE2 GLN A 493       9.981  -7.558  -7.405  1.00 14.69           N  
ATOM   3779  N   GLU A 494      11.004 -13.918  -7.967  1.00 15.66           N  
ATOM   3780  CA  GLU A 494      11.872 -15.078  -8.158  1.00 16.30           C  
ATOM   3781  C   GLU A 494      11.130 -16.209  -8.865  1.00 16.49           C  
ATOM   3782  O   GLU A 494      11.702 -16.875  -9.734  1.00 16.16           O  
ATOM   3783  CB  GLU A 494      12.444 -15.559  -6.827  1.00 16.87           C  
ATOM   3784  CG  GLU A 494      13.482 -14.612  -6.254  1.00 18.43           C  
ATOM   3785  CD  GLU A 494      13.975 -15.012  -4.878  1.00 21.29           C  
ATOM   3786  OE1 GLU A 494      13.397 -15.932  -4.251  1.00 22.56           O  
ATOM   3787  OE2 GLU A 494      14.957 -14.392  -4.420  1.00 23.04           O  
ATOM   3788  N   LEU A 495       9.859 -16.404  -8.501  1.00 16.23           N  
ATOM   3789  CA  LEU A 495       8.996 -17.391  -9.162  1.00 16.48           C  
ATOM   3790  C   LEU A 495       8.801 -17.079 -10.643  1.00 16.35           C  
ATOM   3791  O   LEU A 495       8.969 -17.955 -11.494  1.00 16.47           O  
ATOM   3792  CB  LEU A 495       7.634 -17.486  -8.463  1.00 16.33           C  
ATOM   3793  CG  LEU A 495       6.592 -18.443  -9.063  1.00 17.44           C  
ATOM   3794  CD1 LEU A 495       7.093 -19.890  -9.072  1.00 17.48           C  
ATOM   3795  CD2 LEU A 495       5.276 -18.333  -8.308  1.00 16.99           C  
ATOM   3796  N   TYR A 496       8.445 -15.833 -10.944  1.00 16.01           N  
ATOM   3797  CA  TYR A 496       8.271 -15.399 -12.328  1.00 16.39           C  
ATOM   3798  C   TYR A 496       9.549 -15.649 -13.134  1.00 17.04           C  
ATOM   3799  O   TYR A 496       9.497 -16.140 -14.261  1.00 16.89           O  
ATOM   3800  CB  TYR A 496       7.915 -13.912 -12.396  1.00 15.82           C  
ATOM   3801  CG  TYR A 496       6.625 -13.477 -11.715  1.00 15.58           C  
ATOM   3802  CD1 TYR A 496       6.429 -12.138 -11.388  1.00 14.72           C  
ATOM   3803  CD2 TYR A 496       5.603 -14.388 -11.405  1.00 14.15           C  
ATOM   3804  CE1 TYR A 496       5.258 -11.704 -10.781  1.00 15.00           C  
ATOM   3805  CE2 TYR A 496       4.421 -13.963 -10.788  1.00 14.58           C  
ATOM   3806  CZ  TYR A 496       4.258 -12.618 -10.485  1.00 15.33           C  
ATOM   3807  OH  TYR A 496       3.108 -12.165  -9.879  1.00 15.79           O  
ATOM   3808  N   GLN A 497      10.692 -15.314 -12.536  1.00 17.79           N  
ATOM   3809  CA  GLN A 497      12.003 -15.493 -13.164  1.00 19.37           C  
ATOM   3810  C   GLN A 497      12.301 -16.968 -13.459  1.00 19.54           C  
ATOM   3811  O   GLN A 497      12.667 -17.320 -14.584  1.00 19.89           O  
ATOM   3812  CB  GLN A 497      13.091 -14.906 -12.259  1.00 19.62           C  
ATOM   3813  CG  GLN A 497      14.515 -15.155 -12.725  1.00 22.84           C  
ATOM   3814  CD  GLN A 497      15.044 -14.033 -13.583  1.00 26.67           C  
ATOM   3815  OE1 GLN A 497      14.618 -13.852 -14.728  1.00 29.66           O  
ATOM   3816  NE2 GLN A 497      15.986 -13.269 -13.036  1.00 27.50           N  
ATOM   3817  N   LYS A 498      12.142 -17.809 -12.439  1.00 19.90           N  
ATOM   3818  CA  LYS A 498      12.383 -19.255 -12.528  1.00 20.71           C  
ATOM   3819  C   LYS A 498      11.506 -19.911 -13.598  1.00 20.52           C  
ATOM   3820  O   LYS A 498      11.925 -20.866 -14.265  1.00 20.35           O  
ATOM   3821  CB  LYS A 498      12.142 -19.894 -11.155  1.00 20.83           C  
ATOM   3822  CG  LYS A 498      12.141 -21.420 -11.106  1.00 21.88           C  
ATOM   3823  CD  LYS A 498      12.070 -21.938  -9.666  1.00 22.44           C  
ATOM   3824  CE  LYS A 498      10.778 -21.525  -8.947  1.00 25.52           C  
ATOM   3825  NZ  LYS A 498       9.575 -22.259  -9.445  1.00 27.29           N  
ATOM   3826  N   GLU A 499      10.296 -19.384 -13.756  1.00 20.44           N  
ATOM   3827  CA  GLU A 499       9.329 -19.917 -14.715  1.00 20.30           C  
ATOM   3828  C   GLU A 499       9.479 -19.314 -16.112  1.00 20.26           C  
ATOM   3829  O   GLU A 499       8.817 -19.749 -17.065  1.00 19.97           O  
ATOM   3830  CB  GLU A 499       7.907 -19.732 -14.179  1.00 20.42           C  
ATOM   3831  CG  GLU A 499       7.555 -20.714 -13.069  1.00 20.69           C  
ATOM   3832  CD  GLU A 499       7.370 -22.139 -13.576  1.00 21.79           C  
ATOM   3833  OE1 GLU A 499       6.711 -22.321 -14.623  1.00 21.59           O  
ATOM   3834  OE2 GLU A 499       7.877 -23.073 -12.920  1.00 22.25           O  
ATOM   3835  N   GLY A 500      10.354 -18.315 -16.226  1.00 19.80           N  
ATOM   3836  CA  GLY A 500      10.657 -17.672 -17.505  1.00 19.47           C  
ATOM   3837  C   GLY A 500       9.552 -16.788 -18.055  1.00 19.38           C  
ATOM   3838  O   GLY A 500       9.372 -16.701 -19.272  1.00 19.21           O  
ATOM   3839  N   LEU A 501       8.821 -16.115 -17.165  1.00 18.85           N  
ATOM   3840  CA  LEU A 501       7.663 -15.308 -17.565  1.00 18.75           C  
ATOM   3841  C   LEU A 501       7.988 -13.938 -18.165  1.00 18.88           C  
ATOM   3842  O   LEU A 501       7.125 -13.319 -18.789  1.00 19.03           O  
ATOM   3843  CB  LEU A 501       6.685 -15.131 -16.394  1.00 18.32           C  
ATOM   3844  CG  LEU A 501       6.077 -16.372 -15.741  1.00 18.57           C  
ATOM   3845  CD1 LEU A 501       5.060 -15.939 -14.696  1.00 16.92           C  
ATOM   3846  CD2 LEU A 501       5.424 -17.309 -16.771  1.00 18.67           C  
ATOM   3847  N   GLY A 502       9.215 -13.462 -17.968  1.00 19.28           N  
ATOM   3848  CA  GLY A 502       9.617 -12.140 -18.459  1.00 19.64           C  
ATOM   3849  C   GLY A 502       8.805 -10.981 -17.896  1.00 20.06           C  
ATOM   3850  O   GLY A 502       8.449 -10.047 -18.625  1.00 20.20           O  
ATOM   3851  N   VAL A 503       8.503 -11.046 -16.601  1.00 20.05           N  
ATOM   3852  CA  VAL A 503       7.817  -9.956 -15.909  1.00 20.37           C  
ATOM   3853  C   VAL A 503       8.852  -8.900 -15.516  1.00 20.66           C  
ATOM   3854  O   VAL A 503       9.864  -9.230 -14.891  1.00 20.48           O  
ATOM   3855  CB  VAL A 503       7.073 -10.458 -14.642  1.00 20.24           C  
ATOM   3856  CG1 VAL A 503       6.369  -9.307 -13.929  1.00 19.83           C  
ATOM   3857  CG2 VAL A 503       6.074 -11.553 -15.002  1.00 20.07           C  
ATOM   3858  N   ASN A 504       8.599  -7.646 -15.896  1.00 21.38           N  
ATOM   3859  CA  ASN A 504       9.473  -6.524 -15.540  1.00 21.97           C  
ATOM   3860  C   ASN A 504       9.762  -6.524 -14.042  1.00 21.83           C  
ATOM   3861  O   ASN A 504       8.842  -6.663 -13.234  1.00 21.95           O  
ATOM   3862  CB  ASN A 504       8.836  -5.186 -15.942  1.00 22.56           C  
ATOM   3863  CG  ASN A 504       8.742  -5.002 -17.452  1.00 23.87           C  
ATOM   3864  OD1 ASN A 504       9.494  -5.607 -18.217  1.00 25.67           O  
ATOM   3865  ND2 ASN A 504       7.818  -4.148 -17.884  1.00 25.77           N  
ATOM   3866  N   GLU A 505      11.037  -6.396 -13.678  1.00 21.57           N  
ATOM   3867  CA  GLU A 505      11.417  -6.380 -12.266  1.00 21.27           C  
ATOM   3868  C   GLU A 505      11.010  -5.065 -11.616  1.00 20.33           C  
ATOM   3869  O   GLU A 505      11.203  -3.993 -12.184  1.00 20.33           O  
ATOM   3870  CB  GLU A 505      12.915  -6.643 -12.068  1.00 21.34           C  
ATOM   3871  CG  GLU A 505      13.316  -6.775 -10.588  1.00 22.17           C  
ATOM   3872  CD  GLU A 505      14.805  -6.971 -10.357  1.00 22.97           C  
ATOM   3873  OE1 GLU A 505      15.209  -7.035  -9.171  1.00 24.47           O  
ATOM   3874  OE2 GLU A 505      15.569  -7.060 -11.344  1.00 24.99           O  
ATOM   3875  N   VAL A 506      10.430  -5.168 -10.424  1.00 19.39           N  
ATOM   3876  CA  VAL A 506      10.087  -4.004  -9.622  1.00 18.53           C  
ATOM   3877  C   VAL A 506      11.089  -3.938  -8.475  1.00 18.20           C  
ATOM   3878  O   VAL A 506      11.194  -4.871  -7.677  1.00 17.57           O  
ATOM   3879  CB  VAL A 506       8.633  -4.091  -9.087  1.00 18.66           C  
ATOM   3880  CG1 VAL A 506       8.366  -3.020  -8.039  1.00 18.34           C  
ATOM   3881  CG2 VAL A 506       7.637  -3.971 -10.236  1.00 18.05           C  
ATOM   3882  N   HIS A 507      11.855  -2.854  -8.430  1.00 18.09           N  
ATOM   3883  CA  HIS A 507      12.797  -2.637  -7.339  1.00 18.24           C  
ATOM   3884  C   HIS A 507      12.102  -1.890  -6.207  1.00 18.31           C  
ATOM   3885  O   HIS A 507      11.186  -1.101  -6.439  1.00 17.92           O  
ATOM   3886  CB  HIS A 507      14.030  -1.877  -7.828  1.00 18.58           C  
ATOM   3887  CG  HIS A 507      14.900  -2.680  -8.746  1.00 19.23           C  
ATOM   3888  ND1 HIS A 507      14.697  -2.730 -10.108  1.00 20.44           N  
ATOM   3889  CD2 HIS A 507      15.968  -3.473  -8.496  1.00 20.66           C  
ATOM   3890  CE1 HIS A 507      15.603  -3.519 -10.658  1.00 20.33           C  
ATOM   3891  NE2 HIS A 507      16.390  -3.978  -9.702  1.00 21.45           N  
ATOM   3892  N   TYR A 508      12.543  -2.152  -4.984  1.00 18.29           N  
ATOM   3893  CA  TYR A 508      11.939  -1.567  -3.790  1.00 18.91           C  
ATOM   3894  C   TYR A 508      13.010  -1.438  -2.720  1.00 18.77           C  
ATOM   3895  O   TYR A 508      14.058  -2.082  -2.802  1.00 18.91           O  
ATOM   3896  CB  TYR A 508      10.785  -2.444  -3.279  1.00 19.08           C  
ATOM   3897  CG  TYR A 508      11.210  -3.850  -2.904  1.00 19.64           C  
ATOM   3898  CD1 TYR A 508      11.343  -4.843  -3.877  1.00 19.51           C  
ATOM   3899  CD2 TYR A 508      11.487  -4.186  -1.576  1.00 19.26           C  
ATOM   3900  CE1 TYR A 508      11.743  -6.131  -3.538  1.00 19.73           C  
ATOM   3901  CE2 TYR A 508      11.884  -5.473  -1.227  1.00 20.13           C  
ATOM   3902  CZ  TYR A 508      12.006  -6.439  -2.213  1.00 20.03           C  
ATOM   3903  OH  TYR A 508      12.402  -7.712  -1.878  1.00 21.56           O  
ATOM   3904  N   VAL A 509      12.744  -0.609  -1.717  1.00 18.80           N  
ATOM   3905  CA  VAL A 509      13.685  -0.421  -0.619  1.00 18.79           C  
ATOM   3906  C   VAL A 509      13.411  -1.483   0.438  1.00 18.43           C  
ATOM   3907  O   VAL A 509      12.344  -1.498   1.055  1.00 18.75           O  
ATOM   3908  CB  VAL A 509      13.593   1.003  -0.014  1.00 18.92           C  
ATOM   3909  CG1 VAL A 509      14.606   1.181   1.124  1.00 19.87           C  
ATOM   3910  CG2 VAL A 509      13.818   2.059  -1.094  1.00 20.13           C  
ATOM   3911  N   ASP A 510      14.370  -2.384   0.624  1.00 17.62           N  
ATOM   3912  CA  ASP A 510      14.244  -3.416   1.641  1.00 17.42           C  
ATOM   3913  C   ASP A 510      14.642  -2.876   3.012  1.00 16.67           C  
ATOM   3914  O   ASP A 510      15.380  -1.893   3.106  1.00 16.92           O  
ATOM   3915  CB  ASP A 510      15.084  -4.637   1.286  1.00 17.77           C  
ATOM   3916  CG  ASP A 510      14.758  -5.826   2.160  1.00 18.50           C  
ATOM   3917  OD1 ASP A 510      13.554  -6.114   2.350  1.00 19.80           O  
ATOM   3918  OD2 ASP A 510      15.702  -6.441   2.687  1.00 20.80           O  
ATOM   3919  N   ASN A 511      14.150  -3.516   4.069  1.00 15.56           N  
ATOM   3920  CA  ASN A 511      14.399  -3.037   5.426  1.00 14.82           C  
ATOM   3921  C   ASN A 511      15.245  -3.975   6.290  1.00 14.53           C  
ATOM   3922  O   ASN A 511      15.330  -3.794   7.512  1.00 13.75           O  
ATOM   3923  CB  ASN A 511      13.072  -2.698   6.124  1.00 14.36           C  
ATOM   3924  CG  ASN A 511      12.260  -3.934   6.483  1.00 14.93           C  
ATOM   3925  OD1 ASN A 511      12.342  -4.970   5.818  1.00 15.08           O  
ATOM   3926  ND2 ASN A 511      11.473  -3.827   7.549  1.00 13.89           N  
ATOM   3927  N   GLN A 512      15.882  -4.968   5.666  1.00 14.27           N  
ATOM   3928  CA  GLN A 512      16.723  -5.899   6.421  1.00 14.43           C  
ATOM   3929  C   GLN A 512      17.845  -5.186   7.177  1.00 14.14           C  
ATOM   3930  O   GLN A 512      18.223  -5.613   8.270  1.00 13.77           O  
ATOM   3931  CB  GLN A 512      17.297  -7.010   5.530  1.00 14.92           C  
ATOM   3932  CG  GLN A 512      18.045  -8.117   6.303  1.00 16.13           C  
ATOM   3933  CD  GLN A 512      17.147  -8.946   7.225  1.00 17.74           C  
ATOM   3934  OE1 GLN A 512      16.072  -9.406   6.830  1.00 18.25           O  
ATOM   3935  NE2 GLN A 512      17.602  -9.152   8.459  1.00 17.84           N  
ATOM   3936  N   ASP A 513      18.365  -4.100   6.604  1.00 13.97           N  
ATOM   3937  CA  ASP A 513      19.422  -3.326   7.264  1.00 14.18           C  
ATOM   3938  C   ASP A 513      18.953  -2.712   8.591  1.00 13.94           C  
ATOM   3939  O   ASP A 513      19.728  -2.605   9.546  1.00 13.56           O  
ATOM   3940  CB  ASP A 513      20.043  -2.270   6.322  1.00 14.71           C  
ATOM   3941  CG  ASP A 513      19.044  -1.216   5.840  1.00 15.84           C  
ATOM   3942  OD1 ASP A 513      17.822  -1.471   5.826  1.00 17.13           O  
ATOM   3943  OD2 ASP A 513      19.497  -0.114   5.451  1.00 18.88           O  
ATOM   3944  N   CYS A 514      17.679  -2.337   8.650  1.00 13.38           N  
ATOM   3945  CA  CYS A 514      17.110  -1.787   9.879  1.00 12.74           C  
ATOM   3946  C   CYS A 514      16.971  -2.888  10.926  1.00 12.12           C  
ATOM   3947  O   CYS A 514      17.292  -2.694  12.102  1.00 11.76           O  
ATOM   3948  CB  CYS A 514      15.769  -1.120   9.597  1.00 13.02           C  
ATOM   3949  SG  CYS A 514      15.177  -0.129  10.981  1.00 14.26           S  
ATOM   3950  N   ILE A 515      16.512  -4.054  10.482  1.00 11.34           N  
ATOM   3951  CA  ILE A 515      16.437  -5.230  11.343  1.00 11.33           C  
ATOM   3952  C   ILE A 515      17.822  -5.593  11.898  1.00 11.53           C  
ATOM   3953  O   ILE A 515      17.974  -5.763  13.104  1.00 11.60           O  
ATOM   3954  CB  ILE A 515      15.785  -6.414  10.603  1.00 11.46           C  
ATOM   3955  CG1 ILE A 515      14.318  -6.077  10.309  1.00 11.05           C  
ATOM   3956  CG2 ILE A 515      15.897  -7.712  11.417  1.00 11.41           C  
ATOM   3957  CD1 ILE A 515      13.675  -6.972   9.285  1.00 13.29           C  
ATOM   3958  N   ASP A 516      18.828  -5.660  11.024  1.00 11.94           N  
ATOM   3959  CA  ASP A 516      20.200  -5.974  11.456  1.00 12.52           C  
ATOM   3960  C   ASP A 516      20.759  -4.963  12.460  1.00 11.88           C  
ATOM   3961  O   ASP A 516      21.415  -5.348  13.423  1.00 12.14           O  
ATOM   3962  CB  ASP A 516      21.144  -6.107  10.259  1.00 13.07           C  
ATOM   3963  CG  ASP A 516      20.792  -7.279   9.354  1.00 14.73           C  
ATOM   3964  OD1 ASP A 516      19.994  -8.153   9.753  1.00 17.41           O  
ATOM   3965  OD2 ASP A 516      21.331  -7.324   8.231  1.00 18.40           O  
ATOM   3966  N   LEU A 517      20.490  -3.676  12.242  1.00 11.60           N  
ATOM   3967  CA  LEU A 517      20.883  -2.643  13.208  1.00 11.33           C  
ATOM   3968  C   LEU A 517      20.377  -2.991  14.609  1.00 10.86           C  
ATOM   3969  O   LEU A 517      21.087  -2.819  15.600  1.00 10.19           O  
ATOM   3970  CB  LEU A 517      20.351  -1.266  12.785  1.00 11.25           C  
ATOM   3971  CG  LEU A 517      20.436  -0.123  13.808  1.00 12.11           C  
ATOM   3972  CD1 LEU A 517      21.878   0.226  14.144  1.00 13.05           C  
ATOM   3973  CD2 LEU A 517      19.707   1.115  13.305  1.00 11.82           C  
ATOM   3974  N   ILE A 518      19.149  -3.493  14.674  1.00 10.53           N  
ATOM   3975  CA  ILE A 518      18.510  -3.787  15.949  1.00 11.08           C  
ATOM   3976  C   ILE A 518      18.965  -5.118  16.559  1.00 11.38           C  
ATOM   3977  O   ILE A 518      19.291  -5.177  17.755  1.00 11.46           O  
ATOM   3978  CB  ILE A 518      16.959  -3.717  15.826  1.00 11.11           C  
ATOM   3979  CG1 ILE A 518      16.531  -2.296  15.408  1.00 10.98           C  
ATOM   3980  CG2 ILE A 518      16.291  -4.147  17.137  1.00 11.41           C  
ATOM   3981  CD1 ILE A 518      15.096  -2.172  14.883  1.00 11.37           C  
ATOM   3982  N   GLU A 519      19.006  -6.173  15.746  1.00 11.78           N  
ATOM   3983  CA  GLU A 519      19.107  -7.542  16.280  1.00 12.88           C  
ATOM   3984  C   GLU A 519      20.408  -8.299  15.979  1.00 12.87           C  
ATOM   3985  O   GLU A 519      20.540  -9.463  16.366  1.00 12.98           O  
ATOM   3986  CB  GLU A 519      17.905  -8.390  15.827  1.00 12.89           C  
ATOM   3987  CG  GLU A 519      17.938  -8.724  14.345  1.00 13.99           C  
ATOM   3988  CD  GLU A 519      16.922  -9.773  13.918  1.00 13.91           C  
ATOM   3989  OE1 GLU A 519      17.254 -10.531  12.985  1.00 16.56           O  
ATOM   3990  OE2 GLU A 519      15.806  -9.834  14.479  1.00 13.79           O  
ATOM   3991  N   ALA A 520      21.352  -7.669  15.283  1.00 13.02           N  
ATOM   3992  CA  ALA A 520      22.608  -8.354  14.928  1.00 13.37           C  
ATOM   3993  C   ALA A 520      23.353  -8.846  16.166  1.00 13.62           C  
ATOM   3994  O   ALA A 520      23.351  -8.189  17.207  1.00 13.36           O  
ATOM   3995  CB  ALA A 520      23.502  -7.460  14.098  1.00 13.36           C  
ATOM   3996  N   ARG A 521      23.984 -10.012  16.047  1.00 13.98           N  
ATOM   3997  CA  ARG A 521      24.741 -10.574  17.162  1.00 14.61           C  
ATOM   3998  C   ARG A 521      25.900  -9.668  17.552  1.00 14.53           C  
ATOM   3999  O   ARG A 521      26.631  -9.176  16.689  1.00 15.03           O  
ATOM   4000  CB  ARG A 521      25.242 -11.984  16.835  1.00 14.48           C  
ATOM   4001  CG  ARG A 521      24.128 -13.011  16.705  1.00 15.85           C  
ATOM   4002  CD  ARG A 521      24.685 -14.417  16.580  1.00 16.98           C  
ATOM   4003  NE  ARG A 521      23.629 -15.423  16.514  1.00 19.94           N  
ATOM   4004  CZ  ARG A 521      23.183 -15.979  15.391  1.00 20.61           C  
ATOM   4005  NH1 ARG A 521      23.696 -15.634  14.214  1.00 20.96           N  
ATOM   4006  NH2 ARG A 521      22.219 -16.885  15.444  1.00 22.41           N  
ATOM   4007  N   LEU A 522      26.032  -9.446  18.860  1.00 14.82           N  
ATOM   4008  CA  LEU A 522      27.091  -8.635  19.484  1.00 14.89           C  
ATOM   4009  C   LEU A 522      27.011  -7.137  19.241  1.00 14.84           C  
ATOM   4010  O   LEU A 522      27.127  -6.351  20.181  1.00 15.14           O  
ATOM   4011  CB  LEU A 522      28.495  -9.140  19.109  1.00 15.21           C  
ATOM   4012  CG  LEU A 522      28.897 -10.540  19.563  1.00 16.06           C  
ATOM   4013  CD1 LEU A 522      30.352 -10.775  19.216  1.00 17.73           C  
ATOM   4014  CD2 LEU A 522      28.653 -10.756  21.058  1.00 16.74           C  
ATOM   4015  N   VAL A 523      26.827  -6.750  17.981  1.00 14.51           N  
ATOM   4016  CA  VAL A 523      26.903  -5.351  17.571  1.00 14.30           C  
ATOM   4017  C   VAL A 523      25.522  -4.690  17.450  1.00 14.03           C  
ATOM   4018  O   VAL A 523      25.422  -3.468  17.406  1.00 14.43           O  
ATOM   4019  CB  VAL A 523      27.693  -5.190  16.236  1.00 14.37           C  
ATOM   4020  CG1 VAL A 523      29.132  -5.698  16.391  1.00 15.10           C  
ATOM   4021  CG2 VAL A 523      26.997  -5.929  15.100  1.00 14.50           C  
ATOM   4022  N   GLY A 524      24.468  -5.500  17.379  1.00 13.49           N  
ATOM   4023  CA  GLY A 524      23.104  -4.977  17.287  1.00 12.96           C  
ATOM   4024  C   GLY A 524      22.690  -4.282  18.572  1.00 12.55           C  
ATOM   4025  O   GLY A 524      23.212  -4.583  19.647  1.00 12.33           O  
ATOM   4026  N   ILE A 525      21.737  -3.360  18.460  1.00 12.40           N  
ATOM   4027  CA  ILE A 525      21.294  -2.552  19.600  1.00 12.46           C  
ATOM   4028  C   ILE A 525      20.854  -3.403  20.799  1.00 12.19           C  
ATOM   4029  O   ILE A 525      21.224  -3.110  21.941  1.00 11.91           O  
ATOM   4030  CB  ILE A 525      20.183  -1.545  19.190  1.00 12.28           C  
ATOM   4031  CG1 ILE A 525      20.727  -0.534  18.165  1.00 12.06           C  
ATOM   4032  CG2 ILE A 525      19.610  -0.821  20.415  1.00 12.86           C  
ATOM   4033  CD1 ILE A 525      19.665   0.394  17.563  1.00 12.75           C  
ATOM   4034  N   LEU A 526      20.080  -4.456  20.542  1.00 12.15           N  
ATOM   4035  CA  LEU A 526      19.608  -5.335  21.623  1.00 12.28           C  
ATOM   4036  C   LEU A 526      20.765  -5.995  22.390  1.00 12.42           C  
ATOM   4037  O   LEU A 526      20.734  -6.077  23.622  1.00 12.33           O  
ATOM   4038  CB  LEU A 526      18.642  -6.396  21.087  1.00 12.34           C  
ATOM   4039  CG  LEU A 526      17.331  -5.883  20.464  1.00 12.91           C  
ATOM   4040  CD1 LEU A 526      16.519  -7.061  19.964  1.00 14.13           C  
ATOM   4041  CD2 LEU A 526      16.524  -5.044  21.453  1.00 14.38           C  
ATOM   4042  N   ASP A 527      21.786  -6.441  21.662  1.00 12.56           N  
ATOM   4043  CA  ASP A 527      22.958  -7.066  22.286  1.00 13.02           C  
ATOM   4044  C   ASP A 527      23.856  -6.056  23.015  1.00 12.89           C  
ATOM   4045  O   ASP A 527      24.460  -6.385  24.045  1.00 13.00           O  
ATOM   4046  CB  ASP A 527      23.762  -7.881  21.260  1.00 13.54           C  
ATOM   4047  CG  ASP A 527      23.234  -9.321  21.092  1.00 14.74           C  
ATOM   4048  OD1 ASP A 527      23.945 -10.147  20.477  1.00 16.60           O  
ATOM   4049  OD2 ASP A 527      22.129  -9.645  21.582  1.00 17.23           O  
ATOM   4050  N   ILE A 528      23.937  -4.835  22.492  1.00 12.73           N  
ATOM   4051  CA  ILE A 528      24.672  -3.752  23.168  1.00 13.08           C  
ATOM   4052  C   ILE A 528      23.969  -3.392  24.481  1.00 13.39           C  
ATOM   4053  O   ILE A 528      24.620  -3.148  25.510  1.00 13.63           O  
ATOM   4054  CB  ILE A 528      24.844  -2.504  22.257  1.00 12.88           C  
ATOM   4055  CG1 ILE A 528      25.725  -2.837  21.044  1.00 12.93           C  
ATOM   4056  CG2 ILE A 528      25.466  -1.339  23.028  1.00 13.50           C  
ATOM   4057  CD1 ILE A 528      25.788  -1.721  20.005  1.00 13.02           C  
ATOM   4058  N   LEU A 529      22.638  -3.379  24.445  1.00 13.23           N  
ATOM   4059  CA  LEU A 529      21.847  -3.151  25.650  1.00 13.57           C  
ATOM   4060  C   LEU A 529      22.062  -4.252  26.697  1.00 13.93           C  
ATOM   4061  O   LEU A 529      22.303  -3.955  27.875  1.00 14.41           O  
ATOM   4062  CB  LEU A 529      20.365  -3.003  25.299  1.00 13.24           C  
ATOM   4063  CG  LEU A 529      19.428  -2.511  26.407  1.00 12.86           C  
ATOM   4064  CD1 LEU A 529      19.887  -1.184  27.022  1.00 13.61           C  
ATOM   4065  CD2 LEU A 529      18.024  -2.386  25.833  1.00 13.19           C  
ATOM   4066  N   ASP A 530      21.985  -5.508  26.260  1.00 14.21           N  
ATOM   4067  CA  ASP A 530      22.292  -6.665  27.111  1.00 14.92           C  
ATOM   4068  C   ASP A 530      23.667  -6.523  27.758  1.00 15.52           C  
ATOM   4069  O   ASP A 530      23.815  -6.761  28.957  1.00 15.56           O  
ATOM   4070  CB  ASP A 530      22.260  -7.962  26.298  1.00 14.80           C  
ATOM   4071  CG  ASP A 530      20.849  -8.476  26.052  1.00 14.93           C  
ATOM   4072  OD1 ASP A 530      19.866  -7.773  26.373  1.00 14.11           O  
ATOM   4073  OD2 ASP A 530      20.728  -9.603  25.529  1.00 15.30           O  
ATOM   4074  N   GLU A 531      24.655  -6.124  26.956  1.00 16.10           N  
ATOM   4075  CA  GLU A 531      26.024  -5.896  27.429  1.00 17.31           C  
ATOM   4076  C   GLU A 531      26.044  -4.864  28.564  1.00 16.87           C  
ATOM   4077  O   GLU A 531      26.738  -5.048  29.570  1.00 16.62           O  
ATOM   4078  CB  GLU A 531      26.926  -5.467  26.260  1.00 17.30           C  
ATOM   4079  CG  GLU A 531      28.347  -5.041  26.648  1.00 18.98           C  
ATOM   4080  CD  GLU A 531      29.244  -4.726  25.448  1.00 19.83           C  
ATOM   4081  OE1 GLU A 531      30.443  -4.443  25.681  1.00 24.25           O  
ATOM   4082  OE2 GLU A 531      28.773  -4.758  24.283  1.00 23.51           O  
ATOM   4083  N   GLU A 532      25.266  -3.796  28.405  1.00 16.54           N  
ATOM   4084  CA  GLU A 532      25.158  -2.767  29.437  1.00 16.51           C  
ATOM   4085  C   GLU A 532      24.587  -3.302  30.752  1.00 16.71           C  
ATOM   4086  O   GLU A 532      25.110  -2.992  31.826  1.00 16.84           O  
ATOM   4087  CB  GLU A 532      24.324  -1.583  28.948  1.00 16.38           C  
ATOM   4088  CG  GLU A 532      24.505  -0.315  29.794  1.00 16.36           C  
ATOM   4089  CD  GLU A 532      25.907   0.265  29.705  1.00 17.27           C  
ATOM   4090  OE1 GLU A 532      26.397   0.781  30.734  1.00 17.93           O  
ATOM   4091  OE2 GLU A 532      26.517   0.209  28.611  1.00 16.30           O  
ATOM   4092  N   ASN A 533      23.527  -4.105  30.674  1.00 16.61           N  
ATOM   4093  CA  ASN A 533      22.928  -4.695  31.878  1.00 17.32           C  
ATOM   4094  C   ASN A 533      23.942  -5.509  32.678  1.00 17.78           C  
ATOM   4095  O   ASN A 533      23.819  -5.646  33.896  1.00 17.90           O  
ATOM   4096  CB  ASN A 533      21.742  -5.585  31.523  1.00 17.25           C  
ATOM   4097  CG  ASN A 533      20.496  -4.791  31.155  1.00 17.17           C  
ATOM   4098  OD1 ASN A 533      20.214  -4.580  29.978  1.00 17.25           O  
ATOM   4099  ND2 ASN A 533      19.743  -4.352  32.164  1.00 15.97           N  
ATOM   4100  N   ARG A 534      24.951  -6.020  31.977  1.00 18.31           N  
ATOM   4101  CA  ARG A 534      25.939  -6.932  32.559  1.00 19.15           C  
ATOM   4102  C   ARG A 534      27.217  -6.249  33.054  1.00 19.49           C  
ATOM   4103  O   ARG A 534      28.056  -6.888  33.695  1.00 19.74           O  
ATOM   4104  CB  ARG A 534      26.270  -8.047  31.562  1.00 19.18           C  
ATOM   4105  CG  ARG A 534      25.134  -9.045  31.400  1.00 20.39           C  
ATOM   4106  CD  ARG A 534      25.335  -9.952  30.209  1.00 22.85           C  
ATOM   4107  NE  ARG A 534      24.250 -10.924  30.114  1.00 25.27           N  
ATOM   4108  CZ  ARG A 534      23.780 -11.428  28.976  1.00 26.07           C  
ATOM   4109  NH1 ARG A 534      22.787 -12.306  29.010  1.00 27.52           N  
ATOM   4110  NH2 ARG A 534      24.291 -11.054  27.810  1.00 26.84           N  
ATOM   4111  N   LEU A 535      27.358  -4.958  32.764  1.00 19.86           N  
ATOM   4112  CA  LEU A 535      28.515  -4.182  33.212  1.00 20.43           C  
ATOM   4113  C   LEU A 535      28.448  -3.891  34.717  1.00 20.79           C  
ATOM   4114  O   LEU A 535      27.362  -3.917  35.306  1.00 20.82           O  
ATOM   4115  CB  LEU A 535      28.648  -2.885  32.399  1.00 20.35           C  
ATOM   4116  CG  LEU A 535      29.133  -3.015  30.949  1.00 20.41           C  
ATOM   4117  CD1 LEU A 535      29.056  -1.678  30.230  1.00 20.88           C  
ATOM   4118  CD2 LEU A 535      30.557  -3.586  30.865  1.00 21.63           C  
ATOM   4119  N   PRO A 536      29.613  -3.635  35.354  1.00 21.38           N  
ATOM   4120  CA  PRO A 536      29.635  -3.341  36.790  1.00 21.50           C  
ATOM   4121  C   PRO A 536      28.729  -2.170  37.178  1.00 21.54           C  
ATOM   4122  O   PRO A 536      28.012  -2.257  38.180  1.00 21.71           O  
ATOM   4123  CB  PRO A 536      31.105  -2.988  37.056  1.00 21.51           C  
ATOM   4124  CG  PRO A 536      31.857  -3.665  35.980  1.00 21.94           C  
ATOM   4125  CD  PRO A 536      30.969  -3.621  34.774  1.00 21.38           C  
ATOM   4126  N   GLN A 537      28.754  -1.100  36.382  1.00 21.40           N  
ATOM   4127  CA  GLN A 537      27.946   0.093  36.644  1.00 21.30           C  
ATOM   4128  C   GLN A 537      27.088   0.473  35.429  1.00 20.41           C  
ATOM   4129  O   GLN A 537      27.422   1.424  34.717  1.00 20.46           O  
ATOM   4130  CB  GLN A 537      28.843   1.274  37.049  1.00 21.69           C  
ATOM   4131  CG  GLN A 537      29.859   0.965  38.159  1.00 24.01           C  
ATOM   4132  CD  GLN A 537      29.216   0.685  39.511  1.00 26.83           C  
ATOM   4133  OE1 GLN A 537      29.758  -0.077  40.318  1.00 28.88           O  
ATOM   4134  NE2 GLN A 537      28.063   1.300  39.768  1.00 28.11           N  
ATOM   4135  N   PRO A 538      25.979  -0.262  35.191  1.00 19.69           N  
ATOM   4136  CA  PRO A 538      25.171  -0.031  33.981  1.00 19.12           C  
ATOM   4137  C   PRO A 538      24.665   1.408  33.866  1.00 18.72           C  
ATOM   4138  O   PRO A 538      24.260   2.009  34.867  1.00 18.47           O  
ATOM   4139  CB  PRO A 538      24.003  -1.004  34.147  1.00 19.15           C  
ATOM   4140  CG  PRO A 538      24.537  -2.082  35.031  1.00 19.49           C  
ATOM   4141  CD  PRO A 538      25.404  -1.340  36.016  1.00 19.45           C  
ATOM   4142  N   SER A 539      24.697   1.938  32.643  1.00 18.06           N  
ATOM   4143  CA  SER A 539      24.372   3.334  32.368  1.00 17.58           C  
ATOM   4144  C   SER A 539      23.685   3.486  31.010  1.00 17.34           C  
ATOM   4145  O   SER A 539      24.206   3.014  29.998  1.00 16.84           O  
ATOM   4146  CB  SER A 539      25.654   4.171  32.394  1.00 17.61           C  
ATOM   4147  OG  SER A 539      25.523   5.360  31.645  1.00 17.04           O  
ATOM   4148  N   ASP A 540      22.531   4.158  30.996  1.00 17.07           N  
ATOM   4149  CA  ASP A 540      21.804   4.454  29.753  1.00 17.04           C  
ATOM   4150  C   ASP A 540      22.677   5.248  28.774  1.00 16.98           C  
ATOM   4151  O   ASP A 540      22.669   4.988  27.571  1.00 16.37           O  
ATOM   4152  CB  ASP A 540      20.512   5.242  30.036  1.00 17.21           C  
ATOM   4153  CG  ASP A 540      19.486   4.447  30.842  1.00 18.75           C  
ATOM   4154  OD1 ASP A 540      19.367   3.223  30.637  1.00 19.33           O  
ATOM   4155  OD2 ASP A 540      18.778   5.065  31.669  1.00 18.99           O  
ATOM   4156  N   GLN A 541      23.427   6.214  29.301  1.00 16.75           N  
ATOM   4157  CA  GLN A 541      24.318   7.037  28.485  1.00 17.06           C  
ATOM   4158  C   GLN A 541      25.446   6.217  27.847  1.00 16.61           C  
ATOM   4159  O   GLN A 541      25.749   6.390  26.668  1.00 16.06           O  
ATOM   4160  CB  GLN A 541      24.890   8.205  29.303  1.00 17.33           C  
ATOM   4161  CG  GLN A 541      23.871   9.306  29.638  1.00 19.73           C  
ATOM   4162  CD  GLN A 541      23.048   9.050  30.906  1.00 22.04           C  
ATOM   4163  OE1 GLN A 541      22.177   9.857  31.259  1.00 24.94           O  
ATOM   4164  NE2 GLN A 541      23.321   7.944  31.599  1.00 22.27           N  
ATOM   4165  N   HIS A 542      26.058   5.327  28.630  1.00 16.52           N  
ATOM   4166  CA  HIS A 542      27.112   4.451  28.122  1.00 16.46           C  
ATOM   4167  C   HIS A 542      26.578   3.556  27.001  1.00 16.06           C  
ATOM   4168  O   HIS A 542      27.211   3.428  25.946  1.00 16.28           O  
ATOM   4169  CB  HIS A 542      27.720   3.610  29.249  1.00 17.09           C  
ATOM   4170  CG  HIS A 542      28.939   2.841  28.839  1.00 18.33           C  
ATOM   4171  ND1 HIS A 542      28.888   1.523  28.442  1.00 19.35           N  
ATOM   4172  CD2 HIS A 542      30.241   3.207  28.759  1.00 19.63           C  
ATOM   4173  CE1 HIS A 542      30.106   1.107  28.141  1.00 20.30           C  
ATOM   4174  NE2 HIS A 542      30.945   2.110  28.326  1.00 20.25           N  
ATOM   4175  N   PHE A 543      25.408   2.964  27.232  1.00 15.20           N  
ATOM   4176  CA  PHE A 543      24.717   2.162  26.217  1.00 14.68           C  
ATOM   4177  C   PHE A 543      24.497   2.976  24.945  1.00 14.22           C  
ATOM   4178  O   PHE A 543      24.824   2.522  23.846  1.00 13.89           O  
ATOM   4179  CB  PHE A 543      23.379   1.631  26.760  1.00 14.19           C  
ATOM   4180  CG  PHE A 543      22.351   1.348  25.691  1.00 13.81           C  
ATOM   4181  CD1 PHE A 543      21.239   2.179  25.546  1.00 13.60           C  
ATOM   4182  CD2 PHE A 543      22.500   0.264  24.826  1.00 13.62           C  
ATOM   4183  CE1 PHE A 543      20.286   1.928  24.556  1.00 13.10           C  
ATOM   4184  CE2 PHE A 543      21.552   0.006  23.829  1.00 13.93           C  
ATOM   4185  CZ  PHE A 543      20.443   0.841  23.697  1.00 13.26           C  
ATOM   4186  N   THR A 544      23.953   4.183  25.104  1.00 13.97           N  
ATOM   4187  CA  THR A 544      23.605   5.023  23.960  1.00 14.03           C  
ATOM   4188  C   THR A 544      24.848   5.434  23.171  1.00 14.45           C  
ATOM   4189  O   THR A 544      24.845   5.408  21.943  1.00 14.11           O  
ATOM   4190  CB  THR A 544      22.774   6.247  24.389  1.00 13.97           C  
ATOM   4191  OG1 THR A 544      21.693   5.804  25.219  1.00 13.79           O  
ATOM   4192  CG2 THR A 544      22.209   6.974  23.172  1.00 13.87           C  
ATOM   4193  N   SER A 545      25.911   5.788  23.887  1.00 14.90           N  
ATOM   4194  CA  SER A 545      27.185   6.124  23.260  1.00 15.66           C  
ATOM   4195  C   SER A 545      27.731   4.940  22.465  1.00 15.48           C  
ATOM   4196  O   SER A 545      28.206   5.113  21.342  1.00 15.92           O  
ATOM   4197  CB  SER A 545      28.184   6.600  24.317  1.00 15.89           C  
ATOM   4198  OG  SER A 545      27.755   7.838  24.862  1.00 17.80           O  
ATOM   4199  N   ALA A 546      27.626   3.743  23.039  1.00 15.67           N  
ATOM   4200  CA  ALA A 546      28.063   2.511  22.382  1.00 15.85           C  
ATOM   4201  C   ALA A 546      27.304   2.265  21.077  1.00 15.95           C  
ATOM   4202  O   ALA A 546      27.910   1.907  20.064  1.00 15.64           O  
ATOM   4203  CB  ALA A 546      27.929   1.323  23.322  1.00 15.91           C  
ATOM   4204  N   VAL A 547      25.989   2.485  21.100  1.00 15.82           N  
ATOM   4205  CA  VAL A 547      25.159   2.342  19.903  1.00 16.04           C  
ATOM   4206  C   VAL A 547      25.658   3.254  18.776  1.00 16.27           C  
ATOM   4207  O   VAL A 547      25.852   2.807  17.646  1.00 16.49           O  
ATOM   4208  CB  VAL A 547      23.656   2.604  20.212  1.00 15.89           C  
ATOM   4209  CG1 VAL A 547      22.843   2.749  18.927  1.00 15.57           C  
ATOM   4210  CG2 VAL A 547      23.088   1.488  21.076  1.00 16.06           C  
ATOM   4211  N   HIS A 548      25.881   4.528  19.080  1.00 16.52           N  
ATOM   4212  CA  HIS A 548      26.377   5.452  18.067  1.00 16.84           C  
ATOM   4213  C   HIS A 548      27.794   5.093  17.600  1.00 17.33           C  
ATOM   4214  O   HIS A 548      28.067   5.091  16.397  1.00 17.16           O  
ATOM   4215  CB  HIS A 548      26.288   6.899  18.556  1.00 16.60           C  
ATOM   4216  CG  HIS A 548      24.883   7.412  18.648  1.00 15.80           C  
ATOM   4217  ND1 HIS A 548      24.320   7.844  19.830  1.00 16.59           N  
ATOM   4218  CD2 HIS A 548      23.923   7.542  17.704  1.00 14.67           C  
ATOM   4219  CE1 HIS A 548      23.075   8.226  19.607  1.00 14.29           C  
ATOM   4220  NE2 HIS A 548      22.810   8.058  18.324  1.00 16.20           N  
ATOM   4221  N   GLN A 549      28.672   4.770  18.549  1.00 18.28           N  
ATOM   4222  CA  GLN A 549      30.070   4.426  18.253  1.00 19.43           C  
ATOM   4223  C   GLN A 549      30.185   3.175  17.380  1.00 19.76           C  
ATOM   4224  O   GLN A 549      30.935   3.164  16.396  1.00 19.72           O  
ATOM   4225  CB  GLN A 549      30.865   4.234  19.552  1.00 19.67           C  
ATOM   4226  CG  GLN A 549      32.303   3.735  19.360  1.00 22.26           C  
ATOM   4227  CD  GLN A 549      32.828   2.988  20.573  1.00 25.79           C  
ATOM   4228  OE1 GLN A 549      32.235   2.939  21.704  1.00 30.69           O  
ATOM   4229  NE2 GLN A 549      33.756   2.063  20.344  1.00 28.30           N  
ATOM   4230  N   LYS A 550      29.441   2.131  17.742  1.00 19.85           N  
ATOM   4231  CA  LYS A 550      29.507   0.853  17.028  1.00 20.53           C  
ATOM   4232  C   LYS A 550      28.786   0.883  15.677  1.00 20.40           C  
ATOM   4233  O   LYS A 550      28.977  -0.013  14.847  1.00 21.19           O  
ATOM   4234  CB  LYS A 550      28.998  -0.296  17.910  1.00 20.62           C  
ATOM   4235  CG  LYS A 550      30.027  -0.779  18.934  1.00 22.44           C  
ATOM   4236  CD  LYS A 550      29.386  -1.560  20.076  1.00 25.25           C  
ATOM   4237  CE  LYS A 550      30.407  -2.388  20.860  1.00 27.24           C  
ATOM   4238  NZ  LYS A 550      31.588  -1.605  21.331  1.00 28.92           N  
ATOM   4239  N   HIS A 551      27.977   1.916  15.450  1.00 20.19           N  
ATOM   4240  CA  HIS A 551      27.204   2.027  14.208  1.00 20.13           C  
ATOM   4241  C   HIS A 551      27.469   3.314  13.444  1.00 20.54           C  
ATOM   4242  O   HIS A 551      26.565   3.883  12.825  1.00 19.77           O  
ATOM   4243  CB  HIS A 551      25.711   1.861  14.487  1.00 19.68           C  
ATOM   4244  CG  HIS A 551      25.354   0.509  15.011  1.00 18.85           C  
ATOM   4245  ND1 HIS A 551      25.251  -0.598  14.196  1.00 18.88           N  
ATOM   4246  CD2 HIS A 551      25.103   0.077  16.269  1.00 18.67           C  
ATOM   4247  CE1 HIS A 551      24.938  -1.651  14.928  1.00 17.59           C  
ATOM   4248  NE2 HIS A 551      24.838  -1.268  16.188  1.00 18.93           N  
ATOM   4249  N   LYS A 552      28.725   3.756  13.486  1.00 21.42           N  
ATOM   4250  CA  LYS A 552      29.169   4.912  12.722  1.00 22.26           C  
ATOM   4251  C   LYS A 552      28.758   4.790  11.260  1.00 22.00           C  
ATOM   4252  O   LYS A 552      29.048   3.782  10.605  1.00 22.31           O  
ATOM   4253  CB  LYS A 552      30.690   5.060  12.828  1.00 22.69           C  
ATOM   4254  CG  LYS A 552      31.164   5.973  13.949  1.00 25.07           C  
ATOM   4255  CD  LYS A 552      31.486   7.378  13.426  1.00 27.74           C  
ATOM   4256  CE  LYS A 552      32.805   7.401  12.653  1.00 29.22           C  
ATOM   4257  NZ  LYS A 552      32.873   8.529  11.680  1.00 30.48           N  
ATOM   4258  N   ASP A 553      28.055   5.815  10.779  1.00 21.61           N  
ATOM   4259  CA  ASP A 553      27.640   5.950   9.377  1.00 21.28           C  
ATOM   4260  C   ASP A 553      26.449   5.088   8.942  1.00 20.38           C  
ATOM   4261  O   ASP A 553      25.987   5.218   7.811  1.00 20.38           O  
ATOM   4262  CB  ASP A 553      28.826   5.752   8.414  1.00 22.01           C  
ATOM   4263  CG  ASP A 553      29.906   6.807   8.583  1.00 23.54           C  
ATOM   4264  OD1 ASP A 553      29.577   7.973   8.894  1.00 25.83           O  
ATOM   4265  OD2 ASP A 553      31.092   6.463   8.389  1.00 26.46           O  
ATOM   4266  N   HIS A 554      25.946   4.223   9.824  1.00 19.08           N  
ATOM   4267  CA  HIS A 554      24.830   3.346   9.456  1.00 17.84           C  
ATOM   4268  C   HIS A 554      23.619   4.165   9.009  1.00 17.31           C  
ATOM   4269  O   HIS A 554      23.180   5.068   9.721  1.00 16.78           O  
ATOM   4270  CB  HIS A 554      24.444   2.417  10.612  1.00 17.51           C  
ATOM   4271  CG  HIS A 554      23.536   1.300  10.203  1.00 16.47           C  
ATOM   4272  ND1 HIS A 554      23.905  -0.026  10.277  1.00 15.87           N  
ATOM   4273  CD2 HIS A 554      22.279   1.314   9.699  1.00 14.59           C  
ATOM   4274  CE1 HIS A 554      22.912  -0.780   9.841  1.00 14.31           C  
ATOM   4275  NE2 HIS A 554      21.914   0.008   9.483  1.00 16.28           N  
ATOM   4276  N   PHE A 555      23.083   3.831   7.837  1.00 17.07           N  
ATOM   4277  CA  PHE A 555      21.975   4.572   7.221  1.00 17.20           C  
ATOM   4278  C   PHE A 555      20.702   4.636   8.075  1.00 16.63           C  
ATOM   4279  O   PHE A 555      19.931   5.594   7.976  1.00 16.63           O  
ATOM   4280  CB  PHE A 555      21.654   3.989   5.838  1.00 18.24           C  
ATOM   4281  CG  PHE A 555      20.408   4.551   5.208  1.00 19.63           C  
ATOM   4282  CD1 PHE A 555      20.387   5.852   4.708  1.00 22.13           C  
ATOM   4283  CD2 PHE A 555      19.260   3.768   5.096  1.00 21.37           C  
ATOM   4284  CE1 PHE A 555      19.233   6.374   4.117  1.00 22.36           C  
ATOM   4285  CE2 PHE A 555      18.100   4.277   4.506  1.00 22.74           C  
ATOM   4286  CZ  PHE A 555      18.087   5.585   4.018  1.00 22.10           C  
ATOM   4287  N   ARG A 556      20.496   3.626   8.916  1.00 15.48           N  
ATOM   4288  CA  ARG A 556      19.252   3.507   9.679  1.00 14.97           C  
ATOM   4289  C   ARG A 556      19.313   4.135  11.069  1.00 14.74           C  
ATOM   4290  O   ARG A 556      18.323   4.100  11.806  1.00 14.38           O  
ATOM   4291  CB  ARG A 556      18.829   2.040   9.787  1.00 14.80           C  
ATOM   4292  CG  ARG A 556      18.508   1.383   8.459  1.00 15.34           C  
ATOM   4293  CD  ARG A 556      17.227   1.919   7.853  1.00 16.83           C  
ATOM   4294  NE  ARG A 556      16.861   1.145   6.672  1.00 17.66           N  
ATOM   4295  CZ  ARG A 556      15.672   1.170   6.077  1.00 19.10           C  
ATOM   4296  NH1 ARG A 556      14.689   1.937   6.540  1.00 19.25           N  
ATOM   4297  NH2 ARG A 556      15.467   0.418   5.004  1.00 19.58           N  
ATOM   4298  N   LEU A 557      20.462   4.716  11.416  1.00 14.50           N  
ATOM   4299  CA  LEU A 557      20.648   5.319  12.737  1.00 14.48           C  
ATOM   4300  C   LEU A 557      21.044   6.789  12.643  1.00 14.97           C  
ATOM   4301  O   LEU A 557      21.867   7.160  11.805  1.00 14.63           O  
ATOM   4302  CB  LEU A 557      21.706   4.543  13.528  1.00 14.33           C  
ATOM   4303  CG  LEU A 557      21.996   4.988  14.965  1.00 13.88           C  
ATOM   4304  CD1 LEU A 557      20.851   4.610  15.901  1.00 12.86           C  
ATOM   4305  CD2 LEU A 557      23.311   4.397  15.462  1.00 14.63           C  
ATOM   4306  N   SER A 558      20.462   7.617  13.509  1.00 15.18           N  
ATOM   4307  CA  SER A 558      20.842   9.027  13.596  1.00 15.82           C  
ATOM   4308  C   SER A 558      20.840   9.525  15.048  1.00 16.17           C  
ATOM   4309  O   SER A 558      20.407   8.822  15.962  1.00 15.31           O  
ATOM   4310  CB  SER A 558      19.924   9.888  12.716  1.00 16.07           C  
ATOM   4311  OG  SER A 558      20.473  11.181  12.512  1.00 17.67           O  
ATOM   4312  N   ILE A 559      21.352  10.736  15.252  1.00 16.98           N  
ATOM   4313  CA  ILE A 559      21.342  11.376  16.566  1.00 17.32           C  
ATOM   4314  C   ILE A 559      20.135  12.321  16.659  1.00 17.78           C  
ATOM   4315  O   ILE A 559      19.726  12.898  15.647  1.00 17.86           O  
ATOM   4316  CB  ILE A 559      22.678  12.137  16.848  1.00 17.64           C  
ATOM   4317  CG1 ILE A 559      23.018  13.088  15.700  1.00 17.37           C  
ATOM   4318  CG2 ILE A 559      23.821  11.148  17.097  1.00 17.85           C  
ATOM   4319  CD1 ILE A 559      24.224  13.989  15.959  1.00 17.29           C  
ATOM   4320  N   PRO A 560      19.548  12.469  17.863  1.00 17.96           N  
ATOM   4321  CA  PRO A 560      18.337  13.277  18.045  1.00 18.66           C  
ATOM   4322  C   PRO A 560      18.403  14.712  17.518  1.00 19.55           C  
ATOM   4323  O   PRO A 560      17.384  15.230  17.061  1.00 19.49           O  
ATOM   4324  CB  PRO A 560      18.151  13.289  19.563  1.00 18.50           C  
ATOM   4325  CG  PRO A 560      18.770  12.023  20.016  1.00 17.94           C  
ATOM   4326  CD  PRO A 560      19.974  11.848  19.131  1.00 17.86           C  
ATOM   4327  N   ARG A 561      19.569  15.352  17.583  1.00 20.61           N  
ATOM   4328  CA  ARG A 561      19.675  16.746  17.123  1.00 22.13           C  
ATOM   4329  C   ARG A 561      19.436  16.914  15.613  1.00 22.42           C  
ATOM   4330  O   ARG A 561      19.183  18.025  15.136  1.00 22.80           O  
ATOM   4331  CB  ARG A 561      20.984  17.412  17.579  1.00 22.18           C  
ATOM   4332  CG  ARG A 561      22.264  16.833  17.013  1.00 24.55           C  
ATOM   4333  CD  ARG A 561      23.402  17.846  17.145  1.00 28.60           C  
ATOM   4334  NE  ARG A 561      24.685  17.312  16.690  1.00 31.22           N  
ATOM   4335  CZ  ARG A 561      25.135  17.376  15.438  1.00 32.44           C  
ATOM   4336  NH1 ARG A 561      24.410  17.958  14.485  1.00 33.75           N  
ATOM   4337  NH2 ARG A 561      26.315  16.851  15.138  1.00 32.58           N  
ATOM   4338  N   LYS A 562      19.486  15.801  14.881  1.00 22.81           N  
ATOM   4339  CA  LYS A 562      19.197  15.784  13.444  1.00 23.23           C  
ATOM   4340  C   LYS A 562      17.724  15.486  13.138  1.00 23.17           C  
ATOM   4341  O   LYS A 562      17.348  15.316  11.974  1.00 23.09           O  
ATOM   4342  CB  LYS A 562      20.093  14.764  12.736  1.00 23.53           C  
ATOM   4343  CG  LYS A 562      21.550  14.825  13.162  1.00 24.99           C  
ATOM   4344  CD  LYS A 562      22.405  15.677  12.251  1.00 28.29           C  
ATOM   4345  CE  LYS A 562      23.249  14.795  11.340  1.00 29.40           C  
ATOM   4346  NZ  LYS A 562      24.614  15.355  11.147  1.00 30.44           N  
ATOM   4347  N   SER A 563      16.890  15.432  14.176  1.00 23.10           N  
ATOM   4348  CA  SER A 563      15.468  15.151  13.993  1.00 23.20           C  
ATOM   4349  C   SER A 563      14.749  16.214  13.174  1.00 23.62           C  
ATOM   4350  O   SER A 563      15.126  17.388  13.182  1.00 23.40           O  
ATOM   4351  CB  SER A 563      14.756  14.989  15.331  1.00 23.11           C  
ATOM   4352  OG  SER A 563      13.363  14.821  15.121  1.00 23.14           O  
ATOM   4353  N   LYS A 564      13.696  15.780  12.488  1.00 24.04           N  
ATOM   4354  CA  LYS A 564      12.836  16.668  11.718  1.00 24.56           C  
ATOM   4355  C   LYS A 564      11.929  17.490  12.635  1.00 24.53           C  
ATOM   4356  O   LYS A 564      11.442  18.555  12.248  1.00 24.65           O  
ATOM   4357  CB  LYS A 564      12.003  15.853  10.725  1.00 24.94           C  
ATOM   4358  CG  LYS A 564      12.847  15.020   9.765  1.00 26.42           C  
ATOM   4359  CD  LYS A 564      12.026  14.503   8.589  1.00 29.17           C  
ATOM   4360  CE  LYS A 564      12.931  13.918   7.515  1.00 29.85           C  
ATOM   4361  NZ  LYS A 564      12.235  13.806   6.198  1.00 31.23           N  
ATOM   4362  N   LEU A 565      11.721  16.995  13.855  1.00 24.44           N  
ATOM   4363  CA  LEU A 565      10.817  17.633  14.808  1.00 24.04           C  
ATOM   4364  C   LEU A 565      11.550  18.407  15.907  1.00 23.81           C  
ATOM   4365  O   LEU A 565      12.502  17.907  16.512  1.00 23.80           O  
ATOM   4366  CB  LEU A 565       9.859  16.602  15.419  1.00 24.23           C  
ATOM   4367  CG  LEU A 565       8.854  15.907  14.488  1.00 24.52           C  
ATOM   4368  CD1 LEU A 565       8.117  14.812  15.235  1.00 25.21           C  
ATOM   4369  CD2 LEU A 565       7.858  16.892  13.877  1.00 25.41           C  
ATOM   4370  N   ALA A 566      11.078  19.628  16.155  1.00 23.28           N  
ATOM   4371  CA  ALA A 566      11.643  20.519  17.164  1.00 22.85           C  
ATOM   4372  C   ALA A 566      11.786  19.862  18.538  1.00 22.42           C  
ATOM   4373  O   ALA A 566      12.806  20.023  19.209  1.00 22.22           O  
ATOM   4374  CB  ALA A 566      10.799  21.779  17.274  1.00 22.89           C  
ATOM   4375  N   ILE A 567      10.761  19.117  18.941  1.00 22.26           N  
ATOM   4376  CA  ILE A 567      10.698  18.514  20.278  1.00 22.39           C  
ATOM   4377  C   ILE A 567      11.914  17.630  20.613  1.00 22.21           C  
ATOM   4378  O   ILE A 567      12.240  17.430  21.784  1.00 21.83           O  
ATOM   4379  CB  ILE A 567       9.339  17.766  20.497  1.00 22.31           C  
ATOM   4380  CG1 ILE A 567       9.099  17.475  21.985  1.00 22.98           C  
ATOM   4381  CG2 ILE A 567       9.232  16.511  19.611  1.00 22.32           C  
ATOM   4382  CD1 ILE A 567       7.636  17.317  22.372  1.00 22.98           C  
ATOM   4383  N   HIS A 568      12.599  17.137  19.582  1.00 22.16           N  
ATOM   4384  CA  HIS A 568      13.725  16.219  19.773  1.00 22.42           C  
ATOM   4385  C   HIS A 568      15.112  16.878  19.745  1.00 22.70           C  
ATOM   4386  O   HIS A 568      16.102  16.249  20.123  1.00 22.87           O  
ATOM   4387  CB  HIS A 568      13.659  15.087  18.743  1.00 22.46           C  
ATOM   4388  CG  HIS A 568      12.405  14.274  18.817  1.00 21.69           C  
ATOM   4389  ND1 HIS A 568      11.654  13.962  17.705  1.00 22.47           N  
ATOM   4390  CD2 HIS A 568      11.770  13.708  19.870  1.00 21.65           C  
ATOM   4391  CE1 HIS A 568      10.608  13.244  18.071  1.00 20.63           C  
ATOM   4392  NE2 HIS A 568      10.657  13.073  19.379  1.00 22.47           N  
ATOM   4393  N   ARG A 569      15.163  18.143  19.327  1.00 23.09           N  
ATOM   4394  CA  ARG A 569      16.419  18.857  19.029  1.00 23.55           C  
ATOM   4395  C   ARG A 569      17.367  19.058  20.211  1.00 23.08           C  
ATOM   4396  O   ARG A 569      18.563  19.265  20.007  1.00 23.50           O  
ATOM   4397  CB  ARG A 569      16.123  20.224  18.400  1.00 24.02           C  
ATOM   4398  CG  ARG A 569      15.258  20.176  17.151  1.00 26.00           C  
ATOM   4399  CD  ARG A 569      16.061  20.245  15.863  1.00 29.60           C  
ATOM   4400  NE  ARG A 569      15.176  20.462  14.719  1.00 31.99           N  
ATOM   4401  CZ  ARG A 569      14.665  21.643  14.373  1.00 33.44           C  
ATOM   4402  NH1 ARG A 569      14.950  22.734  15.074  1.00 34.62           N  
ATOM   4403  NH2 ARG A 569      13.865  21.737  13.320  1.00 34.33           N  
ATOM   4404  N   ASN A 570      16.834  19.027  21.431  1.00 22.42           N  
ATOM   4405  CA  ASN A 570      17.655  19.246  22.627  1.00 22.02           C  
ATOM   4406  C   ASN A 570      18.051  17.988  23.398  1.00 21.39           C  
ATOM   4407  O   ASN A 570      18.686  18.069  24.451  1.00 21.52           O  
ATOM   4408  CB  ASN A 570      17.005  20.283  23.554  1.00 22.37           C  
ATOM   4409  CG  ASN A 570      17.129  21.695  23.019  1.00 22.97           C  
ATOM   4410  OD1 ASN A 570      18.118  22.040  22.370  1.00 24.23           O  
ATOM   4411  ND2 ASN A 570      16.126  22.524  23.291  1.00 22.71           N  
ATOM   4412  N   ILE A 571      17.680  16.826  22.868  1.00 20.58           N  
ATOM   4413  CA  ILE A 571      18.148  15.553  23.409  1.00 19.76           C  
ATOM   4414  C   ILE A 571      19.622  15.369  23.033  1.00 19.66           C  
ATOM   4415  O   ILE A 571      19.993  15.492  21.863  1.00 19.54           O  
ATOM   4416  CB  ILE A 571      17.299  14.360  22.882  1.00 19.62           C  
ATOM   4417  CG1 ILE A 571      15.806  14.584  23.162  1.00 19.54           C  
ATOM   4418  CG2 ILE A 571      17.777  13.044  23.489  1.00 18.88           C  
ATOM   4419  CD1 ILE A 571      14.864  13.635  22.397  1.00 19.60           C  
ATOM   4420  N   ARG A 572      20.458  15.094  24.030  1.00 19.67           N  
ATOM   4421  CA  ARG A 572      21.894  14.899  23.811  1.00 19.84           C  
ATOM   4422  C   ARG A 572      22.167  13.600  23.049  1.00 19.29           C  
ATOM   4423  O   ARG A 572      21.348  12.674  23.077  1.00 18.63           O  
ATOM   4424  CB  ARG A 572      22.647  14.912  25.146  1.00 20.29           C  
ATOM   4425  CG  ARG A 572      22.513  16.234  25.914  1.00 22.86           C  
ATOM   4426  CD  ARG A 572      22.966  16.113  27.360  1.00 27.14           C  
ATOM   4427  NE  ARG A 572      24.417  16.223  27.500  1.00 31.08           N  
ATOM   4428  CZ  ARG A 572      25.220  15.231  27.878  1.00 32.22           C  
ATOM   4429  NH1 ARG A 572      24.725  14.033  28.171  1.00 32.52           N  
ATOM   4430  NH2 ARG A 572      26.526  15.443  27.971  1.00 33.20           N  
ATOM   4431  N   ASP A 573      23.317  13.543  22.374  1.00 18.79           N  
ATOM   4432  CA  ASP A 573      23.739  12.353  21.624  1.00 18.75           C  
ATOM   4433  C   ASP A 573      23.692  11.054  22.442  1.00 18.12           C  
ATOM   4434  O   ASP A 573      23.359   9.998  21.903  1.00 18.15           O  
ATOM   4435  CB  ASP A 573      25.148  12.546  21.045  1.00 18.99           C  
ATOM   4436  CG  ASP A 573      25.186  13.528  19.879  1.00 20.44           C  
ATOM   4437  OD1 ASP A 573      26.177  13.491  19.118  1.00 22.13           O  
ATOM   4438  OD2 ASP A 573      24.240  14.333  19.714  1.00 20.77           O  
ATOM   4439  N   ASP A 574      24.027  11.129  23.730  1.00 17.56           N  
ATOM   4440  CA  ASP A 574      24.002   9.945  24.596  1.00 17.15           C  
ATOM   4441  C   ASP A 574      22.689   9.779  25.380  1.00 16.41           C  
ATOM   4442  O   ASP A 574      22.615   8.967  26.305  1.00 16.11           O  
ATOM   4443  CB  ASP A 574      25.225   9.904  25.536  1.00 17.65           C  
ATOM   4444  CG  ASP A 574      25.249  11.056  26.541  1.00 19.27           C  
ATOM   4445  OD1 ASP A 574      26.171  11.080  27.389  1.00 21.73           O  
ATOM   4446  OD2 ASP A 574      24.363  11.931  26.492  1.00 20.20           O  
ATOM   4447  N   GLU A 575      21.665  10.543  24.993  1.00 15.80           N  
ATOM   4448  CA  GLU A 575      20.348  10.483  25.634  1.00 15.84           C  
ATOM   4449  C   GLU A 575      19.268   9.957  24.693  1.00 14.42           C  
ATOM   4450  O   GLU A 575      18.109   9.833  25.082  1.00 13.88           O  
ATOM   4451  CB  GLU A 575      19.915  11.860  26.146  1.00 16.15           C  
ATOM   4452  CG  GLU A 575      20.793  12.471  27.215  1.00 18.48           C  
ATOM   4453  CD  GLU A 575      20.251  13.805  27.710  1.00 18.50           C  
ATOM   4454  OE1 GLU A 575      20.387  14.076  28.922  1.00 23.58           O  
ATOM   4455  OE2 GLU A 575      19.684  14.580  26.900  1.00 22.14           O  
ATOM   4456  N   GLY A 576      19.640   9.661  23.453  1.00 13.68           N  
ATOM   4457  CA  GLY A 576      18.669   9.147  22.502  1.00 12.81           C  
ATOM   4458  C   GLY A 576      19.256   8.775  21.163  1.00 12.13           C  
ATOM   4459  O   GLY A 576      20.418   9.054  20.880  1.00 12.01           O  
ATOM   4460  N   PHE A 577      18.437   8.134  20.341  1.00 11.92           N  
ATOM   4461  CA  PHE A 577      18.807   7.875  18.958  1.00 11.71           C  
ATOM   4462  C   PHE A 577      17.567   7.838  18.086  1.00 11.48           C  
ATOM   4463  O   PHE A 577      16.455   7.603  18.575  1.00 11.88           O  
ATOM   4464  CB  PHE A 577      19.655   6.595  18.803  1.00 11.84           C  
ATOM   4465  CG  PHE A 577      19.035   5.352  19.398  1.00 12.39           C  
ATOM   4466  CD1 PHE A 577      17.873   4.803  18.862  1.00 13.22           C  
ATOM   4467  CD2 PHE A 577      19.640   4.709  20.477  1.00 12.92           C  
ATOM   4468  CE1 PHE A 577      17.301   3.646  19.407  1.00 13.25           C  
ATOM   4469  CE2 PHE A 577      19.075   3.549  21.030  1.00 13.77           C  
ATOM   4470  CZ  PHE A 577      17.907   3.023  20.493  1.00 12.99           C  
ATOM   4471  N   ILE A 578      17.775   8.094  16.802  1.00 11.27           N  
ATOM   4472  CA  ILE A 578      16.734   7.979  15.796  1.00 11.20           C  
ATOM   4473  C   ILE A 578      16.940   6.675  15.026  1.00 10.90           C  
ATOM   4474  O   ILE A 578      18.063   6.353  14.618  1.00 10.93           O  
ATOM   4475  CB  ILE A 578      16.781   9.191  14.824  1.00 11.37           C  
ATOM   4476  CG1 ILE A 578      16.390  10.478  15.557  1.00 11.27           C  
ATOM   4477  CG2 ILE A 578      15.893   8.970  13.596  1.00 11.32           C  
ATOM   4478  CD1 ILE A 578      16.665  11.736  14.752  1.00 11.82           C  
ATOM   4479  N   ILE A 579      15.852   5.931  14.838  1.00 10.89           N  
ATOM   4480  CA  ILE A 579      15.854   4.770  13.948  1.00 10.56           C  
ATOM   4481  C   ILE A 579      15.005   5.106  12.727  1.00 10.54           C  
ATOM   4482  O   ILE A 579      13.845   5.498  12.857  1.00 10.32           O  
ATOM   4483  CB  ILE A 579      15.288   3.495  14.634  1.00 10.43           C  
ATOM   4484  CG1 ILE A 579      16.028   3.186  15.949  1.00 11.07           C  
ATOM   4485  CG2 ILE A 579      15.277   2.301  13.648  1.00 11.00           C  
ATOM   4486  CD1 ILE A 579      17.490   2.771  15.803  1.00 12.02           C  
ATOM   4487  N   ARG A 580      15.598   4.959  11.550  1.00 10.32           N  
ATOM   4488  CA  ARG A 580      14.908   5.235  10.301  1.00 11.65           C  
ATOM   4489  C   ARG A 580      14.107   4.000   9.909  1.00 11.29           C  
ATOM   4490  O   ARG A 580      14.493   3.238   9.020  1.00 11.84           O  
ATOM   4491  CB  ARG A 580      15.899   5.651   9.204  1.00 11.53           C  
ATOM   4492  CG  ARG A 580      16.620   6.972   9.487  1.00 13.58           C  
ATOM   4493  CD  ARG A 580      17.293   7.540   8.249  1.00 13.43           C  
ATOM   4494  NE  ARG A 580      17.864   8.863   8.521  1.00 17.66           N  
ATOM   4495  CZ  ARG A 580      19.148   9.107   8.773  1.00 18.85           C  
ATOM   4496  NH1 ARG A 580      20.039   8.121   8.782  1.00 19.16           N  
ATOM   4497  NH2 ARG A 580      19.546  10.353   9.013  1.00 19.71           N  
ATOM   4498  N   HIS A 581      13.000   3.798  10.615  1.00 11.18           N  
ATOM   4499  CA  HIS A 581      12.099   2.684  10.365  1.00 10.98           C  
ATOM   4500  C   HIS A 581      11.495   2.749   8.969  1.00 11.14           C  
ATOM   4501  O   HIS A 581      11.410   3.822   8.364  1.00 11.05           O  
ATOM   4502  CB  HIS A 581      10.985   2.667  11.408  1.00 10.94           C  
ATOM   4503  CG  HIS A 581      11.435   2.227  12.765  1.00 10.71           C  
ATOM   4504  ND1 HIS A 581      11.544   3.090  13.833  1.00 11.63           N  
ATOM   4505  CD2 HIS A 581      11.797   1.008  13.228  1.00  9.03           C  
ATOM   4506  CE1 HIS A 581      11.952   2.422  14.897  1.00  8.65           C  
ATOM   4507  NE2 HIS A 581      12.114   1.157  14.557  1.00 11.62           N  
ATOM   4508  N   PHE A 582      11.057   1.598   8.467  1.00 11.28           N  
ATOM   4509  CA  PHE A 582      10.414   1.550   7.151  1.00 11.99           C  
ATOM   4510  C   PHE A 582       9.207   2.490   7.111  1.00 12.12           C  
ATOM   4511  O   PHE A 582       8.896   3.067   6.066  1.00 12.70           O  
ATOM   4512  CB  PHE A 582       9.988   0.117   6.808  1.00 12.30           C  
ATOM   4513  CG  PHE A 582       8.709  -0.315   7.479  1.00 12.71           C  
ATOM   4514  CD1 PHE A 582       7.501  -0.291   6.781  1.00 13.33           C  
ATOM   4515  CD2 PHE A 582       8.706  -0.718   8.811  1.00 12.89           C  
ATOM   4516  CE1 PHE A 582       6.310  -0.683   7.393  1.00 13.72           C  
ATOM   4517  CE2 PHE A 582       7.514  -1.114   9.435  1.00 14.34           C  
ATOM   4518  CZ  PHE A 582       6.316  -1.094   8.718  1.00 13.76           C  
ATOM   4519  N   ALA A 583       8.547   2.643   8.261  1.00 12.38           N  
ATOM   4520  CA  ALA A 583       7.319   3.429   8.388  1.00 12.43           C  
ATOM   4521  C   ALA A 583       7.562   4.883   8.802  1.00 12.62           C  
ATOM   4522  O   ALA A 583       6.608   5.651   8.996  1.00 12.73           O  
ATOM   4523  CB  ALA A 583       6.359   2.747   9.369  1.00 12.49           C  
ATOM   4524  N   GLY A 584       8.831   5.256   8.935  1.00 12.54           N  
ATOM   4525  CA  GLY A 584       9.203   6.624   9.293  1.00 12.30           C  
ATOM   4526  C   GLY A 584      10.211   6.674  10.422  1.00 12.19           C  
ATOM   4527  O   GLY A 584      10.272   5.762  11.253  1.00 12.19           O  
ATOM   4528  N   ALA A 585      11.007   7.739  10.445  1.00 11.79           N  
ATOM   4529  CA  ALA A 585      11.993   7.934  11.508  1.00 11.48           C  
ATOM   4530  C   ALA A 585      11.294   8.150  12.848  1.00 11.52           C  
ATOM   4531  O   ALA A 585      10.292   8.875  12.934  1.00 11.76           O  
ATOM   4532  CB  ALA A 585      12.916   9.102  11.189  1.00 12.12           C  
ATOM   4533  N   VAL A 586      11.819   7.493  13.879  1.00 11.02           N  
ATOM   4534  CA  VAL A 586      11.329   7.650  15.243  1.00 10.54           C  
ATOM   4535  C   VAL A 586      12.512   7.958  16.149  1.00 10.86           C  
ATOM   4536  O   VAL A 586      13.519   7.251  16.126  1.00 10.28           O  
ATOM   4537  CB  VAL A 586      10.601   6.373  15.759  1.00 10.24           C  
ATOM   4538  CG1 VAL A 586      10.137   6.567  17.198  1.00 10.30           C  
ATOM   4539  CG2 VAL A 586       9.402   6.049  14.887  1.00 10.21           C  
ATOM   4540  N   CYS A 587      12.379   9.016  16.947  1.00 11.19           N  
ATOM   4541  CA  CYS A 587      13.416   9.388  17.905  1.00 11.03           C  
ATOM   4542  C   CYS A 587      13.075   8.815  19.277  1.00 10.81           C  
ATOM   4543  O   CYS A 587      12.001   9.090  19.820  1.00 10.32           O  
ATOM   4544  CB  CYS A 587      13.563  10.908  17.980  1.00 11.28           C  
ATOM   4545  SG  CYS A 587      14.912  11.425  19.063  1.00 13.67           S  
ATOM   4546  N   TYR A 588      13.986   7.999  19.802  1.00 10.51           N  
ATOM   4547  CA  TYR A 588      13.844   7.348  21.106  1.00 10.69           C  
ATOM   4548  C   TYR A 588      14.713   8.027  22.159  1.00 11.16           C  
ATOM   4549  O   TYR A 588      15.899   8.271  21.928  1.00 11.41           O  
ATOM   4550  CB  TYR A 588      14.249   5.873  21.007  1.00 10.40           C  
ATOM   4551  CG  TYR A 588      13.412   5.086  20.023  1.00  9.52           C  
ATOM   4552  CD1 TYR A 588      13.826   4.917  18.698  1.00  9.76           C  
ATOM   4553  CD2 TYR A 588      12.202   4.520  20.416  1.00 10.25           C  
ATOM   4554  CE1 TYR A 588      13.043   4.202  17.785  1.00  9.21           C  
ATOM   4555  CE2 TYR A 588      11.417   3.808  19.520  1.00  8.83           C  
ATOM   4556  CZ  TYR A 588      11.843   3.643  18.217  1.00  9.63           C  
ATOM   4557  OH  TYR A 588      11.063   2.932  17.342  1.00  9.74           O  
ATOM   4558  N   GLU A 589      14.107   8.344  23.295  1.00 11.70           N  
ATOM   4559  CA  GLU A 589      14.842   8.743  24.487  1.00 13.30           C  
ATOM   4560  C   GLU A 589      15.268   7.453  25.161  1.00 12.97           C  
ATOM   4561  O   GLU A 589      14.443   6.556  25.364  1.00 12.92           O  
ATOM   4562  CB  GLU A 589      13.950   9.557  25.426  1.00 13.26           C  
ATOM   4563  CG  GLU A 589      13.524  10.905  24.858  1.00 15.28           C  
ATOM   4564  CD  GLU A 589      12.388  11.563  25.640  1.00 15.93           C  
ATOM   4565  OE1 GLU A 589      12.024  12.704  25.288  1.00 21.18           O  
ATOM   4566  OE2 GLU A 589      11.856  10.951  26.591  1.00 20.36           O  
ATOM   4567  N   THR A 590      16.551   7.353  25.495  1.00 13.10           N  
ATOM   4568  CA  THR A 590      17.097   6.102  26.011  1.00 13.43           C  
ATOM   4569  C   THR A 590      17.155   5.992  27.543  1.00 14.28           C  
ATOM   4570  O   THR A 590      17.627   4.979  28.065  1.00 13.85           O  
ATOM   4571  CB  THR A 590      18.463   5.738  25.370  1.00 13.62           C  
ATOM   4572  OG1 THR A 590      19.336   6.868  25.429  1.00 12.69           O  
ATOM   4573  CG2 THR A 590      18.277   5.327  23.912  1.00 13.53           C  
ATOM   4574  N   THR A 591      16.676   7.016  28.260  1.00 15.14           N  
ATOM   4575  C   THR A 591      15.659   5.701  30.020  1.00 15.71           C  
ATOM   4576  O   THR A 591      14.626   5.501  29.375  1.00 16.24           O  
ATOM   4577  CA ATHR A 591      16.541   6.915  29.712  0.50 15.55           C  
ATOM   4578  CB ATHR A 591      15.922   8.191  30.324  0.50 15.64           C  
ATOM   4579  OG1ATHR A 591      16.574   9.345  29.786  0.50 16.67           O  
ATOM   4580  CG2ATHR A 591      16.070   8.194  31.841  0.50 14.69           C  
ATOM   4582  CB BTHR A 591      15.915   8.164  30.392  0.50 15.78           C  
ATOM   4583  OG1BTHR A 591      14.781   8.624  29.642  0.50 15.82           O  
ATOM   4584  CG2BTHR A 591      16.932   9.275  30.525  0.50 16.43           C  
ATOM   4585  N   GLN A 592      16.080   4.894  30.988  1.00 15.98           N  
ATOM   4586  CA  GLN A 592      15.353   3.690  31.417  1.00 16.52           C  
ATOM   4587  C   GLN A 592      15.438   2.481  30.469  1.00 15.37           C  
ATOM   4588  O   GLN A 592      14.819   1.456  30.740  1.00 15.12           O  
ATOM   4589  CB  GLN A 592      13.880   3.995  31.758  1.00 16.72           C  
ATOM   4590  CG  GLN A 592      13.681   5.101  32.792  1.00 18.66           C  
ATOM   4591  CD  GLN A 592      12.220   5.355  33.104  1.00 19.00           C  
ATOM   4592  OE1 GLN A 592      11.491   4.447  33.508  1.00 23.57           O  
ATOM   4593  NE2 GLN A 592      11.785   6.594  32.926  1.00 23.09           N  
ATOM   4594  N   PHE A 593      16.201   2.580  29.379  1.00 14.75           N  
ATOM   4595  CA  PHE A 593      16.374   1.427  28.479  1.00 14.14           C  
ATOM   4596  C   PHE A 593      16.985   0.241  29.222  1.00 14.28           C  
ATOM   4597  O   PHE A 593      16.523  -0.889  29.078  1.00 14.02           O  
ATOM   4598  CB  PHE A 593      17.237   1.788  27.263  1.00 13.80           C  
ATOM   4599  CG  PHE A 593      16.450   2.086  26.002  1.00 13.35           C  
ATOM   4600  CD1 PHE A 593      15.406   3.009  26.000  1.00 11.66           C  
ATOM   4601  CD2 PHE A 593      16.782   1.452  24.799  1.00 12.90           C  
ATOM   4602  CE1 PHE A 593      14.696   3.289  24.823  1.00 12.07           C  
ATOM   4603  CE2 PHE A 593      16.076   1.728  23.620  1.00 12.27           C  
ATOM   4604  CZ  PHE A 593      15.036   2.654  23.635  1.00 12.73           C  
ATOM   4605  N   VAL A 594      18.012   0.508  30.030  1.00 14.54           N  
ATOM   4606  CA  VAL A 594      18.695  -0.547  30.788  1.00 15.32           C  
ATOM   4607  C   VAL A 594      17.748  -1.213  31.800  1.00 15.54           C  
ATOM   4608  O   VAL A 594      17.629  -2.439  31.819  1.00 15.33           O  
ATOM   4609  CB  VAL A 594      19.994  -0.030  31.463  1.00 15.12           C  
ATOM   4610  CG1 VAL A 594      20.612  -1.097  32.376  1.00 15.73           C  
ATOM   4611  CG2 VAL A 594      21.003   0.402  30.401  1.00 15.57           C  
ATOM   4612  N   GLU A 595      17.053  -0.419  32.615  1.00 16.27           N  
ATOM   4613  CA  GLU A 595      16.113  -1.021  33.572  1.00 17.70           C  
ATOM   4614  C   GLU A 595      14.962  -1.754  32.875  1.00 16.79           C  
ATOM   4615  O   GLU A 595      14.563  -2.842  33.305  1.00 16.96           O  
ATOM   4616  CB  GLU A 595      15.620  -0.024  34.637  1.00 17.90           C  
ATOM   4617  CG  GLU A 595      14.717   1.107  34.161  1.00 20.75           C  
ATOM   4618  CD  GLU A 595      14.130   1.920  35.317  1.00 20.84           C  
ATOM   4619  OE1 GLU A 595      13.704   3.067  35.080  1.00 25.15           O  
ATOM   4620  OE2 GLU A 595      14.092   1.421  36.466  1.00 26.26           O  
ATOM   4621  N   LYS A 596      14.466  -1.182  31.778  1.00 15.92           N  
ATOM   4622  CA  LYS A 596      13.361  -1.790  31.025  1.00 15.28           C  
ATOM   4623  C   LYS A 596      13.761  -3.055  30.257  1.00 15.22           C  
ATOM   4624  O   LYS A 596      12.903  -3.835  29.850  1.00 15.41           O  
ATOM   4625  CB  LYS A 596      12.711  -0.770  30.091  1.00 15.25           C  
ATOM   4626  CG  LYS A 596      11.862   0.253  30.827  1.00 14.21           C  
ATOM   4627  CD  LYS A 596      11.282   1.291  29.882  1.00 12.91           C  
ATOM   4628  CE  LYS A 596      10.314   2.209  30.622  1.00 12.20           C  
ATOM   4629  NZ  LYS A 596       9.680   3.213  29.704  1.00 12.68           N  
ATOM   4630  N   ASN A 597      15.061  -3.261  30.078  1.00 15.20           N  
ATOM   4631  CA  ASN A 597      15.553  -4.461  29.403  1.00 15.26           C  
ATOM   4632  C   ASN A 597      15.677  -5.684  30.319  1.00 15.80           C  
ATOM   4633  O   ASN A 597      15.946  -6.791  29.849  1.00 15.27           O  
ATOM   4634  CB  ASN A 597      16.888  -4.174  28.718  1.00 14.99           C  
ATOM   4635  CG  ASN A 597      17.310  -5.287  27.774  1.00 14.34           C  
ATOM   4636  OD1 ASN A 597      16.509  -5.780  26.976  1.00 12.56           O  
ATOM   4637  ND2 ASN A 597      18.573  -5.690  27.864  1.00 15.04           N  
ATOM   4638  N   ASN A 598      15.466  -5.478  31.618  1.00 16.32           N  
ATOM   4639  CA  ASN A 598      15.635  -6.540  32.609  1.00 17.49           C  
ATOM   4640  C   ASN A 598      14.306  -7.086  33.120  1.00 18.09           C  
ATOM   4641  O   ASN A 598      13.583  -6.405  33.863  1.00 18.09           O  
ATOM   4642  CB  ASN A 598      16.504  -6.055  33.777  1.00 17.53           C  
ATOM   4643  CG  ASN A 598      16.961  -7.189  34.683  1.00 18.27           C  
ATOM   4644  OD1 ASN A 598      16.607  -8.351  34.478  1.00 18.32           O  
ATOM   4645  ND2 ASN A 598      17.767  -6.852  35.689  1.00 20.60           N  
ATOM   4646  N   ASP A 599      14.008  -8.320  32.721  1.00 19.01           N  
ATOM   4647  CA  ASP A 599      12.758  -8.999  33.060  1.00 20.53           C  
ATOM   4648  C   ASP A 599      12.874  -9.880  34.313  1.00 20.72           C  
ATOM   4649  O   ASP A 599      11.893 -10.506  34.732  1.00 20.83           O  
ATOM   4650  CB  ASP A 599      12.310  -9.858  31.874  1.00 21.08           C  
ATOM   4651  CG  ASP A 599      10.805  -9.836  31.666  1.00 22.78           C  
ATOM   4652  OD1 ASP A 599      10.141  -8.883  32.123  1.00 26.09           O  
ATOM   4653  OD2 ASP A 599      10.285 -10.777  31.032  1.00 26.30           O  
ATOM   4654  N   ALA A 600      14.066  -9.926  34.903  1.00 21.11           N  
ATOM   4655  CA  ALA A 600      14.335 -10.814  36.038  1.00 21.23           C  
ATOM   4656  C   ALA A 600      13.561 -10.423  37.295  1.00 21.39           C  
ATOM   4657  O   ALA A 600      13.308  -9.243  37.544  1.00 21.13           O  
ATOM   4658  CB  ALA A 600      15.836 -10.881  36.333  1.00 21.27           C  
ATOM   4659  N   LEU A 601      13.168 -11.432  38.067  1.00 21.67           N  
ATOM   4660  CA  LEU A 601      12.562 -11.212  39.373  1.00 21.88           C  
ATOM   4661  C   LEU A 601      13.456 -11.858  40.420  1.00 22.34           C  
ATOM   4662  O   LEU A 601      13.841 -13.027  40.286  1.00 21.81           O  
ATOM   4663  CB  LEU A 601      11.143 -11.794  39.433  1.00 21.92           C  
ATOM   4664  CG  LEU A 601      10.311 -11.534  40.699  1.00 21.74           C  
ATOM   4665  CD1 LEU A 601       9.912 -10.064  40.831  1.00 21.64           C  
ATOM   4666  CD2 LEU A 601       9.073 -12.422  40.743  1.00 21.91           C  
ATOM   4667  N   HIS A 602      13.797 -11.085  41.448  1.00 22.81           N  
ATOM   4668  CA  HIS A 602      14.619 -11.580  42.544  1.00 23.79           C  
ATOM   4669  C   HIS A 602      13.959 -12.792  43.192  1.00 23.97           C  
ATOM   4670  O   HIS A 602      12.742 -12.822  43.373  1.00 23.92           O  
ATOM   4671  CB  HIS A 602      14.879 -10.475  43.573  1.00 23.98           C  
ATOM   4672  CG  HIS A 602      15.895  -9.467  43.127  1.00 25.68           C  
ATOM   4673  ND1 HIS A 602      15.568  -8.167  42.808  1.00 26.93           N  
ATOM   4674  CD2 HIS A 602      17.231  -9.577  42.928  1.00 26.81           C  
ATOM   4675  CE1 HIS A 602      16.658  -7.517  42.440  1.00 27.05           C  
ATOM   4676  NE2 HIS A 602      17.681  -8.350  42.504  1.00 27.61           N  
ATOM   4677  N   MET A 603      14.771 -13.791  43.525  1.00 24.64           N  
ATOM   4678  CA  MET A 603      14.264 -15.045  44.083  1.00 25.26           C  
ATOM   4679  C   MET A 603      13.425 -14.867  45.342  1.00 25.01           C  
ATOM   4680  O   MET A 603      12.471 -15.617  45.563  1.00 25.07           O  
ATOM   4681  CB  MET A 603      15.404 -16.036  44.333  1.00 26.15           C  
ATOM   4682  CG  MET A 603      15.451 -17.150  43.312  1.00 28.01           C  
ATOM   4683  SD  MET A 603      14.003 -18.223  43.441  1.00 33.99           S  
ATOM   4684  CE  MET A 603      14.139 -19.148  41.913  1.00 30.39           C  
ATOM   4685  N   SER A 604      13.779 -13.873  46.151  1.00 24.68           N  
ATOM   4686  CA  SER A 604      13.029 -13.538  47.364  1.00 24.62           C  
ATOM   4687  C   SER A 604      11.553 -13.280  47.055  1.00 24.45           C  
ATOM   4688  O   SER A 604      10.664 -13.775  47.756  1.00 24.09           O  
ATOM   4689  CB  SER A 604      13.648 -12.319  48.057  1.00 24.76           C  
ATOM   4690  OG  SER A 604      13.688 -11.193  47.192  1.00 25.72           O  
ATOM   4691  N   LEU A 605      11.310 -12.516  45.992  1.00 23.97           N  
ATOM   4692  CA  LEU A 605       9.957 -12.164  45.563  1.00 24.04           C  
ATOM   4693  C   LEU A 605       9.246 -13.326  44.867  1.00 24.17           C  
ATOM   4694  O   LEU A 605       8.045 -13.521  45.060  1.00 23.90           O  
ATOM   4695  CB  LEU A 605       9.984 -10.915  44.668  1.00 23.72           C  
ATOM   4696  CG  LEU A 605      10.605  -9.652  45.290  1.00 23.80           C  
ATOM   4697  CD1 LEU A 605      10.885  -8.577  44.236  1.00 23.57           C  
ATOM   4698  CD2 LEU A 605       9.738  -9.096  46.414  1.00 23.24           C  
ATOM   4699  N   GLU A 606       9.985 -14.088  44.060  1.00 24.46           N  
ATOM   4700  CA  GLU A 606       9.441 -15.281  43.409  1.00 25.25           C  
ATOM   4701  C   GLU A 606       9.009 -16.309  44.455  1.00 24.82           C  
ATOM   4702  O   GLU A 606       7.920 -16.874  44.360  1.00 24.84           O  
ATOM   4703  CB  GLU A 606      10.463 -15.891  42.444  1.00 25.14           C  
ATOM   4704  CG  GLU A 606       9.911 -17.019  41.574  1.00 26.50           C  
ATOM   4705  CD  GLU A 606      10.960 -17.645  40.664  1.00 27.12           C  
ATOM   4706  OE1 GLU A 606      10.734 -18.785  40.201  1.00 29.55           O  
ATOM   4707  OE2 GLU A 606      12.006 -17.007  40.405  1.00 30.23           O  
ATOM   4708  N   SER A 607       9.863 -16.529  45.454  1.00 24.82           N  
ATOM   4709  CA  SER A 607       9.578 -17.473  46.542  1.00 24.67           C  
ATOM   4710  C   SER A 607       8.351 -17.065  47.350  1.00 24.26           C  
ATOM   4711  O   SER A 607       7.537 -17.916  47.714  1.00 24.46           O  
ATOM   4712  CB  SER A 607      10.795 -17.628  47.461  1.00 24.81           C  
ATOM   4713  OG  SER A 607      11.841 -18.320  46.795  1.00 26.37           O  
ATOM   4714  N   LEU A 608       8.224 -15.764  47.615  1.00 23.60           N  
ATOM   4715  CA  LEU A 608       7.093 -15.210  48.359  1.00 23.16           C  
ATOM   4716  C   LEU A 608       5.755 -15.562  47.709  1.00 23.06           C  
ATOM   4717  O   LEU A 608       4.850 -16.087  48.364  1.00 22.93           O  
ATOM   4718  CB  LEU A 608       7.229 -13.685  48.473  1.00 22.89           C  
ATOM   4719  CG  LEU A 608       6.053 -12.880  49.044  1.00 22.71           C  
ATOM   4720  CD1 LEU A 608       5.935 -13.052  50.561  1.00 22.78           C  
ATOM   4721  CD2 LEU A 608       6.186 -11.415  48.684  1.00 22.96           C  
ATOM   4722  N   ILE A 609       5.644 -15.274  46.417  1.00 22.89           N  
ATOM   4723  CA  ILE A 609       4.393 -15.474  45.697  1.00 22.93           C  
ATOM   4724  C   ILE A 609       4.124 -16.952  45.367  1.00 23.32           C  
ATOM   4725  O   ILE A 609       2.977 -17.397  45.428  1.00 23.17           O  
ATOM   4726  CB  ILE A 609       4.294 -14.528  44.447  1.00 22.69           C  
ATOM   4727  CG1 ILE A 609       2.838 -14.339  44.007  1.00 22.36           C  
ATOM   4728  CG2 ILE A 609       5.221 -14.969  43.312  1.00 22.87           C  
ATOM   4729  CD1 ILE A 609       2.032 -13.423  44.921  1.00 21.25           C  
ATOM   4730  N   CYS A 610       5.177 -17.709  45.052  1.00 23.80           N  
ATOM   4731  CA  CYS A 610       5.033 -19.138  44.735  1.00 24.76           C  
ATOM   4732  C   CYS A 610       4.558 -19.947  45.938  1.00 24.70           C  
ATOM   4733  O   CYS A 610       3.975 -21.021  45.777  1.00 24.90           O  
ATOM   4734  CB  CYS A 610       6.343 -19.725  44.204  1.00 24.86           C  
ATOM   4735  SG  CYS A 610       6.747 -19.214  42.528  1.00 27.47           S  
ATOM   4736  N   GLU A 611       4.808 -19.415  47.132  1.00 24.77           N  
ATOM   4737  CA  GLU A 611       4.418 -20.055  48.386  1.00 25.04           C  
ATOM   4738  C   GLU A 611       3.198 -19.391  49.023  1.00 24.56           C  
ATOM   4739  O   GLU A 611       2.976 -19.503  50.233  1.00 24.68           O  
ATOM   4740  CB  GLU A 611       5.597 -20.064  49.365  1.00 25.40           C  
ATOM   4741  CG  GLU A 611       6.688 -21.064  48.996  1.00 27.33           C  
ATOM   4742  CD  GLU A 611       8.041 -20.734  49.606  1.00 29.52           C  
ATOM   4743  OE1 GLU A 611       8.097 -19.974  50.598  1.00 30.77           O  
ATOM   4744  OE2 GLU A 611       9.058 -21.244  49.087  1.00 31.27           O  
ATOM   4745  N   SER A 612       2.399 -18.703  48.207  1.00 23.90           N  
ATOM   4746  CA  SER A 612       1.154 -18.118  48.692  1.00 23.15           C  
ATOM   4747  C   SER A 612       0.275 -19.215  49.277  1.00 23.14           C  
ATOM   4748  O   SER A 612       0.307 -20.358  48.819  1.00 22.75           O  
ATOM   4749  CB  SER A 612       0.406 -17.400  47.566  1.00 23.17           C  
ATOM   4750  OG  SER A 612      -0.918 -17.075  47.957  1.00 21.71           O  
ATOM   4751  N   ARG A 613      -0.507 -18.860  50.288  1.00 23.22           N  
ATOM   4752  CA  ARG A 613      -1.430 -19.811  50.904  1.00 23.55           C  
ATOM   4753  C   ARG A 613      -2.645 -20.062  50.015  1.00 23.26           C  
ATOM   4754  O   ARG A 613      -3.405 -21.009  50.237  1.00 23.37           O  
ATOM   4755  CB  ARG A 613      -1.844 -19.328  52.295  1.00 23.81           C  
ATOM   4756  CG  ARG A 613      -0.666 -19.251  53.262  1.00 25.61           C  
ATOM   4757  CD  ARG A 613      -1.101 -18.842  54.655  1.00 28.74           C  
ATOM   4758  NE  ARG A 613       0.038 -18.685  55.558  1.00 30.45           N  
ATOM   4759  CZ  ARG A 613      -0.049 -18.669  56.887  1.00 31.55           C  
ATOM   4760  NH1 ARG A 613      -1.225 -18.808  57.487  1.00 30.71           N  
ATOM   4761  NH2 ARG A 613       1.047 -18.518  57.620  1.00 32.25           N  
ATOM   4762  N   ASP A 614      -2.806 -19.219  48.998  1.00 22.71           N  
ATOM   4763  CA  ASP A 614      -3.918 -19.335  48.065  1.00 22.34           C  
ATOM   4764  C   ASP A 614      -3.546 -20.202  46.861  1.00 21.87           C  
ATOM   4765  O   ASP A 614      -2.570 -19.925  46.160  1.00 21.44           O  
ATOM   4766  CB  ASP A 614      -4.384 -17.951  47.614  1.00 22.49           C  
ATOM   4767  CG  ASP A 614      -5.625 -18.013  46.752  1.00 23.41           C  
ATOM   4768  OD1 ASP A 614      -6.708 -18.354  47.281  1.00 24.62           O  
ATOM   4769  OD2 ASP A 614      -5.516 -17.724  45.544  1.00 24.38           O  
ATOM   4770  N   LYS A 615      -4.340 -21.248  46.635  1.00 21.31           N  
ATOM   4771  CA  LYS A 615      -4.097 -22.215  45.565  1.00 21.32           C  
ATOM   4772  C   LYS A 615      -4.035 -21.549  44.191  1.00 20.61           C  
ATOM   4773  O   LYS A 615      -3.122 -21.826  43.407  1.00 20.44           O  
ATOM   4774  CB  LYS A 615      -5.177 -23.304  45.574  1.00 21.27           C  
ATOM   4775  CG  LYS A 615      -4.907 -24.483  44.651  1.00 22.27           C  
ATOM   4776  CD  LYS A 615      -6.039 -25.500  44.717  1.00 22.46           C  
ATOM   4777  CE  LYS A 615      -5.757 -26.699  43.830  1.00 25.11           C  
ATOM   4778  NZ  LYS A 615      -6.999 -27.466  43.521  1.00 26.80           N  
ATOM   4779  N   PHE A 616      -5.004 -20.678  43.914  1.00 20.19           N  
ATOM   4780  CA  PHE A 616      -5.091 -19.986  42.623  1.00 20.15           C  
ATOM   4781  C   PHE A 616      -3.807 -19.228  42.312  1.00 20.15           C  
ATOM   4782  O   PHE A 616      -3.273 -19.331  41.208  1.00 20.15           O  
ATOM   4783  CB  PHE A 616      -6.289 -19.029  42.584  1.00 19.86           C  
ATOM   4784  CG  PHE A 616      -6.499 -18.375  41.240  1.00 19.87           C  
ATOM   4785  CD1 PHE A 616      -7.166 -19.049  40.219  1.00 19.92           C  
ATOM   4786  CD2 PHE A 616      -6.027 -17.089  40.997  1.00 19.02           C  
ATOM   4787  CE1 PHE A 616      -7.360 -18.448  38.970  1.00 19.90           C  
ATOM   4788  CE2 PHE A 616      -6.214 -16.481  39.751  1.00 19.34           C  
ATOM   4789  CZ  PHE A 616      -6.882 -17.163  38.740  1.00 18.39           C  
ATOM   4790  N   ILE A 617      -3.312 -18.485  43.298  1.00 20.43           N  
ATOM   4791  CA  ILE A 617      -2.096 -17.690  43.127  1.00 20.76           C  
ATOM   4792  C   ILE A 617      -0.848 -18.566  42.946  1.00 21.14           C  
ATOM   4793  O   ILE A 617      -0.006 -18.273  42.094  1.00 20.64           O  
ATOM   4794  CB  ILE A 617      -1.969 -16.619  44.231  1.00 20.97           C  
ATOM   4795  CG1 ILE A 617      -2.939 -15.474  43.901  1.00 21.37           C  
ATOM   4796  CG2 ILE A 617      -0.536 -16.079  44.337  1.00 20.99           C  
ATOM   4797  CD1 ILE A 617      -3.256 -14.563  45.028  1.00 22.76           C  
ATOM   4798  N   ARG A 618      -0.749 -19.650  43.715  1.00 21.51           N  
ATOM   4799  CA  ARG A 618       0.309 -20.640  43.501  1.00 22.21           C  
ATOM   4800  C   ARG A 618       0.305 -21.183  42.073  1.00 22.51           C  
ATOM   4801  O   ARG A 618       1.366 -21.353  41.468  1.00 22.91           O  
ATOM   4802  CB  ARG A 618       0.184 -21.810  44.480  1.00 22.18           C  
ATOM   4803  CG  ARG A 618       0.661 -21.510  45.883  1.00 22.37           C  
ATOM   4804  CD  ARG A 618       0.981 -22.798  46.661  1.00 22.41           C  
ATOM   4805  NE  ARG A 618      -0.096 -23.784  46.589  1.00 22.60           N  
ATOM   4806  CZ  ARG A 618      -1.206 -23.753  47.323  1.00 22.43           C  
ATOM   4807  NH1 ARG A 618      -1.409 -22.783  48.208  1.00 22.05           N  
ATOM   4808  NH2 ARG A 618      -2.123 -24.699  47.169  1.00 23.16           N  
ATOM   4809  N   GLU A 619      -0.888 -21.452  41.544  1.00 22.97           N  
ATOM   4810  CA  GLU A 619      -1.033 -22.065  40.219  1.00 23.72           C  
ATOM   4811  C   GLU A 619      -0.746 -21.104  39.057  1.00 23.67           C  
ATOM   4812  O   GLU A 619      -0.574 -21.536  37.914  1.00 23.78           O  
ATOM   4813  CB  GLU A 619      -2.405 -22.731  40.068  1.00 24.06           C  
ATOM   4814  CG  GLU A 619      -2.597 -23.940  40.982  1.00 26.23           C  
ATOM   4815  CD  GLU A 619      -3.548 -24.975  40.414  1.00 29.61           C  
ATOM   4816  OE1 GLU A 619      -3.318 -25.442  39.274  1.00 31.64           O  
ATOM   4817  OE2 GLU A 619      -4.516 -25.338  41.116  1.00 30.90           O  
ATOM   4818  N   LEU A 620      -0.686 -19.806  39.354  1.00 23.71           N  
ATOM   4819  CA  LEU A 620      -0.227 -18.818  38.376  1.00 23.74           C  
ATOM   4820  C   LEU A 620       1.265 -19.001  38.104  1.00 24.20           C  
ATOM   4821  O   LEU A 620       1.761 -18.634  37.035  1.00 24.00           O  
ATOM   4822  CB  LEU A 620      -0.488 -17.391  38.868  1.00 23.53           C  
ATOM   4823  CG  LEU A 620      -1.925 -16.911  39.098  1.00 23.07           C  
ATOM   4824  CD1 LEU A 620      -1.912 -15.490  39.624  1.00 21.99           C  
ATOM   4825  CD2 LEU A 620      -2.755 -16.993  37.825  1.00 23.23           C  
ATOM   4826  N   PHE A 621       1.956 -19.584  39.086  1.00 24.80           N  
ATOM   4827  CA  PHE A 621       3.402 -19.775  39.069  1.00 25.34           C  
ATOM   4828  C   PHE A 621       3.753 -21.258  39.155  1.00 25.67           C  
ATOM   4829  O   PHE A 621       4.014 -21.904  38.142  1.00 26.55           O  
ATOM   4830  CB  PHE A 621       4.033 -19.039  40.251  1.00 25.26           C  
ATOM   4831  CG  PHE A 621       3.904 -17.544  40.176  1.00 25.25           C  
ATOM   4832  CD1 PHE A 621       2.765 -16.901  40.654  1.00 24.72           C  
ATOM   4833  CD2 PHE A 621       4.926 -16.778  39.629  1.00 25.09           C  
ATOM   4834  CE1 PHE A 621       2.644 -15.516  40.577  1.00 24.73           C  
ATOM   4835  CE2 PHE A 621       4.816 -15.394  39.553  1.00 24.91           C  
ATOM   4836  CZ  PHE A 621       3.672 -14.761  40.025  1.00 25.00           C  
ATOM   4837  N   LEU A 638      24.388 -12.777  38.547  1.00 26.06           N  
ATOM   4838  CA  LEU A 638      23.635 -11.566  38.228  1.00 25.78           C  
ATOM   4839  C   LEU A 638      22.171 -11.889  37.942  1.00 25.32           C  
ATOM   4840  O   LEU A 638      21.863 -12.835  37.211  1.00 25.73           O  
ATOM   4841  CB  LEU A 638      24.268 -10.838  37.033  1.00 25.95           C  
ATOM   4842  CG  LEU A 638      23.588  -9.582  36.464  1.00 25.96           C  
ATOM   4843  CD1 LEU A 638      23.681  -8.390  37.421  1.00 26.56           C  
ATOM   4844  CD2 LEU A 638      24.178  -9.232  35.106  1.00 26.01           C  
ATOM   4845  N   SER A 639      21.273 -11.105  38.529  1.00 24.64           N  
ATOM   4846  CA  SER A 639      19.846 -11.260  38.279  1.00 23.59           C  
ATOM   4847  C   SER A 639      19.468 -10.445  37.038  1.00 22.84           C  
ATOM   4848  O   SER A 639      19.133  -9.261  37.143  1.00 22.90           O  
ATOM   4849  CB  SER A 639      19.042 -10.816  39.505  1.00 23.91           C  
ATOM   4850  OG  SER A 639      17.651 -10.807  39.244  1.00 24.08           O  
ATOM   4851  N   PHE A 640      19.554 -11.084  35.870  1.00 21.78           N  
ATOM   4852  CA  PHE A 640      19.247 -10.436  34.587  1.00 20.54           C  
ATOM   4853  C   PHE A 640      18.663 -11.394  33.550  1.00 19.95           C  
ATOM   4854  O   PHE A 640      19.234 -12.457  33.271  1.00 19.81           O  
ATOM   4855  CB  PHE A 640      20.491  -9.735  34.010  1.00 20.41           C  
ATOM   4856  CG  PHE A 640      20.311  -9.237  32.591  1.00 19.85           C  
ATOM   4857  CD1 PHE A 640      19.374  -8.245  32.296  1.00 18.84           C  
ATOM   4858  CD2 PHE A 640      21.082  -9.756  31.557  1.00 19.33           C  
ATOM   4859  CE1 PHE A 640      19.204  -7.791  30.985  1.00 18.40           C  
ATOM   4860  CE2 PHE A 640      20.926  -9.302  30.246  1.00 19.26           C  
ATOM   4861  CZ  PHE A 640      19.985  -8.316  29.962  1.00 18.16           C  
ATOM   4862  N   ILE A 641      17.526 -10.997  32.980  1.00 18.87           N  
ATOM   4863  CA  ILE A 641      16.908 -11.698  31.856  1.00 18.13           C  
ATOM   4864  C   ILE A 641      16.554 -10.648  30.799  1.00 17.15           C  
ATOM   4865  O   ILE A 641      15.816  -9.701  31.079  1.00 17.12           O  
ATOM   4866  CB  ILE A 641      15.652 -12.514  32.283  1.00 18.18           C  
ATOM   4867  CG1 ILE A 641      16.043 -13.639  33.257  1.00 18.83           C  
ATOM   4868  CG2 ILE A 641      14.945 -13.108  31.067  1.00 18.26           C  
ATOM   4869  CD1 ILE A 641      14.877 -14.431  33.809  1.00 18.73           C  
ATOM   4870  N   SER A 642      17.095 -10.817  29.596  1.00 16.12           N  
ATOM   4871  CA  SER A 642      16.931  -9.835  28.518  1.00 15.24           C  
ATOM   4872  C   SER A 642      15.515  -9.754  27.949  1.00 15.11           C  
ATOM   4873  O   SER A 642      14.992 -10.733  27.414  1.00 14.94           O  
ATOM   4874  CB  SER A 642      17.907 -10.124  27.376  1.00 14.81           C  
ATOM   4875  OG  SER A 642      17.661  -9.246  26.286  1.00 13.89           O  
ATOM   4876  N   VAL A 643      14.915  -8.571  28.035  1.00 15.07           N  
ATOM   4877  CA  VAL A 643      13.622  -8.325  27.405  1.00 15.20           C  
ATOM   4878  C   VAL A 643      13.771  -8.313  25.876  1.00 15.13           C  
ATOM   4879  O   VAL A 643      12.951  -8.899  25.172  1.00 15.68           O  
ATOM   4880  CB  VAL A 643      12.961  -7.020  27.927  1.00 14.94           C  
ATOM   4881  CG1 VAL A 643      11.748  -6.633  27.075  1.00 15.40           C  
ATOM   4882  CG2 VAL A 643      12.542  -7.190  29.376  1.00 15.11           C  
ATOM   4883  N   GLY A 644      14.827  -7.672  25.379  1.00 15.59           N  
ATOM   4884  CA  GLY A 644      15.080  -7.580  23.933  1.00 15.76           C  
ATOM   4885  C   GLY A 644      15.257  -8.946  23.293  1.00 16.34           C  
ATOM   4886  O   GLY A 644      14.715  -9.222  22.219  1.00 15.91           O  
ATOM   4887  N   ASN A 645      16.010  -9.808  23.963  1.00 16.69           N  
ATOM   4888  CA  ASN A 645      16.204 -11.172  23.489  1.00 17.94           C  
ATOM   4889  C   ASN A 645      14.891 -11.965  23.504  1.00 18.17           C  
ATOM   4890  O   ASN A 645      14.703 -12.863  22.683  1.00 18.21           O  
ATOM   4891  CB  ASN A 645      17.294 -11.879  24.303  1.00 18.33           C  
ATOM   4892  CG  ASN A 645      17.440 -13.348  23.940  1.00 20.74           C  
ATOM   4893  OD1 ASN A 645      17.150 -14.235  24.754  1.00 23.68           O  
ATOM   4894  ND2 ASN A 645      17.879 -13.614  22.712  1.00 21.81           N  
ATOM   4895  N   LYS A 646      13.979 -11.612  24.415  1.00 18.38           N  
ATOM   4896  CA  LYS A 646      12.620 -12.187  24.391  1.00 18.85           C  
ATOM   4897  C   LYS A 646      11.824 -11.716  23.181  1.00 18.18           C  
ATOM   4898  O   LYS A 646      11.115 -12.506  22.566  1.00 18.76           O  
ATOM   4899  CB  LYS A 646      11.831 -11.895  25.677  1.00 19.10           C  
ATOM   4900  CG  LYS A 646      12.450 -12.427  26.960  1.00 20.67           C  
ATOM   4901  CD  LYS A 646      13.384 -13.612  26.719  1.00 22.51           C  
ATOM   4902  CE  LYS A 646      14.459 -13.656  27.794  1.00 22.84           C  
ATOM   4903  NZ  LYS A 646      15.831 -13.511  27.234  1.00 21.79           N  
ATOM   4904  N   PHE A 647      11.926 -10.434  22.839  1.00 18.01           N  
ATOM   4905  CA  PHE A 647      11.266  -9.946  21.635  1.00 17.28           C  
ATOM   4906  C   PHE A 647      11.794 -10.702  20.416  1.00 16.85           C  
ATOM   4907  O   PHE A 647      11.012 -11.186  19.597  1.00 16.88           O  
ATOM   4908  CB  PHE A 647      11.393  -8.419  21.480  1.00 17.73           C  
ATOM   4909  CG  PHE A 647      10.299  -7.656  22.179  1.00 17.69           C  
ATOM   4910  CD1 PHE A 647      10.419  -7.308  23.522  1.00 18.15           C  
ATOM   4911  CD2 PHE A 647       9.131  -7.308  21.499  1.00 17.67           C  
ATOM   4912  CE1 PHE A 647       9.388  -6.613  24.182  1.00 18.40           C  
ATOM   4913  CE2 PHE A 647       8.092  -6.620  22.147  1.00 17.47           C  
ATOM   4914  CZ  PHE A 647       8.221  -6.271  23.490  1.00 17.74           C  
ATOM   4915  N   LYS A 648      13.113 -10.855  20.331  1.00 15.56           N  
ATOM   4916  CA  LYS A 648      13.724 -11.464  19.154  1.00 15.04           C  
ATOM   4917  C   LYS A 648      13.387 -12.950  19.041  1.00 14.94           C  
ATOM   4918  O   LYS A 648      12.965 -13.419  17.981  1.00 14.65           O  
ATOM   4919  CB  LYS A 648      15.241 -11.255  19.168  1.00 14.55           C  
ATOM   4920  CG  LYS A 648      15.949 -11.840  17.956  1.00 14.56           C  
ATOM   4921  CD  LYS A 648      17.450 -11.696  18.097  1.00 15.88           C  
ATOM   4922  CE  LYS A 648      18.169 -12.163  16.849  1.00 17.65           C  
ATOM   4923  NZ  LYS A 648      19.644 -12.081  17.044  1.00 19.56           N  
ATOM   4924  N   THR A 649      13.575 -13.680  20.137  1.00 15.14           N  
ATOM   4925  CA  THR A 649      13.356 -15.121  20.149  1.00 15.78           C  
ATOM   4926  C   THR A 649      11.903 -15.470  19.821  1.00 15.88           C  
ATOM   4927  O   THR A 649      11.655 -16.358  19.002  1.00 15.87           O  
ATOM   4928  CB  THR A 649      13.804 -15.741  21.491  1.00 16.09           C  
ATOM   4929  OG1 THR A 649      15.203 -15.488  21.675  1.00 16.53           O  
ATOM   4930  CG2 THR A 649      13.569 -17.256  21.503  1.00 16.74           C  
ATOM   4931  N   GLN A 650      10.962 -14.742  20.428  1.00 15.80           N  
ATOM   4932  CA  GLN A 650       9.524 -14.993  20.230  1.00 16.49           C  
ATOM   4933  C   GLN A 650       9.083 -14.701  18.799  1.00 16.17           C  
ATOM   4934  O   GLN A 650       8.336 -15.484  18.198  1.00 16.51           O  
ATOM   4935  CB  GLN A 650       8.679 -14.177  21.222  1.00 16.68           C  
ATOM   4936  CG  GLN A 650       8.734 -14.683  22.665  1.00 19.07           C  
ATOM   4937  CD  GLN A 650       8.256 -16.119  22.800  1.00 21.65           C  
ATOM   4938  OE1 GLN A 650       8.933 -16.954  23.401  1.00 23.82           O  
ATOM   4939  NE2 GLN A 650       7.096 -16.416  22.224  1.00 23.02           N  
ATOM   4940  N   LEU A 651       9.549 -13.577  18.258  1.00 15.81           N  
ATOM   4941  CA  LEU A 651       9.235 -13.190  16.885  1.00 15.54           C  
ATOM   4942  C   LEU A 651       9.798 -14.182  15.883  1.00 15.22           C  
ATOM   4943  O   LEU A 651       9.157 -14.486  14.880  1.00 14.70           O  
ATOM   4944  CB  LEU A 651       9.791 -11.804  16.565  1.00 16.04           C  
ATOM   4945  CG  LEU A 651       9.070 -10.598  17.150  1.00 17.74           C  
ATOM   4946  CD1 LEU A 651       9.915  -9.363  16.912  1.00 19.26           C  
ATOM   4947  CD2 LEU A 651       7.688 -10.462  16.535  1.00 19.82           C  
ATOM   4948  N   ASN A 652      11.004 -14.677  16.148  1.00 14.93           N  
ATOM   4949  CA  ASN A 652      11.617 -15.638  15.240  1.00 15.58           C  
ATOM   4950  C   ASN A 652      10.880 -16.973  15.230  1.00 16.03           C  
ATOM   4951  O   ASN A 652      10.758 -17.598  14.182  1.00 16.43           O  
ATOM   4952  CB  ASN A 652      13.109 -15.793  15.530  1.00 15.57           C  
ATOM   4953  CG  ASN A 652      13.925 -14.653  14.950  1.00 15.20           C  
ATOM   4954  OD1 ASN A 652      13.475 -13.950  14.034  1.00 16.16           O  
ATOM   4955  ND2 ASN A 652      15.131 -14.466  15.467  1.00 15.45           N  
ATOM   4956  N   LEU A 653      10.359 -17.377  16.388  1.00 16.74           N  
ATOM   4957  CA  LEU A 653       9.509 -18.572  16.484  1.00 17.30           C  
ATOM   4958  C   LEU A 653       8.209 -18.374  15.706  1.00 17.35           C  
ATOM   4959  O   LEU A 653       7.779 -19.254  14.945  1.00 17.62           O  
ATOM   4960  CB  LEU A 653       9.208 -18.912  17.946  1.00 17.80           C  
ATOM   4961  CG  LEU A 653      10.366 -19.462  18.790  1.00 18.95           C  
ATOM   4962  CD1 LEU A 653       9.938 -19.578  20.253  1.00 20.54           C  
ATOM   4963  CD2 LEU A 653      10.882 -20.801  18.266  1.00 20.83           C  
ATOM   4964  N   LEU A 654       7.599 -17.209  15.899  1.00 17.17           N  
ATOM   4965  CA  LEU A 654       6.400 -16.817  15.165  1.00 17.10           C  
ATOM   4966  C   LEU A 654       6.643 -16.805  13.658  1.00 17.25           C  
ATOM   4967  O   LEU A 654       5.830 -17.324  12.890  1.00 16.84           O  
ATOM   4968  CB  LEU A 654       5.907 -15.448  15.639  1.00 17.15           C  
ATOM   4969  CG  LEU A 654       4.651 -14.874  14.980  1.00 17.29           C  
ATOM   4970  CD1 LEU A 654       3.469 -15.853  15.058  1.00 17.78           C  
ATOM   4971  CD2 LEU A 654       4.305 -13.552  15.628  1.00 17.07           C  
ATOM   4972  N   LEU A 655       7.764 -16.220  13.239  1.00 17.08           N  
ATOM   4973  CA  LEU A 655       8.093 -16.146  11.817  1.00 17.54           C  
ATOM   4974  C   LEU A 655       8.329 -17.527  11.201  1.00 18.07           C  
ATOM   4975  O   LEU A 655       7.949 -17.766  10.055  1.00 17.78           O  
ATOM   4976  CB  LEU A 655       9.276 -15.208  11.573  1.00 17.43           C  
ATOM   4977  CG  LEU A 655       8.925 -13.716  11.658  1.00 18.05           C  
ATOM   4978  CD1 LEU A 655      10.169 -12.880  11.897  1.00 18.70           C  
ATOM   4979  CD2 LEU A 655       8.192 -13.239  10.404  1.00 18.99           C  
ATOM   4980  N   ASP A 656       8.934 -18.432  11.972  1.00 18.69           N  
ATOM   4981  CA  ASP A 656       9.088 -19.833  11.557  1.00 20.01           C  
ATOM   4982  C   ASP A 656       7.733 -20.459  11.229  1.00 20.06           C  
ATOM   4983  O   ASP A 656       7.588 -21.147  10.217  1.00 20.47           O  
ATOM   4984  CB  ASP A 656       9.752 -20.661  12.660  1.00 20.32           C  
ATOM   4985  CG  ASP A 656      11.245 -20.439  12.753  1.00 22.13           C  
ATOM   4986  OD1 ASP A 656      11.813 -20.805  13.806  1.00 25.09           O  
ATOM   4987  OD2 ASP A 656      11.856 -19.917  11.793  1.00 23.56           O  
ATOM   4988  N   LYS A 657       6.754 -20.221  12.098  1.00 20.23           N  
ATOM   4989  CA  LYS A 657       5.401 -20.748  11.917  1.00 20.77           C  
ATOM   4990  C   LYS A 657       4.743 -20.151  10.672  1.00 20.14           C  
ATOM   4991  O   LYS A 657       4.122 -20.871   9.886  1.00 19.83           O  
ATOM   4992  CB  LYS A 657       4.549 -20.483  13.159  1.00 20.73           C  
ATOM   4993  CG  LYS A 657       3.262 -21.312  13.227  1.00 22.03           C  
ATOM   4994  CD  LYS A 657       2.490 -21.045  14.515  1.00 22.68           C  
ATOM   4995  CE  LYS A 657       3.249 -21.528  15.751  1.00 25.50           C  
ATOM   4996  NZ  LYS A 657       2.800 -20.833  16.985  1.00 26.98           N  
ATOM   4997  N   LEU A 658       4.897 -18.838  10.491  1.00 19.48           N  
ATOM   4998  CA  LEU A 658       4.333 -18.154   9.326  1.00 19.51           C  
ATOM   4999  C   LEU A 658       4.934 -18.657   8.016  1.00 19.68           C  
ATOM   5000  O   LEU A 658       4.225 -18.810   7.024  1.00 19.47           O  
ATOM   5001  CB  LEU A 658       4.509 -16.634   9.436  1.00 19.39           C  
ATOM   5002  CG  LEU A 658       3.829 -15.917  10.608  1.00 19.25           C  
ATOM   5003  CD1 LEU A 658       4.112 -14.423  10.549  1.00 19.27           C  
ATOM   5004  CD2 LEU A 658       2.322 -16.180  10.651  1.00 20.20           C  
ATOM   5005  N   ARG A 659       6.239 -18.919   8.023  1.00 19.94           N  
ATOM   5006  CA  ARG A 659       6.935 -19.370   6.818  1.00 20.54           C  
ATOM   5007  C   ARG A 659       6.479 -20.750   6.356  1.00 20.34           C  
ATOM   5008  O   ARG A 659       6.563 -21.063   5.164  1.00 20.73           O  
ATOM   5009  CB  ARG A 659       8.450 -19.355   7.024  1.00 20.72           C  
ATOM   5010  CG  ARG A 659       9.057 -17.967   6.934  1.00 22.64           C  
ATOM   5011  CD  ARG A 659      10.570 -18.009   7.062  1.00 25.34           C  
ATOM   5012  NE  ARG A 659      11.112 -16.690   7.380  1.00 27.41           N  
ATOM   5013  CZ  ARG A 659      11.579 -16.328   8.574  1.00 28.31           C  
ATOM   5014  NH1 ARG A 659      11.596 -17.190   9.586  1.00 28.72           N  
ATOM   5015  NH2 ARG A 659      12.047 -15.101   8.753  1.00 28.85           N  
ATOM   5016  N   SER A 660       5.987 -21.558   7.295  1.00 20.16           N  
ATOM   5017  CA  SER A 660       5.496 -22.907   6.993  1.00 20.06           C  
ATOM   5018  C   SER A 660       4.064 -22.924   6.442  1.00 19.66           C  
ATOM   5019  O   SER A 660       3.563 -23.979   6.038  1.00 19.75           O  
ATOM   5020  CB  SER A 660       5.605 -23.815   8.222  1.00 20.31           C  
ATOM   5021  OG  SER A 660       4.637 -23.488   9.206  1.00 21.72           O  
ATOM   5022  N   THR A 661       3.417 -21.759   6.415  1.00 18.67           N  
ATOM   5023  CA  THR A 661       2.021 -21.660   5.989  1.00 17.87           C  
ATOM   5024  C   THR A 661       1.871 -20.863   4.695  1.00 17.16           C  
ATOM   5025  O   THR A 661       2.778 -20.135   4.287  1.00 17.01           O  
ATOM   5026  CB  THR A 661       1.144 -20.968   7.064  1.00 17.98           C  
ATOM   5027  OG1 THR A 661       1.566 -19.605   7.210  1.00 17.82           O  
ATOM   5028  CG2 THR A 661       1.231 -21.688   8.412  1.00 18.43           C  
ATOM   5029  N   GLY A 662       0.712 -21.007   4.057  1.00 16.40           N  
ATOM   5030  CA  GLY A 662       0.315 -20.109   2.978  1.00 15.70           C  
ATOM   5031  C   GLY A 662      -0.133 -18.812   3.621  1.00 15.19           C  
ATOM   5032  O   GLY A 662      -0.844 -18.833   4.623  1.00 15.80           O  
ATOM   5033  N   ALA A 663       0.287 -17.683   3.066  1.00 14.33           N  
ATOM   5034  CA  ALA A 663       0.008 -16.400   3.712  1.00 13.78           C  
ATOM   5035  C   ALA A 663      -0.924 -15.527   2.888  1.00 13.37           C  
ATOM   5036  O   ALA A 663      -0.789 -15.452   1.668  1.00 13.84           O  
ATOM   5037  CB  ALA A 663       1.304 -15.666   4.011  1.00 13.92           C  
ATOM   5038  N   SER A 664      -1.875 -14.889   3.572  1.00 12.62           N  
ATOM   5039  CA  SER A 664      -2.758 -13.876   2.989  1.00 12.19           C  
ATOM   5040  C   SER A 664      -2.561 -12.597   3.788  1.00 11.73           C  
ATOM   5041  O   SER A 664      -2.234 -12.657   4.979  1.00 12.17           O  
ATOM   5042  CB  SER A 664      -4.226 -14.308   3.079  1.00 12.52           C  
ATOM   5043  OG  SER A 664      -4.454 -15.524   2.386  1.00 13.75           O  
ATOM   5044  N   PHE A 665      -2.767 -11.447   3.149  1.00 11.02           N  
ATOM   5045  CA  PHE A 665      -2.453 -10.167   3.780  1.00 10.38           C  
ATOM   5046  C   PHE A 665      -3.609  -9.180   3.748  1.00  9.82           C  
ATOM   5047  O   PHE A 665      -4.233  -8.964   2.704  1.00  9.74           O  
ATOM   5048  CB  PHE A 665      -1.219  -9.529   3.128  1.00 10.77           C  
ATOM   5049  CG  PHE A 665       0.039 -10.327   3.300  1.00 11.01           C  
ATOM   5050  CD1 PHE A 665       0.858 -10.121   4.409  1.00 11.85           C  
ATOM   5051  CD2 PHE A 665       0.413 -11.280   2.353  1.00 12.63           C  
ATOM   5052  CE1 PHE A 665       2.026 -10.853   4.578  1.00 13.16           C  
ATOM   5053  CE2 PHE A 665       1.577 -12.028   2.517  1.00 13.04           C  
ATOM   5054  CZ  PHE A 665       2.386 -11.813   3.637  1.00 12.62           C  
ATOM   5055  N   ILE A 666      -3.884  -8.593   4.911  1.00  8.86           N  
ATOM   5056  CA  ILE A 666      -4.813  -7.477   5.030  1.00  8.95           C  
ATOM   5057  C   ILE A 666      -4.005  -6.267   5.510  1.00  8.83           C  
ATOM   5058  O   ILE A 666      -3.384  -6.312   6.581  1.00  8.76           O  
ATOM   5059  CB  ILE A 666      -5.960  -7.790   6.023  1.00  8.26           C  
ATOM   5060  CG1 ILE A 666      -6.739  -9.025   5.552  1.00  8.92           C  
ATOM   5061  CG2 ILE A 666      -6.890  -6.574   6.200  1.00  9.06           C  
ATOM   5062  CD1 ILE A 666      -7.772  -9.519   6.539  1.00  9.72           C  
ATOM   5063  N   ARG A 667      -4.013  -5.207   4.707  1.00  8.58           N  
ATOM   5064  CA  ARG A 667      -3.291  -3.975   5.024  1.00  8.69           C  
ATOM   5065  C   ARG A 667      -4.270  -2.939   5.560  1.00  8.29           C  
ATOM   5066  O   ARG A 667      -5.032  -2.326   4.806  1.00  7.77           O  
ATOM   5067  CB  ARG A 667      -2.514  -3.456   3.798  1.00  8.89           C  
ATOM   5068  CG  ARG A 667      -2.029  -1.996   3.829  1.00 12.46           C  
ATOM   5069  CD  ARG A 667      -1.481  -1.507   5.178  1.00 16.86           C  
ATOM   5070  NE  ARG A 667      -0.346  -2.277   5.682  1.00 19.83           N  
ATOM   5071  CZ  ARG A 667       0.573  -1.787   6.513  1.00 21.46           C  
ATOM   5072  NH1 ARG A 667       0.515  -0.516   6.912  1.00 23.15           N  
ATOM   5073  NH2 ARG A 667       1.570  -2.555   6.921  1.00 20.62           N  
ATOM   5074  N   CYS A 668      -4.250  -2.758   6.875  1.00  7.78           N  
ATOM   5075  CA  CYS A 668      -5.126  -1.780   7.508  1.00  7.99           C  
ATOM   5076  C   CYS A 668      -4.496  -0.399   7.453  1.00  7.78           C  
ATOM   5077  O   CYS A 668      -3.292  -0.240   7.698  1.00  8.04           O  
ATOM   5078  CB  CYS A 668      -5.432  -2.152   8.956  1.00  7.73           C  
ATOM   5079  SG  CYS A 668      -6.351  -3.677   9.116  1.00  9.95           S  
ATOM   5080  N   ILE A 669      -5.341   0.583   7.156  1.00  7.73           N  
ATOM   5081  CA  ILE A 669      -4.934   1.974   6.967  1.00  8.34           C  
ATOM   5082  C   ILE A 669      -5.690   2.893   7.923  1.00  8.22           C  
ATOM   5083  O   ILE A 669      -6.920   2.817   8.025  1.00  7.87           O  
ATOM   5084  CB  ILE A 669      -5.226   2.435   5.514  1.00  8.32           C  
ATOM   5085  CG1 ILE A 669      -4.478   1.571   4.485  1.00  9.70           C  
ATOM   5086  CG2 ILE A 669      -4.957   3.940   5.350  1.00  8.60           C  
ATOM   5087  CD1 ILE A 669      -2.966   1.692   4.497  1.00 11.16           C  
ATOM   5088  N   LYS A 670      -4.955   3.760   8.619  1.00  8.50           N  
ATOM   5089  CA  LYS A 670      -5.573   4.730   9.528  1.00  8.98           C  
ATOM   5090  C   LYS A 670      -5.789   6.074   8.813  1.00  9.17           C  
ATOM   5091  O   LYS A 670      -4.824   6.688   8.341  1.00  9.10           O  
ATOM   5092  CB  LYS A 670      -4.725   4.906  10.790  1.00  9.09           C  
ATOM   5093  CG  LYS A 670      -5.393   5.764  11.866  1.00  9.19           C  
ATOM   5094  CD  LYS A 670      -4.617   5.741  13.197  1.00  9.97           C  
ATOM   5095  CE  LYS A 670      -3.285   6.463  13.096  1.00 12.45           C  
ATOM   5096  NZ  LYS A 670      -2.532   6.387  14.386  1.00 13.39           N  
ATOM   5097  N   PRO A 671      -7.058   6.526   8.718  1.00  9.13           N  
ATOM   5098  CA  PRO A 671      -7.377   7.663   7.840  1.00  9.37           C  
ATOM   5099  C   PRO A 671      -6.959   9.038   8.359  1.00  9.72           C  
ATOM   5100  O   PRO A 671      -6.813   9.967   7.565  1.00  9.69           O  
ATOM   5101  CB  PRO A 671      -8.902   7.588   7.719  1.00  9.50           C  
ATOM   5102  CG  PRO A 671      -9.341   7.005   9.028  1.00  9.18           C  
ATOM   5103  CD  PRO A 671      -8.268   5.984   9.369  1.00  9.19           C  
ATOM   5104  N   ASN A 672      -6.777   9.164   9.672  1.00  9.93           N  
ATOM   5105  CA  ASN A 672      -6.449  10.448  10.302  1.00 10.44           C  
ATOM   5106  C   ASN A 672      -5.978  10.207  11.730  1.00 11.03           C  
ATOM   5107  O   ASN A 672      -6.029   9.079  12.222  1.00 10.33           O  
ATOM   5108  CB  ASN A 672      -7.659  11.393  10.283  1.00 10.33           C  
ATOM   5109  CG  ASN A 672      -8.842  10.844  11.060  1.00  9.99           C  
ATOM   5110  OD1 ASN A 672      -8.838  10.840  12.294  1.00 11.29           O  
ATOM   5111  ND2 ASN A 672      -9.867  10.391  10.343  1.00 10.58           N  
ATOM   5112  N   LEU A 673      -5.530  11.270  12.392  1.00 12.12           N  
ATOM   5113  CA  LEU A 673      -4.973  11.150  13.737  1.00 13.54           C  
ATOM   5114  C   LEU A 673      -5.956  11.580  14.833  1.00 14.17           C  
ATOM   5115  O   LEU A 673      -5.565  11.729  15.998  1.00 14.91           O  
ATOM   5116  CB  LEU A 673      -3.662  11.944  13.833  1.00 14.01           C  
ATOM   5117  CG  LEU A 673      -2.549  11.574  12.837  1.00 14.91           C  
ATOM   5118  CD1 LEU A 673      -1.328  12.462  13.054  1.00 17.64           C  
ATOM   5119  CD2 LEU A 673      -2.161  10.098  12.936  1.00 17.01           C  
ATOM   5120  N   LYS A 674      -7.224  11.750  14.460  1.00 14.26           N  
ATOM   5121  CA  LYS A 674      -8.251  12.293  15.361  1.00 15.14           C  
ATOM   5122  C   LYS A 674      -9.393  11.324  15.695  1.00 14.58           C  
ATOM   5123  O   LYS A 674     -10.364  11.704  16.366  1.00 14.30           O  
ATOM   5124  CB  LYS A 674      -8.820  13.595  14.784  1.00 15.30           C  
ATOM   5125  CG  LYS A 674      -7.767  14.653  14.481  1.00 16.17           C  
ATOM   5126  CD  LYS A 674      -8.365  15.873  13.784  1.00 17.54           C  
ATOM   5127  CE  LYS A 674      -8.764  16.958  14.770  1.00 21.43           C  
ATOM   5128  NZ  LYS A 674      -9.214  18.199  14.069  1.00 23.98           N  
ATOM   5129  N   MET A 675      -9.273  10.078  15.234  1.00 14.12           N  
ATOM   5130  CA  MET A 675     -10.301   9.039  15.449  1.00 14.19           C  
ATOM   5131  C   MET A 675     -11.683   9.448  14.934  1.00 13.94           C  
ATOM   5132  O   MET A 675     -12.709   9.085  15.516  1.00 14.23           O  
ATOM   5133  CB  MET A 675     -10.393   8.652  16.930  1.00 14.27           C  
ATOM   5134  CG  MET A 675      -9.067   8.286  17.557  1.00 14.22           C  
ATOM   5135  SD  MET A 675      -9.280   7.919  19.305  1.00 15.37           S  
ATOM   5136  CE  MET A 675      -7.576   7.627  19.747  1.00 15.36           C  
ATOM   5137  N   THR A 676     -11.700  10.215  13.851  1.00 13.81           N  
ATOM   5138  CA  THR A 676     -12.944  10.731  13.293  1.00 13.99           C  
ATOM   5139  C   THR A 676     -13.349   9.964  12.037  1.00 14.08           C  
ATOM   5140  O   THR A 676     -12.488   9.450  11.311  1.00 13.33           O  
ATOM   5141  CB  THR A 676     -12.827  12.228  12.960  1.00 14.25           C  
ATOM   5142  OG1 THR A 676     -11.717  12.437  12.081  1.00 14.37           O  
ATOM   5143  CG2 THR A 676     -12.616  13.047  14.229  1.00 14.14           C  
ATOM   5144  N   SER A 677     -14.657   9.897  11.793  1.00 13.88           N  
ATOM   5145  CA  SER A 677     -15.199   9.306  10.567  1.00 14.09           C  
ATOM   5146  C   SER A 677     -15.227  10.331   9.429  1.00 14.25           C  
ATOM   5147  O   SER A 677     -15.257  11.537   9.676  1.00 14.38           O  
ATOM   5148  CB  SER A 677     -16.607   8.750  10.815  1.00 14.12           C  
ATOM   5149  OG  SER A 677     -17.483   9.766  11.289  1.00 14.38           O  
ATOM   5150  N   HIS A 678     -15.220   9.833   8.192  1.00 14.50           N  
ATOM   5151  CA  HIS A 678     -15.272  10.663   6.977  1.00 15.09           C  
ATOM   5152  C   HIS A 678     -14.281  11.826   6.980  1.00 14.82           C  
ATOM   5153  O   HIS A 678     -14.630  12.955   6.617  1.00 14.86           O  
ATOM   5154  CB  HIS A 678     -16.702  11.155   6.719  1.00 15.53           C  
ATOM   5155  CG  HIS A 678     -17.718  10.057   6.694  1.00 17.18           C  
ATOM   5156  ND1 HIS A 678     -17.736   9.082   5.720  1.00 19.72           N  
ATOM   5157  CD2 HIS A 678     -18.741   9.771   7.531  1.00 18.35           C  
ATOM   5158  CE1 HIS A 678     -18.734   8.249   5.954  1.00 18.92           C  
ATOM   5159  NE2 HIS A 678     -19.355   8.641   7.051  1.00 19.74           N  
ATOM   5160  N   HIS A 679     -13.053  11.535   7.406  1.00 14.36           N  
ATOM   5161  CA  HIS A 679     -11.943  12.478   7.358  1.00 14.51           C  
ATOM   5162  C   HIS A 679     -10.730  11.774   6.758  1.00 13.95           C  
ATOM   5163  O   HIS A 679      -9.831  11.335   7.473  1.00 13.51           O  
ATOM   5164  CB  HIS A 679     -11.638  13.043   8.749  1.00 15.05           C  
ATOM   5165  CG  HIS A 679     -12.515  14.191   9.136  1.00 17.80           C  
ATOM   5166  ND1 HIS A 679     -12.226  15.495   8.793  1.00 20.39           N  
ATOM   5167  CD2 HIS A 679     -13.679  14.233   9.827  1.00 19.95           C  
ATOM   5168  CE1 HIS A 679     -13.171  16.291   9.262  1.00 20.79           C  
ATOM   5169  NE2 HIS A 679     -14.064  15.551   9.894  1.00 21.29           N  
ATOM   5170  N   PHE A 680     -10.745  11.653   5.433  1.00 12.86           N  
ATOM   5171  CA  PHE A 680      -9.697  10.985   4.664  1.00 12.56           C  
ATOM   5172  C   PHE A 680      -8.515  11.942   4.504  1.00 12.49           C  
ATOM   5173  O   PHE A 680      -8.600  12.915   3.745  1.00 12.75           O  
ATOM   5174  CB  PHE A 680     -10.286  10.595   3.300  1.00 12.24           C  
ATOM   5175  CG  PHE A 680      -9.402   9.719   2.455  1.00 11.48           C  
ATOM   5176  CD1 PHE A 680      -9.607   8.338   2.410  1.00 10.98           C  
ATOM   5177  CD2 PHE A 680      -8.403  10.274   1.658  1.00 10.84           C  
ATOM   5178  CE1 PHE A 680      -8.804   7.529   1.606  1.00 11.32           C  
ATOM   5179  CE2 PHE A 680      -7.592   9.471   0.847  1.00 10.63           C  
ATOM   5180  CZ  PHE A 680      -7.794   8.096   0.822  1.00 11.11           C  
ATOM   5181  N   GLU A 681      -7.429  11.690   5.239  1.00 12.12           N  
ATOM   5182  CA  GLU A 681      -6.225  12.524   5.135  1.00 11.89           C  
ATOM   5183  C   GLU A 681      -5.301  11.966   4.058  1.00 11.28           C  
ATOM   5184  O   GLU A 681      -4.542  11.023   4.297  1.00 10.78           O  
ATOM   5185  CB  GLU A 681      -5.505  12.652   6.482  1.00 12.22           C  
ATOM   5186  CG  GLU A 681      -6.265  13.477   7.526  1.00 13.94           C  
ATOM   5187  CD  GLU A 681      -6.256  14.981   7.248  1.00 17.91           C  
ATOM   5188  OE1 GLU A 681      -7.074  15.698   7.867  1.00 20.52           O  
ATOM   5189  OE2 GLU A 681      -5.442  15.451   6.423  1.00 18.95           O  
ATOM   5190  N   GLY A 682      -5.398  12.551   2.864  1.00 11.09           N  
ATOM   5191  CA  GLY A 682      -4.723  12.031   1.678  1.00 11.00           C  
ATOM   5192  C   GLY A 682      -3.242  11.757   1.811  1.00 10.95           C  
ATOM   5193  O   GLY A 682      -2.779  10.664   1.465  1.00 10.66           O  
ATOM   5194  N   ALA A 683      -2.497  12.749   2.303  1.00 10.58           N  
ATOM   5195  CA  ALA A 683      -1.048  12.625   2.450  1.00 10.64           C  
ATOM   5196  C   ALA A 683      -0.686  11.531   3.459  1.00 10.22           C  
ATOM   5197  O   ALA A 683       0.214  10.727   3.212  1.00 10.43           O  
ATOM   5198  CB  ALA A 683      -0.427  13.969   2.845  1.00 10.38           C  
ATOM   5199  N   GLN A 684      -1.412  11.498   4.576  1.00 10.19           N  
ATOM   5200  CA  GLN A 684      -1.227  10.480   5.612  1.00 10.48           C  
ATOM   5201  C   GLN A 684      -1.452   9.068   5.077  1.00 10.11           C  
ATOM   5202  O   GLN A 684      -0.666   8.152   5.356  1.00 10.19           O  
ATOM   5203  CB  GLN A 684      -2.162  10.747   6.791  1.00 10.34           C  
ATOM   5204  CG  GLN A 684      -1.788  11.993   7.598  1.00 11.18           C  
ATOM   5205  CD  GLN A 684      -2.788  12.325   8.698  1.00 11.13           C  
ATOM   5206  OE1 GLN A 684      -2.934  13.491   9.086  1.00 13.33           O  
ATOM   5207  NE2 GLN A 684      -3.476  11.311   9.209  1.00 10.86           N  
ATOM   5208  N   ILE A 685      -2.522   8.905   4.301  1.00  9.60           N  
ATOM   5209  CA  ILE A 685      -2.883   7.605   3.731  1.00  9.30           C  
ATOM   5210  C   ILE A 685      -1.898   7.200   2.635  1.00  9.42           C  
ATOM   5211  O   ILE A 685      -1.457   6.052   2.590  1.00  9.14           O  
ATOM   5212  CB  ILE A 685      -4.355   7.594   3.246  1.00  8.98           C  
ATOM   5213  CG1 ILE A 685      -5.281   7.668   4.466  1.00  9.31           C  
ATOM   5214  CG2 ILE A 685      -4.667   6.341   2.394  1.00  9.13           C  
ATOM   5215  CD1 ILE A 685      -6.693   8.022   4.157  1.00  9.80           C  
ATOM   5216  N   LEU A 686      -1.529   8.153   1.780  1.00  9.59           N  
ATOM   5217  CA  LEU A 686      -0.502   7.897   0.762  1.00 10.01           C  
ATOM   5218  C   LEU A 686       0.796   7.364   1.370  1.00 10.00           C  
ATOM   5219  O   LEU A 686       1.385   6.424   0.838  1.00  9.39           O  
ATOM   5220  CB  LEU A 686      -0.208   9.150  -0.068  1.00 10.19           C  
ATOM   5221  CG  LEU A 686       0.861   9.015  -1.162  1.00  9.96           C  
ATOM   5222  CD1 LEU A 686       0.499   7.963  -2.226  1.00 11.99           C  
ATOM   5223  CD2 LEU A 686       1.131  10.374  -1.808  1.00 10.58           C  
ATOM   5224  N   SER A 687       1.231   7.974   2.475  1.00 10.55           N  
ATOM   5225  CA  SER A 687       2.439   7.557   3.180  1.00 11.18           C  
ATOM   5226  C   SER A 687       2.369   6.090   3.600  1.00 10.96           C  
ATOM   5227  O   SER A 687       3.340   5.343   3.440  1.00 11.29           O  
ATOM   5228  CB  SER A 687       2.691   8.448   4.402  1.00 11.53           C  
ATOM   5229  OG  SER A 687       3.938   8.124   4.996  1.00 13.73           O  
ATOM   5230  N   GLN A 688       1.213   5.685   4.123  1.00 10.73           N  
ATOM   5231  CA  GLN A 688       0.985   4.299   4.517  1.00 10.44           C  
ATOM   5232  C   GLN A 688       0.982   3.353   3.314  1.00 10.55           C  
ATOM   5233  O   GLN A 688       1.537   2.263   3.386  1.00 10.47           O  
ATOM   5234  CB  GLN A 688      -0.324   4.172   5.299  1.00 10.36           C  
ATOM   5235  CG  GLN A 688      -0.267   4.810   6.677  1.00 10.12           C  
ATOM   5236  CD  GLN A 688      -1.636   4.919   7.288  1.00 10.40           C  
ATOM   5237  OE1 GLN A 688      -2.181   3.933   7.792  1.00 10.11           O  
ATOM   5238  NE2 GLN A 688      -2.218   6.112   7.227  1.00  8.69           N  
ATOM   5239  N   LEU A 689       0.375   3.778   2.209  1.00 10.48           N  
ATOM   5240  CA  LEU A 689       0.317   2.936   1.015  1.00 10.74           C  
ATOM   5241  C   LEU A 689       1.724   2.708   0.465  1.00 10.91           C  
ATOM   5242  O   LEU A 689       2.045   1.628  -0.033  1.00 10.89           O  
ATOM   5243  CB  LEU A 689      -0.603   3.551  -0.047  1.00 10.50           C  
ATOM   5244  CG  LEU A 689      -2.102   3.643   0.266  1.00 11.03           C  
ATOM   5245  CD1 LEU A 689      -2.799   4.517  -0.778  1.00 11.42           C  
ATOM   5246  CD2 LEU A 689      -2.778   2.259   0.349  1.00 11.39           C  
ATOM   5247  N   GLN A 690       2.565   3.733   0.589  1.00 11.42           N  
ATOM   5248  CA  GLN A 690       3.960   3.650   0.177  1.00 12.24           C  
ATOM   5249  C   GLN A 690       4.795   2.736   1.081  1.00 12.55           C  
ATOM   5250  O   GLN A 690       5.366   1.752   0.604  1.00 12.36           O  
ATOM   5251  CB  GLN A 690       4.579   5.049   0.092  1.00 11.93           C  
ATOM   5252  CG  GLN A 690       4.015   5.918  -1.029  1.00 12.66           C  
ATOM   5253  CD  GLN A 690       4.436   7.373  -0.894  1.00 13.46           C  
ATOM   5254  OE1 GLN A 690       4.784   7.828   0.198  1.00 16.00           O  
ATOM   5255  NE2 GLN A 690       4.393   8.113  -2.001  1.00 15.46           N  
ATOM   5256  N   CYS A 691       4.855   3.036   2.382  1.00 12.81           N  
ATOM   5257  CA  CYS A 691       5.743   2.279   3.268  1.00 13.40           C  
ATOM   5258  C   CYS A 691       5.287   0.840   3.520  1.00 12.90           C  
ATOM   5259  O   CYS A 691       6.104  -0.021   3.844  1.00 13.48           O  
ATOM   5260  CB  CYS A 691       6.018   3.019   4.579  1.00 13.40           C  
ATOM   5261  SG  CYS A 691       4.648   3.097   5.695  1.00 15.68           S  
ATOM   5262  N   SER A 692       3.994   0.574   3.343  1.00 12.69           N  
ATOM   5263  CA  SER A 692       3.464  -0.782   3.494  1.00 12.20           C  
ATOM   5264  C   SER A 692       3.850  -1.671   2.312  1.00 12.27           C  
ATOM   5265  O   SER A 692       3.716  -2.894   2.380  1.00 11.59           O  
ATOM   5266  CB  SER A 692       1.941  -0.755   3.618  1.00 12.39           C  
ATOM   5267  OG  SER A 692       1.340  -0.336   2.403  1.00 11.97           O  
ATOM   5268  N   GLY A 693       4.303  -1.043   1.229  1.00 12.05           N  
ATOM   5269  CA  GLY A 693       4.685  -1.763   0.020  1.00 12.48           C  
ATOM   5270  C   GLY A 693       3.572  -1.902  -1.006  1.00 12.76           C  
ATOM   5271  O   GLY A 693       3.776  -2.509  -2.062  1.00 12.78           O  
ATOM   5272  N   MET A 694       2.403  -1.334  -0.714  1.00 12.72           N  
ATOM   5273  CA  MET A 694       1.241  -1.472  -1.609  1.00 13.19           C  
ATOM   5274  C   MET A 694       1.444  -0.821  -2.977  1.00 12.87           C  
ATOM   5275  O   MET A 694       0.956  -1.333  -3.991  1.00 12.68           O  
ATOM   5276  CB  MET A 694      -0.055  -0.980  -0.954  1.00 13.76           C  
ATOM   5277  CG  MET A 694      -0.623  -1.919   0.131  1.00 15.62           C  
ATOM   5278  SD  MET A 694      -0.469  -3.692  -0.202  1.00 20.79           S  
ATOM   5279  CE  MET A 694      -1.550  -3.892  -1.617  1.00 20.35           C  
ATOM   5280  N   VAL A 695       2.161   0.301  -3.008  1.00 12.59           N  
ATOM   5281  CA  VAL A 695       2.480   0.958  -4.281  1.00 12.82           C  
ATOM   5282  C   VAL A 695       3.416   0.070  -5.115  1.00 12.96           C  
ATOM   5283  O   VAL A 695       3.225  -0.074  -6.334  1.00 13.23           O  
ATOM   5284  CB  VAL A 695       3.042   2.387  -4.069  1.00 12.58           C  
ATOM   5285  CG1 VAL A 695       3.536   3.000  -5.397  1.00 13.05           C  
ATOM   5286  CG2 VAL A 695       1.964   3.274  -3.453  1.00 11.95           C  
ATOM   5287  N   SER A 696       4.398  -0.548  -4.455  1.00 13.06           N  
ATOM   5288  CA  SER A 696       5.301  -1.494  -5.120  1.00 13.64           C  
ATOM   5289  C   SER A 696       4.557  -2.714  -5.665  1.00 13.89           C  
ATOM   5290  O   SER A 696       4.819  -3.157  -6.783  1.00 14.14           O  
ATOM   5291  CB  SER A 696       6.417  -1.942  -4.181  1.00 13.58           C  
ATOM   5292  OG  SER A 696       7.262  -0.856  -3.842  1.00 13.74           O  
ATOM   5293  N   VAL A 697       3.633  -3.250  -4.870  1.00 13.96           N  
ATOM   5294  CA  VAL A 697       2.844  -4.415  -5.273  1.00 14.53           C  
ATOM   5295  C   VAL A 697       1.954  -4.100  -6.473  1.00 14.70           C  
ATOM   5296  O   VAL A 697       1.843  -4.913  -7.398  1.00 14.68           O  
ATOM   5297  CB  VAL A 697       2.006  -4.961  -4.096  1.00 14.55           C  
ATOM   5298  CG1 VAL A 697       0.965  -5.980  -4.579  1.00 15.44           C  
ATOM   5299  CG2 VAL A 697       2.929  -5.570  -3.057  1.00 15.10           C  
ATOM   5300  N   LEU A 698       1.337  -2.918  -6.463  1.00 15.02           N  
ATOM   5301  CA  LEU A 698       0.481  -2.496  -7.574  1.00 15.46           C  
ATOM   5302  C   LEU A 698       1.293  -2.402  -8.864  1.00 16.02           C  
ATOM   5303  O   LEU A 698       0.823  -2.808  -9.928  1.00 16.50           O  
ATOM   5304  CB  LEU A 698      -0.219  -1.167  -7.268  1.00 15.41           C  
ATOM   5305  CG  LEU A 698      -1.299  -0.713  -8.263  1.00 15.15           C  
ATOM   5306  CD1 LEU A 698      -2.527  -1.632  -8.249  1.00 16.16           C  
ATOM   5307  CD2 LEU A 698      -1.697   0.730  -7.990  1.00 15.51           C  
ATOM   5308  N   ASP A 699       2.513  -1.882  -8.748  1.00 16.53           N  
ATOM   5309  CA  ASP A 699       3.458  -1.794  -9.864  1.00 17.32           C  
ATOM   5310  C   ASP A 699       3.720  -3.188 -10.437  1.00 17.60           C  
ATOM   5311  O   ASP A 699       3.620  -3.398 -11.652  1.00 17.84           O  
ATOM   5312  CB  ASP A 699       4.759  -1.133  -9.386  1.00 17.26           C  
ATOM   5313  CG  ASP A 699       5.740  -0.832 -10.513  1.00 18.54           C  
ATOM   5314  OD1 ASP A 699       6.817  -0.282 -10.202  1.00 20.00           O  
ATOM   5315  OD2 ASP A 699       5.462  -1.134 -11.692  1.00 19.78           O  
ATOM   5316  N   LEU A 700       4.025  -4.137  -9.558  1.00 18.37           N  
ATOM   5317  CA  LEU A 700       4.307  -5.510  -9.966  1.00 19.08           C  
ATOM   5318  C   LEU A 700       3.102  -6.172 -10.640  1.00 19.97           C  
ATOM   5319  O   LEU A 700       3.265  -6.927 -11.605  1.00 19.52           O  
ATOM   5320  CB  LEU A 700       4.782  -6.339  -8.773  1.00 19.08           C  
ATOM   5321  CG  LEU A 700       5.269  -7.769  -9.030  1.00 18.92           C  
ATOM   5322  CD1 LEU A 700       6.406  -7.809 -10.060  1.00 18.57           C  
ATOM   5323  CD2 LEU A 700       5.696  -8.410  -7.721  1.00 18.98           C  
ATOM   5324  N   MET A 701       1.905  -5.870 -10.134  1.00 20.66           N  
ATOM   5325  CA  MET A 701       0.653  -6.418 -10.673  1.00 21.71           C  
ATOM   5326  C   MET A 701       0.290  -5.950 -12.083  1.00 21.90           C  
ATOM   5327  O   MET A 701      -0.552  -6.569 -12.740  1.00 22.17           O  
ATOM   5328  CB  MET A 701      -0.525  -6.168  -9.720  1.00 22.27           C  
ATOM   5329  CG  MET A 701      -0.651  -7.137  -8.526  1.00 24.38           C  
ATOM   5330  SD  MET A 701      -0.360  -8.920  -8.781  1.00 29.62           S  
ATOM   5331  CE  MET A 701      -0.930  -9.207 -10.445  1.00 29.50           C  
ATOM   5332  N   GLN A 702       0.920  -4.871 -12.555  1.00 21.96           N  
ATOM   5333  CA  GLN A 702       0.730  -4.421 -13.941  1.00 21.92           C  
ATOM   5334  C   GLN A 702       0.971  -5.569 -14.919  1.00 21.73           C  
ATOM   5335  O   GLN A 702       0.287  -5.678 -15.945  1.00 22.07           O  
ATOM   5336  CB  GLN A 702       1.653  -3.249 -14.276  1.00 21.59           C  
ATOM   5337  CG  GLN A 702       1.162  -1.906 -13.761  1.00 22.06           C  
ATOM   5338  CD  GLN A 702       2.065  -0.758 -14.171  1.00 22.21           C  
ATOM   5339  OE1 GLN A 702       1.636   0.171 -14.865  1.00 23.08           O  
ATOM   5340  NE2 GLN A 702       3.325  -0.817 -13.751  1.00 21.16           N  
ATOM   5341  N   GLY A 703       1.935  -6.425 -14.584  1.00 21.32           N  
ATOM   5342  CA  GLY A 703       2.263  -7.589 -15.403  1.00 20.84           C  
ATOM   5343  C   GLY A 703       2.421  -8.896 -14.646  1.00 20.28           C  
ATOM   5344  O   GLY A 703       2.978  -9.853 -15.181  1.00 20.67           O  
ATOM   5345  N   GLY A 704       1.924  -8.949 -13.411  1.00 19.53           N  
ATOM   5346  CA  GLY A 704       2.051 -10.149 -12.581  1.00 18.67           C  
ATOM   5347  C   GLY A 704       0.895 -11.137 -12.674  1.00 18.08           C  
ATOM   5348  O   GLY A 704      -0.080 -10.908 -13.395  1.00 17.78           O  
ATOM   5349  N   PHE A 705       1.010 -12.236 -11.931  1.00 17.50           N  
ATOM   5350  CA  PHE A 705       0.066 -13.354 -12.021  1.00 17.48           C  
ATOM   5351  C   PHE A 705      -0.162 -13.968 -10.639  1.00 17.36           C  
ATOM   5352  O   PHE A 705       0.631 -14.805 -10.200  1.00 17.41           O  
ATOM   5353  CB  PHE A 705       0.605 -14.443 -12.959  1.00 17.54           C  
ATOM   5354  CG  PHE A 705       0.903 -13.972 -14.358  1.00 17.80           C  
ATOM   5355  CD1 PHE A 705       2.163 -13.469 -14.686  1.00 18.10           C  
ATOM   5356  CD2 PHE A 705      -0.066 -14.065 -15.360  1.00 17.76           C  
ATOM   5357  CE1 PHE A 705       2.449 -13.042 -15.985  1.00 18.23           C  
ATOM   5358  CE2 PHE A 705       0.213 -13.649 -16.665  1.00 17.77           C  
ATOM   5359  CZ  PHE A 705       1.476 -13.134 -16.975  1.00 18.47           C  
ATOM   5360  N   PRO A 706      -1.243 -13.561  -9.947  1.00 17.24           N  
ATOM   5361  CA  PRO A 706      -1.446 -14.018  -8.563  1.00 17.34           C  
ATOM   5362  C   PRO A 706      -1.883 -15.481  -8.420  1.00 17.29           C  
ATOM   5363  O   PRO A 706      -1.724 -16.063  -7.342  1.00 17.73           O  
ATOM   5364  CB  PRO A 706      -2.527 -13.066  -8.034  1.00 17.63           C  
ATOM   5365  CG  PRO A 706      -3.269 -12.613  -9.235  1.00 17.26           C  
ATOM   5366  CD  PRO A 706      -2.312 -12.650 -10.398  1.00 17.27           C  
ATOM   5367  N   SER A 707      -2.415 -16.070  -9.491  1.00 17.05           N  
ATOM   5368  CA  SER A 707      -2.862 -17.467  -9.472  1.00 16.97           C  
ATOM   5369  C   SER A 707      -2.008 -18.338 -10.389  1.00 16.91           C  
ATOM   5370  O   SER A 707      -1.646 -17.913 -11.485  1.00 16.91           O  
ATOM   5371  CB  SER A 707      -4.327 -17.565  -9.903  1.00 16.98           C  
ATOM   5372  OG  SER A 707      -5.174 -16.874  -9.003  1.00 17.50           O  
ATOM   5373  N   ARG A 708      -1.686 -19.549  -9.933  1.00 16.94           N  
ATOM   5374  CA  ARG A 708      -0.900 -20.500 -10.732  1.00 17.25           C  
ATOM   5375  C   ARG A 708      -1.014 -21.942 -10.263  1.00 17.34           C  
ATOM   5376  O   ARG A 708      -1.283 -22.210  -9.092  1.00 17.20           O  
ATOM   5377  CB  ARG A 708       0.583 -20.104 -10.795  1.00 17.20           C  
ATOM   5378  CG  ARG A 708       1.273 -19.922  -9.453  1.00 17.99           C  
ATOM   5379  CD  ARG A 708       1.147 -18.483  -8.994  1.00 18.57           C  
ATOM   5380  NE  ARG A 708       1.832 -18.231  -7.733  1.00 19.53           N  
ATOM   5381  CZ  ARG A 708       2.148 -17.017  -7.296  1.00 18.56           C  
ATOM   5382  NH1 ARG A 708       2.775 -16.871  -6.135  1.00 20.14           N  
ATOM   5383  NH2 ARG A 708       1.843 -15.952  -8.022  1.00 19.29           N  
ATOM   5384  N   ALA A 709      -0.795 -22.861 -11.200  1.00 17.66           N  
ATOM   5385  CA  ALA A 709      -0.737 -24.290 -10.912  1.00 18.16           C  
ATOM   5386  C   ALA A 709       0.153 -24.984 -11.938  1.00 18.52           C  
ATOM   5387  O   ALA A 709       0.347 -24.476 -13.041  1.00 18.74           O  
ATOM   5388  CB  ALA A 709      -2.140 -24.894 -10.934  1.00 18.12           C  
ATOM   5389  N   SER A 710       0.698 -26.137 -11.566  1.00 19.01           N  
ATOM   5390  CA  SER A 710       1.419 -26.988 -12.513  1.00 19.38           C  
ATOM   5391  C   SER A 710       0.465 -27.453 -13.609  1.00 19.54           C  
ATOM   5392  O   SER A 710      -0.589 -28.021 -13.311  1.00 19.53           O  
ATOM   5393  CB  SER A 710       2.008 -28.198 -11.791  1.00 19.27           C  
ATOM   5394  OG  SER A 710       2.230 -29.271 -12.693  1.00 19.58           O  
ATOM   5395  N   PHE A 711       0.821 -27.212 -14.870  1.00 20.06           N  
ATOM   5396  CA  PHE A 711      -0.046 -27.642 -15.970  1.00 20.81           C  
ATOM   5397  C   PHE A 711      -0.010 -29.158 -16.196  1.00 21.17           C  
ATOM   5398  O   PHE A 711      -0.962 -29.725 -16.723  1.00 21.44           O  
ATOM   5399  CB  PHE A 711       0.191 -26.851 -17.272  1.00 20.79           C  
ATOM   5400  CG  PHE A 711       1.620 -26.836 -17.750  1.00 21.28           C  
ATOM   5401  CD1 PHE A 711       2.178 -27.952 -18.377  1.00 21.73           C  
ATOM   5402  CD2 PHE A 711       2.393 -25.684 -17.623  1.00 20.52           C  
ATOM   5403  CE1 PHE A 711       3.493 -27.929 -18.834  1.00 21.96           C  
ATOM   5404  CE2 PHE A 711       3.713 -25.652 -18.081  1.00 21.67           C  
ATOM   5405  CZ  PHE A 711       4.262 -26.778 -18.688  1.00 21.60           C  
ATOM   5406  N   HIS A 712       1.078 -29.807 -15.787  1.00 21.78           N  
ATOM   5407  CA  HIS A 712       1.135 -31.272 -15.815  1.00 22.33           C  
ATOM   5408  C   HIS A 712       0.185 -31.877 -14.785  1.00 22.33           C  
ATOM   5409  O   HIS A 712      -0.502 -32.855 -15.075  1.00 22.01           O  
ATOM   5410  CB  HIS A 712       2.561 -31.791 -15.609  1.00 22.76           C  
ATOM   5411  CG  HIS A 712       3.411 -31.716 -16.839  1.00 24.21           C  
ATOM   5412  ND1 HIS A 712       4.469 -30.841 -16.960  1.00 26.35           N  
ATOM   5413  CD2 HIS A 712       3.357 -32.404 -18.004  1.00 25.68           C  
ATOM   5414  CE1 HIS A 712       5.032 -30.995 -18.145  1.00 26.57           C  
ATOM   5415  NE2 HIS A 712       4.375 -31.936 -18.799  1.00 26.55           N  
ATOM   5416  N   GLU A 713       0.140 -31.287 -13.590  1.00 22.43           N  
ATOM   5417  CA  GLU A 713      -0.779 -31.742 -12.544  1.00 22.90           C  
ATOM   5418  C   GLU A 713      -2.242 -31.518 -12.927  1.00 22.47           C  
ATOM   5419  O   GLU A 713      -3.099 -32.363 -12.642  1.00 22.39           O  
ATOM   5420  CB  GLU A 713      -0.461 -31.076 -11.206  1.00 22.85           C  
ATOM   5421  CG  GLU A 713       0.854 -31.544 -10.592  1.00 23.98           C  
ATOM   5422  CD  GLU A 713       1.201 -30.822  -9.302  1.00 24.42           C  
ATOM   5423  OE1 GLU A 713       0.353 -30.061  -8.783  1.00 26.90           O  
ATOM   5424  OE2 GLU A 713       2.330 -31.024  -8.804  1.00 27.56           O  
ATOM   5425  N   LEU A 714      -2.524 -30.389 -13.576  1.00 22.20           N  
ATOM   5426  CA  LEU A 714      -3.870 -30.110 -14.087  1.00 22.04           C  
ATOM   5427  C   LEU A 714      -4.300 -31.162 -15.109  1.00 21.95           C  
ATOM   5428  O   LEU A 714      -5.373 -31.755 -14.987  1.00 21.79           O  
ATOM   5429  CB  LEU A 714      -3.951 -28.706 -14.693  1.00 21.85           C  
ATOM   5430  CG  LEU A 714      -4.048 -27.518 -13.731  1.00 21.86           C  
ATOM   5431  CD1 LEU A 714      -4.028 -26.216 -14.517  1.00 21.48           C  
ATOM   5432  CD2 LEU A 714      -5.299 -27.592 -12.839  1.00 21.11           C  
ATOM   5433  N   TYR A 715      -3.446 -31.401 -16.101  1.00 21.97           N  
ATOM   5434  CA  TYR A 715      -3.679 -32.439 -17.100  1.00 22.05           C  
ATOM   5435  C   TYR A 715      -3.905 -33.795 -16.430  1.00 21.97           C  
ATOM   5436  O   TYR A 715      -4.867 -34.488 -16.757  1.00 21.68           O  
ATOM   5437  CB  TYR A 715      -2.511 -32.494 -18.088  1.00 22.32           C  
ATOM   5438  CG  TYR A 715      -2.540 -33.654 -19.063  1.00 23.15           C  
ATOM   5439  CD1 TYR A 715      -2.031 -34.903 -18.705  1.00 23.74           C  
ATOM   5440  CD2 TYR A 715      -3.052 -33.495 -20.349  1.00 23.66           C  
ATOM   5441  CE1 TYR A 715      -2.043 -35.971 -19.599  1.00 24.25           C  
ATOM   5442  CE2 TYR A 715      -3.064 -34.558 -21.255  1.00 24.44           C  
ATOM   5443  CZ  TYR A 715      -2.560 -35.789 -20.871  1.00 23.82           C  
ATOM   5444  OH  TYR A 715      -2.572 -36.846 -21.756  1.00 24.23           O  
ATOM   5445  N   ASN A 716      -3.027 -34.152 -15.488  1.00 22.00           N  
ATOM   5446  CA  ASN A 716      -3.132 -35.409 -14.738  1.00 22.28           C  
ATOM   5447  C   ASN A 716      -4.474 -35.571 -14.030  1.00 22.07           C  
ATOM   5448  O   ASN A 716      -5.008 -36.677 -13.942  1.00 21.99           O  
ATOM   5449  CB  ASN A 716      -2.004 -35.530 -13.706  1.00 22.42           C  
ATOM   5450  CG  ASN A 716      -0.651 -35.875 -14.328  1.00 23.69           C  
ATOM   5451  OD1 ASN A 716       0.349 -35.981 -13.614  1.00 26.21           O  
ATOM   5452  ND2 ASN A 716      -0.610 -36.045 -15.647  1.00 24.36           N  
ATOM   5453  N   MET A 717      -5.010 -34.460 -13.528  1.00 21.85           N  
ATOM   5454  CA  MET A 717      -6.276 -34.467 -12.802  1.00 21.86           C  
ATOM   5455  C   MET A 717      -7.469 -34.745 -13.719  1.00 21.87           C  
ATOM   5456  O   MET A 717      -8.397 -35.472 -13.342  1.00 21.88           O  
ATOM   5457  CB  MET A 717      -6.460 -33.140 -12.059  1.00 21.82           C  
ATOM   5458  CG  MET A 717      -7.664 -33.105 -11.144  1.00 21.61           C  
ATOM   5459  SD  MET A 717      -7.645 -31.677 -10.053  1.00 21.69           S  
ATOM   5460  CE  MET A 717      -7.918 -30.318 -11.189  1.00 21.23           C  
ATOM   5461  N   TYR A 718      -7.436 -34.171 -14.920  1.00 21.78           N  
ATOM   5462  CA  TYR A 718      -8.533 -34.310 -15.878  1.00 22.09           C  
ATOM   5463  C   TYR A 718      -8.396 -35.538 -16.783  1.00 23.05           C  
ATOM   5464  O   TYR A 718      -9.339 -35.886 -17.502  1.00 22.87           O  
ATOM   5465  CB  TYR A 718      -8.653 -33.048 -16.740  1.00 21.39           C  
ATOM   5466  CG  TYR A 718      -9.224 -31.842 -16.018  1.00 20.68           C  
ATOM   5467  CD1 TYR A 718      -8.392 -30.946 -15.341  1.00 20.01           C  
ATOM   5468  CD2 TYR A 718     -10.595 -31.590 -16.021  1.00 19.53           C  
ATOM   5469  CE1 TYR A 718      -8.917 -29.835 -14.679  1.00 19.52           C  
ATOM   5470  CE2 TYR A 718     -11.128 -30.482 -15.366  1.00 19.17           C  
ATOM   5471  CZ  TYR A 718     -10.286 -29.611 -14.696  1.00 19.80           C  
ATOM   5472  OH  TYR A 718     -10.821 -28.519 -14.042  1.00 19.27           O  
ATOM   5473  N   LYS A 719      -7.232 -36.187 -16.731  1.00 24.15           N  
ATOM   5474  CA  LYS A 719      -6.857 -37.240 -17.686  1.00 25.79           C  
ATOM   5475  C   LYS A 719      -7.894 -38.356 -17.859  1.00 26.50           C  
ATOM   5476  O   LYS A 719      -8.224 -38.721 -18.988  1.00 26.57           O  
ATOM   5477  CB  LYS A 719      -5.470 -37.812 -17.351  1.00 25.77           C  
ATOM   5478  CG  LYS A 719      -4.970 -38.893 -18.317  1.00 27.33           C  
ATOM   5479  CD  LYS A 719      -3.443 -38.971 -18.370  1.00 29.63           C  
ATOM   5480  CE  LYS A 719      -2.820 -39.314 -17.017  1.00 30.70           C  
ATOM   5481  NZ  LYS A 719      -1.370 -38.955 -16.982  1.00 32.41           N  
ATOM   5482  N   LYS A 720      -8.415 -38.876 -16.749  1.00 27.63           N  
ATOM   5483  CA  LYS A 720      -9.337 -40.024 -16.795  1.00 28.89           C  
ATOM   5484  C   LYS A 720     -10.668 -39.747 -17.512  1.00 29.36           C  
ATOM   5485  O   LYS A 720     -11.366 -40.682 -17.911  1.00 29.42           O  
ATOM   5486  CB  LYS A 720      -9.582 -40.605 -15.394  1.00 28.81           C  
ATOM   5487  CG  LYS A 720     -10.171 -39.637 -14.371  1.00 29.30           C  
ATOM   5488  CD  LYS A 720     -10.714 -40.372 -13.144  1.00 29.70           C  
ATOM   5489  CE  LYS A 720      -9.605 -40.959 -12.275  1.00 31.67           C  
ATOM   5490  NZ  LYS A 720     -10.155 -41.726 -11.117  1.00 33.22           N  
ATOM   5491  N   TYR A 721     -11.005 -38.470 -17.678  1.00 30.09           N  
ATOM   5492  CA  TYR A 721     -12.254 -38.075 -18.327  1.00 30.99           C  
ATOM   5493  C   TYR A 721     -12.063 -37.617 -19.774  1.00 31.66           C  
ATOM   5494  O   TYR A 721     -13.041 -37.416 -20.500  1.00 31.49           O  
ATOM   5495  CB  TYR A 721     -12.962 -36.985 -17.510  1.00 31.05           C  
ATOM   5496  CG  TYR A 721     -13.342 -37.431 -16.115  1.00 31.31           C  
ATOM   5497  CD1 TYR A 721     -14.383 -38.337 -15.910  1.00 31.56           C  
ATOM   5498  CD2 TYR A 721     -12.655 -36.954 -15.000  1.00 31.61           C  
ATOM   5499  CE1 TYR A 721     -14.732 -38.756 -14.629  1.00 31.80           C  
ATOM   5500  CE2 TYR A 721     -12.997 -37.367 -13.713  1.00 31.76           C  
ATOM   5501  CZ  TYR A 721     -14.035 -38.267 -13.538  1.00 31.54           C  
ATOM   5502  OH  TYR A 721     -14.377 -38.679 -12.271  1.00 32.04           O  
ATOM   5503  N   MET A 722     -10.807 -37.466 -20.186  1.00 32.43           N  
ATOM   5504  CA  MET A 722     -10.480 -36.876 -21.484  1.00 33.51           C  
ATOM   5505  C   MET A 722     -10.822 -37.769 -22.669  1.00 34.17           C  
ATOM   5506  O   MET A 722     -10.612 -38.984 -22.611  1.00 34.14           O  
ATOM   5507  CB  MET A 722      -8.995 -36.528 -21.555  1.00 33.51           C  
ATOM   5508  CG  MET A 722      -8.614 -35.247 -20.852  1.00 33.78           C  
ATOM   5509  SD  MET A 722      -6.932 -34.760 -21.278  1.00 33.78           S  
ATOM   5510  CE  MET A 722      -6.016 -36.214 -20.790  1.00 34.64           C  
ATOM   5511  N   PRO A 723     -11.345 -37.165 -23.754  1.00 34.93           N  
ATOM   5512  CA  PRO A 723     -11.468 -37.913 -25.000  1.00 35.58           C  
ATOM   5513  C   PRO A 723     -10.094 -38.044 -25.656  1.00 36.08           C  
ATOM   5514  O   PRO A 723      -9.232 -37.180 -25.465  1.00 36.06           O  
ATOM   5515  CB  PRO A 723     -12.388 -37.033 -25.849  1.00 35.61           C  
ATOM   5516  CG  PRO A 723     -12.152 -35.665 -25.359  1.00 35.34           C  
ATOM   5517  CD  PRO A 723     -11.840 -35.781 -23.889  1.00 35.08           C  
ATOM   5518  N   ASP A 724      -9.904 -39.122 -26.414  1.00 36.72           N  
ATOM   5519  CA  ASP A 724      -8.629 -39.416 -27.070  1.00 37.20           C  
ATOM   5520  C   ASP A 724      -8.043 -38.225 -27.839  1.00 37.17           C  
ATOM   5521  O   ASP A 724      -6.823 -38.048 -27.870  1.00 37.25           O  
ATOM   5522  CB  ASP A 724      -8.783 -40.634 -27.989  1.00 37.54           C  
ATOM   5523  CG  ASP A 724      -7.493 -41.004 -28.697  1.00 38.49           C  
ATOM   5524  OD1 ASP A 724      -6.724 -41.824 -28.148  1.00 39.77           O  
ATOM   5525  OD2 ASP A 724      -7.245 -40.469 -29.800  1.00 40.24           O  
ATOM   5526  N   LYS A 725      -8.912 -37.411 -28.438  1.00 37.19           N  
ATOM   5527  CA  LYS A 725      -8.476 -36.293 -29.287  1.00 37.27           C  
ATOM   5528  C   LYS A 725      -7.711 -35.183 -28.550  1.00 37.05           C  
ATOM   5529  O   LYS A 725      -6.873 -34.509 -29.157  1.00 37.11           O  
ATOM   5530  CB  LYS A 725      -9.647 -35.724 -30.108  1.00 37.29           C  
ATOM   5531  CG  LYS A 725     -10.754 -35.051 -29.300  1.00 37.64           C  
ATOM   5532  CD  LYS A 725     -11.979 -34.721 -30.157  1.00 37.74           C  
ATOM   5533  CE  LYS A 725     -11.794 -33.459 -31.003  1.00 38.60           C  
ATOM   5534  NZ  LYS A 725     -11.016 -33.702 -32.253  1.00 39.23           N  
ATOM   5535  N   LEU A 726      -7.998 -34.993 -27.261  1.00 36.79           N  
ATOM   5536  CA  LEU A 726      -7.228 -34.052 -26.433  1.00 36.52           C  
ATOM   5537  C   LEU A 726      -6.180 -34.750 -25.571  1.00 36.14           C  
ATOM   5538  O   LEU A 726      -5.147 -34.161 -25.250  1.00 36.13           O  
ATOM   5539  CB  LEU A 726      -8.128 -33.195 -25.535  1.00 36.70           C  
ATOM   5540  CG  LEU A 726      -9.187 -32.288 -26.155  1.00 36.90           C  
ATOM   5541  CD1 LEU A 726     -10.542 -32.721 -25.663  1.00 37.38           C  
ATOM   5542  CD2 LEU A 726      -8.939 -30.850 -25.751  1.00 37.76           C  
ATOM   5543  N   ALA A 727      -6.458 -35.995 -25.187  1.00 35.79           N  
ATOM   5544  CA  ALA A 727      -5.522 -36.793 -24.390  1.00 35.49           C  
ATOM   5545  C   ALA A 727      -4.187 -36.997 -25.108  1.00 35.26           C  
ATOM   5546  O   ALA A 727      -3.134 -37.059 -24.470  1.00 35.29           O  
ATOM   5547  CB  ALA A 727      -6.141 -38.136 -24.027  1.00 35.53           C  
ATOM   5548  N   ARG A 728      -4.245 -37.085 -26.435  1.00 34.91           N  
ATOM   5549  CA  ARG A 728      -3.065 -37.319 -27.266  1.00 34.82           C  
ATOM   5550  C   ARG A 728      -2.164 -36.094 -27.429  1.00 34.12           C  
ATOM   5551  O   ARG A 728      -0.980 -36.227 -27.752  1.00 34.25           O  
ATOM   5552  CB  ARG A 728      -3.485 -37.832 -28.645  1.00 34.84           C  
ATOM   5553  CG  ARG A 728      -3.742 -39.327 -28.691  1.00 35.60           C  
ATOM   5554  CD  ARG A 728      -3.982 -39.792 -30.120  1.00 35.82           C  
ATOM   5555  NE  ARG A 728      -3.598 -41.193 -30.304  1.00 38.31           N  
ATOM   5556  CZ  ARG A 728      -3.563 -41.820 -31.479  1.00 39.41           C  
ATOM   5557  NH1 ARG A 728      -3.894 -41.181 -32.597  1.00 39.94           N  
ATOM   5558  NH2 ARG A 728      -3.195 -43.095 -31.538  1.00 39.96           N  
ATOM   5559  N   LEU A 729      -2.725 -34.908 -27.206  1.00 33.26           N  
ATOM   5560  CA  LEU A 729      -1.996 -33.662 -27.431  1.00 32.20           C  
ATOM   5561  C   LEU A 729      -1.213 -33.213 -26.202  1.00 31.36           C  
ATOM   5562  O   LEU A 729      -1.468 -33.673 -25.085  1.00 31.36           O  
ATOM   5563  CB  LEU A 729      -2.949 -32.552 -27.891  1.00 32.32           C  
ATOM   5564  CG  LEU A 729      -3.835 -32.801 -29.119  1.00 32.42           C  
ATOM   5565  CD1 LEU A 729      -4.792 -31.638 -29.306  1.00 32.86           C  
ATOM   5566  CD2 LEU A 729      -3.012 -33.035 -30.386  1.00 32.45           C  
ATOM   5567  N   ASP A 730      -0.254 -32.316 -26.431  1.00 30.27           N  
ATOM   5568  CA  ASP A 730       0.539 -31.691 -25.372  1.00 29.30           C  
ATOM   5569  C   ASP A 730      -0.375 -31.212 -24.239  1.00 28.32           C  
ATOM   5570  O   ASP A 730      -1.432 -30.641 -24.509  1.00 28.20           O  
ATOM   5571  CB  ASP A 730       1.339 -30.524 -25.964  1.00 29.57           C  
ATOM   5572  CG  ASP A 730       2.282 -29.883 -24.963  1.00 30.47           C  
ATOM   5573  OD1 ASP A 730       3.484 -30.226 -24.962  1.00 31.49           O  
ATOM   5574  OD2 ASP A 730       1.821 -29.034 -24.176  1.00 31.30           O  
ATOM   5575  N   PRO A 731       0.019 -31.459 -22.970  1.00 27.42           N  
ATOM   5576  CA  PRO A 731      -0.811 -31.094 -21.813  1.00 26.65           C  
ATOM   5577  C   PRO A 731      -1.233 -29.624 -21.787  1.00 25.78           C  
ATOM   5578  O   PRO A 731      -2.284 -29.297 -21.233  1.00 25.55           O  
ATOM   5579  CB  PRO A 731       0.095 -31.411 -20.619  1.00 26.78           C  
ATOM   5580  CG  PRO A 731       0.988 -32.489 -21.117  1.00 27.38           C  
ATOM   5581  CD  PRO A 731       1.269 -32.118 -22.544  1.00 27.37           C  
ATOM   5582  N   ARG A 732      -0.428 -28.752 -22.392  1.00 24.78           N  
ATOM   5583  CA  ARG A 732      -0.763 -27.332 -22.480  1.00 23.88           C  
ATOM   5584  C   ARG A 732      -1.929 -27.073 -23.429  1.00 23.10           C  
ATOM   5585  O   ARG A 732      -2.659 -26.098 -23.263  1.00 22.57           O  
ATOM   5586  CB  ARG A 732       0.454 -26.511 -22.905  1.00 24.25           C  
ATOM   5587  CG  ARG A 732       1.603 -26.561 -21.913  1.00 25.12           C  
ATOM   5588  CD  ARG A 732       2.796 -25.780 -22.428  1.00 28.40           C  
ATOM   5589  NE  ARG A 732       3.433 -26.435 -23.568  1.00 30.33           N  
ATOM   5590  CZ  ARG A 732       4.442 -27.298 -23.477  1.00 32.08           C  
ATOM   5591  NH1 ARG A 732       4.942 -27.627 -22.290  1.00 33.22           N  
ATOM   5592  NH2 ARG A 732       4.954 -27.835 -24.579  1.00 32.37           N  
ATOM   5593  N   LEU A 733      -2.097 -27.949 -24.419  1.00 22.30           N  
ATOM   5594  CA  LEU A 733      -3.189 -27.821 -25.384  1.00 21.66           C  
ATOM   5595  C   LEU A 733      -4.550 -28.140 -24.779  1.00 21.00           C  
ATOM   5596  O   LEU A 733      -5.525 -27.441 -25.054  1.00 20.56           O  
ATOM   5597  CB  LEU A 733      -2.942 -28.673 -26.628  1.00 21.96           C  
ATOM   5598  CG  LEU A 733      -2.013 -28.055 -27.671  1.00 22.65           C  
ATOM   5599  CD1 LEU A 733      -1.759 -29.060 -28.787  1.00 23.51           C  
ATOM   5600  CD2 LEU A 733      -2.583 -26.750 -28.226  1.00 22.59           C  
ATOM   5601  N   PHE A 734      -4.618 -29.188 -23.958  1.00 20.15           N  
ATOM   5602  CA  PHE A 734      -5.844 -29.444 -23.212  1.00 19.49           C  
ATOM   5603  C   PHE A 734      -6.164 -28.242 -22.328  1.00 18.90           C  
ATOM   5604  O   PHE A 734      -7.306 -27.787 -22.288  1.00 18.53           O  
ATOM   5605  CB  PHE A 734      -5.777 -30.708 -22.348  1.00 19.64           C  
ATOM   5606  CG  PHE A 734      -6.890 -30.779 -21.334  1.00 19.99           C  
ATOM   5607  CD1 PHE A 734      -8.179 -31.125 -21.724  1.00 21.02           C  
ATOM   5608  CD2 PHE A 734      -6.664 -30.426 -20.004  1.00 20.95           C  
ATOM   5609  CE1 PHE A 734      -9.223 -31.152 -20.804  1.00 21.08           C  
ATOM   5610  CE2 PHE A 734      -7.700 -30.454 -19.075  1.00 20.39           C  
ATOM   5611  CZ  PHE A 734      -8.981 -30.818 -19.475  1.00 20.18           C  
ATOM   5612  N   CYS A 735      -5.150 -27.739 -21.623  1.00 18.40           N  
ATOM   5613  CA  CYS A 735      -5.326 -26.581 -20.747  1.00 18.08           C  
ATOM   5614  C   CYS A 735      -5.891 -25.400 -21.525  1.00 17.27           C  
ATOM   5615  O   CYS A 735      -6.854 -24.781 -21.088  1.00 16.59           O  
ATOM   5616  CB  CYS A 735      -4.011 -26.198 -20.058  1.00 18.24           C  
ATOM   5617  SG  CYS A 735      -3.438 -27.402 -18.829  1.00 20.27           S  
ATOM   5618  N   LYS A 736      -5.309 -25.110 -22.689  1.00 16.94           N  
ATOM   5619  CA  LYS A 736      -5.785 -24.010 -23.529  1.00 16.93           C  
ATOM   5620  C   LYS A 736      -7.249 -24.193 -23.939  1.00 16.66           C  
ATOM   5621  O   LYS A 736      -8.031 -23.245 -23.901  1.00 16.39           O  
ATOM   5622  CB  LYS A 736      -4.896 -23.836 -24.763  1.00 17.37           C  
ATOM   5623  CG  LYS A 736      -3.562 -23.179 -24.459  1.00 18.71           C  
ATOM   5624  CD  LYS A 736      -2.709 -23.034 -25.711  1.00 21.17           C  
ATOM   5625  CE  LYS A 736      -1.379 -22.365 -25.378  1.00 23.05           C  
ATOM   5626  NZ  LYS A 736      -0.499 -22.233 -26.578  1.00 25.00           N  
ATOM   5627  N   ALA A 737      -7.609 -25.419 -24.315  1.00 16.31           N  
ATOM   5628  CA  ALA A 737      -8.983 -25.748 -24.675  1.00 16.27           C  
ATOM   5629  C   ALA A 737      -9.926 -25.510 -23.497  1.00 16.25           C  
ATOM   5630  O   ALA A 737     -10.975 -24.889 -23.656  1.00 16.31           O  
ATOM   5631  CB  ALA A 737      -9.075 -27.192 -25.163  1.00 16.42           C  
ATOM   5632  N   LEU A 738      -9.530 -25.987 -22.316  1.00 16.26           N  
ATOM   5633  CA  LEU A 738     -10.294 -25.763 -21.088  1.00 16.49           C  
ATOM   5634  C   LEU A 738     -10.500 -24.273 -20.809  1.00 16.51           C  
ATOM   5635  O   LEU A 738     -11.624 -23.837 -20.547  1.00 16.08           O  
ATOM   5636  CB  LEU A 738      -9.611 -26.441 -19.893  1.00 16.53           C  
ATOM   5637  CG  LEU A 738     -10.296 -26.345 -18.520  1.00 16.87           C  
ATOM   5638  CD1 LEU A 738     -11.711 -26.924 -18.555  1.00 17.93           C  
ATOM   5639  CD2 LEU A 738      -9.463 -27.035 -17.463  1.00 16.88           C  
ATOM   5640  N   PHE A 739      -9.415 -23.499 -20.878  1.00 16.87           N  
ATOM   5641  CA  PHE A 739      -9.478 -22.059 -20.603  1.00 17.07           C  
ATOM   5642  C   PHE A 739     -10.450 -21.359 -21.543  1.00 17.61           C  
ATOM   5643  O   PHE A 739     -11.276 -20.552 -21.107  1.00 17.61           O  
ATOM   5644  CB  PHE A 739      -8.095 -21.396 -20.703  1.00 16.99           C  
ATOM   5645  CG  PHE A 739      -7.037 -22.007 -19.811  1.00 16.34           C  
ATOM   5646  CD1 PHE A 739      -5.692 -21.743 -20.053  1.00 16.37           C  
ATOM   5647  CD2 PHE A 739      -7.372 -22.834 -18.739  1.00 16.30           C  
ATOM   5648  CE1 PHE A 739      -4.701 -22.291 -19.254  1.00 15.93           C  
ATOM   5649  CE2 PHE A 739      -6.385 -23.391 -17.930  1.00 16.26           C  
ATOM   5650  CZ  PHE A 739      -5.045 -23.118 -18.190  1.00 16.77           C  
ATOM   5651  N   LYS A 740     -10.353 -21.680 -22.832  1.00 17.97           N  
ATOM   5652  CA  LYS A 740     -11.196 -21.055 -23.849  1.00 18.58           C  
ATOM   5653  C   LYS A 740     -12.670 -21.412 -23.689  1.00 18.77           C  
ATOM   5654  O   LYS A 740     -13.538 -20.555 -23.868  1.00 18.80           O  
ATOM   5655  CB  LYS A 740     -10.707 -21.405 -25.255  1.00 18.63           C  
ATOM   5656  CG  LYS A 740      -9.353 -20.808 -25.595  1.00 19.62           C  
ATOM   5657  CD  LYS A 740      -9.019 -21.003 -27.059  1.00 20.19           C  
ATOM   5658  CE  LYS A 740      -7.669 -20.383 -27.400  1.00 21.23           C  
ATOM   5659  NZ  LYS A 740      -7.480 -20.291 -28.868  1.00 21.21           N  
ATOM   5660  N   ALA A 741     -12.933 -22.676 -23.352  1.00 19.03           N  
ATOM   5661  CA  ALA A 741     -14.281 -23.165 -23.061  1.00 19.58           C  
ATOM   5662  C   ALA A 741     -14.876 -22.476 -21.838  1.00 19.86           C  
ATOM   5663  O   ALA A 741     -16.097 -22.338 -21.732  1.00 20.14           O  
ATOM   5664  CB  ALA A 741     -14.272 -24.682 -22.874  1.00 19.48           C  
ATOM   5665  N   LEU A 742     -14.007 -22.044 -20.922  1.00 20.25           N  
ATOM   5666  CA  LEU A 742     -14.423 -21.290 -19.739  1.00 20.67           C  
ATOM   5667  C   LEU A 742     -14.480 -19.781 -19.994  1.00 20.86           C  
ATOM   5668  O   LEU A 742     -14.780 -18.998 -19.087  1.00 21.07           O  
ATOM   5669  CB  LEU A 742     -13.512 -21.609 -18.544  1.00 20.70           C  
ATOM   5670  CG  LEU A 742     -13.589 -23.034 -17.984  1.00 21.27           C  
ATOM   5671  CD1 LEU A 742     -12.442 -23.276 -17.029  1.00 21.94           C  
ATOM   5672  CD2 LEU A 742     -14.927 -23.312 -17.297  1.00 23.02           C  
ATOM   5673  N   GLY A 743     -14.192 -19.382 -21.231  1.00 20.95           N  
ATOM   5674  CA  GLY A 743     -14.338 -17.994 -21.658  1.00 21.30           C  
ATOM   5675  C   GLY A 743     -13.140 -17.101 -21.391  1.00 21.31           C  
ATOM   5676  O   GLY A 743     -13.240 -15.880 -21.518  1.00 21.46           O  
ATOM   5677  N   LEU A 744     -12.011 -17.705 -21.024  1.00 21.40           N  
ATOM   5678  CA  LEU A 744     -10.764 -16.961 -20.818  1.00 21.55           C  
ATOM   5679  C   LEU A 744     -10.146 -16.534 -22.139  1.00 21.85           C  
ATOM   5680  O   LEU A 744     -10.150 -17.296 -23.111  1.00 21.74           O  
ATOM   5681  CB  LEU A 744      -9.748 -17.781 -20.013  1.00 21.37           C  
ATOM   5682  CG  LEU A 744     -10.004 -17.989 -18.515  1.00 20.93           C  
ATOM   5683  CD1 LEU A 744      -8.939 -18.884 -17.905  1.00 21.30           C  
ATOM   5684  CD2 LEU A 744     -10.060 -16.648 -17.781  1.00 21.43           C  
ATOM   5685  N   ASN A 745      -9.623 -15.309 -22.160  1.00 22.23           N  
ATOM   5686  CA  ASN A 745      -8.919 -14.767 -23.320  1.00 22.88           C  
ATOM   5687  C   ASN A 745      -7.415 -15.009 -23.207  1.00 22.89           C  
ATOM   5688  O   ASN A 745      -6.897 -15.230 -22.108  1.00 22.72           O  
ATOM   5689  CB  ASN A 745      -9.212 -13.268 -23.476  1.00 23.03           C  
ATOM   5690  CG  ASN A 745     -10.702 -12.962 -23.568  1.00 24.20           C  
ATOM   5691  OD1 ASN A 745     -11.396 -13.420 -24.482  1.00 25.69           O  
ATOM   5692  ND2 ASN A 745     -11.199 -12.173 -22.620  1.00 25.57           N  
ATOM   5693  N   GLU A 746      -6.715 -14.967 -24.341  1.00 23.01           N  
ATOM   5694  CA  GLU A 746      -5.279 -15.263 -24.383  1.00 23.46           C  
ATOM   5695  C   GLU A 746      -4.449 -14.408 -23.422  1.00 22.88           C  
ATOM   5696  O   GLU A 746      -3.453 -14.873 -22.870  1.00 23.08           O  
ATOM   5697  CB  GLU A 746      -4.734 -15.129 -25.809  1.00 23.78           C  
ATOM   5698  CG  GLU A 746      -5.397 -16.067 -26.800  1.00 26.24           C  
ATOM   5699  CD  GLU A 746      -4.493 -16.467 -27.955  1.00 29.27           C  
ATOM   5700  OE1 GLU A 746      -3.436 -15.825 -28.172  1.00 29.93           O  
ATOM   5701  OE2 GLU A 746      -4.857 -17.437 -28.652  1.00 30.71           O  
ATOM   5702  N   ILE A 747      -4.874 -13.167 -23.215  1.00 22.49           N  
ATOM   5703  CA  ILE A 747      -4.155 -12.251 -22.330  1.00 22.41           C  
ATOM   5704  C   ILE A 747      -4.332 -12.567 -20.837  1.00 21.79           C  
ATOM   5705  O   ILE A 747      -3.584 -12.056 -19.999  1.00 21.83           O  
ATOM   5706  CB  ILE A 747      -4.515 -10.767 -22.602  1.00 22.63           C  
ATOM   5707  CG1 ILE A 747      -6.001 -10.498 -22.339  1.00 23.31           C  
ATOM   5708  CG2 ILE A 747      -4.099 -10.368 -24.023  1.00 23.76           C  
ATOM   5709  CD1 ILE A 747      -6.316  -9.041 -22.049  1.00 25.48           C  
ATOM   5710  N   ASP A 748      -5.306 -13.422 -20.523  1.00 20.96           N  
ATOM   5711  CA  ASP A 748      -5.658 -13.758 -19.135  1.00 20.10           C  
ATOM   5712  C   ASP A 748      -4.711 -14.756 -18.475  1.00 19.72           C  
ATOM   5713  O   ASP A 748      -4.680 -14.867 -17.246  1.00 19.04           O  
ATOM   5714  CB  ASP A 748      -7.086 -14.314 -19.066  1.00 19.99           C  
ATOM   5715  CG  ASP A 748      -8.136 -13.305 -19.490  1.00 20.77           C  
ATOM   5716  OD1 ASP A 748      -9.240 -13.741 -19.881  1.00 22.18           O  
ATOM   5717  OD2 ASP A 748      -7.874 -12.082 -19.423  1.00 20.56           O  
ATOM   5718  N   TYR A 749      -3.956 -15.489 -19.289  1.00 19.31           N  
ATOM   5719  CA  TYR A 749      -3.076 -16.544 -18.784  1.00 19.46           C  
ATOM   5720  C   TYR A 749      -1.746 -16.607 -19.534  1.00 19.39           C  
ATOM   5721  O   TYR A 749      -1.610 -16.059 -20.635  1.00 19.55           O  
ATOM   5722  CB  TYR A 749      -3.784 -17.911 -18.826  1.00 19.53           C  
ATOM   5723  CG  TYR A 749      -4.318 -18.283 -20.193  1.00 19.72           C  
ATOM   5724  CD1 TYR A 749      -3.525 -18.976 -21.109  1.00 20.19           C  
ATOM   5725  CD2 TYR A 749      -5.615 -17.939 -20.574  1.00 19.84           C  
ATOM   5726  CE1 TYR A 749      -4.014 -19.318 -22.374  1.00 20.05           C  
ATOM   5727  CE2 TYR A 749      -6.109 -18.272 -21.833  1.00 20.60           C  
ATOM   5728  CZ  TYR A 749      -5.302 -18.957 -22.726  1.00 20.40           C  
ATOM   5729  OH  TYR A 749      -5.796 -19.285 -23.968  1.00 20.91           O  
ATOM   5730  N   LYS A 750      -0.774 -17.281 -18.925  1.00 19.45           N  
ATOM   5731  CA  LYS A 750       0.550 -17.458 -19.512  1.00 19.66           C  
ATOM   5732  C   LYS A 750       1.194 -18.742 -19.012  1.00 19.53           C  
ATOM   5733  O   LYS A 750       1.227 -19.002 -17.808  1.00 18.99           O  
ATOM   5734  CB  LYS A 750       1.450 -16.258 -19.191  1.00 20.19           C  
ATOM   5735  CG  LYS A 750       2.738 -16.231 -19.994  1.00 21.75           C  
ATOM   5736  CD  LYS A 750       3.347 -14.840 -20.007  1.00 24.39           C  
ATOM   5737  CE  LYS A 750       4.465 -14.732 -21.036  1.00 25.98           C  
ATOM   5738  NZ  LYS A 750       5.646 -15.558 -20.663  1.00 27.20           N  
ATOM   5739  N   PHE A 751       1.702 -19.543 -19.946  1.00 19.17           N  
ATOM   5740  CA  PHE A 751       2.424 -20.758 -19.601  1.00 19.31           C  
ATOM   5741  C   PHE A 751       3.896 -20.478 -19.328  1.00 19.56           C  
ATOM   5742  O   PHE A 751       4.602 -19.929 -20.176  1.00 19.67           O  
ATOM   5743  CB  PHE A 751       2.273 -21.813 -20.703  1.00 19.34           C  
ATOM   5744  CG  PHE A 751       0.889 -22.363 -20.815  1.00 18.90           C  
ATOM   5745  CD1 PHE A 751       0.529 -23.516 -20.123  1.00 18.78           C  
ATOM   5746  CD2 PHE A 751      -0.068 -21.720 -21.592  1.00 19.05           C  
ATOM   5747  CE1 PHE A 751      -0.760 -24.026 -20.212  1.00 18.90           C  
ATOM   5748  CE2 PHE A 751      -1.366 -22.226 -21.689  1.00 19.48           C  
ATOM   5749  CZ  PHE A 751      -1.709 -23.382 -20.992  1.00 18.74           C  
ATOM   5750  N   GLY A 752       4.340 -20.842 -18.129  1.00 19.72           N  
ATOM   5751  CA  GLY A 752       5.758 -20.827 -17.788  1.00 20.44           C  
ATOM   5752  C   GLY A 752       6.373 -22.175 -18.106  1.00 20.77           C  
ATOM   5753  O   GLY A 752       5.781 -22.976 -18.835  1.00 20.89           O  
ATOM   5754  N   LEU A 753       7.551 -22.431 -17.544  1.00 21.16           N  
ATOM   5755  CA  LEU A 753       8.266 -23.688 -17.768  1.00 21.62           C  
ATOM   5756  C   LEU A 753       7.562 -24.918 -17.189  1.00 21.53           C  
ATOM   5757  O   LEU A 753       7.591 -25.990 -17.800  1.00 21.73           O  
ATOM   5758  CB  LEU A 753       9.701 -23.599 -17.233  1.00 21.74           C  
ATOM   5759  CG  LEU A 753      10.672 -22.703 -18.013  1.00 22.86           C  
ATOM   5760  CD1 LEU A 753      11.992 -22.561 -17.267  1.00 24.25           C  
ATOM   5761  CD2 LEU A 753      10.910 -23.226 -19.431  1.00 24.04           C  
ATOM   5762  N   THR A 754       6.944 -24.773 -16.017  1.00 21.26           N  
ATOM   5763  CA  THR A 754       6.239 -25.899 -15.378  1.00 21.28           C  
ATOM   5764  C   THR A 754       4.819 -25.533 -14.938  1.00 20.91           C  
ATOM   5765  O   THR A 754       3.961 -26.406 -14.789  1.00 20.73           O  
ATOM   5766  CB  THR A 754       7.007 -26.477 -14.156  1.00 21.36           C  
ATOM   5767  OG1 THR A 754       6.995 -25.535 -13.075  1.00 21.85           O  
ATOM   5768  CG2 THR A 754       8.455 -26.838 -14.511  1.00 21.93           C  
ATOM   5769  N   LYS A 755       4.581 -24.240 -14.739  1.00 20.48           N  
ATOM   5770  CA  LYS A 755       3.307 -23.760 -14.216  1.00 20.26           C  
ATOM   5771  C   LYS A 755       2.572 -22.867 -15.212  1.00 19.36           C  
ATOM   5772  O   LYS A 755       3.192 -22.153 -16.008  1.00 19.06           O  
ATOM   5773  CB  LYS A 755       3.525 -23.004 -12.898  1.00 20.27           C  
ATOM   5774  CG  LYS A 755       4.142 -23.847 -11.785  1.00 21.30           C  
ATOM   5775  CD  LYS A 755       4.383 -23.026 -10.531  1.00 21.97           C  
ATOM   5776  CE  LYS A 755       4.988 -23.887  -9.430  1.00 24.23           C  
ATOM   5777  NZ  LYS A 755       5.060 -23.154  -8.131  1.00 26.81           N  
ATOM   5778  N   VAL A 756       1.244 -22.917 -15.168  1.00 18.57           N  
ATOM   5779  CA  VAL A 756       0.423 -21.959 -15.897  1.00 17.80           C  
ATOM   5780  C   VAL A 756      -0.039 -20.874 -14.917  1.00 17.62           C  
ATOM   5781  O   VAL A 756      -0.430 -21.176 -13.787  1.00 17.72           O  
ATOM   5782  CB  VAL A 756      -0.769 -22.641 -16.647  1.00 17.89           C  
ATOM   5783  CG1 VAL A 756      -1.693 -23.387 -15.684  1.00 17.32           C  
ATOM   5784  CG2 VAL A 756      -1.541 -21.625 -17.476  1.00 17.32           C  
ATOM   5785  N   PHE A 757       0.028 -19.624 -15.365  1.00 17.24           N  
ATOM   5786  CA  PHE A 757      -0.229 -18.455 -14.529  1.00 16.73           C  
ATOM   5787  C   PHE A 757      -1.449 -17.701 -15.022  1.00 16.59           C  
ATOM   5788  O   PHE A 757      -1.689 -17.623 -16.224  1.00 16.58           O  
ATOM   5789  CB  PHE A 757       0.980 -17.516 -14.575  1.00 16.61           C  
ATOM   5790  CG  PHE A 757       2.178 -18.029 -13.834  1.00 16.24           C  
ATOM   5791  CD1 PHE A 757       3.036 -18.956 -14.420  1.00 16.38           C  
ATOM   5792  CD2 PHE A 757       2.460 -17.574 -12.550  1.00 16.28           C  
ATOM   5793  CE1 PHE A 757       4.152 -19.430 -13.731  1.00 16.16           C  
ATOM   5794  CE2 PHE A 757       3.567 -18.044 -11.852  1.00 15.91           C  
ATOM   5795  CZ  PHE A 757       4.418 -18.971 -12.441  1.00 16.68           C  
ATOM   5796  N   PHE A 758      -2.200 -17.121 -14.091  1.00 16.34           N  
ATOM   5797  CA  PHE A 758      -3.418 -16.403 -14.423  1.00 16.08           C  
ATOM   5798  C   PHE A 758      -3.351 -14.985 -13.877  1.00 16.28           C  
ATOM   5799  O   PHE A 758      -2.830 -14.757 -12.784  1.00 16.16           O  
ATOM   5800  CB  PHE A 758      -4.641 -17.141 -13.871  1.00 16.17           C  
ATOM   5801  CG  PHE A 758      -4.761 -18.561 -14.362  1.00 15.85           C  
ATOM   5802  CD1 PHE A 758      -4.050 -19.587 -13.746  1.00 16.47           C  
ATOM   5803  CD2 PHE A 758      -5.577 -18.868 -15.446  1.00 16.25           C  
ATOM   5804  CE1 PHE A 758      -4.142 -20.899 -14.200  1.00 16.00           C  
ATOM   5805  CE2 PHE A 758      -5.686 -20.180 -15.904  1.00 15.66           C  
ATOM   5806  CZ  PHE A 758      -4.965 -21.195 -15.283  1.00 15.59           C  
ATOM   5807  N   ARG A 759      -3.891 -14.047 -14.646  1.00 16.60           N  
ATOM   5808  CA  ARG A 759      -3.846 -12.624 -14.314  1.00 17.00           C  
ATOM   5809  C   ARG A 759      -4.832 -12.278 -13.193  1.00 17.21           C  
ATOM   5810  O   ARG A 759      -5.712 -13.083 -12.871  1.00 16.88           O  
ATOM   5811  CB  ARG A 759      -4.132 -11.790 -15.572  1.00 17.26           C  
ATOM   5812  CG  ARG A 759      -3.011 -11.808 -16.610  1.00 18.65           C  
ATOM   5813  CD  ARG A 759      -1.930 -10.786 -16.285  1.00 20.66           C  
ATOM   5814  NE  ARG A 759      -2.405  -9.417 -16.478  1.00 22.66           N  
ATOM   5815  CZ  ARG A 759      -1.943  -8.354 -15.821  1.00 23.14           C  
ATOM   5816  NH1 ARG A 759      -2.448  -7.152 -16.075  1.00 23.96           N  
ATOM   5817  NH2 ARG A 759      -0.986  -8.485 -14.909  1.00 22.76           N  
ATOM   5818  N   PRO A 760      -4.693 -11.077 -12.588  1.00 17.31           N  
ATOM   5819  CA  PRO A 760      -5.702 -10.664 -11.607  1.00 17.43           C  
ATOM   5820  C   PRO A 760      -7.088 -10.633 -12.244  1.00 17.18           C  
ATOM   5821  O   PRO A 760      -7.206 -10.450 -13.461  1.00 17.85           O  
ATOM   5822  CB  PRO A 760      -5.276  -9.239 -11.228  1.00 17.41           C  
ATOM   5823  CG  PRO A 760      -3.845  -9.152 -11.586  1.00 17.60           C  
ATOM   5824  CD  PRO A 760      -3.646 -10.054 -12.768  1.00 17.30           C  
ATOM   5825  N   GLY A 761      -8.121 -10.828 -11.431  1.00 17.30           N  
ATOM   5826  CA  GLY A 761      -9.503 -10.766 -11.904  1.00 17.20           C  
ATOM   5827  C   GLY A 761      -9.990 -12.072 -12.505  1.00 17.08           C  
ATOM   5828  O   GLY A 761     -11.113 -12.148 -13.014  1.00 17.35           O  
ATOM   5829  N   LYS A 762      -9.144 -13.098 -12.452  1.00 16.92           N  
ATOM   5830  CA  LYS A 762      -9.483 -14.405 -13.023  1.00 16.88           C  
ATOM   5831  C   LYS A 762      -9.505 -15.507 -11.965  1.00 16.42           C  
ATOM   5832  O   LYS A 762      -9.336 -16.685 -12.285  1.00 15.76           O  
ATOM   5833  CB  LYS A 762      -8.527 -14.762 -14.169  1.00 16.92           C  
ATOM   5834  CG  LYS A 762      -8.443 -13.704 -15.275  1.00 19.03           C  
ATOM   5835  CD  LYS A 762      -9.793 -13.485 -15.947  1.00 21.79           C  
ATOM   5836  CE  LYS A 762      -9.866 -12.129 -16.638  1.00 24.18           C  
ATOM   5837  NZ  LYS A 762     -11.214 -11.904 -17.230  1.00 26.02           N  
ATOM   5838  N   PHE A 763      -9.726 -15.116 -10.709  1.00 16.11           N  
ATOM   5839  CA  PHE A 763      -9.795 -16.067  -9.599  1.00 15.90           C  
ATOM   5840  C   PHE A 763     -10.975 -17.025  -9.721  1.00 15.84           C  
ATOM   5841  O   PHE A 763     -10.858 -18.201  -9.363  1.00 15.94           O  
ATOM   5842  CB  PHE A 763      -9.852 -15.335  -8.253  1.00 15.85           C  
ATOM   5843  CG  PHE A 763      -8.576 -14.615  -7.902  1.00 15.72           C  
ATOM   5844  CD1 PHE A 763      -8.420 -13.266  -8.200  1.00 16.02           C  
ATOM   5845  CD2 PHE A 763      -7.527 -15.291  -7.278  1.00 16.52           C  
ATOM   5846  CE1 PHE A 763      -7.238 -12.593  -7.879  1.00 16.18           C  
ATOM   5847  CE2 PHE A 763      -6.343 -14.630  -6.948  1.00 16.54           C  
ATOM   5848  CZ  PHE A 763      -6.200 -13.280  -7.252  1.00 15.53           C  
ATOM   5849  N   ALA A 764     -12.106 -16.527 -10.217  1.00 15.73           N  
ATOM   5850  CA  ALA A 764     -13.295 -17.367 -10.393  1.00 15.59           C  
ATOM   5851  C   ALA A 764     -13.013 -18.540 -11.327  1.00 15.45           C  
ATOM   5852  O   ALA A 764     -13.223 -19.701 -10.961  1.00 15.29           O  
ATOM   5853  CB  ALA A 764     -14.471 -16.544 -10.894  1.00 15.85           C  
ATOM   5854  N   GLU A 765     -12.517 -18.230 -12.525  1.00 15.08           N  
ATOM   5855  CA  GLU A 765     -12.164 -19.256 -13.503  1.00 15.02           C  
ATOM   5856  C   GLU A 765     -11.073 -20.187 -12.970  1.00 14.78           C  
ATOM   5857  O   GLU A 765     -11.173 -21.408 -13.111  1.00 14.57           O  
ATOM   5858  CB  GLU A 765     -11.731 -18.612 -14.822  1.00 15.38           C  
ATOM   5859  CG  GLU A 765     -12.840 -17.849 -15.535  1.00 16.19           C  
ATOM   5860  CD  GLU A 765     -12.975 -16.392 -15.097  1.00 17.96           C  
ATOM   5861  OE1 GLU A 765     -13.775 -15.671 -15.733  1.00 20.41           O  
ATOM   5862  OE2 GLU A 765     -12.300 -15.961 -14.130  1.00 18.14           O  
ATOM   5863  N   PHE A 766     -10.047 -19.611 -12.342  1.00 14.50           N  
ATOM   5864  CA  PHE A 766      -8.986 -20.406 -11.727  1.00 14.41           C  
ATOM   5865  C   PHE A 766      -9.560 -21.407 -10.721  1.00 14.28           C  
ATOM   5866  O   PHE A 766      -9.220 -22.587 -10.759  1.00 14.30           O  
ATOM   5867  CB  PHE A 766      -7.928 -19.510 -11.061  1.00 14.56           C  
ATOM   5868  CG  PHE A 766      -6.811 -20.277 -10.393  1.00 14.27           C  
ATOM   5869  CD1 PHE A 766      -6.743 -20.369  -9.002  1.00 14.97           C  
ATOM   5870  CD2 PHE A 766      -5.829 -20.911 -11.155  1.00 14.89           C  
ATOM   5871  CE1 PHE A 766      -5.712 -21.081  -8.385  1.00 15.18           C  
ATOM   5872  CE2 PHE A 766      -4.796 -21.620 -10.547  1.00 15.77           C  
ATOM   5873  CZ  PHE A 766      -4.738 -21.708  -9.159  1.00 15.41           C  
ATOM   5874  N   ASP A 767     -10.442 -20.935  -9.839  1.00 14.43           N  
ATOM   5875  CA  ASP A 767     -11.052 -21.796  -8.815  1.00 14.70           C  
ATOM   5876  C   ASP A 767     -11.855 -22.942  -9.420  1.00 15.04           C  
ATOM   5877  O   ASP A 767     -11.850 -24.061  -8.891  1.00 14.97           O  
ATOM   5878  CB  ASP A 767     -11.918 -20.975  -7.863  1.00 14.57           C  
ATOM   5879  CG  ASP A 767     -11.089 -20.103  -6.927  1.00 15.27           C  
ATOM   5880  OD1 ASP A 767      -9.862 -20.333  -6.803  1.00 16.71           O  
ATOM   5881  OD2 ASP A 767     -11.670 -19.184  -6.316  1.00 16.03           O  
ATOM   5882  N   GLN A 768     -12.527 -22.661 -10.534  1.00 15.50           N  
ATOM   5883  CA  GLN A 768     -13.282 -23.684 -11.268  1.00 16.11           C  
ATOM   5884  C   GLN A 768     -12.357 -24.753 -11.844  1.00 15.96           C  
ATOM   5885  O   GLN A 768     -12.623 -25.950 -11.712  1.00 15.73           O  
ATOM   5886  CB  GLN A 768     -14.136 -23.048 -12.374  1.00 16.45           C  
ATOM   5887  CG  GLN A 768     -15.314 -22.230 -11.853  1.00 18.93           C  
ATOM   5888  CD  GLN A 768     -16.333 -23.079 -11.114  1.00 22.36           C  
ATOM   5889  OE1 GLN A 768     -16.987 -23.938 -11.705  1.00 24.85           O  
ATOM   5890  NE2 GLN A 768     -16.472 -22.841  -9.813  1.00 24.89           N  
ATOM   5891  N   ILE A 769     -11.269 -24.308 -12.472  1.00 16.02           N  
ATOM   5892  CA  ILE A 769     -10.250 -25.195 -13.043  1.00 16.31           C  
ATOM   5893  C   ILE A 769      -9.625 -26.106 -11.979  1.00 16.63           C  
ATOM   5894  O   ILE A 769      -9.317 -27.274 -12.246  1.00 16.61           O  
ATOM   5895  CB  ILE A 769      -9.145 -24.365 -13.763  1.00 16.32           C  
ATOM   5896  CG1 ILE A 769      -9.742 -23.609 -14.957  1.00 16.21           C  
ATOM   5897  CG2 ILE A 769      -7.979 -25.242 -14.210  1.00 16.71           C  
ATOM   5898  CD1 ILE A 769      -8.925 -22.413 -15.414  1.00 16.10           C  
ATOM   5899  N   MET A 770      -9.466 -25.571 -10.772  1.00 16.65           N  
ATOM   5900  CA  MET A 770      -8.761 -26.268  -9.698  1.00 17.50           C  
ATOM   5901  C   MET A 770      -9.592 -27.307  -8.932  1.00 17.68           C  
ATOM   5902  O   MET A 770      -9.027 -28.120  -8.201  1.00 17.59           O  
ATOM   5903  CB  MET A 770      -8.154 -25.254  -8.722  1.00 17.59           C  
ATOM   5904  CG  MET A 770      -7.014 -24.440  -9.320  1.00 18.10           C  
ATOM   5905  SD  MET A 770      -5.506 -25.402  -9.535  1.00 21.11           S  
ATOM   5906  CE  MET A 770      -4.962 -25.557  -7.834  1.00 21.10           C  
ATOM   5907  N   LYS A 771     -10.916 -27.280  -9.094  1.00 18.36           N  
ATOM   5908  CA  LYS A 771     -11.793 -28.215  -8.371  1.00 19.06           C  
ATOM   5909  C   LYS A 771     -11.492 -29.664  -8.749  1.00 19.08           C  
ATOM   5910  O   LYS A 771     -11.456 -30.009  -9.933  1.00 18.80           O  
ATOM   5911  CB  LYS A 771     -13.272 -27.896  -8.607  1.00 19.71           C  
ATOM   5912  CG  LYS A 771     -13.737 -26.593  -7.981  1.00 21.13           C  
ATOM   5913  CD  LYS A 771     -15.249 -26.516  -7.910  1.00 24.88           C  
ATOM   5914  CE  LYS A 771     -15.695 -25.185  -7.325  1.00 26.46           C  
ATOM   5915  NZ  LYS A 771     -17.004 -25.309  -6.617  1.00 29.02           N  
ATOM   5916  N   SER A 772     -11.272 -30.504  -7.737  1.00 19.18           N  
ATOM   5917  CA  SER A 772     -10.824 -31.885  -7.956  1.00 19.68           C  
ATOM   5918  C   SER A 772     -11.948 -32.918  -7.816  1.00 19.95           C  
ATOM   5919  O   SER A 772     -11.722 -34.118  -7.981  1.00 20.18           O  
ATOM   5920  CB  SER A 772      -9.674 -32.225  -7.002  1.00 19.59           C  
ATOM   5921  OG  SER A 772     -10.098 -32.120  -5.656  1.00 20.20           O  
ATOM   5922  N   ASP A 773     -13.142 -32.426  -7.497  1.00 20.32           N  
ATOM   5923  CA  ASP A 773     -14.382 -33.201  -7.399  1.00 20.63           C  
ATOM   5924  C   ASP A 773     -14.696 -33.952  -8.713  1.00 19.77           C  
ATOM   5925  O   ASP A 773     -14.728 -33.333  -9.773  1.00 19.42           O  
ATOM   5926  CB  ASP A 773     -15.492 -32.202  -7.039  1.00 21.32           C  
ATOM   5927  CG  ASP A 773     -16.880 -32.787  -7.115  1.00 23.43           C  
ATOM   5928  OD1 ASP A 773     -17.234 -33.633  -6.263  1.00 27.37           O  
ATOM   5929  OD2 ASP A 773     -17.637 -32.361  -8.007  1.00 25.38           O  
ATOM   5930  N   PRO A 774     -14.903 -35.291  -8.651  1.00 19.50           N  
ATOM   5931  CA  PRO A 774     -15.166 -36.060  -9.882  1.00 19.13           C  
ATOM   5932  C   PRO A 774     -16.296 -35.488 -10.747  1.00 18.68           C  
ATOM   5933  O   PRO A 774     -16.134 -35.370 -11.968  1.00 18.47           O  
ATOM   5934  CB  PRO A 774     -15.526 -37.455  -9.355  1.00 19.42           C  
ATOM   5935  CG  PRO A 774     -14.785 -37.552  -8.072  1.00 19.76           C  
ATOM   5936  CD  PRO A 774     -14.871 -36.174  -7.468  1.00 19.54           C  
ATOM   5937  N   ASP A 775     -17.415 -35.126 -10.124  1.00 18.12           N  
ATOM   5938  CA  ASP A 775     -18.529 -34.506 -10.837  1.00 18.17           C  
ATOM   5939  C   ASP A 775     -18.097 -33.252 -11.598  1.00 17.70           C  
ATOM   5940  O   ASP A 775     -18.463 -33.073 -12.763  1.00 17.36           O  
ATOM   5941  CB  ASP A 775     -19.667 -34.147  -9.872  1.00 18.46           C  
ATOM   5942  CG  ASP A 775     -20.477 -35.359  -9.422  1.00 20.08           C  
ATOM   5943  OD1 ASP A 775     -20.145 -36.503  -9.806  1.00 21.63           O  
ATOM   5944  OD2 ASP A 775     -21.456 -35.154  -8.670  1.00 21.40           O  
ATOM   5945  N   HIS A 776     -17.322 -32.390 -10.937  1.00 17.30           N  
ATOM   5946  CA  HIS A 776     -16.911 -31.122 -11.547  1.00 17.28           C  
ATOM   5947  C   HIS A 776     -15.892 -31.313 -12.670  1.00 16.95           C  
ATOM   5948  O   HIS A 776     -15.951 -30.614 -13.681  1.00 16.91           O  
ATOM   5949  CB  HIS A 776     -16.383 -30.133 -10.500  1.00 17.49           C  
ATOM   5950  CG  HIS A 776     -16.428 -28.705 -10.954  1.00 18.06           C  
ATOM   5951  ND1 HIS A 776     -15.369 -28.089 -11.587  1.00 18.70           N  
ATOM   5952  CD2 HIS A 776     -17.416 -27.779 -10.890  1.00 19.37           C  
ATOM   5953  CE1 HIS A 776     -15.695 -26.843 -11.877  1.00 18.49           C  
ATOM   5954  NE2 HIS A 776     -16.931 -26.630 -11.464  1.00 19.00           N  
ATOM   5955  N   LEU A 777     -14.969 -32.258 -12.495  1.00 16.74           N  
ATOM   5956  CA  LEU A 777     -14.001 -32.589 -13.549  1.00 16.60           C  
ATOM   5957  C   LEU A 777     -14.715 -33.069 -14.813  1.00 16.70           C  
ATOM   5958  O   LEU A 777     -14.420 -32.607 -15.925  1.00 16.33           O  
ATOM   5959  CB  LEU A 777     -13.011 -33.652 -13.067  1.00 16.57           C  
ATOM   5960  CG  LEU A 777     -12.098 -33.274 -11.896  1.00 16.64           C  
ATOM   5961  CD1 LEU A 777     -11.424 -34.514 -11.322  1.00 17.78           C  
ATOM   5962  CD2 LEU A 777     -11.070 -32.239 -12.326  1.00 17.69           C  
ATOM   5963  N   ALA A 778     -15.668 -33.982 -14.628  1.00 16.59           N  
ATOM   5964  CA  ALA A 778     -16.491 -34.481 -15.724  1.00 16.66           C  
ATOM   5965  C   ALA A 778     -17.289 -33.359 -16.375  1.00 16.72           C  
ATOM   5966  O   ALA A 778     -17.398 -33.303 -17.603  1.00 16.66           O  
ATOM   5967  CB  ALA A 778     -17.418 -35.585 -15.231  1.00 16.40           C  
ATOM   5968  N   GLU A 779     -17.833 -32.461 -15.555  1.00 16.91           N  
ATOM   5969  CA  GLU A 779     -18.596 -31.323 -16.061  1.00 17.50           C  
ATOM   5970  C   GLU A 779     -17.773 -30.451 -17.006  1.00 17.53           C  
ATOM   5971  O   GLU A 779     -18.246 -30.078 -18.081  1.00 17.51           O  
ATOM   5972  CB  GLU A 779     -19.165 -30.461 -14.927  1.00 17.38           C  
ATOM   5973  CG  GLU A 779     -20.160 -29.423 -15.440  1.00 18.21           C  
ATOM   5974  CD  GLU A 779     -20.741 -28.517 -14.369  1.00 18.56           C  
ATOM   5975  OE1 GLU A 779     -21.510 -27.608 -14.743  1.00 22.17           O  
ATOM   5976  OE2 GLU A 779     -20.443 -28.696 -13.169  1.00 20.72           O  
ATOM   5977  N   LEU A 780     -16.547 -30.128 -16.601  1.00 17.66           N  
ATOM   5978  CA  LEU A 780     -15.708 -29.241 -17.404  1.00 18.10           C  
ATOM   5979  C   LEU A 780     -15.215 -29.904 -18.687  1.00 18.31           C  
ATOM   5980  O   LEU A 780     -15.177 -29.265 -19.735  1.00 18.31           O  
ATOM   5981  CB  LEU A 780     -14.545 -28.668 -16.586  1.00 17.97           C  
ATOM   5982  CG  LEU A 780     -14.884 -27.781 -15.379  1.00 18.83           C  
ATOM   5983  CD1 LEU A 780     -13.678 -26.909 -15.033  1.00 17.91           C  
ATOM   5984  CD2 LEU A 780     -16.130 -26.911 -15.574  1.00 20.17           C  
ATOM   5985  N   VAL A 781     -14.863 -31.185 -18.609  1.00 18.70           N  
ATOM   5986  CA  VAL A 781     -14.472 -31.928 -19.807  1.00 19.27           C  
ATOM   5987  C   VAL A 781     -15.637 -31.966 -20.807  1.00 19.71           C  
ATOM   5988  O   VAL A 781     -15.435 -31.754 -22.004  1.00 19.57           O  
ATOM   5989  CB  VAL A 781     -13.920 -33.337 -19.478  1.00 19.31           C  
ATOM   5990  CG1 VAL A 781     -13.690 -34.153 -20.752  1.00 19.12           C  
ATOM   5991  CG2 VAL A 781     -12.612 -33.224 -18.691  1.00 19.60           C  
ATOM   5992  N   LYS A 782     -16.853 -32.197 -20.310  1.00 19.99           N  
ATOM   5993  CA  LYS A 782     -18.032 -32.171 -21.173  1.00 20.53           C  
ATOM   5994  C   LYS A 782     -18.194 -30.809 -21.861  1.00 21.00           C  
ATOM   5995  O   LYS A 782     -18.575 -30.745 -23.034  1.00 20.86           O  
ATOM   5996  CB  LYS A 782     -19.300 -32.563 -20.405  1.00 20.61           C  
ATOM   5997  CG  LYS A 782     -20.484 -32.861 -21.323  1.00 20.88           C  
ATOM   5998  CD  LYS A 782     -21.669 -33.455 -20.578  1.00 20.59           C  
ATOM   5999  CE  LYS A 782     -22.820 -33.717 -21.542  1.00 21.24           C  
ATOM   6000  NZ  LYS A 782     -24.004 -34.321 -20.867  1.00 20.86           N  
ATOM   6001  N   ARG A 783     -17.883 -29.733 -21.136  1.00 21.43           N  
ATOM   6002  CA  ARG A 783     -17.915 -28.382 -21.700  1.00 22.09           C  
ATOM   6003  C   ARG A 783     -16.881 -28.224 -22.815  1.00 22.16           C  
ATOM   6004  O   ARG A 783     -17.176 -27.639 -23.861  1.00 22.37           O  
ATOM   6005  CB  ARG A 783     -17.686 -27.321 -20.624  1.00 22.32           C  
ATOM   6006  CG  ARG A 783     -18.835 -27.149 -19.651  1.00 23.67           C  
ATOM   6007  CD  ARG A 783     -18.635 -25.900 -18.816  1.00 25.80           C  
ATOM   6008  NE  ARG A 783     -19.395 -25.936 -17.567  1.00 28.39           N  
ATOM   6009  CZ  ARG A 783     -19.263 -25.041 -16.590  1.00 29.31           C  
ATOM   6010  NH1 ARG A 783     -19.987 -25.149 -15.483  1.00 30.11           N  
ATOM   6011  NH2 ARG A 783     -18.404 -24.036 -16.719  1.00 28.78           N  
ATOM   6012  N   VAL A 784     -15.679 -28.749 -22.580  1.00 22.33           N  
ATOM   6013  CA  VAL A 784     -14.609 -28.765 -23.585  1.00 22.60           C  
ATOM   6014  C   VAL A 784     -15.066 -29.524 -24.833  1.00 23.28           C  
ATOM   6015  O   VAL A 784     -14.921 -29.029 -25.952  1.00 22.76           O  
ATOM   6016  CB  VAL A 784     -13.296 -29.366 -23.020  1.00 22.52           C  
ATOM   6017  CG1 VAL A 784     -12.224 -29.495 -24.103  1.00 22.41           C  
ATOM   6018  CG2 VAL A 784     -12.779 -28.512 -21.866  1.00 22.33           C  
ATOM   6019  N   ASN A 785     -15.641 -30.709 -24.626  1.00 23.98           N  
ATOM   6020  CA  ASN A 785     -16.190 -31.512 -25.725  1.00 25.02           C  
ATOM   6021  C   ASN A 785     -17.217 -30.761 -26.571  1.00 25.65           C  
ATOM   6022  O   ASN A 785     -17.191 -30.841 -27.800  1.00 26.10           O  
ATOM   6023  CB  ASN A 785     -16.793 -32.814 -25.191  1.00 24.90           C  
ATOM   6024  CG  ASN A 785     -15.743 -33.780 -24.677  1.00 24.83           C  
ATOM   6025  OD1 ASN A 785     -14.578 -33.732 -25.081  1.00 25.23           O  
ATOM   6026  ND2 ASN A 785     -16.153 -34.676 -23.788  1.00 24.18           N  
ATOM   6027  N   HIS A 786     -18.109 -30.027 -25.912  1.00 26.35           N  
ATOM   6028  CA  HIS A 786     -19.113 -29.227 -26.610  1.00 27.04           C  
ATOM   6029  C   HIS A 786     -18.489 -28.035 -27.341  1.00 26.95           C  
ATOM   6030  O   HIS A 786     -18.968 -27.630 -28.403  1.00 27.25           O  
ATOM   6031  CB  HIS A 786     -20.196 -28.750 -25.641  1.00 27.39           C  
ATOM   6032  CG  HIS A 786     -21.392 -28.162 -26.321  1.00 28.95           C  
ATOM   6033  ND1 HIS A 786     -21.609 -26.803 -26.402  1.00 30.26           N  
ATOM   6034  CD2 HIS A 786     -22.428 -28.748 -26.967  1.00 30.19           C  
ATOM   6035  CE1 HIS A 786     -22.733 -26.578 -27.060  1.00 30.47           C  
ATOM   6036  NE2 HIS A 786     -23.249 -27.742 -27.414  1.00 30.96           N  
ATOM   6037  N   TRP A 787     -17.423 -27.485 -26.763  1.00 26.66           N  
ATOM   6038  CA  TRP A 787     -16.694 -26.360 -27.347  1.00 26.27           C  
ATOM   6039  C   TRP A 787     -15.968 -26.774 -28.627  1.00 26.54           C  
ATOM   6040  O   TRP A 787     -15.937 -26.019 -29.598  1.00 26.46           O  
ATOM   6041  CB  TRP A 787     -15.717 -25.781 -26.321  1.00 25.76           C  
ATOM   6042  CG  TRP A 787     -14.824 -24.690 -26.834  1.00 25.03           C  
ATOM   6043  CD1 TRP A 787     -15.140 -23.369 -26.990  1.00 24.48           C  
ATOM   6044  CD2 TRP A 787     -13.459 -24.827 -27.242  1.00 24.24           C  
ATOM   6045  NE1 TRP A 787     -14.055 -22.676 -27.477  1.00 24.58           N  
ATOM   6046  CE2 TRP A 787     -13.009 -23.548 -27.637  1.00 24.28           C  
ATOM   6047  CE3 TRP A 787     -12.571 -25.908 -27.314  1.00 24.25           C  
ATOM   6048  CZ2 TRP A 787     -11.710 -23.323 -28.102  1.00 24.62           C  
ATOM   6049  CZ3 TRP A 787     -11.280 -25.682 -27.771  1.00 24.38           C  
ATOM   6050  CH2 TRP A 787     -10.862 -24.399 -28.158  1.00 24.71           C  
ATOM   6051  N   LEU A 788     -15.394 -27.976 -28.620  1.00 26.98           N  
ATOM   6052  CA  LEU A 788     -14.727 -28.527 -29.798  1.00 27.57           C  
ATOM   6053  C   LEU A 788     -15.723 -28.862 -30.906  1.00 27.81           C  
ATOM   6054  O   LEU A 788     -16.751 -29.497 -30.660  1.00 28.32           O  
ATOM   6055  CB  LEU A 788     -13.913 -29.771 -29.428  1.00 27.75           C  
ATOM   6056  CG  LEU A 788     -12.570 -29.576 -28.719  1.00 28.30           C  
ATOM   6057  CD1 LEU A 788     -12.063 -30.912 -28.218  1.00 29.42           C  
ATOM   6058  CD2 LEU A 788     -11.536 -28.918 -29.629  1.00 29.03           C  
TER    6059      LEU A 788                                                      
HETATM 6060  PB  ADP A1789      -5.417  -1.654  15.916  1.00  8.11           P  
HETATM 6061  O1B ADP A1789      -5.708  -3.034  16.472  1.00  6.94           O  
HETATM 6062  O2B ADP A1789      -4.532  -0.835  16.806  1.00  9.16           O  
HETATM 6063  O3B ADP A1789      -4.962  -1.639  14.474  1.00  7.97           O  
HETATM 6064  PA  ADP A1789      -8.272  -1.380  16.276  1.00  8.83           P  
HETATM 6065  O1A ADP A1789      -8.635  -2.580  15.453  1.00  7.95           O  
HETATM 6066  O2A ADP A1789      -8.306  -1.475  17.784  1.00  8.06           O  
HETATM 6067  O3A ADP A1789      -6.810  -0.822  15.871  1.00  8.13           O  
HETATM 6068  O5' ADP A1789      -9.208  -0.152  15.829  1.00  8.81           O  
HETATM 6069  C5' ADP A1789      -9.158   1.081  16.536  1.00  8.88           C  
HETATM 6070  C4' ADP A1789     -10.581   1.609  16.646  1.00  9.91           C  
HETATM 6071  O4' ADP A1789     -11.035   1.956  15.342  1.00  9.72           O  
HETATM 6072  C3' ADP A1789     -11.605   0.597  17.144  1.00 10.20           C  
HETATM 6073  O3' ADP A1789     -11.667   0.516  18.571  1.00 11.35           O  
HETATM 6074  C2' ADP A1789     -12.907   1.091  16.547  1.00 10.14           C  
HETATM 6075  O2' ADP A1789     -13.377   2.241  17.274  1.00  9.54           O  
HETATM 6076  C1' ADP A1789     -12.420   1.607  15.210  1.00 10.33           C  
HETATM 6077  N9  ADP A1789     -12.542   0.634  14.095  1.00 10.32           N  
HETATM 6078  C8  ADP A1789     -11.530   0.004  13.463  1.00 10.50           C  
HETATM 6079  N7  ADP A1789     -11.984  -0.767  12.442  1.00 10.34           N  
HETATM 6080  C5  ADP A1789     -13.320  -0.622  12.411  1.00 10.23           C  
HETATM 6081  C6  ADP A1789     -14.433  -1.153  11.591  1.00 10.50           C  
HETATM 6082  N6  ADP A1789     -14.205  -2.014  10.570  1.00 10.90           N  
HETATM 6083  N1  ADP A1789     -15.688  -0.743  11.901  1.00 11.06           N  
HETATM 6084  C2  ADP A1789     -15.941   0.111  12.911  1.00 10.82           C  
HETATM 6085  N3  ADP A1789     -14.984   0.636  13.695  1.00 11.45           N  
HETATM 6086  C4  ADP A1789     -13.679   0.308  13.495  1.00 10.43           C  
HETATM 6087  V   VO4 A1791      -2.938  -1.236  18.203  1.00  9.06           V  
HETATM 6088  O1  VO4 A1791      -1.500  -1.550  19.454  1.00  8.51           O  
HETATM 6089  O2  VO4 A1791      -4.023  -2.639  18.806  1.00  9.30           O  
HETATM 6090  O3  VO4 A1791      -3.305   0.516  18.780  1.00 10.09           O  
HETATM 6091  O4  VO4 A1791      -1.839  -1.495  16.688  1.00 11.10           O  
HETATM 6092  C1  EDO A1792       5.052 -14.764  26.556  1.00 32.24           C  
HETATM 6093  O1  EDO A1792       3.809 -14.105  26.285  1.00 31.99           O  
HETATM 6094  C2  EDO A1792       5.919 -14.731  25.307  1.00 32.14           C  
HETATM 6095  O2  EDO A1792       6.044 -13.379  24.856  1.00 31.75           O  
HETATM 6096  C1  EDO A1793       4.205  -7.310  19.613  1.00 16.80           C  
HETATM 6097  O1  EDO A1793       2.787  -7.207  19.800  1.00 16.33           O  
HETATM 6098  C2  EDO A1793       4.751  -5.907  19.359  1.00 16.71           C  
HETATM 6099  O2  EDO A1793       4.441  -5.543  18.013  1.00 16.46           O  
HETATM 6100  C1  EDO A1794       2.119   7.738  15.298  1.00 19.16           C  
HETATM 6101  O1  EDO A1794       1.616   6.779  16.241  1.00 17.35           O  
HETATM 6102  C2  EDO A1794       0.978   8.572  14.712  1.00 20.12           C  
HETATM 6103  O2  EDO A1794      -0.016   7.699  14.168  1.00 20.24           O  
HETATM 6104  C1  EDO A1795     -16.979  -2.906   2.404  1.00 18.23           C  
HETATM 6105  O1  EDO A1795     -16.030  -2.135   1.653  1.00 16.05           O  
HETATM 6106  C2  EDO A1795     -17.976  -2.017   3.136  1.00 17.97           C  
HETATM 6107  O2  EDO A1795     -17.309  -0.985   3.874  1.00 17.67           O  
HETATM 6108  C1  EDO A1796     -10.497  14.477  -5.689  1.00 35.22           C  
HETATM 6109  O1  EDO A1796      -9.171  14.960  -5.916  1.00 36.03           O  
HETATM 6110  C2  EDO A1796     -10.452  13.325  -4.696  1.00 34.41           C  
HETATM 6111  O2  EDO A1796      -9.307  12.496  -4.943  1.00 32.89           O  
HETATM 6112  C1  EDO A1797       8.292  11.158  15.662  1.00 27.06           C  
HETATM 6113  O1  EDO A1797       8.683  10.347  14.519  1.00 28.42           O  
HETATM 6114  C2  EDO A1797       8.802  10.474  16.935  1.00 25.89           C  
HETATM 6115  O2  EDO A1797      10.235  10.507  16.922  1.00 24.78           O  
HETATM 6116  C1  EDO A1798       3.235  -4.816  22.868  1.00 21.35           C  
HETATM 6117  O1  EDO A1798       3.473  -6.203  22.584  1.00 21.00           O  
HETATM 6118  C2  EDO A1798       4.283  -4.202  23.807  1.00 22.81           C  
HETATM 6119  O2  EDO A1798       5.015  -5.184  24.559  1.00 23.39           O  
HETATM 6120  S   SO4 A1799     -25.008  -3.728  43.326  1.00 22.55           S  
HETATM 6121  O1  SO4 A1799     -24.299  -3.568  42.060  1.00 24.72           O  
HETATM 6122  O2  SO4 A1799     -26.306  -3.066  43.243  1.00 23.92           O  
HETATM 6123  O3  SO4 A1799     -25.237  -5.146  43.561  1.00 23.86           O  
HETATM 6124  O4  SO4 A1799     -24.204  -3.202  44.422  1.00 22.90           O  
HETATM 6125  S   SO4 A1800      21.317 -15.780  19.377  0.50 26.97           S  
HETATM 6126  O1  SO4 A1800      21.257 -16.782  18.317  0.50 27.10           O  
HETATM 6127  O2  SO4 A1800      20.034 -15.092  19.481  0.50 27.08           O  
HETATM 6128  O3  SO4 A1800      21.618 -16.437  20.645  0.50 26.94           O  
HETATM 6129  O4  SO4 A1800      22.359 -14.808  19.069  0.50 27.05           O  
HETATM 6130 MG    MG A1801      -5.139  -3.919  18.238  1.00  7.52          MG  
HETATM 6131  O   HOH A2001      -3.690  18.125 -18.929  1.00 28.06           O  
HETATM 6132  O   HOH A2002      -4.717  11.654 -17.552  1.00 25.09           O  
HETATM 6133  O   HOH A2003      -7.853   8.629 -11.031  1.00 15.38           O  
HETATM 6134  O   HOH A2004       2.052  13.737   0.177  1.00 25.60           O  
HETATM 6135  O   HOH A2005       4.232  21.807  -1.178  1.00 30.15           O  
HETATM 6136  O   HOH A2006       2.325  21.017  -5.102  1.00 30.12           O  
HETATM 6137  O   HOH A2007      -0.711  15.461   6.168  1.00 37.08           O  
HETATM 6138  O   HOH A2008       3.420  17.336  -1.808  1.00 27.82           O  
HETATM 6139  O   HOH A2009       0.157  23.669  -1.946  1.00 36.89           O  
HETATM 6140  O   HOH A2010       2.780  15.713   1.990  1.00 28.21           O  
HETATM 6141  O   HOH A2011       3.143  19.794  -2.697  1.00 26.65           O  
HETATM 6142  O   HOH A2012      -3.045  14.661   5.118  1.00 18.18           O  
HETATM 6143  O   HOH A2013      -7.151  14.538   1.760  1.00 21.27           O  
HETATM 6144  O   HOH A2014      -6.442  12.427  -1.617  1.00 15.98           O  
HETATM 6145  O   HOH A2015     -11.316  13.847  -8.807  1.00 24.00           O  
HETATM 6146  O   HOH A2016       2.473  14.538  -2.409  1.00 27.71           O  
HETATM 6147  O   HOH A2017      -7.128  16.255  -4.005  1.00 25.67           O  
HETATM 6148  O   HOH A2018      -6.534  21.159  -7.635  1.00 26.49           O  
HETATM 6149  O   HOH A2019      -1.340  23.401  -4.626  1.00 33.76           O  
HETATM 6150  O   HOH A2020      -7.972  26.893  -8.119  1.00 32.96           O  
HETATM 6151  O   HOH A2021     -16.338  12.992   0.548  1.00 31.44           O  
HETATM 6152  O   HOH A2022      -1.763  19.809 -22.543  1.00 36.02           O  
HETATM 6153  O   HOH A2023     -10.057  12.708 -10.871  1.00 31.73           O  
HETATM 6154  O   HOH A2024     -20.687   9.182  -7.070  1.00 28.05           O  
HETATM 6155  O   HOH A2025     -20.138  -2.384  -2.389  1.00 26.09           O  
HETATM 6156  O   HOH A2026     -11.958  -7.984 -11.811  1.00 28.23           O  
HETATM 6157  O   HOH A2027     -10.263  -9.617  -6.831  1.00 33.97           O  
HETATM 6158  O   HOH A2028     -13.163  -6.858  -9.589  1.00 19.91           O  
HETATM 6159  O   HOH A2029       6.694  24.010 -16.932  1.00 25.71           O  
HETATM 6160  O   HOH A2030       3.912   4.657 -11.501  1.00 27.53           O  
HETATM 6161  O   HOH A2031      -9.294  27.013 -11.380  1.00 38.50           O  
HETATM 6162  O   HOH A2032      -7.061  28.333 -11.957  1.00 44.42           O  
HETATM 6163  O   HOH A2033     -14.672  10.512   3.365  1.00 20.35           O  
HETATM 6164  O   HOH A2034     -17.111  11.697   2.848  1.00 24.38           O  
HETATM 6165  O   HOH A2035     -23.178   1.268   3.472  1.00 30.17           O  
HETATM 6166  O   HOH A2036     -23.486  -2.909   0.827  1.00 29.70           O  
HETATM 6167  O   HOH A2037       4.199  19.992  -7.345  1.00 22.80           O  
HETATM 6168  O   HOH A2038       5.076  26.135  -8.016  1.00 31.87           O  
HETATM 6169  O   HOH A2039       4.493  12.881 -16.390  1.00 38.23           O  
HETATM 6170  O   HOH A2040       6.338   9.043 -12.628  1.00 35.79           O  
HETATM 6171  O   HOH A2041      10.956  14.432 -13.378  1.00 30.91           O  
HETATM 6172  O   HOH A2042     -20.289   6.826  16.002  1.00 22.30           O  
HETATM 6173  O   HOH A2043     -16.040   8.784  17.379  1.00 27.48           O  
HETATM 6174  O   HOH A2044     -18.689  -4.413  14.332  1.00 36.12           O  
HETATM 6175  O   HOH A2045     -23.862  -2.097  13.181  1.00 30.71           O  
HETATM 6176  O   HOH A2046     -25.209  -9.516  47.759  1.00 32.81           O  
HETATM 6177  O   HOH A2047       1.570  11.590 -17.219  1.00 35.53           O  
HETATM 6178  O   HOH A2048      -7.285  10.439 -18.385  1.00 23.36           O  
HETATM 6179  O   HOH A2049     -26.466 -16.150   0.898  1.00 30.15           O  
HETATM 6180  O   HOH A2050     -20.834  -5.674   3.029  1.00 28.89           O  
HETATM 6181  O   HOH A2051     -10.151  10.107 -11.707  1.00 16.97           O  
HETATM 6182  O   HOH A2052     -10.749   4.471 -16.362  1.00 34.43           O  
HETATM 6183  O   HOH A2053     -19.467  -3.909  -0.213  1.00 19.44           O  
HETATM 6184  O   HOH A2054      -9.553   6.071 -17.746  1.00 28.73           O  
HETATM 6185  O   HOH A2055     -24.996 -11.961  -2.841  1.00 35.95           O  
HETATM 6186  O   HOH A2056     -20.078   8.522 -13.084  1.00 34.41           O  
HETATM 6187  O   HOH A2057     -18.871 -17.001 -10.391  1.00 34.52           O  
HETATM 6188  O   HOH A2058     -12.262  -7.620  -7.162  1.00 19.71           O  
HETATM 6189  O   HOH A2059     -14.686  11.823  -6.968  1.00 34.15           O  
HETATM 6190  O   HOH A2060     -17.816   9.651  -6.172  1.00 23.66           O  
HETATM 6191  O   HOH A2061     -12.591   7.369  -9.979  1.00 19.81           O  
HETATM 6192  O   HOH A2062     -18.016   0.042  -7.506  1.00 24.58           O  
HETATM 6193  O   HOH A2063      -3.531 -22.061  -5.578  1.00 31.68           O  
HETATM 6194  O   HOH A2064     -15.075  -3.008  -9.927  1.00 18.75           O  
HETATM 6195  O   HOH A2065     -17.727  -2.408  -3.863  1.00 17.29           O  
HETATM 6196  O   HOH A2066     -18.428  -8.080  -6.814  1.00 24.55           O  
HETATM 6197  O   HOH A2067      -9.025  -7.223 -11.706  1.00 25.52           O  
HETATM 6198  O   HOH A2068      -8.184  -9.599  -8.813  1.00 26.16           O  
HETATM 6199  O   HOH A2069      -1.745 -28.320  12.813  1.00 32.49           O  
HETATM 6200  O   HOH A2070     -12.497  -4.333 -10.168  1.00 19.01           O  
HETATM 6201  O   HOH A2071      -5.520  -2.433 -15.772  1.00 29.36           O  
HETATM 6202  O   HOH A2072      -7.264   8.763 -20.547  1.00 24.76           O  
HETATM 6203  O   HOH A2073       2.458   1.287 -10.909  1.00 26.64           O  
HETATM 6204  O   HOH A2074       0.353   5.167 -14.560  1.00 20.04           O  
HETATM 6205  O   HOH A2075       5.235   5.793  -7.425  1.00 25.52           O  
HETATM 6206  O   HOH A2076       3.137   4.796  -8.793  1.00 17.16           O  
HETATM 6207  O   HOH A2077      -5.070  10.989  -6.073  1.00 14.52           O  
HETATM 6208  O   HOH A2078      -8.318   6.498  -9.532  1.00 10.45           O  
HETATM 6209  O   HOH A2079     -10.934   5.290  -9.324  1.00 14.23           O  
HETATM 6210  O   HOH A2080     -13.127   9.799   1.232  1.00 17.66           O  
HETATM 6211  O   HOH A2081     -13.907  11.382  -3.192  1.00 40.04           O  
HETATM 6212  O   HOH A2082     -19.417  10.392   2.571  1.00 30.58           O  
HETATM 6213  O   HOH A2083     -22.158   2.714  -0.802  1.00 23.01           O  
HETATM 6214  O   HOH A2084     -16.242   5.654   5.515  1.00 18.27           O  
HETATM 6215  O   HOH A2085     -22.188   7.601   5.764  1.00 28.60           O  
HETATM 6216  O   HOH A2086     -20.963   0.067   2.217  1.00 27.60           O  
HETATM 6217  O   HOH A2087     -21.376  -0.350  -0.999  1.00 27.49           O  
HETATM 6218  O   HOH A2088     -11.678   2.741   1.104  1.00 12.32           O  
HETATM 6219  O   HOH A2089     -10.018   0.445   0.745  1.00  9.92           O  
HETATM 6220  O   HOH A2090       2.139 -19.695  23.356  1.00 41.98           O  
HETATM 6221  O   HOH A2091      -0.880 -20.368  26.669  1.00 21.82           O  
HETATM 6222  O   HOH A2092     -14.410 -10.884  -3.242  1.00 12.70           O  
HETATM 6223  O   HOH A2093      -0.354 -11.668  -3.600  1.00 33.06           O  
HETATM 6224  O   HOH A2094      -3.909 -16.439  -4.735  1.00 30.18           O  
HETATM 6225  O   HOH A2095      -6.159 -13.717  -0.668  1.00 25.16           O  
HETATM 6226  O   HOH A2096     -15.738   7.125   7.859  1.00 12.28           O  
HETATM 6227  O   HOH A2097      -7.575   4.593  16.987  1.00  9.31           O  
HETATM 6228  O   HOH A2098     -17.894   7.577  15.185  1.00 22.02           O  
HETATM 6229  O   HOH A2099     -19.069  -9.586  38.704  1.00 30.48           O  
HETATM 6230  O   HOH A2100     -24.273  -8.319  45.286  1.00 21.82           O  
HETATM 6231  O   HOH A2101     -20.833   4.208  15.083  1.00 22.54           O  
HETATM 6232  O   HOH A2102     -17.541  -1.717  16.479  1.00 31.11           O  
HETATM 6233  O   HOH A2103     -19.302  -2.397  12.729  1.00 31.69           O  
HETATM 6234  O   HOH A2104     -24.680   4.865   8.515  1.00 37.72           O  
HETATM 6235  O   HOH A2105     -21.914  -2.883  11.618  1.00 22.91           O  
HETATM 6236  O   HOH A2106     -24.601  -0.455   4.999  1.00 31.40           O  
HETATM 6237  O   HOH A2107     -25.792  -3.439  11.581  1.00 28.99           O  
HETATM 6238  O   HOH A2108     -22.854  -5.349  10.636  1.00 19.88           O  
HETATM 6239  O   HOH A2109     -27.499  -7.682   6.486  1.00 26.11           O  
HETATM 6240  O   HOH A2110     -26.446 -10.433  12.296  1.00 28.42           O  
HETATM 6241  O   HOH A2111     -27.169 -14.219   2.855  1.00 26.11           O  
HETATM 6242  O   HOH A2112     -28.128 -11.168   9.304  1.00 25.42           O  
HETATM 6243  O   HOH A2113     -20.255   8.263  23.077  1.00 26.92           O  
HETATM 6244  O   HOH A2114     -23.440  -6.241   3.562  1.00 33.97           O  
HETATM 6245  O   HOH A2115     -22.652 -18.076  -0.180  1.00 22.21           O  
HETATM 6246  O   HOH A2116     -23.631  -9.509   0.817  1.00 26.81           O  
HETATM 6247  O   HOH A2117     -15.407   4.112  48.504  1.00 38.54           O  
HETATM 6248  O   HOH A2118     -21.386  11.200  41.251  1.00 40.43           O  
HETATM 6249  O   HOH A2119     -20.213  -6.647   0.705  1.00 23.14           O  
HETATM 6250  O   HOH A2120     -15.845 -15.100  -0.472  1.00 13.28           O  
HETATM 6251  O   HOH A2121      -7.681  13.668  41.994  1.00 32.70           O  
HETATM 6252  O   HOH A2122     -23.273 -19.634   8.326  1.00 28.85           O  
HETATM 6253  O   HOH A2123     -20.112 -22.856   0.545  1.00 35.60           O  
HETATM 6254  O   HOH A2124     -22.241  12.113  29.802  1.00 40.54           O  
HETATM 6255  O   HOH A2125     -23.324 -14.659  -5.281  1.00 27.58           O  
HETATM 6256  O   HOH A2126     -15.389 -19.848  -9.027  1.00 23.67           O  
HETATM 6257  O   HOH A2127     -17.513 -18.048  -6.752  1.00 19.04           O  
HETATM 6258  O   HOH A2128     -15.581 -13.245  -2.619  1.00 13.57           O  
HETATM 6259  O   HOH A2129     -11.636 -12.774  -9.842  1.00 22.34           O  
HETATM 6260  O   HOH A2130     -19.705 -16.937  -7.784  1.00 25.34           O  
HETATM 6261  O   HOH A2131     -21.146 -14.147  -6.951  1.00 30.35           O  
HETATM 6262  O   HOH A2132     -14.764  -7.698  -5.731  1.00 16.88           O  
HETATM 6263  O   HOH A2133     -19.710  -8.836  24.079  1.00 36.83           O  
HETATM 6264  O   HOH A2134     -16.631  -3.761  -0.563  1.00 14.90           O  
HETATM 6265  O   HOH A2135     -12.731 -15.440  -1.491  1.00 18.78           O  
HETATM 6266  O   HOH A2136      -8.508 -21.939  38.376  1.00 35.52           O  
HETATM 6267  O   HOH A2137      -4.211 -15.432  -1.233  1.00 36.66           O  
HETATM 6268  O   HOH A2138      -6.408 -22.541  -4.538  1.00 35.80           O  
HETATM 6269  O   HOH A2139      -0.298 -27.279  10.366  1.00 30.85           O  
HETATM 6270  O   HOH A2140       0.285 -27.388   6.578  1.00 22.41           O  
HETATM 6271  O   HOH A2141      -1.543 -21.318   0.188  1.00 29.26           O  
HETATM 6272  O   HOH A2142      -0.473  -8.189  12.866  1.00 16.60           O  
HETATM 6273  O   HOH A2143      -0.439  -7.643   6.161  1.00 14.47           O  
HETATM 6274  O   HOH A2144      -0.018  -5.307   4.560  1.00 24.45           O  
HETATM 6275  O   HOH A2145       1.821  -7.328  11.047  1.00 24.77           O  
HETATM 6276  O   HOH A2146      14.595 -13.011  55.021  1.00 36.98           O  
HETATM 6277  O   HOH A2147       2.708   6.570  11.279  1.00 31.37           O  
HETATM 6278  O   HOH A2148      -0.571   7.868   9.808  1.00 15.98           O  
HETATM 6279  O   HOH A2149       2.103   3.402   8.985  1.00 28.84           O  
HETATM 6280  O   HOH A2150      -0.917   3.193  20.524  1.00 15.46           O  
HETATM 6281  O   HOH A2151      -8.702  -1.040   8.817  1.00 11.69           O  
HETATM 6282  O   HOH A2152     -15.733  -5.021  18.342  1.00 33.31           O  
HETATM 6283  O   HOH A2153     -16.155  -3.075  14.901  1.00 32.26           O  
HETATM 6284  O   HOH A2154      17.651  -4.070  43.463  1.00 40.11           O  
HETATM 6285  O   HOH A2155     -14.474 -12.411  16.824  1.00 19.57           O  
HETATM 6286  O   HOH A2156      -1.116 -20.234  33.400  1.00 24.95           O  
HETATM 6287  O   HOH A2157      -0.797 -24.559  26.204  1.00 25.68           O  
HETATM 6288  O   HOH A2158     -19.094 -17.749  15.794  1.00 23.51           O  
HETATM 6289  O   HOH A2159      -3.648 -27.644  22.174  1.00 41.05           O  
HETATM 6290  O   HOH A2160     -24.092 -16.858   9.109  1.00 31.74           O  
HETATM 6291  O   HOH A2161     -20.255 -15.516  15.812  1.00 37.81           O  
HETATM 6292  O   HOH A2162     -17.580 -23.156   1.544  1.00 36.01           O  
HETATM 6293  O   HOH A2163     -18.952 -27.275   9.351  1.00 34.23           O  
HETATM 6294  O   HOH A2164     -21.447 -14.478  18.462  1.00 35.85           O  
HETATM 6295  O   HOH A2165     -15.435 -21.296  18.923  1.00 30.51           O  
HETATM 6296  O   HOH A2166     -17.965 -22.821  20.520  1.00 36.74           O  
HETATM 6297  O   HOH A2167       5.745  17.251  18.065  1.00 35.17           O  
HETATM 6298  O   HOH A2168       2.280 -15.703  -1.993  1.00 30.85           O  
HETATM 6299  O   HOH A2169      13.264  -8.691  -5.327  1.00 30.33           O  
HETATM 6300  O   HOH A2170      -6.175  -6.927  21.470  1.00 17.34           O  
HETATM 6301  O   HOH A2171      13.373   0.596 -11.351  1.00 36.19           O  
HETATM 6302  O   HOH A2172       9.684   2.142  -4.034  1.00 33.22           O  
HETATM 6303  O   HOH A2173      -3.401  10.245  17.331  1.00 19.87           O  
HETATM 6304  O   HOH A2174      -4.579   7.634  16.272  1.00 14.42           O  
HETATM 6305  O   HOH A2175     -10.332   9.512  23.872  1.00 35.10           O  
HETATM 6306  O   HOH A2176      -9.505   4.631  19.049  1.00 12.15           O  
HETATM 6307  O   HOH A2177      -7.069   8.008  23.444  1.00 13.29           O  
HETATM 6308  O   HOH A2178      31.238   0.910  24.622  1.00 37.76           O  
HETATM 6309  O   HOH A2179      -2.902  -8.509  20.027  1.00 29.15           O  
HETATM 6310  O   HOH A2180      -9.141 -13.679  20.071  1.00 31.48           O  
HETATM 6311  O   HOH A2181      -8.632  -9.267  17.609  1.00 26.91           O  
HETATM 6312  O   HOH A2182      28.227  11.648  23.315  1.00 33.05           O  
HETATM 6313  O   HOH A2183      24.754   7.849  15.015  1.00 21.65           O  
HETATM 6314  O   HOH A2184     -12.553 -34.805  14.216  1.00 36.25           O  
HETATM 6315  O   HOH A2185      15.463  11.618  10.815  1.00 25.67           O  
HETATM 6316  O   HOH A2186      14.797  17.685  25.468  1.00 35.85           O  
HETATM 6317  O   HOH A2187     -17.050 -27.003   7.016  1.00 30.60           O  
HETATM 6318  O   HOH A2188      13.054   8.593   7.420  1.00 33.14           O  
HETATM 6319  O   HOH A2189     -14.100 -30.548  19.139  1.00 37.73           O  
HETATM 6320  O   HOH A2190      15.362  12.317  27.729  1.00 38.63           O  
HETATM 6321  O   HOH A2191      -1.362 -19.893  18.136  1.00 21.48           O  
HETATM 6322  O   HOH A2192      -0.725 -18.578  24.686  1.00 18.01           O  
HETATM 6323  O   HOH A2193       3.761 -17.571  23.042  1.00 41.96           O  
HETATM 6324  O   HOH A2194       9.698  -3.367  25.898  1.00 15.15           O  
HETATM 6325  O   HOH A2195      16.456 -15.086  37.142  1.00 33.45           O  
HETATM 6326  O   HOH A2196       6.573  -8.817  27.737  1.00 21.78           O  
HETATM 6327  O   HOH A2197       4.113   2.724  26.184  1.00 17.58           O  
HETATM 6328  O   HOH A2198       7.070  -3.601  29.043  1.00 26.79           O  
HETATM 6329  O   HOH A2199       4.058   2.222  29.155  1.00 42.61           O  
HETATM 6330  O   HOH A2200      -5.800 -22.259  38.585  1.00 30.22           O  
HETATM 6331  O   HOH A2201       1.952   4.017  24.548  1.00 28.37           O  
HETATM 6332  O   HOH A2202       1.969   3.049  30.421  1.00 30.24           O  
HETATM 6333  O   HOH A2203      -0.789   5.536  37.248  1.00 16.32           O  
HETATM 6334  O   HOH A2204      -0.139  10.713  28.041  1.00 23.36           O  
HETATM 6335  O   HOH A2205       1.313   5.520  29.016  1.00 22.75           O  
HETATM 6336  O   HOH A2206      -7.596   1.501  29.396  1.00  9.66           O  
HETATM 6337  O   HOH A2207     -14.130  -6.040  25.600  1.00 33.59           O  
HETATM 6338  O   HOH A2208     -12.133  -3.676  24.632  1.00 28.52           O  
HETATM 6339  O   HOH A2209      -3.574  15.809  12.649  1.00 34.49           O  
HETATM 6340  O   HOH A2210     -20.897   1.148  40.010  1.00 24.36           O  
HETATM 6341  O   HOH A2211     -22.020  -5.887  38.575  1.00 32.79           O  
HETATM 6342  O   HOH A2212     -22.102  -1.336  40.753  1.00 28.53           O  
HETATM 6343  O   HOH A2213     -20.490  -7.545  40.015  1.00 21.04           O  
HETATM 6344  O   HOH A2214     -22.018  -9.542  41.474  1.00 32.31           O  
HETATM 6345  O   HOH A2215     -22.037  -9.378  44.135  1.00 26.44           O  
HETATM 6346  O   HOH A2216       1.923  10.963   7.676  1.00 31.53           O  
HETATM 6347  O   HOH A2217     -24.042  -5.341  48.721  1.00 21.45           O  
HETATM 6348  O   HOH A2218       6.591   3.059  -3.211  1.00 27.51           O  
HETATM 6349  O   HOH A2219       8.236   4.257  -0.914  1.00 30.95           O  
HETATM 6350  O   HOH A2220      -1.330 -26.397  -6.931  1.00 30.26           O  
HETATM 6351  O   HOH A2221      -9.510   1.475  48.476  1.00 25.68           O  
HETATM 6352  O   HOH A2222     -11.951  10.477  45.297  1.00 27.95           O  
HETATM 6353  O   HOH A2223     -12.678   8.027  47.069  1.00 26.32           O  
HETATM 6354  O   HOH A2224     -15.465 -20.608 -14.851  1.00 39.39           O  
HETATM 6355  O   HOH A2225      -5.401   5.783  35.001  1.00 27.02           O  
HETATM 6356  O   HOH A2226      -3.571   8.022  46.398  1.00 36.54           O  
HETATM 6357  O   HOH A2227       0.807   8.270  42.751  1.00 36.37           O  
HETATM 6358  O   HOH A2228      -5.352  10.836  39.675  1.00 28.32           O  
HETATM 6359  O   HOH A2229     -13.345   7.839  37.483  1.00 17.76           O  
HETATM 6360  O   HOH A2230      -7.116  11.838  37.951  1.00 30.06           O  
HETATM 6361  O   HOH A2231     -15.534 -13.128 -11.816  1.00 30.12           O  
HETATM 6362  O   HOH A2232     -12.283 -26.302  -4.687  1.00 26.45           O  
HETATM 6363  O   HOH A2233     -18.507   7.111  25.450  1.00 27.44           O  
HETATM 6364  O   HOH A2234     -13.197 -36.016  -4.506  1.00 28.46           O  
HETATM 6365  O   HOH A2235     -25.274  11.209  32.702  1.00 31.37           O  
HETATM 6366  O   HOH A2236     -25.887   3.203  25.950  1.00 32.96           O  
HETATM 6367  O   HOH A2237     -30.109   8.182  30.086  1.00 38.75           O  
HETATM 6368  O   HOH A2238     -23.952  -0.405  31.133  1.00 30.90           O  
HETATM 6369  O   HOH A2239     -24.534   7.077  40.081  1.00 30.63           O  
HETATM 6370  O   HOH A2240     -14.234   5.903  46.341  1.00 27.02           O  
HETATM 6371  O   HOH A2241     -22.893   9.485  40.007  1.00 31.64           O  
HETATM 6372  O   HOH A2242     -15.241   8.478  44.510  1.00 35.70           O  
HETATM 6373  O   HOH A2243     -14.060  11.404  43.861  1.00 30.41           O  
HETATM 6374  O   HOH A2244     -14.041  17.285  40.599  1.00 30.27           O  
HETATM 6375  O   HOH A2245      -8.803  12.526  39.800  1.00 24.58           O  
HETATM 6376  O   HOH A2246     -19.145  13.935  35.256  1.00 43.01           O  
HETATM 6377  O   HOH A2247     -19.864  12.751  31.091  1.00 23.22           O  
HETATM 6378  O   HOH A2248     -16.539  14.511  28.837  1.00 30.40           O  
HETATM 6379  O   HOH A2249     -13.246  11.756  25.000  1.00 28.68           O  
HETATM 6380  O   HOH A2250     -13.175   8.843  19.986  1.00 33.36           O  
HETATM 6381  O   HOH A2251     -17.365  -2.391  23.685  1.00 28.83           O  
HETATM 6382  O   HOH A2252     -19.179   4.723  26.059  1.00 23.14           O  
HETATM 6383  O   HOH A2253     -19.381   3.121  31.355  1.00 17.65           O  
HETATM 6384  O   HOH A2254     -13.676  -0.784  28.654  1.00 20.46           O  
HETATM 6385  O   HOH A2255     -17.266  -5.952  25.396  1.00 37.28           O  
HETATM 6386  O   HOH A2256     -22.947  -9.872  33.176  1.00 22.61           O  
HETATM 6387  O   HOH A2257     -20.375 -10.644  25.963  1.00 29.94           O  
HETATM 6388  O   HOH A2258     -23.326  -0.168  26.984  1.00 48.27           O  
HETATM 6389  O   HOH A2259     -20.011 -20.689  33.276  1.00 36.65           O  
HETATM 6390  O   HOH A2260     -14.550 -23.321  30.026  1.00 24.12           O  
HETATM 6391  O   HOH A2261     -12.816 -22.558  39.989  1.00 38.23           O  
HETATM 6392  O   HOH A2262     -20.611 -20.173  38.611  1.00 33.23           O  
HETATM 6393  O   HOH A2263     -18.115 -21.335  41.280  1.00 35.75           O  
HETATM 6394  O   HOH A2264      -9.460 -22.769  36.014  1.00 38.03           O  
HETATM 6395  O   HOH A2265     -10.215 -20.340  39.793  1.00 27.67           O  
HETATM 6396  O   HOH A2266     -13.088 -17.103  44.219  1.00 24.98           O  
HETATM 6397  O   HOH A2267      -1.858   1.305  43.330  1.00 11.81           O  
HETATM 6398  O   HOH A2268      -4.743   0.558  49.189  1.00 18.52           O  
HETATM 6399  O   HOH A2269       7.620   4.848  48.288  1.00 21.02           O  
HETATM 6400  O   HOH A2270      11.752   8.942  52.903  1.00 27.77           O  
HETATM 6401  O   HOH A2271      17.875   5.534  55.534  1.00 26.95           O  
HETATM 6402  O   HOH A2272      22.784   9.358  61.430  1.00 33.55           O  
HETATM 6403  O   HOH A2273      13.642   1.827  61.840  1.00 28.60           O  
HETATM 6404  O   HOH A2274      14.349  -0.866  58.526  1.00 30.09           O  
HETATM 6405  O   HOH A2275      22.654  -1.640  56.693  1.00 17.75           O  
HETATM 6406  O   HOH A2276      10.757  -2.136  58.326  1.00 32.61           O  
HETATM 6407  O   HOH A2277       8.234  -1.416  57.642  1.00 23.30           O  
HETATM 6408  O   HOH A2278       5.128   6.946  58.268  1.00 27.37           O  
HETATM 6409  O   HOH A2279       2.896   7.633  56.923  1.00 26.05           O  
HETATM 6410  O   HOH A2280      -2.716   2.190  53.098  1.00 23.29           O  
HETATM 6411  O   HOH A2281      -3.684  -9.071  55.722  1.00 24.09           O  
HETATM 6412  O   HOH A2282      -5.549 -14.454  52.632  1.00 28.82           O  
HETATM 6413  O   HOH A2283      -2.839 -11.556  55.273  1.00 28.39           O  
HETATM 6414  O   HOH A2284       8.926 -12.503  57.808  1.00 37.20           O  
HETATM 6415  O   HOH A2285       7.830 -16.671  57.247  1.00 32.98           O  
HETATM 6416  O   HOH A2286       3.489 -15.315  53.241  1.00 23.70           O  
HETATM 6417  O   HOH A2287      13.480  -8.699  48.233  1.00 27.62           O  
HETATM 6418  O   HOH A2288      11.989  -4.199  57.139  1.00 32.55           O  
HETATM 6419  O   HOH A2289      14.969  -1.990  55.176  1.00 18.36           O  
HETATM 6420  O   HOH A2290      14.932 -10.916  53.005  1.00 32.57           O  
HETATM 6421  O   HOH A2291      24.201 -14.942  55.239  1.00 37.48           O  
HETATM 6422  O   HOH A2292      19.931  -9.483  58.909  1.00 27.73           O  
HETATM 6423  O   HOH A2293      12.147 -10.339  60.198  1.00 34.43           O  
HETATM 6424  O   HOH A2294      13.445 -12.953  57.411  1.00 33.49           O  
HETATM 6425  O   HOH A2295      16.566   5.443  47.654  1.00 24.83           O  
HETATM 6426  O   HOH A2296      14.600  -4.343  44.521  1.00 27.68           O  
HETATM 6427  O   HOH A2297      20.882  -1.879  49.536  1.00 27.92           O  
HETATM 6428  O   HOH A2298      11.198  -2.863  39.319  1.00 30.24           O  
HETATM 6429  O   HOH A2299      16.578  -2.136  42.466  1.00 30.72           O  
HETATM 6430  O   HOH A2300       2.162 -12.003  29.857  1.00 16.73           O  
HETATM 6431  O   HOH A2301       0.291 -18.045  34.788  1.00 27.30           O  
HETATM 6432  O   HOH A2302       3.094 -18.183  32.926  1.00 30.39           O  
HETATM 6433  O   HOH A2303       4.471 -13.860  32.812  1.00 26.11           O  
HETATM 6434  O   HOH A2304      -0.360 -18.992  28.978  1.00 17.99           O  
HETATM 6435  O   HOH A2305      -2.557 -22.492  26.590  1.00 18.17           O  
HETATM 6436  O   HOH A2306      -6.943 -24.909  23.114  1.00 17.86           O  
HETATM 6437  O   HOH A2307      -5.450 -26.357  26.506  1.00 40.56           O  
HETATM 6438  O   HOH A2308     -13.736 -26.040  28.780  1.00 28.52           O  
HETATM 6439  O   HOH A2309      -7.428 -23.335  34.384  1.00 36.75           O  
HETATM 6440  O   HOH A2310     -13.202 -27.311  21.259  1.00 28.19           O  
HETATM 6441  O   HOH A2311      -6.198 -27.888  22.741  1.00 19.29           O  
HETATM 6442  O   HOH A2312     -10.367 -33.513  17.955  1.00 36.66           O  
HETATM 6443  O   HOH A2313      -3.068 -30.654  16.090  1.00 28.88           O  
HETATM 6444  O   HOH A2314      -3.568  -5.132  17.401  1.00 10.12           O  
HETATM 6445  O   HOH A2315       0.912  -0.389  19.082  1.00 11.50           O  
HETATM 6446  O   HOH A2316       7.178  13.077  17.991  1.00 28.81           O  
HETATM 6447  O   HOH A2317       4.799  19.257  20.244  1.00 40.32           O  
HETATM 6448  O   HOH A2318       2.318  12.191  22.113  1.00 21.22           O  
HETATM 6449  O   HOH A2319       6.187  16.809  26.109  1.00 23.82           O  
HETATM 6450  O   HOH A2320       4.705  11.313  24.803  1.00 19.41           O  
HETATM 6451  O   HOH A2321       6.666   3.889  26.952  1.00 38.00           O  
HETATM 6452  O   HOH A2322      13.054  -0.731  16.946  1.00 24.68           O  
HETATM 6453  O   HOH A2323       3.062  -1.038  10.842  1.00 34.93           O  
HETATM 6454  O   HOH A2324       4.330  -4.306   9.768  1.00 16.88           O  
HETATM 6455  O   HOH A2325       1.807  -4.146  11.408  1.00 17.91           O  
HETATM 6456  O   HOH A2326      13.378 -11.680  10.351  1.00 26.52           O  
HETATM 6457  O   HOH A2327      11.070 -11.113   9.026  1.00 20.77           O  
HETATM 6458  O   HOH A2328      13.509 -10.306   2.033  1.00 36.96           O  
HETATM 6459  O   HOH A2329       8.050  -2.615   0.896  1.00 21.82           O  
HETATM 6460  O   HOH A2330      10.960 -13.012   6.964  1.00 32.92           O  
HETATM 6461  O   HOH A2331       8.722 -16.689   2.802  1.00 27.85           O  
HETATM 6462  O   HOH A2332       4.659 -15.061  -3.402  1.00 32.76           O  
HETATM 6463  O   HOH A2333       1.928 -17.750   0.575  1.00 26.82           O  
HETATM 6464  O   HOH A2334      13.278 -10.915  -6.776  1.00 30.67           O  
HETATM 6465  O   HOH A2335       9.606 -18.142  -5.261  1.00 28.88           O  
HETATM 6466  O   HOH A2336      10.809 -11.660 -12.321  1.00 21.22           O  
HETATM 6467  O   HOH A2337      13.756 -11.938  -9.166  1.00 29.94           O  
HETATM 6468  O   HOH A2338       9.348  -9.522 -11.777  1.00 18.17           O  
HETATM 6469  O   HOH A2339      14.597 -16.928  -9.797  1.00 26.90           O  
HETATM 6470  O   HOH A2340      12.082 -18.355  -4.363  1.00 30.02           O  
HETATM 6471  O   HOH A2341      13.550 -16.079 -16.739  1.00 32.14           O  
HETATM 6472  O   HOH A2342       8.613 -19.969 -19.973  1.00 32.02           O  
HETATM 6473  O   HOH A2343      11.737 -13.934 -16.672  1.00 28.99           O  
HETATM 6474  O   HOH A2344      10.008 -12.869 -14.805  1.00 18.33           O  
HETATM 6475  O   HOH A2345       6.118  -5.786 -13.404  1.00 32.71           O  
HETATM 6476  O   HOH A2346       9.206  -2.343 -13.498  1.00 33.06           O  
HETATM 6477  O   HOH A2347      13.510  -6.342  -6.914  1.00 25.16           O  
HETATM 6478  O   HOH A2348      11.200  -0.472 -10.126  1.00 21.04           O  
HETATM 6479  O   HOH A2349      14.696  -4.386  -5.068  1.00 20.29           O  
HETATM 6480  O   HOH A2350      11.011  -1.964   3.386  1.00 24.92           O  
HETATM 6481  O   HOH A2351      10.414   0.727  -1.748  1.00 25.80           O  
HETATM 6482  O   HOH A2352      16.987  -1.841  -0.577  1.00 30.19           O  
HETATM 6483  O   HOH A2353      12.908  -8.203   0.778  1.00 36.73           O  
HETATM 6484  O   HOH A2354      18.183  -3.831   3.587  1.00 24.28           O  
HETATM 6485  O   HOH A2355      22.242   0.068   5.100  1.00 24.98           O  
HETATM 6486  O   HOH A2356      22.890  -3.507   9.007  1.00 30.37           O  
HETATM 6487  O   HOH A2357      21.411  -9.702   7.151  1.00 32.43           O  
HETATM 6488  O   HOH A2358      19.769 -10.059  11.756  1.00 28.99           O  
HETATM 6489  O   HOH A2359      24.078  -4.205  14.165  1.00 21.59           O  
HETATM 6490  O   HOH A2360      17.072 -13.125  13.515  1.00 22.19           O  
HETATM 6491  O   HOH A2361      16.338 -11.120  10.383  1.00 24.71           O  
HETATM 6492  O   HOH A2362      21.270  -7.479  18.909  1.00 13.49           O  
HETATM 6493  O   HOH A2363      24.221 -14.940  11.073  1.00 32.14           O  
HETATM 6494  O   HOH A2364      26.790  -9.629  13.893  1.00 26.00           O  
HETATM 6495  O   HOH A2365      24.497 -11.016  13.327  1.00 23.54           O  
HETATM 6496  O   HOH A2366      17.975  -6.152  24.499  1.00 15.41           O  
HETATM 6497  O   HOH A2367      25.131  -8.990  24.693  1.00 32.44           O  
HETATM 6498  O   HOH A2368      22.975 -10.825  24.584  1.00 30.24           O  
HETATM 6499  O   HOH A2369      20.785 -12.201  26.800  1.00 32.00           O  
HETATM 6500  O   HOH A2370      27.983  -6.922  22.875  1.00 33.69           O  
HETATM 6501  O   HOH A2371      29.366  -1.441  25.515  1.00 29.63           O  
HETATM 6502  O   HOH A2372      26.798  -1.346  26.224  1.00 19.57           O  
HETATM 6503  O   HOH A2373      28.636   1.606  31.963  1.00 21.86           O  
HETATM 6504  O   HOH A2374      21.145  -5.050  34.866  1.00 26.50           O  
HETATM 6505  O   HOH A2375      26.487  -9.371  26.933  1.00 28.50           O  
HETATM 6506  O   HOH A2376      23.962 -12.310  32.713  1.00 36.98           O  
HETATM 6507  O   HOH A2377      25.569  -5.677  36.006  1.00 22.89           O  
HETATM 6508  O   HOH A2378      30.556  -0.194  34.336  1.00 32.08           O  
HETATM 6509  O   HOH A2379      19.773   9.320  29.596  1.00 35.23           O  
HETATM 6510  O   HOH A2380      30.013   3.792  25.474  1.00 23.07           O  
HETATM 6511  O   HOH A2381      28.187   9.290  27.077  1.00 34.23           O  
HETATM 6512  O   HOH A2382      27.182   9.503  21.209  1.00 34.11           O  
HETATM 6513  O   HOH A2383      24.908   6.394  12.704  1.00 31.01           O  
HETATM 6514  O   HOH A2384      24.424   6.838   6.812  1.00 26.01           O  
HETATM 6515  O   HOH A2385      31.977   3.597   7.176  1.00 29.95           O  
HETATM 6516  O   HOH A2386      33.426   7.591   8.047  1.00 27.40           O  
HETATM 6517  O   HOH A2387      12.654   0.595   4.506  1.00 22.66           O  
HETATM 6518  O   HOH A2388      22.411  11.077  10.155  1.00 36.99           O  
HETATM 6519  O   HOH A2389      24.295  10.367  13.541  1.00 29.18           O  
HETATM 6520  O   HOH A2390      12.642  12.126  14.563  1.00 32.11           O  
HETATM 6521  O   HOH A2391      13.461  12.787  12.206  1.00 29.59           O  
HETATM 6522  O   HOH A2392       8.323  20.430  14.900  1.00 31.70           O  
HETATM 6523  O   HOH A2393       8.181  19.049  17.474  1.00 25.41           O  
HETATM 6524  O   HOH A2394      14.444  18.382  22.892  1.00 25.65           O  
HETATM 6525  O   HOH A2395      11.527  15.674  23.749  1.00 25.56           O  
HETATM 6526  O   HOH A2396      20.974  18.094  21.269  1.00 28.83           O  
HETATM 6527  O   HOH A2397      21.549  14.622  19.760  1.00 19.21           O  
HETATM 6528  O   HOH A2398      25.269  15.585  22.624  1.00 26.59           O  
HETATM 6529  O   HOH A2399      20.729   7.817  27.767  1.00 20.62           O  
HETATM 6530  O   HOH A2400      26.139  13.352  24.378  1.00 30.30           O  
HETATM 6531  O   HOH A2401      15.242  10.409   8.438  1.00 31.52           O  
HETATM 6532  O   HOH A2402      22.959   8.012   9.087  1.00 26.95           O  
HETATM 6533  O   HOH A2403       3.845   5.305   9.160  1.00 28.80           O  
HETATM 6534  O   HOH A2404      10.811   9.791   8.311  1.00 28.73           O  
HETATM 6535  O   HOH A2405       8.549  10.082  11.173  1.00 35.09           O  
HETATM 6536  O   HOH A2406      11.464  10.426  22.187  1.00 16.27           O  
HETATM 6537  O   HOH A2407      13.172  15.427  25.830  1.00 30.03           O  
HETATM 6538  O   HOH A2408      11.272  13.101  22.748  1.00 21.33           O  
HETATM 6539  O   HOH A2409      10.981   8.463  27.548  1.00 32.63           O  
HETATM 6540  O   HOH A2410      13.007   6.297  27.492  1.00 20.25           O  
HETATM 6541  O   HOH A2411      16.843   9.972  27.379  1.00 19.89           O  
HETATM 6542  O   HOH A2412      17.792   2.329  33.149  1.00 17.79           O  
HETATM 6543  O   HOH A2413      16.658   4.176  34.753  1.00 34.05           O  
HETATM 6544  O   HOH A2414       7.503   3.813  31.654  1.00 28.98           O  
HETATM 6545  O   HOH A2415      10.488  -3.467  28.676  1.00 25.78           O  
HETATM 6546  O   HOH A2416      13.699 -14.280  36.960  1.00 36.29           O  
HETATM 6547  O   HOH A2417      13.213  -8.089  41.135  1.00 25.90           O  
HETATM 6548  O   HOH A2418      13.406  -6.042  42.612  1.00 36.34           O  
HETATM 6549  O   HOH A2419      18.354 -13.181  43.271  1.00 31.15           O  
HETATM 6550  O   HOH A2420      16.434 -12.510  46.099  1.00 29.08           O  
HETATM 6551  O   HOH A2421       4.544 -16.569  50.944  1.00 27.58           O  
HETATM 6552  O   HOH A2422       1.881 -22.822  50.558  1.00 33.94           O  
HETATM 6553  O   HOH A2423       2.375 -17.997  53.706  1.00 42.83           O  
HETATM 6554  O   HOH A2424      -3.502 -20.029  56.390  1.00 32.89           O  
HETATM 6555  O   HOH A2425      -2.857 -22.960  52.235  1.00 37.48           O  
HETATM 6556  O   HOH A2426      -6.103 -22.322  48.644  1.00 26.03           O  
HETATM 6557  O   HOH A2427      -7.557 -20.608  45.477  1.00 23.33           O  
HETATM 6558  O   HOH A2428      -4.197 -19.969  38.666  1.00 28.73           O  
HETATM 6559  O   HOH A2429      -8.012 -22.866  42.447  1.00 42.51           O  
HETATM 6560  O   HOH A2430      -4.145 -24.371  49.073  1.00 29.81           O  
HETATM 6561  O   HOH A2431      -2.163 -26.894  45.498  1.00 38.03           O  
HETATM 6562  O   HOH A2432      21.894  -9.052  40.597  1.00 32.78           O  
HETATM 6563  O   HOH A2433      18.943 -12.984  28.940  1.00 20.76           O  
HETATM 6564  O   HOH A2434      20.517 -13.473  14.860  1.00 34.48           O  
HETATM 6565  O   HOH A2435      13.563 -18.141  18.144  1.00 22.02           O  
HETATM 6566  O   HOH A2436      11.898 -16.073  24.697  1.00 33.77           O  
HETATM 6567  O   HOH A2437      15.960 -16.573  17.288  1.00 26.76           O  
HETATM 6568  O   HOH A2438       7.782 -21.936  15.553  1.00 29.52           O  
HETATM 6569  O   HOH A2439      13.495 -19.497  15.424  1.00 32.48           O  
HETATM 6570  O   HOH A2440      10.514 -23.050  15.097  1.00 33.70           O  
HETATM 6571  O   HOH A2441       4.279 -21.953   1.824  1.00 46.88           O  
HETATM 6572  O   HOH A2442      -0.975 -13.132  -0.823  1.00 32.54           O  
HETATM 6573  O   HOH A2443       1.816 -15.320   0.536  1.00 32.93           O  
HETATM 6574  O   HOH A2444      -3.938 -17.520   3.947  1.00 16.25           O  
HETATM 6575  O   HOH A2445      -7.017 -14.988   1.489  1.00 19.55           O  
HETATM 6576  O   HOH A2446      -3.005 -11.803   0.404  1.00 17.14           O  
HETATM 6577  O   HOH A2447       2.415   0.858   9.142  1.00 28.17           O  
HETATM 6578  O   HOH A2448       2.361  -4.488   5.123  1.00 26.95           O  
HETATM 6579  O   HOH A2449      -3.297   8.564   9.707  1.00 12.85           O  
HETATM 6580  O   HOH A2450      -6.909   8.322  14.643  1.00 12.67           O  
HETATM 6581  O   HOH A2451      -5.158  13.898  11.260  1.00 19.11           O  
HETATM 6582  O   HOH A2452      -6.996  11.533  18.735  1.00 38.53           O  
HETATM 6583  O   HOH A2453     -12.834  11.703  17.664  1.00 28.53           O  
HETATM 6584  O   HOH A2454     -13.937   7.085  17.083  1.00 22.42           O  
HETATM 6585  O   HOH A2455     -16.179  11.331  13.986  1.00 23.07           O  
HETATM 6586  O   HOH A2456     -18.787  11.722   9.750  1.00 31.17           O  
HETATM 6587  O   HOH A2457     -18.638   9.707  13.665  1.00 29.19           O  
HETATM 6588  O   HOH A2458     -21.363   8.753  10.313  1.00 43.96           O  
HETATM 6589  O   HOH A2459     -14.152  15.151   4.563  1.00 30.68           O  
HETATM 6590  O   HOH A2460     -12.094   9.196   8.557  1.00 11.37           O  
HETATM 6591  O   HOH A2461     -12.905  12.772   3.915  1.00 19.87           O  
HETATM 6592  O   HOH A2462      -7.628  15.125  10.540  1.00 24.72           O  
HETATM 6593  O   HOH A2463       2.385  11.624   1.708  1.00 22.85           O  
HETATM 6594  O   HOH A2464       0.898   8.453   7.572  1.00 16.61           O  
HETATM 6595  O   HOH A2465       1.549  12.782   5.707  1.00 32.80           O  
HETATM 6596  O   HOH A2466       3.023   6.501   7.012  1.00 24.19           O  
HETATM 6597  O   HOH A2467      -1.243   1.443   8.635  1.00 10.66           O  
HETATM 6598  O   HOH A2468       4.528  10.198   1.170  1.00 27.97           O  
HETATM 6599  O   HOH A2469       5.278   0.757  -1.992  1.00 13.31           O  
HETATM 6600  O   HOH A2470       8.496  -0.912   2.926  1.00 21.50           O  
HETATM 6601  O   HOH A2471       7.973   4.367   1.806  1.00 25.83           O  
HETATM 6602  O   HOH A2472       2.346   1.774  -8.436  1.00 18.96           O  
HETATM 6603  O   HOH A2473       8.820  -0.030  -5.766  1.00 20.38           O  
HETATM 6604  O   HOH A2474       8.120  -0.882  -1.210  1.00 21.77           O  
HETATM 6605  O   HOH A2475       6.416  -3.137 -13.449  1.00 25.30           O  
HETATM 6606  O   HOH A2476       7.172   0.582  -7.777  1.00 22.98           O  
HETATM 6607  O   HOH A2477       9.010  -0.161 -11.704  1.00 24.87           O  
HETATM 6608  O   HOH A2478       3.593  -9.930 -17.905  1.00 39.62           O  
HETATM 6609  O   HOH A2479      -0.766 -15.064  -5.032  1.00 24.43           O  
HETATM 6610  O   HOH A2480      -5.332 -18.022  -6.562  1.00 23.59           O  
HETATM 6611  O   HOH A2481      -1.821 -23.660  -6.816  1.00 23.26           O  
HETATM 6612  O   HOH A2482      -2.623 -19.870  -7.078  1.00 24.26           O  
HETATM 6613  O   HOH A2483       3.620 -19.642  -5.081  1.00 42.77           O  
HETATM 6614  O   HOH A2484       0.461 -27.066  -8.839  1.00 38.19           O  
HETATM 6615  O   HOH A2485      -2.871 -34.057 -10.622  1.00 30.64           O  
HETATM 6616  O   HOH A2486      -7.058 -38.409 -14.192  1.00 27.02           O  
HETATM 6617  O   HOH A2487     -11.102 -38.182 -10.420  1.00 37.47           O  
HETATM 6618  O   HOH A2488     -16.500 -19.399 -17.036  1.00 34.94           O  
HETATM 6619  O   HOH A2489      -8.182 -17.753 -24.797  1.00 27.90           O  
HETATM 6620  O   HOH A2490      -1.605 -16.721 -23.488  1.00 27.81           O  
HETATM 6621  O   HOH A2491      -8.140 -14.095 -26.869  1.00 32.42           O  
HETATM 6622  O   HOH A2492      -9.558 -10.453 -20.827  1.00 28.06           O  
HETATM 6623  O   HOH A2493      -6.274 -10.147 -18.142  1.00 33.58           O  
HETATM 6624  O   HOH A2494      -4.035 -19.800 -26.044  1.00 31.73           O  
HETATM 6625  O   HOH A2495       1.646 -18.741 -22.738  1.00 21.42           O  
HETATM 6626  O   HOH A2496       5.406 -23.650 -21.573  1.00 29.12           O  
HETATM 6627  O   HOH A2497       8.094 -26.236 -20.470  1.00 38.19           O  
HETATM 6628  O   HOH A2498       4.086 -28.858 -14.929  1.00 24.66           O  
HETATM 6629  O   HOH A2499      -6.134 -14.836 -10.719  1.00 26.67           O  
HETATM 6630  O   HOH A2500     -12.897 -14.008 -12.304  1.00 27.11           O  
HETATM 6631  O   HOH A2501     -11.911  -9.970 -14.695  1.00 40.37           O  
HETATM 6632  O   HOH A2502     -10.839 -17.131  -4.932  1.00 16.40           O  
HETATM 6633  O   HOH A2503     -11.197 -24.285  -6.288  1.00 22.67           O  
HETATM 6634  O   HOH A2504      -8.154 -18.456  -5.983  1.00 29.62           O  
HETATM 6635  O   HOH A2505      -8.745 -22.720  -5.915  1.00 31.64           O  
HETATM 6636  O   HOH A2506     -17.465 -19.487 -10.686  1.00 26.09           O  
HETATM 6637  O   HOH A2507      -6.781 -29.177  -6.995  1.00 28.96           O  
HETATM 6638  O   HOH A2508     -11.680 -28.943  -4.927  1.00 30.69           O  
HETATM 6639  O   HOH A2509     -12.017 -33.673  -4.044  1.00 30.50           O  
HETATM 6640  O   HOH A2510     -18.169 -35.705  -7.260  1.00 25.00           O  
HETATM 6641  O   HOH A2511     -21.107 -33.498 -13.429  1.00 18.78           O  
HETATM 6642  O   HOH A2512     -18.900 -38.563 -11.294  1.00 29.38           O  
HETATM 6643  O   HOH A2513     -12.989 -29.265 -12.264  1.00 19.12           O  
HETATM 6644  O   HOH A2514     -20.272 -30.541 -11.257  1.00 28.72           O  
HETATM 6645  O   HOH A2515     -21.900 -27.572 -17.582  1.00 31.75           O  
HETATM 6646  O   HOH A2516     -21.057 -30.022 -18.787  1.00 23.66           O  
HETATM 6647  O   HOH A2517     -18.180 -22.593 -19.419  1.00 37.36           O  
HETATM 6648  O   HOH A2518     -19.003 -25.619 -24.066  1.00 31.33           O  
HETATM 6649  O   HOH A2519     -17.486 -22.856 -14.422  1.00 33.43           O  
HETATM 6650  O   HOH A2520     -16.009 -32.747 -29.181  1.00 32.84           O  
HETATM 6651  O   HOH A2521     -14.814 -37.058 -22.801  1.00 27.41           O  
HETATM 6652  O   HOH A2522     -19.185 -34.831 -24.186  1.00 27.11           O  
HETATM 6653  O   HOH A2523     -17.213 -23.701 -30.071  1.00 27.35           O  
HETATM 6654  O   HOH A2524     -18.060  -0.661  10.576  1.00 19.30           O  
HETATM 6655  O   HOH A2525     -10.727  -2.004  18.871  1.00 10.44           O  
HETATM 6656  O   HOH A2526     -11.449   2.634  20.135  1.00 21.36           O  
HETATM 6657  O   HOH A2527      -6.830  -3.092  19.292  1.00 10.05           O  
HETATM 6658  O   HOH A2528     -11.300  -1.535   9.750  1.00 11.19           O  
HETATM 6659  O   HOH A2529     -15.954   2.556  15.323  1.00 19.93           O  
HETATM 6660  O   HOH A2530       3.495 -11.683  27.593  1.00 18.73           O  
HETATM 6661  O   HOH A2531       0.477   4.919  14.847  1.00 19.86           O  
HETATM 6662  O   HOH A2532      -8.070  17.184  -6.637  1.00 23.11           O  
HETATM 6663  O   HOH A2533      -6.966  11.286  -4.073  1.00 15.71           O  
HETATM 6664  O   HOH A2534       7.004  -3.753  26.349  1.00 17.17           O  
HETATM 6665  O   HOH A2535     -23.759  -5.742  46.058  1.00 15.79           O  
HETATM 6666  O   HOH A2536     -28.224  -2.630  41.375  1.00 20.14           O  
CONECT 1189 6130                                                                
CONECT 1509 6130                                                                
CONECT 6060 6061 6062 6063 6067                                                 
CONECT 6061 6060 6130                                                           
CONECT 6062 6060 6087                                                           
CONECT 6063 6060                                                                
CONECT 6064 6065 6066 6067 6068                                                 
CONECT 6065 6064                                                                
CONECT 6066 6064                                                                
CONECT 6067 6060 6064                                                           
CONECT 6068 6064 6069                                                           
CONECT 6069 6068 6070                                                           
CONECT 6070 6069 6071 6072                                                      
CONECT 6071 6070 6076                                                           
CONECT 6072 6070 6073 6074                                                      
CONECT 6073 6072                                                                
CONECT 6074 6072 6075 6076                                                      
CONECT 6075 6074                                                                
CONECT 6076 6071 6074 6077                                                      
CONECT 6077 6076 6078 6086                                                      
CONECT 6078 6077 6079                                                           
CONECT 6079 6078 6080                                                           
CONECT 6080 6079 6081 6086                                                      
CONECT 6081 6080 6082 6083                                                      
CONECT 6082 6081                                                                
CONECT 6083 6081 6084                                                           
CONECT 6084 6083 6085                                                           
CONECT 6085 6084 6086                                                           
CONECT 6086 6077 6080 6085                                                      
CONECT 6087 6062 6088 6089 6090                                                 
CONECT 6087 6091                                                                
CONECT 6088 6087                                                                
CONECT 6089 6087 6130                                                           
CONECT 6090 6087                                                                
CONECT 6091 6087                                                                
CONECT 6092 6093 6094                                                           
CONECT 6093 6092                                                                
CONECT 6094 6092 6095                                                           
CONECT 6095 6094                                                                
CONECT 6096 6097 6098                                                           
CONECT 6097 6096                                                                
CONECT 6098 6096 6099                                                           
CONECT 6099 6098                                                                
CONECT 6100 6101 6102                                                           
CONECT 6101 6100                                                                
CONECT 6102 6100 6103                                                           
CONECT 6103 6102                                                                
CONECT 6104 6105 6106                                                           
CONECT 6105 6104                                                                
CONECT 6106 6104 6107                                                           
CONECT 6107 6106                                                                
CONECT 6108 6109 6110                                                           
CONECT 6109 6108                                                                
CONECT 6110 6108 6111                                                           
CONECT 6111 6110                                                                
CONECT 6112 6113 6114                                                           
CONECT 6113 6112                                                                
CONECT 6114 6112 6115                                                           
CONECT 6115 6114                                                                
CONECT 6116 6117 6118                                                           
CONECT 6117 6116                                                                
CONECT 6118 6116 6119                                                           
CONECT 6119 6118                                                                
CONECT 6120 6121 6122 6123 6124                                                 
CONECT 6121 6120                                                                
CONECT 6122 6120                                                                
CONECT 6123 6120                                                                
CONECT 6124 6120                                                                
CONECT 6125 6126 6127 6128 6129                                                 
CONECT 6126 6125                                                                
CONECT 6127 6125                                                                
CONECT 6128 6125                                                                
CONECT 6129 6125                                                                
CONECT 6130 1189 1509 6061 6089                                                 
CONECT 6130 6444 6657                                                           
CONECT 6444 6130                                                                
CONECT 6657 6130                                                                
MASTER      396    0   12   41   24    0   29    6 6665    1   77   61          
END                                                                             


A second structure was input as follows:


HEADER    MOTOR PROTEIN                           22-MAY-17   5O2L              
TITLE     MYOSIN VI MOTOR DOMAIN IN THE PRE-TRANSITION STATE                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UNCONVENTIONAL MYOSIN-VI;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 GENE: MYO6;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    MYOSIN, MOTOR DOMAIN, PRE-TRANSITION STATE, MOTOR PROTEIN             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.ISABET,H.BENISTY,A.HOUDUSSE                                         
REVDAT   3   20-JUN-18 5O2L    1       JRNL                                     
REVDAT   2   13-JUN-18 5O2L    1       JRNL                                     
REVDAT   1   23-MAY-18 5O2L    0                                                
JRNL        AUTH   F.BLANC,T.ISABET,H.BENISTY,H.L.SWEENEY,M.CECCHINI,A.HOUDUSSE 
JRNL        TITL   AN INTERMEDIATE ALONG THE RECOVERY STROKE OF MYOSIN VI       
JRNL        TITL 2 REVEALED BY X-RAY CRYSTALLOGRAPHY AND MOLECULAR DYNAMICS.    
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 115  6213 2018              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   29844196                                                     
JRNL        DOI    10.1073/PNAS.1711512115                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.5                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 55469                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.184                          
REMARK   3   R VALUE            (WORKING SET)  : 0.182                          
REMARK   3   FREE R VALUE                      : 0.227                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.990                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2769                           
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               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.20                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.26                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.78                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4037                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2635                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3835                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2605                   
REMARK   3   BIN FREE R VALUE                        : 0.3194                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.00                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 202                      
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            : 6045                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 80                                      
REMARK   3   SOLVENT ATOMS            : 239                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.48                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.33                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.08720                                             
REMARK   3    B22 (A**2) : -5.60200                                             
REMARK   3    B33 (A**2) : 7.68920                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.367               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.186               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.168               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.185               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.169               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6265   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 8457   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2926   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 165    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 919    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6265   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 1      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 801    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7456   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.06                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.19                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 3.01                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|5 - A|704 A|995 - A|1006 S|* }                     
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.5110   31.9703   24.9344           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0660 T22:   -0.0329                                    
REMARK   3     T33:   -0.2999 T12:   -0.0615                                    
REMARK   3     T13:    0.0453 T23:   -0.0191                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4788 L22:    0.6633                                    
REMARK   3     L33:    1.7810 L12:   -0.3459                                    
REMARK   3     L13:    0.4638 L23:    0.0649                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0407 S12:   -0.1833 S13:    0.1246                     
REMARK   3     S21:   -0.1564 S22:    0.0390 S23:   -0.0518                     
REMARK   3     S31:   -0.3194 S32:   -0.0250 S33:    0.0017                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|705 - A|789 T|* }                                  
REMARK   3    ORIGIN FOR THE GROUP (A):   31.4716   64.0577   34.9460           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2960 T22:    0.1920                                    
REMARK   3     T33:   -0.1732 T12:   -0.1009                                    
REMARK   3     T13:   -0.0408 T23:   -0.0381                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    8.3155 L22:    8.3154                                    
REMARK   3     L33:    3.4091 L12:    2.9104                                    
REMARK   3     L13:   -0.3144 L23:    2.9104                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0202 S12:   -0.0147 S13:   -0.5442                     
REMARK   3     S21:   -0.5308 S22:   -0.2461 S23:    0.5072                     
REMARK   3     S31:   -0.3337 S32:   -0.4617 S33:    0.2663                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5O2L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003012.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9800                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55469                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.5700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
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         : 1.290                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2V26                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% POLYETHYLENE GLYCOL [PEG] 8000, 50    
REMARK 280  MM TRIS, PH 7.5, 1 MM TCEP, 15% GLYCEROL, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       36.17000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.83000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.91500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.83000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.17000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.91500            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   356                                                      
REMARK 465     SER A   357                                                      
REMARK 465     THR A   358                                                      
REMARK 465     SER A   359                                                      
REMARK 465     GLY A   360                                                      
REMARK 465     THR A   397                                                      
REMARK 465     THR A   398                                                      
REMARK 465     ALA A   399                                                      
REMARK 465     GLY A   400                                                      
REMARK 465     GLY A   401                                                      
REMARK 465     ALA A   402                                                      
REMARK 465     LYS A   403                                                      
REMARK 465     GLY A   404                                                      
REMARK 465     THR A   405                                                      
REMARK 465     SER A   624                                                      
REMARK 465     THR A   625                                                      
REMARK 465     ASN A   626                                                      
REMARK 465     ASN A   627                                                      
REMARK 465     ASN A   628                                                      
REMARK 465     LYS A   629                                                      
REMARK 465     ASP A   630                                                      
REMARK 465     THR A   631                                                      
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   5    CG   CD   CE   NZ                                   
REMARK 470     LYS A  37    CG   CD   CE   NZ                                   
REMARK 470     LYS A  39    CG   CD   CE   NZ                                   
REMARK 470     GLU A 110    CD   OE1  OE2                                       
REMARK 470     GLN A 176    CG   CD   OE1  NE2                                  
REMARK 470     ILE A 178    CG1  CG2  CD1                                       
REMARK 470     GLU A 184    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 216    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 217    CD   CE   NZ                                        
REMARK 470     LYS A 240    CD   CE   NZ                                        
REMARK 470     GLU A 261    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 285    CD   CE   NZ                                        
REMARK 470     LYS A 289    CD   CE   NZ                                        
REMARK 470     LYS A 325    CD   CE   NZ                                        
REMARK 470     GLU A 354    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 406    CG1  CG2                                            
REMARK 470     LYS A 408    CD   CE   NZ                                        
REMARK 470     GLU A 446    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 564    CE   NZ                                             
REMARK 470     LYS A 615    CE   NZ                                             
REMARK 470     GLU A 622    CD   OE1  OE2                                       
REMARK 470     LYS A 632    CG   CD   CE   NZ                                   
REMARK 470     GLN A 633    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 634    CG   CD   CE   NZ                                   
REMARK 470     LYS A 637    CG   CD   CE   NZ                                   
REMARK 470     ARG A 728    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 746    CD   OE1  OE2                                       
REMARK 470     LYS A 755    CG   CD   CE   NZ                                   
REMARK 470     LYS A 762    CD   CE   NZ                                        
REMARK 470     GLN A 768    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 771    CG   CD   CE   NZ                                   
REMARK 470     LYS A 782    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  MG     MG A   802     F2   BEF A   803              1.66            
REMARK 500   NH1  ARG A   393     SD   MET A   395              2.11            
REMARK 500   NH1  ARG A   393     CE   MET A   395              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    THR A 392   C     ARG A 393   N      -0.296                       
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    THR A 392   CA  -  C   -  N   ANGL. DEV. = -15.0 DEGREES          
REMARK 500    THR A 392   O   -  C   -  N   ANGL. DEV. =  11.2 DEGREES          
REMARK 500    ARG A 393   C   -  N   -  CA  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    ARG A 393   CA  -  C   -  N   ANGL. DEV. =  20.9 DEGREES          
REMARK 500    ARG A 393   O   -  C   -  N   ANGL. DEV. = -21.0 DEGREES          
REMARK 500    VAL A 394   C   -  N   -  CA  ANGL. DEV. =  18.3 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    ALA A  91     -114.96     60.16                                   
REMARK 500    LYS A 105       -2.31     58.46                                   
REMARK 500    ASP A 177       -5.67    -55.22                                   
REMARK 500    PHE A 443       59.72   -140.50                                   
REMARK 500    SER A 467     -166.94   -117.91                                   
REMARK 500    LEU A 522      -54.14     70.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 802  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 158   OG1                                                    
REMARK 620 2 SER A 204   OG   89.0                                              
REMARK 620 3 ADP A 801   O1B  82.9 171.9                                        
REMARK 620 4 HOH A 937   O    89.3  85.3  94.5                                  
REMARK 620 5 HOH A 902   O    85.7  93.9  85.6 175.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             BEF A 803  BE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 801   O3B                                                    
REMARK 620 2 BEF A 803   F1   87.3                                              
REMARK 620 3 BEF A 803   F2   85.7 109.4                                        
REMARK 620 4 BEF A 803   F3  150.2 110.0 109.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BEF A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 807                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 808                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 809                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 810                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 811                 
DBREF  5O2L A    5   789  UNP    F1RQI7   F1RQI7_PIG       5    789             
SEQRES   1 A  785  LYS PRO VAL TRP ALA PRO HIS PRO THR ASP GLY PHE GLN          
SEQRES   2 A  785  VAL GLY ASN ILE VAL ASP ILE GLY PRO ASP SER LEU THR          
SEQRES   3 A  785  ILE GLU PRO LEU ASN GLN LYS GLY LYS THR PHE LEU ALA          
SEQRES   4 A  785  LEU ILE ASN GLN VAL PHE PRO ALA GLU GLU ASP SER LYS          
SEQRES   5 A  785  LYS ASP VAL GLU ASP ASN CYS SER LEU MET TYR LEU ASN          
SEQRES   6 A  785  GLU ALA THR LEU LEU HIS ASN ILE LYS VAL ARG TYR SER          
SEQRES   7 A  785  LYS ASP ARG ILE TYR THR TYR VAL ALA ASN ILE LEU ILE          
SEQRES   8 A  785  ALA VAL ASN PRO TYR PHE ASP ILE PRO LYS ILE TYR SER          
SEQRES   9 A  785  SER GLU THR ILE LYS SER TYR GLN GLY LYS SER LEU GLY          
SEQRES  10 A  785  THR MET PRO PRO HIS VAL PHE ALA ILE ALA ASP LYS ALA          
SEQRES  11 A  785  PHE ARG ASP MET LYS VAL LEU LYS LEU SER GLN SER ILE          
SEQRES  12 A  785  ILE VAL SER GLY GLU SER GLY ALA GLY LYS THR GLU ASN          
SEQRES  13 A  785  THR LYS PHE VAL LEU ARG TYR LEU THR GLU SER TYR GLY          
SEQRES  14 A  785  THR GLY GLN ASP ILE ASP ASP ARG ILE VAL GLU ALA ASN          
SEQRES  15 A  785  PRO LEU LEU GLU ALA PHE GLY ASN ALA LYS THR VAL ARG          
SEQRES  16 A  785  ASN ASN ASN SER SER ARG PHE GLY LYS PHE VAL GLU ILE          
SEQRES  17 A  785  HIS PHE ASN GLU LYS SER SER VAL VAL GLY GLY PHE VAL          
SEQRES  18 A  785  SER HIS TYR LEU LEU GLU LYS SER ARG ILE CYS VAL GLN          
SEQRES  19 A  785  GLY LYS GLU GLU ARG ASN TYR HIS ILE PHE TYR ARG LEU          
SEQRES  20 A  785  CYS ALA GLY ALA SER GLU ASP ILE ARG GLU ARG LEU HIS          
SEQRES  21 A  785  LEU SER SER PRO ASP ASN PHE ARG TYR LEU ASN ARG GLY          
SEQRES  22 A  785  CYS THR ARG TYR PHE ALA ASN LYS GLU THR ASP LYS GLN          
SEQRES  23 A  785  ILE LEU GLN ASN ARG LYS SER PRO GLU TYR LEU LYS ALA          
SEQRES  24 A  785  GLY SER LEU LYS ASP PRO LEU LEU ASP ASP HIS GLY ASP          
SEQRES  25 A  785  PHE ILE ARG MET CYS THR ALA MET LYS LYS ILE GLY LEU          
SEQRES  26 A  785  ASP ASP GLU GLU LYS LEU ASP LEU PHE ARG VAL VAL ALA          
SEQRES  27 A  785  GLY VAL LEU HIS LEU GLY ASN ILE ASP PHE GLU GLU ALA          
SEQRES  28 A  785  GLY SER THR SER GLY GLY CYS ASN LEU LYS ASN LYS SER          
SEQRES  29 A  785  THR GLN ALA LEU GLU TYR CYS ALA GLU LEU LEU GLY LEU          
SEQRES  30 A  785  ASP GLN ASP ASP LEU ARG VAL SER LEU THR THR ARG VAL          
SEQRES  31 A  785  MET LEU THR THR ALA GLY GLY ALA LYS GLY THR VAL ILE          
SEQRES  32 A  785  LYS VAL PRO LEU LYS VAL GLU GLN ALA ASN ASN ALA ARG          
SEQRES  33 A  785  ASP ALA LEU ALA LYS THR VAL TYR SER HIS LEU PHE ASP          
SEQRES  34 A  785  HIS VAL VAL ASN ARG VAL ASN GLN CYS PHE PRO PHE GLU          
SEQRES  35 A  785  THR SER SER TYR PHE ILE GLY VAL LEU ASP ILE ALA GLY          
SEQRES  36 A  785  PHE GLU TYR PHE GLU HIS ASN SER PHE GLU GLN PHE CYS          
SEQRES  37 A  785  ILE ASN TYR CYS ASN GLU LYS LEU GLN GLN PHE PHE ASN          
SEQRES  38 A  785  GLU ARG ILE LEU LYS GLU GLU GLN GLU LEU TYR GLN LYS          
SEQRES  39 A  785  GLU GLY LEU GLY VAL ASN GLU VAL HIS TYR VAL ASP ASN          
SEQRES  40 A  785  GLN ASP CYS ILE ASP LEU ILE GLU ALA ARG LEU VAL GLY          
SEQRES  41 A  785  ILE LEU ASP ILE LEU ASP GLU GLU ASN ARG LEU PRO GLN          
SEQRES  42 A  785  PRO SER ASP GLN HIS PHE THR SER ALA VAL HIS GLN LYS          
SEQRES  43 A  785  HIS LYS ASP HIS PHE ARG LEU SER ILE PRO ARG LYS SER          
SEQRES  44 A  785  LYS LEU ALA ILE HIS ARG ASN ILE ARG ASP ASP GLU GLY          
SEQRES  45 A  785  PHE ILE ILE ARG HIS PHE ALA GLY ALA VAL CYS TYR GLU          
SEQRES  46 A  785  THR THR GLN PHE VAL GLU LYS ASN ASN ASP ALA LEU HIS          
SEQRES  47 A  785  MET SER LEU GLU SER LEU ILE CYS GLU SER ARG ASP LYS          
SEQRES  48 A  785  PHE ILE ARG GLU LEU PHE GLU SER SER THR ASN ASN ASN          
SEQRES  49 A  785  LYS ASP THR LYS GLN LYS ALA GLY LYS LEU SER PHE ILE          
SEQRES  50 A  785  SER VAL GLY ASN LYS PHE LYS THR GLN LEU ASN LEU LEU          
SEQRES  51 A  785  LEU ASP LYS LEU ARG SER THR GLY ALA SER PHE ILE ARG          
SEQRES  52 A  785  CYS ILE LYS PRO ASN LEU LYS MET THR SER HIS HIS PHE          
SEQRES  53 A  785  GLU GLY ALA GLN ILE LEU SER GLN LEU GLN CYS SER GLY          
SEQRES  54 A  785  MET VAL SER VAL LEU ASP LEU MET GLN GLY GLY PHE PRO          
SEQRES  55 A  785  SER ARG ALA SER PHE HIS GLU LEU TYR ASN MET TYR LYS          
SEQRES  56 A  785  LYS TYR MET PRO ASP LYS LEU ALA ARG LEU ASP PRO ARG          
SEQRES  57 A  785  LEU PHE CYS LYS ALA LEU PHE LYS ALA LEU GLY LEU ASN          
SEQRES  58 A  785  GLU ILE ASP TYR LYS PHE GLY LEU THR LYS VAL PHE PHE          
SEQRES  59 A  785  ARG PRO GLY LYS PHE ALA GLU PHE ASP GLN ILE MET LYS          
SEQRES  60 A  785  SER ASP PRO ASP HIS LEU ALA GLU LEU VAL LYS ARG VAL          
SEQRES  61 A  785  ASN HIS TRP LEU ILE                                          
HET    ADP  A 801      27                                                       
HET     MG  A 802       1                                                       
HET    BEF  A 803       4                                                       
HET    GOL  A 804       6                                                       
HET    GOL  A 805       6                                                       
HET    GOL  A 806       6                                                       
HET    GOL  A 807       6                                                       
HET    GOL  A 808       6                                                       
HET    GOL  A 809       6                                                       
HET    GOL  A 810       6                                                       
HET    GOL  A 811       6                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     BEF BERYLLIUM TRIFLUORIDE ION                                        
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  ADP    C10 H15 N5 O10 P2                                            
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  BEF    BE F3 1-                                                     
FORMUL   5  GOL    8(C3 H8 O3)                                                  
FORMUL  13  HOH   *239(H2 O)                                                    
HELIX    1 AA1 ASN A   46  VAL A   48  5                                   3    
HELIX    2 AA2 ASP A   61  LEU A   65  5                                   5    
HELIX    3 AA3 ASN A   69  LYS A   83  1                                  15    
HELIX    4 AA4 SER A  108  TYR A  115  1                                   8    
HELIX    5 AA5 HIS A  126  LYS A  142  1                                  17    
HELIX    6 AA6 GLY A  156  GLY A  173  1                                  18    
HELIX    7 AA7 GLN A  176  ILE A  178  5                                   3    
HELIX    8 AA8 ASP A  179  ALA A  185  1                                   7    
HELIX    9 AA9 ALA A  185  GLY A  193  1                                   9    
HELIX   10 AB1 LYS A  232  CYS A  236  5                                   5    
HELIX   11 AB2 TYR A  245  ALA A  255  1                                  11    
HELIX   12 AB3 SER A  256  LEU A  263  1                                   8    
HELIX   13 AB4 SER A  267  ASN A  270  5                                   4    
HELIX   14 AB5 PHE A  271  ARG A  276  1                                   6    
HELIX   15 AB6 ASN A  284  ILE A  291  1                                   8    
HELIX   16 AB7 LEU A  292  LYS A  296  5                                   5    
HELIX   17 AB8 SER A  297  GLY A  304  1                                   8    
HELIX   18 AB9 ASP A  312  ILE A  327  1                                  16    
HELIX   19 AC1 ASP A  330  ASN A  349  1                                  20    
HELIX   20 AC2 SER A  368  GLY A  380  1                                  13    
HELIX   21 AC3 ASP A  382  THR A  391  1                                  10    
HELIX   22 AC4 LYS A  412  CYS A  442  1                                  31    
HELIX   23 AC5 SER A  467  LEU A  489  1                                  23    
HELIX   24 AC6 LEU A  489  GLY A  500  1                                  12    
HELIX   25 AC7 ASN A  511  ALA A  520  1                                  10    
HELIX   26 AC8 GLY A  524  ARG A  534  1                                  11    
HELIX   27 AC9 SER A  539  HIS A  551  1                                  13    
HELIX   28 AD1 ILE A  559  SER A  563  5                                   5    
HELIX   29 AD2 LEU A  565  ARG A  569  5                                   5    
HELIX   30 AD3 ARG A  572  ASP A  574  5                                   3    
HELIX   31 AD4 GLN A  592  ASN A  597  1                                   6    
HELIX   32 AD5 HIS A  602  GLU A  611  1                                  10    
HELIX   33 AD6 ASP A  614  PHE A  621  1                                   8    
HELIX   34 AD7 SER A  642  THR A  661  1                                  20    
HELIX   35 AD8 GLU A  681  SER A  692  1                                  12    
HELIX   36 AD9 GLY A  693  GLY A  704  1                                  12    
HELIX   37 AE1 PHE A  711  LYS A  719  1                                   9    
HELIX   38 AE2 LYS A  720  MET A  722  5                                   3    
HELIX   39 AE3 PRO A  723  ALA A  727  5                                   5    
HELIX   40 AE4 ASP A  730  GLY A  743  1                                  14    
HELIX   41 AE5 LYS A  762  LYS A  771  1                                  10    
HELIX   42 AE6 ASP A  773  ASN A  785  1                                  13    
HELIX   43 AE7 HIS A  786  ILE A  789  5                                   4    
SHEET    1 AA1 5 PHE A  41  LEU A  44  0                                        
SHEET    2 AA1 5 SER A  28  PRO A  33 -1  N  LEU A  29   O  ALA A  43           
SHEET    3 AA1 5 GLY A  15  ILE A  24 -1  N  VAL A  22   O  THR A  30           
SHEET    4 AA1 5 VAL A   7  HIS A  11 -1  N  VAL A   7   O  GLY A  19           
SHEET    5 AA1 5 PHE A  49  PRO A  50 -1  O  PHE A  49   N  TRP A   8           
SHEET    1 AA2 7 TYR A  87  VAL A  90  0                                        
SHEET    2 AA2 7 ILE A  93  VAL A  97 -1  O  ILE A  95   N  THR A  88           
SHEET    3 AA2 7 GLY A 662  ILE A 669  1  O  ARG A 667   N  LEU A  94           
SHEET    4 AA2 7 GLN A 145  SER A 150  1  N  SER A 150   O  CYS A 668           
SHEET    5 AA2 7 TYR A 450  ASP A 456  1  O  PHE A 451   N  GLN A 145           
SHEET    6 AA2 7 GLY A 207  PHE A 214 -1  N  LYS A 208   O  ASP A 456           
SHEET    7 AA2 7 VAL A 220  TYR A 228 -1  O  GLY A 222   N  HIS A 213           
SHEET    1 AA3 2 ASN A 194  THR A 197  0                                        
SHEET    2 AA3 2 ASN A 200  SER A 204 -1  O  ASN A 200   N  THR A 197           
SHEET    1 AA4 2 PHE A 352  GLU A 353  0                                        
SHEET    2 AA4 2 ASN A 363  LEU A 364 -1  O  ASN A 363   N  GLU A 353           
SHEET    1 AA5 2 THR A 392  MET A 395  0                                        
SHEET    2 AA5 2 ILE A 407  PRO A 410 -1  O  VAL A 409   N  ARG A 393           
SHEET    1 AA6 3 LEU A 557  SER A 558  0                                        
SHEET    2 AA6 3 GLY A 576  HIS A 581 -1  O  ILE A 578   N  SER A 558           
SHEET    3 AA6 3 GLY A 584  GLU A 589 -1  O  TYR A 588   N  PHE A 577           
SHEET    1 AA7 3 SER A 707  SER A 710  0                                        
SHEET    2 AA7 3 LYS A 755  PHE A 758 -1  O  PHE A 758   N  SER A 707           
SHEET    3 AA7 3 TYR A 749  PHE A 751 -1  N  LYS A 750   O  PHE A 757           
LINK         OG1 THR A 158                MG    MG A 802     1555   1555  1.98  
LINK         OG  SER A 204                MG    MG A 802     1555   1555  2.08  
LINK         O1B ADP A 801                MG    MG A 802     1555   1555  2.22  
LINK         O3B ADP A 801                BE   BEF A 803     1555   1555  2.11  
LINK        MG    MG A 802                 O   HOH A 937     1555   1555  2.15  
LINK        MG    MG A 802                 O   HOH A 902     1555   1555  2.06  
CISPEP   1 GLN A   36    LYS A   37          0        -3.50                     
SITE     1 AC1 22 ASN A  98  PRO A  99  TYR A 100  PHE A 101                    
SITE     2 AC1 22 TYR A 107  GLU A 152  GLY A 154  ALA A 155                    
SITE     3 AC1 22 GLY A 156  LYS A 157  THR A 158  GLU A 159                    
SITE     4 AC1 22 PHE A 163  ASN A 200  LEU A 310   MG A 802                    
SITE     5 AC1 22 BEF A 803  HOH A 902  HOH A 933  HOH A 937                    
SITE     6 AC1 22 HOH A1024  HOH A1028                                          
SITE     1 AC2  6 THR A 158  SER A 204  ADP A 801  BEF A 803                    
SITE     2 AC2  6 HOH A 902  HOH A 937                                          
SITE     1 AC3 10 SER A 153  THR A 158  ASN A 200  SER A 203                    
SITE     2 AC3 10 SER A 204  ADP A 801   MG A 802  HOH A 902                    
SITE     3 AC3 10 HOH A 937  HOH A1066                                          
SITE     1 AC4  5 ILE A 148  ASN A 477  GLN A 481  ARG A 667                    
SITE     2 AC4  5 GOL A 805                                                     
SITE     1 AC5  9 ILE A 148  SER A 150  PHE A 484  PHE A 665                    
SITE     2 AC5  9 ILE A 666  ARG A 667  SER A 692  MET A 694                    
SITE     3 AC5  9 GOL A 804                                                     
SITE     1 AC6  5 LYS A 196  ASN A 201  LEU A 306  LYS A 307                    
SITE     2 AC6  5 HOH A1074                                                     
SITE     1 AC7  3 ASP A 385  ASP A 527  LYS A 648                               
SITE     1 AC8  2 HIS A 507  TYR A 508                                          
SITE     1 AC9  3 GLU A 211  LYS A 657  HOH A1027                               
SITE     1 AD1  2 LYS A 674  GLU A 681                                          
SITE     1 AD2  5 SER A 563  LYS A 564  LEU A 565  ALA A 566                    
SITE     2 AD2  5 ARG A 569                                                     
CRYST1   72.340   83.830  177.660  90.00  90.00  90.00 P 21 21 21    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      0.013824  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011929  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005629        0.00000                         
ATOM      1  N   LYS A   5      21.704  41.564  59.723  1.00 89.53           N  
ANISOU    1  N   LYS A   5     9494  16264   8260   -892  -1446  -3624       N  
ATOM      2  CA  LYS A   5      21.550  40.190  60.206  1.00 88.09           C  
ANISOU    2  CA  LYS A   5     9207  16327   7935   -713  -1385  -3449       C  
ATOM      3  C   LYS A   5      20.409  39.396  59.456  1.00 87.63           C  
ANISOU    3  C   LYS A   5     9244  16160   7893   -621  -1240  -3218       C  
ATOM      4  O   LYS A   5      20.701  38.266  59.053  1.00 84.10           O  
ANISOU    4  O   LYS A   5     8716  15783   7454   -598  -1160  -3027       O  
ATOM      5  CB  LYS A   5      21.341  40.160  61.727  1.00 91.90           C  
ANISOU    5  CB  LYS A   5     9634  17080   8203   -530  -1478  -3564       C  
ATOM      6  N   PRO A   6      19.162  39.943  59.226  1.00 83.91           N  
ANISOU    6  N   PRO A   6     8934  15518   7431   -571  -1208  -3232       N  
ATOM      7  CA  PRO A   6      18.105  39.163  58.530  1.00 80.56           C  
ANISOU    7  CA  PRO A   6     8583  15006   7022   -493  -1076  -3015       C  
ATOM      8  C   PRO A   6      18.384  38.690  57.100  1.00 78.79           C  
ANISOU    8  C   PRO A   6     8374  14599   6965   -625   -974  -2849       C  
ATOM      9  O   PRO A   6      18.972  39.397  56.268  1.00 78.72           O  
ANISOU    9  O   PRO A   6     8398  14407   7106   -806   -984  -2910       O  
ATOM     10  CB  PRO A   6      16.919  40.134  58.498  1.00 82.44           C  
ANISOU   10  CB  PRO A   6     8986  15076   7262   -450  -1086  -3115       C  
ATOM     11  CG  PRO A   6      17.116  40.985  59.691  1.00 89.24           C  
ANISOU   11  CG  PRO A   6     9832  16060   8014   -397  -1219  -3353       C  
ATOM     12  CD  PRO A   6      18.605  41.234  59.694  1.00 86.62           C  
ANISOU   12  CD  PRO A   6     9396  15762   7755   -559  -1296  -3451       C  
ATOM     13  N   VAL A   7      17.904  37.469  56.809  1.00 71.00           N  
ANISOU   13  N   VAL A   7     7367  13662   5947   -530   -873  -2631       N  
ATOM     14  CA  VAL A   7      18.030  36.846  55.489  1.00 68.72           C  
ANISOU   14  CA  VAL A   7     7095  13222   5794   -617   -770  -2458       C  
ATOM     15  C   VAL A   7      16.670  36.252  55.029  1.00 69.93           C  
ANISOU   15  C   VAL A   7     7348  13289   5935   -515   -671  -2292       C  
ATOM     16  O   VAL A   7      15.705  36.204  55.798  1.00 70.00           O  
ANISOU   16  O   VAL A   7     7388  13386   5822   -376   -679  -2296       O  
ATOM     17  CB  VAL A   7      19.165  35.779  55.437  1.00 72.31           C  
ANISOU   17  CB  VAL A   7     7394  13833   6247   -627   -755  -2355       C  
ATOM     18  CG1 VAL A   7      20.536  36.416  55.676  1.00 73.52           C  
ANISOU   18  CG1 VAL A   7     7443  14057   6435   -754   -846  -2516       C  
ATOM     19  CG2 VAL A   7      18.917  34.636  56.423  1.00 71.82           C  
ANISOU   19  CG2 VAL A   7     7252  14014   6024   -438   -752  -2243       C  
ATOM     20  N   TRP A   8      16.620  35.803  53.779  1.00 63.45           N  
ANISOU   20  N   TRP A   8     6567  12305   5237   -590   -581  -2152       N  
ATOM     21  CA  TRP A   8      15.484  35.125  53.196  1.00 61.80           C  
ANISOU   21  CA  TRP A   8     6437  12008   5038   -518   -488  -1984       C  
ATOM     22  C   TRP A   8      15.831  33.664  53.014  1.00 66.74           C  
ANISOU   22  C   TRP A   8     6974  12734   5651   -468   -430  -1796       C  
ATOM     23  O   TRP A   8      16.853  33.350  52.403  1.00 65.75           O  
ANISOU   23  O   TRP A   8     6786  12590   5607   -556   -417  -1767       O  
ATOM     24  CB  TRP A   8      15.105  35.745  51.850  1.00 58.85           C  
ANISOU   24  CB  TRP A   8     6190  11357   4814   -638   -436  -1973       C  
ATOM     25  CG  TRP A   8      14.416  37.073  51.938  1.00 59.38           C  
ANISOU   25  CG  TRP A   8     6379  11288   4893   -656   -482  -2124       C  
ATOM     26  CD1 TRP A   8      14.842  38.254  51.407  1.00 62.61           C  
ANISOU   26  CD1 TRP A   8     6860  11517   5412   -802   -522  -2252       C  
ATOM     27  CD2 TRP A   8      13.125  37.325  52.497  1.00 58.64           C  
ANISOU   27  CD2 TRP A   8     6361  11212   4709   -522   -487  -2149       C  
ATOM     28  NE1 TRP A   8      13.896  39.228  51.605  1.00 62.09           N  
ANISOU   28  NE1 TRP A   8     6919  11340   5330   -758   -558  -2360       N  
ATOM     29  CE2 TRP A   8      12.835  38.688  52.282  1.00 63.13           C  
ANISOU   29  CE2 TRP A   8     7049  11601   5337   -581   -537  -2305       C  
ATOM     30  CE3 TRP A   8      12.145  36.512  53.090  1.00 59.32           C  
ANISOU   30  CE3 TRP A   8     6425  11441   4674   -362   -449  -2042       C  
ATOM     31  CZ2 TRP A   8      11.632  39.269  52.694  1.00 63.33           C  
ANISOU   31  CZ2 TRP A   8     7167  11600   5295   -465   -556  -2374       C  
ATOM     32  CZ3 TRP A   8      10.961  37.088  53.510  1.00 61.34           C  
ANISOU   32  CZ3 TRP A   8     6760  11688   4860   -259   -461  -2104       C  
ATOM     33  CH2 TRP A   8      10.706  38.449  53.300  1.00 62.85           C  
ANISOU   33  CH2 TRP A   8     7065  11708   5105   -302   -514  -2273       C  
ATOM     34  N   ALA A   9      15.012  32.778  53.578  1.00 63.18           N  
ANISOU   34  N   ALA A   9     6513  12398   5094   -325   -401  -1671       N  
ATOM     35  CA  ALA A   9      15.232  31.340  53.515  1.00 61.87           C  
ANISOU   35  CA  ALA A   9     6278  12320   4909   -260   -356  -1485       C  
ATOM     36  C   ALA A   9      13.962  30.705  53.029  1.00 66.38           C  
ANISOU   36  C   ALA A   9     6934  12793   5492   -207   -276  -1326       C  
ATOM     37  O   ALA A   9      12.909  31.327  53.190  1.00 66.07           O  
ANISOU   37  O   ALA A   9     6974  12709   5422   -178   -271  -1370       O  
ATOM     38  CB  ALA A   9      15.624  30.814  54.886  1.00 63.44           C  
ANISOU   38  CB  ALA A   9     6366  12788   4952   -140   -415  -1483       C  
ATOM     39  N   PRO A  10      14.003  29.494  52.421  1.00 63.26           N  
ANISOU   39  N   PRO A  10     6528  12363   5144   -190   -218  -1147       N  
ATOM     40  CA  PRO A  10      12.776  28.947  51.801  1.00 61.95           C  
ANISOU   40  CA  PRO A  10     6450  12077   5011   -163   -145  -1004       C  
ATOM     41  C   PRO A  10      11.612  28.709  52.752  1.00 64.57           C  
ANISOU   41  C   PRO A  10     6788  12533   5211    -47   -142   -942       C  
ATOM     42  O   PRO A  10      11.785  28.580  53.955  1.00 63.80           O  
ANISOU   42  O   PRO A  10     6618  12642   4981     38   -188   -962       O  
ATOM     43  CB  PRO A  10      13.251  27.638  51.167  1.00 62.73           C  
ANISOU   43  CB  PRO A  10     6521  12141   5173   -159   -104   -843       C  
ATOM     44  CG  PRO A  10      14.707  27.872  50.913  1.00 67.24           C  
ANISOU   44  CG  PRO A  10     7018  12734   5797   -228   -137   -934       C  
ATOM     45  CD  PRO A  10      15.175  28.651  52.102  1.00 63.93           C  
ANISOU   45  CD  PRO A  10     6529  12488   5274   -206   -217  -1082       C  
ATOM     46  N   HIS A  11      10.404  28.720  52.163  1.00 60.91           N  
ANISOU   46  N   HIS A  11     6412  11946   4784    -49    -86   -873       N  
ATOM     47  CA  HIS A  11       9.101  28.509  52.808  1.00 59.23           C  
ANISOU   47  CA  HIS A  11     6212  11827   4468     44    -65   -798       C  
ATOM     48  C   HIS A  11       8.202  27.845  51.765  1.00 61.71           C  
ANISOU   48  C   HIS A  11     6593  11981   4872     16      8   -646       C  
ATOM     49  O   HIS A  11       8.135  28.338  50.635  1.00 58.19           O  
ANISOU   49  O   HIS A  11     6224  11337   4547    -68     31   -689       O  
ATOM     50  CB  HIS A  11       8.509  29.829  53.322  1.00 59.52           C  
ANISOU   50  CB  HIS A  11     6283  11893   4438     72    -97   -969       C  
ATOM     51  CG  HIS A  11       7.256  29.644  54.113  1.00 63.24           C  
ANISOU   51  CG  HIS A  11     6742  12507   4778    181    -76   -904       C  
ATOM     52  ND1 HIS A  11       6.041  29.386  53.498  1.00 63.89           N  
ANISOU   52  ND1 HIS A  11     6881  12499   4897    184    -14   -798       N  
ATOM     53  CD2 HIS A  11       7.067  29.688  55.453  1.00 66.02           C  
ANISOU   53  CD2 HIS A  11     7025  13101   4960    289   -109   -930       C  
ATOM     54  CE1 HIS A  11       5.160  29.278  54.478  1.00 63.53           C  
ANISOU   54  CE1 HIS A  11     6790  12643   4705    287     -7   -760       C  
ATOM     55  NE2 HIS A  11       5.727  29.468  55.671  1.00 65.44           N  
ANISOU   55  NE2 HIS A  11     6960  13089   4815    357    -61   -837       N  
ATOM     56  N   PRO A  12       7.512  26.731  52.111  1.00 60.37           N  
ANISOU   56  N   PRO A  12     6398  11892   4647     78     40   -466       N  
ATOM     57  CA  PRO A  12       6.739  25.989  51.093  1.00 59.30           C  
ANISOU   57  CA  PRO A  12     6323  11600   4608     39    100   -319       C  
ATOM     58  C   PRO A  12       5.556  26.727  50.461  1.00 64.11           C  
ANISOU   58  C   PRO A  12     7011  12091   5257     14    132   -362       C  
ATOM     59  O   PRO A  12       5.200  26.390  49.338  1.00 62.61           O  
ANISOU   59  O   PRO A  12     6883  11728   5179    -44    170   -295       O  
ATOM     60  CB  PRO A  12       6.246  24.756  51.852  1.00 61.56           C  
ANISOU   60  CB  PRO A  12     6558  12026   4808    110    115   -129       C  
ATOM     61  CG  PRO A  12       6.291  25.149  53.298  1.00 67.33           C  
ANISOU   61  CG  PRO A  12     7213  12999   5369    198     77   -189       C  
ATOM     62  CD  PRO A  12       7.519  26.010  53.397  1.00 63.42           C  
ANISOU   62  CD  PRO A  12     6699  12510   4886    176     21   -375       C  
ATOM     63  N   THR A  13       4.922  27.687  51.153  1.00 62.97           N  
ANISOU   63  N   THR A  13     6866  12042   5019     67    115   -471       N  
ATOM     64  CA  THR A  13       3.769  28.365  50.536  1.00 62.21           C  
ANISOU   64  CA  THR A  13     6842  11836   4957     59    143   -508       C  
ATOM     65  C   THR A  13       4.055  29.844  50.256  1.00 62.67           C  
ANISOU   65  C   THR A  13     6967  11792   5053     31    106   -716       C  
ATOM     66  O   THR A  13       3.403  30.428  49.392  1.00 61.11           O  
ANISOU   66  O   THR A  13     6852  11440   4927      2    124   -750       O  
ATOM     67  CB  THR A  13       2.486  28.202  51.381  1.00 71.99           C  
ANISOU   67  CB  THR A  13     8039  13248   6068    153    164   -442       C  
ATOM     68  OG1 THR A  13       2.562  28.996  52.562  1.00 74.33           O  
ANISOU   68  OG1 THR A  13     8291  13726   6226    237    121   -576       O  
ATOM     69  CG2 THR A  13       2.181  26.753  51.724  1.00 70.62           C  
ANISOU   69  CG2 THR A  13     7803  13173   5856    168    198   -223       C  
ATOM     70  N   ASP A  14       4.996  30.456  51.002  1.00 58.08           N  
ANISOU   70  N   ASP A  14     6351  11297   4421     40     48   -853       N  
ATOM     71  CA  ASP A  14       5.338  31.859  50.791  1.00 56.92           C  
ANISOU   71  CA  ASP A  14     6269  11044   4314      2      1  -1053       C  
ATOM     72  C   ASP A  14       6.528  32.031  49.836  1.00 57.17           C  
ANISOU   72  C   ASP A  14     6333  10906   4484   -126     -6  -1091       C  
ATOM     73  O   ASP A  14       6.772  33.145  49.389  1.00 56.54           O  
ANISOU   73  O   ASP A  14     6325  10688   4468   -188    -35  -1227       O  
ATOM     74  CB  ASP A  14       5.622  32.548  52.130  1.00 60.23           C  
ANISOU   74  CB  ASP A  14     6636  11647   4600     79    -66  -1202       C  
ATOM     75  CG  ASP A  14       4.439  32.567  53.088  1.00 68.92           C  
ANISOU   75  CG  ASP A  14     7706  12931   5551    214    -60  -1192       C  
ATOM     76  OD1 ASP A  14       3.304  32.288  52.645  1.00 68.44           O  
ANISOU   76  OD1 ASP A  14     7675  12830   5500    239     -6  -1096       O  
ATOM     77  OD2 ASP A  14       4.650  32.843  54.274  1.00 76.05           O  
ANISOU   77  OD2 ASP A  14     8548  14028   6320    294   -107  -1280       O  
ATOM     78  N   GLY A  15       7.232  30.943  49.519  1.00 52.76           N  
ANISOU   78  N   GLY A  15     5722  10358   3967   -163     20   -968       N  
ATOM     79  CA  GLY A  15       8.426  30.976  48.683  1.00 53.59           C  
ANISOU   79  CA  GLY A  15     5831  10347   4185   -273     18   -993       C  
ATOM     80  C   GLY A  15       9.624  31.239  49.577  1.00 60.74           C  
ANISOU   80  C   GLY A  15     6649  11392   5036   -277    -45  -1099       C  
ATOM     81  O   GLY A  15      10.538  30.418  49.675  1.00 63.21           O  
ANISOU   81  O   GLY A  15     6882  11781   5353   -284    -46  -1037       O  
ATOM     82  N   PHE A  16       9.588  32.356  50.301  1.00 56.32           N  
ANISOU   82  N   PHE A  16     6100  10880   4418   -260   -104  -1264       N  
ATOM     83  CA  PHE A  16      10.630  32.734  51.252  1.00 56.10           C  
ANISOU   83  CA  PHE A  16     5991  10998   4327   -260   -178  -1389       C  
ATOM     84  C   PHE A  16      10.036  33.218  52.566  1.00 61.51           C  
ANISOU   84  C   PHE A  16     6657  11850   4863   -145   -229  -1484       C  
ATOM     85  O   PHE A  16       8.895  33.672  52.594  1.00 61.11           O  
ANISOU   85  O   PHE A  16     6677  11758   4783    -90   -216  -1507       O  
ATOM     86  CB  PHE A  16      11.537  33.811  50.654  1.00 56.90           C  
ANISOU   86  CB  PHE A  16     6128  10957   4536   -398   -215  -1536       C  
ATOM     87  CG  PHE A  16      12.372  33.281  49.522  1.00 56.69           C  
ANISOU   87  CG  PHE A  16     6085  10825   4631   -505   -168  -1450       C  
ATOM     88  CD1 PHE A  16      13.491  32.496  49.769  1.00 59.42           C  
ANISOU   88  CD1 PHE A  16     6312  11300   4963   -511   -179  -1409       C  
ATOM     89  CD2 PHE A  16      12.040  33.557  48.205  1.00 56.25           C  
ANISOU   89  CD2 PHE A  16     6129  10551   4694   -590   -114  -1410       C  
ATOM     90  CE1 PHE A  16      14.263  32.006  48.717  1.00 58.63           C  
ANISOU   90  CE1 PHE A  16     6192  11118   4969   -597   -134  -1338       C  
ATOM     91  CE2 PHE A  16      12.826  33.077  47.158  1.00 57.82           C  
ANISOU   91  CE2 PHE A  16     6307  10668   4991   -682    -69  -1337       C  
ATOM     92  CZ  PHE A  16      13.919  32.291  47.422  1.00 55.90           C  
ANISOU   92  CZ  PHE A  16     5943  10561   4734   -681    -77  -1302       C  
ATOM     93  N   GLN A  17      10.811  33.091  53.660  1.00 58.96           N  
ANISOU   93  N   GLN A  17     6233  11732   4438    -99   -288  -1541       N  
ATOM     94  CA  GLN A  17      10.451  33.580  54.982  1.00 59.82           C  
ANISOU   94  CA  GLN A  17     6310  12029   4389     13   -348  -1653       C  
ATOM     95  C   GLN A  17      11.674  34.282  55.549  1.00 65.52           C  
ANISOU   95  C   GLN A  17     6979  12819   5098    -36   -441  -1834       C  
ATOM     96  O   GLN A  17      12.782  34.027  55.072  1.00 64.32           O  
ANISOU   96  O   GLN A  17     6778  12627   5032   -134   -448  -1821       O  
ATOM     97  CB  GLN A  17       9.925  32.459  55.913  1.00 60.88           C  
ANISOU   97  CB  GLN A  17     6364  12394   4372    149   -320  -1500       C  
ATOM     98  CG  GLN A  17      10.960  31.393  56.275  1.00 71.59           C  
ANISOU   98  CG  GLN A  17     7613  13891   5699    157   -332  -1399       C  
ATOM     99  CD  GLN A  17      10.405  30.248  57.079  1.00 79.84           C  
ANISOU   99  CD  GLN A  17     8596  15128   6611    278   -300  -1219       C  
ATOM    100  OE1 GLN A  17       9.888  30.417  58.194  1.00 74.07           O  
ANISOU  100  OE1 GLN A  17     7831  14594   5717    388   -324  -1251       O  
ATOM    101  NE2 GLN A  17      10.544  29.041  56.541  1.00 68.37           N  
ANISOU  101  NE2 GLN A  17     7130  13628   5221    260   -248  -1024       N  
ATOM    102  N   VAL A  18      11.470  35.199  56.512  1.00 64.58           N  
ANISOU  102  N   VAL A  18     6867  12797   4874     30   -516  -2011       N  
ATOM    103  CA  VAL A  18      12.551  35.930  57.180  1.00 66.23           C  
ANISOU  103  CA  VAL A  18     7023  13083   5056    -10   -620  -2205       C  
ATOM    104  C   VAL A  18      13.155  35.018  58.223  1.00 74.18           C  
ANISOU  104  C   VAL A  18     7892  14369   5924     79   -646  -2144       C  
ATOM    105  O   VAL A  18      12.439  34.446  59.043  1.00 74.26           O  
ANISOU  105  O   VAL A  18     7868  14564   5785    221   -626  -2060       O  
ATOM    106  CB  VAL A  18      12.107  37.272  57.832  1.00 71.66           C  
ANISOU  106  CB  VAL A  18     7781  13761   5685     34   -702  -2436       C  
ATOM    107  CG1 VAL A  18      13.298  38.026  58.415  1.00 73.43           C  
ANISOU  107  CG1 VAL A  18     7957  14037   5907    -37   -817  -2641       C  
ATOM    108  CG2 VAL A  18      11.367  38.158  56.856  1.00 71.09           C  
ANISOU  108  CG2 VAL A  18     7859  13415   5736    -26   -677  -2481       C  
ATOM    109  N   GLY A  19      14.469  34.927  58.209  1.00 73.61           N  
ANISOU  109  N   GLY A  19     7737  14335   5897     -5   -692  -2186       N  
ATOM    110  CA  GLY A  19      15.215  34.132  59.165  1.00 74.85           C  
ANISOU  110  CA  GLY A  19     7759  14752   5930     74   -732  -2145       C  
ATOM    111  C   GLY A  19      16.538  34.783  59.478  1.00 81.83           C  
ANISOU  111  C   GLY A  19     8566  15689   6836    -14   -833  -2327       C  
ATOM    112  O   GLY A  19      16.867  35.848  58.939  1.00 82.60           O  
ANISOU  112  O   GLY A  19     8720  15611   7054   -150   -869  -2476       O  
ATOM    113  N   ASN A  20      17.281  34.157  60.383  1.00 79.13           N  
ANISOU  113  N   ASN A  20     8096  15595   6375     62   -884  -2313       N  
ATOM    114  CA  ASN A  20      18.626  34.555  60.777  1.00 79.93           C  
ANISOU  114  CA  ASN A  20     8092  15800   6480     -8   -984  -2464       C  
ATOM    115  C   ASN A  20      19.518  33.360  60.594  1.00 83.05           C  
ANISOU  115  C   ASN A  20     8370  16298   6887      3   -957  -2306       C  
ATOM    116  O   ASN A  20      19.057  32.236  60.836  1.00 82.09           O  
ANISOU  116  O   ASN A  20     8233  16275   6684    128   -903  -2114       O  
ATOM    117  CB  ASN A  20      18.670  35.035  62.232  1.00 81.11           C  
ANISOU  117  CB  ASN A  20     8188  16187   6443    101  -1092  -2631       C  
ATOM    118  CG  ASN A  20      17.834  36.250  62.533  1.00110.93           C  
ANISOU  118  CG  ASN A  20    12077  19881  10192    114  -1134  -2814       C  
ATOM    119  OD1 ASN A  20      18.336  37.379  62.607  1.00105.03           O  
ANISOU  119  OD1 ASN A  20    11352  19052   9503     12  -1223  -3033       O  
ATOM    120  ND2 ASN A  20      16.550  36.030  62.791  1.00105.75           N  
ANISOU  120  ND2 ASN A  20    11486  19257   9435    248  -1077  -2732       N  
ATOM    121  N   ILE A  21      20.778  33.573  60.147  1.00 79.20           N  
ANISOU  121  N   ILE A  21     7801  15786   6503   -127   -995  -2379       N  
ATOM    122  CA  ILE A  21      21.738  32.474  60.023  1.00 78.19           C  
ANISOU  122  CA  ILE A  21     7548  15777   6381   -104   -983  -2252       C  
ATOM    123  C   ILE A  21      22.260  32.201  61.434  1.00 84.36           C  
ANISOU  123  C   ILE A  21     8206  16868   6979     24  -1082  -2310       C  
ATOM    124  O   ILE A  21      22.719  33.137  62.103  1.00 85.04           O  
ANISOU  124  O   ILE A  21     8248  17043   7019    -16  -1185  -2521       O  
ATOM    125  CB  ILE A  21      22.891  32.763  59.013  1.00 80.76           C  
ANISOU  125  CB  ILE A  21     7819  15989   6879   -285   -979  -2303       C  
ATOM    126  CG1 ILE A  21      22.349  33.022  57.593  1.00 80.18           C  
ANISOU  126  CG1 ILE A  21     7874  15617   6974   -403   -877  -2233       C  
ATOM    127  CG2 ILE A  21      23.903  31.603  58.998  1.00 79.78           C  
ANISOU  127  CG2 ILE A  21     7550  16022   6740   -231   -976  -2188       C  
ATOM    128  CD1 ILE A  21      23.210  33.935  56.769  1.00 87.93           C  
ANISOU  128  CD1 ILE A  21     8841  16460   8108   -610   -891  -2354       C  
ATOM    129  N   VAL A  22      22.164  30.950  61.905  1.00 82.50           N  
ANISOU  129  N   VAL A  22     7922  16791   6633    180  -1056  -2126       N  
ATOM    130  CA  VAL A  22      22.691  30.626  63.242  1.00 85.73           C  
ANISOU  130  CA  VAL A  22     8212  17506   6854    313  -1151  -2163       C  
ATOM    131  C   VAL A  22      23.958  29.762  63.087  1.00 92.70           C  
ANISOU  131  C   VAL A  22     8955  18505   7762    326  -1174  -2090       C  
ATOM    132  O   VAL A  22      24.851  29.843  63.928  1.00 94.43           O  
ANISOU  132  O   VAL A  22     9048  18954   7877    372  -1275  -2190       O  
ATOM    133  CB  VAL A  22      21.664  30.026  64.244  1.00 89.45           C  
ANISOU  133  CB  VAL A  22     8720  18134   7135    500  -1133  -2040       C  
ATOM    134  CG1 VAL A  22      20.609  31.059  64.613  1.00 89.80           C  
ANISOU  134  CG1 VAL A  22     8866  18131   7123    504  -1140  -2172       C  
ATOM    135  CG2 VAL A  22      21.008  28.753  63.721  1.00 87.31           C  
ANISOU  135  CG2 VAL A  22     8503  17778   6893    567  -1023  -1761       C  
ATOM    136  N   ASP A  23      24.052  28.994  61.986  1.00 89.26           N  
ANISOU  136  N   ASP A  23     8540  17911   7463    286  -1085  -1931       N  
ATOM    137  CA  ASP A  23      25.209  28.163  61.705  1.00 90.24           C  
ANISOU  137  CA  ASP A  23     8541  18122   7624    306  -1096  -1858       C  
ATOM    138  C   ASP A  23      25.427  28.020  60.195  1.00 92.05           C  
ANISOU  138  C   ASP A  23     8806  18114   8055    179  -1006  -1796       C  
ATOM    139  O   ASP A  23      24.509  27.655  59.457  1.00 90.05           O  
ANISOU  139  O   ASP A  23     8677  17666   7871    177   -910  -1660       O  
ATOM    140  CB  ASP A  23      25.072  26.781  62.372  1.00 93.15           C  
ANISOU  140  CB  ASP A  23     8883  18650   7861    507  -1092  -1652       C  
ATOM    141  CG  ASP A  23      26.321  25.921  62.264  1.00110.28           C  
ANISOU  141  CG  ASP A  23    10915  20946  10040    566  -1126  -1591       C  
ATOM    142  OD1 ASP A  23      27.297  26.195  62.999  1.00112.77           O  
ANISOU  142  OD1 ASP A  23    11092  21484  10272    589  -1229  -1719       O  
ATOM    143  OD2 ASP A  23      26.326  24.978  61.433  1.00118.19           O  
ANISOU  143  OD2 ASP A  23    11947  21828  11130    595  -1055  -1421       O  
ATOM    144  N   ILE A  24      26.649  28.342  59.743  1.00 88.32           N  
ANISOU  144  N   ILE A  24     8217  17671   7669     68  -1040  -1902       N  
ATOM    145  CA  ILE A  24      27.070  28.193  58.348  1.00 86.54           C  
ANISOU  145  CA  ILE A  24     7994  17270   7618    -48   -960  -1854       C  
ATOM    146  C   ILE A  24      27.810  26.863  58.267  1.00 90.37           C  
ANISOU  146  C   ILE A  24     8378  17877   8083     81   -953  -1711       C  
ATOM    147  O   ILE A  24      28.637  26.571  59.127  1.00 90.72           O  
ANISOU  147  O   ILE A  24     8284  18161   8024    170  -1040  -1750       O  
ATOM    148  CB  ILE A  24      27.927  29.386  57.801  1.00 90.06           C  
ANISOU  148  CB  ILE A  24     8373  17669   8178   -262   -990  -2046       C  
ATOM    149  CG1 ILE A  24      27.370  30.764  58.243  1.00 90.70           C  
ANISOU  149  CG1 ILE A  24     8534  17679   8247   -364  -1042  -2224       C  
ATOM    150  CG2 ILE A  24      28.074  29.300  56.266  1.00 89.77           C  
ANISOU  150  CG2 ILE A  24     8372  17423   8315   -386   -886  -1977       C  
ATOM    151  CD1 ILE A  24      28.267  31.984  57.999  1.00 97.46           C  
ANISOU  151  CD1 ILE A  24     9317  18520   9194   -572  -1102  -2427       C  
ATOM    152  N   GLY A  25      27.485  26.068  57.261  1.00 86.95           N  
ANISOU  152  N   GLY A  25     8017  17277   7742    101   -857  -1552       N  
ATOM    153  CA  GLY A  25      28.116  24.779  57.037  1.00 87.61           C  
ANISOU  153  CA  GLY A  25     8029  17433   7825    229   -845  -1414       C  
ATOM    154  C   GLY A  25      28.629  24.617  55.620  1.00 93.45           C  
ANISOU  154  C   GLY A  25     8754  18033   8720    137   -769  -1393       C  
ATOM    155  O   GLY A  25      28.237  25.370  54.721  1.00 91.79           O  
ANISOU  155  O   GLY A  25     8624  17630   8621    -21   -707  -1441       O  
ATOM    156  N   PRO A  26      29.485  23.601  55.381  1.00 92.39           N  
ANISOU  156  N   PRO A  26     8522  17991   8590    246   -772  -1314       N  
ATOM    157  CA  PRO A  26      30.012  23.382  54.028  1.00 91.90           C  
ANISOU  157  CA  PRO A  26     8435  17820   8662    176   -698  -1297       C  
ATOM    158  C   PRO A  26      28.951  23.238  52.943  1.00 95.96           C  
ANISOU  158  C   PRO A  26     9128  18052   9280    124   -591  -1196       C  
ATOM    159  O   PRO A  26      29.184  23.712  51.833  1.00 97.14           O  
ANISOU  159  O   PRO A  26     9280  18087   9543    -13   -528  -1243       O  
ATOM    160  CB  PRO A  26      30.794  22.079  54.178  1.00 94.39           C  
ANISOU  160  CB  PRO A  26     8653  18277   8933    367   -727  -1198       C  
ATOM    161  CG  PRO A  26      31.227  22.074  55.594  1.00 99.88           C  
ANISOU  161  CG  PRO A  26     9243  19223   9482    470   -839  -1244       C  
ATOM    162  CD  PRO A  26      30.070  22.640  56.340  1.00 95.03           C  
ANISOU  162  CD  PRO A  26     8757  18548   8801    443   -850  -1246       C  
ATOM    163  N   ASP A  27      27.810  22.595  53.227  1.00 91.22           N  
ANISOU  163  N   ASP A  27     8672  17347   8643    226   -570  -1058       N  
ATOM    164  CA  ASP A  27      26.803  22.407  52.184  1.00 89.20           C  
ANISOU  164  CA  ASP A  27     8577  16831   8485    179   -474   -964       C  
ATOM    165  C   ASP A  27      25.436  23.058  52.479  1.00 88.43           C  
ANISOU  165  C   ASP A  27     8625  16607   8369    120   -453   -960       C  
ATOM    166  O   ASP A  27      24.639  23.225  51.553  1.00 86.12           O  
ANISOU  166  O   ASP A  27     8454  16101   8165     42   -378   -923       O  
ATOM    167  CB  ASP A  27      26.616  20.917  51.896  1.00 91.74           C  
ANISOU  167  CB  ASP A  27     8950  17092   8815    340   -449   -784       C  
ATOM    168  CG  ASP A  27      27.709  20.367  51.009  1.00109.22           C  
ANISOU  168  CG  ASP A  27    11070  19332  11098    369   -430   -789       C  
ATOM    169  OD1 ASP A  27      28.874  20.324  51.462  1.00112.43           O  
ANISOU  169  OD1 ASP A  27    11313  19949  11456    418   -491   -858       O  
ATOM    170  OD2 ASP A  27      27.405  20.002  49.848  1.00115.88           O  
ANISOU  170  OD2 ASP A  27    11998  19994  12039    348   -355   -729       O  
ATOM    171  N   SER A  28      25.173  23.448  53.736  1.00 84.07           N  
ANISOU  171  N   SER A  28     8055  16193   7696    161   -521  -1006       N  
ATOM    172  CA  SER A  28      23.888  24.047  54.092  1.00 81.74           C  
ANISOU  172  CA  SER A  28     7885  15806   7367    129   -505  -1009       C  
ATOM    173  C   SER A  28      24.020  25.081  55.204  1.00 84.24           C  
ANISOU  173  C   SER A  28     8146  16281   7582    102   -585  -1166       C  
ATOM    174  O   SER A  28      25.046  25.144  55.885  1.00 85.70           O  
ANISOU  174  O   SER A  28     8193  16670   7700    134   -663  -1249       O  
ATOM    175  CB  SER A  28      22.908  22.957  54.515  1.00 84.47           C  
ANISOU  175  CB  SER A  28     8318  16128   7647    271   -485   -817       C  
ATOM    176  OG  SER A  28      23.423  22.229  55.620  1.00 96.28           O  
ANISOU  176  OG  SER A  28     9723  17844   9016    418   -557   -765       O  
ATOM    177  N   LEU A  29      22.975  25.903  55.371  1.00 77.70           N  
ANISOU  177  N   LEU A  29     7425  15360   6740     48   -571  -1216       N  
ATOM    178  CA  LEU A  29      22.885  26.916  56.426  1.00 77.47           C  
ANISOU  178  CA  LEU A  29     7371  15455   6608     35   -647  -1371       C  
ATOM    179  C   LEU A  29      21.828  26.479  57.425  1.00 76.39           C  
ANISOU  179  C   LEU A  29     7291  15404   6330    176   -652  -1274       C  
ATOM    180  O   LEU A  29      20.926  25.718  57.066  1.00 73.76           O  
ANISOU  180  O   LEU A  29     7051  14960   6015    227   -583  -1106       O  
ATOM    181  CB  LEU A  29      22.526  28.288  55.813  1.00 77.46           C  
ANISOU  181  CB  LEU A  29     7451  15277   6701   -132   -630  -1520       C  
ATOM    182  CG  LEU A  29      23.680  29.212  55.361  1.00 83.31           C  
ANISOU  182  CG  LEU A  29     8110  16008   7535   -295   -667  -1688       C  
ATOM    183  CD1 LEU A  29      24.580  28.556  54.339  1.00 83.51           C  
ANISOU  183  CD1 LEU A  29     8067  15997   7666   -338   -617  -1613       C  
ATOM    184  CD2 LEU A  29      23.144  30.470  54.745  1.00 84.33           C  
ANISOU  184  CD2 LEU A  29     8352  15932   7758   -447   -646  -1798       C  
ATOM    185  N   THR A  30      21.951  26.910  58.672  1.00 73.25           N  
ANISOU  185  N   THR A  30     6832  15211   5787    239   -735  -1372       N  
ATOM    186  CA  THR A  30      20.958  26.610  59.699  1.00 73.01           C  
ANISOU  186  CA  THR A  30     6846  15293   5603    371   -740  -1291       C  
ATOM    187  C   THR A  30      20.190  27.899  59.933  1.00 76.69           C  
ANISOU  187  C   THR A  30     7386  15707   6047    310   -752  -1450       C  
ATOM    188  O   THR A  30      20.756  28.919  60.345  1.00 77.19           O  
ANISOU  188  O   THR A  30     7400  15842   6087    253   -830  -1656       O  
ATOM    189  CB  THR A  30      21.572  25.997  60.966  1.00 82.61           C  
ANISOU  189  CB  THR A  30     7945  16794   6647    517   -820  -1260       C  
ATOM    190  OG1 THR A  30      22.314  24.842  60.591  1.00 82.90           O  
ANISOU  190  OG1 THR A  30     7926  16844   6728    571   -810  -1118       O  
ATOM    191  CG2 THR A  30      20.504  25.572  61.979  1.00 82.05           C  
ANISOU  191  CG2 THR A  30     7920  16847   6409    654   -812  -1142       C  
ATOM    192  N   ILE A  31      18.908  27.862  59.602  1.00 72.41           N  
ANISOU  192  N   ILE A  31     6963  15026   5522    317   -677  -1361       N  
ATOM    193  CA  ILE A  31      18.063  29.037  59.734  1.00 72.39           C  
ANISOU  193  CA  ILE A  31     7043  14957   5506    276   -682  -1502       C  
ATOM    194  C   ILE A  31      17.129  28.884  60.920  1.00 78.11           C  
ANISOU  194  C   ILE A  31     7774  15863   6041    420   -693  -1461       C  
ATOM    195  O   ILE A  31      16.490  27.848  61.102  1.00 77.37           O  
ANISOU  195  O   ILE A  31     7693  15818   5888    513   -640  -1257       O  
ATOM    196  CB  ILE A  31      17.273  29.327  58.427  1.00 73.28           C  
ANISOU  196  CB  ILE A  31     7284  14782   5779    172   -594  -1464       C  
ATOM    197  CG1 ILE A  31      18.182  29.285  57.151  1.00 71.57           C  
ANISOU  197  CG1 ILE A  31     7056  14395   5741     37   -567  -1466       C  
ATOM    198  CG2 ILE A  31      16.461  30.642  58.525  1.00 74.57           C  
ANISOU  198  CG2 ILE A  31     7536  14862   5934    134   -610  -1628       C  
ATOM    199  CD1 ILE A  31      19.289  30.317  57.056  1.00 67.31           C  
ANISOU  199  CD1 ILE A  31     6457  13859   5259    -85   -637  -1671       C  
ATOM    200  N   GLU A  32      17.064  29.933  61.716  1.00 77.03           N  
ANISOU  200  N   GLU A  32     7629  15829   5811    436   -764  -1658       N  
ATOM    201  CA  GLU A  32      16.137  30.072  62.819  1.00 78.83           C  
ANISOU  201  CA  GLU A  32     7867  16232   5853    566   -777  -1667       C  
ATOM    202  C   GLU A  32      15.057  31.031  62.321  1.00 84.89           C  
ANISOU  202  C   GLU A  32     8756  16818   6681    519   -738  -1756       C  
ATOM    203  O   GLU A  32      15.368  32.215  62.154  1.00 85.07           O  
ANISOU  203  O   GLU A  32     8810  16746   6765    435   -795  -1971       O  
ATOM    204  CB  GLU A  32      16.870  30.593  64.055  1.00 82.03           C  
ANISOU  204  CB  GLU A  32     8178  16885   6106    630   -894  -1846       C  
ATOM    205  CG  GLU A  32      15.961  31.059  65.176  1.00 91.38           C  
ANISOU  205  CG  GLU A  32     9378  18248   7096    757   -919  -1921       C  
ATOM    206  CD  GLU A  32      16.719  31.539  66.393  1.00112.11           C  
ANISOU  206  CD  GLU A  32    11909  21127   9561    826  -1041  -2105       C  
ATOM    207  OE1 GLU A  32      17.409  30.709  67.029  1.00105.27           O  
ANISOU  207  OE1 GLU A  32    10940  20472   8586    908  -1075  -2012       O  
ATOM    208  OE2 GLU A  32      16.655  32.754  66.690  1.00107.09           O  
ANISOU  208  OE2 GLU A  32    11306  20473   8912    800  -1111  -2347       O  
ATOM    209  N   PRO A  33      13.814  30.570  62.016  1.00 83.53           N  
ANISOU  209  N   PRO A  33     8654  16579   6504    562   -647  -1596       N  
ATOM    210  CA  PRO A  33      12.794  31.511  61.490  1.00 84.23           C  
ANISOU  210  CA  PRO A  33     8855  16494   6653    524   -614  -1687       C  
ATOM    211  C   PRO A  33      12.509  32.638  62.477  1.00 93.90           C  
ANISOU  211  C   PRO A  33    10084  17851   7742    598   -691  -1908       C  
ATOM    212  O   PRO A  33      12.754  32.474  63.675  1.00 95.07           O  
ANISOU  212  O   PRO A  33    10149  18263   7710    710   -744  -1936       O  
ATOM    213  CB  PRO A  33      11.557  30.633  61.235  1.00 84.51           C  
ANISOU  213  CB  PRO A  33     8931  16507   6672    579   -511  -1461       C  
ATOM    214  CG  PRO A  33      12.043  29.233  61.260  1.00 88.36           C  
ANISOU  214  CG  PRO A  33     9352  17075   7148    605   -484  -1244       C  
ATOM    215  CD  PRO A  33      13.272  29.204  62.142  1.00 84.94           C  
ANISOU  215  CD  PRO A  33     8814  16837   6624    643   -575  -1331       C  
ATOM    216  N   LEU A  34      12.063  33.800  61.974  1.00 94.57           N  
ANISOU  216  N   LEU A  34    10268  17753   7913    539   -705  -2074       N  
ATOM    217  CA  LEU A  34      11.857  34.969  62.818  1.00 99.05           C  
ANISOU  217  CA  LEU A  34    10855  18407   8372    604   -791  -2316       C  
ATOM    218  C   LEU A  34      10.722  34.800  63.835  1.00109.99           C  
ANISOU  218  C   LEU A  34    12223  20020   9548    784   -769  -2283       C  
ATOM    219  O   LEU A  34       9.609  34.388  63.492  1.00109.02           O  
ANISOU  219  O   LEU A  34    12141  19859   9423    825   -679  -2138       O  
ATOM    220  CB  LEU A  34      11.640  36.249  61.998  1.00 98.93           C  
ANISOU  220  CB  LEU A  34    10964  18117   8506    502   -816  -2492       C  
ATOM    221  CG  LEU A  34      12.233  37.517  62.645  1.00105.05           C  
ANISOU  221  CG  LEU A  34    11748  18914   9251    486   -947  -2783       C  
ATOM    222  CD1 LEU A  34      13.680  37.731  62.227  1.00104.83           C  
ANISOU  222  CD1 LEU A  34    11680  18790   9360    319  -1003  -2850       C  
ATOM    223  CD2 LEU A  34      11.419  38.737  62.294  1.00107.88           C  
ANISOU  223  CD2 LEU A  34    12244  19081   9664    485   -969  -2948       C  
ATOM    224  N   ASN A  35      11.056  35.131  65.097  1.00113.45           N  
ANISOU  224  N   ASN A  35    12592  20709   9805    888   -856  -2423       N  
ATOM    225  CA  ASN A  35      10.220  35.136  66.306  1.00116.99           C  
ANISOU  225  CA  ASN A  35    13002  21435  10015   1071   -862  -2446       C  
ATOM    226  C   ASN A  35       9.439  33.796  66.490  1.00125.62           C  
ANISOU  226  C   ASN A  35    14038  22688  11002   1156   -755  -2150       C  
ATOM    227  O   ASN A  35       8.224  33.799  66.754  1.00125.88           O  
ANISOU  227  O   ASN A  35    14078  22842  10910   1268   -704  -2109       O  
ATOM    228  CB  ASN A  35       9.271  36.365  66.309  1.00116.35           C  
ANISOU  228  CB  ASN A  35    13021  21269   9920   1125   -879  -2637       C  
ATOM    229  CG  ASN A  35       9.960  37.717  66.177  1.00121.27           C  
ANISOU  229  CG  ASN A  35    13712  21729  10635   1050   -995  -2933       C  
ATOM    230  OD1 ASN A  35      11.079  37.945  66.676  1.00102.19           O  
ANISOU  230  OD1 ASN A  35    11241  19390   8197   1014  -1095  -3068       O  
ATOM    231  ND2 ASN A  35       9.294  38.653  65.497  1.00111.31           N  
ANISOU  231  ND2 ASN A  35    12575  20236   9480   1023   -989  -3040       N  
ATOM    232  N   GLN A  36      10.160  32.654  66.361  1.00123.92           N  
ANISOU  232  N   GLN A  36    13765  22481  10837   1104   -724  -1946       N  
ATOM    233  CA  GLN A  36       9.579  31.321  66.547  1.00123.81           C  
ANISOU  233  CA  GLN A  36    13703  22601  10736   1170   -635  -1658       C  
ATOM    234  C   GLN A  36       9.808  30.822  68.008  1.00131.39           C  
ANISOU  234  C   GLN A  36    14555  23926  11441   1318   -679  -1630       C  
ATOM    235  O   GLN A  36       8.808  30.573  68.689  1.00132.72           O  
ANISOU  235  O   GLN A  36    14700  24288  11439   1433   -631  -1545       O  
ATOM    236  CB  GLN A  36      10.079  30.313  65.486  1.00123.03           C  
ANISOU  236  CB  GLN A  36    13612  22319  10816   1057   -580  -1446       C  
ATOM    237  CG  GLN A  36       8.997  29.855  64.505  1.00125.95           C  
ANISOU  237  CG  GLN A  36    14055  22493  11307   1002   -470  -1271       C  
ATOM    238  CD  GLN A  36       8.178  30.995  63.932  1.00139.74           C  
ANISOU  238  CD  GLN A  36    15896  24062  13136    966   -458  -1432       C  
ATOM    239  OE1 GLN A  36       7.061  31.272  64.383  1.00135.92           O  
ANISOU  239  OE1 GLN A  36    15426  23664  12552   1049   -418  -1426       O  
ATOM    240  NE2 GLN A  36       8.722  31.703  62.950  1.00126.38           N  
ANISOU  240  NE2 GLN A  36    14268  22130  11619    847   -494  -1579       N  
ATOM    241  N   LYS A  37      11.059  30.733  68.544  1.00128.40           N  
ANISOU  241  N   LYS A  37    14106  23665  11017   1325   -771  -1707       N  
ATOM    242  CA  LYS A  37      12.374  30.981  67.938  1.00127.26           C  
ANISOU  242  CA  LYS A  37    13955  23357  11041   1199   -836  -1811       C  
ATOM    243  C   LYS A  37      13.220  29.708  67.942  1.00129.16           C  
ANISOU  243  C   LYS A  37    14121  23664  11291   1197   -830  -1603       C  
ATOM    244  O   LYS A  37      14.020  29.516  67.030  1.00128.07           O  
ANISOU  244  O   LYS A  37    13986  23343  11332   1081   -837  -1597       O  
ATOM    245  CB  LYS A  37      13.110  32.113  68.672  1.00131.57           C  
ANISOU  245  CB  LYS A  37    14470  24004  11514   1215   -967  -2115       C  
ATOM    246  N   GLY A  38      13.008  28.847  68.945  1.00124.60           N  
ANISOU  246  N   GLY A  38    13478  23344  10520   1328   -815  -1432       N  
ATOM    247  CA  GLY A  38      13.702  27.574  69.137  1.00123.32           C  
ANISOU  247  CA  GLY A  38    13250  23273  10334   1361   -815  -1219       C  
ATOM    248  C   GLY A  38      13.716  26.616  67.955  1.00122.39           C  
ANISOU  248  C   GLY A  38    13179  22905  10418   1264   -737  -1006       C  
ATOM    249  O   GLY A  38      14.585  25.741  67.893  1.00122.49           O  
ANISOU  249  O   GLY A  38    13144  22932  10464   1268   -761   -897       O  
ATOM    250  N   LYS A  39      12.760  26.769  67.006  1.00114.19           N  
ANISOU  250  N   LYS A  39    12234  21642   9511   1186   -649   -953       N  
ATOM    251  CA  LYS A  39      12.650  25.954  65.791  1.00110.84           C  
ANISOU  251  CA  LYS A  39    11867  20964   9282   1091   -573   -770       C  
ATOM    252  C   LYS A  39      13.749  26.345  64.783  1.00110.50           C  
ANISOU  252  C   LYS A  39    11834  20714   9438    968   -610   -901       C  
ATOM    253  O   LYS A  39      14.008  27.539  64.611  1.00111.78           O  
ANISOU  253  O   LYS A  39    12010  20817   9645    908   -656  -1137       O  
ATOM    254  CB  LYS A  39      11.255  26.122  65.157  1.00111.94           C  
ANISOU  254  CB  LYS A  39    12096  20949   9488   1049   -479   -704       C  
ATOM    255  N   THR A  40      14.435  25.350  64.169  1.00100.51           N  
ANISOU  255  N   THR A  40    10556  19352   8282    937   -595   -752       N  
ATOM    256  CA  THR A  40      15.492  25.596  63.173  1.00 96.46           C  
ANISOU  256  CA  THR A  40    10038  18662   7950    825   -618   -851       C  
ATOM    257  C   THR A  40      15.379  24.607  62.022  1.00 92.81           C  
ANISOU  257  C   THR A  40     9631  17981   7650    771   -542   -658       C  
ATOM    258  O   THR A  40      14.954  23.468  62.221  1.00 93.04           O  
ANISOU  258  O   THR A  40     9671  18046   7636    841   -506   -435       O  
ATOM    259  CB  THR A  40      16.934  25.559  63.749  1.00100.17           C  
ANISOU  259  CB  THR A  40    10392  19304   8365    861   -715   -941       C  
ATOM    260  OG1 THR A  40      17.360  24.208  63.943  1.00 95.30           O  
ANISOU  260  OG1 THR A  40     9733  18763   7715    946   -713   -729       O  
ATOM    261  CG2 THR A  40      17.124  26.400  65.003  1.00101.22           C  
ANISOU  261  CG2 THR A  40    10459  19684   8316    931   -804  -1126       C  
ATOM    262  N   PHE A  41      15.785  25.029  60.830  1.00 82.70           N  
ANISOU  262  N   PHE A  41     8389  16479   6554    646   -523   -743       N  
ATOM    263  CA  PHE A  41      15.738  24.162  59.663  1.00 79.22           C  
ANISOU  263  CA  PHE A  41     8003  15828   6269    595   -457   -587       C  
ATOM    264  C   PHE A  41      16.986  24.360  58.817  1.00 83.37           C  
ANISOU  264  C   PHE A  41     8490  16255   6932    509   -480   -688       C  
ATOM    265  O   PHE A  41      17.679  25.377  58.943  1.00 82.49           O  
ANISOU  265  O   PHE A  41     8330  16186   6825    450   -534   -889       O  
ATOM    266  CB  PHE A  41      14.456  24.400  58.845  1.00 77.91           C  
ANISOU  266  CB  PHE A  41     7952  15461   6191    528   -374   -543       C  
ATOM    267  CG  PHE A  41      14.327  25.760  58.205  1.00 77.16           C  
ANISOU  267  CG  PHE A  41     7907  15225   6185    418   -372   -745       C  
ATOM    268  CD1 PHE A  41      13.911  26.861  58.946  1.00 79.92           C  
ANISOU  268  CD1 PHE A  41     8259  15672   6435    437   -408   -906       C  
ATOM    269  CD2 PHE A  41      14.589  25.935  56.852  1.00 76.96           C  
ANISOU  269  CD2 PHE A  41     7935  14967   6340    301   -334   -770       C  
ATOM    270  CE1 PHE A  41      13.788  28.115  58.352  1.00 80.00           C  
ANISOU  270  CE1 PHE A  41     8331  15532   6535    338   -414  -1088       C  
ATOM    271  CE2 PHE A  41      14.456  27.189  56.256  1.00 78.97           C  
ANISOU  271  CE2 PHE A  41     8246  15083   6677    196   -333   -941       C  
ATOM    272  CZ  PHE A  41      14.054  28.269  57.009  1.00 77.79           C  
ANISOU  272  CZ  PHE A  41     8106  15014   6437    215   -375  -1096       C  
ATOM    273  N   LEU A  42      17.273  23.381  57.962  1.00 80.37           N  
ANISOU  273  N   LEU A  42     8128  15747   6662    501   -441   -549       N  
ATOM    274  CA  LEU A  42      18.440  23.461  57.098  1.00 80.44           C  
ANISOU  274  CA  LEU A  42     8091  15675   6797    427   -451   -629       C  
ATOM    275  C   LEU A  42      18.024  23.924  55.725  1.00 83.18           C  
ANISOU  275  C   LEU A  42     8532  15765   7307    298   -381   -659       C  
ATOM    276  O   LEU A  42      17.009  23.457  55.203  1.00 83.74           O  
ANISOU  276  O   LEU A  42     8700  15695   7423    297   -316   -531       O  
ATOM    277  CB  LEU A  42      19.184  22.106  57.011  1.00 80.99           C  
ANISOU  277  CB  LEU A  42     8112  15783   6879    517   -463   -480       C  
ATOM    278  CG  LEU A  42      19.685  21.436  58.318  1.00 86.79           C  
ANISOU  278  CG  LEU A  42     8756  16769   7451    665   -535   -412       C  
ATOM    279  CD1 LEU A  42      20.425  20.144  58.009  1.00 87.43           C  
ANISOU  279  CD1 LEU A  42     8808  16839   7574    751   -545   -269       C  
ATOM    280  CD2 LEU A  42      20.601  22.347  59.118  1.00 88.73           C  
ANISOU  280  CD2 LEU A  42     8884  17222   7608    663   -621   -610       C  
ATOM    281  N   ALA A  43      18.789  24.856  55.141  1.00 78.74           N  
ANISOU  281  N   ALA A  43     7941  15146   6832    183   -394   -825       N  
ATOM    282  CA  ALA A  43      18.552  25.362  53.783  1.00 76.71           C  
ANISOU  282  CA  ALA A  43     7766  14652   6727     52   -331   -861       C  
ATOM    283  C   ALA A  43      19.844  25.397  52.992  1.00 80.80           C  
ANISOU  283  C   ALA A  43     8209  15147   7345    -23   -334   -923       C  
ATOM    284  O   ALA A  43      20.894  25.706  53.544  1.00 82.65           O  
ANISOU  284  O   ALA A  43     8326  15541   7534    -24   -399  -1027       O  
ATOM    285  CB  ALA A  43      17.944  26.746  53.835  1.00 77.33           C  
ANISOU  285  CB  ALA A  43     7906  14668   6809    -35   -337  -1013       C  
ATOM    286  N   LEU A  44      19.769  25.106  51.699  1.00 76.59           N  
ANISOU  286  N   LEU A  44     7735  14427   6940    -87   -265   -866       N  
ATOM    287  CA  LEU A  44      20.919  25.114  50.806  1.00 75.61           C  
ANISOU  287  CA  LEU A  44     7541  14278   6909   -160   -253   -915       C  
ATOM    288  C   LEU A  44      21.485  26.517  50.676  1.00 77.60           C  
ANISOU  288  C   LEU A  44     7757  14529   7200   -309   -278  -1101       C  
ATOM    289  O   LEU A  44      20.757  27.492  50.836  1.00 77.50           O  
ANISOU  289  O   LEU A  44     7824  14440   7184   -373   -282  -1179       O  
ATOM    290  CB  LEU A  44      20.534  24.561  49.429  1.00 74.66           C  
ANISOU  290  CB  LEU A  44     7509  13954   6905   -189   -169   -813       C  
ATOM    291  CG  LEU A  44      20.143  23.084  49.378  1.00 79.04           C  
ANISOU  291  CG  LEU A  44     8098  14485   7449    -56   -149   -632       C  
ATOM    292  CD1 LEU A  44      19.496  22.753  48.062  1.00 76.75           C  
ANISOU  292  CD1 LEU A  44     7919  13974   7268    -99    -73   -555       C  
ATOM    293  CD2 LEU A  44      21.351  22.164  49.638  1.00 84.62           C  
ANISOU  293  CD2 LEU A  44     8683  15339   8129     44   -189   -601       C  
ATOM    294  N   ILE A  45      22.798  26.604  50.427  1.00 72.89           N  
ANISOU  294  N   ILE A  45     7035  14021   6637   -362   -299  -1172       N  
ATOM    295  CA  ILE A  45      23.587  27.832  50.275  1.00 72.71           C  
ANISOU  295  CA  ILE A  45     6951  14016   6661   -520   -329  -1342       C  
ATOM    296  C   ILE A  45      22.953  28.782  49.239  1.00 73.06           C  
ANISOU  296  C   ILE A  45     7123  13825   6811   -669   -270  -1377       C  
ATOM    297  O   ILE A  45      22.867  29.986  49.466  1.00 73.23           O  
ANISOU  297  O   ILE A  45     7175  13807   6844   -776   -306  -1508       O  
ATOM    298  CB  ILE A  45      25.039  27.412  49.872  1.00 76.93           C  
ANISOU  298  CB  ILE A  45     7329  14671   7231   -540   -332  -1357       C  
ATOM    299  CG1 ILE A  45      25.792  26.841  51.089  1.00 79.48           C  
ANISOU  299  CG1 ILE A  45     7509  15251   7439   -411   -418  -1371       C  
ATOM    300  CG2 ILE A  45      25.839  28.549  49.191  1.00 78.17           C  
ANISOU  300  CG2 ILE A  45     7433  14789   7479   -743   -326  -1489       C  
ATOM    301  CD1 ILE A  45      26.939  25.900  50.738  1.00 91.04           C  
ANISOU  301  CD1 ILE A  45     8841  16833   8917   -344   -411  -1319       C  
ATOM    302  N   ASN A  46      22.505  28.216  48.121  1.00 66.93           N  
ANISOU  302  N   ASN A  46     6428  12893   6110   -668   -185  -1261       N  
ATOM    303  CA  ASN A  46      21.940  28.903  46.977  1.00 66.27           C  
ANISOU  303  CA  ASN A  46     6464  12589   6126   -792   -120  -1265       C  
ATOM    304  C   ASN A  46      20.441  29.203  47.128  1.00 70.38           C  
ANISOU  304  C   ASN A  46     7140  12971   6629   -759   -107  -1233       C  
ATOM    305  O   ASN A  46      19.843  29.739  46.188  1.00 69.77           O  
ANISOU  305  O   ASN A  46     7175  12704   6628   -843    -56  -1226       O  
ATOM    306  CB  ASN A  46      22.179  28.036  45.731  1.00 71.49           C  
ANISOU  306  CB  ASN A  46     7129  13172   6860   -784    -40  -1155       C  
ATOM    307  CG  ASN A  46      21.896  26.564  45.962  1.00 98.51           C  
ANISOU  307  CG  ASN A  46    10546  16646  10237   -610    -32  -1016       C  
ATOM    308  OD1 ASN A  46      22.643  25.854  46.663  1.00 99.17           O  
ANISOU  308  OD1 ASN A  46    10514  16906  10260   -512    -78  -1004       O  
ATOM    309  ND2 ASN A  46      20.806  26.079  45.394  1.00 83.67           N  
ANISOU  309  ND2 ASN A  46     8795  14611   8386   -567     20   -908       N  
ATOM    310  N   GLN A  47      19.834  28.887  48.297  1.00 67.20           N  
ANISOU  310  N   GLN A  47     6739  12674   6119   -636   -153  -1215       N  
ATOM    311  CA  GLN A  47      18.410  29.114  48.552  1.00 65.77           C  
ANISOU  311  CA  GLN A  47     6683  12402   5904   -589   -141  -1184       C  
ATOM    312  C   GLN A  47      18.201  30.164  49.648  1.00 70.54           C  
ANISOU  312  C   GLN A  47     7286  13086   6429   -592   -215  -1327       C  
ATOM    313  O   GLN A  47      17.072  30.523  49.976  1.00 71.75           O  
ANISOU  313  O   GLN A  47     7530  13190   6541   -549   -214  -1331       O  
ATOM    314  CB  GLN A  47      17.735  27.791  48.917  1.00 66.74           C  
ANISOU  314  CB  GLN A  47     6817  12579   5964   -439   -120  -1021       C  
ATOM    315  CG  GLN A  47      17.753  26.781  47.765  1.00 81.53           C  
ANISOU  315  CG  GLN A  47     8720  14337   7922   -431    -52   -887       C  
ATOM    316  CD  GLN A  47      16.844  25.602  47.982  1.00102.35           C  
ANISOU  316  CD  GLN A  47    11403  16967  10519   -310    -30   -723       C  
ATOM    317  OE1 GLN A  47      16.760  25.017  49.075  1.00 99.00           O  
ANISOU  317  OE1 GLN A  47    10930  16692   9993   -203    -70   -670       O  
ATOM    318  NE2 GLN A  47      16.165  25.207  46.919  1.00 98.81           N  
ANISOU  318  NE2 GLN A  47    11048  16345  10150   -330     31   -635       N  
ATOM    319  N   VAL A  48      19.306  30.674  50.186  1.00 65.91           N  
ANISOU  319  N   VAL A  48     6594  12627   5823   -642   -282  -1453       N  
ATOM    320  CA  VAL A  48      19.341  31.697  51.222  1.00 64.80           C  
ANISOU  320  CA  VAL A  48     6440  12571   5611   -654   -367  -1616       C  
ATOM    321  C   VAL A  48      19.908  32.952  50.572  1.00 66.79           C  
ANISOU  321  C   VAL A  48     6716  12691   5971   -838   -384  -1755       C  
ATOM    322  O   VAL A  48      20.905  32.893  49.844  1.00 65.50           O  
ANISOU  322  O   VAL A  48     6484  12513   5890   -942   -362  -1752       O  
ATOM    323  CB  VAL A  48      20.114  31.240  52.477  1.00 67.93           C  
ANISOU  323  CB  VAL A  48     6694  13231   5885   -558   -444  -1650       C  
ATOM    324  CG1 VAL A  48      20.043  32.287  53.594  1.00 68.40           C  
ANISOU  324  CG1 VAL A  48     6749  13384   5857   -554   -537  -1827       C  
ATOM    325  CG2 VAL A  48      19.577  29.900  52.967  1.00 66.67           C  
ANISOU  325  CG2 VAL A  48     6522  13175   5634   -388   -416  -1477       C  
ATOM    326  N   PHE A  49      19.197  34.068  50.768  1.00 61.60           N  
ANISOU  326  N   PHE A  49     6165  11924   5315   -875   -416  -1866       N  
ATOM    327  CA  PHE A  49      19.475  35.331  50.119  1.00 60.06           C  
ANISOU  327  CA  PHE A  49     6034  11556   5229  -1048   -432  -1984       C  
ATOM    328  C   PHE A  49      19.508  36.451  51.096  1.00 65.93           C  
ANISOU  328  C   PHE A  49     6791  12335   5925  -1069   -537  -2176       C  
ATOM    329  O   PHE A  49      18.778  36.401  52.088  1.00 68.55           O  
ANISOU  329  O   PHE A  49     7143  12763   6139   -930   -576  -2209       O  
ATOM    330  CB  PHE A  49      18.377  35.601  49.074  1.00 59.37           C  
ANISOU  330  CB  PHE A  49     6111  11227   5219  -1073   -358  -1910       C  
ATOM    331  CG  PHE A  49      18.326  34.590  47.952  1.00 58.37           C  
ANISOU  331  CG  PHE A  49     5987  11038   5153  -1068   -257  -1734       C  
ATOM    332  CD1 PHE A  49      19.132  34.731  46.830  1.00 59.39           C  
ANISOU  332  CD1 PHE A  49     6097  11078   5391  -1211   -212  -1712       C  
ATOM    333  CD2 PHE A  49      17.482  33.488  48.025  1.00 57.48           C  
ANISOU  333  CD2 PHE A  49     5894  10963   4984   -923   -209  -1591       C  
ATOM    334  CE1 PHE A  49      19.100  33.784  45.806  1.00 58.13           C  
ANISOU  334  CE1 PHE A  49     5939  10872   5278  -1193   -123  -1562       C  
ATOM    335  CE2 PHE A  49      17.456  32.540  47.004  1.00 57.59           C  
ANISOU  335  CE2 PHE A  49     5915  10913   5055   -916   -126  -1441       C  
ATOM    336  CZ  PHE A  49      18.257  32.699  45.897  1.00 55.28           C  
ANISOU  336  CZ  PHE A  49     5606  10534   4865  -1044    -85  -1434       C  
ATOM    337  N   PRO A  50      20.322  37.502  50.857  1.00 62.41           N  
ANISOU  337  N   PRO A  50     6337  11814   5564  -1241   -589  -2311       N  
ATOM    338  CA  PRO A  50      20.284  38.655  51.780  1.00 62.29           C  
ANISOU  338  CA  PRO A  50     6354  11802   5510  -1263   -701  -2513       C  
ATOM    339  C   PRO A  50      18.957  39.400  51.616  1.00 65.91           C  
ANISOU  339  C   PRO A  50     7001  12062   5981  -1222   -695  -2544       C  
ATOM    340  O   PRO A  50      18.385  39.414  50.529  1.00 65.30           O  
ANISOU  340  O   PRO A  50     7028  11794   5990  -1261   -614  -2440       O  
ATOM    341  CB  PRO A  50      21.487  39.504  51.360  1.00 65.02           C  
ANISOU  341  CB  PRO A  50     6649  12087   5968  -1482   -747  -2620       C  
ATOM    342  CG  PRO A  50      21.852  39.063  49.995  1.00 68.14           C  
ANISOU  342  CG  PRO A  50     7034  12380   6475  -1586   -641  -2472       C  
ATOM    343  CD  PRO A  50      21.226  37.739  49.704  1.00 62.61           C  
ANISOU  343  CD  PRO A  50     6333  11732   5724  -1429   -546  -2284       C  
ATOM    344  N   ALA A  51      18.441  39.939  52.699  1.00 65.05           N  
ANISOU  344  N   ALA A  51     6926  12017   5773  -1124   -778  -2681       N  
ATOM    345  CA  ALA A  51      17.171  40.663  52.759  1.00 64.72           C  
ANISOU  345  CA  ALA A  51     7047  11828   5716  -1049   -787  -2736       C  
ATOM    346  C   ALA A  51      17.409  42.126  52.941  1.00 71.94           C  
ANISOU  346  C   ALA A  51     8046  12599   6690  -1159   -891  -2946       C  
ATOM    347  O   ALA A  51      18.401  42.511  53.570  1.00 75.10           O  
ANISOU  347  O   ALA A  51     8358  13094   7082  -1237   -982  -3083       O  
ATOM    348  CB  ALA A  51      16.337  40.142  53.926  1.00 64.80           C  
ANISOU  348  CB  ALA A  51     7031  12042   5550   -831   -803  -2736       C  
ATOM    349  N   GLU A  52      16.473  42.945  52.456  1.00 67.40           N  
ANISOU  349  N   GLU A  52     7643  11797   6168  -1155   -888  -2980       N  
ATOM    350  CA  GLU A  52      16.498  44.392  52.651  1.00 69.24           C  
ANISOU  350  CA  GLU A  52     7991  11858   6457  -1234   -995  -3184       C  
ATOM    351  C   GLU A  52      16.409  44.712  54.117  1.00 77.12           C  
ANISOU  351  C   GLU A  52     8951  13038   7313  -1105  -1107  -3371       C  
ATOM    352  O   GLU A  52      15.697  44.031  54.861  1.00 77.22           O  
ANISOU  352  O   GLU A  52     8922  13241   7176   -907  -1085  -3332       O  
ATOM    353  CB  GLU A  52      15.339  45.069  51.915  1.00 69.83           C  
ANISOU  353  CB  GLU A  52     8263  11674   6596  -1206   -966  -3167       C  
ATOM    354  CG  GLU A  52      15.445  44.949  50.407  1.00 74.72           C  
ANISOU  354  CG  GLU A  52     8939  12089   7361  -1351   -869  -3005       C  
ATOM    355  CD  GLU A  52      16.674  45.635  49.855  1.00 86.14           C  
ANISOU  355  CD  GLU A  52    10372  13414   8943  -1596   -907  -3058       C  
ATOM    356  OE1 GLU A  52      16.762  46.879  49.967  1.00 77.09           O  
ANISOU  356  OE1 GLU A  52     9336  12093   7862  -1685  -1004  -3216       O  
ATOM    357  OE2 GLU A  52      17.582  44.918  49.381  1.00 79.95           O  
ANISOU  357  OE2 GLU A  52     9459  12725   8195  -1697   -848  -2948       O  
ATOM    358  N   GLU A  53      17.147  45.739  54.535  1.00 77.04           N  
ANISOU  358  N   GLU A  53     8950  12976   7347  -1222  -1228  -3570       N  
ATOM    359  CA  GLU A  53      17.205  46.253  55.902  1.00 79.51           C  
ANISOU  359  CA  GLU A  53     9237  13437   7538  -1125  -1358  -3789       C  
ATOM    360  C   GLU A  53      15.788  46.687  56.347  1.00 83.48           C  
ANISOU  360  C   GLU A  53     9878  13894   7949   -923  -1373  -3860       C  
ATOM    361  O   GLU A  53      15.284  46.198  57.360  1.00 84.06           O  
ANISOU  361  O   GLU A  53     9886  14205   7846   -725  -1377  -3876       O  
ATOM    362  CB  GLU A  53      18.255  47.404  56.006  1.00 83.44           C  
ANISOU  362  CB  GLU A  53     9750  13812   8141  -1328  -1489  -3992       C  
ATOM    363  CG  GLU A  53      18.160  48.565  54.996  1.00 97.74           C  
ANISOU  363  CG  GLU A  53    11743  15257  10137  -1501  -1509  -4033       C  
ATOM    364  CD  GLU A  53      17.819  48.288  53.532  1.00111.33           C  
ANISOU  364  CD  GLU A  53    13541  16776  11982  -1584  -1374  -3815       C  
ATOM    365  OE1 GLU A  53      18.722  47.885  52.759  1.00 96.94           O  
ANISOU  365  OE1 GLU A  53    11629  14950  10254  -1755  -1312  -3692       O  
ATOM    366  OE2 GLU A  53      16.632  48.464  53.166  1.00 91.09           O  
ANISOU  366  OE2 GLU A  53    11124  14073   9414  -1467  -1332  -3770       O  
ATOM    367  N   ASP A  54      15.126  47.522  55.535  1.00 79.12           N  
ANISOU  367  N   ASP A  54     9505  13046   7509   -968  -1368  -3877       N  
ATOM    368  CA  ASP A  54      13.774  48.014  55.763  1.00 78.77           C  
ANISOU  368  CA  ASP A  54     9601  12926   7401   -786  -1378  -3940       C  
ATOM    369  C   ASP A  54      12.801  47.096  55.004  1.00 79.47           C  
ANISOU  369  C   ASP A  54     9702  13015   7479   -694  -1229  -3701       C  
ATOM    370  O   ASP A  54      12.760  47.116  53.769  1.00 77.10           O  
ANISOU  370  O   ASP A  54     9473  12502   7317   -814  -1157  -3569       O  
ATOM    371  CB  ASP A  54      13.692  49.485  55.298  1.00 82.25           C  
ANISOU  371  CB  ASP A  54    10237  13034   7980   -890  -1469  -4099       C  
ATOM    372  CG  ASP A  54      12.386  50.231  55.519  1.00 89.32           C  
ANISOU  372  CG  ASP A  54    11295  13818   8824   -704  -1507  -4207       C  
ATOM    373  OD1 ASP A  54      11.315  49.578  55.518  1.00 87.90           O  
ANISOU  373  OD1 ASP A  54    11104  13752   8542   -521  -1418  -4091       O  
ATOM    374  OD2 ASP A  54      12.422  51.480  55.569  1.00 94.05           O  
ANISOU  374  OD2 ASP A  54    12042  14194   9500   -753  -1621  -4395       O  
ATOM    375  N   SER A  55      12.063  46.251  55.758  1.00 75.61           N  
ANISOU  375  N   SER A  55     9133  12776   6818   -487  -1183  -3640       N  
ATOM    376  CA  SER A  55      11.094  45.284  55.224  1.00 73.05           C  
ANISOU  376  CA  SER A  55     8800  12494   6461   -386  -1051  -3420       C  
ATOM    377  C   SER A  55       9.723  45.928  54.988  1.00 76.91           C  
ANISOU  377  C   SER A  55     9441  12842   6941   -258  -1045  -3458       C  
ATOM    378  O   SER A  55       8.856  45.319  54.359  1.00 73.78           O  
ANISOU  378  O   SER A  55     9060  12428   6546   -196   -942  -3287       O  
ATOM    379  CB  SER A  55      10.953  44.093  56.161  1.00 75.39           C  
ANISOU  379  CB  SER A  55     8937  13127   6581   -239  -1009  -3327       C  
ATOM    380  OG  SER A  55      10.640  44.528  57.471  1.00 86.41           O  
ANISOU  380  OG  SER A  55    10316  14700   7815    -81  -1096  -3507       O  
ATOM    381  N   LYS A  56       9.527  47.158  55.487  1.00 76.85           N  
ANISOU  381  N   LYS A  56     9541  12734   6923   -212  -1159  -3688       N  
ATOM    382  CA  LYS A  56       8.268  47.884  55.290  1.00 76.96           C  
ANISOU  382  CA  LYS A  56     9705  12607   6930    -77  -1168  -3748       C  
ATOM    383  C   LYS A  56       8.240  48.604  53.921  1.00 79.40           C  
ANISOU  383  C   LYS A  56    10180  12553   7438   -226  -1159  -3710       C  
ATOM    384  O   LYS A  56       7.202  48.592  53.256  1.00 78.72           O  
ANISOU  384  O   LYS A  56    10178  12361   7370   -147  -1098  -3620       O  
ATOM    385  CB  LYS A  56       8.022  48.884  56.434  1.00 81.23           C  
ANISOU  385  CB  LYS A  56    10299  13203   7363     66  -1299  -4019       C  
ATOM    386  CG  LYS A  56       7.447  48.248  57.698  1.00103.44           C  
ANISOU  386  CG  LYS A  56    12983  16376   9945    287  -1286  -4039       C  
ATOM    387  CD  LYS A  56       5.962  47.866  57.539  1.00115.39           C  
ANISOU  387  CD  LYS A  56    14519  17954  11369    482  -1201  -3944       C  
ATOM    388  CE  LYS A  56       5.395  47.172  58.756  1.00127.99           C  
ANISOU  388  CE  LYS A  56    15970  19925  12734    680  -1169  -3922       C  
ATOM    389  NZ  LYS A  56       5.172  48.115  59.884  1.00137.32           N  
ANISOU  389  NZ  LYS A  56    17178  21222  13775    844  -1287  -4189       N  
ATOM    390  N   LYS A  57       9.375  49.214  53.509  1.00 75.29           N  
ANISOU  390  N   LYS A  57     9697  11852   7058   -442  -1220  -3773       N  
ATOM    391  CA  LYS A  57       9.510  49.988  52.273  1.00 75.18           C  
ANISOU  391  CA  LYS A  57     9840  11495   7231   -606  -1223  -3743       C  
ATOM    392  C   LYS A  57       9.387  49.150  50.987  1.00 77.02           C  
ANISOU  392  C   LYS A  57    10057  11663   7545   -690  -1082  -3481       C  
ATOM    393  O   LYS A  57       9.431  47.914  50.989  1.00 76.07           O  
ANISOU  393  O   LYS A  57     9792  11749   7361   -661   -985  -3321       O  
ATOM    394  CB  LYS A  57      10.851  50.749  52.258  1.00 79.44           C  
ANISOU  394  CB  LYS A  57    10393  11901   7888   -833  -1319  -3863       C  
ATOM    395  CG  LYS A  57      12.089  49.884  51.986  1.00 96.48           C  
ANISOU  395  CG  LYS A  57    12384  14186  10089  -1013  -1259  -3733       C  
ATOM    396  CD  LYS A  57      12.776  50.239  50.667  1.00107.85           C  
ANISOU  396  CD  LYS A  57    13890  15369  11717  -1261  -1223  -3629       C  
ATOM    397  CE  LYS A  57      14.228  49.804  50.621  1.00122.42           C  
ANISOU  397  CE  LYS A  57    15577  17325  13612  -1459  -1214  -3590       C  
ATOM    398  NZ  LYS A  57      14.383  48.330  50.462  1.00128.40           N  
ANISOU  398  NZ  LYS A  57    16163  18322  14300  -1412  -1092  -3395       N  
ATOM    399  N   ASP A  58       9.251  49.863  49.880  1.00 72.53           N  
ANISOU  399  N   ASP A  58     9645  10796   7119   -795  -1077  -3445       N  
ATOM    400  CA  ASP A  58       9.212  49.300  48.551  1.00 69.93           C  
ANISOU  400  CA  ASP A  58     9328  10360   6882   -895   -961  -3223       C  
ATOM    401  C   ASP A  58       9.878  50.277  47.591  1.00 69.69           C  
ANISOU  401  C   ASP A  58     9431  10022   7024  -1112   -998  -3236       C  
ATOM    402  O   ASP A  58       9.914  51.486  47.835  1.00 70.17           O  
ANISOU  402  O   ASP A  58     9627   9898   7136  -1137  -1112  -3406       O  
ATOM    403  CB  ASP A  58       7.774  48.927  48.107  1.00 71.60           C  
ANISOU  403  CB  ASP A  58     9596  10565   7043   -718   -885  -3111       C  
ATOM    404  CG  ASP A  58       6.826  50.098  47.868  1.00 87.81           C  
ANISOU  404  CG  ASP A  58    11851  12379   9133   -630   -949  -3212       C  
ATOM    405  OD1 ASP A  58       6.872  50.691  46.756  1.00 88.11           O  
ANISOU  405  OD1 ASP A  58    12026  12148   9306   -754   -943  -3153       O  
ATOM    406  OD2 ASP A  58       5.982  50.366  48.750  1.00 96.43           O  
ANISOU  406  OD2 ASP A  58    12962  13563  10113   -426   -998  -3335       O  
ATOM    407  N   VAL A  59      10.420  49.745  46.516  1.00 62.51           N  
ANISOU  407  N   VAL A  59     8487   9063   6202  -1267   -904  -3055       N  
ATOM    408  CA  VAL A  59      11.058  50.536  45.474  1.00 62.28           C  
ANISOU  408  CA  VAL A  59     8569   8763   6330  -1487   -915  -3023       C  
ATOM    409  C   VAL A  59      10.259  50.317  44.194  1.00 63.42           C  
ANISOU  409  C   VAL A  59     8812   8766   6519  -1463   -817  -2842       C  
ATOM    410  O   VAL A  59       9.780  49.202  43.941  1.00 60.73           O  
ANISOU  410  O   VAL A  59     8381   8580   6112  -1366   -716  -2699       O  
ATOM    411  CB  VAL A  59      12.586  50.248  45.323  1.00 65.95           C  
ANISOU  411  CB  VAL A  59     8896   9303   6859  -1716   -899  -2988       C  
ATOM    412  CG1 VAL A  59      13.355  50.744  46.542  1.00 66.93           C  
ANISOU  412  CG1 VAL A  59     8955   9518   6956  -1754  -1023  -3196       C  
ATOM    413  CG2 VAL A  59      12.880  48.763  45.070  1.00 63.73           C  
ANISOU  413  CG2 VAL A  59     8430   9264   6520  -1697   -776  -2813       C  
ATOM    414  N   GLU A  60      10.075  51.386  43.406  1.00 60.21           N  
ANISOU  414  N   GLU A  60     8596   8060   6222  -1545   -855  -2850       N  
ATOM    415  CA  GLU A  60       9.321  51.335  42.139  1.00 57.19           C  
ANISOU  415  CA  GLU A  60     8326   7520   5883  -1526   -776  -2687       C  
ATOM    416  C   GLU A  60      10.046  50.494  41.111  1.00 61.78           C  
ANISOU  416  C   GLU A  60     8809   8153   6510  -1682   -656  -2489       C  
ATOM    417  O   GLU A  60       9.425  49.867  40.220  1.00 59.72           O  
ANISOU  417  O   GLU A  60     8562   7892   6239  -1627   -561  -2330       O  
ATOM    418  CB  GLU A  60       9.073  52.751  41.606  1.00 59.39           C  
ANISOU  418  CB  GLU A  60     8837   7460   6267  -1585   -857  -2747       C  
ATOM    419  CG  GLU A  60       8.012  53.500  42.406  1.00 65.01           C  
ANISOU  419  CG  GLU A  60     9670   8109   6923  -1371   -962  -2923       C  
ATOM    420  CD  GLU A  60       7.510  54.841  41.898  1.00 83.56           C  
ANISOU  420  CD  GLU A  60    12268  10120   9362  -1367  -1046  -2979       C  
ATOM    421  OE1 GLU A  60       8.246  55.541  41.162  1.00 80.17           O  
ANISOU  421  OE1 GLU A  60    11941   9458   9062  -1582  -1065  -2933       O  
ATOM    422  OE2 GLU A  60       6.381  55.216  42.292  1.00 70.61           O  
ANISOU  422  OE2 GLU A  60    10719   8452   7658  -1143  -1097  -3073       O  
ATOM    423  N   ASP A  61      11.369  50.480  41.230  1.00 60.36           N  
ANISOU  423  N   ASP A  61     8526   8028   6379  -1874   -665  -2507       N  
ATOM    424  CA  ASP A  61      12.252  49.718  40.340  1.00 60.14           C  
ANISOU  424  CA  ASP A  61     8385   8074   6393  -2032   -558  -2341       C  
ATOM    425  C   ASP A  61      13.088  48.804  41.219  1.00 66.16           C  
ANISOU  425  C   ASP A  61     8927   9124   7087  -2034   -548  -2375       C  
ATOM    426  O   ASP A  61      13.789  49.279  42.104  1.00 66.34           O  
ANISOU  426  O   ASP A  61     8902   9190   7116  -2102   -638  -2522       O  
ATOM    427  CB  ASP A  61      13.118  50.663  39.488  1.00 62.38           C  
ANISOU  427  CB  ASP A  61     8758   8134   6811  -2285   -573  -2312       C  
ATOM    428  CG  ASP A  61      13.905  50.012  38.372  1.00 76.95           C  
ANISOU  428  CG  ASP A  61    10511  10030   8696  -2441   -454  -2131       C  
ATOM    429  OD1 ASP A  61      14.342  48.838  38.547  1.00 75.82           O  
ANISOU  429  OD1 ASP A  61    10181  10136   8492  -2411   -386  -2075       O  
ATOM    430  OD2 ASP A  61      14.110  50.678  37.326  1.00 86.57           O  
ANISOU  430  OD2 ASP A  61    11845  11042  10005  -2593   -432  -2045       O  
ATOM    431  N   ASN A  62      13.007  47.498  40.971  1.00 63.01           N  
ANISOU  431  N   ASN A  62     8399   8916   6625  -1958   -446  -2241       N  
ATOM    432  CA  ASN A  62      13.716  46.475  41.728  1.00 63.06           C  
ANISOU  432  CA  ASN A  62     8200   9201   6559  -1933   -428  -2244       C  
ATOM    433  C   ASN A  62      15.247  46.629  41.670  1.00 72.43           C  
ANISOU  433  C   ASN A  62     9272  10438   7810  -2149   -439  -2266       C  
ATOM    434  O   ASN A  62      15.918  46.135  42.567  1.00 73.31           O  
ANISOU  434  O   ASN A  62     9225  10764   7865  -2133   -465  -2326       O  
ATOM    435  CB  ASN A  62      13.287  45.105  41.243  1.00 61.41           C  
ANISOU  435  CB  ASN A  62     7910   9129   6293  -1824   -315  -2077       C  
ATOM    436  CG  ASN A  62      11.885  44.786  41.684  1.00 68.71           C  
ANISOU  436  CG  ASN A  62     8887  10091   7129  -1602   -316  -2077       C  
ATOM    437  OD1 ASN A  62      11.618  44.566  42.870  1.00 59.81           O  
ANISOU  437  OD1 ASN A  62     7694   9124   5908  -1473   -365  -2167       O  
ATOM    438  ND2 ASN A  62      10.961  44.732  40.742  1.00 57.45           N  
ANISOU  438  ND2 ASN A  62     7569   8536   5722  -1550   -260  -1972       N  
ATOM    439  N   CYS A  63      15.796  47.355  40.669  1.00 72.16           N  
ANISOU  439  N   CYS A  63     9313  10213   7890  -2351   -424  -2221       N  
ATOM    440  CA  CYS A  63      17.228  47.657  40.566  1.00 74.44           C  
ANISOU  440  CA  CYS A  63     9498  10538   8249  -2579   -438  -2245       C  
ATOM    441  C   CYS A  63      17.698  48.565  41.717  1.00 77.34           C  
ANISOU  441  C   CYS A  63     9861  10897   8628  -2636   -578  -2452       C  
ATOM    442  O   CYS A  63      18.898  48.606  41.995  1.00 77.77           O  
ANISOU  442  O   CYS A  63     9777  11062   8710  -2788   -605  -2500       O  
ATOM    443  CB  CYS A  63      17.549  48.282  39.218  1.00 76.72           C  
ANISOU  443  CB  CYS A  63     9883  10617   8649  -2777   -386  -2135       C  
ATOM    444  SG  CYS A  63      17.316  47.154  37.830  1.00 79.78           S  
ANISOU  444  SG  CYS A  63    10233  11062   9019  -2743   -222  -1901       S  
ATOM    445  N   SER A  64      16.749  49.260  42.395  1.00 72.34           N  
ANISOU  445  N   SER A  64     9370  10149   7968  -2505   -669  -2580       N  
ATOM    446  CA  SER A  64      16.991  50.160  43.533  1.00 72.65           C  
ANISOU  446  CA  SER A  64     9433  10165   8006  -2521   -814  -2798       C  
ATOM    447  C   SER A  64      17.179  49.385  44.838  1.00 74.16           C  
ANISOU  447  C   SER A  64     9452  10658   8069  -2378   -848  -2891       C  
ATOM    448  O   SER A  64      17.534  49.985  45.858  1.00 74.14           O  
ANISOU  448  O   SER A  64     9433  10691   8047  -2387   -968  -3078       O  
ATOM    449  CB  SER A  64      15.846  51.155  43.690  1.00 76.48           C  
ANISOU  449  CB  SER A  64    10141  10418   8501  -2408   -893  -2898       C  
ATOM    450  OG  SER A  64      15.533  51.796  42.465  1.00 90.96           O  
ANISOU  450  OG  SER A  64    12148  11976  10437  -2499   -856  -2792       O  
ATOM    451  N   LEU A  65      16.934  48.058  44.819  1.00 67.77           N  
ANISOU  451  N   LEU A  65     8520  10062   7169  -2242   -748  -2761       N  
ATOM    452  CA  LEU A  65      17.125  47.225  46.011  1.00 66.31           C  
ANISOU  452  CA  LEU A  65     8169  10170   6855  -2103   -772  -2819       C  
ATOM    453  C   LEU A  65      18.619  47.162  46.402  1.00 71.77           C  
ANISOU  453  C   LEU A  65     8686  11014   7568  -2265   -814  -2882       C  
ATOM    454  O   LEU A  65      19.494  47.256  45.524  1.00 71.52           O  
ANISOU  454  O   LEU A  65     8613  10925   7637  -2465   -769  -2805       O  
ATOM    455  CB  LEU A  65      16.570  45.806  45.755  1.00 63.19           C  
ANISOU  455  CB  LEU A  65     7695   9936   6376  -1944   -653  -2643       C  
ATOM    456  CG  LEU A  65      15.035  45.659  45.690  1.00 65.47           C  
ANISOU  456  CG  LEU A  65     8110  10159   6607  -1744   -622  -2597       C  
ATOM    457  CD1 LEU A  65      14.643  44.272  45.237  1.00 63.16           C  
ANISOU  457  CD1 LEU A  65     7740   9997   6262  -1640   -504  -2408       C  
ATOM    458  CD2 LEU A  65      14.380  45.942  47.036  1.00 68.90           C  
ANISOU  458  CD2 LEU A  65     8559  10692   6928  -1570   -714  -2755       C  
ATOM    459  N   MET A  66      18.913  47.010  47.706  1.00 69.74           N  
ANISOU  459  N   MET A  66     8322  10964   7213  -2177   -899  -3019       N  
ATOM    460  CA  MET A  66      20.296  46.867  48.183  1.00 71.49           C  
ANISOU  460  CA  MET A  66     8359  11368   7437  -2305   -946  -3086       C  
ATOM    461  C   MET A  66      20.847  45.533  47.677  1.00 73.10           C  
ANISOU  461  C   MET A  66     8396  11761   7617  -2297   -828  -2905       C  
ATOM    462  O   MET A  66      21.987  45.445  47.222  1.00 73.29           O  
ANISOU  462  O   MET A  66     8305  11834   7710  -2471   -806  -2869       O  
ATOM    463  CB  MET A  66      20.379  46.953  49.712  1.00 75.89           C  
ANISOU  463  CB  MET A  66     8845  12116   7873  -2182  -1064  -3271       C  
ATOM    464  CG  MET A  66      21.798  47.151  50.201  1.00 83.07           C  
ANISOU  464  CG  MET A  66     9595  13163   8806  -2342  -1146  -3383       C  
ATOM    465  SD  MET A  66      22.016  46.976  51.984  1.00 90.49           S  
ANISOU  465  SD  MET A  66    10409  14394   9578  -2183  -1274  -3574       S  
ATOM    466  CE  MET A  66      23.773  47.397  52.117  1.00 89.79           C  
ANISOU  466  CE  MET A  66    10148  14398   9572  -2445  -1359  -3683       C  
ATOM    467  N   TYR A  67      19.999  44.505  47.722  1.00 67.34           N  
ANISOU  467  N   TYR A  67     7661  11131   6795  -2093   -753  -2787       N  
ATOM    468  CA  TYR A  67      20.289  43.175  47.218  1.00 65.38           C  
ANISOU  468  CA  TYR A  67     7289  11034   6519  -2046   -642  -2610       C  
ATOM    469  C   TYR A  67      19.240  42.832  46.215  1.00 68.43           C  
ANISOU  469  C   TYR A  67     7802  11267   6931  -1979   -540  -2456       C  
ATOM    470  O   TYR A  67      18.056  42.825  46.537  1.00 67.42           O  
ANISOU  470  O   TYR A  67     7777  11096   6743  -1822   -544  -2459       O  
ATOM    471  CB  TYR A  67      20.319  42.154  48.362  1.00 66.13           C  
ANISOU  471  CB  TYR A  67     7246  11411   6469  -1859   -663  -2616       C  
ATOM    472  CG  TYR A  67      21.198  42.590  49.514  1.00 66.55           C  
ANISOU  472  CG  TYR A  67     7187  11624   6475  -1896   -784  -2793       C  
ATOM    473  CD1 TYR A  67      22.584  42.570  49.404  1.00 68.74           C  
ANISOU  473  CD1 TYR A  67     7309  12008   6801  -2052   -803  -2818       C  
ATOM    474  CD2 TYR A  67      20.642  43.068  50.694  1.00 67.68           C  
ANISOU  474  CD2 TYR A  67     7377  11813   6524  -1779   -883  -2946       C  
ATOM    475  CE1 TYR A  67      23.397  43.011  50.441  1.00 71.20           C  
ANISOU  475  CE1 TYR A  67     7514  12465   7072  -2096   -922  -2990       C  
ATOM    476  CE2 TYR A  67      21.446  43.488  51.752  1.00 70.45           C  
ANISOU  476  CE2 TYR A  67     7628  12312   6827  -1811  -1003  -3122       C  
ATOM    477  CZ  TYR A  67      22.824  43.455  51.622  1.00 77.62           C  
ANISOU  477  CZ  TYR A  67     8382  13321   7789  -1974  -1025  -3143       C  
ATOM    478  OH  TYR A  67      23.631  43.866  52.651  1.00 81.36           O  
ANISOU  478  OH  TYR A  67     8749  13947   8217  -2013  -1149  -3321       O  
ATOM    479  N   LEU A  68      19.649  42.630  44.975  1.00 65.92           N  
ANISOU  479  N   LEU A  68     7481  10864   6702  -2103   -451  -2330       N  
ATOM    480  CA  LEU A  68      18.691  42.282  43.958  1.00 63.51           C  
ANISOU  480  CA  LEU A  68     7293  10420   6419  -2042   -356  -2185       C  
ATOM    481  C   LEU A  68      18.788  40.799  43.729  1.00 66.28           C  
ANISOU  481  C   LEU A  68     7526  10943   6716  -1937   -268  -2039       C  
ATOM    482  O   LEU A  68      19.787  40.322  43.204  1.00 68.23           O  
ANISOU  482  O   LEU A  68     7653  11275   6995  -2029   -222  -1980       O  
ATOM    483  CB  LEU A  68      18.908  43.099  42.683  1.00 63.82           C  
ANISOU  483  CB  LEU A  68     7438  10227   6583  -2230   -317  -2138       C  
ATOM    484  CG  LEU A  68      18.012  42.746  41.504  1.00 67.57           C  
ANISOU  484  CG  LEU A  68     8029  10565   7081  -2178   -218  -1983       C  
ATOM    485  CD1 LEU A  68      16.526  42.942  41.831  1.00 66.89           C  
ANISOU  485  CD1 LEU A  68     8090  10381   6946  -2006   -242  -2003       C  
ATOM    486  CD2 LEU A  68      18.427  43.518  40.273  1.00 69.79           C  
ANISOU  486  CD2 LEU A  68     8390  10652   7474  -2377   -178  -1928       C  
ATOM    487  N   ASN A  69      17.779  40.065  44.200  1.00 59.94           N  
ANISOU  487  N   ASN A  69     6746  10202   5825  -1742   -252  -1989       N  
ATOM    488  CA  ASN A  69      17.697  38.618  44.077  1.00 57.22           C  
ANISOU  488  CA  ASN A  69     6313  10003   5426  -1621   -180  -1850       C  
ATOM    489  C   ASN A  69      16.210  38.216  44.076  1.00 60.54           C  
ANISOU  489  C   ASN A  69     6842  10364   5797  -1460   -148  -1776       C  
ATOM    490  O   ASN A  69      15.340  39.064  44.310  1.00 59.81           O  
ANISOU  490  O   ASN A  69     6873  10153   5700  -1431   -188  -1848       O  
ATOM    491  CB  ASN A  69      18.515  37.927  45.194  1.00 53.16           C  
ANISOU  491  CB  ASN A  69     5624   9748   4826  -1555   -227  -1892       C  
ATOM    492  CG  ASN A  69      17.953  38.108  46.562  1.00 64.82           C  
ANISOU  492  CG  ASN A  69     7105  11327   6197  -1426   -308  -1992       C  
ATOM    493  OD1 ASN A  69      16.850  37.645  46.850  1.00 58.24           O  
ANISOU  493  OD1 ASN A  69     6331  10501   5298  -1277   -288  -1934       O  
ATOM    494  ND2 ASN A  69      18.703  38.733  47.455  1.00 59.50           N  
ANISOU  494  ND2 ASN A  69     6358  10753   5497  -1475   -402  -2142       N  
ATOM    495  N   GLU A  70      15.922  36.939  43.782  1.00 55.79           N  
ANISOU  495  N   GLU A  70     6195   9839   5161  -1359    -79  -1634       N  
ATOM    496  CA  GLU A  70      14.561  36.438  43.662  1.00 55.03           C  
ANISOU  496  CA  GLU A  70     6186   9695   5028  -1225    -41  -1544       C  
ATOM    497  C   GLU A  70      13.754  36.621  44.947  1.00 58.70           C  
ANISOU  497  C   GLU A  70     6661  10252   5389  -1092   -103  -1618       C  
ATOM    498  O   GLU A  70      12.550  36.854  44.844  1.00 60.37           O  
ANISOU  498  O   GLU A  70     6978  10376   5586  -1019    -92  -1601       O  
ATOM    499  CB  GLU A  70      14.535  34.963  43.199  1.00 55.08           C  
ANISOU  499  CB  GLU A  70     6129   9775   5021  -1152     32  -1385       C  
ATOM    500  CG  GLU A  70      15.237  34.006  44.149  1.00 64.76           C  
ANISOU  500  CG  GLU A  70     7206  11227   6173  -1076      7  -1371       C  
ATOM    501  CD  GLU A  70      15.712  32.721  43.511  1.00 81.10           C  
ANISOU  501  CD  GLU A  70     9205  13347   8264  -1052     68  -1240       C  
ATOM    502  OE1 GLU A  70      16.801  32.738  42.895  1.00 92.24           O  
ANISOU  502  OE1 GLU A  70    10552  14765   9731  -1151     88  -1250       O  
ATOM    503  OE2 GLU A  70      15.035  31.684  43.688  1.00 62.65           O  
ANISOU  503  OE2 GLU A  70     6869  11053   5883   -932     92  -1132       O  
ATOM    504  N   ALA A  71      14.387  36.514  46.135  1.00 53.32           N  
ANISOU  504  N   ALA A  71     5869   9760   4631  -1054   -166  -1697       N  
ATOM    505  CA  ALA A  71      13.686  36.676  47.401  1.00 52.52           C  
ANISOU  505  CA  ALA A  71     5766   9776   4414   -922   -224  -1771       C  
ATOM    506  C   ALA A  71      13.389  38.136  47.710  1.00 57.58           C  
ANISOU  506  C   ALA A  71     6506  10303   5067   -958   -296  -1942       C  
ATOM    507  O   ALA A  71      12.339  38.426  48.300  1.00 57.41           O  
ANISOU  507  O   ALA A  71     6546  10294   4971   -840   -320  -1985       O  
ATOM    508  CB  ALA A  71      14.482  36.062  48.523  1.00 53.93           C  
ANISOU  508  CB  ALA A  71     5795  10198   4499   -866   -269  -1796       C  
ATOM    509  N   THR A  72      14.288  39.062  47.316  1.00 56.40           N  
ANISOU  509  N   THR A  72     6376  10045   5010  -1119   -335  -2040       N  
ATOM    510  CA  THR A  72      14.063  40.498  47.573  1.00 58.88           C  
ANISOU  510  CA  THR A  72     6801  10221   5349  -1163   -416  -2209       C  
ATOM    511  C   THR A  72      13.049  41.049  46.562  1.00 63.55           C  
ANISOU  511  C   THR A  72     7562  10571   6014  -1173   -375  -2163       C  
ATOM    512  O   THR A  72      12.227  41.889  46.924  1.00 65.02           O  
ANISOU  512  O   THR A  72     7856  10672   6177  -1104   -426  -2263       O  
ATOM    513  CB  THR A  72      15.353  41.316  47.585  1.00 59.19           C  
ANISOU  513  CB  THR A  72     6803  10225   5461  -1340   -482  -2333       C  
ATOM    514  OG1 THR A  72      16.089  41.035  46.398  1.00 61.28           O  
ANISOU  514  OG1 THR A  72     7044  10406   5833  -1489   -411  -2224       O  
ATOM    515  CG2 THR A  72      16.180  41.055  48.805  1.00 58.69           C  
ANISOU  515  CG2 THR A  72     6588  10402   5309  -1308   -552  -2425       C  
ATOM    516  N   LEU A  73      13.097  40.568  45.324  1.00 58.73           N  
ANISOU  516  N   LEU A  73     6972   9861   5484  -1244   -287  -2018       N  
ATOM    517  CA  LEU A  73      12.136  40.936  44.287  1.00 58.81           C  
ANISOU  517  CA  LEU A  73     7133   9660   5554  -1243   -243  -1953       C  
ATOM    518  C   LEU A  73      10.719  40.488  44.708  1.00 59.95           C  
ANISOU  518  C   LEU A  73     7312   9862   5606  -1050   -226  -1912       C  
ATOM    519  O   LEU A  73       9.791  41.285  44.655  1.00 61.42           O  
ANISOU  519  O   LEU A  73     7621   9922   5793   -996   -254  -1970       O  
ATOM    520  CB  LEU A  73      12.542  40.300  42.945  1.00 58.57           C  
ANISOU  520  CB  LEU A  73     7094   9557   5605  -1340   -148  -1798       C  
ATOM    521  CG  LEU A  73      11.455  40.177  41.882  1.00 63.77           C  
ANISOU  521  CG  LEU A  73     7872  10062   6294  -1297    -84  -1688       C  
ATOM    522  CD1 LEU A  73      11.298  41.451  41.145  1.00 65.40           C  
ANISOU  522  CD1 LEU A  73     8233  10030   6587  -1397   -108  -1737       C  
ATOM    523  CD2 LEU A  73      11.809  39.111  40.882  1.00 69.14           C  
ANISOU  523  CD2 LEU A  73     8499  10764   7007  -1332      8  -1531       C  
ATOM    524  N   LEU A  74      10.577  39.222  45.139  1.00 53.41           N  
ANISOU  524  N   LEU A  74     6370   9225   4698   -950   -183  -1811       N  
ATOM    525  CA  LEU A  74       9.317  38.630  45.587  1.00 52.09           C  
ANISOU  525  CA  LEU A  74     6207   9147   4439   -783   -159  -1749       C  
ATOM    526  C   LEU A  74       8.695  39.445  46.725  1.00 54.79           C  
ANISOU  526  C   LEU A  74     6580   9548   4690   -673   -237  -1900       C  
ATOM    527  O   LEU A  74       7.503  39.718  46.683  1.00 56.13           O  
ANISOU  527  O   LEU A  74     6829   9669   4830   -574   -231  -1901       O  
ATOM    528  CB  LEU A  74       9.530  37.176  46.042  1.00 51.22           C  
ANISOU  528  CB  LEU A  74     5959   9244   4259   -716   -118  -1625       C  
ATOM    529  CG  LEU A  74       8.285  36.383  46.409  1.00 54.29           C  
ANISOU  529  CG  LEU A  74     6336   9732   4561   -568    -81  -1526       C  
ATOM    530  CD1 LEU A  74       7.468  36.013  45.167  1.00 52.82           C  
ANISOU  530  CD1 LEU A  74     6228   9396   4443   -578    -10  -1397       C  
ATOM    531  CD2 LEU A  74       8.653  35.171  47.227  1.00 55.03           C  
ANISOU  531  CD2 LEU A  74     6293  10047   4568   -502    -71  -1441       C  
ATOM    532  N   HIS A  75       9.484  39.831  47.721  1.00 50.84           N  
ANISOU  532  N   HIS A  75     6014   9161   4141   -685   -311  -2031       N  
ATOM    533  CA  HIS A  75       9.021  40.636  48.846  1.00 50.04           C  
ANISOU  533  CA  HIS A  75     5938   9128   3947   -580   -394  -2197       C  
ATOM    534  C   HIS A  75       8.574  42.017  48.374  1.00 58.16           C  
ANISOU  534  C   HIS A  75     7131   9916   5050   -613   -443  -2318       C  
ATOM    535  O   HIS A  75       7.488  42.447  48.723  1.00 58.41           O  
ANISOU  535  O   HIS A  75     7231   9943   5021   -480   -463  -2375       O  
ATOM    536  CB  HIS A  75      10.111  40.776  49.903  1.00 51.20           C  
ANISOU  536  CB  HIS A  75     5982   9431   4040   -608   -471  -2320       C  
ATOM    537  CG  HIS A  75       9.744  41.718  51.021  1.00 55.26           C  
ANISOU  537  CG  HIS A  75     6531  10001   4463   -510   -569  -2519       C  
ATOM    538  ND1 HIS A  75       8.829  41.363  51.992  1.00 56.73           N  
ANISOU  538  ND1 HIS A  75     6679  10381   4497   -323   -569  -2525       N  
ATOM    539  CD2 HIS A  75      10.145  42.995  51.248  1.00 58.23           C  
ANISOU  539  CD2 HIS A  75     6986  10255   4883   -576   -667  -2714       C  
ATOM    540  CE1 HIS A  75       8.741  42.408  52.806  1.00 57.86           C  
ANISOU  540  CE1 HIS A  75     6869  10529   4585   -268   -668  -2732       C  
ATOM    541  NE2 HIS A  75       9.512  43.416  52.396  1.00 59.01           N  
ANISOU  541  NE2 HIS A  75     7091  10478   4850   -416   -734  -2855       N  
ATOM    542  N   ASN A  76       9.420  42.711  47.605  1.00 59.16           N  
ANISOU  542  N   ASN A  76     7320   9853   5306   -786   -463  -2355       N  
ATOM    543  CA  ASN A  76       9.155  44.041  47.063  1.00 60.46           C  
ANISOU  543  CA  ASN A  76     7653   9759   5560   -844   -514  -2455       C  
ATOM    544  C   ASN A  76       7.817  44.083  46.333  1.00 61.99           C  
ANISOU  544  C   ASN A  76     7960   9832   5762   -745   -464  -2372       C  
ATOM    545  O   ASN A  76       6.970  44.910  46.682  1.00 62.17           O  
ANISOU  545  O   ASN A  76     8082   9788   5750   -636   -520  -2484       O  
ATOM    546  CB  ASN A  76      10.284  44.489  46.110  1.00 59.49           C  
ANISOU  546  CB  ASN A  76     7562   9461   5582  -1069   -511  -2437       C  
ATOM    547  CG  ASN A  76      10.224  45.962  45.812  1.00 67.74           C  
ANISOU  547  CG  ASN A  76     8775  10249   6714  -1145   -590  -2566       C  
ATOM    548  OD1 ASN A  76      10.204  46.799  46.721  1.00 62.77           O  
ANISOU  548  OD1 ASN A  76     8183   9616   6050  -1102   -694  -2749       O  
ATOM    549  ND2 ASN A  76      10.104  46.302  44.546  1.00 50.28           N  
ANISOU  549  ND2 ASN A  76     6678   7816   4611  -1242   -547  -2474       N  
ATOM    550  N   ILE A  77       7.609  43.165  45.365  1.00 57.20           N  
ANISOU  550  N   ILE A  77     7332   9208   5192   -773   -364  -2185       N  
ATOM    551  CA  ILE A  77       6.361  43.131  44.591  1.00 55.33           C  
ANISOU  551  CA  ILE A  77     7191   8866   4965   -688   -316  -2097       C  
ATOM    552  C   ILE A  77       5.163  42.704  45.496  1.00 56.86           C  
ANISOU  552  C   ILE A  77     7337   9244   5023   -481   -314  -2105       C  
ATOM    553  O   ILE A  77       4.055  43.150  45.221  1.00 56.42           O  
ANISOU  553  O   ILE A  77     7375   9105   4956   -382   -317  -2117       O  
ATOM    554  CB  ILE A  77       6.414  42.327  43.258  1.00 56.46           C  
ANISOU  554  CB  ILE A  77     7334   8936   5184   -771   -218  -1908       C  
ATOM    555  CG1 ILE A  77       6.624  40.814  43.501  1.00 55.82           C  
ANISOU  555  CG1 ILE A  77     7095   9069   5046   -743   -151  -1778       C  
ATOM    556  CG2 ILE A  77       7.424  42.915  42.265  1.00 56.23           C  
ANISOU  556  CG2 ILE A  77     7371   8713   5281   -965   -216  -1900       C  
ATOM    557  CD1 ILE A  77       6.251  39.853  42.224  1.00 52.72           C  
ANISOU  557  CD1 ILE A  77     6708   8622   4702   -764    -53  -1587       C  
ATOM    558  N   LYS A  78       5.397  41.924  46.589  1.00 52.76           N  
ANISOU  558  N   LYS A  78     6674   8977   4397   -415   -313  -2104       N  
ATOM    559  CA  LYS A  78       4.362  41.509  47.559  1.00 54.09           C  
ANISOU  559  CA  LYS A  78     6779   9352   4422   -229   -308  -2106       C  
ATOM    560  C   LYS A  78       3.824  42.713  48.339  1.00 59.94           C  
ANISOU  560  C   LYS A  78     7595  10079   5100   -116   -398  -2305       C  
ATOM    561  O   LYS A  78       2.621  42.903  48.421  1.00 59.74           O  
ANISOU  561  O   LYS A  78     7608  10076   5015     24   -391  -2314       O  
ATOM    562  CB  LYS A  78       4.928  40.456  48.538  1.00 56.60           C  
ANISOU  562  CB  LYS A  78     6932   9933   4641   -203   -293  -2054       C  
ATOM    563  CG  LYS A  78       4.009  40.039  49.660  1.00 57.26           C  
ANISOU  563  CG  LYS A  78     6937  10257   4563    -25   -291  -2056       C  
ATOM    564  CD  LYS A  78       4.774  39.243  50.747  1.00 73.61           C  
ANISOU  564  CD  LYS A  78     8860  12575   6534     -8   -300  -2036       C  
ATOM    565  CE  LYS A  78       5.752  40.064  51.576  1.00 82.60           C  
ANISOU  565  CE  LYS A  78     9985  13755   7643    -33   -398  -2230       C  
ATOM    566  NZ  LYS A  78       6.910  39.255  52.084  1.00 79.34           N  
ANISOU  566  NZ  LYS A  78     9443  13497   7204    -92   -401  -2184       N  
ATOM    567  N   VAL A  79       4.727  43.512  48.898  1.00 59.20           N  
ANISOU  567  N   VAL A  79     7520   9954   5020   -176   -484  -2469       N  
ATOM    568  CA  VAL A  79       4.441  44.727  49.673  1.00 60.57           C  
ANISOU  568  CA  VAL A  79     7774  10094   5145    -84   -588  -2688       C  
ATOM    569  C   VAL A  79       3.690  45.711  48.768  1.00 63.66           C  
ANISOU  569  C   VAL A  79     8345  10216   5627    -72   -607  -2723       C  
ATOM    570  O   VAL A  79       2.669  46.280  49.185  1.00 63.80           O  
ANISOU  570  O   VAL A  79     8422  10246   5572     95   -644  -2821       O  
ATOM    571  CB  VAL A  79       5.761  45.332  50.247  1.00 65.15           C  
ANISOU  571  CB  VAL A  79     8340  10662   5754   -198   -681  -2843       C  
ATOM    572  CG1 VAL A  79       5.548  46.719  50.841  1.00 66.50           C  
ANISOU  572  CG1 VAL A  79     8628  10732   5909   -129   -801  -3082       C  
ATOM    573  CG2 VAL A  79       6.366  44.409  51.283  1.00 65.08           C  
ANISOU  573  CG2 VAL A  79     8154  10946   5629   -168   -673  -2823       C  
ATOM    574  N   ARG A  80       4.166  45.863  47.510  1.00 57.37           N  
ANISOU  574  N   ARG A  80     7628   9189   4979   -237   -577  -2633       N  
ATOM    575  CA  ARG A  80       3.520  46.775  46.586  1.00 56.59           C  
ANISOU  575  CA  ARG A  80     7705   8828   4968   -233   -595  -2648       C  
ATOM    576  C   ARG A  80       2.101  46.313  46.287  1.00 58.98           C  
ANISOU  576  C   ARG A  80     8010   9193   5208    -71   -533  -2549       C  
ATOM    577  O   ARG A  80       1.171  47.113  46.390  1.00 57.38           O  
ANISOU  577  O   ARG A  80     7907   8917   4977     66   -581  -2646       O  
ATOM    578  CB  ARG A  80       4.347  46.916  45.318  1.00 56.66           C  
ANISOU  578  CB  ARG A  80     7784   8613   5132   -445   -565  -2551       C  
ATOM    579  CG  ARG A  80       5.572  47.793  45.550  1.00 55.54           C  
ANISOU  579  CG  ARG A  80     7682   8354   5068   -603   -651  -2685       C  
ATOM    580  CD  ARG A  80       6.456  47.917  44.321  1.00 53.93           C  
ANISOU  580  CD  ARG A  80     7528   7954   5008   -826   -614  -2582       C  
ATOM    581  NE  ARG A  80       5.754  48.580  43.217  1.00 55.72           N  
ANISOU  581  NE  ARG A  80     7929   7929   5315   -828   -605  -2528       N  
ATOM    582  CZ  ARG A  80       5.600  49.897  43.120  1.00 70.08           C  
ANISOU  582  CZ  ARG A  80     9920   9512   7196   -837   -697  -2650       C  
ATOM    583  NH1 ARG A  80       6.096  50.701  44.052  1.00 59.84           N  
ANISOU  583  NH1 ARG A  80     8648   8193   5897   -852   -806  -2841       N  
ATOM    584  NH2 ARG A  80       4.932  50.418  42.104  1.00 55.37           N  
ANISOU  584  NH2 ARG A  80     8211   7431   5396   -825   -685  -2584       N  
ATOM    585  N   TYR A  81       1.923  44.999  46.034  1.00 55.95           N  
ANISOU  585  N   TYR A  81     7503   8964   4792    -75   -433  -2367       N  
ATOM    586  CA  TYR A  81       0.619  44.409  45.704  1.00 55.17           C  
ANISOU  586  CA  TYR A  81     7384   8938   4640     53   -368  -2252       C  
ATOM    587  C   TYR A  81      -0.383  44.620  46.828  1.00 57.36           C  
ANISOU  587  C   TYR A  81     7622   9400   4773    262   -402  -2358       C  
ATOM    588  O   TYR A  81      -1.523  44.971  46.550  1.00 57.17           O  
ANISOU  588  O   TYR A  81     7659   9335   4727    385   -402  -2367       O  
ATOM    589  CB  TYR A  81       0.749  42.912  45.353  1.00 54.12           C  
ANISOU  589  CB  TYR A  81     7120   8942   4501     -4   -267  -2049       C  
ATOM    590  CG  TYR A  81      -0.525  42.251  44.870  1.00 54.35           C  
ANISOU  590  CG  TYR A  81     7128   9023   4497     92   -202  -1918       C  
ATOM    591  CD1 TYR A  81      -0.967  42.423  43.561  1.00 55.57           C  
ANISOU  591  CD1 TYR A  81     7386   8982   4745     51   -174  -1839       C  
ATOM    592  CD2 TYR A  81      -1.214  41.347  45.674  1.00 55.32           C  
ANISOU  592  CD2 TYR A  81     7118   9401   4499    205   -162  -1854       C  
ATOM    593  CE1 TYR A  81      -2.078  41.741  43.076  1.00 53.57           C  
ANISOU  593  CE1 TYR A  81     7104   8785   4467    124   -117  -1716       C  
ATOM    594  CE2 TYR A  81      -2.351  40.679  45.205  1.00 55.21           C  
ANISOU  594  CE2 TYR A  81     7073   9440   4463    270   -102  -1724       C  
ATOM    595  CZ  TYR A  81      -2.771  40.877  43.903  1.00 59.60           C  
ANISOU  595  CZ  TYR A  81     7731   9798   5117    229    -82  -1661       C  
ATOM    596  OH  TYR A  81      -3.871  40.223  43.407  1.00 61.49           O  
ANISOU  596  OH  TYR A  81     7935  10090   5338    286    -30  -1540       O  
ATOM    597  N   SER A  82       0.050  44.461  48.087  1.00 55.61           N  
ANISOU  597  N   SER A  82     7298   9385   4446    309   -435  -2447       N  
ATOM    598  CA  SER A  82      -0.787  44.665  49.272  1.00 55.60           C  
ANISOU  598  CA  SER A  82     7246   9592   4287    511   -468  -2560       C  
ATOM    599  C   SER A  82      -1.294  46.137  49.377  1.00 59.44           C  
ANISOU  599  C   SER A  82     7886   9918   4780    621   -565  -2765       C  
ATOM    600  O   SER A  82      -2.264  46.367  50.084  1.00 56.79           O  
ANISOU  600  O   SER A  82     7528   9730   4321    814   -582  -2847       O  
ATOM    601  CB  SER A  82      -0.032  44.267  50.540  1.00 57.80           C  
ANISOU  601  CB  SER A  82     7397  10108   4458    522   -492  -2620       C  
ATOM    602  OG  SER A  82       0.857  45.286  50.975  1.00 62.62           O  
ANISOU  602  OG  SER A  82     8078  10614   5100    472   -596  -2816       O  
ATOM    603  N   LYS A  83      -0.655  47.101  48.646  1.00 56.97           N  
ANISOU  603  N   LYS A  83     7729   9306   4610    498   -626  -2839       N  
ATOM    604  CA  LYS A  83      -0.979  48.543  48.620  1.00 58.27           C  
ANISOU  604  CA  LYS A  83     8069   9260   4812    575   -730  -3028       C  
ATOM    605  C   LYS A  83      -1.563  48.954  47.249  1.00 62.33           C  
ANISOU  605  C   LYS A  83     8729   9512   5444    549   -710  -2941       C  
ATOM    606  O   LYS A  83      -1.593  50.142  46.896  1.00 62.50           O  
ANISOU  606  O   LYS A  83     8924   9278   5544    552   -794  -3057       O  
ATOM    607  CB  LYS A  83       0.269  49.377  48.940  1.00 61.48           C  
ANISOU  607  CB  LYS A  83     8546   9521   5292    442   -829  -3184       C  
ATOM    608  CG  LYS A  83       0.777  49.195  50.364  1.00 69.48           C  
ANISOU  608  CG  LYS A  83     9437  10784   6180    494   -874  -3311       C  
ATOM    609  CD  LYS A  83       2.098  49.895  50.582  1.00 77.64           C  
ANISOU  609  CD  LYS A  83    10519  11681   7298    329   -967  -3444       C  
ATOM    610  CE  LYS A  83       2.542  49.793  52.023  1.00 82.49           C  
ANISOU  610  CE  LYS A  83    11018  12549   7776    400  -1025  -3589       C  
ATOM    611  NZ  LYS A  83       3.979  50.158  52.179  1.00 94.30           N  
ANISOU  611  NZ  LYS A  83    12513  13959   9357    205  -1096  -3676       N  
ATOM    612  N   ASP A  84      -2.067  47.945  46.508  1.00 57.03           N  
ANISOU  612  N   ASP A  84     7983   8908   4777    530   -604  -2735       N  
ATOM    613  CA  ASP A  84      -2.693  48.032  45.195  1.00 56.91           C  
ANISOU  613  CA  ASP A  84     8067   8707   4850    511   -565  -2615       C  
ATOM    614  C   ASP A  84      -1.777  48.685  44.158  1.00 60.69           C  
ANISOU  614  C   ASP A  84     8693   8876   5491    317   -592  -2596       C  
ATOM    615  O   ASP A  84      -2.239  49.419  43.280  1.00 60.56           O  
ANISOU  615  O   ASP A  84     8829   8634   5547    333   -617  -2591       O  
ATOM    616  CB  ASP A  84      -4.068  48.727  45.278  1.00 59.96           C  
ANISOU  616  CB  ASP A  84     8529   9079   5175    733   -604  -2701       C  
ATOM    617  CG  ASP A  84      -5.093  47.919  46.056  1.00 65.24           C  
ANISOU  617  CG  ASP A  84     9033  10069   5685    909   -551  -2669       C  
ATOM    618  OD1 ASP A  84      -4.839  46.714  46.306  1.00 62.88           O  
ANISOU  618  OD1 ASP A  84     8574   9976   5340    846   -472  -2537       O  
ATOM    619  OD2 ASP A  84      -6.162  48.481  46.393  1.00 72.08           O  
ANISOU  619  OD2 ASP A  84     9931  10983   6474   1111   -589  -2768       O  
ATOM    620  N   ARG A  85      -0.470  48.378  44.260  1.00 56.81           N  
ANISOU  620  N   ARG A  85     8145   8388   5050    134   -583  -2578       N  
ATOM    621  CA  ARG A  85       0.582  48.755  43.307  1.00 56.07           C  
ANISOU  621  CA  ARG A  85     8144   8058   5103    -85   -587  -2528       C  
ATOM    622  C   ARG A  85       0.921  47.471  42.608  1.00 56.51           C  
ANISOU  622  C   ARG A  85     8083   8210   5177   -191   -473  -2323       C  
ATOM    623  O   ARG A  85       1.623  46.627  43.164  1.00 56.49           O  
ANISOU  623  O   ARG A  85     7932   8396   5134   -244   -438  -2290       O  
ATOM    624  CB  ARG A  85       1.788  49.395  44.025  1.00 57.71           C  
ANISOU  624  CB  ARG A  85     8359   8224   5344   -201   -669  -2677       C  
ATOM    625  CG  ARG A  85       1.765  50.914  44.057  1.00 63.54           C  
ANISOU  625  CG  ARG A  85     9290   8703   6149   -194   -788  -2848       C  
ATOM    626  CD  ARG A  85       0.708  51.428  45.008  1.00 69.02           C  
ANISOU  626  CD  ARG A  85    10016   9477   6732     53   -859  -3013       C  
ATOM    627  NE  ARG A  85       0.978  52.792  45.454  1.00 78.42           N  
ANISOU  627  NE  ARG A  85    11359  10470   7968     59   -994  -3224       N  
ATOM    628  CZ  ARG A  85       0.072  53.574  46.029  1.00 86.29           C  
ANISOU  628  CZ  ARG A  85    12447  11441   8901    269  -1077  -3388       C  
ATOM    629  NH1 ARG A  85      -1.167  53.140  46.211  1.00 60.14           N  
ANISOU  629  NH1 ARG A  85     9077   8300   5473    486  -1031  -3358       N  
ATOM    630  NH2 ARG A  85       0.399  54.797  46.428  1.00 75.64           N  
ANISOU  630  NH2 ARG A  85    11244   9895   7602    265  -1209  -3587       N  
ATOM    631  N   ILE A  86       0.258  47.236  41.483  1.00 51.90           N  
ANISOU  631  N   ILE A  86     7557   7530   4635   -186   -416  -2188       N  
ATOM    632  CA  ILE A  86       0.347  45.986  40.745  1.00 49.92           C  
ANISOU  632  CA  ILE A  86     7207   7366   4394   -256   -311  -1996       C  
ATOM    633  C   ILE A  86       1.488  45.999  39.739  1.00 52.57           C  
ANISOU  633  C   ILE A  86     7582   7546   4845   -469   -280  -1913       C  
ATOM    634  O   ILE A  86       1.876  44.929  39.261  1.00 47.96           O  
ANISOU  634  O   ILE A  86     6902   7050   4272   -546   -200  -1776       O  
ATOM    635  CB  ILE A  86      -1.004  45.635  40.070  1.00 52.03           C  
ANISOU  635  CB  ILE A  86     7497   7640   4634   -132   -268  -1897       C  
ATOM    636  CG1 ILE A  86      -1.411  46.665  38.954  1.00 51.63           C  
ANISOU  636  CG1 ILE A  86     7640   7313   4666   -139   -300  -1894       C  
ATOM    637  CG2 ILE A  86      -2.098  45.443  41.143  1.00 53.25           C  
ANISOU  637  CG2 ILE A  86     7570   8005   4659     74   -283  -1963       C  
ATOM    638  CD1 ILE A  86      -2.438  46.155  37.954  1.00 46.20           C  
ANISOU  638  CD1 ILE A  86     6965   6619   3971    -70   -244  -1759       C  
ATOM    639  N   TYR A  87       2.056  47.192  39.477  1.00 50.33           N  
ANISOU  639  N   TYR A  87     7436   7042   4646   -565   -346  -1999       N  
ATOM    640  CA  TYR A  87       3.147  47.386  38.522  1.00 50.38           C  
ANISOU  640  CA  TYR A  87     7490   6892   4762   -778   -321  -1926       C  
ATOM    641  C   TYR A  87       4.460  47.757  39.217  1.00 55.70           C  
ANISOU  641  C   TYR A  87     8116   7578   5469   -918   -370  -2029       C  
ATOM    642  O   TYR A  87       4.484  48.659  40.059  1.00 55.55           O  
ANISOU  642  O   TYR A  87     8154   7510   5443   -880   -466  -2194       O  
ATOM    643  CB  TYR A  87       2.773  48.484  37.511  1.00 52.51           C  
ANISOU  643  CB  TYR A  87     7964   6876   5112   -805   -355  -1914       C  
ATOM    644  CG  TYR A  87       1.543  48.186  36.675  1.00 52.40           C  
ANISOU  644  CG  TYR A  87     8002   6836   5072   -680   -311  -1808       C  
ATOM    645  CD1 TYR A  87       1.536  47.140  35.759  1.00 52.70           C  
ANISOU  645  CD1 TYR A  87     7970   6942   5111   -728   -213  -1639       C  
ATOM    646  CD2 TYR A  87       0.416  49.004  36.735  1.00 53.76           C  
ANISOU  646  CD2 TYR A  87     8301   6902   5222   -518   -375  -1881       C  
ATOM    647  CE1 TYR A  87       0.415  46.868  34.975  1.00 52.07           C  
ANISOU  647  CE1 TYR A  87     7936   6841   5009   -621   -180  -1548       C  
ATOM    648  CE2 TYR A  87      -0.710  48.747  35.949  1.00 53.64           C  
ANISOU  648  CE2 TYR A  87     8326   6872   5183   -404   -340  -1786       C  
ATOM    649  CZ  TYR A  87      -0.696  47.688  35.053  1.00 57.03           C  
ANISOU  649  CZ  TYR A  87     8681   7375   5614   -464   -243  -1618       C  
ATOM    650  OH  TYR A  87      -1.774  47.419  34.243  1.00 53.86           O  
ANISOU  650  OH  TYR A  87     8313   6961   5189   -362   -214  -1527       O  
ATOM    651  N   THR A  88       5.558  47.061  38.853  1.00 52.52           N  
ANISOU  651  N   THR A  88     7606   7248   5102  -1076   -307  -1937       N  
ATOM    652  CA  THR A  88       6.924  47.295  39.350  1.00 53.55           C  
ANISOU  652  CA  THR A  88     7668   7409   5271  -1234   -342  -2012       C  
ATOM    653  C   THR A  88       7.914  47.041  38.230  1.00 59.15           C  
ANISOU  653  C   THR A  88     8355   8055   6063  -1432   -271  -1882       C  
ATOM    654  O   THR A  88       7.745  46.065  37.500  1.00 58.76           O  
ANISOU  654  O   THR A  88     8249   8080   6000  -1419   -179  -1736       O  
ATOM    655  CB  THR A  88       7.253  46.393  40.572  1.00 60.81           C  
ANISOU  655  CB  THR A  88     8401   8609   6094  -1165   -342  -2060       C  
ATOM    656  OG1 THR A  88       6.142  46.318  41.455  1.00 59.98           O  
ANISOU  656  OG1 THR A  88     8293   8610   5887   -956   -375  -2133       O  
ATOM    657  CG2 THR A  88       8.456  46.872  41.348  1.00 57.82           C  
ANISOU  657  CG2 THR A  88     7966   8263   5739  -1286   -412  -2188       C  
ATOM    658  N   TYR A  89       8.964  47.868  38.108  1.00 58.58           N  
ANISOU  658  N   TYR A  89     8319   7861   6076  -1618   -313  -1935       N  
ATOM    659  CA  TYR A  89       9.995  47.632  37.093  1.00 58.79           C  
ANISOU  659  CA  TYR A  89     8306   7857   6175  -1817   -242  -1814       C  
ATOM    660  C   TYR A  89      11.117  46.723  37.560  1.00 65.32           C  
ANISOU  660  C   TYR A  89     8927   8916   6977  -1890   -206  -1805       C  
ATOM    661  O   TYR A  89      11.388  46.591  38.758  1.00 66.89           O  
ANISOU  661  O   TYR A  89     9029   9262   7124  -1840   -262  -1922       O  
ATOM    662  CB  TYR A  89      10.655  48.943  36.636  1.00 61.18           C  
ANISOU  662  CB  TYR A  89     8737   7920   6587  -2010   -296  -1852       C  
ATOM    663  CG  TYR A  89       9.725  49.931  35.980  1.00 62.18           C  
ANISOU  663  CG  TYR A  89     9086   7781   6757  -1968   -333  -1842       C  
ATOM    664  CD1 TYR A  89       9.026  49.601  34.819  1.00 61.54           C  
ANISOU  664  CD1 TYR A  89     9078   7632   6674  -1922   -256  -1689       C  
ATOM    665  CD2 TYR A  89       9.574  51.215  36.490  1.00 64.47           C  
ANISOU  665  CD2 TYR A  89     9522   7881   7095  -1975   -452  -1987       C  
ATOM    666  CE1 TYR A  89       8.161  50.508  34.213  1.00 60.67           C  
ANISOU  666  CE1 TYR A  89     9172   7282   6598  -1872   -295  -1676       C  
ATOM    667  CE2 TYR A  89       8.742  52.144  35.872  1.00 66.30           C  
ANISOU  667  CE2 TYR A  89     9966   7855   7368  -1929   -493  -1976       C  
ATOM    668  CZ  TYR A  89       8.023  51.781  34.743  1.00 69.67           C  
ANISOU  668  CZ  TYR A  89    10457   8230   7785  -1873   -413  -1817       C  
ATOM    669  OH  TYR A  89       7.169  52.684  34.163  1.00 69.86           O  
ANISOU  669  OH  TYR A  89    10690   8010   7843  -1809   -460  -1807       O  
ATOM    670  N   VAL A  90      11.801  46.143  36.575  1.00 62.35           N  
ANISOU  670  N   VAL A  90     8487   8569   6634  -2008   -114  -1669       N  
ATOM    671  CA  VAL A  90      13.058  45.391  36.644  1.00 62.31           C  
ANISOU  671  CA  VAL A  90     8299   8747   6628  -2116    -68  -1635       C  
ATOM    672  C   VAL A  90      13.829  45.991  35.478  1.00 65.72           C  
ANISOU  672  C   VAL A  90     8783   9035   7152  -2328    -26  -1555       C  
ATOM    673  O   VAL A  90      13.791  45.466  34.372  1.00 62.22           O  
ANISOU  673  O   VAL A  90     8341   8586   6712  -2347     66  -1414       O  
ATOM    674  CB  VAL A  90      12.937  43.842  36.617  1.00 64.76           C  
ANISOU  674  CB  VAL A  90     8467   9274   6863  -1996     13  -1537       C  
ATOM    675  CG1 VAL A  90      14.316  43.185  36.667  1.00 64.64           C  
ANISOU  675  CG1 VAL A  90     8271   9436   6853  -2105     51  -1516       C  
ATOM    676  CG2 VAL A  90      12.071  43.338  37.767  1.00 64.27           C  
ANISOU  676  CG2 VAL A  90     8370   9340   6709  -1794    -28  -1602       C  
ATOM    677  N   ALA A  91      14.424  47.183  35.716  1.00 65.15           N  
ANISOU  677  N   ALA A  91     8773   8827   7153  -2484   -103  -1648       N  
ATOM    678  CA  ALA A  91      15.075  48.005  34.703  1.00 66.20           C  
ANISOU  678  CA  ALA A  91     8983   8788   7381  -2702    -82  -1580       C  
ATOM    679  C   ALA A  91      13.995  48.361  33.643  1.00 68.93           C  
ANISOU  679  C   ALA A  91     9523   8927   7742  -2643    -48  -1474       C  
ATOM    680  O   ALA A  91      12.997  48.994  34.009  1.00 69.14           O  
ANISOU  680  O   ALA A  91     9697   8807   7765  -2527   -121  -1546       O  
ATOM    681  CB  ALA A  91      16.297  47.298  34.104  1.00 66.87           C  
ANISOU  681  CB  ALA A  91     8895   9037   7475  -2849     10  -1484       C  
ATOM    682  N   ASN A  92      14.124  47.895  32.392  1.00 63.34           N  
ANISOU  682  N   ASN A  92     8807   8225   7035  -2696     58  -1313       N  
ATOM    683  CA  ASN A  92      13.134  48.191  31.355  1.00 62.07           C  
ANISOU  683  CA  ASN A  92     8821   7884   6878  -2638     88  -1210       C  
ATOM    684  C   ASN A  92      11.992  47.150  31.297  1.00 62.03           C  
ANISOU  684  C   ASN A  92     8805   7977   6788  -2403    127  -1169       C  
ATOM    685  O   ASN A  92      11.079  47.286  30.468  1.00 62.20           O  
ANISOU  685  O   ASN A  92     8960   7873   6801  -2329    148  -1090       O  
ATOM    686  CB  ASN A  92      13.819  48.292  29.997  1.00 63.80           C  
ANISOU  686  CB  ASN A  92     9049   8058   7134  -2814    179  -1056       C  
ATOM    687  CG  ASN A  92      14.790  49.441  29.886  1.00 90.92           C  
ANISOU  687  CG  ASN A  92    12529  11353  10662  -3060    142  -1070       C  
ATOM    688  OD1 ASN A  92      14.512  50.591  30.272  1.00 80.15           O  
ANISOU  688  OD1 ASN A  92    11318   9778   9359  -3096     43  -1152       O  
ATOM    689  ND2 ASN A  92      15.955  49.145  29.336  1.00 87.13           N  
ANISOU  689  ND2 ASN A  92    11919  10990  10197  -3235    220   -990       N  
ATOM    690  N   ILE A  93      12.049  46.112  32.148  1.00 55.22           N  
ANISOU  690  N   ILE A  93     7783   7336   5861  -2293    135  -1216       N  
ATOM    691  CA  ILE A  93      11.016  45.065  32.178  1.00 53.33           C  
ANISOU  691  CA  ILE A  93     7516   7202   5544  -2087    169  -1174       C  
ATOM    692  C   ILE A  93       9.940  45.456  33.192  1.00 56.69           C  
ANISOU  692  C   ILE A  93     8012   7593   5935  -1922     81  -1289       C  
ATOM    693  O   ILE A  93      10.277  45.987  34.250  1.00 58.21           O  
ANISOU  693  O   ILE A  93     8183   7800   6133  -1938      3  -1422       O  
ATOM    694  CB  ILE A  93      11.658  43.677  32.475  1.00 55.32           C  
ANISOU  694  CB  ILE A  93     7564   7708   5747  -2059    229  -1142       C  
ATOM    695  CG1 ILE A  93      12.505  43.215  31.247  1.00 56.86           C  
ANISOU  695  CG1 ILE A  93     7704   7937   5964  -2187    327  -1016       C  
ATOM    696  CG2 ILE A  93      10.591  42.624  32.813  1.00 53.21           C  
ANISOU  696  CG2 ILE A  93     7262   7552   5404  -1853    245  -1116       C  
ATOM    697  CD1 ILE A  93      13.610  42.248  31.565  1.00 69.27           C  
ANISOU  697  CD1 ILE A  93     9075   9731   7512  -2219    369  -1011       C  
ATOM    698  N   LEU A  94       8.651  45.204  32.869  1.00 51.58           N  
ANISOU  698  N   LEU A  94     7443   6908   5247  -1762     93  -1244       N  
ATOM    699  CA  LEU A  94       7.543  45.498  33.768  1.00 50.49           C  
ANISOU  699  CA  LEU A  94     7358   6765   5063  -1588     21  -1344       C  
ATOM    700  C   LEU A  94       6.923  44.234  34.339  1.00 53.33           C  
ANISOU  700  C   LEU A  94     7589   7339   5336  -1430     54  -1321       C  
ATOM    701  O   LEU A  94       6.485  43.377  33.579  1.00 52.56           O  
ANISOU  701  O   LEU A  94     7468   7284   5218  -1386    123  -1203       O  
ATOM    702  CB  LEU A  94       6.452  46.335  33.060  1.00 50.57           C  
ANISOU  702  CB  LEU A  94     7560   6564   5091  -1519     -6  -1323       C  
ATOM    703  CG  LEU A  94       5.249  46.812  33.931  1.00 54.69           C  
ANISOU  703  CG  LEU A  94     8148   7070   5564  -1326    -86  -1437       C  
ATOM    704  CD1 LEU A  94       5.652  47.923  34.881  1.00 56.04           C  
ANISOU  704  CD1 LEU A  94     8371   7158   5763  -1359   -188  -1602       C  
ATOM    705  CD2 LEU A  94       4.131  47.317  33.073  1.00 57.17           C  
ANISOU  705  CD2 LEU A  94     8620   7218   5884  -1235    -94  -1387       C  
ATOM    706  N   ILE A  95       6.832  44.154  35.676  1.00 50.52           N  
ANISOU  706  N   ILE A  95     7158   7111   4925  -1342      0  -1433       N  
ATOM    707  CA  ILE A  95       6.142  43.084  36.401  1.00 49.48           C  
ANISOU  707  CA  ILE A  95     6916   7180   4705  -1184     19  -1417       C  
ATOM    708  C   ILE A  95       4.766  43.638  36.754  1.00 52.62           C  
ANISOU  708  C   ILE A  95     7409   7525   5059  -1021    -31  -1477       C  
ATOM    709  O   ILE A  95       4.669  44.681  37.403  1.00 54.30           O  
ANISOU  709  O   ILE A  95     7695   7663   5273   -995   -112  -1611       O  
ATOM    710  CB  ILE A  95       6.905  42.529  37.643  1.00 53.51           C  
ANISOU  710  CB  ILE A  95     7267   7898   5165  -1181     -1  -1483       C  
ATOM    711  CG1 ILE A  95       8.265  41.911  37.236  1.00 54.18           C  
ANISOU  711  CG1 ILE A  95     7246   8049   5291  -1330     51  -1420       C  
ATOM    712  CG2 ILE A  95       6.019  41.487  38.407  1.00 53.50           C  
ANISOU  712  CG2 ILE A  95     7169   8092   5065  -1010     17  -1452       C  
ATOM    713  CD1 ILE A  95       9.027  41.238  38.431  1.00 60.29           C  
ANISOU  713  CD1 ILE A  95     7853   9044   6010  -1315     33  -1471       C  
ATOM    714  N   ALA A  96       3.720  42.952  36.288  1.00 47.64           N  
ANISOU  714  N   ALA A  96     6778   6933   4392   -913     14  -1383       N  
ATOM    715  CA  ALA A  96       2.303  43.282  36.434  1.00 47.07           C  
ANISOU  715  CA  ALA A  96     6775   6838   4273   -749    -16  -1411       C  
ATOM    716  C   ALA A  96       1.616  42.139  37.143  1.00 52.92           C  
ANISOU  716  C   ALA A  96     7378   7804   4923   -624     15  -1371       C  
ATOM    717  O   ALA A  96       1.535  41.037  36.581  1.00 52.55           O  
ANISOU  717  O   ALA A  96     7264   7827   4876   -638     82  -1244       O  
ATOM    718  CB  ALA A  96       1.684  43.514  35.054  1.00 46.40           C  
ANISOU  718  CB  ALA A  96     6812   6587   4232   -754     13  -1316       C  
ATOM    719  N   VAL A  97       1.195  42.355  38.399  1.00 50.50           N  
ANISOU  719  N   VAL A  97     7026   7620   4540   -509    -35  -1478       N  
ATOM    720  CA  VAL A  97       0.560  41.296  39.181  1.00 49.80           C  
ANISOU  720  CA  VAL A  97     6802   7761   4358   -397     -6  -1434       C  
ATOM    721  C   VAL A  97      -0.929  41.521  39.083  1.00 54.87           C  
ANISOU  721  C   VAL A  97     7490   8404   4953   -246    -15  -1434       C  
ATOM    722  O   VAL A  97      -1.394  42.632  39.338  1.00 57.74           O  
ANISOU  722  O   VAL A  97     7949   8684   5306   -168    -77  -1551       O  
ATOM    723  CB  VAL A  97       1.082  41.206  40.636  1.00 54.58           C  
ANISOU  723  CB  VAL A  97     7302   8546   4890   -364    -42  -1531       C  
ATOM    724  CG1 VAL A  97       0.617  39.911  41.312  1.00 54.36           C  
ANISOU  724  CG1 VAL A  97     7125   8756   4772   -283      3  -1441       C  
ATOM    725  CG2 VAL A  97       2.599  41.317  40.686  1.00 53.88           C  
ANISOU  725  CG2 VAL A  97     7190   8424   4859   -518    -54  -1564       C  
ATOM    726  N   ASN A  98      -1.677  40.498  38.640  1.00 48.00           N  
ANISOU  726  N   ASN A  98     6559   7618   4063   -207     43  -1304       N  
ATOM    727  CA  ASN A  98      -3.121  40.622  38.430  1.00 47.21           C  
ANISOU  727  CA  ASN A  98     6487   7531   3922    -73     39  -1290       C  
ATOM    728  C   ASN A  98      -3.854  40.960  39.736  1.00 50.70           C  
ANISOU  728  C   ASN A  98     6874   8135   4256     82     -1  -1396       C  
ATOM    729  O   ASN A  98      -3.819  40.158  40.665  1.00 49.24           O  
ANISOU  729  O   ASN A  98     6555   8158   3998    111     21  -1372       O  
ATOM    730  CB  ASN A  98      -3.696  39.342  37.782  1.00 45.95           C  
ANISOU  730  CB  ASN A  98     6251   7446   3761    -80    105  -1130       C  
ATOM    731  CG  ASN A  98      -5.162  39.394  37.435  1.00 53.62           C  
ANISOU  731  CG  ASN A  98     7238   8438   4697     42    103  -1104       C  
ATOM    732  OD1 ASN A  98      -5.920  40.310  37.804  1.00 46.36           O  
ANISOU  732  OD1 ASN A  98     6368   7512   3734    164     56  -1203       O  
ATOM    733  ND2 ASN A  98      -5.615  38.386  36.738  1.00 43.33           N  
ANISOU  733  ND2 ASN A  98     5887   7168   3409     17    151   -974       N  
ATOM    734  N   PRO A  99      -4.531  42.142  39.824  1.00 47.80           N  
ANISOU  734  N   PRO A  99     6610   7679   3873    192    -62  -1514       N  
ATOM    735  CA  PRO A  99      -5.234  42.491  41.075  1.00 47.50           C  
ANISOU  735  CA  PRO A  99     6517   7810   3720    357   -101  -1629       C  
ATOM    736  C   PRO A  99      -6.539  41.726  41.285  1.00 52.08           C  
ANISOU  736  C   PRO A  99     6985   8591   4213    479    -58  -1549       C  
ATOM    737  O   PRO A  99      -6.986  41.626  42.422  1.00 52.75           O  
ANISOU  737  O   PRO A  99     6971   8885   4185    593    -65  -1604       O  
ATOM    738  CB  PRO A  99      -5.530  43.980  40.903  1.00 50.08           C  
ANISOU  738  CB  PRO A  99     7008   7946   4074    434   -181  -1773       C  
ATOM    739  CG  PRO A  99      -5.651  44.176  39.439  1.00 52.80           C  
ANISOU  739  CG  PRO A  99     7471   8071   4519    362   -166  -1684       C  
ATOM    740  CD  PRO A  99      -4.667  43.216  38.814  1.00 48.04           C  
ANISOU  740  CD  PRO A  99     6815   7454   3982    178   -100  -1548       C  
ATOM    741  N   TYR A 100      -7.168  41.229  40.194  1.00 48.23           N  
ANISOU  741  N   TYR A 100     6509   8046   3770    456    -17  -1423       N  
ATOM    742  CA  TYR A 100      -8.437  40.493  40.215  1.00 47.66           C  
ANISOU  742  CA  TYR A 100     6331   8145   3632    549     21  -1335       C  
ATOM    743  C   TYR A 100      -9.636  41.369  40.733  1.00 55.67           C  
ANISOU  743  C   TYR A 100     7355   9238   4558    750    -24  -1451       C  
ATOM    744  O   TYR A 100     -10.644  40.834  41.207  1.00 57.63           O  
ANISOU  744  O   TYR A 100     7478   9703   4716    847      4  -1410       O  
ATOM    745  CB  TYR A 100      -8.318  39.159  40.992  1.00 46.47           C  
ANISOU  745  CB  TYR A 100     6007   8229   3421    512     78  -1231       C  
ATOM    746  CG  TYR A 100      -7.819  38.020  40.118  1.00 45.44           C  
ANISOU  746  CG  TYR A 100     5852   8041   3373    361    132  -1072       C  
ATOM    747  CD1 TYR A 100      -8.494  37.661  38.951  1.00 45.92           C  
ANISOU  747  CD1 TYR A 100     5943   8017   3488    339    154   -977       C  
ATOM    748  CD2 TYR A 100      -6.737  37.237  40.510  1.00 44.93           C  
ANISOU  748  CD2 TYR A 100     5722   8028   3321    257    158  -1019       C  
ATOM    749  CE1 TYR A 100      -8.067  36.589  38.163  1.00 45.67           C  
ANISOU  749  CE1 TYR A 100     5890   7938   3526    214    198   -843       C  
ATOM    750  CE2 TYR A 100      -6.326  36.136  39.753  1.00 44.81           C  
ANISOU  750  CE2 TYR A 100     5682   7970   3376    139    204   -880       C  
ATOM    751  CZ  TYR A 100      -6.989  35.823  38.572  1.00 51.31           C  
ANISOU  751  CZ  TYR A 100     6544   8696   4254    117    223   -796       C  
ATOM    752  OH  TYR A 100      -6.607  34.744  37.816  1.00 47.54           O  
ANISOU  752  OH  TYR A 100     6047   8174   3841     11    262   -672       O  
ATOM    753  N   PHE A 101      -9.536  42.699  40.563  1.00 51.27           N  
ANISOU  753  N   PHE A 101     6951   8499   4032    808    -94  -1588       N  
ATOM    754  CA  PHE A 101     -10.566  43.688  40.843  1.00 52.87           C  
ANISOU  754  CA  PHE A 101     7201   8717   4171   1003   -150  -1713       C  
ATOM    755  C   PHE A 101     -10.175  45.001  40.149  1.00 60.29           C  
ANISOU  755  C   PHE A 101     8352   9353   5200    998   -224  -1812       C  
ATOM    756  O   PHE A 101      -9.042  45.130  39.685  1.00 58.87           O  
ANISOU  756  O   PHE A 101     8258   8992   5116    836   -227  -1794       O  
ATOM    757  CB  PHE A 101     -10.842  43.868  42.354  1.00 55.88           C  
ANISOU  757  CB  PHE A 101     7480   9335   4417   1143   -169  -1833       C  
ATOM    758  CG  PHE A 101      -9.923  44.802  43.094  1.00 58.38           C  
ANISOU  758  CG  PHE A 101     7884   9564   4734   1149   -240  -2005       C  
ATOM    759  CD1 PHE A 101      -8.625  44.420  43.409  1.00 58.52           C  
ANISOU  759  CD1 PHE A 101     7879   9566   4788    992   -229  -1991       C  
ATOM    760  CD2 PHE A 101     -10.371  46.051  43.519  1.00 62.50           C  
ANISOU  760  CD2 PHE A 101     8505  10028   5215   1318   -323  -2189       C  
ATOM    761  CE1 PHE A 101      -7.777  45.290  44.087  1.00 61.45           C  
ANISOU  761  CE1 PHE A 101     8326   9860   5162    988   -302  -2156       C  
ATOM    762  CE2 PHE A 101      -9.517  46.921  44.198  1.00 65.65           C  
ANISOU  762  CE2 PHE A 101     8992  10332   5621   1315   -399  -2358       C  
ATOM    763  CZ  PHE A 101      -8.228  46.534  44.482  1.00 62.91           C  
ANISOU  763  CZ  PHE A 101     8617   9971   5313   1145   -388  -2340       C  
ATOM    764  N   ASP A 102     -11.118  45.957  40.049  1.00 60.33           N  
ANISOU  764  N   ASP A 102     8443   9304   5177   1172   -282  -1909       N  
ATOM    765  CA  ASP A 102     -10.849  47.220  39.382  1.00 60.94           C  
ANISOU  765  CA  ASP A 102     8734   9080   5341   1176   -359  -1994       C  
ATOM    766  C   ASP A 102     -10.254  48.228  40.339  1.00 64.43           C  
ANISOU  766  C   ASP A 102     9255   9457   5770   1221   -439  -2184       C  
ATOM    767  O   ASP A 102     -10.902  48.663  41.283  1.00 64.79           O  
ANISOU  767  O   ASP A 102     9263   9641   5713   1406   -480  -2318       O  
ATOM    768  CB  ASP A 102     -12.108  47.774  38.703  1.00 64.04           C  
ANISOU  768  CB  ASP A 102     9200   9411   5721   1341   -392  -2000       C  
ATOM    769  CG  ASP A 102     -12.545  46.894  37.555  1.00 84.11           C  
ANISOU  769  CG  ASP A 102    11699  11958   8300   1265   -327  -1817       C  
ATOM    770  OD1 ASP A 102     -11.913  46.974  36.467  1.00 85.68           O  
ANISOU  770  OD1 ASP A 102    12014  11937   8603   1120   -321  -1736       O  
ATOM    771  OD2 ASP A 102     -13.445  46.049  37.767  1.00 92.82           O  
ANISOU  771  OD2 ASP A 102    12640  13298   9327   1333   -279  -1750       O  
ATOM    772  N   ILE A 103      -9.002  48.595  40.083  1.00 60.92           N  
ANISOU  772  N   ILE A 103     8916   8807   5426   1048   -462  -2197       N  
ATOM    773  CA  ILE A 103      -8.297  49.590  40.874  1.00 61.96           C  
ANISOU  773  CA  ILE A 103     9140   8835   5569   1054   -549  -2378       C  
ATOM    774  C   ILE A 103      -8.758  50.924  40.318  1.00 68.59           C  
ANISOU  774  C   ILE A 103    10192   9408   6463   1154   -640  -2469       C  
ATOM    775  O   ILE A 103      -8.631  51.158  39.106  1.00 69.62           O  
ANISOU  775  O   ILE A 103    10444   9314   6694   1058   -635  -2369       O  
ATOM    776  CB  ILE A 103      -6.760  49.407  40.922  1.00 63.61           C  
ANISOU  776  CB  ILE A 103     9349   8963   5856    823   -539  -2359       C  
ATOM    777  CG1 ILE A 103      -6.395  47.924  41.261  1.00 60.43           C  
ANISOU  777  CG1 ILE A 103     8738   8818   5405    731   -440  -2229       C  
ATOM    778  CG2 ILE A 103      -6.164  50.398  41.967  1.00 65.40           C  
ANISOU  778  CG2 ILE A 103     9645   9133   6072    854   -639  -2571       C  
ATOM    779  CD1 ILE A 103      -5.028  47.586  41.130  1.00 54.21           C  
ANISOU  779  CD1 ILE A 103     7935   7970   4693    517   -416  -2179       C  
ATOM    780  N   PRO A 104      -9.443  51.718  41.172  1.00 65.55           N  
ANISOU  780  N   PRO A 104     9838   9070   5997   1372   -718  -2648       N  
ATOM    781  CA  PRO A 104     -10.045  52.969  40.705  1.00 67.08           C  
ANISOU  781  CA  PRO A 104    10233   9023   6231   1509   -813  -2743       C  
ATOM    782  C   PRO A 104      -9.105  53.947  40.020  1.00 73.97           C  
ANISOU  782  C   PRO A 104    11329   9526   7252   1354   -882  -2763       C  
ATOM    783  O   PRO A 104      -8.011  54.250  40.516  1.00 75.64           O  
ANISOU  783  O   PRO A 104    11571   9658   7511   1217   -917  -2840       O  
ATOM    784  CB  PRO A 104     -10.582  53.604  41.998  1.00 69.90           C  
ANISOU  784  CB  PRO A 104    10575   9510   6475   1741   -890  -2965       C  
ATOM    785  CG  PRO A 104     -10.818  52.464  42.905  1.00 72.83           C  
ANISOU  785  CG  PRO A 104    10698  10259   6713   1778   -806  -2929       C  
ATOM    786  CD  PRO A 104      -9.705  51.516  42.618  1.00 67.28           C  
ANISOU  786  CD  PRO A 104     9914   9573   6076   1514   -726  -2776       C  
ATOM    787  N   LYS A 105      -9.599  54.492  38.901  1.00 69.28           N  
ANISOU  787  N   LYS A 105    10890   8711   6723   1388   -908  -2699       N  
ATOM    788  CA  LYS A 105      -9.016  55.558  38.087  1.00 70.72           C  
ANISOU  788  CA  LYS A 105    11313   8519   7040   1281   -981  -2700       C  
ATOM    789  C   LYS A 105      -7.609  55.269  37.525  1.00 74.06           C  
ANISOU  789  C   LYS A 105    11754   8813   7574    973   -935  -2585       C  
ATOM    790  O   LYS A 105      -7.113  56.098  36.755  1.00 75.16           O  
ANISOU  790  O   LYS A 105    12085   8647   7825    863   -984  -2559       O  
ATOM    791  CB  LYS A 105      -8.960  56.907  38.867  1.00 76.24           C  
ANISOU  791  CB  LYS A 105    12178   9039   7753   1403  -1122  -2931       C  
ATOM    792  CG  LYS A 105      -9.983  57.133  40.004  1.00 99.68           C  
ANISOU  792  CG  LYS A 105    15076  12215  10583   1698  -1173  -3117       C  
ATOM    793  CD  LYS A 105     -11.431  57.304  39.524  1.00115.46           C  
ANISOU  793  CD  LYS A 105    17098  14249  12520   1946  -1184  -3098       C  
ATOM    794  CE  LYS A 105     -12.407  57.317  40.678  1.00128.05           C  
ANISOU  794  CE  LYS A 105    18571  16122  13960   2222  -1208  -3263       C  
ATOM    795  NZ  LYS A 105     -13.814  57.411  40.207  1.00137.09           N  
ANISOU  795  NZ  LYS A 105    19709  17341  15039   2461  -1210  -3240       N  
ATOM    796  N   ILE A 106      -6.983  54.113  37.836  1.00 67.71           N  
ANISOU  796  N   ILE A 106    10754   8230   6741    836   -840  -2505       N  
ATOM    797  CA  ILE A 106      -5.600  53.891  37.406  1.00 66.64           C  
ANISOU  797  CA  ILE A 106    10627   7989   6706    558   -802  -2417       C  
ATOM    798  C   ILE A 106      -5.472  53.679  35.878  1.00 68.71           C  
ANISOU  798  C   ILE A 106    10964   8095   7047    424   -742  -2218       C  
ATOM    799  O   ILE A 106      -4.344  53.710  35.394  1.00 68.03           O  
ANISOU  799  O   ILE A 106    10915   7882   7050    200   -720  -2149       O  
ATOM    800  CB  ILE A 106      -4.837  52.801  38.205  1.00 68.55           C  
ANISOU  800  CB  ILE A 106    10654   8491   6900    450   -731  -2401       C  
ATOM    801  CG1 ILE A 106      -5.322  51.380  37.902  1.00 66.42           C  
ANISOU  801  CG1 ILE A 106    10202   8470   6566    462   -614  -2238       C  
ATOM    802  CG2 ILE A 106      -4.875  53.115  39.721  1.00 69.38           C  
ANISOU  802  CG2 ILE A 106    10699   8742   6921    578   -799  -2605       C  
ATOM    803  CD1 ILE A 106      -4.265  50.336  38.222  1.00 72.78           C  
ANISOU  803  CD1 ILE A 106    10841   9442   7369    291   -539  -2170       C  
ATOM    804  N   TYR A 107      -6.598  53.563  35.123  1.00 64.37           N  
ANISOU  804  N   TYR A 107    10443   7550   6464    562   -723  -2135       N  
ATOM    805  CA  TYR A 107      -6.573  53.482  33.657  1.00 63.40           C  
ANISOU  805  CA  TYR A 107    10409   7274   6404    461   -679  -1958       C  
ATOM    806  C   TYR A 107      -7.414  54.612  33.031  1.00 69.25           C  
ANISOU  806  C   TYR A 107    11364   7780   7170    606   -765  -1983       C  
ATOM    807  O   TYR A 107      -7.650  54.591  31.831  1.00 67.98           O  
ANISOU  807  O   TYR A 107    11281   7511   7038    575   -737  -1842       O  
ATOM    808  CB  TYR A 107      -7.029  52.105  33.128  1.00 61.62           C  
ANISOU  808  CB  TYR A 107    10015   7276   6123    459   -568  -1803       C  
ATOM    809  CG  TYR A 107      -6.278  50.948  33.743  1.00 61.57           C  
ANISOU  809  CG  TYR A 107     9805   7497   6090    336   -488  -1773       C  
ATOM    810  CD1 TYR A 107      -4.980  50.641  33.342  1.00 61.45           C  
ANISOU  810  CD1 TYR A 107     9778   7423   6148    101   -440  -1695       C  
ATOM    811  CD2 TYR A 107      -6.844  50.189  34.765  1.00 62.55           C  
ANISOU  811  CD2 TYR A 107     9751   7901   6115    459   -465  -1824       C  
ATOM    812  CE1 TYR A 107      -4.262  49.614  33.949  1.00 58.31           C  
ANISOU  812  CE1 TYR A 107     9199   7230   5725      4   -376  -1675       C  
ATOM    813  CE2 TYR A 107      -6.148  49.132  35.351  1.00 61.79           C  
ANISOU  813  CE2 TYR A 107     9479   8005   5994    353   -398  -1790       C  
ATOM    814  CZ  TYR A 107      -4.860  48.848  34.937  1.00 61.78           C  
ANISOU  814  CZ  TYR A 107     9474   7932   6068    132   -357  -1718       C  
ATOM    815  OH  TYR A 107      -4.186  47.802  35.507  1.00 59.31           O  
ANISOU  815  OH  TYR A 107     8990   7818   5728     46   -297  -1686       O  
ATOM    816  N   SER A 108      -7.816  55.616  33.832  1.00 68.75           N  
ANISOU  816  N   SER A 108    11400   7628   7093    766   -874  -2163       N  
ATOM    817  CA  SER A 108      -8.615  56.772  33.396  1.00 70.94           C  
ANISOU  817  CA  SER A 108    11888   7674   7391    934   -973  -2213       C  
ATOM    818  C   SER A 108      -7.908  57.606  32.310  1.00 78.14           C  
ANISOU  818  C   SER A 108    13025   8238   8428    762  -1007  -2118       C  
ATOM    819  O   SER A 108      -6.705  57.443  32.084  1.00 77.48           O  
ANISOU  819  O   SER A 108    12936   8085   8418    510   -966  -2050       O  
ATOM    820  CB  SER A 108      -8.934  57.670  34.589  1.00 74.73           C  
ANISOU  820  CB  SER A 108    12429   8125   7839   1118  -1088  -2447       C  
ATOM    821  OG  SER A 108      -7.814  58.450  34.986  1.00 79.09           O  
ANISOU  821  OG  SER A 108    13098   8469   8483    964  -1157  -2543       O  
ATOM    822  N   SER A 109      -8.661  58.517  31.665  1.00 77.46           N  
ANISOU  822  N   SER A 109    13132   7939   8360    906  -1084  -2113       N  
ATOM    823  CA  SER A 109      -8.171  59.423  30.618  1.00 78.93           C  
ANISOU  823  CA  SER A 109    13558   7778   8655    779  -1128  -2016       C  
ATOM    824  C   SER A 109      -7.136  60.401  31.180  1.00 83.43           C  
ANISOU  824  C   SER A 109    14265   8108   9325    639  -1215  -2132       C  
ATOM    825  O   SER A 109      -6.142  60.696  30.506  1.00 83.11           O  
ANISOU  825  O   SER A 109    14323   7872   9383    394  -1200  -2024       O  
ATOM    826  CB  SER A 109      -9.333  60.182  29.986  1.00 84.94           C  
ANISOU  826  CB  SER A 109    14489   8387   9397   1011  -1207  -2010       C  
ATOM    827  OG  SER A 109     -10.104  59.293  29.193  1.00 97.08           O  
ANISOU  827  OG  SER A 109    15912  10114  10860   1082  -1122  -1868       O  
ATOM    828  N   GLU A 110      -7.364  60.873  32.429  1.00 80.46           N  
ANISOU  828  N   GLU A 110    13885   7767   8919    790  -1304  -2354       N  
ATOM    829  CA  GLU A 110      -6.456  61.744  33.177  1.00 81.56           C  
ANISOU  829  CA  GLU A 110    14130   7716   9141    680  -1400  -2504       C  
ATOM    830  C   GLU A 110      -5.118  61.023  33.375  1.00 82.00           C  
ANISOU  830  C   GLU A 110    14031   7892   9233    391  -1313  -2448       C  
ATOM    831  O   GLU A 110      -4.070  61.615  33.123  1.00 82.62           O  
ANISOU  831  O   GLU A 110    14222   7745   9426    161  -1344  -2424       O  
ATOM    832  CB  GLU A 110      -7.082  62.133  34.530  1.00 84.30           C  
ANISOU  832  CB  GLU A 110    14458   8159   9415    930  -1496  -2758       C  
ATOM    833  CG  GLU A 110      -6.332  63.225  35.273  1.00 98.13           C  
ANISOU  833  CG  GLU A 110    16361   9669  11253    859  -1626  -2942       C  
ATOM    834  N   THR A 111      -5.168  59.725  33.765  1.00 74.76           N  
ANISOU  834  N   THR A 111    12856   7329   8222    399  -1202  -2413       N  
ATOM    835  CA  THR A 111      -4.002  58.859  33.977  1.00 72.37           C  
ANISOU  835  CA  THR A 111    12378   7186   7935    159  -1112  -2354       C  
ATOM    836  C   THR A 111      -3.232  58.731  32.664  1.00 74.73           C  
ANISOU  836  C   THR A 111    12733   7341   8320    -87  -1039  -2141       C  
ATOM    837  O   THR A 111      -2.034  59.015  32.663  1.00 75.87           O  
ANISOU  837  O   THR A 111    12903   7373   8552   -324  -1044  -2132       O  
ATOM    838  CB  THR A 111      -4.429  57.511  34.572  1.00 77.50           C  
ANISOU  838  CB  THR A 111    12763   8223   8460    255  -1015  -2345       C  
ATOM    839  OG1 THR A 111      -5.232  57.771  35.726  1.00 74.07           O  
ANISOU  839  OG1 THR A 111    12296   7908   7938    495  -1088  -2540       O  
ATOM    840  CG2 THR A 111      -3.241  56.640  34.963  1.00 76.57           C  
ANISOU  840  CG2 THR A 111    12466   8276   8352     37   -936  -2306       C  
ATOM    841  N   ILE A 112      -3.929  58.394  31.537  1.00 68.53           N  
ANISOU  841  N   ILE A 112    11979   6551   7510    -27   -981  -1978       N  
ATOM    842  CA  ILE A 112      -3.350  58.330  30.196  1.00 66.77           C  
ANISOU  842  CA  ILE A 112    11826   6194   7351   -226   -915  -1771       C  
ATOM    843  C   ILE A 112      -2.589  59.650  29.939  1.00 73.03           C  
ANISOU  843  C   ILE A 112    12848   6632   8269   -384  -1006  -1786       C  
ATOM    844  O   ILE A 112      -1.415  59.597  29.603  1.00 73.85           O  
ANISOU  844  O   ILE A 112    12934   6684   8443   -646   -959  -1701       O  
ATOM    845  CB  ILE A 112      -4.463  58.027  29.124  1.00 68.63           C  
ANISOU  845  CB  ILE A 112    12098   6450   7528    -72   -878  -1637       C  
ATOM    846  CG1 ILE A 112      -4.745  56.520  29.035  1.00 66.01           C  
ANISOU  846  CG1 ILE A 112    11525   6451   7105    -46   -756  -1553       C  
ATOM    847  CG2 ILE A 112      -4.135  58.582  27.726  1.00 69.10           C  
ANISOU  847  CG2 ILE A 112    12343   6254   7657   -207   -869  -1461       C  
ATOM    848  CD1 ILE A 112      -6.170  56.144  28.805  1.00 71.84           C  
ANISOU  848  CD1 ILE A 112    12226   7319   7751    204   -755  -1544       C  
ATOM    849  N   LYS A 113      -3.225  60.810  30.174  1.00 71.26           N  
ANISOU  849  N   LYS A 113    12828   6174   8074   -228  -1138  -1903       N  
ATOM    850  CA  LYS A 113      -2.621  62.139  29.974  1.00 74.08           C  
ANISOU  850  CA  LYS A 113    13428   6161   8556   -361  -1243  -1926       C  
ATOM    851  C   LYS A 113      -1.321  62.335  30.773  1.00 79.18           C  
ANISOU  851  C   LYS A 113    14024   6781   9278   -590  -1269  -2026       C  
ATOM    852  O   LYS A 113      -0.322  62.760  30.189  1.00 80.38           O  
ANISOU  852  O   LYS A 113    14265   6742   9534   -850  -1264  -1926       O  
ATOM    853  CB  LYS A 113      -3.615  63.266  30.328  1.00 78.34           C  
ANISOU  853  CB  LYS A 113    14178   6485   9101   -106  -1393  -2076       C  
ATOM    854  CG  LYS A 113      -4.352  63.860  29.134  1.00 96.10           C  
ANISOU  854  CG  LYS A 113    16637   8509  11368    -12  -1422  -1938       C  
ATOM    855  CD  LYS A 113      -3.529  64.916  28.390  1.00111.01           C  
ANISOU  855  CD  LYS A 113    18767  10017  13394   -239  -1479  -1839       C  
ATOM    856  CE  LYS A 113      -4.033  65.110  26.977  1.00124.82           C  
ANISOU  856  CE  LYS A 113    20662  11622  15140   -212  -1453  -1626       C  
ATOM    857  NZ  LYS A 113      -3.181  66.047  26.200  1.00136.27           N  
ANISOU  857  NZ  LYS A 113    22330  12730  16718   -462  -1488  -1493       N  
ATOM    858  N   SER A 114      -1.322  61.998  32.089  1.00 74.72           N  
ANISOU  858  N   SER A 114    13310   6423   8658   -498  -1294  -2216       N  
ATOM    859  CA  SER A 114      -0.169  62.145  32.998  1.00 74.60           C  
ANISOU  859  CA  SER A 114    13228   6419   8697   -683  -1331  -2340       C  
ATOM    860  C   SER A 114       1.053  61.296  32.592  1.00 76.64           C  
ANISOU  860  C   SER A 114    13314   6824   8982   -970  -1206  -2192       C  
ATOM    861  O   SER A 114       2.175  61.628  32.977  1.00 77.66           O  
ANISOU  861  O   SER A 114    13430   6887   9189  -1185  -1239  -2247       O  
ATOM    862  CB  SER A 114      -0.564  61.815  34.437  1.00 76.41           C  
ANISOU  862  CB  SER A 114    13317   6884   8830   -488  -1373  -2559       C  
ATOM    863  OG  SER A 114      -0.794  60.432  34.641  1.00 78.69           O  
ANISOU  863  OG  SER A 114    13355   7541   9002   -417  -1249  -2499       O  
ATOM    864  N   TYR A 115       0.843  60.216  31.831  1.00 70.84           N  
ANISOU  864  N   TYR A 115    12445   6290   8183   -970  -1070  -2015       N  
ATOM    865  CA  TYR A 115       1.934  59.337  31.404  1.00 69.35           C  
ANISOU  865  CA  TYR A 115    12085   6259   8006  -1211   -947  -1876       C  
ATOM    866  C   TYR A 115       2.518  59.706  30.031  1.00 76.47           C  
ANISOU  866  C   TYR A 115    13107   6959   8990  -1427   -899  -1670       C  
ATOM    867  O   TYR A 115       3.497  59.076  29.617  1.00 75.93           O  
ANISOU  867  O   TYR A 115    12907   7010   8935  -1636   -798  -1554       O  
ATOM    868  CB  TYR A 115       1.454  57.874  31.400  1.00 66.41           C  
ANISOU  868  CB  TYR A 115    11488   6231   7514  -1093   -827  -1809       C  
ATOM    869  CG  TYR A 115       1.649  57.230  32.748  1.00 67.10           C  
ANISOU  869  CG  TYR A 115    11379   6578   7537  -1033   -831  -1960       C  
ATOM    870  CD1 TYR A 115       2.846  56.598  33.073  1.00 67.31           C  
ANISOU  870  CD1 TYR A 115    11236   6759   7579  -1229   -773  -1947       C  
ATOM    871  CD2 TYR A 115       0.685  57.352  33.744  1.00 68.93           C  
ANISOU  871  CD2 TYR A 115    11602   6896   7692   -781   -900  -2125       C  
ATOM    872  CE1 TYR A 115       3.062  56.071  34.340  1.00 65.08           C  
ANISOU  872  CE1 TYR A 115    10784   6707   7235  -1173   -786  -2085       C  
ATOM    873  CE2 TYR A 115       0.893  56.832  35.019  1.00 69.50           C  
ANISOU  873  CE2 TYR A 115    11503   7207   7698   -728   -908  -2263       C  
ATOM    874  CZ  TYR A 115       2.085  56.196  35.311  1.00 73.05           C  
ANISOU  874  CZ  TYR A 115    11793   7800   8164   -925   -853  -2241       C  
ATOM    875  OH  TYR A 115       2.263  55.641  36.547  1.00 74.57           O  
ANISOU  875  OH  TYR A 115    11816   8237   8280   -862   -860  -2365       O  
ATOM    876  N   GLN A 116       1.947  60.730  29.347  1.00 75.21           N  
ANISOU  876  N   GLN A 116    13195   6502   8880  -1375   -972  -1627       N  
ATOM    877  CA  GLN A 116       2.346  61.146  27.998  1.00 76.30           C  
ANISOU  877  CA  GLN A 116    13470   6439   9082  -1555   -930  -1418       C  
ATOM    878  C   GLN A 116       3.655  61.942  27.961  1.00 83.44           C  
ANISOU  878  C   GLN A 116    14450   7140  10114  -1860   -967  -1403       C  
ATOM    879  O   GLN A 116       3.754  63.041  28.518  1.00 85.81           O  
ANISOU  879  O   GLN A 116    14912   7194  10498  -1877  -1101  -1533       O  
ATOM    880  CB  GLN A 116       1.227  61.944  27.313  1.00 78.73           C  
ANISOU  880  CB  GLN A 116    14017   6509   9390  -1372  -1000  -1372       C  
ATOM    881  CG  GLN A 116       0.065  61.063  26.849  1.00 86.98           C  
ANISOU  881  CG  GLN A 116    14981   7755  10313  -1140   -929  -1299       C  
ATOM    882  CD  GLN A 116      -1.153  61.838  26.408  1.00104.21           C  
ANISOU  882  CD  GLN A 116    17376   9737  12481   -909  -1018  -1300       C  
ATOM    883  OE1 GLN A 116      -1.088  63.013  26.026  1.00103.75           O  
ANISOU  883  OE1 GLN A 116    17560   9353  12508   -954  -1109  -1277       O  
ATOM    884  NE2 GLN A 116      -2.292  61.170  26.400  1.00 91.36           N  
ANISOU  884  NE2 GLN A 116    15663   8303  10746   -659   -992  -1315       N  
ATOM    885  N   GLY A 117       4.633  61.365  27.269  1.00 80.12           N  
ANISOU  885  N   GLY A 117    13908   6829   9705  -2097   -848  -1242       N  
ATOM    886  CA  GLY A 117       5.954  61.942  27.054  1.00 82.33           C  
ANISOU  886  CA  GLY A 117    14217   6969  10095  -2419   -852  -1185       C  
ATOM    887  C   GLY A 117       6.863  61.922  28.259  1.00 88.83           C  
ANISOU  887  C   GLY A 117    14904   7886  10961  -2540   -898  -1359       C  
ATOM    888  O   GLY A 117       7.828  62.691  28.301  1.00 91.50           O  
ANISOU  888  O   GLY A 117    15306   8049  11409  -2788   -947  -1363       O  
ATOM    889  N   LYS A 118       6.569  61.046  29.243  1.00 84.14           N  
ANISOU  889  N   LYS A 118    14119   7571  10279  -2374   -883  -1500       N  
ATOM    890  CA  LYS A 118       7.336  60.938  30.489  1.00 84.89           C  
ANISOU  890  CA  LYS A 118    14070   7792  10391  -2450   -932  -1680       C  
ATOM    891  C   LYS A 118       8.211  59.680  30.481  1.00 90.14           C  
ANISOU  891  C   LYS A 118    14456   8789  11003  -2571   -797  -1607       C  
ATOM    892  O   LYS A 118       7.721  58.569  30.233  1.00 87.49           O  
ANISOU  892  O   LYS A 118    13986   8690  10565  -2430   -696  -1536       O  
ATOM    893  CB  LYS A 118       6.417  60.966  31.727  1.00 85.98           C  
ANISOU  893  CB  LYS A 118    14206   7997  10463  -2170  -1029  -1906       C  
ATOM    894  CG  LYS A 118       5.510  62.191  31.788  1.00 92.18           C  
ANISOU  894  CG  LYS A 118    15263   8467  11292  -2016  -1169  -2000       C  
ATOM    895  CD  LYS A 118       5.508  62.850  33.142  1.00 96.57           C  
ANISOU  895  CD  LYS A 118    15857   8966  11868  -1937  -1315  -2264       C  
ATOM    896  CE  LYS A 118       4.643  64.085  33.138  1.00110.46           C  
ANISOU  896  CE  LYS A 118    17896  10397  13675  -1779  -1458  -2358       C  
ATOM    897  NZ  LYS A 118       3.420  63.921  33.972  1.00119.16           N  
ANISOU  897  NZ  LYS A 118    18982  11630  14664  -1429  -1506  -2523       N  
ATOM    898  N   SER A 119       9.516  59.874  30.757  1.00 89.62           N  
ANISOU  898  N   SER A 119    14305   8735  11012  -2833   -803  -1626       N  
ATOM    899  CA  SER A 119      10.537  58.822  30.781  1.00 88.52           C  
ANISOU  899  CA  SER A 119    13905   8890  10838  -2974   -690  -1568       C  
ATOM    900  C   SER A 119      10.343  57.881  31.971  1.00 91.23           C  
ANISOU  900  C   SER A 119    14051   9527  11085  -2798   -691  -1719       C  
ATOM    901  O   SER A 119       9.763  58.301  32.978  1.00 91.91           O  
ANISOU  901  O   SER A 119    14197   9567  11157  -2643   -803  -1904       O  
ATOM    902  CB  SER A 119      11.926  59.451  30.835  1.00 94.02           C  
ANISOU  902  CB  SER A 119    14576   9502  11646  -3294   -719  -1572       C  
ATOM    903  OG  SER A 119      12.107  60.386  29.783  1.00103.79           O  
ANISOU  903  OG  SER A 119    16008  10452  12977  -3469   -726  -1430       O  
ATOM    904  N   LEU A 120      10.826  56.612  31.863  1.00 84.91           N  
ANISOU  904  N   LEU A 120    13019   9028  10214  -2815   -569  -1640       N  
ATOM    905  CA  LEU A 120      10.719  55.628  32.956  1.00 82.58           C  
ANISOU  905  CA  LEU A 120    12529   9024   9825  -2660   -562  -1757       C  
ATOM    906  C   LEU A 120      11.349  56.189  34.235  1.00 87.58           C  
ANISOU  906  C   LEU A 120    13125   9658  10494  -2722   -680  -1963       C  
ATOM    907  O   LEU A 120      12.451  56.755  34.192  1.00 89.26           O  
ANISOU  907  O   LEU A 120    13330   9788  10798  -2968   -711  -1974       O  
ATOM    908  CB  LEU A 120      11.363  54.268  32.597  1.00 80.55           C  
ANISOU  908  CB  LEU A 120    12038   9059   9508  -2711   -424  -1636       C  
ATOM    909  CG  LEU A 120      10.735  53.407  31.476  1.00 82.61           C  
ANISOU  909  CG  LEU A 120    12291   9390   9708  -2618   -303  -1454       C  
ATOM    910  CD1 LEU A 120      11.421  52.077  31.387  1.00 81.09           C  
ANISOU  910  CD1 LEU A 120    11866   9487   9460  -2652   -191  -1379       C  
ATOM    911  CD2 LEU A 120       9.272  53.132  31.722  1.00 82.78           C  
ANISOU  911  CD2 LEU A 120    12377   9425   9652  -2338   -324  -1491       C  
ATOM    912  N   GLY A 121      10.606  56.105  35.331  1.00 82.48           N  
ANISOU  912  N   GLY A 121    12468   9094   9776  -2501   -752  -2127       N  
ATOM    913  CA  GLY A 121      11.056  56.620  36.617  1.00 83.54           C  
ANISOU  913  CA  GLY A 121    12573   9245   9924  -2518   -873  -2343       C  
ATOM    914  C   GLY A 121      10.532  58.001  36.955  1.00 88.77           C  
ANISOU  914  C   GLY A 121    13471   9607  10649  -2469  -1022  -2490       C  
ATOM    915  O   GLY A 121      10.574  58.392  38.124  1.00 89.49           O  
ANISOU  915  O   GLY A 121    13556   9725  10723  -2400  -1133  -2698       O  
ATOM    916  N   THR A 122      10.035  58.757  35.940  1.00 85.42           N  
ANISOU  916  N   THR A 122    13263   8896  10296  -2494  -1030  -2388       N  
ATOM    917  CA  THR A 122       9.469  60.107  36.133  1.00 86.54           C  
ANISOU  917  CA  THR A 122    13659   8717  10506  -2433  -1176  -2514       C  
ATOM    918  C   THR A 122       8.092  59.965  36.788  1.00 86.07           C  
ANISOU  918  C   THR A 122    13637   8729  10335  -2090  -1217  -2632       C  
ATOM    919  O   THR A 122       7.699  60.781  37.629  1.00 87.68           O  
ANISOU  919  O   THR A 122    13957   8811  10545  -1972  -1352  -2833       O  
ATOM    920  CB  THR A 122       9.399  60.879  34.792  1.00 95.82           C  
ANISOU  920  CB  THR A 122    15045   9577  11783  -2564  -1164  -2344       C  
ATOM    921  OG1 THR A 122      10.670  60.819  34.146  1.00 96.19           O  
ANISOU  921  OG1 THR A 122    15012   9627  11909  -2876  -1096  -2206       O  
ATOM    922  CG2 THR A 122       8.987  62.341  34.962  1.00 98.07           C  
ANISOU  922  CG2 THR A 122    15606   9493  12162  -2541  -1327  -2468       C  
ATOM    923  N   MET A 123       7.389  58.898  36.406  1.00 77.12           N  
ANISOU  923  N   MET A 123    12396   7806   9099  -1935  -1098  -2510       N  
ATOM    924  CA  MET A 123       6.054  58.534  36.845  1.00 74.53           C  
ANISOU  924  CA  MET A 123    12065   7597   8654  -1623  -1101  -2571       C  
ATOM    925  C   MET A 123       6.070  57.176  37.543  1.00 75.34           C  
ANISOU  925  C   MET A 123    11909   8083   8633  -1530  -1015  -2573       C  
ATOM    926  O   MET A 123       7.001  56.406  37.294  1.00 73.86           O  
ANISOU  926  O   MET A 123    11562   8047   8454  -1698   -926  -2470       O  
ATOM    927  CB  MET A 123       5.146  58.462  35.610  1.00 75.63           C  
ANISOU  927  CB  MET A 123    12319   7627   8790  -1536  -1035  -2394       C  
ATOM    928  CG  MET A 123       4.702  59.800  35.087  1.00 81.44           C  
ANISOU  928  CG  MET A 123    13333   7997   9612  -1519  -1138  -2413       C  
ATOM    929  SD  MET A 123       3.781  60.779  36.300  1.00 87.53           S  
ANISOU  929  SD  MET A 123    14245   8661  10353  -1252  -1308  -2688       S  
ATOM    930  CE  MET A 123       2.204  59.983  36.279  1.00 82.31           C  
ANISOU  930  CE  MET A 123    13515   8217   9542   -917  -1241  -2652       C  
ATOM    931  N   PRO A 124       5.047  56.805  38.360  1.00 70.27           N  
ANISOU  931  N   PRO A 124    11216   7610   7873  -1263  -1031  -2673       N  
ATOM    932  CA  PRO A 124       5.052  55.463  38.969  1.00 68.34           C  
ANISOU  932  CA  PRO A 124    10731   7724   7512  -1184   -944  -2648       C  
ATOM    933  C   PRO A 124       5.071  54.352  37.921  1.00 70.71           C  
ANISOU  933  C   PRO A 124    10930   8138   7799  -1242   -797  -2418       C  
ATOM    934  O   PRO A 124       4.704  54.610  36.764  1.00 69.45           O  
ANISOU  934  O   PRO A 124    10895   7805   7690  -1267   -763  -2288       O  
ATOM    935  CB  PRO A 124       3.735  55.433  39.750  1.00 69.84           C  
ANISOU  935  CB  PRO A 124    10930   8021   7587   -885   -984  -2762       C  
ATOM    936  CG  PRO A 124       3.443  56.873  40.045  1.00 75.89           C  
ANISOU  936  CG  PRO A 124    11910   8517   8408   -828  -1129  -2935       C  
ATOM    937  CD  PRO A 124       3.848  57.562  38.777  1.00 72.26           C  
ANISOU  937  CD  PRO A 124    11619   7749   8086  -1018  -1128  -2809       C  
ATOM    938  N   PRO A 125       5.484  53.103  38.260  1.00 66.20           N  
ANISOU  938  N   PRO A 125    10140   7853   7159  -1257   -711  -2360       N  
ATOM    939  CA  PRO A 125       5.440  52.044  37.241  1.00 63.68           C  
ANISOU  939  CA  PRO A 125     9737   7629   6828  -1294   -580  -2153       C  
ATOM    940  C   PRO A 125       4.012  51.860  36.729  1.00 67.13           C  
ANISOU  940  C   PRO A 125    10247   8047   7212  -1094   -552  -2086       C  
ATOM    941  O   PRO A 125       3.058  51.932  37.513  1.00 67.83           O  
ANISOU  941  O   PRO A 125    10339   8212   7222   -888   -599  -2191       O  
ATOM    942  CB  PRO A 125       5.967  50.806  37.973  1.00 63.76           C  
ANISOU  942  CB  PRO A 125     9515   7948   6762  -1292   -521  -2144       C  
ATOM    943  CG  PRO A 125       6.660  51.324  39.176  1.00 69.12           C  
ANISOU  943  CG  PRO A 125    10156   8665   7441  -1334   -615  -2325       C  
ATOM    944  CD  PRO A 125       5.951  52.577  39.558  1.00 66.65           C  
ANISOU  944  CD  PRO A 125    10025   8158   7143  -1225   -732  -2477       C  
ATOM    945  N   HIS A 126       3.869  51.724  35.408  1.00 61.30           N  
ANISOU  945  N   HIS A 126     9575   7201   6516  -1158   -484  -1920       N  
ATOM    946  CA  HIS A 126       2.581  51.558  34.741  1.00 60.06           C  
ANISOU  946  CA  HIS A 126     9487   7015   6317   -991   -457  -1840       C  
ATOM    947  C   HIS A 126       2.762  51.024  33.375  1.00 62.75           C  
ANISOU  947  C   HIS A 126     9831   7324   6687  -1095   -360  -1647       C  
ATOM    948  O   HIS A 126       3.730  51.382  32.706  1.00 62.51           O  
ANISOU  948  O   HIS A 126     9847   7169   6736  -1296   -341  -1581       O  
ATOM    949  CB  HIS A 126       1.841  52.899  34.620  1.00 62.58           C  
ANISOU  949  CB  HIS A 126    10027   7078   6672   -895   -559  -1924       C  
ATOM    950  CG  HIS A 126       0.358  52.767  34.555  1.00 64.96           C  
ANISOU  950  CG  HIS A 126    10360   7424   6896   -651   -564  -1922       C  
ATOM    951  ND1 HIS A 126      -0.274  52.206  33.455  1.00 64.80           N  
ANISOU  951  ND1 HIS A 126    10347   7414   6860   -616   -489  -1761       N  
ATOM    952  CD2 HIS A 126      -0.576  53.128  35.463  1.00 66.79           C  
ANISOU  952  CD2 HIS A 126    10611   7705   7062   -435   -636  -2067       C  
ATOM    953  CE1 HIS A 126      -1.566  52.225  33.741  1.00 63.89           C  
ANISOU  953  CE1 HIS A 126    10246   7357   6672   -387   -518  -1810       C  
ATOM    954  NE2 HIS A 126      -1.794  52.753  34.946  1.00 65.45           N  
ANISOU  954  NE2 HIS A 126    10445   7588   6833   -269   -602  -1991       N  
ATOM    955  N   VAL A 127       1.759  50.257  32.911  1.00 59.83           N  
ANISOU  955  N   VAL A 127     9424   7056   6253   -955   -303  -1557       N  
ATOM    956  CA  VAL A 127       1.665  49.677  31.566  1.00 58.26           C  
ANISOU  956  CA  VAL A 127     9232   6841   6062  -1008   -215  -1379       C  
ATOM    957  C   VAL A 127       1.677  50.827  30.524  1.00 62.06           C  
ANISOU  957  C   VAL A 127     9928   7035   6618  -1083   -249  -1325       C  
ATOM    958  O   VAL A 127       2.231  50.646  29.449  1.00 61.62           O  
ANISOU  958  O   VAL A 127     9889   6927   6597  -1225   -183  -1190       O  
ATOM    959  CB  VAL A 127       0.436  48.715  31.453  1.00 60.85           C  
ANISOU  959  CB  VAL A 127     9484   7332   6304   -821   -173  -1325       C  
ATOM    960  CG1 VAL A 127      -0.893  49.413  31.730  1.00 61.87           C  
ANISOU  960  CG1 VAL A 127     9718   7393   6396   -614   -249  -1407       C  
ATOM    961  CG2 VAL A 127       0.398  47.984  30.125  1.00 59.54           C  
ANISOU  961  CG2 VAL A 127     9310   7173   6141   -876    -86  -1155       C  
ATOM    962  N   PHE A 128       1.174  52.030  30.900  1.00 59.99           N  
ANISOU  962  N   PHE A 128     9826   6587   6381   -997   -355  -1436       N  
ATOM    963  CA  PHE A 128       1.150  53.241  30.074  1.00 61.18           C  
ANISOU  963  CA  PHE A 128    10199   6440   6606  -1055   -407  -1398       C  
ATOM    964  C   PHE A 128       2.569  53.797  29.823  1.00 65.47           C  
ANISOU  964  C   PHE A 128    10781   6848   7246  -1323   -406  -1370       C  
ATOM    965  O   PHE A 128       2.803  54.418  28.783  1.00 64.71           O  
ANISOU  965  O   PHE A 128    10827   6553   7207  -1436   -399  -1258       O  
ATOM    966  CB  PHE A 128       0.286  54.331  30.743  1.00 64.39           C  
ANISOU  966  CB  PHE A 128    10757   6695   7014   -880   -533  -1551       C  
ATOM    967  CG  PHE A 128      -1.200  54.068  30.861  1.00 65.29           C  
ANISOU  967  CG  PHE A 128    10866   6901   7039   -611   -547  -1578       C  
ATOM    968  CD1 PHE A 128      -1.789  52.978  30.225  1.00 66.40           C  
ANISOU  968  CD1 PHE A 128    10899   7216   7115   -547   -456  -1452       C  
ATOM    969  CD2 PHE A 128      -2.018  54.924  31.584  1.00 69.00           C  
ANISOU  969  CD2 PHE A 128    11439   7286   7492   -422   -656  -1733       C  
ATOM    970  CE1 PHE A 128      -3.164  52.743  30.331  1.00 66.49           C  
ANISOU  970  CE1 PHE A 128    10893   7322   7046   -312   -472  -1476       C  
ATOM    971  CE2 PHE A 128      -3.397  54.696  31.671  1.00 70.96           C  
ANISOU  971  CE2 PHE A 128    11670   7639   7654   -173   -666  -1756       C  
ATOM    972  CZ  PHE A 128      -3.958  53.607  31.044  1.00 66.32           C  
ANISOU  972  CZ  PHE A 128    10964   7230   7005   -127   -573  -1624       C  
ATOM    973  N   ALA A 129       3.496  53.623  30.793  1.00 61.62           N  
ANISOU  973  N   ALA A 129    10170   6470   6774  -1423   -419  -1470       N  
ATOM    974  CA  ALA A 129       4.873  54.112  30.646  1.00 61.78           C  
ANISOU  974  CA  ALA A 129    10200   6388   6884  -1684   -420  -1452       C  
ATOM    975  C   ALA A 129       5.632  53.256  29.628  1.00 65.75           C  
ANISOU  975  C   ALA A 129    10595   7002   7386  -1842   -292  -1273       C  
ATOM    976  O   ALA A 129       6.355  53.796  28.791  1.00 67.28           O  
ANISOU  976  O   ALA A 129    10868   7047   7648  -2034   -271  -1174       O  
ATOM    977  CB  ALA A 129       5.581  54.105  31.986  1.00 62.43           C  
ANISOU  977  CB  ALA A 129    10167   6582   6972  -1729   -474  -1617       C  
ATOM    978  N   ILE A 130       5.439  51.923  29.680  1.00 60.35           N  
ANISOU  978  N   ILE A 130     9732   6576   6620  -1757   -207  -1228       N  
ATOM    979  CA  ILE A 130       6.025  50.953  28.751  1.00 58.97           C  
ANISOU  979  CA  ILE A 130     9445   6534   6428  -1861    -86  -1073       C  
ATOM    980  C   ILE A 130       5.551  51.270  27.314  1.00 63.78           C  
ANISOU  980  C   ILE A 130    10203   6986   7044  -1871    -48   -920       C  
ATOM    981  O   ILE A 130       6.361  51.219  26.377  1.00 65.53           O  
ANISOU  981  O   ILE A 130    10417   7189   7291  -2042     23   -796       O  
ATOM    982  CB  ILE A 130       5.645  49.501  29.195  1.00 59.39           C  
ANISOU  982  CB  ILE A 130     9308   6865   6391  -1721    -26  -1073       C  
ATOM    983  CG1 ILE A 130       6.403  49.088  30.498  1.00 59.43           C  
ANISOU  983  CG1 ILE A 130     9147   7048   6385  -1748    -47  -1194       C  
ATOM    984  CG2 ILE A 130       5.802  48.466  28.065  1.00 56.92           C  
ANISOU  984  CG2 ILE A 130     8919   6661   6047  -1760     89   -912       C  
ATOM    985  CD1 ILE A 130       7.986  48.858  30.362  1.00 66.57           C  
ANISOU  985  CD1 ILE A 130     9926   8035   7332  -1972      5  -1159       C  
ATOM    986  N   ALA A 131       4.249  51.629  27.162  1.00 58.47           N  
ANISOU  986  N   ALA A 131     9663   6211   6343  -1684    -99   -933       N  
ATOM    987  CA  ALA A 131       3.620  51.995  25.884  1.00 57.07           C  
ANISOU  987  CA  ALA A 131     9641   5883   6162  -1655    -82   -802       C  
ATOM    988  C   ALA A 131       4.178  53.304  25.369  1.00 65.68           C  
ANISOU  988  C   ALA A 131    10914   6702   7338  -1821   -125   -758       C  
ATOM    989  O   ALA A 131       4.406  53.415  24.174  1.00 67.68           O  
ANISOU  989  O   ALA A 131    11234   6885   7597  -1920    -67   -604       O  
ATOM    990  CB  ALA A 131       2.120  52.099  26.040  1.00 56.52           C  
ANISOU  990  CB  ALA A 131     9651   5783   6040  -1405   -140   -851       C  
ATOM    991  N   ASP A 132       4.421  54.285  26.264  1.00 65.12           N  
ANISOU  991  N   ASP A 132    10926   6483   7335  -1856   -228   -891       N  
ATOM    992  CA  ASP A 132       4.966  55.595  25.899  1.00 67.72           C  
ANISOU  992  CA  ASP A 132    11440   6528   7761  -2024   -287   -863       C  
ATOM    993  C   ASP A 132       6.430  55.494  25.505  1.00 72.66           C  
ANISOU  993  C   ASP A 132    11978   7191   8438  -2309   -214   -772       C  
ATOM    994  O   ASP A 132       6.839  56.182  24.576  1.00 73.51           O  
ANISOU  994  O   ASP A 132    12214   7121   8596  -2465   -200   -644       O  
ATOM    995  CB  ASP A 132       4.808  56.610  27.032  1.00 70.81           C  
ANISOU  995  CB  ASP A 132    11935   6758   8210  -1976   -427  -1052       C  
ATOM    996  CG  ASP A 132       4.798  58.033  26.515  1.00 87.19           C  
ANISOU  996  CG  ASP A 132    14271   8482  10374  -2050   -514  -1018       C  
ATOM    997  OD1 ASP A 132       3.767  58.449  25.949  1.00 89.96           O  
ANISOU  997  OD1 ASP A 132    14781   8697  10702  -1887   -548   -974       O  
ATOM    998  OD2 ASP A 132       5.839  58.713  26.626  1.00 91.85           O  
ANISOU  998  OD2 ASP A 132    14906   8932  11059  -2276   -548  -1027       O  
ATOM    999  N   LYS A 133       7.222  54.641  26.205  1.00 68.26           N  
ANISOU  999  N   LYS A 133    11200   6872   7864  -2376   -167   -833       N  
ATOM   1000  CA  LYS A 133       8.642  54.449  25.889  1.00 68.33           C  
ANISOU 1000  CA  LYS A 133    11092   6958   7911  -2635    -94   -757       C  
ATOM   1001  C   LYS A 133       8.748  53.862  24.487  1.00 69.51           C  
ANISOU 1001  C   LYS A 133    11221   7176   8014  -2684     29   -557       C  
ATOM   1002  O   LYS A 133       9.603  54.284  23.718  1.00 70.09           O  
ANISOU 1002  O   LYS A 133    11326   7173   8130  -2897     73   -440       O  
ATOM   1003  CB  LYS A 133       9.360  53.570  26.938  1.00 69.65           C  
ANISOU 1003  CB  LYS A 133    11021   7388   8056  -2655    -73   -867       C  
ATOM   1004  CG  LYS A 133      10.846  53.314  26.634  1.00 77.35           C  
ANISOU 1004  CG  LYS A 133    11848   8479   9063  -2907      6   -794       C  
ATOM   1005  CD  LYS A 133      11.481  52.344  27.623  1.00 85.38           C  
ANISOU 1005  CD  LYS A 133    12626   9769  10045  -2895     26   -895       C  
ATOM   1006  CE  LYS A 133      12.759  51.719  27.120  1.00 95.07           C  
ANISOU 1006  CE  LYS A 133    13675  11174  11271  -3083    129   -802       C  
ATOM   1007  NZ  LYS A 133      13.892  52.681  27.146  1.00111.59           N  
ANISOU 1007  NZ  LYS A 133    15784  13155  13459  -3349     97   -808       N  
ATOM   1008  N   ALA A 134       7.840  52.929  24.148  1.00 64.43           N  
ANISOU 1008  N   ALA A 134    10531   6670   7280  -2488     79   -520       N  
ATOM   1009  CA  ALA A 134       7.737  52.304  22.827  1.00 62.36           C  
ANISOU 1009  CA  ALA A 134    10258   6480   6957  -2490    185   -349       C  
ATOM   1010  C   ALA A 134       7.462  53.363  21.762  1.00 66.90           C  
ANISOU 1010  C   ALA A 134    11058   6801   7560  -2550    167   -223       C  
ATOM   1011  O   ALA A 134       8.220  53.446  20.796  1.00 66.55           O  
ANISOU 1011  O   ALA A 134    11016   6752   7519  -2724    244    -80       O  
ATOM   1012  CB  ALA A 134       6.647  51.251  22.830  1.00 60.80           C  
ANISOU 1012  CB  ALA A 134     9994   6438   6668  -2252    209   -362       C  
ATOM   1013  N   PHE A 135       6.443  54.225  21.976  1.00 65.68           N  
ANISOU 1013  N   PHE A 135    11093   6436   7428  -2413     62   -278       N  
ATOM   1014  CA  PHE A 135       6.131  55.309  21.037  1.00 68.09           C  
ANISOU 1014  CA  PHE A 135    11633   6474   7764  -2452     28   -163       C  
ATOM   1015  C   PHE A 135       7.296  56.308  20.905  1.00 74.21           C  
ANISOU 1015  C   PHE A 135    12485   7074   8640  -2731     13   -111       C  
ATOM   1016  O   PHE A 135       7.584  56.767  19.797  1.00 75.77           O  
ANISOU 1016  O   PHE A 135    12790   7157   8843  -2858     56     58       O  
ATOM   1017  CB  PHE A 135       4.845  56.057  21.437  1.00 70.67           C  
ANISOU 1017  CB  PHE A 135    12140   6612   8099  -2234    -96   -257       C  
ATOM   1018  CG  PHE A 135       4.542  57.204  20.498  1.00 74.58           C  
ANISOU 1018  CG  PHE A 135    12891   6817   8631  -2267   -142   -136       C  
ATOM   1019  CD1 PHE A 135       3.915  56.978  19.276  1.00 77.19           C  
ANISOU 1019  CD1 PHE A 135    13292   7150   8886  -2184    -90     18       C  
ATOM   1020  CD2 PHE A 135       4.947  58.502  20.803  1.00 78.84           C  
ANISOU 1020  CD2 PHE A 135    13600   7079   9278  -2395   -237   -169       C  
ATOM   1021  CE1 PHE A 135       3.682  58.032  18.387  1.00 80.19           C  
ANISOU 1021  CE1 PHE A 135    13910   7266   9293  -2218   -131    144       C  
ATOM   1022  CE2 PHE A 135       4.728  59.550  19.906  1.00 83.78           C  
ANISOU 1022  CE2 PHE A 135    14468   7425   9940  -2439   -279    -40       C  
ATOM   1023  CZ  PHE A 135       4.085  59.311  18.712  1.00 81.31           C  
ANISOU 1023  CZ  PHE A 135    14224   7125   9546  -2344   -225    119       C  
ATOM   1024  N   ARG A 136       7.940  56.660  22.022  1.00 71.18           N  
ANISOU 1024  N   ARG A 136    12046   6668   8330  -2826    -50   -254       N  
ATOM   1025  CA  ARG A 136       9.043  57.618  22.003  1.00 73.30           C  
ANISOU 1025  CA  ARG A 136    12377   6770   8705  -3103    -77   -222       C  
ATOM   1026  C   ARG A 136      10.280  57.036  21.300  1.00 77.62           C  
ANISOU 1026  C   ARG A 136    12757   7500   9235  -3332     57    -83       C  
ATOM   1027  O   ARG A 136      10.880  57.748  20.501  1.00 79.74           O  
ANISOU 1027  O   ARG A 136    13122   7627   9549  -3538     83     61       O  
ATOM   1028  CB  ARG A 136       9.403  58.094  23.412  1.00 72.65           C  
ANISOU 1028  CB  ARG A 136    12265   6639   8701  -3138   -187   -428       C  
ATOM   1029  CG  ARG A 136       8.341  58.957  24.099  1.00 76.72           C  
ANISOU 1029  CG  ARG A 136    12974   6928   9248  -2946   -334   -572       C  
ATOM   1030  CD  ARG A 136       8.844  59.574  25.402  1.00 79.51           C  
ANISOU 1030  CD  ARG A 136    13317   7210   9684  -3011   -450   -774       C  
ATOM   1031  NE  ARG A 136       9.851  58.757  26.091  1.00 80.69           N  
ANISOU 1031  NE  ARG A 136    13210   7629   9822  -3126   -395   -842       N  
ATOM   1032  CZ  ARG A 136       9.587  57.890  27.064  1.00 94.26           C  
ANISOU 1032  CZ  ARG A 136    14758   9584  11471  -2963   -395   -982       C  
ATOM   1033  NH1 ARG A 136      10.567  57.191  27.625  1.00 78.94           N  
ANISOU 1033  NH1 ARG A 136    12594   7877   9522  -3077   -348  -1028       N  
ATOM   1034  NH2 ARG A 136       8.341  57.717  27.489  1.00 82.20           N  
ANISOU 1034  NH2 ARG A 136    13281   8072   9881  -2685   -442  -1072       N  
ATOM   1035  N   ASP A 137      10.652  55.760  21.574  1.00 71.49           N  
ANISOU 1035  N   ASP A 137    11735   7037   8391  -3292    143   -120       N  
ATOM   1036  CA  ASP A 137      11.810  55.114  20.942  1.00 71.42           C  
ANISOU 1036  CA  ASP A 137    11547   7235   8353  -3476    273     -5       C  
ATOM   1037  C   ASP A 137      11.572  54.977  19.450  1.00 76.78           C  
ANISOU 1037  C   ASP A 137    12301   7909   8964  -3480    367    198       C  
ATOM   1038  O   ASP A 137      12.504  55.154  18.672  1.00 77.81           O  
ANISOU 1038  O   ASP A 137    12396   8067   9099  -3693    448    336       O  
ATOM   1039  CB  ASP A 137      12.112  53.734  21.552  1.00 71.28           C  
ANISOU 1039  CB  ASP A 137    11272   7540   8270  -3383    332    -94       C  
ATOM   1040  CG  ASP A 137      12.661  53.723  22.971  1.00 86.98           C  
ANISOU 1040  CG  ASP A 137    13137   9600  10311  -3419    263   -276       C  
ATOM   1041  OD1 ASP A 137      13.169  54.778  23.426  1.00 91.02           O  
ANISOU 1041  OD1 ASP A 137    13727   9937  10920  -3581    182   -330       O  
ATOM   1042  OD2 ASP A 137      12.608  52.649  23.619  1.00 90.81           O  
ANISOU 1042  OD2 ASP A 137    13447  10317  10739  -3290    286   -362       O  
ATOM   1043  N   MET A 138      10.313  54.689  19.055  1.00 72.49           N  
ANISOU 1043  N   MET A 138    11857   7334   8351  -3244    355    217       N  
ATOM   1044  CA  MET A 138       9.887  54.564  17.661  1.00 72.03           C  
ANISOU 1044  CA  MET A 138    11888   7265   8215  -3206    428    396       C  
ATOM   1045  C   MET A 138      10.077  55.885  16.914  1.00 80.28           C  
ANISOU 1045  C   MET A 138    13153   8034   9318  -3369    399    535       C  
ATOM   1046  O   MET A 138      10.565  55.882  15.789  1.00 81.43           O  
ANISOU 1046  O   MET A 138    13306   8214   9419  -3496    493    713       O  
ATOM   1047  CB  MET A 138       8.414  54.144  17.611  1.00 71.96           C  
ANISOU 1047  CB  MET A 138    11948   7257   8137  -2913    388    353       C  
ATOM   1048  CG  MET A 138       7.907  53.850  16.215  1.00 74.35           C  
ANISOU 1048  CG  MET A 138    12319   7587   8344  -2843    458    517       C  
ATOM   1049  SD  MET A 138       6.127  54.106  16.072  1.00 76.99           S  
ANISOU 1049  SD  MET A 138    12841   7772   8639  -2551    361    487       S  
ATOM   1050  CE  MET A 138       6.023  55.913  16.274  1.00 76.65           C  
ANISOU 1050  CE  MET A 138    13071   7343   8709  -2641    237    499       C  
ATOM   1051  N   LYS A 139       9.682  57.003  17.550  1.00 78.70           N  
ANISOU 1051  N   LYS A 139    13133   7559   9212  -3360    267    454       N  
ATOM   1052  CA  LYS A 139       9.734  58.351  16.998  1.00 81.39           C  
ANISOU 1052  CA  LYS A 139    13714   7588   9623  -3495    211    568       C  
ATOM   1053  C   LYS A 139      11.174  58.853  16.863  1.00 88.50           C  
ANISOU 1053  C   LYS A 139    14562   8463  10600  -3832    253    650       C  
ATOM   1054  O   LYS A 139      11.495  59.491  15.864  1.00 90.82           O  
ANISOU 1054  O   LYS A 139    14976   8631  10901  -3991    292    839       O  
ATOM   1055  CB  LYS A 139       8.913  59.296  17.900  1.00 84.68           C  
ANISOU 1055  CB  LYS A 139    14318   7734  10121  -3365     46    418       C  
ATOM   1056  CG  LYS A 139       8.683  60.704  17.345  1.00 96.34           C  
ANISOU 1056  CG  LYS A 139    16085   8848  11672  -3444    -38    525       C  
ATOM   1057  CD  LYS A 139       7.640  61.447  18.172  1.00105.82           C  
ANISOU 1057  CD  LYS A 139    17466   9816  12924  -3234   -198    363       C  
ATOM   1058  CE  LYS A 139       7.107  62.678  17.479  1.00117.91           C  
ANISOU 1058  CE  LYS A 139    19303  10995  14504  -3230   -283    477       C  
ATOM   1059  NZ  LYS A 139       5.845  63.159  18.104  1.00125.61           N  
ANISOU 1059  NZ  LYS A 139    20437  11800  15489  -2948   -424    325       N  
ATOM   1060  N   VAL A 140      12.026  58.592  17.871  1.00 84.77           N  
ANISOU 1060  N   VAL A 140    13911   8114  10183  -3941    244    512       N  
ATOM   1061  CA  VAL A 140      13.414  59.071  17.929  1.00 85.90           C  
ANISOU 1061  CA  VAL A 140    13977   8251  10410  -4264    269    557       C  
ATOM   1062  C   VAL A 140      14.344  58.156  17.109  1.00 88.58           C  
ANISOU 1062  C   VAL A 140    14099   8893  10663  -4391    438    694       C  
ATOM   1063  O   VAL A 140      15.039  58.662  16.235  1.00 90.44           O  
ANISOU 1063  O   VAL A 140    14374   9078  10909  -4612    502    874       O  
ATOM   1064  CB  VAL A 140      13.903  59.237  19.403  1.00 89.93           C  
ANISOU 1064  CB  VAL A 140    14390   8766  11012  -4314    173    336       C  
ATOM   1065  CG1 VAL A 140      15.383  59.609  19.472  1.00 91.78           C  
ANISOU 1065  CG1 VAL A 140    14506   9039  11326  -4652    204    375       C  
ATOM   1066  CG2 VAL A 140      13.067  60.275  20.149  1.00 90.76           C  
ANISOU 1066  CG2 VAL A 140    14727   8553  11203  -4206      3    203       C  
ATOM   1067  N   LEU A 141      14.357  56.831  17.376  1.00 82.44           N  
ANISOU 1067  N   LEU A 141    13097   8426   9799  -4249    508    613       N  
ATOM   1068  CA  LEU A 141      15.245  55.889  16.675  1.00 81.91           C  
ANISOU 1068  CA  LEU A 141    12812   8662   9647  -4339    662    716       C  
ATOM   1069  C   LEU A 141      14.737  55.485  15.260  1.00 83.74           C  
ANISOU 1069  C   LEU A 141    13108   8951   9759  -4246    762    896       C  
ATOM   1070  O   LEU A 141      15.430  54.734  14.562  1.00 82.64           O  
ANISOU 1070  O   LEU A 141    12805   9059   9537  -4309    891    989       O  
ATOM   1071  CB  LEU A 141      15.487  54.622  17.519  1.00 80.05           C  
ANISOU 1071  CB  LEU A 141    12325   8722   9368  -4215    690    560       C  
ATOM   1072  CG  LEU A 141      16.219  54.803  18.850  1.00 86.45           C  
ANISOU 1072  CG  LEU A 141    13012   9564  10271  -4320    618    391       C  
ATOM   1073  CD1 LEU A 141      15.596  53.937  19.928  1.00 84.76           C  
ANISOU 1073  CD1 LEU A 141    12701   9478  10025  -4075    567    205       C  
ATOM   1074  CD2 LEU A 141      17.708  54.502  18.711  1.00 90.81           C  
ANISOU 1074  CD2 LEU A 141    13340  10338  10827  -4558    713    441       C  
ATOM   1075  N   LYS A 142      13.541  55.975  14.848  1.00 79.56           N  
ANISOU 1075  N   LYS A 142    12811   8205   9213  -4087    698    939       N  
ATOM   1076  CA  LYS A 142      12.892  55.717  13.547  1.00 79.17           C  
ANISOU 1076  CA  LYS A 142    12853   8178   9049  -3976    768   1099       C  
ATOM   1077  C   LYS A 142      12.851  54.190  13.226  1.00 83.31           C  
ANISOU 1077  C   LYS A 142    13168   9037   9447  -3825    874   1078       C  
ATOM   1078  O   LYS A 142      13.030  53.774  12.080  1.00 84.53           O  
ANISOU 1078  O   LYS A 142    13293   9326   9500  -3840    982   1222       O  
ATOM   1079  CB  LYS A 142      13.577  56.530  12.427  1.00 82.85           C  
ANISOU 1079  CB  LYS A 142    13416   8551   9512  -4218    834   1325       C  
ATOM   1080  CG  LYS A 142      13.334  58.042  12.538  1.00 86.94           C  
ANISOU 1080  CG  LYS A 142    14193   8693  10146  -4330    718   1371       C  
ATOM   1081  CD  LYS A 142      14.282  58.858  11.676  1.00 96.97           C  
ANISOU 1081  CD  LYS A 142    15520   9885  11438  -4631    784   1585       C  
ATOM   1082  CE  LYS A 142      15.495  59.317  12.452  1.00111.35           C  
ANISOU 1082  CE  LYS A 142    17231  11694  13382  -4911    767   1531       C  
ATOM   1083  NZ  LYS A 142      16.320  60.285  11.674  1.00122.26           N  
ANISOU 1083  NZ  LYS A 142    18701  12946  14805  -5220    810   1746       N  
ATOM   1084  N   LEU A 143      12.566  53.379  14.253  1.00 78.14           N  
ANISOU 1084  N   LEU A 143    12382   8507   8800  -3670    836    895       N  
ATOM   1085  CA  LEU A 143      12.535  51.918  14.196  1.00 76.15           C  
ANISOU 1085  CA  LEU A 143    11934   8549   8453  -3525    914    847       C  
ATOM   1086  C   LEU A 143      11.270  51.393  14.880  1.00 76.90           C  
ANISOU 1086  C   LEU A 143    12055   8631   8531  -3251    833    709       C  
ATOM   1087  O   LEU A 143      10.927  51.854  15.970  1.00 76.66           O  
ANISOU 1087  O   LEU A 143    12068   8479   8580  -3207    729    576       O  
ATOM   1088  CB  LEU A 143      13.821  51.395  14.881  1.00 76.70           C  
ANISOU 1088  CB  LEU A 143    11762   8826   8554  -3668    962    772       C  
ATOM   1089  CG  LEU A 143      13.859  50.015  15.536  1.00 79.28           C  
ANISOU 1089  CG  LEU A 143    11879   9409   8836  -3514    988    643       C  
ATOM   1090  CD1 LEU A 143      14.457  48.993  14.598  1.00 79.10           C  
ANISOU 1090  CD1 LEU A 143    11706   9643   8707  -3516   1121    731       C  
ATOM   1091  CD2 LEU A 143      14.705  50.053  16.815  1.00 81.41           C  
ANISOU 1091  CD2 LEU A 143    12001   9742   9189  -3617    946    505       C  
ATOM   1092  N   SER A 144      10.582  50.425  14.234  1.00 70.71           N  
ANISOU 1092  N   SER A 144    11242   7982   7643  -3071    881    739       N  
ATOM   1093  CA  SER A 144       9.357  49.814  14.753  1.00 67.87           C  
ANISOU 1093  CA  SER A 144    10891   7640   7258  -2818    818    627       C  
ATOM   1094  C   SER A 144       9.594  49.174  16.105  1.00 69.33           C  
ANISOU 1094  C   SER A 144    10909   7947   7486  -2774    785    459       C  
ATOM   1095  O   SER A 144      10.733  48.868  16.480  1.00 67.95           O  
ANISOU 1095  O   SER A 144    10573   7909   7334  -2911    834    433       O  
ATOM   1096  CB  SER A 144       8.781  48.793  13.778  1.00 69.55           C  
ANISOU 1096  CB  SER A 144    11069   8004   7353  -2669    884    690       C  
ATOM   1097  OG  SER A 144       8.013  49.450  12.784  1.00 80.59           O  
ANISOU 1097  OG  SER A 144    12665   9246   8710  -2616    864    803       O  
ATOM   1098  N   GLN A 145       8.513  49.019  16.862  1.00 63.98           N  
ANISOU 1098  N   GLN A 145    10268   7223   6816  -2584    700    346       N  
ATOM   1099  CA  GLN A 145       8.616  48.520  18.209  1.00 61.83           C  
ANISOU 1099  CA  GLN A 145     9860   7052   6581  -2532    658    191       C  
ATOM   1100  C   GLN A 145       7.632  47.413  18.465  1.00 62.76           C  
ANISOU 1100  C   GLN A 145     9907   7301   6639  -2309    650    128       C  
ATOM   1101  O   GLN A 145       6.577  47.340  17.829  1.00 61.08           O  
ANISOU 1101  O   GLN A 145     9794   7036   6377  -2169    635    171       O  
ATOM   1102  CB  GLN A 145       8.384  49.673  19.199  1.00 63.65           C  
ANISOU 1102  CB  GLN A 145    10204   7080   6900  -2553    544     91       C  
ATOM   1103  CG  GLN A 145       9.378  50.842  19.071  1.00 64.76           C  
ANISOU 1103  CG  GLN A 145    10422   7065   7120  -2795    534    141       C  
ATOM   1104  CD  GLN A 145      10.742  50.507  19.616  1.00 78.29           C  
ANISOU 1104  CD  GLN A 145    11944   8935   8868  -2968    578     99       C  
ATOM   1105  OE1 GLN A 145      10.916  50.200  20.799  1.00 75.31           O  
ANISOU 1105  OE1 GLN A 145    11455   8643   8516  -2930    533    -43       O  
ATOM   1106  NE2 GLN A 145      11.749  50.587  18.772  1.00 68.92           N  
ANISOU 1106  NE2 GLN A 145    10714   7797   7677  -3162    665    222       N  
ATOM   1107  N  BSER A 146       7.976  46.552  19.418  1.00 58.23           N  
ANISOU 1107  N  BSER A 146     9159   6899   6069  -2278    656     28       N  
ATOM   1108  CA BSER A 146       7.082  45.484  19.836  1.00 56.35           C  
ANISOU 1108  CA BSER A 146     8844   6783   5783  -2081    642    -34       C  
ATOM   1109  C  BSER A 146       7.074  45.401  21.362  1.00 57.97           C  
ANISOU 1109  C  BSER A 146     8964   7035   6027  -2035    576   -177       C  
ATOM   1110  O  BSER A 146       8.095  45.644  22.015  1.00 58.81           O  
ANISOU 1110  O  BSER A 146     8991   7174   6179  -2163    574   -228       O  
ATOM   1111  CB BSER A 146       7.434  44.152  19.173  1.00 58.09           C  
ANISOU 1111  CB BSER A 146     8928   7204   5939  -2056    733     21       C  
ATOM   1112  OG BSER A 146       8.687  43.664  19.616  1.00 68.59           O  
ANISOU 1112  OG BSER A 146    10091   8684   7285  -2164    780     -9       O  
ATOM   1113  N   ILE A 147       5.886  45.146  21.918  1.00 51.22           N  
ANISOU 1113  N   ILE A 147     8131   6181   5150  -1852    519   -242       N  
ATOM   1114  CA  ILE A 147       5.643  44.983  23.344  1.00 50.26           C  
ANISOU 1114  CA  ILE A 147     7932   6123   5042  -1770    457   -372       C  
ATOM   1115  C   ILE A 147       5.133  43.534  23.531  1.00 53.26           C  
ANISOU 1115  C   ILE A 147     8178   6695   5364  -1634    489   -375       C  
ATOM   1116  O   ILE A 147       4.091  43.194  22.987  1.00 50.38           O  
ANISOU 1116  O   ILE A 147     7861   6321   4958  -1512    487   -335       O  
ATOM   1117  CB  ILE A 147       4.646  46.079  23.858  1.00 52.95           C  
ANISOU 1117  CB  ILE A 147     8425   6291   5403  -1673    357   -445       C  
ATOM   1118  CG1 ILE A 147       5.187  47.503  23.591  1.00 55.09           C  
ANISOU 1118  CG1 ILE A 147     8846   6344   5741  -1818    320   -433       C  
ATOM   1119  CG2 ILE A 147       4.313  45.879  25.334  1.00 50.72           C  
ANISOU 1119  CG2 ILE A 147     8057   6098   5115  -1569    297   -582       C  
ATOM   1120  CD1 ILE A 147       4.148  48.596  23.621  1.00 63.62           C  
ANISOU 1120  CD1 ILE A 147    10118   7218   6836  -1712    231   -464       C  
ATOM   1121  N   ILE A 148       5.906  42.676  24.232  1.00 51.08           N  
ANISOU 1121  N   ILE A 148     7734   6587   5085  -1664    517   -415       N  
ATOM   1122  CA  ILE A 148       5.551  41.271  24.453  1.00 49.66           C  
ANISOU 1122  CA  ILE A 148     7429   6579   4860  -1553    544   -411       C  
ATOM   1123  C   ILE A 148       4.999  41.172  25.860  1.00 54.04           C  
ANISOU 1123  C   ILE A 148     7930   7193   5409  -1449    479   -513       C  
ATOM   1124  O   ILE A 148       5.698  41.470  26.829  1.00 53.80           O  
ANISOU 1124  O   ILE A 148     7840   7199   5401  -1504    452   -591       O  
ATOM   1125  CB  ILE A 148       6.750  40.315  24.167  1.00 52.83           C  
ANISOU 1125  CB  ILE A 148     7688   7129   5255  -1638    619   -373       C  
ATOM   1126  CG1 ILE A 148       7.077  40.313  22.666  1.00 55.57           C  
ANISOU 1126  CG1 ILE A 148     8089   7439   5586  -1710    689   -266       C  
ATOM   1127  CG2 ILE A 148       6.480  38.872  24.608  1.00 48.91           C  
ANISOU 1127  CG2 ILE A 148     7064   6796   4724  -1526    633   -380       C  
ATOM   1128  CD1 ILE A 148       8.480  40.687  22.328  1.00 69.00           C  
ANISOU 1128  CD1 ILE A 148     9749   9156   7313  -1886    738   -240       C  
ATOM   1129  N   VAL A 149       3.702  40.845  25.946  1.00 50.30           N  
ANISOU 1129  N   VAL A 149     7483   6729   4900  -1299    452   -513       N  
ATOM   1130  CA  VAL A 149       2.952  40.731  27.198  1.00 50.22           C  
ANISOU 1130  CA  VAL A 149     7425   6789   4866  -1178    397   -597       C  
ATOM   1131  C   VAL A 149       2.787  39.236  27.489  1.00 53.21           C  
ANISOU 1131  C   VAL A 149     7662   7346   5209  -1113    431   -564       C  
ATOM   1132  O   VAL A 149       1.968  38.572  26.860  1.00 51.68           O  
ANISOU 1132  O   VAL A 149     7475   7169   4990  -1039    448   -504       O  
ATOM   1133  CB  VAL A 149       1.597  41.493  27.118  1.00 53.12           C  
ANISOU 1133  CB  VAL A 149     7917   7048   5217  -1056    340   -618       C  
ATOM   1134  CG1 VAL A 149       0.907  41.507  28.472  1.00 51.73           C  
ANISOU 1134  CG1 VAL A 149     7689   6957   5010   -936    284   -715       C  
ATOM   1135  CG2 VAL A 149       1.797  42.919  26.603  1.00 54.06           C  
ANISOU 1135  CG2 VAL A 149     8201   6963   5379  -1126    308   -626       C  
ATOM   1136  N   SER A 150       3.590  38.703  28.408  1.00 50.29           N  
ANISOU 1136  N   SER A 150     7167   7103   4839  -1144    437   -602       N  
ATOM   1137  CA  SER A 150       3.573  37.274  28.637  1.00 49.61           C  
ANISOU 1137  CA  SER A 150     6957   7168   4726  -1093    468   -560       C  
ATOM   1138  C   SER A 150       3.122  36.907  30.040  1.00 52.09           C  
ANISOU 1138  C   SER A 150     7185   7602   5004  -1001    429   -615       C  
ATOM   1139  O   SER A 150       3.001  37.762  30.912  1.00 52.09           O  
ANISOU 1139  O   SER A 150     7208   7588   4996   -980    379   -700       O  
ATOM   1140  CB  SER A 150       4.939  36.666  28.321  1.00 54.51           C  
ANISOU 1140  CB  SER A 150     7490   7856   5364  -1194    521   -530       C  
ATOM   1141  OG  SER A 150       5.957  37.158  29.170  1.00 64.22           O  
ANISOU 1141  OG  SER A 150     8664   9124   6611  -1270    502   -601       O  
ATOM   1142  N   GLY A 151       2.789  35.640  30.198  1.00 45.61           N  
ANISOU 1142  N   GLY A 151     6275   6895   4158   -940    449   -561       N  
ATOM   1143  CA  GLY A 151       2.314  35.096  31.445  1.00 45.01           C  
ANISOU 1143  CA  GLY A 151     6110   6953   4041   -854    422   -583       C  
ATOM   1144  C   GLY A 151       1.352  33.952  31.232  1.00 48.97           C  
ANISOU 1144  C   GLY A 151     6572   7513   4521   -777    436   -502       C  
ATOM   1145  O   GLY A 151       0.886  33.698  30.107  1.00 46.63           O  
ANISOU 1145  O   GLY A 151     6333   7144   4242   -777    456   -444       O  
ATOM   1146  N   GLU A 152       1.071  33.252  32.340  1.00 42.95           N  
ANISOU 1146  N   GLU A 152     5710   6888   3719   -717    422   -497       N  
ATOM   1147  CA  GLU A 152       0.184  32.117  32.434  1.00 42.42           C  
ANISOU 1147  CA  GLU A 152     5587   6898   3632   -654    428   -419       C  
ATOM   1148  C   GLU A 152      -1.218  32.508  32.066  1.00 46.70           C  
ANISOU 1148  C   GLU A 152     6189   7396   4157   -587    410   -412       C  
ATOM   1149  O   GLU A 152      -1.529  33.703  32.020  1.00 49.04           O  
ANISOU 1149  O   GLU A 152     6564   7621   4447   -567    385   -479       O  
ATOM   1150  CB  GLU A 152       0.161  31.663  33.920  1.00 45.30           C  
ANISOU 1150  CB  GLU A 152     5843   7424   3945   -604    410   -426       C  
ATOM   1151  CG  GLU A 152       1.206  30.623  34.240  1.00 62.14           C  
ANISOU 1151  CG  GLU A 152     7889   9633   6087   -639    428   -385       C  
ATOM   1152  CD  GLU A 152       1.069  30.082  35.646  1.00 81.79           C  
ANISOU 1152  CD  GLU A 152    10277  12285   8516   -582    410   -372       C  
ATOM   1153  OE1 GLU A 152       0.474  30.777  36.503  1.00 70.45           O  
ANISOU 1153  OE1 GLU A 152     8833  10910   7024   -526    384   -429       O  
ATOM   1154  OE2 GLU A 152       1.579  28.966  35.894  1.00 81.38           O  
ANISOU 1154  OE2 GLU A 152    10153  12300   8466   -586    420   -306       O  
ATOM   1155  N   SER A 153      -2.104  31.510  31.912  1.00 40.34           N  
ANISOU 1155  N   SER A 153     5342   6642   3345   -547    415   -335       N  
ATOM   1156  CA  SER A 153      -3.515  31.792  31.719  1.00 40.08           C  
ANISOU 1156  CA  SER A 153     5336   6606   3287   -476    394   -328       C  
ATOM   1157  C   SER A 153      -4.075  32.450  33.019  1.00 45.10           C  
ANISOU 1157  C   SER A 153     5930   7348   3859   -395    366   -392       C  
ATOM   1158  O   SER A 153      -3.882  31.926  34.116  1.00 43.96           O  
ANISOU 1158  O   SER A 153     5689   7337   3678   -380    367   -381       O  
ATOM   1159  CB  SER A 153      -4.266  30.513  31.369  1.00 40.75           C  
ANISOU 1159  CB  SER A 153     5368   6735   3380   -467    402   -231       C  
ATOM   1160  OG  SER A 153      -5.657  30.780  31.357  1.00 45.74           O  
ANISOU 1160  OG  SER A 153     5999   7400   3981   -396    379   -227       O  
ATOM   1161  N   GLY A 154      -4.765  33.584  32.868  1.00 42.67           N  
ANISOU 1161  N   GLY A 154     5697   6983   3534   -336    337   -458       N  
ATOM   1162  CA  GLY A 154      -5.320  34.314  34.000  1.00 42.49           C  
ANISOU 1162  CA  GLY A 154     5646   7052   3445   -243    306   -537       C  
ATOM   1163  C   GLY A 154      -4.384  35.386  34.518  1.00 47.76           C  
ANISOU 1163  C   GLY A 154     6367   7666   4115   -262    282   -647       C  
ATOM   1164  O   GLY A 154      -4.763  36.128  35.418  1.00 47.25           O  
ANISOU 1164  O   GLY A 154     6297   7659   3997   -179    248   -735       O  
ATOM   1165  N   ALA A 155      -3.149  35.504  33.943  1.00 44.19           N  
ANISOU 1165  N   ALA A 155     5963   7103   3723   -372    297   -649       N  
ATOM   1166  CA  ALA A 155      -2.163  36.469  34.451  1.00 43.26           C  
ANISOU 1166  CA  ALA A 155     5884   6936   3616   -415    272   -750       C  
ATOM   1167  C   ALA A 155      -2.517  37.942  34.172  1.00 48.58           C  
ANISOU 1167  C   ALA A 155     6692   7464   4301   -380    226   -840       C  
ATOM   1168  O   ALA A 155      -2.068  38.809  34.925  1.00 50.73           O  
ANISOU 1168  O   ALA A 155     6989   7722   4565   -377    186   -947       O  
ATOM   1169  CB  ALA A 155      -0.791  36.156  33.911  1.00 42.80           C  
ANISOU 1169  CB  ALA A 155     5826   6819   3617   -545    304   -718       C  
ATOM   1170  N   GLY A 156      -3.247  38.219  33.090  1.00 44.06           N  
ANISOU 1170  N   GLY A 156     6211   6778   3752   -357    227   -800       N  
ATOM   1171  CA  GLY A 156      -3.615  39.586  32.731  1.00 43.95           C  
ANISOU 1171  CA  GLY A 156     6338   6608   3752   -316    180   -872       C  
ATOM   1172  C   GLY A 156      -3.026  40.085  31.421  1.00 46.62           C  
ANISOU 1172  C   GLY A 156     6801   6753   4158   -419    193   -830       C  
ATOM   1173  O   GLY A 156      -3.022  41.306  31.171  1.00 44.08           O  
ANISOU 1173  O   GLY A 156     6612   6277   3862   -417    151   -888       O  
ATOM   1174  N   LYS A 157      -2.560  39.139  30.540  1.00 41.64           N  
ANISOU 1174  N   LYS A 157     6136   6130   3555   -506    251   -726       N  
ATOM   1175  CA  LYS A 157      -1.950  39.496  29.262  1.00 40.72           C  
ANISOU 1175  CA  LYS A 157     6122   5861   3489   -606    275   -675       C  
ATOM   1176  C   LYS A 157      -2.912  40.251  28.400  1.00 44.87           C  
ANISOU 1176  C   LYS A 157     6779   6258   4013   -538    246   -660       C  
ATOM   1177  O   LYS A 157      -2.551  41.304  27.881  1.00 45.93           O  
ANISOU 1177  O   LYS A 157     7041   6230   4181   -587    227   -675       O  
ATOM   1178  CB  LYS A 157      -1.421  38.287  28.466  1.00 42.56           C  
ANISOU 1178  CB  LYS A 157     6290   6143   3736   -681    339   -575       C  
ATOM   1179  CG  LYS A 157      -0.485  37.322  29.183  1.00 42.32           C  
ANISOU 1179  CG  LYS A 157     6124   6248   3707   -736    370   -570       C  
ATOM   1180  CD  LYS A 157      -0.102  36.225  28.188  1.00 40.06           C  
ANISOU 1180  CD  LYS A 157     5802   5982   3436   -788    425   -477       C  
ATOM   1181  CE  LYS A 157      -1.243  35.256  27.941  1.00 39.82           C  
ANISOU 1181  CE  LYS A 157     5735   6015   3381   -702    425   -419       C  
ATOM   1182  NZ  LYS A 157      -1.596  34.524  29.197  1.00 40.04           N  
ANISOU 1182  NZ  LYS A 157     5644   6191   3379   -642    411   -430       N  
ATOM   1183  N   THR A 158      -4.125  39.705  28.220  1.00 41.00           N  
ANISOU 1183  N   THR A 158     6255   5839   3483   -429    241   -626       N  
ATOM   1184  CA  THR A 158      -5.209  40.275  27.402  1.00 40.83           C  
ANISOU 1184  CA  THR A 158     6339   5728   3448   -339    209   -608       C  
ATOM   1185  C   THR A 158      -5.613  41.655  27.938  1.00 47.12           C  
ANISOU 1185  C   THR A 158     7236   6428   4237   -254    142   -707       C  
ATOM   1186  O   THR A 158      -5.648  42.595  27.157  1.00 46.64           O  
ANISOU 1186  O   THR A 158     7323   6199   4200   -256    116   -700       O  
ATOM   1187  CB  THR A 158      -6.375  39.275  27.335  1.00 44.95           C  
ANISOU 1187  CB  THR A 158     6766   6386   3927   -247    214   -562       C  
ATOM   1188  OG1 THR A 158      -5.935  38.115  26.614  1.00 44.27           O  
ANISOU 1188  OG1 THR A 158     6625   6338   3859   -331    266   -473       O  
ATOM   1189  CG2 THR A 158      -7.607  39.833  26.683  1.00 42.56           C  
ANISOU 1189  CG2 THR A 158     6544   6028   3599   -131    172   -559       C  
ATOM   1190  N   GLU A 159      -5.839  41.798  29.272  1.00 46.58           N  
ANISOU 1190  N   GLU A 159     7096   6464   4137   -181    112   -800       N  
ATOM   1191  CA  GLU A 159      -6.214  43.091  29.857  1.00 47.47           C  
ANISOU 1191  CA  GLU A 159     7304   6493   4240    -85     41   -913       C  
ATOM   1192  C   GLU A 159      -5.103  44.145  29.647  1.00 51.07           C  
ANISOU 1192  C   GLU A 159     7894   6749   4761   -199     18   -952       C  
ATOM   1193  O   GLU A 159      -5.394  45.245  29.186  1.00 51.48           O  
ANISOU 1193  O   GLU A 159     8101   6626   4835   -160    -33   -978       O  
ATOM   1194  CB  GLU A 159      -6.585  42.954  31.349  1.00 49.46           C  
ANISOU 1194  CB  GLU A 159     7440   6920   4433     13     19  -1008       C  
ATOM   1195  CG  GLU A 159      -7.945  42.307  31.585  1.00 55.73           C  
ANISOU 1195  CG  GLU A 159     8132   7887   5157    155     22   -985       C  
ATOM   1196  CD  GLU A 159      -9.079  42.741  30.668  1.00 71.82           C  
ANISOU 1196  CD  GLU A 159    10255   9848   7184    262     -7   -961       C  
ATOM   1197  OE1 GLU A 159      -9.381  43.957  30.603  1.00 68.35           O  
ANISOU 1197  OE1 GLU A 159     9949   9272   6750    346    -69  -1038       O  
ATOM   1198  OE2 GLU A 159      -9.660  41.855  30.001  1.00 55.35           O  
ANISOU 1198  OE2 GLU A 159     8108   7835   5088    262     26   -865       O  
ATOM   1199  N   ASN A 160      -3.842  43.784  29.888  1.00 47.14           N  
ANISOU 1199  N   ASN A 160     7339   6275   4298   -346     55   -943       N  
ATOM   1200  CA  ASN A 160      -2.725  44.706  29.698  1.00 48.86           C  
ANISOU 1200  CA  ASN A 160     7660   6323   4581   -480     38   -972       C  
ATOM   1201  C   ASN A 160      -2.475  45.057  28.237  1.00 52.39           C  
ANISOU 1201  C   ASN A 160     8233   6600   5072   -569     62   -869       C  
ATOM   1202  O   ASN A 160      -2.045  46.176  27.965  1.00 52.99           O  
ANISOU 1202  O   ASN A 160     8449   6487   5197   -633     24   -892       O  
ATOM   1203  CB  ASN A 160      -1.466  44.180  30.351  1.00 50.37           C  
ANISOU 1203  CB  ASN A 160     7735   6613   4790   -608     71   -989       C  
ATOM   1204  CG  ASN A 160      -1.490  44.476  31.814  1.00 63.60           C  
ANISOU 1204  CG  ASN A 160     9352   8380   6432   -537     19  -1122       C  
ATOM   1205  OD1 ASN A 160      -1.333  45.624  32.236  1.00 61.98           O  
ANISOU 1205  OD1 ASN A 160     9246   8053   6250   -530    -50  -1227       O  
ATOM   1206  ND2 ASN A 160      -1.757  43.462  32.610  1.00 49.57           N  
ANISOU 1206  ND2 ASN A 160     7420   6817   4596   -475     45  -1120       N  
ATOM   1207  N   THR A 161      -2.785  44.138  27.293  1.00 49.33           N  
ANISOU 1207  N   THR A 161     7805   6275   4664   -569    119   -757       N  
ATOM   1208  CA  THR A 161      -2.696  44.392  25.845  1.00 48.64           C  
ANISOU 1208  CA  THR A 161     7832   6052   4597   -629    145   -653       C  
ATOM   1209  C   THR A 161      -3.707  45.515  25.511  1.00 53.86           C  
ANISOU 1209  C   THR A 161     8655   6559   5252   -508     74   -676       C  
ATOM   1210  O   THR A 161      -3.337  46.512  24.876  1.00 54.22           O  
ANISOU 1210  O   THR A 161     8854   6412   5337   -574     53   -650       O  
ATOM   1211  CB  THR A 161      -2.914  43.092  25.081  1.00 57.05           C  
ANISOU 1211  CB  THR A 161     8804   7242   5631   -631    210   -554       C  
ATOM   1212  OG1 THR A 161      -1.835  42.212  25.389  1.00 55.23           O  
ANISOU 1212  OG1 THR A 161     8448   7122   5415   -744    267   -539       O  
ATOM   1213  CG2 THR A 161      -3.003  43.288  23.575  1.00 57.89           C  
ANISOU 1213  CG2 THR A 161     9021   7237   5736   -663    233   -451       C  
ATOM   1214  N   LYS A 162      -4.952  45.386  26.023  1.00 50.77           N  
ANISOU 1214  N   LYS A 162     8226   6254   4810   -332     33   -729       N  
ATOM   1215  CA  LYS A 162      -6.014  46.392  25.876  1.00 52.28           C  
ANISOU 1215  CA  LYS A 162     8550   6328   4985   -181    -42   -770       C  
ATOM   1216  C   LYS A 162      -5.576  47.757  26.411  1.00 58.39           C  
ANISOU 1216  C   LYS A 162     9461   6919   5807   -197   -112   -865       C  
ATOM   1217  O   LYS A 162      -5.839  48.773  25.764  1.00 60.72           O  
ANISOU 1217  O   LYS A 162     9931   7017   6124   -166   -161   -850       O  
ATOM   1218  CB  LYS A 162      -7.284  45.962  26.616  1.00 54.40           C  
ANISOU 1218  CB  LYS A 162     8715   6768   5188      5    -70   -830       C  
ATOM   1219  CG  LYS A 162      -8.013  44.792  25.986  1.00 71.07           C  
ANISOU 1219  CG  LYS A 162    10718   9029   7256     43    -24   -740       C  
ATOM   1220  CD  LYS A 162      -9.433  44.833  26.473  1.00 80.38           C  
ANISOU 1220  CD  LYS A 162    11848  10318   8374    239    -71   -794       C  
ATOM   1221  CE  LYS A 162     -10.142  43.539  26.261  1.00 81.52           C  
ANISOU 1221  CE  LYS A 162    11844  10651   8477    267    -30   -725       C  
ATOM   1222  NZ  LYS A 162      -9.883  42.590  27.371  1.00 68.93           N  
ANISOU 1222  NZ  LYS A 162    10075   9249   6866    230      9   -745       N  
ATOM   1223  N   PHE A 163      -4.889  47.786  27.575  1.00 52.44           N  
ANISOU 1223  N   PHE A 163     8634   6223   5068   -246   -121   -963       N  
ATOM   1224  CA  PHE A 163      -4.440  49.047  28.179  1.00 52.46           C  
ANISOU 1224  CA  PHE A 163     8757   6056   5118   -267   -197  -1073       C  
ATOM   1225  C   PHE A 163      -3.417  49.719  27.284  1.00 55.32           C  
ANISOU 1225  C   PHE A 163     9256   6205   5558   -451   -188   -998       C  
ATOM   1226  O   PHE A 163      -3.489  50.934  27.090  1.00 56.70           O  
ANISOU 1226  O   PHE A 163     9611   6157   5774   -438   -259  -1028       O  
ATOM   1227  CB  PHE A 163      -3.880  48.855  29.601  1.00 53.01           C  
ANISOU 1227  CB  PHE A 163     8705   6257   5180   -290   -207  -1192       C  
ATOM   1228  CG  PHE A 163      -4.820  48.203  30.585  1.00 53.36           C  
ANISOU 1228  CG  PHE A 163     8607   6529   5139   -118   -212  -1261       C  
ATOM   1229  CD1 PHE A 163      -6.171  48.526  30.603  1.00 56.30           C  
ANISOU 1229  CD1 PHE A 163     9019   6914   5459     84   -257  -1297       C  
ATOM   1230  CD2 PHE A 163      -4.348  47.282  31.513  1.00 54.00           C  
ANISOU 1230  CD2 PHE A 163     8511   6820   5188   -157   -171  -1284       C  
ATOM   1231  CE1 PHE A 163      -7.039  47.915  31.514  1.00 57.34           C  
ANISOU 1231  CE1 PHE A 163     9004   7277   5506    234   -254  -1351       C  
ATOM   1232  CE2 PHE A 163      -5.216  46.652  32.401  1.00 56.18           C  
ANISOU 1232  CE2 PHE A 163     8652   7314   5380     -9   -168  -1327       C  
ATOM   1233  CZ  PHE A 163      -6.555  46.985  32.412  1.00 55.18           C  
ANISOU 1233  CZ  PHE A 163     8558   7207   5201    182   -207  -1361       C  
ATOM   1234  N   VAL A 164      -2.495  48.926  26.724  1.00 50.99           N  
ANISOU 1234  N   VAL A 164     8622   5727   5025   -617   -101   -896       N  
ATOM   1235  CA  VAL A 164      -1.477  49.389  25.770  1.00 52.57           C  
ANISOU 1235  CA  VAL A 164     8919   5770   5286   -809    -70   -800       C  
ATOM   1236  C   VAL A 164      -2.150  50.000  24.560  1.00 56.61           C  
ANISOU 1236  C   VAL A 164     9600   6114   5794   -757    -87   -705       C  
ATOM   1237  O   VAL A 164      -1.862  51.157  24.233  1.00 57.75           O  
ANISOU 1237  O   VAL A 164     9918   6032   5993   -820   -136   -696       O  
ATOM   1238  CB  VAL A 164      -0.454  48.296  25.351  1.00 55.46           C  
ANISOU 1238  CB  VAL A 164     9141   6281   5651   -966     34   -708       C  
ATOM   1239  CG1 VAL A 164       0.442  48.782  24.209  1.00 55.76           C  
ANISOU 1239  CG1 VAL A 164     9278   6176   5734  -1145     75   -591       C  
ATOM   1240  CG2 VAL A 164       0.406  47.881  26.543  1.00 55.03           C  
ANISOU 1240  CG2 VAL A 164     8940   6359   5611  -1039     40   -801       C  
ATOM   1241  N   LEU A 165      -3.053  49.248  23.917  1.00 53.68           N  
ANISOU 1241  N   LEU A 165     9186   5850   5360   -642    -55   -637       N  
ATOM   1242  CA  LEU A 165      -3.739  49.706  22.711  1.00 55.51           C  
ANISOU 1242  CA  LEU A 165     9566   5950   5573   -581    -71   -541       C  
ATOM   1243  C   LEU A 165      -4.551  50.975  22.969  1.00 61.86           C  
ANISOU 1243  C   LEU A 165    10542   6569   6392   -439   -179   -616       C  
ATOM   1244  O   LEU A 165      -4.372  51.954  22.242  1.00 62.06           O  
ANISOU 1244  O   LEU A 165    10751   6374   6454   -488   -211   -554       O  
ATOM   1245  CB  LEU A 165      -4.635  48.603  22.115  1.00 54.84           C  
ANISOU 1245  CB  LEU A 165     9385   6038   5415   -471    -29   -477       C  
ATOM   1246  CG  LEU A 165      -3.937  47.312  21.651  1.00 58.77           C  
ANISOU 1246  CG  LEU A 165     9736   6699   5895   -590     72   -393       C  
ATOM   1247  CD1 LEU A 165      -4.958  46.274  21.244  1.00 59.07           C  
ANISOU 1247  CD1 LEU A 165     9686   6890   5866   -465     90   -357       C  
ATOM   1248  CD2 LEU A 165      -2.994  47.573  20.473  1.00 59.66           C  
ANISOU 1248  CD2 LEU A 165     9938   6702   6027   -756    126   -271       C  
ATOM   1249  N   ARG A 166      -5.381  50.982  24.041  1.00 59.80           N  
ANISOU 1249  N   ARG A 166    10223   6396   6101   -268   -236   -748       N  
ATOM   1250  CA  ARG A 166      -6.232  52.111  24.438  1.00 61.51           C  
ANISOU 1250  CA  ARG A 166    10582   6468   6321    -96   -344   -846       C  
ATOM   1251  C   ARG A 166      -5.382  53.346  24.746  1.00 68.75           C  
ANISOU 1251  C   ARG A 166    11657   7141   7323   -205   -406   -902       C  
ATOM   1252  O   ARG A 166      -5.752  54.450  24.335  1.00 70.12           O  
ANISOU 1252  O   ARG A 166    12030   7086   7524   -142   -483   -900       O  
ATOM   1253  CB  ARG A 166      -7.116  51.732  25.636  1.00 63.13           C  
ANISOU 1253  CB  ARG A 166    10653   6865   6466     92   -375   -982       C  
ATOM   1254  CG  ARG A 166      -8.130  52.802  26.036  1.00 85.28           C  
ANISOU 1254  CG  ARG A 166    13588   9558   9257    308   -485  -1093       C  
ATOM   1255  CD  ARG A 166      -9.144  52.269  27.036  1.00102.60           C  
ANISOU 1255  CD  ARG A 166    15624  11990  11368    506   -498  -1200       C  
ATOM   1256  NE  ARG A 166      -9.885  53.355  27.681  1.00112.64           N  
ANISOU 1256  NE  ARG A 166    17006  13165  12628    704   -606  -1344       N  
ATOM   1257  CZ  ARG A 166      -9.684  53.762  28.930  1.00122.62           C  
ANISOU 1257  CZ  ARG A 166    18251  14447  13893    747   -655  -1502       C  
ATOM   1258  NH1 ARG A 166     -10.397  54.764  29.430  1.00110.35           N  
ANISOU 1258  NH1 ARG A 166    16809  12797  12324    944   -758  -1637       N  
ATOM   1259  NH2 ARG A 166      -8.778  53.162  29.695  1.00100.54           N  
ANISOU 1259  NH2 ARG A 166    15322  11772  11105    606   -605  -1532       N  
ATOM   1260  N   TYR A 167      -4.240  53.157  25.456  1.00 64.24           N  
ANISOU 1260  N   TYR A 167    10999   6614   6795   -371   -378   -950       N  
ATOM   1261  CA  TYR A 167      -3.325  54.251  25.751  1.00 64.33           C  
ANISOU 1261  CA  TYR A 167    11142   6405   6895   -508   -436  -1003       C  
ATOM   1262  C   TYR A 167      -2.781  54.876  24.451  1.00 65.43           C  
ANISOU 1262  C   TYR A 167    11450   6321   7090   -664   -419   -849       C  
ATOM   1263  O   TYR A 167      -2.866  56.090  24.289  1.00 65.23           O  
ANISOU 1263  O   TYR A 167    11629   6035   7118   -654   -505   -864       O  
ATOM   1264  CB  TYR A 167      -2.163  53.784  26.648  1.00 64.40           C  
ANISOU 1264  CB  TYR A 167    10998   6540   6932   -669   -399  -1069       C  
ATOM   1265  CG  TYR A 167      -1.132  54.869  26.866  1.00 67.53           C  
ANISOU 1265  CG  TYR A 167    11520   6713   7427   -842   -457  -1115       C  
ATOM   1266  CD1 TYR A 167      -1.298  55.824  27.864  1.00 70.44           C  
ANISOU 1266  CD1 TYR A 167    11981   6956   7827   -763   -572  -1285       C  
ATOM   1267  CD2 TYR A 167      -0.029  54.991  26.022  1.00 68.80           C  
ANISOU 1267  CD2 TYR A 167    11717   6777   7648  -1084   -401   -985       C  
ATOM   1268  CE1 TYR A 167      -0.372  56.843  28.048  1.00 72.76           C  
ANISOU 1268  CE1 TYR A 167    12399   7026   8220   -931   -636  -1331       C  
ATOM   1269  CE2 TYR A 167       0.903  56.009  26.195  1.00 71.94           C  
ANISOU 1269  CE2 TYR A 167    12228   6964   8142  -1261   -457  -1018       C  
ATOM   1270  CZ  TYR A 167       0.730  56.928  27.216  1.00 81.02           C  
ANISOU 1270  CZ  TYR A 167    13471   7981   9333  -1188   -578  -1193       C  
ATOM   1271  OH  TYR A 167       1.636  57.935  27.398  1.00 86.25           O  
ANISOU 1271  OH  TYR A 167    14249   8423  10098  -1371   -643  -1232       O  
ATOM   1272  N   LEU A 168      -2.206  54.047  23.555  1.00 61.25           N  
ANISOU 1272  N   LEU A 168    10834   5896   6544   -805   -311   -701       N  
ATOM   1273  CA  LEU A 168      -1.603  54.468  22.277  1.00 62.89           C  
ANISOU 1273  CA  LEU A 168    11168   5944   6784   -967   -273   -535       C  
ATOM   1274  C   LEU A 168      -2.592  55.130  21.317  1.00 70.70           C  
ANISOU 1274  C   LEU A 168    12348   6767   7748   -832   -321   -453       C  
ATOM   1275  O   LEU A 168      -2.212  56.106  20.675  1.00 74.00           O  
ANISOU 1275  O   LEU A 168    12950   6947   8219   -935   -350   -370       O  
ATOM   1276  CB  LEU A 168      -0.911  53.305  21.550  1.00 61.08           C  
ANISOU 1276  CB  LEU A 168    10783   5905   6517  -1104   -143   -409       C  
ATOM   1277  CG  LEU A 168       0.353  52.715  22.210  1.00 64.52           C  
ANISOU 1277  CG  LEU A 168    11050   6478   6986  -1287    -83   -446       C  
ATOM   1278  CD1 LEU A 168       0.757  51.407  21.527  1.00 62.27           C  
ANISOU 1278  CD1 LEU A 168    10602   6411   6646  -1352     37   -340       C  
ATOM   1279  CD2 LEU A 168       1.529  53.723  22.226  1.00 65.65           C  
ANISOU 1279  CD2 LEU A 168    11295   6427   7224  -1512   -105   -431       C  
ATOM   1280  N   THR A 169      -3.830  54.620  21.195  1.00 66.84           N  
ANISOU 1280  N   THR A 169    11816   6401   7180   -613   -330   -466       N  
ATOM   1281  CA  THR A 169      -4.825  55.234  20.294  1.00 67.78           C  
ANISOU 1281  CA  THR A 169    12108   6379   7267   -465   -383   -393       C  
ATOM   1282  C   THR A 169      -5.356  56.544  20.884  1.00 74.68           C  
ANISOU 1282  C   THR A 169    13167   7021   8188   -335   -516   -505       C  
ATOM   1283  O   THR A 169      -5.527  57.508  20.143  1.00 77.22           O  
ANISOU 1283  O   THR A 169    13702   7103   8536   -325   -571   -427       O  
ATOM   1284  CB  THR A 169      -6.000  54.280  19.950  1.00 71.44           C  
ANISOU 1284  CB  THR A 169    12459   7055   7632   -272   -358   -376       C  
ATOM   1285  OG1 THR A 169      -6.756  53.964  21.126  1.00 73.27           O  
ANISOU 1285  OG1 THR A 169    12570   7434   7836   -103   -399   -533       O  
ATOM   1286  CG2 THR A 169      -5.552  53.014  19.231  1.00 63.23           C  
ANISOU 1286  CG2 THR A 169    11264   6216   6545   -386   -239   -263       C  
ATOM   1287  N   GLU A 170      -5.607  56.588  22.209  1.00 70.89           N  
ANISOU 1287  N   GLU A 170    12611   6610   7714   -231   -570   -687       N  
ATOM   1288  CA  GLU A 170      -6.135  57.777  22.875  1.00 72.79           C  
ANISOU 1288  CA  GLU A 170    13015   6651   7992    -84   -701   -822       C  
ATOM   1289  C   GLU A 170      -5.069  58.875  23.029  1.00 79.29           C  
ANISOU 1289  C   GLU A 170    14004   7194   8928   -276   -755   -836       C  
ATOM   1290  O   GLU A 170      -5.424  60.047  23.192  1.00 81.85           O  
ANISOU 1290  O   GLU A 170    14530   7269   9299   -181   -872   -904       O  
ATOM   1291  CB  GLU A 170      -6.706  57.399  24.241  1.00 73.58           C  
ANISOU 1291  CB  GLU A 170    12963   6946   8048     85   -733  -1012       C  
ATOM   1292  CG  GLU A 170      -7.863  58.250  24.723  1.00 84.88           C  
ANISOU 1292  CG  GLU A 170    14510   8284   9457    356   -854  -1146       C  
ATOM   1293  CD  GLU A 170      -8.522  57.675  25.960  1.00109.27           C  
ANISOU 1293  CD  GLU A 170    17413  11630  12475    528   -861  -1310       C  
ATOM   1294  OE1 GLU A 170      -9.089  56.562  25.872  1.00106.76           O  
ANISOU 1294  OE1 GLU A 170    16906  11582  12077    592   -786  -1268       O  
ATOM   1295  OE2 GLU A 170      -8.456  58.331  27.023  1.00105.27           O  
ANISOU 1295  OE2 GLU A 170    16950  11057  11992    595   -943  -1481       O  
ATOM   1296  N   SER A 171      -3.777  58.507  22.969  1.00 75.33           N  
ANISOU 1296  N   SER A 171    13419   6729   8473   -542   -676   -772       N  
ATOM   1297  CA  SER A 171      -2.676  59.461  23.122  1.00 77.13           C  
ANISOU 1297  CA  SER A 171    13776   6719   8813   -758   -719   -779       C  
ATOM   1298  C   SER A 171      -2.083  59.933  21.796  1.00 83.27           C  
ANISOU 1298  C   SER A 171    14702   7304   9632   -949   -682   -572       C  
ATOM   1299  O   SER A 171      -1.721  61.101  21.701  1.00 85.42           O  
ANISOU 1299  O   SER A 171    15178   7283   9994  -1042   -762   -562       O  
ATOM   1300  CB  SER A 171      -1.553  58.865  23.968  1.00 79.00           C  
ANISOU 1300  CB  SER A 171    13821   7119   9078   -940   -665   -853       C  
ATOM   1301  OG  SER A 171      -1.966  58.580  25.294  1.00 86.45           O  
ANISOU 1301  OG  SER A 171    14647   8212   9988   -784   -711  -1049       O  
ATOM   1302  N   TYR A 172      -1.918  59.039  20.806  1.00 79.48           N  
ANISOU 1302  N   TYR A 172    14122   6987   9090  -1020   -562   -407       N  
ATOM   1303  CA  TYR A 172      -1.265  59.413  19.551  1.00 81.31           C  
ANISOU 1303  CA  TYR A 172    14473   7075   9346  -1212   -512   -202       C  
ATOM   1304  C   TYR A 172      -2.156  59.179  18.318  1.00 88.17           C  
ANISOU 1304  C   TYR A 172    15410   7964  10125  -1076   -483    -55       C  
ATOM   1305  O   TYR A 172      -1.651  59.058  17.202  1.00 87.72           O  
ANISOU 1305  O   TYR A 172    15384   7898  10048  -1219   -405    127       O  
ATOM   1306  CB  TYR A 172       0.099  58.697  19.444  1.00 81.22           C  
ANISOU 1306  CB  TYR A 172    14288   7222   9351  -1481   -392   -134       C  
ATOM   1307  CG  TYR A 172       0.970  59.063  20.627  1.00 83.18           C  
ANISOU 1307  CG  TYR A 172    14487   7427   9689  -1617   -437   -278       C  
ATOM   1308  CD1 TYR A 172       1.397  60.374  20.820  1.00 87.63           C  
ANISOU 1308  CD1 TYR A 172    15248   7685  10361  -1732   -534   -301       C  
ATOM   1309  CD2 TYR A 172       1.232  58.140  21.638  1.00 81.63           C  
ANISOU 1309  CD2 TYR A 172    14062   7483   9469  -1600   -402   -411       C  
ATOM   1310  CE1 TYR A 172       2.122  60.743  21.951  1.00 89.44           C  
ANISOU 1310  CE1 TYR A 172    15438   7871  10673  -1840   -593   -456       C  
ATOM   1311  CE2 TYR A 172       1.961  58.498  22.776  1.00 83.09           C  
ANISOU 1311  CE2 TYR A 172    14204   7637   9728  -1701   -456   -559       C  
ATOM   1312  CZ  TYR A 172       2.407  59.803  22.926  1.00 92.04           C  
ANISOU 1312  CZ  TYR A 172    15529   8472  10969  -1822   -553   -586       C  
ATOM   1313  OH  TYR A 172       3.130  60.198  24.029  1.00 90.97           O  
ANISOU 1313  OH  TYR A 172    15357   8298  10907  -1927   -617   -741       O  
ATOM   1314  N   GLY A 173      -3.471  59.230  18.530  1.00 87.34           N  
ANISOU 1314  N   GLY A 173    15342   7877   9969   -799   -555   -137       N  
ATOM   1315  CA  GLY A 173      -4.473  59.113  17.480  1.00 88.28           C  
ANISOU 1315  CA  GLY A 173    15532   8007  10002   -632   -555    -27       C  
ATOM   1316  C   GLY A 173      -4.743  60.454  16.826  1.00 99.30           C  
ANISOU 1316  C   GLY A 173    17219   9073  11439   -601   -649     59       C  
ATOM   1317  O   GLY A 173      -4.171  61.476  17.223  1.00100.89           O  
ANISOU 1317  O   GLY A 173    17568   9025  11742   -708   -720     24       O  
ATOM   1318  N   THR A 174      -5.613  60.456  15.807  1.00 99.52           N  
ANISOU 1318  N   THR A 174    17332   9093  11387   -456   -656    174       N  
ATOM   1319  CA  THR A 174      -5.975  61.655  15.043  1.00103.11           C  
ANISOU 1319  CA  THR A 174    18069   9247  11863   -400   -744    282       C  
ATOM   1320  C   THR A 174      -7.055  62.479  15.770  1.00111.70           C  
ANISOU 1320  C   THR A 174    19285  10186  12972   -129   -894    124       C  
ATOM   1321  O   THR A 174      -7.193  63.676  15.507  1.00113.42           O  
ANISOU 1321  O   THR A 174    19757  10094  13243    -94   -995    163       O  
ATOM   1322  CB  THR A 174      -6.408  61.274  13.611  1.00108.05           C  
ANISOU 1322  CB  THR A 174    18725   9947  12382   -356   -687    475       C  
ATOM   1323  OG1 THR A 174      -7.152  60.047  13.628  1.00100.98           O  
ANISOU 1323  OG1 THR A 174    17615   9369  11385   -202   -636    420       O  
ATOM   1324  CG2 THR A 174      -5.217  61.151  12.657  1.00106.45           C  
ANISOU 1324  CG2 THR A 174    18529   9736  12181   -644   -575    673       C  
ATOM   1325  N   GLY A 175      -7.767  61.841  16.697  1.00109.78           N  
ANISOU 1325  N   GLY A 175    18866  10161  12685     55   -906    -52       N  
ATOM   1326  CA  GLY A 175      -8.837  62.461  17.471  1.00112.06           C  
ANISOU 1326  CA  GLY A 175    19229  10375  12974    334  -1035   -222       C  
ATOM   1327  C   GLY A 175     -10.204  61.974  17.040  1.00118.14           C  
ANISOU 1327  C   GLY A 175    19940  11319  13629    608  -1049   -217       C  
ATOM   1328  O   GLY A 175     -11.096  61.804  17.880  1.00117.21           O  
ANISOU 1328  O   GLY A 175    19733  11327  13475    833  -1102   -382       O  
ATOM   1329  N   GLN A 176     -10.369  61.740  15.714  1.00116.72           N  
ANISOU 1329  N   GLN A 176    19802  11160  13385    587  -1000    -26       N  
ATOM   1330  CA  GLN A 176     -11.599  61.231  15.103  1.00116.87           C  
ANISOU 1330  CA  GLN A 176    19764  11352  13291    819  -1008      4       C  
ATOM   1331  C   GLN A 176     -11.875  59.806  15.583  1.00120.64           C  
ANISOU 1331  C   GLN A 176    19936  12201  13702    844   -920    -75       C  
ATOM   1332  O   GLN A 176     -10.935  59.071  15.899  1.00118.84           O  
ANISOU 1332  O   GLN A 176    19558  12097  13499    633   -821    -73       O  
ATOM   1333  CB  GLN A 176     -11.506  61.276  13.571  1.00118.80           C  
ANISOU 1333  CB  GLN A 176    20127  11531  13483    754   -972    231       C  
ATOM   1334  N   ASP A 177     -13.165  59.420  15.619  1.00118.55           N  
ANISOU 1334  N   ASP A 177    19578  12112  13352   1099   -958   -141       N  
ATOM   1335  CA  ASP A 177     -13.677  58.125  16.089  1.00116.82           C  
ANISOU 1335  CA  ASP A 177    19080  12239  13068   1159   -895   -219       C  
ATOM   1336  C   ASP A 177     -13.053  56.889  15.387  1.00119.13           C  
ANISOU 1336  C   ASP A 177    19215  12726  13325    961   -763    -99       C  
ATOM   1337  O   ASP A 177     -13.317  55.762  15.821  1.00117.46           O  
ANISOU 1337  O   ASP A 177    18773  12781  13074    973   -706   -159       O  
ATOM   1338  CB  ASP A 177     -15.207  58.082  15.957  1.00119.30           C  
ANISOU 1338  CB  ASP A 177    19358  12677  13295   1458   -967   -269       C  
ATOM   1339  CG  ASP A 177     -15.922  59.020  16.909  1.00132.39           C  
ANISOU 1339  CG  ASP A 177    21093  14238  14971   1689  -1085   -434       C  
ATOM   1340  OD1 ASP A 177     -15.976  58.708  18.121  1.00132.74           O  
ANISOU 1340  OD1 ASP A 177    20988  14423  15025   1723  -1078   -589       O  
ATOM   1341  OD2 ASP A 177     -16.437  60.061  16.442  1.00139.54           O  
ANISOU 1341  OD2 ASP A 177    22208  14936  15873   1849  -1188   -410       O  
ATOM   1342  N   ILE A 178     -12.204  57.092  14.349  1.00115.37           N  
ANISOU 1342  N   ILE A 178    18858  12118  12861    778   -715     67       N  
ATOM   1343  CA  ILE A 178     -11.497  56.015  13.640  1.00113.07           C  
ANISOU 1343  CA  ILE A 178    18437  11991  12534    588   -591    179       C  
ATOM   1344  C   ILE A 178     -10.459  55.330  14.569  1.00114.04           C  
ANISOU 1344  C   ILE A 178    18389  12226  12716    396   -509    105       C  
ATOM   1345  O   ILE A 178     -10.139  54.154  14.357  1.00111.51           O  
ANISOU 1345  O   ILE A 178    17891  12118  12359    302   -415    136       O  
ATOM   1346  CB  ILE A 178     -10.824  56.561  12.363  1.00117.51           C  
ANISOU 1346  CB  ILE A 178    19184  12375  13090    448   -564    371       C  
ATOM   1347  N   ASP A 179      -9.948  56.074  15.596  1.00110.14           N  
ANISOU 1347  N   ASP A 179    17953  11584  12310    346   -552      4       N  
ATOM   1348  CA  ASP A 179      -8.973  55.601  16.596  1.00107.97           C  
ANISOU 1348  CA  ASP A 179    17534  11396  12095    179   -493    -81       C  
ATOM   1349  C   ASP A 179      -9.623  54.626  17.584  1.00107.24           C  
ANISOU 1349  C   ASP A 179    17214  11569  11964    303   -482   -218       C  
ATOM   1350  O   ASP A 179      -8.937  53.767  18.147  1.00105.96           O  
ANISOU 1350  O   ASP A 179    16879  11565  11816    175   -407   -253       O  
ATOM   1351  CB  ASP A 179      -8.353  56.777  17.383  1.00111.59           C  
ANISOU 1351  CB  ASP A 179    18135  11610  12653    110   -563   -160       C  
ATOM   1352  CG  ASP A 179      -7.878  57.976  16.579  1.00122.75           C  
ANISOU 1352  CG  ASP A 179    19806  12713  14119     14   -605    -40       C  
ATOM   1353  OD1 ASP A 179      -7.231  57.772  15.523  1.00122.08           O  
ANISOU 1353  OD1 ASP A 179    19750  12616  14019   -150   -528    128       O  
ATOM   1354  OD2 ASP A 179      -8.074  59.113  17.050  1.00131.56           O  
ANISOU 1354  OD2 ASP A 179    21095  13598  15296     90   -713   -115       O  
ATOM   1355  N   ASP A 180     -10.946  54.787  17.810  1.00100.66           N  
ANISOU 1355  N   ASP A 180    16382  10785  11081    553   -558   -294       N  
ATOM   1356  CA  ASP A 180     -11.744  53.951  18.702  1.00 97.31           C  
ANISOU 1356  CA  ASP A 180    15750  10614  10609    692   -555   -413       C  
ATOM   1357  C   ASP A 180     -11.868  52.515  18.184  1.00 93.73           C  
ANISOU 1357  C   ASP A 180    15104  10412  10096    641   -464   -340       C  
ATOM   1358  O   ASP A 180     -11.999  51.618  19.002  1.00 92.09           O  
ANISOU 1358  O   ASP A 180    14700  10416   9873    650   -428   -415       O  
ATOM   1359  CB  ASP A 180     -13.162  54.542  18.896  1.00100.46           C  
ANISOU 1359  CB  ASP A 180    16205  11005  10962    976   -660   -494       C  
ATOM   1360  CG  ASP A 180     -13.248  55.954  19.462  1.00115.90           C  
ANISOU 1360  CG  ASP A 180    18351  12719  12969   1079   -768   -593       C  
ATOM   1361  OD1 ASP A 180     -12.239  56.434  20.034  1.00117.01           O  
ANISOU 1361  OD1 ASP A 180    18549  12722  13186    934   -769   -638       O  
ATOM   1362  OD2 ASP A 180     -14.334  56.565  19.367  1.00124.55           O  
ANISOU 1362  OD2 ASP A 180    19531  13766  14026   1313   -858   -635       O  
ATOM   1363  N   ARG A 181     -11.833  52.301  16.847  1.00 85.98           N  
ANISOU 1363  N   ARG A 181    14183   9408   9079    592   -431   -196       N  
ATOM   1364  CA  ARG A 181     -12.019  51.001  16.180  1.00 81.91           C  
ANISOU 1364  CA  ARG A 181    13513   9106   8502    559   -359   -126       C  
ATOM   1365  C   ARG A 181     -10.989  49.932  16.546  1.00 81.11           C  
ANISOU 1365  C   ARG A 181    13247   9144   8428    367   -259   -125       C  
ATOM   1366  O   ARG A 181     -11.365  48.763  16.639  1.00 78.25           O  
ANISOU 1366  O   ARG A 181    12708   8995   8028    387   -221   -138       O  
ATOM   1367  CB  ARG A 181     -12.050  51.159  14.668  1.00 79.97           C  
ANISOU 1367  CB  ARG A 181    13394   8781   8210    539   -351     23       C  
ATOM   1368  CG  ARG A 181     -13.332  51.790  14.196  1.00 81.66           C  
ANISOU 1368  CG  ARG A 181    13711   8947   8370    765   -446     26       C  
ATOM   1369  CD  ARG A 181     -13.529  51.560  12.726  1.00 80.11           C  
ANISOU 1369  CD  ARG A 181    13574   8763   8100    766   -430    163       C  
ATOM   1370  NE  ARG A 181     -14.752  52.215  12.284  1.00 80.53           N  
ANISOU 1370  NE  ARG A 181    13731   8767   8099    993   -530    166       N  
ATOM   1371  CZ  ARG A 181     -15.185  52.240  11.031  1.00 83.26           C  
ANISOU 1371  CZ  ARG A 181    14156   9108   8369   1052   -548    274       C  
ATOM   1372  NH1 ARG A 181     -14.505  51.620  10.073  1.00 64.54           N  
ANISOU 1372  NH1 ARG A 181    11772   6786   5962    902   -469    387       N  
ATOM   1373  NH2 ARG A 181     -16.312  52.869  10.727  1.00 63.35           N  
ANISOU 1373  NH2 ARG A 181    11724   6545   5800   1272   -647    266       N  
ATOM   1374  N   ILE A 182      -9.713  50.309  16.747  1.00 77.40           N  
ANISOU 1374  N   ILE A 182    12829   8556   8023    184   -220   -108       N  
ATOM   1375  CA  ILE A 182      -8.656  49.369  17.162  1.00 75.92           C  
ANISOU 1375  CA  ILE A 182    12487   8496   7863      8   -130   -113       C  
ATOM   1376  C   ILE A 182      -9.028  48.808  18.574  1.00 77.42           C  
ANISOU 1376  C   ILE A 182    12506   8848   8060     82   -142   -250       C  
ATOM   1377  O   ILE A 182      -8.829  47.612  18.852  1.00 75.72           O  
ANISOU 1377  O   ILE A 182    12114   8823   7832     29    -81   -256       O  
ATOM   1378  CB  ILE A 182      -7.238  50.045  17.138  1.00 80.13           C  
ANISOU 1378  CB  ILE A 182    13118   8862   8467   -196    -99    -74       C  
ATOM   1379  CG1 ILE A 182      -6.875  50.613  15.742  1.00 81.42           C  
ANISOU 1379  CG1 ILE A 182    13449   8875   8614   -276    -81     78       C  
ATOM   1380  CG2 ILE A 182      -6.130  49.106  17.649  1.00 79.79           C  
ANISOU 1380  CG2 ILE A 182    12907   8958   8452   -365    -13    -91       C  
ATOM   1381  CD1 ILE A 182      -7.146  52.130  15.576  1.00 89.81           C  
ANISOU 1381  CD1 ILE A 182    14747   9668   9709   -218   -173     94       C  
ATOM   1382  N   VAL A 183      -9.629  49.679  19.423  1.00 72.31           N  
ANISOU 1382  N   VAL A 183    11919   8127   7427    218   -226   -357       N  
ATOM   1383  CA  VAL A 183     -10.081  49.353  20.778  1.00 70.52           C  
ANISOU 1383  CA  VAL A 183    11552   8050   7194    313   -247   -490       C  
ATOM   1384  C   VAL A 183     -11.409  48.590  20.696  1.00 73.37           C  
ANISOU 1384  C   VAL A 183    11791   8606   7482    479   -257   -497       C  
ATOM   1385  O   VAL A 183     -11.508  47.495  21.249  1.00 72.73           O  
ANISOU 1385  O   VAL A 183    11523   8731   7382    460   -210   -517       O  
ATOM   1386  CB  VAL A 183     -10.205  50.638  21.648  1.00 74.99           C  
ANISOU 1386  CB  VAL A 183    12240   8458   7794    404   -336   -608       C  
ATOM   1387  CG1 VAL A 183     -10.846  50.346  22.995  1.00 74.82           C  
ANISOU 1387  CG1 VAL A 183    12075   8612   7742    539   -362   -747       C  
ATOM   1388  CG2 VAL A 183      -8.857  51.315  21.831  1.00 75.17           C  
ANISOU 1388  CG2 VAL A 183    12362   8301   7897    217   -328   -609       C  
ATOM   1389  N   GLU A 184     -12.405  49.156  19.981  1.00 69.35           N  
ANISOU 1389  N   GLU A 184    11386   8031   6934    634   -320   -473       N  
ATOM   1390  CA  GLU A 184     -13.763  48.629  19.815  1.00 69.28           C  
ANISOU 1390  CA  GLU A 184    11277   8190   6855    806   -347   -482       C  
ATOM   1391  C   GLU A 184     -13.833  47.282  19.103  1.00 74.15           C  
ANISOU 1391  C   GLU A 184    11759   8975   7440    729   -281   -395       C  
ATOM   1392  O   GLU A 184     -14.904  46.687  19.107  1.00 75.01           O  
ANISOU 1392  O   GLU A 184    11754   9249   7498    845   -299   -408       O  
ATOM   1393  CB  GLU A 184     -14.647  49.633  19.064  1.00 72.14           C  
ANISOU 1393  CB  GLU A 184    11807   8417   7187    974   -432   -464       C  
ATOM   1394  N   ALA A 185     -12.732  46.796  18.502  1.00 70.67           N  
ANISOU 1394  N   ALA A 185    11327   8500   7027    539   -208   -312       N  
ATOM   1395  CA  ALA A 185     -12.719  45.509  17.797  1.00 69.83           C  
ANISOU 1395  CA  ALA A 185    11105   8536   6892    466   -149   -238       C  
ATOM   1396  C   ALA A 185     -12.481  44.341  18.744  1.00 72.80           C  
ANISOU 1396  C   ALA A 185    11280   9098   7284    399    -98   -282       C  
ATOM   1397  O   ALA A 185     -12.865  43.215  18.411  1.00 71.05           O  
ANISOU 1397  O   ALA A 185    10938   9021   7036    387    -72   -248       O  
ATOM   1398  CB  ALA A 185     -11.663  45.510  16.702  1.00 70.76           C  
ANISOU 1398  CB  ALA A 185    11321   8544   7021    311    -95   -133       C  
ATOM   1399  N   ASN A 186     -11.847  44.593  19.911  1.00 70.30           N  
ANISOU 1399  N   ASN A 186    10931   8772   7008    354    -87   -354       N  
ATOM   1400  CA  ASN A 186     -11.561  43.566  20.928  1.00 69.67           C  
ANISOU 1400  CA  ASN A 186    10669   8862   6940    295    -42   -394       C  
ATOM   1401  C   ASN A 186     -12.816  42.809  21.404  1.00 73.06           C  
ANISOU 1401  C   ASN A 186    10943   9491   7323    417    -62   -424       C  
ATOM   1402  O   ASN A 186     -12.743  41.585  21.412  1.00 71.86           O  
ANISOU 1402  O   ASN A 186    10659   9474   7171    348    -17   -387       O  
ATOM   1403  CB  ASN A 186     -10.815  44.139  22.141  1.00 71.48           C  
ANISOU 1403  CB  ASN A 186    10903   9049   7208    257    -45   -478       C  
ATOM   1404  CG  ASN A 186      -9.326  44.000  21.980  1.00 99.60           C  
ANISOU 1404  CG  ASN A 186    14489  12534  10819     67     14   -438       C  
ATOM   1405  OD1 ASN A 186      -8.662  44.841  21.365  1.00 99.85           O  
ANISOU 1405  OD1 ASN A 186    14669  12388  10880     -2     10   -404       O  
ATOM   1406  ND2 ASN A 186      -8.783  42.887  22.450  1.00 90.41           N  
ANISOU 1406  ND2 ASN A 186    13178  11509   9664    -24     72   -429       N  
ATOM   1407  N   PRO A 187     -13.967  43.441  21.763  1.00 70.96           N  
ANISOU 1407  N   PRO A 187    10686   9257   7020    592   -128   -485       N  
ATOM   1408  CA  PRO A 187     -15.127  42.640  22.204  1.00 70.07           C  
ANISOU 1408  CA  PRO A 187    10402   9361   6862    689   -138   -503       C  
ATOM   1409  C   PRO A 187     -15.583  41.643  21.156  1.00 69.85           C  
ANISOU 1409  C   PRO A 187    10315   9407   6816    654   -123   -418       C  
ATOM   1410  O   PRO A 187     -16.142  40.598  21.503  1.00 68.83           O  
ANISOU 1410  O   PRO A 187    10021   9456   6673    645   -106   -408       O  
ATOM   1411  CB  PRO A 187     -16.219  43.694  22.452  1.00 73.65           C  
ANISOU 1411  CB  PRO A 187    10910   9802   7272    892   -216   -575       C  
ATOM   1412  CG  PRO A 187     -15.471  44.937  22.755  1.00 79.34           C  
ANISOU 1412  CG  PRO A 187    11795  10324   8028    892   -242   -629       C  
ATOM   1413  CD  PRO A 187     -14.267  44.889  21.860  1.00 74.74           C  
ANISOU 1413  CD  PRO A 187    11319   9584   7496    714   -197   -545       C  
ATOM   1414  N   LEU A 188     -15.325  41.964  19.874  1.00 64.02           N  
ANISOU 1414  N   LEU A 188     9715   8531   6078    628   -131   -355       N  
ATOM   1415  CA  LEU A 188     -15.700  41.127  18.754  1.00 61.81           C  
ANISOU 1415  CA  LEU A 188     9406   8303   5775    601   -126   -283       C  
ATOM   1416  C   LEU A 188     -14.791  39.895  18.655  1.00 58.16           C  
ANISOU 1416  C   LEU A 188     8860   7890   5347    433    -55   -237       C  
ATOM   1417  O   LEU A 188     -15.315  38.788  18.598  1.00 56.65           O  
ANISOU 1417  O   LEU A 188     8540   7838   5148    419    -51   -220       O  
ATOM   1418  CB  LEU A 188     -15.715  41.932  17.452  1.00 63.66           C  
ANISOU 1418  CB  LEU A 188     9820   8381   5985    638   -157   -231       C  
ATOM   1419  CG  LEU A 188     -16.588  41.331  16.363  1.00 70.46           C  
ANISOU 1419  CG  LEU A 188    10650   9322   6798    686   -186   -183       C  
ATOM   1420  CD1 LEU A 188     -18.015  41.156  16.861  1.00 71.83           C  
ANISOU 1420  CD1 LEU A 188    10695   9660   6937    830   -242   -234       C  
ATOM   1421  CD2 LEU A 188     -16.527  42.154  15.068  1.00 73.37           C  
ANISOU 1421  CD2 LEU A 188    11205   9541   7132    725   -216   -123       C  
ATOM   1422  N   LEU A 189     -13.457  40.065  18.701  1.00 51.04           N  
ANISOU 1422  N   LEU A 189     8023   6883   4485    308     -4   -222       N  
ATOM   1423  CA  LEU A 189     -12.525  38.923  18.673  1.00 49.28           C  
ANISOU 1423  CA  LEU A 189     7719   6711   4293    164     62   -187       C  
ATOM   1424  C   LEU A 189     -12.710  38.002  19.887  1.00 51.13           C  
ANISOU 1424  C   LEU A 189     7779   7101   4545    149     78   -222       C  
ATOM   1425  O   LEU A 189     -12.603  36.775  19.766  1.00 49.44           O  
ANISOU 1425  O   LEU A 189     7466   6974   4344     80    105   -189       O  
ATOM   1426  CB  LEU A 189     -11.070  39.400  18.615  1.00 49.36           C  
ANISOU 1426  CB  LEU A 189     7820   6595   4340     43    111   -172       C  
ATOM   1427  CG  LEU A 189     -10.689  40.275  17.404  1.00 54.61           C  
ANISOU 1427  CG  LEU A 189     8659   7103   4989     26    109   -117       C  
ATOM   1428  CD1 LEU A 189      -9.345  40.959  17.632  1.00 55.74           C  
ANISOU 1428  CD1 LEU A 189     8880   7124   5173    -91    149   -113       C  
ATOM   1429  CD2 LEU A 189     -10.679  39.491  16.136  1.00 51.69           C  
ANISOU 1429  CD2 LEU A 189     8291   6764   4585     -8    130    -49       C  
ATOM   1430  N   GLU A 190     -12.992  38.609  21.054  1.00 46.26           N  
ANISOU 1430  N   GLU A 190     7133   6518   3926    218     57   -287       N  
ATOM   1431  CA  GLU A 190     -13.239  37.925  22.327  1.00 44.65           C  
ANISOU 1431  CA  GLU A 190     6769   6472   3723    223     69   -319       C  
ATOM   1432  C   GLU A 190     -14.561  37.165  22.324  1.00 48.44           C  
ANISOU 1432  C   GLU A 190     7124   7109   4171    294     42   -303       C  
ATOM   1433  O   GLU A 190     -14.628  36.096  22.915  1.00 48.14           O  
ANISOU 1433  O   GLU A 190     6949   7198   4143    241     67   -282       O  
ATOM   1434  CB  GLU A 190     -13.214  38.906  23.496  1.00 45.74           C  
ANISOU 1434  CB  GLU A 190     6921   6607   3853    293     50   -402       C  
ATOM   1435  CG  GLU A 190     -11.827  39.478  23.724  1.00 56.25           C  
ANISOU 1435  CG  GLU A 190     8339   7808   5225    195     78   -423       C  
ATOM   1436  CD  GLU A 190     -11.605  40.127  25.076  1.00 76.82           C  
ANISOU 1436  CD  GLU A 190    10926  10436   7826    236     63   -514       C  
ATOM   1437  OE1 GLU A 190     -12.542  40.140  25.907  1.00 60.37           O  
ANISOU 1437  OE1 GLU A 190     8755   8482   5700    351     37   -563       O  
ATOM   1438  OE2 GLU A 190     -10.478  40.614  25.310  1.00 68.76           O  
ANISOU 1438  OE2 GLU A 190     9971   9311   6842    150     78   -538       O  
ATOM   1439  N   ALA A 191     -15.598  37.683  21.663  1.00 45.60           N  
ANISOU 1439  N   ALA A 191     6808   6743   3774    407    -11   -308       N  
ATOM   1440  CA  ALA A 191     -16.844  36.923  21.579  1.00 47.13           C  
ANISOU 1440  CA  ALA A 191     6871   7096   3939    460    -39   -291       C  
ATOM   1441  C   ALA A 191     -16.623  35.552  20.861  1.00 51.25           C  
ANISOU 1441  C   ALA A 191     7334   7647   4491    337    -15   -223       C  
ATOM   1442  O   ALA A 191     -17.176  34.544  21.290  1.00 52.36           O  
ANISOU 1442  O   ALA A 191     7328   7929   4638    307    -13   -202       O  
ATOM   1443  CB  ALA A 191     -17.900  37.727  20.839  1.00 48.50           C  
ANISOU 1443  CB  ALA A 191     7111   7250   4067    601   -104   -306       C  
ATOM   1444  N   PHE A 192     -15.773  35.529  19.820  1.00 44.25           N  
ANISOU 1444  N   PHE A 192     6563   6629   3623    264      3   -190       N  
ATOM   1445  CA  PHE A 192     -15.533  34.362  18.968  1.00 42.64           C  
ANISOU 1445  CA  PHE A 192     6334   6430   3439    170     17   -140       C  
ATOM   1446  C   PHE A 192     -14.302  33.529  19.307  1.00 45.17           C  
ANISOU 1446  C   PHE A 192     6624   6731   3807     39     77   -120       C  
ATOM   1447  O   PHE A 192     -14.262  32.380  18.886  1.00 42.60           O  
ANISOU 1447  O   PHE A 192     6244   6438   3502    -26     81    -89       O  
ATOM   1448  CB  PHE A 192     -15.415  34.825  17.491  1.00 44.38           C  
ANISOU 1448  CB  PHE A 192     6697   6535   3630    187      0   -117       C  
ATOM   1449  CG  PHE A 192     -16.722  35.317  16.923  1.00 45.65           C  
ANISOU 1449  CG  PHE A 192     6872   6732   3740    314    -70   -126       C  
ATOM   1450  CD1 PHE A 192     -17.625  34.429  16.346  1.00 48.57           C  
ANISOU 1450  CD1 PHE A 192     7157   7201   4096    321   -110   -112       C  
ATOM   1451  CD2 PHE A 192     -17.076  36.660  17.013  1.00 48.03           C  
ANISOU 1451  CD2 PHE A 192     7268   6972   4009    430   -102   -152       C  
ATOM   1452  CE1 PHE A 192     -18.858  34.880  15.842  1.00 50.26           C  
ANISOU 1452  CE1 PHE A 192     7370   7467   4258    443   -180   -124       C  
ATOM   1453  CE2 PHE A 192     -18.313  37.110  16.539  1.00 52.09           C  
ANISOU 1453  CE2 PHE A 192     7788   7531   4472    564   -171   -163       C  
ATOM   1454  CZ  PHE A 192     -19.189  36.218  15.935  1.00 50.69           C  
ANISOU 1454  CZ  PHE A 192     7517   7467   4276    570   -208   -148       C  
ATOM   1455  N   GLY A 193     -13.311  34.106  20.010  1.00 42.03           N  
ANISOU 1455  N   GLY A 193     6265   6276   3428      6    117   -141       N  
ATOM   1456  CA  GLY A 193     -12.056  33.429  20.331  1.00 40.33           C  
ANISOU 1456  CA  GLY A 193     6025   6045   3255   -109    172   -125       C  
ATOM   1457  C   GLY A 193     -11.754  33.204  21.799  1.00 44.71           C  
ANISOU 1457  C   GLY A 193     6479   6682   3829   -130    195   -146       C  
ATOM   1458  O   GLY A 193     -10.772  32.529  22.120  1.00 43.71           O  
ANISOU 1458  O   GLY A 193     6315   6557   3734   -216    235   -131       O  
ATOM   1459  N   ASN A 194     -12.600  33.735  22.701  1.00 41.21           N  
ANISOU 1459  N   ASN A 194     5983   6317   3358    -42    167   -182       N  
ATOM   1460  CA  ASN A 194     -12.452  33.561  24.140  1.00 40.83           C  
ANISOU 1460  CA  ASN A 194     5834   6372   3309    -44    185   -204       C  
ATOM   1461  C   ASN A 194     -13.507  32.634  24.709  1.00 43.49           C  
ANISOU 1461  C   ASN A 194     6022   6872   3632    -22    171   -173       C  
ATOM   1462  O   ASN A 194     -14.632  32.551  24.190  1.00 45.05           O  
ANISOU 1462  O   ASN A 194     6194   7116   3808     33    133   -162       O  
ATOM   1463  CB  ASN A 194     -12.473  34.894  24.887  1.00 42.87           C  
ANISOU 1463  CB  ASN A 194     6143   6607   3540     38    169   -278       C  
ATOM   1464  CG  ASN A 194     -11.229  35.724  24.669  1.00 56.06           C  
ANISOU 1464  CG  ASN A 194     7938   8126   5236    -17    188   -305       C  
ATOM   1465  OD1 ASN A 194     -10.575  35.663  23.625  1.00 42.47           O  
ANISOU 1465  OD1 ASN A 194     6300   6297   3538    -86    207   -269       O  
ATOM   1466  ND2 ASN A 194     -10.874  36.520  25.649  1.00 48.05           N  
ANISOU 1466  ND2 ASN A 194     6936   7108   4214     10    183   -371       N  
ATOM   1467  N   ALA A 195     -13.130  31.914  25.767  1.00 37.94           N  
ANISOU 1467  N   ALA A 195     5216   6262   2939    -72    199   -154       N  
ATOM   1468  CA  ALA A 195     -14.035  30.982  26.418  1.00 39.64           C  
ANISOU 1468  CA  ALA A 195     5284   6637   3142    -71    193   -108       C  
ATOM   1469  C   ALA A 195     -13.708  30.808  27.889  1.00 44.18           C  
ANISOU 1469  C   ALA A 195     5764   7326   3696    -76    221   -109       C  
ATOM   1470  O   ALA A 195     -12.564  31.025  28.288  1.00 42.26           O  
ANISOU 1470  O   ALA A 195     5562   7028   3465   -112    247   -134       O  
ATOM   1471  CB  ALA A 195     -13.981  29.637  25.725  1.00 39.73           C  
ANISOU 1471  CB  ALA A 195     5263   6631   3203   -166    193    -36       C  
ATOM   1472  N   LYS A 196     -14.712  30.385  28.685  1.00 39.57           N  
ANISOU 1472  N   LYS A 196     5046   6914   3074    -43    216    -79       N  
ATOM   1473  CA  LYS A 196     -14.513  30.042  30.082  1.00 39.88           C  
ANISOU 1473  CA  LYS A 196     4980   7090   3082    -50    244    -60       C  
ATOM   1474  C   LYS A 196     -13.711  28.735  30.216  1.00 46.32           C  
ANISOU 1474  C   LYS A 196     5759   7889   3951   -171    269     23       C  
ATOM   1475  O   LYS A 196     -14.183  27.670  29.789  1.00 47.17           O  
ANISOU 1475  O   LYS A 196     5815   8011   4095   -235    259    101       O  
ATOM   1476  CB  LYS A 196     -15.861  29.910  30.808  1.00 42.30           C  
ANISOU 1476  CB  LYS A 196     5145   7600   3326     14    236    -37       C  
ATOM   1477  CG  LYS A 196     -15.744  29.747  32.326  1.00 43.57           C  
ANISOU 1477  CG  LYS A 196     5196   7927   3430     28    266    -23       C  
ATOM   1478  CD  LYS A 196     -16.999  29.112  32.881  1.00 34.75           C  
ANISOU 1478  CD  LYS A 196     3917   7017   2269     35    270     51       C  
ATOM   1479  CE  LYS A 196     -17.085  29.064  34.398  1.00 38.50           C  
ANISOU 1479  CE  LYS A 196     4272   7696   2660     75    302     64       C  
ATOM   1480  NZ  LYS A 196     -16.076  28.141  34.983  1.00 41.47           N  
ANISOU 1480  NZ  LYS A 196     4631   8061   3063    -25    331    137       N  
ATOM   1481  N   THR A 197     -12.484  28.831  30.780  1.00 42.51           N  
ANISOU 1481  N   THR A 197     5308   7369   3475   -200    295      1       N  
ATOM   1482  CA  THR A 197     -11.652  27.681  31.148  1.00 42.04           C  
ANISOU 1482  CA  THR A 197     5207   7312   3453   -289    317     73       C  
ATOM   1483  C   THR A 197     -11.593  27.655  32.683  1.00 47.36           C  
ANISOU 1483  C   THR A 197     5780   8149   4065   -261    336     83       C  
ATOM   1484  O   THR A 197     -11.945  28.660  33.294  1.00 46.98           O  
ANISOU 1484  O   THR A 197     5722   8177   3953   -173    333     11       O  
ATOM   1485  CB  THR A 197     -10.279  27.732  30.549  1.00 44.69           C  
ANISOU 1485  CB  THR A 197     5642   7499   3839   -341    330     45       C  
ATOM   1486  OG1 THR A 197      -9.598  28.820  31.175  1.00 45.54           O  
ANISOU 1486  OG1 THR A 197     5785   7606   3911   -301    341    -38       O  
ATOM   1487  CG2 THR A 197     -10.283  27.839  28.993  1.00 40.83           C  
ANISOU 1487  CG2 THR A 197     5259   6860   3396   -363    316     31       C  
ATOM   1488  N   VAL A 198     -11.088  26.573  33.305  1.00 45.35           N  
ANISOU 1488  N   VAL A 198     5463   7942   3826   -324    353    164       N  
ATOM   1489  CA  VAL A 198     -11.003  26.512  34.777  1.00 47.16           C  
ANISOU 1489  CA  VAL A 198     5595   8337   3984   -294    371    183       C  
ATOM   1490  C   VAL A 198     -10.046  27.593  35.338  1.00 50.45           C  
ANISOU 1490  C   VAL A 198     6063   8742   4363   -244    376     73       C  
ATOM   1491  O   VAL A 198     -10.314  28.097  36.410  1.00 49.70           O  
ANISOU 1491  O   VAL A 198     5907   8790   4186   -176    380     37       O  
ATOM   1492  CB  VAL A 198     -10.636  25.109  35.321  1.00 52.77           C  
ANISOU 1492  CB  VAL A 198     6236   9095   4717   -370    383    305       C  
ATOM   1493  CG1 VAL A 198     -11.762  24.117  35.073  1.00 52.54           C  
ANISOU 1493  CG1 VAL A 198     6135   9113   4712   -420    373    417       C  
ATOM   1494  CG2 VAL A 198      -9.325  24.593  34.726  1.00 52.84           C  
ANISOU 1494  CG2 VAL A 198     6325   8950   4803   -432    383    308       C  
ATOM   1495  N   ARG A 199      -9.000  28.014  34.576  1.00 48.05           N  
ANISOU 1495  N   ARG A 199     5868   8275   4114   -276    374     13       N  
ATOM   1496  CA  ARG A 199      -8.014  29.009  35.041  1.00 46.37           C  
ANISOU 1496  CA  ARG A 199     5703   8036   3878   -252    374    -90       C  
ATOM   1497  C   ARG A 199      -8.358  30.457  34.668  1.00 48.99           C  
ANISOU 1497  C   ARG A 199     6122   8298   4194   -186    352   -202       C  
ATOM   1498  O   ARG A 199      -7.739  31.370  35.201  1.00 49.57           O  
ANISOU 1498  O   ARG A 199     6231   8362   4242   -158    343   -295       O  
ATOM   1499  CB  ARG A 199      -6.633  28.675  34.500  1.00 41.23           C  
ANISOU 1499  CB  ARG A 199     5109   7264   3294   -332    385    -89       C  
ATOM   1500  CG  ARG A 199      -5.966  27.473  35.151  1.00 48.86           C  
ANISOU 1500  CG  ARG A 199     5998   8299   4266   -375    399     -7       C  
ATOM   1501  CD  ARG A 199      -4.894  26.955  34.196  1.00 57.34           C  
ANISOU 1501  CD  ARG A 199     7132   9237   5418   -447    409      8       C  
ATOM   1502  NE  ARG A 199      -3.942  26.007  34.784  1.00 63.92           N  
ANISOU 1502  NE  ARG A 199     7911  10115   6260   -476    417     59       N  
ATOM   1503  CZ  ARG A 199      -4.188  24.717  35.006  1.00 89.44           C  
ANISOU 1503  CZ  ARG A 199    11087  13388   9508   -493    414    167       C  
ATOM   1504  NH1 ARG A 199      -5.385  24.204  34.741  1.00 92.26           N  
ANISOU 1504  NH1 ARG A 199    11424  13759   9872   -496    406    237       N  
ATOM   1505  NH2 ARG A 199      -3.240  23.930  35.502  1.00 72.05           N  
ANISOU 1505  NH2 ARG A 199     8849  11213   7315   -508    416    209       N  
ATOM   1506  N   ASN A 200      -9.300  30.679  33.747  1.00 44.35           N  
ANISOU 1506  N   ASN A 200     5576   7653   3622   -160    339   -195       N  
ATOM   1507  CA  ASN A 200      -9.666  32.042  33.345  1.00 43.69           C  
ANISOU 1507  CA  ASN A 200     5587   7490   3524    -87    312   -293       C  
ATOM   1508  C   ASN A 200     -11.061  32.047  32.723  1.00 48.06           C  
ANISOU 1508  C   ASN A 200     6128   8067   4065    -30    294   -266       C  
ATOM   1509  O   ASN A 200     -11.332  31.306  31.781  1.00 47.95           O  
ANISOU 1509  O   ASN A 200     6121   8000   4097    -84    296   -196       O  
ATOM   1510  CB  ASN A 200      -8.607  32.643  32.385  1.00 40.34           C  
ANISOU 1510  CB  ASN A 200     5298   6869   3163   -147    311   -335       C  
ATOM   1511  CG  ASN A 200      -8.811  34.088  32.005  1.00 52.65           C  
ANISOU 1511  CG  ASN A 200     6972   8317   4714    -84    280   -428       C  
ATOM   1512  OD1 ASN A 200      -9.840  34.686  32.314  1.00 39.48           O  
ANISOU 1512  OD1 ASN A 200     5296   6708   2997     22    252   -471       O  
ATOM   1513  ND2 ASN A 200      -7.885  34.655  31.221  1.00 37.42           N  
ANISOU 1513  ND2 ASN A 200     5159   6222   2836   -148    282   -453       N  
ATOM   1514  N   ASN A 201     -11.951  32.872  33.271  1.00 44.84           N  
ANISOU 1514  N   ASN A 201     5697   7748   3590     86    272   -330       N  
ATOM   1515  CA  ASN A 201     -13.330  32.992  32.821  1.00 44.31           C  
ANISOU 1515  CA  ASN A 201     5602   7736   3499    161    250   -318       C  
ATOM   1516  C   ASN A 201     -13.393  33.559  31.432  1.00 47.68           C  
ANISOU 1516  C   ASN A 201     6161   7980   3973    164    225   -338       C  
ATOM   1517  O   ASN A 201     -14.318  33.229  30.696  1.00 47.70           O  
ANISOU 1517  O   ASN A 201     6144   7999   3981    179    209   -295       O  
ATOM   1518  CB  ASN A 201     -14.145  33.865  33.767  1.00 41.49           C  
ANISOU 1518  CB  ASN A 201     5195   7517   3051    304    232   -400       C  
ATOM   1519  CG  ASN A 201     -14.488  33.194  35.052  1.00 51.24           C  
ANISOU 1519  CG  ASN A 201     6272   8982   4217    318    259   -359       C  
ATOM   1520  OD1 ASN A 201     -14.447  31.977  35.185  1.00 52.52           O  
ANISOU 1520  OD1 ASN A 201     6344   9213   4397    225    288   -248       O  
ATOM   1521  ND2 ASN A 201     -14.815  33.980  36.028  1.00 41.45           N  
ANISOU 1521  ND2 ASN A 201     4998   7860   2891    437    249   -448       N  
ATOM   1522  N   ASN A 202     -12.423  34.424  31.087  1.00 42.76           N  
ANISOU 1522  N   ASN A 202     5672   7193   3381    147    218   -401       N  
ATOM   1523  CA  ASN A 202     -12.309  35.047  29.780  1.00 41.69           C  
ANISOU 1523  CA  ASN A 202     5679   6875   3287    140    198   -413       C  
ATOM   1524  C   ASN A 202     -11.040  34.578  29.044  1.00 43.33           C  
ANISOU 1524  C   ASN A 202     5952   6951   3561      7    228   -369       C  
ATOM   1525  O   ASN A 202     -10.321  35.396  28.461  1.00 43.15           O  
ANISOU 1525  O   ASN A 202     6055   6774   3566    -19    224   -404       O  
ATOM   1526  CB  ASN A 202     -12.324  36.572  29.919  1.00 42.59           C  
ANISOU 1526  CB  ASN A 202     5906   6898   3380    236    160   -519       C  
ATOM   1527  CG  ASN A 202     -12.499  37.231  28.592  1.00 51.75           C  
ANISOU 1527  CG  ASN A 202     7207   7889   4568    251    133   -515       C  
ATOM   1528  OD1 ASN A 202     -13.085  36.644  27.670  1.00 44.27           O  
ANISOU 1528  OD1 ASN A 202     6248   6945   3629    241    132   -449       O  
ATOM   1529  ND2 ASN A 202     -11.877  38.385  28.420  1.00 44.04           N  
ANISOU 1529  ND2 ASN A 202     6370   6752   3610    257    112   -577       N  
ATOM   1530  N   SER A 203     -10.779  33.268  29.030  1.00 37.94           N  
ANISOU 1530  N   SER A 203     5184   6327   2904    -77    258   -291       N  
ATOM   1531  CA  SER A 203      -9.544  32.791  28.439  1.00 38.31           C  
ANISOU 1531  CA  SER A 203     5279   6272   3006   -187    288   -259       C  
ATOM   1532  C   SER A 203      -9.497  32.953  26.937  1.00 43.66           C  
ANISOU 1532  C   SER A 203     6066   6811   3713   -213    283   -239       C  
ATOM   1533  O   SER A 203     -10.443  32.572  26.263  1.00 43.89           O  
ANISOU 1533  O   SER A 203     6084   6856   3737   -184    263   -204       O  
ATOM   1534  CB  SER A 203      -9.294  31.330  28.792  1.00 40.52           C  
ANISOU 1534  CB  SER A 203     5451   6638   3306   -255    313   -184       C  
ATOM   1535  OG  SER A 203      -8.043  30.941  28.244  1.00 40.64           O  
ANISOU 1535  OG  SER A 203     5512   6561   3368   -343    340   -168       O  
ATOM   1536  N   SER A 204      -8.368  33.478  26.416  1.00 41.52           N  
ANISOU 1536  N   SER A 204     5892   6415   3471   -274    303   -257       N  
ATOM   1537  CA  SER A 204      -8.097  33.601  24.978  1.00 41.71           C  
ANISOU 1537  CA  SER A 204     6020   6315   3515   -311    310   -229       C  
ATOM   1538  C   SER A 204      -7.695  32.239  24.452  1.00 45.90           C  
ANISOU 1538  C   SER A 204     6499   6869   4073   -381    336   -168       C  
ATOM   1539  O   SER A 204      -6.674  31.690  24.870  1.00 43.60           O  
ANISOU 1539  O   SER A 204     6162   6599   3804   -446    369   -161       O  
ATOM   1540  CB  SER A 204      -6.975  34.605  24.698  1.00 44.62           C  
ANISOU 1540  CB  SER A 204     6494   6559   3899   -365    328   -260       C  
ATOM   1541  OG  SER A 204      -7.092  35.784  25.469  1.00 50.92           O  
ANISOU 1541  OG  SER A 204     7332   7331   4683   -315    300   -330       O  
ATOM   1542  N   ARG A 205      -8.466  31.708  23.521  1.00 45.34           N  
ANISOU 1542  N   ARG A 205     6437   6791   3998   -363    318   -132       N  
ATOM   1543  CA  ARG A 205      -8.185  30.404  22.916  1.00 43.87           C  
ANISOU 1543  CA  ARG A 205     6215   6613   3839   -419    330    -85       C  
ATOM   1544  C   ARG A 205      -7.493  30.571  21.559  1.00 46.62           C  
ANISOU 1544  C   ARG A 205     6668   6858   4189   -455    351    -78       C  
ATOM   1545  O   ARG A 205      -7.416  29.630  20.766  1.00 46.94           O  
ANISOU 1545  O   ARG A 205     6705   6890   4241   -480    352    -51       O  
ATOM   1546  CB  ARG A 205      -9.469  29.553  22.844  1.00 42.70           C  
ANISOU 1546  CB  ARG A 205     5996   6538   3689   -387    290    -52       C  
ATOM   1547  CG  ARG A 205     -10.303  29.533  24.150  1.00 47.34           C  
ANISOU 1547  CG  ARG A 205     6477   7251   4260   -344    274    -51       C  
ATOM   1548  CD  ARG A 205      -9.550  29.247  25.452  1.00 42.32           C  
ANISOU 1548  CD  ARG A 205     5767   6682   3632   -374    303    -50       C  
ATOM   1549  NE  ARG A 205      -8.794  27.990  25.396  1.00 43.00           N  
ANISOU 1549  NE  ARG A 205     5814   6763   3761   -448    322     -5       N  
ATOM   1550  CZ  ARG A 205      -7.691  27.739  26.090  1.00 55.44           C  
ANISOU 1550  CZ  ARG A 205     7363   8351   5350   -487    352     -6       C  
ATOM   1551  NH1 ARG A 205      -7.191  28.656  26.911  1.00 43.66           N  
ANISOU 1551  NH1 ARG A 205     5875   6881   3834   -470    367    -53       N  
ATOM   1552  NH2 ARG A 205      -7.054  26.584  25.941  1.00 34.84           N  
ANISOU 1552  NH2 ARG A 205     4727   5730   2780   -538    362     34       N  
ATOM   1553  N   PHE A 206      -6.878  31.752  21.352  1.00 40.68           N  
ANISOU 1553  N   PHE A 206     6006   6027   3425   -465    370   -102       N  
ATOM   1554  CA  PHE A 206      -6.054  32.101  20.194  1.00 38.69           C  
ANISOU 1554  CA  PHE A 206     5850   5685   3166   -512    401    -87       C  
ATOM   1555  C   PHE A 206      -5.001  33.123  20.634  1.00 44.35           C  
ANISOU 1555  C   PHE A 206     6610   6348   3892   -564    432   -112       C  
ATOM   1556  O   PHE A 206      -5.239  33.909  21.567  1.00 45.47           O  
ANISOU 1556  O   PHE A 206     6752   6489   4037   -535    411   -151       O  
ATOM   1557  CB  PHE A 206      -6.910  32.680  19.024  1.00 39.91           C  
ANISOU 1557  CB  PHE A 206     6106   5776   3281   -457    371    -71       C  
ATOM   1558  CG  PHE A 206      -7.464  34.072  19.278  1.00 41.44           C  
ANISOU 1558  CG  PHE A 206     6377   5912   3457   -399    340    -94       C  
ATOM   1559  CD1 PHE A 206      -8.510  34.273  20.178  1.00 43.01           C  
ANISOU 1559  CD1 PHE A 206     6522   6170   3650   -318    296   -126       C  
ATOM   1560  CD2 PHE A 206      -6.903  35.184  18.661  1.00 42.83           C  
ANISOU 1560  CD2 PHE A 206     6679   5975   3622   -423    355    -85       C  
ATOM   1561  CE1 PHE A 206      -8.997  35.557  20.438  1.00 43.96           C  
ANISOU 1561  CE1 PHE A 206     6717   6234   3752   -247    263   -159       C  
ATOM   1562  CE2 PHE A 206      -7.412  36.466  18.900  1.00 45.85           C  
ANISOU 1562  CE2 PHE A 206     7145   6282   3993   -363    317   -109       C  
ATOM   1563  CZ  PHE A 206      -8.459  36.644  19.788  1.00 43.01           C  
ANISOU 1563  CZ  PHE A 206     6735   5979   3627   -267    269   -152       C  
ATOM   1564  N   GLY A 207      -3.876  33.159  19.939  1.00 41.08           N  
ANISOU 1564  N   GLY A 207     6235   5893   3482   -639    480    -94       N  
ATOM   1565  CA  GLY A 207      -2.860  34.159  20.239  1.00 41.09           C  
ANISOU 1565  CA  GLY A 207     6278   5837   3496   -707    507   -112       C  
ATOM   1566  C   GLY A 207      -2.956  35.278  19.237  1.00 44.85           C  
ANISOU 1566  C   GLY A 207     6894   6199   3949   -713    505    -86       C  
ATOM   1567  O   GLY A 207      -3.463  35.063  18.133  1.00 41.82           O  
ANISOU 1567  O   GLY A 207     6562   5796   3531   -679    501    -47       O  
ATOM   1568  N   LYS A 208      -2.543  36.493  19.607  1.00 44.21           N  
ANISOU 1568  N   LYS A 208     6880   6033   3883   -751    501   -106       N  
ATOM   1569  CA  LYS A 208      -2.622  37.563  18.604  1.00 45.62           C  
ANISOU 1569  CA  LYS A 208     7204   6087   4042   -763    498    -65       C  
ATOM   1570  C   LYS A 208      -1.441  38.516  18.669  1.00 52.22           C  
ANISOU 1570  C   LYS A 208     8095   6841   4906   -880    528    -61       C  
ATOM   1571  O   LYS A 208      -0.835  38.680  19.727  1.00 52.24           O  
ANISOU 1571  O   LYS A 208     8036   6865   4946   -927    528   -113       O  
ATOM   1572  CB  LYS A 208      -3.950  38.367  18.665  1.00 47.24           C  
ANISOU 1572  CB  LYS A 208     7495   6225   4230   -648    428    -82       C  
ATOM   1573  CG  LYS A 208      -4.195  39.169  19.929  1.00 57.14           C  
ANISOU 1573  CG  LYS A 208     8750   7449   5512   -611    382   -156       C  
ATOM   1574  CD  LYS A 208      -5.583  39.826  19.915  1.00 64.29           C  
ANISOU 1574  CD  LYS A 208     9726   8310   6391   -472    313   -176       C  
ATOM   1575  CE  LYS A 208      -5.876  40.579  21.198  1.00 87.31           C  
ANISOU 1575  CE  LYS A 208    12637  11214   9324   -412    265   -263       C  
ATOM   1576  NZ  LYS A 208      -6.131  39.669  22.364  1.00101.29           N  
ANISOU 1576  NZ  LYS A 208    14247  13146  11093   -380    267   -311       N  
ATOM   1577  N   PHE A 209      -1.137  39.141  17.512  1.00 48.44           N  
ANISOU 1577  N   PHE A 209     7727   6273   4404   -931    553      7       N  
ATOM   1578  CA  PHE A 209      -0.152  40.203  17.389  1.00 49.17           C  
ANISOU 1578  CA  PHE A 209     7896   6264   4523  -1053    578     31       C  
ATOM   1579  C   PHE A 209      -0.900  41.410  16.841  1.00 55.60           C  
ANISOU 1579  C   PHE A 209     8881   6921   5325  -1008    529     67       C  
ATOM   1580  O   PHE A 209      -1.423  41.330  15.746  1.00 55.23           O  
ANISOU 1580  O   PHE A 209     8901   6859   5225   -960    533    131       O  
ATOM   1581  CB  PHE A 209       1.047  39.804  16.511  1.00 50.13           C  
ANISOU 1581  CB  PHE A 209     7983   6438   4624  -1172    662     96       C  
ATOM   1582  CG  PHE A 209       2.215  40.764  16.603  1.00 52.17           C  
ANISOU 1582  CG  PHE A 209     8277   6624   4920  -1325    693    116       C  
ATOM   1583  CD1 PHE A 209       2.787  41.078  17.834  1.00 55.52           C  
ANISOU 1583  CD1 PHE A 209     8639   7050   5405  -1384    674     42       C  
ATOM   1584  CD2 PHE A 209       2.778  41.314  15.455  1.00 54.83           C  
ANISOU 1584  CD2 PHE A 209     8703   6902   5228  -1417    741    212       C  
ATOM   1585  CE1 PHE A 209       3.863  41.969  17.919  1.00 57.76           C  
ANISOU 1585  CE1 PHE A 209     8951   7265   5729  -1538    695     57       C  
ATOM   1586  CE2 PHE A 209       3.860  42.190  15.540  1.00 58.92           C  
ANISOU 1586  CE2 PHE A 209     9246   7355   5785  -1576    770    239       C  
ATOM   1587  CZ  PHE A 209       4.411  42.496  16.769  1.00 57.06           C  
ANISOU 1587  CZ  PHE A 209     8946   7115   5619  -1641    745    159       C  
ATOM   1588  N   VAL A 210      -1.102  42.454  17.658  1.00 52.93           N  
ANISOU 1588  N   VAL A 210     8610   6472   5029   -995    472     14       N  
ATOM   1589  CA  VAL A 210      -1.852  43.616  17.192  1.00 52.93           C  
ANISOU 1589  CA  VAL A 210     8782   6309   5021   -934    414     41       C  
ATOM   1590  C   VAL A 210      -0.890  44.731  16.932  1.00 57.22           C  
ANISOU 1590  C   VAL A 210     9436   6702   5602  -1077    428     87       C  
ATOM   1591  O   VAL A 210      -0.235  45.240  17.853  1.00 55.56           O  
ANISOU 1591  O   VAL A 210     9210   6449   5452  -1158    414     25       O  
ATOM   1592  CB  VAL A 210      -2.993  44.063  18.125  1.00 56.20           C  
ANISOU 1592  CB  VAL A 210     9217   6690   5446   -785    327    -50       C  
ATOM   1593  CG1 VAL A 210      -3.771  45.218  17.504  1.00 56.63           C  
ANISOU 1593  CG1 VAL A 210     9457   6572   5488   -707    265    -17       C  
ATOM   1594  CG2 VAL A 210      -3.925  42.907  18.426  1.00 54.81           C  
ANISOU 1594  CG2 VAL A 210     8916   6678   5233   -662    318    -83       C  
ATOM   1595  N   GLU A 211      -0.798  45.101  15.654  1.00 55.58           N  
ANISOU 1595  N   GLU A 211     9340   6421   5356  -1115    455    198       N  
ATOM   1596  CA  GLU A 211       0.075  46.182  15.216  1.00 57.34           C  
ANISOU 1596  CA  GLU A 211     9681   6495   5609  -1265    474    272       C  
ATOM   1597  C   GLU A 211      -0.683  47.491  15.043  1.00 63.02           C  
ANISOU 1597  C   GLU A 211    10602   7000   6344  -1199    391    292       C  
ATOM   1598  O   GLU A 211      -1.742  47.502  14.421  1.00 63.61           O  
ANISOU 1598  O   GLU A 211    10751   7053   6364  -1060    355    325       O  
ATOM   1599  CB  GLU A 211       0.739  45.819  13.888  1.00 58.65           C  
ANISOU 1599  CB  GLU A 211     9848   6720   5714  -1357    563    398       C  
ATOM   1600  CG  GLU A 211       1.685  44.642  13.970  1.00 62.57           C  
ANISOU 1600  CG  GLU A 211    10161   7412   6199  -1438    648    384       C  
ATOM   1601  CD  GLU A 211       2.120  44.186  12.597  1.00 71.70           C  
ANISOU 1601  CD  GLU A 211    11316   8651   7276  -1485    730    495       C  
ATOM   1602  OE1 GLU A 211       2.328  45.057  11.727  1.00 65.10           O  
ANISOU 1602  OE1 GLU A 211    10608   7709   6418  -1563    749    603       O  
ATOM   1603  OE2 GLU A 211       2.218  42.959  12.378  1.00 66.38           O  
ANISOU 1603  OE2 GLU A 211    10517   8145   6558  -1440    773    474       O  
ATOM   1604  N   ILE A 212      -0.133  48.586  15.576  1.00 59.97           N  
ANISOU 1604  N   ILE A 212    10303   6452   6032  -1298    356    270       N  
ATOM   1605  CA  ILE A 212      -0.669  49.931  15.373  1.00 61.43           C  
ANISOU 1605  CA  ILE A 212    10699   6399   6242  -1257    275    298       C  
ATOM   1606  C   ILE A 212       0.344  50.598  14.459  1.00 64.94           C  
ANISOU 1606  C   ILE A 212    11244   6731   6699  -1452    327    437       C  
ATOM   1607  O   ILE A 212       1.512  50.687  14.828  1.00 64.48           O  
ANISOU 1607  O   ILE A 212    11122   6681   6694  -1633    368    431       O  
ATOM   1608  CB  ILE A 212      -0.949  50.738  16.684  1.00 65.45           C  
ANISOU 1608  CB  ILE A 212    11256   6784   6827  -1204    177    159       C  
ATOM   1609  CG1 ILE A 212      -2.063  50.075  17.543  1.00 64.41           C  
ANISOU 1609  CG1 ILE A 212    11022   6785   6666   -996    129     33       C  
ATOM   1610  CG2 ILE A 212      -1.319  52.195  16.328  1.00 68.17           C  
ANISOU 1610  CG2 ILE A 212    11844   6853   7207  -1185     94    203       C  
ATOM   1611  CD1 ILE A 212      -2.500  50.888  18.812  1.00 71.86           C  
ANISOU 1611  CD1 ILE A 212    12017   7624   7663   -904     28   -112       C  
ATOM   1612  N   HIS A 213      -0.074  50.988  13.254  1.00 61.86           N  
ANISOU 1612  N   HIS A 213    10994   6259   6251  -1419    330    567       N  
ATOM   1613  CA  HIS A 213       0.818  51.589  12.268  1.00 63.63           C  
ANISOU 1613  CA  HIS A 213    11315   6390   6469  -1601    387    723       C  
ATOM   1614  C   HIS A 213       0.714  53.102  12.300  1.00 69.77           C  
ANISOU 1614  C   HIS A 213    12317   6877   7314  -1640    303    763       C  
ATOM   1615  O   HIS A 213      -0.353  53.649  12.605  1.00 69.78           O  
ANISOU 1615  O   HIS A 213    12436   6749   7327  -1467    201    704       O  
ATOM   1616  CB  HIS A 213       0.535  51.032  10.871  1.00 64.07           C  
ANISOU 1616  CB  HIS A 213    11383   6550   6408  -1554    449    853       C  
ATOM   1617  CG  HIS A 213       0.903  49.586  10.748  1.00 65.53           C  
ANISOU 1617  CG  HIS A 213    11357   7004   6537  -1559    539    825       C  
ATOM   1618  ND1 HIS A 213       2.008  49.184  10.028  1.00 67.65           N  
ANISOU 1618  ND1 HIS A 213    11551   7387   6765  -1718    649    919       N  
ATOM   1619  CD2 HIS A 213       0.313  48.496  11.286  1.00 64.60           C  
ANISOU 1619  CD2 HIS A 213    11093   7050   6400  -1424    530    711       C  
ATOM   1620  CE1 HIS A 213       2.050  47.865  10.143  1.00 64.82           C  
ANISOU 1620  CE1 HIS A 213    11014   7250   6367  -1662    697    853       C  
ATOM   1621  NE2 HIS A 213       1.041  47.409  10.876  1.00 63.58           N  
ANISOU 1621  NE2 HIS A 213    10812   7121   6224  -1493    627    733       N  
ATOM   1622  N   PHE A 214       1.846  53.765  12.010  1.00 67.62           N  
ANISOU 1622  N   PHE A 214    12099   6504   7089  -1869    345    860       N  
ATOM   1623  CA  PHE A 214       2.009  55.220  12.028  1.00 70.18           C  
ANISOU 1623  CA  PHE A 214    12638   6532   7494  -1961    271    913       C  
ATOM   1624  C   PHE A 214       2.672  55.729  10.733  1.00 79.97           C  
ANISOU 1624  C   PHE A 214    13988   7699   8698  -2133    340   1130       C  
ATOM   1625  O   PHE A 214       3.310  54.948  10.009  1.00 79.23           O  
ANISOU 1625  O   PHE A 214    13767   7807   8530  -2224    457   1217       O  
ATOM   1626  CB  PHE A 214       2.889  55.630  13.229  1.00 71.81           C  
ANISOU 1626  CB  PHE A 214    12792   6672   7822  -2117    242    799       C  
ATOM   1627  CG  PHE A 214       2.424  55.215  14.606  1.00 71.00           C  
ANISOU 1627  CG  PHE A 214    12576   6645   7755  -1978    179    587       C  
ATOM   1628  CD1 PHE A 214       2.634  53.922  15.070  1.00 70.61           C  
ANISOU 1628  CD1 PHE A 214    12289   6871   7666  -1949    246    505       C  
ATOM   1629  CD2 PHE A 214       1.846  56.139  15.469  1.00 73.46           C  
ANISOU 1629  CD2 PHE A 214    13019   6753   8139  -1882     51    469       C  
ATOM   1630  CE1 PHE A 214       2.215  53.544  16.340  1.00 70.22           C  
ANISOU 1630  CE1 PHE A 214    12138   6901   7643  -1826    191    325       C  
ATOM   1631  CE2 PHE A 214       1.433  55.762  16.750  1.00 74.36           C  
ANISOU 1631  CE2 PHE A 214    13022   6958   8273  -1752     -2    276       C  
ATOM   1632  CZ  PHE A 214       1.627  54.472  17.180  1.00 70.21           C  
ANISOU 1632  CZ  PHE A 214    12261   6714   7703  -1730     70    212       C  
ATOM   1633  N   ASN A 215       2.556  57.055  10.467  1.00 80.21           N  
ANISOU 1633  N   ASN A 215    14256   7439   8781  -2179    266   1217       N  
ATOM   1634  CA  ASN A 215       3.190  57.702   9.315  1.00 82.41           C  
ANISOU 1634  CA  ASN A 215    14661   7615   9035  -2361    322   1438       C  
ATOM   1635  C   ASN A 215       4.576  58.249   9.746  1.00 89.44           C  
ANISOU 1635  C   ASN A 215    15520   8428  10035  -2660    353   1459       C  
ATOM   1636  O   ASN A 215       5.104  57.815  10.777  1.00 88.15           O  
ANISOU 1636  O   ASN A 215    15188   8372   9933  -2716    359   1309       O  
ATOM   1637  CB  ASN A 215       2.282  58.807   8.726  1.00 83.08           C  
ANISOU 1637  CB  ASN A 215    15028   7425   9116  -2247    223   1538       C  
ATOM   1638  CG  ASN A 215       1.659  59.769   9.722  1.00101.45           C  
ANISOU 1638  CG  ASN A 215    17509   9484  11555  -2144     70   1404       C  
ATOM   1639  OD1 ASN A 215       2.125  59.948  10.855  1.00 91.50           O  
ANISOU 1639  OD1 ASN A 215    16189   8176  10402  -2226     31   1261       O  
ATOM   1640  ND2 ASN A 215       0.583  60.426   9.307  1.00 92.96           N  
ANISOU 1640  ND2 ASN A 215    16638   8231  10453  -1952    -25   1444       N  
ATOM   1641  N   GLU A 216       5.174  59.170   8.960  1.00 88.66           N  
ANISOU 1641  N   GLU A 216    15574   8155   9956  -2856    372   1648       N  
ATOM   1642  CA  GLU A 216       6.465  59.764   9.301  1.00 90.15           C  
ANISOU 1642  CA  GLU A 216    15741   8260  10252  -3157    396   1683       C  
ATOM   1643  C   GLU A 216       6.303  60.720  10.488  1.00 95.27           C  
ANISOU 1643  C   GLU A 216    16512   8634  11053  -3162    249   1534       C  
ATOM   1644  O   GLU A 216       7.217  60.841  11.304  1.00 94.89           O  
ANISOU 1644  O   GLU A 216    16363   8588  11102  -3344    247   1448       O  
ATOM   1645  CB  GLU A 216       7.064  60.491   8.090  1.00 94.17           C  
ANISOU 1645  CB  GLU A 216    16385   8662  10733  -3365    458   1944       C  
ATOM   1646  N   LYS A 217       5.109  61.351  10.600  1.00 93.19           N  
ANISOU 1646  N   LYS A 217    16457   8147  10803  -2945    123   1492       N  
ATOM   1647  CA  LYS A 217       4.714  62.321  11.630  1.00 94.65           C  
ANISOU 1647  CA  LYS A 217    16796   8050  11115  -2888    -34   1345       C  
ATOM   1648  C   LYS A 217       4.378  61.641  12.970  1.00 98.45           C  
ANISOU 1648  C   LYS A 217    17104   8684  11619  -2733    -76   1083       C  
ATOM   1649  O   LYS A 217       4.013  62.332  13.932  1.00 99.05           O  
ANISOU 1649  O   LYS A 217    17281   8569  11787  -2656   -205    928       O  
ATOM   1650  CB  LYS A 217       3.505  63.146  11.141  1.00 98.29           C  
ANISOU 1650  CB  LYS A 217    17531   8255  11560  -2677   -145   1401       C  
ATOM   1651  CG  LYS A 217       3.834  64.138  10.021  1.00112.48           C  
ANISOU 1651  CG  LYS A 217    19556   9816  13366  -2840   -140   1653       C  
ATOM   1652  N   SER A 218       4.518  60.288  13.025  1.00 93.13           N  
ANISOU 1652  N   SER A 218    16174   8355  10858  -2688     31   1038       N  
ATOM   1653  CA  SER A 218       4.261  59.407  14.166  1.00 90.74           C  
ANISOU 1653  CA  SER A 218    15672   8256  10550  -2550     20    824       C  
ATOM   1654  C   SER A 218       2.834  59.616  14.722  1.00 94.67           C  
ANISOU 1654  C   SER A 218    16273   8660  11038  -2248   -102    686       C  
ATOM   1655  O   SER A 218       2.635  60.003  15.877  1.00 94.91           O  
ANISOU 1655  O   SER A 218    16323   8595  11143  -2185   -201    510       O  
ATOM   1656  CB  SER A 218       5.334  59.572  15.240  1.00 94.31           C  
ANISOU 1656  CB  SER A 218    16012   8713  11107  -2746      8    705       C  
ATOM   1657  OG  SER A 218       6.575  59.065  14.773  1.00101.69           O  
ANISOU 1657  OG  SER A 218    16788   9825  12025  -2985    137    814       O  
ATOM   1658  N   SER A 219       1.849  59.384  13.851  1.00 90.83           N  
ANISOU 1658  N   SER A 219    15853   8204  10453  -2062    -94    772       N  
ATOM   1659  CA  SER A 219       0.420  59.460  14.131  1.00 90.64           C  
ANISOU 1659  CA  SER A 219    15908   8138  10393  -1760   -191    673       C  
ATOM   1660  C   SER A 219      -0.262  58.262  13.477  1.00 93.61           C  
ANISOU 1660  C   SER A 219    16148   8782  10636  -1604   -115    714       C  
ATOM   1661  O   SER A 219       0.038  57.938  12.330  1.00 93.25           O  
ANISOU 1661  O   SER A 219    16098   8813  10520  -1685    -25    882       O  
ATOM   1662  CB  SER A 219      -0.171  60.775  13.636  1.00 96.96           C  
ANISOU 1662  CB  SER A 219    17004   8610  11227  -1694   -299    754       C  
ATOM   1663  OG  SER A 219      -0.033  60.911  12.232  1.00108.75           O  
ANISOU 1663  OG  SER A 219    18595  10070  12655  -1770   -235    983       O  
ATOM   1664  N   VAL A 220      -1.145  57.588  14.227  1.00 89.86           N  
ANISOU 1664  N   VAL A 220    15556   8460  10129  -1389   -148    557       N  
ATOM   1665  CA  VAL A 220      -1.862  56.365  13.835  1.00 87.96           C  
ANISOU 1665  CA  VAL A 220    15163   8481   9776  -1234    -91    558       C  
ATOM   1666  C   VAL A 220      -2.499  56.516  12.446  1.00 93.02           C  
ANISOU 1666  C   VAL A 220    15935   9080  10327  -1150    -84    722       C  
ATOM   1667  O   VAL A 220      -3.173  57.512  12.177  1.00 94.92           O  
ANISOU 1667  O   VAL A 220    16386   9101  10579  -1044   -177    756       O  
ATOM   1668  CB  VAL A 220      -2.915  55.947  14.900  1.00 90.55           C  
ANISOU 1668  CB  VAL A 220    15397   8914  10094  -1001   -160    370       C  
ATOM   1669  CG1 VAL A 220      -3.598  54.628  14.532  1.00 88.47           C  
ANISOU 1669  CG1 VAL A 220    14965   8923   9727   -868   -101    371       C  
ATOM   1670  CG2 VAL A 220      -2.288  55.847  16.283  1.00 89.81           C  
ANISOU 1670  CG2 VAL A 220    15183   8863  10077  -1078   -171    211       C  
ATOM   1671  N   VAL A 221      -2.232  55.532  11.565  1.00 88.18           N  
ANISOU 1671  N   VAL A 221    15203   8677   9625  -1198     25    821       N  
ATOM   1672  CA  VAL A 221      -2.757  55.457  10.193  1.00 87.84           C  
ANISOU 1672  CA  VAL A 221    15247   8652   9474  -1123     47    974       C  
ATOM   1673  C   VAL A 221      -3.708  54.245  10.075  1.00 88.16           C  
ANISOU 1673  C   VAL A 221    15134   8942   9421   -929     61    907       C  
ATOM   1674  O   VAL A 221      -4.484  54.142   9.122  1.00 87.62           O  
ANISOU 1674  O   VAL A 221    15130   8902   9261   -800     48    987       O  
ATOM   1675  CB  VAL A 221      -1.635  55.432   9.111  1.00 92.46           C  
ANISOU 1675  CB  VAL A 221    15849   9261  10022  -1347    158   1160       C  
ATOM   1676  CG1 VAL A 221      -0.810  56.715   9.146  1.00 94.78           C  
ANISOU 1676  CG1 VAL A 221    16314   9289  10409  -1541    133   1246       C  
ATOM   1677  CG2 VAL A 221      -0.740  54.199   9.226  1.00 90.35           C  
ANISOU 1677  CG2 VAL A 221    15338   9260   9731  -1473    279   1131       C  
ATOM   1678  N   GLY A 222      -3.631  53.359  11.065  1.00 82.41           N  
ANISOU 1678  N   GLY A 222    14205   8387   8719   -915     83    763       N  
ATOM   1679  CA  GLY A 222      -4.440  52.149  11.149  1.00 79.19           C  
ANISOU 1679  CA  GLY A 222    13632   8213   8244   -760     95    688       C  
ATOM   1680  C   GLY A 222      -3.737  51.048  11.907  1.00 77.69           C  
ANISOU 1680  C   GLY A 222    13217   8223   8079   -851    167    598       C  
ATOM   1681  O   GLY A 222      -2.709  51.290  12.545  1.00 76.96           O  
ANISOU 1681  O   GLY A 222    13090   8091   8061  -1012    194    569       O  
ATOM   1682  N   GLY A 223      -4.289  49.843  11.817  1.00 70.34           N  
ANISOU 1682  N   GLY A 223    12136   7505   7087   -750    193    557       N  
ATOM   1683  CA  GLY A 223      -3.756  48.668  12.492  1.00 67.14           C  
ANISOU 1683  CA  GLY A 223    11516   7297   6697   -810    255    477       C  
ATOM   1684  C   GLY A 223      -3.924  47.367  11.732  1.00 67.35           C  
ANISOU 1684  C   GLY A 223    11420   7528   6641   -777    316    509       C  
ATOM   1685  O   GLY A 223      -4.597  47.320  10.702  1.00 66.80           O  
ANISOU 1685  O   GLY A 223    11420   7468   6494   -689    303    581       O  
ATOM   1686  N   PHE A 224      -3.326  46.287  12.264  1.00 60.55           N  
ANISOU 1686  N   PHE A 224    10377   6832   5796   -841    374    450       N  
ATOM   1687  CA  PHE A 224      -3.383  44.948  11.680  1.00 55.89           C  
ANISOU 1687  CA  PHE A 224     9660   6434   5143   -818    428    461       C  
ATOM   1688  C   PHE A 224      -3.252  43.869  12.769  1.00 55.98           C  
ANISOU 1688  C   PHE A 224     9481   6593   5194   -813    441    351       C  
ATOM   1689  O   PHE A 224      -2.301  43.894  13.540  1.00 54.66           O  
ANISOU 1689  O   PHE A 224     9250   6432   5086   -924    472    313       O  
ATOM   1690  CB  PHE A 224      -2.278  44.785  10.627  1.00 56.54           C  
ANISOU 1690  CB  PHE A 224     9749   6553   5181   -960    522    568       C  
ATOM   1691  CG  PHE A 224      -2.424  43.516   9.837  1.00 55.34           C  
ANISOU 1691  CG  PHE A 224     9500   6577   4950   -913    566    580       C  
ATOM   1692  CD1 PHE A 224      -3.220  43.479   8.692  1.00 58.60           C  
ANISOU 1692  CD1 PHE A 224     9995   6998   5273   -814    544    644       C  
ATOM   1693  CD2 PHE A 224      -1.784  42.351  10.241  1.00 53.58           C  
ANISOU 1693  CD2 PHE A 224     9107   6509   4742   -961    620    523       C  
ATOM   1694  CE1 PHE A 224      -3.377  42.296   7.968  1.00 58.31           C  
ANISOU 1694  CE1 PHE A 224     9872   7120   5164   -768    575    640       C  
ATOM   1695  CE2 PHE A 224      -1.972  41.160   9.544  1.00 56.16           C  
ANISOU 1695  CE2 PHE A 224     9353   6981   5002   -908    647    520       C  
ATOM   1696  CZ  PHE A 224      -2.742  41.146   8.393  1.00 55.67           C  
ANISOU 1696  CZ  PHE A 224     9375   6924   4852   -817    625    576       C  
ATOM   1697  N   VAL A 225      -4.158  42.876  12.746  1.00 51.86           N  
ANISOU 1697  N   VAL A 225     8869   6198   4636   -693    420    310       N  
ATOM   1698  CA  VAL A 225      -4.247  41.753  13.684  1.00 50.31           C  
ANISOU 1698  CA  VAL A 225     8500   6146   4468   -670    425    222       C  
ATOM   1699  C   VAL A 225      -3.873  40.433  12.991  1.00 53.76           C  
ANISOU 1699  C   VAL A 225     8837   6727   4864   -698    484    246       C  
ATOM   1700  O   VAL A 225      -4.505  40.026  12.005  1.00 52.98           O  
ANISOU 1700  O   VAL A 225     8765   6665   4701   -628    472    283       O  
ATOM   1701  CB  VAL A 225      -5.667  41.644  14.310  1.00 54.04           C  
ANISOU 1701  CB  VAL A 225     8944   6650   4941   -511    345    152       C  
ATOM   1702  CG1 VAL A 225      -5.739  40.525  15.358  1.00 52.59           C  
ANISOU 1702  CG1 VAL A 225     8583   6611   4788   -501    352     75       C  
ATOM   1703  CG2 VAL A 225      -6.127  42.975  14.907  1.00 55.15           C  
ANISOU 1703  CG2 VAL A 225     9196   6647   5111   -451    278    119       C  
ATOM   1704  N   SER A 226      -2.846  39.764  13.538  1.00 50.20           N  
ANISOU 1704  N   SER A 226     8270   6357   4448   -795    540    219       N  
ATOM   1705  CA  SER A 226      -2.416  38.420  13.151  1.00 49.16           C  
ANISOU 1705  CA  SER A 226     8025   6362   4291   -813    590    218       C  
ATOM   1706  C   SER A 226      -2.918  37.491  14.256  1.00 52.77           C  
ANISOU 1706  C   SER A 226     8352   6910   4789   -754    557    138       C  
ATOM   1707  O   SER A 226      -2.692  37.762  15.435  1.00 52.04           O  
ANISOU 1707  O   SER A 226     8213   6810   4751   -777    545     88       O  
ATOM   1708  CB  SER A 226      -0.899  38.327  12.979  1.00 52.25           C  
ANISOU 1708  CB  SER A 226     8375   6788   4689   -951    674    247       C  
ATOM   1709  OG  SER A 226      -0.354  39.372  12.199  1.00 63.45           O  
ANISOU 1709  OG  SER A 226     9911   8115   6083  -1031    707    327       O  
ATOM   1710  N   HIS A 227      -3.696  36.482  13.894  1.00 49.75           N  
ANISOU 1710  N   HIS A 227     7919   6606   4379   -675    533    127       N  
ATOM   1711  CA  HIS A 227      -4.255  35.547  14.857  1.00 48.99           C  
ANISOU 1711  CA  HIS A 227     7702   6595   4319   -626    501     69       C  
ATOM   1712  C   HIS A 227      -3.542  34.211  14.683  1.00 51.26           C  
ANISOU 1712  C   HIS A 227     7889   6977   4610   -667    544     64       C  
ATOM   1713  O   HIS A 227      -3.053  33.913  13.593  1.00 50.74           O  
ANISOU 1713  O   HIS A 227     7853   6924   4501   -692    582     96       O  
ATOM   1714  CB  HIS A 227      -5.789  35.435  14.715  1.00 50.05           C  
ANISOU 1714  CB  HIS A 227     7846   6741   4430   -508    429     58       C  
ATOM   1715  CG  HIS A 227      -6.264  34.844  13.417  1.00 53.52           C  
ANISOU 1715  CG  HIS A 227     8315   7208   4812   -468    418     88       C  
ATOM   1716  ND1 HIS A 227      -6.129  35.527  12.206  1.00 56.47           N  
ANISOU 1716  ND1 HIS A 227     8812   7519   5126   -467    431    143       N  
ATOM   1717  CD2 HIS A 227      -6.888  33.666  13.184  1.00 54.50           C  
ANISOU 1717  CD2 HIS A 227     8364   7413   4930   -428    391     70       C  
ATOM   1718  CE1 HIS A 227      -6.663  34.738  11.285  1.00 55.30           C  
ANISOU 1718  CE1 HIS A 227     8654   7427   4929   -419    410    148       C  
ATOM   1719  NE2 HIS A 227      -7.124  33.604  11.823  1.00 54.87           N  
ANISOU 1719  NE2 HIS A 227     8485   7454   4911   -398    383    101       N  
ATOM   1720  N   TYR A 228      -3.456  33.431  15.772  1.00 45.78           N  
ANISOU 1720  N   TYR A 228     7079   6353   3964   -669    538     22       N  
ATOM   1721  CA  TYR A 228      -2.753  32.167  15.783  1.00 44.48           C  
ANISOU 1721  CA  TYR A 228     6821   6267   3813   -700    570     12       C  
ATOM   1722  C   TYR A 228      -3.501  31.112  16.532  1.00 49.38           C  
ANISOU 1722  C   TYR A 228     7346   6950   4465   -651    526    -13       C  
ATOM   1723  O   TYR A 228      -3.993  31.364  17.628  1.00 48.11           O  
ANISOU 1723  O   TYR A 228     7143   6803   4332   -630    497    -33       O  
ATOM   1724  CB  TYR A 228      -1.379  32.328  16.457  1.00 45.45           C  
ANISOU 1724  CB  TYR A 228     6892   6410   3967   -786    624      1       C  
ATOM   1725  CG  TYR A 228      -0.558  33.470  15.904  1.00 48.17           C  
ANISOU 1725  CG  TYR A 228     7319   6693   4292   -861    669     32       C  
ATOM   1726  CD1 TYR A 228       0.151  33.332  14.720  1.00 49.69           C  
ANISOU 1726  CD1 TYR A 228     7543   6899   4437   -899    723     71       C  
ATOM   1727  CD2 TYR A 228      -0.451  34.674  16.592  1.00 49.19           C  
ANISOU 1727  CD2 TYR A 228     7492   6752   4448   -898    658     22       C  
ATOM   1728  CE1 TYR A 228       0.905  34.379  14.203  1.00 52.49           C  
ANISOU 1728  CE1 TYR A 228     7970   7203   4772   -981    769    115       C  
ATOM   1729  CE2 TYR A 228       0.309  35.726  16.091  1.00 51.18           C  
ANISOU 1729  CE2 TYR A 228     7823   6932   4690   -984    695     59       C  
ATOM   1730  CZ  TYR A 228       0.968  35.582  14.881  1.00 56.00           C  
ANISOU 1730  CZ  TYR A 228     8464   7561   5254  -1030    753    113       C  
ATOM   1731  OH  TYR A 228       1.699  36.621  14.348  1.00 52.36           O  
ANISOU 1731  OH  TYR A 228     8079   7035   4779  -1126    794    166       O  
ATOM   1732  N   LEU A 229      -3.483  29.898  15.992  1.00 46.70           N  
ANISOU 1732  N   LEU A 229     6969   6652   4123   -639    524    -14       N  
ATOM   1733  CA  LEU A 229      -3.994  28.688  16.618  1.00 46.48           C  
ANISOU 1733  CA  LEU A 229     6849   6676   4133   -614    487    -27       C  
ATOM   1734  C   LEU A 229      -5.305  28.818  17.389  1.00 45.08           C  
ANISOU 1734  C   LEU A 229     6639   6517   3972   -568    429    -29       C  
ATOM   1735  O   LEU A 229      -5.330  28.555  18.586  1.00 43.69           O  
ANISOU 1735  O   LEU A 229     6382   6386   3831   -575    424    -34       O  
ATOM   1736  CB  LEU A 229      -2.938  28.137  17.600  1.00 47.33           C  
ANISOU 1736  CB  LEU A 229     6869   6830   4284   -657    520    -38       C  
ATOM   1737  CG  LEU A 229      -1.669  27.544  17.041  1.00 54.97           C  
ANISOU 1737  CG  LEU A 229     7823   7816   5246   -690    570    -44       C  
ATOM   1738  CD1 LEU A 229      -0.626  27.505  18.120  1.00 57.30           C  
ANISOU 1738  CD1 LEU A 229     8041   8156   5575   -731    602    -55       C  
ATOM   1739  CD2 LEU A 229      -1.907  26.132  16.447  1.00 56.55           C  
ANISOU 1739  CD2 LEU A 229     8004   8029   5453   -653    541    -53       C  
ATOM   1740  N   LEU A 230      -6.387  29.134  16.725  1.00 40.16           N  
ANISOU 1740  N   LEU A 230     6066   5876   3318   -516    387    -23       N  
ATOM   1741  CA  LEU A 230      -7.687  29.068  17.385  1.00 38.55           C  
ANISOU 1741  CA  LEU A 230     5808   5714   3125   -468    331    -25       C  
ATOM   1742  C   LEU A 230      -7.905  27.608  17.843  1.00 42.10           C  
ANISOU 1742  C   LEU A 230     6155   6221   3619   -489    310    -18       C  
ATOM   1743  O   LEU A 230      -7.654  26.693  17.056  1.00 42.54           O  
ANISOU 1743  O   LEU A 230     6221   6263   3682   -505    305    -18       O  
ATOM   1744  CB  LEU A 230      -8.805  29.495  16.409  1.00 38.46           C  
ANISOU 1744  CB  LEU A 230     5861   5684   3069   -405    283    -22       C  
ATOM   1745  CG  LEU A 230     -10.211  29.395  17.004  1.00 43.01           C  
ANISOU 1745  CG  LEU A 230     6365   6325   3650   -351    225    -25       C  
ATOM   1746  CD1 LEU A 230     -10.473  30.495  18.085  1.00 41.98           C  
ANISOU 1746  CD1 LEU A 230     6225   6210   3517   -312    227    -40       C  
ATOM   1747  CD2 LEU A 230     -11.253  29.284  15.950  1.00 43.59           C  
ANISOU 1747  CD2 LEU A 230     6469   6403   3688   -299    169    -24       C  
ATOM   1748  N   GLU A 231      -8.300  27.386  19.101  1.00 38.18           N  
ANISOU 1748  N   GLU A 231     5569   5787   3151   -489    299    -10       N  
ATOM   1749  CA  GLU A 231      -8.530  26.026  19.618  1.00 37.74           C  
ANISOU 1749  CA  GLU A 231     5420   5779   3141   -518    277     14       C  
ATOM   1750  C   GLU A 231      -9.814  25.432  19.015  1.00 43.87           C  
ANISOU 1750  C   GLU A 231     6178   6572   3919   -500    214     24       C  
ATOM   1751  O   GLU A 231     -10.913  25.937  19.213  1.00 44.47           O  
ANISOU 1751  O   GLU A 231     6228   6693   3973   -460    182     27       O  
ATOM   1752  CB  GLU A 231      -8.602  26.045  21.145  1.00 38.38           C  
ANISOU 1752  CB  GLU A 231     5410   5935   3237   -523    286     30       C  
ATOM   1753  CG  GLU A 231      -8.734  24.667  21.761  1.00 39.53           C  
ANISOU 1753  CG  GLU A 231     5465   6126   3430   -560    267     72       C  
ATOM   1754  CD  GLU A 231      -8.794  24.746  23.268  1.00 55.28           C  
ANISOU 1754  CD  GLU A 231     7371   8210   5424   -561    281     95       C  
ATOM   1755  OE1 GLU A 231      -9.581  25.583  23.755  1.00 43.49           O  
ANISOU 1755  OE1 GLU A 231     5853   6777   3894   -518    272     84       O  
ATOM   1756  OE2 GLU A 231      -7.930  24.136  23.941  1.00 60.37           O  
ANISOU 1756  OE2 GLU A 231     7977   8867   6092   -592    303    114       O  
ATOM   1757  N   LYS A 232      -9.666  24.351  18.307  1.00 40.10           N  
ANISOU 1757  N   LYS A 232     5709   6061   3468   -526    193     25       N  
ATOM   1758  CA  LYS A 232     -10.763  23.714  17.596  1.00 39.43           C  
ANISOU 1758  CA  LYS A 232     5613   5980   3388   -521    127     25       C  
ATOM   1759  C   LYS A 232     -11.496  22.681  18.427  1.00 45.21           C  
ANISOU 1759  C   LYS A 232     6239   6764   4176   -563     87     64       C  
ATOM   1760  O   LYS A 232     -12.685  22.494  18.207  1.00 44.54           O  
ANISOU 1760  O   LYS A 232     6115   6717   4091   -560     32     72       O  
ATOM   1761  CB  LYS A 232     -10.219  23.045  16.324  1.00 39.51           C  
ANISOU 1761  CB  LYS A 232     5694   5922   3396   -527    115     -6       C  
ATOM   1762  CG  LYS A 232      -9.881  23.988  15.191  1.00 44.29           C  
ANISOU 1762  CG  LYS A 232     6404   6491   3931   -485    139    -35       C  
ATOM   1763  CD  LYS A 232      -9.614  23.096  13.968  1.00 63.20           C  
ANISOU 1763  CD  LYS A 232     8850   8846   6318   -484    114    -69       C  
ATOM   1764  CE  LYS A 232      -9.828  23.724  12.617  1.00 74.92           C  
ANISOU 1764  CE  LYS A 232    10425  10317   7724   -435    102    -92       C  
ATOM   1765  NZ  LYS A 232      -9.939  22.663  11.582  1.00 81.15           N  
ANISOU 1765  NZ  LYS A 232    11239  11085   8509   -429     53   -135       N  
ATOM   1766  N   SER A 233     -10.791  21.968  19.327  1.00 45.10           N  
ANISOU 1766  N   SER A 233     6177   6751   4207   -606    110     95       N  
ATOM   1767  CA  SER A 233     -11.379  20.929  20.194  1.00 47.06           C  
ANISOU 1767  CA  SER A 233     6328   7042   4510   -657     76    151       C  
ATOM   1768  C   SER A 233     -12.514  21.477  21.062  1.00 52.32           C  
ANISOU 1768  C   SER A 233     6905   7822   5152   -646     69    185       C  
ATOM   1769  O   SER A 233     -13.528  20.788  21.237  1.00 55.78           O  
ANISOU 1769  O   SER A 233     7268   8306   5619   -685     22    225       O  
ATOM   1770  CB  SER A 233     -10.322  20.287  21.080  1.00 50.62           C  
ANISOU 1770  CB  SER A 233     6754   7481   5000   -688    109    183       C  
ATOM   1771  OG  SER A 233      -9.510  21.285  21.673  1.00 64.00           O  
ANISOU 1771  OG  SER A 233     8456   9206   6655   -657    171    167       O  
ATOM   1772  N   ARG A 234     -12.393  22.748  21.479  1.00 45.19           N  
ANISOU 1772  N   ARG A 234     6013   6963   4195   -590    110    161       N  
ATOM   1773  CA  ARG A 234     -13.388  23.492  22.259  1.00 44.94           C  
ANISOU 1773  CA  ARG A 234     5907   7045   4123   -549    108    172       C  
ATOM   1774  C   ARG A 234     -14.756  23.650  21.560  1.00 46.93           C  
ANISOU 1774  C   ARG A 234     6138   7338   4355   -520     52    162       C  
ATOM   1775  O   ARG A 234     -15.756  23.843  22.241  1.00 47.16           O  
ANISOU 1775  O   ARG A 234     6071   7486   4363   -501     39    185       O  
ATOM   1776  CB  ARG A 234     -12.868  24.920  22.548  1.00 44.57           C  
ANISOU 1776  CB  ARG A 234     5916   6996   4024   -482    151    124       C  
ATOM   1777  CG  ARG A 234     -13.861  25.731  23.405  1.00 49.23           C  
ANISOU 1777  CG  ARG A 234     6437   7703   4564   -417    145    118       C  
ATOM   1778  CD  ARG A 234     -13.239  26.752  24.292  1.00 48.00           C  
ANISOU 1778  CD  ARG A 234     6295   7568   4374   -373    186     84       C  
ATOM   1779  NE  ARG A 234     -12.058  26.213  24.941  1.00 45.23           N  
ANISOU 1779  NE  ARG A 234     5934   7199   4053   -431    224    104       N  
ATOM   1780  CZ  ARG A 234     -12.017  25.731  26.172  1.00 52.05           C  
ANISOU 1780  CZ  ARG A 234     6701   8159   4916   -451    240    143       C  
ATOM   1781  NH1 ARG A 234     -10.896  25.228  26.648  1.00 53.40           N  
ANISOU 1781  NH1 ARG A 234     6871   8306   5113   -495    268    160       N  
ATOM   1782  NH2 ARG A 234     -13.093  25.789  26.955  1.00 41.82           N  
ANISOU 1782  NH2 ARG A 234     5305   6998   3586   -419    228    167       N  
ATOM   1783  N   ILE A 235     -14.787  23.628  20.223  1.00 40.98           N  
ANISOU 1783  N   ILE A 235     5469   6503   3598   -509     21    126       N  
ATOM   1784  CA  ILE A 235     -15.994  23.901  19.455  1.00 41.01           C  
ANISOU 1784  CA  ILE A 235     5464   6545   3572   -469    -35    107       C  
ATOM   1785  C   ILE A 235     -17.068  22.802  19.680  1.00 44.87           C  
ANISOU 1785  C   ILE A 235     5834   7110   4105   -535    -91    152       C  
ATOM   1786  O   ILE A 235     -18.248  23.120  19.729  1.00 44.05           O  
ANISOU 1786  O   ILE A 235     5657   7108   3974   -503   -125    154       O  
ATOM   1787  CB  ILE A 235     -15.642  24.143  17.935  1.00 42.61           C  
ANISOU 1787  CB  ILE A 235     5795   6644   3750   -439    -54     59       C  
ATOM   1788  CG1 ILE A 235     -14.581  25.247  17.813  1.00 41.51           C  
ANISOU 1788  CG1 ILE A 235     5764   6436   3572   -394      7     33       C  
ATOM   1789  CG2 ILE A 235     -16.881  24.521  17.107  1.00 44.24           C  
ANISOU 1789  CG2 ILE A 235     5999   6897   3914   -381   -116     36       C  
ATOM   1790  CD1 ILE A 235     -13.849  25.494  16.354  1.00 31.98           C  
ANISOU 1790  CD1 ILE A 235     4694   5125   2331   -377     13     -1       C  
ATOM   1791  N   CYS A 236     -16.665  21.561  19.892  1.00 43.94           N  
ANISOU 1791  N   CYS A 236     5693   6948   4055   -626    -99    189       N  
ATOM   1792  CA  CYS A 236     -17.625  20.459  19.993  1.00 46.44           C  
ANISOU 1792  CA  CYS A 236     5911   7309   4424   -708   -158    236       C  
ATOM   1793  C   CYS A 236     -17.848  19.934  21.418  1.00 51.07           C  
ANISOU 1793  C   CYS A 236     6375   7990   5039   -770   -135    322       C  
ATOM   1794  O   CYS A 236     -18.970  19.545  21.754  1.00 51.50           O  
ANISOU 1794  O   CYS A 236     6314   8148   5106   -817   -170    369       O  
ATOM   1795  CB  CYS A 236     -17.215  19.331  19.054  1.00 47.16           C  
ANISOU 1795  CB  CYS A 236     6070   7272   4578   -770   -207    218       C  
ATOM   1796  SG  CYS A 236     -17.052  19.857  17.332  1.00 52.17           S  
ANISOU 1796  SG  CYS A 236     6838   7823   5163   -697   -238    122       S  
ATOM   1797  N   VAL A 237     -16.801  19.874  22.229  1.00 46.62           N  
ANISOU 1797  N   VAL A 237     5830   7399   4483   -775    -78    347       N  
ATOM   1798  CA  VAL A 237     -16.955  19.338  23.578  1.00 46.51           C  
ANISOU 1798  CA  VAL A 237     5706   7479   4488   -830    -56    437       C  
ATOM   1799  C   VAL A 237     -16.061  20.112  24.534  1.00 51.90           C  
ANISOU 1799  C   VAL A 237     6400   8197   5123   -772     16    430       C  
ATOM   1800  O   VAL A 237     -14.975  20.533  24.145  1.00 52.52           O  
ANISOU 1800  O   VAL A 237     6582   8179   5194   -733     44    375       O  
ATOM   1801  CB  VAL A 237     -16.675  17.807  23.602  1.00 49.61           C  
ANISOU 1801  CB  VAL A 237     6096   7780   4971   -940    -92    501       C  
ATOM   1802  CG1 VAL A 237     -15.190  17.480  23.349  1.00 48.82           C  
ANISOU 1802  CG1 VAL A 237     6110   7538   4900   -927    -69    471       C  
ATOM   1803  CG2 VAL A 237     -17.200  17.154  24.872  1.00 49.35           C  
ANISOU 1803  CG2 VAL A 237     5936   7858   4958  -1015    -84    616       C  
ATOM   1804  N   GLN A 238     -16.536  20.315  25.773  1.00 49.06           N  
ANISOU 1804  N   GLN A 238     5928   7985   4725   -767     45    484       N  
ATOM   1805  CA  GLN A 238     -15.815  20.992  26.852  1.00 48.20           C  
ANISOU 1805  CA  GLN A 238     5811   7937   4565   -714    106    479       C  
ATOM   1806  C   GLN A 238     -15.970  20.178  28.122  1.00 54.09           C  
ANISOU 1806  C   GLN A 238     6444   8791   5317   -775    123    586       C  
ATOM   1807  O   GLN A 238     -16.898  19.364  28.211  1.00 55.51           O  
ANISOU 1807  O   GLN A 238     6536   9029   5526   -849     92    663       O  
ATOM   1808  CB  GLN A 238     -16.353  22.418  27.093  1.00 49.04           C  
ANISOU 1808  CB  GLN A 238     5900   8146   4586   -606    126    413       C  
ATOM   1809  CG  GLN A 238     -16.516  23.306  25.866  1.00 49.65           C  
ANISOU 1809  CG  GLN A 238     6076   8142   4648   -539    101    325       C  
ATOM   1810  CD  GLN A 238     -17.801  22.975  25.112  1.00 59.19           C  
ANISOU 1810  CD  GLN A 238     7233   9391   5867   -556     44    337       C  
ATOM   1811  OE1 GLN A 238     -18.825  22.612  25.696  1.00 47.76           O  
ANISOU 1811  OE1 GLN A 238     5653   8085   4408   -581     32    392       O  
ATOM   1812  NE2 GLN A 238     -17.743  22.960  23.798  1.00 49.86           N  
ANISOU 1812  NE2 GLN A 238     6145   8092   4709   -556      7    294       N  
ATOM   1813  N   GLY A 239     -15.088  20.417  29.100  1.00 48.85           N  
ANISOU 1813  N   GLY A 239     5779   8159   4621   -748    170    594       N  
ATOM   1814  CA  GLY A 239     -15.186  19.827  30.431  1.00 47.26           C  
ANISOU 1814  CA  GLY A 239     5473   8083   4402   -786    193    696       C  
ATOM   1815  C   GLY A 239     -16.345  20.490  31.143  1.00 51.87           C  
ANISOU 1815  C   GLY A 239     5936   8869   4902   -740    210    706       C  
ATOM   1816  O   GLY A 239     -16.726  21.595  30.762  1.00 50.39           O  
ANISOU 1816  O   GLY A 239     5770   8708   4667   -652    210    613       O  
ATOM   1817  N   LYS A 240     -16.918  19.848  32.185  1.00 52.55           N  
ANISOU 1817  N   LYS A 240     5896   9106   4966   -792    224    820       N  
ATOM   1818  CA  LYS A 240     -18.111  20.346  32.893  1.00 53.55           C  
ANISOU 1818  CA  LYS A 240     5882   9456   5007   -752    243    842       C  
ATOM   1819  C   LYS A 240     -17.950  21.758  33.577  1.00 56.89           C  
ANISOU 1819  C   LYS A 240     6301   9993   5321   -608    282    740       C  
ATOM   1820  O   LYS A 240     -18.973  22.370  33.923  1.00 58.50           O  
ANISOU 1820  O   LYS A 240     6408  10368   5450   -543    290    721       O  
ATOM   1821  CB  LYS A 240     -18.610  19.308  33.922  1.00 58.26           C  
ANISOU 1821  CB  LYS A 240     6346  10194   5595   -846    258   1000       C  
ATOM   1822  CG  LYS A 240     -17.836  19.267  35.245  1.00 74.37           C  
ANISOU 1822  CG  LYS A 240     8361  12325   7573   -819    307   1048       C  
ATOM   1823  N   GLU A 241     -16.716  22.256  33.789  1.00 50.70           N  
ANISOU 1823  N   GLU A 241     5613   9122   4527   -559    302    673       N  
ATOM   1824  CA  GLU A 241     -16.540  23.581  34.396  1.00 50.72           C  
ANISOU 1824  CA  GLU A 241     5624   9211   4437   -432    328    568       C  
ATOM   1825  C   GLU A 241     -16.075  24.606  33.363  1.00 51.83           C  
ANISOU 1825  C   GLU A 241     5906   9186   4600   -368    309    436       C  
ATOM   1826  O   GLU A 241     -15.713  25.741  33.700  1.00 51.37           O  
ANISOU 1826  O   GLU A 241     5892   9138   4487   -272    320    336       O  
ATOM   1827  CB  GLU A 241     -15.559  23.527  35.584  1.00 52.93           C  
ANISOU 1827  CB  GLU A 241     5892   9549   4672   -420    363    585       C  
ATOM   1828  CG  GLU A 241     -16.050  22.722  36.790  1.00 66.72           C  
ANISOU 1828  CG  GLU A 241     7494  11492   6365   -461    389    717       C  
ATOM   1829  CD  GLU A 241     -17.354  23.113  37.478  1.00112.98           C  
ANISOU 1829  CD  GLU A 241    13210  17597  12122   -401    409    733       C  
ATOM   1830  OE1 GLU A 241     -17.851  22.289  38.284  1.00121.17           O  
ANISOU 1830  OE1 GLU A 241    14123  18790  13124   -460    432    865       O  
ATOM   1831  OE2 GLU A 241     -17.877  24.226  37.228  1.00112.97           O  
ANISOU 1831  OE2 GLU A 241    13216  17636  12073   -294    402    619       O  
ATOM   1832  N   GLU A 242     -16.076  24.190  32.098  1.00 45.73           N  
ANISOU 1832  N   GLU A 242     5207   8258   3908   -424    276    439       N  
ATOM   1833  CA  GLU A 242     -15.620  24.996  30.992  1.00 44.27           C  
ANISOU 1833  CA  GLU A 242     5160   7913   3748   -380    259    338       C  
ATOM   1834  C   GLU A 242     -16.753  25.278  30.026  1.00 48.19           C  
ANISOU 1834  C   GLU A 242     5656   8408   4247   -351    221    314       C  
ATOM   1835  O   GLU A 242     -17.811  24.645  30.094  1.00 48.95           O  
ANISOU 1835  O   GLU A 242     5642   8612   4343   -387    203    381       O  
ATOM   1836  CB  GLU A 242     -14.467  24.289  30.296  1.00 45.28           C  
ANISOU 1836  CB  GLU A 242     5386   7861   3956   -458    257    351       C  
ATOM   1837  CG  GLU A 242     -13.248  24.130  31.200  1.00 52.96           C  
ANISOU 1837  CG  GLU A 242     6365   8834   4922   -473    291    361       C  
ATOM   1838  CD  GLU A 242     -11.896  24.205  30.529  1.00 57.52           C  
ANISOU 1838  CD  GLU A 242     7060   9246   5547   -494    299    313       C  
ATOM   1839  OE1 GLU A 242     -11.858  24.166  29.278  1.00 49.76           O  
ANISOU 1839  OE1 GLU A 242     6161   8137   4610   -512    279    288       O  
ATOM   1840  OE2 GLU A 242     -10.876  24.352  31.247  1.00 50.67           O  
ANISOU 1840  OE2 GLU A 242     6199   8387   4665   -489    325    297       O  
ATOM   1841  N   ARG A 243     -16.572  26.270  29.168  1.00 43.03           N  
ANISOU 1841  N   ARG A 243     5116   7644   3588   -284    205    223       N  
ATOM   1842  CA  ARG A 243     -17.607  26.572  28.196  1.00 42.52           C  
ANISOU 1842  CA  ARG A 243     5061   7576   3520   -243    163    199       C  
ATOM   1843  C   ARG A 243     -17.035  26.629  26.817  1.00 45.58           C  
ANISOU 1843  C   ARG A 243     5588   7772   3957   -266    141    165       C  
ATOM   1844  O   ARG A 243     -15.813  26.689  26.656  1.00 44.86           O  
ANISOU 1844  O   ARG A 243     5592   7559   3894   -296    166    147       O  
ATOM   1845  CB  ARG A 243     -18.289  27.904  28.523  1.00 41.43           C  
ANISOU 1845  CB  ARG A 243     4915   7526   3302   -102    158    120       C  
ATOM   1846  CG  ARG A 243     -19.132  27.900  29.802  1.00 44.86           C  
ANISOU 1846  CG  ARG A 243     5190   8189   3667    -56    176    145       C  
ATOM   1847  CD  ARG A 243     -20.058  29.101  29.868  1.00 44.69           C  
ANISOU 1847  CD  ARG A 243     5151   8261   3569     97    155     63       C  
ATOM   1848  NE  ARG A 243     -19.512  30.338  29.282  1.00 42.84           N  
ANISOU 1848  NE  ARG A 243     5080   7868   3329    187    138    -39       N  
ATOM   1849  CZ  ARG A 243     -20.196  31.482  29.234  1.00 60.14           C  
ANISOU 1849  CZ  ARG A 243     7292  10096   5462    333    110   -120       C  
ATOM   1850  NH1 ARG A 243     -21.404  31.560  29.769  1.00 44.93           N  
ANISOU 1850  NH1 ARG A 243     5225   8376   3471    414    101   -120       N  
ATOM   1851  NH2 ARG A 243     -19.669  32.557  28.660  1.00 45.45           N  
ANISOU 1851  NH2 ARG A 243     5594   8069   3607    401     90   -199       N  
ATOM   1852  N   ASN A 244     -17.928  26.673  25.796  1.00 43.23           N  
ANISOU 1852  N   ASN A 244     5301   7463   3661   -245     95    154       N  
ATOM   1853  CA  ASN A 244     -17.525  26.886  24.403  1.00 42.42           C  
ANISOU 1853  CA  ASN A 244     5335   7198   3583   -244     72    116       C  
ATOM   1854  C   ASN A 244     -17.193  28.393  24.262  1.00 43.92           C  
ANISOU 1854  C   ASN A 244     5635   7328   3726   -137     82     38       C  
ATOM   1855  O   ASN A 244     -17.219  29.133  25.245  1.00 43.20           O  
ANISOU 1855  O   ASN A 244     5514   7308   3592    -72    102      8       O  
ATOM   1856  CB  ASN A 244     -18.692  26.455  23.465  1.00 41.06           C  
ANISOU 1856  CB  ASN A 244     5125   7058   3418   -249     12    128       C  
ATOM   1857  CG  ASN A 244     -18.290  26.025  22.091  1.00 46.53           C  
ANISOU 1857  CG  ASN A 244     5923   7607   4149   -293    -16    117       C  
ATOM   1858  OD1 ASN A 244     -17.362  26.552  21.485  1.00 46.29           O  
ANISOU 1858  OD1 ASN A 244     6023   7450   4114   -274      3     80       O  
ATOM   1859  ND2 ASN A 244     -18.994  25.052  21.565  1.00 37.49           N  
ANISOU 1859  ND2 ASN A 244     4719   6486   3038   -355    -64    148       N  
ATOM   1860  N   TYR A 245     -16.978  28.858  23.054  1.00 41.93           N  
ANISOU 1860  N   TYR A 245     5507   6951   3475   -114     62      7       N  
ATOM   1861  CA  TYR A 245     -16.748  30.267  22.777  1.00 41.28           C  
ANISOU 1861  CA  TYR A 245     5542   6791   3353    -21     62    -53       C  
ATOM   1862  C   TYR A 245     -17.927  31.163  23.307  1.00 47.13           C  
ANISOU 1862  C   TYR A 245     6226   7647   4032    109     32    -92       C  
ATOM   1863  O   TYR A 245     -19.095  30.746  23.308  1.00 46.20           O  
ANISOU 1863  O   TYR A 245     5999   7656   3898    133     -1    -72       O  
ATOM   1864  CB  TYR A 245     -16.473  30.434  21.288  1.00 40.46           C  
ANISOU 1864  CB  TYR A 245     5568   6552   3254    -26     42    -59       C  
ATOM   1865  CG  TYR A 245     -15.106  29.858  21.000  1.00 41.36           C  
ANISOU 1865  CG  TYR A 245     5741   6561   3413   -128     85    -40       C  
ATOM   1866  CD1 TYR A 245     -13.957  30.432  21.552  1.00 42.87           C  
ANISOU 1866  CD1 TYR A 245     5987   6690   3611   -147    132    -60       C  
ATOM   1867  CD2 TYR A 245     -14.960  28.664  20.282  1.00 40.23           C  
ANISOU 1867  CD2 TYR A 245     5584   6395   3307   -206     75     -8       C  
ATOM   1868  CE1 TYR A 245     -12.694  29.879  21.337  1.00 43.05           C  
ANISOU 1868  CE1 TYR A 245     6046   6640   3671   -236    173    -45       C  
ATOM   1869  CE2 TYR A 245     -13.695  28.121  20.029  1.00 39.59           C  
ANISOU 1869  CE2 TYR A 245     5552   6230   3261   -283    113      2       C  
ATOM   1870  CZ  TYR A 245     -12.566  28.721  20.588  1.00 47.95           C  
ANISOU 1870  CZ  TYR A 245     6655   7242   4322   -297    165    -14       C  
ATOM   1871  OH  TYR A 245     -11.296  28.217  20.434  1.00 46.81           O  
ANISOU 1871  OH  TYR A 245     6542   7036   4208   -366    205     -6       O  
ATOM   1872  N   HIS A 246     -17.573  32.359  23.843  1.00 44.15           N  
ANISOU 1872  N   HIS A 246     5919   7232   3625    189     44   -150       N  
ATOM   1873  CA  HIS A 246     -18.522  33.292  24.477  1.00 45.22           C  
ANISOU 1873  CA  HIS A 246     6013   7469   3699    330     17   -203       C  
ATOM   1874  C   HIS A 246     -19.763  33.574  23.627  1.00 50.36           C  
ANISOU 1874  C   HIS A 246     6657   8160   4316    424    -41   -210       C  
ATOM   1875  O   HIS A 246     -20.859  33.615  24.176  1.00 52.67           O  
ANISOU 1875  O   HIS A 246     6826   8621   4566    504    -61   -222       O  
ATOM   1876  CB  HIS A 246     -17.837  34.625  24.853  1.00 45.86           C  
ANISOU 1876  CB  HIS A 246     6219   7443   3764    401     23   -276       C  
ATOM   1877  CG  HIS A 246     -16.835  34.537  25.968  1.00 48.20           C  
ANISOU 1877  CG  HIS A 246     6493   7748   4075    341     69   -290       C  
ATOM   1878  ND1 HIS A 246     -17.012  33.672  27.043  1.00 49.16           N  
ANISOU 1878  ND1 HIS A 246     6459   8034   4186    301     98   -257       N  
ATOM   1879  CD2 HIS A 246     -15.707  35.264  26.177  1.00 48.73           C  
ANISOU 1879  CD2 HIS A 246     6670   7687   4159    321     87   -334       C  
ATOM   1880  CE1 HIS A 246     -15.943  33.841  27.814  1.00 47.58           C  
ANISOU 1880  CE1 HIS A 246     6282   7799   3995    260    131   -282       C  
ATOM   1881  NE2 HIS A 246     -15.161  34.821  27.365  1.00 47.62           N  
ANISOU 1881  NE2 HIS A 246     6440   7635   4017    272    123   -335       N  
ATOM   1882  N   ILE A 247     -19.591  33.736  22.297  1.00 46.37           N  
ANISOU 1882  N   ILE A 247     6275   7519   3825    416    -66   -201       N  
ATOM   1883  CA  ILE A 247     -20.635  34.052  21.327  1.00 45.27           C  
ANISOU 1883  CA  ILE A 247     6154   7396   3651    507   -128   -208       C  
ATOM   1884  C   ILE A 247     -21.849  33.132  21.483  1.00 51.37           C  
ANISOU 1884  C   ILE A 247     6743   8362   4413    499   -155   -179       C  
ATOM   1885  O   ILE A 247     -22.975  33.617  21.396  1.00 52.23           O  
ANISOU 1885  O   ILE A 247     6801   8573   4472    621   -202   -207       O  
ATOM   1886  CB  ILE A 247     -20.108  34.031  19.849  1.00 46.32           C  
ANISOU 1886  CB  ILE A 247     6432   7368   3800    462   -142   -183       C  
ATOM   1887  CG1 ILE A 247     -21.189  34.515  18.829  1.00 46.12           C  
ANISOU 1887  CG1 ILE A 247     6441   7358   3725    578   -213   -194       C  
ATOM   1888  CG2 ILE A 247     -19.497  32.669  19.428  1.00 43.88           C  
ANISOU 1888  CG2 ILE A 247     6089   7040   3544    306   -116   -131       C  
ATOM   1889  CD1 ILE A 247     -21.778  35.940  19.099  1.00 47.90           C  
ANISOU 1889  CD1 ILE A 247     6725   7578   3896    757   -250   -249       C  
ATOM   1890  N   PHE A 248     -21.630  31.823  21.731  1.00 46.54           N  
ANISOU 1890  N   PHE A 248     6032   7802   3850    358   -129   -124       N  
ATOM   1891  CA  PHE A 248     -22.746  30.877  21.876  1.00 46.12           C  
ANISOU 1891  CA  PHE A 248     5803   7923   3798    323   -157    -85       C  
ATOM   1892  C   PHE A 248     -23.662  31.240  23.030  1.00 52.58           C  
ANISOU 1892  C   PHE A 248     6475   8940   4561    413   -152   -102       C  
ATOM   1893  O   PHE A 248     -24.874  31.117  22.907  1.00 55.77           O  
ANISOU 1893  O   PHE A 248     6763   9494   4934    465   -193   -101       O  
ATOM   1894  CB  PHE A 248     -22.234  29.449  22.052  1.00 45.12           C  
ANISOU 1894  CB  PHE A 248     5614   7789   3739    152   -130    -18       C  
ATOM   1895  CG  PHE A 248     -21.566  28.909  20.815  1.00 44.10           C  
ANISOU 1895  CG  PHE A 248     5600   7498   3656     72   -146     -8       C  
ATOM   1896  CD1 PHE A 248     -22.313  28.553  19.701  1.00 45.91           C  
ANISOU 1896  CD1 PHE A 248     5824   7734   3885     69   -209     -9       C  
ATOM   1897  CD2 PHE A 248     -20.185  28.745  20.765  1.00 44.54           C  
ANISOU 1897  CD2 PHE A 248     5765   7410   3750      3    -99     -2       C  
ATOM   1898  CE1 PHE A 248     -21.694  28.055  18.545  1.00 45.80           C  
ANISOU 1898  CE1 PHE A 248     5918   7581   3901      6   -225     -8       C  
ATOM   1899  CE2 PHE A 248     -19.568  28.234  19.621  1.00 47.13           C  
ANISOU 1899  CE2 PHE A 248     6191   7608   4109    -59   -110      2       C  
ATOM   1900  CZ  PHE A 248     -20.328  27.910  18.505  1.00 45.03           C  
ANISOU 1900  CZ  PHE A 248     5926   7346   3835    -54   -173     -3       C  
ATOM   1901  N   TYR A 249     -23.096  31.725  24.126  1.00 49.12           N  
ANISOU 1901  N   TYR A 249     6041   8515   4106    441   -104   -125       N  
ATOM   1902  CA  TYR A 249     -23.844  32.057  25.338  1.00 49.44           C  
ANISOU 1902  CA  TYR A 249     5942   8758   4085    531    -90   -146       C  
ATOM   1903  C   TYR A 249     -24.392  33.474  25.267  1.00 54.56           C  
ANISOU 1903  C   TYR A 249     6652   9411   4666    728   -127   -235       C  
ATOM   1904  O   TYR A 249     -25.494  33.703  25.734  1.00 54.42           O  
ANISOU 1904  O   TYR A 249     6504   9587   4588    833   -145   -257       O  
ATOM   1905  CB  TYR A 249     -22.958  31.836  26.578  1.00 48.67           C  
ANISOU 1905  CB  TYR A 249     5817   8681   3992    472    -27   -132       C  
ATOM   1906  CG  TYR A 249     -22.341  30.454  26.574  1.00 47.02           C  
ANISOU 1906  CG  TYR A 249     5572   8438   3855    288      2    -41       C  
ATOM   1907  CD1 TYR A 249     -21.129  30.222  25.941  1.00 47.79           C  
ANISOU 1907  CD1 TYR A 249     5812   8332   4016    201     15    -34       C  
ATOM   1908  CD2 TYR A 249     -23.044  29.348  27.066  1.00 47.08           C  
ANISOU 1908  CD2 TYR A 249     5405   8612   3870    201     10     40       C  
ATOM   1909  CE1 TYR A 249     -20.599  28.946  25.834  1.00 46.27           C  
ANISOU 1909  CE1 TYR A 249     5593   8097   3888     50     32     41       C  
ATOM   1910  CE2 TYR A 249     -22.521  28.056  26.958  1.00 46.29           C  
ANISOU 1910  CE2 TYR A 249     5289   8455   3845     36     23    124       C  
ATOM   1911  CZ  TYR A 249     -21.297  27.869  26.331  1.00 49.00           C  
ANISOU 1911  CZ  TYR A 249     5782   8589   4248    -30     32    118       C  
ATOM   1912  OH  TYR A 249     -20.707  26.646  26.174  1.00 53.34           O  
ANISOU 1912  OH  TYR A 249     6331   9065   4870   -172     40    187       O  
ATOM   1913  N   ARG A 250     -23.637  34.412  24.670  1.00 52.74           N  
ANISOU 1913  N   ARG A 250     6620   8973   4447    778   -140   -284       N  
ATOM   1914  CA  ARG A 250     -24.082  35.790  24.470  1.00 53.96           C  
ANISOU 1914  CA  ARG A 250     6868   9085   4548    965   -185   -366       C  
ATOM   1915  C   ARG A 250     -25.319  35.811  23.587  1.00 61.79           C  
ANISOU 1915  C   ARG A 250     7810  10161   5508   1051   -249   -363       C  
ATOM   1916  O   ARG A 250     -26.258  36.547  23.879  1.00 64.49           O  
ANISOU 1916  O   ARG A 250     8100  10618   5784   1220   -285   -419       O  
ATOM   1917  CB  ARG A 250     -22.965  36.637  23.859  1.00 50.88           C  
ANISOU 1917  CB  ARG A 250     6707   8435   4190    963   -188   -392       C  
ATOM   1918  CG  ARG A 250     -21.877  36.915  24.864  1.00 44.33           C  
ANISOU 1918  CG  ARG A 250     5923   7544   3377    923   -140   -425       C  
ATOM   1919  CD  ARG A 250     -20.666  37.576  24.223  1.00 54.54           C  
ANISOU 1919  CD  ARG A 250     7423   8583   4715    872   -134   -432       C  
ATOM   1920  NE  ARG A 250     -19.564  37.617  25.185  1.00 64.52           N  
ANISOU 1920  NE  ARG A 250     8703   9808   6003    800    -86   -454       N  
ATOM   1921  CZ  ARG A 250     -18.458  38.340  25.057  1.00 72.09           C  
ANISOU 1921  CZ  ARG A 250     9818  10578   6995    765    -77   -481       C  
ATOM   1922  NH1 ARG A 250     -18.281  39.114  23.997  1.00 57.44           N  
ANISOU 1922  NH1 ARG A 250     8129   8545   5152    792   -109   -479       N  
ATOM   1923  NH2 ARG A 250     -17.536  38.322  26.009  1.00 56.78           N  
ANISOU 1923  NH2 ARG A 250     7868   8633   5073    702    -39   -508       N  
ATOM   1924  N   LEU A 251     -25.348  34.941  22.557  1.00 56.64           N  
ANISOU 1924  N   LEU A 251     7158   9467   4897    938   -266   -301       N  
ATOM   1925  CA  LEU A 251     -26.447  34.805  21.620  1.00 57.52           C  
ANISOU 1925  CA  LEU A 251     7217   9656   4983    994   -331   -294       C  
ATOM   1926  C   LEU A 251     -27.654  34.136  22.284  1.00 60.89           C  
ANISOU 1926  C   LEU A 251     7401  10355   5380    996   -337   -276       C  
ATOM   1927  O   LEU A 251     -28.765  34.649  22.155  1.00 60.13           O  
ANISOU 1927  O   LEU A 251     7230  10391   5224   1140   -388   -313       O  
ATOM   1928  CB  LEU A 251     -25.963  34.008  20.383  1.00 57.09           C  
ANISOU 1928  CB  LEU A 251     7241   9470   4982    858   -345   -242       C  
ATOM   1929  CG  LEU A 251     -26.737  34.034  19.092  1.00 63.23           C  
ANISOU 1929  CG  LEU A 251     8041  10249   5734    912   -419   -242       C  
ATOM   1930  CD1 LEU A 251     -26.935  35.444  18.582  1.00 64.65           C  
ANISOU 1930  CD1 LEU A 251     8367  10341   5857   1099   -464   -293       C  
ATOM   1931  CD2 LEU A 251     -26.002  33.217  18.047  1.00 64.59           C  
ANISOU 1931  CD2 LEU A 251     8302  10282   5957    768   -418   -199       C  
ATOM   1932  N   CYS A 252     -27.459  33.016  23.003  1.00 57.49           N  
ANISOU 1932  N   CYS A 252     6841  10014   4989    841   -288   -215       N  
ATOM   1933  CA  CYS A 252     -28.596  32.357  23.671  1.00 57.99           C  
ANISOU 1933  CA  CYS A 252     6666  10345   5024    826   -288   -182       C  
ATOM   1934  C   CYS A 252     -29.179  33.266  24.778  1.00 62.42           C  
ANISOU 1934  C   CYS A 252     7140  11079   5498    999   -272   -243       C  
ATOM   1935  O   CYS A 252     -30.395  33.361  24.881  1.00 63.32           O  
ANISOU 1935  O   CYS A 252     7102  11402   5555   1092   -303   -258       O  
ATOM   1936  CB  CYS A 252     -28.212  30.981  24.212  1.00 57.44           C  
ANISOU 1936  CB  CYS A 252     6491  10316   5016    619   -240    -91       C  
ATOM   1937  SG  CYS A 252     -27.890  29.740  22.924  1.00 60.67           S  
ANISOU 1937  SG  CYS A 252     6955  10577   5520    432   -278    -31       S  
ATOM   1938  N   ALA A 253     -28.334  34.005  25.512  1.00 57.34           N  
ANISOU 1938  N   ALA A 253     6599  10347   4839   1055   -231   -290       N  
ATOM   1939  CA  ALA A 253     -28.809  34.896  26.569  1.00 59.26           C  
ANISOU 1939  CA  ALA A 253     6777  10744   4996   1230   -220   -364       C  
ATOM   1940  C   ALA A 253     -29.393  36.224  26.071  1.00 67.47           C  
ANISOU 1940  C   ALA A 253     7908  11748   5979   1458   -287   -461       C  
ATOM   1941  O   ALA A 253     -30.334  36.703  26.709  1.00 69.74           O  
ANISOU 1941  O   ALA A 253     8069  12244   6184   1616   -299   -515       O  
ATOM   1942  CB  ALA A 253     -27.692  35.200  27.556  1.00 59.01           C  
ANISOU 1942  CB  ALA A 253     6825  10627   4968   1212   -164   -392       C  
ATOM   1943  N   GLY A 254     -28.819  36.815  24.999  1.00 62.21           N  
ANISOU 1943  N   GLY A 254     7458  10829   5352   1478   -327   -481       N  
ATOM   1944  CA  GLY A 254     -29.174  38.150  24.527  1.00 61.79           C  
ANISOU 1944  CA  GLY A 254     7536  10687   5252   1690   -392   -565       C  
ATOM   1945  C   GLY A 254     -30.021  38.328  23.286  1.00 66.84           C  
ANISOU 1945  C   GLY A 254     8195  11326   5875   1773   -469   -561       C  
ATOM   1946  O   GLY A 254     -30.717  39.340  23.175  1.00 66.80           O  
ANISOU 1946  O   GLY A 254     8220  11352   5808   1986   -526   -632       O  
ATOM   1947  N   ALA A 255     -29.953  37.392  22.324  1.00 63.30           N  
ANISOU 1947  N   ALA A 255     7741  10832   5476   1621   -479   -485       N  
ATOM   1948  CA  ALA A 255     -30.711  37.506  21.074  1.00 64.22           C  
ANISOU 1948  CA  ALA A 255     7881  10947   5572   1693   -558   -480       C  
ATOM   1949  C   ALA A 255     -32.194  37.782  21.338  1.00 70.07           C  
ANISOU 1949  C   ALA A 255     8438  11953   6234   1865   -607   -524       C  
ATOM   1950  O   ALA A 255     -32.754  37.266  22.298  1.00 71.09           O  
ANISOU 1950  O   ALA A 255     8356  12315   6340   1842   -571   -519       O  
ATOM   1951  CB  ALA A 255     -30.559  36.245  20.243  1.00 63.98           C  
ANISOU 1951  CB  ALA A 255     7814  10895   5600   1492   -559   -401       C  
ATOM   1952  N   SER A 256     -32.796  38.649  20.530  1.00 66.40           N  
ANISOU 1952  N   SER A 256     8053  11454   5720   2047   -687   -566       N  
ATOM   1953  CA  SER A 256     -34.211  38.977  20.602  1.00 68.53           C  
ANISOU 1953  CA  SER A 256     8159  11967   5910   2233   -747   -613       C  
ATOM   1954  C   SER A 256     -35.045  37.712  20.311  1.00 76.91           C  
ANISOU 1954  C   SER A 256     8988  13252   6981   2096   -758   -554       C  
ATOM   1955  O   SER A 256     -34.536  36.797  19.650  1.00 76.91           O  
ANISOU 1955  O   SER A 256     9023  13150   7048   1898   -750   -488       O  
ATOM   1956  CB  SER A 256     -34.527  40.065  19.575  1.00 72.49           C  
ANISOU 1956  CB  SER A 256     8832  12343   6370   2435   -838   -655       C  
ATOM   1957  OG  SER A 256     -34.403  39.601  18.236  1.00 78.61           O  
ANISOU 1957  OG  SER A 256     9686  13011   7172   2340   -880   -597       O  
ATOM   1958  N   GLU A 257     -36.325  37.669  20.733  1.00 75.51           N  
ANISOU 1958  N   GLU A 257     8579  13372   6737   2205   -784   -582       N  
ATOM   1959  CA  GLU A 257     -37.191  36.522  20.436  1.00 76.34           C  
ANISOU 1959  CA  GLU A 257     8456  13695   6855   2072   -805   -527       C  
ATOM   1960  C   GLU A 257     -37.338  36.298  18.908  1.00 81.52           C  
ANISOU 1960  C   GLU A 257     9202  14240   7532   2039   -890   -508       C  
ATOM   1961  O   GLU A 257     -37.592  35.171  18.463  1.00 80.34           O  
ANISOU 1961  O   GLU A 257     8937  14161   7428   1856   -904   -453       O  
ATOM   1962  CB  GLU A 257     -38.565  36.688  21.094  1.00 79.47           C  
ANISOU 1962  CB  GLU A 257     8592  14439   7165   2218   -823   -567       C  
ATOM   1963  CG  GLU A 257     -38.639  36.046  22.468  1.00 87.38           C  
ANISOU 1963  CG  GLU A 257     9388  15649   8164   2110   -732   -531       C  
ATOM   1964  CD  GLU A 257     -38.423  34.545  22.509  1.00107.50           C  
ANISOU 1964  CD  GLU A 257    11818  18231  10796   1808   -691   -422       C  
ATOM   1965  OE1 GLU A 257     -38.996  33.826  21.657  1.00108.81           O  
ANISOU 1965  OE1 GLU A 257    11893  18458  10991   1707   -748   -385       O  
ATOM   1966  OE2 GLU A 257     -37.670  34.086  23.395  1.00104.35           O  
ANISOU 1966  OE2 GLU A 257    11421  17794  10434   1675   -607   -376       O  
ATOM   1967  N   ASP A 258     -37.112  37.366  18.116  1.00 79.41           N  
ANISOU 1967  N   ASP A 258     9152  13788   7232   2211   -946   -551       N  
ATOM   1968  CA  ASP A 258     -37.158  37.301  16.663  1.00 79.53           C  
ANISOU 1968  CA  ASP A 258     9282  13688   7250   2205  -1025   -534       C  
ATOM   1969  C   ASP A 258     -35.919  36.565  16.149  1.00 81.19           C  
ANISOU 1969  C   ASP A 258     9643  13662   7545   1975   -981   -472       C  
ATOM   1970  O   ASP A 258     -36.049  35.682  15.288  1.00 80.94           O  
ANISOU 1970  O   ASP A 258     9571  13640   7543   1839  -1016   -437       O  
ATOM   1971  CB  ASP A 258     -37.278  38.704  16.029  1.00 82.79           C  
ANISOU 1971  CB  ASP A 258     9889  13973   7595   2463  -1094   -586       C  
ATOM   1972  CG  ASP A 258     -37.186  38.689  14.510  1.00 98.36           C  
ANISOU 1972  CG  ASP A 258    12009  15805   9559   2460  -1169   -558       C  
ATOM   1973  OD1 ASP A 258     -37.993  37.965  13.871  1.00101.96           O  
ANISOU 1973  OD1 ASP A 258    12319  16423  10000   2416  -1230   -549       O  
ATOM   1974  OD2 ASP A 258     -36.284  39.370  13.960  1.00102.32           O  
ANISOU 1974  OD2 ASP A 258    12770  16040  10067   2492  -1166   -544       O  
ATOM   1975  N   ILE A 259     -34.726  36.922  16.680  1.00 74.49           N  
ANISOU 1975  N   ILE A 259     8958  12610   6734   1935   -907   -465       N  
ATOM   1976  CA  ILE A 259     -33.468  36.297  16.276  1.00 71.74           C  
ANISOU 1976  CA  ILE A 259     8753  12042   6462   1734   -857   -411       C  
ATOM   1977  C   ILE A 259     -33.466  34.819  16.758  1.00 72.36           C  
ANISOU 1977  C   ILE A 259     8646  12242   6607   1502   -813   -361       C  
ATOM   1978  O   ILE A 259     -33.094  33.932  15.978  1.00 71.57           O  
ANISOU 1978  O   ILE A 259     8579  12058   6556   1344   -823   -322       O  
ATOM   1979  CB  ILE A 259     -32.234  37.130  16.748  1.00 73.63           C  
ANISOU 1979  CB  ILE A 259     9198  12055   6721   1757   -794   -422       C  
ATOM   1980  CG1 ILE A 259     -32.182  38.475  15.964  1.00 74.81           C  
ANISOU 1980  CG1 ILE A 259     9565  12041   6820   1954   -853   -452       C  
ATOM   1981  CG2 ILE A 259     -30.917  36.360  16.538  1.00 71.87           C  
ANISOU 1981  CG2 ILE A 259     9080  11649   6579   1537   -730   -366       C  
ATOM   1982  CD1 ILE A 259     -31.153  39.534  16.472  1.00 81.10           C  
ANISOU 1982  CD1 ILE A 259    10565  12618   7631   2007   -809   -474       C  
ATOM   1983  N   ARG A 260     -33.982  34.564  17.979  1.00 67.04           N  
ANISOU 1983  N   ARG A 260     7772  11775   5926   1495   -772   -362       N  
ATOM   1984  CA  ARG A 260     -34.083  33.237  18.602  1.00 66.04           C  
ANISOU 1984  CA  ARG A 260     7457  11778   5856   1286   -729   -303       C  
ATOM   1985  C   ARG A 260     -34.879  32.263  17.717  1.00 71.95           C  
ANISOU 1985  C   ARG A 260     8081  12632   6626   1182   -800   -277       C  
ATOM   1986  O   ARG A 260     -34.395  31.170  17.429  1.00 70.92           O  
ANISOU 1986  O   ARG A 260     7953  12421   6571    979   -790   -227       O  
ATOM   1987  CB  ARG A 260     -34.734  33.344  20.005  1.00 65.42           C  
ANISOU 1987  CB  ARG A 260     7176  11943   5737   1340   -682   -309       C  
ATOM   1988  CG  ARG A 260     -34.688  32.051  20.824  1.00 71.62           C  
ANISOU 1988  CG  ARG A 260     7788  12844   6580   1120   -623   -230       C  
ATOM   1989  CD  ARG A 260     -35.922  31.786  21.683  1.00 76.38           C  
ANISOU 1989  CD  ARG A 260     8108  13780   7132   1142   -615   -216       C  
ATOM   1990  NE  ARG A 260     -37.174  31.842  20.926  1.00 93.81           N  
ANISOU 1990  NE  ARG A 260    10189  16158   9298   1225   -702   -243       N  
ATOM   1991  CZ  ARG A 260     -37.682  30.842  20.211  1.00115.18           C  
ANISOU 1991  CZ  ARG A 260    12793  18920  12052   1074   -756   -201       C  
ATOM   1992  NH1 ARG A 260     -38.826  31.001  19.557  1.00111.55           N  
ANISOU 1992  NH1 ARG A 260    12213  18627  11543   1167   -840   -236       N  
ATOM   1993  NH2 ARG A 260     -37.044  29.680  20.132  1.00 99.14           N  
ANISOU 1993  NH2 ARG A 260    10780  16772  10117    833   -734   -129       N  
ATOM   1994  N   GLU A 261     -36.081  32.675  17.271  1.00 71.09           N  
ANISOU 1994  N   GLU A 261     7866  12695   6449   1327   -879   -317       N  
ATOM   1995  CA  GLU A 261     -36.997  31.875  16.451  1.00 72.08           C  
ANISOU 1995  CA  GLU A 261     7854  12950   6583   1250   -961   -307       C  
ATOM   1996  C   GLU A 261     -36.442  31.631  15.046  1.00 73.30           C  
ANISOU 1996  C   GLU A 261     8196  12891   6765   1194  -1015   -308       C  
ATOM   1997  O   GLU A 261     -36.477  30.498  14.570  1.00 71.42           O  
ANISOU 1997  O   GLU A 261     7904  12646   6588   1009  -1042   -279       O  
ATOM   1998  CB  GLU A 261     -38.384  32.545  16.371  1.00 75.45           C  
ANISOU 1998  CB  GLU A 261     8128  13621   6917   1452  -1032   -359       C  
ATOM   1999  N   ARG A 262     -35.912  32.687  14.409  1.00 69.56           N  
ANISOU 1999  N   ARG A 262     7946  12240   6244   1350  -1030   -341       N  
ATOM   2000  CA  ARG A 262     -35.319  32.657  13.074  1.00 68.94           C  
ANISOU 2000  CA  ARG A 262     8065  11961   6167   1329  -1074   -341       C  
ATOM   2001  C   ARG A 262     -34.100  31.699  13.039  1.00 69.98           C  
ANISOU 2001  C   ARG A 262     8288  11911   6389   1107  -1011   -297       C  
ATOM   2002  O   ARG A 262     -33.973  30.927  12.090  1.00 69.82           O  
ANISOU 2002  O   ARG A 262     8300  11834   6394   1000  -1056   -292       O  
ATOM   2003  CB  ARG A 262     -34.915  34.093  12.682  1.00 72.40           C  
ANISOU 2003  CB  ARG A 262     8726  12244   6540   1536  -1080   -366       C  
ATOM   2004  CG  ARG A 262     -34.449  34.302  11.248  1.00 86.32           C  
ANISOU 2004  CG  ARG A 262    10691  13833   8273   1560  -1131   -361       C  
ATOM   2005  CD  ARG A 262     -33.805  35.669  11.100  1.00 98.37           C  
ANISOU 2005  CD  ARG A 262    12451  15170   9755   1719  -1112   -363       C  
ATOM   2006  NE  ARG A 262     -34.566  36.554  10.215  1.00110.67           N  
ANISOU 2006  NE  ARG A 262    14076  16754  11221   1928  -1207   -385       N  
ATOM   2007  CZ  ARG A 262     -35.073  37.729  10.578  1.00125.17           C  
ANISOU 2007  CZ  ARG A 262    15940  18618  13000   2147  -1234   -416       C  
ATOM   2008  NH1 ARG A 262     -34.910  38.176  11.817  1.00104.65           N  
ANISOU 2008  NH1 ARG A 262    13307  16031  10424   2186  -1173   -437       N  
ATOM   2009  NH2 ARG A 262     -35.740  38.469   9.701  1.00119.94           N  
ANISOU 2009  NH2 ARG A 262    15347  17971  12254   2337  -1327   -430       N  
ATOM   2010  N   LEU A 263     -33.239  31.725  14.086  1.00 63.31           N  
ANISOU 2010  N   LEU A 263     7476  10990   5589   1045   -914   -271       N  
ATOM   2011  CA  LEU A 263     -32.050  30.875  14.187  1.00 61.36           C  
ANISOU 2011  CA  LEU A 263     7308  10580   5424    853   -850   -230       C  
ATOM   2012  C   LEU A 263     -32.319  29.547  14.925  1.00 67.22           C  
ANISOU 2012  C   LEU A 263     7854  11444   6241    662   -830   -188       C  
ATOM   2013  O   LEU A 263     -31.396  28.742  15.089  1.00 66.39           O  
ANISOU 2013  O   LEU A 263     7800  11216   6209    503   -783   -152       O  
ATOM   2014  CB  LEU A 263     -30.903  31.631  14.880  1.00 60.01           C  
ANISOU 2014  CB  LEU A 263     7288  10251   5262    886   -762   -224       C  
ATOM   2015  CG  LEU A 263     -30.383  32.900  14.201  1.00 64.65           C  
ANISOU 2015  CG  LEU A 263     8098  10673   5795   1038   -770   -250       C  
ATOM   2016  CD1 LEU A 263     -29.215  33.464  14.963  1.00 64.13           C  
ANISOU 2016  CD1 LEU A 263     8154  10458   5753   1029   -684   -243       C  
ATOM   2017  CD2 LEU A 263     -29.968  32.639  12.766  1.00 66.91           C  
ANISOU 2017  CD2 LEU A 263     8526  10823   6073   1001   -812   -242       C  
ATOM   2018  N   HIS A 264     -33.575  29.331  15.377  1.00 65.57           N  
ANISOU 2018  N   HIS A 264     7423  11478   6013    678   -865   -187       N  
ATOM   2019  CA  HIS A 264     -34.067  28.145  16.093  1.00 65.91           C  
ANISOU 2019  CA  HIS A 264     7255  11671   6118    501   -853   -135       C  
ATOM   2020  C   HIS A 264     -33.204  27.841  17.337  1.00 66.53           C  
ANISOU 2020  C   HIS A 264     7335  11699   6246    404   -748    -82       C  
ATOM   2021  O   HIS A 264     -32.886  26.687  17.617  1.00 66.09           O  
ANISOU 2021  O   HIS A 264     7230  11610   6270    211   -729    -25       O  
ATOM   2022  CB  HIS A 264     -34.171  26.924  15.153  1.00 67.61           C  
ANISOU 2022  CB  HIS A 264     7452  11838   6400    329   -923   -124       C  
ATOM   2023  CG  HIS A 264     -35.061  27.159  13.969  1.00 72.63           C  
ANISOU 2023  CG  HIS A 264     8070  12544   6982    419  -1033   -179       C  
ATOM   2024  ND1 HIS A 264     -36.440  27.111  14.083  1.00 76.43           N  
ANISOU 2024  ND1 HIS A 264     8332  13279   7431    451  -1093   -188       N  
ATOM   2025  CD2 HIS A 264     -34.740  27.477  12.692  1.00 74.39           C  
ANISOU 2025  CD2 HIS A 264     8466  12629   7171    488  -1089   -224       C  
ATOM   2026  CE1 HIS A 264     -36.911  27.379  12.874  1.00 76.52           C  
ANISOU 2026  CE1 HIS A 264     8390  13293   7393    539  -1190   -243       C  
ATOM   2027  NE2 HIS A 264     -35.928  27.602  12.003  1.00 75.85           N  
ANISOU 2027  NE2 HIS A 264     8542  12976   7303    565  -1190   -264       N  
ATOM   2028  N   LEU A 265     -32.843  28.890  18.079  1.00 61.00           N  
ANISOU 2028  N   LEU A 265     6693  10991   5494    542   -688   -103       N  
ATOM   2029  CA  LEU A 265     -32.059  28.781  19.297  1.00 60.52           C  
ANISOU 2029  CA  LEU A 265     6632  10902   5460    482   -593    -64       C  
ATOM   2030  C   LEU A 265     -32.967  28.464  20.494  1.00 67.18           C  
ANISOU 2030  C   LEU A 265     7229  12013   6282    458   -563    -24       C  
ATOM   2031  O   LEU A 265     -34.183  28.635  20.413  1.00 67.96           O  
ANISOU 2031  O   LEU A 265     7171  12319   6331    532   -610    -42       O  
ATOM   2032  CB  LEU A 265     -31.283  30.078  19.551  1.00 60.14           C  
ANISOU 2032  CB  LEU A 265     6758  10727   5364    641   -551   -115       C  
ATOM   2033  CG  LEU A 265     -30.237  30.494  18.491  1.00 64.69           C  
ANISOU 2033  CG  LEU A 265     7585  11038   5958    656   -562   -140       C  
ATOM   2034  CD1 LEU A 265     -29.891  31.949  18.637  1.00 66.12           C  
ANISOU 2034  CD1 LEU A 265     7910  11133   6080    840   -546   -195       C  
ATOM   2035  CD2 LEU A 265     -28.949  29.668  18.589  1.00 62.21           C  
ANISOU 2035  CD2 LEU A 265     7359  10555   5724    481   -506    -95       C  
ATOM   2036  N   SER A 266     -32.375  27.981  21.598  1.00 63.73           N  
ANISOU 2036  N   SER A 266     6753  11582   5878    353   -484     34       N  
ATOM   2037  CA  SER A 266     -33.052  27.673  22.865  1.00 63.93           C  
ANISOU 2037  CA  SER A 266     6558  11857   5876    320   -437     87       C  
ATOM   2038  C   SER A 266     -32.016  27.717  23.968  1.00 67.56           C  
ANISOU 2038  C   SER A 266     7077  12251   6341    292   -346    116       C  
ATOM   2039  O   SER A 266     -30.966  28.325  23.766  1.00 68.66           O  
ANISOU 2039  O   SER A 266     7416  12184   6488    349   -327     70       O  
ATOM   2040  CB  SER A 266     -33.781  26.330  22.814  1.00 66.93           C  
ANISOU 2040  CB  SER A 266     6755  12357   6317    120   -466    173       C  
ATOM   2041  OG  SER A 266     -32.993  25.289  22.266  1.00 74.94           O  
ANISOU 2041  OG  SER A 266     7876  13161   7435    -63   -480    217       O  
ATOM   2042  N   SER A 267     -32.291  27.112  25.135  1.00 62.24           N  
ANISOU 2042  N   SER A 267     6231  11759   5660    207   -291    193       N  
ATOM   2043  CA  SER A 267     -31.337  27.106  26.232  1.00 60.02           C  
ANISOU 2043  CA  SER A 267     5993  11438   5375    182   -209    223       C  
ATOM   2044  C   SER A 267     -30.123  26.214  25.862  1.00 60.16           C  
ANISOU 2044  C   SER A 267     6158  11203   5499     13   -200    273       C  
ATOM   2045  O   SER A 267     -30.276  25.259  25.092  1.00 59.86           O  
ANISOU 2045  O   SER A 267     6113  11094   5538   -127   -248    315       O  
ATOM   2046  CB  SER A 267     -32.003  26.681  27.543  1.00 62.84           C  
ANISOU 2046  CB  SER A 267     6121  12072   5683    138   -154    301       C  
ATOM   2047  OG  SER A 267     -32.842  25.549  27.409  1.00 69.63           O  
ANISOU 2047  OG  SER A 267     6806  13060   6588    -28   -180    396       O  
ATOM   2048  N   PRO A 268     -28.914  26.544  26.360  1.00 54.68           N  
ANISOU 2048  N   PRO A 268     5599  10369   4807     33   -145    257       N  
ATOM   2049  CA  PRO A 268     -27.703  25.800  25.962  1.00 54.21           C  
ANISOU 2049  CA  PRO A 268     5685  10073   4840   -102   -138    291       C  
ATOM   2050  C   PRO A 268     -27.715  24.274  26.139  1.00 58.74           C  
ANISOU 2050  C   PRO A 268     6170  10650   5497   -310   -140    406       C  
ATOM   2051  O   PRO A 268     -26.998  23.592  25.417  1.00 59.15           O  
ANISOU 2051  O   PRO A 268     6338  10506   5631   -410   -164    417       O  
ATOM   2052  CB  PRO A 268     -26.619  26.414  26.858  1.00 54.65           C  
ANISOU 2052  CB  PRO A 268     5830  10069   4865    -41    -71    266       C  
ATOM   2053  CG  PRO A 268     -27.072  27.813  27.064  1.00 58.75           C  
ANISOU 2053  CG  PRO A 268     6357  10677   5290    161    -72    170       C  
ATOM   2054  CD  PRO A 268     -28.562  27.676  27.245  1.00 55.85           C  
ANISOU 2054  CD  PRO A 268     5784  10564   4873    191    -96    193       C  
ATOM   2055  N   ASP A 269     -28.465  23.749  27.106  1.00 54.28           N  
ANISOU 2055  N   ASP A 269     5412  10302   4910   -374   -113    491       N  
ATOM   2056  CA  ASP A 269     -28.593  22.317  27.382  1.00 53.63           C  
ANISOU 2056  CA  ASP A 269     5235  10235   4905   -578   -117    616       C  
ATOM   2057  C   ASP A 269     -29.210  21.538  26.186  1.00 56.87           C  
ANISOU 2057  C   ASP A 269     5632  10581   5396   -688   -204    624       C  
ATOM   2058  O   ASP A 269     -29.098  20.315  26.148  1.00 56.09           O  
ANISOU 2058  O   ASP A 269     5512  10412   5386   -865   -225    711       O  
ATOM   2059  CB  ASP A 269     -29.449  22.110  28.650  1.00 56.51           C  
ANISOU 2059  CB  ASP A 269     5377  10885   5207   -605    -69    707       C  
ATOM   2060  CG  ASP A 269     -30.853  22.703  28.540  1.00 66.64           C  
ANISOU 2060  CG  ASP A 269     6497  12408   6415   -511    -94    670       C  
ATOM   2061  OD1 ASP A 269     -30.960  23.937  28.346  1.00 63.89           O  
ANISOU 2061  OD1 ASP A 269     6199  12087   5989   -316    -97    556       O  
ATOM   2062  OD2 ASP A 269     -31.851  21.929  28.693  1.00 72.49           O  
ANISOU 2062  OD2 ASP A 269     7054  13316   7174   -633   -113    758       O  
ATOM   2063  N   ASN A 270     -29.835  22.245  25.203  1.00 53.80           N  
ANISOU 2063  N   ASN A 270     5261  10206   4974   -580   -261    530       N  
ATOM   2064  CA  ASN A 270     -30.443  21.624  24.028  1.00 53.63           C  
ANISOU 2064  CA  ASN A 270     5229  10133   5013   -664   -352    517       C  
ATOM   2065  C   ASN A 270     -29.429  21.420  22.900  1.00 57.13           C  
ANISOU 2065  C   ASN A 270     5891  10294   5520   -682   -389    460       C  
ATOM   2066  O   ASN A 270     -29.796  20.888  21.842  1.00 57.48           O  
ANISOU 2066  O   ASN A 270     5955  10274   5613   -744   -470    435       O  
ATOM   2067  CB  ASN A 270     -31.638  22.449  23.550  1.00 57.18           C  
ANISOU 2067  CB  ASN A 270     5583  10756   5387   -532   -398    448       C  
ATOM   2068  CG  ASN A 270     -32.736  22.516  24.596  1.00 75.33           C  
ANISOU 2068  CG  ASN A 270     7640  13360   7621   -522   -366    505       C  
ATOM   2069  OD1 ASN A 270     -33.323  21.505  24.981  1.00 69.48           O  
ANISOU 2069  OD1 ASN A 270     6739  12735   6925   -689   -373    604       O  
ATOM   2070  ND2 ASN A 270     -32.919  23.676  25.198  1.00 66.14           N  
ANISOU 2070  ND2 ASN A 270     6451  12329   6351   -333   -321    450       N  
ATOM   2071  N   PHE A 271     -28.136  21.769  23.136  1.00 51.53           N  
ANISOU 2071  N   PHE A 271     5341   9427   4811   -636   -332    441       N  
ATOM   2072  CA  PHE A 271     -27.122  21.625  22.092  1.00 50.13           C  
ANISOU 2072  CA  PHE A 271     5362   9003   4682   -645   -358    387       C  
ATOM   2073  C   PHE A 271     -25.961  20.779  22.569  1.00 53.77           C  
ANISOU 2073  C   PHE A 271     5895   9321   5214   -755   -318    445       C  
ATOM   2074  O   PHE A 271     -25.300  21.124  23.551  1.00 52.92           O  
ANISOU 2074  O   PHE A 271     5797   9230   5079   -721   -245    470       O  
ATOM   2075  CB  PHE A 271     -26.644  23.008  21.585  1.00 50.59           C  
ANISOU 2075  CB  PHE A 271     5565   8989   4668   -466   -341    290       C  
ATOM   2076  CG  PHE A 271     -27.790  23.877  21.098  1.00 52.29           C  
ANISOU 2076  CG  PHE A 271     5720   9340   4810   -339   -389    233       C  
ATOM   2077  CD1 PHE A 271     -28.309  23.723  19.815  1.00 55.25           C  
ANISOU 2077  CD1 PHE A 271     6125   9675   5193   -336   -472    189       C  
ATOM   2078  CD2 PHE A 271     -28.382  24.811  21.939  1.00 55.03           C  
ANISOU 2078  CD2 PHE A 271     5969   9866   5076   -215   -355    221       C  
ATOM   2079  CE1 PHE A 271     -29.381  24.511  19.374  1.00 56.87           C  
ANISOU 2079  CE1 PHE A 271     6268  10013   5326   -210   -521    139       C  
ATOM   2080  CE2 PHE A 271     -29.450  25.602  21.496  1.00 58.82           C  
ANISOU 2080  CE2 PHE A 271     6388  10474   5486    -83   -404    166       C  
ATOM   2081  CZ  PHE A 271     -29.935  25.455  20.212  1.00 56.12           C  
ANISOU 2081  CZ  PHE A 271     6081  10088   5155    -80   -487    128       C  
ATOM   2082  N   ARG A 272     -25.677  19.684  21.834  1.00 49.56           N  
ANISOU 2082  N   ARG A 272     5420   8642   4770   -875   -372    457       N  
ATOM   2083  CA  ARG A 272     -24.555  18.796  22.136  1.00 48.15           C  
ANISOU 2083  CA  ARG A 272     5322   8307   4665   -970   -347    504       C  
ATOM   2084  C   ARG A 272     -23.229  19.573  22.205  1.00 50.84           C  
ANISOU 2084  C   ARG A 272     5813   8534   4970   -868   -282    453       C  
ATOM   2085  O   ARG A 272     -22.390  19.283  23.059  1.00 52.65           O  
ANISOU 2085  O   ARG A 272     6057   8729   5218   -900   -229    502       O  
ATOM   2086  CB  ARG A 272     -24.470  17.681  21.100  1.00 49.00           C  
ANISOU 2086  CB  ARG A 272     5495   8259   4862  -1077   -428    490       C  
ATOM   2087  CG  ARG A 272     -23.356  16.668  21.333  1.00 62.56           C  
ANISOU 2087  CG  ARG A 272     7298   9810   6663  -1168   -416    535       C  
ATOM   2088  CD  ARG A 272     -22.914  16.043  20.032  1.00 73.48           C  
ANISOU 2088  CD  ARG A 272     8814  11004   8101  -1192   -485    462       C  
ATOM   2089  NE  ARG A 272     -23.300  14.634  19.912  1.00 89.35           N  
ANISOU 2089  NE  ARG A 272    10788  12943  10216  -1348   -562    512       N  
ATOM   2090  CZ  ARG A 272     -24.464  14.188  19.438  1.00105.44           C  
ANISOU 2090  CZ  ARG A 272    12736  15040  12286  -1428   -646    512       C  
ATOM   2091  NH1 ARG A 272     -24.690  12.885  19.338  1.00 97.56           N  
ANISOU 2091  NH1 ARG A 272    11724  13949  11395  -1579   -719    555       N  
ATOM   2092  NH2 ARG A 272     -25.412  15.044  19.064  1.00 84.44           N  
ANISOU 2092  NH2 ARG A 272     9999  12530   9553  -1358   -661    468       N  
ATOM   2093  N   TYR A 273     -23.071  20.597  21.376  1.00 45.31           N  
ANISOU 2093  N   TYR A 273     5213   7788   4214   -747   -287    361       N  
ATOM   2094  CA  TYR A 273     -21.837  21.388  21.325  1.00 44.02           C  
ANISOU 2094  CA  TYR A 273     5192   7513   4019   -662   -230    312       C  
ATOM   2095  C   TYR A 273     -21.677  22.305  22.537  1.00 48.31           C  
ANISOU 2095  C   TYR A 273     5693   8162   4501   -584   -160    321       C  
ATOM   2096  O   TYR A 273     -20.637  22.947  22.688  1.00 47.78           O  
ANISOU 2096  O   TYR A 273     5730   8012   4414   -529   -111    287       O  
ATOM   2097  CB  TYR A 273     -21.768  22.170  20.005  1.00 43.94           C  
ANISOU 2097  CB  TYR A 273     5307   7420   3969   -569   -261    223       C  
ATOM   2098  CG  TYR A 273     -21.418  21.292  18.820  1.00 43.81           C  
ANISOU 2098  CG  TYR A 273     5378   7264   4006   -634   -315    198       C  
ATOM   2099  CD1 TYR A 273     -21.092  19.943  18.996  1.00 44.79           C  
ANISOU 2099  CD1 TYR A 273     5483   7320   4216   -760   -333    244       C  
ATOM   2100  CD2 TYR A 273     -21.352  21.817  17.535  1.00 44.57           C  
ANISOU 2100  CD2 TYR A 273     5584   7288   4060   -562   -348    127       C  
ATOM   2101  CE1 TYR A 273     -20.725  19.142  17.924  1.00 43.62           C  
ANISOU 2101  CE1 TYR A 273     5423   7038   4114   -805   -386    206       C  
ATOM   2102  CE2 TYR A 273     -21.030  21.011  16.441  1.00 46.63           C  
ANISOU 2102  CE2 TYR A 273     5925   7435   4358   -610   -398     93       C  
ATOM   2103  CZ  TYR A 273     -20.691  19.680  16.650  1.00 49.43           C  
ANISOU 2103  CZ  TYR A 273     6260   7722   4800   -729   -417    126       C  
ATOM   2104  OH  TYR A 273     -20.402  18.875  15.604  1.00 41.32           O  
ANISOU 2104  OH  TYR A 273     5311   6582   3807   -766   -473     81       O  
ATOM   2105  N   LEU A 274     -22.673  22.308  23.435  1.00 46.18           N  
ANISOU 2105  N   LEU A 274     5263   8080   4201   -586   -154    369       N  
ATOM   2106  CA  LEU A 274     -22.610  23.099  24.661  1.00 45.71           C  
ANISOU 2106  CA  LEU A 274     5147   8145   4075   -507    -91    374       C  
ATOM   2107  C   LEU A 274     -22.930  22.308  25.901  1.00 49.44           C  
ANISOU 2107  C   LEU A 274     5471   8758   4557   -595    -62    476       C  
ATOM   2108  O   LEU A 274     -22.473  22.686  26.957  1.00 50.01           O  
ANISOU 2108  O   LEU A 274     5524   8891   4588   -556     -4    488       O  
ATOM   2109  CB  LEU A 274     -23.612  24.282  24.607  1.00 46.30           C  
ANISOU 2109  CB  LEU A 274     5171   8356   4064   -366   -105    313       C  
ATOM   2110  CG  LEU A 274     -23.661  25.192  23.373  1.00 48.80           C  
ANISOU 2110  CG  LEU A 274     5614   8573   4355   -261   -146    223       C  
ATOM   2111  CD1 LEU A 274     -24.823  26.137  23.468  1.00 49.08           C  
ANISOU 2111  CD1 LEU A 274     5565   8769   4311   -130   -170    182       C  
ATOM   2112  CD2 LEU A 274     -22.373  25.976  23.195  1.00 47.40           C  
ANISOU 2112  CD2 LEU A 274     5610   8232   4167   -201   -108    169       C  
ATOM   2113  N   ASN A 275     -23.767  21.268  25.824  1.00 47.73           N  
ANISOU 2113  N   ASN A 275     5141   8607   4389   -713   -101    551       N  
ATOM   2114  CA  ASN A 275     -24.297  20.633  27.033  1.00 47.76           C  
ANISOU 2114  CA  ASN A 275     4981   8782   4386   -793    -71    662       C  
ATOM   2115  C   ASN A 275     -23.341  19.644  27.737  1.00 52.85           C  
ANISOU 2115  C   ASN A 275     5653   9338   5088   -902    -40    753       C  
ATOM   2116  O   ASN A 275     -23.744  19.073  28.757  1.00 51.44           O  
ANISOU 2116  O   ASN A 275     5345   9299   4901   -976    -14    862       O  
ATOM   2117  CB  ASN A 275     -25.666  19.971  26.763  1.00 48.21           C  
ANISOU 2117  CB  ASN A 275     4886   8964   4468   -886   -125    718       C  
ATOM   2118  CG  ASN A 275     -25.716  18.871  25.754  1.00 62.43           C  
ANISOU 2118  CG  ASN A 275     6735  10611   6375  -1018   -201    735       C  
ATOM   2119  OD1 ASN A 275     -24.726  18.169  25.492  1.00 56.12           O  
ANISOU 2119  OD1 ASN A 275     6059   9615   5648  -1083   -209    745       O  
ATOM   2120  ND2 ASN A 275     -26.908  18.676  25.181  1.00 53.87           N  
ANISOU 2120  ND2 ASN A 275     5548   9620   5299  -1057   -263    731       N  
ATOM   2121  N   ARG A 276     -22.087  19.462  27.257  1.00 51.72           N  
ANISOU 2121  N   ARG A 276     5671   8984   4995   -906    -40    716       N  
ATOM   2122  CA  ARG A 276     -21.133  18.643  28.037  1.00 52.04           C  
ANISOU 2122  CA  ARG A 276     5737   8960   5078   -980     -8    796       C  
ATOM   2123  C   ARG A 276     -20.339  19.569  28.948  1.00 55.45           C  
ANISOU 2123  C   ARG A 276     6194   9445   5431   -874     62    761       C  
ATOM   2124  O   ARG A 276     -19.791  19.130  29.972  1.00 56.52           O  
ANISOU 2124  O   ARG A 276     6299   9615   5561   -908    100    836       O  
ATOM   2125  CB  ARG A 276     -20.209  17.790  27.164  1.00 51.65           C  
ANISOU 2125  CB  ARG A 276     5825   8676   5125  -1046    -47    784       C  
ATOM   2126  CG  ARG A 276     -20.815  16.435  26.769  1.00 58.09           C  
ANISOU 2126  CG  ARG A 276     6598   9437   6035  -1194   -114    862       C  
ATOM   2127  CD  ARG A 276     -21.818  16.501  25.620  1.00 56.35           C  
ANISOU 2127  CD  ARG A 276     6361   9218   5831  -1206   -184    804       C  
ATOM   2128  NE  ARG A 276     -21.264  17.129  24.408  1.00 65.15           N  
ANISOU 2128  NE  ARG A 276     7621  10200   6934  -1113   -202    676       N  
ATOM   2129  CZ  ARG A 276     -20.553  16.492  23.481  1.00 73.07           C  
ANISOU 2129  CZ  ARG A 276     8750  11011   8003  -1143   -244    634       C  
ATOM   2130  NH1 ARG A 276     -20.113  17.140  22.414  1.00 55.50           N  
ANISOU 2130  NH1 ARG A 276     6642   8696   5749  -1054   -252    527       N  
ATOM   2131  NH2 ARG A 276     -20.287  15.197  23.608  1.00 65.61           N  
ANISOU 2131  NH2 ARG A 276     7816   9964   7150  -1259   -279    701       N  
ATOM   2132  N   GLY A 277     -20.300  20.848  28.567  1.00 49.99           N  
ANISOU 2132  N   GLY A 277     5560   8756   4678   -745     72    649       N  
ATOM   2133  CA  GLY A 277     -19.681  21.914  29.343  1.00 48.36           C  
ANISOU 2133  CA  GLY A 277     5380   8599   4394   -635    126    592       C  
ATOM   2134  C   GLY A 277     -20.670  22.528  30.315  1.00 53.54           C  
ANISOU 2134  C   GLY A 277     5893   9493   4957   -564    151    602       C  
ATOM   2135  O   GLY A 277     -21.782  22.020  30.502  1.00 53.84           O  
ANISOU 2135  O   GLY A 277     5795   9673   4990   -616    137    673       O  
ATOM   2136  N   CYS A 278     -20.260  23.623  30.947  1.00 50.70           N  
ANISOU 2136  N   CYS A 278     5561   9182   4520   -446    188    529       N  
ATOM   2137  CA  CYS A 278     -21.056  24.417  31.871  1.00 50.90           C  
ANISOU 2137  CA  CYS A 278     5472   9426   4440   -341    213    505       C  
ATOM   2138  C   CYS A 278     -22.119  25.217  31.071  1.00 51.88           C  
ANISOU 2138  C   CYS A 278     5584   9591   4535   -246    173    429       C  
ATOM   2139  O   CYS A 278     -21.763  25.982  30.177  1.00 49.31           O  
ANISOU 2139  O   CYS A 278     5395   9116   4223   -178    148    336       O  
ATOM   2140  CB  CYS A 278     -20.138  25.339  32.664  1.00 52.11           C  
ANISOU 2140  CB  CYS A 278     5690   9575   4534   -244    251    429       C  
ATOM   2141  SG  CYS A 278     -21.005  26.351  33.877  1.00 58.41           S  
ANISOU 2141  SG  CYS A 278     6361  10641   5192    -91    279    377       S  
ATOM   2142  N   THR A 279     -23.402  25.011  31.354  1.00 49.90           N  
ANISOU 2142  N   THR A 279     5172   9544   4244   -245    166    475       N  
ATOM   2143  CA  THR A 279     -24.458  25.674  30.581  1.00 52.06           C  
ANISOU 2143  CA  THR A 279     5419   9871   4490   -153    122    409       C  
ATOM   2144  C   THR A 279     -25.011  26.928  31.284  1.00 57.91           C  
ANISOU 2144  C   THR A 279     6106  10783   5115     30    140    322       C  
ATOM   2145  O   THR A 279     -26.019  27.491  30.842  1.00 59.30           O  
ANISOU 2145  O   THR A 279     6229  11053   5250    126    105    273       O  
ATOM   2146  CB  THR A 279     -25.579  24.686  30.235  1.00 61.34           C  
ANISOU 2146  CB  THR A 279     6449  11156   5700   -264     89    499       C  
ATOM   2147  OG1 THR A 279     -26.110  24.123  31.432  1.00 63.55           O  
ANISOU 2147  OG1 THR A 279     6548  11663   5934   -318    133    599       O  
ATOM   2148  CG2 THR A 279     -25.121  23.599  29.273  1.00 60.52           C  
ANISOU 2148  CG2 THR A 279     6428  10852   5716   -420     49    550       C  
ATOM   2149  N   ARG A 280     -24.319  27.395  32.323  1.00 53.28           N  
ANISOU 2149  N   ARG A 280     5540  10229   4473     90    186    293       N  
ATOM   2150  CA  ARG A 280     -24.713  28.577  33.086  1.00 53.13           C  
ANISOU 2150  CA  ARG A 280     5483  10362   4342    270    201    198       C  
ATOM   2151  C   ARG A 280     -24.169  29.838  32.440  1.00 56.84           C  
ANISOU 2151  C   ARG A 280     6140  10642   4815    398    169     62       C  
ATOM   2152  O   ARG A 280     -23.142  29.798  31.765  1.00 55.06           O  
ANISOU 2152  O   ARG A 280     6073  10182   4664    335    159     49       O  
ATOM   2153  CB  ARG A 280     -24.230  28.471  34.531  1.00 51.77           C  
ANISOU 2153  CB  ARG A 280     5243  10323   4103    274    260    226       C  
ATOM   2154  CG  ARG A 280     -24.883  27.345  35.318  1.00 53.45           C  
ANISOU 2154  CG  ARG A 280     5258  10761   4290    165    297    370       C  
ATOM   2155  CD  ARG A 280     -24.011  26.913  36.479  1.00 52.63           C  
ANISOU 2155  CD  ARG A 280     5140  10699   4158    113    349    429       C  
ATOM   2156  NE  ARG A 280     -23.940  27.918  37.525  1.00 56.39           N  
ANISOU 2156  NE  ARG A 280     5592  11322   4511    274    377    334       N  
ATOM   2157  CZ  ARG A 280     -23.060  27.899  38.518  1.00 67.03           C  
ANISOU 2157  CZ  ARG A 280     6957  12695   5816    276    413    338       C  
ATOM   2158  NH1 ARG A 280     -23.091  28.835  39.455  1.00 61.45           N  
ANISOU 2158  NH1 ARG A 280     6223  12135   4990    432    430    237       N  
ATOM   2159  NH2 ARG A 280     -22.149  26.940  38.589  1.00 47.34           N  
ANISOU 2159  NH2 ARG A 280     4508  10087   3394    131    427    436       N  
ATOM   2160  N   TYR A 281     -24.888  30.954  32.622  1.00 55.66           N  
ANISOU 2160  N   TYR A 281     5970  10596   4581    579    150    -37       N  
ATOM   2161  CA  TYR A 281     -24.496  32.265  32.094  1.00 54.28           C  
ANISOU 2161  CA  TYR A 281     5974  10248   4402    715    113   -166       C  
ATOM   2162  C   TYR A 281     -23.819  33.085  33.149  1.00 56.59           C  
ANISOU 2162  C   TYR A 281     6316  10549   4636    808    137   -251       C  
ATOM   2163  O   TYR A 281     -24.151  32.947  34.324  1.00 56.37           O  
ANISOU 2163  O   TYR A 281     6149  10741   4528    844    174   -240       O  
ATOM   2164  CB  TYR A 281     -25.722  33.084  31.635  1.00 55.95           C  
ANISOU 2164  CB  TYR A 281     6150  10552   4557    883     63   -237       C  
ATOM   2165  CG  TYR A 281     -26.577  32.482  30.552  1.00 58.91           C  
ANISOU 2165  CG  TYR A 281     6469  10942   4973    826     24   -177       C  
ATOM   2166  CD1 TYR A 281     -26.069  32.274  29.273  1.00 58.47           C  
ANISOU 2166  CD1 TYR A 281     6558  10651   5005    743    -10   -161       C  
ATOM   2167  CD2 TYR A 281     -27.935  32.237  30.765  1.00 61.36           C  
ANISOU 2167  CD2 TYR A 281     6579  11510   5225    871     16   -150       C  
ATOM   2168  CE1 TYR A 281     -26.861  31.747  28.259  1.00 60.13           C  
ANISOU 2168  CE1 TYR A 281     6720  10879   5247    697    -55   -119       C  
ATOM   2169  CE2 TYR A 281     -28.750  31.747  29.742  1.00 62.24           C  
ANISOU 2169  CE2 TYR A 281     6636  11639   5373    822    -31   -108       C  
ATOM   2170  CZ  TYR A 281     -28.207  31.516  28.489  1.00 64.33           C  
ANISOU 2170  CZ  TYR A 281     7055  11661   5726    738    -69    -97       C  
ATOM   2171  OH  TYR A 281     -28.968  30.986  27.492  1.00 58.37           O  
ANISOU 2171  OH  TYR A 281     6247  10925   5005    685   -120    -60       O  
ATOM   2172  N   PHE A 282     -22.993  34.041  32.724  1.00 51.99           N  
ANISOU 2172  N   PHE A 282     5926   9744   4082    864    110   -344       N  
ATOM   2173  CA  PHE A 282     -22.437  35.044  33.613  1.00 51.33           C  
ANISOU 2173  CA  PHE A 282     5910   9649   3946    975    113   -455       C  
ATOM   2174  C   PHE A 282     -23.502  36.127  33.723  1.00 58.64           C  
ANISOU 2174  C   PHE A 282     6815  10679   4788   1189     72   -561       C  
ATOM   2175  O   PHE A 282     -23.894  36.716  32.719  1.00 57.88           O  
ANISOU 2175  O   PHE A 282     6814  10461   4716   1260     21   -598       O  
ATOM   2176  CB  PHE A 282     -21.113  35.603  33.101  1.00 51.15           C  
ANISOU 2176  CB  PHE A 282     6098   9342   3997    927     99   -504       C  
ATOM   2177  CG  PHE A 282     -19.965  34.631  33.126  1.00 51.28           C  
ANISOU 2177  CG  PHE A 282     6131   9270   4084    741    140   -418       C  
ATOM   2178  CD1 PHE A 282     -19.213  34.445  34.287  1.00 53.48           C  
ANISOU 2178  CD1 PHE A 282     6369   9617   4333    707    177   -424       C  
ATOM   2179  CD2 PHE A 282     -19.582  33.952  31.969  1.00 51.86           C  
ANISOU 2179  CD2 PHE A 282     6270   9186   4248    611    137   -342       C  
ATOM   2180  CE1 PHE A 282     -18.150  33.539  34.309  1.00 52.90           C  
ANISOU 2180  CE1 PHE A 282     6311   9466   4324    549    210   -346       C  
ATOM   2181  CE2 PHE A 282     -18.509  33.056  31.988  1.00 52.79           C  
ANISOU 2181  CE2 PHE A 282     6405   9224   4429    455    171   -272       C  
ATOM   2182  CZ  PHE A 282     -17.801  32.855  33.153  1.00 50.89           C  
ANISOU 2182  CZ  PHE A 282     6118   9056   4162    426    207   -272       C  
ATOM   2183  N   ALA A 283     -24.050  36.300  34.923  1.00 58.25           N  
ANISOU 2183  N   ALA A 283     6627  10873   4633   1296     94   -600       N  
ATOM   2184  CA  ALA A 283     -25.096  37.280  35.236  1.00 59.25           C  
ANISOU 2184  CA  ALA A 283     6706  11144   4661   1522     60   -710       C  
ATOM   2185  C   ALA A 283     -25.008  37.684  36.693  1.00 64.86           C  
ANISOU 2185  C   ALA A 283     7344  12036   5264   1629     86   -790       C  
ATOM   2186  O   ALA A 283     -24.337  37.022  37.477  1.00 64.35           O  
ANISOU 2186  O   ALA A 283     7226  12033   5192   1517    137   -734       O  
ATOM   2187  CB  ALA A 283     -26.475  36.690  34.944  1.00 60.72           C  
ANISOU 2187  CB  ALA A 283     6705  11553   4810   1540     61   -639       C  
ATOM   2188  N   ASN A 284     -25.641  38.797  37.031  1.00 64.51           N  
ANISOU 2188  N   ASN A 284     7309  12068   5134   1855     47   -928       N  
ATOM   2189  CA  ASN A 284     -25.823  39.296  38.384  1.00 66.53           C  
ANISOU 2189  CA  ASN A 284     7479  12537   5262   2006     62  -1028       C  
ATOM   2190  C   ASN A 284     -27.339  39.330  38.618  1.00 75.17           C  
ANISOU 2190  C   ASN A 284     8376  13939   6247   2163     65  -1038       C  
ATOM   2191  O   ASN A 284     -28.095  38.929  37.710  1.00 75.52           O  
ANISOU 2191  O   ASN A 284     8365  14000   6330   2129     52   -962       O  
ATOM   2192  CB  ASN A 284     -25.134  40.662  38.599  1.00 66.48           C  
ANISOU 2192  CB  ASN A 284     7676  12330   5254   2145      3  -1206       C  
ATOM   2193  CG  ASN A 284     -25.510  41.765  37.639  1.00 75.35           C  
ANISOU 2193  CG  ASN A 284     8962  13252   6414   2291    -80  -1302       C  
ATOM   2194  OD1 ASN A 284     -26.651  41.904  37.196  1.00 73.49           O  
ANISOU 2194  OD1 ASN A 284     8652  13127   6143   2410   -104  -1303       O  
ATOM   2195  ND2 ASN A 284     -24.558  42.624  37.358  1.00 64.62           N  
ANISOU 2195  ND2 ASN A 284     7828  11600   5124   2294   -129  -1390       N  
ATOM   2196  N   LYS A 285     -27.790  39.797  39.806  1.00 73.97           N  
ANISOU 2196  N   LYS A 285     8114  14038   5953   2337     80  -1134       N  
ATOM   2197  CA  LYS A 285     -29.204  39.880  40.178  1.00 75.56           C  
ANISOU 2197  CA  LYS A 285     8109  14572   6029   2507     90  -1157       C  
ATOM   2198  C   LYS A 285     -29.999  40.669  39.135  1.00 79.82           C  
ANISOU 2198  C   LYS A 285     8722  15013   6594   2662     14  -1230       C  
ATOM   2199  O   LYS A 285     -31.100  40.256  38.762  1.00 81.44           O  
ANISOU 2199  O   LYS A 285     8763  15409   6772   2680     20  -1164       O  
ATOM   2200  CB  LYS A 285     -29.343  40.521  41.572  1.00 79.66           C  
ANISOU 2200  CB  LYS A 285     8558  15317   6392   2703    104  -1292       C  
ATOM   2201  CG  LYS A 285     -30.665  40.228  42.264  1.00 97.82           C  
ANISOU 2201  CG  LYS A 285    10580  18048   8539   2820    153  -1268       C  
ATOM   2202  N   GLU A 286     -29.411  41.767  38.632  1.00 75.64           N  
ANISOU 2202  N   GLU A 286     8440  14176   6123   2759    -62  -1356       N  
ATOM   2203  CA  GLU A 286     -29.999  42.662  37.625  1.00 76.20           C  
ANISOU 2203  CA  GLU A 286     8630  14100   6223   2919   -146  -1434       C  
ATOM   2204  C   GLU A 286     -30.088  42.013  36.234  1.00 79.04           C  
ANISOU 2204  C   GLU A 286     9025  14306   6699   2755   -159  -1298       C  
ATOM   2205  O   GLU A 286     -31.157  42.052  35.619  1.00 80.69           O  
ANISOU 2205  O   GLU A 286     9152  14620   6885   2850   -191  -1288       O  
ATOM   2206  CB  GLU A 286     -29.193  43.982  37.522  1.00 78.06           C  
ANISOU 2206  CB  GLU A 286     9142  14020   6499   3038   -222  -1590       C  
ATOM   2207  CG  GLU A 286     -29.046  44.776  38.821  1.00 94.36           C  
ANISOU 2207  CG  GLU A 286    11205  16193   8454   3219   -231  -1755       C  
ATOM   2208  CD  GLU A 286     -27.835  44.464  39.689  1.00119.25           C  
ANISOU 2208  CD  GLU A 286    14399  19290  11620   3072   -188  -1754       C  
ATOM   2209  OE1 GLU A 286     -28.030  43.896  40.788  1.00123.85           O  
ANISOU 2209  OE1 GLU A 286    14791  20169  12098   3064   -121  -1732       O  
ATOM   2210  OE2 GLU A 286     -26.702  44.834  39.303  1.00104.92           O  
ANISOU 2210  OE2 GLU A 286    12804  17149   9913   2974   -223  -1779       O  
ATOM   2211  N   THR A 287     -28.978  41.442  35.719  1.00 72.94           N  
ANISOU 2211  N   THR A 287     8374  13295   6046   2520   -138  -1203       N  
ATOM   2212  CA  THR A 287     -28.973  40.897  34.349  1.00 71.26           C  
ANISOU 2212  CA  THR A 287     8218  12916   5940   2374   -156  -1091       C  
ATOM   2213  C   THR A 287     -29.741  39.565  34.221  1.00 74.31           C  
ANISOU 2213  C   THR A 287     8371  13543   6322   2234   -107   -944       C  
ATOM   2214  O   THR A 287     -30.306  39.315  33.156  1.00 73.67           O  
ANISOU 2214  O   THR A 287     8282  13427   6285   2205   -141   -890       O  
ATOM   2215  CB  THR A 287     -27.564  40.793  33.805  1.00 76.11           C  
ANISOU 2215  CB  THR A 287     9041  13201   6675   2193   -153  -1052       C  
ATOM   2216  OG1 THR A 287     -26.758  40.074  34.732  1.00 75.63           O  
ANISOU 2216  OG1 THR A 287     8918  13203   6615   2046    -85  -1004       O  
ATOM   2217  CG2 THR A 287     -26.950  42.168  33.546  1.00 72.96           C  
ANISOU 2217  CG2 THR A 287     8893  12523   6304   2317   -220  -1181       C  
ATOM   2218  N   ASP A 288     -29.830  38.766  35.312  1.00 70.79           N  
ANISOU 2218  N   ASP A 288     7734  13348   5816   2156    -33   -882       N  
ATOM   2219  CA  ASP A 288     -30.588  37.509  35.373  1.00 69.41           C  
ANISOU 2219  CA  ASP A 288     7324  13418   5630   2017     15   -738       C  
ATOM   2220  C   ASP A 288     -32.050  37.778  35.017  1.00 74.72           C  
ANISOU 2220  C   ASP A 288     7849  14305   6235   2173    -21   -766       C  
ATOM   2221  O   ASP A 288     -32.651  36.993  34.272  1.00 75.43           O  
ANISOU 2221  O   ASP A 288     7843  14445   6371   2060    -30   -665       O  
ATOM   2222  CB  ASP A 288     -30.459  36.859  36.772  1.00 71.17           C  
ANISOU 2222  CB  ASP A 288     7379  13888   5776   1952     98   -683       C  
ATOM   2223  CG  ASP A 288     -31.559  35.862  37.095  1.00 81.95           C  
ANISOU 2223  CG  ASP A 288     8466  15584   7087   1877    145   -559       C  
ATOM   2224  OD1 ASP A 288     -31.501  34.727  36.568  1.00 82.72           O  
ANISOU 2224  OD1 ASP A 288     8517  15637   7274   1656    161   -413       O  
ATOM   2225  OD2 ASP A 288     -32.527  36.245  37.817  1.00 82.17           O  
ANISOU 2225  OD2 ASP A 288     8320  15915   6984   2046    159   -611       O  
ATOM   2226  N   LYS A 289     -32.608  38.912  35.529  1.00 71.45           N  
ANISOU 2226  N   LYS A 289     7426  14011   5713   2441    -51   -913       N  
ATOM   2227  CA  LYS A 289     -33.974  39.379  35.265  1.00 72.07           C  
ANISOU 2227  CA  LYS A 289     7373  14299   5711   2641    -94   -969       C  
ATOM   2228  C   LYS A 289     -34.191  39.653  33.758  1.00 76.00           C  
ANISOU 2228  C   LYS A 289     8006  14574   6296   2653   -175   -967       C  
ATOM   2229  O   LYS A 289     -35.292  39.433  33.255  1.00 76.96           O  
ANISOU 2229  O   LYS A 289     7979  14870   6391   2696   -201   -938       O  
ATOM   2230  CB  LYS A 289     -34.274  40.646  36.077  1.00 75.79           C  
ANISOU 2230  CB  LYS A 289     7867  14870   6061   2941   -120  -1149       C  
ATOM   2231  CG  LYS A 289     -34.216  40.453  37.595  1.00 80.55           C  
ANISOU 2231  CG  LYS A 289     8319  15740   6547   2969    -44  -1169       C  
ATOM   2232  N   GLN A 290     -33.138  40.109  33.044  1.00 70.79           N  
ANISOU 2232  N   GLN A 290     7619  13543   5735   2607   -214   -993       N  
ATOM   2233  CA  GLN A 290     -33.194  40.431  31.612  1.00 70.12           C  
ANISOU 2233  CA  GLN A 290     7691  13225   5726   2619   -290   -988       C  
ATOM   2234  C   GLN A 290     -33.194  39.173  30.714  1.00 72.22           C  
ANISOU 2234  C   GLN A 290     7897  13461   6081   2370   -275   -837       C  
ATOM   2235  O   GLN A 290     -33.581  39.267  29.550  1.00 72.01           O  
ANISOU 2235  O   GLN A 290     7926  13344   6091   2389   -336   -823       O  
ATOM   2236  CB  GLN A 290     -32.025  41.355  31.220  1.00 70.59           C  
ANISOU 2236  CB  GLN A 290     8059  12910   5854   2646   -329  -1059       C  
ATOM   2237  CG  GLN A 290     -32.106  42.758  31.831  1.00 83.94           C  
ANISOU 2237  CG  GLN A 290     9851  14573   7471   2916   -375  -1226       C  
ATOM   2238  CD  GLN A 290     -33.233  43.586  31.236  1.00 93.73           C  
ANISOU 2238  CD  GLN A 290    11088  15872   8655   3164   -459  -1301       C  
ATOM   2239  OE1 GLN A 290     -33.250  43.880  30.041  1.00 86.70           O  
ANISOU 2239  OE1 GLN A 290    10340  14780   7822   3174   -521  -1278       O  
ATOM   2240  NE2 GLN A 290     -34.194  43.994  32.058  1.00 83.07           N  
ANISOU 2240  NE2 GLN A 290     9574  14805   7184   3381   -463  -1393       N  
ATOM   2241  N   ILE A 291     -32.768  38.008  31.245  1.00 67.76           N  
ANISOU 2241  N   ILE A 291     7225  12971   5551   2146   -200   -727       N  
ATOM   2242  CA  ILE A 291     -32.724  36.752  30.491  1.00 66.49           C  
ANISOU 2242  CA  ILE A 291     7010  12776   5479   1906   -189   -589       C  
ATOM   2243  C   ILE A 291     -34.078  35.987  30.610  1.00 72.31           C  
ANISOU 2243  C   ILE A 291     7461  13848   6165   1883   -182   -523       C  
ATOM   2244  O   ILE A 291     -34.494  35.615  31.696  1.00 73.20           O  
ANISOU 2244  O   ILE A 291     7378  14231   6206   1880   -124   -495       O  
ATOM   2245  CB  ILE A 291     -31.506  35.870  30.918  1.00 67.96           C  
ANISOU 2245  CB  ILE A 291     7244  12839   5738   1674   -122   -501       C  
ATOM   2246  CG1 ILE A 291     -30.176  36.644  30.826  1.00 66.12           C  
ANISOU 2246  CG1 ILE A 291     7274  12295   5554   1689   -129   -568       C  
ATOM   2247  CG2 ILE A 291     -31.435  34.592  30.077  1.00 68.79           C  
ANISOU 2247  CG2 ILE A 291     7308  12887   5940   1437   -121   -370       C  
ATOM   2248  CD1 ILE A 291     -29.069  36.076  31.649  1.00 70.43           C  
ANISOU 2248  CD1 ILE A 291     7838  12792   6129   1539    -62   -522       C  
ATOM   2249  N   LEU A 292     -34.741  35.744  29.476  1.00 70.93           N  
ANISOU 2249  N   LEU A 292     7263  13660   6026   1860   -242   -494       N  
ATOM   2250  CA  LEU A 292     -36.005  35.001  29.406  1.00 72.00           C  
ANISOU 2250  CA  LEU A 292     7136  14090   6132   1814   -248   -428       C  
ATOM   2251  C   LEU A 292     -35.855  33.544  29.871  1.00 76.78           C  
ANISOU 2251  C   LEU A 292     7592  14793   6789   1542   -184   -283       C  
ATOM   2252  O   LEU A 292     -34.840  32.903  29.582  1.00 75.40           O  
ANISOU 2252  O   LEU A 292     7547  14387   6713   1355   -167   -218       O  
ATOM   2253  CB  LEU A 292     -36.549  35.022  27.985  1.00 71.83           C  
ANISOU 2253  CB  LEU A 292     7158  13983   6153   1826   -336   -432       C  
ATOM   2254  CG  LEU A 292     -36.920  36.400  27.431  1.00 77.03           C  
ANISOU 2254  CG  LEU A 292     7934  14580   6753   2101   -412   -557       C  
ATOM   2255  CD1 LEU A 292     -37.240  36.323  25.945  1.00 76.25           C  
ANISOU 2255  CD1 LEU A 292     7910  14356   6705   2081   -498   -543       C  
ATOM   2256  CD2 LEU A 292     -38.070  37.030  28.224  1.00 79.88           C  
ANISOU 2256  CD2 LEU A 292     8091  15274   6985   2328   -414   -631       C  
ATOM   2257  N   GLN A 293     -36.892  33.025  30.562  1.00 74.19           N  
ANISOU 2257  N   GLN A 293     6986  14810   6394   1523   -151   -228       N  
ATOM   2258  CA  GLN A 293     -36.977  31.661  31.101  1.00 73.13           C  
ANISOU 2258  CA  GLN A 293     6673  14817   6294   1275    -92    -78       C  
ATOM   2259  C   GLN A 293     -36.642  30.569  30.039  1.00 71.59           C  
ANISOU 2259  C   GLN A 293     6546  14413   6240   1028   -130     18       C  
ATOM   2260  O   GLN A 293     -36.002  29.553  30.372  1.00 69.01           O  
ANISOU 2260  O   GLN A 293     6223  14012   5983    813    -85    127       O  
ATOM   2261  CB  GLN A 293     -38.393  31.443  31.666  1.00 77.07           C  
ANISOU 2261  CB  GLN A 293     6860  15727   6697   1318    -74    -45       C  
ATOM   2262  CG  GLN A 293     -38.642  30.103  32.378  1.00 96.94           C  
ANISOU 2262  CG  GLN A 293     9161  18442   9230   1073     -8    121       C  
ATOM   2263  CD  GLN A 293     -37.875  29.888  33.668  1.00106.53           C  
ANISOU 2263  CD  GLN A 293    10381  19689  10407   1023     85    173       C  
ATOM   2264  OE1 GLN A 293     -37.432  30.829  34.345  1.00 99.94           O  
ANISOU 2264  OE1 GLN A 293     9631  18851   9489   1210    113     71       O  
ATOM   2265  NE2 GLN A 293     -37.748  28.625  34.055  1.00 95.13           N  
ANISOU 2265  NE2 GLN A 293     8838  18287   9020    770    130    334       N  
ATOM   2266  N   ASN A 294     -37.040  30.803  28.769  1.00 65.57           N  
ANISOU 2266  N   ASN A 294     5851  13550   5515   1073   -216    -30       N  
ATOM   2267  CA  ASN A 294     -36.796  29.861  27.685  1.00 64.53           C  
ANISOU 2267  CA  ASN A 294     5785  13230   5502    869   -264     36       C  
ATOM   2268  C   ASN A 294     -35.304  29.818  27.278  1.00 65.46           C  
ANISOU 2268  C   ASN A 294     6179  12986   5708    793   -256     32       C  
ATOM   2269  O   ASN A 294     -34.937  28.969  26.463  1.00 63.79           O  
ANISOU 2269  O   ASN A 294     6035  12607   5595    620   -287     85       O  
ATOM   2270  CB  ASN A 294     -37.701  30.152  26.476  1.00 66.72           C  
ANISOU 2270  CB  ASN A 294     6039  13536   5775    954   -361    -18       C  
ATOM   2271  CG  ASN A 294     -37.485  31.447  25.715  1.00 79.96           C  
ANISOU 2271  CG  ASN A 294     7924  15039   7419   1181   -418   -142       C  
ATOM   2272  OD1 ASN A 294     -36.614  32.266  26.010  1.00 74.10           O  
ANISOU 2272  OD1 ASN A 294     7366  14129   6659   1292   -391   -202       O  
ATOM   2273  ND2 ASN A 294     -38.316  31.665  24.717  1.00 67.12           N  
ANISOU 2273  ND2 ASN A 294     6266  13455   5779   1256   -504   -180       N  
ATOM   2274  N   ARG A 295     -34.449  30.708  27.866  1.00 61.59           N  
ANISOU 2274  N   ARG A 295     5837  12384   5180    918   -215    -35       N  
ATOM   2275  CA  ARG A 295     -33.000  30.749  27.590  1.00 59.91           C  
ANISOU 2275  CA  ARG A 295     5869  11854   5041    850   -200    -41       C  
ATOM   2276  C   ARG A 295     -32.200  30.053  28.670  1.00 63.50           C  
ANISOU 2276  C   ARG A 295     6295  12315   5518    710   -119     37       C  
ATOM   2277  O   ARG A 295     -31.036  29.695  28.441  1.00 61.97           O  
ANISOU 2277  O   ARG A 295     6258  11885   5401    596   -104     63       O  
ATOM   2278  CB  ARG A 295     -32.474  32.191  27.451  1.00 58.00           C  
ANISOU 2278  CB  ARG A 295     5827  11454   4756   1060   -215   -164       C  
ATOM   2279  CG  ARG A 295     -33.283  33.093  26.523  1.00 63.91           C  
ANISOU 2279  CG  ARG A 295     6616  12206   5462   1247   -296   -249       C  
ATOM   2280  CD  ARG A 295     -33.384  32.608  25.086  1.00 58.33           C  
ANISOU 2280  CD  ARG A 295     5975  11364   4823   1157   -362   -220       C  
ATOM   2281  NE  ARG A 295     -34.227  33.525  24.324  1.00 62.89           N  
ANISOU 2281  NE  ARG A 295     6574  11978   5342   1357   -440   -297       N  
ATOM   2282  CZ  ARG A 295     -33.786  34.627  23.727  1.00 75.35           C  
ANISOU 2282  CZ  ARG A 295     8369  13355   6907   1506   -478   -372       C  
ATOM   2283  NH1 ARG A 295     -32.491  34.927  23.739  1.00 60.69           N  
ANISOU 2283  NH1 ARG A 295     6722  11243   5096   1463   -444   -379       N  
ATOM   2284  NH2 ARG A 295     -34.633  35.443  23.121  1.00 60.49           N  
ANISOU 2284  NH2 ARG A 295     6492  11526   4964   1700   -551   -435       N  
ATOM   2285  N   LYS A 296     -32.801  29.875  29.846  1.00 60.46           N  
ANISOU 2285  N   LYS A 296     5708  12206   5058    725    -68     75       N  
ATOM   2286  CA  LYS A 296     -32.101  29.325  31.008  1.00 60.58           C  
ANISOU 2286  CA  LYS A 296     5688  12261   5069    622     10    149       C  
ATOM   2287  C   LYS A 296     -32.139  27.798  31.056  1.00 66.50           C  
ANISOU 2287  C   LYS A 296     6333  13035   5900    367     27    302       C  
ATOM   2288  O   LYS A 296     -33.217  27.197  30.989  1.00 69.63           O  
ANISOU 2288  O   LYS A 296     6538  13626   6293    294     12    369       O  
ATOM   2289  CB  LYS A 296     -32.673  29.907  32.301  1.00 62.86           C  
ANISOU 2289  CB  LYS A 296     5818  12843   5223    770     61    117       C  
ATOM   2290  CG  LYS A 296     -32.650  31.432  32.329  1.00 72.41           C  
ANISOU 2290  CG  LYS A 296     7138  14022   6354   1035     36    -45       C  
ATOM   2291  CD  LYS A 296     -33.539  31.954  33.416  1.00 76.98           C  
ANISOU 2291  CD  LYS A 296     7528  14930   6791   1200     71    -88       C  
ATOM   2292  CE  LYS A 296     -33.102  33.298  33.926  1.00 90.96           C  
ANISOU 2292  CE  LYS A 296     9433  16640   8487   1428     68   -239       C  
ATOM   2293  NZ  LYS A 296     -33.698  33.557  35.266  1.00107.87           N  
ANISOU 2293  NZ  LYS A 296    11389  19110  10487   1554    122   -265       N  
ATOM   2294  N   SER A 297     -30.953  27.181  31.174  1.00 59.37           N  
ANISOU 2294  N   SER A 297     5556  11928   5073    233     54    356       N  
ATOM   2295  CA  SER A 297     -30.788  25.731  31.280  1.00 58.61           C  
ANISOU 2295  CA  SER A 297     5398  11808   5064     -4     66    501       C  
ATOM   2296  C   SER A 297     -31.246  25.229  32.660  1.00 62.13           C  
ANISOU 2296  C   SER A 297     5636  12530   5439    -59    135    608       C  
ATOM   2297  O   SER A 297     -31.197  26.019  33.597  1.00 62.27           O  
ANISOU 2297  O   SER A 297     5622  12688   5350     87    184    556       O  
ATOM   2298  CB  SER A 297     -29.315  25.376  31.081  1.00 60.25           C  
ANISOU 2298  CB  SER A 297     5810  11726   5358    -92     76    511       C  
ATOM   2299  OG  SER A 297     -28.524  25.843  32.162  1.00 63.46           O  
ANISOU 2299  OG  SER A 297     6254  12154   5705    -25    139    494       O  
ATOM   2300  N   PRO A 298     -31.589  23.929  32.849  1.00 59.24           N  
ANISOU 2300  N   PRO A 298     5142  12234   5131   -268    142    759       N  
ATOM   2301  CA  PRO A 298     -31.925  23.441  34.206  1.00 60.54           C  
ANISOU 2301  CA  PRO A 298     5121  12658   5224   -328    216    881       C  
ATOM   2302  C   PRO A 298     -30.764  23.655  35.198  1.00 64.81           C  
ANISOU 2302  C   PRO A 298     5761  13142   5722   -284    279    880       C  
ATOM   2303  O   PRO A 298     -31.017  24.046  36.329  1.00 64.73           O  
ANISOU 2303  O   PRO A 298     5634  13371   5590   -192    339    887       O  
ATOM   2304  CB  PRO A 298     -32.226  21.953  33.982  1.00 62.02           C  
ANISOU 2304  CB  PRO A 298     5225  12821   5520   -587    196   1044       C  
ATOM   2305  CG  PRO A 298     -32.647  21.877  32.555  1.00 65.90           C  
ANISOU 2305  CG  PRO A 298     5770  13172   6099   -616    106    982       C  
ATOM   2306  CD  PRO A 298     -31.711  22.839  31.864  1.00 60.44           C  
ANISOU 2306  CD  PRO A 298     5314  12236   5414   -460     81    829       C  
ATOM   2307  N   GLU A 299     -29.493  23.485  34.755  1.00 62.08           N  
ANISOU 2307  N   GLU A 299     5629  12492   5468   -330    261    857       N  
ATOM   2308  CA  GLU A 299     -28.278  23.747  35.567  1.00 61.92           C  
ANISOU 2308  CA  GLU A 299     5721  12389   5416   -284    309    838       C  
ATOM   2309  C   GLU A 299     -28.284  25.215  36.078  1.00 65.91           C  
ANISOU 2309  C   GLU A 299     6246  13002   5797    -47    330    687       C  
ATOM   2310  O   GLU A 299     -27.957  25.452  37.224  1.00 65.46           O  
ANISOU 2310  O   GLU A 299     6148  13076   5649     12    384    692       O  
ATOM   2311  CB  GLU A 299     -27.000  23.460  34.735  1.00 62.10           C  
ANISOU 2311  CB  GLU A 299     5969  12064   5561   -353    274    809       C  
ATOM   2312  CG  GLU A 299     -25.643  23.609  35.441  1.00 73.60           C  
ANISOU 2312  CG  GLU A 299     7547  13411   7007   -330    313    794       C  
ATOM   2313  CD  GLU A 299     -24.376  23.587  34.578  1.00 94.20           C  
ANISOU 2313  CD  GLU A 299    10373  15700   9718   -363    282    739       C  
ATOM   2314  OE1 GLU A 299     -24.453  23.198  33.388  1.00 77.14           O  
ANISOU 2314  OE1 GLU A 299     8279  13378   7654   -437    230    738       O  
ATOM   2315  OE2 GLU A 299     -23.290  23.929  35.106  1.00 85.50           O  
ANISOU 2315  OE2 GLU A 299     9367  14520   8597   -317    309    698       O  
ATOM   2316  N   TYR A 300     -28.659  26.188  35.217  1.00 63.65           N  
ANISOU 2316  N   TYR A 300     6027  12655   5504     91    281    553       N  
ATOM   2317  CA  TYR A 300     -28.721  27.611  35.580  1.00 61.95           C  
ANISOU 2317  CA  TYR A 300     5847  12509   5181    323    285    402       C  
ATOM   2318  C   TYR A 300     -29.805  27.862  36.632  1.00 63.46           C  
ANISOU 2318  C   TYR A 300     5813  13066   5232    423    328    414       C  
ATOM   2319  O   TYR A 300     -29.600  28.668  37.528  1.00 62.36           O  
ANISOU 2319  O   TYR A 300     5673  13032   4987    573    360    333       O  
ATOM   2320  CB  TYR A 300     -28.979  28.483  34.329  1.00 61.67           C  
ANISOU 2320  CB  TYR A 300     5932  12322   5178    438    216    278       C  
ATOM   2321  CG  TYR A 300     -28.922  29.968  34.622  1.00 62.19           C  
ANISOU 2321  CG  TYR A 300     6075  12402   5153    674    208    118       C  
ATOM   2322  CD1 TYR A 300     -27.719  30.657  34.576  1.00 62.00           C  
ANISOU 2322  CD1 TYR A 300     6258  12144   5154    724    203     30       C  
ATOM   2323  CD2 TYR A 300     -30.072  30.681  34.967  1.00 64.66           C  
ANISOU 2323  CD2 TYR A 300     6250  12964   5354    849    203     52       C  
ATOM   2324  CE1 TYR A 300     -27.659  32.022  34.842  1.00 62.64           C  
ANISOU 2324  CE1 TYR A 300     6423  12215   5163    932    186   -119       C  
ATOM   2325  CE2 TYR A 300     -30.013  32.039  35.283  1.00 65.35           C  
ANISOU 2325  CE2 TYR A 300     6419  13052   5360   1076    188   -102       C  
ATOM   2326  CZ  TYR A 300     -28.803  32.707  35.207  1.00 65.35           C  
ANISOU 2326  CZ  TYR A 300     6640  12793   5397   1112    176   -187       C  
ATOM   2327  OH  TYR A 300     -28.703  34.044  35.482  1.00 63.27           O  
ANISOU 2327  OH  TYR A 300     6474  12501   5067   1324    152   -341       O  
ATOM   2328  N   LEU A 301     -30.965  27.209  36.489  1.00 61.60           N  
ANISOU 2328  N   LEU A 301     5386  13027   4992    345    326    506       N  
ATOM   2329  CA  LEU A 301     -32.099  27.328  37.409  1.00 63.27           C  
ANISOU 2329  CA  LEU A 301     5355  13617   5070    423    370    534       C  
ATOM   2330  C   LEU A 301     -31.759  26.723  38.764  1.00 67.47           C  
ANISOU 2330  C   LEU A 301     5786  14315   5533    346    450    649       C  
ATOM   2331  O   LEU A 301     -32.046  27.324  39.804  1.00 68.09           O  
ANISOU 2331  O   LEU A 301     5763  14641   5468    494    498    603       O  
ATOM   2332  CB  LEU A 301     -33.348  26.646  36.801  1.00 64.57           C  
ANISOU 2332  CB  LEU A 301     5339  13928   5268    318    342    619       C  
ATOM   2333  CG  LEU A 301     -33.914  27.266  35.521  1.00 68.35           C  
ANISOU 2333  CG  LEU A 301     5877  14307   5787    415    260    507       C  
ATOM   2334  CD1 LEU A 301     -35.011  26.393  34.936  1.00 69.65           C  
ANISOU 2334  CD1 LEU A 301     5866  14596   6002    269    227    606       C  
ATOM   2335  CD2 LEU A 301     -34.443  28.669  35.757  1.00 70.02           C  
ANISOU 2335  CD2 LEU A 301     6070  14664   5871    699    252    346       C  
ATOM   2336  N   LYS A 302     -31.076  25.572  38.753  1.00 64.08           N  
ANISOU 2336  N   LYS A 302     5403  13738   5205    130    461    789       N  
ATOM   2337  CA  LYS A 302     -30.643  24.885  39.966  1.00 64.68           C  
ANISOU 2337  CA  LYS A 302     5408  13939   5230     39    530    919       C  
ATOM   2338  C   LYS A 302     -29.470  25.624  40.693  1.00 68.17           C  
ANISOU 2338  C   LYS A 302     5995  14295   5610    168    555    818       C  
ATOM   2339  O   LYS A 302     -29.577  25.903  41.890  1.00 66.97           O  
ANISOU 2339  O   LYS A 302     5739  14387   5319    258    612    821       O  
ATOM   2340  CB  LYS A 302     -30.241  23.426  39.627  1.00 66.35           C  
ANISOU 2340  CB  LYS A 302     5645  13982   5581   -225    520   1096       C  
ATOM   2341  CG  LYS A 302     -30.179  22.518  40.858  1.00 86.42           C  
ANISOU 2341  CG  LYS A 302     8060  16709   8068   -346    589   1277       C  
ATOM   2342  CD  LYS A 302     -29.521  21.164  40.561  1.00 92.71           C  
ANISOU 2342  CD  LYS A 302     8937  17278   9010   -582    570   1435       C  
ATOM   2343  CE  LYS A 302     -29.123  20.409  41.820  1.00 94.36           C  
ANISOU 2343  CE  LYS A 302     9080  17611   9160   -669    634   1599       C  
ATOM   2344  NZ  LYS A 302     -30.289  19.914  42.606  1.00 89.96           N  
ANISOU 2344  NZ  LYS A 302     8269  17403   8509   -743    690   1753       N  
ATOM   2345  N   ALA A 303     -28.362  25.926  39.972  1.00 65.04           N  
ANISOU 2345  N   ALA A 303     5831  13567   5314    174    510    729       N  
ATOM   2346  CA  ALA A 303     -27.131  26.496  40.563  1.00 63.60           C  
ANISOU 2346  CA  ALA A 303     5793  13275   5099    257    526    644       C  
ATOM   2347  C   ALA A 303     -27.012  28.041  40.512  1.00 65.94           C  
ANISOU 2347  C   ALA A 303     6188  13540   5326    490    500    432       C  
ATOM   2348  O   ALA A 303     -26.170  28.617  41.214  1.00 63.60           O  
ANISOU 2348  O   ALA A 303     5973  13218   4974    577    514    351       O  
ATOM   2349  CB  ALA A 303     -25.909  25.876  39.886  1.00 62.59           C  
ANISOU 2349  CB  ALA A 303     5849  12816   5117    115    498    680       C  
ATOM   2350  N   GLY A 304     -27.820  28.678  39.673  1.00 64.62           N  
ANISOU 2350  N   GLY A 304     6022  13362   5168    586    455    344       N  
ATOM   2351  CA  GLY A 304     -27.802  30.124  39.502  1.00 64.64           C  
ANISOU 2351  CA  GLY A 304     6132  13310   5120    806    419    149       C  
ATOM   2352  C   GLY A 304     -26.747  30.551  38.509  1.00 67.58           C  
ANISOU 2352  C   GLY A 304     6751  13315   5609    789    367     69       C  
ATOM   2353  O   GLY A 304     -26.171  29.721  37.791  1.00 64.87           O  
ANISOU 2353  O   GLY A 304     6486  12772   5387    616    357    156       O  
ATOM   2354  N   SER A 305     -26.449  31.849  38.503  1.00 64.85           N  
ANISOU 2354  N   SER A 305     6534  12881   5227    968    335    -99       N  
ATOM   2355  CA  SER A 305     -25.474  32.374  37.562  1.00 62.81           C  
ANISOU 2355  CA  SER A 305     6509  12284   5071    956    288   -175       C  
ATOM   2356  C   SER A 305     -24.048  32.126  37.991  1.00 63.39           C  
ANISOU 2356  C   SER A 305     6693  12205   5187    861    311   -162       C  
ATOM   2357  O   SER A 305     -23.764  31.786  39.139  1.00 62.52           O  
ANISOU 2357  O   SER A 305     6498  12248   5007    847    356   -128       O  
ATOM   2358  CB  SER A 305     -25.682  33.870  37.348  1.00 66.02           C  
ANISOU 2358  CB  SER A 305     7023  12628   5432   1173    238   -351       C  
ATOM   2359  OG  SER A 305     -25.174  34.606  38.444  1.00 71.59           O  
ANISOU 2359  OG  SER A 305     7753  13397   6051   1289    253   -453       O  
ATOM   2360  N   LEU A 306     -23.151  32.299  37.011  1.00 56.96           N  
ANISOU 2360  N   LEU A 306     6067  11092   4484    797    278   -190       N  
ATOM   2361  CA  LEU A 306     -21.713  32.302  37.168  1.00 53.23           C  
ANISOU 2361  CA  LEU A 306     5728  10434   4063    723    287   -207       C  
ATOM   2362  C   LEU A 306     -21.341  33.736  37.518  1.00 58.08           C  
ANISOU 2362  C   LEU A 306     6458  10985   4627    886    258   -376       C  
ATOM   2363  O   LEU A 306     -21.968  34.679  37.014  1.00 59.56           O  
ANISOU 2363  O   LEU A 306     6698  11135   4796   1020    215   -471       O  
ATOM   2364  CB  LEU A 306     -21.054  31.857  35.861  1.00 50.44           C  
ANISOU 2364  CB  LEU A 306     5510   9812   3844    588    265   -161       C  
ATOM   2365  CG  LEU A 306     -21.147  30.400  35.476  1.00 51.90           C  
ANISOU 2365  CG  LEU A 306     5619  10001   4099    413    283     -6       C  
ATOM   2366  CD1 LEU A 306     -20.603  30.189  34.024  1.00 48.65           C  
ANISOU 2366  CD1 LEU A 306     5356   9322   3806    324    250      2       C  
ATOM   2367  CD2 LEU A 306     -20.380  29.528  36.481  1.00 52.28           C  
ANISOU 2367  CD2 LEU A 306     5609  10115   4140    313    329     81       C  
ATOM   2368  N   LYS A 307     -20.352  33.916  38.365  1.00 53.57           N  
ANISOU 2368  N   LYS A 307     5927  10396   4032    878    275   -417       N  
ATOM   2369  CA  LYS A 307     -19.968  35.252  38.777  1.00 53.75           C  
ANISOU 2369  CA  LYS A 307     6058  10356   4009   1023    240   -585       C  
ATOM   2370  C   LYS A 307     -18.623  35.632  38.217  1.00 58.02           C  
ANISOU 2370  C   LYS A 307     6788  10609   4648    943    217   -630       C  
ATOM   2371  O   LYS A 307     -17.667  34.841  38.255  1.00 57.03           O  
ANISOU 2371  O   LYS A 307     6673  10417   4579    796    245   -551       O  
ATOM   2372  CB  LYS A 307     -19.955  35.403  40.333  1.00 55.65           C  
ANISOU 2372  CB  LYS A 307     6189  10836   4119   1113    267   -634       C  
ATOM   2373  CG  LYS A 307     -21.296  35.126  41.050  1.00 64.29           C  
ANISOU 2373  CG  LYS A 307     7077  12261   5090   1209    298   -596       C  
ATOM   2374  CD  LYS A 307     -22.482  35.995  40.581  1.00 74.89           C  
ANISOU 2374  CD  LYS A 307     8411  13652   6391   1384    258   -689       C  
ATOM   2375  CE  LYS A 307     -23.784  35.755  41.343  1.00 79.41           C  
ANISOU 2375  CE  LYS A 307     8761  14580   6829   1486    293   -659       C  
ATOM   2376  NZ  LYS A 307     -24.315  34.356  41.237  1.00 71.63           N  
ANISOU 2376  NZ  LYS A 307     7610  13742   5865   1323    345   -463       N  
ATOM   2377  N   ASP A 308     -18.545  36.881  37.743  1.00 54.49           N  
ANISOU 2377  N   ASP A 308     6490   9996   4217   1047    164   -759       N  
ATOM   2378  CA  ASP A 308     -17.327  37.512  37.267  1.00 53.05           C  
ANISOU 2378  CA  ASP A 308     6494   9545   4117    989    137   -822       C  
ATOM   2379  C   ASP A 308     -17.436  39.038  37.408  1.00 58.18           C  
ANISOU 2379  C   ASP A 308     7267  10103   4735   1154     75   -991       C  
ATOM   2380  O   ASP A 308     -18.540  39.574  37.247  1.00 56.26           O  
ANISOU 2380  O   ASP A 308     7006   9928   4443   1302     46  -1038       O  
ATOM   2381  CB  ASP A 308     -17.052  37.129  35.794  1.00 53.93           C  
ANISOU 2381  CB  ASP A 308     6703   9445   4344    868    133   -738       C  
ATOM   2382  CG  ASP A 308     -15.659  37.507  35.325  1.00 59.06           C  
ANISOU 2382  CG  ASP A 308     7516   9846   5079    768    123   -768       C  
ATOM   2383  OD1 ASP A 308     -14.691  36.826  35.734  1.00 56.95           O  
ANISOU 2383  OD1 ASP A 308     7220   9581   4836    650    157   -723       O  
ATOM   2384  OD2 ASP A 308     -15.522  38.564  34.669  1.00 66.39           O  
ANISOU 2384  OD2 ASP A 308     8597  10587   6041    818     78   -843       O  
ATOM   2385  N   PRO A 309     -16.319  39.766  37.693  1.00 58.18           N  
ANISOU 2385  N   PRO A 309     7394   9944   4765   1132     49  -1085       N  
ATOM   2386  CA  PRO A 309     -16.400  41.243  37.740  1.00 61.08           C  
ANISOU 2386  CA  PRO A 309     7904  10186   5120   1278    -21  -1246       C  
ATOM   2387  C   PRO A 309     -16.811  41.909  36.398  1.00 69.87           C  
ANISOU 2387  C   PRO A 309     9162  11085   6300   1315    -65  -1246       C  
ATOM   2388  O   PRO A 309     -17.516  42.919  36.428  1.00 71.50           O  
ANISOU 2388  O   PRO A 309     9427  11273   6465   1490   -121  -1352       O  
ATOM   2389  CB  PRO A 309     -14.970  41.655  38.118  1.00 62.20           C  
ANISOU 2389  CB  PRO A 309     8149  10175   5308   1186    -35  -1313       C  
ATOM   2390  CG  PRO A 309     -14.365  40.435  38.750  1.00 63.97           C  
ANISOU 2390  CG  PRO A 309     8236  10551   5518   1055     29  -1216       C  
ATOM   2391  CD  PRO A 309     -14.941  39.307  37.973  1.00 57.91           C  
ANISOU 2391  CD  PRO A 309     7384   9837   4783    975     76  -1055       C  
ATOM   2392  N   LEU A 310     -16.396  41.358  35.233  1.00 67.33           N  
ANISOU 2392  N   LEU A 310     8898  10611   6073   1164    -44  -1131       N  
ATOM   2393  CA  LEU A 310     -16.695  41.958  33.907  1.00 68.14           C  
ANISOU 2393  CA  LEU A 310     9146  10511   6235   1187    -84  -1118       C  
ATOM   2394  C   LEU A 310     -17.672  41.154  33.027  1.00 70.21           C  
ANISOU 2394  C   LEU A 310     9323  10856   6497   1179    -66  -1005       C  
ATOM   2395  O   LEU A 310     -18.647  41.738  32.541  1.00 70.56           O  
ANISOU 2395  O   LEU A 310     9403  10891   6517   1316   -111  -1036       O  
ATOM   2396  CB  LEU A 310     -15.427  42.258  33.066  1.00 67.58           C  
ANISOU 2396  CB  LEU A 310     9246  10165   6268   1037    -87  -1094       C  
ATOM   2397  CG  LEU A 310     -14.308  41.207  33.023  1.00 71.30           C  
ANISOU 2397  CG  LEU A 310     9667  10631   6794    834    -25   -997       C  
ATOM   2398  CD1 LEU A 310     -13.634  41.129  31.609  1.00 69.60           C  
ANISOU 2398  CD1 LEU A 310     9581  10194   6670    703    -16   -918       C  
ATOM   2399  CD2 LEU A 310     -13.300  41.474  34.113  1.00 74.83           C  
ANISOU 2399  CD2 LEU A 310    10107  11093   7233    793    -21  -1073       C  
ATOM   2400  N   LEU A 311     -17.404  39.854  32.787  1.00 63.55           N  
ANISOU 2400  N   LEU A 311     8380  10081   5686   1025     -9   -879       N  
ATOM   2401  CA  LEU A 311     -18.277  39.054  31.921  1.00 62.48           C  
ANISOU 2401  CA  LEU A 311     8170  10010   5560   1002     -1   -778       C  
ATOM   2402  C   LEU A 311     -19.712  39.021  32.399  1.00 65.35           C  
ANISOU 2402  C   LEU A 311     8384  10611   5834   1150    -13   -796       C  
ATOM   2403  O   LEU A 311     -19.986  38.788  33.577  1.00 65.56           O  
ANISOU 2403  O   LEU A 311     8275  10846   5789   1195     12   -817       O  
ATOM   2404  CB  LEU A 311     -17.786  37.607  31.779  1.00 61.55           C  
ANISOU 2404  CB  LEU A 311     7961   9937   5488    819     56   -651       C  
ATOM   2405  CG  LEU A 311     -16.482  37.343  31.050  1.00 64.80           C  
ANISOU 2405  CG  LEU A 311     8491  10141   5989    662     75   -608       C  
ATOM   2406  CD1 LEU A 311     -16.142  35.891  31.157  1.00 63.67           C  
ANISOU 2406  CD1 LEU A 311     8236  10080   5876    518    125   -499       C  
ATOM   2407  CD2 LEU A 311     -16.586  37.727  29.568  1.00 67.43           C  
ANISOU 2407  CD2 LEU A 311     8960  10291   6370    657     44   -586       C  
ATOM   2408  N   ASP A 312     -20.610  39.280  31.462  1.00 60.91           N  
ANISOU 2408  N   ASP A 312     7848  10025   5272   1227    -52   -786       N  
ATOM   2409  CA  ASP A 312     -22.050  39.224  31.570  1.00 61.65           C  
ANISOU 2409  CA  ASP A 312     7802  10329   5291   1360    -70   -791       C  
ATOM   2410  C   ASP A 312     -22.565  38.835  30.231  1.00 62.92           C  
ANISOU 2410  C   ASP A 312     7984  10426   5496   1320    -93   -715       C  
ATOM   2411  O   ASP A 312     -22.521  39.660  29.329  1.00 64.39           O  
ANISOU 2411  O   ASP A 312     8331  10429   5708   1383   -142   -750       O  
ATOM   2412  CB  ASP A 312     -22.645  40.563  32.010  1.00 66.00           C  
ANISOU 2412  CB  ASP A 312     8403  10903   5771   1590   -124   -930       C  
ATOM   2413  CG  ASP A 312     -24.065  40.370  32.478  1.00 75.72           C  
ANISOU 2413  CG  ASP A 312     9439  12424   6906   1727   -126   -938       C  
ATOM   2414  OD1 ASP A 312     -24.963  40.230  31.613  1.00 73.67           O  
ANISOU 2414  OD1 ASP A 312     9145  12199   6648   1767   -155   -898       O  
ATOM   2415  OD2 ASP A 312     -24.266  40.239  33.704  1.00 87.44           O  
ANISOU 2415  OD2 ASP A 312    10789  14122   8312   1780    -94   -973       O  
ATOM   2416  N   ASP A 313     -23.067  37.613  30.073  1.00 56.33           N  
ANISOU 2416  N   ASP A 313     6996   9738   4670   1216    -64   -611       N  
ATOM   2417  CA  ASP A 313     -23.474  37.123  28.759  1.00 55.68           C  
ANISOU 2417  CA  ASP A 313     6933   9590   4634   1157    -89   -540       C  
ATOM   2418  C   ASP A 313     -24.571  37.969  28.088  1.00 62.31           C  
ANISOU 2418  C   ASP A 313     7801  10445   5429   1335   -157   -595       C  
ATOM   2419  O   ASP A 313     -24.502  38.204  26.867  1.00 61.87           O  
ANISOU 2419  O   ASP A 313     7875  10220   5411   1331   -196   -580       O  
ATOM   2420  CB  ASP A 313     -23.873  35.659  28.841  1.00 56.53           C  
ANISOU 2420  CB  ASP A 313     6860   9860   4758   1016    -55   -430       C  
ATOM   2421  CG  ASP A 313     -22.707  34.756  29.216  1.00 59.54           C  
ANISOU 2421  CG  ASP A 313     7246  10181   5197    835      1   -363       C  
ATOM   2422  OD1 ASP A 313     -21.572  35.012  28.748  1.00 58.15           O  
ANISOU 2422  OD1 ASP A 313     7229   9787   5078    771      6   -374       O  
ATOM   2423  OD2 ASP A 313     -22.936  33.776  29.905  1.00 64.97           O  
ANISOU 2423  OD2 ASP A 313     7777  11035   5875    755     38   -294       O  
ATOM   2424  N   HIS A 314     -25.532  38.473  28.879  1.00 59.68           N  
ANISOU 2424  N   HIS A 314     7354  10312   5009   1504   -171   -662       N  
ATOM   2425  CA  HIS A 314     -26.589  39.325  28.356  1.00 59.96           C  
ANISOU 2425  CA  HIS A 314     7407  10382   4994   1701   -239   -725       C  
ATOM   2426  C   HIS A 314     -26.033  40.699  27.943  1.00 62.68           C  
ANISOU 2426  C   HIS A 314     7995  10468   5353   1817   -291   -813       C  
ATOM   2427  O   HIS A 314     -26.260  41.116  26.812  1.00 59.73           O  
ANISOU 2427  O   HIS A 314     7737   9958   4999   1864   -343   -804       O  
ATOM   2428  CB  HIS A 314     -27.751  39.484  29.344  1.00 61.67           C  
ANISOU 2428  CB  HIS A 314     7428  10898   5107   1860   -238   -779       C  
ATOM   2429  CG  HIS A 314     -28.914  40.196  28.725  1.00 66.57           C  
ANISOU 2429  CG  HIS A 314     8037  11581   5674   2059   -309   -832       C  
ATOM   2430  ND1 HIS A 314     -29.014  41.576  28.754  1.00 69.52