CNRS Nantes University UFIP UFIP
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***  SIRT1  ***

elNémo ID: 19120820005893450

Job options:

ID        	=	 19120820005893450
JOBID     	=	 SIRT1
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER SIRT1

HEADER    HYDROLASE/HYDROLASE ACTIVATOR           22-MAY-15   4ZZH              
TITLE     SIRT1/ACTIVATOR COMPLEX                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-1;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HSIRT1,REGULATORY PROTEIN SIR2 HOMOLOG 1,SIR2-LIKE PROTEIN  
COMPND   5 1,HSIR2;                                                             
COMPND   6 EC: 3.5.1.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SIRT1, SIR2L1;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SIRTUIN, ACTIVATOR, DEACYLASE, COMPLEX, HYDROLASE-HYDROLASE ACTIVATOR 
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.DAI                                                                 
REVDAT   3   22-NOV-17 4ZZH    1       REMARK                                   
REVDAT   2   23-SEP-15 4ZZH    1       REMARK                                   
REVDAT   1   15-JUL-15 4ZZH    0                                                
JRNL        AUTH   H.DAI,A.W.CASE,T.V.RIERA,T.CONSIDINE,J.E.LEE,Y.HAMURO,       
JRNL        AUTH 2 H.ZHAO,Y.JIANG,S.M.SWEITZER,B.PIETRAK,B.SCHWARTZ,C.A.BLUM,   
JRNL        AUTH 3 J.S.DISCH,R.CALDWELL,B.SZCZEPANKIEWICZ,C.OALMANN,P.YEE NG,   
JRNL        AUTH 4 B.H.WHITE,R.CASAUBON,R.NARAYAN,K.KOPPETSCH,F.BOURBONAIS,     
JRNL        AUTH 5 B.WU,J.WANG,D.QIAN,F.JIANG,C.MAO,M.WANG,E.HU,J.C.WU,         
JRNL        AUTH 6 R.B.PERNI,G.P.VLASUK,J.L.ELLIS                               
JRNL        TITL   CRYSTALLOGRAPHIC STRUCTURE OF A SMALL MOLECULE SIRT1         
JRNL        TITL 2 ACTIVATOR-ENZYME COMPLEX.                                    
JRNL        REF    NAT COMMUN                    V.   6  7645 2015              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   26134520                                                     
JRNL        DOI    10.1038/NCOMMS8645                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.67                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 13610                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.960                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 675                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 45.6713 -  5.2988    0.99     2670   145  0.1656 0.2230        
REMARK   3     2  5.2988 -  4.2068    0.99     2605   135  0.1621 0.2122        
REMARK   3     3  4.2068 -  3.6753    1.00     2559   132  0.1817 0.2103        
REMARK   3     4  3.6753 -  3.3393    0.99     2554   133  0.2424 0.3088        
REMARK   3     5  3.3393 -  3.1001    0.99     2547   130  0.2974 0.3774        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.440            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.300           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           2829                                  
REMARK   3   ANGLE     :  1.039           3846                                  
REMARK   3   CHIRALITY :  0.039            422                                  
REMARK   3   PLANARITY :  0.005            500                                  
REMARK   3   DIHEDRAL  : 14.129           1076                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 278 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4992 -47.4175  -6.0560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6020 T22:   0.6880                                     
REMARK   3      T33:   0.7225 T12:   0.0066                                     
REMARK   3      T13:  -0.0425 T23:  -0.0296                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4090 L22:   2.0066                                     
REMARK   3      L33:   3.1536 L12:   0.2643                                     
REMARK   3      L13:   0.6533 L23:  -0.2411                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1336 S12:  -0.1466 S13:  -0.1133                       
REMARK   3      S21:   0.0543 S22:  -0.0274 S23:  -0.0969                       
REMARK   3      S31:   0.4614 S32:  -0.2412 S33:  -0.1058                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 279 THROUGH 439 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4042 -17.7405 -22.8322              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0952 T22:   0.8452                                     
REMARK   3      T33:   1.1069 T12:   0.0801                                     
REMARK   3      T13:  -0.1756 T23:  -0.1277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0130 L22:   3.3911                                     
REMARK   3      L33:   1.9895 L12:  -0.1684                                     
REMARK   3      L13:  -0.2864 L23:  -0.7691                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0905 S12:  -0.4150 S13:   1.1083                       
REMARK   3      S21:  -0.0400 S22:  -0.0619 S23:  -0.4258                       
REMARK   3      S31:  -0.7710 S32:  -0.0735 S33:   0.1589                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 440 THROUGH 658 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.2033 -43.3574 -25.7575              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7676 T22:   0.7230                                     
REMARK   3      T33:   0.6214 T12:   0.0338                                     
REMARK   3      T13:  -0.0424 T23:  -0.0259                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7232 L22:   4.7255                                     
REMARK   3      L33:   2.9026 L12:  -0.1270                                     
REMARK   3      L13:  -0.2683 L23:   0.3627                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0876 S12:  -0.2331 S13:  -0.0460                       
REMARK   3      S21:  -0.8021 S22:  -0.0386 S23:  -0.1048                       
REMARK   3      S31:  -0.1703 S32:  -0.0433 S33:   0.1380                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4ZZH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209908.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-DEC-11                          
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               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97923                            
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 : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13615                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.670                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.78100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 0.1 M TRIS     
REMARK 280  PH 8.5, AND 16 % W/V PEG 4000, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y+1/2,Z                                             
REMARK 290       7555   -X+1/2,Y,-Z                                             
REMARK 290       8555   X,-Y,-Z+1/2                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       49.59500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.26000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.82000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.26000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.59500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.82000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       49.59500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.82000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       66.26000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.82000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       49.59500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       66.26000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       49.59500            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASN A   630                                                      
REMARK 465     PRO A   631                                                      
REMARK 465     VAL A   632                                                      
REMARK 465     GLY A   633                                                      
REMARK 465     GLY A   634                                                      
REMARK 465     GLY A   635                                                      
REMARK 465     SER A   636                                                      
REMARK 465     GLY A   637                                                      
REMARK 465     GLY A   638                                                      
REMARK 465     GLY A   639                                                      
REMARK 465     SER A   659                                                      
REMARK 465     ASP A   660                                                      
REMARK 465     SER A   661                                                      
REMARK 465     GLU A   662                                                      
REMARK 465     ASP A   663                                                      
REMARK 465     ASP A   664                                                      
REMARK 465     VAL A   665                                                      
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   OD2  ASP A   272     OG   SER A   275              2.15            
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    PRO A 318   C   -  N   -  CA  ANGL. DEV. =   9.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A 212      153.30    -49.32                                   
REMARK 500    ASN A 241      -45.15   -142.16                                   
REMARK 500    PHE A 273       -6.66   -143.69                                   
REMARK 500    THR A 349       17.55     55.54                                   
REMARK 500    ILE A 373      -70.20   -106.83                                   
REMARK 500    ASP A 401       43.39    -91.88                                   
REMARK 500    ALA A 405       43.75    -81.83                                   
REMARK 500    GLU A 410       48.62    -77.81                                   
REMARK 500    LEU A 435      126.47   -170.86                                   
REMARK 500    LEU A 443       50.72     35.88                                   
REMARK 500    LEU A 469       72.98   -118.79                                   
REMARK 500    LYS A 499       26.08    -76.99                                   
REMARK 500    ASN A 648       17.59   -168.28                                   
REMARK 500    PHE A 652     -161.48   -104.84                                   
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                              ZN A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 371   SG                                                     
REMARK 620 2 CYS A 374   SG  111.4                                              
REMARK 620 3 CYS A 395   SG  104.7  79.7                                        
REMARK 620 4 CYS A 398   SG  138.6  91.6 113.3                                  
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 ZN A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 4TO A 702                 
DBREF  4ZZH A  183   632  UNP    Q96EB6   SIR1_HUMAN     183    505             
SEQADV 4ZZH GLY A  633  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH GLY A  634  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH GLY A  635  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH SER A  636  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH GLY A  637  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH GLY A  638  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH GLY A  639  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH SER A  640  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH GLN A  641  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH TYR A  642  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH LEU A  643  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH PHE A  644  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH LEU A  645  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH PRO A  646  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH PRO A  647  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH ASN A  648  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH ARG A  649  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH TYR A  650  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH ILE A  651  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH PHE A  652  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH HIS A  653  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH GLY A  654  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH ALA A  655  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH GLU A  656  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH VAL A  657  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH TYR A  658  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH SER A  659  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH ASP A  660  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH SER A  661  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH GLU A  662  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH ASP A  663  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH ASP A  664  UNP  Q96EB6              EXPRESSION TAG                 
SEQADV 4ZZH VAL A  665  UNP  Q96EB6              EXPRESSION TAG                 
SEQRES   1 A  356  GLY PRO TYR THR PHE VAL GLN GLN HIS LEU MET ILE GLY          
SEQRES   2 A  356  THR ASP PRO ARG THR ILE LEU LYS ASP LEU LEU PRO GLU          
SEQRES   3 A  356  THR ILE PRO PRO PRO GLU LEU ASP ASP MET THR LEU TRP          
SEQRES   4 A  356  GLN ILE VAL ILE ASN ILE LEU SER GLU PRO PRO LYS ARG          
SEQRES   5 A  356  LYS LYS ARG LYS ASP ILE ASN THR ILE GLU ASP ALA VAL          
SEQRES   6 A  356  LYS LEU LEU GLN GLU CYS LYS LYS ILE ILE VAL LEU THR          
SEQRES   7 A  356  GLY ALA GLY VAL SER VAL SER CYS GLY ILE PRO ASP PHE          
SEQRES   8 A  356  ARG SER ARG ASP GLY ILE TYR ALA ARG LEU ALA VAL ASP          
SEQRES   9 A  356  PHE PRO ASP LEU PRO ASP PRO GLN ALA MET PHE ASP ILE          
SEQRES  10 A  356  GLU TYR PHE ARG LYS ASP PRO ARG PRO PHE PHE LYS PHE          
SEQRES  11 A  356  ALA LYS GLU ILE TYR PRO GLY GLN PHE GLN PRO SER LEU          
SEQRES  12 A  356  CYS HIS LYS PHE ILE ALA LEU SER ASP LYS GLU GLY LYS          
SEQRES  13 A  356  LEU LEU ARG ASN TYR THR GLN ASN ILE ASP THR LEU GLU          
SEQRES  14 A  356  GLN VAL ALA GLY ILE GLN ARG ILE ILE GLN CYS HIS GLY          
SEQRES  15 A  356  SER PHE ALA THR ALA SER CYS LEU ILE CYS LYS TYR LYS          
SEQRES  16 A  356  VAL ASP CYS GLU ALA VAL ARG GLY ASP ILE PHE ASN GLN          
SEQRES  17 A  356  VAL VAL PRO ARG CYS PRO ARG CYS PRO ALA ASP GLU PRO          
SEQRES  18 A  356  LEU ALA ILE MET LYS PRO GLU ILE VAL PHE PHE GLY GLU          
SEQRES  19 A  356  ASN LEU PRO GLU GLN PHE HIS ARG ALA MET LYS TYR ASP          
SEQRES  20 A  356  LYS ASP GLU VAL ASP LEU LEU ILE VAL ILE GLY SER SER          
SEQRES  21 A  356  LEU LYS VAL ARG PRO VAL ALA LEU ILE PRO SER SER ILE          
SEQRES  22 A  356  PRO HIS GLU VAL PRO GLN ILE LEU ILE ASN ARG GLU PRO          
SEQRES  23 A  356  LEU PRO HIS LEU HIS PHE ASP VAL GLU LEU LEU GLY ASP          
SEQRES  24 A  356  CYS ASP VAL ILE ILE ASN GLU LEU CYS HIS ARG LEU GLY          
SEQRES  25 A  356  GLY GLU TYR ALA LYS LEU CYS CYS ASN PRO VAL GLY GLY          
SEQRES  26 A  356  GLY SER GLY GLY GLY SER GLN TYR LEU PHE LEU PRO PRO          
SEQRES  27 A  356  ASN ARG TYR ILE PHE HIS GLY ALA GLU VAL TYR SER ASP          
SEQRES  28 A  356  SER GLU ASP ASP VAL                                          
HET     ZN  A 701       1                                                       
HET    4TO  A 702      36                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     4TO (4S)-N-[3-(1,3-OXAZOL-5-YL)PHENYL]-7-[3-                         
HETNAM   2 4TO  (TRIFLUOROMETHYL)PHENYL]-3,4-DIHYDRO-1,4-                       
HETNAM   3 4TO  METHANOPYRIDO[2,3-B][1,4]DIAZEPINE-5(2H)-CARBOXAMIDE            
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  4TO    C26 H20 F3 N5 O2                                             
HELIX    1 AA1 GLY A  183  ILE A  194  1                                  12    
HELIX    2 AA2 ASP A  197  LEU A  206  1                                  10    
HELIX    3 AA3 ASP A  216  GLU A  230  1                                  15    
HELIX    4 AA4 THR A  242  CYS A  253  1                                  12    
HELIX    5 AA5 ALA A  262  VAL A  266  5                                   5    
HELIX    6 AA6 GLY A  278  VAL A  285  1                                   8    
HELIX    7 AA7 GLN A  294  PHE A  297  5                                   4    
HELIX    8 AA8 ASP A  298  ASP A  305  1                                   8    
HELIX    9 AA9 PRO A  306  TYR A  317  1                                  12    
HELIX   10 AB1 SER A  324  GLU A  336  1                                  13    
HELIX   11 AB2 THR A  349  ALA A  354  1                                   6    
HELIX   12 AB3 VAL A  383  ASN A  389  1                                   7    
HELIX   13 AB4 PRO A  419  LYS A  430  1                                  12    
HELIX   14 AB5 PRO A  447  ILE A  455  5                                   9    
HELIX   15 AB6 ASP A  481  GLY A  494  1                                  14    
HELIX   16 AB7 GLY A  494  LYS A  499  1                                   6    
SHEET    1 AA1 8 ILE A 359  GLN A 361  0                                        
SHEET    2 AA1 8 LEU A 339  THR A 344  1  N  THR A 344   O  ILE A 360           
SHEET    3 AA1 8 ILE A 256  THR A 260  1  N  VAL A 258   O  ARG A 341           
SHEET    4 AA1 8 LEU A 435  ILE A 439  1  O  ILE A 439   N  LEU A 259           
SHEET    5 AA1 8 GLN A 461  ASN A 465  1  O  ILE A 462   N  VAL A 438           
SHEET    6 AA1 8 VAL A 476  LEU A 479  1  O  LEU A 478   N  LEU A 463           
SHEET    7 AA1 8 ARG A 649  ILE A 651  1  O  TYR A 650   N  LEU A 479           
SHEET    8 AA1 8 LEU A 643  LEU A 645 -1  N  LEU A 645   O  ARG A 649           
SHEET    1 AA2 3 LYS A 377  ASP A 379  0                                        
SHEET    2 AA2 3 GLY A 364  CYS A 371 -1  N  ALA A 369   O  VAL A 378           
SHEET    3 AA2 3 MET A 407  ILE A 411 -1  O  LYS A 408   N  SER A 370           
LINK         SG  CYS A 371                ZN    ZN A 701     1555   1555  2.30  
LINK         SG  CYS A 374                ZN    ZN A 701     1555   1555  2.71  
LINK         SG  CYS A 395                ZN    ZN A 701     1555   1555  2.46  
LINK         SG  CYS A 398                ZN    ZN A 701     1555   1555  2.49  
CISPEP   1 ARG A  446    PRO A  447          0         9.90                     
CISPEP   2 PRO A  646    PRO A  647          0         8.98                     
SITE     1 AC1  4 CYS A 371  CYS A 374  CYS A 395  CYS A 398                    
SITE     1 AC2  7 THR A 209  PRO A 211  PRO A 212  ILE A 223                    
SITE     2 AC2  7 ASN A 226  ILE A 227  GLU A 230                               
CRYST1   99.190  111.640  132.520  90.00  90.00  90.00 I 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010082  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008957  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007546        0.00000                         
ATOM      1  N   GLY A 183      15.118 -42.015  11.495  1.00 91.60           N  
ANISOU    1  N   GLY A 183    11173  13120  10510   -312    -69   -523       N  
ATOM      2  CA  GLY A 183      13.986 -42.886  11.784  1.00 92.93           C  
ANISOU    2  CA  GLY A 183    11298  13464  10547   -448     37   -435       C  
ATOM      3  C   GLY A 183      14.388 -44.342  11.953  1.00 88.97           C  
ANISOU    3  C   GLY A 183    10907  12884  10015   -617    -74   -272       C  
ATOM      4  O   GLY A 183      14.304 -44.885  13.054  1.00 90.02           O  
ANISOU    4  O   GLY A 183    11160  13088   9955   -739    -78   -206       O  
ATOM      5  N   PRO A 184      14.817 -44.989  10.852  1.00 86.04           N  
ANISOU    5  N   PRO A 184    10510  12357   9823   -620   -166   -207       N  
ATOM      6  CA  PRO A 184      15.505 -46.283  10.875  1.00 78.84           C  
ANISOU    6  CA  PRO A 184     9732  11298   8926   -726   -310    -73       C  
ATOM      7  C   PRO A 184      16.739 -46.264  11.774  1.00 77.73           C  
ANISOU    7  C   PRO A 184     9748  11049   8737   -701   -454    -64       C  
ATOM      8  O   PRO A 184      17.102 -47.273  12.359  1.00 79.06           O  
ANISOU    8  O   PRO A 184    10062  11156   8823   -805   -557     53       O  
ATOM      9  CB  PRO A 184      15.916 -46.480   9.412  1.00 63.01           C  
ANISOU    9  CB  PRO A 184     7654   9139   7149   -648   -367    -73       C  
ATOM     10  CG  PRO A 184      14.908 -45.752   8.651  1.00 62.51           C  
ANISOU   10  CG  PRO A 184     7415   9198   7138   -595   -228   -148       C  
ATOM     11  CD  PRO A 184      14.574 -44.538   9.471  1.00 91.03           C  
ANISOU   11  CD  PRO A 184    10989  12950  10646   -517   -129   -261       C  
ATOM     12  N   TYR A 185      17.384 -45.107  11.855  1.00 87.95           N  
ANISOU   12  N   TYR A 185    11016  12315  10086   -566   -474   -184       N  
ATOM     13  CA  TYR A 185      18.588 -44.929  12.655  1.00 92.69           C  
ANISOU   13  CA  TYR A 185    11740  12825  10654   -540   -623   -189       C  
ATOM     14  C   TYR A 185      18.269 -45.114  14.140  1.00 87.22           C  
ANISOU   14  C   TYR A 185    11193  12251   9698   -650   -612   -157       C  
ATOM     15  O   TYR A 185      19.012 -45.783  14.874  1.00 82.18           O  
ANISOU   15  O   TYR A 185    10700  11541   8982   -712   -759    -67       O  
ATOM     16  CB  TYR A 185      19.188 -43.541  12.386  1.00 64.25           C  
ANISOU   16  CB  TYR A 185     8074   9180   7158   -400   -633   -331       C  
ATOM     17  CG  TYR A 185      20.533 -43.252  13.038  1.00 64.68           C  
ANISOU   17  CG  TYR A 185     8223   9136   7215   -376   -806   -343       C  
ATOM     18  CD1 TYR A 185      21.725 -43.546  12.387  1.00 63.79           C  
ANISOU   18  CD1 TYR A 185     8074   8876   7288   -325   -950   -301       C  
ATOM     19  CD2 TYR A 185      20.607 -42.651  14.295  1.00 66.17           C  
ANISOU   19  CD2 TYR A 185     8530   9394   7216   -404   -826   -403       C  
ATOM     20  CE1 TYR A 185      22.951 -43.266  12.975  1.00 64.41           C  
ANISOU   20  CE1 TYR A 185     8208   8887   7376   -309  -1117   -307       C  
ATOM     21  CE2 TYR A 185      21.822 -42.367  14.884  1.00 66.73           C  
ANISOU   21  CE2 TYR A 185     8684   9383   7287   -397  -1002   -413       C  
ATOM     22  CZ  TYR A 185      22.991 -42.672  14.225  1.00 65.86           C  
ANISOU   22  CZ  TYR A 185     8512   9137   7375   -354  -1151   -361       C  
ATOM     23  OH  TYR A 185      24.198 -42.378  14.820  1.00 66.65           O  
ANISOU   23  OH  TYR A 185     8666   9178   7479   -354  -1335   -365       O  
ATOM     24  N   THR A 186      17.156 -44.527  14.573  1.00 81.63           N  
ANISOU   24  N   THR A 186    10441  11730   8844   -666   -436   -228       N  
ATOM     25  CA  THR A 186      16.723 -44.658  15.955  1.00 87.91           C  
ANISOU   25  CA  THR A 186    11366  12671   9365   -773   -388   -207       C  
ATOM     26  C   THR A 186      16.336 -46.096  16.236  1.00 89.50           C  
ANISOU   26  C   THR A 186    11650  12895   9462   -957   -409    -27       C  
ATOM     27  O   THR A 186      16.680 -46.644  17.288  1.00 92.53           O  
ANISOU   27  O   THR A 186    12212  13279   9668  -1062   -496     59       O  
ATOM     28  CB  THR A 186      15.548 -43.730  16.271  1.00 89.00           C  
ANISOU   28  CB  THR A 186    11416  13025   9376   -728   -170   -330       C  
ATOM     29  OG1 THR A 186      16.030 -42.387  16.362  1.00 91.61           O  
ANISOU   29  OG1 THR A 186    11754  13309   9746   -571   -182   -496       O  
ATOM     30  CG2 THR A 186      14.911 -44.108  17.605  1.00 91.20           C  
ANISOU   30  CG2 THR A 186    11811  13490   9350   -867    -83   -282       C  
ATOM     31  N   PHE A 187      15.636 -46.702  15.280  1.00 81.32           N  
ANISOU   31  N   PHE A 187    10497  11867   8533  -1005   -342     34       N  
ATOM     32  CA  PHE A 187      15.227 -48.099  15.374  1.00 79.56           C  
ANISOU   32  CA  PHE A 187    10357  11636   8236  -1197   -370    209       C  
ATOM     33  C   PHE A 187      16.394 -49.010  15.735  1.00 80.98           C  
ANISOU   33  C   PHE A 187    10738  11609   8422  -1233   -595    326       C  
ATOM     34  O   PHE A 187      16.260 -49.906  16.573  1.00 83.96           O  
ANISOU   34  O   PHE A 187    11281  11999   8621  -1395   -642    462       O  
ATOM     35  CB  PHE A 187      14.605 -48.549  14.056  1.00 80.34           C  
ANISOU   35  CB  PHE A 187    10312  11708   8506  -1216   -321    239       C  
ATOM     36  CG  PHE A 187      14.480 -50.047  13.914  1.00 83.17           C  
ANISOU   36  CG  PHE A 187    10790  11968   8845  -1398   -408    415       C  
ATOM     37  CD1 PHE A 187      13.398 -50.721  14.460  1.00 84.95           C  
ANISOU   37  CD1 PHE A 187    11040  12353   8882  -1619   -310    524       C  
ATOM     38  CD2 PHE A 187      15.434 -50.776  13.214  1.00 76.66           C  
ANISOU   38  CD2 PHE A 187    10053  10887   8187  -1347   -583    471       C  
ATOM     39  CE1 PHE A 187      13.279 -52.087  14.326  1.00 82.50           C  
ANISOU   39  CE1 PHE A 187    10865  11929   8551  -1803   -403    690       C  
ATOM     40  CE2 PHE A 187      15.321 -52.144  13.077  1.00 74.58           C  
ANISOU   40  CE2 PHE A 187     9930  10504   7904  -1501   -673    624       C  
ATOM     41  CZ  PHE A 187      14.244 -52.800  13.630  1.00 80.29           C  
ANISOU   41  CZ  PHE A 187    10700  11365   8440  -1738   -590    736       C  
ATOM     42  N   VAL A 188      17.535 -48.764  15.095  1.00 78.10           N  
ANISOU   42  N   VAL A 188    10353  11059   8262  -1077   -732    279       N  
ATOM     43  CA  VAL A 188      18.738 -49.567  15.288  1.00 76.93           C  
ANISOU   43  CA  VAL A 188    10356  10712   8163  -1062   -955    378       C  
ATOM     44  C   VAL A 188      19.411 -49.228  16.607  1.00 71.84           C  
ANISOU   44  C   VAL A 188     9852  10094   7349  -1068  -1057    376       C  
ATOM     45  O   VAL A 188      20.008 -50.097  17.243  1.00 75.87           O  
ANISOU   45  O   VAL A 188    10538  10506   7782  -1128  -1222    502       O  
ATOM     46  CB  VAL A 188      19.727 -49.370  14.118  1.00 68.50           C  
ANISOU   46  CB  VAL A 188     9183   9472   7373   -885  -1048    321       C  
ATOM     47  CG1 VAL A 188      21.118 -49.911  14.452  1.00 69.02           C  
ANISOU   47  CG1 VAL A 188     9366   9367   7491   -821  -1278    392       C  
ATOM     48  CG2 VAL A 188      19.170 -50.015  12.866  1.00 67.50           C  
ANISOU   48  CG2 VAL A 188     8978   9283   7385   -900   -989    353       C  
ATOM     49  N   GLN A 189      19.296 -47.966  17.023  1.00 74.50           N  
ANISOU   49  N   GLN A 189    10128  10556   7622  -1005   -968    232       N  
ATOM     50  CA  GLN A 189      19.809 -47.520  18.318  1.00 73.34           C  
ANISOU   50  CA  GLN A 189    10127  10457   7284  -1023  -1051    208       C  
ATOM     51  C   GLN A 189      19.112 -48.240  19.457  1.00 82.02           C  
ANISOU   51  C   GLN A 189    11397  11676   8091  -1208  -1010    323       C  
ATOM     52  O   GLN A 189      19.752 -48.688  20.413  1.00 77.20           O  
ANISOU   52  O   GLN A 189    10975  11020   7336  -1270  -1169    412       O  
ATOM     53  CB  GLN A 189      19.617 -46.022  18.484  1.00 73.06           C  
ANISOU   53  CB  GLN A 189    10010  10530   7221   -926   -937     17       C  
ATOM     54  CG  GLN A 189      20.641 -45.153  17.802  1.00 71.73           C  
ANISOU   54  CG  GLN A 189     9743  10232   7277   -771  -1036    -89       C  
ATOM     55  CD  GLN A 189      20.333 -43.686  18.004  1.00 74.26           C  
ANISOU   55  CD  GLN A 189    10022  10641   7551   -691   -923   -275       C  
ATOM     56  OE1 GLN A 189      19.393 -43.148  17.412  1.00 70.86           O  
ANISOU   56  OE1 GLN A 189     9466  10294   7163   -638   -738   -359       O  
ATOM     57  NE2 GLN A 189      21.109 -43.033  18.860  1.00 72.58           N  
ANISOU   57  NE2 GLN A 189     9926  10407   7245   -679  -1043   -340       N  
ATOM     58  N   GLN A 190      17.789 -48.326  19.338  1.00 86.26           N  
ANISOU   58  N   GLN A 190    11858  12379   8537  -1301   -796    325       N  
ATOM     59  CA  GLN A 190      16.958 -49.062  20.279  1.00 93.18           C  
ANISOU   59  CA  GLN A 190    12866  13399   9140  -1506   -718    448       C  
ATOM     60  C   GLN A 190      17.476 -50.482  20.410  1.00 92.57           C  
ANISOU   60  C   GLN A 190    12971  13148   9056  -1624   -912    653       C  
ATOM     61  O   GLN A 190      17.710 -50.969  21.512  1.00101.05           O  
ANISOU   61  O   GLN A 190    14255  14230   9910  -1739  -1005    760       O  
ATOM     62  CB  GLN A 190      15.492 -49.073  19.828  1.00 98.89           C  
ANISOU   62  CB  GLN A 190    13423  14317   9834  -1588   -471    437       C  
ATOM     63  CG  GLN A 190      14.813 -47.710  19.829  1.00111.63           C  
ANISOU   63  CG  GLN A 190    14869  16127  11419  -1465   -263    242       C  
ATOM     64  CD  GLN A 190      14.648 -47.140  21.226  1.00130.11           C  
ANISOU   64  CD  GLN A 190    17338  18640  13460  -1496   -189    181       C  
ATOM     65  OE1 GLN A 190      15.226 -46.105  21.556  1.00134.56           O  
ANISOU   65  OE1 GLN A 190    17935  19177  14015  -1352   -224     33       O  
ATOM     66  NE2 GLN A 190      13.851 -47.811  22.054  1.00137.65           N  
ANISOU   66  NE2 GLN A 190    18374  19772  14156  -1694    -84    296       N  
ATOM     67  N   HIS A 191      17.678 -51.134  19.273  1.00 84.84           N  
ANISOU   67  N   HIS A 191    11925  11999   8313  -1586   -979    705       N  
ATOM     68  CA  HIS A 191      18.109 -52.525  19.256  1.00 86.85           C  
ANISOU   68  CA  HIS A 191    12359  12058   8583  -1676  -1160    892       C  
ATOM     69  C   HIS A 191      19.498 -52.733  19.852  1.00 85.25           C  
ANISOU   69  C   HIS A 191    12319  11689   8384  -1588  -1416    941       C  
ATOM     70  O   HIS A 191      19.751 -53.727  20.520  1.00 89.97           O  
ANISOU   70  O   HIS A 191    13137  12193   8854  -1696  -1562   1106       O  
ATOM     71  CB  HIS A 191      18.069 -53.060  17.832  1.00 87.01           C  
ANISOU   71  CB  HIS A 191    12272  11926   8862  -1621  -1172    902       C  
ATOM     72  CG  HIS A 191      16.723 -53.573  17.423  1.00 94.36           C  
ANISOU   72  CG  HIS A 191    13147  12963   9742  -1802  -1008    961       C  
ATOM     73  ND1 HIS A 191      16.372 -54.903  17.523  1.00 96.83           N  
ANISOU   73  ND1 HIS A 191    13635  13180   9976  -1998  -1075   1143       N  
ATOM     74  CD2 HIS A 191      15.638 -52.935  16.923  1.00 95.11           C  
ANISOU   74  CD2 HIS A 191    13030  13255   9853  -1823   -790    868       C  
ATOM     75  CE1 HIS A 191      15.134 -55.063  17.093  1.00 99.19           C  
ANISOU   75  CE1 HIS A 191    13821  13621  10246  -2151   -906   1160       C  
ATOM     76  NE2 HIS A 191      14.664 -53.885  16.723  1.00 98.37           N  
ANISOU   76  NE2 HIS A 191    13471  13705  10201  -2040   -730    995       N  
ATOM     77  N   LEU A 192      20.399 -51.794  19.616  1.00 77.75           N  
ANISOU   77  N   LEU A 192    11259  10703   7580  -1397  -1481    805       N  
ATOM     78  CA  LEU A 192      21.736 -51.872  20.194  1.00 82.79           C  
ANISOU   78  CA  LEU A 192    12011  11216   8228  -1310  -1728    842       C  
ATOM     79  C   LEU A 192      21.690 -51.810  21.714  1.00 87.56           C  
ANISOU   79  C   LEU A 192    12818  11932   8518  -1436  -1776    896       C  
ATOM     80  O   LEU A 192      22.556 -52.372  22.386  1.00 82.36           O  
ANISOU   80  O   LEU A 192    12331  11165   7796  -1438  -2004   1007       O  
ATOM     81  CB  LEU A 192      22.623 -50.742  19.666  1.00 76.76           C  
ANISOU   81  CB  LEU A 192    11068  10430   7669  -1113  -1767    678       C  
ATOM     82  CG  LEU A 192      23.038 -50.747  18.199  1.00 74.57           C  
ANISOU   82  CG  LEU A 192    10600  10024   7708   -960  -1766    627       C  
ATOM     83  CD1 LEU A 192      23.140 -49.326  17.749  1.00 73.00           C  
ANISOU   83  CD1 LEU A 192    10211   9907   7619   -852  -1664    442       C  
ATOM     84  CD2 LEU A 192      24.361 -51.459  17.999  1.00 74.88           C  
ANISOU   84  CD2 LEU A 192    10678   9870   7901   -843  -2011    711       C  
ATOM     85  N   MET A 193      20.684 -51.111  22.242  1.00 90.93           N  
ANISOU   85  N   MET A 193    13224  12581   8745  -1529  -1562    814       N  
ATOM     86  CA  MET A 193      20.542 -50.908  23.686  1.00 90.00           C  
ANISOU   86  CA  MET A 193    13295  12603   8299  -1647  -1567    837       C  
ATOM     87  C   MET A 193      20.273 -52.220  24.408  1.00 96.83           C  
ANISOU   87  C   MET A 193    14399  13437   8956  -1845  -1645   1062       C  
ATOM     88  O   MET A 193      20.546 -52.345  25.601  1.00102.53           O  
ANISOU   88  O   MET A 193    15333  14201   9424  -1934  -1748   1133       O  
ATOM     89  CB  MET A 193      19.413 -49.912  24.001  1.00 84.57           C  
ANISOU   89  CB  MET A 193    12517  12171   7443  -1685  -1285    690       C  
ATOM     90  CG  MET A 193      19.788 -48.446  23.873  1.00 83.53           C  
ANISOU   90  CG  MET A 193    12262  12080   7395  -1512  -1248    466       C  
ATOM     91  SD  MET A 193      21.332 -48.087  24.728  1.00 85.45           S  
ANISOU   91  SD  MET A 193    12669  12205   7592  -1449  -1549    452       S  
ATOM     92  CE  MET A 193      21.155 -46.333  25.006  1.00143.21           C  
ANISOU   92  CE  MET A 193    19919  19653  14841  -1345  -1411    187       C  
ATOM     93  N   ILE A 194      19.745 -53.198  23.677  1.00 98.00           N  
ANISOU   93  N   ILE A 194    14530  13502   9203  -1924  -1607   1177       N  
ATOM     94  CA  ILE A 194      19.331 -54.460  24.276  1.00 95.97           C  
ANISOU   94  CA  ILE A 194    14507  13208   8749  -2144  -1661   1399       C  
ATOM     95  C   ILE A 194      20.081 -55.675  23.726  1.00 97.04           C  
ANISOU   95  C   ILE A 194    14761  13046   9065  -2104  -1901   1552       C  
ATOM     96  O   ILE A 194      19.847 -56.796  24.156  1.00107.67           O  
ANISOU   96  O   ILE A 194    16332  14307  10271  -2276  -1984   1748       O  
ATOM     97  CB  ILE A 194      17.823 -54.681  24.087  1.00 88.63           C  
ANISOU   97  CB  ILE A 194    13501  12465   7711  -2340  -1392   1429       C  
ATOM     98  CG1 ILE A 194      17.507 -55.106  22.660  1.00 86.66           C  
ANISOU   98  CG1 ILE A 194    13087  12095   7743  -2300  -1350   1423       C  
ATOM     99  CG2 ILE A 194      17.060 -53.425  24.430  1.00 88.53           C  
ANISOU   99  CG2 ILE A 194    13324  12745   7567  -2323  -1135   1250       C  
ATOM    100  CD1 ILE A 194      16.045 -55.007  22.333  1.00 86.78           C  
ANISOU  100  CD1 ILE A 194    12944  12334   7696  -2454  -1075   1404       C  
ATOM    101  N   GLY A 195      20.980 -55.459  22.777  1.00 91.51           N  
ANISOU  101  N   GLY A 195    13918  12183   8668  -1874  -2010   1463       N  
ATOM    102  CA  GLY A 195      21.856 -56.520  22.307  1.00 91.88           C  
ANISOU  102  CA  GLY A 195    14074  11948   8888  -1782  -2250   1584       C  
ATOM    103  C   GLY A 195      21.306 -57.451  21.235  1.00 92.80           C  
ANISOU  103  C   GLY A 195    14184  11921   9155  -1827  -2201   1648       C  
ATOM    104  O   GLY A 195      21.668 -58.630  21.186  1.00 89.87           O  
ANISOU  104  O   GLY A 195    14014  11322   8810  -1844  -2382   1803       O  
ATOM    105  N   THR A 196      20.449 -56.928  20.365  1.00 83.76           N  
ANISOU  105  N   THR A 196    12819  10896   8108  -1841  -1972   1529       N  
ATOM    106  CA  THR A 196      19.889 -57.720  19.282  1.00 83.13           C  
ANISOU  106  CA  THR A 196    12720  10694   8170  -1892  -1924   1571       C  
ATOM    107  C   THR A 196      20.974 -58.188  18.320  1.00103.34           C  
ANISOU  107  C   THR A 196    15273  12984  11008  -1662  -2103   1554       C  
ATOM    108  O   THR A 196      21.878 -57.419  17.988  1.00101.16           O  
ANISOU  108  O   THR A 196    14836  12702  10896  -1437  -2146   1427       O  
ATOM    109  CB  THR A 196      18.839 -56.920  18.506  1.00 82.82           C  
ANISOU  109  CB  THR A 196    12418  10856   8196  -1922  -1657   1430       C  
ATOM    110  OG1 THR A 196      17.777 -56.547  19.389  1.00 82.65           O  
ANISOU  110  OG1 THR A 196    12390  11100   7912  -2125  -1476   1446       O  
ATOM    111  CG2 THR A 196      18.275 -57.733  17.348  1.00 80.77           C  
ANISOU  111  CG2 THR A 196    12141  10469   8079  -1984  -1626   1470       C  
ATOM    112  N   ASP A 197      20.892 -59.450  17.894  1.00 98.71           N  
ANISOU  112  N   ASP A 197    14867  12174  10465  -1721  -2205   1682       N  
ATOM    113  CA  ASP A 197      21.735 -59.954  16.810  1.00100.60           C  
ANISOU  113  CA  ASP A 197    15092  12163  10969  -1500  -2333   1649       C  
ATOM    114  C   ASP A 197      21.169 -59.499  15.464  1.00 98.20           C  
ANISOU  114  C   ASP A 197    14554  11913  10844  -1455  -2147   1505       C  
ATOM    115  O   ASP A 197      20.125 -59.985  15.036  1.00100.53           O  
ANISOU  115  O   ASP A 197    14884  12215  11097  -1639  -2045   1547       O  
ATOM    116  CB  ASP A 197      21.840 -61.480  16.866  1.00104.52           C  
ANISOU  116  CB  ASP A 197    15904  12376  11433  -1570  -2519   1831       C  
ATOM    117  CG  ASP A 197      22.796 -62.052  15.818  1.00106.99           C  
ANISOU  117  CG  ASP A 197    16227  12418  12006  -1306  -2660   1790       C  
ATOM    118  OD1 ASP A 197      23.518 -61.275  15.156  1.00 94.82           O  
ANISOU  118  OD1 ASP A 197    14445  10921  10661  -1066  -2630   1636       O  
ATOM    119  OD2 ASP A 197      22.834 -63.297  15.671  1.00118.77           O  
ANISOU  119  OD2 ASP A 197    17980  13648  13497  -1338  -2803   1914       O  
ATOM    120  N   PRO A 198      21.870 -58.562  14.794  1.00 93.37           N  
ANISOU  120  N   PRO A 198    13705  11344  10428  -1221  -2112   1343       N  
ATOM    121  CA  PRO A 198      21.490 -57.937  13.518  1.00 89.18           C  
ANISOU  121  CA  PRO A 198    12936  10876  10071  -1145  -1945   1194       C  
ATOM    122  C   PRO A 198      20.987 -58.940  12.494  1.00 92.57           C  
ANISOU  122  C   PRO A 198    13455  11135  10581  -1201  -1942   1233       C  
ATOM    123  O   PRO A 198      20.125 -58.632  11.672  1.00 94.10           O  
ANISOU  123  O   PRO A 198    13511  11422  10821  -1268  -1782   1161       O  
ATOM    124  CB  PRO A 198      22.798 -57.312  13.028  1.00 81.95           C  
ANISOU  124  CB  PRO A 198    11865   9910   9364   -861  -2019   1081       C  
ATOM    125  CG  PRO A 198      23.599 -57.098  14.242  1.00 82.17           C  
ANISOU  125  CG  PRO A 198    11963   9965   9290   -826  -2163   1130       C  
ATOM    126  CD  PRO A 198      23.220 -58.153  15.223  1.00 88.69           C  
ANISOU  126  CD  PRO A 198    13078  10715   9907  -1010  -2269   1311       C  
ATOM    127  N   ARG A 199      21.542 -60.144  12.557  1.00 90.66           N  
ANISOU  127  N   ARG A 199    13457  10635  10354  -1167  -2132   1348       N  
ATOM    128  CA  ARG A 199      21.275 -61.161  11.564  1.00 82.68           C  
ANISOU  128  CA  ARG A 199    12574   9410   9432  -1185  -2166   1374       C  
ATOM    129  C   ARG A 199      19.828 -61.603  11.600  1.00 80.63           C  
ANISOU  129  C   ARG A 199    12395   9218   9021  -1506  -2061   1455       C  
ATOM    130  O   ARG A 199      19.271 -61.985  10.573  1.00 81.10           O  
ANISOU  130  O   ARG A 199    12453   9206   9158  -1558  -2011   1423       O  
ATOM    131  CB  ARG A 199      22.201 -62.346  11.773  1.00 80.40           C  
ANISOU  131  CB  ARG A 199    12559   8817   9173  -1068  -2407   1483       C  
ATOM    132  CG  ARG A 199      23.654 -61.965  11.743  1.00 81.83           C  
ANISOU  132  CG  ARG A 199    12632   8949   9509   -749  -2519   1413       C  
ATOM    133  CD  ARG A 199      24.513 -63.186  11.635  1.00 87.71           C  
ANISOU  133  CD  ARG A 199    13620   9380  10326   -585  -2741   1495       C  
ATOM    134  NE  ARG A 199      25.889 -62.853  11.300  1.00 93.55           N  
ANISOU  134  NE  ARG A 199    14204  10085  11257   -250  -2825   1407       N  
ATOM    135  CZ  ARG A 199      26.373 -62.873  10.065  1.00 90.85           C  
ANISOU  135  CZ  ARG A 199    13745   9661  11115    -33  -2781   1285       C  
ATOM    136  NH1 ARG A 199      25.579 -63.214   9.053  1.00 82.77           N  
ANISOU  136  NH1 ARG A 199    12765   8565  10119   -116  -2669   1234       N  
ATOM    137  NH2 ARG A 199      27.647 -62.558   9.847  1.00 90.32           N  
ANISOU  137  NH2 ARG A 199    13514   9594  11211    260  -2852   1216       N  
ATOM    138  N   THR A 200      19.212 -61.536  12.775  1.00 79.70           N  
ANISOU  138  N   THR A 200    12343   9257   8682  -1728  -2026   1560       N  
ATOM    139  CA  THR A 200      17.816 -61.936  12.895  1.00 95.49           C  
ANISOU  139  CA  THR A 200    14392  11363  10526  -2055  -1916   1650       C  
ATOM    140  C   THR A 200      16.934 -60.878  12.255  1.00 93.37           C  
ANISOU  140  C   THR A 200    13805  11368  10305  -2083  -1682   1511       C  
ATOM    141  O   THR A 200      15.818 -61.159  11.813  1.00 98.81           O  
ANISOU  141  O   THR A 200    14458  12131  10953  -2295  -1584   1540       O  
ATOM    142  CB  THR A 200      17.394 -62.143  14.354  1.00 87.83           C  
ANISOU  142  CB  THR A 200    13571  10512   9287  -2290  -1923   1805       C  
ATOM    143  OG1 THR A 200      17.050 -60.883  14.932  1.00 82.07           O  
ANISOU  143  OG1 THR A 200    12606  10108   8468  -2289  -1746   1712       O  
ATOM    144  CG2 THR A 200      18.514 -62.800  15.154  1.00 87.81           C  
ANISOU  144  CG2 THR A 200    13836  10286   9242  -2186  -2163   1917       C  
ATOM    145  N   ILE A 201      17.448 -59.656  12.214  1.00 88.67           N  
ANISOU  145  N   ILE A 201    12980  10915   9794  -1870  -1606   1363       N  
ATOM    146  CA  ILE A 201      16.788 -58.570  11.505  1.00 90.10           C  
ANISOU  146  CA  ILE A 201    12865  11317  10052  -1834  -1408   1217       C  
ATOM    147  C   ILE A 201      17.074 -58.696  10.013  1.00 84.44           C  
ANISOU  147  C   ILE A 201    12079  10446   9559  -1681  -1426   1123       C  
ATOM    148  O   ILE A 201      16.180 -58.552   9.186  1.00 85.44           O  
ANISOU  148  O   ILE A 201    12079  10660   9725  -1765  -1313   1077       O  
ATOM    149  CB  ILE A 201      17.252 -57.191  12.027  1.00 89.20           C  
ANISOU  149  CB  ILE A 201    12564  11389   9939  -1669  -1331   1095       C  
ATOM    150  CG1 ILE A 201      16.906 -57.047  13.508  1.00 86.58           C  
ANISOU  150  CG1 ILE A 201    12314  11225   9359  -1825  -1301   1175       C  
ATOM    151  CG2 ILE A 201      16.606 -56.060  11.233  1.00 87.10           C  
ANISOU  151  CG2 ILE A 201    12011  11318   9765  -1607  -1142    943       C  
ATOM    152  CD1 ILE A 201      15.423 -57.038  13.778  1.00 85.60           C  
ANISOU  152  CD1 ILE A 201    12119  11336   9068  -2080  -1120   1220       C  
ATOM    153  N   LEU A 202      18.325 -58.989   9.680  1.00 81.06           N  
ANISOU  153  N   LEU A 202    11735   9795   9269  -1456  -1571   1097       N  
ATOM    154  CA  LEU A 202      18.732 -59.194   8.294  1.00 85.87           C  
ANISOU  154  CA  LEU A 202    12309  10243  10076  -1292  -1593   1008       C  
ATOM    155  C   LEU A 202      18.149 -60.466   7.668  1.00 94.79           C  
ANISOU  155  C   LEU A 202    13644  11179  11191  -1445  -1657   1088       C  
ATOM    156  O   LEU A 202      17.883 -60.502   6.466  1.00 96.42           O  
ANISOU  156  O   LEU A 202    13788  11341  11506  -1410  -1610   1008       O  
ATOM    157  CB  LEU A 202      20.253 -59.233   8.200  1.00 84.47           C  
ANISOU  157  CB  LEU A 202    12162   9898  10036  -1009  -1728    968       C  
ATOM    158  CG  LEU A 202      20.961 -57.889   8.291  1.00 79.92           C  
ANISOU  158  CG  LEU A 202    11342   9481   9544   -823  -1665    848       C  
ATOM    159  CD1 LEU A 202      22.459 -58.087   8.159  1.00 81.04           C  
ANISOU  159  CD1 LEU A 202    11506   9460   9826   -563  -1811    827       C  
ATOM    160  CD2 LEU A 202      20.446 -56.956   7.215  1.00 76.96           C  
ANISOU  160  CD2 LEU A 202    10730   9242   9269   -786  -1494    714       C  
ATOM    161  N   LYS A 203      17.953 -61.510   8.471  1.00 97.09           N  
ANISOU  161  N   LYS A 203    14200  11348  11344  -1625  -1772   1247       N  
ATOM    162  CA  LYS A 203      17.260 -62.699   7.985  1.00103.69           C  
ANISOU  162  CA  LYS A 203    15252  12005  12140  -1826  -1835   1335       C  
ATOM    163  C   LYS A 203      15.871 -62.333   7.472  1.00113.14           C  
ANISOU  163  C   LYS A 203    16273  13422  13295  -2053  -1670   1310       C  
ATOM    164  O   LYS A 203      15.297 -63.046   6.650  1.00123.94           O  
ANISOU  164  O   LYS A 203    17737  14671  14683  -2183  -1698   1326       O  
ATOM    165  CB  LYS A 203      17.153 -63.768   9.074  1.00108.37           C  
ANISOU  165  CB  LYS A 203    16155  12460  12560  -2029  -1975   1531       C  
ATOM    166  CG  LYS A 203      18.351 -64.708   9.143  1.00120.43           C  
ANISOU  166  CG  LYS A 203    17962  13642  14154  -1833  -2199   1580       C  
ATOM    167  CD  LYS A 203      18.052 -65.950   9.983  1.00129.99           C  
ANISOU  167  CD  LYS A 203    19534  14663  15194  -2074  -2353   1788       C  
ATOM    168  CE  LYS A 203      17.125 -66.932   9.256  1.00132.39           C  
ANISOU  168  CE  LYS A 203    20024  14806  15472  -2322  -2377   1845       C  
ATOM    169  NZ  LYS A 203      17.723 -67.464   7.997  1.00131.77           N  
ANISOU  169  NZ  LYS A 203    20049  14442  15575  -2096  -2465   1737       N  
ATOM    170  N   ASP A 204      15.345 -61.210   7.953  1.00108.81           N  
ANISOU  170  N   ASP A 204    15465  13191  12685  -2090  -1505   1265       N  
ATOM    171  CA  ASP A 204      14.034 -60.726   7.543  1.00104.04           C  
ANISOU  171  CA  ASP A 204    14647  12839  12046  -2271  -1340   1236       C  
ATOM    172  C   ASP A 204      14.121 -59.737   6.388  1.00 98.63           C  
ANISOU  172  C   ASP A 204    13705  12237  11532  -2063  -1241   1061       C  
ATOM    173  O   ASP A 204      13.274 -59.749   5.500  1.00105.71           O  
ANISOU  173  O   ASP A 204    14504  13199  12463  -2164  -1182   1031       O  
ATOM    174  CB  ASP A 204      13.310 -60.077   8.723  1.00114.67           C  
ANISOU  174  CB  ASP A 204    15859  14495  13216  -2423  -1204   1283       C  
ATOM    175  CG  ASP A 204      12.407 -61.047   9.466  1.00131.39           C  
ANISOU  175  CG  ASP A 204    18144  16643  15136  -2777  -1223   1468       C  
ATOM    176  OD1 ASP A 204      12.584 -62.278   9.317  1.00134.74           O  
ANISOU  176  OD1 ASP A 204    18851  16793  15549  -2890  -1383   1577       O  
ATOM    177  OD2 ASP A 204      11.516 -60.570  10.202  1.00137.26           O  
ANISOU  177  OD2 ASP A 204    18739  17684  15731  -2944  -1074   1503       O  
ATOM    178  N   LEU A 205      15.141 -58.884   6.400  1.00 93.19           N  
ANISOU  178  N   LEU A 205    12913  11550  10945  -1785  -1233    954       N  
ATOM    179  CA  LEU A 205      15.278 -57.836   5.389  1.00 85.15           C  
ANISOU  179  CA  LEU A 205    11657  10620  10077  -1592  -1135    798       C  
ATOM    180  C   LEU A 205      15.950 -58.358   4.128  1.00 88.81           C  
ANISOU  180  C   LEU A 205    12209  10841  10694  -1440  -1221    738       C  
ATOM    181  O   LEU A 205      15.720 -57.844   3.028  1.00 91.51           O  
ANISOU  181  O   LEU A 205    12405  11232  11134  -1367  -1148    638       O  
ATOM    182  CB  LEU A 205      16.070 -56.653   5.942  1.00 76.50           C  
ANISOU  182  CB  LEU A 205    10416   9634   9018  -1386  -1088    712       C  
ATOM    183  CG  LEU A 205      15.400 -55.840   7.048  1.00 78.61           C  
ANISOU  183  CG  LEU A 205    10560  10169   9141  -1485   -971    721       C  
ATOM    184  CD1 LEU A 205      16.294 -54.686   7.456  1.00 85.20           C  
ANISOU  184  CD1 LEU A 205    11283  11063  10025  -1272   -950    621       C  
ATOM    185  CD2 LEU A 205      14.039 -55.328   6.611  1.00 75.50           C  
ANISOU  185  CD2 LEU A 205     9965  10005   8717  -1608   -814    688       C  
ATOM    186  N   LEU A 206      16.793 -59.372   4.303  1.00 85.85           N  
ANISOU  186  N   LEU A 206    12081  10205  10331  -1381  -1375    798       N  
ATOM    187  CA  LEU A 206      17.438 -60.045   3.187  1.00 84.90           C  
ANISOU  187  CA  LEU A 206    12088   9836  10335  -1233  -1461    745       C  
ATOM    188  C   LEU A 206      17.188 -61.528   3.281  1.00101.30           C  
ANISOU  188  C   LEU A 206    14484  11670  12336  -1397  -1602    861       C  
ATOM    189  O   LEU A 206      18.079 -62.282   3.667  1.00107.72           O  
ANISOU  189  O   LEU A 206    15509  12260  13161  -1287  -1743    912       O  
ATOM    190  CB  LEU A 206      18.940 -59.780   3.172  1.00 77.32           C  
ANISOU  190  CB  LEU A 206    11110   8770   9498   -924  -1519    679       C  
ATOM    191  CG  LEU A 206      19.404 -58.327   3.158  1.00 77.04           C  
ANISOU  191  CG  LEU A 206    10790   8938   9542   -759  -1407    572       C  
ATOM    192  CD1 LEU A 206      20.925 -58.262   3.085  1.00 74.12           C  
ANISOU  192  CD1 LEU A 206    10415   8451   9299   -480  -1486    524       C  
ATOM    193  CD2 LEU A 206      18.774 -57.595   1.991  1.00 74.67           C  
ANISOU  193  CD2 LEU A 206    10304   8760   9308   -756  -1273    467       C  
ATOM    194  N   PRO A 207      15.965 -61.962   2.955  1.00104.90           N  
ANISOU  194  N   PRO A 207    14980  12166  12713  -1667  -1576    911       N  
ATOM    195  CA  PRO A 207      15.785 -63.409   2.909  1.00107.60           C  
ANISOU  195  CA  PRO A 207    15657  12234  12992  -1827  -1728   1015       C  
ATOM    196  C   PRO A 207      16.476 -63.873   1.650  1.00116.36           C  
ANISOU  196  C   PRO A 207    16886  13093  14232  -1615  -1795    906       C  
ATOM    197  O   PRO A 207      16.691 -63.038   0.767  1.00126.61           O  
ANISOU  197  O   PRO A 207    17972  14497  15638  -1440  -1694    769       O  
ATOM    198  CB  PRO A 207      14.265 -63.590   2.835  1.00103.00           C  
ANISOU  198  CB  PRO A 207    15032  11807  12297  -2185  -1668   1088       C  
ATOM    199  CG  PRO A 207      13.678 -62.182   2.908  1.00101.29           C  
ANISOU  199  CG  PRO A 207    14436  11962  12086  -2176  -1477   1017       C  
ATOM    200  CD  PRO A 207      14.765 -61.245   2.501  1.00 98.00           C  
ANISOU  200  CD  PRO A 207    13866  11554  11814  -1824  -1431    873       C  
ATOM    201  N   GLU A 208      16.840 -65.146   1.569  1.00112.56           N  
ANISOU  201  N   GLU A 208    16745  12286  13738  -1617  -1959    962       N  
ATOM    202  CA  GLU A 208      17.543 -65.662   0.395  1.00113.56           C  
ANISOU  202  CA  GLU A 208    17015  12158  13975  -1391  -2021    847       C  
ATOM    203  C   GLU A 208      18.842 -64.878   0.187  1.00 96.65           C  
ANISOU  203  C   GLU A 208    14687  10060  11976  -1009  -1968    727       C  
ATOM    204  O   GLU A 208      19.288 -64.640  -0.941  1.00 95.26           O  
ANISOU  204  O   GLU A 208    14442   9849  11902   -808  -1916    590       O  
ATOM    205  CB  GLU A 208      16.647 -65.606  -0.854  1.00119.56           C  
ANISOU  205  CB  GLU A 208    17725  12963  14741  -1522  -1957    765       C  
ATOM    206  CG  GLU A 208      15.314 -66.358  -0.688  1.00128.89           C  
ANISOU  206  CG  GLU A 208    19060  14127  15786  -1931  -2014    889       C  
ATOM    207  CD  GLU A 208      15.466 -67.736  -0.021  1.00133.94           C  
ANISOU  207  CD  GLU A 208    20102  14448  16341  -2055  -2202   1026       C  
ATOM    208  OE1 GLU A 208      16.184 -68.598  -0.573  1.00133.53           O  
ANISOU  208  OE1 GLU A 208    20333  14062  16339  -1883  -2327    976       O  
ATOM    209  OE2 GLU A 208      14.874 -67.953   1.063  1.00133.01           O  
ANISOU  209  OE2 GLU A 208    20025  14413  16101  -2318  -2224   1184       O  
ATOM    210  N   THR A 209      19.430 -64.466   1.304  1.00 80.53           N  
ANISOU  210  N   THR A 209    12562   8110   9927   -929  -1981    786       N  
ATOM    211  CA  THR A 209      20.732 -63.813   1.313  1.00 77.14           C  
ANISOU  211  CA  THR A 209    11969   7717   9624   -596  -1963    701       C  
ATOM    212  C   THR A 209      21.359 -64.013   2.691  1.00 82.50           C  
ANISOU  212  C   THR A 209    12728   8364  10256   -561  -2078    817       C  
ATOM    213  O   THR A 209      20.782 -63.620   3.713  1.00 79.83           O  
ANISOU  213  O   THR A 209    12329   8200   9802   -759  -2049    908       O  
ATOM    214  CB  THR A 209      20.666 -62.289   1.014  1.00 96.54           C  
ANISOU  214  CB  THR A 209    14052  10486  12143   -535  -1782    597       C  
ATOM    215  OG1 THR A 209      19.586 -61.970   0.118  1.00 97.60           O  
ANISOU  215  OG1 THR A 209    14094  10731  12257   -695  -1672    544       O  
ATOM    216  CG2 THR A 209      21.985 -61.831   0.427  1.00 93.54           C  
ANISOU  216  CG2 THR A 209    13538  10084  11918   -196  -1761    481       C  
ATOM    217  N   ILE A 210      22.533 -64.630   2.729  1.00 92.31           N  
ANISOU  217  N   ILE A 210    14107   9389  11578   -302  -2209    814       N  
ATOM    218  CA  ILE A 210      23.215 -64.824   4.001  1.00 95.06           C  
ANISOU  218  CA  ILE A 210    14531   9702  11886   -245  -2342    926       C  
ATOM    219  C   ILE A 210      24.556 -64.112   4.007  1.00 92.33           C  
ANISOU  219  C   ILE A 210    13958   9439  11682     79  -2339    842       C  
ATOM    220  O   ILE A 210      25.495 -64.517   3.309  1.00 95.05           O  
ANISOU  220  O   ILE A 210    14332   9628  12156    358  -2389    768       O  
ATOM    221  CB  ILE A 210      23.415 -66.314   4.335  1.00103.43           C  
ANISOU  221  CB  ILE A 210    15989  10417  12895   -248  -2551   1042       C  
ATOM    222  CG1 ILE A 210      22.053 -66.984   4.528  1.00106.00           C  
ANISOU  222  CG1 ILE A 210    16537  10681  13057   -631  -2564   1155       C  
ATOM    223  CG2 ILE A 210      24.249 -66.465   5.600  1.00102.22           C  
ANISOU  223  CG2 ILE A 210    15901  10229  12711   -149  -2704   1156       C  
ATOM    224  CD1 ILE A 210      22.127 -68.357   5.129  1.00111.53           C  
ANISOU  224  CD1 ILE A 210    17647  11059  13670   -704  -2778   1307       C  
ATOM    225  N   PRO A 211      24.640 -63.035   4.803  1.00 80.69           N  
ANISOU  225  N   PRO A 211    12255   8221  10181     38  -2280    852       N  
ATOM    226  CA  PRO A 211      25.809 -62.156   4.922  1.00 77.70           C  
ANISOU  226  CA  PRO A 211    11624   7974   9924    283  -2271    781       C  
ATOM    227  C   PRO A 211      27.015 -62.890   5.470  1.00 83.98           C  
ANISOU  227  C   PRO A 211    12545   8594  10772    509  -2471    846       C  
ATOM    228  O   PRO A 211      26.878 -63.633   6.444  1.00 91.55           O  
ANISOU  228  O   PRO A 211    13740   9431  11614    406  -2621    986       O  
ATOM    229  CB  PRO A 211      25.342 -61.067   5.894  1.00 76.06           C  
ANISOU  229  CB  PRO A 211    11250   8035   9615    105  -2196    810       C  
ATOM    230  CG  PRO A 211      24.145 -61.632   6.582  1.00 79.92           C  
ANISOU  230  CG  PRO A 211    11947   8504   9914   -200  -2211    932       C  
ATOM    231  CD  PRO A 211      23.508 -62.574   5.625  1.00 77.81           C  
ANISOU  231  CD  PRO A 211    11863   8049   9654   -273  -2206    928       C  
ATOM    232  N   PRO A 212      28.187 -62.680   4.852  1.00 83.16           N  
ANISOU  232  N   PRO A 212    12275   8484  10837    813  -2475    751       N  
ATOM    233  CA  PRO A 212      29.427 -63.397   5.174  1.00 86.02           C  
ANISOU  233  CA  PRO A 212    12716   8684  11282   1087  -2662    794       C  
ATOM    234  C   PRO A 212      29.715 -63.405   6.675  1.00 95.92           C  
ANISOU  234  C   PRO A 212    14033   9973  12441   1021  -2829    934       C  
ATOM    235  O   PRO A 212      29.272 -62.506   7.386  1.00 96.75           O  
ANISOU  235  O   PRO A 212    14017  10293  12452    827  -2768    956       O  
ATOM    236  CB  PRO A 212      30.493 -62.609   4.411  1.00 84.51           C  
ANISOU  236  CB  PRO A 212    12199   8639  11274   1352  -2572    661       C  
ATOM    237  CG  PRO A 212      29.753 -61.967   3.290  1.00 86.64           C  
ANISOU  237  CG  PRO A 212    12342   9018  11561   1252  -2352    542       C  
ATOM    238  CD  PRO A 212      28.388 -61.657   3.813  1.00 79.22           C  
ANISOU  238  CD  PRO A 212    11478   8163  10458    909  -2291    601       C  
ATOM    239  N   PRO A 213      30.441 -64.418   7.160  1.00105.84           N  
ANISOU  239  N   PRO A 213    15492  11012  13710   1188  -3045   1028       N  
ATOM    240  CA  PRO A 213      30.690 -64.578   8.598  1.00112.88           C  
ANISOU  240  CA  PRO A 213    16497  11905  14488   1119  -3233   1181       C  
ATOM    241  C   PRO A 213      31.563 -63.482   9.207  1.00116.89           C  
ANISOU  241  C   PRO A 213    16698  12666  15049   1207  -3255   1158       C  
ATOM    242  O   PRO A 213      31.311 -63.045  10.331  1.00117.20           O  
ANISOU  242  O   PRO A 213    16755  12830  14946   1023  -3306   1242       O  
ATOM    243  CB  PRO A 213      31.409 -65.924   8.672  1.00114.44           C  
ANISOU  243  CB  PRO A 213    16961  11788  14732   1351  -3459   1261       C  
ATOM    244  CG  PRO A 213      32.072 -66.061   7.339  1.00113.84           C  
ANISOU  244  CG  PRO A 213    16753  11646  14853   1654  -3379   1109       C  
ATOM    245  CD  PRO A 213      31.106 -65.466   6.366  1.00108.84           C  
ANISOU  245  CD  PRO A 213    16015  11130  14210   1473  -3129    990       C  
ATOM    246  N   GLU A 214      32.571 -63.044   8.461  1.00122.42           N  
ANISOU  246  N   GLU A 214    17125  13444  15943   1475  -3214   1043       N  
ATOM    247  CA  GLU A 214      33.593 -62.143   8.982  1.00126.08           C  
ANISOU  247  CA  GLU A 214    17301  14120  16483   1585  -3273   1028       C  
ATOM    248  C   GLU A 214      33.159 -60.671   9.005  1.00118.52           C  
ANISOU  248  C   GLU A 214    16091  13446  15495   1390  -3090    945       C  
ATOM    249  O   GLU A 214      33.983 -59.776   9.201  1.00118.54           O  
ANISOU  249  O   GLU A 214    15826  13633  15580   1466  -3106    903       O  
ATOM    250  CB  GLU A 214      34.882 -62.293   8.165  1.00137.76           C  
ANISOU  250  CB  GLU A 214    18572  15583  18185   1946  -3299    948       C  
ATOM    251  CG  GLU A 214      34.857 -61.637   6.781  1.00142.83           C  
ANISOU  251  CG  GLU A 214    18972  16339  18956   2009  -3054    783       C  
ATOM    252  CD  GLU A 214      33.942 -62.340   5.786  1.00149.56           C  
ANISOU  252  CD  GLU A 214    20041  17008  19778   1964  -2930    729       C  
ATOM    253  OE1 GLU A 214      33.705 -63.560   5.940  1.00151.25           O  
ANISOU  253  OE1 GLU A 214    20576  16957  19935   1997  -3057    804       O  
ATOM    254  OE2 GLU A 214      33.463 -61.661   4.846  1.00151.08           O  
ANISOU  254  OE2 GLU A 214    20091  17313  20000   1888  -2717    616       O  
ATOM    255  N   LEU A 215      31.867 -60.422   8.815  1.00109.41           N  
ANISOU  255  N   LEU A 215    15022  12324  14223   1139  -2927    922       N  
ATOM    256  CA  LEU A 215      31.343 -59.065   8.878  1.00 95.48           C  
ANISOU  256  CA  LEU A 215    13055  10807  12417    961  -2759    845       C  
ATOM    257  C   LEU A 215      31.180 -58.592  10.313  1.00107.12           C  
ANISOU  257  C   LEU A 215    14579  12399  13723    786  -2850    927       C  
ATOM    258  O   LEU A 215      30.546 -59.256  11.137  1.00108.43           O  
ANISOU  258  O   LEU A 215    15002  12480  13714    630  -2929   1044       O  
ATOM    259  CB  LEU A 215      30.004 -58.957   8.150  1.00 81.27           C  
ANISOU  259  CB  LEU A 215    11310   9016  10555    774  -2556    790       C  
ATOM    260  CG  LEU A 215      30.032 -58.837   6.625  1.00 79.68           C  
ANISOU  260  CG  LEU A 215    10975   8797  10504    898  -2400    663       C  
ATOM    261  CD1 LEU A 215      28.707 -58.311   6.106  1.00 70.97           C  
ANISOU  261  CD1 LEU A 215     9854   7785   9326    682  -2203    606       C  
ATOM    262  CD2 LEU A 215      31.167 -57.947   6.179  1.00 81.77           C  
ANISOU  262  CD2 LEU A 215    10932   9201  10935   1090  -2366    571       C  
ATOM    263  N   ASP A 216      31.770 -57.432  10.586  1.00113.46           N  
ANISOU  263  N   ASP A 216    15140  13397  14571    806  -2837    865       N  
ATOM    264  CA  ASP A 216      31.661 -56.749  11.867  1.00111.43           C  
ANISOU  264  CA  ASP A 216    14903  13279  14155    645  -2903    907       C  
ATOM    265  C   ASP A 216      30.191 -56.513  12.209  1.00109.27           C  
ANISOU  265  C   ASP A 216    14764  13069  13685    377  -2751    911       C  
ATOM    266  O   ASP A 216      29.379 -56.237  11.331  1.00109.25           O  
ANISOU  266  O   ASP A 216    14700  13096  13713    317  -2555    830       O  
ATOM    267  CB  ASP A 216      32.438 -55.432  11.810  1.00113.53           C  
ANISOU  267  CB  ASP A 216    14876  13735  14525    698  -2878    806       C  
ATOM    268  CG  ASP A 216      32.600 -54.788  13.163  1.00120.26           C  
ANISOU  268  CG  ASP A 216    15758  14709  15224    572  -2994    844       C  
ATOM    269  OD1 ASP A 216      33.420 -55.290  13.969  1.00124.64           O  
ANISOU  269  OD1 ASP A 216    16383  15219  15757    646  -3225    943       O  
ATOM    270  OD2 ASP A 216      31.921 -53.766  13.402  1.00117.39           O  
ANISOU  270  OD2 ASP A 216    15354  14485  14764    409  -2860    770       O  
ATOM    271  N   ASP A 217      29.843 -56.637  13.482  1.00 99.37           N  
ANISOU  271  N   ASP A 217    13690  11847  12222    219  -2841   1008       N  
ATOM    272  CA  ASP A 217      28.442 -56.558  13.886  1.00 90.61           C  
ANISOU  272  CA  ASP A 217    12712  10807  10908    -34  -2697   1029       C  
ATOM    273  C   ASP A 217      27.879 -55.144  13.762  1.00 84.11           C  
ANISOU  273  C   ASP A 217    11694  10200  10063   -122  -2497    892       C  
ATOM    274  O   ASP A 217      26.678 -54.957  13.563  1.00 74.32           O  
ANISOU  274  O   ASP A 217    10470   9034   8734   -274  -2317    863       O  
ATOM    275  CB  ASP A 217      28.270 -57.066  15.315  1.00 91.97           C  
ANISOU  275  CB  ASP A 217    13134  10969  10843   -179  -2841   1175       C  
ATOM    276  CG  ASP A 217      27.517 -58.368  15.369  1.00111.97           C  
ANISOU  276  CG  ASP A 217    15939  13336  13269   -300  -2867   1309       C  
ATOM    277  OD1 ASP A 217      26.336 -58.370  14.975  1.00112.96           O  
ANISOU  277  OD1 ASP A 217    16080  13509  13331   -466  -2682   1288       O  
ATOM    278  OD2 ASP A 217      28.101 -59.387  15.793  1.00125.79           O  
ANISOU  278  OD2 ASP A 217    17888  14905  15002   -233  -3080   1440       O  
ATOM    279  N   MET A 218      28.743 -54.146  13.881  1.00 79.58           N  
ANISOU  279  N   MET A 218    10938   9728   9573    -27  -2537    809       N  
ATOM    280  CA  MET A 218      28.308 -52.781  13.662  1.00 75.67           C  
ANISOU  280  CA  MET A 218    10270   9402   9080    -84  -2362    672       C  
ATOM    281  C   MET A 218      28.088 -52.574  12.162  1.00 78.63           C  
ANISOU  281  C   MET A 218    10478   9754   9644      2  -2200    577       C  
ATOM    282  O   MET A 218      27.162 -51.875  11.749  1.00 72.48           O  
ANISOU  282  O   MET A 218     9628   9070   8841    -80  -2012    494       O  
ATOM    283  CB  MET A 218      29.330 -51.788  14.219  1.00 71.98           C  
ANISOU  283  CB  MET A 218     9678   9027   8643    -29  -2470    617       C  
ATOM    284  CG  MET A 218      28.821 -50.361  14.284  1.00 70.66           C  
ANISOU  284  CG  MET A 218     9404   9016   8428   -113  -2316    483       C  
ATOM    285  SD  MET A 218      27.310 -50.220  15.271  1.00 77.22           S  
ANISOU  285  SD  MET A 218    10422   9958   8960   -327  -2180    492       S  
ATOM    286  CE  MET A 218      27.961 -50.213  16.942  1.00 93.71           C  
ANISOU  286  CE  MET A 218    12681  12086  10840   -395  -2398    564       C  
ATOM    287  N   THR A 219      28.941 -53.200  11.351  1.00 83.39           N  
ANISOU  287  N   THR A 219    11022  10232  10429    177  -2274    591       N  
ATOM    288  CA  THR A 219      28.801 -53.156   9.897  1.00 80.25           C  
ANISOU  288  CA  THR A 219    10496   9799  10197    266  -2133    510       C  
ATOM    289  C   THR A 219      27.443 -53.709   9.481  1.00 82.14           C  
ANISOU  289  C   THR A 219    10863   9997  10349    135  -2001    527       C  
ATOM    290  O   THR A 219      26.761 -53.135   8.631  1.00 79.55           O  
ANISOU  290  O   THR A 219    10428   9735  10063    102  -1830    441       O  
ATOM    291  CB  THR A 219      29.907 -53.954   9.185  1.00 72.64           C  
ANISOU  291  CB  THR A 219     9489   8699   9412    485  -2238    530       C  
ATOM    292  OG1 THR A 219      31.189 -53.496   9.619  1.00 74.41           O  
ANISOU  292  OG1 THR A 219     9571   8982   9719    599  -2374    529       O  
ATOM    293  CG2 THR A 219      29.806 -53.785   7.684  1.00 71.28           C  
ANISOU  293  CG2 THR A 219     9181   8512   9391    574  -2079    434       C  
ATOM    294  N   LEU A 220      27.055 -54.824  10.093  1.00 79.08           N  
ANISOU  294  N   LEU A 220    10708   9503   9836     49  -2092    647       N  
ATOM    295  CA  LEU A 220      25.751 -55.428   9.840  1.00 78.60           C  
ANISOU  295  CA  LEU A 220    10782   9411   9674   -117  -1990    686       C  
ATOM    296  C   LEU A 220      24.602 -54.456  10.116  1.00 81.16           C  
ANISOU  296  C   LEU A 220    11024   9938   9875   -290  -1813    630       C  
ATOM    297  O   LEU A 220      23.627 -54.378   9.364  1.00 67.09           O  
ANISOU  297  O   LEU A 220     9195   8196   8100   -367  -1665    589       O  
ATOM    298  CB  LEU A 220      25.580 -56.684  10.690  1.00 78.27           C  
ANISOU  298  CB  LEU A 220    11018   9232   9489   -216  -2135    842       C  
ATOM    299  CG  LEU A 220      26.452 -57.880  10.331  1.00 80.96           C  
ANISOU  299  CG  LEU A 220    11495   9329   9936    -48  -2307    908       C  
ATOM    300  CD1 LEU A 220      26.114 -59.025  11.255  1.00 84.41           C  
ANISOU  300  CD1 LEU A 220    12236   9631  10204   -184  -2446   1074       C  
ATOM    301  CD2 LEU A 220      26.222 -58.271   8.889  1.00 71.85           C  
ANISOU  301  CD2 LEU A 220    10310   8067   8921     29  -2214    837       C  
ATOM    302  N   TRP A 221      24.721 -53.717  11.208  1.00 78.97           N  
ANISOU  302  N   TRP A 221    10732   9791   9481   -342  -1834    625       N  
ATOM    303  CA  TRP A 221      23.713 -52.731  11.555  1.00 76.11           C  
ANISOU  303  CA  TRP A 221    10295   9625   8999   -470  -1667    557       C  
ATOM    304  C   TRP A 221      23.665 -51.606  10.542  1.00 71.23           C  
ANISOU  304  C   TRP A 221     9451   9083   8529   -376  -1529    412       C  
ATOM    305  O   TRP A 221      22.598 -51.084  10.228  1.00 71.39           O  
ANISOU  305  O   TRP A 221     9397   9218   8509   -453  -1364    356       O  
ATOM    306  CB  TRP A 221      23.980 -52.158  12.941  1.00 73.43           C  
ANISOU  306  CB  TRP A 221    10010   9392   8497   -522  -1731    566       C  
ATOM    307  CG  TRP A 221      23.486 -53.015  14.030  1.00 77.43           C  
ANISOU  307  CG  TRP A 221    10741   9897   8783   -686  -1791    702       C  
ATOM    308  CD1 TRP A 221      24.222 -53.568  15.027  1.00 72.64           C  
ANISOU  308  CD1 TRP A 221    10300   9220   8081   -691  -1984    807       C  
ATOM    309  CD2 TRP A 221      22.134 -53.433  14.240  1.00 75.32           C  
ANISOU  309  CD2 TRP A 221    10555   9710   8352   -883  -1659    759       C  
ATOM    310  NE1 TRP A 221      23.414 -54.293  15.858  1.00 74.30           N  
ANISOU  310  NE1 TRP A 221    10711   9453   8068   -884  -1979    929       N  
ATOM    311  CE2 TRP A 221      22.127 -54.234  15.396  1.00 73.62           C  
ANISOU  311  CE2 TRP A 221    10569   9465   7937  -1013  -1775    903       C  
ATOM    312  CE3 TRP A 221      20.928 -53.212  13.573  1.00 70.47           C  
ANISOU  312  CE3 TRP A 221     9836   9201   7739   -970  -1462    710       C  
ATOM    313  CZ2 TRP A 221      20.968 -54.816  15.894  1.00 74.93           C  
ANISOU  313  CZ2 TRP A 221    10860   9706   7903  -1239  -1687   1002       C  
ATOM    314  CZ3 TRP A 221      19.772 -53.786  14.076  1.00 71.80           C  
ANISOU  314  CZ3 TRP A 221    10106   9457   7717  -1188  -1379    803       C  
ATOM    315  CH2 TRP A 221      19.804 -54.581  15.223  1.00 74.01           C  
ANISOU  315  CH2 TRP A 221    10614   9709   7798  -1327  -1485    949       C  
ATOM    316  N   GLN A 222      24.833 -51.214  10.054  1.00 66.47           N  
ANISOU  316  N   GLN A 222     8734   8426   8097   -211  -1600    359       N  
ATOM    317  CA  GLN A 222      24.884 -50.136   9.095  1.00 74.07           C  
ANISOU  317  CA  GLN A 222     9498   9449   9196   -131  -1482    235       C  
ATOM    318  C   GLN A 222      24.098 -50.555   7.849  1.00 77.96           C  
ANISOU  318  C   GLN A 222     9961   9901   9760   -137  -1362    220       C  
ATOM    319  O   GLN A 222      23.295 -49.774   7.318  1.00 74.09           O  
ANISOU  319  O   GLN A 222     9367   9508   9276   -168  -1215    144       O  
ATOM    320  CB  GLN A 222      26.331 -49.771   8.772  1.00 76.19           C  
ANISOU  320  CB  GLN A 222     9647   9671   9632     26  -1584    201       C  
ATOM    321  CG  GLN A 222      26.944 -48.847   9.805  1.00 73.72           C  
ANISOU  321  CG  GLN A 222     9306   9444   9262     10  -1665    171       C  
ATOM    322  CD  GLN A 222      28.438 -48.692   9.656  1.00 81.21           C  
ANISOU  322  CD  GLN A 222    10139  10355  10363    140  -1803    169       C  
ATOM    323  OE1 GLN A 222      29.064 -49.289   8.774  1.00 84.52           O  
ANISOU  323  OE1 GLN A 222    10489  10692  10934    264  -1826    187       O  
ATOM    324  NE2 GLN A 222      29.025 -47.884  10.526  1.00 84.17           N  
ANISOU  324  NE2 GLN A 222    10488  10800  10693    111  -1894    144       N  
ATOM    325  N   ILE A 223      24.305 -51.801   7.425  1.00 75.02           N  
ANISOU  325  N   ILE A 223     9696   9380   9430   -107  -1437    293       N  
ATOM    326  CA  ILE A 223      23.522 -52.404   6.361  1.00 62.62           C  
ANISOU  326  CA  ILE A 223     8149   7749   7893   -141  -1353    293       C  
ATOM    327  C   ILE A 223      22.033 -52.344   6.654  1.00 69.72           C  
ANISOU  327  C   ILE A 223     9081   8766   8646   -334  -1240    312       C  
ATOM    328  O   ILE A 223      21.231 -52.095   5.763  1.00 71.16           O  
ANISOU  328  O   ILE A 223     9179   8997   8861   -366  -1122    263       O  
ATOM    329  CB  ILE A 223      23.902 -53.865   6.154  1.00 66.90           C  
ANISOU  329  CB  ILE A 223     8869   8092   8459   -104  -1476    379       C  
ATOM    330  CG1 ILE A 223      25.372 -53.984   5.769  1.00 68.60           C  
ANISOU  330  CG1 ILE A 223     9026   8206   8832    118  -1577    355       C  
ATOM    331  CG2 ILE A 223      23.001 -54.525   5.118  1.00 63.59           C  
ANISOU  331  CG2 ILE A 223     8508   7604   8050   -173  -1402    377       C  
ATOM    332  CD1 ILE A 223      25.791 -55.402   5.501  1.00 65.55           C  
ANISOU  332  CD1 ILE A 223     8818   7607   8480    199  -1697    423       C  
ATOM    333  N   VAL A 224      21.660 -52.603   7.901  1.00 70.53           N  
ANISOU  333  N   VAL A 224     9300   8923   8577   -465  -1277    390       N  
ATOM    334  CA  VAL A 224      20.254 -52.573   8.275  1.00 74.99           C  
ANISOU  334  CA  VAL A 224     9876   9629   8987   -656  -1159    417       C  
ATOM    335  C   VAL A 224      19.684 -51.188   8.029  1.00 73.26           C  
ANISOU  335  C   VAL A 224     9459   9593   8784   -628  -1002    296       C  
ATOM    336  O   VAL A 224      18.641 -51.045   7.391  1.00 69.59           O  
ANISOU  336  O   VAL A 224     8909   9215   8320   -692   -882    271       O  
ATOM    337  CB  VAL A 224      20.042 -52.966   9.749  1.00 78.02           C  
ANISOU  337  CB  VAL A 224    10414  10064   9164   -799  -1214    518       C  
ATOM    338  CG1 VAL A 224      18.643 -52.565  10.213  1.00 73.91           C  
ANISOU  338  CG1 VAL A 224     9840   9761   8482   -970  -1051    515       C  
ATOM    339  CG2 VAL A 224      20.278 -54.451   9.931  1.00 79.98           C  
ANISOU  339  CG2 VAL A 224    10890  10124   9376   -866  -1360    659       C  
ATOM    340  N   ILE A 225      20.396 -50.175   8.514  1.00 77.66           N  
ANISOU  340  N   ILE A 225     9949  10199   9358   -528  -1017    223       N  
ATOM    341  CA  ILE A 225      19.981 -48.788   8.340  1.00 77.68           C  
ANISOU  341  CA  ILE A 225     9794  10342   9378   -479   -888    103       C  
ATOM    342  C   ILE A 225      19.848 -48.454   6.862  1.00 73.94           C  
ANISOU  342  C   ILE A 225     9186   9835   9072   -392   -818     37       C  
ATOM    343  O   ILE A 225      18.847 -47.877   6.449  1.00 73.65           O  
ANISOU  343  O   ILE A 225     9048   9913   9024   -416   -690    -14       O  
ATOM    344  CB  ILE A 225      20.965 -47.805   9.017  1.00 80.59           C  
ANISOU  344  CB  ILE A 225    10142  10722   9755   -388   -951     35       C  
ATOM    345  CG1 ILE A 225      21.021 -48.066  10.532  1.00 79.44           C  
ANISOU  345  CG1 ILE A 225    10143  10626   9413   -482  -1020     95       C  
ATOM    346  CG2 ILE A 225      20.531 -46.372   8.775  1.00 60.85           C  
ANISOU  346  CG2 ILE A 225     7511   8332   7279   -332   -826    -93       C  
ATOM    347  CD1 ILE A 225      22.174 -47.411  11.257  1.00 63.77           C  
ANISOU  347  CD1 ILE A 225     8180   8620   7431   -412  -1141     56       C  
ATOM    348  N   ASN A 226      20.840 -48.856   6.069  1.00 73.85           N  
ANISOU  348  N   ASN A 226     9175   9675   9209   -288   -901     43       N  
ATOM    349  CA  ASN A 226      20.840 -48.618   4.622  1.00 70.40           C  
ANISOU  349  CA  ASN A 226     8633   9197   8921   -205   -842    -13       C  
ATOM    350  C   ASN A 226      19.609 -49.172   3.910  1.00 75.70           C  
ANISOU  350  C   ASN A 226     9307   9896   9560   -303   -764     12       C  
ATOM    351  O   ASN A 226      18.999 -48.485   3.092  1.00 83.13           O  
ANISOU  351  O   ASN A 226    10130  10907  10548   -281   -666    -50       O  
ATOM    352  CB  ASN A 226      22.097 -49.215   3.986  1.00 58.29           C  
ANISOU  352  CB  ASN A 226     7121   7505   7521    -83   -941      2       C  
ATOM    353  CG  ASN A 226      23.331 -48.383   4.252  1.00 64.87           C  
ANISOU  353  CG  ASN A 226     7872   8340   8437     28   -996    -43       C  
ATOM    354  OD1 ASN A 226      23.236 -47.217   4.638  1.00 67.10           O  
ANISOU  354  OD1 ASN A 226     8078   8718   8698     21   -951   -105       O  
ATOM    355  ND2 ASN A 226      24.498 -48.971   4.041  1.00 60.94           N  
ANISOU  355  ND2 ASN A 226     7385   7734   8034    132  -1098    -15       N  
ATOM    356  N   ILE A 227      19.253 -50.416   4.212  1.00 68.12           N  
ANISOU  356  N   ILE A 227     8489   8875   8520   -418   -819    108       N  
ATOM    357  CA  ILE A 227      18.102 -51.047   3.586  1.00 61.11           C  
ANISOU  357  CA  ILE A 227     7616   8009   7596   -545   -768    143       C  
ATOM    358  C   ILE A 227      16.833 -50.296   3.947  1.00 65.18           C  
ANISOU  358  C   ILE A 227     8009   8742   8014   -642   -640    120       C  
ATOM    359  O   ILE A 227      16.051 -49.946   3.075  1.00 74.07           O  
ANISOU  359  O   ILE A 227     9021   9942   9180   -650   -561     81       O  
ATOM    360  CB  ILE A 227      17.971 -52.521   3.998  1.00 66.53           C  
ANISOU  360  CB  ILE A 227     8504   8576   8197   -679   -866    262       C  
ATOM    361  CG1 ILE A 227      19.185 -53.320   3.523  1.00 61.30           C  
ANISOU  361  CG1 ILE A 227     7965   7685   7640   -549   -992    275       C  
ATOM    362  CG2 ILE A 227      16.693 -53.130   3.433  1.00 61.70           C  
ANISOU  362  CG2 ILE A 227     7904   8004   7533   -853   -819    304       C  
ATOM    363  CD1 ILE A 227      19.240 -54.718   4.092  1.00 63.05           C  
ANISOU  363  CD1 ILE A 227     8421   7755   7779   -651  -1117    395       C  
ATOM    364  N   LEU A 228      16.646 -50.026   5.232  1.00 66.03           N  
ANISOU  364  N   LEU A 228     8137   8960   7990   -702   -620    141       N  
ATOM    365  CA  LEU A 228      15.488 -49.256   5.693  1.00 74.99           C  
ANISOU  365  CA  LEU A 228     9149  10322   9023   -765   -484    107       C  
ATOM    366  C   LEU A 228      15.477 -47.794   5.202  1.00 75.98           C  
ANISOU  366  C   LEU A 228     9108  10523   9236   -606   -399    -22       C  
ATOM    367  O   LEU A 228      14.417 -47.200   5.009  1.00 77.50           O  
ANISOU  367  O   LEU A 228     9168  10877   9403   -617   -285    -63       O  
ATOM    368  CB  LEU A 228      15.428 -49.270   7.221  1.00 77.90           C  
ANISOU  368  CB  LEU A 228     9601  10784   9214   -848   -479    147       C  
ATOM    369  CG  LEU A 228      15.507 -50.632   7.910  1.00 76.73           C  
ANISOU  369  CG  LEU A 228     9646  10555   8952  -1011   -575    288       C  
ATOM    370  CD1 LEU A 228      15.684 -50.479   9.416  1.00 71.89           C  
ANISOU  370  CD1 LEU A 228     9128  10024   8163  -1062   -585    318       C  
ATOM    371  CD2 LEU A 228      14.279 -51.461   7.594  1.00 76.72           C  
ANISOU  371  CD2 LEU A 228     9638  10627   8886  -1209   -522    373       C  
ATOM    372  N   SER A 229      16.656 -47.212   5.015  1.00 74.65           N  
ANISOU  372  N   SER A 229     8948  10240   9174   -460   -459    -82       N  
ATOM    373  CA  SER A 229      16.758 -45.808   4.638  1.00 74.86           C  
ANISOU  373  CA  SER A 229     8855  10311   9279   -324   -397   -194       C  
ATOM    374  C   SER A 229      16.673 -45.597   3.127  1.00 87.61           C  
ANISOU  374  C   SER A 229    10379  11871  11037   -253   -375   -225       C  
ATOM    375  O   SER A 229      16.435 -44.482   2.676  1.00 91.70           O  
ANISOU  375  O   SER A 229    10796  12438  11608   -161   -312   -304       O  
ATOM    376  CB  SER A 229      18.065 -45.206   5.161  1.00 64.81           C  
ANISOU  376  CB  SER A 229     7629   8952   8046   -230   -477   -237       C  
ATOM    377  OG  SER A 229      18.112 -45.223   6.575  1.00 68.76           O  
ANISOU  377  OG  SER A 229     8216   9513   8396   -289   -499   -222       O  
ATOM    378  N   GLU A 230      16.877 -46.658   2.351  1.00 87.11           N  
ANISOU  378  N   GLU A 230    10372  11698  11028   -291   -431   -166       N  
ATOM    379  CA  GLU A 230      16.891 -46.545   0.898  1.00 85.43           C  
ANISOU  379  CA  GLU A 230    10100  11426  10934   -227   -418   -195       C  
ATOM    380  C   GLU A 230      15.543 -46.053   0.390  1.00 82.07           C  
ANISOU  380  C   GLU A 230     9554  11144  10485   -259   -326   -218       C  
ATOM    381  O   GLU A 230      14.515 -46.698   0.616  1.00 82.05           O  
ANISOU  381  O   GLU A 230     9544  11236  10394   -391   -302   -164       O  
ATOM    382  CB  GLU A 230      17.238 -47.883   0.238  1.00 90.61           C  
ANISOU  382  CB  GLU A 230    10866  11938  11622   -269   -493   -134       C  
ATOM    383  CG  GLU A 230      17.408 -47.810  -1.283  1.00 87.91           C  
ANISOU  383  CG  GLU A 230    10489  11524  11388   -195   -482   -171       C  
ATOM    384  CD  GLU A 230      18.664 -47.058  -1.702  1.00 92.35           C  
ANISOU  384  CD  GLU A 230    11010  12015  12063    -41   -488   -228       C  
ATOM    385  OE1 GLU A 230      19.615 -46.967  -0.893  1.00 90.35           O  
ANISOU  385  OE1 GLU A 230    10783  11723  11821      4   -538   -224       O  
ATOM    386  OE2 GLU A 230      18.692 -46.546  -2.842  1.00 96.53           O  
ANISOU  386  OE2 GLU A 230    11478  12534  12663     23   -448   -269       O  
ATOM    387  N   PRO A 231      15.553 -44.898  -0.300  1.00 79.71           N  
ANISOU  387  N   PRO A 231     9156  10864  10266   -141   -280   -291       N  
ATOM    388  CA  PRO A 231      14.376 -44.253  -0.897  1.00 78.15           C  
ANISOU  388  CA  PRO A 231     8831  10794  10068   -126   -208   -319       C  
ATOM    389  C   PRO A 231      13.879 -45.023  -2.103  1.00 91.44           C  
ANISOU  389  C   PRO A 231    10509  12452  11782   -190   -231   -277       C  
ATOM    390  O   PRO A 231      14.708 -45.491  -2.881  1.00 94.13           O  
ANISOU  390  O   PRO A 231    10930  12645  12190   -164   -285   -270       O  
ATOM    391  CB  PRO A 231      14.905 -42.883  -1.307  1.00 69.49           C  
ANISOU  391  CB  PRO A 231     7689   9657   9059     28   -188   -398       C  
ATOM    392  CG  PRO A 231      16.369 -43.109  -1.549  1.00 67.66           C  
ANISOU  392  CG  PRO A 231     7544   9260   8906     67   -256   -394       C  
ATOM    393  CD  PRO A 231      16.790 -44.132  -0.553  1.00 72.76           C  
ANISOU  393  CD  PRO A 231     8285   9876   9485    -15   -309   -342       C  
ATOM    394  N   PRO A 232      12.553 -45.159  -2.256  1.00102.02           N  
ANISOU  394  N   PRO A 232    11753  13942  13069   -273   -193   -253       N  
ATOM    395  CA  PRO A 232      11.993 -45.914  -3.384  1.00106.24           C  
ANISOU  395  CA  PRO A 232    12288  14460  13618   -361   -233   -212       C  
ATOM    396  C   PRO A 232      12.434 -45.342  -4.732  1.00 99.84           C  
ANISOU  396  C   PRO A 232    11471  13556  12906   -241   -251   -256       C  
ATOM    397  O   PRO A 232      12.098 -44.217  -5.086  1.00 97.67           O  
ANISOU  397  O   PRO A 232    11090  13350  12668   -135   -211   -300       O  
ATOM    398  CB  PRO A 232      10.476 -45.777  -3.187  1.00110.03           C  
ANISOU  398  CB  PRO A 232    12610  15165  14032   -445   -180   -189       C  
ATOM    399  CG  PRO A 232      10.299 -44.587  -2.304  1.00107.46           C  
ANISOU  399  CG  PRO A 232    12183  14961  13688   -325    -94   -249       C  
ATOM    400  CD  PRO A 232      11.505 -44.562  -1.414  1.00105.45           C  
ANISOU  400  CD  PRO A 232    12061  14582  13425   -283   -110   -268       C  
ATOM    401  N   LYS A 233      13.226 -46.126  -5.454  1.00100.38           N  
ANISOU  401  N   LYS A 233    11669  13462  13009   -252   -309   -244       N  
ATOM    402  CA  LYS A 233      13.681 -45.777  -6.794  1.00 88.69           C  
ANISOU  402  CA  LYS A 233    10205  11896  11599   -162   -320   -277       C  
ATOM    403  C   LYS A 233      13.013 -46.711  -7.778  1.00 86.74           C  
ANISOU  403  C   LYS A 233    10008  11632  11317   -272   -371   -246       C  
ATOM    404  O   LYS A 233      13.002 -47.921  -7.581  1.00 89.96           O  
ANISOU  404  O   LYS A 233    10529  11971  11679   -388   -421   -207       O  
ATOM    405  CB  LYS A 233      15.201 -45.883  -6.920  1.00 88.47           C  
ANISOU  405  CB  LYS A 233    10277  11705  11633    -67   -334   -301       C  
ATOM    406  CG  LYS A 233      15.971 -45.059  -5.896  1.00102.69           C  
ANISOU  406  CG  LYS A 233    12042  13510  13464     16   -309   -328       C  
ATOM    407  CD  LYS A 233      15.942 -43.576  -6.222  1.00110.79           C  
ANISOU  407  CD  LYS A 233    12973  14582  14539    119   -262   -374       C  
ATOM    408  CE  LYS A 233      16.738 -43.280  -7.482  1.00113.10           C  
ANISOU  408  CE  LYS A 233    13290  14780  14901    193   -259   -391       C  
ATOM    409  NZ  LYS A 233      16.736 -41.830  -7.825  1.00114.84           N  
ANISOU  409  NZ  LYS A 233    13444  15023  15166    279   -226   -422       N  
ATOM    410  N   ARG A 234      12.441 -46.132  -8.825  1.00 85.16           N  
ANISOU  410  N   ARG A 234     9737  11487  11132   -241   -370   -260       N  
ATOM    411  CA  ARG A 234      11.833 -46.888  -9.910  1.00 84.22           C  
ANISOU  411  CA  ARG A 234     9671  11352  10976   -341   -431   -239       C  
ATOM    412  C   ARG A 234      12.727 -48.034 -10.394  1.00 81.32           C  
ANISOU  412  C   ARG A 234     9507  10792  10600   -365   -477   -247       C  
ATOM    413  O   ARG A 234      13.928 -47.850 -10.632  1.00 83.76           O  
ANISOU  413  O   ARG A 234     9881  10984  10958   -239   -450   -285       O  
ATOM    414  CB  ARG A 234      11.504 -45.944 -11.080  1.00 84.45           C  
ANISOU  414  CB  ARG A 234     9629  11428  11032   -256   -429   -261       C  
ATOM    415  CG  ARG A 234      11.950 -46.473 -12.437  1.00 74.30           C  
ANISOU  415  CG  ARG A 234     8484  10015   9731   -258   -473   -278       C  
ATOM    416  CD  ARG A 234      11.742 -45.477 -13.540  1.00 67.09           C  
ANISOU  416  CD  ARG A 234     7519   9140   8832   -171   -471   -290       C  
ATOM    417  NE  ARG A 234      10.751 -45.981 -14.471  1.00 69.52           N  
ANISOU  417  NE  ARG A 234     7839   9499   9075   -283   -553   -266       N  
ATOM    418  CZ  ARG A 234      11.022 -46.866 -15.416  1.00 70.72           C  
ANISOU  418  CZ  ARG A 234     8158   9539   9173   -342   -602   -281       C  
ATOM    419  NH1 ARG A 234      12.261 -47.312 -15.553  1.00 71.63           N  
ANISOU  419  NH1 ARG A 234     8423   9495   9299   -277   -563   -322       N  
ATOM    420  NH2 ARG A 234      10.061 -47.301 -16.219  1.00 70.64           N  
ANISOU  420  NH2 ARG A 234     8163   9581   9096   -462   -692   -260       N  
ATOM    421  N   LYS A 235      12.147 -49.224 -10.515  1.00 82.57           N  
ANISOU  421  N   LYS A 235     9761  10918  10694   -527   -546   -210       N  
ATOM    422  CA  LYS A 235      12.856 -50.339 -11.138  1.00 84.24           C  
ANISOU  422  CA  LYS A 235    10189  10932  10888   -539   -600   -229       C  
ATOM    423  C   LYS A 235      12.343 -50.570 -12.566  1.00 85.83           C  
ANISOU  423  C   LYS A 235    10450  11114  11046   -589   -651   -249       C  
ATOM    424  O   LYS A 235      11.190 -50.256 -12.888  1.00 89.97           O  
ANISOU  424  O   LYS A 235    10861  11783  11540   -685   -680   -221       O  
ATOM    425  CB  LYS A 235      12.715 -51.607 -10.301  1.00 86.11           C  
ANISOU  425  CB  LYS A 235    10556  11088  11073   -687   -662   -177       C  
ATOM    426  CG  LYS A 235      11.271 -52.011 -10.033  1.00 96.40           C  
ANISOU  426  CG  LYS A 235    11796  12527  12304   -914   -709   -109       C  
ATOM    427  CD  LYS A 235      11.191 -53.428  -9.472  1.00103.95           C  
ANISOU  427  CD  LYS A 235    12943  13356  13197  -1088   -790    -51       C  
ATOM    428  CE  LYS A 235      12.128 -53.615  -8.278  1.00102.39           C  
ANISOU  428  CE  LYS A 235    12811  13074  13020  -1012   -767    -33       C  
ATOM    429  NZ  LYS A 235      12.232 -55.043  -7.873  1.00 98.77           N  
ANISOU  429  NZ  LYS A 235    12589  12437  12503  -1151   -863     23       N  
ATOM    430  N   LYS A 236      13.206 -51.116 -13.416  1.00 76.04           N  
ANISOU  430  N   LYS A 236     9387   9704   9799   -515   -663   -300       N  
ATOM    431  CA  LYS A 236      12.898 -51.271 -14.835  1.00 72.97           C  
ANISOU  431  CA  LYS A 236     9084   9285   9355   -539   -703   -334       C  
ATOM    432  C   LYS A 236      11.683 -52.146 -15.113  1.00 76.36           C  
ANISOU  432  C   LYS A 236     9579   9734   9699   -763   -816   -296       C  
ATOM    433  O   LYS A 236      11.537 -53.224 -14.534  1.00 86.21           O  
ANISOU  433  O   LYS A 236    10950  10892  10915   -892   -876   -267       O  
ATOM    434  CB  LYS A 236      14.100 -51.857 -15.571  1.00 71.02           C  
ANISOU  434  CB  LYS A 236     9036   8848   9100   -415   -683   -405       C  
ATOM    435  CG  LYS A 236      13.801 -52.231 -17.011  1.00 58.73           C  
ANISOU  435  CG  LYS A 236     7621   7238   7454   -454   -731   -449       C  
ATOM    436  CD  LYS A 236      14.871 -53.133 -17.576  1.00 59.44           C  
ANISOU  436  CD  LYS A 236     7944   7126   7515   -349   -718   -526       C  
ATOM    437  CE  LYS A 236      14.692 -53.340 -19.066  1.00 60.40           C  
ANISOU  437  CE  LYS A 236     8212   7204   7533   -360   -744   -585       C  
ATOM    438  NZ  LYS A 236      13.259 -53.452 -19.435  1.00 68.07           N  
ANISOU  438  NZ  LYS A 236     9171   8260   8430   -573   -861   -541       N  
ATOM    439  N   ARG A 237      10.820 -51.687 -16.011  1.00 68.91           N  
ANISOU  439  N   ARG A 237     8561   8904   8719   -819   -856   -291       N  
ATOM    440  CA  ARG A 237       9.712 -52.516 -16.462  1.00 68.71           C  
ANISOU  440  CA  ARG A 237     8601   8898   8608  -1043   -980   -259       C  
ATOM    441  C   ARG A 237      10.249 -53.677 -17.279  1.00 74.56           C  
ANISOU  441  C   ARG A 237     9646   9408   9276  -1072  -1044   -319       C  
ATOM    442  O   ARG A 237      10.948 -53.475 -18.269  1.00 75.68           O  
ANISOU  442  O   ARG A 237     9892   9467   9396   -934  -1011   -389       O  
ATOM    443  CB  ARG A 237       8.702 -51.699 -17.272  1.00 61.40           C  
ANISOU  443  CB  ARG A 237     7512   8156   7661  -1077  -1022   -237       C  
ATOM    444  CG  ARG A 237       7.862 -50.791 -16.396  1.00 61.66           C  
ANISOU  444  CG  ARG A 237     7251   8425   7751  -1084   -983   -175       C  
ATOM    445  CD  ARG A 237       6.777 -50.046 -17.145  1.00 68.91           C  
ANISOU  445  CD  ARG A 237     7996   9533   8655  -1109  -1044   -145       C  
ATOM    446  NE  ARG A 237       5.904 -50.919 -17.925  1.00 76.28           N  
ANISOU  446  NE  ARG A 237     9009  10477   9499  -1326  -1188   -122       N  
ATOM    447  CZ  ARG A 237       4.695 -50.571 -18.361  1.00 78.95           C  
ANISOU  447  CZ  ARG A 237     9169  11013   9816  -1420  -1277    -72       C  
ATOM    448  NH1 ARG A 237       4.192 -49.379 -18.071  1.00 80.45           N  
ANISOU  448  NH1 ARG A 237     9093  11403  10072  -1296  -1228    -43       N  
ATOM    449  NH2 ARG A 237       3.982 -51.421 -19.083  1.00 78.88           N  
ANISOU  449  NH2 ARG A 237     9250  11000   9720  -1635  -1423    -53       N  
ATOM    450  N   LYS A 238       9.926 -54.894 -16.848  1.00 78.91           N  
ANISOU  450  N   LYS A 238    10350   9851   9780  -1253  -1133   -291       N  
ATOM    451  CA  LYS A 238      10.391 -56.105 -17.517  1.00 78.32           C  
ANISOU  451  CA  LYS A 238    10601   9527   9631  -1283  -1208   -353       C  
ATOM    452  C   LYS A 238       9.728 -56.296 -18.878  1.00 79.01           C  
ANISOU  452  C   LYS A 238    10790   9614   9617  -1390  -1306   -389       C  
ATOM    453  O   LYS A 238      10.269 -56.980 -19.740  1.00 85.96           O  
ANISOU  453  O   LYS A 238    11937  10300  10425  -1344  -1338   -474       O  
ATOM    454  CB  LYS A 238      10.131 -57.337 -16.646  1.00 82.10           C  
ANISOU  454  CB  LYS A 238    11234   9877  10083  -1471  -1295   -300       C  
ATOM    455  CG  LYS A 238      10.708 -57.267 -15.236  1.00 94.33           C  
ANISOU  455  CG  LYS A 238    12708  11423  11711  -1395  -1222   -252       C  
ATOM    456  CD  LYS A 238      12.202 -56.971 -15.255  1.00110.16           C  
ANISOU  456  CD  LYS A 238    14764  13310  13784  -1098  -1119   -329       C  
ATOM    457  CE  LYS A 238      12.801 -57.034 -13.849  1.00118.82           C  
ANISOU  457  CE  LYS A 238    15817  14384  14946  -1037  -1077   -279       C  
ATOM    458  NZ  LYS A 238      12.782 -58.429 -13.292  1.00121.46           N  
ANISOU  458  NZ  LYS A 238    16405  14512  15233  -1173  -1185   -238       N  
ATOM    459  N   ASP A 239       8.565 -55.678 -19.076  1.00 74.16           N  
ANISOU  459  N   ASP A 239     9964   9222   8991  -1521  -1356   -327       N  
ATOM    460  CA  ASP A 239       7.770 -55.868 -20.294  1.00 72.74           C  
ANISOU  460  CA  ASP A 239     9860   9070   8708  -1660  -1482   -342       C  
ATOM    461  C   ASP A 239       8.005 -54.813 -21.382  1.00 77.35           C  
ANISOU  461  C   ASP A 239    10378   9736   9275  -1487  -1433   -387       C  
ATOM    462  O   ASP A 239       7.300 -54.777 -22.388  1.00 78.23           O  
ANISOU  462  O   ASP A 239    10519   9905   9300  -1588  -1540   -389       O  
ATOM    463  CB  ASP A 239       6.283 -55.895 -19.939  1.00 79.00           C  
ANISOU  463  CB  ASP A 239    10453  10073   9490  -1925  -1590   -239       C  
ATOM    464  CG  ASP A 239       5.795 -54.582 -19.349  1.00 86.76           C  
ANISOU  464  CG  ASP A 239    11063  11335  10567  -1836  -1504   -174       C  
ATOM    465  OD1 ASP A 239       6.630 -53.793 -18.850  1.00 87.42           O  
ANISOU  465  OD1 ASP A 239    11060  11422  10735  -1606  -1362   -197       O  
ATOM    466  OD2 ASP A 239       4.569 -54.340 -19.379  1.00 88.52           O  
ANISOU  466  OD2 ASP A 239    11079  11774  10780  -1995  -1584   -103       O  
ATOM    467  N   ILE A 240       8.983 -53.942 -21.166  1.00 77.84           N  
ANISOU  467  N   ILE A 240    10353   9805   9416  -1240  -1282   -414       N  
ATOM    468  CA  ILE A 240       9.350 -52.938 -22.151  1.00 73.69           C  
ANISOU  468  CA  ILE A 240     9790   9336   8874  -1076  -1223   -448       C  
ATOM    469  C   ILE A 240      10.852 -53.011 -22.330  1.00 73.09           C  
ANISOU  469  C   ILE A 240     9866   9095   8811   -862  -1092   -532       C  
ATOM    470  O   ILE A 240      11.608 -52.689 -21.403  1.00 66.33           O  
ANISOU  470  O   ILE A 240     8912   8230   8060   -735   -984   -525       O  
ATOM    471  CB  ILE A 240       8.924 -51.523 -21.718  1.00 72.72           C  
ANISOU  471  CB  ILE A 240     9352   9434   8845   -995  -1168   -379       C  
ATOM    472  CG1 ILE A 240       7.399 -51.446 -21.617  1.00 73.96           C  
ANISOU  472  CG1 ILE A 240     9330   9782   8988  -1187  -1295   -299       C  
ATOM    473  CG2 ILE A 240       9.453 -50.468 -22.695  1.00 66.30           C  
ANISOU  473  CG2 ILE A 240     8531   8645   8015   -821  -1103   -404       C  
ATOM    474  CD1 ILE A 240       6.879 -50.121 -21.125  1.00 71.71           C  
ANISOU  474  CD1 ILE A 240     8738   9713   8796  -1092  -1248   -237       C  
ATOM    475  N   ASN A 241      11.286 -53.449 -23.512  1.00 73.80           N  
ANISOU  475  N   ASN A 241    10190   9064   8787   -824  -1103   -614       N  
ATOM    476  CA  ASN A 241      12.689 -53.795 -23.709  1.00 76.02           C  
ANISOU  476  CA  ASN A 241    10636   9183   9065   -632   -983   -704       C  
ATOM    477  C   ASN A 241      13.269 -53.421 -25.056  1.00 81.57           C  
ANISOU  477  C   ASN A 241    11456   9874   9665   -512   -915   -773       C  
ATOM    478  O   ASN A 241      14.376 -52.899 -25.126  1.00 80.24           O  
ANISOU  478  O   ASN A 241    11246   9703   9539   -320   -766   -804       O  
ATOM    479  CB  ASN A 241      12.884 -55.297 -23.499  1.00 78.63           C  
ANISOU  479  CB  ASN A 241    11232   9295   9350   -696  -1051   -762       C  
ATOM    480  CG  ASN A 241      12.604 -55.720 -22.081  1.00 77.71           C  
ANISOU  480  CG  ASN A 241    11029   9165   9331   -789  -1089   -692       C  
ATOM    481  OD1 ASN A 241      13.497 -55.723 -21.228  1.00 71.23           O  
ANISOU  481  OD1 ASN A 241    10165   8292   8607   -649   -999   -694       O  
ATOM    482  ND2 ASN A 241      11.353 -56.074 -21.813  1.00 79.54           N  
ANISOU  482  ND2 ASN A 241    11228   9459   9535  -1036  -1226   -622       N  
ATOM    483  N   THR A 242      12.534 -53.703 -26.125  1.00 89.22           N  
ANISOU  483  N   THR A 242    12569  10841  10489   -636  -1028   -795       N  
ATOM    484  CA  THR A 242      13.095 -53.600 -27.465  1.00 86.43           C  
ANISOU  484  CA  THR A 242    12395  10449   9997   -539   -971   -874       C  
ATOM    485  C   THR A 242      12.741 -52.291 -28.157  1.00 78.96           C  
ANISOU  485  C   THR A 242    11297   9682   9022   -523   -959   -809       C  
ATOM    486  O   THR A 242      11.772 -51.633 -27.803  1.00 82.77           O  
ANISOU  486  O   THR A 242    11576  10310   9565   -620  -1046   -712       O  
ATOM    487  CB  THR A 242      12.641 -54.781 -28.351  1.00 96.53           C  
ANISOU  487  CB  THR A 242    13992  11585  11100   -673  -1106   -957       C  
ATOM    488  OG1 THR A 242      13.472 -54.859 -29.516  1.00113.62           O  
ANISOU  488  OG1 THR A 242    16367  13680  13122   -534  -1010  -1062       O  
ATOM    489  CG2 THR A 242      11.206 -54.622 -28.781  1.00 94.25           C  
ANISOU  489  CG2 THR A 242    13658  11413  10740   -902  -1296   -887       C  
ATOM    490  N   ILE A 243      13.549 -51.914 -29.140  1.00 73.46           N  
ANISOU  490  N   ILE A 243    10705   8978   8231   -393   -847   -861       N  
ATOM    491  CA  ILE A 243      13.309 -50.707 -29.936  1.00 80.30           C  
ANISOU  491  CA  ILE A 243    11481   9988   9042   -377   -838   -797       C  
ATOM    492  C   ILE A 243      11.926 -50.714 -30.616  1.00 79.05           C  
ANISOU  492  C   ILE A 243    11360   9903   8773   -563  -1044   -750       C  
ATOM    493  O   ILE A 243      11.326 -49.662 -30.841  1.00 70.69           O  
ANISOU  493  O   ILE A 243    10143   8986   7728   -579  -1095   -656       O  
ATOM    494  CB  ILE A 243      14.423 -50.514 -30.998  1.00 67.79           C  
ANISOU  494  CB  ILE A 243    10054   8372   7332   -235   -682   -867       C  
ATOM    495  CG1 ILE A 243      14.063 -49.390 -31.953  1.00 70.03           C  
ANISOU  495  CG1 ILE A 243    10303   8784   7520   -253   -703   -792       C  
ATOM    496  CG2 ILE A 243      14.667 -51.790 -31.773  1.00 81.29           C  
ANISOU  496  CG2 ILE A 243    12084   9931   8870   -246   -699   -999       C  
ATOM    497  CD1 ILE A 243      15.263 -48.665 -32.492  1.00 79.55           C  
ANISOU  497  CD1 ILE A 243    11515  10020   8689   -103   -502   -800       C  
ATOM    498  N   GLU A 244      11.406 -51.902 -30.912  1.00 82.73           N  
ANISOU  498  N   GLU A 244    12033  10267   9133   -706  -1176   -812       N  
ATOM    499  CA  GLU A 244      10.033 -52.023 -31.389  1.00 88.12           C  
ANISOU  499  CA  GLU A 244    12723  11030   9731   -914  -1397   -761       C  
ATOM    500  C   GLU A 244       9.052 -51.603 -30.300  1.00 89.40           C  
ANISOU  500  C   GLU A 244    12574  11334  10058  -1009  -1483   -646       C  
ATOM    501  O   GLU A 244       8.063 -50.935 -30.587  1.00 94.05           O  
ANISOU  501  O   GLU A 244    13014  12083  10639  -1086  -1605   -559       O  
ATOM    502  CB  GLU A 244       9.732 -53.447 -31.856  1.00 94.05           C  
ANISOU  502  CB  GLU A 244    13777  11622  10337  -1069  -1526   -856       C  
ATOM    503  CG  GLU A 244      10.292 -53.777 -33.232  1.00108.39           C  
ANISOU  503  CG  GLU A 244    15914  13339  11929  -1014  -1496   -967       C  
ATOM    504  CD  GLU A 244      11.803 -53.939 -33.228  1.00115.30           C  
ANISOU  504  CD  GLU A 244    16903  14096  12809   -779  -1261  -1069       C  
ATOM    505  OE1 GLU A 244      12.390 -53.964 -32.123  1.00107.97           O  
ANISOU  505  OE1 GLU A 244    15830  13136  12059   -677  -1151  -1058       O  
ATOM    506  OE2 GLU A 244      12.397 -54.051 -34.329  1.00120.46           O  
ANISOU  506  OE2 GLU A 244    17787  14700  13283   -696  -1187  -1160       O  
ATOM    507  N   ASP A 245       9.332 -51.983 -29.052  1.00 87.91           N  
ANISOU  507  N   ASP A 245    12289  11097  10014   -992  -1416   -644       N  
ATOM    508  CA  ASP A 245       8.506 -51.557 -27.920  1.00 87.26           C  
ANISOU  508  CA  ASP A 245    11909  11161  10085  -1061  -1461   -542       C  
ATOM    509  C   ASP A 245       8.570 -50.047 -27.758  1.00 84.81           C  
ANISOU  509  C   ASP A 245    11348  11004   9870   -909  -1378   -469       C  
ATOM    510  O   ASP A 245       7.577 -49.409 -27.406  1.00 87.21           O  
ANISOU  510  O   ASP A 245    11418  11477  10241   -960  -1458   -381       O  
ATOM    511  CB  ASP A 245       8.947 -52.223 -26.614  1.00 88.55           C  
ANISOU  511  CB  ASP A 245    12045  11233  10366  -1056  -1388   -556       C  
ATOM    512  CG  ASP A 245       8.912 -53.723 -26.682  1.00 94.48           C  
ANISOU  512  CG  ASP A 245    13066  11802  11033  -1201  -1477   -622       C  
ATOM    513  OD1 ASP A 245       8.259 -54.261 -27.600  1.00 98.49           O  
ANISOU  513  OD1 ASP A 245    13739  12283  11400  -1357  -1624   -645       O  
ATOM    514  OD2 ASP A 245       9.555 -54.365 -25.824  1.00 97.61           O  
ANISOU  514  OD2 ASP A 245    13522  12068  11498  -1159  -1408   -651       O  
ATOM    515  N   ALA A 246       9.751 -49.487 -28.006  1.00 80.81           N  
ANISOU  515  N   ALA A 246    10894  10437   9372   -721  -1216   -505       N  
ATOM    516  CA  ALA A 246       9.957 -48.048 -27.939  1.00 75.20           C  
ANISOU  516  CA  ALA A 246     9999   9834   8741   -580  -1136   -440       C  
ATOM    517  C   ALA A 246       9.009 -47.341 -28.899  1.00 78.33           C  
ANISOU  517  C   ALA A 246    10359  10351   9051   -629  -1271   -373       C  
ATOM    518  O   ALA A 246       8.291 -46.419 -28.518  1.00 77.41           O  
ANISOU  518  O   ALA A 246    10020  10370   9023   -604  -1320   -288       O  
ATOM    519  CB  ALA A 246      11.402 -47.706 -28.261  1.00 69.96           C  
ANISOU  519  CB  ALA A 246     9435   9081   8067   -413   -954   -490       C  
ATOM    520  N   VAL A 247       8.993 -47.807 -30.143  1.00 80.54           N  
ANISOU  520  N   VAL A 247    10871  10579   9150   -691  -1339   -414       N  
ATOM    521  CA  VAL A 247       8.167 -47.198 -31.176  1.00 80.36           C  
ANISOU  521  CA  VAL A 247    10854  10662   9019   -739  -1482   -350       C  
ATOM    522  C   VAL A 247       6.666 -47.274 -30.847  1.00 78.61           C  
ANISOU  522  C   VAL A 247    10441  10586   8841   -885  -1682   -277       C  
ATOM    523  O   VAL A 247       5.949 -46.295 -31.040  1.00 78.33           O  
ANISOU  523  O   VAL A 247    10239  10690   8834   -849  -1768   -186       O  
ATOM    524  CB  VAL A 247       8.432 -47.840 -32.557  1.00 75.74           C  
ANISOU  524  CB  VAL A 247    10586   9988   8204   -797  -1524   -421       C  
ATOM    525  CG1 VAL A 247       7.495 -47.257 -33.594  1.00 78.18           C  
ANISOU  525  CG1 VAL A 247    10902  10411   8391   -864  -1702   -345       C  
ATOM    526  CG2 VAL A 247       9.871 -47.599 -32.985  1.00 75.22           C  
ANISOU  526  CG2 VAL A 247    10671   9824   8086   -639  -1313   -482       C  
ATOM    527  N   LYS A 248       6.194 -48.417 -30.351  1.00 75.25           N  
ANISOU  527  N   LYS A 248    10036  10134   8421  -1049  -1758   -310       N  
ATOM    528  CA  LYS A 248       4.790 -48.543 -29.945  1.00 78.86           C  
ANISOU  528  CA  LYS A 248    10281  10756   8927  -1208  -1932   -234       C  
ATOM    529  C   LYS A 248       4.409 -47.436 -28.987  1.00 82.95           C  
ANISOU  529  C   LYS A 248    10463  11431   9622  -1087  -1879   -151       C  
ATOM    530  O   LYS A 248       3.356 -46.807 -29.117  1.00 87.69           O  
ANISOU  530  O   LYS A 248    10858  12211  10247  -1103  -2005    -68       O  
ATOM    531  CB  LYS A 248       4.516 -49.883 -29.266  1.00 84.69           C  
ANISOU  531  CB  LYS A 248    11073  11430   9676  -1401  -1978   -272       C  
ATOM    532  CG  LYS A 248       4.642 -51.084 -30.150  1.00104.08           C  
ANISOU  532  CG  LYS A 248    13865  13725  11954  -1552  -2073   -357       C  
ATOM    533  CD  LYS A 248       3.906 -52.259 -29.538  1.00115.91           C  
ANISOU  533  CD  LYS A 248    15369  15208  13463  -1801  -2194   -351       C  
ATOM    534  CE  LYS A 248       2.465 -51.886 -29.216  1.00119.99           C  
ANISOU  534  CE  LYS A 248    15566  15982  14044  -1949  -2347   -233       C  
ATOM    535  NZ  LYS A 248       1.624 -53.083 -28.937  1.00125.39           N  
ANISOU  535  NZ  LYS A 248    16287  16665  14692  -2254  -2505   -218       N  
ATOM    536  N   LEU A 249       5.281 -47.235 -28.004  1.00 80.16           N  
ANISOU  536  N   LEU A 249    10059  11007   9389   -960  -1695   -179       N  
ATOM    537  CA  LEU A 249       5.119 -46.209 -26.994  1.00 76.25           C  
ANISOU  537  CA  LEU A 249     9289  10626   9055   -826  -1617   -124       C  
ATOM    538  C   LEU A 249       4.970 -44.856 -27.662  1.00 77.19           C  
ANISOU  538  C   LEU A 249     9338  10817   9173   -676  -1643    -65       C  
ATOM    539  O   LEU A 249       3.960 -44.171 -27.486  1.00 80.12           O  
ANISOU  539  O   LEU A 249     9483  11356   9604   -649  -1735      8       O  
ATOM    540  CB  LEU A 249       6.317 -46.215 -26.046  1.00 77.77           C  
ANISOU  540  CB  LEU A 249     9509  10696   9343   -710  -1421   -176       C  
ATOM    541  CG  LEU A 249       6.345 -47.288 -24.953  1.00 76.10           C  
ANISOU  541  CG  LEU A 249     9289  10444   9183   -822  -1389   -205       C  
ATOM    542  CD1 LEU A 249       7.674 -47.280 -24.217  1.00 62.79           C  
ANISOU  542  CD1 LEU A 249     7666   8621   7572   -690  -1212   -258       C  
ATOM    543  CD2 LEU A 249       5.209 -47.050 -23.979  1.00 74.49           C  
ANISOU  543  CD2 LEU A 249     8799  10432   9072   -885  -1438   -137       C  
ATOM    544  N   LEU A 250       5.986 -44.501 -28.445  1.00 76.97           N  
ANISOU  544  N   LEU A 250     9510  10663   9073   -578  -1560    -93       N  
ATOM    545  CA  LEU A 250       5.972 -43.318 -29.300  1.00 66.87           C  
ANISOU  545  CA  LEU A 250     8243   9413   7753   -462  -1593    -32       C  
ATOM    546  C   LEU A 250       4.686 -43.142 -30.101  1.00 68.87           C  
ANISOU  546  C   LEU A 250     8434   9805   7928   -537  -1814     40       C  
ATOM    547  O   LEU A 250       4.260 -42.019 -30.348  1.00 81.44           O  
ANISOU  547  O   LEU A 250     9918  11474   9551   -422  -1874    118       O  
ATOM    548  CB  LEU A 250       7.164 -43.369 -30.248  1.00 66.75           C  
ANISOU  548  CB  LEU A 250     8500   9252   7611   -423  -1493    -78       C  
ATOM    549  CG  LEU A 250       8.440 -42.947 -29.533  1.00 64.93           C  
ANISOU  549  CG  LEU A 250     8261   8924   7484   -290  -1280   -111       C  
ATOM    550  CD1 LEU A 250       9.691 -43.129 -30.379  1.00 64.98           C  
ANISOU  550  CD1 LEU A 250     8508   8809   7371   -257  -1153   -164       C  
ATOM    551  CD2 LEU A 250       8.280 -41.503 -29.110  1.00 64.36           C  
ANISOU  551  CD2 LEU A 250     8014   8908   7531   -152  -1265    -32       C  
ATOM    552  N   GLN A 251       4.066 -44.243 -30.504  1.00 71.18           N  
ANISOU  552  N   GLN A 251     8800  10125   8120   -730  -1947     17       N  
ATOM    553  CA  GLN A 251       2.803 -44.162 -31.216  1.00 76.34           C  
ANISOU  553  CA  GLN A 251     9373  10930   8703   -826  -2178     88       C  
ATOM    554  C   GLN A 251       1.628 -43.984 -30.263  1.00 85.10           C  
ANISOU  554  C   GLN A 251    10136  12242   9957   -848  -2256    149       C  
ATOM    555  O   GLN A 251       0.867 -43.030 -30.375  1.00 92.39           O  
ANISOU  555  O   GLN A 251    10865  13309  10932   -746  -2351    231       O  
ATOM    556  CB  GLN A 251       2.588 -45.412 -32.069  1.00 86.21           C  
ANISOU  556  CB  GLN A 251    10852  12129   9774  -1046  -2306     36       C  
ATOM    557  CG  GLN A 251       3.646 -45.644 -33.134  1.00 96.94           C  
ANISOU  557  CG  GLN A 251    12563  13311  10957  -1023  -2236    -33       C  
ATOM    558  CD  GLN A 251       3.428 -46.940 -33.905  1.00107.93           C  
ANISOU  558  CD  GLN A 251    14207  14634  12166  -1235  -2362   -104       C  
ATOM    559  OE1 GLN A 251       2.924 -47.935 -33.363  1.00108.80           O  
ANISOU  559  OE1 GLN A 251    14283  14749  12306  -1404  -2432   -133       O  
ATOM    560  NE2 GLN A 251       3.797 -46.931 -35.181  1.00111.74           N  
ANISOU  560  NE2 GLN A 251    14962  15047  12448  -1236  -2396   -132       N  
ATOM    561  N   GLU A 252       1.492 -44.900 -29.313  1.00 89.43           N  
ANISOU  561  N   GLU A 252    10609  12802  10569   -975  -2211    110       N  
ATOM    562  CA  GLU A 252       0.285 -44.978 -28.495  1.00 96.34           C  
ANISOU  562  CA  GLU A 252    11164  13895  11545  -1055  -2292    167       C  
ATOM    563  C   GLU A 252       0.211 -43.936 -27.382  1.00 93.96           C  
ANISOU  563  C   GLU A 252    10591  13691  11417   -850  -2166    196       C  
ATOM    564  O   GLU A 252      -0.869 -43.675 -26.845  1.00 94.88           O  
ANISOU  564  O   GLU A 252    10409  14027  11615   -854  -2231    253       O  
ATOM    565  CB  GLU A 252       0.163 -46.370 -27.883  1.00105.57           C  
ANISOU  565  CB  GLU A 252    12373  15036  12701  -1291  -2291    127       C  
ATOM    566  CG  GLU A 252       0.050 -47.494 -28.887  1.00111.75           C  
ANISOU  566  CG  GLU A 252    13420  15728  13314  -1520  -2441     93       C  
ATOM    567  CD  GLU A 252       0.113 -48.844 -28.216  1.00120.59           C  
ANISOU  567  CD  GLU A 252    14631  16762  14426  -1735  -2424     48       C  
ATOM    568  OE1 GLU A 252       0.232 -48.873 -26.974  1.00121.61           O  
ANISOU  568  OE1 GLU A 252    14607  16920  14680  -1706  -2294     54       O  
ATOM    569  OE2 GLU A 252       0.047 -49.871 -28.920  1.00128.62           O  
ANISOU  569  OE2 GLU A 252    15891  17674  15306  -1935  -2545      7       O  
ATOM    570  N   CYS A 253       1.353 -43.352 -27.028  1.00 90.46           N  
ANISOU  570  N   CYS A 253    10251  13094  11026   -673  -1986    154       N  
ATOM    571  CA  CYS A 253       1.398 -42.340 -25.978  1.00 88.97           C  
ANISOU  571  CA  CYS A 253     9854  12963  10989   -474  -1864    166       C  
ATOM    572  C   CYS A 253       0.973 -40.968 -26.490  1.00 95.04           C  
ANISOU  572  C   CYS A 253    10524  13800  11787   -275  -1938    230       C  
ATOM    573  O   CYS A 253       1.073 -40.689 -27.680  1.00 99.43           O  
ANISOU  573  O   CYS A 253    11239  14299  12242   -263  -2036    261       O  
ATOM    574  CB  CYS A 253       2.797 -42.261 -25.381  1.00 84.94           C  
ANISOU  574  CB  CYS A 253     9495  12258  10521   -382  -1662     98       C  
ATOM    575  SG  CYS A 253       3.235 -43.685 -24.382  1.00 84.06           S  
ANISOU  575  SG  CYS A 253     9441  12078  10420   -556  -1565     32       S  
ATOM    576  N   LYS A 254       0.517 -40.110 -25.580  1.00 94.32           N  
ANISOU  576  N   LYS A 254    10188  13822  11826   -112  -1889    249       N  
ATOM    577  CA  LYS A 254      -0.032 -38.812 -25.955  1.00 96.31           C  
ANISOU  577  CA  LYS A 254    10327  14143  12121     97  -1974    312       C  
ATOM    578  C   LYS A 254       0.253 -37.693 -24.952  1.00 87.17           C  
ANISOU  578  C   LYS A 254     9065  12957  11098    335  -1838    290       C  
ATOM    579  O   LYS A 254      -0.196 -36.564 -25.133  1.00 87.74           O  
ANISOU  579  O   LYS A 254     9051  13067  11220    536  -1902    335       O  
ATOM    580  CB  LYS A 254      -1.540 -38.938 -26.156  1.00106.20           C  
ANISOU  580  CB  LYS A 254    11313  15658  13379     46  -2157    378       C  
ATOM    581  CG  LYS A 254      -2.250 -39.567 -24.987  1.00113.60           C  
ANISOU  581  CG  LYS A 254    11981  16789  14391    -50  -2103    360       C  
ATOM    582  CD  LYS A 254      -3.478 -40.335 -25.436  1.00122.30           C  
ANISOU  582  CD  LYS A 254    12910  18118  15442   -254  -2291    419       C  
ATOM    583  CE  LYS A 254      -4.098 -41.106 -24.275  1.00128.67           C  
ANISOU  583  CE  LYS A 254    13471  19113  16303   -404  -2222    409       C  
ATOM    584  NZ  LYS A 254      -5.179 -42.035 -24.719  1.00130.42           N  
ANISOU  584  NZ  LYS A 254    13554  19536  16463   -670  -2405    468       N  
ATOM    585  N   LYS A 255       0.998 -38.010 -23.900  1.00 79.87           N  
ANISOU  585  N   LYS A 255     8165  11956  10227    316  -1662    220       N  
ATOM    586  CA  LYS A 255       1.379 -37.032 -22.886  1.00 71.44           C  
ANISOU  586  CA  LYS A 255     7033  10840   9270    518  -1529    184       C  
ATOM    587  C   LYS A 255       2.844 -37.247 -22.521  1.00 65.31           C  
ANISOU  587  C   LYS A 255     6474   9848   8491    485  -1371    123       C  
ATOM    588  O   LYS A 255       3.177 -37.721 -21.440  1.00 70.75           O  
ANISOU  588  O   LYS A 255     7120  10539   9223    439  -1252     69       O  
ATOM    589  CB  LYS A 255       0.478 -37.150 -21.661  1.00 68.23           C  
ANISOU  589  CB  LYS A 255     6336  10645   8944    542  -1482    165       C  
ATOM    590  CG  LYS A 255      -0.239 -35.876 -21.340  1.00 69.57           C  
ANISOU  590  CG  LYS A 255     6319  10912   9200    801  -1504    179       C  
ATOM    591  CD  LYS A 255      -1.734 -36.066 -21.162  1.00 84.25           C  
ANISOU  591  CD  LYS A 255     7853  13073  11083    796  -1596    219       C  
ATOM    592  CE  LYS A 255      -2.412 -34.704 -20.965  1.00 87.94           C  
ANISOU  592  CE  LYS A 255     8152  13621  11639   1105  -1626    228       C  
ATOM    593  NZ  LYS A 255      -3.807 -34.787 -20.456  1.00 91.54           N  
ANISOU  593  NZ  LYS A 255     8236  14404  12141   1148  -1661    247       N  
ATOM    594  N   ILE A 256       3.715 -36.889 -23.452  1.00 64.80           N  
ANISOU  594  N   ILE A 256     6640   9610   8371    506  -1375    138       N  
ATOM    595  CA  ILE A 256       5.114 -37.291 -23.424  1.00 63.39           C  
ANISOU  595  CA  ILE A 256     6670   9249   8165    441  -1247     89       C  
ATOM    596  C   ILE A 256       6.034 -36.202 -22.901  1.00 63.60           C  
ANISOU  596  C   ILE A 256     6756   9140   8271    592  -1135     71       C  
ATOM    597  O   ILE A 256       6.009 -35.071 -23.374  1.00 62.71           O  
ANISOU  597  O   ILE A 256     6686   8971   8170    722  -1181    117       O  
ATOM    598  CB  ILE A 256       5.602 -37.685 -24.839  1.00 63.36           C  
ANISOU  598  CB  ILE A 256     6894   9153   8029    345  -1301    113       C  
ATOM    599  CG1 ILE A 256       4.573 -38.585 -25.517  1.00 68.64           C  
ANISOU  599  CG1 ILE A 256     7524   9951   8606    199  -1454    138       C  
ATOM    600  CG2 ILE A 256       6.976 -38.326 -24.785  1.00 61.88           C  
ANISOU  600  CG2 ILE A 256     6888   8814   7810    274  -1162     53       C  
ATOM    601  CD1 ILE A 256       4.956 -39.006 -26.921  1.00 66.81           C  
ANISOU  601  CD1 ILE A 256     7529   9636   8219    103  -1517    151       C  
ATOM    602  N   ILE A 257       6.869 -36.557 -21.940  1.00 60.59           N  
ANISOU  602  N   ILE A 257     6391   8694   7938    564  -1001      9       N  
ATOM    603  CA  ILE A 257       7.881 -35.636 -21.449  1.00 61.82           C  
ANISOU  603  CA  ILE A 257     6620   8710   8160    670   -900    -12       C  
ATOM    604  C   ILE A 257       9.233 -35.960 -22.062  1.00 58.75           C  
ANISOU  604  C   ILE A 257     6428   8176   7717    592   -824    -20       C  
ATOM    605  O   ILE A 257       9.706 -37.086 -21.975  1.00 71.49           O  
ANISOU  605  O   ILE A 257     8087   9780   9296    479   -773    -60       O  
ATOM    606  CB  ILE A 257       7.981 -35.678 -19.911  1.00 63.58           C  
ANISOU  606  CB  ILE A 257     6724   8963   8470    704   -804    -75       C  
ATOM    607  CG1 ILE A 257       6.724 -35.091 -19.279  1.00 65.99           C  
ANISOU  607  CG1 ILE A 257     6829   9415   8829    823   -852    -73       C  
ATOM    608  CG2 ILE A 257       9.167 -34.889 -19.435  1.00 59.19           C  
ANISOU  608  CG2 ILE A 257     6267   8253   7971    772   -710   -102       C  
ATOM    609  CD1 ILE A 257       6.767 -35.109 -17.786  1.00 69.06           C  
ANISOU  609  CD1 ILE A 257     7113   9847   9279    857   -753   -137       C  
ATOM    610  N   VAL A 258       9.853 -34.973 -22.691  1.00 58.96           N  
ANISOU  610  N   VAL A 258     6575   8090   7735    654   -815     20       N  
ATOM    611  CA  VAL A 258      11.153 -35.186 -23.317  1.00 66.85           C  
ANISOU  611  CA  VAL A 258     7741   8979   8680    585   -728     20       C  
ATOM    612  C   VAL A 258      12.211 -34.304 -22.675  1.00 61.43           C  
ANISOU  612  C   VAL A 258     7083   8180   8077    638   -631     11       C  
ATOM    613  O   VAL A 258      12.083 -33.093 -22.677  1.00 67.56           O  
ANISOU  613  O   VAL A 258     7879   8899   8893    728   -667     52       O  
ATOM    614  CB  VAL A 258      11.109 -34.906 -24.837  1.00 63.56           C  
ANISOU  614  CB  VAL A 258     7472   8536   8143    560   -794     90       C  
ATOM    615  CG1 VAL A 258      12.426 -35.297 -25.482  1.00 59.18           C  
ANISOU  615  CG1 VAL A 258     7071   7902   7514    481   -680     79       C  
ATOM    616  CG2 VAL A 258       9.970 -35.670 -25.463  1.00 60.49           C  
ANISOU  616  CG2 VAL A 258     7053   8262   7670    503   -920    103       C  
ATOM    617  N   LEU A 259      13.252 -34.919 -22.125  1.00 59.59           N  
ANISOU  617  N   LEU A 259     6860   7911   7871    582   -520    -42       N  
ATOM    618  CA  LEU A 259      14.366 -34.193 -21.521  1.00 59.79           C  
ANISOU  618  CA  LEU A 259     6905   7840   7971    603   -433    -51       C  
ATOM    619  C   LEU A 259      15.555 -34.186 -22.465  1.00 69.11           C  
ANISOU  619  C   LEU A 259     8208   8957   9091    537   -355    -19       C  
ATOM    620  O   LEU A 259      16.005 -35.242 -22.894  1.00 72.58           O  
ANISOU  620  O   LEU A 259     8683   9426   9469    476   -301    -49       O  
ATOM    621  CB  LEU A 259      14.779 -34.821 -20.190  1.00 59.67           C  
ANISOU  621  CB  LEU A 259     6797   7842   8032    590   -369   -124       C  
ATOM    622  CG  LEU A 259      13.970 -34.606 -18.916  1.00 68.12           C  
ANISOU  622  CG  LEU A 259     7744   8965   9174    656   -400   -162       C  
ATOM    623  CD1 LEU A 259      12.555 -35.067 -19.102  1.00 66.06           C  
ANISOU  623  CD1 LEU A 259     7402   8825   8874    665   -484   -155       C  
ATOM    624  CD2 LEU A 259      14.621 -35.367 -17.775  1.00 78.35           C  
ANISOU  624  CD2 LEU A 259     8990  10267  10514    614   -331   -222       C  
ATOM    625  N   THR A 260      16.069 -33.000 -22.786  1.00 68.73           N  
ANISOU  625  N   THR A 260     8233   8825   9057    549   -346     40       N  
ATOM    626  CA  THR A 260      17.167 -32.893 -23.743  1.00 66.51           C  
ANISOU  626  CA  THR A 260     8060   8507   8706    473   -261     85       C  
ATOM    627  C   THR A 260      18.397 -32.168 -23.204  1.00 65.35           C  
ANISOU  627  C   THR A 260     7905   8287   8639    438   -178     96       C  
ATOM    628  O   THR A 260      18.291 -31.231 -22.414  1.00 63.82           O  
ANISOU  628  O   THR A 260     7692   8022   8534    478   -221    101       O  
ATOM    629  CB  THR A 260      16.706 -32.189 -25.038  1.00 67.82           C  
ANISOU  629  CB  THR A 260     8357   8647   8765    468   -331    179       C  
ATOM    630  OG1 THR A 260      16.258 -30.859 -24.751  1.00 71.99           O  
ANISOU  630  OG1 THR A 260     8909   9089   9356    536   -418    233       O  
ATOM    631  CG2 THR A 260      15.572 -32.954 -25.672  1.00 70.39           C  
ANISOU  631  CG2 THR A 260     8691   9056   9000    481   -424    172       C  
ATOM    632  N   GLY A 261      19.567 -32.627 -23.636  1.00 62.46           N  
ANISOU  632  N   GLY A 261     7552   7942   8236    365    -60     96       N  
ATOM    633  CA  GLY A 261      20.827 -32.026 -23.246  1.00 62.13           C  
ANISOU  633  CA  GLY A 261     7484   7860   8263    305     22    117       C  
ATOM    634  C   GLY A 261      21.673 -31.629 -24.441  1.00 73.00           C  
ANISOU  634  C   GLY A 261     8951   9241   9547    215    107    198       C  
ATOM    635  O   GLY A 261      21.168 -31.485 -25.559  1.00 74.93           O  
ANISOU  635  O   GLY A 261     9312   9487   9670    205     79    255       O  
ATOM    636  N   ALA A 262      22.969 -31.455 -24.193  1.00 75.96           N  
ANISOU  636  N   ALA A 262     9263   9628   9970    141    211    209       N  
ATOM    637  CA  ALA A 262      23.927 -31.008 -25.202  1.00 77.24           C  
ANISOU  637  CA  ALA A 262     9480   9814  10052     33    316    294       C  
ATOM    638  C   ALA A 262      23.899 -31.871 -26.448  1.00 84.44           C  
ANISOU  638  C   ALA A 262    10459  10818  10805     37    395    289       C  
ATOM    639  O   ALA A 262      24.256 -31.419 -27.541  1.00 91.46           O  
ANISOU  639  O   ALA A 262    11448  11725  11576    -42    456    373       O  
ATOM    640  CB  ALA A 262      25.324 -31.001 -24.621  1.00 79.40           C  
ANISOU  640  CB  ALA A 262     9620  10135  10415    -39    422    286       C  
ATOM    641  N   GLY A 263      23.481 -33.117 -26.267  1.00 81.97           N  
ANISOU  641  N   GLY A 263    10108  10557  10480    123    392    189       N  
ATOM    642  CA  GLY A 263      23.450 -34.084 -27.340  1.00 85.94           C  
ANISOU  642  CA  GLY A 263    10689  11134  10831    138    460    156       C  
ATOM    643  C   GLY A 263      22.610 -33.660 -28.521  1.00 82.17           C  
ANISOU  643  C   GLY A 263    10384  10638  10201    111    390    228       C  
ATOM    644  O   GLY A 263      22.971 -33.907 -29.665  1.00 87.13           O  
ANISOU  644  O   GLY A 263    11110  11322  10672     72    479    248       O  
ATOM    645  N   VAL A 264      21.488 -33.013 -28.246  1.00 73.19           N  
ANISOU  645  N   VAL A 264     9282   9426   9101    140    229    266       N  
ATOM    646  CA  VAL A 264      20.551 -32.656 -29.298  1.00 73.46           C  
ANISOU  646  CA  VAL A 264     9469   9443   8999    133    126    336       C  
ATOM    647  C   VAL A 264      21.174 -31.639 -30.261  1.00 75.70           C  
ANISOU  647  C   VAL A 264     9877   9704   9182     37    182    461       C  
ATOM    648  O   VAL A 264      20.855 -31.615 -31.452  1.00 81.16           O  
ANISOU  648  O   VAL A 264    10720  10417   9700      3    162    517       O  
ATOM    649  CB  VAL A 264      19.230 -32.121 -28.695  1.00 68.95           C  
ANISOU  649  CB  VAL A 264     8877   8810   8512    208    -60    350       C  
ATOM    650  CG1 VAL A 264      18.360 -31.527 -29.746  1.00 69.90           C  
ANISOU  650  CG1 VAL A 264     9144   8906   8509    208   -181    444       C  
ATOM    651  CG2 VAL A 264      18.479 -33.246 -28.042  1.00 69.14           C  
ANISOU  651  CG2 VAL A 264     8802   8886   8582    272   -112    244       C  
ATOM    652  N   SER A 265      22.123 -30.858 -29.762  1.00 73.42           N  
ANISOU  652  N   SER A 265     9531   9377   8988    -26    255    506       N  
ATOM    653  CA  SER A 265      22.671 -29.753 -30.534  1.00 79.26           C  
ANISOU  653  CA  SER A 265    10390  10077   9649   -142    290    643       C  
ATOM    654  C   SER A 265      24.124 -29.956 -30.982  1.00 90.08           C  
ANISOU  654  C   SER A 265    11714  11552  10960   -252    502    660       C  
ATOM    655  O   SER A 265      24.822 -28.986 -31.288  1.00 96.59           O  
ANISOU  655  O   SER A 265    12586  12350  11765   -380    553    775       O  
ATOM    656  CB  SER A 265      22.550 -28.469 -29.716  1.00 73.11           C  
ANISOU  656  CB  SER A 265     9614   9153   9012   -155    184    707       C  
ATOM    657  OG  SER A 265      21.227 -28.327 -29.212  1.00 69.71           O  
ANISOU  657  OG  SER A 265     9193   8648   8646    -25      7    675       O  
ATOM    658  N   VAL A 266      24.574 -31.208 -31.041  1.00 87.54           N  
ANISOU  658  N   VAL A 266    11303  11351  10606   -203    625    550       N  
ATOM    659  CA  VAL A 266      25.965 -31.494 -31.391  1.00 86.44           C  
ANISOU  659  CA  VAL A 266    11081  11338  10425   -273    839    549       C  
ATOM    660  C   VAL A 266      26.195 -31.335 -32.891  1.00 93.54           C  
ANISOU  660  C   VAL A 266    12141  12309  11090   -359    939    631       C  
ATOM    661  O   VAL A 266      27.295 -30.983 -33.330  1.00 95.83           O  
ANISOU  661  O   VAL A 266    12394  12690  11327   -470   1103    698       O  
ATOM    662  CB  VAL A 266      26.387 -32.918 -30.950  1.00 76.55           C  
ANISOU  662  CB  VAL A 266     9690  10181   9216   -160    936    396       C  
ATOM    663  CG1 VAL A 266      27.886 -33.113 -31.100  1.00 68.36           C  
ANISOU  663  CG1 VAL A 266     8514   9283   8177   -207   1151    393       C  
ATOM    664  CG2 VAL A 266      26.012 -33.146 -29.521  1.00 68.76           C  
ANISOU  664  CG2 VAL A 266     8575   9122   8429    -79    822    321       C  
ATOM    665  N   SER A 267      25.149 -31.581 -33.673  1.00 94.11           N  
ANISOU  665  N   SER A 267    12389  12352  11015   -317    836    632       N  
ATOM    666  CA  SER A 267      25.235 -31.445 -35.126  1.00 99.16           C  
ANISOU  666  CA  SER A 267    13216  13054  11405   -396    908    710       C  
ATOM    667  C   SER A 267      25.039 -30.006 -35.590  1.00109.31           C  
ANISOU  667  C   SER A 267    14647  14245  12640   -522    822    894       C  
ATOM    668  O   SER A 267      25.202 -29.704 -36.768  1.00117.95           O  
ANISOU  668  O   SER A 267    15907  15386  13523   -616    882    989       O  
ATOM    669  CB  SER A 267      24.195 -32.336 -35.806  1.00 93.81           C  
ANISOU  669  CB  SER A 267    12682  12383  10577   -310    815    635       C  
ATOM    670  OG  SER A 267      22.876 -31.894 -35.518  1.00 91.15           O  
ANISOU  670  OG  SER A 267    12409  11926  10300   -267    573    672       O  
ATOM    671  N   CYS A 268      24.686 -29.122 -34.663  1.00109.67           N  
ANISOU  671  N   CYS A 268    14651  14151  12870   -519    678    942       N  
ATOM    672  CA  CYS A 268      24.242 -27.780 -35.015  1.00107.91           C  
ANISOU  672  CA  CYS A 268    14598  13788  12612   -599    541   1105       C  
ATOM    673  C   CYS A 268      25.389 -26.791 -35.188  1.00111.64           C  
ANISOU  673  C   CYS A 268    15085  14255  13077   -789    658   1240       C  
ATOM    674  O   CYS A 268      25.165 -25.630 -35.517  1.00113.06           O  
ANISOU  674  O   CYS A 268    15432  14303  13221   -879    555   1390       O  
ATOM    675  CB  CYS A 268      23.270 -27.262 -33.957  1.00106.83           C  
ANISOU  675  CB  CYS A 268    14431  13493  12669   -489    328   1085       C  
ATOM    676  SG  CYS A 268      21.795 -28.274 -33.750  1.00100.46           S  
ANISOU  676  SG  CYS A 268    13596  12701  11872   -296    169    956       S  
ATOM    677  N   GLY A 269      26.615 -27.249 -34.961  1.00115.26           N  
ANISOU  677  N   GLY A 269    15366  14855  13571   -852    867   1192       N  
ATOM    678  CA  GLY A 269      27.790 -26.426 -35.197  1.00117.50           C  
ANISOU  678  CA  GLY A 269    15632  15179  13834  -1059   1001   1321       C  
ATOM    679  C   GLY A 269      27.931 -25.213 -34.292  1.00122.29           C  
ANISOU  679  C   GLY A 269    16230  15612  14622  -1152    881   1406       C  
ATOM    680  O   GLY A 269      28.521 -24.202 -34.674  1.00127.64           O  
ANISOU  680  O   GLY A 269    16999  16247  15251  -1351    911   1563       O  
ATOM    681  N   ILE A 270      27.395 -25.320 -33.085  1.00120.21           N  
ANISOU  681  N   ILE A 270    15870  15245  14558  -1016    746   1300       N  
ATOM    682  CA  ILE A 270      27.484 -24.253 -32.102  1.00115.64           C  
ANISOU  682  CA  ILE A 270    15291  14491  14155  -1077    625   1347       C  
ATOM    683  C   ILE A 270      28.861 -24.203 -31.450  1.00122.82           C  
ANISOU  683  C   ILE A 270    15992  15495  15179  -1218    763   1341       C  
ATOM    684  O   ILE A 270      29.356 -25.222 -30.978  1.00120.97           O  
ANISOU  684  O   ILE A 270    15537  15415  15010  -1142    874   1216       O  
ATOM    685  CB  ILE A 270      26.421 -24.440 -31.018  1.00106.61           C  
ANISOU  685  CB  ILE A 270    14111  13228  13168   -873    447   1224       C  
ATOM    686  CG1 ILE A 270      25.029 -24.417 -31.644  1.00 98.86           C  
ANISOU  686  CG1 ILE A 270    13311  12167  12086   -739    294   1241       C  
ATOM    687  CG2 ILE A 270      26.562 -23.387 -29.936  1.00109.12           C  
ANISOU  687  CG2 ILE A 270    14435  13367  13660   -923    332   1247       C  
ATOM    688  CD1 ILE A 270      23.938 -24.795 -30.684  1.00 90.07           C  
ANISOU  688  CD1 ILE A 270    12125  10994  11104   -532    149   1113       C  
ATOM    689  N   PRO A 271      29.489 -23.016 -31.429  1.00133.18           N  
ANISOU  689  N   PRO A 271    17375  16712  16515  -1430    746   1481       N  
ATOM    690  CA  PRO A 271      30.760 -22.853 -30.712  1.00136.75           C  
ANISOU  690  CA  PRO A 271    17621  17245  17094  -1585    843   1485       C  
ATOM    691  C   PRO A 271      30.620 -23.196 -29.233  1.00132.98           C  
ANISOU  691  C   PRO A 271    16981  16717  16828  -1450    749   1334       C  
ATOM    692  O   PRO A 271      29.722 -22.677 -28.568  1.00128.82           O  
ANISOU  692  O   PRO A 271    16577  15984  16385  -1354    559   1303       O  
ATOM    693  CB  PRO A 271      31.084 -21.366 -30.898  1.00139.07           C  
ANISOU  693  CB  PRO A 271    18097  17368  17376  -1830    766   1667       C  
ATOM    694  CG  PRO A 271      30.347 -20.970 -32.127  1.00140.73           C  
ANISOU  694  CG  PRO A 271    18582  17500  17390  -1836    722   1786       C  
ATOM    695  CD  PRO A 271      29.083 -21.780 -32.119  1.00137.35           C  
ANISOU  695  CD  PRO A 271    18188  17053  16945  -1550    630   1655       C  
ATOM    696  N   ASP A 272      31.487 -24.069 -28.730  1.00135.98           N  
ANISOU  696  N   ASP A 272    17094  17289  17286  -1432    879   1242       N  
ATOM    697  CA  ASP A 272      31.455 -24.413 -27.315  1.00136.73           C  
ANISOU  697  CA  ASP A 272    17036  17347  17567  -1322    793   1110       C  
ATOM    698  C   ASP A 272      31.964 -23.226 -26.507  1.00135.18           C  
ANISOU  698  C   ASP A 272    16862  17008  17494  -1504    688   1178       C  
ATOM    699  O   ASP A 272      32.721 -22.392 -27.007  1.00137.19           O  
ANISOU  699  O   ASP A 272    17159  17262  17705  -1743    734   1321       O  
ATOM    700  CB  ASP A 272      32.276 -25.674 -27.025  1.00136.69           C  
ANISOU  700  CB  ASP A 272    16749  17578  17607  -1246    948   1003       C  
ATOM    701  CG  ASP A 272      33.768 -25.422 -27.047  1.00138.21           C  
ANISOU  701  CG  ASP A 272    16746  17932  17836  -1453   1084   1079       C  
ATOM    702  OD1 ASP A 272      34.231 -24.622 -27.886  1.00142.86           O  
ANISOU  702  OD1 ASP A 272    17415  18536  18328  -1660   1151   1227       O  
ATOM    703  OD2 ASP A 272      34.476 -26.024 -26.216  1.00135.56           O  
ANISOU  703  OD2 ASP A 272    16170  17713  17624  -1412   1120    997       O  
ATOM    704  N   PHE A 273      31.547 -23.153 -25.254  1.00131.45           N  
ANISOU  704  N   PHE A 273    16371  16412  17163  -1403    544   1076       N  
ATOM    705  CA  PHE A 273      31.769 -21.950 -24.479  1.00130.44           C  
ANISOU  705  CA  PHE A 273    16336  16093  17133  -1549    405   1124       C  
ATOM    706  C   PHE A 273      32.073 -22.234 -23.023  1.00136.89           C  
ANISOU  706  C   PHE A 273    16989  16915  18108  -1500    339   1001       C  
ATOM    707  O   PHE A 273      32.402 -21.319 -22.266  1.00145.19           O  
ANISOU  707  O   PHE A 273    18098  17823  19244  -1633    225   1022       O  
ATOM    708  CB  PHE A 273      30.549 -21.043 -24.580  1.00124.59           C  
ANISOU  708  CB  PHE A 273    15893  15085  16361  -1470    232   1153       C  
ATOM    709  CG  PHE A 273      29.238 -21.760 -24.411  1.00115.41           C  
ANISOU  709  CG  PHE A 273    14759  13904  15188  -1184    172   1032       C  
ATOM    710  CD1 PHE A 273      28.692 -21.949 -23.148  1.00114.59           C  
ANISOU  710  CD1 PHE A 273    14608  13730  15200  -1028     67    895       C  
ATOM    711  CD2 PHE A 273      28.541 -22.226 -25.516  1.00104.36           C  
ANISOU  711  CD2 PHE A 273    13436  12563  13653  -1085    215   1060       C  
ATOM    712  CE1 PHE A 273      27.479 -22.599 -22.987  1.00109.30           C  
ANISOU  712  CE1 PHE A 273    13947  13062  14518   -786     17    794       C  
ATOM    713  CE2 PHE A 273      27.331 -22.873 -25.362  1.00101.48           C  
ANISOU  713  CE2 PHE A 273    13085  12191  13281   -847    149    957       C  
ATOM    714  CZ  PHE A 273      26.798 -23.060 -24.094  1.00105.52           C  
ANISOU  714  CZ  PHE A 273    13530  12645  13916   -701     54    828       C  
ATOM    715  N   ARG A 274      31.960 -23.500 -22.633  1.00131.37           N  
ANISOU  715  N   ARG A 274    16107  16368  17439  -1316    399    874       N  
ATOM    716  CA  ARG A 274      32.222 -23.885 -21.253  1.00128.71           C  
ANISOU  716  CA  ARG A 274    15618  16048  17236  -1258    335    760       C  
ATOM    717  C   ARG A 274      33.712 -24.134 -21.053  1.00126.73           C  
ANISOU  717  C   ARG A 274    15114  15988  17049  -1418    434    792       C  
ATOM    718  O   ARG A 274      34.274 -23.803 -20.004  1.00127.57           O  
ANISOU  718  O   ARG A 274    15140  16066  17265  -1506    347    767       O  
ATOM    719  CB  ARG A 274      31.402 -25.123 -20.873  1.00128.04           C  
ANISOU  719  CB  ARG A 274    15468  16027  17155   -997    339    621       C  
ATOM    720  CG  ARG A 274      29.909 -24.946 -21.098  1.00127.99           C  
ANISOU  720  CG  ARG A 274    15669  15872  17089   -838    246    593       C  
ATOM    721  CD  ARG A 274      29.074 -25.919 -20.284  1.00124.94           C  
ANISOU  721  CD  ARG A 274    15222  15510  16739   -622    203    453       C  
ATOM    722  NE  ARG A 274      27.657 -25.558 -20.331  1.00131.82           N  
ANISOU  722  NE  ARG A 274    16268  16242  17573   -487     95    430       N  
ATOM    723  CZ  ARG A 274      26.707 -26.131 -19.597  1.00137.72           C  
ANISOU  723  CZ  ARG A 274    16996  16985  18347   -314     35    323       C  
ATOM    724  NH1 ARG A 274      25.442 -25.731 -19.703  1.00137.79           N  
ANISOU  724  NH1 ARG A 274    17142  16889  18325   -194    -57    312       N  
ATOM    725  NH2 ARG A 274      27.019 -27.105 -18.752  1.00140.52           N  
ANISOU  725  NH2 ARG A 274    17189  17445  18757   -262     65    233       N  
ATOM    726  N   SER A 275      34.346 -24.698 -22.079  1.00126.04           N  
ANISOU  726  N   SER A 275    14902  16104  16885  -1454    615    846       N  
ATOM    727  CA  SER A 275      35.771 -25.011 -22.046  1.00126.04           C  
ANISOU  727  CA  SER A 275    14625  16329  16936  -1584    736    881       C  
ATOM    728  C   SER A 275      36.632 -23.757 -22.078  1.00138.05           C  
ANISOU  728  C   SER A 275    16157  17812  18485  -1896    707   1020       C  
ATOM    729  O   SER A 275      36.304 -22.795 -22.773  1.00146.15           O  
ANISOU  729  O   SER A 275    17406  18697  19428  -2031    680   1130       O  
ATOM    730  CB  SER A 275      36.128 -25.917 -23.221  1.00118.50           C  
ANISOU  730  CB  SER A 275    13557  15599  15870  -1517    953    894       C  
ATOM    731  OG  SER A 275      35.494 -25.462 -24.403  1.00116.90           O  
ANISOU  731  OG  SER A 275    13582  15321  15515  -1553    992    978       O  
ATOM    732  N   ARG A 276      37.733 -23.769 -21.329  1.00144.66           N  
ANISOU  732  N   ARG A 276    16757  18772  19437  -2020    699   1022       N  
ATOM    733  CA  ARG A 276      38.660 -22.638 -21.320  1.00154.90           C  
ANISOU  733  CA  ARG A 276    18032  20057  20767  -2351    667   1159       C  
ATOM    734  C   ARG A 276      39.173 -22.389 -22.732  1.00159.84           C  
ANISOU  734  C   ARG A 276    18642  20824  21267  -2518    854   1306       C  
ATOM    735  O   ARG A 276      39.450 -21.256 -23.128  1.00161.53           O  
ANISOU  735  O   ARG A 276    18990  20942  21444  -2792    823   1450       O  
ATOM    736  CB  ARG A 276      39.826 -22.885 -20.359  1.00160.75           C  
ANISOU  736  CB  ARG A 276    18465  20966  21648  -2446    642   1135       C  
ATOM    737  CG  ARG A 276      40.793 -21.713 -20.251  1.00166.87           C  
ANISOU  737  CG  ARG A 276    19207  21730  22467  -2818    585   1275       C  
ATOM    738  CD  ARG A 276      41.723 -21.868 -19.065  1.00170.36           C  
ANISOU  738  CD  ARG A 276    19389  22283  23056  -2898    489   1233       C  
ATOM    739  NE  ARG A 276      40.988 -21.903 -17.803  1.00171.38           N  
ANISOU  739  NE  ARG A 276    19660  22204  23253  -2744    286   1096       N  
ATOM    740  CZ  ARG A 276      40.686 -20.826 -17.083  1.00173.75           C  
ANISOU  740  CZ  ARG A 276    20197  22237  23581  -2887     84   1097       C  
ATOM    741  NH1 ARG A 276      41.056 -19.620 -17.501  1.00174.02           N  
ANISOU  741  NH1 ARG A 276    20368  22160  23591  -3198     43   1235       N  
ATOM    742  NH2 ARG A 276      40.012 -20.955 -15.945  1.00172.71           N  
ANISOU  742  NH2 ARG A 276    20181  21946  23494  -2722    -75    960       N  
ATOM    743  N   ASP A 277      39.278 -23.472 -23.490  1.00160.01           N  
ANISOU  743  N   ASP A 277    18518  21066  21212  -2352   1047   1268       N  
ATOM    744  CA  ASP A 277      39.589 -23.399 -24.906  1.00164.12           C  
ANISOU  744  CA  ASP A 277    19053  21730  21577  -2456   1245   1384       C  
ATOM    745  C   ASP A 277      38.311 -23.545 -25.729  1.00161.01           C  
ANISOU  745  C   ASP A 277    18952  21189  21034  -2284   1243   1363       C  
ATOM    746  O   ASP A 277      37.805 -24.649 -25.913  1.00161.84           O  
ANISOU  746  O   ASP A 277    19028  21364  21099  -2021   1306   1243       O  
ATOM    747  CB  ASP A 277      40.600 -24.480 -25.279  1.00169.29           C  
ANISOU  747  CB  ASP A 277    19358  22738  22225  -2381   1474   1350       C  
ATOM    748  CG  ASP A 277      40.722 -24.669 -26.770  1.00174.92           C  
ANISOU  748  CG  ASP A 277    20107  23609  22744  -2406   1701   1427       C  
ATOM    749  OD1 ASP A 277      40.671 -23.657 -27.507  1.00178.63           O  
ANISOU  749  OD1 ASP A 277    20766  23999  23107  -2641   1709   1580       O  
ATOM    750  OD2 ASP A 277      40.856 -25.834 -27.201  1.00174.75           O  
ANISOU  750  OD2 ASP A 277    19945  23783  22669  -2187   1865   1331       O  
ATOM    751  N   GLY A 278      37.788 -22.426 -26.219  1.00153.57           N  
ANISOU  751  N   GLY A 278    18301  20036  20012  -2437   1154   1482       N  
ATOM    752  CA  GLY A 278      36.547 -22.438 -26.969  1.00144.98           C  
ANISOU  752  CA  GLY A 278    17498  18798  18788  -2286   1118   1477       C  
ATOM    753  C   GLY A 278      36.228 -21.056 -27.484  1.00141.14           C  
ANISOU  753  C   GLY A 278    17314  18088  18227  -2498   1015   1641       C  
ATOM    754  O   GLY A 278      37.023 -20.470 -28.219  1.00143.95           O  
ANISOU  754  O   GLY A 278    17664  18529  18500  -2762   1120   1799       O  
ATOM    755  N   ILE A 279      35.069 -20.525 -27.103  1.00142.79           N  
ANISOU  755  N   ILE A 279    16956  15535  21764  -1051   -359    993       N  
ATOM    756  CA  ILE A 279      34.751 -19.148 -27.452  1.00135.32           C  
ANISOU  756  CA  ILE A 279    16154  14300  20962  -1118   -406    956       C  
ATOM    757  C   ILE A 279      35.510 -18.219 -26.527  1.00134.63           C  
ANISOU  757  C   ILE A 279    15832  14073  21250  -1322   -670    822       C  
ATOM    758  O   ILE A 279      35.841 -17.100 -26.901  1.00138.64           O  
ANISOU  758  O   ILE A 279    16337  14281  22059  -1448   -650    879       O  
ATOM    759  CB  ILE A 279      33.248 -18.835 -27.369  1.00129.57           C  
ANISOU  759  CB  ILE A 279    15738  13595  19897   -970   -536    755       C  
ATOM    760  CG1 ILE A 279      32.959 -17.541 -28.129  1.00133.10           C  
ANISOU  760  CG1 ILE A 279    16361  13715  20498  -1003   -479    821       C  
ATOM    761  CG2 ILE A 279      32.795 -18.694 -25.925  1.00126.14           C  
ANISOU  761  CG2 ILE A 279    15256  13299  19372   -973   -894    422       C  
ATOM    762  CD1 ILE A 279      31.500 -17.184 -28.213  1.00132.48           C  
ANISOU  762  CD1 ILE A 279    16577  13632  20126   -842   -575    673       C  
ATOM    763  N   TYR A 280      35.808 -18.699 -25.324  1.00131.48           N  
ANISOU  763  N   TYR A 280    15236  13888  20832  -1362   -922    651       N  
ATOM    764  CA  TYR A 280      36.571 -17.919 -24.367  1.00134.21           C  
ANISOU  764  CA  TYR A 280    15351  14137  21507  -1567  -1212    501       C  
ATOM    765  C   TYR A 280      37.953 -17.602 -24.933  1.00137.90           C  
ANISOU  765  C   TYR A 280    15537  14405  22453  -1756  -1051    768       C  
ATOM    766  O   TYR A 280      38.600 -16.641 -24.521  1.00144.54           O  
ANISOU  766  O   TYR A 280    16215  15044  23660  -1962  -1234    697       O  
ATOM    767  CB  TYR A 280      36.684 -18.667 -23.041  1.00134.66           C  
ANISOU  767  CB  TYR A 280    15249  14508  21407  -1560  -1494    313       C  
ATOM    768  CG  TYR A 280      37.559 -17.969 -22.029  1.00139.00           C  
ANISOU  768  CG  TYR A 280    15546  14994  22274  -1784  -1821    158       C  
ATOM    769  CD1 TYR A 280      37.061 -16.932 -21.253  1.00141.57           C  
ANISOU  769  CD1 TYR A 280    16000  15203  22589  -1851  -2117   -167       C  
ATOM    770  CD2 TYR A 280      38.886 -18.345 -21.850  1.00141.36           C  
ANISOU  770  CD2 TYR A 280    15474  15344  22893  -1929  -1838    332       C  
ATOM    771  CE1 TYR A 280      37.860 -16.290 -20.327  1.00147.56           C  
ANISOU  771  CE1 TYR A 280    16546  15897  23625  -2071  -2437   -334       C  
ATOM    772  CE2 TYR A 280      39.691 -17.709 -20.927  1.00146.10           C  
ANISOU  772  CE2 TYR A 280    15832  15892  23787  -2151  -2171    189       C  
ATOM    773  CZ  TYR A 280      39.173 -16.682 -20.168  1.00150.16           C  
ANISOU  773  CZ  TYR A 280    16501  16289  24262  -2228  -2477   -154       C  
ATOM    774  OH  TYR A 280      39.970 -16.044 -19.248  1.00155.49           O  
ANISOU  774  OH  TYR A 280    16955  16907  25217  -2463  -2829   -324       O  
ATOM    775  N   ALA A 281      38.390 -18.414 -25.890  1.00136.47           N  
ANISOU  775  N   ALA A 281    15302  14276  22276  -1684   -698   1071       N  
ATOM    776  CA  ALA A 281      39.658 -18.195 -26.571  1.00141.02           C  
ANISOU  776  CA  ALA A 281    15616  14673  23291  -1833   -467   1367       C  
ATOM    777  C   ALA A 281      39.644 -16.904 -27.387  1.00145.19           C  
ANISOU  777  C   ALA A 281    16270  14832  24064  -1936   -344   1465       C  
ATOM    778  O   ALA A 281      40.554 -16.082 -27.278  1.00148.04           O  
ANISOU  778  O   ALA A 281    16395  14971  24882  -2155   -404   1527       O  
ATOM    779  CB  ALA A 281      39.980 -19.378 -27.466  1.00141.88           C  
ANISOU  779  CB  ALA A 281    15699  14921  23289  -1693    -77   1649       C  
ATOM    780  N   ARG A 282      38.606 -16.731 -28.202  1.00145.24           N  
ANISOU  780  N   ARG A 282    16642  14770  23773  -1781   -182   1489       N  
ATOM    781  CA  ARG A 282      38.493 -15.565 -29.077  1.00145.54           C  
ANISOU  781  CA  ARG A 282    16837  14462  23998  -1844    -39   1622       C  
ATOM    782  C   ARG A 282      38.031 -14.329 -28.322  1.00140.30           C  
ANISOU  782  C   ARG A 282    16250  13586  23470  -1945   -380   1344       C  
ATOM    783  O   ARG A 282      38.041 -13.220 -28.856  1.00141.86           O  
ANISOU  783  O   ARG A 282    16537  13453  23912  -2032   -317   1433       O  
ATOM    784  CB  ARG A 282      37.525 -15.849 -30.224  1.00146.37           C  
ANISOU  784  CB  ARG A 282    17310  14587  23715  -1632    232   1757       C  
ATOM    785  CG  ARG A 282      37.842 -17.109 -31.003  1.00146.80           C  
ANISOU  785  CG  ARG A 282    17355  14847  23573  -1510    575   1989       C  
ATOM    786  CD  ARG A 282      36.881 -17.287 -32.162  1.00146.67           C  
ANISOU  786  CD  ARG A 282    17726  14835  23169  -1324    811   2106       C  
ATOM    787  NE  ARG A 282      35.495 -17.428 -31.721  1.00142.86           N  
ANISOU  787  NE  ARG A 282    17499  14492  22290  -1172    569   1843       N  
ATOM    788  CZ  ARG A 282      34.894 -18.594 -31.513  1.00136.04           C  
ANISOU  788  CZ  ARG A 282    16719  13919  21049  -1019    549   1736       C  
ATOM    789  NH1 ARG A 282      35.563 -19.720 -31.702  1.00137.82           N  
ANISOU  789  NH1 ARG A 282    16808  14314  21243   -990    753   1861       N  
ATOM    790  NH2 ARG A 282      33.629 -18.635 -31.118  1.00130.59           N  
ANISOU  790  NH2 ARG A 282    16240  13341  20038   -893    336   1512       N  
ATOM    791  N   LEU A 283      37.612 -14.528 -27.079  1.00135.54           N  
ANISOU  791  N   LEU A 283    15627  13170  22702  -1925   -728   1009       N  
ATOM    792  CA  LEU A 283      37.147 -13.427 -26.255  1.00136.96           C  
ANISOU  792  CA  LEU A 283    15894  13169  22975  -2003  -1057    695       C  
ATOM    793  C   LEU A 283      38.274 -12.894 -25.383  1.00144.07           C  
ANISOU  793  C   LEU A 283    16466  13960  24313  -2274  -1308    590       C  
ATOM    794  O   LEU A 283      38.374 -11.691 -25.148  1.00143.05           O  
ANISOU  794  O   LEU A 283    16351  13518  24485  -2429  -1467    462       O  
ATOM    795  CB  LEU A 283      35.965 -13.869 -25.393  1.00129.02           C  
ANISOU  795  CB  LEU A 283    15084  12424  21513  -1820  -1284    373       C  
ATOM    796  CG  LEU A 283      34.743 -14.290 -26.208  1.00123.31           C  
ANISOU  796  CG  LEU A 283    14683  11791  20377  -1566  -1083    449       C  
ATOM    797  CD1 LEU A 283      33.589 -14.706 -25.310  1.00117.96           C  
ANISOU  797  CD1 LEU A 283    14163  11368  19290  -1397  -1302    139       C  
ATOM    798  CD2 LEU A 283      34.328 -13.176 -27.157  1.00124.74           C  
ANISOU  798  CD2 LEU A 283    15080  11618  20699  -1557   -947    572       C  
ATOM    799  N   ALA A 284      39.134 -13.794 -24.920  1.00149.50           N  
ANISOU  799  N   ALA A 284    16854  14897  25053  -2333  -1350    650       N  
ATOM    800  CA  ALA A 284      40.234 -13.412 -24.042  1.00156.43           C  
ANISOU  800  CA  ALA A 284    17386  15721  26328  -2592  -1627    556       C  
ATOM    801  C   ALA A 284      41.211 -12.461 -24.734  1.00161.24           C  
ANISOU  801  C   ALA A 284    17808  15951  27504  -2827  -1484    790       C  
ATOM    802  O   ALA A 284      41.974 -11.759 -24.072  1.00166.21           O  
ANISOU  802  O   ALA A 284    18203  16424  28524  -3078  -1746    673       O  
ATOM    803  CB  ALA A 284      40.964 -14.655 -23.543  1.00158.83           C  
ANISOU  803  CB  ALA A 284    17391  16378  26578  -2580  -1664    641       C  
ATOM    804  N   VAL A 285      41.175 -12.431 -26.064  1.00162.52           N  
ANISOU  804  N   VAL A 285    18081  15966  27703  -2751  -1071   1121       N  
ATOM    805  CA  VAL A 285      42.093 -11.597 -26.834  1.00166.11           C  
ANISOU  805  CA  VAL A 285    18363  16070  28682  -2958   -870   1401       C  
ATOM    806  C   VAL A 285      41.578 -10.154 -26.961  1.00164.94           C  
ANISOU  806  C   VAL A 285    18440  15515  28716  -3045   -966   1281       C  
ATOM    807  O   VAL A 285      42.361  -9.203 -26.911  1.00168.46           O  
ANISOU  807  O   VAL A 285    18691  15641  29674  -3305  -1036   1326       O  
ATOM    808  CB  VAL A 285      42.354 -12.203 -28.243  1.00136.37           C  
ANISOU  808  CB  VAL A 285    14620  12327  24868  -2836   -351   1835       C  
ATOM    809  CG1 VAL A 285      41.052 -12.512 -28.960  1.00133.44           C  
ANISOU  809  CG1 VAL A 285    14691  12038  23972  -2555   -168   1841       C  
ATOM    810  CG2 VAL A 285      43.242 -11.287 -29.078  1.00140.13           C  
ANISOU  810  CG2 VAL A 285    14938  12432  25873  -3042   -108   2149       C  
ATOM    811  N   ASP A 286      40.265  -9.992 -27.100  1.00160.52           N  
ANISOU  811  N   ASP A 286    18276  14956  27760  -2832   -978   1129       N  
ATOM    812  CA  ASP A 286      39.663  -8.663 -27.177  1.00161.77           C  
ANISOU  812  CA  ASP A 286    18668  14731  28067  -2874  -1075   1001       C  
ATOM    813  C   ASP A 286      39.304  -8.142 -25.780  1.00165.19           C  
ANISOU  813  C   ASP A 286    19129  15145  28489  -2945  -1536    520       C  
ATOM    814  O   ASP A 286      39.240  -6.934 -25.555  1.00165.59           O  
ANISOU  814  O   ASP A 286    19249  14828  28839  -3079  -1691    367       O  
ATOM    815  CB  ASP A 286      38.417  -8.685 -28.071  1.00157.66           C  
ANISOU  815  CB  ASP A 286    18548  14204  27151  -2599   -856   1099       C  
ATOM    816  CG  ASP A 286      38.684  -9.297 -29.437  1.00155.41           C  
ANISOU  816  CG  ASP A 286    18287  13983  26778  -2505   -408   1543       C  
ATOM    817  OD1 ASP A 286      39.781  -9.067 -29.988  1.00156.37           O  
ANISOU  817  OD1 ASP A 286    18177  13937  27300  -2684   -199   1836       O  
ATOM    818  OD2 ASP A 286      37.800 -10.012 -29.958  1.00151.45           O  
ANISOU  818  OD2 ASP A 286    18035  13703  25805  -2255   -262   1595       O  
ATOM    819  N   PHE A 287      39.077  -9.065 -24.848  1.00169.36           N  
ANISOU  819  N   PHE A 287    19613  16067  28670  -2851  -1745    285       N  
ATOM    820  CA  PHE A 287      38.692  -8.718 -23.481  1.00172.64           C  
ANISOU  820  CA  PHE A 287    20080  16533  28982  -2889  -2167   -180       C  
ATOM    821  C   PHE A 287      39.566  -9.461 -22.469  1.00171.78           C  
ANISOU  821  C   PHE A 287    19646  16730  28893  -3021  -2418   -290       C  
ATOM    822  O   PHE A 287      39.174 -10.512 -21.954  1.00168.14           O  
ANISOU  822  O   PHE A 287    19207  16667  28010  -2854  -2480   -381       O  
ATOM    823  CB  PHE A 287      37.215  -9.042 -23.234  1.00173.45           C  
ANISOU  823  CB  PHE A 287    20532  16834  28538  -2591  -2201   -403       C  
ATOM    824  CG  PHE A 287      36.290  -8.527 -24.303  1.00175.72           C  
ANISOU  824  CG  PHE A 287    21126  16894  28746  -2419  -1945   -247       C  
ATOM    825  CD1 PHE A 287      36.063  -9.261 -25.457  1.00174.54           C  
ANISOU  825  CD1 PHE A 287    21054  16872  28390  -2255  -1595    106       C  
ATOM    826  CD2 PHE A 287      35.637  -7.319 -24.151  1.00180.99           C  
ANISOU  826  CD2 PHE A 287    22012  17220  29536  -2413  -2064   -455       C  
ATOM    827  CE1 PHE A 287      35.214  -8.793 -26.445  1.00174.00           C  
ANISOU  827  CE1 PHE A 287    21270  16615  28228  -2098  -1388    262       C  
ATOM    828  CE2 PHE A 287      34.784  -6.848 -25.133  1.00181.59           C  
ANISOU  828  CE2 PHE A 287    22357  17093  29546  -2243  -1845   -285       C  
ATOM    829  CZ  PHE A 287      34.573  -7.589 -26.282  1.00176.74           C  
ANISOU  829  CZ  PHE A 287    21812  16630  28710  -2089  -1517     80       C  
ATOM    830  N   PRO A 288      40.761  -8.915 -22.188  1.00171.34           N  
ANISOU  830  N   PRO A 288    19275  16484  29341  -3325  -2568   -265       N  
ATOM    831  CA  PRO A 288      41.740  -9.537 -21.287  1.00172.23           C  
ANISOU  831  CA  PRO A 288    19029  16861  29550  -3480  -2824   -323       C  
ATOM    832  C   PRO A 288      41.399  -9.406 -19.800  1.00176.91           C  
ANISOU  832  C   PRO A 288    19691  17616  29912  -3513  -3296   -803       C  
ATOM    833  O   PRO A 288      42.252  -9.690 -18.962  1.00179.86           O  
ANISOU  833  O   PRO A 288    19770  18159  30407  -3684  -3581   -884       O  
ATOM    834  CB  PRO A 288      43.036  -8.776 -21.603  1.00172.58           C  
ANISOU  834  CB  PRO A 288    18735  16576  30264  -3810  -2821   -130       C  
ATOM    835  CG  PRO A 288      42.781  -8.077 -22.905  1.00170.65           C  
ANISOU  835  CG  PRO A 288    18663  15961  30215  -3778  -2442    144       C  
ATOM    836  CD  PRO A 288      41.331  -7.752 -22.884  1.00168.59           C  
ANISOU  836  CD  PRO A 288    18860  15657  29538  -3540  -2452    -95       C  
ATOM    837  N   ASP A 289      40.180  -8.981 -19.479  1.00176.52           N  
ANISOU  837  N   ASP A 289    20019  17521  29531  -3347  -3374  -1107       N  
ATOM    838  CA  ASP A 289      39.762  -8.861 -18.086  1.00177.08           C  
ANISOU  838  CA  ASP A 289    20200  17757  29326  -3347  -3780  -1574       C  
ATOM    839  C   ASP A 289      38.944 -10.086 -17.671  1.00178.03           C  
ANISOU  839  C   ASP A 289    20452  18356  28837  -3061  -3753  -1626       C  
ATOM    840  O   ASP A 289      38.523 -10.204 -16.521  1.00180.25           O  
ANISOU  840  O   ASP A 289    20834  18855  28797  -3015  -4046  -1976       O  
ATOM    841  CB  ASP A 289      38.958  -7.574 -17.873  1.00173.84           C  
ANISOU  841  CB  ASP A 289    20110  16982  28959  -3346  -3890  -1911       C  
ATOM    842  CG  ASP A 289      38.877  -7.169 -16.411  1.00172.40           C  
ANISOU  842  CG  ASP A 289    19992  16868  28643  -3444  -4341  -2416       C  
ATOM    843  OD1 ASP A 289      39.744  -7.603 -15.623  1.00172.10           O  
ANISOU  843  OD1 ASP A 289    19690  17062  28640  -3613  -4616  -2479       O  
ATOM    844  OD2 ASP A 289      37.949  -6.411 -16.051  1.00170.74           O  
ANISOU  844  OD2 ASP A 289    20100  16483  28290  -3346  -4419  -2749       O  
ATOM    845  N   LEU A 290      38.733 -10.994 -18.621  1.00175.83           N  
ANISOU  845  N   LEU A 290    20175  18231  28402  -2874  -3393  -1275       N  
ATOM    846  CA  LEU A 290      38.015 -12.242 -18.371  1.00173.74           C  
ANISOU  846  CA  LEU A 290    20009  18397  27607  -2614  -3326  -1267       C  
ATOM    847  C   LEU A 290      38.878 -13.266 -17.637  1.00178.78           C  
ANISOU  847  C   LEU A 290    20336  19397  28195  -2681  -3497  -1205       C  
ATOM    848  O   LEU A 290      39.889 -13.718 -18.173  1.00182.33           O  
ANISOU  848  O   LEU A 290    20488  19856  28932  -2778  -3355   -883       O  
ATOM    849  CB  LEU A 290      37.528 -12.848 -19.690  1.00167.93           C  
ANISOU  849  CB  LEU A 290    19389  17674  26743  -2410  -2890   -920       C  
ATOM    850  CG  LEU A 290      36.154 -12.458 -20.233  1.00164.05           C  
ANISOU  850  CG  LEU A 290    19276  17061  25994  -2191  -2728   -991       C  
ATOM    851  CD1 LEU A 290      35.951 -13.066 -21.611  1.00160.80           C  
ANISOU  851  CD1 LEU A 290    18928  16657  25512  -2045  -2320   -608       C  
ATOM    852  CD2 LEU A 290      35.060 -12.916 -19.284  1.00161.48           C  
ANISOU  852  CD2 LEU A 290    19150  17036  25171  -1994  -2895  -1297       C  
ATOM    853  N   PRO A 291      38.482 -13.640 -16.408  1.00179.24           N  
ANISOU  853  N   PRO A 291    20461  19758  27886  -2619  -3791  -1500       N  
ATOM    854  CA  PRO A 291      39.213 -14.694 -15.695  1.00180.41           C  
ANISOU  854  CA  PRO A 291    20331  20278  27938  -2649  -3956  -1416       C  
ATOM    855  C   PRO A 291      38.816 -16.091 -16.173  1.00176.11           C  
ANISOU  855  C   PRO A 291    19802  20035  27078  -2401  -3665  -1144       C  
ATOM    856  O   PRO A 291      39.676 -16.896 -16.531  1.00177.97           O  
ANISOU  856  O   PRO A 291    19755  20384  27481  -2426  -3540   -834       O  
ATOM    857  CB  PRO A 291      38.808 -14.474 -14.234  1.00181.79           C  
ANISOU  857  CB  PRO A 291    20633  20644  27794  -2661  -4364  -1843       C  
ATOM    858  CG  PRO A 291      37.456 -13.852 -14.309  1.00179.28           C  
ANISOU  858  CG  PRO A 291    20718  20189  27211  -2491  -4276  -2096       C  
ATOM    859  CD  PRO A 291      37.421 -13.038 -15.581  1.00178.86           C  
ANISOU  859  CD  PRO A 291    20730  19707  27522  -2529  -3994  -1923       C  
ATOM    860  N   ASP A 292      37.516 -16.358 -16.188  1.00171.51           N  
ANISOU  860  N   ASP A 292    19541  19564  26062  -2163  -3551  -1264       N  
ATOM    861  CA  ASP A 292      36.993 -17.667 -16.542  1.00164.53           C  
ANISOU  861  CA  ASP A 292    18708  18961  24845  -1930  -3308  -1059       C  
ATOM    862  C   ASP A 292      36.070 -17.569 -17.747  1.00161.58           C  
ANISOU  862  C   ASP A 292    18593  18416  24383  -1765  -2953   -937       C  
ATOM    863  O   ASP A 292      35.582 -16.487 -18.076  1.00162.57           O  
ANISOU  863  O   ASP A 292    18909  18254  24607  -1786  -2939  -1069       O  
ATOM    864  CB  ASP A 292      36.235 -18.267 -15.357  1.00162.02           C  
ANISOU  864  CB  ASP A 292    18517  19001  24044  -1791  -3517  -1296       C  
ATOM    865  CG  ASP A 292      37.004 -18.161 -14.056  1.00165.19           C  
ANISOU  865  CG  ASP A 292    18727  19566  24470  -1955  -3926  -1480       C  
ATOM    866  OD1 ASP A 292      38.139 -18.678 -13.996  1.00169.10           O  
ANISOU  866  OD1 ASP A 292    18897  20155  25200  -2071  -3988  -1264       O  
ATOM    867  OD2 ASP A 292      36.476 -17.553 -13.098  1.00162.76           O  
ANISOU  867  OD2 ASP A 292    18596  19297  23948  -1965  -4187  -1841       O  
ATOM    868  N   PRO A 293      35.828 -18.702 -18.420  1.00158.37           N  
ANISOU  868  N   PRO A 293    18199  18178  23795  -1599  -2673   -683       N  
ATOM    869  CA  PRO A 293      34.699 -18.744 -19.356  1.00155.98           C  
ANISOU  869  CA  PRO A 293    18189  17798  23279  -1411  -2402   -627       C  
ATOM    870  C   PRO A 293      33.384 -18.766 -18.583  1.00154.26           C  
ANISOU  870  C   PRO A 293    18220  17751  22642  -1250  -2542   -917       C  
ATOM    871  O   PRO A 293      32.316 -18.624 -19.177  1.00154.47           O  
ANISOU  871  O   PRO A 293    18491  17709  22489  -1099  -2387   -931       O  
ATOM    872  CB  PRO A 293      34.913 -20.052 -20.127  1.00152.33           C  
ANISOU  872  CB  PRO A 293    17649  17495  22732  -1301  -2108   -308       C  
ATOM    873  CG  PRO A 293      36.342 -20.416 -19.885  1.00155.69           C  
ANISOU  873  CG  PRO A 293    17715  17969  23469  -1454  -2160   -141       C  
ATOM    874  CD  PRO A 293      36.676 -19.899 -18.524  1.00158.14           C  
ANISOU  874  CD  PRO A 293    17907  18359  23821  -1591  -2569   -408       C  
ATOM    875  N   GLN A 294      33.479 -18.947 -17.265  1.00153.32           N  
ANISOU  875  N   GLN A 294    18028  17861  22366  -1280  -2833  -1135       N  
ATOM    876  CA  GLN A 294      32.321 -18.890 -16.376  1.00148.35           C  
ANISOU  876  CA  GLN A 294    17615  17402  21348  -1140  -2976  -1432       C  
ATOM    877  C   GLN A 294      31.959 -17.453 -16.034  1.00148.97           C  
ANISOU  877  C   GLN A 294    17853  17220  21530  -1203  -3140  -1743       C  
ATOM    878  O   GLN A 294      30.795 -17.144 -15.778  1.00146.71           O  
ANISOU  878  O   GLN A 294    17803  16949  20992  -1051  -3141  -1951       O  
ATOM    879  CB  GLN A 294      32.581 -19.662 -15.078  1.00146.17           C  
ANISOU  879  CB  GLN A 294    17216  17489  20831  -1141  -3213  -1532       C  
ATOM    880  CG  GLN A 294      32.672 -21.161 -15.241  1.00140.69           C  
ANISOU  880  CG  GLN A 294    16411  17078  19967  -1030  -3056  -1261       C  
ATOM    881  CD  GLN A 294      34.049 -21.607 -15.666  1.00142.25           C  
ANISOU  881  CD  GLN A 294    16304  17240  20503  -1163  -3004   -974       C  
ATOM    882  OE1 GLN A 294      35.058 -21.116 -15.155  1.00142.90           O  
ANISOU  882  OE1 GLN A 294    16182  17272  20840  -1351  -3233  -1023       O  
ATOM    883  NE2 GLN A 294      34.102 -22.543 -16.609  1.00141.35           N  
ANISOU  883  NE2 GLN A 294    16152  17150  20404  -1068  -2702   -678       N  
ATOM    884  N   ALA A 295      32.968 -16.586 -16.029  1.00151.82           N  
ANISOU  884  N   ALA A 295    18072  17329  22283  -1427  -3275  -1772       N  
ATOM    885  CA  ALA A 295      32.805 -15.193 -15.619  1.00151.32           C  
ANISOU  885  CA  ALA A 295    18139  16983  22374  -1523  -3462  -2085       C  
ATOM    886  C   ALA A 295      31.806 -14.434 -16.495  1.00145.03           C  
ANISOU  886  C   ALA A 295    17599  15898  21608  -1393  -3256  -2094       C  
ATOM    887  O   ALA A 295      31.150 -13.497 -16.033  1.00144.68           O  
ANISOU  887  O   ALA A 295    17747  15696  21530  -1358  -3373  -2398       O  
ATOM    888  CB  ALA A 295      34.149 -14.491 -15.630  1.00156.30           C  
ANISOU  888  CB  ALA A 295    18537  17370  23479  -1809  -3613  -2053       C  
ATOM    889  N   MET A 296      31.686 -14.844 -17.754  1.00136.63           N  
ANISOU  889  N   MET A 296    16545  14769  20601  -1314  -2950  -1761       N  
ATOM    890  CA  MET A 296      30.753 -14.201 -18.670  1.00127.90           C  
ANISOU  890  CA  MET A 296    15671  13413  19510  -1184  -2759  -1718       C  
ATOM    891  C   MET A 296      29.321 -14.668 -18.396  1.00122.50           C  
ANISOU  891  C   MET A 296    15197  12959  18389   -925  -2717  -1849       C  
ATOM    892  O   MET A 296      28.366 -14.117 -18.942  1.00121.72           O  
ANISOU  892  O   MET A 296    15298  12692  18258   -787  -2610  -1867       O  
ATOM    893  CB  MET A 296      31.153 -14.472 -20.128  1.00122.13           C  
ANISOU  893  CB  MET A 296    14893  12546  18966  -1196  -2455  -1314       C  
ATOM    894  CG  MET A 296      30.522 -15.699 -20.758  1.00117.41           C  
ANISOU  894  CG  MET A 296    14359  12213  18038  -1003  -2228  -1102       C  
ATOM    895  SD  MET A 296      31.055 -16.003 -22.455  1.00130.49           S  
ANISOU  895  SD  MET A 296    15988  13713  19877  -1022  -1868   -655       S  
ATOM    896  CE  MET A 296      32.760 -16.492 -22.198  1.00158.51           C  
ANISOU  896  CE  MET A 296    19175  17323  23727  -1242  -1891   -497       C  
ATOM    897  N   PHE A 297      29.181 -15.676 -17.536  1.00120.57           N  
ANISOU  897  N   PHE A 297    14892  13095  17823   -860  -2805  -1924       N  
ATOM    898  CA  PHE A 297      27.869 -16.169 -17.116  1.00117.90           C  
ANISOU  898  CA  PHE A 297    14718  13003  17075   -632  -2777  -2055       C  
ATOM    899  C   PHE A 297      27.598 -15.845 -15.649  1.00117.66           C  
ANISOU  899  C   PHE A 297    14738  13116  16850   -622  -3033  -2435       C  
ATOM    900  O   PHE A 297      26.622 -16.317 -15.062  1.00107.92           O  
ANISOU  900  O   PHE A 297    13608  12136  15263   -447  -3027  -2561       O  
ATOM    901  CB  PHE A 297      27.752 -17.678 -17.348  1.00116.60           C  
ANISOU  901  CB  PHE A 297    14474  13172  16656   -537  -2632  -1817       C  
ATOM    902  CG  PHE A 297      27.674 -18.063 -18.797  1.00114.94           C  
ANISOU  902  CG  PHE A 297    14291  12854  16527   -490  -2356  -1490       C  
ATOM    903  CD1 PHE A 297      26.456 -18.084 -19.458  1.00110.75           C  
ANISOU  903  CD1 PHE A 297    13950  12304  15826   -310  -2209  -1452       C  
ATOM    904  CD2 PHE A 297      28.821 -18.402 -19.498  1.00116.32           C  
ANISOU  904  CD2 PHE A 297    14299  12953  16944   -624  -2244  -1221       C  
ATOM    905  CE1 PHE A 297      26.384 -18.433 -20.795  1.00109.92           C  
ANISOU  905  CE1 PHE A 297    13893  12112  15760   -272  -1976  -1163       C  
ATOM    906  CE2 PHE A 297      28.758 -18.753 -20.833  1.00115.03           C  
ANISOU  906  CE2 PHE A 297    14188  12697  16821   -576  -1976   -934       C  
ATOM    907  CZ  PHE A 297      27.538 -18.769 -21.484  1.00112.49           C  
ANISOU  907  CZ  PHE A 297    14081  12363  16297   -404  -1852   -911       C  
ATOM    908  N   ASP A 298      28.480 -15.045 -15.059  1.00128.59           N  
ANISOU  908  N   ASP A 298    16049  14341  18467   -817  -3254  -2617       N  
ATOM    909  CA  ASP A 298      28.258 -14.521 -13.721  1.00132.79           C  
ANISOU  909  CA  ASP A 298    16672  14949  18833   -824  -3508  -3019       C  
ATOM    910  C   ASP A 298      27.578 -13.170 -13.826  1.00135.56           C  
ANISOU  910  C   ASP A 298    17236  14943  19328   -772  -3509  -3266       C  
ATOM    911  O   ASP A 298      27.978 -12.331 -14.633  1.00135.05           O  
ANISOU  911  O   ASP A 298    17167  14499  19648   -879  -3457  -3174       O  
ATOM    912  CB  ASP A 298      29.570 -14.390 -12.947  1.00133.33           C  
ANISOU  912  CB  ASP A 298    16553  15048  19059  -1073  -3789  -3115       C  
ATOM    913  CG  ASP A 298      29.361 -13.884 -11.531  1.00134.58           C  
ANISOU  913  CG  ASP A 298    16830  15309  18994  -1086  -4070  -3551       C  
ATOM    914  OD1 ASP A 298      28.262 -14.105 -10.973  1.00130.49           O  
ANISOU  914  OD1 ASP A 298    16492  14993  18095   -876  -4025  -3724       O  
ATOM    915  OD2 ASP A 298      30.296 -13.268 -10.973  1.00139.05           O  
ANISOU  915  OD2 ASP A 298    17310  15757  19764  -1309  -4335  -3724       O  
ATOM    916  N   ILE A 299      26.552 -12.966 -13.009  1.00143.97           N  
ANISOU  916  N   ILE A 299    18485  16125  20093   -600  -3553  -3568       N  
ATOM    917  CA  ILE A 299      25.790 -11.723 -13.038  1.00148.12           C  
ANISOU  917  CA  ILE A 299    19221  16319  20737   -508  -3537  -3819       C  
ATOM    918  C   ILE A 299      26.625 -10.566 -12.490  1.00152.35           C  
ANISOU  918  C   ILE A 299    19771  16548  21566   -728  -3781  -4107       C  
ATOM    919  O   ILE A 299      26.495  -9.433 -12.945  1.00157.20           O  
ANISOU  919  O   ILE A 299    20493  16741  22495   -748  -3752  -4188       O  
ATOM    920  CB  ILE A 299      24.464 -11.855 -12.244  1.00140.11           C  
ANISOU  920  CB  ILE A 299    18386  15532  19319   -249  -3498  -4074       C  
ATOM    921  CG1 ILE A 299      23.618 -10.587 -12.379  1.00133.25           C  
ANISOU  921  CG1 ILE A 299    17724  14300  18604   -119  -3443  -4305       C  
ATOM    922  CG2 ILE A 299      24.727 -12.205 -10.783  1.00145.73           C  
ANISOU  922  CG2 ILE A 299    19097  16569  19706   -293  -3718  -4360       C  
ATOM    923  CD1 ILE A 299      23.176 -10.296 -13.796  1.00129.73           C  
ANISOU  923  CD1 ILE A 299    17299  13577  18414    -33  -3224  -4002       C  
ATOM    924  N   GLU A 300      27.502 -10.865 -11.535  1.00152.70           N  
ANISOU  924  N   GLU A 300    19702  16796  21523   -901  -4030  -4246       N  
ATOM    925  CA  GLU A 300      28.337  -9.847 -10.901  1.00158.94           C  
ANISOU  925  CA  GLU A 300    20494  17332  22565  -1137  -4310  -4547       C  
ATOM    926  C   GLU A 300      29.343  -9.235 -11.873  1.00161.38           C  
ANISOU  926  C   GLU A 300    20649  17241  23426  -1371  -4296  -4321       C  
ATOM    927  O   GLU A 300      29.492  -8.013 -11.933  1.00163.33           O  
ANISOU  927  O   GLU A 300    20988  17066  24002  -1480  -4374  -4516       O  
ATOM    928  CB  GLU A 300      29.078 -10.434  -9.701  1.00161.83           C  
ANISOU  928  CB  GLU A 300    20747  18056  22687  -1272  -4600  -4700       C  
ATOM    929  CG  GLU A 300      30.094  -9.483  -9.100  1.00168.40           C  
ANISOU  929  CG  GLU A 300    21539  18645  23802  -1561  -4928  -4981       C  
ATOM    930  CD  GLU A 300      30.976 -10.154  -8.073  1.00170.84           C  
ANISOU  930  CD  GLU A 300    21685  19322  23905  -1718  -5234  -5047       C  
ATOM    931  OE1 GLU A 300      32.004  -9.553  -7.690  1.00175.39           O  
ANISOU  931  OE1 GLU A 300    22153  19735  24751  -1996  -5527  -5197       O  
ATOM    932  OE2 GLU A 300      30.640 -11.281  -7.650  1.00167.03           O  
ANISOU  932  OE2 GLU A 300    21175  19288  23000  -1568  -5191  -4937       O  
ATOM    933  N   TYR A 301      30.038 -10.086 -12.622  1.00160.98           N  
ANISOU  933  N   TYR A 301    20365  17315  23484  -1448  -4183  -3909       N  
ATOM    934  CA  TYR A 301      30.985  -9.615 -13.627  1.00162.93           C  
ANISOU  934  CA  TYR A 301    20450  17216  24242  -1654  -4113  -3639       C  
ATOM    935  C   TYR A 301      30.246  -9.013 -14.814  1.00159.46           C  
ANISOU  935  C   TYR A 301    20166  16439  23983  -1517  -3831  -3469       C  
ATOM    936  O   TYR A 301      30.780  -8.160 -15.519  1.00163.74           O  
ANISOU  936  O   TYR A 301    20671  16576  24967  -1669  -3788  -3356       O  
ATOM    937  CB  TYR A 301      31.897 -10.751 -14.097  1.00164.74           C  
ANISOU  937  CB  TYR A 301    20390  17689  24513  -1743  -4034  -3244       C  
ATOM    938  CG  TYR A 301      32.874 -10.344 -15.185  1.00167.83           C  
ANISOU  938  CG  TYR A 301    20599  17750  25419  -1940  -3912  -2929       C  
ATOM    939  CD1 TYR A 301      34.118  -9.809 -14.866  1.00173.06           C  
ANISOU  939  CD1 TYR A 301    21047  18239  26468  -2243  -4137  -2978       C  
ATOM    940  CD2 TYR A 301      32.553 -10.494 -16.531  1.00164.27           C  
ANISOU  940  CD2 TYR A 301    20187  17166  25061  -1828  -3571  -2576       C  
ATOM    941  CE1 TYR A 301      35.014  -9.434 -15.858  1.00173.41           C  
ANISOU  941  CE1 TYR A 301    20907  17982  27001  -2426  -4000  -2671       C  
ATOM    942  CE2 TYR A 301      33.440 -10.119 -17.528  1.00164.75           C  
ANISOU  942  CE2 TYR A 301    20093  16934  25570  -2000  -3431  -2274       C  
ATOM    943  CZ  TYR A 301      34.669  -9.592 -17.186  1.00167.44           C  
ANISOU  943  CZ  TYR A 301    20207  17103  26311  -2297  -3632  -2316       C  
ATOM    944  OH  TYR A 301      35.554  -9.222 -18.175  1.00163.61           O  
ANISOU  944  OH  TYR A 301    19549  16328  26288  -2470  -3468  -1996       O  
ATOM    945  N   PHE A 302      29.019  -9.470 -15.035  1.00153.53           N  
ANISOU  945  N   PHE A 302    19580  15861  22894  -1233  -3646  -3434       N  
ATOM    946  CA  PHE A 302      28.194  -8.944 -16.115  1.00151.63           C  
ANISOU  946  CA  PHE A 302    19496  15342  22774  -1074  -3404  -3273       C  
ATOM    947  C   PHE A 302      27.941  -7.455 -15.919  1.00157.50           C  
ANISOU  947  C   PHE A 302    20412  15635  23797  -1102  -3494  -3561       C  
ATOM    948  O   PHE A 302      27.906  -6.690 -16.882  1.00163.22           O  
ANISOU  948  O   PHE A 302    21190  15975  24851  -1114  -3357  -3385       O  
ATOM    949  CB  PHE A 302      26.870  -9.699 -16.194  1.00147.58           C  
ANISOU  949  CB  PHE A 302    19113  15126  21834   -770  -3242  -3237       C  
ATOM    950  CG  PHE A 302      25.986  -9.259 -17.324  1.00146.67           C  
ANISOU  950  CG  PHE A 302    19142  14772  21814   -595  -3015  -3044       C  
ATOM    951  CD1 PHE A 302      26.354  -9.493 -18.638  1.00147.06           C  
ANISOU  951  CD1 PHE A 302    19123  14713  22040   -638  -2818  -2631       C  
ATOM    952  CD2 PHE A 302      24.778  -8.627 -17.072  1.00146.35           C  
ANISOU  952  CD2 PHE A 302    19305  14627  21673   -378  -2995  -3268       C  
ATOM    953  CE1 PHE A 302      25.537  -9.098 -19.683  1.00145.76           C  
ANISOU  953  CE1 PHE A 302    19101  14348  21931   -477  -2632  -2441       C  
ATOM    954  CE2 PHE A 302      23.957  -8.228 -18.113  1.00146.56           C  
ANISOU  954  CE2 PHE A 302    19450  14445  21793   -210  -2810  -3070       C  
ATOM    955  CZ  PHE A 302      24.338  -8.462 -19.420  1.00145.78           C  
ANISOU  955  CZ  PHE A 302    19291  14249  21850   -264  -2641  -2653       C  
ATOM    956  N   ARG A 303      27.770  -7.054 -14.663  1.00154.64           N  
ANISOU  956  N   ARG A 303    20146  15315  23294  -1109  -3721  -4003       N  
ATOM    957  CA  ARG A 303      27.559  -5.655 -14.322  1.00153.40           C  
ANISOU  957  CA  ARG A 303    20168  14725  23392  -1139  -3826  -4340       C  
ATOM    958  C   ARG A 303      28.800  -4.821 -14.617  1.00153.22           C  
ANISOU  958  C   ARG A 303    20020  14299  23898  -1463  -3947  -4294       C  
ATOM    959  O   ARG A 303      28.695  -3.711 -15.142  1.00158.15           O  
ANISOU  959  O   ARG A 303    20750  14446  24895  -1489  -3890  -4304       O  
ATOM    960  CB  ARG A 303      27.168  -5.518 -12.852  1.00155.96           C  
ANISOU  960  CB  ARG A 303    20631  15229  23397  -1081  -4041  -4842       C  
ATOM    961  CG  ARG A 303      25.791  -6.063 -12.527  1.00153.14           C  
ANISOU  961  CG  ARG A 303    20427  15183  22577   -743  -3896  -4930       C  
ATOM    962  CD  ARG A 303      25.648  -6.330 -11.038  1.00158.97           C  
ANISOU  962  CD  ARG A 303    21244  16248  22911   -716  -4097  -5341       C  
ATOM    963  NE  ARG A 303      24.334  -6.871 -10.703  1.00160.79           N  
ANISOU  963  NE  ARG A 303    21600  16785  22709   -396  -3935  -5409       N  
ATOM    964  CZ  ARG A 303      24.082  -7.611  -9.628  1.00163.19           C  
ANISOU  964  CZ  ARG A 303    21926  17529  22549   -318  -4015  -5593       C  
ATOM    965  NH1 ARG A 303      22.853  -8.062  -9.403  1.00161.06           N  
ANISOU  965  NH1 ARG A 303    21755  17510  21929    -28  -3836  -5623       N  
ATOM    966  NH2 ARG A 303      25.058  -7.908  -8.779  1.00165.63           N  
ANISOU  966  NH2 ARG A 303    22150  18036  22748   -533  -4276  -5728       N  
ATOM    967  N   LYS A 304      29.970  -5.354 -14.273  1.00147.13           N  
ANISOU  967  N   LYS A 304    19011  13713  23179  -1709  -4115  -4232       N  
ATOM    968  CA  LYS A 304      31.228  -4.667 -14.551  1.00150.80           C  
ANISOU  968  CA  LYS A 304    19301  13829  24167  -2039  -4232  -4155       C  
ATOM    969  C   LYS A 304      31.407  -4.484 -16.057  1.00152.58           C  
ANISOU  969  C   LYS A 304    19459  13774  24741  -2050  -3937  -3685       C  
ATOM    970  O   LYS A 304      31.639  -3.374 -16.533  1.00155.97           O  
ANISOU  970  O   LYS A 304    19935  13716  25613  -2170  -3914  -3669       O  
ATOM    971  CB  LYS A 304      32.423  -5.427 -13.962  1.00151.22           C  
ANISOU  971  CB  LYS A 304    19068  14191  24198  -2275  -4452  -4116       C  
ATOM    972  CG  LYS A 304      32.455  -5.491 -12.434  1.00154.99           C  
ANISOU  972  CG  LYS A 304    19603  14919  24366  -2322  -4797  -4581       C  
ATOM    973  CD  LYS A 304      33.858  -5.821 -11.917  1.00156.97           C  
ANISOU  973  CD  LYS A 304    19549  15313  24778  -2635  -5081  -4555       C  
ATOM    974  CE  LYS A 304      33.825  -6.376 -10.498  1.00157.12           C  
ANISOU  974  CE  LYS A 304    19602  15766  24332  -2619  -5381  -4888       C  
ATOM    975  NZ  LYS A 304      33.267  -7.762 -10.459  1.00152.40           N  
ANISOU  975  NZ  LYS A 304    18983  15683  23241  -2368  -5218  -4676       N  
ATOM    976  N   ASP A 305      31.289  -5.576 -16.805  1.00152.69           N  
ANISOU  976  N   ASP A 305    19378  14091  24545  -1924  -3708  -3302       N  
ATOM    977  CA  ASP A 305      31.377  -5.511 -18.261  1.00153.33           C  
ANISOU  977  CA  ASP A 305    19429  13962  24868  -1903  -3406  -2849       C  
ATOM    978  C   ASP A 305      30.488  -6.574 -18.910  1.00147.19           C  
ANISOU  978  C   ASP A 305    18725  13522  23679  -1621  -3156  -2594       C  
ATOM    979  O   ASP A 305      30.762  -7.770 -18.809  1.00143.97           O  
ANISOU  979  O   ASP A 305    18172  13514  23015  -1604  -3127  -2458       O  
ATOM    980  CB  ASP A 305      32.832  -5.668 -18.724  1.00153.98           C  
ANISOU  980  CB  ASP A 305    19208  13971  25325  -2194  -3391  -2556       C  
ATOM    981  CG  ASP A 305      33.017  -5.363 -20.207  1.00151.91           C  
ANISOU  981  CG  ASP A 305    18936  13420  25365  -2204  -3077  -2110       C  
ATOM    982  OD1 ASP A 305      32.085  -4.815 -20.832  1.00151.65           O  
ANISOU  982  OD1 ASP A 305    19138  13170  25312  -2020  -2921  -2055       O  
ATOM    983  OD2 ASP A 305      34.103  -5.662 -20.748  1.00150.18           O  
ANISOU  983  OD2 ASP A 305    18469  13191  25403  -2391  -2981  -1803       O  
ATOM    984  N   PRO A 306      29.406  -6.131 -19.567  1.00146.94           N  
ANISOU  984  N   PRO A 306    18916  13318  23595  -1400  -2986  -2532       N  
ATOM    985  CA  PRO A 306      28.460  -6.988 -20.282  1.00146.16           C  
ANISOU  985  CA  PRO A 306    18909  13484  23143  -1137  -2762  -2295       C  
ATOM    986  C   PRO A 306      28.873  -7.251 -21.732  1.00145.69           C  
ANISOU  986  C   PRO A 306    18789  13335  23234  -1169  -2495  -1808       C  
ATOM    987  O   PRO A 306      28.391  -8.207 -22.349  1.00140.19           O  
ANISOU  987  O   PRO A 306    18117  12913  22235  -1010  -2322  -1581       O  
ATOM    988  CB  PRO A 306      27.166  -6.175 -20.227  1.00145.91           C  
ANISOU  988  CB  PRO A 306    19132  13255  23053   -907  -2751  -2487       C  
ATOM    989  CG  PRO A 306      27.629  -4.778 -20.268  1.00146.82           C  
ANISOU  989  CG  PRO A 306    19291  12849  23644  -1067  -2827  -2589       C  
ATOM    990  CD  PRO A 306      28.930  -4.738 -19.506  1.00150.12           C  
ANISOU  990  CD  PRO A 306    19510  13262  24265  -1375  -3038  -2743       C  
ATOM    991  N   ARG A 307      29.757  -6.405 -22.257  1.00146.69           N  
ANISOU  991  N   ARG A 307    18842  13075  23820  -1379  -2460  -1658       N  
ATOM    992  CA  ARG A 307      30.209  -6.489 -23.647  1.00142.87           C  
ANISOU  992  CA  ARG A 307    18317  12460  23509  -1421  -2186  -1193       C  
ATOM    993  C   ARG A 307      30.722  -7.864 -24.115  1.00133.53           C  
ANISOU  993  C   ARG A 307    16974  11655  22105  -1424  -2023   -909       C  
ATOM    994  O   ARG A 307      30.405  -8.270 -25.233  1.00123.78           O  
ANISOU  994  O   ARG A 307    15826  10467  20739  -1302  -1774   -587       O  
ATOM    995  CB  ARG A 307      31.296  -5.439 -23.902  1.00145.93           C  
ANISOU  995  CB  ARG A 307    18587  12403  24456  -1698  -2198  -1100       C  
ATOM    996  CG  ARG A 307      30.790  -4.013 -23.890  1.00151.23           C  
ANISOU  996  CG  ARG A 307    19448  12600  25411  -1681  -2264  -1252       C  
ATOM    997  CD  ARG A 307      31.905  -3.039 -24.226  1.00159.39           C  
ANISOU  997  CD  ARG A 307    20353  13185  27025  -1974  -2253  -1115       C  
ATOM    998  NE  ARG A 307      33.016  -3.126 -23.281  1.00164.21           N  
ANISOU  998  NE  ARG A 307    20709  13849  27832  -2253  -2483  -1324       N  
ATOM    999  CZ  ARG A 307      34.287  -3.310 -23.628  1.00165.79           C  
ANISOU  999  CZ  ARG A 307    20636  14018  28340  -2504  -2416  -1071       C  
ATOM   1000  NH1 ARG A 307      34.621  -3.428 -24.906  1.00163.54           N  
ANISOU 1000  NH1 ARG A 307    20312  13643  28184  -2507  -2098   -602       N  
ATOM   1001  NH2 ARG A 307      35.228  -3.371 -22.695  1.00169.26           N  
ANISOU 1001  NH2 ARG A 307    20837  14519  28955  -2750  -2669  -1282       N  
ATOM   1002  N   PRO A 308      31.521  -8.578 -23.286  1.00136.64           N  
ANISOU 1002  N   PRO A 308    17143  12312  22463  -1559  -2164  -1022       N  
ATOM   1003  CA  PRO A 308      31.989  -9.892 -23.760  1.00134.37           C  
ANISOU 1003  CA  PRO A 308    16708  12357  21989  -1541  -1987   -745       C  
ATOM   1004  C   PRO A 308      30.863 -10.916 -23.956  1.00124.17           C  
ANISOU 1004  C   PRO A 308    15577  11411  20193  -1268  -1885   -720       C  
ATOM   1005  O   PRO A 308      30.859 -11.655 -24.945  1.00115.88           O  
ANISOU 1005  O   PRO A 308    14544  10476  19009  -1191  -1637   -414       O  
ATOM   1006  CB  PRO A 308      32.946 -10.347 -22.646  1.00135.55           C  
ANISOU 1006  CB  PRO A 308    16592  12708  22202  -1719  -2214   -916       C  
ATOM   1007  CG  PRO A 308      32.542  -9.569 -21.448  1.00137.26           C  
ANISOU 1007  CG  PRO A 308    16897  12841  22416  -1744  -2527  -1354       C  
ATOM   1008  CD  PRO A 308      32.128  -8.236 -21.985  1.00139.41           C  
ANISOU 1008  CD  PRO A 308    17355  12656  22959  -1744  -2477  -1368       C  
ATOM   1009  N   PHE A 309      29.929 -10.953 -23.013  1.00123.14           N  
ANISOU 1009  N   PHE A 309    15560  11438  19788  -1131  -2071  -1047       N  
ATOM   1010  CA  PHE A 309      28.760 -11.811 -23.114  1.00118.25           C  
ANISOU 1010  CA  PHE A 309    15086  11120  18725   -881  -1996  -1049       C  
ATOM   1011  C   PHE A 309      27.983 -11.539 -24.399  1.00118.61           C  
ANISOU 1011  C   PHE A 309    15330  11007  18728   -731  -1781   -804       C  
ATOM   1012  O   PHE A 309      27.510 -12.464 -25.059  1.00117.91           O  
ANISOU 1012  O   PHE A 309    15300  11141  18358   -598  -1623   -617       O  
ATOM   1013  CB  PHE A 309      27.855 -11.611 -21.895  1.00121.99           C  
ANISOU 1013  CB  PHE A 309    15657  11716  18977   -764  -2217  -1447       C  
ATOM   1014  CG  PHE A 309      26.513 -12.280 -22.014  1.00124.99           C  
ANISOU 1014  CG  PHE A 309    16188  12349  18955   -503  -2140  -1456       C  
ATOM   1015  CD1 PHE A 309      26.345 -13.596 -21.618  1.00128.92           C  
ANISOU 1015  CD1 PHE A 309    16613  13257  19115   -434  -2131  -1447       C  
ATOM   1016  CD2 PHE A 309      25.417 -11.593 -22.519  1.00125.28           C  
ANISOU 1016  CD2 PHE A 309    16424  12204  18972   -330  -2082  -1461       C  
ATOM   1017  CE1 PHE A 309      25.111 -14.218 -21.726  1.00127.83           C  
ANISOU 1017  CE1 PHE A 309    16594  13341  18635   -214  -2064  -1449       C  
ATOM   1018  CE2 PHE A 309      24.182 -12.206 -22.630  1.00125.32           C  
ANISOU 1018  CE2 PHE A 309    16536  12445  18634   -102  -2026  -1461       C  
ATOM   1019  CZ  PHE A 309      24.027 -13.518 -22.231  1.00126.66           C  
ANISOU 1019  CZ  PHE A 309    16627  13020  18476    -52  -2016  -1460       C  
ATOM   1020  N   PHE A 310      27.846 -10.266 -24.749  1.00124.83           N  
ANISOU 1020  N   PHE A 310    16228  11404  19799   -754  -1787   -806       N  
ATOM   1021  CA  PHE A 310      27.026  -9.894 -25.891  1.00125.79           C  
ANISOU 1021  CA  PHE A 310    16551  11366  19876   -596  -1621   -582       C  
ATOM   1022  C   PHE A 310      27.699 -10.218 -27.222  1.00133.56           C  
ANISOU 1022  C   PHE A 310    17515  12298  20935   -664  -1360   -159       C  
ATOM   1023  O   PHE A 310      27.024 -10.333 -28.245  1.00137.96           O  
ANISOU 1023  O   PHE A 310    18239  12856  21324   -518  -1207     67       O  
ATOM   1024  CB  PHE A 310      26.655  -8.409 -25.818  1.00121.40           C  
ANISOU 1024  CB  PHE A 310    16123  10389  19616   -584  -1708   -705       C  
ATOM   1025  CG  PHE A 310      25.448  -8.138 -24.962  1.00116.06           C  
ANISOU 1025  CG  PHE A 310    15570   9774  18753   -388  -1868  -1044       C  
ATOM   1026  CD1 PHE A 310      24.184  -8.526 -25.386  1.00109.58           C  
ANISOU 1026  CD1 PHE A 310    14890   9122  17623   -135  -1802   -978       C  
ATOM   1027  CD2 PHE A 310      25.571  -7.517 -23.732  1.00117.65           C  
ANISOU 1027  CD2 PHE A 310    15743   9875  19083   -457  -2082  -1431       C  
ATOM   1028  CE1 PHE A 310      23.065  -8.295 -24.598  1.00106.12           C  
ANISOU 1028  CE1 PHE A 310    14540   8750  17031     55  -1924  -1275       C  
ATOM   1029  CE2 PHE A 310      24.453  -7.281 -22.942  1.00116.01           C  
ANISOU 1029  CE2 PHE A 310    15655   9731  18691   -260  -2194  -1745       C  
ATOM   1030  CZ  PHE A 310      23.201  -7.671 -23.376  1.00108.69           C  
ANISOU 1030  CZ  PHE A 310    14846   8973  17480      1  -2104  -1658       C  
ATOM   1031  N   LYS A 311      29.019 -10.372 -27.217  1.00136.68           N  
ANISOU 1031  N   LYS A 311    17705  12655  21573   -881  -1307    -49       N  
ATOM   1032  CA  LYS A 311      29.711 -10.812 -28.422  1.00137.59           C  
ANISOU 1032  CA  LYS A 311    17786  12763  21731   -936  -1024    345       C  
ATOM   1033  C   LYS A 311      29.490 -12.307 -28.576  1.00129.92           C  
ANISOU 1033  C   LYS A 311    16802  12207  20356   -821   -923    410       C  
ATOM   1034  O   LYS A 311      29.397 -12.820 -29.693  1.00126.90           O  
ANISOU 1034  O   LYS A 311    16523  11885  19809   -746   -687    690       O  
ATOM   1035  CB  LYS A 311      31.204 -10.481 -28.371  1.00144.25           C  
ANISOU 1035  CB  LYS A 311    18382  13424  23003  -1202   -981    456       C  
ATOM   1036  CG  LYS A 311      31.949 -10.789 -29.668  1.00147.70           C  
ANISOU 1036  CG  LYS A 311    18786  13809  23522  -1254   -646    880       C  
ATOM   1037  CD  LYS A 311      33.187  -9.916 -29.821  1.00153.54           C  
ANISOU 1037  CD  LYS A 311    19334  14213  24792  -1509   -587   1028       C  
ATOM   1038  CE  LYS A 311      33.988 -10.297 -31.059  1.00154.19           C  
ANISOU 1038  CE  LYS A 311    19363  14275  24947  -1556   -219   1454       C  
ATOM   1039  NZ  LYS A 311      34.517 -11.695 -30.982  1.00150.57           N  
ANISOU 1039  NZ  LYS A 311    18739  14181  24289  -1536   -109   1508       N  
ATOM   1040  N   PHE A 312      29.396 -12.993 -27.440  1.00129.41           N  
ANISOU 1040  N   PHE A 312    16625  12419  20126   -807  -1106    146       N  
ATOM   1041  CA  PHE A 312      29.025 -14.405 -27.414  1.00126.44           C  
ANISOU 1041  CA  PHE A 312    16248  12429  19363   -685  -1045    164       C  
ATOM   1042  C   PHE A 312      27.577 -14.569 -27.858  1.00121.71           C  
ANISOU 1042  C   PHE A 312    15896  11924  18424   -459  -1028    151       C  
ATOM   1043  O   PHE A 312      27.270 -15.398 -28.715  1.00119.25           O  
ANISOU 1043  O   PHE A 312    15679  11764  17865   -365   -854    343       O  
ATOM   1044  CB  PHE A 312      29.221 -15.003 -26.014  1.00125.45           C  
ANISOU 1044  CB  PHE A 312    15950  12564  19152   -721  -1263   -109       C  
ATOM   1045  CG  PHE A 312      28.306 -16.159 -25.718  1.00123.02           C  
ANISOU 1045  CG  PHE A 312    15710  12614  18418   -545  -1276   -190       C  
ATOM   1046  CD1 PHE A 312      28.580 -17.424 -26.220  1.00116.22           C  
ANISOU 1046  CD1 PHE A 312    14801  11976  17380   -513  -1097      4       C  
ATOM   1047  CD2 PHE A 312      27.168 -15.983 -24.947  1.00121.95           C  
ANISOU 1047  CD2 PHE A 312    15685  12578  18072   -410  -1452   -457       C  
ATOM   1048  CE1 PHE A 312      27.737 -18.491 -25.957  1.00103.72           C  
ANISOU 1048  CE1 PHE A 312    13278  10696  15433   -366  -1110    -65       C  
ATOM   1049  CE2 PHE A 312      26.318 -17.051 -24.684  1.00117.89           C  
ANISOU 1049  CE2 PHE A 312    15216  12387  17189   -260  -1452   -511       C  
ATOM   1050  CZ  PHE A 312      26.604 -18.305 -25.192  1.00105.17           C  
ANISOU 1050  CZ  PHE A 312    13556  10983  15420   -246  -1289   -313       C  
ATOM   1051  N   ALA A 313      26.697 -13.763 -27.270  1.00117.70           N  
ANISOU 1051  N   ALA A 313    15488  11317  17917   -374  -1211    -83       N  
ATOM   1052  CA  ALA A 313      25.273 -13.776 -27.592  1.00111.63           C  
ANISOU 1052  CA  ALA A 313    14919  10617  16877   -156  -1225   -109       C  
ATOM   1053  C   ALA A 313      25.019 -13.529 -29.078  1.00111.05           C  
ANISOU 1053  C   ALA A 313    15019  10389  16784    -95  -1034    215       C  
ATOM   1054  O   ALA A 313      23.986 -13.935 -29.612  1.00107.22           O  
ANISOU 1054  O   ALA A 313    14682  10041  16017     71  -1007    279       O  
ATOM   1055  CB  ALA A 313      24.537 -12.740 -26.754  1.00110.77           C  
ANISOU 1055  CB  ALA A 313    14870  10353  16864    -84  -1425   -397       C  
ATOM   1056  N   LYS A 314      25.960 -12.867 -29.743  1.00112.95           N  
ANISOU 1056  N   LYS A 314    15241  10352  17325   -234   -905    427       N  
ATOM   1057  CA  LYS A 314      25.855 -12.659 -31.180  1.00118.65           C  
ANISOU 1057  CA  LYS A 314    16132  10938  18011   -189   -701    767       C  
ATOM   1058  C   LYS A 314      26.189 -13.927 -31.961  1.00125.74           C  
ANISOU 1058  C   LYS A 314    17043  12090  18643   -183   -490    976       C  
ATOM   1059  O   LYS A 314      25.501 -14.260 -32.922  1.00128.02           O  
ANISOU 1059  O   LYS A 314    17524  12458  18662    -58   -393   1144       O  
ATOM   1060  CB  LYS A 314      26.770 -11.530 -31.641  1.00122.22           C  
ANISOU 1060  CB  LYS A 314    16558  11002  18878   -343   -605    949       C  
ATOM   1061  CG  LYS A 314      26.646 -11.247 -33.128  1.00122.79           C  
ANISOU 1061  CG  LYS A 314    16827  10932  18896   -289   -386   1323       C  
ATOM   1062  CD  LYS A 314      27.763 -10.362 -33.640  1.00124.09           C  
ANISOU 1062  CD  LYS A 314    16929  10751  19468   -469   -229   1558       C  
ATOM   1063  CE  LYS A 314      27.612 -10.123 -35.132  1.00125.32           C  
ANISOU 1063  CE  LYS A 314    17303  10794  19519   -402      4   1951       C  
ATOM   1064  NZ  LYS A 314      28.819  -9.496 -35.730  1.00127.83           N  
ANISOU 1064  NZ  LYS A 314    17543  10827  20199   -586    226   2235       N  
ATOM   1065  N   GLU A 315      27.244 -14.630 -31.552  1.00128.65           N  
ANISOU 1065  N   GLU A 315    17209  12581  19092   -315   -424    963       N  
ATOM   1066  CA  GLU A 315      27.682 -15.837 -32.260  1.00130.62           C  
ANISOU 1066  CA  GLU A 315    17459  13040  19132   -311   -197   1152       C  
ATOM   1067  C   GLU A 315      26.713 -17.008 -32.109  1.00126.01           C  
ANISOU 1067  C   GLU A 315    16958  12788  18131   -160   -253   1034       C  
ATOM   1068  O   GLU A 315      26.884 -18.046 -32.745  1.00125.67           O  
ANISOU 1068  O   GLU A 315    16961  12913  17876   -133    -74   1166       O  
ATOM   1069  CB  GLU A 315      29.068 -16.274 -31.777  1.00138.47           C  
ANISOU 1069  CB  GLU A 315    18180  14071  20363   -478   -121   1169       C  
ATOM   1070  CG  GLU A 315      30.213 -15.403 -32.267  1.00147.98           C  
ANISOU 1070  CG  GLU A 315    19284  14972  21969   -646     31   1383       C  
ATOM   1071  CD  GLU A 315      31.565 -16.074 -32.099  1.00152.73           C  
ANISOU 1071  CD  GLU A 315    19616  15652  22762   -784    173   1479       C  
ATOM   1072  OE1 GLU A 315      31.601 -17.321 -31.995  1.00150.09           O  
ANISOU 1072  OE1 GLU A 315    19237  15596  22193   -719    238   1460       O  
ATOM   1073  OE2 GLU A 315      32.587 -15.352 -32.070  1.00157.40           O  
ANISOU 1073  OE2 GLU A 315    20029  16017  23759   -958    219   1579       O  
ATOM   1074  N   ILE A 316      25.693 -16.826 -31.278  1.00119.68           N  
ANISOU 1074  N   ILE A 316    16179  12068  17227    -63   -491    785       N  
ATOM   1075  CA  ILE A 316      24.799 -17.910 -30.890  1.00114.85           C  
ANISOU 1075  CA  ILE A 316    15592  11771  16272     58   -571    644       C  
ATOM   1076  C   ILE A 316      23.346 -17.623 -31.263  1.00115.53           C  
ANISOU 1076  C   ILE A 316    15874  11875  16146    227   -670    618       C  
ATOM   1077  O   ILE A 316      22.561 -18.544 -31.482  1.00112.71           O  
ANISOU 1077  O   ILE A 316    15592  11748  15484    325   -674    608       O  
ATOM   1078  CB  ILE A 316      24.907 -18.167 -29.370  1.00113.50           C  
ANISOU 1078  CB  ILE A 316    15225  11754  16148     24   -762    360       C  
ATOM   1079  CG1 ILE A 316      26.338 -18.566 -29.011  1.00119.02           C  
ANISOU 1079  CG1 ILE A 316    15707  12469  17047   -138   -686    407       C  
ATOM   1080  CG2 ILE A 316      23.951 -19.244 -28.909  1.00108.63           C  
ANISOU 1080  CG2 ILE A 316    14626  11452  15198    146   -837    228       C  
ATOM   1081  CD1 ILE A 316      26.832 -19.822 -29.721  1.00116.78           C  
ANISOU 1081  CD1 ILE A 316    15412  12344  16613   -140   -460    602       C  
ATOM   1082  N   TYR A 317      23.010 -16.339 -31.362  1.00117.04           N  
ANISOU 1082  N   TYR A 317    16138  11809  16522    258   -751    618       N  
ATOM   1083  CA  TYR A 317      21.626 -15.883 -31.512  1.00111.68           C  
ANISOU 1083  CA  TYR A 317    15599  11121  15714    430   -881    570       C  
ATOM   1084  C   TYR A 317      20.808 -16.630 -32.574  1.00107.19           C  
ANISOU 1084  C   TYR A 317    15200  10721  14806    540   -820    740       C  
ATOM   1085  O   TYR A 317      21.278 -16.838 -33.696  1.00106.07           O  
ANISOU 1085  O   TYR A 317    15176  10535  14592    498   -644    990       O  
ATOM   1086  CB  TYR A 317      21.612 -14.387 -31.823  1.00112.81           C  
ANISOU 1086  CB  TYR A 317    15820  10900  16142    438   -909    646       C  
ATOM   1087  CG  TYR A 317      20.586 -13.617 -31.023  1.00109.66           C  
ANISOU 1087  CG  TYR A 317    15422  10432  15812    571  -1111    413       C  
ATOM   1088  CD1 TYR A 317      20.837 -13.261 -29.707  1.00109.31           C  
ANISOU 1088  CD1 TYR A 317    15238  10354  15940    521  -1237    115       C  
ATOM   1089  CD2 TYR A 317      19.368 -13.250 -31.582  1.00105.63           C  
ANISOU 1089  CD2 TYR A 317    15051   9894  15189    753  -1174    490       C  
ATOM   1090  CE1 TYR A 317      19.907 -12.560 -28.967  1.00109.55           C  
ANISOU 1090  CE1 TYR A 317    15283  10317  16023    656  -1392   -114       C  
ATOM   1091  CE2 TYR A 317      18.432 -12.549 -30.852  1.00105.40           C  
ANISOU 1091  CE2 TYR A 317    15008   9794  15243    893  -1333    282       C  
ATOM   1092  CZ  TYR A 317      18.707 -12.207 -29.544  1.00108.15           C  
ANISOU 1092  CZ  TYR A 317    15231  10102  15758    848  -1427    -27       C  
ATOM   1093  OH  TYR A 317      17.779 -11.512 -28.802  1.00111.19           O  
ANISOU 1093  OH  TYR A 317    15615  10414  16216   1001  -1557   -253       O  
ATOM   1094  N   PRO A 318      19.583 -17.049 -32.197  1.00102.48           N  
ANISOU 1094  N   PRO A 318    14614  10326  13998    676   -965    597       N  
ATOM   1095  CA  PRO A 318      18.583 -17.806 -32.966  1.00103.78           C  
ANISOU 1095  CA  PRO A 318    14907  10687  13838    782   -980    690       C  
ATOM   1096  C   PRO A 318      18.425 -17.371 -34.424  1.00109.27           C  
ANISOU 1096  C   PRO A 318    15819  11243  14454    819   -905    979       C  
ATOM   1097  O   PRO A 318      18.243 -16.191 -34.706  1.00104.49           O  
ANISOU 1097  O   PRO A 318    15280  10395  14028    869   -948   1070       O  
ATOM   1098  CB  PRO A 318      17.280 -17.543 -32.200  1.00 91.89           C  
ANISOU 1098  CB  PRO A 318    13345   9267  12303    932  -1183    494       C  
ATOM   1099  CG  PRO A 318      17.689 -17.013 -30.856  1.00 85.87           C  
ANISOU 1099  CG  PRO A 318    12420   8432  11773    895  -1250    248       C  
ATOM   1100  CD  PRO A 318      19.175 -16.909 -30.792  1.00 89.16           C  
ANISOU 1100  CD  PRO A 318    12778   8718  12382    717  -1128    296       C  
ATOM   1101  N   GLY A 319      18.471 -18.340 -35.334  1.00113.08           N  
ANISOU 1101  N   GLY A 319    16425  11881  14659    798   -796   1119       N  
ATOM   1102  CA  GLY A 319      18.356 -18.075 -36.756  1.00113.89           C  
ANISOU 1102  CA  GLY A 319    16761  11897  14613    828   -716   1396       C  
ATOM   1103  C   GLY A 319      19.694 -18.308 -37.419  1.00114.76           C  
ANISOU 1103  C   GLY A 319    16930  11925  14749    698   -447   1572       C  
ATOM   1104  O   GLY A 319      19.771 -18.682 -38.592  1.00117.64           O  
ANISOU 1104  O   GLY A 319    17498  12327  14874    699   -316   1772       O  
ATOM   1105  N   GLN A 320      20.753 -18.095 -36.645  1.00111.09           N  
ANISOU 1105  N   GLN A 320    16280  11356  14575    586   -363   1494       N  
ATOM   1106  CA  GLN A 320      22.110 -18.313 -37.118  1.00110.05           C  
ANISOU 1106  CA  GLN A 320    16137  11144  14533    458    -96   1653       C  
ATOM   1107  C   GLN A 320      22.431 -19.790 -37.245  1.00104.30           C  
ANISOU 1107  C   GLN A 320    15405  10659  13566    428     38   1614       C  
ATOM   1108  O   GLN A 320      23.358 -20.174 -37.961  1.00 99.43           O  
ANISOU 1108  O   GLN A 320    14843  10015  12922    362    295   1780       O  
ATOM   1109  CB  GLN A 320      23.113 -17.653 -36.183  1.00114.87           C  
ANISOU 1109  CB  GLN A 320    16517  11578  15552    339    -85   1570       C  
ATOM   1110  CG  GLN A 320      23.505 -16.253 -36.592  1.00123.00           C  
ANISOU 1110  CG  GLN A 320    17589  12273  16871    299    -41   1746       C  
ATOM   1111  CD  GLN A 320      24.641 -15.726 -35.751  1.00131.24           C  
ANISOU 1111  CD  GLN A 320    18398  13145  18324    144    -18   1670       C  
ATOM   1112  OE1 GLN A 320      25.067 -16.376 -34.793  1.00131.23           O  
ANISOU 1112  OE1 GLN A 320    18198  13291  18372     82    -66   1474       O  
ATOM   1113  NE2 GLN A 320      25.142 -14.544 -36.098  1.00138.52           N  
ANISOU 1113  NE2 GLN A 320    19334  13748  19548     76     45   1833       N  
ATOM   1114  N   PHE A 321      21.665 -20.618 -36.544  1.00102.93           N  
ANISOU 1114  N   PHE A 321    15163  10712  13234    481   -121   1400       N  
ATOM   1115  CA  PHE A 321      21.891 -22.049 -36.596  1.00 95.44           C  
ANISOU 1115  CA  PHE A 321    14209   9975  12079    457     -9   1350       C  
ATOM   1116  C   PHE A 321      20.647 -22.845 -36.926  1.00 94.60           C  
ANISOU 1116  C   PHE A 321    14242  10072  11628    546   -137   1281       C  
ATOM   1117  O   PHE A 321      19.550 -22.540 -36.461  1.00 78.83           O  
ANISOU 1117  O   PHE A 321    12215   8134   9602    626   -371   1166       O  
ATOM   1118  CB  PHE A 321      22.472 -22.527 -35.279  1.00 99.10           C  
ANISOU 1118  CB  PHE A 321    14401  10524  12728    394    -41   1165       C  
ATOM   1119  CG  PHE A 321      23.882 -22.085 -35.056  1.00106.66           C  
ANISOU 1119  CG  PHE A 321    15203  11320  14004    279    112   1246       C  
ATOM   1120  CD1 PHE A 321      24.910 -22.607 -35.822  1.00109.70           C  
ANISOU 1120  CD1 PHE A 321    15619  11675  14389    220    397   1422       C  
ATOM   1121  CD2 PHE A 321      24.184 -21.151 -34.082  1.00108.33           C  
ANISOU 1121  CD2 PHE A 321    15231  11408  14523    227    -26   1139       C  
ATOM   1122  CE1 PHE A 321      26.215 -22.210 -35.619  1.00111.71           C  
ANISOU 1122  CE1 PHE A 321    15694  11784  14967    109    540   1513       C  
ATOM   1123  CE2 PHE A 321      25.487 -20.748 -33.874  1.00110.89           C  
ANISOU 1123  CE2 PHE A 321    15390  11581  15161    100     90   1213       C  
ATOM   1124  CZ  PHE A 321      26.505 -21.279 -34.643  1.00111.81           C  
ANISOU 1124  CZ  PHE A 321    15508  11675  15298     40    374   1412       C  
ATOM   1125  N   GLN A 322      20.845 -23.872 -37.746  1.00101.43           N  
ANISOU 1125  N   GLN A 322    15258  11037  12245    530     27   1350       N  
ATOM   1126  CA  GLN A 322      19.794 -24.819 -38.067  1.00102.80           C  
ANISOU 1126  CA  GLN A 322    15557  11406  12098    582    -83   1269       C  
ATOM   1127  C   GLN A 322      19.671 -25.862 -36.977  1.00 98.69           C  
ANISOU 1127  C   GLN A 322    14840  11058  11599    563   -143   1063       C  
ATOM   1128  O   GLN A 322      20.662 -26.482 -36.586  1.00 97.17           O  
ANISOU 1128  O   GLN A 322    14530  10873  11515    501     25   1043       O  
ATOM   1129  CB  GLN A 322      20.064 -25.494 -39.408  1.00109.88           C  
ANISOU 1129  CB  GLN A 322    16723  12321  12705    567    117   1406       C  
ATOM   1130  CG  GLN A 322      19.645 -24.655 -40.590  1.00124.26           C  
ANISOU 1130  CG  GLN A 322    18799  14051  14363    615     92   1601       C  
ATOM   1131  CD  GLN A 322      18.189 -24.226 -40.503  1.00133.57           C  
ANISOU 1131  CD  GLN A 322    20001  15301  15447    702   -234   1548       C  
ATOM   1132  OE1 GLN A 322      17.284 -25.051 -40.631  1.00137.66           O  
ANISOU 1132  OE1 GLN A 322    20581  15995  15729    722   -376   1445       O  
ATOM   1133  NE2 GLN A 322      17.958 -22.931 -40.270  1.00131.45           N  
ANISOU 1133  NE2 GLN A 322    19669  14886  15389    752   -352   1619       N  
ATOM   1134  N   PRO A 323      18.445 -26.043 -36.471  1.00 95.44           N  
ANISOU 1134  N   PRO A 323    14380  10784  11098    621   -381    926       N  
ATOM   1135  CA  PRO A 323      18.107 -27.105 -35.520  1.00 92.22           C  
ANISOU 1135  CA  PRO A 323    13814  10561  10665    611   -448    750       C  
ATOM   1136  C   PRO A 323      18.461 -28.490 -36.061  1.00 91.27           C  
ANISOU 1136  C   PRO A 323    13799  10521  10360    561   -279    759       C  
ATOM   1137  O   PRO A 323      18.577 -28.661 -37.278  1.00 92.65           O  
ANISOU 1137  O   PRO A 323    14213  10647  10344    552   -165    870       O  
ATOM   1138  CB  PRO A 323      16.594 -26.947 -35.348  1.00 88.89           C  
ANISOU 1138  CB  PRO A 323    13388  10250  10135    690   -706    667       C  
ATOM   1139  CG  PRO A 323      16.347 -25.496 -35.606  1.00 88.39           C  
ANISOU 1139  CG  PRO A 323    13367  10033  10184    754   -799    752       C  
ATOM   1140  CD  PRO A 323      17.321 -25.113 -36.686  1.00 90.84           C  
ANISOU 1140  CD  PRO A 323    13859  10175  10482    709   -600    947       C  
ATOM   1141  N   SER A 324      18.643 -29.456 -35.163  1.00 91.78           N  
ANISOU 1141  N   SER A 324    13698  10698  10477    533   -258    644       N  
ATOM   1142  CA  SER A 324      18.996 -30.819 -35.549  1.00 89.23           C  
ANISOU 1142  CA  SER A 324    13455  10427  10021    493    -92    638       C  
ATOM   1143  C   SER A 324      17.751 -31.639 -35.857  1.00 86.25           C  
ANISOU 1143  C   SER A 324    13188  10180   9405    500   -236    552       C  
ATOM   1144  O   SER A 324      16.626 -31.188 -35.625  1.00 80.28           O  
ANISOU 1144  O   SER A 324    12395   9497   8611    540   -469    501       O  
ATOM   1145  CB  SER A 324      19.799 -31.508 -34.445  1.00 84.15           C  
ANISOU 1145  CB  SER A 324    12576   9831   9566    463     -3    581       C  
ATOM   1146  OG  SER A 324      18.948 -31.947 -33.398  1.00 78.40           O  
ANISOU 1146  OG  SER A 324    11692   9260   8837    480   -188    449       O  
ATOM   1147  N   LEU A 325      17.961 -32.846 -36.376  1.00 82.88           N  
ANISOU 1147  N   LEU A 325    12884   9769   8835    460    -95    535       N  
ATOM   1148  CA  LEU A 325      16.869 -33.786 -36.584  1.00 80.19           C  
ANISOU 1148  CA  LEU A 325    12627   9541   8300    439   -228    436       C  
ATOM   1149  C   LEU A 325      16.042 -33.980 -35.308  1.00 85.64           C  
ANISOU 1149  C   LEU A 325    13063  10372   9105    450   -425    330       C  
ATOM   1150  O   LEU A 325      14.818 -34.107 -35.361  1.00 84.24           O  
ANISOU 1150  O   LEU A 325    12893  10292   8821    452   -629    272       O  
ATOM   1151  CB  LEU A 325      17.424 -35.123 -37.072  1.00 76.43           C  
ANISOU 1151  CB  LEU A 325    12284   9032   7725    391    -15    409       C  
ATOM   1152  CG  LEU A 325      16.440 -36.263 -37.344  1.00 78.13           C  
ANISOU 1152  CG  LEU A 325    12603   9326   7757    342   -124    294       C  
ATOM   1153  CD1 LEU A 325      15.253 -35.813 -38.179  1.00 72.11           C  
ANISOU 1153  CD1 LEU A 325    12014   8616   6768    337   -361    286       C  
ATOM   1154  CD2 LEU A 325      17.167 -37.388 -38.031  1.00 74.78           C  
ANISOU 1154  CD2 LEU A 325    12368   8811   7234    306    131    272       C  
ATOM   1155  N   CYS A 326      16.731 -33.976 -34.167  1.00 83.87           N  
ANISOU 1155  N   CYS A 326    12608  10163   9096    458   -361    313       N  
ATOM   1156  CA  CYS A 326      16.111 -34.147 -32.855  1.00 76.45           C  
ANISOU 1156  CA  CYS A 326    11427   9364   8255    475   -506    223       C  
ATOM   1157  C   CYS A 326      15.172 -33.008 -32.481  1.00 73.75           C  
ANISOU 1157  C   CYS A 326    11006   9074   7944    539   -724    188       C  
ATOM   1158  O   CYS A 326      14.076 -33.239 -31.964  1.00 72.35           O  
ANISOU 1158  O   CYS A 326    10727   9027   7735    559   -879    117       O  
ATOM   1159  CB  CYS A 326      17.175 -34.259 -31.770  1.00 76.46           C  
ANISOU 1159  CB  CYS A 326    11222   9371   8457    473   -398    228       C  
ATOM   1160  SG  CYS A 326      18.454 -35.466 -32.040  1.00 87.50           S  
ANISOU 1160  SG  CYS A 326    12652  10692   9900    429   -122    293       S  
ATOM   1161  N   HIS A 327      15.622 -31.778 -32.685  1.00 75.09           N  
ANISOU 1161  N   HIS A 327    11202   9128   8199    574   -721    243       N  
ATOM   1162  CA  HIS A 327      14.739 -30.652 -32.451  1.00 84.59           C  
ANISOU 1162  CA  HIS A 327    12356  10342   9444    650   -912    214       C  
ATOM   1163  C   HIS A 327      13.480 -30.848 -33.293  1.00 87.85           C  
ANISOU 1163  C   HIS A 327    12894  10814   9670    668  -1061    228       C  
ATOM   1164  O   HIS A 327      12.358 -30.773 -32.780  1.00 83.22           O  
ANISOU 1164  O   HIS A 327    12186  10344   9089    717  -1230    162       O  
ATOM   1165  CB  HIS A 327      15.414 -29.323 -32.795  1.00 87.08           C  
ANISOU 1165  CB  HIS A 327    12728  10478   9878    676   -876    294       C  
ATOM   1166  CG  HIS A 327      16.536 -28.952 -31.877  1.00 79.19           C  
ANISOU 1166  CG  HIS A 327    11572   9421   9094    651   -787    266       C  
ATOM   1167  ND1 HIS A 327      17.854 -28.945 -32.277  1.00 78.67           N  
ANISOU 1167  ND1 HIS A 327    11547   9228   9115    588   -595    363       N  
ATOM   1168  CD2 HIS A 327      16.532 -28.563 -30.581  1.00 75.61           C  
ANISOU 1168  CD2 HIS A 327    10920   9025   8785    676   -872    150       C  
ATOM   1169  CE1 HIS A 327      18.618 -28.571 -31.267  1.00 80.18           C  
ANISOU 1169  CE1 HIS A 327    11554   9401   9511    566   -589    312       C  
ATOM   1170  NE2 HIS A 327      17.841 -28.340 -30.222  1.00 80.41           N  
ANISOU 1170  NE2 HIS A 327    11450   9542   9561    618   -760    174       N  
ATOM   1171  N   LYS A 328      13.688 -31.125 -34.581  1.00 87.40           N  
ANISOU 1171  N   LYS A 328    13078  10686   9445    627   -993    314       N  
ATOM   1172  CA  LYS A 328      12.599 -31.345 -35.525  1.00 85.68           C  
ANISOU 1172  CA  LYS A 328    13012  10523   9020    625  -1149    334       C  
ATOM   1173  C   LYS A 328      11.664 -32.463 -35.048  1.00 81.02           C  
ANISOU 1173  C   LYS A 328    12308  10094   8382    584  -1257    228       C  
ATOM   1174  O   LYS A 328      10.436 -32.351 -35.143  1.00 73.68           O  
ANISOU 1174  O   LYS A 328    11332   9258   7405    610  -1469    211       O  
ATOM   1175  CB  LYS A 328      13.158 -31.676 -36.909  1.00 84.10           C  
ANISOU 1175  CB  LYS A 328    13112  10233   8611    572  -1021    422       C  
ATOM   1176  CG  LYS A 328      14.005 -30.579 -37.557  1.00 84.37           C  
ANISOU 1176  CG  LYS A 328    13280  10106   8672    607   -902    565       C  
ATOM   1177  CD  LYS A 328      14.614 -31.075 -38.882  1.00 91.16           C  
ANISOU 1177  CD  LYS A 328    14444  10897   9295    557   -725    646       C  
ATOM   1178  CE  LYS A 328      15.386 -29.987 -39.632  1.00 97.14           C  
ANISOU 1178  CE  LYS A 328    15348  11500  10061    589   -594    822       C  
ATOM   1179  NZ  LYS A 328      16.592 -29.466 -38.918  1.00 99.65           N  
ANISOU 1179  NZ  LYS A 328    15496  11700  10667    585   -403    860       N  
ATOM   1180  N   PHE A 329      12.256 -33.536 -34.528  1.00 80.76           N  
ANISOU 1180  N   PHE A 329    12215  10086   8385    519  -1107    171       N  
ATOM   1181  CA  PHE A 329      11.488 -34.661 -34.004  1.00 77.48           C  
ANISOU 1181  CA  PHE A 329    11683   9800   7955    468  -1176     87       C  
ATOM   1182  C   PHE A 329      10.545 -34.250 -32.866  1.00 75.27           C  
ANISOU 1182  C   PHE A 329    11136   9656   7806    533  -1331     37       C  
ATOM   1183  O   PHE A 329       9.348 -34.545 -32.910  1.00 77.17           O  
ANISOU 1183  O   PHE A 329    11312  10002   8005    522  -1497      9       O  
ATOM   1184  CB  PHE A 329      12.424 -35.768 -33.528  1.00 71.48           C  
ANISOU 1184  CB  PHE A 329    10888   9018   7252    408   -967     62       C  
ATOM   1185  CG  PHE A 329      11.708 -36.916 -32.903  1.00 75.81           C  
ANISOU 1185  CG  PHE A 329    11306   9679   7819    353  -1017     -4       C  
ATOM   1186  CD1 PHE A 329      10.883 -37.723 -33.660  1.00 79.21           C  
ANISOU 1186  CD1 PHE A 329    11859  10126   8112    273  -1112    -42       C  
ATOM   1187  CD2 PHE A 329      11.836 -37.180 -31.551  1.00 78.55           C  
ANISOU 1187  CD2 PHE A 329    11411  10117   8317    375   -977    -23       C  
ATOM   1188  CE1 PHE A 329      10.204 -38.775 -33.084  1.00 80.62           C  
ANISOU 1188  CE1 PHE A 329    11904  10389   8338    207  -1156    -92       C  
ATOM   1189  CE2 PHE A 329      11.154 -38.236 -30.966  1.00 73.38           C  
ANISOU 1189  CE2 PHE A 329    10633   9562   7686    323  -1009    -57       C  
ATOM   1190  CZ  PHE A 329      10.337 -39.029 -31.734  1.00 75.24           C  
ANISOU 1190  CZ  PHE A 329    10976   9793   7819    235  -1094    -88       C  
ATOM   1191  N   ILE A 330      11.086 -33.566 -31.859  1.00 71.15           N  
ANISOU 1191  N   ILE A 330    10460   9133   7442    598  -1273     21       N  
ATOM   1192  CA  ILE A 330      10.288 -33.054 -30.746  1.00 74.34           C  
ANISOU 1192  CA  ILE A 330    10634   9657   7955    680  -1387    -40       C  
ATOM   1193  C   ILE A 330       9.189 -32.102 -31.218  1.00 80.15           C  
ANISOU 1193  C   ILE A 330    11375  10400   8680    763  -1578    -21       C  
ATOM   1194  O   ILE A 330       8.057 -32.128 -30.716  1.00 78.09           O  
ANISOU 1194  O   ILE A 330    10949  10268   8454    809  -1701    -59       O  
ATOM   1195  CB  ILE A 330      11.174 -32.321 -29.720  1.00 73.93           C  
ANISOU 1195  CB  ILE A 330    10467   9574   8047    734  -1304    -75       C  
ATOM   1196  CG1 ILE A 330      12.338 -33.217 -29.309  1.00 69.90           C  
ANISOU 1196  CG1 ILE A 330     9941   9056   7564    660  -1129    -66       C  
ATOM   1197  CG2 ILE A 330      10.358 -31.864 -28.505  1.00 65.21           C  
ANISOU 1197  CG2 ILE A 330     9147   8604   7025    825  -1396   -164       C  
ATOM   1198  CD1 ILE A 330      13.235 -32.614 -28.278  1.00 68.04           C  
ANISOU 1198  CD1 ILE A 330     9582   8809   7462    691  -1076   -102       C  
ATOM   1199  N   ALA A 331       9.542 -31.260 -32.185  1.00 82.13           N  
ANISOU 1199  N   ALA A 331    11806  10507   8892    788  -1592     57       N  
ATOM   1200  CA  ALA A 331       8.614 -30.291 -32.754  1.00 80.54           C  
ANISOU 1200  CA  ALA A 331    11633  10285   8685    878  -1772    110       C  
ATOM   1201  C   ALA A 331       7.382 -30.962 -33.360  1.00 78.84           C  
ANISOU 1201  C   ALA A 331    11420  10189   8348    843  -1949    126       C  
ATOM   1202  O   ALA A 331       6.251 -30.508 -33.145  1.00 78.94           O  
ANISOU 1202  O   ALA A 331    11285  10282   8426    927  -2116    126       O  
ATOM   1203  CB  ALA A 331       9.316 -29.451 -33.798  1.00 79.25           C  
ANISOU 1203  CB  ALA A 331    11695   9942   8475    890  -1733    224       C  
ATOM   1204  N   LEU A 332       7.600 -32.041 -34.111  1.00 73.32           N  
ANISOU 1204  N   LEU A 332    10881   9495   7484    718  -1912    132       N  
ATOM   1205  CA  LEU A 332       6.501 -32.703 -34.799  1.00 81.32           C  
ANISOU 1205  CA  LEU A 332    11925  10604   8370    655  -2100    137       C  
ATOM   1206  C   LEU A 332       5.545 -33.373 -33.805  1.00 89.24           C  
ANISOU 1206  C   LEU A 332    12649  11769   9490    639  -2170     62       C  
ATOM   1207  O   LEU A 332       4.322 -33.323 -33.985  1.00 91.25           O  
ANISOU 1207  O   LEU A 332    12791  12123   9757    655  -2378     80       O  
ATOM   1208  CB  LEU A 332       7.046 -33.718 -35.803  1.00 72.63           C  
ANISOU 1208  CB  LEU A 332    11089   9448   7061    520  -2024    131       C  
ATOM   1209  CG  LEU A 332       6.069 -34.668 -36.509  1.00 76.67           C  
ANISOU 1209  CG  LEU A 332    11663  10044   7425    409  -2208     96       C  
ATOM   1210  CD1 LEU A 332       4.870 -33.932 -37.081  1.00 76.12           C  
ANISOU 1210  CD1 LEU A 332    11560  10046   7316    466  -2500    168       C  
ATOM   1211  CD2 LEU A 332       6.784 -35.449 -37.603  1.00 74.95           C  
ANISOU 1211  CD2 LEU A 332    11772   9731   6975    298  -2104     77       C  
ATOM   1212  N  BSER A 333       6.103 -33.979 -32.769  0.36 86.11           N  
ANISOU 1212  N  BSER A 333    12131  11402   9183    611  -1998     -2       N  
ATOM   1213  N  CSER A 333       6.100 -33.980 -32.768  0.64 86.42           N  
ANISOU 1213  N  CSER A 333    12170  11442   9223    611  -1998     -2       N  
ATOM   1214  CA BSER A 333       5.299 -34.645 -31.752  0.36 84.22           C  
ANISOU 1214  CA BSER A 333    11632  11317   9051    596  -2022    -52       C  
ATOM   1215  CA CSER A 333       5.297 -34.651 -31.751  0.64 82.06           C  
ANISOU 1215  CA CSER A 333    11358  11044   8777    595  -2022    -52       C  
ATOM   1216  C  BSER A 333       4.435 -33.649 -30.992  0.36 84.01           C  
ANISOU 1216  C  BSER A 333    11374  11382   9165    743  -2116    -55       C  
ATOM   1217  C  CSER A 333       4.456 -33.660 -30.954  0.64 84.10           C  
ANISOU 1217  C  CSER A 333    11381  11393   9178    743  -2110    -57       C  
ATOM   1218  O  BSER A 333       3.355 -33.993 -30.509  0.36 84.83           O  
ANISOU 1218  O  BSER A 333    11263  11626   9343    748  -2201    -65       O  
ATOM   1219  O  CSER A 333       3.414 -34.019 -30.406  0.64 84.92           O  
ANISOU 1219  O  CSER A 333    11266  11640   9360    749  -2184    -70       O  
ATOM   1220  CB BSER A 333       6.186 -35.412 -30.777  0.36 77.65           C  
ANISOU 1220  CB BSER A 333    10736  10495   8273    553  -1809    -94       C  
ATOM   1221  CB CSER A 333       6.194 -35.443 -30.814  0.64 77.11           C  
ANISOU 1221  CB CSER A 333    10674  10423   8199    548  -1809    -93       C  
ATOM   1222  OG BSER A 333       5.405 -35.961 -29.733  0.36 79.45           O  
ANISOU 1222  OG BSER A 333    10711  10878   8597    551  -1817   -119       O  
ATOM   1223  OG CSER A 333       7.294 -34.646 -30.426  0.64 76.15           O  
ANISOU 1223  OG CSER A 333    10593  10218   8124    623  -1680    -95       O  
ATOM   1224  N   ASP A 334       4.916 -32.413 -30.888  1.00 83.60           N  
ANISOU 1224  N   ASP A 334    11363  11238   9164    864  -2088    -47       N  
ATOM   1225  CA  ASP A 334       4.150 -31.359 -30.248  1.00 81.81           C  
ANISOU 1225  CA  ASP A 334    10949  11058   9076   1023  -2163    -63       C  
ATOM   1226  C   ASP A 334       3.078 -30.849 -31.216  1.00 83.72           C  
ANISOU 1226  C   ASP A 334    11201  11302   9307   1075  -2388     22       C  
ATOM   1227  O   ASP A 334       2.015 -30.376 -30.797  1.00 79.26           O  
ANISOU 1227  O   ASP A 334    10425  10826   8865   1188  -2488     24       O  
ATOM   1228  CB  ASP A 334       5.062 -30.223 -29.788  1.00 82.85           C  
ANISOU 1228  CB  ASP A 334    11131  11062   9287   1124  -2060    -99       C  
ATOM   1229  CG  ASP A 334       4.360 -29.257 -28.844  1.00 88.79           C  
ANISOU 1229  CG  ASP A 334    11682  11861  10191   1293  -2090   -163       C  
ATOM   1230  OD1 ASP A 334       3.286 -29.622 -28.305  1.00 97.09           O  
ANISOU 1230  OD1 ASP A 334    12524  13076  11290   1332  -2136   -183       O  
ATOM   1231  OD2 ASP A 334       4.887 -28.141 -28.637  1.00 80.47           O  
ANISOU 1231  OD2 ASP A 334    10681  10673   9221   1386  -2054   -195       O  
ATOM   1232  N   LYS A 335       3.353 -30.953 -32.514  1.00 86.20           N  
ANISOU 1232  N   LYS A 335    11758  11525   9468    999  -2466     99       N  
ATOM   1233  CA  LYS A 335       2.348 -30.599 -33.511  1.00 89.90           C  
ANISOU 1233  CA  LYS A 335    12252  12015   9889   1029  -2710    195       C  
ATOM   1234  C   LYS A 335       1.207 -31.600 -33.450  1.00 91.57           C  
ANISOU 1234  C   LYS A 335    12285  12398  10110    942  -2851    178       C  
ATOM   1235  O   LYS A 335       0.038 -31.247 -33.629  1.00 91.76           O  
ANISOU 1235  O   LYS A 335    12146  12506  10213   1010  -3054    237       O  
ATOM   1236  CB  LYS A 335       2.942 -30.559 -34.922  1.00 89.95           C  
ANISOU 1236  CB  LYS A 335    12592  11904   9682    958  -2753    281       C  
ATOM   1237  CG  LYS A 335       1.902 -30.304 -36.008  1.00 98.76           C  
ANISOU 1237  CG  LYS A 335    13754  13065  10704    973  -3038    391       C  
ATOM   1238  CD  LYS A 335       2.498 -30.353 -37.411  1.00102.91           C  
ANISOU 1238  CD  LYS A 335    14641  13497  10964    896  -3069    473       C  
ATOM   1239  CE  LYS A 335       1.464 -29.986 -38.467  1.00104.93           C  
ANISOU 1239  CE  LYS A 335    14949  13810  11110    926  -3382    599       C  
ATOM   1240  NZ  LYS A 335       2.031 -29.041 -39.474  1.00106.52           N  
ANISOU 1240  NZ  LYS A 335    15431  13876  11167    995  -3387    749       N  
ATOM   1241  N   GLU A 336       1.561 -32.851 -33.175  1.00 91.74           N  
ANISOU 1241  N   GLU A 336    12320  12461  10077    790  -2741    107       N  
ATOM   1242  CA  GLU A 336       0.594 -33.936 -33.149  1.00 94.56           C  
ANISOU 1242  CA  GLU A 336    12525  12951  10452    669  -2857     89       C  
ATOM   1243  C   GLU A 336      -0.163 -34.016 -31.833  1.00 92.55           C  
ANISOU 1243  C   GLU A 336    11917  12841  10406    737  -2805     62       C  
ATOM   1244  O   GLU A 336      -1.045 -34.857 -31.673  1.00 91.28           O  
ANISOU 1244  O   GLU A 336    11576  12797  10310    642  -2887     64       O  
ATOM   1245  CB  GLU A 336       1.294 -35.258 -33.430  1.00102.18           C  
ANISOU 1245  CB  GLU A 336    13667  13869  11289    480  -2748     30       C  
ATOM   1246  CG  GLU A 336       1.968 -35.279 -34.783  1.00112.93           C  
ANISOU 1246  CG  GLU A 336    15389  15102  12419    411  -2782     47       C  
ATOM   1247  CD  GLU A 336       1.997 -36.657 -35.398  1.00124.46           C  
ANISOU 1247  CD  GLU A 336    17000  16544  13746    213  -2801    -17       C  
ATOM   1248  OE1 GLU A 336       2.135 -37.644 -34.637  1.00126.93           O  
ANISOU 1248  OE1 GLU A 336    17199  16876  14151    130  -2665    -78       O  
ATOM   1249  OE2 GLU A 336       1.873 -36.747 -36.642  1.00128.87           O  
ANISOU 1249  OE2 GLU A 336    17801  17063  14102    143  -2953     -7       O  
ATOM   1250  N   GLY A 337       0.190 -33.135 -30.899  1.00 89.91           N  
ANISOU 1250  N   GLY A 337    11491  12495  10175    896  -2662     35       N  
ATOM   1251  CA  GLY A 337      -0.508 -33.017 -29.631  1.00 80.56           C  
ANISOU 1251  CA  GLY A 337     9995  11450   9162    997  -2590      4       C  
ATOM   1252  C   GLY A 337      -0.013 -34.000 -28.601  1.00 78.45           C  
ANISOU 1252  C   GLY A 337     9659  11253   8896    913  -2383    -54       C  
ATOM   1253  O   GLY A 337      -0.651 -34.224 -27.574  1.00 80.38           O  
ANISOU 1253  O   GLY A 337     9650  11642   9249    958  -2310    -65       O  
ATOM   1254  N   LYS A 338       1.138 -34.592 -28.886  1.00 81.41           N  
ANISOU 1254  N   LYS A 338    10260  11525   9148    799  -2278    -76       N  
ATOM   1255  CA  LYS A 338       1.662 -35.683 -28.075  1.00 79.38           C  
ANISOU 1255  CA  LYS A 338     9961  11315   8886    703  -2100   -103       C  
ATOM   1256  C   LYS A 338       2.646 -35.202 -27.030  1.00 77.26           C  
ANISOU 1256  C   LYS A 338     9692  11038   8625    799  -1913   -154       C  
ATOM   1257  O   LYS A 338       2.803 -35.838 -25.996  1.00 80.31           O  
ANISOU 1257  O   LYS A 338     9957  11522   9033    781  -1777   -164       O  
ATOM   1258  CB  LYS A 338       2.335 -36.735 -28.958  1.00 77.09           C  
ANISOU 1258  CB  LYS A 338     9899  10913   8478    526  -2084    -97       C  
ATOM   1259  CG  LYS A 338       1.380 -37.688 -29.635  1.00 78.70           C  
ANISOU 1259  CG  LYS A 338    10069  11152   8681    378  -2238    -75       C  
ATOM   1260  CD  LYS A 338       2.160 -38.714 -30.435  1.00 85.50           C  
ANISOU 1260  CD  LYS A 338    11190  11879   9419    216  -2187   -100       C  
ATOM   1261  CE  LYS A 338       1.270 -39.844 -30.907  1.00 95.46           C  
ANISOU 1261  CE  LYS A 338    12409  13163  10698     41  -2320   -106       C  
ATOM   1262  NZ  LYS A 338       2.005 -40.698 -31.877  1.00103.11           N  
ANISOU 1262  NZ  LYS A 338    13683  13973  11522   -100  -2285   -158       N  
ATOM   1263  N   LEU A 339       3.312 -34.086 -27.307  1.00 76.74           N  
ANISOU 1263  N   LEU A 339     9764  10854   8540    893  -1915   -179       N  
ATOM   1264  CA  LEU A 339       4.290 -33.544 -26.378  1.00 73.48           C  
ANISOU 1264  CA  LEU A 339     9360  10417   8142    968  -1771   -242       C  
ATOM   1265  C   LEU A 339       3.609 -32.851 -25.216  1.00 76.99           C  
ANISOU 1265  C   LEU A 339     9592  10989   8672   1120  -1749   -305       C  
ATOM   1266  O   LEU A 339       2.908 -31.858 -25.386  1.00 83.52           O  
ANISOU 1266  O   LEU A 339    10366  11798   9571   1246  -1841   -319       O  
ATOM   1267  CB  LEU A 339       5.224 -32.570 -27.072  1.00 68.47           C  
ANISOU 1267  CB  LEU A 339     8935   9593   7488   1002  -1779   -245       C  
ATOM   1268  CG  LEU A 339       6.354 -32.073 -26.183  1.00 66.72           C  
ANISOU 1268  CG  LEU A 339     8727   9330   7296   1044  -1650   -313       C  
ATOM   1269  CD1 LEU A 339       7.342 -33.178 -25.953  1.00 69.05           C  
ANISOU 1269  CD1 LEU A 339     9068   9632   7536    923  -1520   -291       C  
ATOM   1270  CD2 LEU A 339       7.037 -30.898 -26.808  1.00 69.53           C  
ANISOU 1270  CD2 LEU A 339     9242   9493   7684   1092  -1675   -311       C  
ATOM   1271  N   LEU A 340       3.810 -33.401 -24.031  1.00 73.63           N  
ANISOU 1271  N   LEU A 340     9050  10695   8233   1116  -1616   -338       N  
ATOM   1272  CA  LEU A 340       3.326 -32.779 -22.820  1.00 78.08           C  
ANISOU 1272  CA  LEU A 340     9443  11388   8836   1263  -1556   -417       C  
ATOM   1273  C   LEU A 340       4.262 -31.644 -22.474  1.00 78.12           C  
ANISOU 1273  C   LEU A 340     9563  11280   8839   1352  -1529   -523       C  
ATOM   1274  O   LEU A 340       3.822 -30.546 -22.155  1.00 89.21           O  
ANISOU 1274  O   LEU A 340    10920  12667  10307   1502  -1553   -606       O  
ATOM   1275  CB  LEU A 340       3.256 -33.786 -21.678  1.00 78.17           C  
ANISOU 1275  CB  LEU A 340     9312  11589   8800   1224  -1422   -400       C  
ATOM   1276  CG  LEU A 340       2.874 -33.278 -20.290  1.00 69.63           C  
ANISOU 1276  CG  LEU A 340     8080  10671   7704   1372  -1321   -487       C  
ATOM   1277  CD1 LEU A 340       1.401 -32.924 -20.235  1.00 71.45           C  
ANISOU 1277  CD1 LEU A 340     8111  11002   8035   1484  -1351   -479       C  
ATOM   1278  CD2 LEU A 340       3.210 -34.335 -19.270  1.00 69.22           C  
ANISOU 1278  CD2 LEU A 340     7959  10779   7561   1307  -1184   -441       C  
ATOM   1279  N   ARG A 341       5.560 -31.914 -22.557  1.00 69.02           N  
ANISOU 1279  N   ARG A 341     8554  10037   7632   1257  -1478   -518       N  
ATOM   1280  CA  ARG A 341       6.565 -30.899 -22.278  1.00 74.48           C  
ANISOU 1280  CA  ARG A 341     9350  10606   8344   1306  -1464   -611       C  
ATOM   1281  C   ARG A 341       7.961 -31.339 -22.704  1.00 74.16           C  
ANISOU 1281  C   ARG A 341     9454  10448   8276   1177  -1418   -559       C  
ATOM   1282  O   ARG A 341       8.324 -32.499 -22.569  1.00 78.84           O  
ANISOU 1282  O   ARG A 341    10031  11113   8814   1077  -1349   -490       O  
ATOM   1283  CB  ARG A 341       6.571 -30.549 -20.787  1.00 81.80           C  
ANISOU 1283  CB  ARG A 341    10168  11674   9239   1402  -1396   -738       C  
ATOM   1284  CG  ARG A 341       7.129 -29.163 -20.445  1.00 82.62           C  
ANISOU 1284  CG  ARG A 341    10348  11645   9399   1493  -1423   -883       C  
ATOM   1285  CD  ARG A 341       6.033 -28.107 -20.383  1.00 84.40           C  
ANISOU 1285  CD  ARG A 341    10513  11845   9709   1664  -1465   -967       C  
ATOM   1286  NE  ARG A 341       4.916 -28.516 -19.541  1.00 85.77           N  
ANISOU 1286  NE  ARG A 341    10503  12248   9837   1754  -1400   -990       N  
ATOM   1287  CZ  ARG A 341       3.763 -27.860 -19.464  1.00 88.76           C  
ANISOU 1287  CZ  ARG A 341    10775  12649  10300   1911  -1410  -1032       C  
ATOM   1288  NH1 ARG A 341       3.578 -26.751 -20.172  1.00 92.53           N  
ANISOU 1288  NH1 ARG A 341    11322  12926  10911   2001  -1497  -1055       N  
ATOM   1289  NH2 ARG A 341       2.794 -28.313 -18.683  1.00 87.41           N  
ANISOU 1289  NH2 ARG A 341    10421  12699  10094   1985  -1322  -1035       N  
ATOM   1290  N   ASN A 342       8.729 -30.396 -23.235  1.00 72.96           N  
ANISOU 1290  N   ASN A 342     9434  10105   8184   1183  -1447   -580       N  
ATOM   1291  CA  ASN A 342      10.152 -30.580 -23.474  1.00 71.53           C  
ANISOU 1291  CA  ASN A 342     9359   9809   8012   1082  -1385   -542       C  
ATOM   1292  C   ASN A 342      10.943 -29.777 -22.449  1.00 79.40           C  
ANISOU 1292  C   ASN A 342    10322  10790   9057   1119  -1378   -662       C  
ATOM   1293  O   ASN A 342      11.006 -28.557 -22.530  1.00 93.85           O  
ANISOU 1293  O   ASN A 342    12200  12483  10975   1182  -1432   -739       O  
ATOM   1294  CB  ASN A 342      10.530 -30.148 -24.898  1.00 70.10           C  
ANISOU 1294  CB  ASN A 342     9354   9413   7867   1041  -1407   -456       C  
ATOM   1295  CG  ASN A 342      12.036 -30.254 -25.178  1.00 74.60           C  
ANISOU 1295  CG  ASN A 342    10016   9854   8475    945  -1315   -406       C  
ATOM   1296  OD1 ASN A 342      12.788 -30.844 -24.399  1.00 78.90           O  
ANISOU 1296  OD1 ASN A 342    10486  10475   9019    898  -1247   -418       O  
ATOM   1297  ND2 ASN A 342      12.475 -29.693 -26.306  1.00 69.20           N  
ANISOU 1297  ND2 ASN A 342     9486   8979   7829    921  -1308   -332       N  
ATOM   1298  N   TYR A 343      11.536 -30.454 -21.474  1.00 65.09           N  
ANISOU 1298  N   TYR A 343     8429   9112   7190   1078  -1324   -678       N  
ATOM   1299  CA  TYR A 343      12.422 -29.793 -20.520  1.00 65.69           C  
ANISOU 1299  CA  TYR A 343     8481   9183   7294   1085  -1343   -791       C  
ATOM   1300  C   TYR A 343      13.857 -29.836 -21.053  1.00 65.23           C  
ANISOU 1300  C   TYR A 343     8490   8967   7326    973  -1313   -713       C  
ATOM   1301  O   TYR A 343      14.315 -30.892 -21.484  1.00 85.40           O  
ANISOU 1301  O   TYR A 343    11051  11534   9862    893  -1236   -580       O  
ATOM   1302  CB  TYR A 343      12.346 -30.468 -19.143  1.00 66.67           C  
ANISOU 1302  CB  TYR A 343     8481   9555   7294   1104  -1317   -834       C  
ATOM   1303  CG  TYR A 343      11.031 -30.312 -18.399  1.00 70.55           C  
ANISOU 1303  CG  TYR A 343     8889  10219   7699   1228  -1317   -925       C  
ATOM   1304  CD1 TYR A 343       9.934 -31.109 -18.702  1.00 75.64           C  
ANISOU 1304  CD1 TYR A 343     9467  10968   8306   1243  -1275   -830       C  
ATOM   1305  CD2 TYR A 343      10.898 -29.386 -17.374  1.00 73.02           C  
ANISOU 1305  CD2 TYR A 343     9182  10588   7973   1326  -1351  -1110       C  
ATOM   1306  CE1 TYR A 343       8.731 -30.975 -18.011  1.00 78.95           C  
ANISOU 1306  CE1 TYR A 343     9777  11550   8669   1358  -1253   -895       C  
ATOM   1307  CE2 TYR A 343       9.703 -29.245 -16.681  1.00 78.47           C  
ANISOU 1307  CE2 TYR A 343     9791  11439   8585   1455  -1316  -1192       C  
ATOM   1308  CZ  TYR A 343       8.622 -30.041 -17.003  1.00 82.38           C  
ANISOU 1308  CZ  TYR A 343    10196  12044   9061   1473  -1260  -1073       C  
ATOM   1309  OH  TYR A 343       7.436 -29.904 -16.311  1.00 85.75           O  
ANISOU 1309  OH  TYR A 343    10514  12635   9433   1603  -1205  -1137       O  
ATOM   1310  N   THR A 344      14.579 -28.716 -21.040  1.00 66.10           N  
ANISOU 1310  N   THR A 344     8644   8916   7554    964  -1363   -790       N  
ATOM   1311  CA  THR A 344      15.942 -28.727 -21.593  1.00 74.74           C  
ANISOU 1311  CA  THR A 344     9776   9856   8766    854  -1319   -695       C  
ATOM   1312  C   THR A 344      16.990 -28.039 -20.710  1.00 75.22           C  
ANISOU 1312  C   THR A 344     9776   9882   8922    810  -1386   -800       C  
ATOM   1313  O   THR A 344      16.680 -27.120 -19.954  1.00 68.21           O  
ANISOU 1313  O   THR A 344     8880   8999   8039    869  -1480   -975       O  
ATOM   1314  CB  THR A 344      15.978 -28.088 -23.022  1.00 79.48           C  
ANISOU 1314  CB  THR A 344    10519  10215   9465    839  -1291   -608       C  
ATOM   1315  OG1 THR A 344      17.318 -27.709 -23.366  1.00 74.43           O  
ANISOU 1315  OG1 THR A 344     9897   9404   8977    745  -1248   -548       O  
ATOM   1316  CG2 THR A 344      15.069 -26.877 -23.103  1.00 83.90           C  
ANISOU 1316  CG2 THR A 344    11130  10683  10066    942  -1381   -711       C  
ATOM   1317  N   GLN A 345      18.230 -28.515 -20.810  1.00 77.46           N  
ANISOU 1317  N   GLN A 345    10012  10131   9287    707  -1339   -695       N  
ATOM   1318  CA  GLN A 345      19.361 -27.898 -20.132  1.00 82.78           C  
ANISOU 1318  CA  GLN A 345    10611  10754  10086    636  -1419   -766       C  
ATOM   1319  C   GLN A 345      20.021 -26.854 -21.032  1.00 85.82           C  
ANISOU 1319  C   GLN A 345    11065  10854  10689    574  -1406   -736       C  
ATOM   1320  O   GLN A 345      20.777 -26.000 -20.557  1.00 83.01           O  
ANISOU 1320  O   GLN A 345    10664  10400  10478    512  -1499   -830       O  
ATOM   1321  CB  GLN A 345      20.392 -28.953 -19.733  1.00 87.10           C  
ANISOU 1321  CB  GLN A 345    11034  11418  10643    561  -1381   -645       C  
ATOM   1322  CG  GLN A 345      19.832 -30.198 -19.070  1.00 90.46           C  
ANISOU 1322  CG  GLN A 345    11399  12097  10874    611  -1352   -601       C  
ATOM   1323  CD  GLN A 345      20.906 -31.242 -18.815  1.00 96.70           C  
ANISOU 1323  CD  GLN A 345    12069  12963  11710    548  -1302   -445       C  
ATOM   1324  OE1 GLN A 345      21.656 -31.607 -19.724  1.00 98.07           O  
ANISOU 1324  OE1 GLN A 345    12246  12996  12022    493  -1185   -297       O  
ATOM   1325  NE2 GLN A 345      20.991 -31.724 -17.576  1.00100.78           N  
ANISOU 1325  NE2 GLN A 345    12480  13704  12109    565  -1383   -469       N  
ATOM   1326  N   ASN A 346      19.736 -26.953 -22.334  1.00 88.28           N  
ANISOU 1326  N   ASN A 346    11491  11034  11018    583  -1295   -599       N  
ATOM   1327  CA  ASN A 346      20.333 -26.101 -23.362  1.00 88.33           C  
ANISOU 1327  CA  ASN A 346    11580  10773  11208    528  -1241   -514       C  
ATOM   1328  C   ASN A 346      19.897 -24.655 -23.248  1.00 93.34           C  
ANISOU 1328  C   ASN A 346    12277  11244  11943    571  -1350   -651       C  
ATOM   1329  O   ASN A 346      18.838 -24.355 -22.694  1.00 99.84           O  
ANISOU 1329  O   ASN A 346    13119  12151  12663    677  -1438   -797       O  
ATOM   1330  CB  ASN A 346      19.969 -26.602 -24.767  1.00 93.82           C  
ANISOU 1330  CB  ASN A 346    12415  11402  11831    545  -1102   -340       C  
ATOM   1331  CG  ASN A 346      20.493 -27.994 -25.062  1.00 95.52           C  
ANISOU 1331  CG  ASN A 346    12596  11717  11978    501   -962   -203       C  
ATOM   1332  OD1 ASN A 346      21.431 -28.469 -24.423  1.00 97.87           O  
ANISOU 1332  OD1 ASN A 346    12756  12080  12352    443   -944   -183       O  
ATOM   1333  ND2 ASN A 346      19.892 -28.651 -26.050  1.00 94.89           N  
ANISOU 1333  ND2 ASN A 346    12647  11642  11762    529   -870   -109       N  
ATOM   1334  N   ILE A 347      20.718 -23.763 -23.791  1.00 94.92           N  
ANISOU 1334  N   ILE A 347    12506  11196  12362    493  -1329   -595       N  
ATOM   1335  CA  ILE A 347      20.362 -22.349 -23.900  1.00 92.63           C  
ANISOU 1335  CA  ILE A 347    12298  10685  12210    529  -1409   -690       C  
ATOM   1336  C   ILE A 347      20.451 -21.872 -25.349  1.00 96.05           C  
ANISOU 1336  C   ILE A 347    12868  10885  12741    518  -1297   -489       C  
ATOM   1337  O   ILE A 347      20.322 -20.680 -25.624  1.00 98.11           O  
ANISOU 1337  O   ILE A 347    13203  10915  13160    535  -1338   -511       O  
ATOM   1338  CB  ILE A 347      21.270 -21.455 -23.033  1.00 80.51           C  
ANISOU 1338  CB  ILE A 347    10672   9029  10888    432  -1521   -839       C  
ATOM   1339  CG1 ILE A 347      22.739 -21.751 -23.339  1.00 79.99           C  
ANISOU 1339  CG1 ILE A 347    10502   8893  10999    273  -1441   -684       C  
ATOM   1340  CG2 ILE A 347      20.966 -21.648 -21.563  1.00 75.63           C  
ANISOU 1340  CG2 ILE A 347     9968   8631  10135    471  -1661  -1075       C  
ATOM   1341  CD1 ILE A 347      23.717 -21.080 -22.417  1.00 84.45           C  
ANISOU 1341  CD1 ILE A 347    10937   9380  11769    149  -1579   -823       C  
ATOM   1342  N   ASP A 348      20.663 -22.803 -26.275  1.00 90.80           N  
ANISOU 1342  N   ASP A 348    12249  10274  11975    494  -1149   -293       N  
ATOM   1343  CA  ASP A 348      20.850 -22.447 -27.675  1.00 88.82           C  
ANISOU 1343  CA  ASP A 348    12145   9828  11774    477  -1022    -86       C  
ATOM   1344  C   ASP A 348      19.540 -21.950 -28.289  1.00 87.86           C  
ANISOU 1344  C   ASP A 348    12178   9663  11541    606  -1085    -74       C  
ATOM   1345  O   ASP A 348      19.530 -21.405 -29.395  1.00 81.19           O  
ANISOU 1345  O   ASP A 348    11476   8642  10730    613  -1019     90       O  
ATOM   1346  CB  ASP A 348      21.421 -23.637 -28.468  1.00 94.72           C  
ANISOU 1346  CB  ASP A 348    12920  10657  12413    426   -835     94       C  
ATOM   1347  CG  ASP A 348      20.723 -24.954 -28.162  1.00 98.52           C  
ANISOU 1347  CG  ASP A 348    13384  11402  12649    481   -845     44       C  
ATOM   1348  OD1 ASP A 348      19.476 -25.000 -28.196  1.00100.30           O  
ANISOU 1348  OD1 ASP A 348    13679  11716  12715    578   -938    -18       O  
ATOM   1349  OD2 ASP A 348      21.431 -25.951 -27.889  1.00 98.65           O  
ANISOU 1349  OD2 ASP A 348    13302  11528  12653    427   -757     79       O  
ATOM   1350  N   THR A 349      18.445 -22.142 -27.553  1.00 93.82           N  
ANISOU 1350  N   THR A 349    12895  10588  12166    711  -1209   -234       N  
ATOM   1351  CA  THR A 349      17.108 -21.664 -27.930  1.00 93.65           C  
ANISOU 1351  CA  THR A 349    12966  10551  12066    849  -1297   -242       C  
ATOM   1352  C   THR A 349      16.664 -22.155 -29.310  1.00 93.53           C  
ANISOU 1352  C   THR A 349    13104  10546  11885    870  -1231    -37       C  
ATOM   1353  O   THR A 349      15.716 -21.611 -29.905  1.00 74.14           O  
ANISOU 1353  O   THR A 349    10744   8033   9395    972  -1306     18       O  
ATOM   1354  CB  THR A 349      17.025 -20.128 -27.907  1.00 89.60           C  
ANISOU 1354  CB  THR A 349    12496   9772  11775    897  -1368   -287       C  
ATOM   1355  OG1 THR A 349      17.733 -19.603 -29.029  1.00103.30           O  
ANISOU 1355  OG1 THR A 349    14349  11275  13627    829  -1270    -76       O  
ATOM   1356  CG2 THR A 349      17.639 -19.593 -26.656  1.00 77.99           C  
ANISOU 1356  CG2 THR A 349    10906   8256  10472    847  -1433   -498       C  
ATOM   1357  N   LEU A 350      17.344 -23.197 -29.795  1.00 83.53           N  
ANISOU 1357  N   LEU A 350    11864   9360  10515    778  -1098     71       N  
ATOM   1358  CA  LEU A 350      17.019 -23.836 -31.062  1.00 79.24           C  
ANISOU 1358  CA  LEU A 350    11486   8849   9774    781  -1026    236       C  
ATOM   1359  C   LEU A 350      15.646 -24.477 -30.983  1.00 71.26           C  
ANISOU 1359  C   LEU A 350    10471   8037   8567    866  -1148    171       C  
ATOM   1360  O   LEU A 350      15.042 -24.787 -31.994  1.00 76.75           O  
ANISOU 1360  O   LEU A 350    11308   8759   9095    888  -1163    278       O  
ATOM   1361  CB  LEU A 350      18.082 -24.866 -31.428  1.00 71.44           C  
ANISOU 1361  CB  LEU A 350    10512   7899   8734    674   -838    325       C  
ATOM   1362  CG  LEU A 350      19.355 -24.246 -31.994  1.00 72.84           C  
ANISOU 1362  CG  LEU A 350    10731   7861   9085    593   -682    467       C  
ATOM   1363  CD1 LEU A 350      20.531 -25.194 -31.948  1.00 72.28           C  
ANISOU 1363  CD1 LEU A 350    10586   7833   9042    499   -496    517       C  
ATOM   1364  CD2 LEU A 350      19.096 -23.806 -33.408  1.00 79.36           C  
ANISOU 1364  CD2 LEU A 350    11788   8561   9806    622   -623    654       C  
ATOM   1365  N   GLU A 351      15.156 -24.653 -29.764  1.00 70.42           N  
ANISOU 1365  N   GLU A 351    10199   8076   8482    909  -1238     -3       N  
ATOM   1366  CA  GLU A 351      13.803 -25.130 -29.521  1.00 76.25           C  
ANISOU 1366  CA  GLU A 351    10886   8999   9086    994  -1353    -69       C  
ATOM   1367  C   GLU A 351      12.750 -24.219 -30.170  1.00 77.53           C  
ANISOU 1367  C   GLU A 351    11126   9077   9257   1109  -1477    -14       C  
ATOM   1368  O   GLU A 351      11.779 -24.709 -30.747  1.00 71.40           O  
ANISOU 1368  O   GLU A 351    10386   8408   8335   1145  -1554     41       O  
ATOM   1369  CB  GLU A 351      13.546 -25.255 -28.012  1.00 69.22           C  
ANISOU 1369  CB  GLU A 351     9803   8260   8239   1032  -1402   -259       C  
ATOM   1370  CG  GLU A 351      14.304 -26.391 -27.307  1.00 81.29           C  
ANISOU 1370  CG  GLU A 351    11236   9935   9717    938  -1312   -294       C  
ATOM   1371  CD  GLU A 351      15.819 -26.175 -27.209  1.00 92.95           C  
ANISOU 1371  CD  GLU A 351    12706  11282  11327    838  -1216   -264       C  
ATOM   1372  OE1 GLU A 351      16.245 -25.019 -26.995  1.00103.99           O  
ANISOU 1372  OE1 GLU A 351    14102  12517  12892    844  -1252   -310       O  
ATOM   1373  OE2 GLU A 351      16.581 -27.166 -27.341  1.00 89.76           O  
ANISOU 1373  OE2 GLU A 351    12289  10931  10883    753  -1103   -191       O  
ATOM   1374  N   GLN A 352      12.939 -22.902 -30.078  1.00 83.98           N  
ANISOU 1374  N   GLN A 352    11959   9691  10258   1165  -1508    -24       N  
ATOM   1375  CA  GLN A 352      11.975 -21.960 -30.651  1.00 81.59           C  
ANISOU 1375  CA  GLN A 352    11718   9283   9998   1294  -1625     45       C  
ATOM   1376  C   GLN A 352      12.203 -21.772 -32.136  1.00 82.04           C  
ANISOU 1376  C   GLN A 352    11983   9210   9978   1262  -1596    278       C  
ATOM   1377  O   GLN A 352      11.249 -21.670 -32.911  1.00 83.42           O  
ANISOU 1377  O   GLN A 352    12231   9412  10052   1341  -1708    385       O  
ATOM   1378  CB  GLN A 352      12.041 -20.617 -29.944  1.00 80.64           C  
ANISOU 1378  CB  GLN A 352    11545   8973  10123   1376  -1663    -63       C  
ATOM   1379  CG  GLN A 352      11.296 -20.581 -28.633  1.00 83.31           C  
ANISOU 1379  CG  GLN A 352    11708   9448  10497   1476  -1728   -286       C  
ATOM   1380  CD  GLN A 352      12.193 -20.856 -27.455  1.00 86.56           C  
ANISOU 1380  CD  GLN A 352    12023   9921  10946   1388  -1664   -463       C  
ATOM   1381  OE1 GLN A 352      13.329 -21.318 -27.612  1.00 85.14           O  
ANISOU 1381  OE1 GLN A 352    11872   9721  10755   1244  -1575   -408       O  
ATOM   1382  NE2 GLN A 352      11.695 -20.561 -26.260  1.00 89.61           N  
ANISOU 1382  NE2 GLN A 352    12291  10384  11374   1480  -1708   -672       N  
ATOM   1383  N   VAL A 353      13.474 -21.723 -32.520  1.00 75.64           N  
ANISOU 1383  N   VAL A 353    11261   8267   9212   1149  -1447    363       N  
ATOM   1384  CA  VAL A 353      13.853 -21.780 -33.927  1.00 81.86           C  
ANISOU 1384  CA  VAL A 353    12262   8967   9874   1101  -1365    587       C  
ATOM   1385  C   VAL A 353      13.143 -22.945 -34.619  1.00 84.10           C  
ANISOU 1385  C   VAL A 353    12630   9459   9865   1090  -1408    630       C  
ATOM   1386  O   VAL A 353      12.534 -22.769 -35.664  1.00 86.86           O  
ANISOU 1386  O   VAL A 353    13135   9797  10070   1135  -1488    774       O  
ATOM   1387  CB  VAL A 353      15.380 -21.933 -34.093  1.00 84.07           C  
ANISOU 1387  CB  VAL A 353    12578   9138  10227    965  -1153    652       C  
ATOM   1388  CG1 VAL A 353      15.796 -21.656 -35.526  1.00 82.74           C  
ANISOU 1388  CG1 VAL A 353    12641   8834   9963    938  -1043    899       C  
ATOM   1389  CG2 VAL A 353      16.112 -21.004 -33.131  1.00 86.57           C  
ANISOU 1389  CG2 VAL A 353    12757   9288  10848    941  -1137    551       C  
ATOM   1390  N   ALA A 354      13.194 -24.125 -34.002  1.00 89.51           N  
ANISOU 1390  N   ALA A 354    13212  10332  10466   1028  -1371    502       N  
ATOM   1391  CA  ALA A 354      12.609 -25.341 -34.567  1.00 87.34           C  
ANISOU 1391  CA  ALA A 354    13010  10236   9939    991  -1403    514       C  
ATOM   1392  C   ALA A 354      11.083 -25.404 -34.426  1.00 88.81           C  
ANISOU 1392  C   ALA A 354    13112  10567  10066   1083  -1623    465       C  
ATOM   1393  O   ALA A 354      10.442 -26.301 -34.978  1.00 90.60           O  
ANISOU 1393  O   ALA A 354    13398  10929  10096   1047  -1694    480       O  
ATOM   1394  CB  ALA A 354      13.240 -26.568 -33.928  1.00 84.39           C  
ANISOU 1394  CB  ALA A 354    12547   9982   9537    895  -1274    410       C  
ATOM   1395  N   GLY A 355      10.502 -24.464 -33.689  1.00 83.07           N  
ANISOU 1395  N   GLY A 355    12239   9804   9519   1198  -1728    401       N  
ATOM   1396  CA  GLY A 355       9.054 -24.350 -33.620  1.00 84.54           C  
ANISOU 1396  CA  GLY A 355    12326  10104   9691   1307  -1924    384       C  
ATOM   1397  C   GLY A 355       8.350 -25.171 -32.552  1.00 87.43           C  
ANISOU 1397  C   GLY A 355    12471  10687  10062   1314  -1962    224       C  
ATOM   1398  O   GLY A 355       7.178 -25.507 -32.707  1.00 90.10           O  
ANISOU 1398  O   GLY A 355    12731  11162  10340   1358  -2107    234       O  
ATOM   1399  N   ILE A 356       9.051 -25.481 -31.463  1.00 85.52           N  
ANISOU 1399  N   ILE A 356    12118  10480   9895   1269  -1837     91       N  
ATOM   1400  CA  ILE A 356       8.462 -26.224 -30.351  1.00 80.08           C  
ANISOU 1400  CA  ILE A 356    11223   9997   9208   1280  -1846    -45       C  
ATOM   1401  C   ILE A 356       7.766 -25.289 -29.371  1.00 83.30           C  
ANISOU 1401  C   ILE A 356    11464  10412   9776   1432  -1906   -157       C  
ATOM   1402  O   ILE A 356       8.420 -24.484 -28.711  1.00 84.77           O  
ANISOU 1402  O   ILE A 356    11637  10481  10092   1466  -1847   -244       O  
ATOM   1403  CB  ILE A 356       9.522 -27.028 -29.585  1.00 72.70           C  
ANISOU 1403  CB  ILE A 356    10246   9116   8259   1172  -1692   -124       C  
ATOM   1404  CG1 ILE A 356      10.328 -27.902 -30.547  1.00 69.27           C  
ANISOU 1404  CG1 ILE A 356     9983   8642   7693   1038  -1594    -21       C  
ATOM   1405  CG2 ILE A 356       8.864 -27.864 -28.504  1.00 76.81           C  
ANISOU 1405  CG2 ILE A 356    10570   9858   8755   1181  -1697   -229       C  
ATOM   1406  CD1 ILE A 356      11.625 -28.437 -29.959  1.00 67.62           C  
ANISOU 1406  CD1 ILE A 356     9748   8423   7522    947  -1428    -57       C  
ATOM   1407  N   GLN A 357       6.447 -25.406 -29.264  1.00 84.92           N  
ANISOU 1407  N   GLN A 357    11536  10751   9979   1522  -2019   -162       N  
ATOM   1408  CA  GLN A 357       5.681 -24.539 -28.381  1.00 90.98           C  
ANISOU 1408  CA  GLN A 357    12141  11528  10899   1692  -2055   -266       C  
ATOM   1409  C   GLN A 357       5.733 -24.970 -26.903  1.00 86.24           C  
ANISOU 1409  C   GLN A 357    11374  11088  10306   1700  -1952   -440       C  
ATOM   1410  O   GLN A 357       6.101 -24.183 -26.038  1.00 85.29           O  
ANISOU 1410  O   GLN A 357    11228  10895  10285   1772  -1898   -574       O  
ATOM   1411  CB  GLN A 357       4.226 -24.458 -28.858  1.00100.10           C  
ANISOU 1411  CB  GLN A 357    13191  12768  12076   1799  -2209   -182       C  
ATOM   1412  CG  GLN A 357       3.978 -23.422 -29.979  1.00104.59           C  
ANISOU 1412  CG  GLN A 357    13886  13147  12707   1886  -2334    -32       C  
ATOM   1413  CD  GLN A 357       3.854 -24.045 -31.375  1.00109.52           C  
ANISOU 1413  CD  GLN A 357    14661  13798  13153   1779  -2447    146       C  
ATOM   1414  OE1 GLN A 357       4.267 -25.185 -31.595  1.00116.94           O  
ANISOU 1414  OE1 GLN A 357    15666  14838  13929   1619  -2399    143       O  
ATOM   1415  NE2 GLN A 357       3.279 -23.296 -32.319  1.00104.03           N  
ANISOU 1415  NE2 GLN A 357    14034  13010  12485   1873  -2600    300       N  
ATOM   1416  N   ARG A 358       5.375 -26.211 -26.607  1.00 92.34           N  
ANISOU 1416  N   ARG A 358    12044  12073  10968   1622  -1927   -438       N  
ATOM   1417  CA  ARG A 358       5.240 -26.626 -25.212  1.00 88.45           C  
ANISOU 1417  CA  ARG A 358    11385  11758  10465   1649  -1834   -571       C  
ATOM   1418  C   ARG A 358       6.596 -26.936 -24.586  1.00 84.64           C  
ANISOU 1418  C   ARG A 358    10969  11258   9932   1544  -1721   -640       C  
ATOM   1419  O   ARG A 358       6.983 -28.089 -24.468  1.00 82.99           O  
ANISOU 1419  O   ARG A 358    10750  11160   9624   1424  -1660   -600       O  
ATOM   1420  CB  ARG A 358       4.293 -27.818 -25.127  1.00 89.80           C  
ANISOU 1420  CB  ARG A 358    11406  12150  10564   1604  -1847   -517       C  
ATOM   1421  CG  ARG A 358       3.014 -27.544 -25.910  1.00103.11           C  
ANISOU 1421  CG  ARG A 358    13018  13847  12313   1684  -1993   -425       C  
ATOM   1422  CD  ARG A 358       1.906 -28.496 -25.558  1.00114.89           C  
ANISOU 1422  CD  ARG A 358    14295  15562  13795   1667  -2007   -397       C  
ATOM   1423  NE  ARG A 358       1.921 -28.800 -24.136  1.00121.78           N  
ANISOU 1423  NE  ARG A 358    15023  16589  14659   1704  -1855   -506       N  
ATOM   1424  CZ  ARG A 358       1.612 -27.929 -23.182  1.00136.57           C  
ANISOU 1424  CZ  ARG A 358    16796  18487  16607   1874  -1788   -624       C  
ATOM   1425  NH1 ARG A 358       1.654 -28.301 -21.907  1.00143.70           N  
ANISOU 1425  NH1 ARG A 358    17592  19554  17453   1897  -1646   -717       N  
ATOM   1426  NH2 ARG A 358       1.265 -26.686 -23.499  1.00140.40           N  
ANISOU 1426  NH2 ARG A 358    17301  18830  17217   2028  -1857   -647       N  
ATOM   1427  N   ILE A 359       7.294 -25.880 -24.166  1.00 86.94           N  
ANISOU 1427  N   ILE A 359    11318  11402  10312   1594  -1702   -742       N  
ATOM   1428  CA  ILE A 359       8.680 -25.973 -23.707  1.00 84.41           C  
ANISOU 1428  CA  ILE A 359    11061  11030   9980   1489  -1630   -794       C  
ATOM   1429  C   ILE A 359       8.937 -25.290 -22.342  1.00 81.99           C  
ANISOU 1429  C   ILE A 359    10691  10751   9711   1562  -1606   -995       C  
ATOM   1430  O   ILE A 359       8.126 -24.490 -21.874  1.00 85.21           O  
ANISOU 1430  O   ILE A 359    11044  11153  10177   1711  -1630  -1106       O  
ATOM   1431  CB  ILE A 359       9.631 -25.361 -24.767  1.00 84.60           C  
ANISOU 1431  CB  ILE A 359    11259  10799  10085   1418  -1639   -701       C  
ATOM   1432  CG1 ILE A 359      11.088 -25.753 -24.494  1.00 88.63           C  
ANISOU 1432  CG1 ILE A 359    11806  11278  10592   1281  -1557   -703       C  
ATOM   1433  CG2 ILE A 359       9.432 -23.854 -24.867  1.00 83.91           C  
ANISOU 1433  CG2 ILE A 359    11220  10503  10158   1536  -1699   -759       C  
ATOM   1434  CD1 ILE A 359      12.078 -24.680 -24.808  1.00 94.61           C  
ANISOU 1434  CD1 ILE A 359    12663  11784  11500   1248  -1556   -705       C  
ATOM   1435  N   ILE A 360      10.061 -25.651 -21.715  1.00 81.54           N  
ANISOU 1435  N   ILE A 360    10641  10729   9613   1458  -1561  -1040       N  
ATOM   1436  CA  ILE A 360      10.553 -25.110 -20.446  1.00 70.74           C  
ANISOU 1436  CA  ILE A 360     9241   9393   8245   1486  -1561  -1233       C  
ATOM   1437  C   ILE A 360      12.090 -25.105 -20.453  1.00 85.35           C  
ANISOU 1437  C   ILE A 360    11149  11134  10146   1340  -1562  -1218       C  
ATOM   1438  O   ILE A 360      12.698 -26.161 -20.347  1.00 86.37           O  
ANISOU 1438  O   ILE A 360    11241  11383  10194   1237  -1517  -1127       O  
ATOM   1439  CB  ILE A 360      10.086 -25.950 -19.229  1.00 70.61           C  
ANISOU 1439  CB  ILE A 360     9096   9674   8060   1522  -1510  -1301       C  
ATOM   1440  CG1 ILE A 360       8.565 -26.009 -19.124  1.00 71.32           C  
ANISOU 1440  CG1 ILE A 360     9087   9891   8118   1664  -1488  -1307       C  
ATOM   1441  CG2 ILE A 360      10.693 -25.418 -17.946  1.00 71.81           C  
ANISOU 1441  CG2 ILE A 360     9245   9872   8168   1539  -1526  -1503       C  
ATOM   1442  CD1 ILE A 360       7.947 -24.761 -18.623  1.00 82.38           C  
ANISOU 1442  CD1 ILE A 360    10486  11218   9595   1832  -1503  -1487       C  
ATOM   1443  N   GLN A 361      12.726 -23.942 -20.573  1.00 78.87           N  
ANISOU 1443  N   GLN A 361    10405  10079   9482   1328  -1610  -1297       N  
ATOM   1444  CA  GLN A 361      14.194 -23.885 -20.600  1.00 73.44           C  
ANISOU 1444  CA  GLN A 361     9743   9280   8882   1180  -1614  -1271       C  
ATOM   1445  C   GLN A 361      14.772 -23.636 -19.212  1.00 85.65           C  
ANISOU 1445  C   GLN A 361    11230  10917  10395   1159  -1673  -1471       C  
ATOM   1446  O   GLN A 361      14.809 -22.505 -18.725  1.00 94.61           O  
ANISOU 1446  O   GLN A 361    12405  11919  11623   1201  -1742  -1658       O  
ATOM   1447  CB  GLN A 361      14.672 -22.809 -21.566  1.00 75.94           C  
ANISOU 1447  CB  GLN A 361    10168   9278   9408   1148  -1631  -1216       C  
ATOM   1448  CG  GLN A 361      15.440 -23.342 -22.758  1.00 85.50           C  
ANISOU 1448  CG  GLN A 361    11433  10394  10659   1029  -1553   -986       C  
ATOM   1449  CD  GLN A 361      14.914 -22.815 -24.096  1.00 90.34           C  
ANISOU 1449  CD  GLN A 361    12172  10821  11333   1077  -1539   -843       C  
ATOM   1450  OE1 GLN A 361      13.925 -22.068 -24.146  1.00 80.83           O  
ANISOU 1450  OE1 GLN A 361    10995   9556  10159   1206  -1599   -902       O  
ATOM   1451  NE2 GLN A 361      15.580 -23.205 -25.188  1.00 87.92           N  
ANISOU 1451  NE2 GLN A 361    11943  10425  11038    982  -1454   -647       N  
ATOM   1452  N   CYS A 362      15.242 -24.707 -18.588  1.00 89.88           N  
ANISOU 1452  N   CYS A 362    11681  11673  10797   1091  -1653  -1429       N  
ATOM   1453  CA  CYS A 362      15.579 -24.701 -17.170  1.00 95.41           C  
ANISOU 1453  CA  CYS A 362    12323  12543  11387   1089  -1720  -1602       C  
ATOM   1454  C   CYS A 362      16.713 -23.749 -16.780  1.00 96.91           C  
ANISOU 1454  C   CYS A 362    12534  12565  11722    995  -1831  -1738       C  
ATOM   1455  O   CYS A 362      16.650 -23.121 -15.722  1.00 97.58           O  
ANISOU 1455  O   CYS A 362    12633  12698  11744   1035  -1917  -1971       O  
ATOM   1456  CB  CYS A 362      15.922 -26.124 -16.729  1.00 98.32           C  
ANISOU 1456  CB  CYS A 362    12593  13165  11598   1031  -1676  -1469       C  
ATOM   1457  SG  CYS A 362      14.591 -27.325 -17.043  1.00100.42           S  
ANISOU 1457  SG  CYS A 362    12817  13629  11708   1116  -1555  -1322       S  
ATOM   1458  N   HIS A 363      17.743 -23.639 -17.616  1.00 99.60           N  
ANISOU 1458  N   HIS A 363    12879  12711  12256    866  -1825  -1601       N  
ATOM   1459  CA  HIS A 363      18.833 -22.705 -17.335  1.00103.24           C  
ANISOU 1459  CA  HIS A 363    13338  12985  12903    754  -1935  -1713       C  
ATOM   1460  C   HIS A 363      18.626 -21.407 -18.091  1.00102.46           C  
ANISOU 1460  C   HIS A 363    13348  12559  13023    777  -1939  -1760       C  
ATOM   1461  O   HIS A 363      19.580 -20.678 -18.349  1.00102.37           O  
ANISOU 1461  O   HIS A 363    13339  12316  13240    658  -1988  -1763       O  
ATOM   1462  CB  HIS A 363      20.193 -23.305 -17.696  1.00109.14           C  
ANISOU 1462  CB  HIS A 363    13989  13708  13769    592  -1919  -1526       C  
ATOM   1463  CG  HIS A 363      20.455 -24.632 -17.072  1.00114.17           C  
ANISOU 1463  CG  HIS A 363    14515  14639  14227    575  -1904  -1434       C  
ATOM   1464  ND1 HIS A 363      19.825 -25.048 -15.909  1.00115.02           N  
ANISOU 1464  ND1 HIS A 363    14600  15018  14084    659  -1955  -1560       N  
ATOM   1465  CD2 HIS A 363      21.257 -25.657 -17.438  1.00117.69           C  
ANISOU 1465  CD2 HIS A 363    14866  15144  14707    496  -1831  -1217       C  
ATOM   1466  CE1 HIS A 363      20.231 -26.256 -15.599  1.00117.91           C  
ANISOU 1466  CE1 HIS A 363    14865  15591  14345    626  -1925  -1411       C  
ATOM   1467  NE2 HIS A 363      21.105 -26.657 -16.514  1.00120.73           N  
ANISOU 1467  NE2 HIS A 363    15174  15818  14881    530  -1850  -1205       N  
ATOM   1468  N   GLY A 364      17.375 -21.131 -18.446  1.00107.53           N  
ANISOU 1468  N   GLY A 364    14066  13178  13613    930  -1889  -1780       N  
ATOM   1469  CA  GLY A 364      17.029 -19.915 -19.159  1.00111.28           C  
ANISOU 1469  CA  GLY A 364    14646  13347  14290    984  -1893  -1803       C  
ATOM   1470  C   GLY A 364      17.312 -19.998 -20.647  1.00119.60           C  
ANISOU 1470  C   GLY A 364    15749  14222  15473    927  -1804  -1529       C  
ATOM   1471  O   GLY A 364      17.783 -21.025 -21.144  1.00125.93           O  
ANISOU 1471  O   GLY A 364    16507  15134  16205    847  -1728  -1338       O  
ATOM   1472  N   SER A 365      17.026 -18.911 -21.361  1.00118.16           N  
ANISOU 1472  N   SER A 365    15666  13756  15472    977  -1806  -1508       N  
ATOM   1473  CA  SER A 365      17.227 -18.860 -22.807  1.00107.04           C  
ANISOU 1473  CA  SER A 365    14334  12171  14165    937  -1720  -1242       C  
ATOM   1474  C   SER A 365      17.286 -17.420 -23.328  1.00102.24           C  
ANISOU 1474  C   SER A 365    13827  11199  13819    954  -1745  -1241       C  
ATOM   1475  O   SER A 365      17.240 -16.463 -22.558  1.00100.81           O  
ANISOU 1475  O   SER A 365    13654  10881  13768    985  -1830  -1464       O  
ATOM   1476  CB  SER A 365      16.118 -19.625 -23.531  1.00 96.80           C  
ANISOU 1476  CB  SER A 365    13072  11033  12676   1050  -1664  -1095       C  
ATOM   1477  OG  SER A 365      14.866 -18.986 -23.375  1.00 96.89           O  
ANISOU 1477  OG  SER A 365    13113  11020  12683   1227  -1716  -1195       O  
ATOM   1478  N   PHE A 366      17.401 -17.292 -24.646  1.00100.46           N  
ANISOU 1478  N   PHE A 366    13689  10815  13665    934  -1664   -987       N  
ATOM   1479  CA  PHE A 366      17.420 -16.012 -25.339  1.00 98.82           C  
ANISOU 1479  CA  PHE A 366    13589  10257  13702    955  -1666   -912       C  
ATOM   1480  C   PHE A 366      16.021 -15.632 -25.802  1.00102.11           C  
ANISOU 1480  C   PHE A 366    14087  10649  14063   1158  -1695   -872       C  
ATOM   1481  O   PHE A 366      15.843 -14.641 -26.509  1.00108.05           O  
ANISOU 1481  O   PHE A 366    14939  11123  14992   1210  -1696   -764       O  
ATOM   1482  CB  PHE A 366      18.367 -16.069 -26.538  1.00 97.11           C  
ANISOU 1482  CB  PHE A 366    13428   9887  13580    822  -1547   -625       C  
ATOM   1483  CG  PHE A 366      19.817 -16.047 -26.163  1.00105.69           C  
ANISOU 1483  CG  PHE A 366    14417  10897  14841    623  -1522   -645       C  
ATOM   1484  CD1 PHE A 366      20.424 -17.161 -25.625  1.00106.97           C  
ANISOU 1484  CD1 PHE A 366    14456  11316  14874    534  -1502   -676       C  
ATOM   1485  CD2 PHE A 366      20.577 -14.908 -26.349  1.00117.72           C  
ANISOU 1485  CD2 PHE A 366    15961  12084  16685    523  -1523   -619       C  
ATOM   1486  CE1 PHE A 366      21.761 -17.141 -25.277  1.00110.11           C  
ANISOU 1486  CE1 PHE A 366    14734  11650  15451    356  -1495   -679       C  
ATOM   1487  CE2 PHE A 366      21.915 -14.885 -26.003  1.00119.66           C  
ANISOU 1487  CE2 PHE A 366    16085  12261  17118    328  -1513   -630       C  
ATOM   1488  CZ  PHE A 366      22.506 -16.005 -25.467  1.00115.60           C  
ANISOU 1488  CZ  PHE A 366    15433  12021  16468    248  -1505   -658       C  
ATOM   1489  N   ALA A 367      15.034 -16.423 -25.397  1.00 99.73           N  
ANISOU 1489  N   ALA A 367    13728  10635  13529   1272  -1720   -945       N  
ATOM   1490  CA  ALA A 367      13.657 -16.234 -25.840  1.00 98.69           C  
ANISOU 1490  CA  ALA A 367    13631  10529  13339   1463  -1756   -888       C  
ATOM   1491  C   ALA A 367      13.145 -14.842 -25.516  1.00102.88           C  
ANISOU 1491  C   ALA A 367    14197  10796  14095   1602  -1815  -1022       C  
ATOM   1492  O   ALA A 367      12.414 -14.245 -26.304  1.00109.25           O  
ANISOU 1492  O   ALA A 367    15071  11456  14981   1730  -1837   -879       O  
ATOM   1493  CB  ALA A 367      12.749 -17.286 -25.216  1.00 94.89           C  
ANISOU 1493  CB  ALA A 367    13041  10400  12613   1544  -1770   -980       C  
ATOM   1494  N   THR A 368      13.531 -14.342 -24.345  1.00103.36           N  
ANISOU 1494  N   THR A 368    14218  10797  14255   1582  -1846  -1299       N  
ATOM   1495  CA  THR A 368      13.118 -13.026 -23.870  1.00106.49           C  
ANISOU 1495  CA  THR A 368    14658  10927  14875   1711  -1892  -1486       C  
ATOM   1496  C   THR A 368      14.282 -12.321 -23.173  1.00106.96           C  
ANISOU 1496  C   THR A 368    14741  10771  15130   1557  -1925  -1682       C  
ATOM   1497  O   THR A 368      15.278 -12.957 -22.819  1.00100.24           O  
ANISOU 1497  O   THR A 368    13832  10048  14205   1374  -1926  -1707       O  
ATOM   1498  CB  THR A 368      11.930 -13.121 -22.891  1.00107.06           C  
ANISOU 1498  CB  THR A 368    14657  11198  14825   1912  -1907  -1715       C  
ATOM   1499  OG1 THR A 368      12.312 -13.902 -21.754  1.00114.10           O  
ANISOU 1499  OG1 THR A 368    15467  12366  15519   1830  -1908  -1918       O  
ATOM   1500  CG2 THR A 368      10.718 -13.763 -23.555  1.00 97.38           C  
ANISOU 1500  CG2 THR A 368    13378  10175  13447   2058  -1895  -1524       C  
ATOM   1501  N   ALA A 369      14.155 -11.009 -22.982  1.00112.27           N  
ANISOU 1501  N   ALA A 369    15488  11103  16067   1631  -1959  -1818       N  
ATOM   1502  CA  ALA A 369      15.173 -10.239 -22.271  1.00116.53           C  
ANISOU 1502  CA  ALA A 369    16053  11406  16816   1483  -2016  -2041       C  
ATOM   1503  C   ALA A 369      14.525  -9.325 -21.239  1.00128.54           C  
ANISOU 1503  C   ALA A 369    17620  12793  18427   1641  -2063  -2396       C  
ATOM   1504  O   ALA A 369      13.473  -8.736 -21.490  1.00134.46           O  
ANISOU 1504  O   ALA A 369    18413  13416  19260   1862  -2035  -2385       O  
ATOM   1505  CB  ALA A 369      16.013  -9.434 -23.244  1.00109.66           C  
ANISOU 1505  CB  ALA A 369    15256  10152  16259   1349  -1996  -1826       C  
ATOM   1506  N   SER A 370      15.152  -9.210 -20.074  1.00127.22           N  
ANISOU 1506  N   SER A 370    17442  12657  18238   1535  -2136  -2712       N  
ATOM   1507  CA  SER A 370      14.593  -8.407 -18.996  1.00131.83           C  
ANISOU 1507  CA  SER A 370    18092  13138  18861   1679  -2171  -3093       C  
ATOM   1508  C   SER A 370      15.656  -7.497 -18.392  1.00139.37           C  
ANISOU 1508  C   SER A 370    19115  13787  20051   1494  -2279  -3349       C  
ATOM   1509  O   SER A 370      16.777  -7.933 -18.105  1.00131.40           O  
ANISOU 1509  O   SER A 370    18046  12876  19005   1255  -2357  -3364       O  
ATOM   1510  CB  SER A 370      13.982  -9.309 -17.917  1.00131.51           C  
ANISOU 1510  CB  SER A 370    17984  13537  18447   1782  -2157  -3294       C  
ATOM   1511  OG  SER A 370      12.924  -8.659 -17.230  1.00133.03           O  
ANISOU 1511  OG  SER A 370    18233  13674  18637   2028  -2116  -3560       O  
ATOM   1512  N   CYS A 371      15.296  -6.228 -18.212  1.00152.80           N  
ANISOU 1512  N   CYS A 371    20934  15107  22016   1605  -2288  -3547       N  
ATOM   1513  CA  CYS A 371      16.194  -5.255 -17.606  1.00155.78           C  
ANISOU 1513  CA  CYS A 371    21395  15150  22647   1436  -2402  -3832       C  
ATOM   1514  C   CYS A 371      16.568  -5.647 -16.183  1.00154.73           C  
ANISOU 1514  C   CYS A 371    21254  15288  22249   1352  -2511  -4212       C  
ATOM   1515  O   CYS A 371      15.725  -6.107 -15.412  1.00153.51           O  
ANISOU 1515  O   CYS A 371    21102  15440  21786   1536  -2467  -4393       O  
ATOM   1516  CB  CYS A 371      15.561  -3.867 -17.604  1.00163.61           C  
ANISOU 1516  CB  CYS A 371    22529  15685  23951   1613  -2376  -4004       C  
ATOM   1517  SG  CYS A 371      16.543  -2.632 -16.714  1.00232.04           S  
ANISOU 1517  SG  CYS A 371    31321  23917  32925   1412  -2529  -4434       S  
ATOM   1518  N   LEU A 372      17.835  -5.449 -15.837  1.00142.56           N  
ANISOU 1518  N   LEU A 372    19697  13636  20833   1072  -2655  -4321       N  
ATOM   1519  CA  LEU A 372      18.328  -5.794 -14.512  1.00134.40           C  
ANISOU 1519  CA  LEU A 372    18659  12857  19551    962  -2799  -4665       C  
ATOM   1520  C   LEU A 372      17.646  -4.963 -13.424  1.00142.38           C  
ANISOU 1520  C   LEU A 372    19840  13752  20507   1130  -2825  -5140       C  
ATOM   1521  O   LEU A 372      17.643  -5.343 -12.251  1.00142.08           O  
ANISOU 1521  O   LEU A 372    19829  14008  20145   1134  -2901  -5440       O  
ATOM   1522  CB  LEU A 372      19.844  -5.596 -14.445  1.00126.24           C  
ANISOU 1522  CB  LEU A 372    17561  11670  18735    618  -2973  -4676       C  
ATOM   1523  CG  LEU A 372      20.660  -6.056 -15.651  1.00118.79           C  
ANISOU 1523  CG  LEU A 372    16469  10687  17977    439  -2922  -4217       C  
ATOM   1524  CD1 LEU A 372      22.091  -5.564 -15.536  1.00121.01           C  
ANISOU 1524  CD1 LEU A 372    16685  10726  18568    112  -3088  -4268       C  
ATOM   1525  CD2 LEU A 372      20.630  -7.567 -15.767  1.00116.72           C  
ANISOU 1525  CD2 LEU A 372    16065  10929  17354    456  -2859  -3973       C  
ATOM   1526  N   ILE A 373      17.056  -3.838 -13.823  1.00148.35           N  
ANISOU 1526  N   ILE A 373    20715  14078  21572   1280  -2750  -5199       N  
ATOM   1527  CA  ILE A 373      16.549  -2.848 -12.875  1.00146.49           C  
ANISOU 1527  CA  ILE A 373    20663  13620  21376   1424  -2767  -5670       C  
ATOM   1528  C   ILE A 373      15.020  -2.811 -12.766  1.00144.20           C  
ANISOU 1528  C   ILE A 373    20420  13427  20943   1805  -2573  -5723       C  
ATOM   1529  O   ILE A 373      14.465  -3.209 -11.743  1.00143.11           O  
ANISOU 1529  O   ILE A 373    20316  13610  20448   1945  -2537  -5992       O  
ATOM   1530  CB  ILE A 373      17.062  -1.445 -13.240  1.00147.95           C  
ANISOU 1530  CB  ILE A 373    20962  13177  22074   1312  -2833  -5767       C  
ATOM   1531  CG1 ILE A 373      18.589  -1.417 -13.155  1.00145.51           C  
ANISOU 1531  CG1 ILE A 373    20593  12773  21922    922  -3040  -5777       C  
ATOM   1532  CG2 ILE A 373      16.454  -0.392 -12.327  1.00153.25           C  
ANISOU 1532  CG2 ILE A 373    21843  13575  22809   1489  -2826  -6262       C  
ATOM   1533  CD1 ILE A 373      19.192  -0.070 -13.456  1.00150.35           C  
ANISOU 1533  CD1 ILE A 373    21304  12764  23059    767  -3118  -5876       C  
ATOM   1534  N   CYS A 374      14.339  -2.332 -13.804  1.00144.72           N  
ANISOU 1534  N   CYS A 374    20479  13223  21285   1977  -2447  -5456       N  
ATOM   1535  CA  CYS A 374      12.883  -2.213 -13.742  1.00147.85           C  
ANISOU 1535  CA  CYS A 374    20892  13678  21607   2345  -2271  -5490       C  
ATOM   1536  C   CYS A 374      12.199  -3.496 -14.207  1.00148.89           C  
ANISOU 1536  C   CYS A 374    20846  14292  21434   2454  -2170  -5142       C  
ATOM   1537  O   CYS A 374      10.968  -3.590 -14.197  1.00147.91           O  
ANISOU 1537  O   CYS A 374    20684  14290  21227   2746  -2027  -5117       O  
ATOM   1538  CB  CYS A 374      12.402  -1.023 -14.573  1.00148.83           C  
ANISOU 1538  CB  CYS A 374    21090  13270  22188   2503  -2200  -5379       C  
ATOM   1539  SG  CYS A 374      12.672  -1.188 -16.341  1.00129.08           S  
ANISOU 1539  SG  CYS A 374    18479  10625  19941   2407  -2189  -4753       S  
ATOM   1540  N   LYS A 375      13.011  -4.475 -14.607  1.00150.16           N  
ANISOU 1540  N   LYS A 375    20892  14711  21450   2215  -2244  -4878       N  
ATOM   1541  CA  LYS A 375      12.543  -5.796 -15.037  1.00149.08           C  
ANISOU 1541  CA  LYS A 375    20595  15028  21020   2263  -2170  -4559       C  
ATOM   1542  C   LYS A 375      11.532  -5.737 -16.178  1.00154.50           C  
ANISOU 1542  C   LYS A 375    21223  15635  21846   2473  -2057  -4217       C  
ATOM   1543  O   LYS A 375      10.638  -6.578 -16.270  1.00153.36           O  
ANISOU 1543  O   LYS A 375    20966  15833  21469   2625  -1970  -4074       O  
ATOM   1544  CB  LYS A 375      11.940  -6.561 -13.857  1.00148.03           C  
ANISOU 1544  CB  LYS A 375    20429  15345  20472   2387  -2116  -4795       C  
ATOM   1545  CG  LYS A 375      12.911  -7.511 -13.174  1.00149.51           C  
ANISOU 1545  CG  LYS A 375    20569  15877  20363   2146  -2225  -4851       C  
ATOM   1546  CD  LYS A 375      14.058  -6.770 -12.512  1.00156.07           C  
ANISOU 1546  CD  LYS A 375    21516  16469  21314   1928  -2396  -5160       C  
ATOM   1547  CE  LYS A 375      14.976  -7.728 -11.765  1.00157.09           C  
ANISOU 1547  CE  LYS A 375    21580  16969  21136   1709  -2524  -5211       C  
ATOM   1548  NZ  LYS A 375      15.973  -7.008 -10.919  1.00160.46           N  
ANISOU 1548  NZ  LYS A 375    22121  17212  21635   1513  -2718  -5571       N  
ATOM   1549  N   TYR A 376      11.680  -4.742 -17.046  1.00161.06           N  
ANISOU 1549  N   TYR A 376    22125  16010  23060   2474  -2068  -4077       N  
ATOM   1550  CA  TYR A 376      10.838  -4.633 -18.230  1.00164.13           C  
ANISOU 1550  CA  TYR A 376    22467  16303  23591   2651  -1995  -3714       C  
ATOM   1551  C   TYR A 376      11.181  -5.781 -19.172  1.00159.45           C  
ANISOU 1551  C   TYR A 376    21766  15998  22822   2499  -2007  -3312       C  
ATOM   1552  O   TYR A 376      12.332  -5.938 -19.579  1.00160.36           O  
ANISOU 1552  O   TYR A 376    21892  16042  22994   2238  -2066  -3181       O  
ATOM   1553  CB  TYR A 376      11.028  -3.270 -18.913  1.00169.45           C  
ANISOU 1553  CB  TYR A 376    23259  16404  24719   2672  -2010  -3644       C  
ATOM   1554  CG  TYR A 376      10.226  -3.076 -20.187  1.00170.45           C  
ANISOU 1554  CG  TYR A 376    23352  16411  25001   2850  -1959  -3240       C  
ATOM   1555  CD1 TYR A 376       8.867  -3.362 -20.229  1.00171.89           C  
ANISOU 1555  CD1 TYR A 376    23441  16803  25068   3142  -1886  -3176       C  
ATOM   1556  CD2 TYR A 376      10.829  -2.590 -21.342  1.00170.24           C  
ANISOU 1556  CD2 TYR A 376    23380  16064  25238   2726  -1987  -2913       C  
ATOM   1557  CE1 TYR A 376       8.133  -3.183 -21.391  1.00172.81           C  
ANISOU 1557  CE1 TYR A 376    23519  16823  25321   3301  -1874  -2801       C  
ATOM   1558  CE2 TYR A 376      10.105  -2.407 -22.506  1.00171.05           C  
ANISOU 1558  CE2 TYR A 376    23468  16071  25451   2890  -1959  -2533       C  
ATOM   1559  CZ  TYR A 376       8.759  -2.703 -22.526  1.00172.88           C  
ANISOU 1559  CZ  TYR A 376    23605  16522  25558   3176  -1918  -2482       C  
ATOM   1560  OH  TYR A 376       8.041  -2.519 -23.687  1.00173.83           O  
ANISOU 1560  OH  TYR A 376    23703  16560  25783   3334  -1923  -2097       O  
ATOM   1561  N   LYS A 377      10.184  -6.600 -19.489  1.00152.49           N  
ANISOU 1561  N   LYS A 377    20772  15439  21727   2659  -1946  -3127       N  
ATOM   1562  CA  LYS A 377      10.396  -7.766 -20.337  1.00143.90           C  
ANISOU 1562  CA  LYS A 377    19595  14640  20441   2532  -1952  -2779       C  
ATOM   1563  C   LYS A 377      10.136  -7.449 -21.805  1.00142.21           C  
ANISOU 1563  C   LYS A 377    19405  14219  20408   2578  -1952  -2388       C  
ATOM   1564  O   LYS A 377       9.193  -6.731 -22.137  1.00146.94           O  
ANISOU 1564  O   LYS A 377    20016  14633  21180   2809  -1933  -2333       O  
ATOM   1565  CB  LYS A 377       9.504  -8.925 -19.890  1.00142.70           C  
ANISOU 1565  CB  LYS A 377    19307  14963  19949   2645  -1901  -2788       C  
ATOM   1566  CG  LYS A 377       9.991  -9.655 -18.655  1.00141.41           C  
ANISOU 1566  CG  LYS A 377    19110  15107  19514   2532  -1906  -3052       C  
ATOM   1567  CD  LYS A 377       9.272 -10.984 -18.506  1.00141.69           C  
ANISOU 1567  CD  LYS A 377    19002  15607  19228   2589  -1850  -2943       C  
ATOM   1568  CE  LYS A 377       9.990 -11.900 -17.526  1.00144.80           C  
ANISOU 1568  CE  LYS A 377    19361  16315  19340   2425  -1866  -3094       C  
ATOM   1569  NZ  LYS A 377       9.439 -13.290 -17.540  1.00142.25           N  
ANISOU 1569  NZ  LYS A 377    18900  16415  18734   2438  -1811  -2927       N  
ATOM   1570  N   VAL A 378      10.985  -7.983 -22.680  1.00137.08           N  
ANISOU 1570  N   VAL A 378    18765  13602  19715   2366  -1969  -2111       N  
ATOM   1571  CA  VAL A 378      10.840  -7.784 -24.119  1.00131.10           C  
ANISOU 1571  CA  VAL A 378    18055  12687  19068   2386  -1966  -1719       C  
ATOM   1572  C   VAL A 378      11.004  -9.096 -24.874  1.00130.73           C  
ANISOU 1572  C   VAL A 378    17956  12980  18736   2268  -1954  -1446       C  
ATOM   1573  O   VAL A 378      11.532 -10.070 -24.342  1.00128.23           O  
ANISOU 1573  O   VAL A 378    17574  12947  18200   2123  -1943  -1540       O  
ATOM   1574  CB  VAL A 378      11.867  -6.770 -24.676  1.00125.29           C  
ANISOU 1574  CB  VAL A 378    17441  11506  18656   2238  -1971  -1617       C  
ATOM   1575  CG1 VAL A 378      11.817  -5.469 -23.894  1.00128.35           C  
ANISOU 1575  CG1 VAL A 378    17897  11518  19350   2325  -1988  -1918       C  
ATOM   1576  CG2 VAL A 378      13.271  -7.353 -24.658  1.00120.33           C  
ANISOU 1576  CG2 VAL A 378    16801  10955  17961   1936  -1964  -1590       C  
ATOM   1577  N   ASP A 379      10.556  -9.107 -26.124  1.00132.86           N  
ANISOU 1577  N   ASP A 379    18265  13208  19007   2332  -1960  -1108       N  
ATOM   1578  CA  ASP A 379      10.663 -10.282 -26.980  1.00133.44           C  
ANISOU 1578  CA  ASP A 379    18324  13565  18812   2228  -1950   -846       C  
ATOM   1579  C   ASP A 379      12.121 -10.544 -27.344  1.00131.20           C  
ANISOU 1579  C   ASP A 379    18102  13214  18534   1963  -1894   -745       C  
ATOM   1580  O   ASP A 379      12.998  -9.746 -27.034  1.00133.65           O  
ANISOU 1580  O   ASP A 379    18455  13243  19084   1857  -1881   -842       O  
ATOM   1581  CB  ASP A 379       9.819 -10.089 -28.245  1.00141.87           C  
ANISOU 1581  CB  ASP A 379    19444  14580  19879   2368  -1992   -519       C  
ATOM   1582  CG  ASP A 379       9.619 -11.372 -29.018  1.00141.87           C  
ANISOU 1582  CG  ASP A 379    19429  14916  19559   2300  -2002   -307       C  
ATOM   1583  OD1 ASP A 379      10.469 -11.687 -29.875  1.00142.31           O  
ANISOU 1583  OD1 ASP A 379    19586  14943  19541   2134  -1955    -98       O  
ATOM   1584  OD2 ASP A 379       8.612 -12.064 -28.770  1.00142.80           O  
ANISOU 1584  OD2 ASP A 379    19432  15318  19507   2410  -2048   -353       O  
ATOM   1585  N   CYS A 380      12.376 -11.670 -27.997  1.00130.26           N  
ANISOU 1585  N   CYS A 380    17979  13348  18167   1854  -1859   -554       N  
ATOM   1586  CA  CYS A 380      13.709 -11.977 -28.504  1.00130.55           C  
ANISOU 1586  CA  CYS A 380    18066  13330  18209   1625  -1777   -411       C  
ATOM   1587  C   CYS A 380      14.091 -11.025 -29.628  1.00132.27           C  
ANISOU 1587  C   CYS A 380    18423  13199  18635   1604  -1738   -137       C  
ATOM   1588  O   CYS A 380      15.240 -10.603 -29.743  1.00130.42           O  
ANISOU 1588  O   CYS A 380    18219  12749  18587   1437  -1670    -90       O  
ATOM   1589  CB  CYS A 380      13.779 -13.423 -29.005  1.00127.22           C  
ANISOU 1589  CB  CYS A 380    17624  13249  17466   1545  -1730   -271       C  
ATOM   1590  SG  CYS A 380      15.134 -13.763 -30.161  1.00115.65           S  
ANISOU 1590  SG  CYS A 380    16261  11696  15986   1331  -1591     22       S  
ATOM   1591  N   GLU A 381      13.110 -10.688 -30.455  1.00138.56           N  
ANISOU 1591  N   GLU A 381    19294  13946  19407   1775  -1784     60       N  
ATOM   1592  CA  GLU A 381      13.352  -9.885 -31.642  1.00140.96           C  
ANISOU 1592  CA  GLU A 381    19748  13958  19854   1774  -1747    376       C  
ATOM   1593  C   GLU A 381      13.637  -8.426 -31.281  1.00138.61           C  
ANISOU 1593  C   GLU A 381    19482  13225  19960   1800  -1752    298       C  
ATOM   1594  O   GLU A 381      14.186  -7.673 -32.087  1.00142.14           O  
ANISOU 1594  O   GLU A 381    20041  13371  20596   1743  -1692    540       O  
ATOM   1595  CB  GLU A 381      12.153  -9.984 -32.587  1.00150.12           C  
ANISOU 1595  CB  GLU A 381    20971  15219  20849   1959  -1828    612       C  
ATOM   1596  CG  GLU A 381      12.396  -9.424 -33.978  1.00155.91           C  
ANISOU 1596  CG  GLU A 381    21883  15737  21619   1951  -1789    997       C  
ATOM   1597  CD  GLU A 381      13.467 -10.179 -34.737  1.00155.58           C  
ANISOU 1597  CD  GLU A 381    21930  15794  21387   1743  -1650   1179       C  
ATOM   1598  OE1 GLU A 381      13.648 -11.391 -34.471  1.00147.39           O  
ANISOU 1598  OE1 GLU A 381    20829  15074  20100   1652  -1621   1066       O  
ATOM   1599  OE2 GLU A 381      14.130  -9.553 -35.594  1.00159.93           O  
ANISOU 1599  OE2 GLU A 381    22616  16097  22053   1677  -1554   1443       O  
ATOM   1600  N   ALA A 382      13.273  -8.039 -30.063  1.00128.66           N  
ANISOU 1600  N   ALA A 382    18130  11926  18829   1883  -1814    -43       N  
ATOM   1601  CA  ALA A 382      13.434  -6.659 -29.608  1.00127.49           C  
ANISOU 1601  CA  ALA A 382    18020  11353  19068   1922  -1830   -177       C  
ATOM   1602  C   ALA A 382      14.896  -6.213 -29.569  1.00126.87           C  
ANISOU 1602  C   ALA A 382    17971  11011  19225   1668  -1762   -175       C  
ATOM   1603  O   ALA A 382      15.221  -5.077 -29.931  1.00128.19           O  
ANISOU 1603  O   ALA A 382    18222  10761  19722   1652  -1740    -67       O  
ATOM   1604  CB  ALA A 382      12.802  -6.487 -28.238  1.00126.50           C  
ANISOU 1604  CB  ALA A 382    17803  11287  18975   2052  -1894   -584       C  
ATOM   1605  N   VAL A 383      15.776  -7.110 -29.136  1.00122.16           N  
ANISOU 1605  N   VAL A 383    17289  10650  18478   1469  -1729   -279       N  
ATOM   1606  CA  VAL A 383      17.183  -6.769 -28.965  1.00119.13           C  
ANISOU 1606  CA  VAL A 383    16882  10053  18328   1217  -1680   -302       C  
ATOM   1607  C   VAL A 383      18.093  -7.459 -29.994  1.00120.66           C  
ANISOU 1607  C   VAL A 383    17089  10343  18413   1044  -1547     30       C  
ATOM   1608  O   VAL A 383      19.315  -7.499 -29.823  1.00119.45           O  
ANISOU 1608  O   VAL A 383    16867  10115  18404    821  -1492     22       O  
ATOM   1609  CB  VAL A 383      17.658  -7.123 -27.538  1.00109.60           C  
ANISOU 1609  CB  VAL A 383    15549   8999  17094   1109  -1755   -698       C  
ATOM   1610  CG1 VAL A 383      16.747  -6.487 -26.510  1.00105.61           C  
ANISOU 1610  CG1 VAL A 383    15052   8420  16655   1292  -1859  -1043       C  
ATOM   1611  CG2 VAL A 383      17.671  -8.622 -27.343  1.00110.71           C  
ANISOU 1611  CG2 VAL A 383    15594   9617  16853   1074  -1737   -709       C  
ATOM   1612  N   ARG A 384      17.502  -7.986 -31.067  1.00117.92           N  
ANISOU 1612  N   ARG A 384    16829  10159  17817   1148  -1495    319       N  
ATOM   1613  CA  ARG A 384      18.282  -8.637 -32.120  1.00115.66           C  
ANISOU 1613  CA  ARG A 384    16589   9965  17393   1010  -1346    632       C  
ATOM   1614  C   ARG A 384      19.232  -7.664 -32.814  1.00120.51           C  
ANISOU 1614  C   ARG A 384    17271  10184  18333    877  -1229    877       C  
ATOM   1615  O   ARG A 384      20.430  -7.939 -32.945  1.00118.27           O  
ANISOU 1615  O   ARG A 384    16926   9884  18127    671  -1106    958       O  
ATOM   1616  CB  ARG A 384      17.368  -9.284 -33.165  1.00117.71           C  
ANISOU 1616  CB  ARG A 384    16964  10452  17310   1157  -1336    877       C  
ATOM   1617  CG  ARG A 384      18.128  -9.809 -34.389  1.00121.28           C  
ANISOU 1617  CG  ARG A 384    17517  10955  17610   1037  -1161   1216       C  
ATOM   1618  CD  ARG A 384      17.230 -10.543 -35.379  1.00123.14           C  
ANISOU 1618  CD  ARG A 384    17882  11445  17461   1165  -1177   1417       C  
ATOM   1619  NE  ARG A 384      17.543 -11.970 -35.471  1.00119.50           N  
ANISOU 1619  NE  ARG A 384    17391  11333  16682   1078  -1101   1388       N  
ATOM   1620  CZ  ARG A 384      16.706 -12.945 -35.127  1.00117.96           C  
ANISOU 1620  CZ  ARG A 384    17146  11463  16212   1159  -1203   1235       C  
ATOM   1621  NH1 ARG A 384      15.494 -12.661 -34.667  1.00112.08           N  
ANISOU 1621  NH1 ARG A 384    16359  10763  15464   1332  -1380   1103       N  
ATOM   1622  NH2 ARG A 384      17.080 -14.210 -35.247  1.00123.42           N  
ANISOU 1622  NH2 ARG A 384    17820  12424  16648   1070  -1117   1222       N  
ATOM   1623  N   GLY A 385      18.685  -6.532 -33.256  1.00122.65           N  
ANISOU 1623  N   GLY A 385    17656  10134  18810   1001  -1262   1010       N  
ATOM   1624  CA  GLY A 385      19.456  -5.522 -33.954  1.00119.64           C  
ANISOU 1624  CA  GLY A 385    17352   9347  18758    893  -1149   1274       C  
ATOM   1625  C   GLY A 385      20.612  -5.006 -33.123  1.00125.16           C  
ANISOU 1625  C   GLY A 385    17923   9805  19829    668  -1138   1076       C  
ATOM   1626  O   GLY A 385      21.749  -4.973 -33.596  1.00126.25           O  
ANISOU 1626  O   GLY A 385    18029   9826  20112    466   -989   1275       O  
ATOM   1627  N   ASP A 386      20.316  -4.610 -31.885  1.00130.20           N  
ANISOU 1627  N   ASP A 386    18483  10373  20616    702  -1295    682       N  
ATOM   1628  CA  ASP A 386      21.322  -4.095 -30.953  1.00136.46           C  
ANISOU 1628  CA  ASP A 386    19156  10945  21748    488  -1340    430       C  
ATOM   1629  C   ASP A 386      22.530  -5.028 -30.818  1.00133.89           C  
ANISOU 1629  C   ASP A 386    18677  10851  21343    250  -1262    444       C  
ATOM   1630  O   ASP A 386      23.683  -4.593 -30.902  1.00131.86           O  
ANISOU 1630  O   ASP A 386    18342  10357  21402     25  -1194    530       O  
ATOM   1631  CB  ASP A 386      20.698  -3.867 -29.568  1.00141.29           C  
ANISOU 1631  CB  ASP A 386    19722  11585  22377    585  -1526    -43       C  
ATOM   1632  CG  ASP A 386      20.092  -2.479 -29.409  1.00145.27           C  
ANISOU 1632  CG  ASP A 386    20335  11647  23214    717  -1593   -136       C  
ATOM   1633  OD1 ASP A 386      20.568  -1.532 -30.073  1.00147.41           O  
ANISOU 1633  OD1 ASP A 386    20673  11504  23831    635  -1521     97       O  
ATOM   1634  OD2 ASP A 386      19.146  -2.337 -28.601  1.00143.60           O  
ANISOU 1634  OD2 ASP A 386    20138  11494  22929    906  -1705   -440       O  
ATOM   1635  N   ILE A 387      22.248  -6.313 -30.618  1.00128.91           N  
ANISOU 1635  N   ILE A 387    17992  10675  20313    305  -1269    374       N  
ATOM   1636  CA  ILE A 387      23.278  -7.307 -30.361  1.00122.73           C  
ANISOU 1636  CA  ILE A 387    17050  10145  19435    117  -1209    357       C  
ATOM   1637  C   ILE A 387      24.060  -7.645 -31.631  1.00123.62           C  
ANISOU 1637  C   ILE A 387    17188  10246  19535     14   -976    772       C  
ATOM   1638  O   ILE A 387      25.255  -7.954 -31.572  1.00120.65           O  
ANISOU 1638  O   ILE A 387    16666   9881  19296   -191   -884    829       O  
ATOM   1639  CB  ILE A 387      22.652  -8.573 -29.746  1.00117.42           C  
ANISOU 1639  CB  ILE A 387    16325   9942  18348    225  -1283    161       C  
ATOM   1640  CG1 ILE A 387      22.019  -8.219 -28.399  1.00115.36           C  
ANISOU 1640  CG1 ILE A 387    16028   9696  18107    310  -1487   -257       C  
ATOM   1641  CG2 ILE A 387      23.689  -9.673 -29.559  1.00118.23           C  
ANISOU 1641  CG2 ILE A 387    16267  10308  18348     55  -1209    182       C  
ATOM   1642  CD1 ILE A 387      21.439  -9.390 -27.647  1.00110.94           C  
ANISOU 1642  CD1 ILE A 387    15400   9580  17172    404  -1558   -461       C  
ATOM   1643  N   PHE A 388      23.389  -7.557 -32.779  1.00128.30           N  
ANISOU 1643  N   PHE A 388    17966  10814  19969    159   -878   1065       N  
ATOM   1644  CA  PHE A 388      24.034  -7.793 -34.070  1.00131.41           C  
ANISOU 1644  CA  PHE A 388    18431  11186  20312     86   -637   1471       C  
ATOM   1645  C   PHE A 388      24.947  -6.631 -34.479  1.00139.64           C  
ANISOU 1645  C   PHE A 388    19465  11786  21807    -74   -525   1680       C  
ATOM   1646  O   PHE A 388      25.813  -6.787 -35.342  1.00141.25           O  
ANISOU 1646  O   PHE A 388    19667  11949  22051   -192   -296   1990       O  
ATOM   1647  CB  PHE A 388      22.978  -8.042 -35.148  1.00131.79           C  
ANISOU 1647  CB  PHE A 388    18700  11361  20015    294   -598   1710       C  
ATOM   1648  CG  PHE A 388      23.547  -8.233 -36.524  1.00136.29           C  
ANISOU 1648  CG  PHE A 388    19392  11912  20481    241   -347   2126       C  
ATOM   1649  CD1 PHE A 388      24.130  -9.435 -36.886  1.00136.72           C  
ANISOU 1649  CD1 PHE A 388    19414  12261  20274    171   -184   2202       C  
ATOM   1650  CD2 PHE A 388      23.494  -7.210 -37.460  1.00141.36           C  
ANISOU 1650  CD2 PHE A 388    20193  12236  21282    272   -260   2446       C  
ATOM   1651  CE1 PHE A 388      24.653  -9.612 -38.154  1.00140.31           C  
ANISOU 1651  CE1 PHE A 388    20000  12702  20610    134     73   2572       C  
ATOM   1652  CE2 PHE A 388      24.015  -7.381 -38.729  1.00143.06           C  
ANISOU 1652  CE2 PHE A 388    20538  12448  21368    230    -11   2838       C  
ATOM   1653  CZ  PHE A 388      24.595  -8.584 -39.076  1.00141.12           C  
ANISOU 1653  CZ  PHE A 388    20268  12508  20844    162    162   2891       C  
ATOM   1654  N   ASN A 389      24.747  -5.469 -33.859  1.00141.19           N  
ANISOU 1654  N   ASN A 389    19655  11643  22349    -77   -671   1509       N  
ATOM   1655  CA  ASN A 389      25.584  -4.300 -34.121  1.00144.82           C  
ANISOU 1655  CA  ASN A 389    20093  11640  23292   -246   -590   1673       C  
ATOM   1656  C   ASN A 389      26.632  -4.091 -33.029  1.00148.34           C  
ANISOU 1656  C   ASN A 389    20306  11970  24085   -491   -682   1396       C  
ATOM   1657  O   ASN A 389      27.277  -3.040 -32.970  1.00156.04           O  
ANISOU 1657  O   ASN A 389    21236  12533  25519   -652   -675   1436       O  
ATOM   1658  CB  ASN A 389      24.722  -3.040 -34.258  1.00146.08           C  
ANISOU 1658  CB  ASN A 389    20415  11426  23663    -98   -683   1696       C  
ATOM   1659  CG  ASN A 389      23.911  -3.015 -35.545  1.00142.70           C  
ANISOU 1659  CG  ASN A 389    20211  11027  22983    105   -579   2076       C  
ATOM   1660  OD1 ASN A 389      24.251  -3.682 -36.523  1.00142.27           O  
ANISOU 1660  OD1 ASN A 389    20213  11161  22683     80   -388   2388       O  
ATOM   1661  ND2 ASN A 389      22.835  -2.233 -35.549  1.00138.82           N  
ANISOU 1661  ND2 ASN A 389    19849  10345  22550    311   -705   2051       N  
ATOM   1662  N   GLN A 390      26.797  -5.102 -32.179  1.00141.76           N  
ANISOU 1662  N   GLN A 390    19327  11501  23035   -524   -777   1127       N  
ATOM   1663  CA  GLN A 390      27.666  -5.028 -31.003  1.00141.23           C  
ANISOU 1663  CA  GLN A 390    19038  11401  23223   -734   -923    820       C  
ATOM   1664  C   GLN A 390      27.312  -3.829 -30.124  1.00141.10           C  
ANISOU 1664  C   GLN A 390    19060  11039  23514   -738  -1140    502       C  
ATOM   1665  O   GLN A 390      28.183  -3.191 -29.530  1.00140.15           O  
ANISOU 1665  O   GLN A 390    18805  10663  23782   -962  -1229    359       O  
ATOM   1666  CB  GLN A 390      29.142  -4.980 -31.414  1.00144.59           C  
ANISOU 1666  CB  GLN A 390    19281  11689  23969  -1004   -755   1064       C  
ATOM   1667  CG  GLN A 390      29.711  -6.341 -31.784  1.00145.59           C  
ANISOU 1667  CG  GLN A 390    19292  12209  23816  -1032   -586   1228       C  
ATOM   1668  CD  GLN A 390      29.473  -7.390 -30.704  1.00147.39           C  
ANISOU 1668  CD  GLN A 390    19413  12845  23743   -982   -765    890       C  
ATOM   1669  OE1 GLN A 390      28.823  -8.407 -30.944  1.00144.95           O  
ANISOU 1669  OE1 GLN A 390    19186  12881  23006   -813   -716    914       O  
ATOM   1670  NE2 GLN A 390      30.002  -7.146 -29.510  1.00149.61           N  
ANISOU 1670  NE2 GLN A 390    19514  13085  24246  -1135   -981    579       N  
ATOM   1671  N   VAL A 391      26.019  -3.536 -30.055  1.00139.20           N  
ANISOU 1671  N   VAL A 391    19000  10788  23101   -487  -1225    388       N  
ATOM   1672  CA  VAL A 391      25.498  -2.475 -29.206  1.00137.18           C  
ANISOU 1672  CA  VAL A 391    18809  10230  23083   -434  -1413     56       C  
ATOM   1673  C   VAL A 391      24.793  -3.097 -28.007  1.00138.73           C  
ANISOU 1673  C   VAL A 391    18980  10768  22963   -306  -1599   -371       C  
ATOM   1674  O   VAL A 391      23.985  -4.012 -28.160  1.00137.72           O  
ANISOU 1674  O   VAL A 391    18893  11014  22419   -116  -1573   -339       O  
ATOM   1675  CB  VAL A 391      24.519  -1.558 -29.980  1.00130.18           C  
ANISOU 1675  CB  VAL A 391    18138   9038  22288   -220  -1360    248       C  
ATOM   1676  CG1 VAL A 391      23.694  -0.704 -29.028  1.00127.90           C  
ANISOU 1676  CG1 VAL A 391    17930   8530  22137    -80  -1546   -142       C  
ATOM   1677  CG2 VAL A 391      25.274  -0.694 -30.981  1.00128.65           C  
ANISOU 1677  CG2 VAL A 391    17976   8420  22486   -368  -1196    634       C  
ATOM   1678  N   VAL A 392      25.114  -2.615 -26.811  1.00140.55           N  
ANISOU 1678  N   VAL A 392    19144  10874  23385   -419  -1786   -768       N  
ATOM   1679  CA  VAL A 392      24.485  -3.125 -25.599  1.00140.22           C  
ANISOU 1679  CA  VAL A 392    19090  11143  23043   -303  -1955  -1184       C  
ATOM   1680  C   VAL A 392      23.056  -2.596 -25.468  1.00146.72           C  
ANISOU 1680  C   VAL A 392    20093  11879  23774     -3  -1987  -1328       C  
ATOM   1681  O   VAL A 392      22.849  -1.396 -25.302  1.00150.37           O  
ANISOU 1681  O   VAL A 392    20656  11915  24562     24  -2037  -1457       O  
ATOM   1682  CB  VAL A 392      25.297  -2.750 -24.351  1.00134.81           C  
ANISOU 1682  CB  VAL A 392    18298  10358  22564   -522  -2157  -1575       C  
ATOM   1683  CG1 VAL A 392      24.542  -3.137 -23.095  1.00129.36           C  
ANISOU 1683  CG1 VAL A 392    17640   9962  21549   -375  -2318  -2008       C  
ATOM   1684  CG2 VAL A 392      26.665  -3.421 -24.393  1.00131.24           C  
ANISOU 1684  CG2 VAL A 392    17625  10062  22179   -800  -2143  -1434       C  
ATOM   1685  N   PRO A 393      22.064  -3.500 -25.544  1.00149.63           N  
ANISOU 1685  N   PRO A 393    20491  12642  23720    223  -1955  -1301       N  
ATOM   1686  CA  PRO A 393      20.648  -3.116 -25.544  1.00150.05           C  
ANISOU 1686  CA  PRO A 393    20679  12656  23676    527  -1966  -1377       C  
ATOM   1687  C   PRO A 393      20.253  -2.362 -24.287  1.00146.60           C  
ANISOU 1687  C   PRO A 393    20288  12057  23356    597  -2108  -1850       C  
ATOM   1688  O   PRO A 393      20.526  -2.798 -23.169  1.00146.38           O  
ANISOU 1688  O   PRO A 393    20188  12256  23173    520  -2219  -2185       O  
ATOM   1689  CB  PRO A 393      19.916  -4.460 -25.630  1.00145.53           C  
ANISOU 1689  CB  PRO A 393    20065  12611  22619    679  -1931  -1310       C  
ATOM   1690  CG  PRO A 393      20.880  -5.448 -25.103  1.00142.06           C  
ANISOU 1690  CG  PRO A 393    19476  12481  22020    470  -1958  -1388       C  
ATOM   1691  CD  PRO A 393      22.230  -4.962 -25.540  1.00143.72           C  
ANISOU 1691  CD  PRO A 393    19630  12398  22580    199  -1917  -1221       C  
ATOM   1692  N   ARG A 394      19.606  -1.224 -24.489  1.00143.82           N  
ANISOU 1692  N   ARG A 394    20067  11306  23270    753  -2098  -1869       N  
ATOM   1693  CA  ARG A 394      19.247  -0.344 -23.394  1.00145.91           C  
ANISOU 1693  CA  ARG A 394    20409  11332  23700    829  -2206  -2318       C  
ATOM   1694  C   ARG A 394      17.766  -0.450 -23.053  1.00140.31           C  
ANISOU 1694  C   ARG A 394    19758  10796  22756   1178  -2190  -2465       C  
ATOM   1695  O   ARG A 394      16.935  -0.785 -23.897  1.00137.62           O  
ANISOU 1695  O   ARG A 394    19427  10590  22273   1375  -2103  -2162       O  
ATOM   1696  CB  ARG A 394      19.619   1.098 -23.744  1.00154.69           C  
ANISOU 1696  CB  ARG A 394    21621  11812  25341    754  -2202  -2277       C  
ATOM   1697  CG  ARG A 394      21.124   1.343 -23.820  1.00157.94           C  
ANISOU 1697  CG  ARG A 394    21952  12010  26050    384  -2239  -2220       C  
ATOM   1698  CD  ARG A 394      21.734   1.409 -22.427  1.00162.45           C  
ANISOU 1698  CD  ARG A 394    22476  12612  26634    205  -2422  -2719       C  
ATOM   1699  NE  ARG A 394      21.133   2.481 -21.634  1.00168.44           N  
ANISOU 1699  NE  ARG A 394    23388  13025  27589    337  -2502  -3126       N  
ATOM   1700  CZ  ARG A 394      21.359   2.678 -20.338  1.00168.46           C  
ANISOU 1700  CZ  ARG A 394    23415  13034  27560    254  -2666  -3631       C  
ATOM   1701  NH1 ARG A 394      22.179   1.875 -19.669  1.00167.11           N  
ANISOU 1701  NH1 ARG A 394    23111  13211  27171     35  -2789  -3775       N  
ATOM   1702  NH2 ARG A 394      20.760   3.680 -19.708  1.00170.52           N  
ANISOU 1702  NH2 ARG A 394    23840  12953  27998    398  -2708  -3993       N  
ATOM   1703  N   CYS A 395      17.451  -0.171 -21.797  1.00140.46           N  
ANISOU 1703  N   CYS A 395    19815  10823  22732   1249  -2275  -2935       N  
ATOM   1704  CA  CYS A 395      16.082  -0.200 -21.315  1.00143.22           C  
ANISOU 1704  CA  CYS A 395    20206  11321  22889   1579  -2242  -3122       C  
ATOM   1705  C   CYS A 395      15.350   1.097 -21.666  1.00151.43           C  
ANISOU 1705  C   CYS A 395    21374  11864  24298   1798  -2192  -3108       C  
ATOM   1706  O   CYS A 395      15.794   2.186 -21.295  1.00159.42           O  
ANISOU 1706  O   CYS A 395    22486  12417  25670   1715  -2239  -3333       O  
ATOM   1707  CB  CYS A 395      16.074  -0.426 -19.805  1.00141.61           C  
ANISOU 1707  CB  CYS A 395    20005  11335  22466   1572  -2329  -3633       C  
ATOM   1708  SG  CYS A 395      14.446  -0.585 -19.085  1.00123.57           S  
ANISOU 1708  SG  CYS A 395    17746   9295  19910   1970  -2253  -3878       S  
ATOM   1709  N   PRO A 396      14.221   0.986 -22.384  1.00145.94           N  
ANISOU 1709  N   PRO A 396    20671  11248  23530   2079  -2108  -2843       N  
ATOM   1710  CA  PRO A 396      13.458   2.160 -22.830  1.00148.19           C  
ANISOU 1710  CA  PRO A 396    21057  11078  24169   2319  -2058  -2761       C  
ATOM   1711  C   PRO A 396      12.674   2.865 -21.718  1.00157.89           C  
ANISOU 1711  C   PRO A 396    22359  12144  25488   2553  -2051  -3226       C  
ATOM   1712  O   PRO A 396      12.380   4.058 -21.846  1.00165.35           O  
ANISOU 1712  O   PRO A 396    23413  12587  26826   2688  -2023  -3266       O  
ATOM   1713  CB  PRO A 396      12.501   1.575 -23.869  1.00141.22           C  
ANISOU 1713  CB  PRO A 396    20109  10451  23097   2533  -1999  -2334       C  
ATOM   1714  CG  PRO A 396      12.314   0.174 -23.438  1.00141.47           C  
ANISOU 1714  CG  PRO A 396    20015  11091  22647   2510  -2010  -2405       C  
ATOM   1715  CD  PRO A 396      13.634  -0.271 -22.877  1.00141.05           C  
ANISOU 1715  CD  PRO A 396    19938  11145  22508   2172  -2067  -2579       C  
ATOM   1716  N   ARG A 397      12.336   2.144 -20.653  1.00155.24           N  
ANISOU 1716  N   ARG A 397    21971  12217  24795   2611  -2061  -3565       N  
ATOM   1717  CA  ARG A 397      11.601   2.734 -19.539  1.00164.09           C  
ANISOU 1717  CA  ARG A 397    23170  13231  25947   2839  -2027  -4029       C  
ATOM   1718  C   ARG A 397      12.521   3.560 -18.645  1.00174.21           C  
ANISOU 1718  C   ARG A 397    24592  14155  27445   2635  -2113  -4465       C  
ATOM   1719  O   ARG A 397      12.257   4.735 -18.386  1.00179.60           O  
ANISOU 1719  O   ARG A 397    25411  14356  28474   2763  -2087  -4689       O  
ATOM   1720  CB  ARG A 397      10.904   1.651 -18.714  1.00159.19           C  
ANISOU 1720  CB  ARG A 397    22448  13191  24846   2973  -1989  -4217       C  
ATOM   1721  CG  ARG A 397       9.840   0.881 -19.478  1.00163.18           C  
ANISOU 1721  CG  ARG A 397    22807  14037  25157   3194  -1913  -3842       C  
ATOM   1722  CD  ARG A 397       8.790   1.810 -20.074  1.00171.79           C  
ANISOU 1722  CD  ARG A 397    23921  14781  26572   3518  -1837  -3687       C  
ATOM   1723  NE  ARG A 397       7.784   1.079 -20.844  1.00173.06           N  
ANISOU 1723  NE  ARG A 397    23927  15271  26557   3712  -1799  -3316       N  
ATOM   1724  CZ  ARG A 397       7.800   0.943 -22.168  1.00171.61           C  
ANISOU 1724  CZ  ARG A 397    23708  15053  26442   3678  -1836  -2829       C  
ATOM   1725  NH1 ARG A 397       8.771   1.495 -22.884  1.00172.30           N  
ANISOU 1725  NH1 ARG A 397    23900  14789  26776   3467  -1882  -2632       N  
ATOM   1726  NH2 ARG A 397       6.841   0.257 -22.777  1.00168.46           N  
ANISOU 1726  NH2 ARG A 397    23171  14975  25862   3850  -1827  -2537       N  
ATOM   1727  N   CYS A 398      13.601   2.939 -18.182  1.00172.30           N  
ANISOU 1727  N   CYS A 398    24312  14143  27011   2318  -2224  -4584       N  
ATOM   1728  CA  CYS A 398      14.565   3.603 -17.309  1.00177.82           C  
ANISOU 1728  CA  CYS A 398    25123  14560  27881   2078  -2350  -5000       C  
ATOM   1729  C   CYS A 398      15.195   4.829 -17.968  1.00182.71           C  
ANISOU 1729  C   CYS A 398    25835  14524  29062   1939  -2378  -4885       C  
ATOM   1730  O   CYS A 398      15.313   4.886 -19.193  1.00179.52           O  
ANISOU 1730  O   CYS A 398    25378  13982  28851   1911  -2323  -4401       O  
ATOM   1731  CB  CYS A 398      15.662   2.621 -16.886  1.00175.27           C  
ANISOU 1731  CB  CYS A 398    24698  14630  27268   1750  -2481  -5041       C  
ATOM   1732  SG  CYS A 398      15.172   1.476 -15.577  1.00231.79           S  
ANISOU 1732  SG  CYS A 398    31812  22447  33811   1856  -2494  -5382       S  
ATOM   1733  N   PRO A 399      15.596   5.819 -17.149  1.00189.30           N  
ANISOU 1733  N   PRO A 399    26821  14948  30158   1848  -2461  -5332       N  
ATOM   1734  CA  PRO A 399      16.287   7.014 -17.647  1.00196.90           C  
ANISOU 1734  CA  PRO A 399    27874  15252  31687   1675  -2500  -5268       C  
ATOM   1735  C   PRO A 399      17.517   6.656 -18.475  1.00199.31           C  
ANISOU 1735  C   PRO A 399    28047  15568  32113   1313  -2565  -4873       C  
ATOM   1736  O   PRO A 399      18.164   5.644 -18.202  1.00199.50           O  
ANISOU 1736  O   PRO A 399    27943  16045  31814   1110  -2647  -4863       O  
ATOM   1737  CB  PRO A 399      16.691   7.748 -16.365  1.00199.87           C  
ANISOU 1737  CB  PRO A 399    28409  15362  32169   1559  -2630  -5900       C  
ATOM   1738  CG  PRO A 399      15.707   7.301 -15.351  1.00198.03           C  
ANISOU 1738  CG  PRO A 399    28228  15513  31502   1845  -2575  -6272       C  
ATOM   1739  CD  PRO A 399      15.381   5.876 -15.692  1.00190.95           C  
ANISOU 1739  CD  PRO A 399    27138  15284  30130   1909  -2518  -5934       C  
ATOM   1740  N   ALA A 400      17.830   7.474 -19.476  1.00201.21           N  
ANISOU 1740  N   ALA A 400    28316  15315  32821   1243  -2513  -4536       N  
ATOM   1741  CA  ALA A 400      18.994   7.229 -20.319  1.00195.80           C  
ANISOU 1741  CA  ALA A 400    27507  14597  32290    910  -2535  -4138       C  
ATOM   1742  C   ALA A 400      20.288   7.425 -19.529  1.00195.23           C  
ANISOU 1742  C   ALA A 400    27405  14402  32369    518  -2721  -4467       C  
ATOM   1743  O   ALA A 400      21.346   6.932 -19.926  1.00188.54           O  
ANISOU 1743  O   ALA A 400    26406  13685  31544    218  -2761  -4221       O  
ATOM   1744  CB  ALA A 400      18.969   8.135 -21.542  1.00195.77           C  
ANISOU 1744  CB  ALA A 400    27558  14072  32756    945  -2420  -3698       C  
ATOM   1745  N   ASP A 401      20.197   8.140 -18.408  1.00200.42           N  
ANISOU 1745  N   ASP A 401    28207  14814  33130    525  -2834  -5028       N  
ATOM   1746  CA  ASP A 401      21.352   8.360 -17.539  1.00204.01           C  
ANISOU 1746  CA  ASP A 401    28647  15161  33705    157  -3053  -5403       C  
ATOM   1747  C   ASP A 401      21.439   7.286 -16.454  1.00201.29           C  
ANISOU 1747  C   ASP A 401    28240  15439  32802    122  -3183  -5729       C  
ATOM   1748  O   ASP A 401      21.713   7.584 -15.289  1.00204.89           O  
ANISOU 1748  O   ASP A 401    28792  15853  33204     15  -3360  -6260       O  
ATOM   1749  CB  ASP A 401      21.316   9.767 -16.910  1.00210.53           C  
ANISOU 1749  CB  ASP A 401    29685  15355  34951    141  -3126  -5852       C  
ATOM   1750  CG  ASP A 401      19.988  10.093 -16.229  1.00211.07           C  
ANISOU 1750  CG  ASP A 401    29941  15466  34790    543  -3018  -6195       C  
ATOM   1751  OD1 ASP A 401      19.449   9.238 -15.495  1.00210.21           O  
ANISOU 1751  OD1 ASP A 401    29831  15830  34209    709  -3049  -6453       O  
ATOM   1752  OD2 ASP A 401      19.489  11.225 -16.420  1.00211.17           O  
ANISOU 1752  OD2 ASP A 401    30094  15059  35081    690  -2880  -6181       O  
ATOM   1753  N   GLU A 402      21.216   6.037 -16.857  1.00194.02           N  
ANISOU 1753  N   GLU A 402    27167  15090  31463    208  -3098  -5402       N  
ATOM   1754  CA  GLU A 402      21.241   4.898 -15.942  1.00188.28           C  
ANISOU 1754  CA  GLU A 402    26363  14984  30189    198  -3193  -5622       C  
ATOM   1755  C   GLU A 402      22.208   3.818 -16.433  1.00181.92           C  
ANISOU 1755  C   GLU A 402    25320  14558  29244    -55  -3228  -5250       C  
ATOM   1756  O   GLU A 402      22.125   3.382 -17.580  1.00182.98           O  
ANISOU 1756  O   GLU A 402    25356  14773  29396     -7  -3069  -4748       O  
ATOM   1757  CB  GLU A 402      19.834   4.317 -15.783  1.00184.79           C  
ANISOU 1757  CB  GLU A 402    25972  14915  29326    602  -3038  -5639       C  
ATOM   1758  CG  GLU A 402      19.730   3.186 -14.776  1.00181.07           C  
ANISOU 1758  CG  GLU A 402    25444  15069  28287    625  -3112  -5874       C  
ATOM   1759  CD  GLU A 402      19.881   3.662 -13.345  1.00184.66           C  
ANISOU 1759  CD  GLU A 402    26052  15468  28642    569  -3281  -6500       C  
ATOM   1760  OE1 GLU A 402      19.576   4.844 -13.076  1.00191.02           O  
ANISOU 1760  OE1 GLU A 402    27046  15783  29748    651  -3278  -6804       O  
ATOM   1761  OE2 GLU A 402      20.310   2.855 -12.491  1.00180.07           O  
ANISOU 1761  OE2 GLU A 402    25412  15328  27679    446  -3419  -6688       O  
ATOM   1762  N   PRO A 403      23.127   3.379 -15.558  1.00174.09           N  
ANISOU 1762  N   PRO A 403    24240  13802  28104   -319  -3437  -5499       N  
ATOM   1763  CA  PRO A 403      24.194   2.429 -15.902  1.00164.92           C  
ANISOU 1763  CA  PRO A 403    22835  12958  26868   -583  -3490  -5188       C  
ATOM   1764  C   PRO A 403      23.691   1.026 -16.213  1.00154.00           C  
ANISOU 1764  C   PRO A 403    21342  12171  25001   -405  -3357  -4898       C  
ATOM   1765  O   PRO A 403      23.909   0.503 -17.307  1.00146.96           O  
ANISOU 1765  O   PRO A 403    20324  11363  24151   -430  -3212  -4418       O  
ATOM   1766  CB  PRO A 403      25.063   2.396 -14.636  1.00167.54           C  
ANISOU 1766  CB  PRO A 403    23135  13403  27120   -845  -3781  -5627       C  
ATOM   1767  CG  PRO A 403      24.645   3.582 -13.833  1.00174.83           C  
ANISOU 1767  CG  PRO A 403    24303  13921  28204   -784  -3879  -6143       C  
ATOM   1768  CD  PRO A 403      23.211   3.809 -14.154  1.00174.26           C  
ANISOU 1768  CD  PRO A 403    24397  13788  28025   -376  -3645  -6110       C  
ATOM   1769  N   LEU A 404      23.028   0.424 -15.234  1.00155.73           N  
ANISOU 1769  N   LEU A 404    21616  12794  24758   -232  -3401  -5197       N  
ATOM   1770  CA  LEU A 404      22.647  -0.975 -15.319  1.00155.60           C  
ANISOU 1770  CA  LEU A 404    21484  13364  24273   -104  -3311  -4978       C  
ATOM   1771  C   LEU A 404      21.243  -1.143 -15.878  1.00155.74           C  
ANISOU 1771  C   LEU A 404    21583  13466  24124    259  -3090  -4809       C  
ATOM   1772  O   LEU A 404      20.575  -2.140 -15.609  1.00153.02           O  
ANISOU 1772  O   LEU A 404    21201  13588  23353    432  -3026  -4783       O  
ATOM   1773  CB  LEU A 404      22.756  -1.627 -13.941  1.00154.48           C  
ANISOU 1773  CB  LEU A 404    21337  13648  23711   -133  -3480  -5352       C  
ATOM   1774  CG  LEU A 404      24.120  -1.409 -13.281  1.00152.79           C  
ANISOU 1774  CG  LEU A 404    21041  13357  23655   -494  -3748  -5558       C  
ATOM   1775  CD1 LEU A 404      24.147  -1.991 -11.877  1.00152.43           C  
ANISOU 1775  CD1 LEU A 404    21022  13736  23158   -499  -3932  -5939       C  
ATOM   1776  CD2 LEU A 404      25.236  -1.993 -14.144  1.00145.07           C  
ANISOU 1776  CD2 LEU A 404    19814  12437  22867   -744  -3740  -5113       C  
ATOM   1777  N   ALA A 405      20.799  -0.163 -16.660  1.00160.36           N  
ANISOU 1777  N   ALA A 405    22270  13595  25063    371  -2980  -4681       N  
ATOM   1778  CA  ALA A 405      19.523  -0.260 -17.362  1.00155.77           C  
ANISOU 1778  CA  ALA A 405    21739  13059  24386    701  -2787  -4454       C  
ATOM   1779  C   ALA A 405      19.715  -1.071 -18.638  1.00146.52           C  
ANISOU 1779  C   ALA A 405    20435  12070  23166    662  -2666  -3906       C  
ATOM   1780  O   ALA A 405      19.220  -0.713 -19.705  1.00137.09           O  
ANISOU 1780  O   ALA A 405    19280  10665  22141    794  -2538  -3585       O  
ATOM   1781  CB  ALA A 405      18.971   1.122 -17.675  1.00159.54           C  
ANISOU 1781  CB  ALA A 405    22380  12973  25267    850  -2729  -4522       C  
ATOM   1782  N   ILE A 406      20.452  -2.169 -18.504  1.00147.42           N  
ANISOU 1782  N   ILE A 406    20398  12577  23037    484  -2713  -3806       N  
ATOM   1783  CA  ILE A 406      20.790  -3.052 -19.613  1.00142.27           C  
ANISOU 1783  CA  ILE A 406    19622  12127  22307    418  -2599  -3329       C  
ATOM   1784  C   ILE A 406      19.757  -4.161 -19.761  1.00135.36           C  
ANISOU 1784  C   ILE A 406    18718  11712  20998    656  -2497  -3200       C  
ATOM   1785  O   ILE A 406      19.271  -4.699 -18.766  1.00130.46           O  
ANISOU 1785  O   ILE A 406    18091  11418  20060    758  -2547  -3472       O  
ATOM   1786  CB  ILE A 406      22.187  -3.668 -19.409  1.00142.43           C  
ANISOU 1786  CB  ILE A 406    19477  12307  22334    101  -2691  -3278       C  
ATOM   1787  CG1 ILE A 406      23.230  -2.558 -19.277  1.00149.23           C  
ANISOU 1787  CG1 ILE A 406    20338  12701  23661   -160  -2805  -3397       C  
ATOM   1788  CG2 ILE A 406      22.539  -4.603 -20.549  1.00138.25           C  
ANISOU 1788  CG2 ILE A 406    18830  11979  21717     50  -2543  -2803       C  
ATOM   1789  CD1 ILE A 406      24.636  -3.063 -19.136  1.00150.97           C  
ANISOU 1789  CD1 ILE A 406    20363  13041  23958   -479  -2901  -3320       C  
ATOM   1790  N   MET A 407      19.420  -4.493 -21.005  1.00139.01           N  
ANISOU 1790  N   MET A 407    19171  12199  21448    738  -2356  -2784       N  
ATOM   1791  CA  MET A 407      18.481  -5.577 -21.287  1.00139.47           C  
ANISOU 1791  CA  MET A 407    19192  12675  21124    933  -2270  -2627       C  
ATOM   1792  C   MET A 407      19.182  -6.938 -21.353  1.00137.78           C  
ANISOU 1792  C   MET A 407    18837  12867  20644    776  -2256  -2469       C  
ATOM   1793  O   MET A 407      19.890  -7.235 -22.316  1.00140.83           O  
ANISOU 1793  O   MET A 407    19178  13216  21115    638  -2180  -2140       O  
ATOM   1794  CB  MET A 407      17.737  -5.298 -22.594  1.00136.28           C  
ANISOU 1794  CB  MET A 407    18857  12115  20808   1100  -2151  -2268       C  
ATOM   1795  CG  MET A 407      16.819  -4.098 -22.513  1.00139.14           C  
ANISOU 1795  CG  MET A 407    19342  12129  21397   1320  -2153  -2401       C  
ATOM   1796  SD  MET A 407      15.660  -4.267 -21.143  1.00133.35           S  
ANISOU 1796  SD  MET A 407    18612  11653  20401   1568  -2190  -2839       S  
ATOM   1797  CE  MET A 407      14.715  -5.679 -21.691  1.00147.48           C  
ANISOU 1797  CE  MET A 407    20301  13959  21777   1726  -2110  -2563       C  
ATOM   1798  N   LYS A 408      18.984  -7.763 -20.328  1.00131.80           N  
ANISOU 1798  N   LYS A 408    18017  12492  19568    807  -2315  -2696       N  
ATOM   1799  CA  LYS A 408      19.648  -9.062 -20.268  1.00128.23           C  
ANISOU 1799  CA  LYS A 408    17429  12416  18878    669  -2309  -2566       C  
ATOM   1800  C   LYS A 408      18.743 -10.210 -20.701  1.00122.43           C  
ANISOU 1800  C   LYS A 408    16665  12046  17807    834  -2203  -2371       C  
ATOM   1801  O   LYS A 408      17.674 -10.414 -20.124  1.00120.49           O  
ANISOU 1801  O   LYS A 408    16441  11991  17349   1030  -2203  -2534       O  
ATOM   1802  CB  LYS A 408      20.163  -9.338 -18.856  1.00129.35           C  
ANISOU 1802  CB  LYS A 408    17508  12762  18879    565  -2458  -2904       C  
ATOM   1803  CG  LYS A 408      20.716 -10.747 -18.670  1.00126.25           C  
ANISOU 1803  CG  LYS A 408    16967  12784  18219    464  -2455  -2775       C  
ATOM   1804  CD  LYS A 408      21.171 -10.987 -17.238  1.00125.87           C  
ANISOU 1804  CD  LYS A 408    16866  12950  18008    377  -2622  -3097       C  
ATOM   1805  CE  LYS A 408      20.065 -11.571 -16.377  1.00122.13           C  
ANISOU 1805  CE  LYS A 408    16430  12823  17151    588  -2607  -3283       C  
ATOM   1806  NZ  LYS A 408      19.848 -13.007 -16.681  1.00116.33           N  
ANISOU 1806  NZ  LYS A 408    15592  12471  16138    630  -2507  -3028       N  
ATOM   1807  N   PRO A 409      19.175 -10.964 -21.724  1.00121.45           N  
ANISOU 1807  N   PRO A 409    16490  12014  17642    750  -2105  -2025       N  
ATOM   1808  CA  PRO A 409      18.511 -12.217 -22.097  1.00119.48           C  
ANISOU 1808  CA  PRO A 409    16202  12126  17067    854  -2021  -1853       C  
ATOM   1809  C   PRO A 409      18.370 -13.104 -20.870  1.00122.05           C  
ANISOU 1809  C   PRO A 409    16439  12827  17109    870  -2083  -2076       C  
ATOM   1810  O   PRO A 409      19.318 -13.219 -20.093  1.00126.36           O  
ANISOU 1810  O   PRO A 409    16910  13425  17675    712  -2169  -2216       O  
ATOM   1811  CB  PRO A 409      19.463 -12.831 -23.125  1.00111.15           C  
ANISOU 1811  CB  PRO A 409    15105  11077  16051    691  -1922  -1524       C  
ATOM   1812  CG  PRO A 409      20.174 -11.678 -23.707  1.00115.01           C  
ANISOU 1812  CG  PRO A 409    15647  11149  16904    580  -1910  -1433       C  
ATOM   1813  CD  PRO A 409      20.327 -10.676 -22.594  1.00122.23           C  
ANISOU 1813  CD  PRO A 409    16567  11868  18005    550  -2053  -1781       C  
ATOM   1814  N   GLU A 410      17.206 -13.716 -20.691  1.00116.37           N  
ANISOU 1814  N   GLU A 410    15717  12366  16133   1055  -2046  -2097       N  
ATOM   1815  CA  GLU A 410      16.896 -14.352 -19.418  1.00111.75           C  
ANISOU 1815  CA  GLU A 410    15068  12105  15287   1103  -2094  -2332       C  
ATOM   1816  C   GLU A 410      17.576 -15.710 -19.228  1.00100.76           C  
ANISOU 1816  C   GLU A 410    13559  11032  13693    974  -2081  -2214       C  
ATOM   1817  O   GLU A 410      16.939 -16.687 -18.846  1.00 95.03           O  
ANISOU 1817  O   GLU A 410    12780  10626  12700   1059  -2044  -2208       O  
ATOM   1818  CB  GLU A 410      15.380 -14.473 -19.259  1.00112.57           C  
ANISOU 1818  CB  GLU A 410    15189  12358  15223   1349  -2043  -2389       C  
ATOM   1819  CG  GLU A 410      14.694 -13.112 -19.153  1.00117.26           C  
ANISOU 1819  CG  GLU A 410    15883  12652  16017   1506  -2060  -2564       C  
ATOM   1820  CD  GLU A 410      13.414 -13.159 -18.344  1.00121.59           C  
ANISOU 1820  CD  GLU A 410    16418  13391  16390   1737  -2026  -2762       C  
ATOM   1821  OE1 GLU A 410      12.397 -13.655 -18.873  1.00121.23           O  
ANISOU 1821  OE1 GLU A 410    16325  13491  16247   1880  -1956  -2593       O  
ATOM   1822  OE2 GLU A 410      13.428 -12.706 -17.176  1.00123.83           O  
ANISOU 1822  OE2 GLU A 410    16735  13684  16629   1773  -2067  -3089       O  
ATOM   1823  N   ILE A 411      18.881 -15.740 -19.495  1.00102.81           N  
ANISOU 1823  N   ILE A 411    13769  11185  14109    770  -2104  -2111       N  
ATOM   1824  CA  ILE A 411      19.766 -16.814 -19.050  1.00105.59           C  
ANISOU 1824  CA  ILE A 411    13993  11792  14334    633  -2124  -2056       C  
ATOM   1825  C   ILE A 411      19.838 -16.846 -17.528  1.00110.45           C  
ANISOU 1825  C   ILE A 411    14571  12602  14793    631  -2261  -2357       C  
ATOM   1826  O   ILE A 411      19.982 -15.800 -16.890  1.00116.85           O  
ANISOU 1826  O   ILE A 411    15439  13235  15724    611  -2375  -2615       O  
ATOM   1827  CB  ILE A 411      21.210 -16.634 -19.586  1.00 85.16           C  
ANISOU 1827  CB  ILE A 411    11337   9011  12010    416  -2126  -1902       C  
ATOM   1828  CG1 ILE A 411      21.248 -16.683 -21.111  1.00 87.18           C  
ANISOU 1828  CG1 ILE A 411    11644   9099  12383    411  -1966  -1583       C  
ATOM   1829  CG2 ILE A 411      22.157 -17.649 -18.973  1.00 84.35           C  
ANISOU 1829  CG2 ILE A 411    11078   9162  11808    288  -2171  -1867       C  
ATOM   1830  CD1 ILE A 411      20.410 -17.740 -21.700  1.00 81.49           C  
ANISOU 1830  CD1 ILE A 411    10949   8605  11409    532  -1849  -1412       C  
ATOM   1831  N   VAL A 412      19.745 -18.033 -16.939  1.00107.43           N  
ANISOU 1831  N   VAL A 412    14104  12577  14137    650  -2252  -2329       N  
ATOM   1832  CA  VAL A 412      20.033 -18.161 -15.522  1.00110.62           C  
ANISOU 1832  CA  VAL A 412    14470  13191  14371    619  -2390  -2570       C  
ATOM   1833  C   VAL A 412      21.547 -18.065 -15.346  1.00118.85           C  
ANISOU 1833  C   VAL A 412    15410  14153  15594    393  -2516  -2549       C  
ATOM   1834  O   VAL A 412      22.278 -19.006 -15.652  1.00122.46           O  
ANISOU 1834  O   VAL A 412    15741  14736  16051    298  -2479  -2320       O  
ATOM   1835  CB  VAL A 412      19.483 -19.475 -14.932  1.00102.21           C  
ANISOU 1835  CB  VAL A 412    13341  12531  12964    708  -2336  -2513       C  
ATOM   1836  CG1 VAL A 412      19.938 -19.659 -13.494  1.00101.15           C  
ANISOU 1836  CG1 VAL A 412    13169  12630  12635    661  -2486  -2721       C  
ATOM   1837  CG2 VAL A 412      17.965 -19.478 -15.003  1.00100.21           C  
ANISOU 1837  CG2 VAL A 412    13161  12354  12561    924  -2224  -2555       C  
ATOM   1838  N   PHE A 413      21.998 -16.895 -14.894  1.00121.96           N  
ANISOU 1838  N   PHE A 413    15853  14314  16171    309  -2661  -2787       N  
ATOM   1839  CA  PHE A 413      23.397 -16.646 -14.551  1.00121.80           C  
ANISOU 1839  CA  PHE A 413    15723  14211  16343     82  -2826  -2822       C  
ATOM   1840  C   PHE A 413      23.696 -17.210 -13.182  1.00128.46           C  
ANISOU 1840  C   PHE A 413    16507  15388  16915     51  -2995  -2994       C  
ATOM   1841  O   PHE A 413      22.773 -17.548 -12.445  1.00127.57           O  
ANISOU 1841  O   PHE A 413    16471  15518  16480    210  -2977  -3134       O  
ATOM   1842  CB  PHE A 413      23.703 -15.153 -14.568  1.00123.47           C  
ANISOU 1842  CB  PHE A 413    16020  14028  16864     -7  -2932  -3029       C  
ATOM   1843  CG  PHE A 413      23.992 -14.612 -15.929  1.00121.10           C  
ANISOU 1843  CG  PHE A 413    15723  13376  16914    -67  -2804  -2789       C  
ATOM   1844  CD1 PHE A 413      24.378 -15.458 -16.954  1.00120.10           C  
ANISOU 1844  CD1 PHE A 413    15495  13305  16830   -103  -2645  -2425       C  
ATOM   1845  CD2 PHE A 413      23.878 -13.258 -16.189  1.00116.57           C  
ANISOU 1845  CD2 PHE A 413    15265  12407  16618    -82  -2832  -2925       C  
ATOM   1846  CE1 PHE A 413      24.648 -14.962 -18.211  1.00117.16           C  
ANISOU 1846  CE1 PHE A 413    15145  12627  16746   -153  -2512  -2195       C  
ATOM   1847  CE2 PHE A 413      24.149 -12.758 -17.442  1.00114.68           C  
ANISOU 1847  CE2 PHE A 413    15035  11847  16689   -136  -2707  -2675       C  
ATOM   1848  CZ  PHE A 413      24.534 -13.609 -18.453  1.00116.11           C  
ANISOU 1848  CZ  PHE A 413    15121  12112  16882   -171  -2545  -2307       C  
ATOM   1849  N   PHE A 414      24.975 -17.293 -12.831  1.00142.89           N  
ANISOU 1849  N   PHE A 414    18190  17229  18872   -152  -3160  -2974       N  
ATOM   1850  CA  PHE A 414      25.360 -17.942 -11.585  1.00146.72           C  
ANISOU 1850  CA  PHE A 414    18602  18059  19088   -189  -3338  -3082       C  
ATOM   1851  C   PHE A 414      24.640 -17.370 -10.363  1.00145.92           C  
ANISOU 1851  C   PHE A 414    18672  18063  18710    -91  -3466  -3475       C  
ATOM   1852  O   PHE A 414      24.482 -16.153 -10.221  1.00145.95           O  
ANISOU 1852  O   PHE A 414    18807  17793  18854   -107  -3540  -3748       O  
ATOM   1853  CB  PHE A 414      26.870 -17.859 -11.370  1.00160.30           C  
ANISOU 1853  CB  PHE A 414    20134  19728  21044   -435  -3543  -3037       C  
ATOM   1854  CG  PHE A 414      27.298 -18.281  -9.990  1.00174.88           C  
ANISOU 1854  CG  PHE A 414    21924  21901  22621   -486  -3790  -3194       C  
ATOM   1855  CD1 PHE A 414      27.233 -19.613  -9.605  1.00177.27           C  
ANISOU 1855  CD1 PHE A 414    22135  22583  22636   -407  -3750  -3005       C  
ATOM   1856  CD2 PHE A 414      27.742 -17.341  -9.066  1.00182.76           C  
ANISOU 1856  CD2 PHE A 414    22975  22823  23641   -613  -4070  -3534       C  
ATOM   1857  CE1 PHE A 414      27.616 -20.005  -8.329  1.00182.25           C  
ANISOU 1857  CE1 PHE A 414    22722  23527  22997   -445  -3983  -3123       C  
ATOM   1858  CE2 PHE A 414      28.128 -17.723  -7.787  1.00186.34           C  
ANISOU 1858  CE2 PHE A 414    23395  23597  23807   -660  -4318  -3680       C  
ATOM   1859  CZ  PHE A 414      28.065 -19.057  -7.418  1.00186.27           C  
ANISOU 1859  CZ  PHE A 414    23291  23982  23502   -571  -4275  -3462       C  
ATOM   1860  N   GLY A 415      24.192 -18.277  -9.497  1.00140.28           N  
ANISOU 1860  N   GLY A 415    17960  17739  17601     17  -3470  -3493       N  
ATOM   1861  CA  GLY A 415      23.535 -17.925  -8.254  1.00138.01           C  
ANISOU 1861  CA  GLY A 415    17832  17624  16982    123  -3565  -3842       C  
ATOM   1862  C   GLY A 415      22.040 -17.749  -8.411  1.00132.43           C  
ANISOU 1862  C   GLY A 415    17279  16912  16126    368  -3343  -3924       C  
ATOM   1863  O   GLY A 415      21.267 -18.105  -7.518  1.00127.77           O  
ANISOU 1863  O   GLY A 415    16768  16607  15170    516  -3306  -4056       O  
ATOM   1864  N   GLU A 416      21.640 -17.201  -9.556  1.00131.53           N  
ANISOU 1864  N   GLU A 416    17197  16478  16300    412  -3194  -3827       N  
ATOM   1865  CA  GLU A 416      20.247 -16.863  -9.814  1.00132.40           C  
ANISOU 1865  CA  GLU A 416    17434  16528  16345    640  -3004  -3900       C  
ATOM   1866  C   GLU A 416      19.339 -18.070  -9.660  1.00139.72           C  
ANISOU 1866  C   GLU A 416    18315  17819  16953    803  -2838  -3730       C  
ATOM   1867  O   GLU A 416      19.768 -19.217  -9.800  1.00140.59           O  
ANISOU 1867  O   GLU A 416    18292  18148  16979    738  -2819  -3466       O  
ATOM   1868  CB  GLU A 416      20.095 -16.269 -11.210  1.00126.63           C  
ANISOU 1868  CB  GLU A 416    16712  15422  15979    644  -2886  -3731       C  
ATOM   1869  CG  GLU A 416      20.922 -15.016 -11.435  1.00132.32           C  
ANISOU 1869  CG  GLU A 416    17478  15740  17058    485  -3023  -3875       C  
ATOM   1870  CD  GLU A 416      20.610 -14.342 -12.758  1.00136.76           C  
ANISOU 1870  CD  GLU A 416    18080  15931  17952    523  -2888  -3710       C  
ATOM   1871  OE1 GLU A 416      20.867 -13.126 -12.882  1.00139.86           O  
ANISOU 1871  OE1 GLU A 416    18558  15955  18626    463  -2958  -3873       O  
ATOM   1872  OE2 GLU A 416      20.105 -15.027 -13.675  1.00136.82           O  
ANISOU 1872  OE2 GLU A 416    18041  16010  17934    610  -2718  -3414       O  
ATOM   1873  N   ASN A 417      18.075 -17.808  -9.367  1.00149.27           N  
ANISOU 1873  N   ASN A 417    19627  19081  18008   1016  -2710  -3878       N  
ATOM   1874  CA  ASN A 417      17.147 -18.889  -9.112  1.00153.27           C  
ANISOU 1874  CA  ASN A 417    20083  19932  18221   1166  -2551  -3738       C  
ATOM   1875  C   ASN A 417      16.597 -19.493 -10.399  1.00146.55           C  
ANISOU 1875  C   ASN A 417    19145  19024  17512   1216  -2379  -3406       C  
ATOM   1876  O   ASN A 417      16.534 -18.831 -11.436  1.00146.41           O  
ANISOU 1876  O   ASN A 417    19155  18692  17783   1211  -2347  -3340       O  
ATOM   1877  CB  ASN A 417      16.007 -18.398  -8.223  1.00161.52           C  
ANISOU 1877  CB  ASN A 417    21250  21080  19040   1378  -2467  -4026       C  
ATOM   1878  CG  ASN A 417      15.619 -19.415  -7.176  1.00164.79           C  
ANISOU 1878  CG  ASN A 417    21633  21937  19042   1455  -2412  -4011       C  
ATOM   1879  OD1 ASN A 417      15.521 -20.610  -7.465  1.00172.14           O  
ANISOU 1879  OD1 ASN A 417    22435  23081  19888   1442  -2328  -3709       O  
ATOM   1880  ND2 ASN A 417      15.417 -18.955  -5.947  1.00156.72           N  
ANISOU 1880  ND2 ASN A 417    20740  21050  17757   1532  -2456  -4335       N  
ATOM   1881  N   LEU A 418      16.226 -20.766 -10.330  1.00140.42           N  
ANISOU 1881  N   LEU A 418    18272  18551  16530   1255  -2279  -3191       N  
ATOM   1882  CA  LEU A 418      15.537 -21.412 -11.436  1.00132.23           C  
ANISOU 1882  CA  LEU A 418    17167  17497  15578   1312  -2121  -2911       C  
ATOM   1883  C   LEU A 418      14.207 -20.706 -11.640  1.00124.21           C  
ANISOU 1883  C   LEU A 418    16215  16382  14599   1511  -2010  -3025       C  
ATOM   1884  O   LEU A 418      13.546 -20.344 -10.669  1.00129.18           O  
ANISOU 1884  O   LEU A 418    16897  17132  15054   1647  -1980  -3257       O  
ATOM   1885  CB  LEU A 418      15.320 -22.908 -11.172  1.00132.03           C  
ANISOU 1885  CB  LEU A 418    17031  17812  15320   1318  -2036  -2693       C  
ATOM   1886  CG  LEU A 418      16.544 -23.804 -10.927  1.00130.90           C  
ANISOU 1886  CG  LEU A 418    16801  17806  15130   1152  -2125  -2538       C  
ATOM   1887  CD1 LEU A 418      17.646 -23.514 -11.941  1.00123.11           C  
ANISOU 1887  CD1 LEU A 418    15788  16537  14449    992  -2189  -2415       C  
ATOM   1888  CD2 LEU A 418      17.060 -23.688  -9.482  1.00138.53           C  
ANISOU 1888  CD2 LEU A 418    17792  18980  15863   1126  -2267  -2743       C  
ATOM   1889  N   PRO A 419      13.832 -20.481 -12.904  1.00113.04           N  
ANISOU 1889  N   PRO A 419    14796  14744  13411   1535  -1949  -2858       N  
ATOM   1890  CA  PRO A 419      12.554 -19.878 -13.297  1.00114.06           C  
ANISOU 1890  CA  PRO A 419    14952  14766  13618   1728  -1853  -2900       C  
ATOM   1891  C   PRO A 419      11.372 -20.486 -12.558  1.00115.25           C  
ANISOU 1891  C   PRO A 419    15037  15227  13525   1894  -1730  -2933       C  
ATOM   1892  O   PRO A 419      11.322 -21.698 -12.393  1.00112.82           O  
ANISOU 1892  O   PRO A 419    14634  15188  13042   1851  -1680  -2764       O  
ATOM   1893  CB  PRO A 419      12.477 -20.185 -14.791  1.00109.57           C  
ANISOU 1893  CB  PRO A 419    14350  14049  13231   1682  -1817  -2602       C  
ATOM   1894  CG  PRO A 419      13.903 -20.209 -15.224  1.00106.56           C  
ANISOU 1894  CG  PRO A 419    13986  13522  12979   1472  -1905  -2510       C  
ATOM   1895  CD  PRO A 419      14.696 -20.749 -14.066  1.00107.02           C  
ANISOU 1895  CD  PRO A 419    14004  13808  12850   1376  -1974  -2612       C  
ATOM   1896  N   GLU A 420      10.435 -19.658 -12.119  1.00127.18           N  
ANISOU 1896  N   GLU A 420    16591  16691  15041   2087  -1666  -3140       N  
ATOM   1897  CA  GLU A 420       9.288 -20.166 -11.382  1.00131.04           C  
ANISOU 1897  CA  GLU A 420    17002  17473  15314   2256  -1522  -3173       C  
ATOM   1898  C   GLU A 420       8.409 -21.031 -12.279  1.00125.16           C  
ANISOU 1898  C   GLU A 420    16115  16824  14618   2292  -1430  -2875       C  
ATOM   1899  O   GLU A 420       7.616 -21.837 -11.792  1.00125.80           O  
ANISOU 1899  O   GLU A 420    16086  17186  14524   2368  -1313  -2809       O  
ATOM   1900  CB  GLU A 420       8.467 -19.019 -10.788  1.00143.61           C  
ANISOU 1900  CB  GLU A 420    18666  18963  16935   2473  -1450  -3462       C  
ATOM   1901  CG  GLU A 420       7.455 -19.460  -9.735  1.00153.77           C  
ANISOU 1901  CG  GLU A 420    19888  20579  17959   2647  -1281  -3550       C  
ATOM   1902  CD  GLU A 420       6.230 -18.563  -9.686  1.00166.40           C  
ANISOU 1902  CD  GLU A 420    21477  22066  19681   2907  -1147  -3695       C  
ATOM   1903  OE1 GLU A 420       6.237 -17.511 -10.360  1.00171.16           O  
ANISOU 1903  OE1 GLU A 420    22148  22320  20564   2953  -1205  -3760       O  
ATOM   1904  OE2 GLU A 420       5.257 -18.916  -8.983  1.00170.51           O  
ANISOU 1904  OE2 GLU A 420    21913  22843  20031   3070   -973  -3728       O  
ATOM   1905  N   GLN A 421       8.555 -20.870 -13.590  1.00120.49           N  
ANISOU 1905  N   GLN A 421    15526  15997  14257   2228  -1487  -2694       N  
ATOM   1906  CA  GLN A 421       7.735 -21.620 -14.533  1.00115.82           C  
ANISOU 1906  CA  GLN A 421    14820  15472  13715   2248  -1435  -2429       C  
ATOM   1907  C   GLN A 421       8.042 -23.108 -14.450  1.00110.49           C  
ANISOU 1907  C   GLN A 421    14061  15057  12864   2110  -1408  -2236       C  
ATOM   1908  O   GLN A 421       7.176 -23.944 -14.706  1.00115.98           O  
ANISOU 1908  O   GLN A 421    14636  15916  13515   2142  -1336  -2075       O  
ATOM   1909  CB  GLN A 421       7.942 -21.125 -15.965  1.00115.47           C  
ANISOU 1909  CB  GLN A 421    14832  15125  13915   2198  -1515  -2276       C  
ATOM   1910  CG  GLN A 421       6.974 -21.756 -16.959  1.00121.08           C  
ANISOU 1910  CG  GLN A 421    15440  15895  14668   2234  -1490  -2033       C  
ATOM   1911  CD  GLN A 421       7.152 -21.239 -18.372  1.00126.55           C  
ANISOU 1911  CD  GLN A 421    16212  16308  15561   2195  -1572  -1876       C  
ATOM   1912  OE1 GLN A 421       7.890 -20.283 -18.604  1.00133.81           O  
ANISOU 1912  OE1 GLN A 421    17255  16964  16624   2165  -1628  -1947       O  
ATOM   1913  NE2 GLN A 421       6.468 -21.869 -19.325  1.00120.45           N  
ANISOU 1913  NE2 GLN A 421    15375  15591  14798   2190  -1585  -1657       N  
ATOM   1914  N   PHE A 422       9.277 -23.430 -14.081  1.00101.19           N  
ANISOU 1914  N   PHE A 422    12936  13906  11606   1955  -1471  -2251       N  
ATOM   1915  CA  PHE A 422       9.714 -24.817 -13.994  1.00 92.96           C  
ANISOU 1915  CA  PHE A 422    11822  13077  10423   1826  -1448  -2062       C  
ATOM   1916  C   PHE A 422       8.968 -25.626 -12.937  1.00 99.85           C  
ANISOU 1916  C   PHE A 422    12593  14282  11061   1905  -1338  -2065       C  
ATOM   1917  O   PHE A 422       8.392 -26.668 -13.236  1.00103.12           O  
ANISOU 1917  O   PHE A 422    12903  14839  11440   1887  -1264  -1868       O  
ATOM   1918  CB  PHE A 422      11.206 -24.890 -13.699  1.00 85.39           C  
ANISOU 1918  CB  PHE A 422    10919  12079   9444   1665  -1545  -2085       C  
ATOM   1919  CG  PHE A 422      11.658 -26.248 -13.252  1.00 86.79           C  
ANISOU 1919  CG  PHE A 422    11019  12505   9454   1569  -1516  -1928       C  
ATOM   1920  CD1 PHE A 422      11.754 -27.288 -14.154  1.00 86.75           C  
ANISOU 1920  CD1 PHE A 422    10961  12496   9503   1478  -1473  -1674       C  
ATOM   1921  CD2 PHE A 422      11.984 -26.488 -11.933  1.00 94.58           C  
ANISOU 1921  CD2 PHE A 422    11995  13720  10222   1575  -1533  -2033       C  
ATOM   1922  CE1 PHE A 422      12.169 -28.542 -13.752  1.00 86.09           C  
ANISOU 1922  CE1 PHE A 422    10806  12610   9294   1399  -1437  -1522       C  
ATOM   1923  CE2 PHE A 422      12.398 -27.745 -11.523  1.00 95.67           C  
ANISOU 1923  CE2 PHE A 422    12057  14076  10216   1497  -1508  -1859       C  
ATOM   1924  CZ  PHE A 422      12.490 -28.771 -12.436  1.00 87.18           C  
ANISOU 1924  CZ  PHE A 422    10919  12972   9232   1411  -1455  -1601       C  
ATOM   1925  N   HIS A 423       9.000 -25.153 -11.697  1.00102.24           N  
ANISOU 1925  N   HIS A 423    12938  14708  11202   1985  -1326  -2288       N  
ATOM   1926  CA  HIS A 423       8.414 -25.901 -10.594  1.00102.27           C  
ANISOU 1926  CA  HIS A 423    12865  15045  10950   2058  -1208  -2284       C  
ATOM   1927  C   HIS A 423       6.919 -26.045 -10.755  1.00101.12           C  
ANISOU 1927  C   HIS A 423    12597  14987  10837   2209  -1060  -2223       C  
ATOM   1928  O   HIS A 423       6.359 -27.108 -10.490  1.00104.90           O  
ANISOU 1928  O   HIS A 423    12953  15698  11205   2207   -953  -2057       O  
ATOM   1929  CB  HIS A 423       8.737 -25.231  -9.266  1.00108.16           C  
ANISOU 1929  CB  HIS A 423    13712  15893  11490   2125  -1228  -2564       C  
ATOM   1930  CG  HIS A 423      10.185 -25.298  -8.913  1.00117.21           C  
ANISOU 1930  CG  HIS A 423    14939  17028  12570   1962  -1387  -2601       C  
ATOM   1931  ND1 HIS A 423      11.002 -24.189  -8.907  1.00124.49           N  
ANISOU 1931  ND1 HIS A 423    15984  17719  13598   1914  -1534  -2816       N  
ATOM   1932  CD2 HIS A 423      10.972 -26.350  -8.588  1.00121.48           C  
ANISOU 1932  CD2 HIS A 423    15434  17746  12978   1833  -1430  -2433       C  
ATOM   1933  CE1 HIS A 423      12.228 -24.551  -8.573  1.00128.42           C  
ANISOU 1933  CE1 HIS A 423    16496  18270  14029   1756  -1668  -2783       C  
ATOM   1934  NE2 HIS A 423      12.237 -25.858  -8.377  1.00127.77           N  
ANISOU 1934  NE2 HIS A 423    16312  18436  13799   1714  -1608  -2547       N  
ATOM   1935  N   ARG A 424       6.278 -24.975 -11.206  1.00 96.84           N  
ANISOU 1935  N   ARG A 424    12076  14247  10471   2339  -1058  -2343       N  
ATOM   1936  CA  ARG A 424       4.836 -24.974 -11.354  1.00 96.39           C  
ANISOU 1936  CA  ARG A 424    11879  14262  10482   2501   -930  -2293       C  
ATOM   1937  C   ARG A 424       4.440 -26.016 -12.388  1.00 94.34           C  
ANISOU 1937  C   ARG A 424    11490  14026  10327   2399   -939  -1996       C  
ATOM   1938  O   ARG A 424       3.387 -26.645 -12.273  1.00 96.23           O  
ANISOU 1938  O   ARG A 424    11565  14446  10551   2460   -826  -1880       O  
ATOM   1939  CB  ARG A 424       4.341 -23.588 -11.754  1.00 99.88           C  
ANISOU 1939  CB  ARG A 424    12371  14447  11133   2660   -950  -2456       C  
ATOM   1940  CG  ARG A 424       2.866 -23.328 -11.470  1.00109.07           C  
ANISOU 1940  CG  ARG A 424    13389  15712  12342   2886   -792  -2488       C  
ATOM   1941  CD  ARG A 424       2.415 -22.006 -12.091  1.00112.78           C  
ANISOU 1941  CD  ARG A 424    13895  15881  13074   3040   -831  -2595       C  
ATOM   1942  NE  ARG A 424       3.407 -20.945 -11.918  1.00111.27           N  
ANISOU 1942  NE  ARG A 424    13918  15441  12919   3016   -931  -2827       N  
ATOM   1943  CZ  ARG A 424       4.219 -20.513 -12.880  1.00103.33           C  
ANISOU 1943  CZ  ARG A 424    13019  14153  12090   2891  -1090  -2769       C  
ATOM   1944  NH1 ARG A 424       4.161 -21.052 -14.088  1.00105.04           N  
ANISOU 1944  NH1 ARG A 424    13171  14311  12427   2789  -1164  -2497       N  
ATOM   1945  NH2 ARG A 424       5.093 -19.550 -12.634  1.00 97.10           N  
ANISOU 1945  NH2 ARG A 424    12405  13137  11350   2861  -1172  -2983       N  
ATOM   1946  N   ALA A 425       5.315 -26.211 -13.376  1.00 91.25           N  
ANISOU 1946  N   ALA A 425    11176  13454  10041   2235  -1068  -1879       N  
ATOM   1947  CA  ALA A 425       5.081 -27.132 -14.490  1.00 85.36           C  
ANISOU 1947  CA  ALA A 425    10358  12687   9390   2121  -1098  -1626       C  
ATOM   1948  C   ALA A 425       5.193 -28.596 -14.078  1.00 83.45           C  
ANISOU 1948  C   ALA A 425    10029  12679   8997   2007  -1028  -1463       C  
ATOM   1949  O   ALA A 425       4.351 -29.413 -14.448  1.00 77.94           O  
ANISOU 1949  O   ALA A 425     9200  12077   8336   1987   -980  -1300       O  
ATOM   1950  CB  ALA A 425       6.050 -26.833 -15.622  1.00 82.46           C  
ANISOU 1950  CB  ALA A 425    10125  12051   9156   1995  -1230  -1568       C  
ATOM   1951  N   MET A 426       6.240 -28.911 -13.316  1.00 88.10           N  
ANISOU 1951  N   MET A 426    10688  13351   9434   1929  -1033  -1500       N  
ATOM   1952  CA  MET A 426       6.473 -30.253 -12.784  1.00 82.26           C  
ANISOU 1952  CA  MET A 426     9880  12828   8549   1834   -966  -1342       C  
ATOM   1953  C   MET A 426       5.346 -30.761 -11.898  1.00 83.79           C  
ANISOU 1953  C   MET A 426     9927  13289   8619   1935   -810  -1306       C  
ATOM   1954  O   MET A 426       4.908 -31.901 -12.050  1.00 86.35           O  
ANISOU 1954  O   MET A 426    10137  13724   8949   1865   -742  -1106       O  
ATOM   1955  CB  MET A 426       7.779 -30.276 -12.002  1.00 82.80           C  
ANISOU 1955  CB  MET A 426    10044  12943   8474   1765  -1020  -1408       C  
ATOM   1956  CG  MET A 426       8.998 -30.194 -12.887  1.00 86.63           C  
ANISOU 1956  CG  MET A 426    10625  13198   9093   1624  -1142  -1360       C  
ATOM   1957  SD  MET A 426       9.461 -31.794 -13.573  1.00126.51           S  
ANISOU 1957  SD  MET A 426    15624  18261  14182   1460  -1110  -1070       S  
ATOM   1958  CE  MET A 426      10.207 -32.546 -12.132  1.00128.73           C  
ANISOU 1958  CE  MET A 426    15871  18802  14238   1434  -1086  -1030       C  
ATOM   1959  N   LYS A 427       4.889 -29.914 -10.980  1.00 77.86           N  
ANISOU 1959  N   LYS A 427     9183  12633   7766   2099   -742  -1502       N  
ATOM   1960  CA  LYS A 427       3.785 -30.240 -10.076  1.00 88.87           C  
ANISOU 1960  CA  LYS A 427    10440  14288   9039   2223   -560  -1485       C  
ATOM   1961  C   LYS A 427       2.555 -30.761 -10.846  1.00 84.48           C  
ANISOU 1961  C   LYS A 427     9692  13736   8669   2231   -498  -1307       C  
ATOM   1962  O   LYS A 427       1.831 -31.640 -10.361  1.00 87.48           O  
ANISOU 1962  O   LYS A 427     9918  14331   8990   2234   -356  -1163       O  
ATOM   1963  CB  LYS A 427       3.428 -29.003  -9.227  1.00 96.86           C  
ANISOU 1963  CB  LYS A 427    11513  15330   9960   2423   -495  -1764       C  
ATOM   1964  CG  LYS A 427       2.280 -29.164  -8.224  1.00100.42           C  
ANISOU 1964  CG  LYS A 427    11833  16052  10271   2587   -269  -1777       C  
ATOM   1965  CD  LYS A 427       2.682 -29.993  -7.021  1.00107.41           C  
ANISOU 1965  CD  LYS A 427    12741  17228  10843   2550   -174  -1719       C  
ATOM   1966  CE  LYS A 427       1.555 -30.051  -5.994  1.00117.67           C  
ANISOU 1966  CE  LYS A 427    13926  18799  11985   2728     80  -1740       C  
ATOM   1967  NZ  LYS A 427       1.921 -30.836  -4.772  1.00122.52           N  
ANISOU 1967  NZ  LYS A 427    14579  19716  12258   2704    182  -1666       N  
ATOM   1968  N   TYR A 428       2.336 -30.227 -12.048  1.00 79.19           N  
ANISOU 1968  N   TYR A 428     9030  12830   8227   2224   -615  -1305       N  
ATOM   1969  CA  TYR A 428       1.264 -30.692 -12.929  1.00 78.38           C  
ANISOU 1969  CA  TYR A 428     8757  12711   8313   2205   -617  -1136       C  
ATOM   1970  C   TYR A 428       1.684 -31.920 -13.713  1.00 76.55           C  
ANISOU 1970  C   TYR A 428     8526  12440   8120   1990   -688   -926       C  
ATOM   1971  O   TYR A 428       0.981 -32.931 -13.734  1.00 76.71           O  
ANISOU 1971  O   TYR A 428     8388  12586   8173   1926   -620   -758       O  
ATOM   1972  CB  TYR A 428       0.846 -29.586 -13.908  1.00 78.70           C  
ANISOU 1972  CB  TYR A 428     8817  12522   8562   2296   -731  -1210       C  
ATOM   1973  CG  TYR A 428      -0.212 -29.995 -14.922  1.00 78.67           C  
ANISOU 1973  CG  TYR A 428     8646  12494   8753   2267   -787  -1037       C  
ATOM   1974  CD1 TYR A 428      -1.523 -30.219 -14.533  1.00 85.30           C  
ANISOU 1974  CD1 TYR A 428     9242  13510   9660   2370   -668   -975       C  
ATOM   1975  CD2 TYR A 428       0.099 -30.141 -16.275  1.00 77.02           C  
ANISOU 1975  CD2 TYR A 428     8518  12088   8656   2136   -961   -937       C  
ATOM   1976  CE1 TYR A 428      -2.495 -30.592 -15.453  1.00 85.92           C  
ANISOU 1976  CE1 TYR A 428     9145  13571   9930   2329   -749   -817       C  
ATOM   1977  CE2 TYR A 428      -0.871 -30.511 -17.201  1.00 77.33           C  
ANISOU 1977  CE2 TYR A 428     8415  12116   8850   2100  -1044   -791       C  
ATOM   1978  CZ  TYR A 428      -2.169 -30.731 -16.779  1.00 86.62           C  
ANISOU 1978  CZ  TYR A 428     9333  13470  10109   2192   -951   -732       C  
ATOM   1979  OH  TYR A 428      -3.152 -31.102 -17.672  1.00 85.90           O  
ANISOU 1979  OH  TYR A 428     9074  13376  10186   2145  -1058   -586       O  
ATOM   1980  N   ASP A 429       2.843 -31.810 -14.356  1.00 74.38           N  
ANISOU 1980  N   ASP A 429     8430  11976   7856   1880   -814   -941       N  
ATOM   1981  CA  ASP A 429       3.287 -32.772 -15.359  1.00 80.13           C  
ANISOU 1981  CA  ASP A 429     9197  12598   8649   1694   -890   -773       C  
ATOM   1982  C   ASP A 429       3.581 -34.155 -14.796  1.00 89.61           C  
ANISOU 1982  C   ASP A 429    10344  13954   9748   1578   -797   -622       C  
ATOM   1983  O   ASP A 429       3.399 -35.161 -15.488  1.00 87.73           O  
ANISOU 1983  O   ASP A 429    10068  13679   9588   1447   -811   -467       O  
ATOM   1984  CB  ASP A 429       4.531 -32.242 -16.083  1.00 70.98           C  
ANISOU 1984  CB  ASP A 429     8241  11207   7521   1624  -1010   -829       C  
ATOM   1985  CG  ASP A 429       4.199 -31.164 -17.120  1.00 84.10           C  
ANISOU 1985  CG  ASP A 429     9963  12659   9332   1687  -1122   -889       C  
ATOM   1986  OD1 ASP A 429       3.016 -31.033 -17.516  1.00 77.89           O  
ANISOU 1986  OD1 ASP A 429     9057  11895   8642   1756  -1138   -851       O  
ATOM   1987  OD2 ASP A 429       5.133 -30.452 -17.552  1.00 83.21           O  
ANISOU 1987  OD2 ASP A 429    10007  12356   9252   1665  -1198   -956       O  
ATOM   1988  N   LYS A 430       4.033 -34.207 -13.545  1.00 96.63           N  
ANISOU 1988  N   LYS A 430    11243  15012  10462   1626   -709   -668       N  
ATOM   1989  CA  LYS A 430       4.488 -35.465 -12.966  1.00 95.66           C  
ANISOU 1989  CA  LYS A 430    11090  15022  10236   1525   -631   -508       C  
ATOM   1990  C   LYS A 430       3.345 -36.472 -12.848  1.00 94.30           C  
ANISOU 1990  C   LYS A 430    10728  14989  10113   1494   -514   -336       C  
ATOM   1991  O   LYS A 430       3.560 -37.676 -12.975  1.00 93.01           O  
ANISOU 1991  O   LYS A 430    10536  14829   9973   1362   -481   -158       O  
ATOM   1992  CB  LYS A 430       5.155 -35.229 -11.600  1.00101.12           C  
ANISOU 1992  CB  LYS A 430    11832  15889  10699   1596   -580   -590       C  
ATOM   1993  CG  LYS A 430       4.222 -34.870 -10.446  1.00106.82           C  
ANISOU 1993  CG  LYS A 430    12459  16853  11276   1754   -439   -666       C  
ATOM   1994  CD  LYS A 430       4.927 -35.003  -9.095  1.00111.29           C  
ANISOU 1994  CD  LYS A 430    13089  17629  11568   1789   -390   -694       C  
ATOM   1995  CE  LYS A 430       3.930 -35.217  -7.958  1.00120.57           C  
ANISOU 1995  CE  LYS A 430    14147  19091  12571   1910   -190   -663       C  
ATOM   1996  NZ  LYS A 430       4.531 -35.874  -6.752  1.00123.26           N  
ANISOU 1996  NZ  LYS A 430    14526  19670  12637   1900   -127   -570       N  
ATOM   1997  N   ASP A 431       2.130 -35.977 -12.641  1.00 85.71           N  
ANISOU 1997  N   ASP A 431     9500  13996   9068   1613   -450   -383       N  
ATOM   1998  CA  ASP A 431       0.966 -36.844 -12.489  1.00 89.57           C  
ANISOU 1998  CA  ASP A 431     9773  14624   9635   1585   -334   -218       C  
ATOM   1999  C   ASP A 431       0.171 -36.950 -13.784  1.00 82.59           C  
ANISOU 1999  C   ASP A 431     8803  13590   8988   1510   -446   -164       C  
ATOM   2000  O   ASP A 431      -1.003 -37.313 -13.773  1.00 79.31           O  
ANISOU 2000  O   ASP A 431     8176  13271   8688   1513   -383    -69       O  
ATOM   2001  CB  ASP A 431       0.052 -36.327 -11.377  1.00100.62           C  
ANISOU 2001  CB  ASP A 431    11034  16254  10943   1767   -164   -279       C  
ATOM   2002  CG  ASP A 431       0.801 -36.023 -10.101  1.00110.20           C  
ANISOU 2002  CG  ASP A 431    12365  17625  11880   1859    -78   -377       C  
ATOM   2003  OD1 ASP A 431       1.743 -36.780  -9.781  1.00109.21           O  
ANISOU 2003  OD1 ASP A 431    12329  17528  11638   1755    -88   -280       O  
ATOM   2004  OD2 ASP A 431       0.452 -35.026  -9.426  1.00114.71           O  
ANISOU 2004  OD2 ASP A 431    12945  18288  12353   2039     -6   -555       O  
ATOM   2005  N   GLU A 432       0.812 -36.644 -14.902  1.00 78.57           N  
ANISOU 2005  N   GLU A 432     8456  12851   8548   1440   -616   -217       N  
ATOM   2006  CA  GLU A 432       0.093 -36.518 -16.160  1.00 79.34           C  
ANISOU 2006  CA  GLU A 432     8508  12810   8828   1392   -755   -194       C  
ATOM   2007  C   GLU A 432       0.803 -37.248 -17.300  1.00 80.95           C  
ANISOU 2007  C   GLU A 432     8866  12818   9075   1204   -874   -125       C  
ATOM   2008  O   GLU A 432       0.169 -37.729 -18.241  1.00 72.29           O  
ANISOU 2008  O   GLU A 432     7717  11648   8101   1099   -970    -53       O  
ATOM   2009  CB  GLU A 432      -0.080 -35.037 -16.503  1.00 81.19           C  
ANISOU 2009  CB  GLU A 432     8794  12949   9104   1550   -845   -353       C  
ATOM   2010  CG  GLU A 432      -1.142 -34.765 -17.537  1.00 94.15           C  
ANISOU 2010  CG  GLU A 432    10325  14518  10931   1558   -975   -314       C  
ATOM   2011  CD  GLU A 432      -2.538 -34.880 -16.978  1.00102.02           C  
ANISOU 2011  CD  GLU A 432    11030  15705  12029   1645   -877   -253       C  
ATOM   2012  OE1 GLU A 432      -2.677 -34.797 -15.743  1.00103.67           O  
ANISOU 2012  OE1 GLU A 432    11155  16091  12143   1756   -689   -287       O  
ATOM   2013  OE2 GLU A 432      -3.490 -35.049 -17.774  1.00109.80           O  
ANISOU 2013  OE2 GLU A 432    11867  16668  13183   1603   -988   -168       O  
ATOM   2014  N   VAL A 433       2.125 -37.323 -17.200  1.00 75.53           N  
ANISOU 2014  N   VAL A 433     8364  12049   8284   1164   -866   -155       N  
ATOM   2015  CA  VAL A 433       2.957 -37.925 -18.231  1.00 73.78           C  
ANISOU 2015  CA  VAL A 433     8310  11633   8090   1012   -943   -107       C  
ATOM   2016  C   VAL A 433       2.710 -39.420 -18.348  1.00 78.03           C  
ANISOU 2016  C   VAL A 433     8781  12185   8682    855   -890     48       C  
ATOM   2017  O   VAL A 433       2.495 -40.094 -17.343  1.00 78.06           O  
ANISOU 2017  O   VAL A 433     8657  12347   8655    854   -759    139       O  
ATOM   2018  CB  VAL A 433       4.449 -37.680 -17.946  1.00 70.13           C  
ANISOU 2018  CB  VAL A 433     8019  11101   7529   1018   -922   -157       C  
ATOM   2019  CG1 VAL A 433       4.831 -38.224 -16.583  1.00 68.34           C  
ANISOU 2019  CG1 VAL A 433     7721  11056   7189   1041   -790   -102       C  
ATOM   2020  CG2 VAL A 433       5.310 -38.300 -19.026  1.00 71.08           C  
ANISOU 2020  CG2 VAL A 433     8302  11017   7687    879   -965   -103       C  
ATOM   2021  N   ASP A 434       2.733 -39.933 -19.578  1.00 76.63           N  
ANISOU 2021  N   ASP A 434     8702  11835   8580    721   -987     76       N  
ATOM   2022  CA  ASP A 434       2.581 -41.364 -19.818  1.00 71.36           C  
ANISOU 2022  CA  ASP A 434     8007  11125   7982    555   -948    198       C  
ATOM   2023  C   ASP A 434       3.817 -41.962 -20.472  1.00 68.89           C  
ANISOU 2023  C   ASP A 434     7913  10617   7643    457   -937    208       C  
ATOM   2024  O   ASP A 434       3.834 -43.146 -20.809  1.00 75.48           O  
ANISOU 2024  O   ASP A 434     8772  11364   8544    318   -904    288       O  
ATOM   2025  CB  ASP A 434       1.339 -41.649 -20.676  1.00 71.44           C  
ANISOU 2025  CB  ASP A 434     7919  11107   8117    462  -1072    218       C  
ATOM   2026  CG  ASP A 434       1.338 -40.898 -22.001  1.00 75.15           C  
ANISOU 2026  CG  ASP A 434     8545  11428   8580    460  -1256    123       C  
ATOM   2027  OD1 ASP A 434       2.397 -40.373 -22.409  1.00 72.46           O  
ANISOU 2027  OD1 ASP A 434     8415  10965   8152    495  -1266     58       O  
ATOM   2028  OD2 ASP A 434       0.262 -40.843 -22.640  1.00 75.57           O  
ANISOU 2028  OD2 ASP A 434     8503  11492   8720    419  -1395    129       O  
ATOM   2029  N   LEU A 435       4.850 -41.142 -20.633  1.00 67.14           N  
ANISOU 2029  N   LEU A 435     7846  10319   7345    530   -953    127       N  
ATOM   2030  CA  LEU A 435       6.086 -41.577 -21.276  1.00 73.44           C  
ANISOU 2030  CA  LEU A 435     8840  10933   8130    459   -922    138       C  
ATOM   2031  C   LEU A 435       7.204 -40.539 -21.149  1.00 74.18           C  
ANISOU 2031  C   LEU A 435     9040  10985   8161    556   -923     63       C  
ATOM   2032  O   LEU A 435       7.036 -39.379 -21.520  1.00 69.89           O  
ANISOU 2032  O   LEU A 435     8540  10415   7600    629  -1014    -32       O  
ATOM   2033  CB  LEU A 435       5.842 -41.882 -22.760  1.00 72.76           C  
ANISOU 2033  CB  LEU A 435     8902  10665   8077    348  -1017    110       C  
ATOM   2034  CG  LEU A 435       7.097 -42.295 -23.526  1.00 70.79           C  
ANISOU 2034  CG  LEU A 435     8873  10216   7809    288   -956    110       C  
ATOM   2035  CD1 LEU A 435       7.601 -43.606 -22.987  1.00 73.88           C  
ANISOU 2035  CD1 LEU A 435     9232  10583   8255    221   -813    215       C  
ATOM   2036  CD2 LEU A 435       6.816 -42.394 -25.001  1.00 71.43           C  
ANISOU 2036  CD2 LEU A 435     9132  10139   7870    199  -1056     57       C  
ATOM   2037  N   LEU A 436       8.353 -40.966 -20.643  1.00 63.75           N  
ANISOU 2037  N   LEU A 436     7751   9645   6824    550   -827    117       N  
ATOM   2038  CA  LEU A 436       9.500 -40.080 -20.540  1.00 63.06           C  
ANISOU 2038  CA  LEU A 436     7747   9506   6706    614   -835     58       C  
ATOM   2039  C   LEU A 436      10.653 -40.521 -21.430  1.00 75.65           C  
ANISOU 2039  C   LEU A 436     9497  10898   8349    543   -781     98       C  
ATOM   2040  O   LEU A 436      11.081 -41.673 -21.399  1.00 62.40           O  
ANISOU 2040  O   LEU A 436     7823   9173   6712    480   -684    199       O  
ATOM   2041  CB  LEU A 436       9.981 -39.988 -19.100  1.00 63.32           C  
ANISOU 2041  CB  LEU A 436     7667   9712   6678    685   -789     79       C  
ATOM   2042  CG  LEU A 436      11.213 -39.109 -18.890  1.00 72.88           C  
ANISOU 2042  CG  LEU A 436     8940  10875   7877    731   -819     14       C  
ATOM   2043  CD1 LEU A 436      10.916 -38.076 -17.835  1.00 80.46           C  
ANISOU 2043  CD1 LEU A 436     9824  11999   8747    839   -875   -100       C  
ATOM   2044  CD2 LEU A 436      12.419 -39.930 -18.491  1.00 68.54           C  
ANISOU 2044  CD2 LEU A 436     8379  10311   7352    693   -743    133       C  
ATOM   2045  N   ILE A 437      11.157 -39.579 -22.217  1.00 72.98           N  
ANISOU 2045  N   ILE A 437     9285  10429   8013    562   -828     26       N  
ATOM   2046  CA  ILE A 437      12.270 -39.832 -23.113  1.00 70.56           C  
ANISOU 2046  CA  ILE A 437     9129   9932   7749    511   -754     61       C  
ATOM   2047  C   ILE A 437      13.398 -38.888 -22.771  1.00 61.38           C  
ANISOU 2047  C   ILE A 437     7964   8741   6616    564   -753     34       C  
ATOM   2048  O   ILE A 437      13.182 -37.704 -22.596  1.00 61.51           O  
ANISOU 2048  O   ILE A 437     7970   8784   6616    624   -845    -55       O  
ATOM   2049  CB  ILE A 437      11.865 -39.641 -24.585  1.00 71.27           C  
ANISOU 2049  CB  ILE A 437     9398   9870   7812    465   -798     21       C  
ATOM   2050  CG1 ILE A 437      10.631 -40.478 -24.900  1.00 70.26           C  
ANISOU 2050  CG1 ILE A 437     9254   9781   7662    397   -846     27       C  
ATOM   2051  CG2 ILE A 437      13.010 -39.986 -25.533  1.00 61.73           C  
ANISOU 2051  CG2 ILE A 437     8359   8468   6627    418   -680     60       C  
ATOM   2052  CD1 ILE A 437       9.940 -40.057 -26.155  1.00 65.59           C  
ANISOU 2052  CD1 ILE A 437     8804   9104   7014    367   -958    -26       C  
ATOM   2053  N   VAL A 438      14.601 -39.425 -22.662  1.00 61.25           N  
ANISOU 2053  N   VAL A 438     7946   8661   6664    540   -650    115       N  
ATOM   2054  CA  VAL A 438      15.785 -38.612 -22.435  1.00 61.27           C  
ANISOU 2054  CA  VAL A 438     7932   8618   6730    566   -652    105       C  
ATOM   2055  C   VAL A 438      16.675 -38.630 -23.668  1.00 67.64           C  
ANISOU 2055  C   VAL A 438     8882   9209   7610    524   -548    148       C  
ATOM   2056  O   VAL A 438      16.952 -39.684 -24.226  1.00 73.34           O  
ANISOU 2056  O   VAL A 438     9667   9842   8358    484   -423    224       O  
ATOM   2057  CB  VAL A 438      16.586 -39.097 -21.212  1.00 61.53           C  
ANISOU 2057  CB  VAL A 438     7811   8772   6797    583   -628    182       C  
ATOM   2058  CG1 VAL A 438      17.914 -38.363 -21.124  1.00 61.83           C  
ANISOU 2058  CG1 VAL A 438     7820   8739   6934    584   -638    184       C  
ATOM   2059  CG2 VAL A 438      15.763 -38.913 -19.937  1.00 61.86           C  
ANISOU 2059  CG2 VAL A 438     7729   9045   6729    636   -721    132       C  
ATOM   2060  N   ILE A 439      17.104 -37.455 -24.111  1.00 65.04           N  
ANISOU 2060  N   ILE A 439     8611   8785   7316    536   -585     99       N  
ATOM   2061  CA  ILE A 439      17.949 -37.362 -25.288  1.00 65.91           C  
ANISOU 2061  CA  ILE A 439     8858   8698   7487    503   -466    153       C  
ATOM   2062  C   ILE A 439      19.130 -36.426 -25.075  1.00 67.30           C  
ANISOU 2062  C   ILE A 439     8970   8807   7795    505   -460    167       C  
ATOM   2063  O   ILE A 439      18.958 -35.231 -24.896  1.00 66.39           O  
ANISOU 2063  O   ILE A 439     8848   8686   7693    524   -574     89       O  
ATOM   2064  CB  ILE A 439      17.161 -36.862 -26.521  1.00 61.90           C  
ANISOU 2064  CB  ILE A 439     8544   8092   6883    495   -500    109       C  
ATOM   2065  CG1 ILE A 439      15.696 -37.292 -26.460  1.00 61.71           C  
ANISOU 2065  CG1 ILE A 439     8526   8179   6741    498   -605     55       C  
ATOM   2066  CG2 ILE A 439      17.834 -37.323 -27.800  1.00 62.40           C  
ANISOU 2066  CG2 ILE A 439     8786   7981   6943    455   -331    178       C  
ATOM   2067  CD1 ILE A 439      14.980 -37.109 -27.758  1.00 62.19           C  
ANISOU 2067  CD1 ILE A 439     8779   8150   6699    477   -644     36       C  
ATOM   2068  N   GLY A 440      20.333 -36.972 -25.100  1.00 70.42           N  
ANISOU 2068  N   GLY A 440     9729   8800   8229    206   -350   -516       N  
ATOM   2069  CA  GLY A 440      21.521 -36.145 -25.173  1.00 75.19           C  
ANISOU 2069  CA  GLY A 440    10347   9283   8938     86   -200   -532       C  
ATOM   2070  C   GLY A 440      22.097 -35.706 -23.848  1.00 80.50           C  
ANISOU 2070  C   GLY A 440    10734  10114   9739     30   -232   -652       C  
ATOM   2071  O   GLY A 440      23.176 -35.115 -23.801  1.00 85.77           O  
ANISOU 2071  O   GLY A 440    11350  10704  10534    -94   -117   -683       O  
ATOM   2072  N   SER A 441      21.390 -36.009 -22.766  1.00 78.95           N  
ANISOU 2072  N   SER A 441    10346  10146   9504    113   -383   -725       N  
ATOM   2073  CA  SER A 441      21.821 -35.589 -21.435  1.00 74.03           C  
ANISOU 2073  CA  SER A 441     9481   9706   8942     74   -445   -860       C  
ATOM   2074  C   SER A 441      22.392 -36.730 -20.609  1.00 71.97           C  
ANISOU 2074  C   SER A 441     8960   9715   8671     68   -436   -804       C  
ATOM   2075  O   SER A 441      21.918 -37.859 -20.665  1.00 73.74           O  
ANISOU 2075  O   SER A 441     9158  10038   8822    140   -438   -691       O  
ATOM   2076  CB  SER A 441      20.661 -34.951 -20.681  1.00 66.12           C  
ANISOU 2076  CB  SER A 441     8462   8779   7880    178   -602  -1002       C  
ATOM   2077  OG  SER A 441      21.078 -34.518 -19.408  1.00 68.10           O  
ANISOU 2077  OG  SER A 441     8517   9210   8149    139   -660  -1158       O  
ATOM   2078  N   SER A 442      23.423 -36.424 -19.838  1.00 65.83           N  
ANISOU 2078  N   SER A 442     7990   9043   7980    -20   -442   -880       N  
ATOM   2079  CA  SER A 442      24.001 -37.407 -18.950  1.00 65.39           C  
ANISOU 2079  CA  SER A 442     7681   9251   7911     -8   -476   -819       C  
ATOM   2080  C   SER A 442      23.427 -37.234 -17.547  1.00 68.23           C  
ANISOU 2080  C   SER A 442     7913   9877   8132     49   -643   -935       C  
ATOM   2081  O   SER A 442      23.981 -37.743 -16.570  1.00 73.42           O  
ANISOU 2081  O   SER A 442     8367  10780   8749     49   -715   -916       O  
ATOM   2082  CB  SER A 442      25.521 -37.294 -18.962  1.00 71.28           C  
ANISOU 2082  CB  SER A 442     8264   9983   8838   -129   -403   -822       C  
ATOM   2083  OG  SER A 442      26.022 -37.876 -20.160  1.00 78.69           O  
ANISOU 2083  OG  SER A 442     9288  10740   9871   -149   -207   -679       O  
ATOM   2084  N   LEU A 443      22.305 -36.514 -17.482  1.00 62.72           N  
ANISOU 2084  N   LEU A 443     7346   9128   7355    108   -698  -1050       N  
ATOM   2085  CA  LEU A 443      21.496 -36.314 -16.275  1.00 62.00           C  
ANISOU 2085  CA  LEU A 443     7176   9270   7110    184   -809  -1175       C  
ATOM   2086  C   LEU A 443      22.237 -36.190 -14.938  1.00 72.44           C  
ANISOU 2086  C   LEU A 443     8309  10861   8355    139   -909  -1285       C  
ATOM   2087  O   LEU A 443      21.881 -36.857 -13.962  1.00 73.47           O  
ANISOU 2087  O   LEU A 443     8336  11273   8307    206   -961  -1244       O  
ATOM   2088  CB  LEU A 443      20.490 -37.447 -16.167  1.00 59.58           C  
ANISOU 2088  CB  LEU A 443     6849   9102   6685    290   -794  -1025       C  
ATOM   2089  CG  LEU A 443      19.364 -37.414 -17.189  1.00 58.54           C  
ANISOU 2089  CG  LEU A 443     6887   8771   6587    358   -767   -987       C  
ATOM   2090  CD1 LEU A 443      18.475 -38.650 -17.050  1.00 57.68           C  
ANISOU 2090  CD1 LEU A 443     6714   8799   6402    427   -752   -839       C  
ATOM   2091  CD2 LEU A 443      18.561 -36.142 -17.023  1.00 59.46           C  
ANISOU 2091  CD2 LEU A 443     7078   8807   6706    415   -827  -1190       C  
ATOM   2092  N   LYS A 444      23.238 -35.318 -14.878  1.00 79.58           N  
ANISOU 2092  N   LYS A 444     9173  11680   9382     19   -943  -1428       N  
ATOM   2093  CA  LYS A 444      23.977 -35.143 -13.635  1.00 78.57           C  
ANISOU 2093  CA  LYS A 444     8865  11808   9179    -35  -1083  -1562       C  
ATOM   2094  C   LYS A 444      23.956 -33.712 -13.091  1.00 85.08           C  
ANISOU 2094  C   LYS A 444     9735  12575  10015   -100  -1169  -1880       C  
ATOM   2095  O   LYS A 444      24.631 -33.421 -12.113  1.00 94.75           O  
ANISOU 2095  O   LYS A 444    10827  13992  11182   -168  -1309  -2038       O  
ATOM   2096  CB  LYS A 444      25.426 -35.602 -13.810  1.00 79.85           C  
ANISOU 2096  CB  LYS A 444     8847  11988   9504   -137  -1088  -1458       C  
ATOM   2097  CG  LYS A 444      26.182 -34.925 -14.926  1.00 81.77           C  
ANISOU 2097  CG  LYS A 444     9139  11905  10025   -272   -967  -1480       C  
ATOM   2098  CD  LYS A 444      27.665 -35.255 -14.844  1.00 87.52           C  
ANISOU 2098  CD  LYS A 444     9616  12701  10937   -379   -984  -1433       C  
ATOM   2099  CE  LYS A 444      28.207 -35.746 -16.183  1.00 92.77           C  
ANISOU 2099  CE  LYS A 444    10310  13131  11807   -412   -758  -1240       C  
ATOM   2100  NZ  LYS A 444      29.700 -35.783 -16.179  1.00 97.37           N  
ANISOU 2100  NZ  LYS A 444    10619  13733  12642   -537   -743  -1242       N  
ATOM   2101  N   VAL A 445      23.184 -32.823 -13.707  1.00 85.31           N  
ANISOU 2101  N   VAL A 445     9956  12337  10121    -73  -1105  -1981       N  
ATOM   2102  CA  VAL A 445      23.073 -31.457 -13.201  1.00 81.05           C  
ANISOU 2102  CA  VAL A 445     9481  11698   9616   -116  -1175  -2294       C  
ATOM   2103  C   VAL A 445      21.603 -31.057 -13.044  1.00 86.38           C  
ANISOU 2103  C   VAL A 445    10292  12345  10182     51  -1153  -2396       C  
ATOM   2104  O   VAL A 445      20.774 -31.241 -13.947  1.00 87.15           O  
ANISOU 2104  O   VAL A 445    10510  12274  10330    149  -1071  -2250       O  
ATOM   2105  CB  VAL A 445      23.835 -30.448 -14.104  1.00 96.01           C  
ANISOU 2105  CB  VAL A 445    11465  13210  11805   -273  -1117  -2354       C  
ATOM   2106  CG1 VAL A 445      24.291 -31.123 -15.398  1.00111.38           C  
ANISOU 2106  CG1 VAL A 445    13447  14986  13886   -313   -970  -2062       C  
ATOM   2107  CG2 VAL A 445      23.001 -29.201 -14.380  1.00 92.92           C  
ANISOU 2107  CG2 VAL A 445    11288  12521  11496   -222  -1098  -2534       C  
ATOM   2108  N   ARG A 446      21.295 -30.533 -11.863  1.00 82.75           N  
ANISOU 2108  N   ARG A 446     9801  12072   9569     88  -1233  -2660       N  
ATOM   2109  CA  ARG A 446      19.934 -30.215 -11.471  1.00 76.83           C  
ANISOU 2109  CA  ARG A 446     9123  11365   8703    259  -1196  -2790       C  
ATOM   2110  C   ARG A 446      19.492 -28.931 -12.164  1.00 77.69           C  
ANISOU 2110  C   ARG A 446     9408  11070   9042    291  -1168  -2947       C  
ATOM   2111  O   ARG A 446      20.324 -28.078 -12.464  1.00 79.73           O  
ANISOU 2111  O   ARG A 446     9727  11076   9490    151  -1199  -3059       O  
ATOM   2112  CB  ARG A 446      19.869 -30.096  -9.949  1.00 82.87           C  
ANISOU 2112  CB  ARG A 446     9811  12478   9198    283  -1267  -3032       C  
ATOM   2113  CG  ARG A 446      20.567 -31.257  -9.246  1.00 94.61           C  
ANISOU 2113  CG  ARG A 446    11144  14338  10464    233  -1335  -2861       C  
ATOM   2114  CD  ARG A 446      21.505 -30.805  -8.136  1.00107.74           C  
ANISOU 2114  CD  ARG A 446    12741  16207  11989    122  -1501  -3110       C  
ATOM   2115  NE  ARG A 446      20.768 -30.318  -6.975  1.00116.20           N  
ANISOU 2115  NE  ARG A 446    13870  17496  12786    215  -1508  -3396       N  
ATOM   2116  CZ  ARG A 446      20.195 -31.108  -6.071  1.00116.56           C  
ANISOU 2116  CZ  ARG A 446    13884  17916  12488    320  -1471  -3316       C  
ATOM   2117  NH1 ARG A 446      20.273 -32.431  -6.194  1.00113.14           N  
ANISOU 2117  NH1 ARG A 446    13361  17657  11969    344  -1443  -2950       N  
ATOM   2118  NH2 ARG A 446      19.539 -30.573  -5.048  1.00117.26           N  
ANISOU 2118  NH2 ARG A 446    14042  18192  12322    401  -1442  -3604       N  
ATOM   2119  N   PRO A 447      18.179 -28.765 -12.398  1.00 78.78           N  
ANISOU 2119  N   PRO A 447     9615  11133   9186    475  -1114  -2956       N  
ATOM   2120  CA  PRO A 447      17.032 -29.543 -11.924  1.00 80.67           C  
ANISOU 2120  CA  PRO A 447     9763  11649   9241    638  -1060  -2893       C  
ATOM   2121  C   PRO A 447      16.658 -30.702 -12.819  1.00 80.11           C  
ANISOU 2121  C   PRO A 447     9665  11589   9186    672  -1016  -2550       C  
ATOM   2122  O   PRO A 447      15.811 -31.509 -12.453  1.00 82.86           O  
ANISOU 2122  O   PRO A 447     9910  12169   9403    767   -964  -2461       O  
ATOM   2123  CB  PRO A 447      15.911 -28.512 -11.929  1.00 82.85           C  
ANISOU 2123  CB  PRO A 447    10118  11737   9625    808  -1033  -3112       C  
ATOM   2124  CG  PRO A 447      16.229 -27.666 -13.101  1.00 75.33           C  
ANISOU 2124  CG  PRO A 447     9341  10333   8947    769  -1068  -3074       C  
ATOM   2125  CD  PRO A 447      17.739 -27.621 -13.213  1.00 77.36           C  
ANISOU 2125  CD  PRO A 447     9615  10532   9248    535  -1104  -3042       C  
ATOM   2126  N   VAL A 448      17.276 -30.768 -13.986  1.00 81.87           N  
ANISOU 2126  N   VAL A 448     9986  11552   9568    585  -1023  -2371       N  
ATOM   2127  CA  VAL A 448      16.859 -31.705 -15.012  1.00 84.45           C  
ANISOU 2127  CA  VAL A 448    10340  11821   9926    623   -991  -2089       C  
ATOM   2128  C   VAL A 448      17.221 -33.145 -14.628  1.00 80.75           C  
ANISOU 2128  C   VAL A 448     9724  11650   9307    571   -959  -1891       C  
ATOM   2129  O   VAL A 448      16.520 -34.095 -14.986  1.00 72.40           O  
ANISOU 2129  O   VAL A 448     8632  10657   8220    631   -927  -1712       O  
ATOM   2130  CB  VAL A 448      17.486 -31.321 -16.360  1.00 86.97           C  
ANISOU 2130  CB  VAL A 448    10843  11782  10420    541   -984  -1967       C  
ATOM   2131  CG1 VAL A 448      16.762 -32.008 -17.507  1.00 76.34           C  
ANISOU 2131  CG1 VAL A 448     9586  10329   9092    618   -978  -1742       C  
ATOM   2132  CG2 VAL A 448      17.432 -29.806 -16.533  1.00 91.26           C  
ANISOU 2132  CG2 VAL A 448    11537  12018  11118    557  -1014  -2165       C  
ATOM   2133  N   ALA A 449      18.299 -33.295 -13.865  1.00 83.87           N  
ANISOU 2133  N   ALA A 449    10026  12218   9621    462   -983  -1928       N  
ATOM   2134  CA  ALA A 449      18.786 -34.617 -13.467  1.00 82.29           C  
ANISOU 2134  CA  ALA A 449     9693  12276   9297    425   -970  -1725       C  
ATOM   2135  C   ALA A 449      17.818 -35.363 -12.537  1.00 83.08           C  
ANISOU 2135  C   ALA A 449     9692  12682   9192    526   -937  -1683       C  
ATOM   2136  O   ALA A 449      17.878 -36.594 -12.414  1.00 88.37           O  
ANISOU 2136  O   ALA A 449    10282  13507   9785    522   -904  -1456       O  
ATOM   2137  CB  ALA A 449      20.140 -34.482 -12.805  1.00 80.83           C  
ANISOU 2137  CB  ALA A 449     9414  12212   9084    305  -1044  -1792       C  
ATOM   2138  N   LEU A 450      16.928 -34.619 -11.888  1.00 73.96           N  
ANISOU 2138  N   LEU A 450     8541  11598   7961    615   -925  -1900       N  
ATOM   2139  CA  LEU A 450      16.058 -35.200 -10.873  1.00 78.40           C  
ANISOU 2139  CA  LEU A 450     9001  12474   8312    696   -854  -1888       C  
ATOM   2140  C   LEU A 450      14.670 -35.505 -11.388  1.00 83.24           C  
ANISOU 2140  C   LEU A 450     9588  13023   9018    802   -768  -1816       C  
ATOM   2141  O   LEU A 450      13.808 -35.952 -10.634  1.00 99.64           O  
ANISOU 2141  O   LEU A 450    11563  15336  10961    865   -670  -1804       O  
ATOM   2142  CB  LEU A 450      15.941 -34.271  -9.672  1.00 76.57           C  
ANISOU 2142  CB  LEU A 450     8769  12419   7905    733   -862  -2197       C  
ATOM   2143  CG  LEU A 450      17.259 -33.890  -9.025  1.00 75.98           C  
ANISOU 2143  CG  LEU A 450     8702  12440   7726    621   -986  -2321       C  
ATOM   2144  CD1 LEU A 450      16.995 -32.925  -7.884  1.00 73.67           C  
ANISOU 2144  CD1 LEU A 450     8440  12304   7248    664   -996  -2672       C  
ATOM   2145  CD2 LEU A 450      17.996 -35.141  -8.567  1.00 70.29           C  
ANISOU 2145  CD2 LEU A 450     7889  11978   6840    563  -1025  -2060       C  
ATOM   2146  N   ILE A 451      14.445 -35.254 -12.665  1.00 68.05           N  
ANISOU 2146  N   ILE A 451     7751  10787   7317    817   -805  -1766       N  
ATOM   2147  CA  ILE A 451      13.130 -35.485 -13.246  1.00 69.28           C  
ANISOU 2147  CA  ILE A 451     7867  10867   7588    918   -775  -1713       C  
ATOM   2148  C   ILE A 451      12.772 -36.979 -13.456  1.00 77.37           C  
ANISOU 2148  C   ILE A 451     8798  12004   8596    879   -721  -1444       C  
ATOM   2149  O   ILE A 451      11.641 -37.372 -13.170  1.00 73.28           O  
ANISOU 2149  O   ILE A 451     8149  11607   8085    942   -651  -1428       O  
ATOM   2150  CB  ILE A 451      12.996 -34.711 -14.574  1.00 70.93           C  
ANISOU 2150  CB  ILE A 451     8230  10706   8013    957   -868  -1738       C  
ATOM   2151  CG1 ILE A 451      13.425 -33.257 -14.369  1.00 67.30           C  
ANISOU 2151  CG1 ILE A 451     7879  10090   7602    976   -910  -1985       C  
ATOM   2152  CG2 ILE A 451      11.576 -34.782 -15.106  1.00 69.75           C  
ANISOU 2152  CG2 ILE A 451     8019  10491   7991   1084   -889  -1723       C  
ATOM   2153  CD1 ILE A 451      13.185 -32.386 -15.564  1.00 68.39           C  
ANISOU 2153  CD1 ILE A 451     8189   9855   7942   1036   -992  -1999       C  
ATOM   2154  N   PRO A 452      13.714 -37.814 -13.949  1.00 77.63           N  
ANISOU 2154  N   PRO A 452     8884  11983   8631    776   -740  -1242       N  
ATOM   2155  CA  PRO A 452      13.393 -39.240 -14.069  1.00 76.75           C  
ANISOU 2155  CA  PRO A 452     8692  11951   8517    738   -683  -1004       C  
ATOM   2156  C   PRO A 452      12.975 -39.868 -12.750  1.00 82.46           C  
ANISOU 2156  C   PRO A 452     9265  12999   9066    745   -573   -950       C  
ATOM   2157  O   PRO A 452      12.015 -40.647 -12.676  1.00 78.36           O  
ANISOU 2157  O   PRO A 452     8640  12552   8582    750   -492   -841       O  
ATOM   2158  CB  PRO A 452      14.714 -39.853 -14.539  1.00 74.27           C  
ANISOU 2158  CB  PRO A 452     8456  11547   8216    645   -704   -846       C  
ATOM   2159  CG  PRO A 452      15.368 -38.792 -15.274  1.00 71.25           C  
ANISOU 2159  CG  PRO A 452     8214  10937   7921    631   -771   -972       C  
ATOM   2160  CD  PRO A 452      15.020 -37.518 -14.564  1.00 78.37           C  
ANISOU 2160  CD  PRO A 452     9104  11896   8777    692   -798  -1221       C  
ATOM   2161  N   SER A 453      13.716 -39.509 -11.709  1.00 89.10           N  
ANISOU 2161  N   SER A 453    10105  14036   9714    736   -574  -1028       N  
ATOM   2162  CA  SER A 453      13.555 -40.104 -10.398  1.00 88.79           C  
ANISOU 2162  CA  SER A 453     9974  14326   9437    737   -477   -952       C  
ATOM   2163  C   SER A 453      12.297 -39.613  -9.694  1.00 84.10           C  
ANISOU 2163  C   SER A 453     9292  13892   8768    820   -355  -1118       C  
ATOM   2164  O   SER A 453      11.913 -40.147  -8.667  1.00 87.57           O  
ANISOU 2164  O   SER A 453     9659  14606   9007    823   -225  -1041       O  
ATOM   2165  CB  SER A 453      14.792 -39.802  -9.559  1.00 99.15           C  
ANISOU 2165  CB  SER A 453    11325  15801  10546    705   -561  -1006       C  
ATOM   2166  OG  SER A 453      15.972 -39.961 -10.337  1.00102.05           O  
ANISOU 2166  OG  SER A 453    11744  15979  11050    640   -669   -917       O  
ATOM   2167  N   SER A 454      11.635 -38.620 -10.274  1.00 73.95           N  
ANISOU 2167  N   SER A 454     8014  12429   7654    897   -384  -1331       N  
ATOM   2168  CA  SER A 454      10.546 -37.916  -9.598  1.00 75.46           C  
ANISOU 2168  CA  SER A 454     8114  12751   7807   1006   -270  -1551       C  
ATOM   2169  C   SER A 454       9.147 -38.198 -10.148  1.00 78.74           C  
ANISOU 2169  C   SER A 454     8377  13095   8447   1065   -196  -1515       C  
ATOM   2170  O   SER A 454       8.157 -37.653  -9.646  1.00 79.51           O  
ANISOU 2170  O   SER A 454     8354  13294   8562   1171    -81  -1695       O  
ATOM   2171  CB  SER A 454      10.793 -36.408  -9.656  1.00 72.57           C  
ANISOU 2171  CB  SER A 454     7848  12240   7486   1081   -359  -1867       C  
ATOM   2172  OG  SER A 454      10.761 -35.945 -10.991  1.00 69.78           O  
ANISOU 2172  OG  SER A 454     7572  11535   7408   1103   -490  -1871       O  
ATOM   2173  N   ILE A 455       9.058 -39.029 -11.181  1.00 77.91           N  
ANISOU 2173  N   ILE A 455     8265  12814   8524   1000   -267  -1305       N  
ATOM   2174  CA  ILE A 455       7.761 -39.353 -11.765  1.00 80.63           C  
ANISOU 2174  CA  ILE A 455     8447  13087   9102   1036   -243  -1275       C  
ATOM   2175  C   ILE A 455       7.402 -40.786 -11.414  1.00 78.67           C  
ANISOU 2175  C   ILE A 455     8070  12992   8830    925   -104  -1024       C  
ATOM   2176  O   ILE A 455       8.292 -41.568 -11.067  1.00 69.57           O  
ANISOU 2176  O   ILE A 455     7003  11912   7517    830    -79   -834       O  
ATOM   2177  CB  ILE A 455       7.738 -39.156 -13.314  1.00 71.99           C  
ANISOU 2177  CB  ILE A 455     7452  11653   8247   1049   -454  -1258       C  
ATOM   2178  CG1 ILE A 455       8.796 -40.015 -14.004  1.00 72.93           C  
ANISOU 2178  CG1 ILE A 455     7729  11643   8338    920   -530  -1046       C  
ATOM   2179  CG2 ILE A 455       7.930 -37.701 -13.672  1.00 72.70           C  
ANISOU 2179  CG2 ILE A 455     7669  11562   8391   1167   -572  -1484       C  
ATOM   2180  CD1 ILE A 455       8.380 -40.486 -15.392  1.00 70.46           C  
ANISOU 2180  CD1 ILE A 455     7457  11087   8229    894   -667   -957       C  
ATOM   2181  N   PRO A 456       6.095 -41.117 -11.465  1.00 69.77           N  
ANISOU 2181  N   PRO A 456     6721  11906   7882    938    -12  -1019       N  
ATOM   2182  CA  PRO A 456       5.586 -42.472 -11.252  1.00 83.37           C  
ANISOU 2182  CA  PRO A 456     8300  13722   9656    811    129   -783       C  
ATOM   2183  C   PRO A 456       6.428 -43.555 -11.924  1.00 90.35           C  
ANISOU 2183  C   PRO A 456     9328  14440  10561    680     30   -539       C  
ATOM   2184  O   PRO A 456       6.733 -43.482 -13.119  1.00 91.55           O  
ANISOU 2184  O   PRO A 456     9596  14333  10855    676   -168   -555       O  
ATOM   2185  CB  PRO A 456       4.195 -42.397 -11.856  1.00 71.83           C  
ANISOU 2185  CB  PRO A 456     6601  12181   8511    848    108   -871       C  
ATOM   2186  CG  PRO A 456       3.756 -41.008 -11.525  1.00 73.23           C  
ANISOU 2186  CG  PRO A 456     6721  12413   8689   1031    119  -1158       C  
ATOM   2187  CD  PRO A 456       4.989 -40.150 -11.592  1.00 71.46           C  
ANISOU 2187  CD  PRO A 456     6779  12096   8277   1084    -15  -1257       C  
ATOM   2188  N   HIS A 457       6.810 -44.553 -11.131  1.00 86.52           N  
ANISOU 2188  N   HIS A 457     8849  14103   9920    585    179   -312       N  
ATOM   2189  CA  HIS A 457       7.733 -45.588 -11.575  1.00 78.34           C  
ANISOU 2189  CA  HIS A 457     7953  12922   8891    487    113    -79       C  
ATOM   2190  C   HIS A 457       7.119 -46.388 -12.699  1.00 77.48           C  
ANISOU 2190  C   HIS A 457     7788  12569   9081    397     42     -8       C  
ATOM   2191  O   HIS A 457       7.832 -46.945 -13.531  1.00 84.37           O  
ANISOU 2191  O   HIS A 457     8808  13227  10022    348    -72     84       O  
ATOM   2192  CB  HIS A 457       8.108 -46.520 -10.424  1.00 83.04           C  
ANISOU 2192  CB  HIS A 457     8551  13722   9277    422    290    174       C  
ATOM   2193  CG  HIS A 457       8.645 -45.814  -9.217  1.00 90.10           C  
ANISOU 2193  CG  HIS A 457     9505  14898   9831    502    349    101       C  
ATOM   2194  ND1 HIS A 457       9.020 -46.482  -8.070  1.00 86.45           N  
ANISOU 2194  ND1 HIS A 457     9078  14665   9104    472    482    319       N  
ATOM   2195  CD2 HIS A 457       8.879 -44.500  -8.979  1.00 90.55           C  
ANISOU 2195  CD2 HIS A 457     9610  15036   9760    607    278   -173       C  
ATOM   2196  CE1 HIS A 457       9.459 -45.612  -7.180  1.00 85.72           C  
ANISOU 2196  CE1 HIS A 457     9052  14806   8711    554    476    168       C  
ATOM   2197  NE2 HIS A 457       9.384 -44.403  -7.705  1.00 87.70           N  
ANISOU 2197  NE2 HIS A 457     9307  14961   9053    631    360   -143       N  
ATOM   2198  N   GLU A 458       5.790 -46.435 -12.729  1.00 72.84           N  
ANISOU 2198  N   GLU A 458     6977  12017   8681    377    108    -70       N  
ATOM   2199  CA  GLU A 458       5.091 -47.221 -13.733  1.00 76.25           C  
ANISOU 2199  CA  GLU A 458     7325  12239   9409    273     20    -26       C  
ATOM   2200  C   GLU A 458       5.250 -46.633 -15.128  1.00 78.94           C  
ANISOU 2200  C   GLU A 458     7802  12329   9861    334   -259   -185       C  
ATOM   2201  O   GLU A 458       5.307 -47.362 -16.108  1.00 83.08           O  
ANISOU 2201  O   GLU A 458     8406  12636  10525    247   -380   -129       O  
ATOM   2202  CB  GLU A 458       3.612 -47.344 -13.389  1.00 88.01           C  
ANISOU 2202  CB  GLU A 458     8494  13846  11101    233    150    -71       C  
ATOM   2203  CG  GLU A 458       2.910 -48.387 -14.244  1.00113.30           C  
ANISOU 2203  CG  GLU A 458    11581  16850  14617     77     74      2       C  
ATOM   2204  CD  GLU A 458       1.410 -48.448 -14.010  1.00134.56           C  
ANISOU 2204  CD  GLU A 458    13904  19649  17574     27    178    -67       C  
ATOM   2205  OE1 GLU A 458       0.931 -47.800 -13.051  1.00140.84           O  
ANISOU 2205  OE1 GLU A 458    14534  20692  18288    114    373   -140       O  
ATOM   2206  OE2 GLU A 458       0.714 -49.141 -14.791  1.00139.07           O  
ANISOU 2206  OE2 GLU A 458    14342  20056  18442   -100     67    -66       O  
ATOM   2207  N   VAL A 459       5.320 -45.311 -15.218  1.00 79.88           N  
ANISOU 2207  N   VAL A 459     7970  12471   9909    483   -354   -383       N  
ATOM   2208  CA  VAL A 459       5.498 -44.651 -16.506  1.00 77.19           C  
ANISOU 2208  CA  VAL A 459     7795  11894   9639    553   -608   -508       C  
ATOM   2209  C   VAL A 459       6.814 -45.073 -17.152  1.00 76.58           C  
ANISOU 2209  C   VAL A 459     8002  11642   9454    497   -672   -401       C  
ATOM   2210  O   VAL A 459       7.873 -44.991 -16.525  1.00 80.31           O  
ANISOU 2210  O   VAL A 459     8578  12192   9742    502   -579   -339       O  
ATOM   2211  CB  VAL A 459       5.463 -43.127 -16.363  1.00 71.87           C  
ANISOU 2211  CB  VAL A 459     7151  11253   8905    725   -670   -714       C  
ATOM   2212  CG1 VAL A 459       5.844 -42.464 -17.671  1.00 68.64           C  
ANISOU 2212  CG1 VAL A 459     6974  10581   8524    788   -911   -789       C  
ATOM   2213  CG2 VAL A 459       4.089 -42.685 -15.915  1.00 72.24           C  
ANISOU 2213  CG2 VAL A 459     6902  11436   9111    809   -618   -847       C  
ATOM   2214  N   PRO A 460       6.741 -45.548 -18.406  1.00 69.42           N  
ANISOU 2214  N   PRO A 460     7210  10505   8662    444   -831   -391       N  
ATOM   2215  CA  PRO A 460       7.882 -46.063 -19.177  1.00 66.27           C  
ANISOU 2215  CA  PRO A 460     7072   9916   8190    390   -867   -305       C  
ATOM   2216  C   PRO A 460       8.954 -45.008 -19.379  1.00 62.64           C  
ANISOU 2216  C   PRO A 460     6821   9407   7573    479   -902   -371       C  
ATOM   2217  O   PRO A 460       8.629 -43.832 -19.370  1.00 67.31           O  
ANISOU 2217  O   PRO A 460     7407  10020   8149    584   -977   -510       O  
ATOM   2218  CB  PRO A 460       7.247 -46.471 -20.510  1.00 61.51           C  
ANISOU 2218  CB  PRO A 460     6539   9103   7728    344  -1058   -358       C  
ATOM   2219  CG  PRO A 460       5.810 -46.733 -20.180  1.00 65.00           C  
ANISOU 2219  CG  PRO A 460     6682   9647   8366    309  -1078   -397       C  
ATOM   2220  CD  PRO A 460       5.470 -45.715 -19.134  1.00 68.93           C  
ANISOU 2220  CD  PRO A 460     7007  10366   8818    426   -982   -470       C  
ATOM   2221  N   GLN A 461      10.207 -45.419 -19.548  1.00 60.43           N  
ANISOU 2221  N   GLN A 461     6706   9048   7207    438   -839   -275       N  
ATOM   2222  CA  GLN A 461      11.317 -44.473 -19.657  1.00 63.63           C  
ANISOU 2222  CA  GLN A 461     7272   9413   7493    492   -841   -328       C  
ATOM   2223  C   GLN A 461      12.367 -44.911 -20.671  1.00 67.25           C  
ANISOU 2223  C   GLN A 461     7955   9663   7935    447   -834   -266       C  
ATOM   2224  O   GLN A 461      12.953 -45.976 -20.541  1.00 73.00           O  
ANISOU 2224  O   GLN A 461     8676  10376   8683    389   -737   -138       O  
ATOM   2225  CB  GLN A 461      11.986 -44.266 -18.291  1.00 60.47           C  
ANISOU 2225  CB  GLN A 461     6761   9235   6977    505   -720   -293       C  
ATOM   2226  CG  GLN A 461      11.087 -43.575 -17.265  1.00 65.61           C  
ANISOU 2226  CG  GLN A 461     7234  10102   7594    569   -695   -399       C  
ATOM   2227  CD  GLN A 461      11.834 -42.944 -16.092  1.00 69.69           C  
ANISOU 2227  CD  GLN A 461     7718  10817   7945    601   -626   -445       C  
ATOM   2228  OE1 GLN A 461      13.053 -42.736 -16.137  1.00 65.30           O  
ANISOU 2228  OE1 GLN A 461     7267  10220   7325    582   -637   -430       O  
ATOM   2229  NE2 GLN A 461      11.091 -42.634 -15.030  1.00 68.98           N  
ANISOU 2229  NE2 GLN A 461     7472  10951   7785    646   -553   -517       N  
ATOM   2230  N   ILE A 462      12.611 -44.074 -21.674  1.00 64.54           N  
ANISOU 2230  N   ILE A 462     7816   9151   7556    482   -920   -353       N  
ATOM   2231  CA  ILE A 462      13.583 -44.390 -22.720  1.00 66.88           C  
ANISOU 2231  CA  ILE A 462     8345   9250   7817    442   -879   -312       C  
ATOM   2232  C   ILE A 462      14.773 -43.439 -22.737  1.00 63.58           C  
ANISOU 2232  C   ILE A 462     8031   8793   7334    455   -807   -336       C  
ATOM   2233  O   ILE A 462      14.605 -42.230 -22.784  1.00 64.94           O  
ANISOU 2233  O   ILE A 462     8256   8939   7477    503   -875   -429       O  
ATOM   2234  CB  ILE A 462      12.944 -44.367 -24.127  1.00 70.10           C  
ANISOU 2234  CB  ILE A 462     8967   9460   8209    446  -1022   -369       C  
ATOM   2235  CG1 ILE A 462      12.034 -45.572 -24.329  1.00 70.80           C  
ANISOU 2235  CG1 ILE A 462     8975   9536   8389    389  -1084   -349       C  
ATOM   2236  CG2 ILE A 462      14.015 -44.382 -25.199  1.00 77.44           C  
ANISOU 2236  CG2 ILE A 462    10177  10197   9048    419   -943   -348       C  
ATOM   2237  CD1 ILE A 462      10.621 -45.307 -23.956  1.00 76.58           C  
ANISOU 2237  CD1 ILE A 462     9507  10378   9214    422  -1229   -413       C  
ATOM   2238  N   LEU A 463      15.973 -44.008 -22.710  1.00 61.80           N  
ANISOU 2238  N   LEU A 463     7820   8545   7115    410   -667   -253       N  
ATOM   2239  CA  LEU A 463      17.200 -43.247 -22.883  1.00 61.17           C  
ANISOU 2239  CA  LEU A 463     7822   8403   7017    394   -580   -272       C  
ATOM   2240  C   LEU A 463      17.713 -43.292 -24.324  1.00 64.07           C  
ANISOU 2240  C   LEU A 463     8460   8531   7351    365   -512   -265       C  
ATOM   2241  O   LEU A 463      17.764 -44.348 -24.955  1.00 70.59           O  
ANISOU 2241  O   LEU A 463     9368   9267   8185    347   -457   -216       O  
ATOM   2242  CB  LEU A 463      18.300 -43.756 -21.945  1.00 58.14           C  
ANISOU 2242  CB  LEU A 463     7253   8159   6680    372   -470   -192       C  
ATOM   2243  CG  LEU A 463      19.611 -42.967 -22.074  1.00 57.02           C  
ANISOU 2243  CG  LEU A 463     7136   7964   6565    335   -384   -225       C  
ATOM   2244  CD1 LEU A 463      19.467 -41.595 -21.458  1.00 55.11           C  
ANISOU 2244  CD1 LEU A 463     6854   7794   6292    338   -468   -351       C  
ATOM   2245  CD2 LEU A 463      20.804 -43.697 -21.486  1.00 56.24           C  
ANISOU 2245  CD2 LEU A 463     6862   7959   6548    323   -286   -130       C  
ATOM   2246  N   ILE A 464      18.080 -42.118 -24.829  1.00 58.47           N  
ANISOU 2246  N   ILE A 464     7906   7710   6600    359   -503   -318       N  
ATOM   2247  CA  ILE A 464      18.813 -41.958 -26.076  1.00 58.25           C  
ANISOU 2247  CA  ILE A 464     8142   7474   6517    320   -380   -297       C  
ATOM   2248  C   ILE A 464      20.047 -41.116 -25.788  1.00 65.23           C  
ANISOU 2248  C   ILE A 464     8974   8342   7467    263   -240   -303       C  
ATOM   2249  O   ILE A 464      19.912 -39.943 -25.430  1.00 69.99           O  
ANISOU 2249  O   ILE A 464     9571   8941   8082    264   -311   -367       O  
ATOM   2250  CB  ILE A 464      17.969 -41.266 -27.144  1.00 61.77           C  
ANISOU 2250  CB  ILE A 464     8875   7758   6837    356   -510   -329       C  
ATOM   2251  CG1 ILE A 464      16.620 -41.958 -27.275  1.00 56.88           C  
ANISOU 2251  CG1 ILE A 464     8239   7183   6191    407   -705   -351       C  
ATOM   2252  CG2 ILE A 464      18.712 -41.211 -28.464  1.00 65.99           C  
ANISOU 2252  CG2 ILE A 464     9724   8089   7259    312   -357   -288       C  
ATOM   2253  CD1 ILE A 464      15.830 -41.470 -28.435  1.00 62.89           C  
ANISOU 2253  CD1 ILE A 464     9285   7792   6817    453   -870   -373       C  
ATOM   2254  N   ASN A 465      21.243 -41.682 -25.934  1.00 56.77           N  
ANISOU 2254  N   ASN A 465     7851   7251   6467    213    -42   -252       N  
ATOM   2255  CA  ASN A 465      22.429 -40.974 -25.450  1.00 70.13           C  
ANISOU 2255  CA  ASN A 465     9398   8970   8277    145     70   -268       C  
ATOM   2256  C   ASN A 465      23.772 -41.585 -25.877  1.00 68.70           C  
ANISOU 2256  C   ASN A 465     9167   8734   8203     97    314   -211       C  
ATOM   2257  O   ASN A 465      23.874 -42.798 -26.056  1.00 63.93           O  
ANISOU 2257  O   ASN A 465     8533   8139   7617    141    382   -156       O  
ATOM   2258  CB  ASN A 465      22.348 -40.897 -23.919  1.00 66.99           C  
ANISOU 2258  CB  ASN A 465     8694   8815   7945    165    -65   -306       C  
ATOM   2259  CG  ASN A 465      23.182 -39.796 -23.345  1.00 76.96           C  
ANISOU 2259  CG  ASN A 465     9836  10104   9301     89    -51   -385       C  
ATOM   2260  OD1 ASN A 465      22.975 -38.626 -23.646  1.00 87.70           O  
ANISOU 2260  OD1 ASN A 465    11341  11334  10647     55    -77   -458       O  
ATOM   2261  ND2 ASN A 465      24.125 -40.159 -22.490  1.00 80.71           N  
ANISOU 2261  ND2 ASN A 465    10042  10739   9885     63    -28   -372       N  
ATOM   2262  N   ARG A 466      24.792 -40.737 -26.026  1.00 71.41           N  
ANISOU 2262  N   ARG A 466     9484   9004   8643      5    456   -231       N  
ATOM   2263  CA  ARG A 466      26.155 -41.178 -26.344  1.00 74.67           C  
ANISOU 2263  CA  ARG A 466     9782   9380   9210    -44    709   -191       C  
ATOM   2264  C   ARG A 466      26.667 -42.287 -25.408  1.00 77.04           C  
ANISOU 2264  C   ARG A 466     9749   9867   9654     20    682   -148       C  
ATOM   2265  O   ARG A 466      27.480 -43.133 -25.808  1.00 70.84           O  
ANISOU 2265  O   ARG A 466     8895   9038   8983     44    876    -98       O  
ATOM   2266  CB  ARG A 466      27.128 -39.993 -26.288  1.00 87.26           C  
ANISOU 2266  CB  ARG A 466    11294  10914  10947   -176    821   -234       C  
ATOM   2267  CG  ARG A 466      26.994 -39.000 -27.419  1.00105.25           C  
ANISOU 2267  CG  ARG A 466    13920  12949  13120   -253    945   -225       C  
ATOM   2268  CD  ARG A 466      28.271 -38.952 -28.266  1.00113.54           C  
ANISOU 2268  CD  ARG A 466    14989  13862  14287   -358   1299   -182       C  
ATOM   2269  NE  ARG A 466      27.994 -38.620 -29.664  1.00115.68           N  
ANISOU 2269  NE  ARG A 466    15694  13907  14351   -382   1468   -120       N  
ATOM   2270  CZ  ARG A 466      28.867 -38.772 -30.656  1.00118.82           C  
ANISOU 2270  CZ  ARG A 466    16214  14176  14757   -449   1819    -68       C  
ATOM   2271  NH1 ARG A 466      30.080 -39.252 -30.408  1.00119.95           N  
ANISOU 2271  NH1 ARG A 466    16035  14386  15153   -492   2041    -79       N  
ATOM   2272  NH2 ARG A 466      28.525 -38.451 -31.899  1.00118.07           N  
ANISOU 2272  NH2 ARG A 466    16560  13891  14410   -463   1950     -3       N  
ATOM   2273  N   GLU A 467      26.190 -42.269 -24.162  1.00 76.69           N  
ANISOU 2273  N   GLU A 467     9510  10026   9601     59    451   -163       N  
ATOM   2274  CA  GLU A 467      26.670 -43.181 -23.123  1.00 74.42           C  
ANISOU 2274  CA  GLU A 467     8917   9935   9424    124    387    -95       C  
ATOM   2275  C   GLU A 467      25.537 -43.697 -22.224  1.00 71.18           C  
ANISOU 2275  C   GLU A 467     8472   9689   8884    204    175    -59       C  
ATOM   2276  O   GLU A 467      24.468 -43.095 -22.166  1.00 68.73           O  
ANISOU 2276  O   GLU A 467     8297   9385   8434    199     55   -124       O  
ATOM   2277  CB  GLU A 467      27.736 -42.478 -22.285  1.00 78.82           C  
ANISOU 2277  CB  GLU A 467     9190  10624  10133     55    346   -147       C  
ATOM   2278  CG  GLU A 467      27.319 -41.106 -21.816  1.00 84.84           C  
ANISOU 2278  CG  GLU A 467     9994  11422  10820    -26    202   -279       C  
ATOM   2279  CD  GLU A 467      28.395 -40.410 -21.009  1.00 90.44           C  
ANISOU 2279  CD  GLU A 467    10425  12249  11690   -117    144   -364       C  
ATOM   2280  OE1 GLU A 467      29.582 -40.798 -21.117  1.00 91.34           O  
ANISOU 2280  OE1 GLU A 467    10328  12369  12008   -142    261   -320       O  
ATOM   2281  OE2 GLU A 467      28.046 -39.472 -20.264  1.00 91.68           O  
ANISOU 2281  OE2 GLU A 467    10563  12490  11781   -163    -24   -491       O  
ATOM   2282  N   PRO A 468      25.758 -44.834 -21.533  1.00 70.77           N  
ANISOU 2282  N   PRO A 468     8236   9760   8893    284    144     57       N  
ATOM   2283  CA  PRO A 468      24.723 -45.326 -20.612  1.00 67.40           C  
ANISOU 2283  CA  PRO A 468     7770   9495   8344    342    -22    116       C  
ATOM   2284  C   PRO A 468      24.754 -44.609 -19.260  1.00 68.07           C  
ANISOU 2284  C   PRO A 468     7672   9838   8354    332   -197     68       C  
ATOM   2285  O   PRO A 468      25.790 -44.079 -18.853  1.00 62.02           O  
ANISOU 2285  O   PRO A 468     6740   9152   7673    295   -219     22       O  
ATOM   2286  CB  PRO A 468      25.068 -46.812 -20.454  1.00 65.01           C  
ANISOU 2286  CB  PRO A 468     7368   9186   8148    429     35    283       C  
ATOM   2287  CG  PRO A 468      26.541 -46.873 -20.658  1.00 69.45           C  
ANISOU 2287  CG  PRO A 468     7773   9709   8905    438    154    299       C  
ATOM   2288  CD  PRO A 468      26.873 -45.791 -21.671  1.00 72.41           C  
ANISOU 2288  CD  PRO A 468     8289   9931   9291    337    281    156       C  
ATOM   2289  N   LEU A 469      23.618 -44.600 -18.572  1.00 68.06           N  
ANISOU 2289  N   LEU A 469     7694   9969   8195    359   -314     65       N  
ATOM   2290  CA  LEU A 469      23.491 -43.875 -17.308  1.00 64.69           C  
ANISOU 2290  CA  LEU A 469     7144   9793   7644    354   -464    -14       C  
ATOM   2291  C   LEU A 469      23.156 -44.792 -16.121  1.00 66.61           C  
ANISOU 2291  C   LEU A 469     7262  10272   7774    425   -541    137       C  
ATOM   2292  O   LEU A 469      22.033 -44.762 -15.612  1.00 63.17           O  
ANISOU 2292  O   LEU A 469     6867   9944   7192    442   -579    125       O  
ATOM   2293  CB  LEU A 469      22.420 -42.788 -17.444  1.00 65.25           C  
ANISOU 2293  CB  LEU A 469     7355   9828   7607    328   -511   -183       C  
ATOM   2294  CG  LEU A 469      22.611 -41.760 -18.566  1.00 64.24           C  
ANISOU 2294  CG  LEU A 469     7395   9455   7560    264   -449   -309       C  
ATOM   2295  CD1 LEU A 469      21.597 -40.644 -18.432  1.00 57.00           C  
ANISOU 2295  CD1 LEU A 469     6580   8526   6551    271   -534   -468       C  
ATOM   2296  CD2 LEU A 469      24.025 -41.199 -18.556  1.00 58.35           C  
ANISOU 2296  CD2 LEU A 469     6541   8685   6943    185   -413   -361       C  
ATOM   2297  N   PRO A 470      24.145 -45.587 -15.664  1.00 60.08           N  
ANISOU 2297  N   PRO A 470     6277   9528   7022    472   -559    288       N  
ATOM   2298  CA  PRO A 470      23.984 -46.661 -14.678  1.00 61.13           C  
ANISOU 2298  CA  PRO A 470     6321   9837   7069    553   -614    500       C  
ATOM   2299  C   PRO A 470      23.117 -46.305 -13.478  1.00 79.52           C  
ANISOU 2299  C   PRO A 470     8647  12435   9134    557   -714    473       C  
ATOM   2300  O   PRO A 470      22.380 -47.165 -12.996  1.00 79.21           O  
ANISOU 2300  O   PRO A 470     8628  12466   9003    596   -685    643       O  
ATOM   2301  CB  PRO A 470      25.420 -46.925 -14.222  1.00 62.98           C  
ANISOU 2301  CB  PRO A 470     6353  10166   7410    600   -692    585       C  
ATOM   2302  CG  PRO A 470      26.267 -46.511 -15.347  1.00 62.59           C  
ANISOU 2302  CG  PRO A 470     6294   9897   7589    550   -584    474       C  
ATOM   2303  CD  PRO A 470      25.564 -45.378 -16.006  1.00 61.04           C  
ANISOU 2303  CD  PRO A 470     6274   9588   7331    451   -535    262       C  
ATOM   2304  N   HIS A 471      23.202 -45.060 -13.008  1.00 72.88           N  
ANISOU 2304  N   HIS A 471     7785  11728   8177    512   -810    258       N  
ATOM   2305  CA  HIS A 471      22.525 -44.659 -11.780  1.00 66.21           C  
ANISOU 2305  CA  HIS A 471     6934  11164   7059    526   -894    198       C  
ATOM   2306  C   HIS A 471      21.006 -44.667 -11.937  1.00 64.07           C  
ANISOU 2306  C   HIS A 471     6777  10856   6712    527   -789    171       C  
ATOM   2307  O   HIS A 471      20.273 -44.696 -10.948  1.00 68.26           O  
ANISOU 2307  O   HIS A 471     7299  11613   7025    552   -791    185       O  
ATOM   2308  CB  HIS A 471      23.034 -43.286 -11.301  1.00 65.96           C  
ANISOU 2308  CB  HIS A 471     6863  11249   6951    472  -1020    -71       C  
ATOM   2309  CG  HIS A 471      22.621 -42.124 -12.150  1.00 69.44           C  
ANISOU 2309  CG  HIS A 471     7415  11476   7493    408   -965   -312       C  
ATOM   2310  ND1 HIS A 471      23.317 -41.737 -13.277  1.00 78.48           N  
ANISOU 2310  ND1 HIS A 471     8585  12358   8875    346   -912   -367       N  
ATOM   2311  CD2 HIS A 471      21.615 -41.227 -12.009  1.00 69.95           C  
ANISOU 2311  CD2 HIS A 471     7576  11547   7456    407   -952   -506       C  
ATOM   2312  CE1 HIS A 471      22.737 -40.680 -13.812  1.00 74.84           C  
ANISOU 2312  CE1 HIS A 471     8255  11740   8441    307   -881   -558       C  
ATOM   2313  NE2 HIS A 471      21.700 -40.350 -13.063  1.00 73.57           N  
ANISOU 2313  NE2 HIS A 471     8128  11732   8094    352   -914   -651       N  
ATOM   2314  N   LEU A 472      20.533 -44.703 -13.176  1.00 60.36           N  
ANISOU 2314  N   LEU A 472     6405  10110   6417    501   -695    141       N  
ATOM   2315  CA  LEU A 472      19.103 -44.778 -13.422  1.00 63.05           C  
ANISOU 2315  CA  LEU A 472     6816  10404   6735    503   -624    119       C  
ATOM   2316  C   LEU A 472      18.703 -46.072 -14.101  1.00 67.81           C  
ANISOU 2316  C   LEU A 472     7453  10836   7474    499   -533    317       C  
ATOM   2317  O   LEU A 472      19.499 -46.712 -14.788  1.00 71.27           O  
ANISOU 2317  O   LEU A 472     7915  11104   8062    499   -504    417       O  
ATOM   2318  CB  LEU A 472      18.642 -43.594 -14.265  1.00 63.02           C  
ANISOU 2318  CB  LEU A 472     6914  10230   6800    481   -636   -115       C  
ATOM   2319  CG  LEU A 472      18.804 -42.265 -13.538  1.00 65.67           C  
ANISOU 2319  CG  LEU A 472     7229  10704   7018    482   -714   -343       C  
ATOM   2320  CD1 LEU A 472      18.701 -41.109 -14.498  1.00 58.74           C  
ANISOU 2320  CD1 LEU A 472     6470   9588   6258    461   -730   -536       C  
ATOM   2321  CD2 LEU A 472      17.768 -42.156 -12.425  1.00 68.71           C  
ANISOU 2321  CD2 LEU A 472     7560  11340   7208    528   -696   -392       C  
ATOM   2322  N   HIS A 473      17.446 -46.438 -13.903  1.00 68.51           N  
ANISOU 2322  N   HIS A 473     7536  10966   7529    492   -479    355       N  
ATOM   2323  CA  HIS A 473      16.877 -47.621 -14.515  1.00 67.90           C  
ANISOU 2323  CA  HIS A 473     7487  10716   7596    463   -402    510       C  
ATOM   2324  C   HIS A 473      16.002 -47.257 -15.686  1.00 66.66           C  
ANISOU 2324  C   HIS A 473     7418  10353   7558    431   -415    359       C  
ATOM   2325  O   HIS A 473      14.844 -46.879 -15.510  1.00 68.27           O  
ANISOU 2325  O   HIS A 473     7576  10627   7738    426   -418    271       O  
ATOM   2326  CB  HIS A 473      16.071 -48.418 -13.496  1.00 74.22           C  
ANISOU 2326  CB  HIS A 473     8199  11692   8311    452   -325    684       C  
ATOM   2327  CG  HIS A 473      16.919 -49.216 -12.563  1.00 83.58           C  
ANISOU 2327  CG  HIS A 473     9340  13012   9407    490   -317    924       C  
ATOM   2328  ND1 HIS A 473      16.967 -50.593 -12.595  1.00 89.26           N  
ANISOU 2328  ND1 HIS A 473    10063  13608  10244    480   -244   1183       N  
ATOM   2329  CD2 HIS A 473      17.766 -48.832 -11.582  1.00 86.52           C  
ANISOU 2329  CD2 HIS A 473     9668  13619   9588    544   -394    946       C  
ATOM   2330  CE1 HIS A 473      17.800 -51.022 -11.666  1.00 91.02           C  
ANISOU 2330  CE1 HIS A 473    10248  13984  10351    544   -277   1379       C  
ATOM   2331  NE2 HIS A 473      18.300 -49.973 -11.036  1.00 88.38           N  
ANISOU 2331  NE2 HIS A 473     9879  13884   9816    582   -381   1236       N  
ATOM   2332  N   PHE A 474      16.564 -47.376 -16.885  1.00 69.03           N  
ANISOU 2332  N   PHE A 474     7843  10405   7981    417   -422    330       N  
ATOM   2333  CA  PHE A 474      15.791 -47.165 -18.100  1.00 68.71           C  
ANISOU 2333  CA  PHE A 474     7924  10158   8024    391   -461    212       C  
ATOM   2334  C   PHE A 474      15.305 -48.482 -18.677  1.00 69.58           C  
ANISOU 2334  C   PHE A 474     8067  10104   8265    341   -421    321       C  
ATOM   2335  O   PHE A 474      16.042 -49.468 -18.710  1.00 75.86           O  
ANISOU 2335  O   PHE A 474     8877  10814   9132    337   -347    463       O  
ATOM   2336  CB  PHE A 474      16.615 -46.411 -19.134  1.00 64.18           C  
ANISOU 2336  CB  PHE A 474     7512   9410   7465    398   -482    100       C  
ATOM   2337  CG  PHE A 474      16.848 -44.983 -18.774  1.00 66.45           C  
ANISOU 2337  CG  PHE A 474     7791   9790   7666    424   -536    -47       C  
ATOM   2338  CD1 PHE A 474      15.855 -44.034 -18.987  1.00 63.34           C  
ANISOU 2338  CD1 PHE A 474     7437   9382   7248    450   -619   -194       C  
ATOM   2339  CD2 PHE A 474      18.048 -44.586 -18.203  1.00 65.24           C  
ANISOU 2339  CD2 PHE A 474     7578   9728   7481    424   -516    -47       C  
ATOM   2340  CE1 PHE A 474      16.060 -42.719 -18.649  1.00 57.59           C  
ANISOU 2340  CE1 PHE A 474     6715   8700   6466    478   -662   -339       C  
ATOM   2341  CE2 PHE A 474      18.263 -43.272 -17.866  1.00 57.73           C  
ANISOU 2341  CE2 PHE A 474     6625   8837   6474    428   -571   -205       C  
ATOM   2342  CZ  PHE A 474      17.265 -42.335 -18.089  1.00 57.13           C  
ANISOU 2342  CZ  PHE A 474     6615   8719   6374    456   -634   -352       C  
ATOM   2343  N   ASP A 475      14.052 -48.482 -19.114  1.00 62.09           N  
ANISOU 2343  N   ASP A 475     7117   9105   7370    306   -481    244       N  
ATOM   2344  CA  ASP A 475      13.435 -49.633 -19.754  1.00 65.97           C  
ANISOU 2344  CA  ASP A 475     7640   9422   8006    232   -476    297       C  
ATOM   2345  C   ASP A 475      14.092 -50.006 -21.089  1.00 73.39           C  
ANISOU 2345  C   ASP A 475     8802  10093   8992    221   -483    249       C  
ATOM   2346  O   ASP A 475      14.359 -51.183 -21.349  1.00 75.28           O  
ANISOU 2346  O   ASP A 475     9084  10181   9340    182   -410    341       O  
ATOM   2347  CB  ASP A 475      11.953 -49.360 -19.969  1.00 64.91           C  
ANISOU 2347  CB  ASP A 475     7423   9310   7930    197   -576    186       C  
ATOM   2348  CG  ASP A 475      11.233 -49.049 -18.683  1.00 69.13           C  
ANISOU 2348  CG  ASP A 475     7731  10107   8427    210   -521    219       C  
ATOM   2349  OD1 ASP A 475      11.831 -49.259 -17.600  1.00 61.97           O  
ANISOU 2349  OD1 ASP A 475     6756   9362   7428    228   -408    354       O  
ATOM   2350  OD2 ASP A 475      10.065 -48.608 -18.760  1.00 70.20           O  
ANISOU 2350  OD2 ASP A 475     7757  10294   8623    208   -592    108       O  
ATOM   2351  N   VAL A 476      14.342 -49.000 -21.930  1.00 71.18           N  
ANISOU 2351  N   VAL A 476     8678   9743   8625    257   -553    107       N  
ATOM   2352  CA  VAL A 476      15.035 -49.188 -23.203  1.00 60.96           C  
ANISOU 2352  CA  VAL A 476     7624   8219   7319    252   -526     54       C  
ATOM   2353  C   VAL A 476      16.222 -48.250 -23.291  1.00 63.25           C  
ANISOU 2353  C   VAL A 476     7987   8524   7523    302   -459     30       C  
ATOM   2354  O   VAL A 476      16.079 -47.060 -23.043  1.00 69.14           O  
ANISOU 2354  O   VAL A 476     8713   9366   8191    331   -526    -43       O  
ATOM   2355  CB  VAL A 476      14.124 -48.913 -24.394  1.00 58.22           C  
ANISOU 2355  CB  VAL A 476     7452   7734   6933    229   -680    -88       C  
ATOM   2356  CG1 VAL A 476      14.813 -49.306 -25.691  1.00 58.69           C  
ANISOU 2356  CG1 VAL A 476     7793   7563   6943    216   -623   -138       C  
ATOM   2357  CG2 VAL A 476      12.794 -49.628 -24.232  1.00 62.70           C  
ANISOU 2357  CG2 VAL A 476     7887   8317   7620    164   -783    -95       C  
ATOM   2358  N   GLU A 477      17.392 -48.766 -23.645  1.00 62.22           N  
ANISOU 2358  N   GLU A 477     7926   8284   7431    309   -317     81       N  
ATOM   2359  CA  GLU A 477      18.561 -47.906 -23.794  1.00 68.24           C  
ANISOU 2359  CA  GLU A 477     8729   9046   8151    333   -232     55       C  
ATOM   2360  C   GLU A 477      19.032 -47.869 -25.245  1.00 73.03           C  
ANISOU 2360  C   GLU A 477     9610   9426   8712    319   -142    -19       C  
ATOM   2361  O   GLU A 477      19.520 -48.858 -25.776  1.00 76.88           O  
ANISOU 2361  O   GLU A 477    10172   9775   9264    321    -17      6       O  
ATOM   2362  CB  GLU A 477      19.701 -48.368 -22.879  1.00 68.40           C  
ANISOU 2362  CB  GLU A 477     8552   9170   8268    366   -125    177       C  
ATOM   2363  CG  GLU A 477      19.293 -48.555 -21.422  1.00 75.55           C  
ANISOU 2363  CG  GLU A 477     9225  10311   9169    384   -200    276       C  
ATOM   2364  CD  GLU A 477      20.427 -49.075 -20.541  1.00 79.44           C  
ANISOU 2364  CD  GLU A 477     9539  10909   9736    433   -138    419       C  
ATOM   2365  OE1 GLU A 477      20.157 -49.958 -19.684  1.00 76.06           O  
ANISOU 2365  OE1 GLU A 477     8992  10571   9336    456   -149    571       O  
ATOM   2366  OE2 GLU A 477      21.577 -48.594 -20.705  1.00 75.65           O  
ANISOU 2366  OE2 GLU A 477     9030  10420   9295    448    -81    387       O  
ATOM   2367  N   LEU A 478      18.874 -46.720 -25.889  1.00 68.06           N  
ANISOU 2367  N   LEU A 478     9148   8749   7962    311   -195   -107       N  
ATOM   2368  CA  LEU A 478      19.363 -46.546 -27.249  1.00 63.40           C  
ANISOU 2368  CA  LEU A 478     8851   7962   7276    294    -88   -159       C  
ATOM   2369  C   LEU A 478      20.620 -45.690 -27.201  1.00 65.59           C  
ANISOU 2369  C   LEU A 478     9105   8239   7575    280     75   -144       C  
ATOM   2370  O   LEU A 478      20.545 -44.480 -27.028  1.00 69.03           O  
ANISOU 2370  O   LEU A 478     9553   8710   7966    268      9   -175       O  
ATOM   2371  CB  LEU A 478      18.292 -45.909 -28.135  1.00 60.31           C  
ANISOU 2371  CB  LEU A 478     8705   7489   6722    294   -267   -240       C  
ATOM   2372  CG  LEU A 478      16.922 -46.581 -28.007  1.00 60.56           C  
ANISOU 2372  CG  LEU A 478     8676   7557   6777    295   -473   -271       C  
ATOM   2373  CD1 LEU A 478      15.882 -45.991 -28.960  1.00 58.22           C  
ANISOU 2373  CD1 LEU A 478     8606   7181   6333    311   -690   -353       C  
ATOM   2374  CD2 LEU A 478      17.064 -48.068 -28.225  1.00 60.07           C  
ANISOU 2374  CD2 LEU A 478     8619   7406   6797    263   -384   -258       C  
ATOM   2375  N   LEU A 479      21.780 -46.322 -27.331  1.00 61.07           N  
ANISOU 2375  N   LEU A 479     8480   7618   7106    280    290   -104       N  
ATOM   2376  CA  LEU A 479      23.042 -45.611 -27.176  1.00 61.17           C  
ANISOU 2376  CA  LEU A 479     8394   7648   7201    252    453    -90       C  
ATOM   2377  C   LEU A 479      23.775 -45.381 -28.498  1.00 66.08           C  
ANISOU 2377  C   LEU A 479     9275   8078   7756    215    690   -120       C  
ATOM   2378  O   LEU A 479      23.890 -46.272 -29.329  1.00 71.46           O  
ANISOU 2378  O   LEU A 479    10119   8632   8399    237    823   -138       O  
ATOM   2379  CB  LEU A 479      23.954 -46.362 -26.218  1.00 65.49           C  
ANISOU 2379  CB  LEU A 479     8621   8311   7953    289    527    -12       C  
ATOM   2380  CG  LEU A 479      23.302 -47.001 -24.994  1.00 70.37           C  
ANISOU 2380  CG  LEU A 479     9022   9103   8614    336    347     59       C  
ATOM   2381  CD1 LEU A 479      24.384 -47.698 -24.181  1.00 74.86           C  
ANISOU 2381  CD1 LEU A 479     9311   9764   9370    389    422    162       C  
ATOM   2382  CD2 LEU A 479      22.531 -45.986 -24.155  1.00 66.41           C  
ANISOU 2382  CD2 LEU A 479     8444   8768   8020    316    145     19       C  
ATOM   2383  N   GLY A 480      24.293 -44.173 -28.659  1.00 65.22           N  
ANISOU 2383  N   GLY A 480     9207   7942   7633    151    760   -130       N  
ATOM   2384  CA  GLY A 480      24.942 -43.748 -29.878  1.00 69.00           C  
ANISOU 2384  CA  GLY A 480     9950   8244   8022     97   1005   -137       C  
ATOM   2385  C   GLY A 480      24.553 -42.310 -30.174  1.00 73.18           C  
ANISOU 2385  C   GLY A 480    10674   8706   8427     41    920   -141       C  
ATOM   2386  O   GLY A 480      23.815 -41.693 -29.416  1.00 70.46           O  
ANISOU 2386  O   GLY A 480    10234   8449   8089     57    677   -160       O  
ATOM   2387  N   ASP A 481      25.061 -41.781 -31.279  1.00 74.46           N  
ANISOU 2387  N   ASP A 481    11117   8699   8475    -20   1140   -117       N  
ATOM   2388  CA  ASP A 481      24.734 -40.440 -31.745  1.00 75.03           C  
ANISOU 2388  CA  ASP A 481    11441   8650   8417    -69   1088    -87       C  
ATOM   2389  C   ASP A 481      23.222 -40.199 -31.730  1.00 70.04           C  
ANISOU 2389  C   ASP A 481    10962   8030   7618     17    734   -106       C  
ATOM   2390  O   ASP A 481      22.452 -41.016 -32.212  1.00 73.28           O  
ANISOU 2390  O   ASP A 481    11520   8444   7878     84    617   -130       O  
ATOM   2391  CB  ASP A 481      25.305 -40.243 -33.149  1.00 83.20           C  
ANISOU 2391  CB  ASP A 481    12846   9494   9270   -127   1386    -33       C  
ATOM   2392  CG  ASP A 481      25.129 -38.852 -33.653  1.00 93.19           C  
ANISOU 2392  CG  ASP A 481    14387  10603  10418   -185   1374     40       C  
ATOM   2393  OD1 ASP A 481      26.004 -38.014 -33.366  1.00104.43           O  
ANISOU 2393  OD1 ASP A 481    15680  11971  12026   -297   1547     70       O  
ATOM   2394  OD2 ASP A 481      24.121 -38.600 -34.340  1.00 97.50           O  
ANISOU 2394  OD2 ASP A 481    15276  11068  10700   -119   1180     70       O  
ATOM   2395  N   CYS A 482      22.792 -39.087 -31.155  1.00 70.29           N  
ANISOU 2395  N   CYS A 482    10938   8063   7704     17    560   -112       N  
ATOM   2396  CA  CYS A 482      21.365 -38.884 -30.939  1.00 72.59           C  
ANISOU 2396  CA  CYS A 482    11276   8396   7909    119    223   -145       C  
ATOM   2397  C   CYS A 482      20.615 -38.643 -32.245  1.00 78.19           C  
ANISOU 2397  C   CYS A 482    12418   8945   8347    170    124    -96       C  
ATOM   2398  O   CYS A 482      19.433 -38.965 -32.346  1.00 63.80           O  
ANISOU 2398  O   CYS A 482    10641   7168   6434    262   -146   -130       O  
ATOM   2399  CB  CYS A 482      21.122 -37.725 -29.966  1.00 68.37           C  
ANISOU 2399  CB  CYS A 482    10568   7891   7517    125     81   -187       C  
ATOM   2400  SG  CYS A 482      21.754 -38.010 -28.313  1.00 85.99           S  
ANISOU 2400  SG  CYS A 482    12309  10362  10002     86    100   -266       S  
ATOM   2401  N   ASP A 483      21.305 -38.077 -33.235  1.00 77.83           N  
ANISOU 2401  N   ASP A 483    12683   8717   8171    105    340    -11       N  
ATOM   2402  CA  ASP A 483      20.713 -37.833 -34.549  1.00 79.35           C  
ANISOU 2402  CA  ASP A 483    13341   8759   8051    152    258     59       C  
ATOM   2403  C   ASP A 483      20.417 -39.135 -35.260  1.00 80.05           C  
ANISOU 2403  C   ASP A 483    13573   8896   7947    184    245      7       C  
ATOM   2404  O   ASP A 483      19.327 -39.328 -35.799  1.00 84.00           O  
ANISOU 2404  O   ASP A 483    14270   9392   8256    268    -37    -13       O  
ATOM   2405  CB  ASP A 483      21.638 -36.986 -35.413  1.00 83.80           C  
ANISOU 2405  CB  ASP A 483    14215   9120   8505     57    554    183       C  
ATOM   2406  CG  ASP A 483      21.370 -35.522 -35.272  1.00 92.92           C  
ANISOU 2406  CG  ASP A 483    15466  10124   9714     65    441    263       C  
ATOM   2407  OD1 ASP A 483      20.387 -35.171 -34.590  1.00 89.65           O  
ANISOU 2407  OD1 ASP A 483    14902   9765   9397    169    118    208       O  
ATOM   2408  OD2 ASP A 483      22.129 -34.727 -35.859  1.00106.68           O  
ANISOU 2408  OD2 ASP A 483    17439  11680  11414    -33    691    382       O  
ATOM   2409  N   VAL A 484      21.417 -40.010 -35.267  1.00 76.09           N  
ANISOU 2409  N   VAL A 484    12964   8430   7518    118    548    -26       N  
ATOM   2410  CA  VAL A 484      21.298 -41.379 -35.757  1.00 77.05           C  
ANISOU 2410  CA  VAL A 484    13159   8586   7531    142    581   -110       C  
ATOM   2411  C   VAL A 484      20.049 -42.083 -35.231  1.00 78.51           C  
ANISOU 2411  C   VAL A 484    13174   8888   7767    216    220   -195       C  
ATOM   2412  O   VAL A 484      19.234 -42.578 -36.005  1.00 86.58           O  
ANISOU 2412  O   VAL A 484    14441   9879   8577    254     35   -250       O  
ATOM   2413  CB  VAL A 484      22.544 -42.204 -35.361  1.00 68.35           C  
ANISOU 2413  CB  VAL A 484    11797   7528   6645     90    927   -141       C  
ATOM   2414  CG1 VAL A 484      22.277 -43.686 -35.455  1.00 70.43           C  
ANISOU 2414  CG1 VAL A 484    12021   7830   6910    133    902   -244       C  
ATOM   2415  CG2 VAL A 484      23.741 -41.805 -36.204  1.00 70.80           C  
ANISOU 2415  CG2 VAL A 484    12321   7711   6868     11   1335    -81       C  
ATOM   2416  N   ILE A 485      19.894 -42.114 -33.912  1.00 74.21           N  
ANISOU 2416  N   ILE A 485    12212   8484   7502    227    121   -211       N  
ATOM   2417  CA  ILE A 485      18.830 -42.898 -33.294  1.00 74.54           C  
ANISOU 2417  CA  ILE A 485    12039   8646   7637    275   -146   -279       C  
ATOM   2418  C   ILE A 485      17.458 -42.268 -33.543  1.00 75.36           C  
ANISOU 2418  C   ILE A 485    12259   8746   7627    345   -507   -293       C  
ATOM   2419  O   ILE A 485      16.465 -42.966 -33.730  1.00 72.00           O  
ANISOU 2419  O   ILE A 485    11833   8356   7167    373   -735   -361       O  
ATOM   2420  CB  ILE A 485      19.091 -43.073 -31.788  1.00 70.18           C  
ANISOU 2420  CB  ILE A 485    11031   8259   7377    269   -122   -273       C  
ATOM   2421  CG1 ILE A 485      20.414 -43.820 -31.584  1.00 70.41           C  
ANISOU 2421  CG1 ILE A 485    10926   8292   7536    224    192   -253       C  
ATOM   2422  CG2 ILE A 485      17.962 -43.838 -31.130  1.00 68.34           C  
ANISOU 2422  CG2 ILE A 485    10583   8146   7236    305   -361   -319       C  
ATOM   2423  CD1 ILE A 485      20.992 -43.719 -30.191  1.00 62.88           C  
ANISOU 2423  CD1 ILE A 485     9570   7492   6828    216    237   -220       C  
ATOM   2424  N   ILE A 486      17.410 -40.945 -33.582  1.00 75.71           N  
ANISOU 2424  N   ILE A 486    12400   8731   7635    375   -562   -230       N  
ATOM   2425  CA  ILE A 486      16.173 -40.249 -33.917  1.00 79.46           C  
ANISOU 2425  CA  ILE A 486    13004   9174   8013    472   -903   -227       C  
ATOM   2426  C   ILE A 486      15.781 -40.496 -35.377  1.00 82.28           C  
ANISOU 2426  C   ILE A 486    13798   9417   8045    494  -1020   -220       C  
ATOM   2427  O   ILE A 486      14.596 -40.601 -35.698  1.00 82.53           O  
ANISOU 2427  O   ILE A 486    13876   9473   8007    569  -1361   -264       O  
ATOM   2428  CB  ILE A 486      16.296 -38.732 -33.640  1.00 81.07           C  
ANISOU 2428  CB  ILE A 486    13236   9293   8273    510   -914   -154       C  
ATOM   2429  CG1 ILE A 486      16.437 -38.500 -32.137  1.00 71.04           C  
ANISOU 2429  CG1 ILE A 486    11533   8164   7296    502   -876   -208       C  
ATOM   2430  CG2 ILE A 486      15.079 -37.975 -34.157  1.00 67.67           C  
ANISOU 2430  CG2 ILE A 486    11719   7523   6470    641  -1264   -129       C  
ATOM   2431  CD1 ILE A 486      15.300 -39.079 -31.345  1.00 62.62           C  
ANISOU 2431  CD1 ILE A 486    10159   7275   6359    568  -1111   -295       C  
ATOM   2432  N   ASN A 487      16.776 -40.604 -36.254  1.00 85.20           N  
ANISOU 2432  N   ASN A 487    14481   9676   8216    429   -737   -173       N  
ATOM   2433  CA  ASN A 487      16.520 -40.960 -37.645  1.00 86.84           C  
ANISOU 2433  CA  ASN A 487    15139   9793   8061    440   -809   -184       C  
ATOM   2434  C   ASN A 487      15.974 -42.383 -37.746  1.00 85.98           C  
ANISOU 2434  C   ASN A 487    14951   9763   7955    423   -935   -340       C  
ATOM   2435  O   ASN A 487      15.031 -42.642 -38.492  1.00 87.24           O  
ANISOU 2435  O   ASN A 487    15320   9913   7913    463  -1242   -403       O  
ATOM   2436  CB  ASN A 487      17.792 -40.821 -38.492  1.00 84.98           C  
ANISOU 2436  CB  ASN A 487    15239   9434   7617    364   -402   -111       C  
ATOM   2437  CG  ASN A 487      17.501 -40.779 -39.986  1.00 93.47           C  
ANISOU 2437  CG  ASN A 487    16873  10406   8234    392   -485    -85       C  
ATOM   2438  OD1 ASN A 487      17.298 -39.709 -40.562  1.00100.30           O  
ANISOU 2438  OD1 ASN A 487    18043  11168   8897    438   -581     57       O  
ATOM   2439  ND2 ASN A 487      17.482 -41.943 -40.619  1.00 96.73           N  
ANISOU 2439  ND2 ASN A 487    17443  10838   8473    366   -452   -222       N  
ATOM   2440  N   GLU A 488      16.559 -43.298 -36.980  1.00 86.18           N  
ANISOU 2440  N   GLU A 488    14667   9855   8223    361   -717   -401       N  
ATOM   2441  CA  GLU A 488      16.145 -44.696 -37.011  1.00 86.23           C  
ANISOU 2441  CA  GLU A 488    14589   9894   8281    330   -791   -540       C  
ATOM   2442  C   GLU A 488      14.725 -44.872 -36.467  1.00 87.43           C  
ANISOU 2442  C   GLU A 488    14488  10148   8583    364  -1194   -599       C  
ATOM   2443  O   GLU A 488      14.024 -45.821 -36.817  1.00 95.14           O  
ANISOU 2443  O   GLU A 488    15490  11121   9539    334  -1375   -722       O  
ATOM   2444  CB  GLU A 488      17.133 -45.562 -36.225  1.00 82.65           C  
ANISOU 2444  CB  GLU A 488    13848   9469   8087    278   -464   -553       C  
ATOM   2445  CG  GLU A 488      16.706 -47.018 -36.026  1.00 89.23           C  
ANISOU 2445  CG  GLU A 488    14537  10309   9058    245   -528   -674       C  
ATOM   2446  CD  GLU A 488      16.842 -47.874 -37.275  1.00102.37           C  
ANISOU 2446  CD  GLU A 488    16584  11837  10476    217   -458   -810       C  
ATOM   2447  OE1 GLU A 488      17.299 -47.348 -38.313  1.00106.01           O  
ANISOU 2447  OE1 GLU A 488    17437  12219  10624    228   -338   -799       O  
ATOM   2448  OE2 GLU A 488      16.499 -49.078 -37.212  1.00105.91           O  
ANISOU 2448  OE2 GLU A 488    16953  12246  11041    180   -509   -929       O  
ATOM   2449  N   LEU A 489      14.289 -43.942 -35.630  1.00 79.94           N  
ANISOU 2449  N   LEU A 489    13291   9283   7799    421  -1326   -526       N  
ATOM   2450  CA  LEU A 489      12.955 -44.023 -35.056  1.00 76.38           C  
ANISOU 2450  CA  LEU A 489    12558   8940   7521    461  -1665   -580       C  
ATOM   2451  C   LEU A 489      11.926 -43.358 -35.948  1.00 76.52           C  
ANISOU 2451  C   LEU A 489    12815   8917   7343    548  -2037   -589       C  
ATOM   2452  O   LEU A 489      10.773 -43.762 -35.969  1.00 85.66           O  
ANISOU 2452  O   LEU A 489    13833  10136   8577    562  -2353   -678       O  
ATOM   2453  CB  LEU A 489      12.922 -43.385 -33.667  1.00 71.68           C  
ANISOU 2453  CB  LEU A 489    11566   8468   7200    496  -1619   -522       C  
ATOM   2454  CG  LEU A 489      13.743 -44.049 -32.561  1.00 68.04           C  
ANISOU 2454  CG  LEU A 489    10800   8095   6957    427  -1333   -503       C  
ATOM   2455  CD1 LEU A 489      13.722 -43.175 -31.338  1.00 61.72           C  
ANISOU 2455  CD1 LEU A 489     9700   7416   6336    472  -1317   -459       C  
ATOM   2456  CD2 LEU A 489      13.226 -45.448 -32.243  1.00 65.03           C  
ANISOU 2456  CD2 LEU A 489    10222   7767   6720    363  -1379   -571       C  
ATOM   2457  N   CYS A 490      12.342 -42.326 -36.672  1.00 74.94           N  
ANISOU 2457  N   CYS A 490    12961   8609   6904    606  -2006   -487       N  
ATOM   2458  CA  CYS A 490      11.458 -41.669 -37.624  1.00 83.43           C  
ANISOU 2458  CA  CYS A 490    14324   9626   7748    709  -2369   -461       C  
ATOM   2459  C   CYS A 490      11.235 -42.577 -38.824  1.00 93.15           C  
ANISOU 2459  C   CYS A 490    15897  10818   8679    662  -2502   -565       C  
ATOM   2460  O   CYS A 490      10.148 -42.604 -39.408  1.00 96.00           O  
ANISOU 2460  O   CYS A 490    16343  11198   8933    722  -2915   -623       O  
ATOM   2461  CB  CYS A 490      12.037 -40.326 -38.064  1.00 84.17           C  
ANISOU 2461  CB  CYS A 490    14732   9586   7663    777  -2267   -291       C  
ATOM   2462  SG  CYS A 490      11.948 -39.032 -36.807  1.00 82.94           S  
ANISOU 2462  SG  CYS A 490    14228   9442   7843    864  -2251   -209       S  
ATOM   2463  N   HIS A 491      12.288 -43.307 -39.186  1.00 97.13           N  
ANISOU 2463  N   HIS A 491    16588  11264   9053    560  -2152   -600       N  
ATOM   2464  CA  HIS A 491      12.210 -44.383 -40.155  1.00100.92           C  
ANISOU 2464  CA  HIS A 491    17352  11704   9290    494  -2202   -750       C  
ATOM   2465  C   HIS A 491      11.057 -45.305 -39.775  1.00100.88           C  
ANISOU 2465  C   HIS A 491    17029  11784   9516    457  -2530   -914       C  
ATOM   2466  O   HIS A 491      10.155 -45.551 -40.571  1.00107.83           O  
ANISOU 2466  O   HIS A 491    18086  12666  10219    468  -2904  -1020       O  
ATOM   2467  CB  HIS A 491      13.539 -45.150 -40.196  1.00111.33           C  
ANISOU 2467  CB  HIS A 491    18749  12958  10593    399  -1714   -786       C  
ATOM   2468  CG  HIS A 491      13.735 -46.003 -41.417  1.00126.19           C  
ANISOU 2468  CG  HIS A 491    21063  14755  12129    350  -1669   -934       C  
ATOM   2469  ND1 HIS A 491      14.369 -47.228 -41.374  1.00127.11           N  
ANISOU 2469  ND1 HIS A 491    21137  14821  12338    269  -1387  -1074       N  
ATOM   2470  CD2 HIS A 491      13.408 -45.796 -42.717  1.00129.75           C  
ANISOU 2470  CD2 HIS A 491    22018  15158  12123    381  -1863   -969       C  
ATOM   2471  CE1 HIS A 491      14.411 -47.745 -42.589  1.00129.35           C  
ANISOU 2471  CE1 HIS A 491    21875  15025  12247    246  -1397  -1216       C  
ATOM   2472  NE2 HIS A 491      13.837 -46.895 -43.423  1.00131.46           N  
ANISOU 2472  NE2 HIS A 491    22489  15306  12153    308  -1688  -1154       N  
ATOM   2473  N   ARG A 492      11.073 -45.780 -38.535  1.00 90.97           N  
ANISOU 2473  N   ARG A 492    15299  10604   8660    408  -2398   -924       N  
ATOM   2474  CA  ARG A 492      10.119 -46.788 -38.075  1.00 92.37           C  
ANISOU 2474  CA  ARG A 492    15149  10845   9103    336  -2612  -1063       C  
ATOM   2475  C   ARG A 492       8.740 -46.227 -37.719  1.00 91.60           C  
ANISOU 2475  C   ARG A 492    14769  10858   9176    407  -3029  -1064       C  
ATOM   2476  O   ARG A 492       7.727 -46.904 -37.877  1.00 96.74           O  
ANISOU 2476  O   ARG A 492    15283  11540   9933    352  -3330  -1201       O  
ATOM   2477  CB  ARG A 492      10.688 -47.524 -36.867  1.00 93.57           C  
ANISOU 2477  CB  ARG A 492    14923  11032   9597    260  -2289  -1040       C  
ATOM   2478  CG  ARG A 492      11.871 -48.424 -37.167  1.00 73.29           C  
ANISOU 2478  CG  ARG A 492    12542   8347   6957    189  -1919  -1080       C  
ATOM   2479  CD  ARG A 492      12.672 -48.589 -35.907  1.00 70.28           C  
ANISOU 2479  CD  ARG A 492    11814   8019   6869    178  -1592   -968       C  
ATOM   2480  NE  ARG A 492      13.702 -49.611 -35.981  1.00 70.24           N  
ANISOU 2480  NE  ARG A 492    11875   7906   6907    127  -1258  -1004       N  
ATOM   2481  CZ  ARG A 492      13.503 -50.877 -35.637  1.00 85.34           C  
ANISOU 2481  CZ  ARG A 492    13624   9763   9037     52  -1233  -1081       C  
ATOM   2482  NH1 ARG A 492      12.299 -51.268 -35.221  1.00 83.72           N  
ANISOU 2482  NH1 ARG A 492    13179   9611   9019     -5  -1513  -1130       N  
ATOM   2483  NH2 ARG A 492      14.498 -51.753 -35.725  1.00 81.86           N  
ANISOU 2483  NH2 ARG A 492    13252   9200   8651     35   -919  -1108       N  
ATOM   2484  N   LEU A 493       8.697 -45.000 -37.222  1.00 91.37           N  
ANISOU 2484  N   LEU A 493    14632  10878   9206    528  -3041   -926       N  
ATOM   2485  CA  LEU A 493       7.420 -44.379 -36.882  1.00 97.60           C  
ANISOU 2485  CA  LEU A 493    15143  11764  10178    629  -3410   -929       C  
ATOM   2486  C   LEU A 493       6.594 -44.175 -38.135  1.00108.05           C  
ANISOU 2486  C   LEU A 493    16766  13046  11241    697  -3854   -986       C  
ATOM   2487  O   LEU A 493       5.367 -44.102 -38.079  1.00114.60           O  
ANISOU 2487  O   LEU A 493    17348  13956  12239    750  -4237  -1052       O  
ATOM   2488  CB  LEU A 493       7.632 -43.042 -36.165  1.00 85.62           C  
ANISOU 2488  CB  LEU A 493    13504  10268   8758    761  -3312   -785       C  
ATOM   2489  CG  LEU A 493       7.970 -43.159 -34.681  1.00 80.82           C  
ANISOU 2489  CG  LEU A 493    12468   9768   8474    718  -3017   -762       C  
ATOM   2490  CD1 LEU A 493       8.494 -41.848 -34.162  1.00 80.31           C  
ANISOU 2490  CD1 LEU A 493    12404   9682   8427    823  -2870   -647       C  
ATOM   2491  CD2 LEU A 493       6.756 -43.616 -33.889  1.00 80.26           C  
ANISOU 2491  CD2 LEU A 493    11924   9842   8729    707  -3206   -850       C  
ATOM   2492  N   GLY A 494       7.290 -44.081 -39.264  1.00107.21           N  
ANISOU 2492  N   GLY A 494    17191  12826  10720    697  -3794   -957       N  
ATOM   2493  CA  GLY A 494       6.666 -43.813 -40.543  1.00112.73           C  
ANISOU 2493  CA  GLY A 494    18273  13487  11072    772  -4204   -984       C  
ATOM   2494  C   GLY A 494       5.871 -42.526 -40.512  1.00112.35           C  
ANISOU 2494  C   GLY A 494    18156  13460  11072    970  -4537   -857       C  
ATOM   2495  O   GLY A 494       6.138 -41.644 -39.693  1.00110.11           O  
ANISOU 2495  O   GLY A 494    17680  13170  10985   1053  -4354   -725       O  
ATOM   2496  N   GLY A 495       4.885 -42.429 -41.398  1.00113.92           N  
ANISOU 2496  N   GLY A 495    18506  13677  11100   1053  -5043   -907       N  
ATOM   2497  CA  GLY A 495       4.016 -41.271 -41.453  1.00113.17           C  
ANISOU 2497  CA  GLY A 495    18337  13591  11071   1271  -5423   -791       C  
ATOM   2498  C   GLY A 495       4.802 -39.985 -41.576  1.00112.62           C  
ANISOU 2498  C   GLY A 495    18592  13384  10815   1400  -5208   -547       C  
ATOM   2499  O   GLY A 495       5.861 -39.959 -42.203  1.00113.31           O  
ANISOU 2499  O   GLY A 495    19143  13367  10542   1335  -4915   -463       O  
ATOM   2500  N   GLU A 496       4.296 -38.929 -40.948  1.00109.87           N  
ANISOU 2500  N   GLU A 496    17983  13024  10740   1577  -5326   -443       N  
ATOM   2501  CA  GLU A 496       4.908 -37.611 -41.025  1.00104.40           C  
ANISOU 2501  CA  GLU A 496    17571  12164   9933   1707  -5166   -214       C  
ATOM   2502  C   GLU A 496       6.343 -37.575 -40.511  1.00 97.68           C  
ANISOU 2502  C   GLU A 496    16802  11241   9072   1561  -4565   -153       C  
ATOM   2503  O   GLU A 496       7.107 -36.685 -40.884  1.00 97.01           O  
ANISOU 2503  O   GLU A 496    17083  10990   8786   1600  -4373     34       O  
ATOM   2504  CB  GLU A 496       4.056 -36.603 -40.257  1.00110.36           C  
ANISOU 2504  CB  GLU A 496    17944  12914  11073   1918  -5375   -168       C  
ATOM   2505  CG  GLU A 496       2.888 -36.073 -41.059  1.00126.49           C  
ANISOU 2505  CG  GLU A 496    20087  14937  13037   2144  -5970   -113       C  
ATOM   2506  CD  GLU A 496       3.332 -35.142 -42.176  1.00138.71           C  
ANISOU 2506  CD  GLU A 496    22284  16278  14141   2266  -6055    138       C  
ATOM   2507  OE1 GLU A 496       2.915 -35.350 -43.338  1.00142.43           O  
ANISOU 2507  OE1 GLU A 496    23118  16759  14240   2316  -6439    169       O  
ATOM   2508  OE2 GLU A 496       4.102 -34.200 -41.885  1.00142.41           O  
ANISOU 2508  OE2 GLU A 496    22910  16573  14628   2302  -5736    307       O  
ATOM   2509  N   TYR A 497       6.708 -38.546 -39.673  1.00 90.79           N  
ANISOU 2509  N   TYR A 497    15586  10485   8426   1392  -4277   -300       N  
ATOM   2510  CA  TYR A 497       8.037 -38.574 -39.056  1.00 86.91           C  
ANISOU 2510  CA  TYR A 497    15083   9953   7986   1262  -3739   -258       C  
ATOM   2511  C   TYR A 497       9.122 -38.962 -40.038  1.00 90.40           C  
ANISOU 2511  C   TYR A 497    16021  10300   8028   1145  -3469   -210       C  
ATOM   2512  O   TYR A 497      10.245 -38.458 -39.967  1.00 87.18           O  
ANISOU 2512  O   TYR A 497    15778   9788   7557   1094  -3086    -93       O  
ATOM   2513  CB  TYR A 497       8.078 -39.544 -37.875  1.00 88.77           C  
ANISOU 2513  CB  TYR A 497    14815  10345   8569   1135  -3542   -407       C  
ATOM   2514  CG  TYR A 497       7.208 -39.146 -36.712  1.00 90.17           C  
ANISOU 2514  CG  TYR A 497    14480  10632   9150   1229  -3673   -453       C  
ATOM   2515  CD1 TYR A 497       5.886 -39.561 -36.643  1.00103.97           C  
ANISOU 2515  CD1 TYR A 497    15935  12496  11075   1281  -4045   -567       C  
ATOM   2516  CD2 TYR A 497       7.701 -38.357 -35.688  1.00 76.91           C  
ANISOU 2516  CD2 TYR A 497    12602   8943   7678   1261  -3419   -400       C  
ATOM   2517  CE1 TYR A 497       5.079 -39.202 -35.590  1.00102.33           C  
ANISOU 2517  CE1 TYR A 497    15247  12396  11238   1371  -4125   -616       C  
ATOM   2518  CE2 TYR A 497       6.897 -37.987 -34.635  1.00 83.68           C  
ANISOU 2518  CE2 TYR A 497    13014   9906   8874   1356  -3515   -463       C  
ATOM   2519  CZ  TYR A 497       5.585 -38.417 -34.591  1.00 95.75           C  
ANISOU 2519  CZ  TYR A 497    14255  11554  10571   1415  -3850   -567       C  
ATOM   2520  OH  TYR A 497       4.760 -38.073 -33.547  1.00103.44           O  
ANISOU 2520  OH  TYR A 497    14769  12644  11888   1511  -3908   -638       O  
ATOM   2521  N   ALA A 498       8.785 -39.871 -40.946  1.00101.20           N  
ANISOU 2521  N   ALA A 498    17613  11703   9135   1095  -3660   -319       N  
ATOM   2522  CA  ALA A 498       9.747 -40.373 -41.917  1.00106.69           C  
ANISOU 2522  CA  ALA A 498    18784  12322   9430    988  -3393   -317       C  
ATOM   2523  C   ALA A 498      10.160 -39.276 -42.897  1.00114.27           C  
ANISOU 2523  C   ALA A 498    20292  13130   9993   1074  -3369    -98       C  
ATOM   2524  O   ALA A 498      11.237 -39.343 -43.489  1.00118.33           O  
ANISOU 2524  O   ALA A 498    21175  13560  10226    987  -2993    -36       O  
ATOM   2525  CB  ALA A 498       9.173 -41.576 -42.658  1.00108.32           C  
ANISOU 2525  CB  ALA A 498    19114  12595   9446    921  -3646   -521       C  
ATOM   2526  N   LYS A 499       9.314 -38.255 -43.043  1.00109.66           N  
ANISOU 2526  N   LYS A 499    19752  12503   9411   1251  -3749     30       N  
ATOM   2527  CA  LYS A 499       9.589 -37.132 -43.938  1.00108.33           C  
ANISOU 2527  CA  LYS A 499    20109  12164   8887   1353  -3768    279       C  
ATOM   2528  C   LYS A 499      10.605 -36.140 -43.357  1.00110.87           C  
ANISOU 2528  C   LYS A 499    20412  12334   9379   1324  -3329    458       C  
ATOM   2529  O   LYS A 499      10.603 -34.965 -43.710  1.00116.96           O  
ANISOU 2529  O   LYS A 499    21458  12935  10045   1436  -3392    682       O  
ATOM   2530  CB  LYS A 499       8.287 -36.397 -44.269  1.00107.45           C  
ANISOU 2530  CB  LYS A 499    20027  12038   8760   1577  -4363    362       C  
ATOM   2531  CG  LYS A 499       7.261 -37.224 -45.039  1.00106.73           C  
ANISOU 2531  CG  LYS A 499    20020  12082   8449   1611  -4867    205       C  
ATOM   2532  CD  LYS A 499       5.904 -36.526 -45.086  1.00112.93           C  
ANISOU 2532  CD  LYS A 499    20652  12883   9372   1847  -5473    262       C  
ATOM   2533  CE  LYS A 499       6.030 -35.047 -45.475  1.00122.26           C  
ANISOU 2533  CE  LYS A 499    22193  13855  10407   2038  -5525    580       C  
ATOM   2534  NZ  LYS A 499       6.435 -34.830 -46.900  1.00130.69           N  
ANISOU 2534  NZ  LYS A 499    24013  14823  10822   2053  -5566    764       N  
ATOM   2535  N   LEU A 500      11.471 -36.622 -42.470  1.00114.41           N  
ANISOU 2535  N   LEU A 500    20535  12834  10101   1171  -2902    360       N  
ATOM   2536  CA  LEU A 500      12.462 -35.790 -41.790  1.00118.15           C  
ANISOU 2536  CA  LEU A 500    20909  13190  10793   1113  -2496    479       C  
ATOM   2537  C   LEU A 500      13.887 -36.304 -42.006  1.00128.95           C  
ANISOU 2537  C   LEU A 500    22424  14533  12038    923  -1953    477       C  
ATOM   2538  O   LEU A 500      14.860 -35.665 -41.597  1.00129.58           O  
ANISOU 2538  O   LEU A 500    22458  14509  12267    842  -1585    575       O  
ATOM   2539  CB  LEU A 500      12.180 -35.744 -40.283  1.00111.44           C  
ANISOU 2539  CB  LEU A 500    19436  12442  10462   1124  -2506    360       C  
ATOM   2540  CG  LEU A 500      11.143 -34.829 -39.626  1.00106.19           C  
ANISOU 2540  CG  LEU A 500    18506  11758  10082   1305  -2848    378       C  
ATOM   2541  CD1 LEU A 500       9.757 -35.053 -40.191  1.00107.69           C  
ANISOU 2541  CD1 LEU A 500    18727  12019  10170   1461  -3382    336       C  
ATOM   2542  CD2 LEU A 500      11.146 -35.074 -38.119  1.00 97.94           C  
ANISOU 2542  CD2 LEU A 500    16872  10857   9483   1260  -2720    222       C  
ATOM   2543  N   CYS A 501      14.001 -37.457 -42.657  1.00135.88           N  
ANISOU 2543  N   CYS A 501    23466  15499  12665    852  -1906    349       N  
ATOM   2544  CA  CYS A 501      15.212 -38.270 -42.577  1.00143.24           C  
ANISOU 2544  CA  CYS A 501    24356  16455  13612    691  -1412    267       C  
ATOM   2545  C   CYS A 501      16.287 -37.978 -43.625  1.00156.61           C  
ANISOU 2545  C   CYS A 501    26562  18014  14930    613  -1010    405       C  
ATOM   2546  O   CYS A 501      16.028 -37.923 -44.831  1.00158.92           O  
ANISOU 2546  O   CYS A 501    27375  18256  14750    656  -1129    469       O  
ATOM   2547  CB  CYS A 501      14.822 -39.745 -42.645  1.00145.52           C  
ANISOU 2547  CB  CYS A 501    24522  16884  13883    652  -1525     29       C  
ATOM   2548  SG  CYS A 501      13.559 -40.178 -41.436  1.00110.12           S  
ANISOU 2548  SG  CYS A 501    19432  12561   9846    712  -1943   -122       S  
ATOM   2549  N   CYS A 502      17.508 -37.813 -43.129  1.00162.57           N  
ANISOU 2549  N   CYS A 502    27146  18722  15901    494   -526    447       N  
ATOM   2550  CA  CYS A 502      18.666 -37.526 -43.961  1.00172.44           C  
ANISOU 2550  CA  CYS A 502    28784  19847  16888    394    -51    576       C  
ATOM   2551  C   CYS A 502      19.942 -37.921 -43.224  1.00166.93           C  
ANISOU 2551  C   CYS A 502    27711  19179  16536    256    444    508       C  
ATOM   2552  O   CYS A 502      20.013 -37.838 -41.996  1.00158.59           O  
ANISOU 2552  O   CYS A 502    26146  18186  15925    241    414    455       O  
ATOM   2553  CB  CYS A 502      18.704 -36.043 -44.336  1.00178.03           C  
ANISOU 2553  CB  CYS A 502    29803  20362  17478    421    -53    851       C  
ATOM   2554  SG  CYS A 502      18.741 -34.911 -42.916  1.00221.26           S  
ANISOU 2554  SG  CYS A 502    34781  25762  23525    421    -98    919       S  
ATOM   2555  N   SER A 640      19.185 -48.557 -39.428  1.00 97.82           N  
ANISOU 2555  N   SER A 640    16746  10989   9430    197    339   -926       N  
ATOM   2556  CA  SER A 640      20.620 -48.741 -39.621  1.00 94.37           C  
ANISOU 2556  CA  SER A 640    16337  10484   9034    198    831   -911       C  
ATOM   2557  C   SER A 640      21.251 -49.680 -38.593  1.00 90.16           C  
ANISOU 2557  C   SER A 640    15370   9957   8930    214   1016   -916       C  
ATOM   2558  O   SER A 640      20.563 -50.251 -37.739  1.00 82.63           O  
ANISOU 2558  O   SER A 640    14125   9052   8218    214    779   -925       O  
ATOM   2559  CB  SER A 640      21.331 -47.395 -39.579  1.00 90.14           C  
ANISOU 2559  CB  SER A 640    15818   9982   8451    188   1017   -732       C  
ATOM   2560  OG  SER A 640      21.020 -46.725 -38.377  1.00 86.53           O  
ANISOU 2560  OG  SER A 640    14969   9641   8268    192    821   -611       O  
ATOM   2561  N   GLN A 641      22.574 -49.807 -38.696  1.00 87.66           N  
ANISOU 2561  N   GLN A 641    15011   9589   8705    232   1450   -897       N  
ATOM   2562  CA  GLN A 641      23.377 -50.779 -37.956  1.00 81.35           C  
ANISOU 2562  CA  GLN A 641    13861   8763   8285    277   1676   -906       C  
ATOM   2563  C   GLN A 641      23.415 -50.563 -36.439  1.00 85.95           C  
ANISOU 2563  C   GLN A 641    13933   9490   9235    289   1542   -752       C  
ATOM   2564  O   GLN A 641      23.638 -49.450 -35.962  1.00 97.11           O  
ANISOU 2564  O   GLN A 641    15206  11014  10676    264   1519   -626       O  
ATOM   2565  CB  GLN A 641      24.802 -50.760 -38.519  1.00 83.34           C  
ANISOU 2565  CB  GLN A 641    14183   8941   8540    301   2176   -917       C  
ATOM   2566  CG  GLN A 641      25.821 -51.557 -37.737  1.00 84.22           C  
ANISOU 2566  CG  GLN A 641    13888   9034   9076    373   2429   -894       C  
ATOM   2567  CD  GLN A 641      27.057 -51.904 -38.566  1.00 95.03           C  
ANISOU 2567  CD  GLN A 641    15384  10287  10438    418   2935   -981       C  
ATOM   2568  OE1 GLN A 641      27.016 -51.919 -39.806  1.00 89.40           O  
ANISOU 2568  OE1 GLN A 641    15124   9478   9366    399   3098  -1110       O  
ATOM   2569  NE2 GLN A 641      28.163 -52.190 -37.882  1.00100.17           N  
ANISOU 2569  NE2 GLN A 641    15628  10953  11478    485   3185   -916       N  
ATOM   2570  N   TYR A 642      23.192 -51.635 -35.684  1.00 80.43           N  
ANISOU 2570  N   TYR A 642    12978   8776   8805    323   1456   -764       N  
ATOM   2571  CA  TYR A 642      23.328 -51.596 -34.230  1.00 71.75           C  
ANISOU 2571  CA  TYR A 642    11417   7818   8028    347   1362   -613       C  
ATOM   2572  C   TYR A 642      23.769 -52.924 -33.630  1.00 73.83           C  
ANISOU 2572  C   TYR A 642    11440   8005   8608    417   1474   -600       C  
ATOM   2573  O   TYR A 642      23.581 -53.985 -34.216  1.00 73.60           O  
ANISOU 2573  O   TYR A 642    11587   7798   8579    434   1529   -727       O  
ATOM   2574  CB  TYR A 642      22.016 -51.165 -33.567  1.00 69.31           C  
ANISOU 2574  CB  TYR A 642    11010   7638   7686    303    966   -566       C  
ATOM   2575  CG  TYR A 642      20.846 -52.120 -33.708  1.00 67.70           C  
ANISOU 2575  CG  TYR A 642    10887   7359   7477    274    731   -661       C  
ATOM   2576  CD1 TYR A 642      20.677 -53.196 -32.841  1.00 66.69           C  
ANISOU 2576  CD1 TYR A 642    10499   7211   7630    288    696   -615       C  
ATOM   2577  CD2 TYR A 642      19.881 -51.911 -34.677  1.00 72.72           C  
ANISOU 2577  CD2 TYR A 642    11850   7944   7834    226    523   -785       C  
ATOM   2578  CE1 TYR A 642      19.592 -54.049 -32.967  1.00 68.46           C  
ANISOU 2578  CE1 TYR A 642    10781   7346   7883    231    492   -702       C  
ATOM   2579  CE2 TYR A 642      18.800 -52.756 -34.806  1.00 74.97           C  
ANISOU 2579  CE2 TYR A 642    12178   8164   8145    177    286   -890       C  
ATOM   2580  CZ  TYR A 642      18.658 -53.819 -33.955  1.00 70.54           C  
ANISOU 2580  CZ  TYR A 642    11346   7566   7891    169    285   -853       C  
ATOM   2581  OH  TYR A 642      17.570 -54.644 -34.110  1.00 71.62           O  
ANISOU 2581  OH  TYR A 642    11517   7615   8080     92     61   -962       O  
ATOM   2582  N   LEU A 643      24.357 -52.847 -32.444  1.00 75.34           N  
ANISOU 2582  N   LEU A 643    11237   8321   9066    462   1491   -447       N  
ATOM   2583  CA  LEU A 643      24.678 -54.035 -31.671  1.00 73.69           C  
ANISOU 2583  CA  LEU A 643    10772   8059   9169    545   1532   -376       C  
ATOM   2584  C   LEU A 643      23.652 -54.181 -30.552  1.00 73.76           C  
ANISOU 2584  C   LEU A 643    10581   8193   9253    512   1217   -263       C  
ATOM   2585  O   LEU A 643      23.368 -53.231 -29.834  1.00 78.42           O  
ANISOU 2585  O   LEU A 643    11020   8988   9789    476   1053   -177       O  
ATOM   2586  CB  LEU A 643      26.101 -53.945 -31.117  1.00 71.82           C  
ANISOU 2586  CB  LEU A 643    10227   7884   9178    634   1761   -271       C  
ATOM   2587  CG  LEU A 643      26.489 -54.929 -30.012  1.00 72.78           C  
ANISOU 2587  CG  LEU A 643    10011   8010   9632    743   1737   -126       C  
ATOM   2588  CD1 LEU A 643      26.228 -56.380 -30.425  1.00 74.53           C  
ANISOU 2588  CD1 LEU A 643    10374   7971   9973    802   1809   -196       C  
ATOM   2589  CD2 LEU A 643      27.951 -54.728 -29.613  1.00 73.38           C  
ANISOU 2589  CD2 LEU A 643     9780   8158   9943    838   1943    -44       C  
ATOM   2590  N   PHE A 644      23.068 -55.360 -30.412  1.00 71.76           N  
ANISOU 2590  N   PHE A 644    10337   7805   9124    517   1147   -271       N  
ATOM   2591  CA  PHE A 644      22.060 -55.537 -29.379  1.00 73.33           C  
ANISOU 2591  CA  PHE A 644    10351   8118   9394    469    890   -154       C  
ATOM   2592  C   PHE A 644      22.603 -56.288 -28.185  1.00 76.39           C  
ANISOU 2592  C   PHE A 644    10428   8534  10061    556    934     48       C  
ATOM   2593  O   PHE A 644      22.950 -57.459 -28.284  1.00 79.25           O  
ANISOU 2593  O   PHE A 644    10799   8688  10625    620   1060     62       O  
ATOM   2594  CB  PHE A 644      20.835 -56.270 -29.908  1.00 74.97           C  
ANISOU 2594  CB  PHE A 644    10753   8171   9562    378    737   -274       C  
ATOM   2595  CG  PHE A 644      19.854 -56.630 -28.836  1.00 73.79           C  
ANISOU 2595  CG  PHE A 644    10385   8111   9541    320    536   -142       C  
ATOM   2596  CD1 PHE A 644      19.001 -55.671 -28.318  1.00 67.35           C  
ANISOU 2596  CD1 PHE A 644     9464   7524   8600    260    324   -105       C  
ATOM   2597  CD2 PHE A 644      19.791 -57.925 -28.337  1.00 80.29           C  
ANISOU 2597  CD2 PHE A 644    11111   8777  10621    330    581    -49       C  
ATOM   2598  CE1 PHE A 644      18.097 -55.993 -27.334  1.00 67.51           C  
ANISOU 2598  CE1 PHE A 644     9277   7640   8733    205    183     13       C  
ATOM   2599  CE2 PHE A 644      18.888 -58.258 -27.352  1.00 82.20           C  
ANISOU 2599  CE2 PHE A 644    11161   9099  10973    262    434     93       C  
ATOM   2600  CZ  PHE A 644      18.037 -57.288 -26.848  1.00 76.83           C  
ANISOU 2600  CZ  PHE A 644    10368   8674  10150    196    245    120       C  
ATOM   2601  N   LEU A 645      22.658 -55.599 -27.051  1.00 75.19           N  
ANISOU 2601  N   LEU A 645    10019   8637   9911    565    819    202       N  
ATOM   2602  CA  LEU A 645      23.047 -56.210 -25.793  1.00 69.04           C  
ANISOU 2602  CA  LEU A 645     8957   7937   9337    646    803    423       C  
ATOM   2603  C   LEU A 645      21.798 -56.424 -24.951  1.00 68.87           C  
ANISOU 2603  C   LEU A 645     8862   8015   9289    566    602    525       C  
ATOM   2604  O   LEU A 645      21.141 -55.464 -24.554  1.00 64.17           O  
ANISOU 2604  O   LEU A 645     8220   7634   8527    500    452    511       O  
ATOM   2605  CB  LEU A 645      24.059 -55.335 -25.059  1.00 63.86           C  
ANISOU 2605  CB  LEU A 645     8062   7514   8687    711    814    516       C  
ATOM   2606  CG  LEU A 645      25.338 -55.014 -25.833  1.00 68.42           C  
ANISOU 2606  CG  LEU A 645     8656   8018   9324    771   1038    422       C  
ATOM   2607  CD1 LEU A 645      26.382 -54.364 -24.942  1.00 71.14           C  
ANISOU 2607  CD1 LEU A 645     8693   8582   9756    829   1024    530       C  
ATOM   2608  CD2 LEU A 645      25.910 -56.258 -26.496  1.00 67.16           C  
ANISOU 2608  CD2 LEU A 645     8574   7576   9369    870   1254    392       C  
ATOM   2609  N   PRO A 646      21.446 -57.690 -24.689  1.00 73.47           N  
ANISOU 2609  N   PRO A 646     9436   8425  10053    570    618    625       N  
ATOM   2610  CA  PRO A 646      20.184 -57.941 -23.991  1.00 74.05           C  
ANISOU 2610  CA  PRO A 646     9447   8570  10117    465    467    716       C  
ATOM   2611  C   PRO A 646      20.265 -57.448 -22.552  1.00 77.96           C  
ANISOU 2611  C   PRO A 646     9693   9374  10556    502    384    928       C  
ATOM   2612  O   PRO A 646      21.364 -57.396 -21.999  1.00 80.58           O  
ANISOU 2612  O   PRO A 646     9888   9793  10936    624    435   1053       O  
ATOM   2613  CB  PRO A 646      20.039 -59.456 -24.074  1.00 69.32           C  
ANISOU 2613  CB  PRO A 646     8902   7669   9768    464    548    789       C  
ATOM   2614  CG  PRO A 646      21.425 -59.934 -24.118  1.00 72.60           C  
ANISOU 2614  CG  PRO A 646     9278   7965  10341    632    716    860       C  
ATOM   2615  CD  PRO A 646      22.217 -58.924 -24.887  1.00 72.87           C  
ANISOU 2615  CD  PRO A 646     9375   8083  10228    676    787    683       C  
ATOM   2616  N   PRO A 647      19.117 -57.102 -21.948  1.00 75.40           N  
ANISOU 2616  N   PRO A 647     9302   9220  10128    403    258    959       N  
ATOM   2617  CA  PRO A 647      17.782 -57.338 -22.500  1.00 72.67           C  
ANISOU 2617  CA  PRO A 647     9058   8765   9791    260    183    836       C  
ATOM   2618  C   PRO A 647      17.204 -56.177 -23.288  1.00 74.66           C  
ANISOU 2618  C   PRO A 647     9414   9101   9852    204     65    602       C  
ATOM   2619  O   PRO A 647      16.079 -56.302 -23.767  1.00 76.42           O  
ANISOU 2619  O   PRO A 647     9697   9255  10084     95    -37    489       O  
ATOM   2620  CB  PRO A 647      16.947 -57.562 -21.247  1.00 70.64           C  
ANISOU 2620  CB  PRO A 647     8613   8678   9548    203    139   1032       C  
ATOM   2621  CG  PRO A 647      17.558 -56.602 -20.267  1.00 70.53           C  
ANISOU 2621  CG  PRO A 647     8453   8983   9362    296    111   1124       C  
ATOM   2622  CD  PRO A 647      19.037 -56.518 -20.597  1.00 70.38           C  
ANISOU 2622  CD  PRO A 647     8464   8903   9372    425    183   1119       C  
ATOM   2623  N   ASN A 648      17.942 -55.077 -23.409  1.00 74.02           N  
ANISOU 2623  N   ASN A 648     9345   9156   9623    274     69    539       N  
ATOM   2624  CA  ASN A 648      17.332 -53.817 -23.825  1.00 71.09           C  
ANISOU 2624  CA  ASN A 648     9038   8906   9068    237    -60    379       C  
ATOM   2625  C   ASN A 648      18.303 -52.707 -24.195  1.00 62.32           C  
ANISOU 2625  C   ASN A 648     7994   7855   7830    299    -16    304       C  
ATOM   2626  O   ASN A 648      17.925 -51.547 -24.222  1.00 59.08           O  
ANISOU 2626  O   ASN A 648     7596   7569   7282    288   -117    220       O  
ATOM   2627  CB  ASN A 648      16.439 -53.293 -22.706  1.00 78.49           C  
ANISOU 2627  CB  ASN A 648     9772  10097   9954    209   -167    447       C  
ATOM   2628  CG  ASN A 648      17.243 -52.729 -21.548  1.00 80.34           C  
ANISOU 2628  CG  ASN A 648     9836  10567  10123    287   -131    569       C  
ATOM   2629  OD1 ASN A 648      18.351 -53.190 -21.257  1.00 78.50           O  
ANISOU 2629  OD1 ASN A 648     9559  10309   9957    355    -34    685       O  
ATOM   2630  ND2 ASN A 648      16.703 -51.711 -20.899  1.00 80.26           N  
ANISOU 2630  ND2 ASN A 648     9725  10783   9986    284   -220    527       N  
ATOM   2631  N   ARG A 649      19.554 -53.049 -24.458  1.00 64.95           N  
ANISOU 2631  N   ARG A 649     8354   8089   8236    364    145    336       N  
ATOM   2632  CA  ARG A 649      20.546 -52.040 -24.802  1.00 65.64           C  
ANISOU 2632  CA  ARG A 649     8475   8220   8243    400    220    273       C  
ATOM   2633  C   ARG A 649      20.969 -52.105 -26.283  1.00 72.66           C  
ANISOU 2633  C   ARG A 649     9642   8883   9084    394    354    132       C  
ATOM   2634  O   ARG A 649      21.297 -53.172 -26.806  1.00 75.49           O  
ANISOU 2634  O   ARG A 649    10088   9047   9549    420    482    120       O  
ATOM   2635  CB  ARG A 649      21.755 -52.191 -23.886  1.00 65.09           C  
ANISOU 2635  CB  ARG A 649     8173   8260   8298    481    308    415       C  
ATOM   2636  CG  ARG A 649      22.860 -51.205 -24.134  1.00 70.39           C  
ANISOU 2636  CG  ARG A 649     8819   8980   8947    497    397    355       C  
ATOM   2637  CD  ARG A 649      23.800 -51.182 -22.951  1.00 77.64           C  
ANISOU 2637  CD  ARG A 649     9444  10083   9972    562    384    487       C  
ATOM   2638  NE  ARG A 649      23.046 -51.185 -21.700  1.00 77.83           N  
ANISOU 2638  NE  ARG A 649     9329  10319   9926    559    209    589       N  
ATOM   2639  CZ  ARG A 649      23.093 -52.162 -20.803  1.00 75.14           C  
ANISOU 2639  CZ  ARG A 649     8846  10035   9670    621    182    774       C  
ATOM   2640  NH1 ARG A 649      22.360 -52.085 -19.698  1.00 74.04           N  
ANISOU 2640  NH1 ARG A 649     8609  10101   9421    606     53    865       N  
ATOM   2641  NH2 ARG A 649      23.878 -53.211 -21.013  1.00 74.17           N  
ANISOU 2641  NH2 ARG A 649     8686   9754   9741    706    299    874       N  
ATOM   2642  N   TYR A 650      20.961 -50.954 -26.952  1.00 70.05           N  
ANISOU 2642  N   TYR A 650     9466   8567   8582    363    335     27       N  
ATOM   2643  CA  TYR A 650      21.343 -50.876 -28.357  1.00 68.94           C  
ANISOU 2643  CA  TYR A 650     9627   8238   8331    352    474    -93       C  
ATOM   2644  C   TYR A 650      22.517 -49.933 -28.538  1.00 68.65           C  
ANISOU 2644  C   TYR A 650     9578   8233   8275    362    646    -89       C  
ATOM   2645  O   TYR A 650      22.474 -48.795 -28.095  1.00 72.00           O  
ANISOU 2645  O   TYR A 650     9924   8788   8643    336    557    -75       O  
ATOM   2646  CB  TYR A 650      20.167 -50.412 -29.212  1.00 71.23           C  
ANISOU 2646  CB  TYR A 650    10180   8477   8407    296    291   -210       C  
ATOM   2647  CG  TYR A 650      18.986 -51.345 -29.157  1.00 79.07           C  
ANISOU 2647  CG  TYR A 650    11172   9423   9448    260    119   -241       C  
ATOM   2648  CD1 TYR A 650      18.154 -51.377 -28.047  1.00 81.46           C  
ANISOU 2648  CD1 TYR A 650    11222   9882   9849    243    -46   -161       C  
ATOM   2649  CD2 TYR A 650      18.701 -52.199 -30.214  1.00 88.66           C  
ANISOU 2649  CD2 TYR A 650    12639  10435  10612    230    133   -363       C  
ATOM   2650  CE1 TYR A 650      17.073 -52.233 -27.988  1.00 84.45           C  
ANISOU 2650  CE1 TYR A 650    11570  10211  10308    185   -179   -183       C  
ATOM   2651  CE2 TYR A 650      17.621 -53.059 -30.163  1.00 90.87           C  
ANISOU 2651  CE2 TYR A 650    12897  10655  10973    169    -33   -407       C  
ATOM   2652  CZ  TYR A 650      16.814 -53.067 -29.046  1.00 88.60           C  
ANISOU 2652  CZ  TYR A 650    12327  10520  10816    141   -182   -307       C  
ATOM   2653  OH  TYR A 650      15.743 -53.916 -28.982  1.00 93.25           O  
ANISOU 2653  OH  TYR A 650    12866  11045  11521     59   -323   -343       O  
ATOM   2654  N   ILE A 651      23.570 -50.409 -29.184  1.00 66.63           N  
ANISOU 2654  N   ILE A 651     9385   7842   8087    395    907   -113       N  
ATOM   2655  CA  ILE A 651      24.712 -49.561 -29.457  1.00 69.93           C  
ANISOU 2655  CA  ILE A 651     9780   8272   8518    383   1111   -113       C  
ATOM   2656  C   ILE A 651      24.726 -49.179 -30.927  1.00 75.77           C  
ANISOU 2656  C   ILE A 651    10910   8851   9029    340   1260   -220       C  
ATOM   2657  O   ILE A 651      24.837 -50.032 -31.805  1.00 77.61           O  
ANISOU 2657  O   ILE A 651    11351   8924   9216    367   1413   -299       O  
ATOM   2658  CB  ILE A 651      26.047 -50.233 -29.093  1.00 69.85           C  
ANISOU 2658  CB  ILE A 651     9513   8252   8776    458   1338    -54       C  
ATOM   2659  CG1 ILE A 651      26.176 -50.395 -27.584  1.00 66.46           C  
ANISOU 2659  CG1 ILE A 651     8705   8016   8531    503   1171     78       C  
ATOM   2660  CG2 ILE A 651      27.212 -49.394 -29.588  1.00 76.24           C  
ANISOU 2660  CG2 ILE A 651    10307   9045   9615    421   1590    -79       C  
ATOM   2661  CD1 ILE A 651      25.558 -51.640 -27.054  1.00 71.74           C  
ANISOU 2661  CD1 ILE A 651     9314   8656   9286    565   1060    151       C  
ATOM   2662  N   PHE A 652      24.604 -47.883 -31.182  1.00 74.05           N  
ANISOU 2662  N   PHE A 652    10812   8668   8657    276   1215   -220       N  
ATOM   2663  CA  PHE A 652      24.650 -47.364 -32.532  1.00 74.57           C  
ANISOU 2663  CA  PHE A 652    11271   8592   8469    234   1354   -280       C  
ATOM   2664  C   PHE A 652      25.981 -46.688 -32.796  1.00 82.12           C  
ANISOU 2664  C   PHE A 652    12180   9520   9501    190   1677   -246       C  
ATOM   2665  O   PHE A 652      26.952 -46.908 -32.070  1.00 81.21           O  
ANISOU 2665  O   PHE A 652    11718   9474   9663    208   1811   -205       O  
ATOM   2666  CB  PHE A 652      23.507 -46.390 -32.766  1.00 73.36           C  
ANISOU 2666  CB  PHE A 652    11332   8457   8086    200   1076   -284       C  
ATOM   2667  CG  PHE A 652      22.167 -47.041 -32.819  1.00 68.28           C  
ANISOU 2667  CG  PHE A 652    10777   7817   7350    228    785   -341       C  
ATOM   2668  CD1 PHE A 652      21.439 -47.245 -31.666  1.00 73.06           C  
ANISOU 2668  CD1 PHE A 652    11087   8561   8110    246    547   -309       C  
ATOM   2669  CD2 PHE A 652      21.635 -47.453 -34.025  1.00 66.96           C  
ANISOU 2669  CD2 PHE A 652    10986   7520   6936    226    754   -434       C  
ATOM   2670  CE1 PHE A 652      20.196 -47.845 -31.716  1.00 78.84           C  
ANISOU 2670  CE1 PHE A 652    11866   9293   8797    251    298   -362       C  
ATOM   2671  CE2 PHE A 652      20.395 -48.055 -34.078  1.00 65.35           C  
ANISOU 2671  CE2 PHE A 652    10831   7318   6681    232    464   -504       C  
ATOM   2672  CZ  PHE A 652      19.674 -48.250 -32.925  1.00 63.48           C  
ANISOU 2672  CZ  PHE A 652    10265   7209   6644    239    245   -465       C  
ATOM   2673  N   HIS A 653      26.015 -45.855 -33.829  1.00 89.74           N  
ANISOU 2673  N   HIS A 653    13488  10383  10226    129   1794   -253       N  
ATOM   2674  CA  HIS A 653      27.270 -45.315 -34.321  1.00 98.17           C  
ANISOU 2674  CA  HIS A 653    14567  11386  11348     66   2169   -223       C  
ATOM   2675  C   HIS A 653      28.022 -44.441 -33.312  1.00 91.21           C  
ANISOU 2675  C   HIS A 653    13302  10607  10745      0   2183   -155       C  
ATOM   2676  O   HIS A 653      29.196 -44.684 -33.015  1.00 94.63           O  
ANISOU 2676  O   HIS A 653    13440  11068  11445     -8   2427   -147       O  
ATOM   2677  CB  HIS A 653      27.028 -44.512 -35.596  1.00107.63           C  
ANISOU 2677  CB  HIS A 653    16251  12450  12193      5   2270   -210       C  
ATOM   2678  CG  HIS A 653      28.252 -43.812 -36.098  1.00106.23           C  
ANISOU 2678  CG  HIS A 653    16099  12197  12066    -90   2678   -155       C  
ATOM   2679  ND1 HIS A 653      29.379 -44.491 -36.507  1.00107.85           N  
ANISOU 2679  ND1 HIS A 653    16220  12359  12398    -81   3091   -197       N  
ATOM   2680  CD2 HIS A 653      28.534 -42.494 -36.231  1.00106.11           C  
ANISOU 2680  CD2 HIS A 653    16161  12129  12026   -201   2753    -61       C  
ATOM   2681  CE1 HIS A 653      30.299 -43.622 -36.883  1.00111.32           C  
ANISOU 2681  CE1 HIS A 653    16671  12740  12886   -194   3415   -130       C  
ATOM   2682  NE2 HIS A 653      29.813 -42.404 -36.723  1.00110.43           N  
ANISOU 2682  NE2 HIS A 653    16664  12610  12683   -278   3216    -42       N  
ATOM   2683  N   GLY A 654      27.362 -43.419 -32.790  1.00 77.77           N  
ANISOU 2683  N   GLY A 654    11593   8958   8998    -43   1915   -121       N  
ATOM   2684  CA  GLY A 654      28.081 -42.436 -32.006  1.00 80.83           C  
ANISOU 2684  CA  GLY A 654    11693   9407   9612   -131   1940    -88       C  
ATOM   2685  C   GLY A 654      28.309 -42.724 -30.533  1.00 83.46           C  
ANISOU 2685  C   GLY A 654    11555   9938  10219    -97   1757    -97       C  
ATOM   2686  O   GLY A 654      28.618 -41.804 -29.783  1.00 93.29           O  
ANISOU 2686  O   GLY A 654    12594  11250  11601   -173   1675   -100       O  
ATOM   2687  N   ALA A 655      28.159 -43.976 -30.112  1.00 78.78           N  
ANISOU 2687  N   ALA A 655    10810   9428   9696     12   1689   -100       N  
ATOM   2688  CA  ALA A 655      28.392 -44.355 -28.724  1.00 81.01           C  
ANISOU 2688  CA  ALA A 655    10676   9904  10201     59   1517    -77       C  
ATOM   2689  C   ALA A 655      29.832 -44.055 -28.336  1.00 99.42           C  
ANISOU 2689  C   ALA A 655    12672  12286  12816      4   1699    -68       C  
ATOM   2690  O   ALA A 655      30.758 -44.736 -28.769  1.00 92.10           O  
ANISOU 2690  O   ALA A 655    11647  11303  12045     40   1965    -58       O  
ATOM   2691  CB  ALA A 655      28.075 -45.814 -28.517  1.00 81.11           C  
ANISOU 2691  CB  ALA A 655    10630   9940  10248    184   1468    -51       C  
ATOM   2692  N   GLU A 656      30.008 -43.024 -27.517  1.00129.82           N  
ANISOU 2692  N   GLU A 656    16335  16242  16751    -82   1552    -89       N  
ATOM   2693  CA  GLU A 656      31.328 -42.449 -27.281  1.00140.78           C  
ANISOU 2693  CA  GLU A 656    17429  17654  18407   -184   1709   -107       C  
ATOM   2694  C   GLU A 656      31.805 -42.744 -25.869  1.00135.34           C  
ANISOU 2694  C   GLU A 656    16297  17199  17926   -138   1490   -103       C  
ATOM   2695  O   GLU A 656      33.003 -42.863 -25.627  1.00139.43           O  
ANISOU 2695  O   GLU A 656    16484  17771  18723   -160   1607   -101       O  
ATOM   2696  CB  GLU A 656      31.306 -40.932 -27.533  1.00151.70           C  
ANISOU 2696  CB  GLU A 656    18955  18935  19749   -351   1729   -152       C  
ATOM   2697  CG  GLU A 656      32.633 -40.222 -27.299  1.00157.22           C  
ANISOU 2697  CG  GLU A 656    19344  19637  20754   -501   1887   -187       C  
ATOM   2698  CD  GLU A 656      33.798 -40.955 -27.929  1.00159.39           C  
ANISOU 2698  CD  GLU A 656    19456  19865  21240   -489   2245   -152       C  
ATOM   2699  OE1 GLU A 656      33.730 -41.241 -29.142  1.00160.74           O  
ANISOU 2699  OE1 GLU A 656    19941  19867  21266   -475   2532   -117       O  
ATOM   2700  OE2 GLU A 656      34.771 -41.262 -27.208  1.00161.62           O  
ANISOU 2700  OE2 GLU A 656    19294  20286  21827   -482   2233   -167       O  
ATOM   2701  N   VAL A 657      30.852 -42.854 -24.949  1.00118.08           N  
ANISOU 2701  N   VAL A 657    14108  15161  15597    -73   1173    -99       N  
ATOM   2702  CA  VAL A 657      31.092 -43.200 -23.539  1.00121.14           C  
ANISOU 2702  CA  VAL A 657    14144  15797  16086    -10    924    -77       C  
ATOM   2703  C   VAL A 657      32.254 -42.426 -22.867  1.00120.32           C  
ANISOU 2703  C   VAL A 657    13689  15805  16221   -118    885   -144       C  
ATOM   2704  O   VAL A 657      32.922 -42.933 -21.963  1.00118.21           O  
ANISOU 2704  O   VAL A 657    13081  15724  16108    -53    754   -106       O  
ATOM   2705  CB  VAL A 657      31.294 -44.760 -23.381  1.00115.54           C  
ANISOU 2705  CB  VAL A 657    13306  15130  15464    160    952     46       C  
ATOM   2706  CG1 VAL A 657      32.658 -45.266 -23.911  1.00119.86           C  
ANISOU 2706  CG1 VAL A 657    13639  15597  16306    187   1227     71       C  
ATOM   2707  CG2 VAL A 657      31.018 -45.220 -21.946  1.00104.67           C  
ANISOU 2707  CG2 VAL A 657    11712  14002  14057    252    646    116       C  
ATOM   2708  N   TYR A 658      32.460 -41.179 -23.289  1.00127.53           N  
ANISOU 2708  N   TYR A 658    14692  16600  17165   -286    975   -242       N  
ATOM   2709  CA  TYR A 658      33.402 -40.281 -22.617  1.00129.20           C  
ANISOU 2709  CA  TYR A 658    14593  16899  17600   -429    900   -343       C  
ATOM   2710  C   TYR A 658      32.836 -38.873 -22.488  1.00120.92           C  
ANISOU 2710  C   TYR A 658    13730  15772  16443   -571    792   -469       C  
ATOM   2711  O   TYR A 658      31.903 -38.642 -21.723  1.00116.29           O  
ANISOU 2711  O   TYR A 658    13228  15299  15657   -519    530   -521       O  
ATOM   2712  CB  TYR A 658      34.737 -40.228 -23.359  1.00144.17           C  
ANISOU 2712  CB  TYR A 658    16295  18675  19807   -527   1221   -336       C  
ATOM   2713  CG  TYR A 658      35.603 -41.454 -23.166  1.00156.21           C  
ANISOU 2713  CG  TYR A 658    17488  20312  21552   -387   1282   -250       C  
ATOM   2714  CD1 TYR A 658      36.342 -41.632 -22.000  1.00161.59           C  
ANISOU 2714  CD1 TYR A 658    17731  21232  22434   -358   1036   -266       C  
ATOM   2715  CD2 TYR A 658      35.693 -42.429 -24.156  1.00159.70           C  
ANISOU 2715  CD2 TYR A 658    18062  20614  22003   -274   1575   -159       C  
ATOM   2716  CE1 TYR A 658      37.143 -42.756 -21.822  1.00165.90           C  
ANISOU 2716  CE1 TYR A 658    17963  21866  23206   -201   1072   -168       C  
ATOM   2717  CE2 TYR A 658      36.489 -43.555 -23.990  1.00163.84           C  
ANISOU 2717  CE2 TYR A 658    18280  21208  22762   -123   1642    -85       C  
ATOM   2718  CZ  TYR A 658      37.212 -43.715 -22.823  1.00166.41           C  
ANISOU 2718  CZ  TYR A 658    18157  21763  23310    -79   1387    -77       C  
ATOM   2719  OH  TYR A 658      38.004 -44.834 -22.660  1.00166.69           O  
ANISOU 2719  OH  TYR A 658    17881  21852  23601     98   1435     15       O  
TER    2720      TYR A 658                                                      
HETATM 2721 ZN    ZN A 701      15.305  -0.697 -16.782  1.00151.58          ZN  
HETATM 2722  FBH 4TO A 702      25.185 -59.766   1.547  1.00 91.65           F  
HETATM 2723  CBG 4TO A 702      25.300 -58.647   2.302  1.00 90.94           C  
HETATM 2724  FBI 4TO A 702      25.051 -58.947   3.524  1.00 94.84           F  
HETATM 2725  FBJ 4TO A 702      24.424 -57.781   1.940  1.00 91.85           F  
HETATM 2726  CBE 4TO A 702      26.597 -58.130   2.170  1.00 84.36           C  
HETATM 2727  CBF 4TO A 702      26.901 -56.833   2.577  1.00 83.86           C  
HETATM 2728  CBD 4TO A 702      27.598 -58.925   1.631  1.00 80.05           C  
HETATM 2729  CBC 4TO A 702      28.887 -58.430   1.500  1.00 80.16           C  
HETATM 2730  CBB 4TO A 702      29.190 -57.136   1.909  1.00 80.53           C  
HETATM 2731  CBA 4TO A 702      28.195 -56.325   2.449  1.00 85.26           C  
HETATM 2732  CAX 4TO A 702      28.495 -55.023   2.870  1.00 87.33           C  
HETATM 2733  CAY 4TO A 702      29.731 -54.768   3.447  1.00 87.71           C  
HETATM 2734  CAZ 4TO A 702      30.043 -53.494   3.886  1.00 85.20           C  
HETATM 2735  NAW 4TO A 702      27.591 -54.032   2.743  1.00 84.28           N  
HETATM 2736  CAP 4TO A 702      27.871 -52.772   3.146  1.00 85.74           C  
HETATM 2737  CAQ 4TO A 702      29.105 -52.485   3.734  1.00 86.30           C  
HETATM 2738  NAR 4TO A 702      29.359 -51.240   4.140  1.00 80.02           N  
HETATM 2739  CAV 4TO A 702      28.843 -50.167   3.303  1.00 70.31           C  
HETATM 2740  CAS 4TO A 702      28.770 -50.927   5.447  1.00 79.05           C  
HETATM 2741  CAT 4TO A 702      27.355 -50.468   5.080  1.00 72.24           C  
HETATM 2742  CAU 4TO A 702      27.373 -50.434   3.565  1.00 73.03           C  
HETATM 2743  NAO 4TO A 702      26.981 -51.764   3.034  1.00 80.19           N  
HETATM 2744  CAM 4TO A 702      25.737 -51.923   2.551  1.00 76.38           C  
HETATM 2745  OAN 4TO A 702      24.991 -50.954   2.562  1.00 75.75           O  
HETATM 2746  NAL 4TO A 702      25.368 -53.146   2.090  1.00 77.10           N  
HETATM 2747  CAH 4TO A 702      24.140 -53.434   1.582  1.00 78.90           C  
HETATM 2748  CAG 4TO A 702      23.137 -52.506   1.263  1.00 85.03           C  
HETATM 2749  CAI 4TO A 702      23.853 -54.775   1.360  1.00 76.08           C  
HETATM 2750  CAJ 4TO A 702      22.628 -55.175   0.848  1.00 76.45           C  
HETATM 2751  CAK 4TO A 702      21.652 -54.242   0.542  1.00 78.76           C  
HETATM 2752  CAF 4TO A 702      21.897 -52.893   0.747  1.00 81.29           C  
HETATM 2753  CAD 4TO A 702      20.945 -52.000   0.437  1.00 77.56           C  
HETATM 2754  OAE 4TO A 702      19.714 -52.311   0.075  1.00 78.53           O  
HETATM 2755  CAA 4TO A 702      19.041 -51.148  -0.163  1.00 74.90           C  
HETATM 2756  NAB 4TO A 702      19.901 -50.164   0.060  1.00 75.11           N  
HETATM 2757  CAC 4TO A 702      21.075 -50.684   0.427  1.00 77.27           C  
CONECT 1517 2721                                                                
CONECT 1539 2721                                                                
CONECT 1708 2721                                                                
CONECT 1732 2721                                                                
CONECT 2721 1517 1539 1708 1732                                                 
CONECT 2722 2723                                                                
CONECT 2723 2722 2724 2725 2726                                                 
CONECT 2724 2723                                                                
CONECT 2725 2723                                                                
CONECT 2726 2723 2727 2728                                                      
CONECT 2727 2726 2731                                                           
CONECT 2728 2726 2729                                                           
CONECT 2729 2728 2730                                                           
CONECT 2730 2729 2731                                                           
CONECT 2731 2727 2730 2732                                                      
CONECT 2732 2731 2733 2735                                                      
CONECT 2733 2732 2734                                                           
CONECT 2734 2733 2737                                                           
CONECT 2735 2732 2736                                                           
CONECT 2736 2735 2737 2743                                                      
CONECT 2737 2734 2736 2738                                                      
CONECT 2738 2737 2739 2740                                                      
CONECT 2739 2738 2742                                                           
CONECT 2740 2738 2741                                                           
CONECT 2741 2740 2742                                                           
CONECT 2742 2739 2741 2743                                                      
CONECT 2743 2736 2742 2744                                                      
CONECT 2744 2743 2745 2746                                                      
CONECT 2745 2744                                                                
CONECT 2746 2744 2747                                                           
CONECT 2747 2746 2748 2749                                                      
CONECT 2748 2747 2752                                                           
CONECT 2749 2747 2750                                                           
CONECT 2750 2749 2751                                                           
CONECT 2751 2750 2752                                                           
CONECT 2752 2748 2751 2753                                                      
CONECT 2753 2752 2754 2757                                                      
CONECT 2754 2753 2755                                                           
CONECT 2755 2754 2756                                                           
CONECT 2756 2755 2757                                                           
CONECT 2757 2753 2756                                                           
MASTER      367    0    2   16   11    0    3    6 2750    1   41   28          
END                                                                             



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