CNRS Nantes University US2B US2B
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***  TRANSPORT PROTEIN 16-FEB-16 5I6C  ***

elNémo ID: 240603151953864293

Job options:

ID        	=	 240603151953864293
JOBID     	=	 TRANSPORT PROTEIN 16-FEB-16 5I6C
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    TRANSPORT PROTEIN                       16-FEB-16   5I6C              
TITLE     THE STRUCTURE OF THE EUKARYOTIC PURINE/H+ SYMPORTER, UAPA, IN COMPLEX 
TITLE    2 WITH XANTHINE                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: URIC ACID-XANTHINE PERMEASE;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: UAPA TRANSPORTER;                                           
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIDULANS FGSC A4;                   
SOURCE   3 ORGANISM_TAXID: 227321;                                              
SOURCE   4 GENE: UAPA, AN6932;                                                  
SOURCE   5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932                                        
KEYWDS    MEMBRANE PROTEIN EUKARYOTIC URIC ACID/XANTHINE H+ SYMPORTER,          
KEYWDS   2 TRANSPORT PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ALGUEL,S.AMILLIS,J.LEUNG,G.LAMBRINIDIS,S.CAPALDI,N.J.SCULL,         
AUTHOR   2 G.CRAVEN,S.IWATA,A.ARMSTRONG,E.MIKROS,G.DIALLINAS,A.D.CAMERON,       
AUTHOR   3 B.BYRNE                                                              
REVDAT   3   30-AUG-17 5I6C    1       REMARK                                   
REVDAT   2   04-MAY-16 5I6C    1       JRNL                                     
REVDAT   1   27-APR-16 5I6C    0                                                
JRNL        AUTH   Y.ALGUEL,S.AMILLIS,J.LEUNG,G.LAMBRINIDIS,S.CAPALDI,          
JRNL        AUTH 2 N.J.SCULL,G.CRAVEN,S.IWATA,A.ARMSTRONG,E.MIKROS,G.DIALLINAS, 
JRNL        AUTH 3 A.D.CAMERON,B.BYRNE                                          
JRNL        TITL   STRUCTURE OF EUKARYOTIC PURINE/H(+) SYMPORTER UAPA SUGGESTS  
JRNL        TITL 2 A ROLE FOR HOMODIMERIZATION IN TRANSPORT ACTIVITY.           
JRNL        REF    NAT COMMUN                    V.   7 11336 2016              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   27088252                                                     
JRNL        DOI    10.1038/NCOMMS11336                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.70 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 76.86                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 20574                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.298                           
REMARK   3   R VALUE            (WORKING SET) : 0.296                           
REMARK   3   FREE R VALUE                     : 0.327                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.180                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1065                            
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 76.8774 -  7.3981    0.94     2398   125  0.2501 0.2910        
REMARK   3     2  7.3981 -  5.8727    0.98     2455   151  0.3252 0.2982        
REMARK   3     3  5.8727 -  5.1306    0.98     2438   131  0.3247 0.3262        
REMARK   3     4  5.1306 -  4.6615    0.98     2427   152  0.2815 0.3305        
REMARK   3     5  4.6615 -  4.3275    0.98     2458   132  0.2820 0.3269        
REMARK   3     6  4.3275 -  4.0723    0.98     2438   129  0.3233 0.3871        
REMARK   3     7  4.0723 -  3.8684    0.98     2456   135  0.3790 0.4109        
REMARK   3     8  3.8684 -  3.7000    0.98     2439   110  0.4029 0.4491        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.20                                          
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)     : 0.710            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 43.010           
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           7292                                  
REMARK   3   ANGLE     :  1.103           9944                                  
REMARK   3   CHIRALITY :  0.041           1226                                  
REMARK   3   PLANARITY :  0.009           1222                                  
REMARK   3   DIHEDRAL  : 11.294           2509                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -62.3381 -15.6395   6.3839              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5216 T22:   1.5620                                     
REMARK   3      T33:   1.5078 T12:  -0.0157                                     
REMARK   3      T13:   0.0119 T23:   0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4643 L22:   3.3391                                     
REMARK   3      L33:   2.9008 L12:   0.0303                                     
REMARK   3      L13:   0.6692 L23:  -0.4215                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1282 S12:   0.0594 S13:   0.7718                       
REMARK   3      S21:  -0.2106 S22:   0.4987 S23:   0.2211                       
REMARK   3      S31:  -0.3516 S32:  -0.1290 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -36.5038 -42.4252   9.7886              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4988 T22:   1.5807                                     
REMARK   3      T33:   2.3112 T12:   0.0027                                     
REMARK   3      T13:   0.1127 T23:   0.1719                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7815 L22:   3.6212                                     
REMARK   3      L33:   4.3070 L12:  -1.3452                                     
REMARK   3      L13:   1.3610 L23:   0.0971                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1807 S12:  -0.6005 S13:  -1.3184                       
REMARK   3      S21:  -0.1393 S22:   0.0002 S23:  -1.0964                       
REMARK   3      S31:   0.1038 S32:   0.3669 S33:   0.0001                       
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 5I6C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000218359.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-OCT-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.992                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20599                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 76.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.10200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.96500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG300, 0.1 MES PH 6.5, VAPOR            
REMARK 280  DIFFUSION, TEMPERATURE 293.15K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       86.91500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     ILE A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     ASP A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     ILE A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     ASN A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     ASN A    19                                                      
REMARK 465     PRO A    20                                                      
REMARK 465     LYS A    21                                                      
REMARK 465     LYS A    22                                                      
REMARK 465     THR A    23                                                      
REMARK 465     VAL A    24                                                      
REMARK 465     ARG A    25                                                      
REMARK 465     GLN A    26                                                      
REMARK 465     ARG A    27                                                      
REMARK 465     VAL A    28                                                      
REMARK 465     ARG A    29                                                      
REMARK 465     LEU A    30                                                      
REMARK 465     LEU A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     ARG A    33                                                      
REMARK 465     HIS A    34                                                      
REMARK 465     LEU A    35                                                      
REMARK 465     THR A    36                                                      
REMARK 465     THR A    37                                                      
REMARK 465     ARG A    38                                                      
REMARK 465     GLU A    39                                                      
REMARK 465     GLY A    40                                                      
REMARK 465     LEU A    41                                                      
REMARK 465     ILE A    42                                                      
REMARK 465     GLY A    43                                                      
REMARK 465     ASP A    44                                                      
REMARK 465     TYR A    45                                                      
REMARK 465     ASP A    46                                                      
REMARK 465     TYR A    47                                                      
REMARK 465     GLY A    48                                                      
REMARK 465     PHE A    49                                                      
REMARK 465     LEU A    50                                                      
REMARK 465     PHE A    51                                                      
REMARK 465     ARG A    52                                                      
REMARK 465     PRO A    53                                                      
REMARK 465     GLU A    54                                                      
REMARK 465     LEU A    55                                                      
REMARK 465     PRO A    56                                                      
REMARK 465     PHE A    57                                                      
REMARK 465     MET A    58                                                      
REMARK 465     LYS A    59                                                      
REMARK 465     LYS A    60                                                      
REMARK 465     ASP A    61                                                      
REMARK 465     PRO A    62                                                      
REMARK 465     ARG A    63                                                      
REMARK 465     ALA A    64                                                      
REMARK 465     PRO A    65                                                      
REMARK 465     VAL A   546                                                      
REMARK 465     GLU A   547                                                      
REMARK 465     GLU A   548                                                      
REMARK 465     ILE A   549                                                      
REMARK 465     GLY A   550                                                      
REMARK 465     ALA A   551                                                      
REMARK 465     VAL A   552                                                      
REMARK 465     THR A   553                                                      
REMARK 465     PRO A   554                                                      
REMARK 465     MET A   555                                                      
REMARK 465     PRO A   556                                                      
REMARK 465     VAL A   557                                                      
REMARK 465     SER A   558                                                      
REMARK 465     ALA A   559                                                      
REMARK 465     HIS A   560                                                      
REMARK 465     ASP A   561                                                      
REMARK 465     ASN A   562                                                      
REMARK 465     ARG A   563                                                      
REMARK 465     ASP A   564                                                      
REMARK 465     GLY A   565                                                      
REMARK 465     GLU A   566                                                      
REMARK 465     ALA A   567                                                      
REMARK 465     GLU A   568                                                      
REMARK 465     TYR A   569                                                      
REMARK 465     GLN A   570                                                      
REMARK 465     SER A   571                                                      
REMARK 465     LYS A   572                                                      
REMARK 465     GLN A   573                                                      
REMARK 465     ALA A   574                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     ILE B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     ASP B     9                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     PRO B    11                                                      
REMARK 465     ASP B    12                                                      
REMARK 465     SER B    13                                                      
REMARK 465     VAL B    14                                                      
REMARK 465     ILE B    15                                                      
REMARK 465     PRO B    16                                                      
REMARK 465     ASN B    17                                                      
REMARK 465     SER B    18                                                      
REMARK 465     ASN B    19                                                      
REMARK 465     PRO B    20                                                      
REMARK 465     LYS B    21                                                      
REMARK 465     LYS B    22                                                      
REMARK 465     THR B    23                                                      
REMARK 465     VAL B    24                                                      
REMARK 465     ARG B    25                                                      
REMARK 465     GLN B    26                                                      
REMARK 465     ARG B    27                                                      
REMARK 465     VAL B    28                                                      
REMARK 465     ARG B    29                                                      
REMARK 465     LEU B    30                                                      
REMARK 465     LEU B    31                                                      
REMARK 465     ALA B    32                                                      
REMARK 465     ARG B    33                                                      
REMARK 465     HIS B    34                                                      
REMARK 465     LEU B    35                                                      
REMARK 465     THR B    36                                                      
REMARK 465     THR B    37                                                      
REMARK 465     ARG B    38                                                      
REMARK 465     GLU B    39                                                      
REMARK 465     GLY B    40                                                      
REMARK 465     LEU B    41                                                      
REMARK 465     ILE B    42                                                      
REMARK 465     GLY B    43                                                      
REMARK 465     ASP B    44                                                      
REMARK 465     TYR B    45                                                      
REMARK 465     ASP B    46                                                      
REMARK 465     TYR B    47                                                      
REMARK 465     GLY B    48                                                      
REMARK 465     PHE B    49                                                      
REMARK 465     LEU B    50                                                      
REMARK 465     PHE B    51                                                      
REMARK 465     ARG B    52                                                      
REMARK 465     PRO B    53                                                      
REMARK 465     GLU B    54                                                      
REMARK 465     LEU B    55                                                      
REMARK 465     PRO B    56                                                      
REMARK 465     PHE B    57                                                      
REMARK 465     MET B    58                                                      
REMARK 465     LYS B    59                                                      
REMARK 465     LYS B    60                                                      
REMARK 465     ASP B    61                                                      
REMARK 465     PRO B    62                                                      
REMARK 465     ARG B    63                                                      
REMARK 465     ALA B    64                                                      
REMARK 465     PRO B    65                                                      
REMARK 465     ARG B   133                                                      
REMARK 465     PHE B   134                                                      
REMARK 465     HIS B   135                                                      
REMARK 465     ILE B   136                                                      
REMARK 465     TYR B   137                                                      
REMARK 465     LYS B   138                                                      
REMARK 465     THR B   139                                                      
REMARK 465     PRO B   140                                                      
REMARK 465     TYR B   141                                                      
REMARK 465     TYR B   142                                                      
REMARK 465     ILE B   143                                                      
REMARK 465     GLY B   144                                                      
REMARK 465     VAL B   546                                                      
REMARK 465     GLU B   547                                                      
REMARK 465     GLU B   548                                                      
REMARK 465     ILE B   549                                                      
REMARK 465     GLY B   550                                                      
REMARK 465     ALA B   551                                                      
REMARK 465     VAL B   552                                                      
REMARK 465     THR B   553                                                      
REMARK 465     PRO B   554                                                      
REMARK 465     MET B   555                                                      
REMARK 465     PRO B   556                                                      
REMARK 465     VAL B   557                                                      
REMARK 465     SER B   558                                                      
REMARK 465     ALA B   559                                                      
REMARK 465     HIS B   560                                                      
REMARK 465     ASP B   561                                                      
REMARK 465     ASN B   562                                                      
REMARK 465     ARG B   563                                                      
REMARK 465     ASP B   564                                                      
REMARK 465     GLY B   565                                                      
REMARK 465     GLU B   566                                                      
REMARK 465     ALA B   567                                                      
REMARK 465     GLU B   568                                                      
REMARK 465     TYR B   569                                                      
REMARK 465     GLN B   570                                                      
REMARK 465     SER B   571                                                      
REMARK 465     LYS B   572                                                      
REMARK 465     GLN B   573                                                      
REMARK 465     ALA B   574                                                      
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   O    LEU A   277     OG   SER A   281              2.17            
REMARK 500   O    LEU B   277     OG   SER B   281              2.19            
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    LEU A 105      -41.09   -137.22                                   
REMARK 500    THR A 139      -62.46   -141.18                                   
REMARK 500    LEU A 148       99.14    -45.67                                   
REMARK 500    SER A 149       79.43   -119.09                                   
REMARK 500    SER A 170      -74.49    -86.12                                   
REMARK 500    ALA A 179       97.29   -176.93                                   
REMARK 500    PRO A 211      -75.47    -58.00                                   
REMARK 500    ALA A 260      148.00   -171.80                                   
REMARK 500    SER A 295       -0.30     59.46                                   
REMARK 500    ALA A 325       46.57   -101.24                                   
REMARK 500    PHE A 437       78.12    -67.65                                   
REMARK 500    ALA A 438       35.09    -73.77                                   
REMARK 500    PHE A 501      -37.84   -155.62                                   
REMARK 500    ASN A 503      -85.19   -105.63                                   
REMARK 500    LEU B 105      -39.70   -135.10                                   
REMARK 500    LEU B 148       93.10    -43.55                                   
REMARK 500    SER B 149       79.94   -115.73                                   
REMARK 500    SER B 170      -72.48    -87.80                                   
REMARK 500    ALA B 179      -34.24     65.98                                   
REMARK 500    PRO B 211      -78.69    -52.14                                   
REMARK 500    SER B 295       -0.56     61.78                                   
REMARK 500    ALA B 325       44.39   -100.79                                   
REMARK 500    PHE B 437       77.98    -67.77                                   
REMARK 500    ALA B 438       35.54    -73.63                                   
REMARK 500    PHE B 501      -37.65   -154.13                                   
REMARK 500    ASN B 503      -85.85   -106.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     LMT A 1003                                                       
REMARK 610     LMT B 1003                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XAN A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XAN B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 1003                
DBREF  5I6C A    1   574  UNP    Q07307   UAPA_EMENI       1    574             
DBREF  5I6C B    1   574  UNP    Q07307   UAPA_EMENI       1    574             
SEQADV 5I6C VAL A  411  UNP  Q07307    GLY   411 ENGINEERED MUTATION            
SEQADV 5I6C VAL B  411  UNP  Q07307    GLY   411 ENGINEERED MUTATION            
SEQRES   1 A  574  MET ASP ASN SER ILE HIS SER THR ASP GLY PRO ASP SER          
SEQRES   2 A  574  VAL ILE PRO ASN SER ASN PRO LYS LYS THR VAL ARG GLN          
SEQRES   3 A  574  ARG VAL ARG LEU LEU ALA ARG HIS LEU THR THR ARG GLU          
SEQRES   4 A  574  GLY LEU ILE GLY ASP TYR ASP TYR GLY PHE LEU PHE ARG          
SEQRES   5 A  574  PRO GLU LEU PRO PHE MET LYS LYS ASP PRO ARG ALA PRO          
SEQRES   6 A  574  PRO PHE PHE GLY LEU ASN GLU LYS ILE PRO VAL LEU LEU          
SEQRES   7 A  574  ALA PHE ILE LEU GLY LEU GLN HIS ALA LEU ALA MET LEU          
SEQRES   8 A  574  ALA GLY VAL VAL THR PRO PRO LEU ILE ILE SER SER SER          
SEQRES   9 A  574  LEU SER LEU PRO SER ASP LEU GLN GLN TYR LEU VAL SER          
SEQRES  10 A  574  THR SER LEU ILE VAL CYS GLY LEU LEU SER MET VAL GLN          
SEQRES  11 A  574  ILE THR ARG PHE HIS ILE TYR LYS THR PRO TYR TYR ILE          
SEQRES  12 A  574  GLY SER GLY VAL LEU SER VAL MET GLY VAL SER PHE SER          
SEQRES  13 A  574  ILE ILE SER VAL ALA SER GLY ALA PHE ASN GLN MET TYR          
SEQRES  14 A  574  SER ASN GLY PHE CYS GLN LEU ASP GLU ALA GLY ASN ARG          
SEQRES  15 A  574  LEU PRO CYS PRO GLU ALA TYR GLY ALA LEU ILE GLY THR          
SEQRES  16 A  574  SER ALA CYS CYS ALA LEU VAL GLU ILE LEU LEU ALA PHE          
SEQRES  17 A  574  VAL PRO PRO LYS VAL ILE GLN LYS ILE PHE PRO PRO ILE          
SEQRES  18 A  574  VAL THR GLY PRO THR VAL MET LEU ILE GLY ILE SER LEU          
SEQRES  19 A  574  ILE GLY THR GLY PHE LYS ASP TRP ALA GLY GLY SER ALA          
SEQRES  20 A  574  CYS MET ASP ASP GLY MET LEU CYS PRO SER ALA THR ALA          
SEQRES  21 A  574  PRO ARG PRO LEU PRO TRP GLY SER PRO GLU PHE ILE GLY          
SEQRES  22 A  574  LEU GLY PHE LEU VAL PHE VAL SER ILE ILE LEU CYS GLU          
SEQRES  23 A  574  ARG PHE GLY ALA PRO ILE MET LYS SER CYS SER VAL VAL          
SEQRES  24 A  574  ILE GLY LEU LEU VAL GLY CYS ILE VAL ALA ALA ALA CYS          
SEQRES  25 A  574  GLY TYR PHE SER HIS ALA ASP ILE ASP ALA ALA PRO ALA          
SEQRES  26 A  574  ALA SER PHE ILE TRP VAL LYS THR PHE PRO LEU SER VAL          
SEQRES  27 A  574  TYR GLY PRO MET VAL LEU PRO ILE ILE ALA VAL PHE ILE          
SEQRES  28 A  574  ILE CYS ALA CYS GLU CYS ILE GLY ASP VAL THR ALA THR          
SEQRES  29 A  574  CYS ASP VAL SER ARG LEU GLU VAL ARG GLY GLY THR PHE          
SEQRES  30 A  574  GLU SER ARG ILE GLN GLY ALA VAL LEU ALA ASP GLY ILE          
SEQRES  31 A  574  ASN SER VAL VAL ALA ALA LEU ALA THR MET THR PRO MET          
SEQRES  32 A  574  THR THR PHE ALA GLN ASN ASN VAL VAL ILE ALA LEU THR          
SEQRES  33 A  574  ARG CYS ALA ASN ARG TRP ALA GLY TYR CYS CYS CYS LEU          
SEQRES  34 A  574  ILE LEU ILE VAL ALA GLY ILE PHE ALA LYS PHE ALA ALA          
SEQRES  35 A  574  ALA ILE VAL ALA ILE PRO ASN SER VAL MET GLY GLY MET          
SEQRES  36 A  574  LYS THR PHE LEU PHE ALA SER VAL VAL ILE SER GLY GLN          
SEQRES  37 A  574  ALA ILE VAL ALA LYS ALA PRO PHE THR ARG ARG ASN ARG          
SEQRES  38 A  574  PHE ILE LEU THR ALA SER MET ALA LEU GLY TYR GLY ALA          
SEQRES  39 A  574  THR LEU VAL PRO THR TRP PHE GLY ASN VAL PHE PRO GLN          
SEQRES  40 A  574  THR GLU ASN ARG ASP LEU GLU GLY PHE GLU ASN ALA ILE          
SEQRES  41 A  574  GLU LEU VAL LEU GLU THR GLY PHE ALA VAL THR ALA PHE          
SEQRES  42 A  574  VAL ALA MET LEU LEU ASN ALA ILE MET PRO ALA GLU VAL          
SEQRES  43 A  574  GLU GLU ILE GLY ALA VAL THR PRO MET PRO VAL SER ALA          
SEQRES  44 A  574  HIS ASP ASN ARG ASP GLY GLU ALA GLU TYR GLN SER LYS          
SEQRES  45 A  574  GLN ALA                                                      
SEQRES   1 B  574  MET ASP ASN SER ILE HIS SER THR ASP GLY PRO ASP SER          
SEQRES   2 B  574  VAL ILE PRO ASN SER ASN PRO LYS LYS THR VAL ARG GLN          
SEQRES   3 B  574  ARG VAL ARG LEU LEU ALA ARG HIS LEU THR THR ARG GLU          
SEQRES   4 B  574  GLY LEU ILE GLY ASP TYR ASP TYR GLY PHE LEU PHE ARG          
SEQRES   5 B  574  PRO GLU LEU PRO PHE MET LYS LYS ASP PRO ARG ALA PRO          
SEQRES   6 B  574  PRO PHE PHE GLY LEU ASN GLU LYS ILE PRO VAL LEU LEU          
SEQRES   7 B  574  ALA PHE ILE LEU GLY LEU GLN HIS ALA LEU ALA MET LEU          
SEQRES   8 B  574  ALA GLY VAL VAL THR PRO PRO LEU ILE ILE SER SER SER          
SEQRES   9 B  574  LEU SER LEU PRO SER ASP LEU GLN GLN TYR LEU VAL SER          
SEQRES  10 B  574  THR SER LEU ILE VAL CYS GLY LEU LEU SER MET VAL GLN          
SEQRES  11 B  574  ILE THR ARG PHE HIS ILE TYR LYS THR PRO TYR TYR ILE          
SEQRES  12 B  574  GLY SER GLY VAL LEU SER VAL MET GLY VAL SER PHE SER          
SEQRES  13 B  574  ILE ILE SER VAL ALA SER GLY ALA PHE ASN GLN MET TYR          
SEQRES  14 B  574  SER ASN GLY PHE CYS GLN LEU ASP GLU ALA GLY ASN ARG          
SEQRES  15 B  574  LEU PRO CYS PRO GLU ALA TYR GLY ALA LEU ILE GLY THR          
SEQRES  16 B  574  SER ALA CYS CYS ALA LEU VAL GLU ILE LEU LEU ALA PHE          
SEQRES  17 B  574  VAL PRO PRO LYS VAL ILE GLN LYS ILE PHE PRO PRO ILE          
SEQRES  18 B  574  VAL THR GLY PRO THR VAL MET LEU ILE GLY ILE SER LEU          
SEQRES  19 B  574  ILE GLY THR GLY PHE LYS ASP TRP ALA GLY GLY SER ALA          
SEQRES  20 B  574  CYS MET ASP ASP GLY MET LEU CYS PRO SER ALA THR ALA          
SEQRES  21 B  574  PRO ARG PRO LEU PRO TRP GLY SER PRO GLU PHE ILE GLY          
SEQRES  22 B  574  LEU GLY PHE LEU VAL PHE VAL SER ILE ILE LEU CYS GLU          
SEQRES  23 B  574  ARG PHE GLY ALA PRO ILE MET LYS SER CYS SER VAL VAL          
SEQRES  24 B  574  ILE GLY LEU LEU VAL GLY CYS ILE VAL ALA ALA ALA CYS          
SEQRES  25 B  574  GLY TYR PHE SER HIS ALA ASP ILE ASP ALA ALA PRO ALA          
SEQRES  26 B  574  ALA SER PHE ILE TRP VAL LYS THR PHE PRO LEU SER VAL          
SEQRES  27 B  574  TYR GLY PRO MET VAL LEU PRO ILE ILE ALA VAL PHE ILE          
SEQRES  28 B  574  ILE CYS ALA CYS GLU CYS ILE GLY ASP VAL THR ALA THR          
SEQRES  29 B  574  CYS ASP VAL SER ARG LEU GLU VAL ARG GLY GLY THR PHE          
SEQRES  30 B  574  GLU SER ARG ILE GLN GLY ALA VAL LEU ALA ASP GLY ILE          
SEQRES  31 B  574  ASN SER VAL VAL ALA ALA LEU ALA THR MET THR PRO MET          
SEQRES  32 B  574  THR THR PHE ALA GLN ASN ASN VAL VAL ILE ALA LEU THR          
SEQRES  33 B  574  ARG CYS ALA ASN ARG TRP ALA GLY TYR CYS CYS CYS LEU          
SEQRES  34 B  574  ILE LEU ILE VAL ALA GLY ILE PHE ALA LYS PHE ALA ALA          
SEQRES  35 B  574  ALA ILE VAL ALA ILE PRO ASN SER VAL MET GLY GLY MET          
SEQRES  36 B  574  LYS THR PHE LEU PHE ALA SER VAL VAL ILE SER GLY GLN          
SEQRES  37 B  574  ALA ILE VAL ALA LYS ALA PRO PHE THR ARG ARG ASN ARG          
SEQRES  38 B  574  PHE ILE LEU THR ALA SER MET ALA LEU GLY TYR GLY ALA          
SEQRES  39 B  574  THR LEU VAL PRO THR TRP PHE GLY ASN VAL PHE PRO GLN          
SEQRES  40 B  574  THR GLU ASN ARG ASP LEU GLU GLY PHE GLU ASN ALA ILE          
SEQRES  41 B  574  GLU LEU VAL LEU GLU THR GLY PHE ALA VAL THR ALA PHE          
SEQRES  42 B  574  VAL ALA MET LEU LEU ASN ALA ILE MET PRO ALA GLU VAL          
SEQRES  43 B  574  GLU GLU ILE GLY ALA VAL THR PRO MET PRO VAL SER ALA          
SEQRES  44 B  574  HIS ASP ASN ARG ASP GLY GLU ALA GLU TYR GLN SER LYS          
SEQRES  45 B  574  GLN ALA                                                      
HET    XAN  A1001      11                                                       
HET    LMT  A1002      35                                                       
HET    LMT  A1003      28                                                       
HET    XAN  B1001      11                                                       
HET    LMT  B1002      35                                                       
HET    LMT  B1003      28                                                       
HETNAM     XAN XANTHINE                                                         
HETNAM     LMT DODECYL-BETA-D-MALTOSIDE                                         
FORMUL   3  XAN    2(C5 H4 N4 O2)                                               
FORMUL   4  LMT    4(C24 H46 O11)                                               
HELIX    1 AA1 PRO A   75  SER A  104  1                                  30    
HELIX    2 AA2 PRO A  108  THR A  132  1                                  25    
HELIX    3 AA3 PHE A  155  ASN A  171  1                                  17    
HELIX    4 AA4 CYS A  185  LEU A  205  1                                  21    
HELIX    5 AA5 PRO A  210  PHE A  218  1                                   9    
HELIX    6 AA6 PRO A  219  GLY A  244  1                                  26    
HELIX    7 AA7 SER A  268  PHE A  288  1                                  21    
HELIX    8 AA8 CYS A  296  GLY A  313  1                                  18    
HELIX    9 AA9 SER A  316  ALA A  322  1                                   7    
HELIX   10 AB1 MET A  342  SER A  368  1                                  27    
HELIX   11 AB2 GLY A  374  ALA A  398  1                                  25    
HELIX   12 AB3 GLN A  408  ARG A  417  1                                  10    
HELIX   13 AB4 ASN A  420  PHE A  437  1                                  18    
HELIX   14 AB5 LYS A  439  ALA A  446  1                                   8    
HELIX   15 AB6 PRO A  448  ALA A  472  1                                  25    
HELIX   16 AB7 THR A  477  VAL A  497  1                                  21    
HELIX   17 AB8 LEU A  513  THR A  526  1                                  14    
HELIX   18 AB9 THR A  526  MET A  542  1                                  17    
HELIX   19 AC1 PRO B   75  SER B  104  1                                  30    
HELIX   20 AC2 PRO B  108  THR B  132  1                                  25    
HELIX   21 AC3 PHE B  155  ASN B  171  1                                  17    
HELIX   22 AC4 CYS B  185  LEU B  205  1                                  21    
HELIX   23 AC5 PRO B  210  PHE B  218  1                                   9    
HELIX   24 AC6 PRO B  219  GLY B  244  1                                  26    
HELIX   25 AC7 SER B  268  PHE B  288  1                                  21    
HELIX   26 AC8 CYS B  296  GLY B  313  1                                  18    
HELIX   27 AC9 SER B  316  ALA B  322  1                                   7    
HELIX   28 AD1 MET B  342  SER B  368  1                                  27    
HELIX   29 AD2 GLY B  374  ALA B  398  1                                  25    
HELIX   30 AD3 ALA B  407  ARG B  417  1                                  11    
HELIX   31 AD4 ASN B  420  PHE B  437  1                                  18    
HELIX   32 AD5 LYS B  439  ALA B  446  1                                   8    
HELIX   33 AD6 PRO B  448  ALA B  472  1                                  25    
HELIX   34 AD7 THR B  477  VAL B  497  1                                  21    
HELIX   35 AD8 LEU B  513  THR B  526  1                                  14    
HELIX   36 AD9 THR B  526  MET B  542  1                                  17    
SHEET    1 AA1 2 MET A 151  VAL A 153  0                                        
SHEET    2 AA1 2 MET A 403  THR A 405 -1  O  THR A 404   N  GLY A 152           
SHEET    1 AA2 2 MET B 151  VAL B 153  0                                        
SHEET    2 AA2 2 MET B 403  THR B 405 -1  O  THR B 404   N  GLY B 152           
SSBOND   1 CYS A  174    CYS A  185                          1555   1555  2.03  
SSBOND   2 CYS B  174    CYS B  185                          1555   1555  2.04  
CISPEP   1 ILE A  143    GLY A  144          0        -2.42                     
CISPEP   2 GLY A  245    SER A  246          0        -0.88                     
CISPEP   3 GLY B  245    SER B  246          0        -0.66                     
SITE     1 AC1 10 GLY A  93  VAL A 153  SER A 154  PHE A 155                    
SITE     2 AC1 10 GLU A 356  THR A 404  PHE A 406  ALA A 407                    
SITE     3 AC1 10 GLN A 408  LMT A1003                                          
SITE     1 AC2 11 THR A 223  VAL A 227  ALA A 348  ILE A 352                    
SITE     2 AC2 11 CYS A 355  ASP A 360  ALA A 363  ALA A 407                    
SITE     3 AC2 11 LYS A 473  ALA A 529  LMT A1003                               
SITE     1 AC3 11 ALA A  89  SER A 295  VAL A 298  GLU A 356                    
SITE     2 AC3 11 GLN A 408  LEU A 459  SER A 462  SER A 466                    
SITE     3 AC3 11 XAN A1001  LMT A1002  ARG B 478                               
SITE     1 AC4  9 VAL B 153  SER B 154  PHE B 155  GLU B 356                    
SITE     2 AC4  9 THR B 405  PHE B 406  ALA B 407  GLN B 408                    
SITE     3 AC4  9 LMT B1003                                                     
SITE     1 AC5 11 THR B 223  VAL B 227  ALA B 348  ILE B 352                    
SITE     2 AC5 11 CYS B 355  ALA B 407  SER B 466  ILE B 470                    
SITE     3 AC5 11 LYS B 473  ALA B 529  LMT B1003                               
SITE     1 AC6 11 ARG A 478  ALA B  89  SER B 295  VAL B 298                    
SITE     2 AC6 11 GLU B 356  GLN B 408  LEU B 459  SER B 462                    
SITE     3 AC6 11 SER B 466  XAN B1001  LMT B1002                               
CRYST1   75.090  173.830   82.390  90.00 111.11  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013317  0.000000  0.005141        0.00000                         
SCALE2      0.000000  0.005753  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013011        0.00000                         
ATOM      1  N   PRO A  66     -84.505 -27.927  27.784  1.00170.43           N  
ANISOU    1  N   PRO A  66    17452  27283  20020    892   3754   4603       N  
ATOM      2  CA  PRO A  66     -85.618 -27.490  26.934  1.00171.67           C  
ANISOU    2  CA  PRO A  66    17162  27437  20626    895   3758   4758       C  
ATOM      3  C   PRO A  66     -85.146 -26.984  25.571  1.00167.48           C  
ANISOU    3  C   PRO A  66    16736  26515  20384    885   3378   4543       C  
ATOM      4  O   PRO A  66     -84.694 -25.842  25.487  1.00166.14           O  
ANISOU    4  O   PRO A  66    16691  26239  20195   1177   3424   4169       O  
ATOM      5  CB  PRO A  66     -86.245 -26.353  27.746  1.00175.32           C  
ANISOU    5  CB  PRO A  66    17399  28201  21015   1290   4222   4595       C  
ATOM      6  CG  PRO A  66     -85.122 -25.823  28.578  1.00174.07           C  
ANISOU    6  CG  PRO A  66    17681  28032  20425   1533   4320   4172       C  
ATOM      7  CD  PRO A  66     -84.278 -27.014  28.919  1.00172.40           C  
ANISOU    7  CD  PRO A  66    17814  27769  19923   1259   4122   4294       C  
ATOM      8  N   PHE A  67     -85.294 -27.788  24.518  1.00165.86           N  
ANISOU    8  N   PHE A  67    16475  26101  20443    553   3016   4778       N  
ATOM      9  CA  PHE A  67     -84.778 -27.396  23.208  1.00162.02           C  
ANISOU    9  CA  PHE A  67    16129  25257  20174    521   2647   4586       C  
ATOM     10  C   PHE A  67     -85.712 -26.388  22.561  1.00163.51           C  
ANISOU   10  C   PHE A  67    15944  25467  20716    692   2701   4602       C  
ATOM     11  O   PHE A  67     -86.901 -26.646  22.422  1.00166.70           O  
ANISOU   11  O   PHE A  67    15920  26045  21374    591   2766   4937       O  
ATOM     12  CB  PHE A  67     -84.599 -28.613  22.287  1.00160.10           C  
ANISOU   12  CB  PHE A  67    15985  24783  20065    116   2233   4803       C  
ATOM     13  CG  PHE A  67     -83.935 -28.289  20.957  1.00156.20           C  
ANISOU   13  CG  PHE A  67    15693  23936  19719     73   1860   4587       C  
ATOM     14  CD1 PHE A  67     -82.551 -28.100  20.874  1.00152.50           C  
ANISOU   14  CD1 PHE A  67    15666  23249  19029    152   1731   4234       C  
ATOM     15  CD2 PHE A  67     -84.686 -28.180  19.794  1.00156.52           C  
ANISOU   15  CD2 PHE A  67    15478  23881  20112    -52   1637   4746       C  
ATOM     16  CE1 PHE A  67     -81.934 -27.804  19.659  1.00149.25           C  
ANISOU   16  CE1 PHE A  67    15433  22540  18737    106   1420   4050       C  
ATOM     17  CE2 PHE A  67     -84.071 -27.885  18.573  1.00153.26           C  
ANISOU   17  CE2 PHE A  67    15270  23167  19794    -95   1306   4561       C  
ATOM     18  CZ  PHE A  67     -82.694 -27.698  18.509  1.00149.65           C  
ANISOU   18  CZ  PHE A  67    15250  22504  19105    -16   1214   4215       C  
ATOM     19  N   PHE A  68     -85.161 -25.247  22.159  1.00161.43           N  
ANISOU   19  N   PHE A  68    15835  25017  20483    946   2661   4253       N  
ATOM     20  CA  PHE A  68     -85.933 -24.189  21.531  1.00162.80           C  
ANISOU   20  CA  PHE A  68    15700  25165  20993   1147   2690   4243       C  
ATOM     21  C   PHE A  68     -85.799 -24.260  20.017  1.00160.11           C  
ANISOU   21  C   PHE A  68    15401  24522  20912    947   2249   4296       C  
ATOM     22  O   PHE A  68     -84.703 -24.220  19.473  1.00156.34           O  
ANISOU   22  O   PHE A  68    15306  23776  20322    890   2010   4065       O  
ATOM     23  CB  PHE A  68     -85.476 -22.824  22.029  1.00162.80           C  
ANISOU   23  CB  PHE A  68    15841  25126  20888   1557   2921   3840       C  
ATOM     24  CG  PHE A  68     -85.755 -22.584  23.474  1.00166.20           C  
ANISOU   24  CG  PHE A  68    16200  25879  21071   1802   3376   3762       C  
ATOM     25  CD1 PHE A  68     -84.795 -22.865  24.421  1.00165.16           C  
ANISOU   25  CD1 PHE A  68    16439  25797  20515   1823   3477   3551       C  
ATOM     26  CD2 PHE A  68     -86.968 -22.081  23.889  1.00170.74           C  
ANISOU   26  CD2 PHE A  68    16333  26718  21823   2018   3703   3897       C  
ATOM     27  CE1 PHE A  68     -85.029 -22.650  25.756  1.00168.55           C  
ANISOU   27  CE1 PHE A  68    16834  26541  20667   2045   3890   3471       C  
ATOM     28  CE2 PHE A  68     -87.213 -21.859  25.227  1.00174.21           C  
ANISOU   28  CE2 PHE A  68    16720  27475  21996   2254   4148   3807       C  
ATOM     29  CZ  PHE A  68     -86.238 -22.146  26.164  1.00173.11           C  
ANISOU   29  CZ  PHE A  68    16987  27389  21398   2262   4239   3592       C  
ATOM     30  N   GLY A  69     -86.940 -24.326  19.351  1.00162.43           N  
ANISOU   30  N   GLY A  69    15285  24881  21550    852   2154   4600       N  
ATOM     31  CA  GLY A  69     -87.025 -24.392  17.906  1.00160.79           C  
ANISOU   31  CA  GLY A  69    15063  24438  21593    660   1736   4696       C  
ATOM     32  C   GLY A  69     -86.774 -23.068  17.224  1.00159.65           C  
ANISOU   32  C   GLY A  69    14984  24092  21585    923   1666   4465       C  
ATOM     33  O   GLY A  69     -86.445 -22.080  17.874  1.00159.88           O  
ANISOU   33  O   GLY A  69    15100  24124  21524   1255   1930   4194       O  
ATOM     34  N   LEU A  70     -86.845 -23.078  15.899  1.00158.43           N  
ANISOU   34  N   LEU A  70    14832  23739  21625    757   1289   4560       N  
ATOM     35  CA  LEU A  70     -86.628 -21.876  15.104  1.00157.53           C  
ANISOU   35  CA  LEU A  70    14787  23412  21657    963   1174   4399       C  
ATOM     36  C   LEU A  70     -87.562 -20.750  15.520  1.00161.22           C  
ANISOU   36  C   LEU A  70    14877  24009  22372   1329   1449   4427       C  
ATOM     37  O   LEU A  70     -87.126 -19.694  15.984  1.00161.09           O  
ANISOU   37  O   LEU A  70    14996  23909  22304   1653   1661   4141       O  
ATOM     38  CB  LEU A  70     -86.854 -22.165  13.624  1.00156.80           C  
ANISOU   38  CB  LEU A  70    14671  23161  21746    706    730   4589       C  
ATOM     39  CG  LEU A  70     -86.296 -23.477  13.086  1.00154.37           C  
ANISOU   39  CG  LEU A  70    14627  22760  21267    306    427   4643       C  
ATOM     40  CD1 LEU A  70     -86.399 -23.509  11.585  1.00153.74           C  
ANISOU   40  CD1 LEU A  70    14585  22507  21322    113      2   4751       C  
ATOM     41  CD2 LEU A  70     -84.846 -23.687  13.501  1.00150.67           C  
ANISOU   41  CD2 LEU A  70    14646  22150  20450    306    485   4315       C  
ATOM     42  N   ASN A  71     -88.858 -21.001  15.360  1.00164.82           N  
ANISOU   42  N   ASN A  71    14848  24663  23111   1276   1439   4770       N  
ATOM     43  CA  ASN A  71     -89.862 -19.983  15.605  1.00168.82           C  
ANISOU   43  CA  ASN A  71    14934  25294  23915   1623   1665   4837       C  
ATOM     44  C   ASN A  71     -90.639 -20.234  16.884  1.00172.56           C  
ANISOU   44  C   ASN A  71    15065  26128  24370   1749   2097   4939       C  
ATOM     45  O   ASN A  71     -91.617 -20.975  16.910  1.00175.37           O  
ANISOU   45  O   ASN A  71    15022  26720  24891   1562   2094   5285       O  
ATOM     46  CB  ASN A  71     -90.822 -19.870  14.433  1.00170.85           C  
ANISOU   46  CB  ASN A  71    14835  25523  24556   1531   1341   5152       C  
ATOM     47  CG  ASN A  71     -91.884 -18.823  14.659  1.00175.33           C  
ANISOU   47  CG  ASN A  71    14936  26212  25470   1913   1561   5235       C  
ATOM     48  OD1 ASN A  71     -91.631 -17.796  15.293  1.00175.96           O  
ANISOU   48  OD1 ASN A  71    15096  26238  25523   2297   1857   4964       O  
ATOM     49  ND2 ASN A  71     -93.073 -19.056  14.118  1.00178.72           N  
ANISOU   49  ND2 ASN A  71    14872  26791  26242   1817   1400   5602       N  
ATOM     50  N   GLU A  72     -90.156 -19.619  17.948  1.00172.71           N  
ANISOU   50  N   GLU A  72    15260  26193  24171   2054   2467   4629       N  
ATOM     51  CA  GLU A  72     -90.827 -19.592  19.226  1.00176.66           C  
ANISOU   51  CA  GLU A  72    15472  27039  24611   2263   2940   4658       C  
ATOM     52  C   GLU A  72     -90.323 -18.357  19.935  1.00177.03           C  
ANISOU   52  C   GLU A  72    15725  27003  24535   2705   3239   4239       C  
ATOM     53  O   GLU A  72     -89.131 -18.059  19.881  1.00173.39           O  
ANISOU   53  O   GLU A  72    15748  26287  23846   2718   3133   3920       O  
ATOM     54  CB  GLU A  72     -90.523 -20.842  20.039  1.00176.02           C  
ANISOU   54  CB  GLU A  72    15527  27162  24190   1986   3054   4748       C  
ATOM     55  CG  GLU A  72     -91.081 -20.791  21.447  1.00180.14           C  
ANISOU   55  CG  GLU A  72    15820  28061  24564   2208   3578   4752       C  
ATOM     56  CD  GLU A  72     -90.659 -21.983  22.271  1.00179.47           C  
ANISOU   56  CD  GLU A  72    15934  28151  24105   1938   3677   4842       C  
ATOM     57  OE1 GLU A  72     -90.034 -22.906  21.702  1.00176.02           O  
ANISOU   57  OE1 GLU A  72    15766  27533  23581   1573   3324   4926       O  
ATOM     58  OE2 GLU A  72     -90.948 -21.990  23.486  1.00182.64           O  
ANISOU   58  OE2 GLU A  72    16232  28868  24293   2102   4110   4826       O  
ATOM     59  N   LYS A  73     -91.197 -17.622  20.603  1.00181.63           N  
ANISOU   59  N   LYS A  73    15947  27790  25274   3071   3613   4221       N  
ATOM     60  CA  LYS A  73     -90.677 -16.485  21.326  1.00182.21           C  
ANISOU   60  CA  LYS A  73    16259  27765  25210   3484   3892   3785       C  
ATOM     61  C   LYS A  73     -90.056 -17.011  22.601  1.00181.85           C  
ANISOU   61  C   LYS A  73    16490  27928  24675   3459   4185   3596       C  
ATOM     62  O   LYS A  73     -90.660 -17.792  23.342  1.00184.45           O  
ANISOU   62  O   LYS A  73    16578  28624  24881   3365   4435   3818       O  
ATOM     63  CB  LYS A  73     -91.753 -15.437  21.623  1.00187.52           C  
ANISOU   63  CB  LYS A  73    16491  28552  26205   3933   4202   3770       C  
ATOM     64  CG  LYS A  73     -91.182 -14.033  21.850  1.00187.72           C  
ANISOU   64  CG  LYS A  73    16796  28292  26235   4353   4317   3312       C  
ATOM     65  CD  LYS A  73     -92.261 -13.051  22.303  1.00193.57           C  
ANISOU   65  CD  LYS A  73    17106  29165  27277   4836   4677   3268       C  
ATOM     66  CE  LYS A  73     -91.675 -11.666  22.558  1.00194.08           C  
ANISOU   66  CE  LYS A  73    17480  28906  27355   5249   4782   2792       C  
ATOM     67  NZ  LYS A  73     -92.710 -10.660  22.950  1.00200.05           N  
ANISOU   67  NZ  LYS A  73    17832  29742  28436   5757   5121   2720       N  
ATOM     68  N   ILE A  74     -88.827 -16.572  22.829  1.00178.78           N  
ANISOU   68  N   ILE A  74    16612  27301  24013   3532   4136   3199       N  
ATOM     69  CA  ILE A  74     -88.075 -16.928  24.013  1.00178.29           C  
ANISOU   69  CA  ILE A  74    16880  27396  23466   3537   4366   2965       C  
ATOM     70  C   ILE A  74     -87.939 -15.623  24.770  1.00180.81           C  
ANISOU   70  C   ILE A  74    17306  27669  23725   4004   4676   2534       C  
ATOM     71  O   ILE A  74     -88.157 -14.559  24.182  1.00181.60           O  
ANISOU   71  O   ILE A  74    17322  27520  24159   4246   4612   2417       O  
ATOM     72  CB  ILE A  74     -86.700 -17.529  23.665  1.00172.88           C  
ANISOU   72  CB  ILE A  74    16699  26470  22515   3226   4023   2843       C  
ATOM     73  CG1 ILE A  74     -85.847 -16.517  22.900  1.00170.02           C  
ANISOU   73  CG1 ILE A  74    16638  25681  22282   3335   3775   2534       C  
ATOM     74  CG2 ILE A  74     -86.865 -18.791  22.840  1.00170.71           C  
ANISOU   74  CG2 ILE A  74    16329  26202  22331   2782   3700   3244       C  
ATOM     75  CD1 ILE A  74     -84.458 -17.021  22.568  1.00165.05           C  
ANISOU   75  CD1 ILE A  74    16481  24827  21404   3060   3468   2388       C  
ATOM     76  N   PRO A  75     -87.606 -15.685  26.069  1.00182.44           N  
ANISOU   76  N   PRO A  75    17703  28108  23510   4137   5005   2300       N  
ATOM     77  CA  PRO A  75     -87.387 -14.438  26.808  1.00184.96           C  
ANISOU   77  CA  PRO A  75    18181  28356  23738   4577   5279   1833       C  
ATOM     78  C   PRO A  75     -86.423 -13.513  26.074  1.00181.69           C  
ANISOU   78  C   PRO A  75    18121  27447  23468   4635   4968   1511       C  
ATOM     79  O   PRO A  75     -85.294 -13.906  25.812  1.00177.33           O  
ANISOU   79  O   PRO A  75    17953  26708  22716   4375   4682   1416       O  
ATOM     80  CB  PRO A  75     -86.796 -14.920  28.132  1.00185.63           C  
ANISOU   80  CB  PRO A  75    18561  28715  23253   4567   5523   1639       C  
ATOM     81  CG  PRO A  75     -87.405 -16.265  28.323  1.00186.32           C  
ANISOU   81  CG  PRO A  75    18390  29167  23237   4263   5589   2107       C  
ATOM     82  CD  PRO A  75     -87.509 -16.866  26.946  1.00182.77           C  
ANISOU   82  CD  PRO A  75    17803  28497  23145   3911   5155   2464       C  
ATOM     83  N   VAL A  76     -86.868 -12.309  25.729  1.00184.02           N  
ANISOU   83  N   VAL A  76    18273  27524  24121   4968   5019   1365       N  
ATOM     84  CA  VAL A  76     -86.048 -11.409  24.925  1.00181.32           C  
ANISOU   84  CA  VAL A  76    18229  26690  23973   5001   4713   1125       C  
ATOM     85  C   VAL A  76     -84.749 -11.071  25.647  1.00179.69           C  
ANISOU   85  C   VAL A  76    18545  26343  23386   5033   4720    653       C  
ATOM     86  O   VAL A  76     -83.790 -10.623  25.025  1.00176.53           O  
ANISOU   86  O   VAL A  76    18459  25563  23051   4935   4425    476       O  
ATOM     87  CB  VAL A  76     -86.802 -10.129  24.569  1.00184.93           C  
ANISOU   87  CB  VAL A  76    18445  26936  24884   5395   4800   1047       C  
ATOM     88  CG1 VAL A  76     -87.935 -10.447  23.609  1.00185.89           C  
ANISOU   88  CG1 VAL A  76    18073  27133  25426   5311   4671   1536       C  
ATOM     89  CG2 VAL A  76     -87.323  -9.459  25.826  1.00190.33           C  
ANISOU   89  CG2 VAL A  76    19036  27827  25452   5841   5284    742       C  
ATOM     90  N   LEU A  77     -84.730 -11.273  26.962  1.00182.20           N  
ANISOU   90  N   LEU A  77    18946  26979  23302   5167   5056    457       N  
ATOM     91  CA  LEU A  77     -83.481 -11.252  27.709  1.00180.55           C  
ANISOU   91  CA  LEU A  77    19223  26717  22659   5120   5025     69       C  
ATOM     92  C   LEU A  77     -82.611 -12.412  27.252  1.00175.39           C  
ANISOU   92  C   LEU A  77    18773  26052  21815   4662   4688    275       C  
ATOM     93  O   LEU A  77     -81.430 -12.235  26.969  1.00172.05           O  
ANISOU   93  O   LEU A  77    18713  25347  21310   4526   4419     51       O  
ATOM     94  CB  LEU A  77     -83.722 -11.355  29.215  1.00184.66           C  
ANISOU   94  CB  LEU A  77    19779  27641  22744   5338   5450   -131       C  
ATOM     95  CG  LEU A  77     -82.435 -11.414  30.044  1.00183.27           C  
ANISOU   95  CG  LEU A  77    20104  27449  22080   5274   5390   -515       C  
ATOM     96  CD1 LEU A  77     -81.662 -10.113  29.900  1.00183.14           C  
ANISOU   96  CD1 LEU A  77    20394  26990  22199   5468   5259   -998       C  
ATOM     97  CD2 LEU A  77     -82.699 -11.739  31.507  1.00187.31           C  
ANISOU   97  CD2 LEU A  77    20654  28425  22092   5429   5788   -633       C  
ATOM     98  N   LEU A  78     -83.205 -13.601  27.182  1.00175.05           N  
ANISOU   98  N   LEU A  78    18483  26310  21719   4425   4705    703       N  
ATOM     99  CA  LEU A  78     -82.496 -14.778  26.695  1.00170.56           C  
ANISOU   99  CA  LEU A  78    18076  25719  21010   3999   4385    928       C  
ATOM    100  C   LEU A  78     -82.050 -14.597  25.249  1.00166.62           C  
ANISOU  100  C   LEU A  78    17637  24821  20848   3807   3975   1008       C  
ATOM    101  O   LEU A  78     -80.892 -14.848  24.928  1.00162.84           O  
ANISOU  101  O   LEU A  78    17491  24144  20234   3598   3705    883       O  
ATOM    102  CB  LEU A  78     -83.362 -16.033  26.824  1.00171.59           C  
ANISOU  102  CB  LEU A  78    17895  26209  21090   3785   4477   1394       C  
ATOM    103  CG  LEU A  78     -82.734 -17.303  26.248  1.00167.34           C  
ANISOU  103  CG  LEU A  78    17505  25618  20458   3347   4134   1649       C  
ATOM    104  CD1 LEU A  78     -81.447 -17.653  26.978  1.00165.33           C  
ANISOU  104  CD1 LEU A  78    17698  25360  19760   3265   4067   1386       C  
ATOM    105  CD2 LEU A  78     -83.712 -18.462  26.311  1.00168.94           C  
ANISOU  105  CD2 LEU A  78    17370  26133  20687   3134   4216   2126       C  
ATOM    106  N   ALA A  79     -82.963 -14.169  24.381  1.00167.76           N  
ANISOU  106  N   ALA A  79    17455  24865  21421   3880   3930   1223       N  
ATOM    107  CA  ALA A  79     -82.630 -13.932  22.979  1.00164.60           C  
ANISOU  107  CA  ALA A  79    17105  24107  21330   3714   3552   1322       C  
ATOM    108  C   ALA A  79     -81.500 -12.912  22.831  1.00162.95           C  
ANISOU  108  C   ALA A  79    17274  23526  21115   3813   3426    915       C  
ATOM    109  O   ALA A  79     -80.628 -13.064  21.979  1.00159.21           O  
ANISOU  109  O   ALA A  79    17022  22805  20665   3572   3109    917       O  
ATOM    110  CB  ALA A  79     -83.854 -13.476  22.214  1.00167.04           C  
ANISOU  110  CB  ALA A  79    16996  24384  22088   3840   3548   1594       C  
ATOM    111  N   PHE A  80     -81.537 -11.860  23.646  1.00166.09           N  
ANISOU  111  N   PHE A  80    17736  23879  21491   4167   3680    566       N  
ATOM    112  CA  PHE A  80     -80.465 -10.863  23.661  1.00165.16           C  
ANISOU  112  CA  PHE A  80    17982  23408  21363   4261   3579    151       C  
ATOM    113  C   PHE A  80     -79.129 -11.434  24.110  1.00162.06           C  
ANISOU  113  C   PHE A  80    17973  23028  20574   4037   3452    -60       C  
ATOM    114  O   PHE A  80     -78.105 -11.161  23.500  1.00159.17           O  
ANISOU  114  O   PHE A  80    17861  22363  20255   3884   3191   -193       O  
ATOM    115  CB  PHE A  80     -80.835  -9.685  24.566  1.00169.78           C  
ANISOU  115  CB  PHE A  80    18564  23959  21984   4697   3892   -207       C  
ATOM    116  CG  PHE A  80     -79.684  -8.762  24.858  1.00169.37           C  
ANISOU  116  CG  PHE A  80    18918  23584  21851   4777   3813   -680       C  
ATOM    117  CD1 PHE A  80     -79.304  -7.798  23.939  1.00168.57           C  
ANISOU  117  CD1 PHE A  80    18920  23030  22101   4792   3592   -758       C  
ATOM    118  CD2 PHE A  80     -78.988  -8.850  26.057  1.00170.13           C  
ANISOU  118  CD2 PHE A  80    19290  23831  21519   4827   3949  -1035       C  
ATOM    119  CE1 PHE A  80     -78.245  -6.944  24.203  1.00168.50           C  
ANISOU  119  CE1 PHE A  80    19269  22709  22045   4837   3510  -1182       C  
ATOM    120  CE2 PHE A  80     -77.932  -8.001  26.328  1.00170.05           C  
ANISOU  120  CE2 PHE A  80    19640  23522  21451   4880   3850  -1476       C  
ATOM    121  CZ  PHE A  80     -77.560  -7.046  25.400  1.00169.24           C  
ANISOU  121  CZ  PHE A  80    19623  22954  21728   4879   3633  -1551       C  
ATOM    122  N   ILE A  81     -79.147 -12.198  25.197  1.00163.04           N  
ANISOU  122  N   ILE A  81    18127  23507  20312   4027   3645    -83       N  
ATOM    123  CA  ILE A  81     -77.937 -12.788  25.759  1.00160.69           C  
ANISOU  123  CA  ILE A  81    18174  23264  19619   3844   3533   -270       C  
ATOM    124  C   ILE A  81     -77.297 -13.780  24.803  1.00156.08           C  
ANISOU  124  C   ILE A  81    17660  22592  19051   3456   3193    -16       C  
ATOM    125  O   ILE A  81     -76.095 -13.729  24.563  1.00153.34           O  
ANISOU  125  O   ILE A  81    17597  22042  18623   3313   2969   -209       O  
ATOM    126  CB  ILE A  81     -78.220 -13.481  27.101  1.00163.15           C  
ANISOU  126  CB  ILE A  81    18480  24005  19507   3910   3811   -274       C  
ATOM    127  CG1 ILE A  81     -78.262 -12.438  28.211  1.00167.27           C  
ANISOU  127  CG1 ILE A  81    19121  24569  19866   4276   4098   -706       C  
ATOM    128  CG2 ILE A  81     -77.123 -14.454  27.445  1.00160.31           C  
ANISOU  128  CG2 ILE A  81    18402  23730  18780   3646   3627   -296       C  
ATOM    129  CD1 ILE A  81     -78.712 -12.987  29.535  1.00170.61           C  
ANISOU  129  CD1 ILE A  81    19511  25447  19866   4387   4425   -701       C  
ATOM    130  N   LEU A  82     -78.094 -14.688  24.259  1.00155.49           N  
ANISOU  130  N   LEU A  82    17321  22672  19088   3287   3153    408       N  
ATOM    131  CA  LEU A  82     -77.574 -15.618  23.272  1.00151.51           C  
ANISOU  131  CA  LEU A  82    16879  22065  18621   2934   2829    639       C  
ATOM    132  C   LEU A  82     -77.140 -14.847  22.030  1.00149.46           C  
ANISOU  132  C   LEU A  82    16691  21425  18671   2885   2583    584       C  
ATOM    133  O   LEU A  82     -76.183 -15.229  21.360  1.00146.10           O  
ANISOU  133  O   LEU A  82    16464  20838  18209   2649   2322    571       O  
ATOM    134  CB  LEU A  82     -78.602 -16.700  22.923  1.00151.84           C  
ANISOU  134  CB  LEU A  82    16617  22330  18747   2759   2824   1096       C  
ATOM    135  CG  LEU A  82     -78.860 -17.735  24.027  1.00153.33           C  
ANISOU  135  CG  LEU A  82    16772  22883  18605   2704   3012   1225       C  
ATOM    136  CD1 LEU A  82     -79.844 -18.805  23.575  1.00153.74           C  
ANISOU  136  CD1 LEU A  82    16519  23105  18789   2486   2969   1693       C  
ATOM    137  CD2 LEU A  82     -77.561 -18.371  24.495  1.00150.89           C  
ANISOU  137  CD2 LEU A  82    16825  22563  17945   2553   2874   1053       C  
ATOM    138  N   GLY A  83     -77.838 -13.757  21.730  1.00151.77           N  
ANISOU  138  N   GLY A  83    16820  21577  19268   3116   2673    559       N  
ATOM    139  CA  GLY A  83     -77.417 -12.861  20.669  1.00150.51           C  
ANISOU  139  CA  GLY A  83    16753  21043  19392   3103   2466    493       C  
ATOM    140  C   GLY A  83     -76.017 -12.333  20.924  1.00148.98           C  
ANISOU  140  C   GLY A  83    16924  20629  19052   3082   2380    106       C  
ATOM    141  O   GLY A  83     -75.206 -12.198  20.007  1.00146.38           O  
ANISOU  141  O   GLY A  83    16750  20053  18815   2896   2137     97       O  
ATOM    142  N   LEU A  84     -75.738 -12.044  22.190  1.00150.89           N  
ANISOU  142  N   LEU A  84    17297  20982  19053   3266   2583   -213       N  
ATOM    143  CA  LEU A  84     -74.435 -11.556  22.610  1.00150.03           C  
ANISOU  143  CA  LEU A  84    17520  20700  18786   3252   2505   -606       C  
ATOM    144  C   LEU A  84     -73.391 -12.639  22.464  1.00146.43           C  
ANISOU  144  C   LEU A  84    17236  20317  18083   2944   2297   -562       C  
ATOM    145  O   LEU A  84     -72.326 -12.391  21.921  1.00144.27           O  
ANISOU  145  O   LEU A  84    17151  19809  17856   2796   2092   -696       O  
ATOM    146  CB  LEU A  84     -74.479 -11.074  24.058  1.00153.42           C  
ANISOU  146  CB  LEU A  84    18046  21274  18974   3526   2766   -954       C  
ATOM    147  CG  LEU A  84     -73.170 -10.508  24.596  1.00153.18           C  
ANISOU  147  CG  LEU A  84    18354  21071  18778   3520   2673  -1391       C  
ATOM    148  CD1 LEU A  84     -72.815  -9.250  23.831  1.00153.40           C  
ANISOU  148  CD1 LEU A  84    18461  20657  19167   3564   2549  -1550       C  
ATOM    149  CD2 LEU A  84     -73.270 -10.238  26.083  1.00156.74           C  
ANISOU  149  CD2 LEU A  84    18909  21732  18911   3770   2922  -1716       C  
ATOM    150  N   GLN A  85     -73.711 -13.846  22.923  1.00146.03           N  
ANISOU  150  N   GLN A  85    17107  20585  17792   2848   2351   -357       N  
ATOM    151  CA  GLN A  85     -72.781 -14.967  22.826  1.00142.96           C  
ANISOU  151  CA  GLN A  85    16872  20265  17181   2578   2154   -298       C  
ATOM    152  C   GLN A  85     -72.420 -15.255  21.377  1.00139.78           C  
ANISOU  152  C   GLN A  85    16464  19649  16996   2330   1886   -105       C  
ATOM    153  O   GLN A  85     -71.258 -15.512  21.058  1.00137.35           O  
ANISOU  153  O   GLN A  85    16348  19226  16611   2161   1696   -221       O  
ATOM    154  CB  GLN A  85     -73.361 -16.222  23.482  1.00143.54           C  
ANISOU  154  CB  GLN A  85    16839  20688  17010   2515   2256    -47       C  
ATOM    155  CG  GLN A  85     -72.469 -17.445  23.320  1.00140.61           C  
ANISOU  155  CG  GLN A  85    16617  20358  16449   2247   2036     46       C  
ATOM    156  CD  GLN A  85     -72.934 -18.640  24.121  1.00141.63           C  
ANISOU  156  CD  GLN A  85    16687  20807  16319   2189   2135    273       C  
ATOM    157  OE1 GLN A  85     -74.002 -18.617  24.733  1.00144.50           O  
ANISOU  157  OE1 GLN A  85    16865  21392  16647   2325   2381    402       O  
ATOM    158  NE2 GLN A  85     -72.139 -19.705  24.103  1.00139.53           N  
ANISOU  158  NE2 GLN A  85    16569  20564  15883   1987   1945    339       N  
ATOM    159  N   HIS A  86     -73.415 -15.198  20.500  1.00140.10           N  
ANISOU  159  N   HIS A  86    16277  19650  17303   2316   1872    184       N  
ATOM    160  CA  HIS A  86     -73.169 -15.369  19.075  1.00137.61           C  
ANISOU  160  CA  HIS A  86    15964  19141  17181   2097   1624    365       C  
ATOM    161  C   HIS A  86     -72.302 -14.236  18.531  1.00137.02           C  
ANISOU  161  C   HIS A  86    16057  18744  17258   2115   1527    131       C  
ATOM    162  O   HIS A  86     -71.351 -14.476  17.771  1.00134.52           O  
ANISOU  162  O   HIS A  86    15887  18294  16929   1908   1332    112       O  
ATOM    163  CB  HIS A  86     -74.486 -15.449  18.298  1.00138.69           C  
ANISOU  163  CB  HIS A  86    15814  19312  17569   2094   1615    720       C  
ATOM    164  CG  HIS A  86     -75.274 -16.691  18.565  1.00139.01           C  
ANISOU  164  CG  HIS A  86    15678  19636  17505   1988   1651   1007       C  
ATOM    165  ND1 HIS A  86     -74.704 -17.948  18.592  1.00136.87           N  
ANISOU  165  ND1 HIS A  86    15526  19463  17017   1756   1523   1078       N  
ATOM    166  CD2 HIS A  86     -76.598 -16.880  18.789  1.00141.50           C  
ANISOU  166  CD2 HIS A  86    15691  20146  17926   2073   1793   1255       C  
ATOM    167  CE1 HIS A  86     -75.635 -18.848  18.838  1.00138.03           C  
ANISOU  167  CE1 HIS A  86    15473  19834  17139   1689   1580   1360       C  
ATOM    168  NE2 HIS A  86     -76.795 -18.228  18.960  1.00140.84           N  
ANISOU  168  NE2 HIS A  86    15558  20267  17686   1870   1748   1476       N  
ATOM    169  N   ALA A  87     -72.640 -13.010  18.924  1.00139.62           N  
ANISOU  169  N   ALA A  87    16362  18948  17739   2365   1673    -45       N  
ATOM    170  CA  ALA A  87     -71.897 -11.832  18.500  1.00139.73           C  
ANISOU  170  CA  ALA A  87    16533  18628  17931   2392   1596   -264       C  
ATOM    171  C   ALA A  87     -70.420 -11.983  18.834  1.00137.93           C  
ANISOU  171  C   ALA A  87    16561  18349  17498   2252   1495   -546       C  
ATOM    172  O   ALA A  87     -69.559 -11.832  17.969  1.00136.10           O  
ANISOU  172  O   ALA A  87    16438  17923  17350   2067   1322   -555       O  
ATOM    173  CB  ALA A  87     -72.455 -10.594  19.152  1.00143.29           C  
ANISOU  173  CB  ALA A  87    16946  18962  18538   2708   1787   -464       C  
ATOM    174  N   LEU A  88     -70.139 -12.318  20.089  1.00138.70           N  
ANISOU  174  N   LEU A  88    16741  18642  17315   2338   1604   -760       N  
ATOM    175  CA  LEU A  88     -68.777 -12.495  20.555  1.00137.46           C  
ANISOU  175  CA  LEU A  88    16805  18473  16952   2228   1500  -1033       C  
ATOM    176  C   LEU A  88     -68.133 -13.653  19.834  1.00134.19           C  
ANISOU  176  C   LEU A  88    16415  18125  16446   1955   1311   -849       C  
ATOM    177  O   LEU A  88     -66.950 -13.620  19.525  1.00132.67           O  
ANISOU  177  O   LEU A  88    16359  17812  16239   1808   1164   -994       O  
ATOM    178  CB  LEU A  88     -68.747 -12.762  22.055  1.00139.25           C  
ANISOU  178  CB  LEU A  88    17104  18947  16856   2377   1642  -1246       C  
ATOM    179  CG  LEU A  88     -69.200 -11.632  22.964  1.00142.92           C  
ANISOU  179  CG  LEU A  88    17598  19365  17341   2668   1842  -1525       C  
ATOM    180  CD1 LEU A  88     -69.131 -12.073  24.413  1.00144.68           C  
ANISOU  180  CD1 LEU A  88    17912  19889  17171   2785   1973  -1708       C  
ATOM    181  CD2 LEU A  88     -68.354 -10.405  22.716  1.00143.53           C  
ANISOU  181  CD2 LEU A  88    17833  19087  17616   2671   1741  -1829       C  
ATOM    182  N   ALA A  89     -68.932 -14.669  19.541  1.00134.23           N  
ANISOU  182  N   ALA A  89    16278  18316  16409   1887   1315   -529       N  
ATOM    183  CA  ALA A  89     -68.412 -15.881  18.932  1.00131.51           C  
ANISOU  183  CA  ALA A  89    15966  18039  15965   1648   1143   -363       C  
ATOM    184  C   ALA A  89     -67.851 -15.607  17.539  1.00129.70           C  
ANISOU  184  C   ALA A  89    15775  17577  15929   1473    974   -304       C  
ATOM    185  O   ALA A  89     -66.725 -16.011  17.215  1.00127.88           O  
ANISOU  185  O   ALA A  89    15666  17302  15621   1317    840   -399       O  
ATOM    186  CB  ALA A  89     -69.501 -16.942  18.863  1.00133.09           C  
ANISOU  186  CB  ALA A  89    15999  18447  16121   1604   1174    -27       C  
ATOM    187  N   MET A  90     -68.639 -14.912  16.726  1.00129.65           N  
ANISOU  187  N   MET A  90    15657  17434  16171   1507    985   -141       N  
ATOM    188  CA  MET A  90     -68.252 -14.629  15.350  1.00128.38           C  
ANISOU  188  CA  MET A  90    15531  17074  16174   1342    836    -35       C  
ATOM    189  C   MET A  90     -67.405 -13.371  15.221  1.00129.05           C  
ANISOU  189  C   MET A  90    15736  16898  16398   1365    831   -272       C  
ATOM    190  O   MET A  90     -66.860 -13.091  14.149  1.00128.16           O  
ANISOU  190  O   MET A  90    15680  16622  16392   1209    721   -210       O  
ATOM    191  CB  MET A  90     -69.487 -14.506  14.476  1.00129.18           C  
ANISOU  191  CB  MET A  90    15462  17152  16470   1351    813    286       C  
ATOM    192  CG  MET A  90     -70.338 -13.311  14.811  1.00131.94           C  
ANISOU  192  CG  MET A  90    15703  17395  17034   1593    949    266       C  
ATOM    193  SD  MET A  90     -71.798 -13.290  13.780  1.00133.10           S  
ANISOU  193  SD  MET A  90    15611  17546  17414   1602    887    676       S  
ATOM    194  CE  MET A  90     -71.091 -12.862  12.199  1.00131.82           C  
ANISOU  194  CE  MET A  90    15583  17135  17367   1389    674    780       C  
ATOM    195  N   LEU A  91     -67.328 -12.602  16.305  1.00130.95           N  
ANISOU  195  N   LEU A  91    16020  17099  16635   1553    954   -537       N  
ATOM    196  CA  LEU A  91     -66.565 -11.351  16.337  1.00132.14           C  
ANISOU  196  CA  LEU A  91    16291  16978  16939   1580    947   -791       C  
ATOM    197  C   LEU A  91     -65.151 -11.464  15.781  1.00130.38           C  
ANISOU  197  C   LEU A  91    16191  16661  16687   1348    807   -893       C  
ATOM    198  O   LEU A  91     -64.764 -10.702  14.897  1.00130.61           O  
ANISOU  198  O   LEU A  91    16257  16453  16915   1246    747   -857       O  
ATOM    199  CB  LEU A  91     -66.479 -10.834  17.772  1.00134.30           C  
ANISOU  199  CB  LEU A  91    16633  17282  17114   1787   1073  -1124       C  
ATOM    200  CG  LEU A  91     -65.640  -9.573  17.983  1.00135.95           C  
ANISOU  200  CG  LEU A  91    16983  17200  17470   1809   1049  -1439       C  
ATOM    201  CD1 LEU A  91     -66.253  -8.387  17.253  1.00137.79           C  
ANISOU  201  CD1 LEU A  91    17176  17126  18050   1891   1071  -1336       C  
ATOM    202  CD2 LEU A  91     -65.487  -9.284  19.470  1.00138.08           C  
ANISOU  202  CD2 LEU A  91    17347  17553  17564   1995   1147  -1796       C  
ATOM    203  N   ALA A  92     -64.399 -12.431  16.297  1.00130.65           N  
ANISOU  203  N   ALA A  92    16276  16887  16477   1267    760  -1002       N  
ATOM    204  CA  ALA A  92     -63.013 -12.633  15.899  1.00129.24           C  
ANISOU  204  CA  ALA A  92    16182  16661  16263   1069    641  -1122       C  
ATOM    205  C   ALA A  92     -62.896 -12.972  14.419  1.00127.63           C  
ANISOU  205  C   ALA A  92    15950  16403  16141    873    556   -867       C  
ATOM    206  O   ALA A  92     -62.123 -12.349  13.686  1.00127.72           O  
ANISOU  206  O   ALA A  92    16005  16238  16285    739    511   -901       O  
ATOM    207  CB  ALA A  92     -62.381 -13.726  16.742  1.00130.12           C  
ANISOU  207  CB  ALA A  92    16331  17007  16102   1054    597  -1246       C  
ATOM    208  N   GLY A  93     -63.695 -13.937  13.978  1.00126.06           N  
ANISOU  208  N   GLY A  93    15680  16358  15859    850    537   -607       N  
ATOM    209  CA  GLY A  93     -63.647 -14.403  12.605  1.00124.73           C  
ANISOU  209  CA  GLY A  93    15505  16174  15713    669    446   -377       C  
ATOM    210  C   GLY A  93     -64.043 -13.339  11.599  1.00125.87           C  
ANISOU  210  C   GLY A  93    15637  16105  16083    638    441   -219       C  
ATOM    211  O   GLY A  93     -63.594 -13.375  10.453  1.00125.26           O  
ANISOU  211  O   GLY A  93    15600  15969  16023    465    372   -103       O  
ATOM    212  N   VAL A  94     -64.916 -12.421  12.020  1.00127.69           N  
ANISOU  212  N   VAL A  94    15813  16227  16477    816    517   -203       N  
ATOM    213  CA  VAL A  94     -65.344 -11.290  11.187  1.00129.31           C  
ANISOU  213  CA  VAL A  94    16007  16193  16931    826    505    -50       C  
ATOM    214  C   VAL A  94     -64.315 -10.160  11.148  1.00130.42           C  
ANISOU  214  C   VAL A  94    16257  16077  17220    768    513   -246       C  
ATOM    215  O   VAL A  94     -64.034  -9.590  10.091  1.00130.92           O  
ANISOU  215  O   VAL A  94    16362  15970  17411    632    460   -101       O  
ATOM    216  CB  VAL A  94     -66.690 -10.725  11.673  1.00130.14           C  
ANISOU  216  CB  VAL A  94    15995  16263  17189   1068    586     36       C  
ATOM    217  CG1 VAL A  94     -67.034  -9.443  10.933  1.00132.24           C  
ANISOU  217  CG1 VAL A  94    16265  16237  17745   1109    563    166       C  
ATOM    218  CG2 VAL A  94     -67.782 -11.759  11.490  1.00129.45           C  
ANISOU  218  CG2 VAL A  94    15766  16409  17008   1084    561    294       C  
ATOM    219  N   VAL A  95     -63.779  -9.840  12.320  1.00130.15           N  
ANISOU  219  N   VAL A  95    16269  16020  17163    863    573   -567       N  
ATOM    220  CA  VAL A  95     -62.812  -8.759  12.508  1.00131.63           C  
ANISOU  220  CA  VAL A  95    16552  15957  17504    812    570   -800       C  
ATOM    221  C   VAL A  95     -61.444  -9.019  11.864  1.00130.40           C  
ANISOU  221  C   VAL A  95    16445  15803  17295    549    500   -842       C  
ATOM    222  O   VAL A  95     -60.833  -8.108  11.293  1.00131.66           O  
ANISOU  222  O   VAL A  95    16655  15728  17644    421    480   -842       O  
ATOM    223  CB  VAL A  95     -62.616  -8.482  14.020  1.00132.89           C  
ANISOU  223  CB  VAL A  95    16754  16133  17604    983    631  -1160       C  
ATOM    224  CG1 VAL A  95     -61.245  -7.882  14.311  1.00133.68           C  
ANISOU  224  CG1 VAL A  95    16949  16079  17763    851    577  -1450       C  
ATOM    225  CG2 VAL A  95     -63.738  -7.598  14.540  1.00135.44           C  
ANISOU  225  CG2 VAL A  95    17055  16314  18091   1244    727  -1184       C  
ATOM    226  N   THR A  96     -60.962 -10.254  11.968  1.00128.95           N  
ANISOU  226  N   THR A  96    16242  15881  16871    474    469   -872       N  
ATOM    227  CA  THR A  96     -59.581 -10.549  11.611  1.00128.11           C  
ANISOU  227  CA  THR A  96    16157  15809  16709    270    422   -978       C  
ATOM    228  C   THR A  96     -59.192 -10.314  10.126  1.00128.09           C  
ANISOU  228  C   THR A  96    16164  15712  16792     56    407   -756       C  
ATOM    229  O   THR A  96     -58.200  -9.627   9.873  1.00129.18           O  
ANISOU  229  O   THR A  96    16320  15707  17054    -90    409   -850       O  
ATOM    230  CB  THR A  96     -59.236 -12.002  12.022  1.00128.17           C  
ANISOU  230  CB  THR A  96    16139  16110  16451    268    387  -1039       C  
ATOM    231  OG1 THR A  96     -59.097 -12.069  13.448  1.00128.69           O  
ANISOU  231  OG1 THR A  96    16218  16251  16427    413    390  -1301       O  
ATOM    232  CG2 THR A  96     -57.944 -12.440  11.391  1.00127.35           C  
ANISOU  232  CG2 THR A  96    16025  16061  16300     71    348  -1089       C  
ATOM    233  N   PRO A  97     -59.971 -10.819   9.146  1.00126.27           N  
ANISOU  233  N   PRO A  97    15922  15559  16494     26    389   -458       N  
ATOM    234  CA  PRO A  97     -59.556 -10.600   7.747  1.00126.59           C  
ANISOU  234  CA  PRO A  97    15996  15539  16565   -180    379   -255       C  
ATOM    235  C   PRO A  97     -59.378  -9.140   7.301  1.00129.01           C  
ANISOU  235  C   PRO A  97    16344  15543  17132   -253    400   -185       C  
ATOM    236  O   PRO A  97     -58.483  -8.898   6.490  1.00129.58           O  
ANISOU  236  O   PRO A  97    16440  15574  17223   -459    420   -132       O  
ATOM    237  CB  PRO A  97     -60.673 -11.269   6.941  1.00125.81           C  
ANISOU  237  CB  PRO A  97    15890  15557  16355   -160    329     43       C  
ATOM    238  CG  PRO A  97     -61.181 -12.297   7.829  1.00124.32           C  
ANISOU  238  CG  PRO A  97    15653  15565  16020    -21    314    -44       C  
ATOM    239  CD  PRO A  97     -61.116 -11.740   9.218  1.00125.09           C  
ANISOU  239  CD  PRO A  97    15731  15590  16209    141    367   -299       C  
ATOM    240  N   PRO A  98     -60.239  -8.203   7.746  1.00130.68           N  
ANISOU  240  N   PRO A  98    16563  15544  17545    -90    402   -161       N  
ATOM    241  CA  PRO A  98     -59.897  -6.811   7.446  1.00133.27           C  
ANISOU  241  CA  PRO A  98    16946  15542  18147   -167    411   -136       C  
ATOM    242  C   PRO A  98     -58.523  -6.428   7.967  1.00133.94           C  
ANISOU  242  C   PRO A  98    17043  15546  18302   -299    432   -427       C  
ATOM    243  O   PRO A  98     -57.759  -5.804   7.240  1.00135.33           O  
ANISOU  243  O   PRO A  98    17245  15573  18600   -509    442   -345       O  
ATOM    244  CB  PRO A  98     -60.984  -6.023   8.173  1.00134.96           C  
ANISOU  244  CB  PRO A  98    17159  15562  18556     89    416   -167       C  
ATOM    245  CG  PRO A  98     -62.153  -6.911   8.125  1.00133.51           C  
ANISOU  245  CG  PRO A  98    16903  15606  18219    235    403      4       C  
ATOM    246  CD  PRO A  98     -61.598  -8.303   8.308  1.00130.75           C  
ANISOU  246  CD  PRO A  98    16525  15585  17570    152    401   -100       C  
ATOM    247  N   LEU A  99     -58.215  -6.798   9.204  1.00133.24           N  
ANISOU  247  N   LEU A  99    16930  15562  18133   -189    431   -747       N  
ATOM    248  CA  LEU A  99     -56.906  -6.501   9.768  1.00134.04           C  
ANISOU  248  CA  LEU A  99    17023  15612  18293   -315    418  -1038       C  
ATOM    249  C   LEU A  99     -55.787  -7.087   8.928  1.00133.10           C  
ANISOU  249  C   LEU A  99    16847  15652  18075   -561    431   -974       C  
ATOM    250  O   LEU A  99     -54.789  -6.424   8.662  1.00134.75           O  
ANISOU  250  O   LEU A  99    17037  15721  18441   -758    439  -1029       O  
ATOM    251  CB  LEU A  99     -56.798  -7.040  11.188  1.00133.28           C  
ANISOU  251  CB  LEU A  99    16913  15677  18051   -151    393  -1363       C  
ATOM    252  CG  LEU A  99     -57.817  -6.486  12.166  1.00134.58           C  
ANISOU  252  CG  LEU A  99    17131  15723  18279    110    411  -1483       C  
ATOM    253  CD1 LEU A  99     -57.621  -7.111  13.531  1.00134.00           C  
ANISOU  253  CD1 LEU A  99    17057  15857  17998    248    392  -1787       C  
ATOM    254  CD2 LEU A  99     -57.640  -4.986  12.233  1.00137.74           C  
ANISOU  254  CD2 LEU A  99    17605  15731  18998     81    399  -1582       C  
ATOM    255  N   ILE A 100     -55.962  -8.327   8.495  1.00130.76           N  
ANISOU  255  N   ILE A 100    16516  15640  17525   -551    440   -858       N  
ATOM    256  CA  ILE A 100     -54.923  -8.986   7.727  1.00130.03           C  
ANISOU  256  CA  ILE A 100    16367  15722  17316   -746    471   -827       C  
ATOM    257  C   ILE A 100     -54.723  -8.342   6.355  1.00131.52           C  
ANISOU  257  C   ILE A 100    16584  15791  17598   -954    529   -553       C  
ATOM    258  O   ILE A 100     -53.603  -7.994   6.000  1.00132.81           O  
ANISOU  258  O   ILE A 100    16694  15924  17844  -1155    578   -597       O  
ATOM    259  CB  ILE A 100     -55.219 -10.483   7.558  1.00127.48           C  
ANISOU  259  CB  ILE A 100    16028  15703  16707   -672    458   -775       C  
ATOM    260  CG1 ILE A 100     -55.078 -11.198   8.905  1.00126.32           C  
ANISOU  260  CG1 ILE A 100    15844  15699  16453   -513    404  -1046       C  
ATOM    261  CG2 ILE A 100     -54.245 -11.101   6.580  1.00127.17           C  
ANISOU  261  CG2 ILE A 100    15944  15824  16553   -855    511   -725       C  
ATOM    262  CD1 ILE A 100     -55.386 -12.677   8.856  1.00124.10           C  
ANISOU  262  CD1 ILE A 100    15557  15677  15920   -436    377   -996       C  
ATOM    263  N   ILE A 101     -55.798  -8.161   5.595  1.00131.67           N  
ANISOU  263  N   ILE A 101    16678  15747  17604   -914    520   -260       N  
ATOM    264  CA  ILE A 101     -55.692  -7.530   4.279  1.00133.41           C  
ANISOU  264  CA  ILE A 101    16949  15858  17883  -1106    563     37       C  
ATOM    265  C   ILE A 101     -55.133  -6.113   4.385  1.00136.29           C  
ANISOU  265  C   ILE A 101    17327  15897  18562  -1231    581     14       C  
ATOM    266  O   ILE A 101     -54.274  -5.723   3.602  1.00137.88           O  
ANISOU  266  O   ILE A 101    17515  16062  18811  -1468    650    122       O  
ATOM    267  CB  ILE A 101     -57.044  -7.468   3.558  1.00133.54           C  
ANISOU  267  CB  ILE A 101    17043  15837  17857  -1018    509    361       C  
ATOM    268  CG1 ILE A 101     -57.594  -8.871   3.311  1.00131.08           C  
ANISOU  268  CG1 ILE A 101    16725  15832  17246   -940    473    409       C  
ATOM    269  CG2 ILE A 101     -56.915  -6.700   2.248  1.00135.83           C  
ANISOU  269  CG2 ILE A 101    17407  15998  18206  -1218    536    684       C  
ATOM    270  CD1 ILE A 101     -59.024  -8.868   2.806  1.00131.23           C  
ANISOU  270  CD1 ILE A 101    16788  15830  17242   -833    385    696       C  
ATOM    271  N   SER A 102     -55.645  -5.336   5.336  1.00137.27           N  
ANISOU  271  N   SER A 102    17480  15776  18900  -1073    526   -123       N  
ATOM    272  CA  SER A 102     -55.206  -3.951   5.522  1.00140.34           C  
ANISOU  272  CA  SER A 102    17903  15799  19620  -1175    518   -171       C  
ATOM    273  C   SER A 102     -53.728  -3.839   5.918  1.00141.15           C  
ANISOU  273  C   SER A 102    17918  15916  19797  -1375    543   -429       C  
ATOM    274  O   SER A 102     -52.979  -3.050   5.333  1.00143.57           O  
ANISOU  274  O   SER A 102    18217  16046  20289  -1618    579   -324       O  
ATOM    275  CB  SER A 102     -56.075  -3.245   6.572  1.00141.34           C  
ANISOU  275  CB  SER A 102    18088  15676  19939   -925    456   -330       C  
ATOM    276  OG  SER A 102     -55.873  -3.782   7.870  1.00140.00           O  
ANISOU  276  OG  SER A 102    17873  15651  19668   -778    434   -701       O  
ATOM    277  N   SER A 103     -53.302  -4.626   6.904  1.00139.40           N  
ANISOU  277  N   SER A 103    17619  15907  19440  -1280    515   -746       N  
ATOM    278  CA  SER A 103     -51.919  -4.543   7.352  1.00140.38           C  
ANISOU  278  CA  SER A 103    17632  16059  19645  -1453    508  -1001       C  
ATOM    279  C   SER A 103     -51.006  -4.929   6.201  1.00140.53           C  
ANISOU  279  C   SER A 103    17554  16257  19583  -1705    613   -818       C  
ATOM    280  O   SER A 103     -49.931  -4.363   6.047  1.00142.72           O  
ANISOU  280  O   SER A 103    17740  16447  20040  -1940    642   -865       O  
ATOM    281  CB  SER A 103     -51.662  -5.443   8.562  1.00138.89           C  
ANISOU  281  CB  SER A 103    17381  16106  19287  -1291    441  -1339       C  
ATOM    282  OG  SER A 103     -51.544  -6.802   8.180  1.00136.28           O  
ANISOU  282  OG  SER A 103    16982  16130  18667  -1260    481  -1277       O  
ATOM    283  N   SER A 104     -51.465  -5.855   5.364  1.00138.90           N  
ANISOU  283  N   SER A 104    17368  16297  19112  -1662    673   -605       N  
ATOM    284  CA  SER A 104     -50.667  -6.335   4.238  1.00139.14           C  
ANISOU  284  CA  SER A 104    17321  16538  19007  -1867    796   -448       C  
ATOM    285  C   SER A 104     -50.773  -5.410   3.024  1.00141.64           C  
ANISOU  285  C   SER A 104    17715  16673  19429  -2071    874    -91       C  
ATOM    286  O   SER A 104     -50.345  -5.777   1.931  1.00142.08           O  
ANISOU  286  O   SER A 104    17747  16915  19321  -2226    994     99       O  
ATOM    287  CB  SER A 104     -51.073  -7.755   3.832  1.00139.98           C  
ANISOU  287  CB  SER A 104    17441  16978  18768  -1739    818   -397       C  
ATOM    288  OG  SER A 104     -52.349  -7.772   3.225  1.00139.35           O  
ANISOU  288  OG  SER A 104    17504  16857  18585  -1644    789   -128       O  
ATOM    289  N   LEU A 105     -51.404  -4.250   3.184  1.00143.10           N  
ANISOU  289  N   LEU A 105    18007  16501  19864  -2052    807     11       N  
ATOM    290  CA  LEU A 105     -51.484  -3.308   2.072  1.00145.89           C  
ANISOU  290  CA  LEU A 105    18443  16649  20341  -2250    862    375       C  
ATOM    291  C   LEU A 105     -51.233  -1.864   2.490  1.00149.16           C  
ANISOU  291  C   LEU A 105    18887  16627  21161  -2362    811    347       C  
ATOM    292  O   LEU A 105     -50.530  -1.129   1.794  1.00152.07           O  
ANISOU  292  O   LEU A 105    19239  16859  21684  -2639    886    536       O  
ATOM    293  CB  LEU A 105     -52.845  -3.420   1.378  1.00145.65           C  
ANISOU  293  CB  LEU A 105    18562  16611  20168  -2103    816    686       C  
ATOM    294  CG  LEU A 105     -53.081  -2.594   0.110  1.00148.49           C  
ANISOU  294  CG  LEU A 105    19034  16803  20584  -2281    850   1123       C  
ATOM    295  CD1 LEU A 105     -52.048  -2.898  -0.954  1.00149.61           C  
ANISOU  295  CD1 LEU A 105    19123  17181  20543  -2562   1013   1275       C  
ATOM    296  CD2 LEU A 105     -54.477  -2.871  -0.423  1.00147.53           C  
ANISOU  296  CD2 LEU A 105    19033  16721  20302  -2096    760   1385       C  
ATOM    297  N   SER A 106     -51.778  -1.462   3.634  1.00150.96           N  
ANISOU  297  N   SER A 106    19162  16635  21560  -2153    691    105       N  
ATOM    298  CA  SER A 106     -51.716  -0.056   4.026  1.00154.35           C  
ANISOU  298  CA  SER A 106    19661  16599  22387  -2222    621     68       C  
ATOM    299  C   SER A 106     -51.406   0.146   5.501  1.00154.48           C  
ANISOU  299  C   SER A 106    19643  16500  22551  -2110    522   -392       C  
ATOM    300  O   SER A 106     -51.358  -0.806   6.283  1.00151.80           O  
ANISOU  300  O   SER A 106    19235  16448  21995  -1949    500   -663       O  
ATOM    301  CB  SER A 106     -53.039   0.650   3.710  1.00153.48           C  
ANISOU  301  CB  SER A 106    19718  16198  22400  -2050    560    328       C  
ATOM    302  OG  SER A 106     -54.016   0.357   4.694  1.00151.68           O  
ANISOU  302  OG  SER A 106    19525  15980  22125  -1706    484    108       O  
ATOM    303  N   LEU A 107     -51.248   1.415   5.868  1.00157.81           N  
ANISOU  303  N   LEU A 107    20137  16483  23341  -2192    450   -468       N  
ATOM    304  CA  LEU A 107     -51.008   1.836   7.246  1.00158.85           C  
ANISOU  304  CA  LEU A 107    20282  16433  23642  -2096    333   -911       C  
ATOM    305  C   LEU A 107     -52.181   2.560   7.932  1.00159.98           C  
ANISOU  305  C   LEU A 107    20599  16242  23946  -1797    252  -1015       C  
ATOM    306  O   LEU A 107     -52.560   2.152   9.031  1.00158.56           O  
ANISOU  306  O   LEU A 107    20434  16177  23636  -1542    206  -1340       O  
ATOM    307  CB  LEU A 107     -49.762   2.729   7.306  1.00160.58           C  
ANISOU  307  CB  LEU A 107    20437  16394  24183  -2436    293  -1013       C  
ATOM    308  CG  LEU A 107     -49.397   3.321   8.670  1.00162.55           C  
ANISOU  308  CG  LEU A 107    20717  16404  24639  -2393    140  -1482       C  
ATOM    309  CD1 LEU A 107     -49.094   2.229   9.681  1.00159.68           C  
ANISOU  309  CD1 LEU A 107    20250  16442  23979  -2235     95  -1846       C  
ATOM    310  CD2 LEU A 107     -48.220   4.280   8.542  1.00166.62           C  
ANISOU  310  CD2 LEU A 107    21166  16626  25517  -2776     88  -1515       C  
ATOM    311  N   PRO A 108     -52.758   3.618   7.297  1.00160.90           N  
ANISOU  311  N   PRO A 108    20843  15954  24339  -1817    241   -735       N  
ATOM    312  CA  PRO A 108     -53.679   4.533   7.998  1.00163.12           C  
ANISOU  312  CA  PRO A 108    21280  15830  24869  -1553    160   -879       C  
ATOM    313  C   PRO A 108     -54.700   3.878   8.925  1.00160.66           C  
ANISOU  313  C   PRO A 108    20984  15728  24333  -1150    163  -1109       C  
ATOM    314  O   PRO A 108     -55.533   3.084   8.486  1.00157.95           O  
ANISOU  314  O   PRO A 108    20604  15667  23744   -988    222   -884       O  
ATOM    315  CB  PRO A 108     -54.400   5.242   6.848  1.00165.08           C  
ANISOU  315  CB  PRO A 108    21625  15797  25302  -1573    174   -401       C  
ATOM    316  CG  PRO A 108     -53.391   5.294   5.779  1.00165.99           C  
ANISOU  316  CG  PRO A 108    21674  15963  25431  -1975    230   -109       C  
ATOM    317  CD  PRO A 108     -52.656   3.982   5.867  1.00162.35           C  
ANISOU  317  CD  PRO A 108    21041  16046  24598  -2059    306   -249       C  
ATOM    318  N   SER A 109     -54.610   4.215  10.208  1.00161.92           N  
ANISOU  318  N   SER A 109    21199  15754  24569  -1006     96  -1558       N  
ATOM    319  CA  SER A 109     -55.527   3.698  11.215  1.00160.30           C  
ANISOU  319  CA  SER A 109    21016  15735  24155   -629    116  -1806       C  
ATOM    320  C   SER A 109     -56.975   4.079  10.900  1.00161.03           C  
ANISOU  320  C   SER A 109    21176  15655  24352   -334    158  -1570       C  
ATOM    321  O   SER A 109     -57.909   3.399  11.329  1.00159.01           O  
ANISOU  321  O   SER A 109    20883  15660  23874    -43    217  -1603       O  
ATOM    322  CB  SER A 109     -55.123   4.202  12.607  1.00162.55           C  
ANISOU  322  CB  SER A 109    21384  15852  24524   -547     32  -2335       C  
ATOM    323  OG  SER A 109     -55.236   5.614  12.703  1.00167.03           O  
ANISOU  323  OG  SER A 109    22103  15853  25508   -544    -36  -2417       O  
ATOM    324  N   ASP A 110     -57.150   5.166  10.152  1.00164.19           N  
ANISOU  324  N   ASP A 110    21664  15616  25105   -415    122  -1317       N  
ATOM    325  CA  ASP A 110     -58.465   5.584   9.688  1.00165.31           C  
ANISOU  325  CA  ASP A 110    21850  15573  25388   -156    139  -1032       C  
ATOM    326  C   ASP A 110     -59.146   4.448   8.932  1.00161.60           C  
ANISOU  326  C   ASP A 110    21258  15549  24593    -95    201   -682       C  
ATOM    327  O   ASP A 110     -60.279   4.079   9.242  1.00160.62           O  
ANISOU  327  O   ASP A 110    21090  15568  24370    221    240   -666       O  
ATOM    328  CB  ASP A 110     -58.357   6.817   8.792  1.00169.20           C  
ANISOU  328  CB  ASP A 110    22450  15553  26287   -325     73   -730       C  
ATOM    329  CG  ASP A 110     -57.822   8.028   9.526  1.00173.48           C  
ANISOU  329  CG  ASP A 110    23131  15578  27204   -370     -9  -1070       C  
ATOM    330  OD1 ASP A 110     -57.948   8.073  10.767  1.00173.96           O  
ANISOU  330  OD1 ASP A 110    23235  15626  27237   -147    -14  -1536       O  
ATOM    331  OD2 ASP A 110     -57.261   8.928   8.862  1.00176.59           O  
ANISOU  331  OD2 ASP A 110    23602  15581  27913   -639    -73   -871       O  
ATOM    332  N   LEU A 111     -58.434   3.879   7.961  1.00159.78           N  
ANISOU  332  N   LEU A 111    20967  15547  24196   -403    215   -419       N  
ATOM    333  CA  LEU A 111     -58.984   2.824   7.115  1.00156.66           C  
ANISOU  333  CA  LEU A 111    20481  15549  23493   -390    253    -85       C  
ATOM    334  C   LEU A 111     -59.156   1.497   7.851  1.00152.84           C  
ANISOU  334  C   LEU A 111    19893  15539  22641   -243    304   -311       C  
ATOM    335  O   LEU A 111     -60.058   0.725   7.536  1.00150.79           O  
ANISOU  335  O   LEU A 111    19568  15543  22182    -97    321   -115       O  
ATOM    336  CB  LEU A 111     -58.102   2.606   5.883  1.00156.26           C  
ANISOU  336  CB  LEU A 111    20414  15609  23348   -760    270    223       C  
ATOM    337  CG  LEU A 111     -58.104   3.700   4.817  1.00159.77           C  
ANISOU  337  CG  LEU A 111    20958  15673  24076   -930    229    611       C  
ATOM    338  CD1 LEU A 111     -57.084   3.387   3.737  1.00159.44           C  
ANISOU  338  CD1 LEU A 111    20887  15813  23881  -1310    285    859       C  
ATOM    339  CD2 LEU A 111     -59.487   3.868   4.217  1.00160.43           C  
ANISOU  339  CD2 LEU A 111    21072  15683  24202   -700    177    964       C  
ATOM    340  N   GLN A 112     -58.278   1.217   8.807  1.00152.91           N  
ANISOU  340  N   GLN A 112    19883  15655  22560   -296    311   -704       N  
ATOM    341  CA  GLN A 112     -58.389  -0.013   9.582  1.00149.67           C  
ANISOU  341  CA  GLN A 112    19390  15670  21808   -158    348   -916       C  
ATOM    342  C   GLN A 112     -59.574   0.020  10.531  1.00150.00           C  
ANISOU  342  C   GLN A 112    19442  15712  21841    213    377  -1069       C  
ATOM    343  O   GLN A 112     -60.369  -0.916  10.558  1.00147.68           O  
ANISOU  343  O   GLN A 112    19067  15730  21314    367    418   -959       O  
ATOM    344  CB  GLN A 112     -57.109  -0.269  10.365  1.00153.41           C  
ANISOU  344  CB  GLN A 112    19841  16251  22197   -310    324  -1282       C  
ATOM    345  CG  GLN A 112     -55.953  -0.696   9.498  1.00152.39           C  
ANISOU  345  CG  GLN A 112    19638  16275  21990   -646    330  -1143       C  
ATOM    346  CD  GLN A 112     -54.690  -0.882  10.294  1.00152.47           C  
ANISOU  346  CD  GLN A 112    19594  16376  21961   -786    287  -1502       C  
ATOM    347  OE1 GLN A 112     -54.393  -0.097  11.196  1.00154.85           O  
ANISOU  347  OE1 GLN A 112    19958  16434  22446   -758    221  -1813       O  
ATOM    348  NE2 GLN A 112     -53.928  -1.921   9.964  1.00150.14           N  
ANISOU  348  NE2 GLN A 112    19182  16430  21434   -932    313  -1473       N  
ATOM    349  N   GLN A 113     -59.678   1.087  11.319  1.00152.38           N  
ANISOU  349  N   GLN A 113    19839  15664  22395    352    361  -1332       N  
ATOM    350  CA  GLN A 113     -60.825   1.276  12.199  1.00153.49           C  
ANISOU  350  CA  GLN A 113    19990  15772  22556    727    418  -1487       C  
ATOM    351  C   GLN A 113     -62.119   1.281  11.386  1.00153.53           C  
ANISOU  351  C   GLN A 113    19927  15766  22641    894    444  -1084       C  
ATOM    352  O   GLN A 113     -63.095   0.595  11.733  1.00152.19           O  
ANISOU  352  O   GLN A 113    19659  15866  22299   1128    512  -1046       O  
ATOM    353  CB  GLN A 113     -60.692   2.578  12.992  1.00157.61           C  
ANISOU  353  CB  GLN A 113    20652  15849  23383    838    390  -1823       C  
ATOM    354  CG  GLN A 113     -59.516   2.638  13.959  1.00158.18           C  
ANISOU  354  CG  GLN A 113    20794  15924  23381    704    336  -2270       C  
ATOM    355  CD  GLN A 113     -58.991   4.056  14.161  1.00162.54           C  
ANISOU  355  CD  GLN A 113    21499  15939  24321    623    249  -2484       C  
ATOM    356  OE1 GLN A 113     -59.312   4.964  13.395  1.00164.91           O  
ANISOU  356  OE1 GLN A 113    21852  15851  24956    600    224  -2241       O  
ATOM    357  NE2 GLN A 113     -58.212   4.257  15.220  1.00163.93           N  
ANISOU  357  NE2 GLN A 113    21753  16076  24455    584    186  -2940       N  
ATOM    358  N   TYR A 114     -62.102   2.045  10.292  1.00155.30           N  
ANISOU  358  N   TYR A 114    20196  15686  23124    756    381   -767       N  
ATOM    359  CA  TYR A 114     -63.235   2.120   9.375  1.00155.74           C  
ANISOU  359  CA  TYR A 114    20191  15711  23271    877    362   -342       C  
ATOM    360  C   TYR A 114     -63.659   0.752   8.893  1.00152.03           C  
ANISOU  360  C   TYR A 114    19588  15723  22453    846    378   -111       C  
ATOM    361  O   TYR A 114     -64.824   0.419   8.972  1.00151.77           O  
ANISOU  361  O   TYR A 114    19451  15830  22387   1085    401     15       O  
ATOM    362  CB  TYR A 114     -62.931   2.991   8.155  1.00157.96           C  
ANISOU  362  CB  TYR A 114    20557  15650  23811    659    274      7       C  
ATOM    363  CG  TYR A 114     -63.892   2.739   7.010  1.00157.63           C  
ANISOU  363  CG  TYR A 114    20444  15706  23743    698    222    498       C  
ATOM    364  CD1 TYR A 114     -65.202   3.202   7.050  1.00159.73           C  
ANISOU  364  CD1 TYR A 114    20654  15820  24215   1021    202    641       C  
ATOM    365  CD2 TYR A 114     -63.494   2.005   5.901  1.00155.46           C  
ANISOU  365  CD2 TYR A 114    20149  15694  23223    420    189    806       C  
ATOM    366  CE1 TYR A 114     -66.081   2.959   6.003  1.00159.66           C  
ANISOU  366  CE1 TYR A 114    20567  15916  24183   1048    122   1096       C  
ATOM    367  CE2 TYR A 114     -64.365   1.753   4.857  1.00155.40           C  
ANISOU  367  CE2 TYR A 114    20092  15791  23161    445    116   1240       C  
ATOM    368  CZ  TYR A 114     -65.655   2.227   4.913  1.00157.47           C  
ANISOU  368  CZ  TYR A 114    20293  15900  23639    751     69   1390       C  
ATOM    369  OH  TYR A 114     -66.508   1.971   3.865  1.00157.65           O  
ANISOU  369  OH  TYR A 114    20254  16038  23607    764    -36   1829       O  
ATOM    370  N   LEU A 115     -62.725  -0.018   8.346  1.00149.49           N  
ANISOU  370  N   LEU A 115    19264  15642  21894    550    362    -47       N  
ATOM    371  CA  LEU A 115     -63.070  -1.323   7.790  1.00146.25           C  
ANISOU  371  CA  LEU A 115    18753  15653  21162    499    360    170       C  
ATOM    372  C   LEU A 115     -63.437  -2.346   8.861  1.00143.97           C  
ANISOU  372  C   LEU A 115    18374  15704  20624    680    426    -72       C  
ATOM    373  O   LEU A 115     -64.164  -3.290   8.579  1.00142.08           O  
ANISOU  373  O   LEU A 115    18037  15753  20193    732    420    114       O  
ATOM    374  CB  LEU A 115     -61.938  -1.872   6.918  1.00144.53           C  
ANISOU  374  CB  LEU A 115    18564  15594  20757    153    342    277       C  
ATOM    375  CG  LEU A 115     -61.938  -1.372   5.467  1.00146.02           C  
ANISOU  375  CG  LEU A 115    18809  15633  21039    -37    282    693       C  
ATOM    376  CD1 LEU A 115     -60.827  -2.024   4.667  1.00144.43           C  
ANISOU  376  CD1 LEU A 115    18622  15649  20605   -358    304    767       C  
ATOM    377  CD2 LEU A 115     -63.286  -1.586   4.802  1.00146.14           C  
ANISOU  377  CD2 LEU A 115    18771  15724  21033    115    215   1044       C  
ATOM    378  N   VAL A 116     -62.932  -2.183  10.079  1.00145.49           N  
ANISOU  378  N   VAL A 116    18605  15868  20807    760    477   -476       N  
ATOM    379  CA  VAL A 116     -63.374  -3.056  11.164  1.00143.94           C  
ANISOU  379  CA  VAL A 116    18338  15980  20374    955    547   -684       C  
ATOM    380  C   VAL A 116     -64.844  -2.787  11.493  1.00145.53           C  
ANISOU  380  C   VAL A 116    18454  16152  20689   1278    609   -594       C  
ATOM    381  O   VAL A 116     -65.673  -3.712  11.472  1.00143.93           O  
ANISOU  381  O   VAL A 116    18125  16247  20313   1368    636   -432       O  
ATOM    382  CB  VAL A 116     -62.514  -2.894  12.439  1.00143.69           C  
ANISOU  382  CB  VAL A 116    18382  15933  20280    978    575  -1143       C  
ATOM    383  CG1 VAL A 116     -63.152  -3.620  13.614  1.00142.94           C  
ANISOU  383  CG1 VAL A 116    18231  16128  19952   1221    662  -1330       C  
ATOM    384  CG2 VAL A 116     -61.116  -3.421  12.207  1.00141.87           C  
ANISOU  384  CG2 VAL A 116    18174  15826  19903    681    516  -1228       C  
ATOM    385  N   SER A 117     -65.172  -1.523  11.763  1.00147.83           N  
ANISOU  385  N   SER A 117    18804  16074  21292   1449    627   -690       N  
ATOM    386  CA  SER A 117     -66.546  -1.161  12.119  1.00149.94           C  
ANISOU  386  CA  SER A 117    18972  16292  21706   1790    702   -631       C  
ATOM    387  C   SER A 117     -67.497  -1.443  10.962  1.00149.50           C  
ANISOU  387  C   SER A 117    18783  16310  21712   1788    636   -157       C  
ATOM    388  O   SER A 117     -68.618  -1.907  11.163  1.00149.50           O  
ANISOU  388  O   SER A 117    18618  16515  21670   1993    691    -36       O  
ATOM    389  CB  SER A 117     -66.631   0.306  12.514  1.00154.08           C  
ANISOU  389  CB  SER A 117    19603  16353  22588   1971    718   -826       C  
ATOM    390  OG  SER A 117     -66.292   1.129  11.414  1.00155.50           O  
ANISOU  390  OG  SER A 117    19863  16180  23039   1795    599   -578       O  
ATOM    391  N   THR A 118     -67.023  -1.170   9.752  1.00149.38           N  
ANISOU  391  N   THR A 118    18835  16139  21783   1542    514    114       N  
ATOM    392  CA  THR A 118     -67.770  -1.410   8.525  1.00149.17           C  
ANISOU  392  CA  THR A 118    18719  16177  21782   1491    411    574       C  
ATOM    393  C   THR A 118     -68.038  -2.890   8.366  1.00145.80           C  
ANISOU  393  C   THR A 118    18177  16210  21012   1405    404    688       C  
ATOM    394  O   THR A 118     -69.124  -3.294   7.951  1.00145.88           O  
ANISOU  394  O   THR A 118    18038  16369  21020   1502    359    962       O  
ATOM    395  CB  THR A 118     -67.010  -0.913   7.284  1.00149.69           C  
ANISOU  395  CB  THR A 118    18916  16030  21929   1200    295    820       C  
ATOM    396  OG1 THR A 118     -66.708   0.477   7.435  1.00153.09           O  
ANISOU  396  OG1 THR A 118    19467  15994  22705   1252    290    723       O  
ATOM    397  CG2 THR A 118     -67.828  -1.123   6.018  1.00149.93           C  
ANISOU  397  CG2 THR A 118    18875  16134  21957   1158    169   1298       C  
ATOM    398  N   SER A 119     -67.038  -3.701   8.692  1.00143.59           N  
ANISOU  398  N   SER A 119    17958  16141  20458   1218    435    481       N  
ATOM    399  CA  SER A 119     -67.199  -5.144   8.627  1.00140.55           C  
ANISOU  399  CA  SER A 119    17486  16160  19755   1135    425    554       C  
ATOM    400  C   SER A 119     -68.266  -5.591   9.611  1.00140.74           C  
ANISOU  400  C   SER A 119    17356  16380  19738   1402    519    481       C  
ATOM    401  O   SER A 119     -69.121  -6.410   9.271  1.00139.84           O  
ANISOU  401  O   SER A 119    17105  16501  19528   1415    480    717       O  
ATOM    402  CB  SER A 119     -65.889  -5.866   8.914  1.00141.68           C  
ANISOU  402  CB  SER A 119    17722  16462  19647    926    443    316       C  
ATOM    403  OG  SER A 119     -66.042  -7.253   8.685  1.00139.02           O  
ANISOU  403  OG  SER A 119    17321  16470  19030    835    411    421       O  
ATOM    404  N   LEU A 120     -68.207  -5.059  10.831  1.00141.69           N  
ANISOU  404  N   LEU A 120    17499  16411  19924   1604    644    152       N  
ATOM    405  CA  LEU A 120     -69.204  -5.384  11.849  1.00142.45           C  
ANISOU  405  CA  LEU A 120    17450  16700  19973   1875    774     66       C  
ATOM    406  C   LEU A 120     -70.620  -5.088  11.346  1.00144.46           C  
ANISOU  406  C   LEU A 120    17515  16923  20449   2061    760    384       C  
ATOM    407  O   LEU A 120     -71.508  -5.957  11.357  1.00143.75           O  
ANISOU  407  O   LEU A 120    17243  17119  20255   2107    774    569       O  
ATOM    408  CB  LEU A 120     -68.932  -4.603  13.137  1.00144.57           C  
ANISOU  408  CB  LEU A 120    17806  16824  20301   2083    909   -345       C  
ATOM    409  CG  LEU A 120     -67.595  -4.850  13.839  1.00143.16           C  
ANISOU  409  CG  LEU A 120    17793  16692  19910   1935    911   -695       C  
ATOM    410  CD1 LEU A 120     -67.377  -3.838  14.952  1.00146.07           C  
ANISOU  410  CD1 LEU A 120    18272  16844  20385   2136   1004  -1094       C  
ATOM    411  CD2 LEU A 120     -67.524  -6.263  14.388  1.00140.50           C  
ANISOU  411  CD2 LEU A 120    17400  16770  19215   1878    946   -722       C  
ATOM    412  N   ILE A 121     -70.807  -3.858  10.879  1.00147.20           N  
ANISOU  412  N   ILE A 121    17900  16910  21118   2157    717    461       N  
ATOM    413  CA  ILE A 121     -72.093  -3.419  10.365  1.00149.65           C  
ANISOU  413  CA  ILE A 121    18029  17143  21689   2353    679    765       C  
ATOM    414  C   ILE A 121     -72.593  -4.299   9.223  1.00147.99           C  
ANISOU  414  C   ILE A 121    17701  17156  21372   2168    517   1179       C  
ATOM    415  O   ILE A 121     -73.645  -4.940   9.333  1.00148.13           O  
ANISOU  415  O   ILE A 121    17494  17425  21364   2276    534   1343       O  
ATOM    416  CB  ILE A 121     -72.001  -1.965   9.876  1.00152.82           C  
ANISOU  416  CB  ILE A 121    18537  17074  22455   2433    613    813       C  
ATOM    417  CG1 ILE A 121     -71.708  -1.040  11.058  1.00155.22           C  
ANISOU  417  CG1 ILE A 121    18945  17130  22902   2660    765    386       C  
ATOM    418  CG2 ILE A 121     -73.279  -1.550   9.175  1.00155.42           C  
ANISOU  418  CG2 ILE A 121    18675  17319  23059   2618    528   1184       C  
ATOM    419  CD1 ILE A 121     -71.304   0.356  10.659  1.00158.19           C  
ANISOU  419  CD1 ILE A 121    19488  16994  23623   2675    690    369       C  
ATOM    420  N   VAL A 122     -71.817  -4.366   8.148  1.00146.60           N  
ANISOU  420  N   VAL A 122    17676  16905  21122   1878    365   1336       N  
ATOM    421  CA  VAL A 122     -72.230  -5.099   6.957  1.00145.50           C  
ANISOU  421  CA  VAL A 122    17469  16945  20868   1691    189   1714       C  
ATOM    422  C   VAL A 122     -72.488  -6.587   7.244  1.00142.80           C  
ANISOU  422  C   VAL A 122    17016  17013  20230   1603    202   1713       C  
ATOM    423  O   VAL A 122     -73.453  -7.162   6.734  1.00143.04           O  
ANISOU  423  O   VAL A 122    16875  17222  20252   1598     97   1994       O  
ATOM    424  CB  VAL A 122     -71.202  -4.927   5.831  1.00144.64           C  
ANISOU  424  CB  VAL A 122    17574  16708  20676   1388     62   1833       C  
ATOM    425  CG1 VAL A 122     -71.495  -5.873   4.683  1.00143.27           C  
ANISOU  425  CG1 VAL A 122    17370  16775  20292   1175   -110   2154       C  
ATOM    426  CG2 VAL A 122     -71.223  -3.483   5.341  1.00147.92           C  
ANISOU  426  CG2 VAL A 122    18070  16713  21421   1464      8   1963       C  
ATOM    427  N   CYS A 123     -71.643  -7.221   8.048  1.00140.51           N  
ANISOU  427  N   CYS A 123    16818  16862  19707   1526    312   1410       N  
ATOM    428  CA  CYS A 123     -71.903  -8.617   8.388  1.00138.31           C  
ANISOU  428  CA  CYS A 123    16444  16938  19171   1454    324   1417       C  
ATOM    429  C   CYS A 123     -73.179  -8.772   9.206  1.00139.93           C  
ANISOU  429  C   CYS A 123    16399  17297  19472   1708    432   1460       C  
ATOM    430  O   CYS A 123     -73.923  -9.724   8.996  1.00139.36           O  
ANISOU  430  O   CYS A 123    16169  17468  19313   1648    370   1666       O  
ATOM    431  CB  CYS A 123     -70.724  -9.242   9.132  1.00142.82           C  
ANISOU  431  CB  CYS A 123    17163  17616  19486   1341    409   1094       C  
ATOM    432  SG  CYS A 123     -69.358  -9.720   8.047  1.00140.36           S  
ANISOU  432  SG  CYS A 123    17064  17294  18973    991    277   1109       S  
ATOM    433  N   GLY A 124     -73.444  -7.851  10.129  1.00142.24           N  
ANISOU  433  N   GLY A 124    16651  17450  19944   1986    598   1264       N  
ATOM    434  CA  GLY A 124     -74.718  -7.891  10.829  1.00144.40           C  
ANISOU  434  CA  GLY A 124    16661  17872  20331   2250    727   1325       C  
ATOM    435  C   GLY A 124     -75.883  -7.863   9.844  1.00146.02           C  
ANISOU  435  C   GLY A 124    16642  18097  20742   2273    575   1735       C  
ATOM    436  O   GLY A 124     -76.784  -8.715   9.885  1.00146.08           O  
ANISOU  436  O   GLY A 124    16420  18377  20706   2266    563   1928       O  
ATOM    437  N   LEU A 125     -75.833  -6.905   8.922  1.00147.50           N  
ANISOU  437  N   LEU A 125    16899  17992  21152   2276    436   1885       N  
ATOM    438  CA  LEU A 125     -76.898  -6.721   7.938  1.00149.54           C  
ANISOU  438  CA  LEU A 125    16960  18234  21624   2312    257   2284       C  
ATOM    439  C   LEU A 125     -77.112  -7.938   7.039  1.00147.54           C  
ANISOU  439  C   LEU A 125    16655  18244  21160   2023     51   2560       C  
ATOM    440  O   LEU A 125     -78.244  -8.342   6.785  1.00148.92           O  
ANISOU  440  O   LEU A 125    16562  18591  21428   2067    -36   2824       O  
ATOM    441  CB  LEU A 125     -76.610  -5.498   7.068  1.00151.42           C  
ANISOU  441  CB  LEU A 125    17342  18093  22096   2328    126   2403       C  
ATOM    442  CG  LEU A 125     -76.615  -4.152   7.789  1.00154.38           C  
ANISOU  442  CG  LEU A 125    17751  18137  22771   2639    281   2184       C  
ATOM    443  CD1 LEU A 125     -76.184  -3.059   6.833  1.00156.04           C  
ANISOU  443  CD1 LEU A 125    18143  17955  23188   2584    124   2334       C  
ATOM    444  CD2 LEU A 125     -77.980  -3.861   8.373  1.00157.65           C  
ANISOU  444  CD2 LEU A 125    17842  18613  23445   3001    391   2249       C  
ATOM    445  N   LEU A 126     -76.035  -8.530   6.553  1.00144.59           N  
ANISOU  445  N   LEU A 126    16527  17900  20510   1728    -32   2491       N  
ATOM    446  CA  LEU A 126     -76.182  -9.621   5.601  1.00143.06           C  
ANISOU  446  CA  LEU A 126    16327  17915  20115   1455   -243   2728       C  
ATOM    447  C   LEU A 126     -76.448 -10.955   6.309  1.00141.33           C  
ANISOU  447  C   LEU A 126    15990  18012  19698   1388   -175   2657       C  
ATOM    448  O   LEU A 126     -76.973 -11.905   5.707  1.00140.92           O  
ANISOU  448  O   LEU A 126    15846  18150  19549   1216   -347   2874       O  
ATOM    449  CB  LEU A 126     -74.962  -9.673   4.693  1.00141.16           C  
ANISOU  449  CB  LEU A 126    16391  17575  19670   1184   -352   2697       C  
ATOM    450  CG  LEU A 126     -74.844  -8.304   4.009  1.00143.51           C  
ANISOU  450  CG  LEU A 126    16779  17553  20195   1252   -418   2826       C  
ATOM    451  CD1 LEU A 126     -73.689  -8.229   3.029  1.00142.30           C  
ANISOU  451  CD1 LEU A 126    16908  17303  19856    982   -508   2843       C  
ATOM    452  CD2 LEU A 126     -76.152  -7.937   3.322  1.00146.52           C  
ANISOU  452  CD2 LEU A 126    16946  17918  20806   1366   -598   3201       C  
ATOM    453  N   SER A 127     -76.095 -11.022   7.589  1.00140.61           N  
ANISOU  453  N   SER A 127    15912  17969  19546   1517     62   2358       N  
ATOM    454  CA  SER A 127     -76.575 -12.104   8.439  1.00139.96           C  
ANISOU  454  CA  SER A 127    15671  18173  19332   1518    162   2331       C  
ATOM    455  C   SER A 127     -78.094 -12.010   8.532  1.00142.91           C  
ANISOU  455  C   SER A 127    15687  18665  19947   1691    168   2588       C  
ATOM    456  O   SER A 127     -78.803 -13.002   8.379  1.00142.91           O  
ANISOU  456  O   SER A 127    15509  18891  19898   1567     78   2790       O  
ATOM    457  CB  SER A 127     -75.962 -12.041   9.836  1.00139.29           C  
ANISOU  457  CB  SER A 127    15672  18119  19133   1656    420   1975       C  
ATOM    458  OG  SER A 127     -74.601 -12.409   9.821  1.00136.51           O  
ANISOU  458  OG  SER A 127    15601  17726  18542   1470    397   1755       O  
ATOM    459  N   MET A 128     -78.597 -10.804   8.781  1.00145.73           N  
ANISOU  459  N   MET A 128    15928  18857  20585   1980    269   2580       N  
ATOM    460  CA  MET A 128     -80.039 -10.599   8.746  1.00149.00           C  
ANISOU  460  CA  MET A 128    15973  19366  21274   2167    262   2843       C  
ATOM    461  C   MET A 128     -80.614 -11.012   7.399  1.00149.37           C  
ANISOU  461  C   MET A 128    15922  19459  21374   1960    -64   3222       C  
ATOM    462  O   MET A 128     -81.701 -11.564   7.337  1.00150.96           O  
ANISOU  462  O   MET A 128    15813  19870  21674   1956   -128   3462       O  
ATOM    463  CB  MET A 128     -80.401  -9.144   9.024  1.00152.24           C  
ANISOU  463  CB  MET A 128    16307  19529  22007   2519    383   2779       C  
ATOM    464  CG  MET A 128     -80.756  -8.850  10.459  1.00154.04           C  
ANISOU  464  CG  MET A 128    16398  19843  22289   2828    719   2530       C  
ATOM    465  SD  MET A 128     -81.761  -7.357  10.503  1.00159.08           S  
ANISOU  465  SD  MET A 128    16796  20248  23399   3264    798   2600       S  
ATOM    466  CE  MET A 128     -80.710  -6.220   9.605  1.00158.58           C  
ANISOU  466  CE  MET A 128    17103  19713  23435   3201    612   2539       C  
ATOM    467  N   VAL A 129     -79.884 -10.753   6.319  1.00148.19           N  
ANISOU  467  N   VAL A 129    16031  19127  21148   1778   -272   3278       N  
ATOM    468  CA  VAL A 129     -80.359 -11.165   5.001  1.00148.70           C  
ANISOU  468  CA  VAL A 129    16048  19248  21204   1566   -599   3619       C  
ATOM    469  C   VAL A 129     -80.509 -12.682   4.905  1.00146.90           C  
ANISOU  469  C   VAL A 129    15777  19300  20738   1294   -704   3682       C  
ATOM    470  O   VAL A 129     -81.503 -13.162   4.374  1.00148.54           O  
ANISOU  470  O   VAL A 129    15751  19656  21034   1214   -902   3968       O  
ATOM    471  CB  VAL A 129     -79.450 -10.676   3.865  1.00147.84           C  
ANISOU  471  CB  VAL A 129    16261  18921  20990   1398   -778   3658       C  
ATOM    472  CG1 VAL A 129     -79.905 -11.280   2.541  1.00148.36           C  
ANISOU  472  CG1 VAL A 129    16309  19098  20962   1153  -1119   3984       C  
ATOM    473  CG2 VAL A 129     -79.509  -9.173   3.771  1.00150.40           C  
ANISOU  473  CG2 VAL A 129    16598  18942  21606   1645   -740   3691       C  
ATOM    474  N   GLN A 130     -79.547 -13.461   5.388  1.00143.80           N  
ANISOU  474  N   GLN A 130    15604  18973  20063   1144   -596   3428       N  
ATOM    475  CA  GLN A 130     -79.730 -14.908   5.205  1.00142.50           C  
ANISOU  475  CA  GLN A 130    15410  19031  19702    882   -728   3511       C  
ATOM    476  C   GLN A 130     -80.490 -15.621   6.340  1.00143.18           C  
ANISOU  476  C   GLN A 130    15222  19346  19835    955   -557   3515       C  
ATOM    477  O   GLN A 130     -80.883 -16.773   6.181  1.00142.91           O  
ANISOU  477  O   GLN A 130    15105  19483  19712    743   -687   3644       O  
ATOM    478  CB  GLN A 130     -78.386 -15.614   4.972  1.00140.33           C  
ANISOU  478  CB  GLN A 130    15496  18728  19095    648   -754   3290       C  
ATOM    479  CG  GLN A 130     -78.569 -17.021   4.384  1.00139.49           C  
ANISOU  479  CG  GLN A 130    15411  18782  18807    355   -976   3408       C  
ATOM    480  CD  GLN A 130     -77.282 -17.733   4.065  1.00136.60           C  
ANISOU  480  CD  GLN A 130    15388  18382  18132    148  -1010   3193       C  
ATOM    481  OE1 GLN A 130     -77.111 -18.905   4.406  1.00135.30           O  
ANISOU  481  OE1 GLN A 130    15264  18329  17814      9  -1019   3120       O  
ATOM    482  NE2 GLN A 130     -76.373 -17.041   3.381  1.00135.87           N  
ANISOU  482  NE2 GLN A 130    15537  18130  17957    124  -1030   3104       N  
ATOM    483  N   ILE A 131     -80.733 -14.959   7.466  1.00144.43           N  
ANISOU  483  N   ILE A 131    15238  19509  20130   1243   -269   3384       N  
ATOM    484  CA  ILE A 131     -81.494 -15.612   8.536  1.00145.55           C  
ANISOU  484  CA  ILE A 131    15109  19897  20297   1312    -81   3415       C  
ATOM    485  C   ILE A 131     -82.975 -15.764   8.130  1.00148.77           C  
ANISOU  485  C   ILE A 131    15103  20455  20969   1321   -215   3778       C  
ATOM    486  O   ILE A 131     -83.699 -16.614   8.656  1.00149.79           O  
ANISOU  486  O   ILE A 131    14985  20819  21111   1254   -155   3904       O  
ATOM    487  CB  ILE A 131     -81.375 -14.835   9.876  1.00146.50           C  
ANISOU  487  CB  ILE A 131    15195  20006  20460   1637    283   3157       C  
ATOM    488  CG1 ILE A 131     -79.956 -14.917  10.436  1.00143.49           C  
ANISOU  488  CG1 ILE A 131    15186  19536  19797   1592    400   2802       C  
ATOM    489  CG2 ILE A 131     -82.336 -15.371  10.930  1.00148.55           C  
ANISOU  489  CG2 ILE A 131    15129  20548  20763   1738    502   3238       C  
ATOM    490  CD1 ILE A 131     -79.752 -14.085  11.682  1.00144.62           C  
ANISOU  490  CD1 ILE A 131    15346  19646  19956   1898    718   2516       C  
ATOM    491  N   THR A 132     -83.411 -14.980   7.149  1.00150.56           N  
ANISOU  491  N   THR A 132    15252  20548  21406   1379   -417   3968       N  
ATOM    492  CA  THR A 132     -84.813 -14.986   6.751  1.00154.05           C  
ANISOU  492  CA  THR A 132    15275  21123  22134   1418   -564   4315       C  
ATOM    493  C   THR A 132     -85.017 -15.348   5.281  1.00154.24           C  
ANISOU  493  C   THR A 132    15346  21120  22141   1146   -991   4578       C  
ATOM    494  O   THR A 132     -84.067 -15.366   4.494  1.00151.96           O  
ANISOU  494  O   THR A 132    15425  20680  21633    974  -1151   4490       O  
ATOM    495  CB  THR A 132     -85.467 -13.618   7.015  1.00157.39           C  
ANISOU  495  CB  THR A 132    15462  21439  22900   1811   -421   4354       C  
ATOM    496  OG1 THR A 132     -86.874 -13.691   6.743  1.00161.09           O  
ANISOU  496  OG1 THR A 132    15466  22074  23669   1867   -544   4694       O  
ATOM    497  CG2 THR A 132     -84.827 -12.530   6.162  1.00157.11           C  
ANISOU  497  CG2 THR A 132    15699  21086  22910   1879   -566   4321       C  
ATOM    498  N   ARG A 133     -86.266 -15.649   4.929  1.00162.68           N  
ANISOU  498  N   ARG A 133    16028  22352  23431   1105  -1172   4897       N  
ATOM    499  CA  ARG A 133     -86.646 -15.963   3.554  1.00163.70           C  
ANISOU  499  CA  ARG A 133    16154  22483  23561    861  -1607   5170       C  
ATOM    500  C   ARG A 133     -87.735 -15.007   3.074  1.00167.87           C  
ANISOU  500  C   ARG A 133    16332  22989  24461   1082  -1751   5463       C  
ATOM    501  O   ARG A 133     -88.268 -15.159   1.973  1.00169.65           O  
ANISOU  501  O   ARG A 133    16479  23244  24737    920  -2132   5737       O  
ATOM    502  CB  ARG A 133     -87.124 -17.411   3.449  1.00168.13           C  
ANISOU  502  CB  ARG A 133    16587  23263  24031    531  -1783   5300       C  
ATOM    503  CG  ARG A 133     -86.064 -18.445   3.789  1.00164.32           C  
ANISOU  503  CG  ARG A 133    16463  22779  23193    299  -1699   5040       C  
ATOM    504  CD  ARG A 133     -86.676 -19.780   4.173  1.00164.97           C  
ANISOU  504  CD  ARG A 133    16339  23071  23272     60  -1747   5154       C  
ATOM    505  NE  ARG A 133     -87.431 -19.704   5.420  1.00166.88           N  
ANISOU  505  NE  ARG A 133    16197  23488  23723    262  -1423   5205       N  
ATOM    506  CZ  ARG A 133     -87.887 -20.762   6.085  1.00167.53           C  
ANISOU  506  CZ  ARG A 133    16090  23757  23805    100  -1348   5285       C  
ATOM    507  NH1 ARG A 133     -87.668 -21.985   5.619  1.00166.38           N  
ANISOU  507  NH1 ARG A 133    16111  23616  23488   -264  -1595   5315       N  
ATOM    508  NH2 ARG A 133     -88.559 -20.600   7.218  1.00169.60           N  
ANISOU  508  NH2 ARG A 133    16003  24198  24238    302  -1018   5336       N  
ATOM    509  N   PHE A 134     -88.045 -14.019   3.914  1.00171.46           N  
ANISOU  509  N   PHE A 134    16587  23388  25171   1465  -1451   5394       N  
ATOM    510  CA  PHE A 134     -89.091 -13.025   3.650  1.00175.81           C  
ANISOU  510  CA  PHE A 134    16771  23901  26127   1753  -1528   5645       C  
ATOM    511  C   PHE A 134     -88.671 -11.950   2.643  1.00176.31           C  
ANISOU  511  C   PHE A 134    17086  23671  26234   1835  -1744   5717       C  
ATOM    512  O   PHE A 134     -89.465 -11.069   2.304  1.00180.05           O  
ANISOU  512  O   PHE A 134    17298  24068  27046   2078  -1853   5944       O  
ATOM    513  CB  PHE A 134     -89.514 -12.333   4.954  1.00180.26           C  
ANISOU  513  CB  PHE A 134    17061  24490  26938   2163  -1098   5501       C  
ATOM    514  CG  PHE A 134     -90.297 -13.209   5.894  1.00181.46           C  
ANISOU  514  CG  PHE A 134    16831  24971  27145   2140   -889   5544       C  
ATOM    515  CD1 PHE A 134     -90.937 -14.353   5.439  1.00182.07           C  
ANISOU  515  CD1 PHE A 134    16693  25282  27203   1811  -1146   5802       C  
ATOM    516  CD2 PHE A 134     -90.402 -12.877   7.238  1.00182.34           C  
ANISOU  516  CD2 PHE A 134    16802  25159  27322   2441   -435   5330       C  
ATOM    517  CE1 PHE A 134     -91.666 -15.159   6.311  1.00183.51           C  
ANISOU  517  CE1 PHE A 134    16511  25762  27453   1767   -946   5873       C  
ATOM    518  CE2 PHE A 134     -91.127 -13.673   8.113  1.00183.81           C  
ANISOU  518  CE2 PHE A 134    16632  25666  27539   2414   -218   5396       C  
ATOM    519  CZ  PHE A 134     -91.761 -14.817   7.650  1.00184.39           C  
ANISOU  519  CZ  PHE A 134    16478  25965  27616   2069   -471   5682       C  
ATOM    520  N   HIS A 135     -87.427 -12.017   2.175  1.00174.88           N  
ANISOU  520  N   HIS A 135    17399  23327  25720   1638  -1798   5537       N  
ATOM    521  CA  HIS A 135     -86.873 -10.982   1.305  1.00175.24           C  
ANISOU  521  CA  HIS A 135    17726  23084  25771   1697  -1949   5588       C  
ATOM    522  C   HIS A 135     -87.127 -11.258  -0.179  1.00176.40           C  
ANISOU  522  C   HIS A 135    17942  23265  25816   1433  -2418   5909       C  
ATOM    523  O   HIS A 135     -87.384 -10.334  -0.961  1.00179.03           O  
ANISOU  523  O   HIS A 135    18276  23434  26314   1549  -2622   6140       O  
ATOM    524  CB  HIS A 135     -85.364 -10.837   1.570  1.00176.31           C  
ANISOU  524  CB  HIS A 135    18344  23038  25609   1623  -1745   5234       C  
ATOM    525  CG  HIS A 135     -84.629 -10.020   0.561  1.00176.26           C  
ANISOU  525  CG  HIS A 135    18678  22767  25527   1571  -1914   5297       C  
ATOM    526  ND1 HIS A 135     -85.157  -8.866  -0.010  1.00179.84           N  
ANISOU  526  ND1 HIS A 135    19032  23021  26277   1783  -2063   5550       N  
ATOM    527  CD2 HIS A 135     -83.396 -10.159   0.013  1.00173.40           C  
ANISOU  527  CD2 HIS A 135    18750  22304  24832   1334  -1950   5157       C  
ATOM    528  CE1 HIS A 135     -84.286  -8.360  -0.854  1.00179.13           C  
ANISOU  528  CE1 HIS A 135    19312  22724  26025   1657  -2183   5576       C  
ATOM    529  NE2 HIS A 135     -83.207  -9.123  -0.861  1.00175.26           N  
ANISOU  529  NE2 HIS A 135    19141  22300  25151   1384  -2106   5336       N  
ATOM    530  N   ILE A 136     -87.063 -12.531  -0.560  1.00177.57           N  
ANISOU  530  N   ILE A 136    18160  23618  25688   1081  -2596   5923       N  
ATOM    531  CA  ILE A 136     -87.044 -12.900  -1.972  1.00178.16           C  
ANISOU  531  CA  ILE A 136    18416  23725  25554    787  -3026   6141       C  
ATOM    532  C   ILE A 136     -88.201 -13.804  -2.392  1.00180.63           C  
ANISOU  532  C   ILE A 136    18390  24295  25948    599  -3349   6411       C  
ATOM    533  O   ILE A 136     -88.749 -13.628  -3.485  1.00183.46           O  
ANISOU  533  O   ILE A 136    18695  24673  26336    515  -3741   6710       O  
ATOM    534  CB  ILE A 136     -85.708 -13.599  -2.341  1.00177.47           C  
ANISOU  534  CB  ILE A 136    18829  23606  24994    485  -3013   5885       C  
ATOM    535  CG1 ILE A 136     -84.533 -12.605  -2.273  1.00175.69           C  
ANISOU  535  CG1 ILE A 136    18957  23114  24684    614  -2792   5687       C  
ATOM    536  CG2 ILE A 136     -85.800 -14.277  -3.709  1.00178.30           C  
ANISOU  536  CG2 ILE A 136    19098  23814  24835    150  -3448   6074       C  
ATOM    537  CD1 ILE A 136     -84.705 -11.342  -3.120  1.00178.65           C  
ANISOU  537  CD1 ILE A 136    19375  23286  25218    757  -2969   5948       C  
ATOM    538  N   TYR A 137     -88.574 -14.761  -1.540  1.00176.85           N  
ANISOU  538  N   TYR A 137    17682  24011  25501    523  -3201   6319       N  
ATOM    539  CA  TYR A 137     -89.620 -15.722  -1.895  1.00179.20           C  
ANISOU  539  CA  TYR A 137    17662  24547  25880    295  -3507   6560       C  
ATOM    540  C   TYR A 137     -90.893 -15.033  -2.375  1.00184.17           C  
ANISOU  540  C   TYR A 137    17853  25230  26894    465  -3766   6942       C  
ATOM    541  O   TYR A 137     -91.570 -14.353  -1.606  1.00186.37           O  
ANISOU  541  O   TYR A 137    17747  25521  27544    797  -3541   7007       O  
ATOM    542  CB  TYR A 137     -89.968 -16.632  -0.718  1.00179.57           C  
ANISOU  542  CB  TYR A 137    17446  24779  26003    255  -3245   6450       C  
ATOM    543  CG  TYR A 137     -90.890 -17.763  -1.122  1.00181.74           C  
ANISOU  543  CG  TYR A 137    17451  25275  26328    -58  -3576   6675       C  
ATOM    544  CD1 TYR A 137     -90.932 -18.208  -2.440  1.00182.66           C  
ANISOU  544  CD1 TYR A 137    17748  25398  26255   -360  -4053   6816       C  
ATOM    545  CD2 TYR A 137     -91.735 -18.371  -0.201  1.00183.28           C  
ANISOU  545  CD2 TYR A 137    17208  25674  26755    -60  -3417   6752       C  
ATOM    546  CE1 TYR A 137     -91.775 -19.227  -2.827  1.00184.97           C  
ANISOU  546  CE1 TYR A 137    17805  25873  26604   -661  -4387   7006       C  
ATOM    547  CE2 TYR A 137     -92.585 -19.397  -0.582  1.00185.60           C  
ANISOU  547  CE2 TYR A 137    17243  26153  27124   -374  -3736   6970       C  
ATOM    548  CZ  TYR A 137     -92.598 -19.818  -1.898  1.00186.43           C  
ANISOU  548  CZ  TYR A 137    17543  26237  27053   -675  -4234   7087       C  
ATOM    549  OH  TYR A 137     -93.433 -20.835  -2.295  1.00189.01           O  
ANISOU  549  OH  TYR A 137    17627  26728  27458  -1005  -4582   7285       O  
ATOM    550  N   LYS A 138     -91.210 -15.213  -3.653  1.00182.73           N  
ANISOU  550  N   LYS A 138    17730  25084  26613    245  -4244   7186       N  
ATOM    551  CA  LYS A 138     -92.429 -14.647  -4.220  1.00187.77           C  
ANISOU  551  CA  LYS A 138    17952  25790  27602    374  -4565   7579       C  
ATOM    552  C   LYS A 138     -93.238 -15.733  -4.923  1.00190.08           C  
ANISOU  552  C   LYS A 138    18048  26316  27858     16  -5015   7796       C  
ATOM    553  O   LYS A 138     -94.453 -15.856  -4.729  1.00193.82           O  
ANISOU  553  O   LYS A 138    17978  26966  28696     67  -5139   8045       O  
ATOM    554  CB  LYS A 138     -92.095 -13.513  -5.193  1.00184.44           C  
ANISOU  554  CB  LYS A 138    17789  25154  27134    505  -4766   7728       C  
ATOM    555  CG  LYS A 138     -91.435 -12.306  -4.543  1.00183.12           C  
ANISOU  555  CG  LYS A 138    17768  24722  27088    872  -4367   7556       C  
ATOM    556  CD  LYS A 138     -92.405 -11.150  -4.352  1.00187.58           C  
ANISOU  556  CD  LYS A 138    17904  25205  28161   1284  -4367   7811       C  
ATOM    557  CE  LYS A 138     -91.702  -9.964  -3.714  1.00186.45           C  
ANISOU  557  CE  LYS A 138    17950  24758  28135   1634  -3983   7606       C  
ATOM    558  NZ  LYS A 138     -92.540  -8.736  -3.694  1.00191.10           N  
ANISOU  558  NZ  LYS A 138    18200  25200  29209   2050  -4020   7852       N  
ATOM    559  N   THR A 139     -92.548 -16.515  -5.745  1.00191.30           N  
ANISOU  559  N   THR A 139    18644  26468  27573   -346  -5258   7688       N  
ATOM    560  CA  THR A 139     -93.143 -17.677  -6.388  1.00193.11           C  
ANISOU  560  CA  THR A 139    18781  26887  27704   -732  -5681   7813       C  
ATOM    561  C   THR A 139     -92.130 -18.833  -6.431  1.00189.11           C  
ANISOU  561  C   THR A 139    18745  26359  26748  -1065  -5628   7482       C  
ATOM    562  O   THR A 139     -92.359 -19.856  -5.793  1.00188.40           O  
ANISOU  562  O   THR A 139    18504  26375  26703  -1239  -5545   7391       O  
ATOM    563  CB  THR A 139     -93.666 -17.345  -7.811  1.00188.28           C  
ANISOU  563  CB  THR A 139    18188  26311  27040   -838  -6248   8134       C  
ATOM    564  OG1 THR A 139     -94.530 -16.203  -7.751  1.00192.04           O  
ANISOU  564  OG1 THR A 139    18242  26773  27952   -487  -6285   8440       O  
ATOM    565  CG2 THR A 139     -94.423 -18.525  -8.391  1.00190.84           C  
ANISOU  565  CG2 THR A 139    18352  26839  27319  -1230  -6707   8265       C  
ATOM    566  N   PRO A 140     -90.987 -18.664  -7.130  1.00190.92           N  
ANISOU  566  N   PRO A 140    19537  26446  26558  -1142  -5648   7303       N  
ATOM    567  CA  PRO A 140     -90.130 -19.839  -7.298  1.00187.91           C  
ANISOU  567  CA  PRO A 140    19569  26060  25767  -1463  -5657   7007       C  
ATOM    568  C   PRO A 140     -89.227 -20.065  -6.088  1.00183.45           C  
ANISOU  568  C   PRO A 140    19142  25407  25154  -1355  -5137   6665       C  
ATOM    569  O   PRO A 140     -89.472 -19.451  -5.047  1.00183.15           O  
ANISOU  569  O   PRO A 140    18813  25353  25423  -1064  -4794   6674       O  
ATOM    570  CB  PRO A 140     -89.312 -19.478  -8.531  1.00184.02           C  
ANISOU  570  CB  PRO A 140    19579  25478  24861  -1555  -5860   6972       C  
ATOM    571  CG  PRO A 140     -89.104 -17.997  -8.374  1.00184.10           C  
ANISOU  571  CG  PRO A 140    19564  25347  25040  -1196  -5641   7075       C  
ATOM    572  CD  PRO A 140     -90.306 -17.450  -7.624  1.00186.85           C  
ANISOU  572  CD  PRO A 140    19312  25753  25928   -931  -5581   7320       C  
ATOM    573  N   TYR A 141     -88.232 -20.947  -6.219  1.00179.47           N  
ANISOU  573  N   TYR A 141    19064  24854  24275  -1578  -5091   6369       N  
ATOM    574  CA  TYR A 141     -87.243 -21.213  -5.165  1.00175.26           C  
ANISOU  574  CA  TYR A 141    18714  24232  23646  -1495  -4639   6035       C  
ATOM    575  C   TYR A 141     -86.694 -19.926  -4.563  1.00173.65           C  
ANISOU  575  C   TYR A 141    18533  23899  23548  -1137  -4259   5962       C  
ATOM    576  O   TYR A 141     -86.491 -18.950  -5.278  1.00174.57           O  
ANISOU  576  O   TYR A 141    18783  23927  23621  -1027  -4345   6064       O  
ATOM    577  CB  TYR A 141     -86.091 -22.056  -5.716  1.00170.33           C  
ANISOU  577  CB  TYR A 141    18611  23540  22568  -1739  -4688   5742       C  
ATOM    578  CG  TYR A 141     -85.815 -21.843  -7.194  1.00171.82           C  
ANISOU  578  CG  TYR A 141    19125  23715  22445  -1883  -5030   5804       C  
ATOM    579  CD1 TYR A 141     -85.441 -20.597  -7.684  1.00172.12           C  
ANISOU  579  CD1 TYR A 141    19292  23672  22433  -1696  -4979   5894       C  
ATOM    580  CD2 TYR A 141     -85.921 -22.895  -8.097  1.00173.23           C  
ANISOU  580  CD2 TYR A 141    19499  23957  22365  -2213  -5404   5771       C  
ATOM    581  CE1 TYR A 141     -85.191 -20.406  -9.034  1.00173.81           C  
ANISOU  581  CE1 TYR A 141    19813  23896  22330  -1836  -5281   5976       C  
ATOM    582  CE2 TYR A 141     -85.670 -22.713  -9.443  1.00174.93           C  
ANISOU  582  CE2 TYR A 141    20030  24188  22249  -2344  -5709   5819       C  
ATOM    583  CZ  TYR A 141     -85.306 -21.471  -9.907  1.00175.21           C  
ANISOU  583  CZ  TYR A 141    20183  24169  22220  -2156  -5639   5933       C  
ATOM    584  OH  TYR A 141     -85.060 -21.304 -11.251  1.00177.21           O  
ANISOU  584  OH  TYR A 141    20761  24459  22112  -2297  -5934   6004       O  
ATOM    585  N   TYR A 142     -86.439 -19.921  -3.258  1.00168.64           N  
ANISOU  585  N   TYR A 142    17788  23246  23042   -964  -3850   5785       N  
ATOM    586  CA  TYR A 142     -86.211 -18.652  -2.566  1.00168.10           C  
ANISOU  586  CA  TYR A 142    17643  23065  23163   -601  -3513   5742       C  
ATOM    587  C   TYR A 142     -84.827 -18.381  -1.964  1.00164.18           C  
ANISOU  587  C   TYR A 142    17502  22419  22462   -498  -3148   5391       C  
ATOM    588  O   TYR A 142     -83.906 -19.195  -2.047  1.00161.48           O  
ANISOU  588  O   TYR A 142    17486  22059  21810   -693  -3121   5158       O  
ATOM    589  CB  TYR A 142     -87.242 -18.492  -1.454  1.00170.69           C  
ANISOU  589  CB  TYR A 142    17466  23506  23882   -389  -3311   5860       C  
ATOM    590  CG  TYR A 142     -87.416 -19.693  -0.559  1.00169.67           C  
ANISOU  590  CG  TYR A 142    17206  23518  23742   -538  -3175   5764       C  
ATOM    591  CD1 TYR A 142     -86.418 -20.076   0.329  1.00166.11           C  
ANISOU  591  CD1 TYR A 142    17002  23015  23096   -522  -2846   5448       C  
ATOM    592  CD2 TYR A 142     -88.594 -20.428  -0.580  1.00172.60           C  
ANISOU  592  CD2 TYR A 142    17191  24074  24314   -698  -3382   6011       C  
ATOM    593  CE1 TYR A 142     -86.581 -21.172   1.152  1.00165.47           C  
ANISOU  593  CE1 TYR A 142    16815  23054  23004   -658  -2730   5392       C  
ATOM    594  CE2 TYR A 142     -88.771 -21.519   0.243  1.00172.02           C  
ANISOU  594  CE2 TYR A 142    16997  24116  24246   -851  -3256   5957       C  
ATOM    595  CZ  TYR A 142     -87.763 -21.886   1.110  1.00168.46           C  
ANISOU  595  CZ  TYR A 142    16819  23602  23584   -825  -2928   5654       C  
ATOM    596  OH  TYR A 142     -87.940 -22.977   1.931  1.00168.15           O  
ANISOU  596  OH  TYR A 142    16674  23670  23547   -980  -2812   5631       O  
ATOM    597  N   ILE A 143     -84.725 -17.194  -1.360  1.00164.41           N  
ANISOU  597  N   ILE A 143    17446  22331  22692   -177  -2881   5359       N  
ATOM    598  CA  ILE A 143     -83.497 -16.626  -0.800  1.00161.46           C  
ANISOU  598  CA  ILE A 143    17364  21791  22194    -37  -2552   5057       C  
ATOM    599  C   ILE A 143     -83.830 -15.876   0.496  1.00162.00           C  
ANISOU  599  C   ILE A 143    17165  21829  22559    305  -2202   4984       C  
ATOM    600  O   ILE A 143     -84.782 -15.094   0.513  1.00165.13           O  
ANISOU  600  O   ILE A 143    17248  22218  23275    520  -2235   5202       O  
ATOM    601  CB  ILE A 143     -82.830 -15.628  -1.785  1.00158.73           C  
ANISOU  601  CB  ILE A 143    17309  21256  21746    -12  -2652   5097       C  
ATOM    602  CG1 ILE A 143     -82.834 -16.163  -3.219  1.00159.66           C  
ANISOU  602  CG1 ILE A 143    17623  21436  21604   -308  -3043   5257       C  
ATOM    603  CG2 ILE A 143     -81.428 -15.247  -1.332  1.00155.60           C  
ANISOU  603  CG2 ILE A 143    17243  20699  21179     45  -2353   4770       C  
ATOM    604  CD1 ILE A 143     -82.373 -15.157  -4.242  1.00160.77           C  
ANISOU  604  CD1 ILE A 143    18006  21425  21653   -288  -3161   5378       C  
ATOM    605  N   GLY A 144     -83.074 -16.090   1.575  1.00152.93           N  
ANISOU  605  N   GLY A 144    16133  20666  21306    371  -1875   4679       N  
ATOM    606  CA  GLY A 144     -81.976 -17.033   1.618  1.00149.52           C  
ANISOU  606  CA  GLY A 144    16036  20244  20532    145  -1836   4429       C  
ATOM    607  C   GLY A 144     -82.354 -18.269   2.402  1.00148.97           C  
ANISOU  607  C   GLY A 144    15811  20361  20428     29  -1773   4397       C  
ATOM    608  O   GLY A 144     -83.167 -19.066   1.948  1.00150.52           O  
ANISOU  608  O   GLY A 144    15840  20690  20661   -161  -2017   4605       O  
ATOM    609  N   SER A 145     -81.765 -18.440   3.579  1.00147.91           N  
ANISOU  609  N   SER A 145    15738  20238  20224    130  -1461   4146       N  
ATOM    610  CA  SER A 145     -82.196 -19.510   4.471  1.00147.87           C  
ANISOU  610  CA  SER A 145    15560  20411  20212     52  -1364   4151       C  
ATOM    611  C   SER A 145     -83.153 -18.981   5.530  1.00150.24           C  
ANISOU  611  C   SER A 145    15472  20828  20785    320  -1113   4240       C  
ATOM    612  O   SER A 145     -83.282 -17.770   5.720  1.00151.44           O  
ANISOU  612  O   SER A 145    15541  20890  21111    598   -974   4218       O  
ATOM    613  CB  SER A 145     -81.014 -20.186   5.154  1.00143.60           C  
ANISOU  613  CB  SER A 145    15316  19846  19400    -16  -1192   3849       C  
ATOM    614  OG  SER A 145     -81.458 -20.879   6.311  1.00144.03           O  
ANISOU  614  OG  SER A 145    15177  20062  19487      4  -1007   3859       O  
ATOM    615  N   GLY A 146     -83.837 -19.896   6.208  1.00153.51           N  
ANISOU  615  N   GLY A 146    15646  21437  21243    235  -1051   4346       N  
ATOM    616  CA  GLY A 146     -84.796 -19.515   7.226  1.00156.16           C  
ANISOU  616  CA  GLY A 146    15587  21931  21816    475   -788   4444       C  
ATOM    617  C   GLY A 146     -84.470 -20.072   8.595  1.00155.15           C  
ANISOU  617  C   GLY A 146    15484  21926  21540    519   -466   4274       C  
ATOM    618  O   GLY A 146     -85.344 -20.180   9.454  1.00157.58           O  
ANISOU  618  O   GLY A 146    15452  22433  21989    627   -259   4395       O  
ATOM    619  N   VAL A 147     -83.210 -20.436   8.793  1.00146.19           N  
ANISOU  619  N   VAL A 147    14745  20687  20114    435   -423   4006       N  
ATOM    620  CA  VAL A 147     -82.750 -20.977  10.064  1.00145.13           C  
ANISOU  620  CA  VAL A 147    14691  20655  19796    471   -151   3836       C  
ATOM    621  C   VAL A 147     -81.398 -20.306  10.294  1.00142.42           C  
ANISOU  621  C   VAL A 147    14719  20134  19262    607    -30   3483       C  
ATOM    622  O   VAL A 147     -80.864 -19.714   9.354  1.00141.31           O  
ANISOU  622  O   VAL A 147    14765  19804  19124    591   -192   3418       O  
ATOM    623  CB  VAL A 147     -82.675 -22.525  10.032  1.00144.37           C  
ANISOU  623  CB  VAL A 147    14670  20634  19551    141   -303   3930       C  
ATOM    624  CG1 VAL A 147     -81.838 -23.000   8.852  1.00141.96           C  
ANISOU  624  CG1 VAL A 147    14703  20144  19090   -100   -621   3850       C  
ATOM    625  CG2 VAL A 147     -82.179 -23.098  11.355  1.00143.52           C  
ANISOU  625  CG2 VAL A 147    14660  20629  19241    178    -38   3785       C  
ATOM    626  N   LEU A 148     -80.866 -20.353  11.520  1.00141.22           N  
ANISOU  626  N   LEU A 148    14663  20047  18948    735    245   3268       N  
ATOM    627  CA  LEU A 148     -79.622 -19.645  11.853  1.00139.14           C  
ANISOU  627  CA  LEU A 148    14712  19625  18528    874    363   2924       C  
ATOM    628  C   LEU A 148     -78.523 -19.828  10.812  1.00136.31           C  
ANISOU  628  C   LEU A 148    14684  19071  18036    680    122   2812       C  
ATOM    629  O   LEU A 148     -77.840 -20.851  10.784  1.00134.36           O  
ANISOU  629  O   LEU A 148    14631  18833  17587    484     31   2747       O  
ATOM    630  CB  LEU A 148     -79.086 -20.072  13.225  1.00138.53           C  
ANISOU  630  CB  LEU A 148    14741  19672  18223    945    607   2727       C  
ATOM    631  CG  LEU A 148     -79.664 -19.325  14.427  1.00141.12           C  
ANISOU  631  CG  LEU A 148    14875  20136  18607   1252    941   2655       C  
ATOM    632  CD1 LEU A 148     -78.935 -19.664  15.701  1.00140.43           C  
ANISOU  632  CD1 LEU A 148    14967  20155  18235   1314   1149   2425       C  
ATOM    633  CD2 LEU A 148     -79.608 -17.836  14.183  1.00141.99           C  
ANISOU  633  CD2 LEU A 148    14991  20062  18897   1504   1002   2508       C  
ATOM    634  N   SER A 149     -78.386 -18.826   9.945  1.00137.25           N  
ANISOU  634  N   SER A 149    14856  19014  18278    743     25   2804       N  
ATOM    635  CA  SER A 149     -77.371 -18.812   8.896  1.00135.08           C  
ANISOU  635  CA  SER A 149    14878  18565  17883    579   -169   2710       C  
ATOM    636  C   SER A 149     -76.473 -17.616   9.125  1.00134.45           C  
ANISOU  636  C   SER A 149    14972  18305  17808    757    -29   2454       C  
ATOM    637  O   SER A 149     -76.617 -16.589   8.465  1.00135.53           O  
ANISOU  637  O   SER A 149    15097  18291  18108    839    -83   2516       O  
ATOM    638  CB  SER A 149     -77.984 -18.730   7.499  1.00138.41           C  
ANISOU  638  CB  SER A 149    15231  18936  18422    444   -448   2972       C  
ATOM    639  OG  SER A 149     -78.483 -19.979   7.081  1.00138.53           O  
ANISOU  639  OG  SER A 149    15183  19074  18380    202   -645   3152       O  
ATOM    640  N   VAL A 150     -75.541 -17.754  10.060  1.00132.13           N  
ANISOU  640  N   VAL A 150    14844  18019  17342    806    134   2177       N  
ATOM    641  CA  VAL A 150     -74.646 -16.661  10.405  1.00131.76           C  
ANISOU  641  CA  VAL A 150    14959  17802  17302    958    263   1907       C  
ATOM    642  C   VAL A 150     -73.657 -16.427   9.264  1.00130.18           C  
ANISOU  642  C   VAL A 150    14992  17422  17048    793     99   1857       C  
ATOM    643  O   VAL A 150     -73.057 -17.371   8.753  1.00128.36           O  
ANISOU  643  O   VAL A 150    14903  17231  16636    581    -29   1848       O  
ATOM    644  CB  VAL A 150     -73.901 -16.952  11.711  1.00130.81           C  
ANISOU  644  CB  VAL A 150    14950  17762  16992   1034    447   1626       C  
ATOM    645  CG1 VAL A 150     -72.765 -15.979  11.893  1.00130.18           C  
ANISOU  645  CG1 VAL A 150    15075  17490  16898   1114    513   1330       C  
ATOM    646  CG2 VAL A 150     -74.859 -16.871  12.889  1.00133.03           C  
ANISOU  646  CG2 VAL A 150    15010  18213  17321   1244    662   1653       C  
ATOM    647  N   MET A 151     -73.510 -15.173   8.850  1.00131.20           N  
ANISOU  647  N   MET A 151    15159  17351  17339    892    110   1835       N  
ATOM    648  CA  MET A 151     -72.605 -14.844   7.758  1.00130.20           C  
ANISOU  648  CA  MET A 151    15241  17062  17165    734    -19   1819       C  
ATOM    649  C   MET A 151     -71.481 -13.920   8.204  1.00129.83           C  
ANISOU  649  C   MET A 151    15362  16835  17131    808    110   1533       C  
ATOM    650  O   MET A 151     -71.662 -13.088   9.091  1.00131.21           O  
ANISOU  650  O   MET A 151    15480  16932  17442   1025    263   1397       O  
ATOM    651  CB  MET A 151     -73.364 -14.209   6.601  1.00132.03           C  
ANISOU  651  CB  MET A 151    15396  17196  17575    719   -177   2111       C  
ATOM    652  CG  MET A 151     -74.418 -15.098   6.002  1.00132.66           C  
ANISOU  652  CG  MET A 151    15315  17444  17645    606   -356   2399       C  
ATOM    653  SD  MET A 151     -74.701 -14.680   4.278  1.00133.98           S  
ANISOU  653  SD  MET A 151    15537  17511  17857    460   -628   2698       S  
ATOM    654  CE  MET A 151     -73.273 -15.473   3.559  1.00131.32           C  
ANISOU  654  CE  MET A 151    15525  17186  17184    183   -697   2532       C  
ATOM    655  N   GLY A 152     -70.311 -14.087   7.594  1.00129.41           N  
ANISOU  655  N   GLY A 152    15510  16721  16937    625     47   1431       N  
ATOM    656  CA  GLY A 152     -69.168 -13.248   7.906  1.00129.22           C  
ANISOU  656  CA  GLY A 152    15633  16526  16938    647    143   1176       C  
ATOM    657  C   GLY A 152     -68.040 -13.435   6.907  1.00127.95           C  
ANISOU  657  C   GLY A 152    15648  16319  16647    417     59   1154       C  
ATOM    658  O   GLY A 152     -68.054 -14.387   6.140  1.00126.93           O  
ANISOU  658  O   GLY A 152    15553  16317  16358    256    -56   1276       O  
ATOM    659  N   VAL A 153     -67.064 -12.530   6.916  1.00131.29           N  
ANISOU  659  N   VAL A 153    16181  16562  17142    398    122    991       N  
ATOM    660  CA  VAL A 153     -65.982 -12.521   5.920  1.00130.68           C  
ANISOU  660  CA  VAL A 153    16247  16436  16969    181     76    989       C  
ATOM    661  C   VAL A 153     -65.154 -13.821   5.857  1.00128.50           C  
ANISOU  661  C   VAL A 153    16038  16354  16431     40     57    860       C  
ATOM    662  O   VAL A 153     -64.710 -14.339   6.884  1.00127.41           O  
ANISOU  662  O   VAL A 153    15888  16303  16217    103    119    632       O  
ATOM    663  CB  VAL A 153     -65.021 -11.351   6.191  1.00128.48           C  
ANISOU  663  CB  VAL A 153    16045  15934  16837    182    166    805       C  
ATOM    664  CG1 VAL A 153     -64.014 -11.222   5.066  1.00128.45           C  
ANISOU  664  CG1 VAL A 153    16158  15884  16761    -48    140    860       C  
ATOM    665  CG2 VAL A 153     -65.802 -10.061   6.355  1.00130.92           C  
ANISOU  665  CG2 VAL A 153    16305  16010  17430    348    187    898       C  
ATOM    666  N   SER A 154     -64.929 -14.323   4.642  1.00128.35           N  
ANISOU  666  N   SER A 154    16098  16397  16272   -140    -33   1000       N  
ATOM    667  CA  SER A 154     -64.216 -15.587   4.435  1.00126.68           C  
ANISOU  667  CA  SER A 154    15956  16353  15825   -258    -60    886       C  
ATOM    668  C   SER A 154     -62.682 -15.445   4.552  1.00126.15           C  
ANISOU  668  C   SER A 154    15960  16259  15710   -333     37    637       C  
ATOM    669  O   SER A 154     -62.138 -14.350   4.411  1.00127.24           O  
ANISOU  669  O   SER A 154    16119  16247  15980   -363    105    609       O  
ATOM    670  CB  SER A 154     -64.598 -16.185   3.076  1.00127.21           C  
ANISOU  670  CB  SER A 154    16092  16501  15741   -410   -193   1106       C  
ATOM    671  OG  SER A 154     -64.031 -17.470   2.887  1.00125.91           O  
ANISOU  671  OG  SER A 154    16000  16479  15360   -500   -226    984       O  
ATOM    672  N   PHE A 155     -61.994 -16.550   4.836  1.00120.70           N  
ANISOU  672  N   PHE A 155    15296  15707  14858   -362     38    464       N  
ATOM    673  CA  PHE A 155     -60.533 -16.557   4.936  1.00120.37           C  
ANISOU  673  CA  PHE A 155    15285  15673  14776   -426    118    231       C  
ATOM    674  C   PHE A 155     -59.872 -16.937   3.636  1.00120.63           C  
ANISOU  674  C   PHE A 155    15402  15769  14661   -595    119    278       C  
ATOM    675  O   PHE A 155     -58.664 -16.844   3.510  1.00120.80           O  
ANISOU  675  O   PHE A 155    15428  15806  14666   -665    203    120       O  
ATOM    676  CB  PHE A 155     -60.071 -17.534   6.009  1.00120.91           C  
ANISOU  676  CB  PHE A 155    15324  15854  14761   -339    115     10       C  
ATOM    677  CG  PHE A 155     -60.333 -17.079   7.398  1.00120.99           C  
ANISOU  677  CG  PHE A 155    15268  15825  14877   -182    150   -108       C  
ATOM    678  CD1 PHE A 155     -60.852 -15.823   7.644  1.00122.23           C  
ANISOU  678  CD1 PHE A 155    15395  15833  15215   -115    196    -60       C  
ATOM    679  CD2 PHE A 155     -60.075 -17.918   8.467  1.00120.12           C  
ANISOU  679  CD2 PHE A 155    15139  15824  14675    -90    134   -269       C  
ATOM    680  CE1 PHE A 155     -61.092 -15.404   8.940  1.00122.65           C  
ANISOU  680  CE1 PHE A 155    15404  15858  15339     46    241   -202       C  
ATOM    681  CE2 PHE A 155     -60.313 -17.507   9.766  1.00120.51           C  
ANISOU  681  CE2 PHE A 155    15147  15865  14776     57    172   -385       C  
ATOM    682  CZ  PHE A 155     -60.822 -16.244  10.003  1.00121.80           C  
ANISOU  682  CZ  PHE A 155    15285  15891  15103    128    233   -366       C  
ATOM    683  N   SER A 156     -60.663 -17.348   2.657  1.00120.62           N  
ANISOU  683  N   SER A 156    15464  15819  14548   -661     26    493       N  
ATOM    684  CA  SER A 156     -60.112 -17.760   1.378  1.00121.22           C  
ANISOU  684  CA  SER A 156    15646  15977  14434   -814     29    531       C  
ATOM    685  C   SER A 156     -59.579 -16.538   0.667  1.00122.85           C  
ANISOU  685  C   SER A 156    15879  16091  14709   -922    124    624       C  
ATOM    686  O   SER A 156     -58.589 -16.604  -0.074  1.00123.57           O  
ANISOU  686  O   SER A 156    16021  16248  14682  -1043    216    566       O  
ATOM    687  CB  SER A 156     -61.169 -18.455   0.525  1.00123.56           C  
ANISOU  687  CB  SER A 156    16018  16346  14582   -865   -124    735       C  
ATOM    688  OG  SER A 156     -62.313 -17.634   0.378  1.00124.53           O  
ANISOU  688  OG  SER A 156    16101  16379  14836   -839   -202    990       O  
ATOM    689  N   ILE A 157     -60.254 -15.417   0.886  1.00123.75           N  
ANISOU  689  N   ILE A 157    15953  16044  15022   -876    109    778       N  
ATOM    690  CA  ILE A 157     -59.879 -14.188   0.213  1.00125.67           C  
ANISOU  690  CA  ILE A 157    16231  16154  15362   -984    177    914       C  
ATOM    691  C   ILE A 157     -58.521 -13.682   0.683  1.00125.90           C  
ANISOU  691  C   ILE A 157    16212  16127  15498  -1035    325    691       C  
ATOM    692  O   ILE A 157     -57.832 -13.013  -0.068  1.00127.53           O  
ANISOU  692  O   ILE A 157    16454  16288  15715  -1186    412    772       O  
ATOM    693  CB  ILE A 157     -60.929 -13.079   0.399  1.00126.89           C  
ANISOU  693  CB  ILE A 157    16354  16111  15748   -896    114   1122       C  
ATOM    694  CG1 ILE A 157     -60.769 -12.043  -0.712  1.00129.28           C  
ANISOU  694  CG1 ILE A 157    16741  16295  16086  -1041    132   1370       C  
ATOM    695  CG2 ILE A 157     -60.847 -12.455   1.789  1.00126.54           C  
ANISOU  695  CG2 ILE A 157    16212  15919  15950   -745    173    925       C  
ATOM    696  CD1 ILE A 157     -60.987 -12.619  -2.089  1.00130.05           C  
ANISOU  696  CD1 ILE A 157    16955  16555  15902  -1179     60   1580       C  
ATOM    697  N   ILE A 158     -58.130 -14.003   1.912  1.00124.55           N  
ANISOU  697  N   ILE A 158    15954  15967  15401   -921    347    426       N  
ATOM    698  CA  ILE A 158     -56.795 -13.646   2.386  1.00124.90           C  
ANISOU  698  CA  ILE A 158    15932  15984  15540   -977    455    195       C  
ATOM    699  C   ILE A 158     -55.732 -14.420   1.624  1.00124.95           C  
ANISOU  699  C   ILE A 158    15945  16174  15355  -1101    536    115       C  
ATOM    700  O   ILE A 158     -54.837 -13.835   1.020  1.00126.53           O  
ANISOU  700  O   ILE A 158    16129  16358  15589  -1254    648    134       O  
ATOM    701  CB  ILE A 158     -56.626 -13.919   3.882  1.00123.65           C  
ANISOU  701  CB  ILE A 158    15690  15827  15462   -820    431    -73       C  
ATOM    702  CG1 ILE A 158     -57.464 -12.939   4.690  1.00124.25           C  
ANISOU  702  CG1 ILE A 158    15754  15709  15746   -696    399    -46       C  
ATOM    703  CG2 ILE A 158     -55.188 -13.751   4.286  1.00124.12           C  
ANISOU  703  CG2 ILE A 158    15669  15901  15590   -891    508   -317       C  
ATOM    704  CD1 ILE A 158     -57.564 -13.305   6.145  1.00123.20           C  
ANISOU  704  CD1 ILE A 158    15568  15617  15626   -522    370   -278       C  
ATOM    705  N   SER A 159     -55.860 -15.742   1.641  1.00123.49           N  
ANISOU  705  N   SER A 159    15783  16160  14978  -1032    483     32       N  
ATOM    706  CA  SER A 159     -54.934 -16.621   0.945  1.00123.67           C  
ANISOU  706  CA  SER A 159    15819  16360  14811  -1105    557    -73       C  
ATOM    707  C   SER A 159     -54.796 -16.233  -0.524  1.00125.57           C  
ANISOU  707  C   SER A 159    16150  16642  14919  -1279    640    128       C  
ATOM    708  O   SER A 159     -53.703 -16.298  -1.082  1.00126.76           O  
ANISOU  708  O   SER A 159    16268  16896  14998  -1381    783     48       O  
ATOM    709  CB  SER A 159     -55.382 -18.081   1.068  1.00123.42           C  
ANISOU  709  CB  SER A 159    15841  16453  14601   -999    453   -145       C  
ATOM    710  OG  SER A 159     -54.445 -18.959   0.466  1.00123.84           O  
ANISOU  710  OG  SER A 159    15908  16658  14489  -1035    528   -287       O  
ATOM    711  N   VAL A 160     -55.898 -15.858  -1.165  1.00127.19           N  
ANISOU  711  N   VAL A 160    16462  16786  15078  -1310    551    398       N  
ATOM    712  CA  VAL A 160     -55.787 -15.341  -2.528  1.00129.40           C  
ANISOU  712  CA  VAL A 160    16843  17098  15223  -1483    619    624       C  
ATOM    713  C   VAL A 160     -55.078 -13.969  -2.576  1.00131.25           C  
ANISOU  713  C   VAL A 160    17016  17190  15664  -1607    750    699       C  
ATOM    714  O   VAL A 160     -54.144 -13.769  -3.364  1.00133.05           O  
ANISOU  714  O   VAL A 160    17246  17508  15799  -1763    907    724       O  
ATOM    715  CB  VAL A 160     -57.170 -15.249  -3.209  1.00128.83           C  
ANISOU  715  CB  VAL A 160    16897  16995  15057  -1485    456    918       C  
ATOM    716  CG1 VAL A 160     -57.122 -14.303  -4.388  1.00131.50           C  
ANISOU  716  CG1 VAL A 160    17332  17302  15330  -1655    509   1202       C  
ATOM    717  CG2 VAL A 160     -57.607 -16.625  -3.672  1.00128.06           C  
ANISOU  717  CG2 VAL A 160    16898  17075  14686  -1457    352    869       C  
ATOM    718  N   ALA A 161     -55.507 -13.037  -1.729  1.00131.54           N  
ANISOU  718  N   ALA A 161    16996  17002  15983  -1540    692    730       N  
ATOM    719  CA  ALA A 161     -54.982 -11.671  -1.740  1.00133.60           C  
ANISOU  719  CA  ALA A 161    17217  17064  16479  -1661    779    816       C  
ATOM    720  C   ALA A 161     -53.494 -11.566  -1.414  1.00134.21           C  
ANISOU  720  C   ALA A 161    17162  17186  16645  -1762    934    586       C  
ATOM    721  O   ALA A 161     -52.861 -10.558  -1.719  1.00136.45           O  
ANISOU  721  O   ALA A 161    17415  17349  17081  -1928   1032    680       O  
ATOM    722  CB  ALA A 161     -55.776 -10.796  -0.779  1.00131.91           C  
ANISOU  722  CB  ALA A 161    16978  16587  16556  -1530    675    834       C  
ATOM    723  N   SER A 162     -52.929 -12.584  -0.782  1.00134.28           N  
ANISOU  723  N   SER A 162    17081  17358  16582  -1667    945    299       N  
ATOM    724  CA  SER A 162     -51.501 -12.539  -0.505  1.00135.13           C  
ANISOU  724  CA  SER A 162    17030  17531  16780  -1755   1077     86       C  
ATOM    725  C   SER A 162     -50.738 -12.520  -1.823  1.00137.37           C  
ANISOU  725  C   SER A 162    17322  17970  16902  -1953   1260    218       C  
ATOM    726  O   SER A 162     -50.017 -11.566  -2.123  1.00139.71           O  
ANISOU  726  O   SER A 162    17549  18188  17348  -2139   1381    304       O  
ATOM    727  CB  SER A 162     -51.071 -13.732   0.354  1.00134.59           C  
ANISOU  727  CB  SER A 162    16868  17622  16649  -1595   1036   -223       C  
ATOM    728  OG  SER A 162     -51.158 -14.953  -0.365  1.00133.91           O  
ANISOU  728  OG  SER A 162    16854  17751  16276  -1551   1055   -230       O  
ATOM    729  N   GLY A 163     -50.963 -13.546  -2.635  1.00139.24           N  
ANISOU  729  N   GLY A 163    17658  18419  16826  -1920   1280    248       N  
ATOM    730  CA  GLY A 163     -50.314 -13.659  -3.926  1.00141.55           C  
ANISOU  730  CA  GLY A 163    17985  18901  16895  -2081   1467    356       C  
ATOM    731  C   GLY A 163     -50.767 -12.556  -4.855  1.00143.87           C  
ANISOU  731  C   GLY A 163    18405  19082  17175  -2258   1495    721       C  
ATOM    732  O   GLY A 163     -49.960 -11.996  -5.603  1.00146.61           O  
ANISOU  732  O   GLY A 163    18716  19490  17498  -2457   1686    843       O  
ATOM    733  N   ALA A 164     -52.059 -12.245  -4.800  1.00141.45           N  
ANISOU  733  N   ALA A 164    18236  18616  16893  -2185   1306    911       N  
ATOM    734  CA  ALA A 164     -52.623 -11.169  -5.606  1.00143.74           C  
ANISOU  734  CA  ALA A 164    18652  18761  17199  -2321   1286   1285       C  
ATOM    735  C   ALA A 164     -51.867  -9.863  -5.393  1.00145.93           C  
ANISOU  735  C   ALA A 164    18826  18832  17786  -2486   1396   1361       C  
ATOM    736  O   ALA A 164     -51.284  -9.319  -6.330  1.00148.84           O  
ANISOU  736  O   ALA A 164    19222  19249  18083  -2700   1553   1568       O  
ATOM    737  CB  ALA A 164     -54.097 -10.991  -5.284  1.00144.60           C  
ANISOU  737  CB  ALA A 164    18860  18699  17385  -2173   1048   1431       C  
ATOM    738  N   PHE A 165     -51.872  -9.377  -4.155  1.00144.10           N  
ANISOU  738  N   PHE A 165    18484  18375  17891  -2394   1314   1190       N  
ATOM    739  CA  PHE A 165     -51.186  -8.137  -3.793  1.00146.23           C  
ANISOU  739  CA  PHE A 165    18658  18401  18500  -2545   1379   1215       C  
ATOM    740  C   PHE A 165     -49.688  -8.189  -4.075  1.00148.01           C  
ANISOU  740  C   PHE A 165    18721  18793  18722  -2742   1600   1107       C  
ATOM    741  O   PHE A 165     -49.095  -7.189  -4.491  1.00151.04           O  
ANISOU  741  O   PHE A 165    19069  19052  19267  -2972   1711   1285       O  
ATOM    742  CB  PHE A 165     -51.408  -7.807  -2.317  1.00142.92           C  
ANISOU  742  CB  PHE A 165    18157  17753  18394  -2384   1242    966       C  
ATOM    743  CG  PHE A 165     -52.750  -7.220  -2.025  1.00142.55           C  
ANISOU  743  CG  PHE A 165    18235  17453  18477  -2237   1068   1120       C  
ATOM    744  CD1 PHE A 165     -53.573  -6.804  -3.059  1.00144.06           C  
ANISOU  744  CD1 PHE A 165    18581  17581  18576  -2286   1026   1495       C  
ATOM    745  CD2 PHE A 165     -53.187  -7.070  -0.720  1.00141.04           C  
ANISOU  745  CD2 PHE A 165    17999  17096  18495  -2041    949    894       C  
ATOM    746  CE1 PHE A 165     -54.804  -6.256  -2.800  1.00144.04           C  
ANISOU  746  CE1 PHE A 165    18661  17348  18721  -2132    864   1644       C  
ATOM    747  CE2 PHE A 165     -54.426  -6.523  -0.455  1.00141.05           C  
ANISOU  747  CE2 PHE A 165    18091  16876  18627  -1885    814   1028       C  
ATOM    748  CZ  PHE A 165     -55.234  -6.116  -1.496  1.00142.54           C  
ANISOU  748  CZ  PHE A 165    18408  16996  18756  -1926    770   1404       C  
ATOM    749  N   ASN A 166     -49.085  -9.348  -3.822  1.00148.91           N  
ANISOU  749  N   ASN A 166    18723  19177  18679  -2649   1661    822       N  
ATOM    750  CA  ASN A 166     -47.669  -9.543  -4.086  1.00150.67           C  
ANISOU  750  CA  ASN A 166    18754  19601  18893  -2799   1878    698       C  
ATOM    751  C   ASN A 166     -47.359  -9.276  -5.555  1.00153.82           C  
ANISOU  751  C   ASN A 166    19228  20149  19068  -3020   2085   1002       C  
ATOM    752  O   ASN A 166     -46.382  -8.599  -5.891  1.00156.81           O  
ANISOU  752  O   ASN A 166    19472  20534  19575  -3252   2269   1088       O  
ATOM    753  CB  ASN A 166     -47.248 -10.958  -3.705  1.00150.04           C  
ANISOU  753  CB  ASN A 166    18575  19791  18643  -2616   1891    371       C  
ATOM    754  CG  ASN A 166     -45.754 -11.152  -3.758  1.00151.89           C  
ANISOU  754  CG  ASN A 166    18555  20220  18938  -2727   2097    199       C  
ATOM    755  OD1 ASN A 166     -44.985 -10.200  -3.607  1.00154.20           O  
ANISOU  755  OD1 ASN A 166    18691  20402  19496  -2924   2178    238       O  
ATOM    756  ND2 ASN A 166     -45.330 -12.388  -3.985  1.00151.19           N  
ANISOU  756  ND2 ASN A 166    18413  20414  18620  -2603   2180      6       N  
ATOM    757  N   GLN A 167     -48.217  -9.787  -6.432  1.00151.75           N  
ANISOU  757  N   GLN A 167    19184  20009  18465  -2960   2049   1176       N  
ATOM    758  CA  GLN A 167     -48.046  -9.552  -7.858  1.00154.94           C  
ANISOU  758  CA  GLN A 167    19704  20573  18593  -3158   2227   1481       C  
ATOM    759  C   GLN A 167     -48.363  -8.101  -8.233  1.00157.62           C  
ANISOU  759  C   GLN A 167    20134  20633  19123  -3357   2204   1869       C  
ATOM    760  O   GLN A 167     -47.769  -7.550  -9.163  1.00161.18           O  
ANISOU  760  O   GLN A 167    20592  21162  19486  -3599   2404   2119       O  
ATOM    761  CB  GLN A 167     -48.918 -10.512  -8.678  1.00159.72           C  
ANISOU  761  CB  GLN A 167    20540  21383  18765  -3040   2155   1546       C  
ATOM    762  CG  GLN A 167     -48.591 -10.506 -10.169  1.00163.23           C  
ANISOU  762  CG  GLN A 167    21110  22079  18833  -3226   2365   1792       C  
ATOM    763  CD  GLN A 167     -47.111 -10.770 -10.457  1.00165.42           C  
ANISOU  763  CD  GLN A 167    21181  22616  19055  -3344   2692   1632       C  
ATOM    764  OE1 GLN A 167     -46.572 -10.302 -11.460  1.00169.13           O  
ANISOU  764  OE1 GLN A 167    21675  23229  19358  -3563   2922   1869       O  
ATOM    765  NE2 GLN A 167     -46.463 -11.557  -9.598  1.00163.39           N  
ANISOU  765  NE2 GLN A 167    20716  22439  18925  -3192   2716   1240       N  
ATOM    766  N   MET A 168     -49.311  -7.490  -7.525  1.00154.61           N  
ANISOU  766  N   MET A 168    19825  19924  18998  -3249   1967   1928       N  
ATOM    767  CA  MET A 168     -49.647  -6.086  -7.772  1.00157.28           C  
ANISOU  767  CA  MET A 168    20250  19935  19573  -3405   1916   2277       C  
ATOM    768  C   MET A 168     -48.519  -5.128  -7.388  1.00159.74           C  
ANISOU  768  C   MET A 168    20375  20071  20247  -3627   2051   2251       C  
ATOM    769  O   MET A 168     -48.373  -4.080  -8.010  1.00163.23           O  
ANISOU  769  O   MET A 168    20877  20342  20800  -3855   2115   2589       O  
ATOM    770  CB  MET A 168     -50.952  -5.700  -7.060  1.00155.66           C  
ANISOU  770  CB  MET A 168    20149  19420  19573  -3196   1637   2312       C  
ATOM    771  CG  MET A 168     -52.108  -6.643  -7.395  1.00153.42           C  
ANISOU  771  CG  MET A 168    20018  19305  18970  -2992   1483   2347       C  
ATOM    772  SD  MET A 168     -53.759  -6.135  -6.882  1.00152.22           S  
ANISOU  772  SD  MET A 168    19980  18837  19020  -2769   1181   2497       S  
ATOM    773  CE  MET A 168     -54.169  -5.021  -8.220  1.00156.53           C  
ANISOU  773  CE  MET A 168    20718  19238  19517  -2966   1163   3058       C  
ATOM    774  N   TYR A 169     -47.745  -5.463  -6.358  1.00156.21           N  
ANISOU  774  N   TYR A 169    19706  19651  19995  -3571   2072   1868       N  
ATOM    775  CA  TYR A 169     -46.574  -4.659  -5.990  1.00158.76           C  
ANISOU  775  CA  TYR A 169    19819  19844  20658  -3801   2189   1809       C  
ATOM    776  C   TYR A 169     -45.363  -5.051  -6.816  1.00161.16           C  
ANISOU  776  C   TYR A 169    19961  20499  20772  -4006   2488   1836       C  
ATOM    777  O   TYR A 169     -44.400  -4.302  -6.913  1.00164.37           O  
ANISOU  777  O   TYR A 169    20203  20840  21410  -4272   2634   1916       O  
ATOM    778  CB  TYR A 169     -46.231  -4.805  -4.507  1.00161.46           C  
ANISOU  778  CB  TYR A 169    19982  20074  21293  -3661   2059   1386       C  
ATOM    779  CG  TYR A 169     -47.024  -3.908  -3.589  1.00160.92           C  
ANISOU  779  CG  TYR A 169    20011  19576  21555  -3563   1825   1362       C  
ATOM    780  CD1 TYR A 169     -47.954  -4.436  -2.709  1.00157.42           C  
ANISOU  780  CD1 TYR A 169    19643  19089  21079  -3254   1629   1148       C  
ATOM    781  CD2 TYR A 169     -46.848  -2.531  -3.609  1.00164.24           C  
ANISOU  781  CD2 TYR A 169    20452  19629  22324  -3778   1809   1555       C  
ATOM    782  CE1 TYR A 169     -48.683  -3.622  -1.868  1.00157.25           C  
ANISOU  782  CE1 TYR A 169    19706  18696  21346  -3141   1443   1107       C  
ATOM    783  CE2 TYR A 169     -47.574  -1.708  -2.772  1.00164.09           C  
ANISOU  783  CE2 TYR A 169    20534  19201  22613  -3663   1601   1503       C  
ATOM    784  CZ  TYR A 169     -48.492  -2.259  -1.903  1.00160.60           C  
ANISOU  784  CZ  TYR A 169    20158  18749  22113  -3334   1428   1270       C  
ATOM    785  OH  TYR A 169     -49.222  -1.445  -1.065  1.00160.76           O  
ANISOU  785  OH  TYR A 169    20274  18382  22425  -3198   1248   1200       O  
ATOM    786  N   SER A 170     -45.424  -6.229  -7.423  1.00159.49           N  
ANISOU  786  N   SER A 170    19796  20658  20145  -3883   2584   1765       N  
ATOM    787  CA  SER A 170     -44.313  -6.706  -8.226  1.00161.90           C  
ANISOU  787  CA  SER A 170    19950  21331  20232  -4031   2893   1757       C  
ATOM    788  C   SER A 170     -44.425  -6.176  -9.649  1.00165.62           C  
ANISOU  788  C   SER A 170    20595  21887  20445  -4260   3066   2205       C  
ATOM    789  O   SER A 170     -43.741  -5.226 -10.023  1.00169.40           O  
ANISOU  789  O   SER A 170    20980  22286  21097  -4552   3228   2443       O  
ATOM    790  CB  SER A 170     -44.286  -8.240  -8.225  1.00163.75           C  
ANISOU  790  CB  SER A 170    20168  21910  20138  -3779   2921   1445       C  
ATOM    791  OG  SER A 170     -43.235  -8.761  -9.022  1.00166.29           O  
ANISOU  791  OG  SER A 170    20346  22601  20236  -3881   3236   1408       O  
ATOM    792  N   ASN A 171     -45.346  -6.740 -10.421  1.00169.12           N  
ANISOU  792  N   ASN A 171    21305  22471  20481  -4139   3007   2341       N  
ATOM    793  CA  ASN A 171     -45.505  -6.348 -11.818  1.00172.77           C  
ANISOU  793  CA  ASN A 171    21966  23061  20619  -4337   3153   2766       C  
ATOM    794  C   ASN A 171     -46.710  -5.451 -12.034  1.00173.18           C  
ANISOU  794  C   ASN A 171    22279  22782  20739  -4353   2908   3140       C  
ATOM    795  O   ASN A 171     -46.893  -4.912 -13.125  1.00176.61           O  
ANISOU  795  O   ASN A 171    22891  23254  20958  -4537   2986   3553       O  
ATOM    796  CB  ASN A 171     -45.621  -7.581 -12.719  1.00174.13           C  
ANISOU  796  CB  ASN A 171    22271  23657  20232  -4220   3266   2681       C  
ATOM    797  CG  ASN A 171     -44.314  -8.349 -12.840  1.00175.25           C  
ANISOU  797  CG  ASN A 171    22164  24162  20263  -4239   3583   2395       C  
ATOM    798  OD1 ASN A 171     -43.261  -7.774 -13.141  1.00178.79           O  
ANISOU  798  OD1 ASN A 171    22418  24694  20822  -4483   3855   2509       O  
ATOM    799  ND2 ASN A 171     -44.376  -9.658 -12.610  1.00172.52           N  
ANISOU  799  ND2 ASN A 171    21812  24025  19713  -3979   3548   2029       N  
ATOM    800  N   GLY A 172     -47.524  -5.284 -10.994  1.00167.86           N  
ANISOU  800  N   GLY A 172    21625  21792  20362  -4154   2617   3003       N  
ATOM    801  CA  GLY A 172     -48.725  -4.474 -11.091  1.00168.16           C  
ANISOU  801  CA  GLY A 172    21881  21503  20510  -4117   2370   3322       C  
ATOM    802  C   GLY A 172     -48.409  -2.987 -11.044  1.00171.61           C  
ANISOU  802  C   GLY A 172    22291  21567  21345  -4357   2390   3611       C  
ATOM    803  O   GLY A 172     -47.264  -2.565 -11.268  1.00174.54           O  
ANISOU  803  O   GLY A 172    22509  21991  21818  -4618   2629   3663       O  
ATOM    804  N   PHE A 173     -49.428  -2.182 -10.760  1.00169.17           N  
ANISOU  804  N   PHE A 173    22126  20871  21281  -4271   2139   3805       N  
ATOM    805  CA  PHE A 173     -49.270  -0.733 -10.769  1.00172.79           C  
ANISOU  805  CA  PHE A 173    22607  20915  22131  -4482   2121   4109       C  
ATOM    806  C   PHE A 173     -48.810  -0.160  -9.432  1.00171.96           C  
ANISOU  806  C   PHE A 173    22312  20468  22555  -4467   2057   3797       C  
ATOM    807  O   PHE A 173     -48.185   0.898  -9.397  1.00175.35           O  
ANISOU  807  O   PHE A 173    22686  20619  23321  -4717   2119   3950       O  
ATOM    808  CB  PHE A 173     -50.588  -0.068 -11.168  1.00173.85           C  
ANISOU  808  CB  PHE A 173    22993  20767  22295  -4386   1876   4491       C  
ATOM    809  CG  PHE A 173     -51.797  -0.702 -10.544  1.00169.77           C  
ANISOU  809  CG  PHE A 173    22531  20230  21744  -4024   1620   4284       C  
ATOM    810  CD1 PHE A 173     -52.180  -0.375  -9.252  1.00167.61           C  
ANISOU  810  CD1 PHE A 173    22172  19626  21886  -3823   1454   4008       C  
ATOM    811  CD2 PHE A 173     -52.565  -1.609 -11.255  1.00168.46           C  
ANISOU  811  CD2 PHE A 173    22504  20376  21127  -3894   1544   4369       C  
ATOM    812  CE1 PHE A 173     -53.299  -0.958  -8.674  1.00164.18           C  
ANISOU  812  CE1 PHE A 173    21769  19195  21417  -3499   1245   3838       C  
ATOM    813  CE2 PHE A 173     -53.685  -2.191 -10.684  1.00165.02           C  
ANISOU  813  CE2 PHE A 173    22094  19923  20682  -3586   1310   4200       C  
ATOM    814  CZ  PHE A 173     -54.052  -1.861  -9.396  1.00162.89           C  
ANISOU  814  CZ  PHE A 173    21720  19342  20831  -3389   1174   3947       C  
ATOM    815  N   CYS A 174     -49.083  -0.876  -8.344  1.00167.74           N  
ANISOU  815  N   CYS A 174    21685  19966  22083  -4191   1932   3359       N  
ATOM    816  CA  CYS A 174     -48.835  -0.360  -6.998  1.00166.85           C  
ANISOU  816  CA  CYS A 174    21435  19527  22432  -4131   1824   3041       C  
ATOM    817  C   CYS A 174     -47.352  -0.068  -6.763  1.00169.01           C  
ANISOU  817  C   CYS A 174    21469  19830  22916  -4407   2012   2898       C  
ATOM    818  O   CYS A 174     -46.487  -0.624  -7.444  1.00170.01           O  
ANISOU  818  O   CYS A 174    21480  20325  22791  -4567   2248   2925       O  
ATOM    819  CB  CYS A 174     -49.339  -1.356  -5.955  1.00164.50           C  
ANISOU  819  CB  CYS A 174    21083  19352  22068  -3792   1686   2611       C  
ATOM    820  SG  CYS A 174     -51.134  -1.530  -5.883  1.00162.15           S  
ANISOU  820  SG  CYS A 174    21003  18935  21670  -3456   1427   2729       S  
ATOM    821  N   GLN A 175     -47.058   0.806  -5.802  1.00170.03           N  
ANISOU  821  N   GLN A 175    21517  19574  23511  -4462   1907   2736       N  
ATOM    822  CA  GLN A 175     -45.688   1.284  -5.632  1.00172.93           C  
ANISOU  822  CA  GLN A 175    21654  19908  24142  -4773   2054   2658       C  
ATOM    823  C   GLN A 175     -45.046   0.928  -4.292  1.00170.86           C  
ANISOU  823  C   GLN A 175    21165  19661  24092  -4679   1977   2136       C  
ATOM    824  O   GLN A 175     -45.722   0.716  -3.283  1.00167.86           O  
ANISOU  824  O   GLN A 175    20843  19153  23783  -4392   1774   1845       O  
ATOM    825  CB  GLN A 175     -45.631   2.812  -5.805  1.00177.49           C  
ANISOU  825  CB  GLN A 175    22319  19985  25134  -5035   2004   2972       C  
ATOM    826  CG  GLN A 175     -46.107   3.343  -7.153  1.00180.61           C  
ANISOU  826  CG  GLN A 175    22930  20328  25364  -5188   2077   3548       C  
ATOM    827  CD  GLN A 175     -45.140   3.050  -8.286  1.00183.30           C  
ANISOU  827  CD  GLN A 175    23161  21063  25421  -5492   2392   3798       C  
ATOM    828  OE1 GLN A 175     -43.927   3.000  -8.088  1.00184.73           O  
ANISOU  828  OE1 GLN A 175    23076  21383  25729  -5710   2562   3639       O  
ATOM    829  NE2 GLN A 175     -45.679   2.852  -9.486  1.00184.28           N  
ANISOU  829  NE2 GLN A 175    23483  21387  25148  -5504   2471   4191       N  
ATOM    830  N   LEU A 176     -43.717   0.893  -4.325  1.00172.91           N  
ANISOU  830  N   LEU A 176    21160  20091  24449  -4935   2149   2044       N  
ATOM    831  CA  LEU A 176     -42.842   0.629  -3.189  1.00172.05           C  
ANISOU  831  CA  LEU A 176    20788  20027  24556  -4924   2092   1594       C  
ATOM    832  C   LEU A 176     -41.732   1.680  -3.286  1.00176.97           C  
ANISOU  832  C   LEU A 176    21225  20444  25572  -5338   2178   1710       C  
ATOM    833  O   LEU A 176     -41.605   2.348  -4.312  1.00180.54           O  
ANISOU  833  O   LEU A 176    21739  20818  26041  -5608   2329   2136       O  
ATOM    834  CB  LEU A 176     -42.300  -0.809  -3.203  1.00174.69           C  
ANISOU  834  CB  LEU A 176    20929  20892  24551  -4780   2224   1342       C  
ATOM    835  CG  LEU A 176     -41.442  -1.320  -2.032  1.00173.41           C  
ANISOU  835  CG  LEU A 176    20490  20851  24547  -4708   2143    870       C  
ATOM    836  CD1 LEU A 176     -41.945  -0.852  -0.675  1.00171.99           C  
ANISOU  836  CD1 LEU A 176    20396  20310  24644  -4545   1843    580       C  
ATOM    837  CD2 LEU A 176     -41.382  -2.834  -2.074  1.00170.02           C  
ANISOU  837  CD2 LEU A 176    19983  20884  23732  -4451   2219    663       C  
ATOM    838  N   ASP A 177     -40.941   1.846  -2.233  1.00177.48           N  
ANISOU  838  N   ASP A 177    21066  20417  25951  -5403   2071   1352       N  
ATOM    839  CA  ASP A 177     -39.881   2.843  -2.257  1.00182.37           C  
ANISOU  839  CA  ASP A 177    21488  20824  26982  -5816   2123   1442       C  
ATOM    840  C   ASP A 177     -38.534   2.233  -1.894  1.00182.98           C  
ANISOU  840  C   ASP A 177    21158  21254  27111  -5936   2224   1159       C  
ATOM    841  O   ASP A 177     -37.602   2.947  -1.500  1.00186.53           O  
ANISOU  841  O   ASP A 177    21386  21528  27960  -6236   2186   1085       O  
ATOM    842  CB  ASP A 177     -40.223   3.994  -1.308  1.00183.86           C  
ANISOU  842  CB  ASP A 177    21812  20423  27623  -5845   1839   1308       C  
ATOM    843  CG  ASP A 177     -40.555   3.515   0.096  1.00180.23           C  
ANISOU  843  CG  ASP A 177    21365  19938  27178  -5511   1586    791       C  
ATOM    844  OD1 ASP A 177     -41.100   2.402   0.233  1.00175.86           O  
ANISOU  844  OD1 ASP A 177    20859  19709  26251  -5175   1589    645       O  
ATOM    845  OD2 ASP A 177     -40.274   4.249   1.066  1.00182.01           O  
ANISOU  845  OD2 ASP A 177    21560  19816  27778  -5591   1380    532       O  
ATOM    846  N   GLU A 178     -38.453   0.910  -2.044  1.00183.82           N  
ANISOU  846  N   GLU A 178    21168  21847  26829  -5698   2341   1007       N  
ATOM    847  CA  GLU A 178     -37.232   0.139  -1.810  1.00184.20           C  
ANISOU  847  CA  GLU A 178    20823  22293  26873  -5745   2457    753       C  
ATOM    848  C   GLU A 178     -36.482   0.552  -0.535  1.00185.42           C  
ANISOU  848  C   GLU A 178    20745  22258  27450  -5839   2225    387       C  
ATOM    849  O   GLU A 178     -35.259   0.706  -0.549  1.00188.77           O  
ANISOU  849  O   GLU A 178    20807  22813  28104  -6115   2324    350       O  
ATOM    850  CB  GLU A 178     -36.305   0.265  -3.023  1.00190.03           C  
ANISOU  850  CB  GLU A 178    21341  23294  27570  -6083   2816   1085       C  
ATOM    851  CG  GLU A 178     -36.752  -0.505  -4.268  1.00188.91           C  
ANISOU  851  CG  GLU A 178    21351  23512  26915  -5963   3082   1348       C  
ATOM    852  CD  GLU A 178     -35.685  -0.516  -5.358  1.00193.24           C  
ANISOU  852  CD  GLU A 178    21633  24401  27389  -6272   3468   1606       C  
ATOM    853  OE1 GLU A 178     -34.633   0.131  -5.166  1.00197.19           O  
ANISOU  853  OE1 GLU A 178    21818  24837  28269  -6600   3529   1617       O  
ATOM    854  OE2 GLU A 178     -35.898  -1.170  -6.402  1.00192.97           O  
ANISOU  854  OE2 GLU A 178    21700  24706  26914  -6192   3713   1792       O  
ATOM    855  N   ALA A 179     -37.227   0.722   0.555  1.00186.99           N  
ANISOU  855  N   ALA A 179    21146  22164  27736  -5608   1916    118       N  
ATOM    856  CA  ALA A 179     -36.673   1.135   1.843  1.00188.09           C  
ANISOU  856  CA  ALA A 179    21136  22098  28232  -5663   1649   -259       C  
ATOM    857  C   ALA A 179     -37.782   1.160   2.891  1.00184.81           C  
ANISOU  857  C   ALA A 179    21028  21420  27770  -5324   1360   -522       C  
ATOM    858  O   ALA A 179     -38.532   2.135   2.983  1.00185.83           O  
ANISOU  858  O   ALA A 179    21428  21105  28075  -5349   1245   -416       O  
ATOM    859  CB  ALA A 179     -36.011   2.508   1.741  1.00185.42           C  
ANISOU  859  CB  ALA A 179    20698  21381  28372  -6111   1626   -106       C  
ATOM    860  N   GLY A 180     -37.896   0.089   3.673  1.00185.52           N  
ANISOU  860  N   GLY A 180    21079  21784  27626  -4999   1250   -853       N  
ATOM    861  CA  GLY A 180     -38.959  -0.009   4.659  1.00182.41           C  
ANISOU  861  CA  GLY A 180    20963  21210  27136  -4661   1013  -1093       C  
ATOM    862  C   GLY A 180     -40.246  -0.517   4.045  1.00178.94           C  
ANISOU  862  C   GLY A 180    20811  20836  26344  -4387   1108   -871       C  
ATOM    863  O   GLY A 180     -40.223  -1.124   2.976  1.00178.21           O  
ANISOU  863  O   GLY A 180    20683  21028  26002  -4402   1335   -616       O  
ATOM    864  N   ASN A 181     -41.373  -0.219   4.685  1.00181.68           N  
ANISOU  864  N   ASN A 181    21440  20914  26677  -4147    936   -963       N  
ATOM    865  CA  ASN A 181     -42.643  -0.862   4.347  1.00178.05           C  
ANISOU  865  CA  ASN A 181    21218  20553  25878  -3838    976   -823       C  
ATOM    866  C   ASN A 181     -43.174  -0.491   2.963  1.00179.02           C  
ANISOU  866  C   ASN A 181    21484  20607  25927  -3954   1154   -353       C  
ATOM    867  O   ASN A 181     -42.597   0.343   2.259  1.00182.67           O  
ANISOU  867  O   ASN A 181    21886  20915  26604  -4279   1258   -109       O  
ATOM    868  CB  ASN A 181     -43.713  -0.522   5.396  1.00180.12           C  
ANISOU  868  CB  ASN A 181    21719  20535  26184  -3563    763  -1028       C  
ATOM    869  CG  ASN A 181     -43.371  -1.040   6.786  1.00178.81           C  
ANISOU  869  CG  ASN A 181    21462  20490  25987  -3393    582  -1483       C  
ATOM    870  OD1 ASN A 181     -42.810  -2.128   6.938  1.00176.98           O  
ANISOU  870  OD1 ASN A 181    21052  20641  25550  -3321    609  -1615       O  
ATOM    871  ND2 ASN A 181     -43.703  -0.257   7.807  1.00180.05           N  
ANISOU  871  ND2 ASN A 181    21751  20316  26343  -3321    391  -1725       N  
ATOM    872  N   ARG A 182     -44.276  -1.133   2.584  1.00171.81           N  
ANISOU  872  N   ARG A 182    20760  19820  24702  -3695   1177   -217       N  
ATOM    873  CA  ARG A 182     -44.912  -0.913   1.291  1.00172.48           C  
ANISOU  873  CA  ARG A 182    21005  19879  24649  -3761   1310    224       C  
ATOM    874  C   ARG A 182     -45.810   0.311   1.349  1.00174.27           C  
ANISOU  874  C   ARG A 182    21463  19620  25133  -3752   1189    396       C  
ATOM    875  O   ARG A 182     -46.429   0.585   2.379  1.00173.34           O  
ANISOU  875  O   ARG A 182    21444  19271  25145  -3539   1010    157       O  
ATOM    876  CB  ARG A 182     -45.720  -2.142   0.857  1.00171.83           C  
ANISOU  876  CB  ARG A 182    21020  20135  24133  -3497   1355    286       C  
ATOM    877  CG  ARG A 182     -44.908  -3.428   0.747  1.00170.15           C  
ANISOU  877  CG  ARG A 182    20605  20384  23658  -3467   1474    115       C  
ATOM    878  CD  ARG A 182     -45.721  -4.566   0.130  1.00167.12           C  
ANISOU  878  CD  ARG A 182    20350  20289  22858  -3249   1521    219       C  
ATOM    879  NE  ARG A 182     -45.006  -5.844   0.176  1.00165.49           N  
ANISOU  879  NE  ARG A 182    19970  20480  22427  -3169   1606      4       N  
ATOM    880  CZ  ARG A 182     -44.041  -6.210  -0.668  1.00167.17           C  
ANISOU  880  CZ  ARG A 182    20024  20963  22529  -3338   1822     76       C  
ATOM    881  NH1 ARG A 182     -43.652  -5.394  -1.641  1.00170.57           N  
ANISOU  881  NH1 ARG A 182    20447  21333  23031  -3624   1987    377       N  
ATOM    882  NH2 ARG A 182     -43.458  -7.397  -0.536  1.00165.72           N  
ANISOU  882  NH2 ARG A 182    19689  21112  22166  -3215   1880   -150       N  
ATOM    883  N   LEU A 183     -45.863   1.056   0.250  1.00167.33           N  
ANISOU  883  N   LEU A 183    20669  18582  24325  -3976   1291    813       N  
ATOM    884  CA  LEU A 183     -46.762   2.196   0.164  1.00169.33           C  
ANISOU  884  CA  LEU A 183    21152  18364  24823  -3952   1176   1032       C  
ATOM    885  C   LEU A 183     -48.206   1.719   0.092  1.00166.31           C  
ANISOU  885  C   LEU A 183    20964  18029  24199  -3602   1095   1117       C  
ATOM    886  O   LEU A 183     -48.513   0.768  -0.628  1.00164.12           O  
ANISOU  886  O   LEU A 183    20699  18116  23544  -3522   1186   1263       O  
ATOM    887  CB  LEU A 183     -46.436   3.043  -1.062  1.00170.53           C  
ANISOU  887  CB  LEU A 183    21348  18361  25084  -4289   1305   1504       C  
ATOM    888  CG  LEU A 183     -44.997   3.537  -1.127  1.00174.07           C  
ANISOU  888  CG  LEU A 183    21576  18779  25784  -4682   1413   1484       C  
ATOM    889  CD1 LEU A 183     -44.766   4.332  -2.403  1.00178.30           C  
ANISOU  889  CD1 LEU A 183    22173  19184  26387  -5015   1561   2007       C  
ATOM    890  CD2 LEU A 183     -44.685   4.360   0.109  1.00175.68           C  
ANISOU  890  CD2 LEU A 183    21745  18576  26429  -4714   1218   1141       C  
ATOM    891  N   PRO A 184     -49.095   2.369   0.857  1.00163.53           N  
ANISOU  891  N   PRO A 184    20754  17309  24069  -3388    922   1009       N  
ATOM    892  CA  PRO A 184     -50.522   2.042   0.828  1.00161.23           C  
ANISOU  892  CA  PRO A 184    20619  17030  23610  -3057    840   1107       C  
ATOM    893  C   PRO A 184     -51.115   2.204  -0.568  1.00162.46           C  
ANISOU  893  C   PRO A 184    20904  17200  23623  -3131    894   1623       C  
ATOM    894  O   PRO A 184     -50.887   3.215  -1.238  1.00166.24           O  
ANISOU  894  O   PRO A 184    21454  17390  24319  -3363    916   1934       O  
ATOM    895  CB  PRO A 184     -51.124   3.045   1.811  1.00162.77           C  
ANISOU  895  CB  PRO A 184    20924  16751  24171  -2887    678    926       C  
ATOM    896  CG  PRO A 184     -50.028   3.287   2.784  1.00163.78           C  
ANISOU  896  CG  PRO A 184    20926  16797  24505  -3022    648    530       C  
ATOM    897  CD  PRO A 184     -48.771   3.294   1.956  1.00165.64           C  
ANISOU  897  CD  PRO A 184    21018  17179  24739  -3413    790    706       C  
ATOM    898  N   CYS A 185     -51.901   1.220  -0.984  1.00159.53           N  
ANISOU  898  N   CYS A 185    20572  17152  22889  -2938    897   1719       N  
ATOM    899  CA  CYS A 185     -52.380   1.164  -2.354  1.00160.54           C  
ANISOU  899  CA  CYS A 185    20816  17390  22794  -3019    940   2183       C  
ATOM    900  C   CYS A 185     -53.856   0.787  -2.396  1.00158.57           C  
ANISOU  900  C   CYS A 185    20676  17173  22402  -2705    802   2290       C  
ATOM    901  O   CYS A 185     -54.193  -0.383  -2.572  1.00155.56           O  
ANISOU  901  O   CYS A 185    20269  17169  21668  -2584    813   2235       O  
ATOM    902  CB  CYS A 185     -51.541   0.162  -3.153  1.00159.58           C  
ANISOU  902  CB  CYS A 185    20602  17741  22291  -3198   1122   2221       C  
ATOM    903  SG  CYS A 185     -51.872   0.105  -4.926  1.00161.62           S  
ANISOU  903  SG  CYS A 185    21015  18184  22211  -3361   1204   2776       S  
ATOM    904  N   PRO A 186     -54.744   1.777  -2.218  1.00160.53           N  
ANISOU  904  N   PRO A 186    21035  17013  22947  -2569    665   2438       N  
ATOM    905  CA  PRO A 186     -56.183   1.518  -2.128  1.00159.07           C  
ANISOU  905  CA  PRO A 186    20911  16832  22697  -2250    526   2523       C  
ATOM    906  C   PRO A 186     -56.774   1.008  -3.438  1.00159.06           C  
ANISOU  906  C   PRO A 186    20992  17088  22356  -2289    506   2933       C  
ATOM    907  O   PRO A 186     -57.771   0.287  -3.410  1.00156.85           O  
ANISOU  907  O   PRO A 186    20708  16996  21891  -2062    413   2941       O  
ATOM    908  CB  PRO A 186     -56.761   2.886  -1.769  1.00162.30           C  
ANISOU  908  CB  PRO A 186    21411  16700  23557  -2143    409   2617       C  
ATOM    909  CG  PRO A 186     -55.802   3.849  -2.347  1.00166.10           C  
ANISOU  909  CG  PRO A 186    21945  16922  24243  -2481    474   2824       C  
ATOM    910  CD  PRO A 186     -54.448   3.220  -2.191  1.00164.73           C  
ANISOU  910  CD  PRO A 186    21637  17044  23909  -2719    633   2570       C  
ATOM    911  N   GLU A 187     -56.153   1.354  -4.564  1.00161.71           N  
ANISOU  911  N   GLU A 187    21400  17447  22596  -2584    591   3265       N  
ATOM    912  CA  GLU A 187     -56.642   0.911  -5.865  1.00162.25           C  
ANISOU  912  CA  GLU A 187    21575  17772  22300  -2645    567   3657       C  
ATOM    913  C   GLU A 187     -56.565  -0.606  -5.996  1.00158.60           C  
ANISOU  913  C   GLU A 187    21050  17820  21391  -2596    627   3457       C  
ATOM    914  O   GLU A 187     -57.323  -1.222  -6.751  1.00158.04           O  
ANISOU  914  O   GLU A 187    21057  17978  21011  -2534    542   3662       O  
ATOM    915  CB  GLU A 187     -55.849   1.575  -6.985  1.00166.14           C  
ANISOU  915  CB  GLU A 187    22158  18217  22750  -2992    683   4030       C  
ATOM    916  CG  GLU A 187     -55.887   3.086  -6.942  1.00170.24           C  
ANISOU  916  CG  GLU A 187    22758  18198  23726  -3072    615   4268       C  
ATOM    917  CD  GLU A 187     -54.814   3.716  -7.806  1.00174.07           C  
ANISOU  917  CD  GLU A 187    23289  18636  24214  -3464    776   4561       C  
ATOM    918  OE1 GLU A 187     -53.709   3.140  -7.902  1.00173.28           O  
ANISOU  918  OE1 GLU A 187    23075  18842  23920  -3666    981   4388       O  
ATOM    919  OE2 GLU A 187     -55.079   4.783  -8.403  1.00178.14           O  
ANISOU  919  OE2 GLU A 187    23944  18810  24929  -3569    702   4981       O  
ATOM    920  N   ALA A 188     -55.646  -1.204  -5.247  1.00156.38           N  
ANISOU  920  N   ALA A 188    20630  17701  21087  -2624    754   3053       N  
ATOM    921  CA  ALA A 188     -55.554  -2.651  -5.186  1.00152.93           C  
ANISOU  921  CA  ALA A 188    20128  17694  20286  -2543    799   2814       C  
ATOM    922  C   ALA A 188     -56.795  -3.199  -4.504  1.00150.20           C  
ANISOU  922  C   ALA A 188    19770  17365  19935  -2227    626   2691       C  
ATOM    923  O   ALA A 188     -57.422  -4.129  -5.001  1.00148.69           O  
ANISOU  923  O   ALA A 188    19619  17444  19433  -2152    562   2764       O  
ATOM    924  CB  ALA A 188     -54.299  -3.085  -4.446  1.00151.74           C  
ANISOU  924  CB  ALA A 188    19816  17672  20167  -2621    950   2417       C  
ATOM    925  N   TYR A 189     -57.175  -2.587  -3.388  1.00149.96           N  
ANISOU  925  N   TYR A 189    19686  17039  20252  -2049    551   2514       N  
ATOM    926  CA  TYR A 189     -58.360  -3.026  -2.672  1.00147.80           C  
ANISOU  926  CA  TYR A 189    19377  16781  20000  -1746    416   2404       C  
ATOM    927  C   TYR A 189     -59.600  -2.848  -3.535  1.00149.13           C  
ANISOU  927  C   TYR A 189    19636  16918  20109  -1665    264   2803       C  
ATOM    928  O   TYR A 189     -60.457  -3.717  -3.564  1.00147.23           O  
ANISOU  928  O   TYR A 189    19369  16893  19677  -1518    169   2811       O  
ATOM    929  CB  TYR A 189     -58.504  -2.263  -1.358  1.00148.06           C  
ANISOU  929  CB  TYR A 189    19352  16491  20414  -1570    389   2146       C  
ATOM    930  CG  TYR A 189     -59.573  -2.816  -0.450  1.00145.80           C  
ANISOU  930  CG  TYR A 189    18996  16275  20126  -1258    303   1972       C  
ATOM    931  CD1 TYR A 189     -59.305  -3.881   0.399  1.00142.66           C  
ANISOU  931  CD1 TYR A 189    18505  16141  19558  -1172    347   1626       C  
ATOM    932  CD2 TYR A 189     -60.846  -2.262  -0.423  1.00147.11           C  
ANISOU  932  CD2 TYR A 189    19178  16244  20474  -1046    181   2165       C  
ATOM    933  CE1 TYR A 189     -60.278  -4.388   1.240  1.00140.89           C  
ANISOU  933  CE1 TYR A 189    18215  15994  19325   -905    287   1492       C  
ATOM    934  CE2 TYR A 189     -61.826  -2.764   0.419  1.00145.37           C  
ANISOU  934  CE2 TYR A 189    18865  16111  20258   -765    130   2016       C  
ATOM    935  CZ  TYR A 189     -61.535  -3.825   1.245  1.00142.28           C  
ANISOU  935  CZ  TYR A 189    18390  15992  19677   -707    190   1686       C  
ATOM    936  OH  TYR A 189     -62.504  -4.324   2.078  1.00140.85           O  
ANISOU  936  OH  TYR A 189    18117  15910  19491   -449    155   1565       O  
ATOM    937  N   GLY A 190     -59.668  -1.732  -4.256  1.00152.67           N  
ANISOU  937  N   GLY A 190    20186  17094  20725  -1776    228   3149       N  
ATOM    938  CA  GLY A 190     -60.752  -1.454  -5.187  1.00154.62           C  
ANISOU  938  CA  GLY A 190    20527  17298  20922  -1723     63   3577       C  
ATOM    939  C   GLY A 190     -60.842  -2.477  -6.304  1.00153.89           C  
ANISOU  939  C   GLY A 190    20504  17612  20356  -1846     40   3755       C  
ATOM    940  O   GLY A 190     -61.931  -2.799  -6.782  1.00154.02           O  
ANISOU  940  O   GLY A 190    20546  17727  20247  -1733   -135   3972       O  
ATOM    941  N   ALA A 191     -59.684  -2.950  -6.756  1.00153.56           N  
ANISOU  941  N   ALA A 191    20491  17800  20056  -2081    214   3666       N  
ATOM    942  CA  ALA A 191     -59.625  -4.017  -7.751  1.00152.92           C  
ANISOU  942  CA  ALA A 191    20486  18121  19494  -2191    224   3749       C  
ATOM    943  C   ALA A 191     -60.137  -5.317  -7.150  1.00149.18           C  
ANISOU  943  C   ALA A 191    19924  17899  18859  -2005    158   3453       C  
ATOM    944  O   ALA A 191     -60.894  -6.054  -7.781  1.00148.82           O  
ANISOU  944  O   ALA A 191    19938  18068  18537  -1971     21   3583       O  
ATOM    945  CB  ALA A 191     -58.209  -4.191  -8.271  1.00153.71           C  
ANISOU  945  CB  ALA A 191    20611  18402  19392  -2458    462   3682       C  
ATOM    946  N   LEU A 192     -59.703  -5.586  -5.924  1.00146.69           N  
ANISOU  946  N   LEU A 192    19472  17549  18715  -1898    245   3061       N  
ATOM    947  CA  LEU A 192     -60.125  -6.756  -5.171  1.00143.29           C  
ANISOU  947  CA  LEU A 192    18948  17316  18179  -1720    195   2772       C  
ATOM    948  C   LEU A 192     -61.640  -6.808  -5.065  1.00143.13           C  
ANISOU  948  C   LEU A 192    18905  17246  18230  -1516    -19   2940       C  
ATOM    949  O   LEU A 192     -62.276  -7.816  -5.377  1.00141.87           O  
ANISOU  949  O   LEU A 192    18753  17324  17827  -1475   -128   2960       O  
ATOM    950  CB  LEU A 192     -59.507  -6.722  -3.769  1.00142.55           C  
ANISOU  950  CB  LEU A 192    18719  17122  18321  -1621    298   2378       C  
ATOM    951  CG  LEU A 192     -59.956  -7.765  -2.745  1.00139.33           C  
ANISOU  951  CG  LEU A 192    18208  16863  17867  -1417    251   2084       C  
ATOM    952  CD1 LEU A 192     -59.743  -9.164  -3.290  1.00137.64           C  
ANISOU  952  CD1 LEU A 192    18027  16996  17273  -1482    257   2011       C  
ATOM    953  CD2 LEU A 192     -59.246  -7.583  -1.408  1.00138.15           C  
ANISOU  953  CD2 LEU A 192    17951  16609  17930  -1341    348   1720       C  
ATOM    954  N   ILE A 193     -62.213  -5.680  -4.673  1.00144.82           N  
ANISOU  954  N   ILE A 193    19089  17140  18798  -1395    -82   3071       N  
ATOM    955  CA  ILE A 193     -63.637  -5.575  -4.447  1.00145.10           C  
ANISOU  955  CA  ILE A 193    19056  17099  18978  -1171   -264   3220       C  
ATOM    956  C   ILE A 193     -64.389  -5.621  -5.766  1.00147.16           C  
ANISOU  956  C   ILE A 193    19415  17458  19041  -1247   -444   3634       C  
ATOM    957  O   ILE A 193     -65.439  -6.239  -5.859  1.00146.57           O  
ANISOU  957  O   ILE A 193    19281  17526  18886  -1134   -609   3721       O  
ATOM    958  CB  ILE A 193     -63.981  -4.280  -3.697  1.00146.92           C  
ANISOU  958  CB  ILE A 193    19232  16932  19658  -1003   -268   3233       C  
ATOM    959  CG1 ILE A 193     -63.354  -4.281  -2.304  1.00145.04           C  
ANISOU  959  CG1 ILE A 193    18904  16616  19590   -907   -120   2795       C  
ATOM    960  CG2 ILE A 193     -65.456  -4.141  -3.554  1.00147.71           C  
ANISOU  960  CG2 ILE A 193    19238  16968  19917   -759   -442   3412       C  
ATOM    961  CD1 ILE A 193     -63.710  -5.484  -1.479  1.00141.80           C  
ANISOU  961  CD1 ILE A 193    18376  16470  19030   -764   -115   2523       C  
ATOM    962  N   GLY A 194     -63.830  -5.002  -6.798  1.00149.78           N  
ANISOU  962  N   GLY A 194    19898  17734  19279  -1455   -418   3897       N  
ATOM    963  CA  GLY A 194     -64.484  -4.998  -8.091  1.00152.18           C  
ANISOU  963  CA  GLY A 194    20323  18142  19357  -1541   -600   4306       C  
ATOM    964  C   GLY A 194     -64.575  -6.399  -8.662  1.00150.50           C  
ANISOU  964  C   GLY A 194    20157  18329  18696  -1623   -656   4229       C  
ATOM    965  O   GLY A 194     -65.632  -6.845  -9.120  1.00150.97           O  
ANISOU  965  O   GLY A 194    20214  18514  18633  -1563   -881   4410       O  
ATOM    966  N   THR A 195     -63.455  -7.103  -8.608  1.00148.73           N  
ANISOU  966  N   THR A 195    19968  18296  18248  -1756   -458   3944       N  
ATOM    967  CA  THR A 195     -63.373  -8.460  -9.112  1.00147.29           C  
ANISOU  967  CA  THR A 195    19849  18466  17648  -1831   -482   3813       C  
ATOM    968  C   THR A 195     -64.260  -9.419  -8.312  1.00144.55           C  
ANISOU  968  C   THR A 195    19365  18208  17350  -1644   -615   3616       C  
ATOM    969  O   THR A 195     -64.953 -10.271  -8.883  1.00144.56           O  
ANISOU  969  O   THR A 195    19413  18412  17102  -1662   -794   3690       O  
ATOM    970  CB  THR A 195     -61.919  -8.950  -9.083  1.00146.16           C  
ANISOU  970  CB  THR A 195    19738  18475  17321  -1974   -218   3519       C  
ATOM    971  OG1 THR A 195     -61.088  -7.995  -9.754  1.00148.98           O  
ANISOU  971  OG1 THR A 195    20190  18743  17672  -2162    -72   3717       O  
ATOM    972  CG2 THR A 195     -61.794 -10.291  -9.772  1.00145.42           C  
ANISOU  972  CG2 THR A 195    19747  18724  16781  -2053   -239   3399       C  
ATOM    973  N   SER A 196     -64.243  -9.271  -6.991  1.00142.51           N  
ANISOU  973  N   SER A 196    18941  17799  17408  -1476   -532   3370       N  
ATOM    974  CA  SER A 196     -65.014 -10.157  -6.126  1.00140.08           C  
ANISOU  974  CA  SER A 196    18491  17578  17154  -1306   -620   3187       C  
ATOM    975  C   SER A 196     -66.515  -9.926  -6.285  1.00141.47           C  
ANISOU  975  C   SER A 196    18584  17703  17466  -1178   -863   3474       C  
ATOM    976  O   SER A 196     -67.294 -10.880  -6.326  1.00140.62           O  
ANISOU  976  O   SER A 196    18423  17772  17236  -1147  -1015   3473       O  
ATOM    977  CB  SER A 196     -64.596  -9.976  -4.672  1.00138.22           C  
ANISOU  977  CB  SER A 196    18115  17209  17195  -1159   -460   2866       C  
ATOM    978  OG  SER A 196     -64.839  -8.659  -4.215  1.00139.83           O  
ANISOU  978  OG  SER A 196    18260  17110  17757  -1047   -440   2968       O  
ATOM    979  N   ALA A 197     -66.912  -8.660  -6.379  1.00143.89           N  
ANISOU  979  N   ALA A 197    18870  17757  18044  -1105   -907   3725       N  
ATOM    980  CA  ALA A 197     -68.299  -8.308  -6.656  1.00145.90           C  
ANISOU  980  CA  ALA A 197    19034  17950  18450   -977  -1146   4042       C  
ATOM    981  C   ALA A 197     -68.719  -8.897  -7.992  1.00147.43           C  
ANISOU  981  C   ALA A 197    19356  18372  18289  -1141  -1365   4303       C  
ATOM    982  O   ALA A 197     -69.829  -9.403  -8.134  1.00147.82           O  
ANISOU  982  O   ALA A 197    19304  18535  18326  -1076  -1587   4432       O  
ATOM    983  CB  ALA A 197     -68.483  -6.802  -6.664  1.00148.72           C  
ANISOU  983  CB  ALA A 197    19386  17971  19151   -883  -1152   4276       C  
ATOM    984  N   CYS A 198     -67.824  -8.821  -8.972  1.00148.60           N  
ANISOU  984  N   CYS A 198    19723  18597  18142  -1360  -1300   4379       N  
ATOM    985  CA  CYS A 198     -68.061  -9.447 -10.269  1.00150.22           C  
ANISOU  985  CA  CYS A 198    20096  19050  17932  -1534  -1484   4575       C  
ATOM    986  C   CYS A 198     -68.331 -10.958 -10.158  1.00147.97           C  
ANISOU  986  C   CYS A 198    19785  19034  17403  -1556  -1566   4334       C  
ATOM    987  O   CYS A 198     -69.298 -11.448 -10.732  1.00149.20           O  
ANISOU  987  O   CYS A 198    19940  19322  17428  -1577  -1837   4508       O  
ATOM    988  CB  CYS A 198     -66.887  -9.189 -11.213  1.00151.76           C  
ANISOU  988  CB  CYS A 198    20528  19314  17822  -1762  -1326   4632       C  
ATOM    989  SG  CYS A 198     -66.912 -10.235 -12.689  1.00153.38           S  
ANISOU  989  SG  CYS A 198    20976  19890  17413  -1979  -1481   4724       S  
ATOM    990  N   CYS A 199     -67.473 -11.701  -9.459  1.00145.00           N  
ANISOU  990  N   CYS A 199    19394  18730  16971  -1563  -1353   3945       N  
ATOM    991  CA  CYS A 199     -67.609 -13.166  -9.424  1.00143.19           C  
ANISOU  991  CA  CYS A 199    19178  18728  16501  -1602  -1427   3716       C  
ATOM    992  C   CYS A 199     -68.560 -13.731  -8.361  1.00141.29           C  
ANISOU  992  C   CYS A 199    18706  18469  16507  -1436  -1526   3614       C  
ATOM    993  O   CYS A 199     -68.825 -14.941  -8.340  1.00140.16           O  
ANISOU  993  O   CYS A 199    18568  18488  16201  -1478  -1626   3469       O  
ATOM    994  CB  CYS A 199     -66.245 -13.824  -9.260  1.00141.29           C  
ANISOU  994  CB  CYS A 199    19035  18589  16060  -1684  -1174   3362       C  
ATOM    995  SG  CYS A 199     -65.166 -13.524 -10.653  1.00143.87           S  
ANISOU  995  SG  CYS A 199    19628  19038  15996  -1909  -1048   3461       S  
ATOM    996  N   ALA A 200     -69.061 -12.884  -7.469  1.00141.15           N  
ANISOU  996  N   ALA A 200    18494  18255  16883  -1250  -1489   3679       N  
ATOM    997  CA  ALA A 200     -70.135 -13.324  -6.586  1.00140.17           C  
ANISOU  997  CA  ALA A 200    18136  18140  16982  -1093  -1589   3654       C  
ATOM    998  C   ALA A 200     -71.321 -13.741  -7.453  1.00142.29           C  
ANISOU  998  C   ALA A 200    18379  18538  17145  -1157  -1917   3936       C  
ATOM    999  O   ALA A 200     -72.046 -14.679  -7.131  1.00141.54           O  
ANISOU  999  O   ALA A 200    18161  18563  17056  -1148  -2045   3887       O  
ATOM   1000  CB  ALA A 200     -70.532 -12.230  -5.620  1.00140.47           C  
ANISOU 1000  CB  ALA A 200    17981  17951  17439   -867  -1493   3698       C  
ATOM   1001  N   LEU A 201     -71.486 -13.038  -8.570  1.00145.19           N  
ANISOU 1001  N   LEU A 201    18870  18884  17412  -1239  -2063   4244       N  
ATOM   1002  CA  LEU A 201     -72.503 -13.345  -9.566  1.00147.77           C  
ANISOU 1002  CA  LEU A 201    19211  19345  17591  -1327  -2406   4533       C  
ATOM   1003  C   LEU A 201     -72.178 -14.651 -10.278  1.00147.33           C  
ANISOU 1003  C   LEU A 201    19353  19525  17101  -1538  -2503   4373       C  
ATOM   1004  O   LEU A 201     -73.066 -15.420 -10.624  1.00148.30           O  
ANISOU 1004  O   LEU A 201    19427  19782  17137  -1603  -2776   4453       O  
ATOM   1005  CB  LEU A 201     -72.620 -12.206 -10.571  1.00151.22           C  
ANISOU 1005  CB  LEU A 201    19763  19692  18003  -1361  -2526   4906       C  
ATOM   1006  CG  LEU A 201     -72.817 -10.839  -9.919  1.00152.04           C  
ANISOU 1006  CG  LEU A 201    19710  19508  18549  -1149  -2420   5048       C  
ATOM   1007  CD1 LEU A 201     -72.562  -9.733 -10.930  1.00155.32           C  
ANISOU 1007  CD1 LEU A 201    20309  19805  18901  -1221  -2479   5384       C  
ATOM   1008  CD2 LEU A 201     -74.206 -10.712  -9.296  1.00152.84           C  
ANISOU 1008  CD2 LEU A 201    19491  19560  19021   -936  -2588   5190       C  
ATOM   1009  N   VAL A 202     -70.896 -14.862 -10.545  1.00146.28           N  
ANISOU 1009  N   VAL A 202    19443  19437  16700  -1647  -2284   4152       N  
ATOM   1010  CA  VAL A 202     -70.412 -16.134 -11.071  1.00145.70           C  
ANISOU 1010  CA  VAL A 202    19563  19562  16233  -1809  -2311   3917       C  
ATOM   1011  C   VAL A 202     -70.824 -17.286 -10.148  1.00143.29           C  
ANISOU 1011  C   VAL A 202    19104  19294  16048  -1756  -2349   3676       C  
ATOM   1012  O   VAL A 202     -71.123 -18.384 -10.615  1.00143.76           O  
ANISOU 1012  O   VAL A 202    19255  19491  15877  -1876  -2537   3596       O  
ATOM   1013  CB  VAL A 202     -68.876 -16.130 -11.262  1.00144.77           C  
ANISOU 1013  CB  VAL A 202    19645  19474  15887  -1885  -2000   3677       C  
ATOM   1014  CG1 VAL A 202     -68.368 -17.540 -11.542  1.00143.86           C  
ANISOU 1014  CG1 VAL A 202    19689  19535  15437  -1991  -1993   3363       C  
ATOM   1015  CG2 VAL A 202     -68.486 -15.194 -12.402  1.00147.80           C  
ANISOU 1015  CG2 VAL A 202    20223  19874  16060  -1999  -1986   3942       C  
ATOM   1016  N   GLU A 203     -70.838 -17.053  -8.839  1.00141.01           N  
ANISOU 1016  N   GLU A 203    18594  18876  16109  -1583  -2174   3560       N  
ATOM   1017  CA  GLU A 203     -71.278 -18.123  -7.950  1.00139.10           C  
ANISOU 1017  CA  GLU A 203    18203  18674  15974  -1540  -2209   3378       C  
ATOM   1018  C   GLU A 203     -72.805 -18.228  -7.755  1.00140.43           C  
ANISOU 1018  C   GLU A 203    18127  18860  16370  -1493  -2471   3621       C  
ATOM   1019  O   GLU A 203     -73.333 -19.339  -7.675  1.00140.26           O  
ANISOU 1019  O   GLU A 203    18063  18932  16298  -1574  -2632   3559       O  
ATOM   1020  CB  GLU A 203     -70.606 -18.017  -6.584  1.00142.28           C  
ANISOU 1020  CB  GLU A 203    18488  18973  16598  -1386  -1911   3121       C  
ATOM   1021  CG  GLU A 203     -70.872 -19.266  -5.723  1.00140.41           C  
ANISOU 1021  CG  GLU A 203    18152  18795  16404  -1370  -1929   2923       C  
ATOM   1022  CD  GLU A 203     -70.606 -20.590  -6.481  1.00140.63           C  
ANISOU 1022  CD  GLU A 203    18389  18946  16099  -1552  -2069   2777       C  
ATOM   1023  OE1 GLU A 203     -69.659 -20.637  -7.302  1.00141.06           O  
ANISOU 1023  OE1 GLU A 203    18681  19046  15869  -1647  -2000   2666       O  
ATOM   1024  OE2 GLU A 203     -71.354 -21.580  -6.280  1.00140.71           O  
ANISOU 1024  OE2 GLU A 203    18325  19004  16133  -1604  -2248   2775       O  
ATOM   1025  N   ILE A 204     -73.519 -17.108  -7.648  1.00141.95           N  
ANISOU 1025  N   ILE A 204    18143  18957  16837  -1362  -2515   3895       N  
ATOM   1026  CA  ILE A 204     -74.971 -17.190  -7.442  1.00143.53           C  
ANISOU 1026  CA  ILE A 204    18063  19191  17280  -1301  -2749   4130       C  
ATOM   1027  C   ILE A 204     -75.713 -17.855  -8.602  1.00146.08           C  
ANISOU 1027  C   ILE A 204    18459  19666  17379  -1498  -3128   4316       C  
ATOM   1028  O   ILE A 204     -76.686 -18.565  -8.386  1.00146.73           O  
ANISOU 1028  O   ILE A 204    18349  19830  17574  -1533  -3325   4382       O  
ATOM   1029  CB  ILE A 204     -75.629 -15.799  -7.205  1.00145.31           C  
ANISOU 1029  CB  ILE A 204    18080  19273  17857  -1095  -2740   4402       C  
ATOM   1030  CG1 ILE A 204     -75.563 -14.900  -8.443  1.00148.13           C  
ANISOU 1030  CG1 ILE A 204    18610  19589  18084  -1159  -2892   4682       C  
ATOM   1031  CG2 ILE A 204     -75.024 -15.115  -6.017  1.00143.26           C  
ANISOU 1031  CG2 ILE A 204    17742  18852  17840   -894  -2397   4209       C  
ATOM   1032  CD1 ILE A 204     -76.306 -13.588  -8.270  1.00150.39           C  
ANISOU 1032  CD1 ILE A 204    18690  19708  18743   -948  -2930   4975       C  
ATOM   1033  N   LEU A 205     -75.250 -17.646  -9.829  1.00147.79           N  
ANISOU 1033  N   LEU A 205    18955  19931  17267  -1639  -3234   4397       N  
ATOM   1034  CA  LEU A 205     -75.936 -18.218 -10.978  1.00150.64           C  
ANISOU 1034  CA  LEU A 205    19416  20445  17377  -1830  -3616   4565       C  
ATOM   1035  C   LEU A 205     -75.536 -19.676 -11.145  1.00149.55           C  
ANISOU 1035  C   LEU A 205    19461  20416  16943  -2008  -3662   4261       C  
ATOM   1036  O   LEU A 205     -76.182 -20.437 -11.863  1.00151.64           O  
ANISOU 1036  O   LEU A 205    19784  20799  17034  -2175  -3991   4322       O  
ATOM   1037  CB  LEU A 205     -75.658 -17.414 -12.247  1.00153.44           C  
ANISOU 1037  CB  LEU A 205    20012  20825  17462  -1910  -3723   4794       C  
ATOM   1038  CG  LEU A 205     -76.234 -15.992 -12.210  1.00155.36           C  
ANISOU 1038  CG  LEU A 205    20075  20933  18020  -1740  -3759   5154       C  
ATOM   1039  CD1 LEU A 205     -76.215 -15.356 -13.599  1.00158.96           C  
ANISOU 1039  CD1 LEU A 205    20768  21444  18186  -1855  -3967   5457       C  
ATOM   1040  CD2 LEU A 205     -77.632 -15.945 -11.592  1.00156.32           C  
ANISOU 1040  CD2 LEU A 205    19802  21038  18555  -1605  -3952   5348       C  
ATOM   1041  N   LEU A 206     -74.447 -20.048 -10.487  1.00147.43           N  
ANISOU 1041  N   LEU A 206    19290  20098  16628  -1968  -3343   3927       N  
ATOM   1042  CA  LEU A 206     -74.075 -21.448 -10.350  1.00146.10           C  
ANISOU 1042  CA  LEU A 206    19246  19984  16280  -2081  -3349   3615       C  
ATOM   1043  C   LEU A 206     -74.457 -21.931  -8.954  1.00143.79           C  
ANISOU 1043  C   LEU A 206    18679  19623  16333  -1971  -3245   3515       C  
ATOM   1044  O   LEU A 206     -73.990 -22.973  -8.498  1.00142.09           O  
ANISOU 1044  O   LEU A 206    18535  19400  16051  -2011  -3167   3242       O  
ATOM   1045  CB  LEU A 206     -72.579 -21.655 -10.617  1.00147.41           C  
ANISOU 1045  CB  LEU A 206    19708  20158  16143  -2110  -3082   3311       C  
ATOM   1046  CG  LEU A 206     -72.108 -21.415 -12.061  1.00150.01           C  
ANISOU 1046  CG  LEU A 206    20350  20599  16046  -2250  -3160   3369       C  
ATOM   1047  CD1 LEU A 206     -70.586 -21.512 -12.150  1.00148.62           C  
ANISOU 1047  CD1 LEU A 206    20394  20436  15637  -2245  -2825   3071       C  
ATOM   1048  CD2 LEU A 206     -72.779 -22.390 -13.039  1.00152.70           C  
ANISOU 1048  CD2 LEU A 206    20850  21068  16100  -2444  -3534   3381       C  
ATOM   1049  N   ALA A 207     -75.261 -21.128  -8.259  1.00145.70           N  
ANISOU 1049  N   ALA A 207    18611  19811  16939  -1815  -3223   3737       N  
ATOM   1050  CA  ALA A 207     -75.834 -21.533  -6.978  1.00144.27           C  
ANISOU 1050  CA  ALA A 207    18139  19601  17075  -1714  -3142   3700       C  
ATOM   1051  C   ALA A 207     -77.179 -22.227  -7.185  1.00146.53           C  
ANISOU 1051  C   ALA A 207    18230  19976  17467  -1837  -3483   3901       C  
ATOM   1052  O   ALA A 207     -77.720 -22.829  -6.258  1.00145.84           O  
ANISOU 1052  O   ALA A 207    17918  19897  17598  -1815  -3455   3882       O  
ATOM   1053  CB  ALA A 207     -75.996 -20.337  -6.044  1.00142.91           C  
ANISOU 1053  CB  ALA A 207    17724  19334  17240  -1465  -2910   3800       C  
ATOM   1054  N   PHE A 208     -77.725 -22.126  -8.397  1.00146.83           N  
ANISOU 1054  N   PHE A 208    18347  20089  17352  -1975  -3810   4107       N  
ATOM   1055  CA  PHE A 208     -79.065 -22.650  -8.665  1.00149.53           C  
ANISOU 1055  CA  PHE A 208    18471  20521  17823  -2100  -4175   4333       C  
ATOM   1056  C   PHE A 208     -79.096 -24.151  -8.973  1.00149.92           C  
ANISOU 1056  C   PHE A 208    18675  20614  17673  -2347  -4386   4151       C  
ATOM   1057  O   PHE A 208     -78.562 -24.613  -9.981  1.00150.82           O  
ANISOU 1057  O   PHE A 208    19131  20759  17413  -2507  -4527   4015       O  
ATOM   1058  CB  PHE A 208     -79.731 -21.886  -9.817  1.00153.06           C  
ANISOU 1058  CB  PHE A 208    18915  21033  18206  -2143  -4486   4657       C  
ATOM   1059  CG  PHE A 208     -80.291 -20.544  -9.417  1.00153.88           C  
ANISOU 1059  CG  PHE A 208    18727  21082  18658  -1902  -4399   4935       C  
ATOM   1060  CD1 PHE A 208     -79.834 -19.379 -10.009  1.00154.67           C  
ANISOU 1060  CD1 PHE A 208    18977  21119  18670  -1807  -4339   5062       C  
ATOM   1061  CD2 PHE A 208     -81.303 -20.454  -8.477  1.00154.30           C  
ANISOU 1061  CD2 PHE A 208    18353  21142  19131  -1771  -4380   5081       C  
ATOM   1062  CE1 PHE A 208     -80.359 -18.147  -9.650  1.00155.77           C  
ANISOU 1062  CE1 PHE A 208    18861  21168  19155  -1574  -4274   5312       C  
ATOM   1063  CE2 PHE A 208     -81.824 -19.227  -8.111  1.00155.40           C  
ANISOU 1063  CE2 PHE A 208    18226  21219  19601  -1522  -4293   5311       C  
ATOM   1064  CZ  PHE A 208     -81.352 -18.074  -8.700  1.00156.13           C  
ANISOU 1064  CZ  PHE A 208    18488  21215  19621  -1419  -4251   5421       C  
ATOM   1065  N   VAL A 209     -79.738 -24.887  -8.068  1.00153.03           N  
ANISOU 1065  N   VAL A 209    18814  21004  18328  -2370  -4396   4153       N  
ATOM   1066  CA  VAL A 209     -80.017 -26.332  -8.169  1.00153.85           C  
ANISOU 1066  CA  VAL A 209    18984  21112  18359  -2608  -4623   4032       C  
ATOM   1067  C   VAL A 209     -78.811 -27.243  -8.527  1.00152.40           C  
ANISOU 1067  C   VAL A 209    19230  20860  17816  -2711  -4555   3655       C  
ATOM   1068  O   VAL A 209     -78.861 -27.998  -9.502  1.00154.49           O  
ANISOU 1068  O   VAL A 209    19735  21145  17821  -2924  -4850   3570       O  
ATOM   1069  CB  VAL A 209     -81.165 -26.595  -9.193  1.00154.45           C  
ANISOU 1069  CB  VAL A 209    18984  21288  18414  -2826  -5114   4275       C  
ATOM   1070  CG1 VAL A 209     -81.829 -27.944  -8.922  1.00155.67           C  
ANISOU 1070  CG1 VAL A 209    19036  21428  18685  -3053  -5342   4241       C  
ATOM   1071  CG2 VAL A 209     -82.213 -25.499  -9.104  1.00156.34           C  
ANISOU 1071  CG2 VAL A 209    18836  21603  18964  -2692  -5193   4656       C  
ATOM   1072  N   PRO A 210     -77.725 -27.192  -7.734  1.00150.01           N  
ANISOU 1072  N   PRO A 210    19023  20476  17498  -2553  -4175   3414       N  
ATOM   1073  CA  PRO A 210     -76.785 -28.287  -7.964  1.00149.17           C  
ANISOU 1073  CA  PRO A 210    19253  20300  17124  -2655  -4153   3070       C  
ATOM   1074  C   PRO A 210     -76.321 -29.049  -6.703  1.00146.60           C  
ANISOU 1074  C   PRO A 210    18875  19871  16957  -2583  -3920   2876       C  
ATOM   1075  O   PRO A 210     -75.134 -29.347  -6.605  1.00144.78           O  
ANISOU 1075  O   PRO A 210    18883  19576  16550  -2518  -3715   2585       O  
ATOM   1076  CB  PRO A 210     -75.597 -27.551  -8.595  1.00146.07           C  
ANISOU 1076  CB  PRO A 210    19137  19926  16436  -2558  -3946   2921       C  
ATOM   1077  CG  PRO A 210     -75.713 -26.088  -8.057  1.00144.99           C  
ANISOU 1077  CG  PRO A 210    18756  19803  16529  -2346  -3725   3139       C  
ATOM   1078  CD  PRO A 210     -76.994 -26.013  -7.249  1.00145.61           C  
ANISOU 1078  CD  PRO A 210    18437  19895  16994  -2312  -3819   3397       C  
ATOM   1079  N   PRO A 211     -77.235 -29.401  -5.784  1.00142.95           N  
ANISOU 1079  N   PRO A 211    18104  19400  16811  -2601  -3958   3041       N  
ATOM   1080  CA  PRO A 211     -76.892 -29.754  -4.391  1.00140.54           C  
ANISOU 1080  CA  PRO A 211    17681  19029  16691  -2478  -3680   2946       C  
ATOM   1081  C   PRO A 211     -75.909 -30.923  -4.182  1.00139.30           C  
ANISOU 1081  C   PRO A 211    17804  18744  16381  -2522  -3620   2624       C  
ATOM   1082  O   PRO A 211     -74.755 -30.695  -3.816  1.00136.94           O  
ANISOU 1082  O   PRO A 211    17647  18407  15979  -2361  -3344   2404       O  
ATOM   1083  CB  PRO A 211     -78.254 -30.116  -3.793  1.00143.24           C  
ANISOU 1083  CB  PRO A 211    17666  19413  17346  -2573  -3828   3223       C  
ATOM   1084  CG  PRO A 211     -79.238 -29.391  -4.658  1.00145.86           C  
ANISOU 1084  CG  PRO A 211    17836  19854  17730  -2633  -4078   3496       C  
ATOM   1085  CD  PRO A 211     -78.676 -29.548  -6.027  1.00146.86           C  
ANISOU 1085  CD  PRO A 211    18336  19965  17501  -2756  -4282   3342       C  
ATOM   1086  N   LYS A 212     -76.380 -32.155  -4.363  1.00140.53           N  
ANISOU 1086  N   LYS A 212    18020  18821  16554  -2735  -3883   2606       N  
ATOM   1087  CA  LYS A 212     -75.560 -33.351  -4.153  1.00139.89           C  
ANISOU 1087  CA  LYS A 212    18198  18582  16373  -2775  -3863   2319       C  
ATOM   1088  C   LYS A 212     -74.459 -33.450  -5.208  1.00139.88           C  
ANISOU 1088  C   LYS A 212    18583  18549  16017  -2762  -3861   2011       C  
ATOM   1089  O   LYS A 212     -73.462 -34.160  -5.028  1.00138.90           O  
ANISOU 1089  O   LYS A 212    18681  18308  15788  -2705  -3749   1725       O  
ATOM   1090  CB  LYS A 212     -76.437 -34.612  -4.179  1.00142.83           C  
ANISOU 1090  CB  LYS A 212    18544  18850  16876  -3031  -4183   2397       C  
ATOM   1091  CG  LYS A 212     -77.400 -34.762  -2.987  1.00143.02           C  
ANISOU 1091  CG  LYS A 212    18192  18898  17252  -3058  -4140   2682       C  
ATOM   1092  CD  LYS A 212     -78.345 -35.963  -3.143  1.00146.13           C  
ANISOU 1092  CD  LYS A 212    18542  19188  17793  -3359  -4490   2797       C  
ATOM   1093  CE  LYS A 212     -79.222 -36.164  -1.898  1.00146.52           C  
ANISOU 1093  CE  LYS A 212    18212  19274  18183  -3391  -4400   3088       C  
ATOM   1094  NZ  LYS A 212     -80.230 -37.263  -2.046  1.00149.94           N  
ANISOU 1094  NZ  LYS A 212    18554  19613  18802  -3715  -4746   3248       N  
ATOM   1095  N   VAL A 213     -74.671 -32.749  -6.320  1.00141.34           N  
ANISOU 1095  N   VAL A 213    18837  18847  16018  -2813  -3990   2084       N  
ATOM   1096  CA  VAL A 213     -73.720 -32.692  -7.427  1.00141.86           C  
ANISOU 1096  CA  VAL A 213    19253  18936  15713  -2808  -3973   1834       C  
ATOM   1097  C   VAL A 213     -72.391 -32.094  -6.984  1.00138.99           C  
ANISOU 1097  C   VAL A 213    18955  18581  15276  -2576  -3573   1646       C  
ATOM   1098  O   VAL A 213     -71.321 -32.638  -7.262  1.00138.69           O  
ANISOU 1098  O   VAL A 213    19176  18486  15034  -2532  -3467   1335       O  
ATOM   1099  CB  VAL A 213     -74.272 -31.859  -8.594  1.00144.07           C  
ANISOU 1099  CB  VAL A 213    19557  19365  15819  -2894  -4164   2023       C  
ATOM   1100  CG1 VAL A 213     -73.279 -31.833  -9.748  1.00145.00           C  
ANISOU 1100  CG1 VAL A 213    20050  19532  15512  -2899  -4124   1772       C  
ATOM   1101  CG2 VAL A 213     -75.617 -32.409  -9.045  1.00147.23           C  
ANISOU 1101  CG2 VAL A 213    19863  19773  16305  -3133  -4593   2220       C  
ATOM   1102  N   ILE A 214     -72.477 -30.955  -6.307  1.00137.20           N  
ANISOU 1102  N   ILE A 214    18480  18423  15227  -2424  -3360   1831       N  
ATOM   1103  CA  ILE A 214     -71.306 -30.297  -5.753  1.00134.60           C  
ANISOU 1103  CA  ILE A 214    18164  18097  14883  -2217  -2997   1680       C  
ATOM   1104  C   ILE A 214     -70.624 -31.201  -4.725  1.00132.84           C  
ANISOU 1104  C   ILE A 214    17962  17757  14755  -2131  -2852   1460       C  
ATOM   1105  O   ILE A 214     -69.398 -31.276  -4.663  1.00131.62           O  
ANISOU 1105  O   ILE A 214    17955  17577  14477  -2019  -2646   1203       O  
ATOM   1106  CB  ILE A 214     -71.680 -28.956  -5.116  1.00133.41           C  
ANISOU 1106  CB  ILE A 214    17733  18008  14948  -2079  -2831   1920       C  
ATOM   1107  CG1 ILE A 214     -72.452 -28.101  -6.114  1.00135.53           C  
ANISOU 1107  CG1 ILE A 214    17967  18371  15158  -2157  -3012   2178       C  
ATOM   1108  CG2 ILE A 214     -70.442 -28.202  -4.736  1.00131.25           C  
ANISOU 1108  CG2 ILE A 214    17503  17733  14634  -1901  -2496   1755       C  
ATOM   1109  CD1 ILE A 214     -73.148 -26.929  -5.480  1.00135.11           C  
ANISOU 1109  CD1 ILE A 214    17605  18348  15382  -2029  -2923   2451       C  
ATOM   1110  N   GLN A 215     -71.431 -31.887  -3.923  1.00133.01           N  
ANISOU 1110  N   GLN A 215    17823  17713  15002  -2187  -2966   1581       N  
ATOM   1111  CA  GLN A 215     -70.922 -32.875  -2.980  1.00131.92           C  
ANISOU 1111  CA  GLN A 215    17721  17449  14954  -2132  -2885   1418       C  
ATOM   1112  C   GLN A 215     -70.083 -33.926  -3.695  1.00132.91           C  
ANISOU 1112  C   GLN A 215    18175  17462  14862  -2182  -2969   1103       C  
ATOM   1113  O   GLN A 215     -69.100 -34.414  -3.145  1.00131.69           O  
ANISOU 1113  O   GLN A 215    18110  17222  14704  -2055  -2812    883       O  
ATOM   1114  CB  GLN A 215     -72.062 -33.587  -2.247  1.00138.01           C  
ANISOU 1114  CB  GLN A 215    18299  18166  15972  -2250  -3051   1634       C  
ATOM   1115  CG  GLN A 215     -72.931 -32.759  -1.319  1.00137.35           C  
ANISOU 1115  CG  GLN A 215    17863  18191  16134  -2179  -2940   1929       C  
ATOM   1116  CD  GLN A 215     -73.972 -33.632  -0.629  1.00138.73           C  
ANISOU 1116  CD  GLN A 215    17858  18321  16533  -2317  -3087   2132       C  
ATOM   1117  OE1 GLN A 215     -74.597 -34.484  -1.266  1.00141.05           O  
ANISOU 1117  OE1 GLN A 215    18219  18543  16831  -2539  -3385   2179       O  
ATOM   1118  NE2 GLN A 215     -74.152 -33.436   0.676  1.00137.60           N  
ANISOU 1118  NE2 GLN A 215    17492  18222  16568  -2198  -2881   2251       N  
ATOM   1119  N   LYS A 216     -70.506 -34.316  -4.899  1.00135.44           N  
ANISOU 1119  N   LYS A 216    18672  17779  15009  -2359  -3232   1079       N  
ATOM   1120  CA  LYS A 216     -69.751 -35.307  -5.667  1.00136.90           C  
ANISOU 1120  CA  LYS A 216    19193  17858  14966  -2397  -3313    751       C  
ATOM   1121  C   LYS A 216     -68.509 -34.714  -6.333  1.00136.33           C  
ANISOU 1121  C   LYS A 216    19293  17885  14621  -2260  -3074    520       C  
ATOM   1122  O   LYS A 216     -67.477 -35.381  -6.420  1.00136.40           O  
ANISOU 1122  O   LYS A 216    19495  17812  14519  -2168  -2970    211       O  
ATOM   1123  CB  LYS A 216     -70.629 -35.991  -6.729  1.00140.27           C  
ANISOU 1123  CB  LYS A 216    19777  18244  15274  -2644  -3695    772       C  
ATOM   1124  CG  LYS A 216     -69.834 -36.975  -7.595  1.00142.21           C  
ANISOU 1124  CG  LYS A 216    20401  18379  15255  -2665  -3770    392       C  
ATOM   1125  CD  LYS A 216     -70.675 -37.998  -8.346  1.00145.74           C  
ANISOU 1125  CD  LYS A 216    21025  18704  15646  -2914  -4179    355       C  
ATOM   1126  CE  LYS A 216     -69.765 -38.881  -9.201  1.00147.81           C  
ANISOU 1126  CE  LYS A 216    21684  18856  15620  -2888  -4205    -72       C  
ATOM   1127  NZ  LYS A 216     -70.351 -40.197  -9.567  1.00151.08           N  
ANISOU 1127  NZ  LYS A 216    22298  19043  16062  -3091  -4576   -196       N  
ATOM   1128  N   ILE A 217     -68.596 -33.470  -6.799  1.00136.03           N  
ANISOU 1128  N   ILE A 217    19178  18019  14490  -2246  -2983    678       N  
ATOM   1129  CA  ILE A 217     -67.454 -32.828  -7.461  1.00135.83           C  
ANISOU 1129  CA  ILE A 217    19296  18103  14210  -2145  -2744    503       C  
ATOM   1130  C   ILE A 217     -66.375 -32.450  -6.446  1.00133.06           C  
ANISOU 1130  C   ILE A 217    18821  17738  13996  -1933  -2406    387       C  
ATOM   1131  O   ILE A 217     -65.184 -32.508  -6.742  1.00133.00           O  
ANISOU 1131  O   ILE A 217    18947  17758  13830  -1835  -2207    132       O  
ATOM   1132  CB  ILE A 217     -67.882 -31.581  -8.261  1.00136.67           C  
ANISOU 1132  CB  ILE A 217    19363  18377  14189  -2207  -2760    744       C  
ATOM   1133  CG1 ILE A 217     -68.765 -31.997  -9.433  1.00139.93           C  
ANISOU 1133  CG1 ILE A 217    19945  18828  14392  -2417  -3110    815       C  
ATOM   1134  CG2 ILE A 217     -66.676 -30.844  -8.808  1.00136.46           C  
ANISOU 1134  CG2 ILE A 217    19451  18464  13936  -2113  -2475    606       C  
ATOM   1135  CD1 ILE A 217     -69.429 -30.837 -10.134  1.00141.11           C  
ANISOU 1135  CD1 ILE A 217    20026  19128  14460  -2487  -3199   1122       C  
ATOM   1136  N   PHE A 218     -66.789 -32.104  -5.233  1.00131.05           N  
ANISOU 1136  N   PHE A 218    18309  17450  14035  -1862  -2344    563       N  
ATOM   1137  CA  PHE A 218     -65.832 -31.824  -4.173  1.00128.67           C  
ANISOU 1137  CA  PHE A 218    17893  17130  13866  -1671  -2068    448       C  
ATOM   1138  C   PHE A 218     -66.050 -32.714  -2.961  1.00127.74           C  
ANISOU 1138  C   PHE A 218    17682  16883  13970  -1623  -2114    444       C  
ATOM   1139  O   PHE A 218     -66.438 -32.234  -1.898  1.00126.25           O  
ANISOU 1139  O   PHE A 218    17272  16710  13988  -1556  -2035    611       O  
ATOM   1140  CB  PHE A 218     -65.940 -30.359  -3.772  1.00127.25           C  
ANISOU 1140  CB  PHE A 218    17504  17047  13799  -1599  -1896    645       C  
ATOM   1141  CG  PHE A 218     -65.857 -29.420  -4.936  1.00128.46           C  
ANISOU 1141  CG  PHE A 218    17739  17312  13758  -1663  -1870    720       C  
ATOM   1142  CD1 PHE A 218     -66.991 -28.787  -5.415  1.00129.62           C  
ANISOU 1142  CD1 PHE A 218    17812  17511  13928  -1766  -2039   1012       C  
ATOM   1143  CD2 PHE A 218     -64.652 -29.219  -5.597  1.00128.84           C  
ANISOU 1143  CD2 PHE A 218    17938  17422  13593  -1626  -1686    513       C  
ATOM   1144  CE1 PHE A 218     -66.917 -27.932  -6.508  1.00131.06           C  
ANISOU 1144  CE1 PHE A 218    18088  17792  13917  -1829  -2033   1111       C  
ATOM   1145  CE2 PHE A 218     -64.567 -28.366  -6.686  1.00130.30           C  
ANISOU 1145  CE2 PHE A 218    18211  17719  13576  -1702  -1653    611       C  
ATOM   1146  CZ  PHE A 218     -65.700 -27.723  -7.145  1.00131.41           C  
ANISOU 1146  CZ  PHE A 218    18300  17898  13731  -1804  -1835    916       C  
ATOM   1147  N   PRO A 219     -65.694 -34.001  -3.091  1.00128.79           N  
ANISOU 1147  N   PRO A 219    17998  16885  14052  -1640  -2221    235       N  
ATOM   1148  CA  PRO A 219     -65.846 -34.989  -2.021  1.00128.41           C  
ANISOU 1148  CA  PRO A 219    17904  16686  14200  -1610  -2288    237       C  
ATOM   1149  C   PRO A 219     -64.870 -34.684  -0.896  1.00126.24           C  
ANISOU 1149  C   PRO A 219    17514  16426  14027  -1399  -2037    145       C  
ATOM   1150  O   PRO A 219     -64.071 -33.774  -1.069  1.00125.25           O  
ANISOU 1150  O   PRO A 219    17357  16413  13822  -1298  -1829     54       O  
ATOM   1151  CB  PRO A 219     -65.525 -36.308  -2.727  1.00130.56           C  
ANISOU 1151  CB  PRO A 219    18452  16800  14355  -1667  -2457     -8       C  
ATOM   1152  CG  PRO A 219     -64.591 -35.931  -3.790  1.00131.19           C  
ANISOU 1152  CG  PRO A 219    18695  16976  14174  -1611  -2327   -243       C  
ATOM   1153  CD  PRO A 219     -65.032 -34.581  -4.273  1.00130.70           C  
ANISOU 1153  CD  PRO A 219    18519  17108  14034  -1671  -2263    -34       C  
ATOM   1154  N   PRO A 220     -64.950 -35.392   0.242  1.00125.75           N  
ANISOU 1154  N   PRO A 220    17387  16258  14136  -1346  -2063    186       N  
ATOM   1155  CA  PRO A 220     -64.004 -35.143   1.342  1.00124.00           C  
ANISOU 1155  CA  PRO A 220    17066  16058  13989  -1145  -1855     95       C  
ATOM   1156  C   PRO A 220     -62.515 -35.320   0.978  1.00124.00           C  
ANISOU 1156  C   PRO A 220    17191  16045  13877   -999  -1723   -232       C  
ATOM   1157  O   PRO A 220     -61.663 -34.694   1.611  1.00122.59           O  
ANISOU 1157  O   PRO A 220    16902  15946  13731   -849  -1529   -310       O  
ATOM   1158  CB  PRO A 220     -64.427 -36.172   2.402  1.00124.35           C  
ANISOU 1158  CB  PRO A 220    17086  15969  14193  -1151  -1972    204       C  
ATOM   1159  CG  PRO A 220     -65.226 -37.201   1.653  1.00126.57           C  
ANISOU 1159  CG  PRO A 220    17515  16102  14472  -1345  -2239    247       C  
ATOM   1160  CD  PRO A 220     -65.945 -36.414   0.607  1.00127.04           C  
ANISOU 1160  CD  PRO A 220    17553  16284  14433  -1483  -2292    347       C  
ATOM   1161  N   ILE A 221     -62.212 -36.166  -0.005  1.00125.83           N  
ANISOU 1161  N   ILE A 221    17642  16181  13986  -1038  -1826   -428       N  
ATOM   1162  CA  ILE A 221     -60.831 -36.389  -0.427  1.00126.33           C  
ANISOU 1162  CA  ILE A 221    17810  16245  13944   -889  -1686   -747       C  
ATOM   1163  C   ILE A 221     -60.281 -35.188  -1.188  1.00125.91           C  
ANISOU 1163  C   ILE A 221    17714  16390  13736   -880  -1480   -803       C  
ATOM   1164  O   ILE A 221     -59.070 -34.995  -1.262  1.00125.85           O  
ANISOU 1164  O   ILE A 221    17688  16445  13685   -743  -1289  -1014       O  
ATOM   1165  CB  ILE A 221     -60.700 -37.642  -1.326  1.00128.90           C  
ANISOU 1165  CB  ILE A 221    18401  16409  14167   -921  -1845   -967       C  
ATOM   1166  CG1 ILE A 221     -59.263 -38.165  -1.318  1.00129.58           C  
ANISOU 1166  CG1 ILE A 221    18550  16447  14236   -705  -1707  -1292       C  
ATOM   1167  CG2 ILE A 221     -61.164 -37.349  -2.745  1.00130.46           C  
ANISOU 1167  CG2 ILE A 221    18745  16692  14131  -1081  -1909   -984       C  
ATOM   1168  CD1 ILE A 221     -58.719 -38.416   0.066  1.00128.30           C  
ANISOU 1168  CD1 ILE A 221    18245  16218  14286   -536  -1661  -1274       C  
ATOM   1169  N   VAL A 222     -61.171 -34.374  -1.746  1.00125.87           N  
ANISOU 1169  N   VAL A 222    17680  16484  13663  -1030  -1521   -595       N  
ATOM   1170  CA  VAL A 222     -60.765 -33.146  -2.418  1.00125.64           C  
ANISOU 1170  CA  VAL A 222    17607  16628  13505  -1043  -1338   -583       C  
ATOM   1171  C   VAL A 222     -60.962 -31.987  -1.473  1.00123.57           C  
ANISOU 1171  C   VAL A 222    17107  16433  13412  -1000  -1219   -387       C  
ATOM   1172  O   VAL A 222     -60.110 -31.127  -1.320  1.00122.79           O  
ANISOU 1172  O   VAL A 222    16911  16420  13322   -921  -1011   -453       O  
ATOM   1173  CB  VAL A 222     -61.569 -32.898  -3.699  1.00127.32           C  
ANISOU 1173  CB  VAL A 222    17952  16904  13521  -1223  -1467   -468       C  
ATOM   1174  CG1 VAL A 222     -61.372 -31.473  -4.184  1.00126.99           C  
ANISOU 1174  CG1 VAL A 222    17831  17024  13396  -1250  -1295   -352       C  
ATOM   1175  CG2 VAL A 222     -61.188 -33.902  -4.766  1.00129.78           C  
ANISOU 1175  CG2 VAL A 222    18529  17175  13606  -1253  -1545   -721       C  
ATOM   1176  N   THR A 223     -62.108 -31.992  -0.823  1.00122.98           N  
ANISOU 1176  N   THR A 223    16933  16314  13478  -1057  -1355   -153       N  
ATOM   1177  CA  THR A 223     -62.470 -30.932   0.084  1.00121.41           C  
ANISOU 1177  CA  THR A 223    16520  16172  13436  -1009  -1255     30       C  
ATOM   1178  C   THR A 223     -61.444 -30.774   1.202  1.00120.00           C  
ANISOU 1178  C   THR A 223    16239  15996  13360   -837  -1084   -117       C  
ATOM   1179  O   THR A 223     -60.819 -29.728   1.320  1.00119.29           O  
ANISOU 1179  O   THR A 223    16057  15979  13287   -779   -909   -156       O  
ATOM   1180  CB  THR A 223     -63.876 -31.181   0.678  1.00121.43           C  
ANISOU 1180  CB  THR A 223    16422  16136  13579  -1082  -1419    290       C  
ATOM   1181  OG1 THR A 223     -64.845 -31.228  -0.385  1.00122.97           O  
ANISOU 1181  OG1 THR A 223    16685  16343  13693  -1251  -1602    439       O  
ATOM   1182  CG2 THR A 223     -64.246 -30.060   1.591  1.00120.16           C  
ANISOU 1182  CG2 THR A 223    16048  16043  13567  -1005  -1292    450       C  
ATOM   1183  N   GLY A 224     -61.254 -31.817   1.998  1.00119.89           N  
ANISOU 1183  N   GLY A 224    16244  15895  13413   -764  -1151   -192       N  
ATOM   1184  CA  GLY A 224     -60.348 -31.755   3.137  1.00118.84           C  
ANISOU 1184  CA  GLY A 224    16014  15770  13370   -600  -1033   -312       C  
ATOM   1185  C   GLY A 224     -58.930 -31.202   3.009  1.00118.59           C  
ANISOU 1185  C   GLY A 224    15945  15806  13306   -496   -848   -540       C  
ATOM   1186  O   GLY A 224     -58.515 -30.374   3.832  1.00117.59           O  
ANISOU 1186  O   GLY A 224    15677  15738  13264   -416   -730   -550       O  
ATOM   1187  N   PRO A 225     -58.158 -31.668   2.007  1.00119.77           N  
ANISOU 1187  N   PRO A 225    16216  15954  13339   -496   -819   -735       N  
ATOM   1188  CA  PRO A 225     -56.791 -31.153   1.864  1.00119.89           C  
ANISOU 1188  CA  PRO A 225    16159  16054  13339   -407   -626   -940       C  
ATOM   1189  C   PRO A 225     -56.753 -29.659   1.564  1.00119.41           C  
ANISOU 1189  C   PRO A 225    15997  16099  13276   -481   -475   -846       C  
ATOM   1190  O   PRO A 225     -56.001 -28.939   2.209  1.00118.80           O  
ANISOU 1190  O   PRO A 225    15774  16068  13297   -412   -350   -913       O  
ATOM   1191  CB  PRO A 225     -56.236 -31.956   0.681  1.00121.73           C  
ANISOU 1191  CB  PRO A 225    16555  16278  13418   -412   -619  -1135       C  
ATOM   1192  CG  PRO A 225     -57.433 -32.404  -0.075  1.00122.50           C  
ANISOU 1192  CG  PRO A 225    16820  16315  13409   -558   -794   -998       C  
ATOM   1193  CD  PRO A 225     -58.452 -32.691   0.987  1.00121.39           C  
ANISOU 1193  CD  PRO A 225    16622  16083  13419   -572   -953   -796       C  
ATOM   1194  N   THR A 226     -57.582 -29.215   0.624  1.00119.93           N  
ANISOU 1194  N   THR A 226    16141  16187  13241   -623   -510   -684       N  
ATOM   1195  CA  THR A 226     -57.685 -27.807   0.267  1.00119.82           C  
ANISOU 1195  CA  THR A 226    16053  16240  13234   -701   -393   -551       C  
ATOM   1196  C   THR A 226     -57.862 -26.945   1.497  1.00118.41           C  
ANISOU 1196  C   THR A 226    15702  16038  13249   -635   -351   -468       C  
ATOM   1197  O   THR A 226     -57.135 -25.972   1.688  1.00118.29           O  
ANISOU 1197  O   THR A 226    15586  16055  13305   -619   -204   -521       O  
ATOM   1198  CB  THR A 226     -58.844 -27.561  -0.690  1.00120.62           C  
ANISOU 1198  CB  THR A 226    16255  16346  13228   -847   -507   -330       C  
ATOM   1199  OG1 THR A 226     -58.583 -28.254  -1.911  1.00122.32           O  
ANISOU 1199  OG1 THR A 226    16653  16601  13221   -914   -534   -436       O  
ATOM   1200  CG2 THR A 226     -58.971 -26.094  -0.991  1.00120.71           C  
ANISOU 1200  CG2 THR A 226    16193  16397  13277   -911   -402   -167       C  
ATOM   1201  N   VAL A 227     -58.836 -27.293   2.325  1.00117.63           N  
ANISOU 1201  N   VAL A 227    15574  15887  13234   -605   -477   -341       N  
ATOM   1202  CA  VAL A 227     -59.065 -26.558   3.558  1.00116.60           C  
ANISOU 1202  CA  VAL A 227    15298  15748  13258   -523   -432   -282       C  
ATOM   1203  C   VAL A 227     -57.842 -26.618   4.474  1.00116.16           C  
ANISOU 1203  C   VAL A 227    15165  15709  13260   -399   -347   -503       C  
ATOM   1204  O   VAL A 227     -57.454 -25.601   5.074  1.00115.85           O  
ANISOU 1204  O   VAL A 227    15018  15682  13316   -360   -247   -542       O  
ATOM   1205  CB  VAL A 227     -60.279 -27.095   4.318  1.00116.23           C  
ANISOU 1205  CB  VAL A 227    15226  15670  13265   -506   -561   -113       C  
ATOM   1206  CG1 VAL A 227     -60.547 -26.245   5.555  1.00115.55           C  
ANISOU 1206  CG1 VAL A 227    14999  15598  13306   -409   -485    -65       C  
ATOM   1207  CG2 VAL A 227     -61.477 -27.114   3.409  1.00116.96           C  
ANISOU 1207  CG2 VAL A 227    15368  15753  13319   -634   -676    104       C  
ATOM   1208  N   MET A 228     -57.246 -27.802   4.602  1.00116.39           N  
ANISOU 1208  N   MET A 228    15250  15727  13245   -335   -405   -649       N  
ATOM   1209  CA  MET A 228     -56.059 -27.919   5.430  1.00116.28           C  
ANISOU 1209  CA  MET A 228    15151  15739  13292   -210   -353   -850       C  
ATOM   1210  C   MET A 228     -55.004 -26.918   4.987  1.00116.73           C  
ANISOU 1210  C   MET A 228    15119  15856  13378   -238   -190   -976       C  
ATOM   1211  O   MET A 228     -54.550 -26.116   5.790  1.00116.46           O  
ANISOU 1211  O   MET A 228    14964  15840  13445   -196   -132  -1032       O  
ATOM   1212  CB  MET A 228     -55.485 -29.331   5.383  1.00116.94           C  
ANISOU 1212  CB  MET A 228    15312  15786  13334   -129   -438   -991       C  
ATOM   1213  CG  MET A 228     -56.195 -30.325   6.264  1.00116.70           C  
ANISOU 1213  CG  MET A 228    15333  15682  13324    -76   -597   -890       C  
ATOM   1214  SD  MET A 228     -55.371 -31.925   6.331  1.00117.83           S  
ANISOU 1214  SD  MET A 228    15567  15738  13466     48   -707  -1064       S  
ATOM   1215  CE  MET A 228     -53.807 -31.489   7.073  1.00117.98           C  
ANISOU 1215  CE  MET A 228    15417  15846  13566    203   -611  -1285       C  
ATOM   1216  N   LEU A 229     -54.690 -26.892   3.694  1.00117.69           N  
ANISOU 1216  N   LEU A 229    15303  16008  13403   -326   -115  -1004       N  
ATOM   1217  CA  LEU A 229     -53.620 -26.030   3.229  1.00118.51           C  
ANISOU 1217  CA  LEU A 229    15313  16182  13535   -369     57  -1109       C  
ATOM   1218  C   LEU A 229     -53.999 -24.572   3.292  1.00118.28           C  
ANISOU 1218  C   LEU A 229    15221  16129  13591   -461    126   -965       C  
ATOM   1219  O   LEU A 229     -53.140 -23.730   3.525  1.00118.74           O  
ANISOU 1219  O   LEU A 229    15155  16206  13754   -479    236  -1052       O  
ATOM   1220  CB  LEU A 229     -53.197 -26.376   1.802  1.00124.00           C  
ANISOU 1220  CB  LEU A 229    16102  16942  14072   -442    146  -1164       C  
ATOM   1221  CG  LEU A 229     -51.868 -25.641   1.577  1.00125.12           C  
ANISOU 1221  CG  LEU A 229    16092  17173  14273   -465    342  -1297       C  
ATOM   1222  CD1 LEU A 229     -50.789 -26.179   2.516  1.00125.19           C  
ANISOU 1222  CD1 LEU A 229    15953  17206  14406   -312    336  -1519       C  
ATOM   1223  CD2 LEU A 229     -51.388 -25.672   0.146  1.00126.99           C  
ANISOU 1223  CD2 LEU A 229    16397  17513  14340   -555    493  -1329       C  
ATOM   1224  N   ILE A 230     -55.278 -24.260   3.139  1.00117.80           N  
ANISOU 1224  N   ILE A 230    15233  16014  13513   -516     51   -748       N  
ATOM   1225  CA  ILE A 230     -55.684 -22.883   3.358  1.00117.76           C  
ANISOU 1225  CA  ILE A 230    15163  15953  13626   -564    102   -619       C  
ATOM   1226  C   ILE A 230     -55.246 -22.506   4.759  1.00117.17           C  
ANISOU 1226  C   ILE A 230    14965  15854  13699   -457    111   -749       C  
ATOM   1227  O   ILE A 230     -54.508 -21.536   4.951  1.00117.75           O  
ANISOU 1227  O   ILE A 230    14948  15906  13884   -488    205   -829       O  
ATOM   1228  CB  ILE A 230     -57.198 -22.658   3.185  1.00117.48           C  
ANISOU 1228  CB  ILE A 230    15187  15863  13586   -596      3   -367       C  
ATOM   1229  CG1 ILE A 230     -57.568 -22.739   1.710  1.00118.52           C  
ANISOU 1229  CG1 ILE A 230    15442  16025  13567   -727    -16   -227       C  
ATOM   1230  CG2 ILE A 230     -57.580 -21.277   3.658  1.00117.59           C  
ANISOU 1230  CG2 ILE A 230    15121  15794  13763   -590     53   -270       C  
ATOM   1231  CD1 ILE A 230     -59.021 -22.546   1.420  1.00118.63           C  
ANISOU 1231  CD1 ILE A 230    15494  15998  13581   -768   -140     30       C  
ATOM   1232  N   GLY A 231     -55.641 -23.322   5.726  1.00116.31           N  
ANISOU 1232  N   GLY A 231    14861  15751  13580   -342      6   -776       N  
ATOM   1233  CA  GLY A 231     -55.242 -23.080   7.094  1.00116.01           C  
ANISOU 1233  CA  GLY A 231    14732  15715  13632   -233     -4   -904       C  
ATOM   1234  C   GLY A 231     -53.737 -23.009   7.284  1.00116.67           C  
ANISOU 1234  C   GLY A 231    14717  15845  13766   -216     49  -1134       C  
ATOM   1235  O   GLY A 231     -53.237 -22.157   8.024  1.00117.04           O  
ANISOU 1235  O   GLY A 231    14671  15875  13922   -200     78  -1237       O  
ATOM   1236  N   ILE A 232     -53.006 -23.905   6.629  1.00117.09           N  
ANISOU 1236  N   ILE A 232    14783  15955  13752   -214     58  -1226       N  
ATOM   1237  CA  ILE A 232     -51.554 -23.949   6.784  1.00118.02           C  
ANISOU 1237  CA  ILE A 232    14770  16138  13935   -183    109  -1442       C  
ATOM   1238  C   ILE A 232     -50.889 -22.674   6.273  1.00119.07           C  
ANISOU 1238  C   ILE A 232    14801  16270  14170   -315    254  -1467       C  
ATOM   1239  O   ILE A 232     -50.315 -21.916   7.054  1.00119.52           O  
ANISOU 1239  O   ILE A 232    14739  16314  14359   -315    256  -1570       O  
ATOM   1240  CB  ILE A 232     -50.942 -25.176   6.050  1.00118.68           C  
ANISOU 1240  CB  ILE A 232    14883  16278  13930   -136    115  -1539       C  
ATOM   1241  CG1 ILE A 232     -51.468 -26.477   6.662  1.00118.00           C  
ANISOU 1241  CG1 ILE A 232    14897  16157  13782     -7    -48  -1523       C  
ATOM   1242  CG2 ILE A 232     -49.410 -25.124   6.081  1.00120.05           C  
ANISOU 1242  CG2 ILE A 232    14878  16538  14197   -103    196  -1753       C  
ATOM   1243  CD1 ILE A 232     -51.129 -27.713   5.868  1.00118.81           C  
ANISOU 1243  CD1 ILE A 232    15079  16263  13802     43    -64  -1605       C  
ATOM   1244  N   SER A 233     -51.037 -22.398   4.980  1.00119.68           N  
ANISOU 1244  N   SER A 233    14938  16354  14180   -442    362  -1356       N  
ATOM   1245  CA  SER A 233     -50.372 -21.251   4.382  1.00121.05           C  
ANISOU 1245  CA  SER A 233    15023  16528  14444   -590    511  -1345       C  
ATOM   1246  C   SER A 233     -50.874 -19.953   5.010  1.00120.90           C  
ANISOU 1246  C   SER A 233    14987  16378  14574   -639    491  -1263       C  
ATOM   1247  O   SER A 233     -50.176 -18.945   4.975  1.00122.17           O  
ANISOU 1247  O   SER A 233    15043  16499  14876   -745    576  -1300       O  
ATOM   1248  CB  SER A 233     -50.556 -21.224   2.862  1.00121.99           C  
ANISOU 1248  CB  SER A 233    15242  16689  14417   -717    625  -1206       C  
ATOM   1249  OG  SER A 233     -51.911 -21.058   2.503  1.00121.22           O  
ANISOU 1249  OG  SER A 233    15303  16516  14240   -751    550   -984       O  
ATOM   1250  N   LEU A 234     -52.067 -19.958   5.598  1.00120.17           N  
ANISOU 1250  N   LEU A 234    14988  16209  14464   -561    385  -1156       N  
ATOM   1251  CA  LEU A 234     -52.505 -18.740   6.271  1.00120.37           C  
ANISOU 1251  CA  LEU A 234    14994  16102  14638   -571    376  -1118       C  
ATOM   1252  C   LEU A 234     -51.929 -18.593   7.676  1.00120.43           C  
ANISOU 1252  C   LEU A 234    14907  16109  14743   -474    311  -1334       C  
ATOM   1253  O   LEU A 234     -51.705 -17.469   8.126  1.00121.39           O  
ANISOU 1253  O   LEU A 234    14980  16124  15017   -519    329  -1393       O  
ATOM   1254  CB  LEU A 234     -54.034 -18.674   6.374  1.00118.98           C  
ANISOU 1254  CB  LEU A 234    14926  15856  14423   -513    310   -921       C  
ATOM   1255  CG  LEU A 234     -54.863 -18.398   5.126  1.00119.31           C  
ANISOU 1255  CG  LEU A 234    15063  15858  14410   -614    335   -669       C  
ATOM   1256  CD1 LEU A 234     -56.288 -18.178   5.550  1.00118.76           C  
ANISOU 1256  CD1 LEU A 234    15036  15716  14370   -530    260   -507       C  
ATOM   1257  CD2 LEU A 234     -54.323 -17.198   4.400  1.00120.90           C  
ANISOU 1257  CD2 LEU A 234    15240  15974  14721   -764    444   -610       C  
ATOM   1258  N   ILE A 235     -51.622 -19.708   8.342  1.00121.57           N  
ANISOU 1258  N   ILE A 235    15032  16360  14800   -350    224  -1455       N  
ATOM   1259  CA  ILE A 235     -51.240 -19.647   9.757  1.00121.75           C  
ANISOU 1259  CA  ILE A 235    14994  16400  14866   -243    130  -1634       C  
ATOM   1260  C   ILE A 235     -49.968 -18.828   9.992  1.00123.35           C  
ANISOU 1260  C   ILE A 235    15047  16590  15229   -326    153  -1822       C  
ATOM   1261  O   ILE A 235     -49.751 -18.277  11.090  1.00124.01           O  
ANISOU 1261  O   ILE A 235    15096  16642  15381   -284     76  -1966       O  
ATOM   1262  CB  ILE A 235     -51.062 -21.066  10.357  1.00118.76           C  
ANISOU 1262  CB  ILE A 235    14624  16137  14361    -99     18  -1700       C  
ATOM   1263  CG1 ILE A 235     -51.229 -21.019  11.876  1.00118.82           C  
ANISOU 1263  CG1 ILE A 235    14639  16166  14343     28    -94  -1795       C  
ATOM   1264  CG2 ILE A 235     -49.690 -21.605  10.075  1.00119.65           C  
ANISOU 1264  CG2 ILE A 235    14609  16341  14511   -103     21  -1857       C  
ATOM   1265  CD1 ILE A 235     -51.288 -22.382  12.526  1.00118.32           C  
ANISOU 1265  CD1 ILE A 235    14616  16195  14144    168   -214  -1793       C  
ATOM   1266  N   GLY A 236     -49.168 -18.701   8.937  1.00128.08           N  
ANISOU 1266  N   GLY A 236    15561  17217  15886   -458    262  -1815       N  
ATOM   1267  CA  GLY A 236     -47.898 -18.009   9.010  1.00129.91           C  
ANISOU 1267  CA  GLY A 236    15615  17455  16290   -569    297  -1970       C  
ATOM   1268  C   GLY A 236     -48.031 -16.590   9.519  1.00130.96           C  
ANISOU 1268  C   GLY A 236    15748  17419  16590   -658    285  -2000       C  
ATOM   1269  O   GLY A 236     -47.175 -16.122  10.263  1.00132.35           O  
ANISOU 1269  O   GLY A 236    15801  17586  16899   -690    216  -2190       O  
ATOM   1270  N   THR A 237     -49.111 -15.915   9.141  1.00130.17           N  
ANISOU 1270  N   THR A 237    15788  17176  16495   -690    333  -1820       N  
ATOM   1271  CA  THR A 237     -49.332 -14.536   9.561  1.00131.43           C  
ANISOU 1271  CA  THR A 237    15972  17133  16834   -756    325  -1844       C  
ATOM   1272  C   THR A 237     -49.694 -14.485  11.038  1.00131.23           C  
ANISOU 1272  C   THR A 237    15993  17087  16782   -593    193  -2017       C  
ATOM   1273  O   THR A 237     -49.385 -13.514  11.747  1.00132.83           O  
ANISOU 1273  O   THR A 237    16176  17160  17132   -629    142  -2176       O  
ATOM   1274  CB  THR A 237     -50.444 -13.875   8.735  1.00132.83           C  
ANISOU 1274  CB  THR A 237    16282  17158  17031   -803    404  -1587       C  
ATOM   1275  OG1 THR A 237     -51.647 -14.644   8.865  1.00130.97           O  
ANISOU 1275  OG1 THR A 237    16162  16982  16620   -643    365  -1469       O  
ATOM   1276  CG2 THR A 237     -50.051 -13.827   7.263  1.00133.51           C  
ANISOU 1276  CG2 THR A 237    16343  17274  17112   -981    536  -1408       C  
ATOM   1277  N   GLY A 238     -50.341 -15.552  11.494  1.00130.40           N  
ANISOU 1277  N   GLY A 238    15958  17110  16479   -422    136  -1987       N  
ATOM   1278  CA  GLY A 238     -50.691 -15.691  12.891  1.00130.34           C  
ANISOU 1278  CA  GLY A 238    16001  17136  16384   -257     26  -2128       C  
ATOM   1279  C   GLY A 238     -49.436 -15.804  13.725  1.00131.57           C  
ANISOU 1279  C   GLY A 238    16041  17380  16571   -259    -91  -2385       C  
ATOM   1280  O   GLY A 238     -49.254 -15.066  14.705  1.00133.01           O  
ANISOU 1280  O   GLY A 238    16234  17497  16805   -239   -172  -2573       O  
ATOM   1281  N   PHE A 239     -48.554 -16.721  13.337  1.00128.67           N  
ANISOU 1281  N   PHE A 239    15559  17157  16174   -277   -111  -2405       N  
ATOM   1282  CA  PHE A 239     -47.291 -16.851  14.058  1.00130.14           C  
ANISOU 1282  CA  PHE A 239    15595  17438  16416   -280   -238  -2634       C  
ATOM   1283  C   PHE A 239     -46.441 -15.582  13.981  1.00132.38           C  
ANISOU 1283  C   PHE A 239    15757  17600  16940   -468   -231  -2769       C  
ATOM   1284  O   PHE A 239     -45.837 -15.174  14.969  1.00134.01           O  
ANISOU 1284  O   PHE A 239    15908  17808  17204   -468   -374  -2986       O  
ATOM   1285  CB  PHE A 239     -46.471 -18.020  13.523  1.00125.86           C  
ANISOU 1285  CB  PHE A 239    14924  17058  15840   -254   -240  -2625       C  
ATOM   1286  CG  PHE A 239     -46.874 -19.351  14.075  1.00124.58           C  
ANISOU 1286  CG  PHE A 239    14846  17016  15473    -57   -340  -2586       C  
ATOM   1287  CD1 PHE A 239     -47.273 -20.373  13.230  1.00123.17           C  
ANISOU 1287  CD1 PHE A 239    14724  16879  15198    -12   -269  -2427       C  
ATOM   1288  CD2 PHE A 239     -46.794 -19.601  15.437  1.00125.14           C  
ANISOU 1288  CD2 PHE A 239    14945  17158  15446     73   -515  -2710       C  
ATOM   1289  CE1 PHE A 239     -47.617 -21.603  13.732  1.00122.32           C  
ANISOU 1289  CE1 PHE A 239    14695  16848  14931    152   -373  -2381       C  
ATOM   1290  CE2 PHE A 239     -47.144 -20.834  15.950  1.00124.28           C  
ANISOU 1290  CE2 PHE A 239    14917  17150  15153    241   -610  -2642       C  
ATOM   1291  CZ  PHE A 239     -47.554 -21.837  15.092  1.00122.86           C  
ANISOU 1291  CZ  PHE A 239    14788  16980  14913    277   -539  -2473       C  
ATOM   1292  N   LYS A 240     -46.439 -14.942  12.815  1.00134.53           N  
ANISOU 1292  N   LYS A 240    16003  17761  17350   -637    -74  -2629       N  
ATOM   1293  CA  LYS A 240     -45.642 -13.740  12.580  1.00136.89           C  
ANISOU 1293  CA  LYS A 240    16184  17923  17906   -853    -47  -2708       C  
ATOM   1294  C   LYS A 240     -46.081 -12.628  13.513  1.00138.11           C  
ANISOU 1294  C   LYS A 240    16451  17876  18147   -849   -139  -2840       C  
ATOM   1295  O   LYS A 240     -45.256 -11.917  14.082  1.00140.39           O  
ANISOU 1295  O   LYS A 240    16643  18096  18602   -957   -243  -3043       O  
ATOM   1296  CB  LYS A 240     -45.774 -13.287  11.125  1.00138.91           C  
ANISOU 1296  CB  LYS A 240    16437  18092  18250  -1026    151  -2473       C  
ATOM   1297  CG  LYS A 240     -44.940 -14.088  10.133  1.00138.97           C  
ANISOU 1297  CG  LYS A 240    16285  18291  18227  -1091    266  -2408       C  
ATOM   1298  CD  LYS A 240     -45.378 -13.782   8.709  1.00138.88           C  
ANISOU 1298  CD  LYS A 240    16345  18221  18201  -1222    463  -2143       C  
ATOM   1299  CE  LYS A 240     -44.658 -14.644   7.683  1.00139.09           C  
ANISOU 1299  CE  LYS A 240    16247  18458  18143  -1260    603  -2089       C  
ATOM   1300  NZ  LYS A 240     -45.181 -14.424   6.301  1.00139.10           N  
ANISOU 1300  NZ  LYS A 240    16359  18431  18062  -1374    783  -1825       N  
ATOM   1301  N   ASP A 241     -47.392 -12.471  13.652  1.00136.04           N  
ANISOU 1301  N   ASP A 241    16390  17519  17781   -723   -101  -2731       N  
ATOM   1302  CA  ASP A 241     -47.933 -11.475  14.563  1.00137.33           C  
ANISOU 1302  CA  ASP A 241    16681  17495  18005   -670   -167  -2871       C  
ATOM   1303  C   ASP A 241     -47.605 -11.842  16.009  1.00137.98           C  
ANISOU 1303  C   ASP A 241    16772  17708  17947   -533   -348  -3140       C  
ATOM   1304  O   ASP A 241     -47.263 -10.973  16.807  1.00140.24           O  
ANISOU 1304  O   ASP A 241    17079  17873  18334   -571   -456  -3374       O  
ATOM   1305  CB  ASP A 241     -49.434 -11.312  14.340  1.00138.09           C  
ANISOU 1305  CB  ASP A 241    16955  17490  18024   -542    -67  -2678       C  
ATOM   1306  CG  ASP A 241     -49.731 -10.499  13.098  1.00138.54           C  
ANISOU 1306  CG  ASP A 241    17029  17343  18268   -695     64  -2452       C  
ATOM   1307  OD1 ASP A 241     -48.777  -9.925  12.533  1.00140.15           O  
ANISOU 1307  OD1 ASP A 241    17124  17461  18667   -911     86  -2463       O  
ATOM   1308  OD2 ASP A 241     -50.898 -10.424  12.677  1.00137.57           O  
ANISOU 1308  OD2 ASP A 241    17016  17150  18102   -609    142  -2247       O  
ATOM   1309  N   TRP A 242     -47.731 -13.121  16.350  1.00136.73           N  
ANISOU 1309  N   TRP A 242    16614  17786  17550   -376   -391  -3102       N  
ATOM   1310  CA  TRP A 242     -47.332 -13.597  17.676  1.00137.53           C  
ANISOU 1310  CA  TRP A 242    16720  18045  17489   -249   -576  -3320       C  
ATOM   1311  C   TRP A 242     -45.896 -13.173  18.010  1.00140.00           C  
ANISOU 1311  C   TRP A 242    16857  18365  17970   -396   -730  -3558       C  
ATOM   1312  O   TRP A 242     -45.610 -12.718  19.123  1.00142.00           O  
ANISOU 1312  O   TRP A 242    17151  18609  18192   -368   -895  -3805       O  
ATOM   1313  CB  TRP A 242     -47.471 -15.115  17.742  1.00133.38           C  
ANISOU 1313  CB  TRP A 242    16189  17754  16734   -100   -602  -3195       C  
ATOM   1314  CG  TRP A 242     -47.311 -15.723  19.104  1.00134.09           C  
ANISOU 1314  CG  TRP A 242    16327  18016  16606     59   -784  -3345       C  
ATOM   1315  CD1 TRP A 242     -46.774 -15.145  20.223  1.00136.48           C  
ANISOU 1315  CD1 TRP A 242    16640  18328  16888     65   -954  -3614       C  
ATOM   1316  CD2 TRP A 242     -47.720 -17.035  19.491  1.00132.70           C  
ANISOU 1316  CD2 TRP A 242    16212  18023  16185    230   -825  -3222       C  
ATOM   1317  NE1 TRP A 242     -46.813 -16.024  21.276  1.00136.66           N  
ANISOU 1317  NE1 TRP A 242    16730  18552  16643    235  -1097  -3654       N  
ATOM   1318  CE2 TRP A 242     -47.394 -17.193  20.852  1.00134.36           C  
ANISOU 1318  CE2 TRP A 242    16468  18361  16220    337  -1015  -3403       C  
ATOM   1319  CE3 TRP A 242     -48.328 -18.099  18.813  1.00130.47           C  
ANISOU 1319  CE3 TRP A 242    15960  17799  15814    292   -732  -2972       C  
ATOM   1320  CZ2 TRP A 242     -47.650 -18.373  21.547  1.00133.86           C  
ANISOU 1320  CZ2 TRP A 242    16477  18481  15901    502  -1104  -3314       C  
ATOM   1321  CZ3 TRP A 242     -48.586 -19.266  19.506  1.00129.97           C  
ANISOU 1321  CZ3 TRP A 242    15965  17894  15524    449   -825  -2899       C  
ATOM   1322  CH2 TRP A 242     -48.250 -19.393  20.859  1.00131.65           C  
ANISOU 1322  CH2 TRP A 242    16221  18232  15570    553  -1003  -3054       C  
ATOM   1323  N   ALA A 243     -45.006 -13.317  17.029  1.00140.20           N  
ANISOU 1323  N   ALA A 243    16682  18417  18171   -556   -672  -3483       N  
ATOM   1324  CA  ALA A 243     -43.609 -12.899  17.158  1.00142.77           C  
ANISOU 1324  CA  ALA A 243    16783  18755  18708   -729   -792  -3670       C  
ATOM   1325  C   ALA A 243     -43.492 -11.397  17.386  1.00145.30           C  
ANISOU 1325  C   ALA A 243    17138  18813  19254   -903   -828  -3819       C  
ATOM   1326  O   ALA A 243     -42.676 -10.947  18.180  1.00147.85           O  
ANISOU 1326  O   ALA A 243    17377  19129  19672   -980  -1022  -4069       O  
ATOM   1327  CB  ALA A 243     -42.819 -13.303  15.921  1.00145.15           C  
ANISOU 1327  CB  ALA A 243    16860  19138  19153   -864   -658  -3525       C  
ATOM   1328  N   GLY A 244     -44.297 -10.633  16.657  1.00143.76           N  
ANISOU 1328  N   GLY A 244    17069  18394  19159   -968   -657  -3660       N  
ATOM   1329  CA  GLY A 244     -44.348  -9.192  16.795  1.00146.21           C  
ANISOU 1329  CA  GLY A 244    17450  18400  19702  -1115   -678  -3772       C  
ATOM   1330  C   GLY A 244     -44.337  -8.544  15.428  1.00146.46           C  
ANISOU 1330  C   GLY A 244    17430  18250  19969  -1327   -487  -3529       C  
ATOM   1331  O   GLY A 244     -44.212  -7.326  15.316  1.00148.85           O  
ANISOU 1331  O   GLY A 244    17759  18269  20528  -1500   -493  -3574       O  
ATOM   1332  N   GLY A 245     -44.511  -9.359  14.389  1.00147.99           N  
ANISOU 1332  N   GLY A 245    17570  18595  20064  -1310   -322  -3266       N  
ATOM   1333  CA  GLY A 245     -44.397  -8.889  13.021  1.00148.41           C  
ANISOU 1333  CA  GLY A 245    17564  18540  20286  -1516   -135  -3015       C  
ATOM   1334  C   GLY A 245     -45.736  -8.522  12.416  1.00147.09           C  
ANISOU 1334  C   GLY A 245    17616  18200  20072  -1444     -6  -2774       C  
ATOM   1335  O   GLY A 245     -46.664  -8.201  13.151  1.00146.78           O  
ANISOU 1335  O   GLY A 245    17758  18037  19975  -1279    -66  -2848       O  
ATOM   1336  N   SER A 246     -45.838  -8.520  11.087  1.00154.48           N  
ANISOU 1336  N   SER A 246    18532  19131  21034  -1566    168  -2488       N  
ATOM   1337  CA  SER A 246     -44.724  -8.834  10.196  1.00155.35           C  
ANISOU 1337  CA  SER A 246    18424  19398  21203  -1762    273  -2408       C  
ATOM   1338  C   SER A 246     -43.731  -7.661  10.064  1.00158.90           C  
ANISOU 1338  C   SER A 246    18730  19658  21986  -2058    268  -2460       C  
ATOM   1339  O   SER A 246     -42.689  -7.771   9.413  1.00160.33           O  
ANISOU 1339  O   SER A 246    18690  19967  22262  -2249    363  -2410       O  
ATOM   1340  CB  SER A 246     -45.251  -9.242   8.817  1.00154.26           C  
ANISOU 1340  CB  SER A 246    18348  19336  20927  -1783    466  -2084       C  
ATOM   1341  OG  SER A 246     -45.967  -8.185   8.218  1.00155.24           O  
ANISOU 1341  OG  SER A 246    18620  19189  21176  -1883    533  -1870       O  
ATOM   1342  N   ALA A 247     -44.073  -6.527  10.659  1.00160.88           N  
ANISOU 1342  N   ALA A 247    19105  19596  22427  -2098    167  -2556       N  
ATOM   1343  CA  ALA A 247     -43.131  -5.424  10.758  1.00164.55           C  
ANISOU 1343  CA  ALA A 247    19445  19848  23229  -2379    111  -2655       C  
ATOM   1344  C   ALA A 247     -43.042  -5.002  12.214  1.00165.83           C  
ANISOU 1344  C   ALA A 247    19663  19885  23462  -2299   -129  -3018       C  
ATOM   1345  O   ALA A 247     -44.024  -4.545  12.799  1.00165.54           O  
ANISOU 1345  O   ALA A 247    19860  19646  23391  -2134   -191  -3091       O  
ATOM   1346  CB  ALA A 247     -43.556  -4.264   9.877  1.00166.56           C  
ANISOU 1346  CB  ALA A 247    19816  19771  23698  -2564    224  -2394       C  
ATOM   1347  N   CYS A 248     -41.867  -5.170  12.800  1.00171.48           N  
ANISOU 1347  N   CYS A 248    20156  20734  24265  -2405   -266  -3251       N  
ATOM   1348  CA  CYS A 248     -41.669  -4.842  14.202  1.00173.04           C  
ANISOU 1348  CA  CYS A 248    20402  20854  24492  -2340   -523  -3617       C  
ATOM   1349  C   CYS A 248     -41.819  -3.336  14.449  1.00176.31           C  
ANISOU 1349  C   CYS A 248    20954  20827  25208  -2504   -602  -3716       C  
ATOM   1350  O   CYS A 248     -41.557  -2.520  13.561  1.00178.28           O  
ANISOU 1350  O   CYS A 248    21152  20853  25733  -2765   -494  -3521       O  
ATOM   1351  CB  CYS A 248     -40.306  -5.346  14.661  1.00177.36           C  
ANISOU 1351  CB  CYS A 248    20649  21650  25090  -2442   -671  -3815       C  
ATOM   1352  SG  CYS A 248     -40.137  -7.145  14.595  1.00173.97           S  
ANISOU 1352  SG  CYS A 248    20083  21699  24318  -2194   -626  -3756       S  
ATOM   1353  N   MET A 249     -42.221  -2.991  15.672  1.00180.01           N  
ANISOU 1353  N   MET A 249    21605  21173  25617  -2347   -790  -4024       N  
ATOM   1354  CA  MET A 249     -42.664  -1.642  16.062  1.00182.88           C  
ANISOU 1354  CA  MET A 249    22182  21092  26211  -2400   -869  -4165       C  
ATOM   1355  C   MET A 249     -41.725  -0.491  15.663  1.00187.06           C  
ANISOU 1355  C   MET A 249    22585  21309  27180  -2792   -926  -4171       C  
ATOM   1356  O   MET A 249     -40.514  -0.658  15.635  1.00188.66           O  
ANISOU 1356  O   MET A 249    22511  21661  27509  -3020  -1006  -4235       O  
ATOM   1357  CB  MET A 249     -42.874  -1.625  17.577  1.00185.27           C  
ANISOU 1357  CB  MET A 249    22643  21409  26343  -2193  -1093  -4576       C  
ATOM   1358  CG  MET A 249     -43.499  -2.924  18.096  1.00181.62           C  
ANISOU 1358  CG  MET A 249    22239  21329  25438  -1854  -1066  -4579       C  
ATOM   1359  SD  MET A 249     -44.386  -2.757  19.655  1.00182.36           S  
ANISOU 1359  SD  MET A 249    22635  21388  25266  -1534  -1207  -4942       S  
ATOM   1360  CE  MET A 249     -45.874  -1.933  19.098  1.00181.93           C  
ANISOU 1360  CE  MET A 249    22832  20979  25314  -1390   -991  -4747       C  
ATOM   1361  N   ASP A 250     -42.298   0.671  15.344  1.00188.90           N  
ANISOU 1361  N   ASP A 250    23008  21102  27663  -2867   -883  -4089       N  
ATOM   1362  CA  ASP A 250     -41.520   1.827  14.873  1.00193.12           C  
ANISOU 1362  CA  ASP A 250    23452  21282  28643  -3257   -922  -4039       C  
ATOM   1363  C   ASP A 250     -41.069   2.771  15.995  1.00197.34           C  
ANISOU 1363  C   ASP A 250    24065  21508  29408  -3366  -1206  -4467       C  
ATOM   1364  O   ASP A 250     -41.222   2.478  17.182  1.00197.12           O  
ANISOU 1364  O   ASP A 250    24141  21592  29164  -3149  -1383  -4829       O  
ATOM   1365  CB  ASP A 250     -42.319   2.627  13.829  1.00193.69           C  
ANISOU 1365  CB  ASP A 250    23691  21001  28902  -3310   -738  -3680       C  
ATOM   1366  CG  ASP A 250     -41.426   3.305  12.793  1.00196.74           C  
ANISOU 1366  CG  ASP A 250    23889  21215  29648  -3741   -656  -3407       C  
ATOM   1367  OD1 ASP A 250     -40.313   3.739  13.159  1.00200.13           O  
ANISOU 1367  OD1 ASP A 250    24137  21568  30335  -4031   -809  -3600       O  
ATOM   1368  OD2 ASP A 250     -41.842   3.427  11.620  1.00196.06           O  
ANISOU 1368  OD2 ASP A 250    23837  21070  29588  -3803   -444  -2992       O  
ATOM   1369  N   ASP A 251     -40.522   3.914  15.587  1.00195.29           N  
ANISOU 1369  N   ASP A 251    23766  20851  29583  -3717  -1250  -4414       N  
ATOM   1370  CA  ASP A 251     -39.897   4.869  16.490  1.00200.03           C  
ANISOU 1370  CA  ASP A 251    24402  21127  30471  -3912  -1535  -4802       C  
ATOM   1371  C   ASP A 251     -40.938   5.748  17.167  1.00201.58           C  
ANISOU 1371  C   ASP A 251    24989  20889  30712  -3690  -1620  -5036       C  
ATOM   1372  O   ASP A 251     -41.909   6.184  16.540  1.00200.91           O  
ANISOU 1372  O   ASP A 251    25099  20544  30693  -3572  -1448  -4784       O  
ATOM   1373  CB  ASP A 251     -38.889   5.758  15.751  1.00201.82           C  
ANISOU 1373  CB  ASP A 251    24424  21076  31182  -4405  -1546  -4631       C  
ATOM   1374  CG  ASP A 251     -37.751   4.971  15.141  1.00201.15           C  
ANISOU 1374  CG  ASP A 251    23916  21422  31088  -4637  -1457  -4439       C  
ATOM   1375  OD1 ASP A 251     -37.385   3.916  15.704  1.00198.93           O  
ANISOU 1375  OD1 ASP A 251    23479  21591  30516  -4475  -1532  -4614       O  
ATOM   1376  OD2 ASP A 251     -37.206   5.419  14.109  1.00203.17           O  
ANISOU 1376  OD2 ASP A 251    23994  21565  31635  -4980  -1312  -4112       O  
ATOM   1377  N   GLY A 252     -40.758   5.952  18.469  1.00199.88           N  
ANISOU 1377  N   GLY A 252    24887  20625  30434  -3607  -1885  -5527       N  
ATOM   1378  CA  GLY A 252     -41.600   6.848  19.240  1.00202.29           C  
ANISOU 1378  CA  GLY A 252    25557  20511  30794  -3406  -1986  -5835       C  
ATOM   1379  C   GLY A 252     -42.905   6.171  19.582  1.00198.38           C  
ANISOU 1379  C   GLY A 252    25272  20235  29871  -2918  -1831  -5832       C  
ATOM   1380  O   GLY A 252     -43.687   6.671  20.391  1.00199.91           O  
ANISOU 1380  O   GLY A 252    25755  20203  29997  -2660  -1889  -6131       O  
ATOM   1381  N   MET A 253     -43.129   5.018  18.965  1.00197.46           N  
ANISOU 1381  N   MET A 253    24998  20562  29466  -2795  -1629  -5500       N  
ATOM   1382  CA  MET A 253     -44.327   4.249  19.218  1.00193.62           C  
ANISOU 1382  CA  MET A 253    24663  20328  28576  -2367  -1476  -5448       C  
ATOM   1383  C   MET A 253     -44.153   3.508  20.529  1.00193.07           C  
ANISOU 1383  C   MET A 253    24620  20616  28124  -2168  -1643  -5833       C  
ATOM   1384  O   MET A 253     -43.049   3.088  20.872  1.00193.75           O  
ANISOU 1384  O   MET A 253    24503  20937  28176  -2351  -1817  -5974       O  
ATOM   1385  CB  MET A 253     -44.596   3.295  18.066  1.00196.14           C  
ANISOU 1385  CB  MET A 253    24815  20965  28742  -2337  -1227  -4963       C  
ATOM   1386  CG  MET A 253     -44.625   3.997  16.723  1.00197.05           C  
ANISOU 1386  CG  MET A 253    24892  20772  29207  -2575  -1077  -4558       C  
ATOM   1387  SD  MET A 253     -45.273   2.935  15.433  1.00192.01           S  
ANISOU 1387  SD  MET A 253    24154  20481  28319  -2460   -784  -4022       S  
ATOM   1388  CE  MET A 253     -46.986   2.808  15.955  1.00189.96           C  
ANISOU 1388  CE  MET A 253    24179  20190  27809  -1976   -703  -4064       C  
ATOM   1389  N   LEU A 254     -45.246   3.344  21.261  1.00194.30           N  
ANISOU 1389  N   LEU A 254    25015  20823  27989  -1789  -1587  -5988       N  
ATOM   1390  CA  LEU A 254     -45.171   2.884  22.641  1.00194.92           C  
ANISOU 1390  CA  LEU A 254    25190  21167  27705  -1593  -1758  -6395       C  
ATOM   1391  C   LEU A 254     -44.699   1.431  22.759  1.00191.39           C  
ANISOU 1391  C   LEU A 254    24530  21289  26901  -1550  -1771  -6282       C  
ATOM   1392  O   LEU A 254     -45.108   0.567  21.980  1.00187.33           O  
ANISOU 1392  O   LEU A 254    23904  21016  26255  -1462  -1564  -5906       O  
ATOM   1393  CB  LEU A 254     -46.533   3.074  23.318  1.00189.65           C  
ANISOU 1393  CB  LEU A 254    24821  20427  26809  -1190  -1642  -6548       C  
ATOM   1394  CG  LEU A 254     -47.068   4.508  23.184  1.00193.36           C  
ANISOU 1394  CG  LEU A 254    25509  20304  27654  -1186  -1620  -6660       C  
ATOM   1395  CD1 LEU A 254     -48.474   4.669  23.749  1.00193.45           C  
ANISOU 1395  CD1 LEU A 254    25777  20262  27462   -756  -1461  -6778       C  
ATOM   1396  CD2 LEU A 254     -46.108   5.496  23.842  1.00198.63           C  
ANISOU 1396  CD2 LEU A 254    26249  20643  28577  -1438  -1916  -7092       C  
ATOM   1397  N   CYS A 255     -43.826   1.194  23.739  1.00191.45           N  
ANISOU 1397  N   CYS A 255    24488  21487  26766  -1613  -2037  -6617       N  
ATOM   1398  CA  CYS A 255     -43.287  -0.133  24.062  1.00188.98           C  
ANISOU 1398  CA  CYS A 255    23991  21691  26123  -1556  -2112  -6572       C  
ATOM   1399  C   CYS A 255     -42.636  -0.866  22.887  1.00186.17           C  
ANISOU 1399  C   CYS A 255    23305  21533  25899  -1745  -1998  -6177       C  
ATOM   1400  O   CYS A 255     -42.991  -2.011  22.604  1.00182.29           O  
ANISOU 1400  O   CYS A 255    22745  21380  25138  -1569  -1856  -5932       O  
ATOM   1401  CB  CYS A 255     -44.374  -1.016  24.682  1.00186.96           C  
ANISOU 1401  CB  CYS A 255    23912  21740  25385  -1157  -1988  -6550       C  
ATOM   1402  SG  CYS A 255     -44.971  -0.431  26.281  1.00190.58           S  
ANISOU 1402  SG  CYS A 255    24732  22123  25559   -900  -2129  -7061       S  
ATOM   1403  N   PRO A 256     -41.694  -0.209  22.192  1.00186.36           N  
ANISOU 1403  N   PRO A 256    23128  21343  26338  -2106  -2051  -6116       N  
ATOM   1404  CA  PRO A 256     -40.963  -0.981  21.188  1.00184.18           C  
ANISOU 1404  CA  PRO A 256    22520  21318  26142  -2272  -1943  -5788       C  
ATOM   1405  C   PRO A 256     -40.004  -1.960  21.852  1.00184.13           C  
ANISOU 1405  C   PRO A 256    22297  21726  25939  -2261  -2153  -5936       C  
ATOM   1406  O   PRO A 256     -39.165  -1.532  22.645  1.00187.77           O  
ANISOU 1406  O   PRO A 256    22698  22147  26500  -2411  -2442  -6258       O  
ATOM   1407  CB  PRO A 256     -40.201   0.082  20.400  1.00186.44           C  
ANISOU 1407  CB  PRO A 256    22654  21261  26923  -2670  -1948  -5709       C  
ATOM   1408  CG  PRO A 256     -40.151   1.299  21.290  1.00190.99           C  
ANISOU 1408  CG  PRO A 256    23433  21448  27684  -2757  -2182  -6102       C  
ATOM   1409  CD  PRO A 256     -41.044   1.083  22.483  1.00190.45           C  
ANISOU 1409  CD  PRO A 256    23674  21462  27227  -2388  -2259  -6394       C  
ATOM   1410  N   SER A 257     -40.106  -3.241  21.517  1.00180.45           N  
ANISOU 1410  N   SER A 257    21711  21634  25217  -2092  -2027  -5703       N  
ATOM   1411  CA  SER A 257     -39.172  -4.245  22.021  1.00180.40           C  
ANISOU 1411  CA  SER A 257    21474  22015  25056  -2068  -2216  -5790       C  
ATOM   1412  C   SER A 257     -38.405  -4.838  20.838  1.00179.06           C  
ANISOU 1412  C   SER A 257    20953  22015  25067  -2230  -2060  -5487       C  
ATOM   1413  O   SER A 257     -37.398  -5.538  20.998  1.00179.69           O  
ANISOU 1413  O   SER A 257    20751  22374  25148  -2274  -2198  -5527       O  
ATOM   1414  CB  SER A 257     -39.909  -5.322  22.824  1.00173.87           C  
ANISOU 1414  CB  SER A 257    20825  21489  23750  -1700  -2235  -5816       C  
ATOM   1415  OG  SER A 257     -40.862  -5.996  22.027  1.00169.74           O  
ANISOU 1415  OG  SER A 257    20374  21043  23079  -1522  -1939  -5480       O  
ATOM   1416  N   ALA A 258     -38.918  -4.558  19.645  1.00185.18           N  
ANISOU 1416  N   ALA A 258    21752  22626  25982  -2302  -1769  -5181       N  
ATOM   1417  CA  ALA A 258     -38.219  -4.832  18.397  1.00184.73           C  
ANISOU 1417  CA  ALA A 258    21393  22666  26129  -2503  -1582  -4898       C  
ATOM   1418  C   ALA A 258     -38.557  -3.706  17.419  1.00185.80           C  
ANISOU 1418  C   ALA A 258    21604  22432  26560  -2728  -1388  -4699       C  
ATOM   1419  O   ALA A 258     -39.716  -3.543  17.029  1.00183.70           O  
ANISOU 1419  O   ALA A 258    21594  22016  26189  -2583  -1214  -4530       O  
ATOM   1420  CB  ALA A 258     -38.607  -6.189  17.836  1.00178.69           C  
ANISOU 1420  CB  ALA A 258    20593  22224  25079  -2270  -1391  -4649       C  
ATOM   1421  N   THR A 259     -37.561  -2.890  17.082  1.00183.46           N  
ANISOU 1421  N   THR A 259    21087  21976  26643  -3084  -1438  -4718       N  
ATOM   1422  CA  THR A 259     -37.737  -1.832  16.094  1.00185.01           C  
ANISOU 1422  CA  THR A 259    21327  21822  27146  -3337  -1260  -4488       C  
ATOM   1423  C   THR A 259     -36.815  -2.040  14.900  1.00185.73           C  
ANISOU 1423  C   THR A 259    21071  22071  27427  -3602  -1062  -4204       C  
ATOM   1424  O   THR A 259     -35.591  -1.984  15.045  1.00188.63           O  
ANISOU 1424  O   THR A 259    21112  22547  28011  -3834  -1180  -4314       O  
ATOM   1425  CB  THR A 259     -37.460  -0.440  16.703  1.00186.06           C  
ANISOU 1425  CB  THR A 259    21549  21531  27615  -3574  -1478  -4740       C  
ATOM   1426  OG1 THR A 259     -38.402  -0.169  17.747  1.00185.71           O  
ANISOU 1426  OG1 THR A 259    21858  21321  27382  -3309  -1622  -5009       O  
ATOM   1427  CG2 THR A 259     -37.554   0.646  15.638  1.00188.09           C  
ANISOU 1427  CG2 THR A 259    21835  21407  28223  -3861  -1302  -4463       C  
ATOM   1428  N   ALA A 260     -37.395  -2.247  13.720  1.00182.49           N  
ANISOU 1428  N   ALA A 260    20721  21680  26936  -3575   -761  -3841       N  
ATOM   1429  CA  ALA A 260     -36.594  -2.510  12.527  1.00183.20           C  
ANISOU 1429  CA  ALA A 260    20506  21959  27142  -3798   -529  -3561       C  
ATOM   1430  C   ALA A 260     -37.418  -2.523  11.249  1.00181.18           C  
ANISOU 1430  C   ALA A 260    20409  21656  26776  -3775   -220  -3166       C  
ATOM   1431  O   ALA A 260     -38.594  -2.891  11.262  1.00177.89           O  
ANISOU 1431  O   ALA A 260    20276  21226  26089  -3492   -173  -3099       O  
ATOM   1432  CB  ALA A 260     -35.854  -3.833  12.669  1.00183.94           C  
ANISOU 1432  CB  ALA A 260    20316  22522  27051  -3658   -537  -3639       C  
ATOM   1433  N   PRO A 261     -36.794  -2.097  10.137  1.00185.46           N  
ANISOU 1433  N   PRO A 261    20761  22179  27527  -4087    -13  -2893       N  
ATOM   1434  CA  PRO A 261     -37.339  -2.313   8.793  1.00183.88           C  
ANISOU 1434  CA  PRO A 261    20649  22046  27171  -4084    295  -2498       C  
ATOM   1435  C   PRO A 261     -36.987  -3.707   8.280  1.00181.51           C  
ANISOU 1435  C   PRO A 261    20158  22223  26583  -3926    463  -2438       C  
ATOM   1436  O   PRO A 261     -35.861  -4.173   8.463  1.00182.95           O  
ANISOU 1436  O   PRO A 261    20001  22664  26849  -4001    442  -2573       O  
ATOM   1437  CB  PRO A 261     -36.665  -1.218   7.958  1.00183.53           C  
ANISOU 1437  CB  PRO A 261    20463  21788  27483  -4513    425  -2260       C  
ATOM   1438  CG  PRO A 261     -35.366  -0.960   8.650  1.00186.99           C  
ANISOU 1438  CG  PRO A 261    20564  22263  28222  -4744    253  -2517       C  
ATOM   1439  CD  PRO A 261     -35.590  -1.241  10.117  1.00185.60           C  
ANISOU 1439  CD  PRO A 261    20491  22071  27957  -4489    -72  -2934       C  
ATOM   1440  N   ARG A 262     -37.976  -4.379   7.702  1.00180.46           N  
ANISOU 1440  N   ARG A 262    20247  22196  26124  -3690    606  -2257       N  
ATOM   1441  CA  ARG A 262     -37.828  -5.723   7.133  1.00178.13           C  
ANISOU 1441  CA  ARG A 262    19841  22309  25530  -3512    770  -2194       C  
ATOM   1442  C   ARG A 262     -37.452  -6.879   8.084  1.00176.34           C  
ANISOU 1442  C   ARG A 262    19481  22363  25155  -3252    605  -2495       C  
ATOM   1443  O   ARG A 262     -36.729  -7.781   7.670  1.00176.34           O  
ANISOU 1443  O   ARG A 262    19243  22687  25072  -3211    724  -2496       O  
ATOM   1444  CB  ARG A 262     -36.785  -5.696   6.010  1.00184.56           C  
ANISOU 1444  CB  ARG A 262    20359  23316  26451  -3783   1034  -1996       C  
ATOM   1445  CG  ARG A 262     -37.141  -4.807   4.838  1.00186.27           C  
ANISOU 1445  CG  ARG A 262    20707  23340  26726  -4025   1249  -1625       C  
ATOM   1446  CD  ARG A 262     -38.023  -5.522   3.830  1.00183.54           C  
ANISOU 1446  CD  ARG A 262    20579  23153  26004  -3848   1447  -1380       C  
ATOM   1447  NE  ARG A 262     -38.256  -4.678   2.661  1.00185.70           N  
ANISOU 1447  NE  ARG A 262    20962  23278  26319  -4097   1649  -1001       N  
ATOM   1448  CZ  ARG A 262     -39.278  -3.836   2.537  1.00185.51           C  
ANISOU 1448  CZ  ARG A 262    21242  22907  26336  -4113   1582   -817       C  
ATOM   1449  NH1 ARG A 262     -40.177  -3.728   3.509  1.00183.22           N  
ANISOU 1449  NH1 ARG A 262    21169  22397  26049  -3885   1343   -995       N  
ATOM   1450  NH2 ARG A 262     -39.404  -3.096   1.440  1.00187.88           N  
ANISOU 1450  NH2 ARG A 262    21628  23086  26673  -4348   1759   -445       N  
ATOM   1451  N   PRO A 263     -37.924  -6.877   9.348  1.00175.95           N  
ANISOU 1451  N   PRO A 263    19586  22202  25065  -3065    337  -2746       N  
ATOM   1452  CA  PRO A 263     -37.873  -8.198   9.976  1.00173.53           C  
ANISOU 1452  CA  PRO A 263    19233  22188  24511  -2766    234  -2920       C  
ATOM   1453  C   PRO A 263     -39.281  -8.789  10.104  1.00169.64           C  
ANISOU 1453  C   PRO A 263    19083  21676  23695  -2466    231  -2852       C  
ATOM   1454  O   PRO A 263     -40.053  -8.424  10.996  1.00168.83           O  
ANISOU 1454  O   PRO A 263    19203  21393  23551  -2344     66  -2971       O  
ATOM   1455  CB  PRO A 263     -37.245  -7.906  11.338  1.00173.61           C  
ANISOU 1455  CB  PRO A 263    19130  22156  24677  -2779    -72  -3251       C  
ATOM   1456  CG  PRO A 263     -37.750  -6.563  11.678  1.00175.15           C  
ANISOU 1456  CG  PRO A 263    19530  21963  25055  -2926   -163  -3281       C  
ATOM   1457  CD  PRO A 263     -38.012  -5.825  10.376  1.00176.02           C  
ANISOU 1457  CD  PRO A 263    19694  21896  25289  -3148     95  -2952       C  
ATOM   1458  N   LEU A 264     -39.610  -9.693   9.188  1.00169.87           N  
ANISOU 1458  N   LEU A 264    19147  21898  23500  -2354    422  -2663       N  
ATOM   1459  CA  LEU A 264     -40.944 -10.276   9.129  1.00166.47           C  
ANISOU 1459  CA  LEU A 264    19013  21456  22781  -2109    436  -2556       C  
ATOM   1460  C   LEU A 264     -41.236 -11.256  10.277  1.00164.35           C  
ANISOU 1460  C   LEU A 264    18808  21320  22317  -1817    238  -2760       C  
ATOM   1461  O   LEU A 264     -42.346 -11.276  10.800  1.00162.45           O  
ANISOU 1461  O   LEU A 264    18815  20977  21932  -1649    162  -2755       O  
ATOM   1462  CB  LEU A 264     -41.151 -10.961   7.774  1.00167.97           C  
ANISOU 1462  CB  LEU A 264    19224  21810  22787  -2100    678  -2308       C  
ATOM   1463  CG  LEU A 264     -40.953 -10.052   6.555  1.00170.17           C  
ANISOU 1463  CG  LEU A 264    19474  21986  23197  -2383    894  -2056       C  
ATOM   1464  CD1 LEU A 264     -41.070 -10.850   5.260  1.00169.36           C  
ANISOU 1464  CD1 LEU A 264    19394  22099  22857  -2358   1125  -1850       C  
ATOM   1465  CD2 LEU A 264     -41.917  -8.870   6.558  1.00170.42           C  
ANISOU 1465  CD2 LEU A 264    19748  21673  23331  -2462    856  -1914       C  
ATOM   1466  N   PRO A 265     -40.259 -12.088  10.672  1.00167.25           N  
ANISOU 1466  N   PRO A 265    18946  21924  22679  -1748    158  -2924       N  
ATOM   1467  CA  PRO A 265     -40.654 -12.894  11.829  1.00165.51           C  
ANISOU 1467  CA  PRO A 265    18831  21788  22267  -1480    -49  -3084       C  
ATOM   1468  C   PRO A 265     -39.805 -12.682  13.093  1.00167.59           C  
ANISOU 1468  C   PRO A 265    18944  22083  22651  -1486   -308  -3367       C  
ATOM   1469  O   PRO A 265     -39.648 -13.631  13.861  1.00166.86           O  
ANISOU 1469  O   PRO A 265    18827  22162  22410  -1281   -464  -3485       O  
ATOM   1470  CB  PRO A 265     -40.476 -14.314  11.301  1.00167.61           C  
ANISOU 1470  CB  PRO A 265    19026  22304  22353  -1314     35  -3019       C  
ATOM   1471  CG  PRO A 265     -39.232 -14.197  10.453  1.00170.08           C  
ANISOU 1471  CG  PRO A 265    19027  22735  22860  -1502    184  -3006       C  
ATOM   1472  CD  PRO A 265     -39.234 -12.784   9.871  1.00171.90           C  
ANISOU 1472  CD  PRO A 265    19262  22754  23298  -1796    304  -2891       C  
ATOM   1473  N   TRP A 266     -39.278 -11.479  13.314  1.00162.20           N  
ANISOU 1473  N   TRP A 266    18171  21230  22230  -1719   -371  -3468       N  
ATOM   1474  CA  TRP A 266     -38.444 -11.227  14.491  1.00164.62           C  
ANISOU 1474  CA  TRP A 266    18332  21562  22653  -1750   -645  -3751       C  
ATOM   1475  C   TRP A 266     -39.270 -10.704  15.660  1.00164.40           C  
ANISOU 1475  C   TRP A 266    18586  21364  22513  -1642   -834  -3914       C  
ATOM   1476  O   TRP A 266     -40.372 -10.196  15.468  1.00163.09           O  
ANISOU 1476  O   TRP A 266    18682  21001  22285  -1608   -732  -3807       O  
ATOM   1477  CB  TRP A 266     -37.324 -10.226  14.170  1.00172.29           C  
ANISOU 1477  CB  TRP A 266    19028  22443  23990  -2084   -643  -3803       C  
ATOM   1478  CG  TRP A 266     -36.047 -10.819  13.596  1.00173.91           C  
ANISOU 1478  CG  TRP A 266    18837  22906  24336  -2170   -568  -3781       C  
ATOM   1479  CD1 TRP A 266     -35.568 -10.673  12.322  1.00174.95           C  
ANISOU 1479  CD1 TRP A 266    18778  23084  24610  -2360   -293  -3583       C  
ATOM   1480  CD2 TRP A 266     -35.073 -11.612  14.298  1.00175.15           C  
ANISOU 1480  CD2 TRP A 266    18727  23314  24507  -2062   -769  -3967       C  
ATOM   1481  NE1 TRP A 266     -34.372 -11.340  12.186  1.00176.72           N  
ANISOU 1481  NE1 TRP A 266    18623  23581  24942  -2365   -287  -3646       N  
ATOM   1482  CE2 TRP A 266     -34.046 -11.924  13.383  1.00176.86           C  
ANISOU 1482  CE2 TRP A 266    18581  23719  24899  -2178   -588  -3878       C  
ATOM   1483  CE3 TRP A 266     -34.977 -12.097  15.610  1.00175.21           C  
ANISOU 1483  CE3 TRP A 266    18769  23417  24386  -1869  -1084  -4188       C  
ATOM   1484  CZ2 TRP A 266     -32.938 -12.698  13.736  1.00178.61           C  
ANISOU 1484  CZ2 TRP A 266    18455  24206  25204  -2093   -717  -4010       C  
ATOM   1485  CZ3 TRP A 266     -33.875 -12.866  15.958  1.00176.92           C  
ANISOU 1485  CZ3 TRP A 266    18657  23891  24672  -1795  -1234  -4301       C  
ATOM   1486  CH2 TRP A 266     -32.872 -13.158  15.024  1.00178.58           C  
ANISOU 1486  CH2 TRP A 266    18490  24272  25091  -1900  -1053  -4215       C  
ATOM   1487  N   GLY A 267     -38.730 -10.833  16.870  1.00154.79           N  
ANISOU 1487  N   GLY A 267    17310  20238  21265  -1578  -1111  -4174       N  
ATOM   1488  CA  GLY A 267     -39.403 -10.351  18.062  1.00155.18           C  
ANISOU 1488  CA  GLY A 267    17622  20163  21178  -1470  -1295  -4370       C  
ATOM   1489  C   GLY A 267     -38.826 -10.881  19.361  1.00156.55           C  
ANISOU 1489  C   GLY A 267    17740  20533  21209  -1343  -1602  -4619       C  
ATOM   1490  O   GLY A 267     -38.343 -12.009  19.426  1.00155.80           O  
ANISOU 1490  O   GLY A 267    17494  20698  21006  -1211  -1660  -4581       O  
ATOM   1491  N   SER A 268     -38.929 -10.071  20.410  1.00157.15           N  
ANISOU 1491  N   SER A 268    17965  20475  21269  -1366  -1807  -4875       N  
ATOM   1492  CA  SER A 268     -38.365 -10.377  21.724  1.00159.19           C  
ANISOU 1492  CA  SER A 268    18201  20905  21381  -1275  -2137  -5139       C  
ATOM   1493  C   SER A 268     -39.216 -11.409  22.491  1.00156.90           C  
ANISOU 1493  C   SER A 268    18144  20809  20662   -946  -2174  -5100       C  
ATOM   1494  O   SER A 268     -40.277 -11.807  22.011  1.00153.81           O  
ANISOU 1494  O   SER A 268    17926  20395  20118   -805  -1944  -4883       O  
ATOM   1495  CB  SER A 268     -38.227  -9.076  22.528  1.00161.18           C  
ANISOU 1495  CB  SER A 268    18566  20926  21750  -1428  -2334  -5445       C  
ATOM   1496  OG  SER A 268     -39.493  -8.593  22.938  1.00160.27           O  
ANISOU 1496  OG  SER A 268    18817  20636  21443  -1284  -2248  -5488       O  
ATOM   1497  N   PRO A 269     -38.719 -11.903  23.646  1.00157.94           N  
ANISOU 1497  N   PRO A 269    18262  21146  20603   -833  -2471  -5284       N  
ATOM   1498  CA  PRO A 269     -39.478 -12.840  24.485  1.00156.41           C  
ANISOU 1498  CA  PRO A 269    18297  21139  19990   -540  -2526  -5240       C  
ATOM   1499  C   PRO A 269     -40.860 -12.359  24.908  1.00155.41           C  
ANISOU 1499  C   PRO A 269    18534  20880  19633   -415  -2391  -5256       C  
ATOM   1500  O   PRO A 269     -41.765 -13.177  25.044  1.00153.01           O  
ANISOU 1500  O   PRO A 269    18396  20692  19049   -201  -2278  -5080       O  
ATOM   1501  CB  PRO A 269     -38.592 -12.982  25.721  1.00160.32           C  
ANISOU 1501  CB  PRO A 269    18729  21816  20370   -515  -2911  -5495       C  
ATOM   1502  CG  PRO A 269     -37.239 -12.831  25.202  1.00162.30           C  
ANISOU 1502  CG  PRO A 269    18595  22087  20985   -729  -3019  -5543       C  
ATOM   1503  CD  PRO A 269     -37.328 -11.787  24.122  1.00162.06           C  
ANISOU 1503  CD  PRO A 269    18502  21775  21297   -975  -2774  -5492       C  
ATOM   1504  N   GLU A 270     -41.001 -11.056  25.133  1.00155.87           N  
ANISOU 1504  N   GLU A 270    18705  20694  19823   -547  -2409  -5469       N  
ATOM   1505  CA  GLU A 270     -42.247 -10.468  25.627  1.00155.72           C  
ANISOU 1505  CA  GLU A 270    19017  20537  19612   -414  -2292  -5538       C  
ATOM   1506  C   GLU A 270     -43.424 -10.725  24.701  1.00152.11           C  
ANISOU 1506  C   GLU A 270    18653  20000  19141   -316  -1955  -5223       C  
ATOM   1507  O   GLU A 270     -44.525 -11.020  25.158  1.00150.92           O  
ANISOU 1507  O   GLU A 270    18722  19911  18708   -104  -1849  -5160       O  
ATOM   1508  CB  GLU A 270     -42.072  -8.962  25.833  1.00156.43           C  
ANISOU 1508  CB  GLU A 270    19181  20318  19936   -594  -2365  -5824       C  
ATOM   1509  CG  GLU A 270     -41.227  -8.599  27.044  1.00160.53           C  
ANISOU 1509  CG  GLU A 270    19715  20905  20374   -650  -2725  -6200       C  
ATOM   1510  CD  GLU A 270     -39.758  -8.968  26.883  1.00161.96           C  
ANISOU 1510  CD  GLU A 270    19547  21230  20760   -835  -2957  -6224       C  
ATOM   1511  OE1 GLU A 270     -39.309  -9.205  25.739  1.00160.34           O  
ANISOU 1511  OE1 GLU A 270    19079  21004  20838   -970  -2812  -5992       O  
ATOM   1512  OE2 GLU A 270     -39.052  -9.033  27.910  1.00164.96           O  
ANISOU 1512  OE2 GLU A 270    19909  21762  21008   -838  -3287  -6476       O  
ATOM   1513  N   PHE A 271     -43.178 -10.624  23.400  1.00153.30           N  
ANISOU 1513  N   PHE A 271    18625  20032  19589   -478  -1791  -5018       N  
ATOM   1514  CA  PHE A 271     -44.204 -10.873  22.396  1.00150.10           C  
ANISOU 1514  CA  PHE A 271    18286  19556  19189   -415  -1499  -4706       C  
ATOM   1515  C   PHE A 271     -44.684 -12.322  22.450  1.00147.31           C  
ANISOU 1515  C   PHE A 271    17959  19470  18542   -205  -1449  -4492       C  
ATOM   1516  O   PHE A 271     -45.893 -12.620  22.386  1.00145.33           O  
ANISOU 1516  O   PHE A 271    17877  19224  18117    -49  -1286  -4324       O  
ATOM   1517  CB  PHE A 271     -43.659 -10.525  21.018  1.00152.43           C  
ANISOU 1517  CB  PHE A 271    18376  19710  19828   -649  -1363  -4542       C  
ATOM   1518  CG  PHE A 271     -43.536  -9.046  20.781  1.00154.86           C  
ANISOU 1518  CG  PHE A 271    18710  19689  20442   -856  -1348  -4661       C  
ATOM   1519  CD1 PHE A 271     -42.725  -8.545  19.780  1.00155.84           C  
ANISOU 1519  CD1 PHE A 271    18623  19687  20900  -1125  -1288  -4575       C  
ATOM   1520  CD2 PHE A 271     -44.258  -8.151  21.556  1.00156.47           C  
ANISOU 1520  CD2 PHE A 271    19155  19697  20598   -776  -1382  -4855       C  
ATOM   1521  CE1 PHE A 271     -42.630  -7.181  19.558  1.00158.35           C  
ANISOU 1521  CE1 PHE A 271    18976  19671  21517  -1330  -1281  -4658       C  
ATOM   1522  CE2 PHE A 271     -44.166  -6.784  21.345  1.00159.00           C  
ANISOU 1522  CE2 PHE A 271    19520  19669  21224   -957  -1381  -4969       C  
ATOM   1523  CZ  PHE A 271     -43.351  -6.300  20.341  1.00159.92           C  
ANISOU 1523  CZ  PHE A 271    19430  19643  21690  -1244  -1338  -4858       C  
ATOM   1524  N   ILE A 272     -43.713 -13.213  22.596  1.00147.27           N  
ANISOU 1524  N   ILE A 272    17775  19679  18502   -202  -1606  -4502       N  
ATOM   1525  CA  ILE A 272     -43.969 -14.631  22.765  1.00145.30           C  
ANISOU 1525  CA  ILE A 272    17543  19666  17997    -10  -1616  -4326       C  
ATOM   1526  C   ILE A 272     -44.852 -14.838  23.987  1.00145.64           C  
ANISOU 1526  C   ILE A 272    17840  19810  17684    195  -1674  -4383       C  
ATOM   1527  O   ILE A 272     -45.871 -15.509  23.914  1.00143.52           O  
ANISOU 1527  O   ILE A 272    17701  19603  17226    340  -1532  -4171       O  
ATOM   1528  CB  ILE A 272     -42.656 -15.418  22.953  1.00150.16           C  
ANISOU 1528  CB  ILE A 272    17923  20476  18654    -22  -1831  -4386       C  
ATOM   1529  CG1 ILE A 272     -41.655 -15.056  21.856  1.00150.70           C  
ANISOU 1529  CG1 ILE A 272    17707  20465  19087   -241  -1769  -4375       C  
ATOM   1530  CG2 ILE A 272     -42.920 -16.921  23.028  1.00148.25           C  
ANISOU 1530  CG2 ILE A 272    17709  20434  18187    180  -1840  -4181       C  
ATOM   1531  CD1 ILE A 272     -40.252 -15.550  22.120  1.00152.77           C  
ANISOU 1531  CD1 ILE A 272    17689  20901  19455   -272  -1996  -4490       C  
ATOM   1532  N   GLY A 273     -44.451 -14.232  25.101  1.00144.07           N  
ANISOU 1532  N   GLY A 273    17710  19634  17395    194  -1881  -4673       N  
ATOM   1533  CA  GLY A 273     -45.185 -14.303  26.350  1.00145.18           C  
ANISOU 1533  CA  GLY A 273    18100  19892  17170    381  -1938  -4771       C  
ATOM   1534  C   GLY A 273     -46.607 -13.807  26.237  1.00144.06           C  
ANISOU 1534  C   GLY A 273    18162  19621  16953    473  -1676  -4688       C  
ATOM   1535  O   GLY A 273     -47.505 -14.362  26.865  1.00143.57           O  
ANISOU 1535  O   GLY A 273    18264  19707  16577    660  -1607  -4591       O  
ATOM   1536  N   LEU A 274     -46.809 -12.758  25.443  1.00145.23           N  
ANISOU 1536  N   LEU A 274    18289  19493  17399    343  -1532  -4712       N  
ATOM   1537  CA  LEU A 274     -48.143 -12.197  25.211  1.00144.39           C  
ANISOU 1537  CA  LEU A 274    18342  19232  17286    434  -1286  -4622       C  
ATOM   1538  C   LEU A 274     -49.045 -13.170  24.481  1.00141.01           C  
ANISOU 1538  C   LEU A 274    17899  18893  16784    525  -1087  -4252       C  
ATOM   1539  O   LEU A 274     -50.094 -13.567  24.994  1.00140.50           O  
ANISOU 1539  O   LEU A 274    17973  18944  16468    705   -981  -4152       O  
ATOM   1540  CB  LEU A 274     -48.054 -10.905  24.405  1.00143.51           C  
ANISOU 1540  CB  LEU A 274    18193  18783  17551    261  -1203  -4690       C  
ATOM   1541  CG  LEU A 274     -47.585  -9.694  25.200  1.00147.30           C  
ANISOU 1541  CG  LEU A 274    18763  19093  18112    194  -1359  -5075       C  
ATOM   1542  CD1 LEU A 274     -47.350  -8.513  24.273  1.00148.16           C  
ANISOU 1542  CD1 LEU A 274    18807  18843  18642    -17  -1294  -5092       C  
ATOM   1543  CD2 LEU A 274     -48.589  -9.364  26.292  1.00148.91           C  
ANISOU 1543  CD2 LEU A 274    19223  19325  18030    423  -1306  -5244       C  
ATOM   1544  N   GLY A 275     -48.625 -13.547  23.275  1.00141.73           N  
ANISOU 1544  N   GLY A 275    17820  18937  17094    392  -1035  -4053       N  
ATOM   1545  CA  GLY A 275     -49.424 -14.434  22.448  1.00138.74           C  
ANISOU 1545  CA  GLY A 275    17428  18613  16672    447   -867  -3717       C  
ATOM   1546  C   GLY A 275     -49.662 -15.766  23.126  1.00137.92           C  
ANISOU 1546  C   GLY A 275    17373  18772  16258    606   -931  -3602       C  
ATOM   1547  O   GLY A 275     -50.742 -16.349  23.025  1.00136.36           O  
ANISOU 1547  O   GLY A 275    17254  18634  15924    712   -797  -3377       O  
ATOM   1548  N   PHE A 276     -48.630 -16.248  23.809  1.00137.66           N  
ANISOU 1548  N   PHE A 276    17283  18890  16130    612  -1151  -3743       N  
ATOM   1549  CA  PHE A 276     -48.699 -17.500  24.541  1.00137.44           C  
ANISOU 1549  CA  PHE A 276    17308  19100  15815    758  -1254  -3635       C  
ATOM   1550  C   PHE A 276     -49.660 -17.377  25.707  1.00138.72           C  
ANISOU 1550  C   PHE A 276    17678  19367  15660    918  -1216  -3673       C  
ATOM   1551  O   PHE A 276     -50.351 -18.330  26.036  1.00137.91           O  
ANISOU 1551  O   PHE A 276    17655  19415  15330   1036  -1170  -3463       O  
ATOM   1552  CB  PHE A 276     -47.320 -17.927  25.030  1.00136.26           C  
ANISOU 1552  CB  PHE A 276    17038  19077  15658    735  -1525  -3786       C  
ATOM   1553  CG  PHE A 276     -47.296 -19.297  25.635  1.00136.11           C  
ANISOU 1553  CG  PHE A 276    17059  19273  15384    881  -1648  -3633       C  
ATOM   1554  CD1 PHE A 276     -47.312 -20.420  24.823  1.00133.97           C  
ANISOU 1554  CD1 PHE A 276    16708  19014  15181    899  -1600  -3381       C  
ATOM   1555  CD2 PHE A 276     -47.262 -19.467  27.009  1.00138.40           C  
ANISOU 1555  CD2 PHE A 276    17484  19743  15360    999  -1818  -3737       C  
ATOM   1556  CE1 PHE A 276     -47.286 -21.685  25.369  1.00134.11           C  
ANISOU 1556  CE1 PHE A 276    16773  19189  14995   1031  -1726  -3228       C  
ATOM   1557  CE2 PHE A 276     -47.235 -20.732  27.561  1.00138.55           C  
ANISOU 1557  CE2 PHE A 276    17548  19945  15148   1127  -1941  -3561       C  
ATOM   1558  CZ  PHE A 276     -47.250 -21.842  26.741  1.00136.39           C  
ANISOU 1558  CZ  PHE A 276    17189  19651  14981   1142  -1897  -3301       C  
ATOM   1559  N   LEU A 277     -49.678 -16.222  26.363  1.00138.61           N  
ANISOU 1559  N   LEU A 277    17757  19280  15627    919  -1234  -3949       N  
ATOM   1560  CA  LEU A 277     -50.681 -16.000  27.393  1.00140.09           C  
ANISOU 1560  CA  LEU A 277    18146  19567  15513   1085  -1144  -4001       C  
ATOM   1561  C   LEU A 277     -52.080 -15.958  26.822  1.00138.28           C  
ANISOU 1561  C   LEU A 277    17956  19265  15320   1151   -858  -3764       C  
ATOM   1562  O   LEU A 277     -53.025 -16.332  27.498  1.00138.75           O  
ANISOU 1562  O   LEU A 277    18128  19480  15109   1300   -747  -3661       O  
ATOM   1563  CB  LEU A 277     -50.421 -14.721  28.172  1.00142.93           C  
ANISOU 1563  CB  LEU A 277    18615  19837  15857   1083  -1218  -4383       C  
ATOM   1564  CG  LEU A 277     -49.558 -14.971  29.401  1.00145.74           C  
ANISOU 1564  CG  LEU A 277    19038  20402  15936   1122  -1497  -4608       C  
ATOM   1565  CD1 LEU A 277     -49.803 -13.870  30.411  1.00149.23           C  
ANISOU 1565  CD1 LEU A 277    19676  20810  16214   1194  -1512  -4961       C  
ATOM   1566  CD2 LEU A 277     -49.865 -16.346  29.991  1.00145.18           C  
ANISOU 1566  CD2 LEU A 277    19024  20624  15514   1259  -1527  -4362       C  
ATOM   1567  N   VAL A 278     -52.215 -15.477  25.592  1.00139.44           N  
ANISOU 1567  N   VAL A 278    17999  19186  15797   1035   -740  -3669       N  
ATOM   1568  CA  VAL A 278     -53.500 -15.520  24.902  1.00137.66           C  
ANISOU 1568  CA  VAL A 278    17777  18893  15636   1083   -502  -3407       C  
ATOM   1569  C   VAL A 278     -53.952 -16.952  24.660  1.00135.55           C  
ANISOU 1569  C   VAL A 278    17476  18798  15227   1119   -473  -3080       C  
ATOM   1570  O   VAL A 278     -55.088 -17.314  24.958  1.00135.38           O  
ANISOU 1570  O   VAL A 278    17513  18878  15047   1232   -331  -2903       O  
ATOM   1571  CB  VAL A 278     -53.427 -14.790  23.558  1.00135.23           C  
ANISOU 1571  CB  VAL A 278    17367  18318  15698    934   -421  -3346       C  
ATOM   1572  CG1 VAL A 278     -54.657 -15.076  22.720  1.00133.23           C  
ANISOU 1572  CG1 VAL A 278    17090  18026  15505    967   -226  -3028       C  
ATOM   1573  CG2 VAL A 278     -53.230 -13.316  23.793  1.00137.60           C  
ANISOU 1573  CG2 VAL A 278    17721  18398  16163    905   -423  -3633       C  
ATOM   1574  N   PHE A 279     -53.044 -17.755  24.117  1.00136.04           N  
ANISOU 1574  N   PHE A 279    17439  18887  15364   1022   -608  -3006       N  
ATOM   1575  CA  PHE A 279     -53.319 -19.146  23.788  1.00134.22           C  
ANISOU 1575  CA  PHE A 279    17183  18772  15044   1041   -613  -2718       C  
ATOM   1576  C   PHE A 279     -53.638 -19.967  25.035  1.00135.48           C  
ANISOU 1576  C   PHE A 279    17454  19163  14859   1180   -672  -2657       C  
ATOM   1577  O   PHE A 279     -54.626 -20.707  25.083  1.00134.76           O  
ANISOU 1577  O   PHE A 279    17404  19156  14644   1237   -568  -2399       O  
ATOM   1578  CB  PHE A 279     -52.130 -19.754  23.064  1.00132.36           C  
ANISOU 1578  CB  PHE A 279    16821  18510  14961    936   -755  -2718       C  
ATOM   1579  CG  PHE A 279     -52.496 -20.873  22.146  1.00130.17           C  
ANISOU 1579  CG  PHE A 279    16505  18228  14725    911   -708  -2434       C  
ATOM   1580  CD1 PHE A 279     -52.632 -20.653  20.784  1.00128.52           C  
ANISOU 1580  CD1 PHE A 279    16221  17868  14743    794   -598  -2335       C  
ATOM   1581  CD2 PHE A 279     -52.681 -22.151  22.639  1.00130.06           C  
ANISOU 1581  CD2 PHE A 279    16545  18353  14519    996   -786  -2267       C  
ATOM   1582  CE1 PHE A 279     -52.954 -21.686  19.932  1.00126.82           C  
ANISOU 1582  CE1 PHE A 279    15991  17646  14550    768   -571  -2105       C  
ATOM   1583  CE2 PHE A 279     -53.010 -23.191  21.793  1.00128.35           C  
ANISOU 1583  CE2 PHE A 279    16309  18101  14356    965   -761  -2027       C  
ATOM   1584  CZ  PHE A 279     -53.141 -22.959  20.436  1.00126.74           C  
ANISOU 1584  CZ  PHE A 279    16035  17751  14367    853   -657  -1963       C  
ATOM   1585  N   VAL A 280     -52.770 -19.841  26.031  1.00135.81           N  
ANISOU 1585  N   VAL A 280    17542  19312  14748   1221   -853  -2885       N  
ATOM   1586  CA  VAL A 280     -52.971 -20.452  27.333  1.00137.68           C  
ANISOU 1586  CA  VAL A 280    17910  19785  14619   1353   -926  -2858       C  
ATOM   1587  C   VAL A 280     -54.286 -19.975  27.925  1.00138.75           C  
ANISOU 1587  C   VAL A 280    18162  19988  14568   1461   -704  -2822       C  
ATOM   1588  O   VAL A 280     -55.005 -20.748  28.546  1.00139.31           O  
ANISOU 1588  O   VAL A 280    18311  20241  14380   1549   -641  -2616       O  
ATOM   1589  CB  VAL A 280     -51.808 -20.123  28.290  1.00138.83           C  
ANISOU 1589  CB  VAL A 280    18091  20023  14635   1369  -1174  -3158       C  
ATOM   1590  CG1 VAL A 280     -52.194 -20.365  29.739  1.00141.49           C  
ANISOU 1590  CG1 VAL A 280    18610  20607  14542   1514  -1211  -3181       C  
ATOM   1591  CG2 VAL A 280     -50.590 -20.929  27.916  1.00138.24           C  
ANISOU 1591  CG2 VAL A 280    17883  19954  14686   1308  -1403  -3129       C  
ATOM   1592  N   SER A 281     -54.605 -18.703  27.719  1.00137.54           N  
ANISOU 1592  N   SER A 281    18012  19684  14563   1456   -576  -3013       N  
ATOM   1593  CA  SER A 281     -55.876 -18.166  28.181  1.00138.74           C  
ANISOU 1593  CA  SER A 281    18247  19880  14589   1582   -339  -2996       C  
ATOM   1594  C   SER A 281     -57.032 -18.885  27.499  1.00136.69           C  
ANISOU 1594  C   SER A 281    17913  19635  14390   1582   -154  -2616       C  
ATOM   1595  O   SER A 281     -58.039 -19.157  28.133  1.00137.82           O  
ANISOU 1595  O   SER A 281    18105  19944  14315   1694      4  -2477       O  
ATOM   1596  CB  SER A 281     -55.969 -16.661  27.929  1.00138.77           C  
ANISOU 1596  CB  SER A 281    18256  19659  14811   1580   -250  -3263       C  
ATOM   1597  OG  SER A 281     -54.893 -15.973  28.542  1.00140.94           O  
ANISOU 1597  OG  SER A 281    18597  19898  15054   1553   -442  -3626       O  
ATOM   1598  N   ILE A 282     -56.881 -19.207  26.218  1.00136.94           N  
ANISOU 1598  N   ILE A 282    17821  19505  14706   1451   -174  -2449       N  
ATOM   1599  CA  ILE A 282     -57.911 -19.954  25.504  1.00135.13           C  
ANISOU 1599  CA  ILE A 282    17521  19279  14542   1425    -45  -2095       C  
ATOM   1600  C   ILE A 282     -58.090 -21.354  26.084  1.00135.27           C  
ANISOU 1600  C   ILE A 282    17583  19503  14312   1451   -103  -1856       C  
ATOM   1601  O   ILE A 282     -59.208 -21.785  26.396  1.00135.79           O  
ANISOU 1601  O   ILE A 282    17651  19690  14252   1504     46  -1625       O  
ATOM   1602  CB  ILE A 282     -57.572 -20.073  24.004  1.00131.25           C  
ANISOU 1602  CB  ILE A 282    16918  18584  14368   1270    -88  -1992       C  
ATOM   1603  CG1 ILE A 282     -57.546 -18.690  23.354  1.00131.30           C  
ANISOU 1603  CG1 ILE A 282    16883  18373  14631   1230    -11  -2159       C  
ATOM   1604  CG2 ILE A 282     -58.589 -20.923  23.294  1.00129.68           C  
ANISOU 1604  CG2 ILE A 282    16661  18394  14217   1230      1  -1642       C  
ATOM   1605  CD1 ILE A 282     -57.059 -18.691  21.923  1.00129.22           C  
ANISOU 1605  CD1 ILE A 282    16526  17930  14643   1069    -53  -2082       C  
ATOM   1606  N   ILE A 283     -56.974 -22.043  26.273  1.00137.78           N  
ANISOU 1606  N   ILE A 283    17925  19858  14569   1416   -324  -1906       N  
ATOM   1607  CA  ILE A 283     -56.989 -23.396  26.818  1.00138.19           C  
ANISOU 1607  CA  ILE A 283    18032  20067  14408   1441   -420  -1677       C  
ATOM   1608  C   ILE A 283     -57.628 -23.420  28.209  1.00140.92           C  
ANISOU 1608  C   ILE A 283    18499  20657  14388   1569   -332  -1647       C  
ATOM   1609  O   ILE A 283     -58.450 -24.284  28.509  1.00141.34           O  
ANISOU 1609  O   ILE A 283    18575  20833  14296   1582   -252  -1350       O  
ATOM   1610  CB  ILE A 283     -55.567 -23.981  26.888  1.00140.67           C  
ANISOU 1610  CB  ILE A 283    18346  20374  14728   1417   -691  -1782       C  
ATOM   1611  CG1 ILE A 283     -54.901 -23.932  25.508  1.00138.35           C  
ANISOU 1611  CG1 ILE A 283    17922  19865  14778   1298   -743  -1826       C  
ATOM   1612  CG2 ILE A 283     -55.596 -25.402  27.447  1.00141.37           C  
ANISOU 1612  CG2 ILE A 283    18505  20592  14617   1453   -806  -1521       C  
ATOM   1613  CD1 ILE A 283     -53.413 -24.195  25.534  1.00138.75           C  
ANISOU 1613  CD1 ILE A 283    17923  19906  14890   1286   -980  -1999       C  
ATOM   1614  N   LEU A 284     -57.237 -22.469  29.053  1.00139.84           N  
ANISOU 1614  N   LEU A 284    18443  20592  14098   1653   -348  -1959       N  
ATOM   1615  CA  LEU A 284     -57.787 -22.343  30.400  1.00142.92           C  
ANISOU 1615  CA  LEU A 284    18969  21231  14102   1789   -250  -1989       C  
ATOM   1616  C   LEU A 284     -59.254 -21.938  30.364  1.00143.33           C  
ANISOU 1616  C   LEU A 284    18982  21325  14153   1852     69  -1857       C  
ATOM   1617  O   LEU A 284     -60.012 -22.233  31.287  1.00145.57           O  
ANISOU 1617  O   LEU A 284    19337  21845  14129   1946    213  -1729       O  
ATOM   1618  CB  LEU A 284     -56.991 -21.326  31.220  1.00142.04           C  
ANISOU 1618  CB  LEU A 284    18964  21159  13846   1858   -357  -2406       C  
ATOM   1619  CG  LEU A 284     -55.512 -21.614  31.487  1.00142.53           C  
ANISOU 1619  CG  LEU A 284    19052  21229  13874   1813   -691  -2571       C  
ATOM   1620  CD1 LEU A 284     -54.868 -20.438  32.215  1.00145.14           C  
ANISOU 1620  CD1 LEU A 284    19475  21570  14100   1858   -788  -3006       C  
ATOM   1621  CD2 LEU A 284     -55.333 -22.911  32.263  1.00143.74           C  
ANISOU 1621  CD2 LEU A 284    19292  21604  13720   1853   -836  -2330       C  
ATOM   1622  N   CYS A 285     -59.634 -21.220  29.312  1.00143.41           N  
ANISOU 1622  N   CYS A 285    18871  21114  14504   1805    181  -1889       N  
ATOM   1623  CA  CYS A 285     -61.020 -20.812  29.098  1.00143.71           C  
ANISOU 1623  CA  CYS A 285    18826  21159  14616   1866    464  -1750       C  
ATOM   1624  C   CYS A 285     -61.910 -22.008  28.810  1.00142.79           C  
ANISOU 1624  C   CYS A 285    18625  21137  14492   1802    541  -1316       C  
ATOM   1625  O   CYS A 285     -63.079 -22.030  29.177  1.00144.25           O  
ANISOU 1625  O   CYS A 285    18760  21469  14581   1874    770  -1146       O  
ATOM   1626  CB  CYS A 285     -61.117 -19.816  27.948  1.00141.93           C  
ANISOU 1626  CB  CYS A 285    18494  20653  14782   1818    514  -1856       C  
ATOM   1627  SG  CYS A 285     -62.678 -18.954  27.903  1.00143.32           S  
ANISOU 1627  SG  CYS A 285    18574  20829  15051   1955    841  -1794       S  
ATOM   1628  N   GLU A 286     -61.345 -22.992  28.121  1.00144.23           N  
ANISOU 1628  N   GLU A 286    18782  21224  14796   1663    348  -1147       N  
ATOM   1629  CA  GLU A 286     -62.032 -24.258  27.880  1.00143.61           C  
ANISOU 1629  CA  GLU A 286    18652  21203  14711   1577    363   -748       C  
ATOM   1630  C   GLU A 286     -62.058 -25.112  29.144  1.00146.06           C  
ANISOU 1630  C   GLU A 286    19081  21769  14646   1631    343   -604       C  
ATOM   1631  O   GLU A 286     -63.068 -25.729  29.475  1.00147.26           O  
ANISOU 1631  O   GLU A 286    19198  22067  14688   1620    489   -299       O  
ATOM   1632  CB  GLU A 286     -61.335 -25.031  26.765  1.00149.83           C  
ANISOU 1632  CB  GLU A 286    19404  21787  15739   1429    152   -658       C  
ATOM   1633  CG  GLU A 286     -62.160 -26.134  26.147  1.00148.90           C  
ANISOU 1633  CG  GLU A 286    19214  21635  15726   1312    167   -280       C  
ATOM   1634  CD  GLU A 286     -63.160 -25.597  25.157  1.00147.75           C  
ANISOU 1634  CD  GLU A 286    18921  21381  15836   1257    319   -186       C  
ATOM   1635  OE1 GLU A 286     -63.128 -24.375  24.892  1.00147.52           O  
ANISOU 1635  OE1 GLU A 286    18853  21277  15922   1317    404   -412       O  
ATOM   1636  OE2 GLU A 286     -63.956 -26.398  24.624  1.00147.26           O  
ANISOU 1636  OE2 GLU A 286    18784  21294  15875   1149    332    116       O  
ATOM   1637  N   ARG A 287     -60.914 -25.138  29.824  1.00148.62           N  
ANISOU 1637  N   ARG A 287    19539  22147  14782   1679    148   -812       N  
ATOM   1638  CA  ARG A 287     -60.682 -25.941  31.024  1.00151.12           C  
ANISOU 1638  CA  ARG A 287    19999  22696  14723   1731     62   -693       C  
ATOM   1639  C   ARG A 287     -61.673 -25.631  32.146  1.00154.35           C  
ANISOU 1639  C   ARG A 287    20465  23390  14791   1847    322   -637       C  
ATOM   1640  O   ARG A 287     -62.100 -26.531  32.868  1.00156.28           O  
ANISOU 1640  O   ARG A 287    20772  23834  14776   1843    360   -345       O  
ATOM   1641  CB  ARG A 287     -59.241 -25.729  31.502  1.00156.28           C  
ANISOU 1641  CB  ARG A 287    20764  23351  15265   1776   -207   -995       C  
ATOM   1642  CG  ARG A 287     -58.840 -26.480  32.766  1.00159.18           C  
ANISOU 1642  CG  ARG A 287    21296  23958  15226   1841   -349   -899       C  
ATOM   1643  CD  ARG A 287     -57.342 -26.286  33.027  1.00159.60           C  
ANISOU 1643  CD  ARG A 287    21411  23978  15251   1868   -662  -1195       C  
ATOM   1644  NE  ARG A 287     -56.860 -26.957  34.236  1.00162.63           N  
ANISOU 1644  NE  ARG A 287    21959  24591  15241   1938   -846  -1115       N  
ATOM   1645  CZ  ARG A 287     -55.589 -26.966  34.631  1.00163.68           C  
ANISOU 1645  CZ  ARG A 287    22144  24742  15304   1970  -1154  -1317       C  
ATOM   1646  NH1 ARG A 287     -54.659 -26.353  33.906  1.00161.92           N  
ANISOU 1646  NH1 ARG A 287    21806  24322  15392   1927  -1295  -1612       N  
ATOM   1647  NH2 ARG A 287     -55.242 -27.597  35.747  1.00166.74           N  
ANISOU 1647  NH2 ARG A 287    22688  25352  15312   2038  -1327  -1207       N  
ATOM   1648  N   PHE A 288     -62.002 -24.354  32.308  1.00150.78           N  
ANISOU 1648  N   PHE A 288    19998  22955  14338   1955    503   -922       N  
ATOM   1649  CA  PHE A 288     -63.005 -23.925  33.279  1.00154.05           C  
ANISOU 1649  CA  PHE A 288    20444  23632  14455   2094    797   -913       C  
ATOM   1650  C   PHE A 288     -64.219 -23.354  32.545  1.00153.25           C  
ANISOU 1650  C   PHE A 288    20145  23446  14636   2108   1075   -827       C  
ATOM   1651  O   PHE A 288     -64.815 -22.370  32.986  1.00155.35           O  
ANISOU 1651  O   PHE A 288    20403  23800  14823   2261   1310  -1019       O  
ATOM   1652  CB  PHE A 288     -62.424 -22.883  34.244  1.00157.70           C  
ANISOU 1652  CB  PHE A 288    21074  24201  14642   2248    783  -1352       C  
ATOM   1653  CG  PHE A 288     -61.191 -23.343  34.975  1.00158.81           C  
ANISOU 1653  CG  PHE A 288    21397  24434  14510   2239    475  -1462       C  
ATOM   1654  CD1 PHE A 288     -59.933 -22.902  34.587  1.00157.38           C  
ANISOU 1654  CD1 PHE A 288    21237  24049  14509   2194    195  -1767       C  
ATOM   1655  CD2 PHE A 288     -61.286 -24.227  36.040  1.00161.56           C  
ANISOU 1655  CD2 PHE A 288    21880  25076  14429   2270    459  -1237       C  
ATOM   1656  CE1 PHE A 288     -58.790 -23.327  35.252  1.00158.66           C  
ANISOU 1656  CE1 PHE A 288    21534  24304  14445   2191   -110  -1862       C  
ATOM   1657  CE2 PHE A 288     -60.150 -24.656  36.711  1.00162.85           C  
ANISOU 1657  CE2 PHE A 288    22206  25325  14345   2271    148  -1320       C  
ATOM   1658  CZ  PHE A 288     -58.899 -24.207  36.318  1.00161.39           C  
ANISOU 1658  CZ  PHE A 288    22023  24939  14360   2237   -144  -1639       C  
ATOM   1659  N   GLY A 289     -64.587 -23.981  31.431  1.00148.28           N  
ANISOU 1659  N   GLY A 289    19359  22645  14335   1957   1038   -542       N  
ATOM   1660  CA  GLY A 289     -65.560 -23.410  30.511  1.00147.11           C  
ANISOU 1660  CA  GLY A 289    19011  22365  14520   1949   1221   -474       C  
ATOM   1661  C   GLY A 289     -67.041 -23.647  30.745  1.00149.02           C  
ANISOU 1661  C   GLY A 289    19093  22800  14727   1979   1516   -165       C  
ATOM   1662  O   GLY A 289     -67.517 -24.778  30.687  1.00149.02           O  
ANISOU 1662  O   GLY A 289    19032  22881  14710   1851   1509    213       O  
ATOM   1663  N   ALA A 290     -67.770 -22.556  30.976  1.00146.52           N  
ANISOU 1663  N   ALA A 290    18697  22541  14432   2149   1773   -331       N  
ATOM   1664  CA  ALA A 290     -69.227 -22.586  31.110  1.00148.58           C  
ANISOU 1664  CA  ALA A 290    18750  22983  14722   2204   2083    -70       C  
ATOM   1665  C   ALA A 290     -69.885 -22.479  29.732  1.00146.18           C  
ANISOU 1665  C   ALA A 290    18209  22450  14882   2101   2069    109       C  
ATOM   1666  O   ALA A 290     -69.276 -21.950  28.802  1.00143.54           O  
ANISOU 1666  O   ALA A 290    17894  21830  14815   2058   1894    -70       O  
ATOM   1667  CB  ALA A 290     -69.697 -21.452  32.023  1.00152.13           C  
ANISOU 1667  CB  ALA A 290    19220  23604  14980   2469   2374   -353       C  
ATOM   1668  N   PRO A 291     -71.129 -22.979  29.596  1.00147.35           N  
ANISOU 1668  N   PRO A 291    18128  22735  15122   2052   2248    473       N  
ATOM   1669  CA  PRO A 291     -71.853 -22.987  28.317  1.00145.52           C  
ANISOU 1669  CA  PRO A 291    17658  22321  15311   1939   2213    686       C  
ATOM   1670  C   PRO A 291     -71.896 -21.658  27.562  1.00144.62           C  
ANISOU 1670  C   PRO A 291    17475  21976  15495   2062   2230    428       C  
ATOM   1671  O   PRO A 291     -72.060 -21.682  26.343  1.00142.34           O  
ANISOU 1671  O   PRO A 291    17072  21474  15536   1935   2089    552       O  
ATOM   1672  CB  PRO A 291     -73.262 -23.403  28.730  1.00148.49           C  
ANISOU 1672  CB  PRO A 291    17787  22967  15664   1948   2487   1034       C  
ATOM   1673  CG  PRO A 291     -73.033 -24.302  29.883  1.00150.46           C  
ANISOU 1673  CG  PRO A 291    18183  23477  15508   1914   2532   1161       C  
ATOM   1674  CD  PRO A 291     -71.877 -23.707  30.637  1.00150.65           C  
ANISOU 1674  CD  PRO A 291    18499  23501  15239   2065   2467    746       C  
ATOM   1675  N   ILE A 292     -71.761 -20.529  28.253  1.00146.61           N  
ANISOU 1675  N   ILE A 292    17810  22262  15635   2300   2388     83       N  
ATOM   1676  CA  ILE A 292     -71.701 -19.238  27.566  1.00146.00           C  
ANISOU 1676  CA  ILE A 292    17700  21920  15853   2415   2381   -170       C  
ATOM   1677  C   ILE A 292     -70.315 -19.010  26.965  1.00142.97           C  
ANISOU 1677  C   ILE A 292    17520  21254  15548   2301   2083   -411       C  
ATOM   1678  O   ILE A 292     -70.190 -18.546  25.835  1.00140.94           O  
ANISOU 1678  O   ILE A 292    17207  20730  15613   2232   1960   -418       O  
ATOM   1679  CB  ILE A 292     -72.057 -18.059  28.503  1.00149.63           C  
ANISOU 1679  CB  ILE A 292    18184  22473  16195   2719   2652   -483       C  
ATOM   1680  CG1 ILE A 292     -73.451 -18.251  29.097  1.00153.04           C  
ANISOU 1680  CG1 ILE A 292    18381  23213  16555   2851   2987   -248       C  
ATOM   1681  CG2 ILE A 292     -72.016 -16.740  27.743  1.00149.20           C  
ANISOU 1681  CG2 ILE A 292    18102  22097  16492   2831   2625   -717       C  
ATOM   1682  CD1 ILE A 292     -73.797 -17.243  30.181  1.00157.22           C  
ANISOU 1682  CD1 ILE A 292    18955  23890  16890   3172   3290   -568       C  
ATOM   1683  N   MET A 293     -69.280 -19.346  27.730  1.00142.96           N  
ANISOU 1683  N   MET A 293    17745  21328  15246   2281   1970   -592       N  
ATOM   1684  CA  MET A 293     -67.886 -19.173  27.313  1.00140.59           C  
ANISOU 1684  CA  MET A 293    17620  20803  14996   2179   1697   -832       C  
ATOM   1685  C   MET A 293     -67.508 -19.986  26.069  1.00137.07           C  
ANISOU 1685  C   MET A 293    17124  20184  14773   1938   1465   -606       C  
ATOM   1686  O   MET A 293     -66.429 -19.790  25.503  1.00135.08           O  
ANISOU 1686  O   MET A 293    16968  19731  14624   1848   1262   -779       O  
ATOM   1687  CB  MET A 293     -66.957 -19.539  28.475  1.00141.79           C  
ANISOU 1687  CB  MET A 293    17991  21124  14758   2207   1613  -1019       C  
ATOM   1688  CG  MET A 293     -67.186 -18.691  29.720  1.00145.54           C  
ANISOU 1688  CG  MET A 293    18565  21770  14965   2444   1818  -1306       C  
ATOM   1689  SD  MET A 293     -66.386 -19.335  31.206  1.00147.75           S  
ANISOU 1689  SD  MET A 293    19090  22344  14703   2477   1738  -1425       S  
ATOM   1690  CE  MET A 293     -64.667 -18.942  30.887  1.00145.74           C  
ANISOU 1690  CE  MET A 293    19005  21833  14537   2378   1380  -1778       C  
ATOM   1691  N   LYS A 294     -68.404 -20.874  25.639  1.00139.25           N  
ANISOU 1691  N   LYS A 294    17244  20539  15125   1834   1500   -230       N  
ATOM   1692  CA  LYS A 294     -68.174 -21.718  24.465  1.00136.37           C  
ANISOU 1692  CA  LYS A 294    16842  20020  14953   1611   1287    -14       C  
ATOM   1693  C   LYS A 294     -68.054 -20.853  23.215  1.00134.64           C  
ANISOU 1693  C   LYS A 294    16567  19530  15060   1573   1215   -102       C  
ATOM   1694  O   LYS A 294     -68.797 -19.888  23.058  1.00135.85           O  
ANISOU 1694  O   LYS A 294    16606  19638  15373   1694   1362   -130       O  
ATOM   1695  CB  LYS A 294     -69.305 -22.731  24.285  1.00136.16           C  
ANISOU 1695  CB  LYS A 294    16650  20123  14963   1505   1345    396       C  
ATOM   1696  CG  LYS A 294     -69.374 -23.817  25.348  1.00137.73           C  
ANISOU 1696  CG  LYS A 294    16912  20562  14859   1479   1379    566       C  
ATOM   1697  CD  LYS A 294     -68.025 -24.156  25.961  1.00137.21           C  
ANISOU 1697  CD  LYS A 294    17085  20496  14551   1482   1212    360       C  
ATOM   1698  CE  LYS A 294     -68.209 -25.186  27.063  1.00139.30           C  
ANISOU 1698  CE  LYS A 294    17414  21009  14504   1470   1256    569       C  
ATOM   1699  NZ  LYS A 294     -66.946 -25.542  27.740  1.00139.27           N  
ANISOU 1699  NZ  LYS A 294    17636  21028  14251   1490   1078    395       N  
ATOM   1700  N   SER A 295     -67.082 -21.165  22.360  1.00132.73           N  
ANISOU 1700  N   SER A 295    16410  19111  14909   1420    994   -150       N  
ATOM   1701  CA  SER A 295     -66.810 -20.409  21.131  1.00131.16           C  
ANISOU 1701  CA  SER A 295    16187  18663  14985   1357    912   -220       C  
ATOM   1702  C   SER A 295     -66.477 -18.954  21.422  1.00132.31           C  
ANISOU 1702  C   SER A 295    16381  18693  15200   1504    995   -529       C  
ATOM   1703  O   SER A 295     -66.241 -18.169  20.508  1.00131.51           O  
ANISOU 1703  O   SER A 295    16269  18374  15326   1463    945   -593       O  
ATOM   1704  CB  SER A 295     -67.979 -20.484  20.141  1.00129.63           C  
ANISOU 1704  CB  SER A 295    15813  18424  15016   1290    938     78       C  
ATOM   1705  OG  SER A 295     -68.410 -21.819  19.933  1.00129.06           O  
ANISOU 1705  OG  SER A 295    15693  18452  14894   1146    860    364       O  
ATOM   1706  N   CYS A 296     -66.486 -18.589  22.696  1.00133.44           N  
ANISOU 1706  N   CYS A 296    16586  18975  15139   1672   1121   -717       N  
ATOM   1707  CA  CYS A 296     -66.020 -17.280  23.101  1.00134.85           C  
ANISOU 1707  CA  CYS A 296    16853  19029  15356   1805   1170  -1064       C  
ATOM   1708  C   CYS A 296     -64.623 -17.430  23.687  1.00134.54           C  
ANISOU 1708  C   CYS A 296    16989  19001  15129   1760   1014  -1332       C  
ATOM   1709  O   CYS A 296     -63.920 -16.438  23.897  1.00135.41           O  
ANISOU 1709  O   CYS A 296    17191  18970  15288   1806    981  -1644       O  
ATOM   1710  CB  CYS A 296     -66.983 -16.629  24.093  1.00135.92           C  
ANISOU 1710  CB  CYS A 296    16946  19297  15399   2044   1417  -1144       C  
ATOM   1711  SG  CYS A 296     -68.541 -16.087  23.338  1.00136.86           S  
ANISOU 1711  SG  CYS A 296    16821  19350  15829   2137   1591   -889       S  
ATOM   1712  N   SER A 297     -64.228 -18.684  23.927  1.00133.62           N  
ANISOU 1712  N   SER A 297    16911  19038  14819   1665    904  -1198       N  
ATOM   1713  CA  SER A 297     -62.934 -19.006  24.525  1.00133.54           C  
ANISOU 1713  CA  SER A 297    17043  19073  14623   1630    733  -1407       C  
ATOM   1714  C   SER A 297     -61.814 -18.335  23.759  1.00132.25           C  
ANISOU 1714  C   SER A 297    16905  18669  14674   1529    585  -1623       C  
ATOM   1715  O   SER A 297     -60.836 -17.892  24.340  1.00133.21           O  
ANISOU 1715  O   SER A 297    17123  18775  14715   1548    488  -1912       O  
ATOM   1716  CB  SER A 297     -62.695 -20.517  24.559  1.00133.97           C  
ANISOU 1716  CB  SER A 297    17112  19260  14531   1526    608  -1174       C  
ATOM   1717  OG  SER A 297     -62.628 -21.046  23.247  1.00131.46           O  
ANISOU 1717  OG  SER A 297    16717  18792  14441   1365    510   -986       O  
ATOM   1718  N   VAL A 298     -61.982 -18.252  22.445  1.00130.36           N  
ANISOU 1718  N   VAL A 298    16574  18253  14702   1411    567  -1470       N  
ATOM   1719  CA  VAL A 298     -61.009 -17.606  21.584  1.00129.31           C  
ANISOU 1719  CA  VAL A 298    16447  17898  14787   1295    458  -1623       C  
ATOM   1720  C   VAL A 298     -60.990 -16.106  21.842  1.00131.18           C  
ANISOU 1720  C   VAL A 298    16719  17974  15151   1383    533  -1880       C  
ATOM   1721  O   VAL A 298     -59.931 -15.490  22.007  1.00131.79           O  
ANISOU 1721  O   VAL A 298    16857  17943  15274   1339    434  -2148       O  
ATOM   1722  CB  VAL A 298     -61.335 -17.884  20.107  1.00130.17           C  
ANISOU 1722  CB  VAL A 298    16465  17882  15112   1155    440  -1368       C  
ATOM   1723  CG1 VAL A 298     -60.316 -17.232  19.194  1.00129.39           C  
ANISOU 1723  CG1 VAL A 298    16371  17578  15214   1023    354  -1500       C  
ATOM   1724  CG2 VAL A 298     -61.399 -19.386  19.867  1.00128.68           C  
ANISOU 1724  CG2 VAL A 298    16261  17825  14806   1072    358  -1137       C  
ATOM   1725  N   VAL A 299     -62.178 -15.529  21.915  1.00130.19           N  
ANISOU 1725  N   VAL A 299    16546  17826  15096   1513    704  -1800       N  
ATOM   1726  CA  VAL A 299     -62.315 -14.102  22.143  1.00132.34           C  
ANISOU 1726  CA  VAL A 299    16856  17911  15515   1626    787  -2033       C  
ATOM   1727  C   VAL A 299     -61.976 -13.779  23.594  1.00134.86           C  
ANISOU 1727  C   VAL A 299    17305  18348  15589   1770    807  -2357       C  
ATOM   1728  O   VAL A 299     -61.476 -12.696  23.896  1.00136.65           O  
ANISOU 1728  O   VAL A 299    17619  18399  15903   1808    781  -2663       O  
ATOM   1729  CB  VAL A 299     -63.732 -13.622  21.789  1.00133.24           C  
ANISOU 1729  CB  VAL A 299    16861  17972  15792   1754    964  -1843       C  
ATOM   1730  CG1 VAL A 299     -63.808 -12.097  21.796  1.00135.46           C  
ANISOU 1730  CG1 VAL A 299    17185  17984  16301   1864   1026  -2070       C  
ATOM   1731  CG2 VAL A 299     -64.101 -14.152  20.420  1.00130.88           C  
ANISOU 1731  CG2 VAL A 299    16444  17615  15670   1600    911  -1499       C  
ATOM   1732  N   ILE A 300     -62.250 -14.721  24.490  1.00135.29           N  
ANISOU 1732  N   ILE A 300    17383  18693  15328   1841    843  -2285       N  
ATOM   1733  CA  ILE A 300     -61.917 -14.543  25.897  1.00137.89           C  
ANISOU 1733  CA  ILE A 300    17855  19182  15355   1971    849  -2572       C  
ATOM   1734  C   ILE A 300     -60.412 -14.618  26.144  1.00137.64           C  
ANISOU 1734  C   ILE A 300    17921  19121  15253   1849    606  -2811       C  
ATOM   1735  O   ILE A 300     -59.872 -13.851  26.927  1.00139.99           O  
ANISOU 1735  O   ILE A 300    18341  19383  15464   1912    554  -3157       O  
ATOM   1736  CB  ILE A 300     -62.640 -15.579  26.765  1.00138.68           C  
ANISOU 1736  CB  ILE A 300    17954  19620  15119   2065    960  -2380       C  
ATOM   1737  CG1 ILE A 300     -64.149 -15.341  26.687  1.00139.78           C  
ANISOU 1737  CG1 ILE A 300    17970  19809  15333   2209   1224  -2189       C  
ATOM   1738  CG2 ILE A 300     -62.180 -15.472  28.203  1.00141.51           C  
ANISOU 1738  CG2 ILE A 300    18485  20170  15111   2184    939  -2667       C  
ATOM   1739  CD1 ILE A 300     -64.980 -16.427  27.321  1.00140.45           C  
ANISOU 1739  CD1 ILE A 300    18002  20217  15147   2257   1354  -1913       C  
ATOM   1740  N   GLY A 301     -59.733 -15.541  25.479  1.00135.07           N  
ANISOU 1740  N   GLY A 301    17538  18811  14973   1679    450  -2640       N  
ATOM   1741  CA  GLY A 301     -58.290 -15.604  25.570  1.00134.89           C  
ANISOU 1741  CA  GLY A 301    17556  18752  14942   1561    220  -2844       C  
ATOM   1742  C   GLY A 301     -57.670 -14.350  24.992  1.00135.34           C  
ANISOU 1742  C   GLY A 301    17605  18516  15303   1474    171  -3074       C  
ATOM   1743  O   GLY A 301     -56.830 -13.719  25.630  1.00137.29           O  
ANISOU 1743  O   GLY A 301    17932  18717  15516   1466     49  -3396       O  
ATOM   1744  N   LEU A 302     -58.130 -13.972  23.800  1.00133.87           N  
ANISOU 1744  N   LEU A 302    17325  18128  15411   1403    259  -2897       N  
ATOM   1745  CA  LEU A 302     -57.678 -12.751  23.138  1.00134.47           C  
ANISOU 1745  CA  LEU A 302    17392  17898  15803   1309    235  -3049       C  
ATOM   1746  C   LEU A 302     -57.819 -11.569  24.084  1.00137.77           C  
ANISOU 1746  C   LEU A 302    17933  18209  16205   1447    276  -3384       C  
ATOM   1747  O   LEU A 302     -56.898 -10.771  24.260  1.00139.33           O  
ANISOU 1747  O   LEU A 302    18183  18241  16516   1364    151  -3668       O  
ATOM   1748  CB  LEU A 302     -58.478 -12.508  21.864  1.00132.99           C  
ANISOU 1748  CB  LEU A 302    17111  17542  15877   1264    352  -2768       C  
ATOM   1749  CG  LEU A 302     -58.328 -11.166  21.151  1.00134.03           C  
ANISOU 1749  CG  LEU A 302    17244  17335  16345   1193    365  -2853       C  
ATOM   1750  CD1 LEU A 302     -56.971 -11.039  20.519  1.00133.39           C  
ANISOU 1750  CD1 LEU A 302    17128  17139  16415    963    216  -2930       C  
ATOM   1751  CD2 LEU A 302     -59.394 -11.003  20.099  1.00133.06           C  
ANISOU 1751  CD2 LEU A 302    17044  17100  16412   1207    486  -2542       C  
ATOM   1752  N   LEU A 303     -58.990 -11.472  24.697  1.00139.11           N  
ANISOU 1752  N   LEU A 303    18142  18477  16237   1658    455  -3356       N  
ATOM   1753  CA  LEU A 303     -59.266 -10.423  25.661  1.00142.62           C  
ANISOU 1753  CA  LEU A 303    18718  18845  16626   1834    527  -3687       C  
ATOM   1754  C   LEU A 303     -58.291 -10.479  26.833  1.00144.59           C  
ANISOU 1754  C   LEU A 303    19106  19234  16600   1834    362  -4025       C  
ATOM   1755  O   LEU A 303     -57.697  -9.472  27.174  1.00146.97           O  
ANISOU 1755  O   LEU A 303    19506  19338  16997   1817    269  -4366       O  
ATOM   1756  CB  LEU A 303     -60.705 -10.526  26.171  1.00143.84           C  
ANISOU 1756  CB  LEU A 303    18862  19159  16631   2078    776  -3572       C  
ATOM   1757  CG  LEU A 303     -61.052  -9.562  27.300  1.00147.91           C  
ANISOU 1757  CG  LEU A 303    19527  19649  17021   2305    883  -3938       C  
ATOM   1758  CD1 LEU A 303     -61.051  -8.133  26.796  1.00149.54           C  
ANISOU 1758  CD1 LEU A 303    19766  19443  17610   2321    891  -4127       C  
ATOM   1759  CD2 LEU A 303     -62.385  -9.915  27.921  1.00149.24           C  
ANISOU 1759  CD2 LEU A 303    19659  20074  16970   2544   1146  -3804       C  
ATOM   1760  N   VAL A 304     -58.127 -11.651  27.442  1.00143.87           N  
ANISOU 1760  N   VAL A 304    19024  19468  16173   1847    307  -3923       N  
ATOM   1761  CA  VAL A 304     -57.247 -11.796  28.599  1.00145.98           C  
ANISOU 1761  CA  VAL A 304    19424  19906  16136   1858    128  -4210       C  
ATOM   1762  C   VAL A 304     -55.824 -11.342  28.290  1.00146.08           C  
ANISOU 1762  C   VAL A 304    19419  19729  16354   1654   -131  -4431       C  
ATOM   1763  O   VAL A 304     -55.272 -10.494  28.991  1.00149.05           O  
ANISOU 1763  O   VAL A 304    19917  20016  16700   1663   -246  -4806       O  
ATOM   1764  CB  VAL A 304     -57.202 -13.252  29.111  1.00144.90           C  
ANISOU 1764  CB  VAL A 304    19282  20125  15651   1873     76  -3986       C  
ATOM   1765  CG1 VAL A 304     -56.112 -13.406  30.167  1.00147.05           C  
ANISOU 1765  CG1 VAL A 304    19676  20554  15643   1857   -169  -4261       C  
ATOM   1766  CG2 VAL A 304     -58.540 -13.659  29.688  1.00145.79           C  
ANISOU 1766  CG2 VAL A 304    19423  20463  15505   2069    328  -3807       C  
ATOM   1767  N   GLY A 305     -55.243 -11.902  27.234  1.00143.11           N  
ANISOU 1767  N   GLY A 305    18887  19297  16192   1468   -217  -4204       N  
ATOM   1768  CA  GLY A 305     -53.900 -11.546  26.825  1.00143.19           C  
ANISOU 1768  CA  GLY A 305    18829  19151  16424   1259   -434  -4364       C  
ATOM   1769  C   GLY A 305     -53.791 -10.080  26.459  1.00144.95           C  
ANISOU 1769  C   GLY A 305    19081  19017  16976   1190   -416  -4582       C  
ATOM   1770  O   GLY A 305     -52.736  -9.480  26.629  1.00146.72           O  
ANISOU 1770  O   GLY A 305    19308  19115  17324   1052   -605  -4846       O  
ATOM   1771  N   CYS A 306     -54.877  -9.499  25.958  1.00144.75           N  
ANISOU 1771  N   CYS A 306    19070  18817  17112   1283   -202  -4462       N  
ATOM   1772  CA  CYS A 306     -54.883  -8.076  25.617  1.00146.77           C  
ANISOU 1772  CA  CYS A 306    19372  18695  17699   1240   -179  -4646       C  
ATOM   1773  C   CYS A 306     -54.957  -7.189  26.871  1.00150.89           C  
ANISOU 1773  C   CYS A 306    20092  19157  18081   1391   -209  -5075       C  
ATOM   1774  O   CYS A 306     -54.422  -6.079  26.902  1.00153.38           O  
ANISOU 1774  O   CYS A 306    20474  19172  18630   1301   -311  -5353       O  
ATOM   1775  CB  CYS A 306     -56.041  -7.753  24.672  1.00145.53           C  
ANISOU 1775  CB  CYS A 306    19162  18367  17767   1312     41  -4364       C  
ATOM   1776  SG  CYS A 306     -56.314  -5.988  24.436  1.00148.71           S  
ANISOU 1776  SG  CYS A 306    19659  18290  18554   1338     91  -4576       S  
ATOM   1777  N   ILE A 307     -55.649  -7.679  27.892  1.00151.86           N  
ANISOU 1777  N   ILE A 307    20317  19563  17820   1616   -113  -5124       N  
ATOM   1778  CA  ILE A 307     -55.737  -7.013  29.182  1.00155.98           C  
ANISOU 1778  CA  ILE A 307    21048  20106  18110   1783   -131  -5540       C  
ATOM   1779  C   ILE A 307     -54.370  -7.012  29.835  1.00157.67           C  
ANISOU 1779  C   ILE A 307    21322  20377  18206   1629   -440  -5842       C  
ATOM   1780  O   ILE A 307     -53.903  -5.987  30.331  1.00161.10           O  
ANISOU 1780  O   ILE A 307    21890  20600  18719   1603   -566  -6236       O  
ATOM   1781  CB  ILE A 307     -56.749  -7.707  30.108  1.00156.64           C  
ANISOU 1781  CB  ILE A 307    21210  20551  17757   2044     59  -5472       C  
ATOM   1782  CG1 ILE A 307     -58.173  -7.435  29.624  1.00156.20           C  
ANISOU 1782  CG1 ILE A 307    21093  20408  17847   2228    368  -5256       C  
ATOM   1783  CG2 ILE A 307     -56.573  -7.238  31.547  1.00161.06           C  
ANISOU 1783  CG2 ILE A 307    22005  21222  17970   2190     -5  -5921       C  
ATOM   1784  CD1 ILE A 307     -59.219  -8.330  30.251  1.00156.11           C  
ANISOU 1784  CD1 ILE A 307    21073  20778  17465   2434    585  -5055       C  
ATOM   1785  N   VAL A 308     -53.738  -8.180  29.834  1.00155.48           N  
ANISOU 1785  N   VAL A 308    20942  20380  17751   1529   -575  -5655       N  
ATOM   1786  CA  VAL A 308     -52.374  -8.322  30.317  1.00156.78           C  
ANISOU 1786  CA  VAL A 308    21104  20624  17842   1369   -894  -5877       C  
ATOM   1787  C   VAL A 308     -51.454  -7.398  29.530  1.00157.26           C  
ANISOU 1787  C   VAL A 308    21066  20323  18363   1117  -1038  -6006       C  
ATOM   1788  O   VAL A 308     -50.563  -6.763  30.092  1.00160.32           O  
ANISOU 1788  O   VAL A 308    21516  20616  18783   1010  -1273  -6359       O  
ATOM   1789  CB  VAL A 308     -51.878  -9.775  30.174  1.00153.97           C  
ANISOU 1789  CB  VAL A 308    20606  20580  17315   1307   -998  -5582       C  
ATOM   1790  CG1 VAL A 308     -50.431  -9.894  30.633  1.00155.59           C  
ANISOU 1790  CG1 VAL A 308    20769  20862  17485   1150  -1344  -5803       C  
ATOM   1791  CG2 VAL A 308     -52.767 -10.718  30.965  1.00153.79           C  
ANISOU 1791  CG2 VAL A 308    20684  20905  16844   1529   -864  -5421       C  
ATOM   1792  N   ALA A 309     -51.701  -7.310  28.227  1.00154.51           N  
ANISOU 1792  N   ALA A 309    20566  19775  18367   1014   -896  -5710       N  
ATOM   1793  CA  ALA A 309     -50.918  -6.450  27.354  1.00154.95           C  
ANISOU 1793  CA  ALA A 309    20516  19487  18870    761   -988  -5759       C  
ATOM   1794  C   ALA A 309     -51.036  -4.999  27.792  1.00158.93           C  
ANISOU 1794  C   ALA A 309    21195  19646  19544    780  -1015  -6128       C  
ATOM   1795  O   ALA A 309     -50.041  -4.280  27.859  1.00161.33           O  
ANISOU 1795  O   ALA A 309    21489  19747  20063    575  -1226  -6379       O  
ATOM   1796  CB  ALA A 309     -51.361  -6.609  25.909  1.00151.61           C  
ANISOU 1796  CB  ALA A 309    19940  18935  18732    682   -799  -5353       C  
ATOM   1797  N   ALA A 310     -52.253  -4.577  28.113  1.00159.93           N  
ANISOU 1797  N   ALA A 310    21478  19703  19585   1030   -803  -6168       N  
ATOM   1798  CA  ALA A 310     -52.476  -3.226  28.606  1.00164.09           C  
ANISOU 1798  CA  ALA A 310    22199  19892  20254   1103   -811  -6545       C  
ATOM   1799  C   ALA A 310     -51.781  -3.039  29.952  1.00167.85           C  
ANISOU 1799  C   ALA A 310    22845  20487  20442   1117  -1048  -7010       C  
ATOM   1800  O   ALA A 310     -51.265  -1.962  30.248  1.00171.51           O  
ANISOU 1800  O   ALA A 310    23424  20642  21101   1018  -1208  -7374       O  
ATOM   1801  CB  ALA A 310     -53.963  -2.939  28.720  1.00164.52           C  
ANISOU 1801  CB  ALA A 310    22361  19901  20249   1411   -516  -6484       C  
ATOM   1802  N   ALA A 311     -51.752  -4.106  30.749  1.00167.14           N  
ANISOU 1802  N   ALA A 311    22776  20841  19889   1227  -1089  -6985       N  
ATOM   1803  CA  ALA A 311     -51.105  -4.091  32.059  1.00170.70           C  
ANISOU 1803  CA  ALA A 311    23391  21477  19989   1250  -1334  -7386       C  
ATOM   1804  C   ALA A 311     -49.599  -3.844  31.945  1.00171.90           C  
ANISOU 1804  C   ALA A 311    23434  21517  20363    932  -1688  -7558       C  
ATOM   1805  O   ALA A 311     -49.031  -3.070  32.716  1.00176.14           O  
ANISOU 1805  O   ALA A 311    24122  21928  20875    874  -1914  -7995       O  
ATOM   1806  CB  ALA A 311     -51.377  -5.400  32.801  1.00169.42           C  
ANISOU 1806  CB  ALA A 311    23250  21824  19298   1415  -1304  -7227       C  
ATOM   1807  N   CYS A 312     -48.955  -4.514  30.992  1.00168.46           N  
ANISOU 1807  N   CYS A 312    22728  21137  20142    729  -1737  -7222       N  
ATOM   1808  CA  CYS A 312     -47.529  -4.308  30.748  1.00169.54           C  
ANISOU 1808  CA  CYS A 312    22697  21178  20543    417  -2039  -7335       C  
ATOM   1809  C   CYS A 312     -47.303  -2.894  30.234  1.00171.98           C  
ANISOU 1809  C   CYS A 312    23029  20987  21330    231  -2065  -7523       C  
ATOM   1810  O   CYS A 312     -46.280  -2.271  30.511  1.00175.18           O  
ANISOU 1810  O   CYS A 312    23411  21238  21909      8  -2345  -7814       O  
ATOM   1811  CB  CYS A 312     -46.982  -5.319  29.734  1.00167.78           C  
ANISOU 1811  CB  CYS A 312    22169  21117  20464    268  -2024  -6919       C  
ATOM   1812  SG  CYS A 312     -47.046  -7.054  30.228  1.00165.09           S  
ANISOU 1812  SG  CYS A 312    21774  21314  19640    444  -2044  -6669       S  
ATOM   1813  N   GLY A 313     -48.282  -2.393  29.493  1.00170.72           N  
ANISOU 1813  N   GLY A 313    22912  20564  21389    320  -1785  -7343       N  
ATOM   1814  CA  GLY A 313     -48.250  -1.037  28.985  1.00173.16           C  
ANISOU 1814  CA  GLY A 313    23274  20363  22156    179  -1780  -7477       C  
ATOM   1815  C   GLY A 313     -48.278  -1.044  27.469  1.00169.96           C  
ANISOU 1815  C   GLY A 313    22652  19779  22146      8  -1618  -7038       C  
ATOM   1816  O   GLY A 313     -47.929  -0.058  26.819  1.00171.65           O  
ANISOU 1816  O   GLY A 313    22837  19588  22796   -206  -1652  -7053       O  
ATOM   1817  N   TYR A 314     -48.721  -2.161  26.905  1.00171.90           N  
ANISOU 1817  N   TYR A 314    22761  20325  22228    101  -1441  -6639       N  
ATOM   1818  CA  TYR A 314     -48.797  -2.303  25.461  1.00168.80           C  
ANISOU 1818  CA  TYR A 314    22178  19823  22135    -42  -1281  -6211       C  
ATOM   1819  C   TYR A 314     -50.147  -1.790  24.994  1.00168.25           C  
ANISOU 1819  C   TYR A 314    22228  19528  22173    153  -1020  -6044       C  
ATOM   1820  O   TYR A 314     -51.095  -2.556  24.801  1.00165.37           O  
ANISOU 1820  O   TYR A 314    21850  19384  21600    357   -825  -5780       O  
ATOM   1821  CB  TYR A 314     -48.598  -3.760  25.047  1.00167.68           C  
ANISOU 1821  CB  TYR A 314    21841  20092  21777    -42  -1238  -5884       C  
ATOM   1822  CG  TYR A 314     -47.178  -4.239  25.197  1.00168.12           C  
ANISOU 1822  CG  TYR A 314    21711  20329  21836   -261  -1484  -5973       C  
ATOM   1823  CD1 TYR A 314     -46.673  -4.577  26.443  1.00170.07           C  
ANISOU 1823  CD1 TYR A 314    22023  20811  21784   -194  -1711  -6276       C  
ATOM   1824  CD2 TYR A 314     -46.347  -4.370  24.093  1.00166.85           C  
ANISOU 1824  CD2 TYR A 314    21301  20126  21967   -525  -1485  -5746       C  
ATOM   1825  CE1 TYR A 314     -45.379  -5.018  26.592  1.00170.75           C  
ANISOU 1825  CE1 TYR A 314    21915  21070  21893   -379  -1956  -6349       C  
ATOM   1826  CE2 TYR A 314     -45.050  -4.814  24.229  1.00167.54           C  
ANISOU 1826  CE2 TYR A 314    21183  20394  22082   -707  -1698  -5827       C  
ATOM   1827  CZ  TYR A 314     -44.569  -5.136  25.482  1.00169.48           C  
ANISOU 1827  CZ  TYR A 314    21481  20858  22057   -631  -1944  -6127       C  
ATOM   1828  OH  TYR A 314     -43.271  -5.580  25.630  1.00170.46           O  
ANISOU 1828  OH  TYR A 314    21374  21166  22226   -800  -2179  -6200       O  
ATOM   1829  N   PHE A 315     -50.230  -0.478  24.833  1.00170.77           N  
ANISOU 1829  N   PHE A 315    22657  19393  22836     90  -1033  -6201       N  
ATOM   1830  CA  PHE A 315     -51.462   0.155  24.403  1.00170.99           C  
ANISOU 1830  CA  PHE A 315    22793  19154  23023    284   -814  -6064       C  
ATOM   1831  C   PHE A 315     -51.125   1.466  23.719  1.00173.75           C  
ANISOU 1831  C   PHE A 315    23170  18970  23877     69   -869  -6085       C  
ATOM   1832  O   PHE A 315     -50.077   2.053  23.977  1.00176.58           O  
ANISOU 1832  O   PHE A 315    23533  19143  24415   -174  -1085  -6343       O  
ATOM   1833  CB  PHE A 315     -52.401   0.391  25.593  1.00167.56           C  
ANISOU 1833  CB  PHE A 315    22586  18762  22316    637   -738  -6377       C  
ATOM   1834  CG  PHE A 315     -51.826   1.293  26.660  1.00172.43           C  
ANISOU 1834  CG  PHE A 315    23400  19172  22945    613   -945  -6916       C  
ATOM   1835  CD1 PHE A 315     -52.009   2.668  26.599  1.00176.30           C  
ANISOU 1835  CD1 PHE A 315    24046  19139  23800    611   -963  -7131       C  
ATOM   1836  CD2 PHE A 315     -51.125   0.765  27.733  1.00173.46           C  
ANISOU 1836  CD2 PHE A 315    23573  19617  22717    599  -1139  -7211       C  
ATOM   1837  CE1 PHE A 315     -51.490   3.497  27.575  1.00181.09           C  
ANISOU 1837  CE1 PHE A 315    24852  19533  24420    583  -1169  -7653       C  
ATOM   1838  CE2 PHE A 315     -50.604   1.595  28.715  1.00178.25           C  
ANISOU 1838  CE2 PHE A 315    24375  20039  23313    570  -1354  -7725       C  
ATOM   1839  CZ  PHE A 315     -50.788   2.961  28.634  1.00182.07           C  
ANISOU 1839  CZ  PHE A 315    25019  19994  24166    557  -1368  -7958       C  
ATOM   1840  N   SER A 316     -52.016   1.929  22.854  1.00171.20           N  
ANISOU 1840  N   SER A 316    22862  18395  23792    151   -687  -5801       N  
ATOM   1841  CA  SER A 316     -51.854   3.231  22.228  1.00174.23           C  
ANISOU 1841  CA  SER A 316    23306  18233  24662    -17   -728  -5792       C  
ATOM   1842  C   SER A 316     -53.109   4.066  22.435  1.00176.53           C  
ANISOU 1842  C   SER A 316    23789  18209  25075    300   -592  -5869       C  
ATOM   1843  O   SER A 316     -53.936   4.183  21.533  1.00175.24           O  
ANISOU 1843  O   SER A 316    23583  17924  25074    387   -431  -5504       O  
ATOM   1844  CB  SER A 316     -51.547   3.079  20.738  1.00174.50           C  
ANISOU 1844  CB  SER A 316    23148  18215  24940   -282   -663  -5304       C  
ATOM   1845  OG  SER A 316     -51.401   4.346  20.121  1.00177.71           O  
ANISOU 1845  OG  SER A 316    23620  18085  25816   -457   -701  -5254       O  
ATOM   1846  N   HIS A 317     -53.251   4.646  23.622  1.00176.51           N  
ANISOU 1846  N   HIS A 317    23995  18080  24990    484   -660  -6352       N  
ATOM   1847  CA  HIS A 317     -54.461   5.392  23.945  1.00179.08           C  
ANISOU 1847  CA  HIS A 317    24500  18140  25404    838   -511  -6477       C  
ATOM   1848  C   HIS A 317     -54.601   6.646  23.081  1.00181.80           C  
ANISOU 1848  C   HIS A 317    24904  17869  26302    740   -523  -6346       C  
ATOM   1849  O   HIS A 317     -55.690   7.203  22.968  1.00183.31           O  
ANISOU 1849  O   HIS A 317    25182  17820  26646   1027   -376  -6294       O  
ATOM   1850  CB  HIS A 317     -54.495   5.766  25.435  1.00183.01           C  
ANISOU 1850  CB  HIS A 317    25231  18636  25669   1051   -584  -7070       C  
ATOM   1851  CG  HIS A 317     -53.408   6.702  25.862  1.00187.33           C  
ANISOU 1851  CG  HIS A 317    25913  18813  26449    795   -859  -7481       C  
ATOM   1852  ND1 HIS A 317     -52.085   6.319  25.968  1.00186.77           N  
ANISOU 1852  ND1 HIS A 317    25738  18910  26318    445  -1094  -7559       N  
ATOM   1853  CD2 HIS A 317     -53.446   8.007  26.224  1.00192.60           C  
ANISOU 1853  CD2 HIS A 317    26809  18941  27428    836   -949  -7848       C  
ATOM   1854  CE1 HIS A 317     -51.362   7.346  26.371  1.00191.48           C  
ANISOU 1854  CE1 HIS A 317    26479  19097  27177    262  -1324  -7945       C  
ATOM   1855  NE2 HIS A 317     -52.163   8.385  26.532  1.00195.09           N  
ANISOU 1855  NE2 HIS A 317    27156  19107  27864    490  -1244  -8134       N  
ATOM   1856  N   ALA A 318     -53.511   7.065  22.444  1.00182.57           N  
ANISOU 1856  N   ALA A 318    24937  17722  26709    336   -693  -6261       N  
ATOM   1857  CA  ALA A 318     -53.535   8.251  21.592  1.00185.43           C  
ANISOU 1857  CA  ALA A 318    25359  17488  27607    194   -722  -6097       C  
ATOM   1858  C   ALA A 318     -54.429   8.060  20.365  1.00182.70           C  
ANISOU 1858  C   ALA A 318    24899  17138  27381    280   -528  -5529       C  
ATOM   1859  O   ALA A 318     -55.303   8.885  20.099  1.00185.07           O  
ANISOU 1859  O   ALA A 318    25310  17048  27960    484   -454  -5453       O  
ATOM   1860  CB  ALA A 318     -52.121   8.620  21.163  1.00186.78           C  
ANISOU 1860  CB  ALA A 318    25450  17465  28052   -294   -930  -6087       C  
ATOM   1861  N   ASP A 319     -54.205   6.983  19.616  1.00178.21           N  
ANISOU 1861  N   ASP A 319    24113  16993  26605    131   -461  -5138       N  
ATOM   1862  CA  ASP A 319     -55.016   6.685  18.432  1.00175.53           C  
ANISOU 1862  CA  ASP A 319    23663  16707  26322    192   -301  -4598       C  
ATOM   1863  C   ASP A 319     -56.425   6.203  18.779  1.00174.03           C  
ANISOU 1863  C   ASP A 319    23480  16749  25893    631   -120  -4550       C  
ATOM   1864  O   ASP A 319     -57.359   6.365  17.988  1.00173.58           O  
ANISOU 1864  O   ASP A 319    23389  16580  25984    768    -11  -4192       O  
ATOM   1865  CB  ASP A 319     -54.313   5.653  17.557  1.00175.21           C  
ANISOU 1865  CB  ASP A 319    23403  17056  26111    -99   -288  -4240       C  
ATOM   1866  CG  ASP A 319     -53.198   6.261  16.742  1.00176.87           C  
ANISOU 1866  CG  ASP A 319    23563  16986  26655   -529   -396  -4092       C  
ATOM   1867  OD1 ASP A 319     -53.437   7.309  16.102  1.00179.73           O  
ANISOU 1867  OD1 ASP A 319    24014  16870  27407   -593   -403  -3916       O  
ATOM   1868  OD2 ASP A 319     -52.083   5.699  16.752  1.00175.62           O  
ANISOU 1868  OD2 ASP A 319    23267  17081  26378   -801   -472  -4142       O  
ATOM   1869  N   ILE A 320     -56.562   5.587  19.950  1.00174.02           N  
ANISOU 1869  N   ILE A 320    23513  17091  25517    837    -94  -4890       N  
ATOM   1870  CA  ILE A 320     -57.868   5.203  20.471  1.00173.43           C  
ANISOU 1870  CA  ILE A 320    23445  17236  25214   1256     90  -4904       C  
ATOM   1871  C   ILE A 320     -58.709   6.450  20.707  1.00177.96           C  
ANISOU 1871  C   ILE A 320    24181  17324  26113   1536    142  -5072       C  
ATOM   1872  O   ILE A 320     -59.880   6.507  20.332  1.00177.84           O  
ANISOU 1872  O   ILE A 320    24111  17282  26177   1804    294  -4827       O  
ATOM   1873  CB  ILE A 320     -57.754   4.407  21.788  1.00174.56           C  
ANISOU 1873  CB  ILE A 320    23624  17818  24884   1404    103  -5268       C  
ATOM   1874  CG1 ILE A 320     -57.141   3.033  21.531  1.00169.90           C  
ANISOU 1874  CG1 ILE A 320    22857  17732  23965   1199     74  -5047       C  
ATOM   1875  CG2 ILE A 320     -59.119   4.230  22.428  1.00175.15           C  
ANISOU 1875  CG2 ILE A 320    23723  18061  24764   1843    314  -5327       C  
ATOM   1876  CD1 ILE A 320     -56.833   2.267  22.795  1.00169.56           C  
ANISOU 1876  CD1 ILE A 320    22857  18095  23473   1291     40  -5381       C  
ATOM   1877  N   ASP A 321     -58.105   7.447  21.344  1.00181.50           N  
ANISOU 1877  N   ASP A 321    24823  17381  26759   1478      4  -5502       N  
ATOM   1878  CA  ASP A 321     -58.787   8.709  21.569  1.00186.40           C  
ANISOU 1878  CA  ASP A 321    25622  17470  27732   1734     31  -5703       C  
ATOM   1879  C   ASP A 321     -59.064   9.440  20.252  1.00187.18           C  
ANISOU 1879  C   ASP A 321    25682  17124  28313   1631     18  -5257       C  
ATOM   1880  O   ASP A 321     -60.110  10.070  20.089  1.00189.51           O  
ANISOU 1880  O   ASP A 321    26020  17137  28847   1940    118  -5177       O  
ATOM   1881  CB  ASP A 321     -57.966   9.598  22.510  1.00191.06           C  
ANISOU 1881  CB  ASP A 321    26447  17714  28435   1648   -150  -6280       C  
ATOM   1882  CG  ASP A 321     -57.740   8.956  23.870  1.00191.00           C  
ANISOU 1882  CG  ASP A 321    26510  18136  27927   1774   -154  -6739       C  
ATOM   1883  OD1 ASP A 321     -58.455   7.985  24.203  1.00188.17           O  
ANISOU 1883  OD1 ASP A 321    26048  18277  27169   2016     28  -6641       O  
ATOM   1884  OD2 ASP A 321     -56.850   9.429  24.609  1.00194.07           O  
ANISOU 1884  OD2 ASP A 321    27058  18358  28321   1621   -349  -7188       O  
ATOM   1885  N   ALA A 322     -58.127   9.336  19.313  1.00185.44           N  
ANISOU 1885  N   ALA A 322    25372  16861  28225   1205   -102  -4954       N  
ATOM   1886  CA  ALA A 322     -58.199  10.066  18.047  1.00186.60           C  
ANISOU 1886  CA  ALA A 322    25506  16581  28811   1040   -139  -4520       C  
ATOM   1887  C   ALA A 322     -59.222   9.491  17.066  1.00183.48           C  
ANISOU 1887  C   ALA A 322    24946  16412  28356   1188      7  -3976       C  
ATOM   1888  O   ALA A 322     -59.477  10.078  16.013  1.00184.63           O  
ANISOU 1888  O   ALA A 322    25088  16230  28834   1111    -17  -3582       O  
ATOM   1889  CB  ALA A 322     -56.824  10.107  17.393  1.00186.06           C  
ANISOU 1889  CB  ALA A 322    25385  16443  28867    523   -289  -4377       C  
ATOM   1890  N   ALA A 323     -59.798   8.343  17.403  1.00179.79           N  
ANISOU 1890  N   ALA A 323    24346  16501  27467   1386    141  -3942       N  
ATOM   1891  CA  ALA A 323     -60.755   7.689  16.517  1.00176.80           C  
ANISOU 1891  CA  ALA A 323    23795  16379  27002   1505    257  -3445       C  
ATOM   1892  C   ALA A 323     -62.153   8.269  16.684  1.00179.50           C  
ANISOU 1892  C   ALA A 323    24156  16510  27536   1948    367  -3425       C  
ATOM   1893  O   ALA A 323     -62.520   8.708  17.774  1.00182.43           O  
ANISOU 1893  O   ALA A 323    24637  16769  27908   2244    426  -3857       O  
ATOM   1894  CB  ALA A 323     -60.772   6.191  16.773  1.00171.96           C  
ANISOU 1894  CB  ALA A 323    23024  16428  25886   1505    341  -3397       C  
ATOM   1895  N   PRO A 324     -62.942   8.263  15.599  1.00178.78           N  
ANISOU 1895  N   PRO A 324    23951  16378  27600   2003    394  -2923       N  
ATOM   1896  CA  PRO A 324     -64.325   8.745  15.673  1.00181.34           C  
ANISOU 1896  CA  PRO A 324    24240  16537  28124   2436    494  -2850       C  
ATOM   1897  C   PRO A 324     -65.234   7.741  16.362  1.00179.09           C  
ANISOU 1897  C   PRO A 324    23794  16786  27466   2741    674  -2921       C  
ATOM   1898  O   PRO A 324     -64.987   6.542  16.281  1.00174.72           O  
ANISOU 1898  O   PRO A 324    23119  16736  26532   2579    701  -2798       O  
ATOM   1899  CB  PRO A 324     -64.714   8.913  14.202  1.00180.91           C  
ANISOU 1899  CB  PRO A 324    24096  16335  28305   2322    424  -2244       C  
ATOM   1900  CG  PRO A 324     -63.871   7.914  13.485  1.00176.32           C  
ANISOU 1900  CG  PRO A 324    23430  16139  27426   1914    374  -1984       C  
ATOM   1901  CD  PRO A 324     -62.560   7.891  14.225  1.00176.13           C  
ANISOU 1901  CD  PRO A 324    23520  16124  27278   1663    321  -2404       C  
ATOM   1902  N   ALA A 325     -66.266   8.226  17.040  1.00182.34           N  
ANISOU 1902  N   ALA A 325    24203  17081  27995   3177    804  -3118       N  
ATOM   1903  CA  ALA A 325     -67.203   7.346  17.721  1.00180.88           C  
ANISOU 1903  CA  ALA A 325    23849  17394  27483   3478   1001  -3171       C  
ATOM   1904  C   ALA A 325     -68.460   7.213  16.873  1.00180.70           C  
ANISOU 1904  C   ALA A 325    23599  17432  27625   3678   1055  -2687       C  
ATOM   1905  O   ALA A 325     -69.577   7.350  17.369  1.00182.99           O  
ANISOU 1905  O   ALA A 325    23777  17779  27971   4083   1218  -2755       O  
ATOM   1906  CB  ALA A 325     -67.534   7.870  19.104  1.00184.79           C  
ANISOU 1906  CB  ALA A 325    24464  17805  27942   3842   1143  -3725       C  
ATOM   1907  N   ALA A 326     -68.257   6.979  15.579  1.00178.33           N  
ANISOU 1907  N   ALA A 326    23231  17119  27408   3391    915  -2201       N  
ATOM   1908  CA  ALA A 326     -69.351   6.787  14.636  1.00177.98           C  
ANISOU 1908  CA  ALA A 326    22974  17153  27497   3516    910  -1698       C  
ATOM   1909  C   ALA A 326     -68.859   6.009  13.418  1.00173.87           C  
ANISOU 1909  C   ALA A 326    22392  16852  26818   3112    773  -1246       C  
ATOM   1910  O   ALA A 326     -67.681   6.068  13.076  1.00172.64           O  
ANISOU 1910  O   ALA A 326    22381  16592  26623   2755    664  -1269       O  
ATOM   1911  CB  ALA A 326     -69.935   8.129  14.213  1.00182.92           C  
ANISOU 1911  CB  ALA A 326    23651  17199  28649   3747    849  -1586       C  
ATOM   1912  N   SER A 327     -69.758   5.287  12.760  1.00172.05           N  
ANISOU 1912  N   SER A 327    21942  16930  26498   3168    778   -842       N  
ATOM   1913  CA  SER A 327     -69.401   4.595  11.529  1.00168.72           C  
ANISOU 1913  CA  SER A 327    21476  16699  25929   2814    642   -408       C  
ATOM   1914  C   SER A 327     -70.610   4.272  10.659  1.00168.68           C  
ANISOU 1914  C   SER A 327    21254  16845  25991   2939    593     69       C  
ATOM   1915  O   SER A 327     -71.470   3.468  11.029  1.00167.46           O  
ANISOU 1915  O   SER A 327    20894  17072  25663   3117    690    102       O  
ATOM   1916  CB  SER A 327     -68.644   3.310  11.837  1.00164.14           C  
ANISOU 1916  CB  SER A 327    20882  16596  24886   2561    680   -535       C  
ATOM   1917  OG  SER A 327     -68.317   2.637  10.634  1.00161.24           O  
ANISOU 1917  OG  SER A 327    20482  16411  24372   2241    561   -142       O  
ATOM   1918  N   PHE A 328     -70.652   4.907   9.493  1.00170.27           N  
ANISOU 1918  N   PHE A 328    21502  16748  26444   2828    430    452       N  
ATOM   1919  CA  PHE A 328     -71.648   4.611   8.476  1.00170.30           C  
ANISOU 1919  CA  PHE A 328    21325  16887  26496   2876    322    951       C  
ATOM   1920  C   PHE A 328     -70.980   3.731   7.429  1.00166.61           C  
ANISOU 1920  C   PHE A 328    20896  16696  25713   2456    205   1244       C  
ATOM   1921  O   PHE A 328     -69.756   3.675   7.350  1.00165.03           O  
ANISOU 1921  O   PHE A 328    20870  16459  25376   2152    198   1109       O  
ATOM   1922  CB  PHE A 328     -72.211   5.894   7.839  1.00175.00           C  
ANISOU 1922  CB  PHE A 328    21952  16976  27565   3054    200   1218       C  
ATOM   1923  CG  PHE A 328     -73.001   6.772   8.793  1.00179.20           C  
ANISOU 1923  CG  PHE A 328    22426  17221  28440   3520    317    945       C  
ATOM   1924  CD1 PHE A 328     -72.372   7.757   9.545  1.00181.90           C  
ANISOU 1924  CD1 PHE A 328    22984  17130  28999   3596    377    539       C  
ATOM   1925  CD2 PHE A 328     -74.372   6.608   8.933  1.00180.74           C  
ANISOU 1925  CD2 PHE A 328    22345  17582  28746   3881    368   1085       C  
ATOM   1926  CE1 PHE A 328     -73.093   8.554  10.413  1.00186.06           C  
ANISOU 1926  CE1 PHE A 328    23477  17391  29827   4041    493    258       C  
ATOM   1927  CE2 PHE A 328     -75.097   7.402   9.801  1.00184.89           C  
ANISOU 1927  CE2 PHE A 328    22805  17863  29582   4332    502    822       C  
ATOM   1928  CZ  PHE A 328     -74.457   8.374  10.541  1.00187.57           C  
ANISOU 1928  CZ  PHE A 328    23386  17765  30115   4420    569    397       C  
ATOM   1929  N   ILE A 329     -71.788   3.046   6.630  1.00165.53           N  
ANISOU 1929  N   ILE A 329    20589  16839  25466   2443    110   1633       N  
ATOM   1930  CA  ILE A 329     -71.286   2.040   5.699  1.00162.05           C  
ANISOU 1930  CA  ILE A 329    20172  16724  24674   2081     14   1874       C  
ATOM   1931  C   ILE A 329     -70.275   2.610   4.705  1.00162.66           C  
ANISOU 1931  C   ILE A 329    20473  16544  24789   1757    -97   2062       C  
ATOM   1932  O   ILE A 329     -69.336   1.925   4.309  1.00159.82           O  
ANISOU 1932  O   ILE A 329    20201  16397  24127   1434    -98   2054       O  
ATOM   1933  CB  ILE A 329     -72.444   1.389   4.918  1.00161.81           C  
ANISOU 1933  CB  ILE A 329    19934  16970  24576   2137   -112   2285       C  
ATOM   1934  CG1 ILE A 329     -73.412   0.690   5.872  1.00161.11           C  
ANISOU 1934  CG1 ILE A 329    19596  17192  24426   2408     13   2129       C  
ATOM   1935  CG2 ILE A 329     -71.921   0.397   3.898  1.00158.70           C  
ANISOU 1935  CG2 ILE A 329    19600  16883  23814   1766   -224   2515       C  
ATOM   1936  CD1 ILE A 329     -74.657   0.160   5.186  1.00161.62           C  
ANISOU 1936  CD1 ILE A 329    19416  17495  24499   2486   -123   2526       C  
ATOM   1937  N   TRP A 330     -70.461   3.858   4.294  1.00166.65           N  
ANISOU 1937  N   TRP A 330    21062  16589  25670   1846   -184   2242       N  
ATOM   1938  CA  TRP A 330     -69.529   4.456   3.344  1.00167.77           C  
ANISOU 1938  CA  TRP A 330    21412  16472  25861   1528   -278   2460       C  
ATOM   1939  C   TRP A 330     -68.838   5.707   3.868  1.00170.83           C  
ANISOU 1939  C   TRP A 330    21975  16338  26594   1542   -236   2219       C  
ATOM   1940  O   TRP A 330     -68.748   6.707   3.156  1.00174.23           O  
ANISOU 1940  O   TRP A 330    22530  16364  27307   1477   -347   2495       O  
ATOM   1941  CB  TRP A 330     -70.227   4.768   2.022  1.00170.03           C  
ANISOU 1941  CB  TRP A 330    21687  16676  26242   1505   -477   3023       C  
ATOM   1942  CG  TRP A 330     -70.636   3.534   1.303  1.00167.14           C  
ANISOU 1942  CG  TRP A 330    21204  16808  25493   1379   -554   3271       C  
ATOM   1943  CD1 TRP A 330     -69.862   2.778   0.481  1.00164.63           C  
ANISOU 1943  CD1 TRP A 330    20984  16768  24801   1016   -582   3402       C  
ATOM   1944  CD2 TRP A 330     -71.927   2.913   1.329  1.00166.82           C  
ANISOU 1944  CD2 TRP A 330    20926  17041  25416   1612   -619   3410       C  
ATOM   1945  NE1 TRP A 330     -70.583   1.715  -0.001  1.00162.74           N  
ANISOU 1945  NE1 TRP A 330    20607  16940  24286   1008   -673   3593       N  
ATOM   1946  CE2 TRP A 330     -71.857   1.776   0.501  1.00164.02           C  
ANISOU 1946  CE2 TRP A 330    20556  17108  24658   1357   -706   3614       C  
ATOM   1947  CE3 TRP A 330     -73.136   3.209   1.970  1.00168.91           C  
ANISOU 1947  CE3 TRP A 330    20978  17239  25962   2013   -607   3378       C  
ATOM   1948  CZ2 TRP A 330     -72.949   0.930   0.297  1.00163.24           C  
ANISOU 1948  CZ2 TRP A 330    20241  17346  24435   1463   -805   3791       C  
ATOM   1949  CZ3 TRP A 330     -74.220   2.368   1.769  1.00168.12           C  
ANISOU 1949  CZ3 TRP A 330    20635  17499  25744   2122   -686   3571       C  
ATOM   1950  CH2 TRP A 330     -74.118   1.240   0.937  1.00165.29           C  
ANISOU 1950  CH2 TRP A 330    20272  17541  24989   1834   -797   3777       C  
ATOM   1951  N   VAL A 331     -68.367   5.656   5.112  1.00169.92           N  
ANISOU 1951  N   VAL A 331    21878  16225  26459   1623    -91   1711       N  
ATOM   1952  CA  VAL A 331     -67.530   6.728   5.640  1.00172.59           C  
ANISOU 1952  CA  VAL A 331    22400  16097  27079   1571    -66   1426       C  
ATOM   1953  C   VAL A 331     -66.303   6.883   4.743  1.00172.31           C  
ANISOU 1953  C   VAL A 331    22516  15973  26981   1119   -127   1618       C  
ATOM   1954  O   VAL A 331     -65.913   7.998   4.393  1.00175.90           O  
ANISOU 1954  O   VAL A 331    23121  15948  27764   1018   -197   1730       O  
ATOM   1955  CB  VAL A 331     -67.079   6.457   7.088  1.00171.25           C  
ANISOU 1955  CB  VAL A 331    22236  16036  26797   1670     81    837       C  
ATOM   1956  CG1 VAL A 331     -66.106   7.526   7.552  1.00174.11           C  
ANISOU 1956  CG1 VAL A 331    22799  15923  27433   1555     71    542       C  
ATOM   1957  CG2 VAL A 331     -68.273   6.402   8.009  1.00172.20           C  
ANISOU 1957  CG2 VAL A 331    22214  16232  26983   2122    175    642       C  
ATOM   1958  N   LYS A 332     -65.716   5.749   4.360  1.00168.31           N  
ANISOU 1958  N   LYS A 332    21963  15930  26058    852    -92   1664       N  
ATOM   1959  CA  LYS A 332     -64.601   5.712   3.416  1.00167.86           C  
ANISOU 1959  CA  LYS A 332    22010  15894  25876    426   -117   1875       C  
ATOM   1960  C   LYS A 332     -64.967   4.837   2.213  1.00165.88           C  
ANISOU 1960  C   LYS A 332    21699  16025  25302    295   -178   2307       C  
ATOM   1961  O   LYS A 332     -65.668   3.839   2.360  1.00163.17           O  
ANISOU 1961  O   LYS A 332    21219  16067  24711    440   -169   2292       O  
ATOM   1962  CB  LYS A 332     -63.337   5.179   4.092  1.00165.33           C  
ANISOU 1962  CB  LYS A 332    21701  15767  25351    205    -10   1471       C  
ATOM   1963  CG  LYS A 332     -63.007   5.838   5.424  1.00166.93           C  
ANISOU 1963  CG  LYS A 332    21956  15681  25791    347     35    975       C  
ATOM   1964  CD  LYS A 332     -62.579   7.282   5.239  1.00171.57           C  
ANISOU 1964  CD  LYS A 332    22702  15668  26817    243    -34   1027       C  
ATOM   1965  CE  LYS A 332     -62.120   7.891   6.552  1.00173.30           C  
ANISOU 1965  CE  LYS A 332    22995  15607  27242    340     -7    490       C  
ATOM   1966  NZ  LYS A 332     -61.703   9.308   6.371  1.00178.16           N  
ANISOU 1966  NZ  LYS A 332    23778  15595  28319    224    -92    533       N  
ATOM   1967  N   THR A 333     -64.462   5.183   1.032  1.00167.40           N  
ANISOU 1967  N   THR A 333    22002  16122  25481      3   -238   2685       N  
ATOM   1968  CA  THR A 333     -64.823   4.453  -0.185  1.00166.23           C  
ANISOU 1968  CA  THR A 333    21833  16311  25015   -124   -313   3103       C  
ATOM   1969  C   THR A 333     -63.623   4.065  -1.030  1.00165.25           C  
ANISOU 1969  C   THR A 333    21795  16387  24604   -537   -250   3224       C  
ATOM   1970  O   THR A 333     -62.524   4.572  -0.832  1.00166.24           O  
ANISOU 1970  O   THR A 333    21993  16322  24849   -751   -167   3074       O  
ATOM   1971  CB  THR A 333     -65.772   5.271  -1.074  1.00170.02           C  
ANISOU 1971  CB  THR A 333    22360  16516  25723    -13   -485   3592       C  
ATOM   1972  OG1 THR A 333     -65.144   6.509  -1.431  1.00173.93           O  
ANISOU 1972  OG1 THR A 333    23021  16533  26530   -179   -508   3753       O  
ATOM   1973  CG2 THR A 333     -67.088   5.543  -0.351  1.00171.14           C  
ANISOU 1973  CG2 THR A 333    22371  16521  26134    427   -544   3512       C  
ATOM   1974  N   PHE A 334     -63.854   3.170  -1.986  1.00163.62           N  
ANISOU 1974  N   PHE A 334    21575  16570  24024   -648   -292   3492       N  
ATOM   1975  CA  PHE A 334     -62.779   2.588  -2.787  1.00162.45           C  
ANISOU 1975  CA  PHE A 334    21490  16703  23532  -1006   -204   3572       C  
ATOM   1976  C   PHE A 334     -63.142   2.551  -4.276  1.00164.24           C  
ANISOU 1976  C   PHE A 334    21815  17047  23542  -1152   -313   4097       C  
ATOM   1977  O   PHE A 334     -64.319   2.617  -4.628  1.00165.30           O  
ANISOU 1977  O   PHE A 334    21929  17163  23713   -959   -480   4361       O  
ATOM   1978  CB  PHE A 334     -62.441   1.183  -2.268  1.00157.92           C  
ANISOU 1978  CB  PHE A 334    20806  16591  22605  -1008   -104   3221       C  
ATOM   1979  CG  PHE A 334     -61.869   1.179  -0.886  1.00156.39           C  
ANISOU 1979  CG  PHE A 334    20538  16323  22558   -922      4   2721       C  
ATOM   1980  CD1 PHE A 334     -62.666   0.918   0.211  1.00154.93           C  
ANISOU 1980  CD1 PHE A 334    20250  16157  22459   -606    -13   2453       C  
ATOM   1981  CD2 PHE A 334     -60.535   1.448  -0.684  1.00156.74           C  
ANISOU 1981  CD2 PHE A 334    20611  16293  22650  -1163    119   2528       C  
ATOM   1982  CE1 PHE A 334     -62.139   0.920   1.484  1.00153.85           C  
ANISOU 1982  CE1 PHE A 334    20068  15970  22417   -528     77   1997       C  
ATOM   1983  CE2 PHE A 334     -60.007   1.452   0.583  1.00155.64           C  
ANISOU 1983  CE2 PHE A 334    20410  16093  22633  -1090    185   2071       C  
ATOM   1984  CZ  PHE A 334     -60.811   1.187   1.669  1.00154.19           C  
ANISOU 1984  CZ  PHE A 334    20153  15934  22500   -769    161   1802       C  
ATOM   1985  N   PRO A 335     -62.123   2.464  -5.152  1.00164.92           N  
ANISOU 1985  N   PRO A 335    22000  17264  23397  -1494   -220   4253       N  
ATOM   1986  CA  PRO A 335     -62.282   2.518  -6.610  1.00167.23           C  
ANISOU 1986  CA  PRO A 335    22425  17672  23444  -1678   -300   4754       C  
ATOM   1987  C   PRO A 335     -63.351   1.600  -7.205  1.00165.90           C  
ANISOU 1987  C   PRO A 335    22234  17849  22950  -1552   -459   4935       C  
ATOM   1988  O   PRO A 335     -63.498   0.440  -6.811  1.00162.25           O  
ANISOU 1988  O   PRO A 335    21671  17733  22245  -1471   -431   4657       O  
ATOM   1989  CB  PRO A 335     -60.900   2.098  -7.109  1.00166.70           C  
ANISOU 1989  CB  PRO A 335    22403  17854  23082  -2028    -98   4694       C  
ATOM   1990  CG  PRO A 335     -59.984   2.621  -6.087  1.00166.56           C  
ANISOU 1990  CG  PRO A 335    22318  17583  23383  -2076     39   4340       C  
ATOM   1991  CD  PRO A 335     -60.696   2.445  -4.775  1.00164.18           C  
ANISOU 1991  CD  PRO A 335    21895  17190  23297  -1733    -24   3966       C  
ATOM   1992  N   LEU A 336     -64.087   2.139  -8.171  1.00169.19           N  
ANISOU 1992  N   LEU A 336    22752  18159  23375  -1547   -642   5416       N  
ATOM   1993  CA  LEU A 336     -65.073   1.361  -8.904  1.00168.75           C  
ANISOU 1993  CA  LEU A 336    22691  18422  23004  -1473   -831   5644       C  
ATOM   1994  C   LEU A 336     -64.705   1.358 -10.384  1.00171.33           C  
ANISOU 1994  C   LEU A 336    23217  18929  22953  -1766   -864   6063       C  
ATOM   1995  O   LEU A 336     -63.927   2.209 -10.837  1.00174.25           O  
ANISOU 1995  O   LEU A 336    23716  19089  23402  -1981   -769   6270       O  
ATOM   1996  CB  LEU A 336     -66.487   1.912  -8.694  1.00171.22           C  
ANISOU 1996  CB  LEU A 336    22914  18495  23646  -1154  -1068   5847       C  
ATOM   1997  CG  LEU A 336     -67.042   1.871  -7.268  1.00169.10           C  
ANISOU 1997  CG  LEU A 336    22440  18095  23714   -827  -1035   5456       C  
ATOM   1998  CD1 LEU A 336     -68.451   2.456  -7.221  1.00171.66           C  
ANISOU 1998  CD1 LEU A 336    22661  18201  24360   -511  -1260   5708       C  
ATOM   1999  CD2 LEU A 336     -67.019   0.446  -6.720  1.00164.45           C  
ANISOU 1999  CD2 LEU A 336    21725  17938  22819   -800   -953   5079       C  
ATOM   2000  N   SER A 337     -65.283   0.404 -11.118  1.00170.54           N  
ANISOU 2000  N   SER A 337    23142  19215  22441  -1780  -1000   6186       N  
ATOM   2001  CA  SER A 337     -64.885   0.067 -12.491  1.00172.40           C  
ANISOU 2001  CA  SER A 337    23574  19747  22182  -2058  -1007   6484       C  
ATOM   2002  C   SER A 337     -63.460  -0.491 -12.481  1.00170.55           C  
ANISOU 2002  C   SER A 337    23377  19742  21683  -2304   -697   6186       C  
ATOM   2003  O   SER A 337     -62.740  -0.423 -13.483  1.00172.83           O  
ANISOU 2003  O   SER A 337    23829  20184  21654  -2573   -592   6406       O  
ATOM   2004  CB  SER A 337     -64.993   1.277 -13.435  1.00177.64           C  
ANISOU 2004  CB  SER A 337    24413  20143  22940  -2172  -1120   7041       C  
ATOM   2005  OG  SER A 337     -66.324   1.749 -13.523  1.00179.69           O  
ANISOU 2005  OG  SER A 337    24628  20211  23435  -1931  -1427   7338       O  
ATOM   2006  N   VAL A 338     -63.065  -1.054 -11.340  1.00166.66           N  
ANISOU 2006  N   VAL A 338    22721  19288  21315  -2202   -550   5690       N  
ATOM   2007  CA  VAL A 338     -61.692  -1.511 -11.137  1.00164.96           C  
ANISOU 2007  CA  VAL A 338    22490  19244  20944  -2395   -262   5372       C  
ATOM   2008  C   VAL A 338     -61.614  -2.988 -10.768  1.00160.83           C  
ANISOU 2008  C   VAL A 338    21880  19103  20123  -2328   -213   4972       C  
ATOM   2009  O   VAL A 338     -62.220  -3.433  -9.794  1.00157.98           O  
ANISOU 2009  O   VAL A 338    21376  18720  19930  -2097   -289   4707       O  
ATOM   2010  CB  VAL A 338     -60.989  -0.687 -10.048  1.00164.71           C  
ANISOU 2010  CB  VAL A 338    22351  18856  21376  -2377   -112   5130       C  
ATOM   2011  CG1 VAL A 338     -59.549  -1.140  -9.885  1.00163.37           C  
ANISOU 2011  CG1 VAL A 338    22136  18879  21059  -2586    166   4829       C  
ATOM   2012  CG2 VAL A 338     -61.044   0.798 -10.390  1.00169.13           C  
ANISOU 2012  CG2 VAL A 338    23008  18982  22271  -2450   -168   5519       C  
ATOM   2013  N   TYR A 339     -60.849  -3.733 -11.559  1.00160.84           N  
ANISOU 2013  N   TYR A 339    21976  19451  19686  -2531    -75   4938       N  
ATOM   2014  CA  TYR A 339     -60.681  -5.172 -11.379  1.00157.51           C  
ANISOU 2014  CA  TYR A 339    21507  19388  18951  -2490    -26   4580       C  
ATOM   2015  C   TYR A 339     -59.220  -5.571 -11.613  1.00157.38           C  
ANISOU 2015  C   TYR A 339    21500  19586  18713  -2696    272   4372       C  
ATOM   2016  O   TYR A 339     -58.473  -4.845 -12.273  1.00160.44           O  
ANISOU 2016  O   TYR A 339    21966  19932  19062  -2911    421   4594       O  
ATOM   2017  CB  TYR A 339     -61.584  -5.946 -12.343  1.00158.12           C  
ANISOU 2017  CB  TYR A 339    21714  19738  18627  -2483   -240   4771       C  
ATOM   2018  CG  TYR A 339     -61.192  -5.791 -13.799  1.00161.78           C  
ANISOU 2018  CG  TYR A 339    22399  20392  18678  -2727   -197   5100       C  
ATOM   2019  CD1 TYR A 339     -60.703  -6.872 -14.524  1.00161.57           C  
ANISOU 2019  CD1 TYR A 339    22485  20756  18149  -2845   -101   4956       C  
ATOM   2020  CD2 TYR A 339     -61.293  -4.562 -14.446  1.00165.76           C  
ANISOU 2020  CD2 TYR A 339    23013  20682  19285  -2836   -243   5553       C  
ATOM   2021  CE1 TYR A 339     -60.335  -6.739 -15.854  1.00165.25           C  
ANISOU 2021  CE1 TYR A 339    23166  21427  18195  -3062    -39   5243       C  
ATOM   2022  CE2 TYR A 339     -60.922  -4.417 -15.776  1.00169.43           C  
ANISOU 2022  CE2 TYR A 339    23692  21343  19339  -3068   -191   5875       C  
ATOM   2023  CZ  TYR A 339     -60.446  -5.510 -16.475  1.00169.17           C  
ANISOU 2023  CZ  TYR A 339    23767  21731  18777  -3180    -80   5713       C  
ATOM   2024  OH  TYR A 339     -60.080  -5.379 -17.797  1.00173.12           O  
ANISOU 2024  OH  TYR A 339    24494  22458  18827  -3405     -9   6021       O  
ATOM   2025  N   GLY A 340     -58.821  -6.723 -11.079  1.00154.15           N  
ANISOU 2025  N   GLY A 340    20999  19402  18168  -2627    360   3961       N  
ATOM   2026  CA  GLY A 340     -57.488  -7.254 -11.309  1.00154.06           C  
ANISOU 2026  CA  GLY A 340    20971  19630  17936  -2782    633   3738       C  
ATOM   2027  C   GLY A 340     -57.570  -8.461 -12.226  1.00154.02           C  
ANISOU 2027  C   GLY A 340    21101  20009  17413  -2817    621   3691       C  
ATOM   2028  O   GLY A 340     -58.631  -8.740 -12.780  1.00154.53           O  
ANISOU 2028  O   GLY A 340    21289  20137  17288  -2764    388   3881       O  
ATOM   2029  N   PRO A 341     -56.449  -9.173 -12.412  1.00153.77           N  
ANISOU 2029  N   PRO A 341    21043  20231  17153  -2904    864   3432       N  
ATOM   2030  CA  PRO A 341     -56.452 -10.418 -13.187  1.00153.74           C  
ANISOU 2030  CA  PRO A 341    21171  20579  16665  -2910    868   3305       C  
ATOM   2031  C   PRO A 341     -56.627 -11.646 -12.307  1.00149.90           C  
ANISOU 2031  C   PRO A 341    20584  20161  16209  -2712    794   2891       C  
ATOM   2032  O   PRO A 341     -56.456 -12.764 -12.783  1.00149.69           O  
ANISOU 2032  O   PRO A 341    20647  20395  15835  -2701    820   2702       O  
ATOM   2033  CB  PRO A 341     -55.074 -10.414 -13.839  1.00156.10           C  
ANISOU 2033  CB  PRO A 341    21474  21093  16743  -3098   1207   3255       C  
ATOM   2034  CG  PRO A 341     -54.211  -9.770 -12.794  1.00155.06           C  
ANISOU 2034  CG  PRO A 341    21103  20752  17059  -3107   1369   3099       C  
ATOM   2035  CD  PRO A 341     -55.078  -8.723 -12.112  1.00154.53           C  
ANISOU 2035  CD  PRO A 341    20999  20300  17413  -3034   1157   3302       C  
ATOM   2036  N   MET A 342     -56.939 -11.433 -11.034  1.00147.18           N  
ANISOU 2036  N   MET A 342    20067  19581  16274  -2557    708   2751       N  
ATOM   2037  CA  MET A 342     -57.158 -12.534 -10.101  1.00143.69           C  
ANISOU 2037  CA  MET A 342    19528  19182  15887  -2371    628   2399       C  
ATOM   2038  C   MET A 342     -58.621 -13.015 -10.126  1.00142.72           C  
ANISOU 2038  C   MET A 342    19475  19044  15710  -2254    323   2509       C  
ATOM   2039  O   MET A 342     -59.111 -13.620  -9.169  1.00139.99           O  
ANISOU 2039  O   MET A 342    19024  18647  15521  -2091    214   2312       O  
ATOM   2040  CB  MET A 342     -56.728 -12.132  -8.680  1.00142.76           C  
ANISOU 2040  CB  MET A 342    19193  18854  16193  -2265    697   2177       C  
ATOM   2041  CG  MET A 342     -57.721 -11.302  -7.892  1.00142.04           C  
ANISOU 2041  CG  MET A 342    19036  18473  16459  -2142    522   2315       C  
ATOM   2042  SD  MET A 342     -57.646  -9.570  -8.333  1.00145.41           S  
ANISOU 2042  SD  MET A 342    19500  18633  17116  -2284    563   2688       S  
ATOM   2043  CE  MET A 342     -56.201  -9.056  -7.429  1.00145.11           C  
ANISOU 2043  CE  MET A 342    19287  18479  17368  -2348    804   2413       C  
ATOM   2044  N   VAL A 343     -59.310 -12.742 -11.232  1.00145.27           N  
ANISOU 2044  N   VAL A 343    19967  19422  15805  -2347    182   2839       N  
ATOM   2045  CA  VAL A 343     -60.704 -13.151 -11.419  1.00145.05           C  
ANISOU 2045  CA  VAL A 343    19996  19403  15714  -2267   -129   2985       C  
ATOM   2046  C   VAL A 343     -60.946 -14.630 -11.100  1.00142.74           C  
ANISOU 2046  C   VAL A 343    19699  19262  15273  -2178   -220   2676       C  
ATOM   2047  O   VAL A 343     -61.803 -14.974 -10.272  1.00140.68           O  
ANISOU 2047  O   VAL A 343    19320  18908  15224  -2037   -388   2619       O  
ATOM   2048  CB  VAL A 343     -61.167 -12.869 -12.867  1.00148.66           C  
ANISOU 2048  CB  VAL A 343    20673  19982  15828  -2416   -259   3346       C  
ATOM   2049  CG1 VAL A 343     -62.585 -13.344 -13.080  1.00148.70           C  
ANISOU 2049  CG1 VAL A 343    20715  20014  15772  -2347   -607   3486       C  
ATOM   2050  CG2 VAL A 343     -61.038 -11.383 -13.197  1.00151.30           C  
ANISOU 2050  CG2 VAL A 343    21025  20133  16332  -2505   -202   3708       C  
ATOM   2051  N   LEU A 344     -60.162 -15.501 -11.726  1.00143.31           N  
ANISOU 2051  N   LEU A 344    19895  19561  14996  -2256    -94   2473       N  
ATOM   2052  CA  LEU A 344     -60.312 -16.933 -11.510  1.00141.60           C  
ANISOU 2052  CA  LEU A 344    19704  19463  14633  -2181   -181   2174       C  
ATOM   2053  C   LEU A 344     -60.075 -17.335 -10.039  1.00138.14           C  
ANISOU 2053  C   LEU A 344    19056  18902  14530  -2018   -124   1885       C  
ATOM   2054  O   LEU A 344     -60.864 -18.105  -9.489  1.00136.44           O  
ANISOU 2054  O   LEU A 344    18798  18656  14387  -1921   -310   1801       O  
ATOM   2055  CB  LEU A 344     -59.391 -17.713 -12.452  1.00143.30           C  
ANISOU 2055  CB  LEU A 344    20094  19925  14427  -2273    -20   1982       C  
ATOM   2056  CG  LEU A 344     -59.308 -19.216 -12.196  1.00141.79           C  
ANISOU 2056  CG  LEU A 344    19939  19823  14111  -2185    -71   1622       C  
ATOM   2057  CD1 LEU A 344     -60.662 -19.855 -12.435  1.00141.86           C  
ANISOU 2057  CD1 LEU A 344    20046  19826  14031  -2182   -423   1719       C  
ATOM   2058  CD2 LEU A 344     -58.251 -19.866 -13.070  1.00143.80           C  
ANISOU 2058  CD2 LEU A 344    20347  20305  13986  -2244    142   1400       C  
ATOM   2059  N   PRO A 345     -59.001 -16.831  -9.395  1.00137.36           N  
ANISOU 2059  N   PRO A 345    18823  18737  14628  -1997    122   1742       N  
ATOM   2060  CA  PRO A 345     -58.900 -17.081  -7.950  1.00134.38           C  
ANISOU 2060  CA  PRO A 345    18255  18236  14567  -1839    137   1509       C  
ATOM   2061  C   PRO A 345     -60.126 -16.653  -7.146  1.00133.14           C  
ANISOU 2061  C   PRO A 345    17993  17898  14695  -1727    -58   1663       C  
ATOM   2062  O   PRO A 345     -60.455 -17.300  -6.153  1.00130.92           O  
ANISOU 2062  O   PRO A 345    17611  17581  14551  -1596   -125   1495       O  
ATOM   2063  CB  PRO A 345     -57.686 -16.250  -7.542  1.00134.60           C  
ANISOU 2063  CB  PRO A 345    18163  18201  14779  -1872    389   1422       C  
ATOM   2064  CG  PRO A 345     -56.826 -16.284  -8.726  1.00137.11           C  
ANISOU 2064  CG  PRO A 345    18599  18703  14793  -2026    563   1446       C  
ATOM   2065  CD  PRO A 345     -57.733 -16.302  -9.930  1.00139.20           C  
ANISOU 2065  CD  PRO A 345    19073  19053  14765  -2119    399   1724       C  
ATOM   2066  N   ILE A 346     -60.781 -15.574  -7.555  1.00134.81           N  
ANISOU 2066  N   ILE A 346    18223  17999  15000  -1769   -139   1985       N  
ATOM   2067  CA  ILE A 346     -62.014 -15.157  -6.895  1.00134.17           C  
ANISOU 2067  CA  ILE A 346    18031  17760  15187  -1644   -319   2145       C  
ATOM   2068  C   ILE A 346     -63.125 -16.192  -7.090  1.00133.75           C  
ANISOU 2068  C   ILE A 346    18008  17813  14999  -1615   -562   2185       C  
ATOM   2069  O   ILE A 346     -63.847 -16.528  -6.145  1.00132.11           O  
ANISOU 2069  O   ILE A 346    17661  17547  14986  -1483   -652   2130       O  
ATOM   2070  CB  ILE A 346     -62.487 -13.786  -7.403  1.00136.57           C  
ANISOU 2070  CB  ILE A 346    18356  17910  15625  -1685   -370   2501       C  
ATOM   2071  CG1 ILE A 346     -61.440 -12.726  -7.080  1.00137.13           C  
ANISOU 2071  CG1 ILE A 346    18382  17828  15891  -1724   -146   2459       C  
ATOM   2072  CG2 ILE A 346     -63.808 -13.413  -6.767  1.00136.27           C  
ANISOU 2072  CG2 ILE A 346    18184  17724  15866  -1527   -554   2657       C  
ATOM   2073  CD1 ILE A 346     -61.156 -12.621  -5.609  1.00134.84           C  
ANISOU 2073  CD1 ILE A 346    17919  17403  15910  -1574    -55   2190       C  
ATOM   2074  N   ILE A 347     -63.250 -16.704  -8.314  1.00135.53           N  
ANISOU 2074  N   ILE A 347    18414  18198  14882  -1747   -665   2279       N  
ATOM   2075  CA  ILE A 347     -64.214 -17.771  -8.589  1.00135.51           C  
ANISOU 2075  CA  ILE A 347    18458  18297  14732  -1755   -915   2290       C  
ATOM   2076  C   ILE A 347     -63.947 -18.981  -7.706  1.00133.01           C  
ANISOU 2076  C   ILE A 347    18081  18010  14445  -1674   -881   1959       C  
ATOM   2077  O   ILE A 347     -64.879 -19.607  -7.201  1.00132.12           O  
ANISOU 2077  O   ILE A 347    17883  17880  14435  -1617  -1058   1970       O  
ATOM   2078  CB  ILE A 347     -64.180 -18.205 -10.058  1.00138.07           C  
ANISOU 2078  CB  ILE A 347    19027  18803  14632  -1920  -1015   2372       C  
ATOM   2079  CG1 ILE A 347     -64.573 -17.035 -10.952  1.00140.91           C  
ANISOU 2079  CG1 ILE A 347    19456  19138  14945  -2004  -1091   2753       C  
ATOM   2080  CG2 ILE A 347     -65.139 -19.347 -10.299  1.00138.24           C  
ANISOU 2080  CG2 ILE A 347    19099  18908  14518  -1945  -1296   2349       C  
ATOM   2081  CD1 ILE A 347     -64.259 -17.259 -12.404  1.00143.84           C  
ANISOU 2081  CD1 ILE A 347    20091  19707  14855  -2176  -1119   2831       C  
ATOM   2082  N   ALA A 348     -62.669 -19.297  -7.524  1.00132.16           N  
ANISOU 2082  N   ALA A 348    18006  17947  14260  -1672   -656   1684       N  
ATOM   2083  CA  ALA A 348     -62.264 -20.356  -6.612  1.00129.95           C  
ANISOU 2083  CA  ALA A 348    17665  17672  14036  -1576   -609   1375       C  
ATOM   2084  C   ALA A 348     -62.724 -20.046  -5.187  1.00127.89           C  
ANISOU 2084  C   ALA A 348    17191  17273  14127  -1428   -611   1370       C  
ATOM   2085  O   ALA A 348     -63.251 -20.920  -4.493  1.00126.58           O  
ANISOU 2085  O   ALA A 348    16965  17102  14028  -1359   -716   1287       O  
ATOM   2086  CB  ALA A 348     -60.763 -20.554  -6.653  1.00129.78           C  
ANISOU 2086  CB  ALA A 348    17679  17719  13914  -1581   -359   1108       C  
ATOM   2087  N   VAL A 349     -62.515 -18.808  -4.746  1.00127.88           N  
ANISOU 2087  N   VAL A 349    17085  17158  14344  -1382   -489   1455       N  
ATOM   2088  CA  VAL A 349     -63.001 -18.379  -3.435  1.00126.44           C  
ANISOU 2088  CA  VAL A 349    16718  16848  14475  -1231   -482   1448       C  
ATOM   2089  C   VAL A 349     -64.493 -18.624  -3.270  1.00126.59           C  
ANISOU 2089  C   VAL A 349    16661  16857  14581  -1182   -694   1646       C  
ATOM   2090  O   VAL A 349     -64.930 -19.164  -2.258  1.00125.19           O  
ANISOU 2090  O   VAL A 349    16367  16672  14526  -1077   -721   1561       O  
ATOM   2091  CB  VAL A 349     -62.724 -16.885  -3.187  1.00127.18           C  
ANISOU 2091  CB  VAL A 349    16743  16789  14790  -1202   -358   1543       C  
ATOM   2092  CG1 VAL A 349     -63.600 -16.348  -2.060  1.00126.53           C  
ANISOU 2092  CG1 VAL A 349    16495  16575  15006  -1035   -393   1596       C  
ATOM   2093  CG2 VAL A 349     -61.245 -16.654  -2.911  1.00126.75           C  
ANISOU 2093  CG2 VAL A 349    16687  16727  14744  -1230   -139   1307       C  
ATOM   2094  N   PHE A 350     -65.273 -18.262  -4.282  1.00128.56           N  
ANISOU 2094  N   PHE A 350    16968  17122  14757  -1265   -851   1922       N  
ATOM   2095  CA  PHE A 350     -66.721 -18.417  -4.187  1.00129.15           C  
ANISOU 2095  CA  PHE A 350    16933  17196  14943  -1225  -1067   2136       C  
ATOM   2096  C   PHE A 350     -67.175 -19.862  -4.299  1.00128.74           C  
ANISOU 2096  C   PHE A 350    16918  17260  14736  -1290  -1234   2062       C  
ATOM   2097  O   PHE A 350     -68.203 -20.212  -3.747  1.00128.57           O  
ANISOU 2097  O   PHE A 350    16748  17239  14865  -1237  -1358   2155       O  
ATOM   2098  CB  PHE A 350     -67.429 -17.564  -5.236  1.00132.80           C  
ANISOU 2098  CB  PHE A 350    17433  17637  15388  -1289  -1218   2473       C  
ATOM   2099  CG  PHE A 350     -67.511 -16.117  -4.864  1.00133.53           C  
ANISOU 2099  CG  PHE A 350    17422  17555  15757  -1178  -1120   2615       C  
ATOM   2100  CD1 PHE A 350     -66.873 -15.154  -5.625  1.00135.13           C  
ANISOU 2100  CD1 PHE A 350    17748  17689  15906  -1257  -1043   2732       C  
ATOM   2101  CD2 PHE A 350     -68.189 -15.723  -3.723  1.00132.86           C  
ANISOU 2101  CD2 PHE A 350    17125  17367  15990   -994  -1092   2622       C  
ATOM   2102  CE1 PHE A 350     -66.931 -13.823  -5.268  1.00136.06           C  
ANISOU 2102  CE1 PHE A 350    17786  17604  16307  -1160   -965   2856       C  
ATOM   2103  CE2 PHE A 350     -68.246 -14.395  -3.365  1.00133.82           C  
ANISOU 2103  CE2 PHE A 350    17170  17299  16377   -876  -1002   2718       C  
ATOM   2104  CZ  PHE A 350     -67.617 -13.446  -4.137  1.00135.41           C  
ANISOU 2104  CZ  PHE A 350    17503  17398  16547   -961   -950   2834       C  
ATOM   2105  N   ILE A 351     -66.438 -20.696  -5.023  1.00128.89           N  
ANISOU 2105  N   ILE A 351    17132  17372  14469  -1405  -1235   1898       N  
ATOM   2106  CA  ILE A 351     -66.717 -22.129  -5.002  1.00128.51           C  
ANISOU 2106  CA  ILE A 351    17138  17388  14302  -1457  -1379   1771       C  
ATOM   2107  C   ILE A 351     -66.501 -22.667  -3.593  1.00126.23           C  
ANISOU 2107  C   ILE A 351    16717  17049  14198  -1330  -1271   1581       C  
ATOM   2108  O   ILE A 351     -67.341 -23.403  -3.053  1.00125.94           O  
ANISOU 2108  O   ILE A 351    16584  17009  14256  -1320  -1404   1625       O  
ATOM   2109  CB  ILE A 351     -65.851 -22.905  -5.999  1.00129.35           C  
ANISOU 2109  CB  ILE A 351    17492  17585  14070  -1572  -1370   1581       C  
ATOM   2110  CG1 ILE A 351     -66.332 -22.633  -7.424  1.00132.08           C  
ANISOU 2110  CG1 ILE A 351    17993  18014  14175  -1719  -1544   1789       C  
ATOM   2111  CG2 ILE A 351     -65.952 -24.386  -5.739  1.00128.79           C  
ANISOU 2111  CG2 ILE A 351    17477  17522  13935  -1592  -1484   1389       C  
ATOM   2112  CD1 ILE A 351     -65.450 -23.231  -8.489  1.00133.44           C  
ANISOU 2112  CD1 ILE A 351    18427  18300  13975  -1823  -1499   1603       C  
ATOM   2113  N   ILE A 352     -65.376 -22.283  -3.002  1.00124.92           N  
ANISOU 2113  N   ILE A 352    16537  16846  14079  -1243  -1036   1386       N  
ATOM   2114  CA  ILE A 352     -65.100 -22.597  -1.606  1.00123.00           C  
ANISOU 2114  CA  ILE A 352    16170  16561  14002  -1109   -928   1220       C  
ATOM   2115  C   ILE A 352     -66.270 -22.201  -0.713  1.00122.82           C  
ANISOU 2115  C   ILE A 352    15945  16498  14221  -1013   -977   1401       C  
ATOM   2116  O   ILE A 352     -66.749 -22.994   0.085  1.00122.13           O  
ANISOU 2116  O   ILE A 352    15777  16426  14200   -973  -1028   1379       O  
ATOM   2117  CB  ILE A 352     -63.835 -21.890  -1.106  1.00122.09           C  
ANISOU 2117  CB  ILE A 352    16036  16409  13943  -1032   -691   1033       C  
ATOM   2118  CG1 ILE A 352     -62.607 -22.488  -1.773  1.00122.26           C  
ANISOU 2118  CG1 ILE A 352    16210  16495  13749  -1099   -611    815       C  
ATOM   2119  CG2 ILE A 352     -63.716 -22.001   0.410  1.00120.47           C  
ANISOU 2119  CG2 ILE A 352    15693  16166  13915   -883   -605    900       C  
ATOM   2120  CD1 ILE A 352     -61.359 -21.731  -1.477  1.00121.91           C  
ANISOU 2120  CD1 ILE A 352    16126  16431  13764  -1060   -391    663       C  
ATOM   2121  N   CYS A 353     -66.708 -20.958  -0.846  1.00123.81           N  
ANISOU 2121  N   CYS A 353    15988  16570  14483   -972   -951   1583       N  
ATOM   2122  CA  CYS A 353     -67.792 -20.426  -0.038  1.00124.07           C  
ANISOU 2122  CA  CYS A 353    15814  16566  14761   -849   -965   1746       C  
ATOM   2123  C   CYS A 353     -69.138 -21.110  -0.292  1.00125.15           C  
ANISOU 2123  C   CYS A 353    15860  16770  14920   -910  -1187   1961       C  
ATOM   2124  O   CYS A 353     -69.963 -21.209   0.608  1.00125.11           O  
ANISOU 2124  O   CYS A 353    15666  16781  15089   -816  -1183   2035       O  
ATOM   2125  CB  CYS A 353     -67.896 -18.926  -0.282  1.00127.57           C  
ANISOU 2125  CB  CYS A 353    16213  16905  15352   -788   -902   1889       C  
ATOM   2126  SG  CYS A 353     -66.392 -18.086   0.242  1.00126.58           S  
ANISOU 2126  SG  CYS A 353    16149  16678  15266   -728   -647   1635       S  
ATOM   2127  N   ALA A 354     -69.365 -21.562  -1.521  1.00126.32           N  
ANISOU 2127  N   ALA A 354    16137  16969  14890  -1073  -1380   2061       N  
ATOM   2128  CA  ALA A 354     -70.586 -22.279  -1.845  1.00127.64           C  
ANISOU 2128  CA  ALA A 354    16225  17201  15073  -1167  -1628   2252       C  
ATOM   2129  C   ALA A 354     -70.606 -23.599  -1.093  1.00126.55           C  
ANISOU 2129  C   ALA A 354    16070  17089  14924  -1192  -1647   2111       C  
ATOM   2130  O   ALA A 354     -71.531 -23.864  -0.318  1.00126.78           O  
ANISOU 2130  O   ALA A 354    15896  17142  15131  -1150  -1682   2231       O  
ATOM   2131  CB  ALA A 354     -70.689 -22.514  -3.338  1.00129.45           C  
ANISOU 2131  CB  ALA A 354    16638  17480  15068  -1347  -1844   2347       C  
ATOM   2132  N   CYS A 355     -69.565 -24.407  -1.300  1.00125.61           N  
ANISOU 2132  N   CYS A 355    16158  16963  14605  -1251  -1611   1863       N  
ATOM   2133  CA  CYS A 355     -69.454 -25.705  -0.626  1.00124.77           C  
ANISOU 2133  CA  CYS A 355    16073  16848  14487  -1272  -1638   1723       C  
ATOM   2134  C   CYS A 355     -69.493 -25.527   0.879  1.00123.42           C  
ANISOU 2134  C   CYS A 355    15720  16668  14506  -1110  -1461   1696       C  
ATOM   2135  O   CYS A 355     -70.088 -26.320   1.613  1.00123.47           O  
ANISOU 2135  O   CYS A 355    15627  16688  14598  -1121  -1512   1752       O  
ATOM   2136  CB  CYS A 355     -68.179 -26.435  -1.036  1.00124.12           C  
ANISOU 2136  CB  CYS A 355    16233  16743  14186  -1308  -1591   1437       C  
ATOM   2137  SG  CYS A 355     -68.094 -26.779  -2.792  1.00126.15           S  
ANISOU 2137  SG  CYS A 355    16739  17035  14156  -1492  -1781   1426       S  
ATOM   2138  N   GLU A 356     -68.797 -24.501   1.331  1.00122.44           N  
ANISOU 2138  N   GLU A 356    15569  16521  14432   -972  -1250   1602       N  
ATOM   2139  CA  GLU A 356     -68.767 -24.148   2.727  1.00121.46           C  
ANISOU 2139  CA  GLU A 356    15297  16396  14456   -805  -1072   1551       C  
ATOM   2140  C   GLU A 356     -70.155 -23.879   3.264  1.00122.56           C  
ANISOU 2140  C   GLU A 356    15199  16580  14788   -753  -1104   1794       C  
ATOM   2141  O   GLU A 356     -70.509 -24.340   4.340  1.00122.34           O  
ANISOU 2141  O   GLU A 356    15056  16596  14830   -689  -1042   1802       O  
ATOM   2142  CB  GLU A 356     -67.896 -22.941   2.931  1.00125.75           C  
ANISOU 2142  CB  GLU A 356    15856  16887  15034   -691   -881   1423       C  
ATOM   2143  CG  GLU A 356     -67.725 -22.605   4.354  1.00124.94           C  
ANISOU 2143  CG  GLU A 356    15643  16785  15043   -523   -709   1316       C  
ATOM   2144  CD  GLU A 356     -66.721 -21.515   4.512  1.00124.47           C  
ANISOU 2144  CD  GLU A 356    15627  16654  15014   -441   -549   1150       C  
ATOM   2145  OE1 GLU A 356     -66.191 -21.036   3.480  1.00124.83           O  
ANISOU 2145  OE1 GLU A 356    15776  16653  15001   -527   -561   1149       O  
ATOM   2146  OE2 GLU A 356     -66.419 -21.184   5.669  1.00123.96           O  
ANISOU 2146  OE2 GLU A 356    15501  16584  15014   -305   -414   1016       O  
ATOM   2147  N   CYS A 357     -70.929 -23.103   2.519  1.00124.02           N  
ANISOU 2147  N   CYS A 357    15303  16761  15057   -772  -1193   2003       N  
ATOM   2148  CA  CYS A 357     -72.317 -22.853   2.876  1.00125.55           C  
ANISOU 2148  CA  CYS A 357    15239  17009  15454   -721  -1241   2255       C  
ATOM   2149  C   CYS A 357     -73.083 -24.154   3.009  1.00126.20           C  
ANISOU 2149  C   CYS A 357    15250  17166  15536   -856  -1398   2364       C  
ATOM   2150  O   CYS A 357     -73.698 -24.399   4.035  1.00126.52           O  
ANISOU 2150  O   CYS A 357    15101  17270  15699   -786  -1314   2435       O  
ATOM   2151  CB  CYS A 357     -72.995 -21.966   1.834  1.00127.36           C  
ANISOU 2151  CB  CYS A 357    15413  17218  15761   -745  -1375   2481       C  
ATOM   2152  SG  CYS A 357     -72.589 -20.231   1.975  1.00127.52           S  
ANISOU 2152  SG  CYS A 357    15413  17122  15915   -548  -1184   2455       S  
ATOM   2153  N   ILE A 358     -72.993 -25.001   1.987  1.00126.63           N  
ANISOU 2153  N   ILE A 358    15467  17207  15440  -1054  -1618   2363       N  
ATOM   2154  CA  ILE A 358     -73.689 -26.280   1.987  1.00127.60           C  
ANISOU 2154  CA  ILE A 358    15551  17361  15571  -1219  -1807   2459       C  
ATOM   2155  C   ILE A 358     -73.400 -27.078   3.251  1.00126.51           C  
ANISOU 2155  C   ILE A 358    15391  17226  15452  -1169  -1671   2354       C  
ATOM   2156  O   ILE A 358     -74.314 -27.432   3.999  1.00127.51           O  
ANISOU 2156  O   ILE A 358    15303  17419  15726  -1176  -1665   2526       O  
ATOM   2157  CB  ILE A 358     -73.296 -27.109   0.761  1.00128.08           C  
ANISOU 2157  CB  ILE A 358    15872  17373  15420  -1419  -2036   2369       C  
ATOM   2158  CG1 ILE A 358     -73.806 -26.426  -0.506  1.00129.81           C  
ANISOU 2158  CG1 ILE A 358    16101  17620  15600  -1497  -2218   2533       C  
ATOM   2159  CG2 ILE A 358     -73.870 -28.496   0.857  1.00129.13           C  
ANISOU 2159  CG2 ILE A 358    15999  17491  15574  -1593  -2231   2422       C  
ATOM   2160  CD1 ILE A 358     -73.166 -26.928  -1.772  1.00130.31           C  
ANISOU 2160  CD1 ILE A 358    16470  17655  15388  -1651  -2378   2393       C  
ATOM   2161  N   GLY A 359     -72.122 -27.301   3.523  1.00124.71           N  
ANISOU 2161  N   GLY A 359    15366  16938  15079  -1109  -1550   2087       N  
ATOM   2162  CA  GLY A 359     -71.722 -28.070   4.687  1.00123.81           C  
ANISOU 2162  CA  GLY A 359    15264  16821  14958  -1055  -1442   1986       C  
ATOM   2163  C   GLY A 359     -72.115 -27.442   6.014  1.00123.73           C  
ANISOU 2163  C   GLY A 359    15039  16899  15074   -879  -1222   2055       C  
ATOM   2164  O   GLY A 359     -72.585 -28.137   6.921  1.00124.30           O  
ANISOU 2164  O   GLY A 359    15009  17023  15195   -889  -1193   2151       O  
ATOM   2165  N   ASP A 360     -71.909 -26.130   6.132  1.00123.30           N  
ANISOU 2165  N   ASP A 360    14927  16856  15065   -718  -1064   2004       N  
ATOM   2166  CA  ASP A 360     -72.214 -25.388   7.359  1.00123.49           C  
ANISOU 2166  CA  ASP A 360    14773  16955  15191   -521   -839   2019       C  
ATOM   2167  C   ASP A 360     -73.706 -25.413   7.674  1.00125.54           C  
ANISOU 2167  C   ASP A 360    14751  17324  15624   -527   -852   2306       C  
ATOM   2168  O   ASP A 360     -74.115 -25.664   8.816  1.00126.15           O  
ANISOU 2168  O   ASP A 360    14693  17504  15736   -450   -712   2361       O  
ATOM   2169  CB  ASP A 360     -71.711 -23.937   7.261  1.00128.49           C  
ANISOU 2169  CB  ASP A 360    15423  17533  15864   -364   -700   1898       C  
ATOM   2170  CG  ASP A 360     -70.173 -23.825   7.360  1.00126.67           C  
ANISOU 2170  CG  ASP A 360    15413  17227  15489   -327   -620   1598       C  
ATOM   2171  OD1 ASP A 360     -69.518 -24.782   7.835  1.00125.76           O  
ANISOU 2171  OD1 ASP A 360    15405  17125  15255   -357   -626   1470       O  
ATOM   2172  OD2 ASP A 360     -69.610 -22.775   6.971  1.00126.39           O  
ANISOU 2172  OD2 ASP A 360    15432  17115  15474   -269   -555   1500       O  
ATOM   2173  N   VAL A 361     -74.512 -25.159   6.648  1.00126.87           N  
ANISOU 2173  N   VAL A 361    14824  17486  15896   -620  -1022   2498       N  
ATOM   2174  CA  VAL A 361     -75.969 -25.198   6.759  1.00129.20           C  
ANISOU 2174  CA  VAL A 361    14815  17890  16385   -647  -1074   2792       C  
ATOM   2175  C   VAL A 361     -76.457 -26.576   7.168  1.00130.00           C  
ANISOU 2175  C   VAL A 361    14858  18052  16483   -819  -1163   2916       C  
ATOM   2176  O   VAL A 361     -77.198 -26.699   8.133  1.00131.30           O  
ANISOU 2176  O   VAL A 361    14793  18342  16752   -761  -1025   3057       O  
ATOM   2177  CB  VAL A 361     -76.649 -24.797   5.424  1.00130.66           C  
ANISOU 2177  CB  VAL A 361    14936  18048  16660   -748  -1310   2977       C  
ATOM   2178  CG1 VAL A 361     -78.088 -25.295   5.354  1.00133.24           C  
ANISOU 2178  CG1 VAL A 361    14967  18487  17171   -865  -1458   3286       C  
ATOM   2179  CG2 VAL A 361     -76.571 -23.296   5.220  1.00130.84           C  
ANISOU 2179  CG2 VAL A 361    14917  18022  16773   -549  -1200   2959       C  
ATOM   2180  N   THR A 362     -76.013 -27.611   6.459  1.00129.46           N  
ANISOU 2180  N   THR A 362    15006  17891  16293  -1026  -1379   2856       N  
ATOM   2181  CA  THR A 362     -76.408 -28.976   6.797  1.00130.42           C  
ANISOU 2181  CA  THR A 362    15108  18019  16427  -1210  -1491   2967       C  
ATOM   2182  C   THR A 362     -76.059 -29.296   8.249  1.00129.84           C  
ANISOU 2182  C   THR A 362    15021  18004  16307  -1093  -1254   2912       C  
ATOM   2183  O   THR A 362     -76.837 -29.934   8.978  1.00131.47           O  
ANISOU 2183  O   THR A 362    15050  18301  16602  -1164  -1222   3115       O  
ATOM   2184  CB  THR A 362     -75.753 -29.992   5.852  1.00129.89           C  
ANISOU 2184  CB  THR A 362    15337  17799  16216  -1410  -1741   2834       C  
ATOM   2185  OG1 THR A 362     -76.111 -29.669   4.502  1.00130.79           O  
ANISOU 2185  OG1 THR A 362    15476  17887  16332  -1521  -1964   2891       O  
ATOM   2186  CG2 THR A 362     -76.254 -31.393   6.150  1.00131.35           C  
ANISOU 2186  CG2 THR A 362    15503  17950  16456  -1617  -1888   2969       C  
ATOM   2187  N   ALA A 363     -74.884 -28.849   8.664  1.00127.76           N  
ANISOU 2187  N   ALA A 363    14945  17700  15899   -925  -1093   2647       N  
ATOM   2188  CA  ALA A 363     -74.489 -28.997  10.051  1.00127.35           C  
ANISOU 2188  CA  ALA A 363    14895  17719  15772   -789   -875   2577       C  
ATOM   2189  C   ALA A 363     -75.527 -28.353  10.960  1.00129.09           C  
ANISOU 2189  C   ALA A 363    14811  18123  16115   -658   -663   2759       C  
ATOM   2190  O   ALA A 363     -75.968 -28.962  11.938  1.00130.36           O  
ANISOU 2190  O   ALA A 363    14865  18394  16270   -674   -563   2897       O  
ATOM   2191  CB  ALA A 363     -73.116 -28.380  10.286  1.00126.79           C  
ANISOU 2191  CB  ALA A 363    15033  17588  15552   -618   -750   2260       C  
ATOM   2192  N   THR A 364     -75.924 -27.128  10.619  1.00129.46           N  
ANISOU 2192  N   THR A 364    14719  18199  16273   -525   -592   2768       N  
ATOM   2193  CA  THR A 364     -76.938 -26.392  11.385  1.00131.47           C  
ANISOU 2193  CA  THR A 364    14667  18619  16668   -361   -379   2917       C  
ATOM   2194  C   THR A 364     -78.311 -27.095  11.479  1.00134.16           C  
ANISOU 2194  C   THR A 364    14710  19094  17171   -511   -436   3260       C  
ATOM   2195  O   THR A 364     -78.950 -27.110  12.540  1.00135.93           O  
ANISOU 2195  O   THR A 364    14723  19495  17430   -422   -219   3383       O  
ATOM   2196  CB  THR A 364     -77.136 -24.993  10.782  1.00131.68           C  
ANISOU 2196  CB  THR A 364    14609  18599  16825   -203   -349   2880       C  
ATOM   2197  OG1 THR A 364     -75.880 -24.298  10.776  1.00129.55           O  
ANISOU 2197  OG1 THR A 364    14592  18205  16425    -79   -278   2576       O  
ATOM   2198  CG2 THR A 364     -78.173 -24.202  11.579  1.00134.08           C  
ANISOU 2198  CG2 THR A 364    14592  19061  17293      5   -116   3007       C  
ATOM   2199  N   CYS A 365     -78.763 -27.648  10.355  1.00134.74           N  
ANISOU 2199  N   CYS A 365    14763  19093  17340   -743   -728   3411       N  
ATOM   2200  CA  CYS A 365     -80.004 -28.399  10.298  1.00137.44           C  
ANISOU 2200  CA  CYS A 365    14829  19535  17855   -938   -842   3734       C  
ATOM   2201  C   CYS A 365     -79.932 -29.572  11.245  1.00137.94           C  
ANISOU 2201  C   CYS A 365    14931  19644  17834  -1056   -776   3806       C  
ATOM   2202  O   CYS A 365     -80.879 -29.830  11.976  1.00140.40           O  
ANISOU 2202  O   CYS A 365    14957  20129  18259  -1083   -648   4051       O  
ATOM   2203  CB  CYS A 365     -80.279 -28.902   8.886  1.00137.87           C  
ANISOU 2203  CB  CYS A 365    14937  19469  17976  -1194  -1216   3824       C  
ATOM   2204  SG  CYS A 365     -80.661 -27.613   7.711  1.00138.30           S  
ANISOU 2204  SG  CYS A 365    14893  19502  18154  -1097  -1338   3853       S  
ATOM   2205  N   ASP A 366     -78.805 -30.279  11.269  1.00135.88           N  
ANISOU 2205  N   ASP A 366    15013  19236  17381  -1116   -852   3608       N  
ATOM   2206  CA  ASP A 366     -78.736 -31.369  12.237  1.00136.66           C  
ANISOU 2206  CA  ASP A 366    15154  19365  17405  -1211   -791   3702       C  
ATOM   2207  C   ASP A 366     -78.668 -30.844  13.665  1.00137.03           C  
ANISOU 2207  C   ASP A 366    15113  19605  17348   -972   -434   3677       C  
ATOM   2208  O   ASP A 366     -79.124 -31.507  14.593  1.00138.92           O  
ANISOU 2208  O   ASP A 366    15241  19968  17573  -1034   -318   3875       O  
ATOM   2209  CB  ASP A 366     -77.558 -32.298  12.011  1.00134.79           C  
ANISOU 2209  CB  ASP A 366    15292  18918  17003  -1307   -957   3506       C  
ATOM   2210  CG  ASP A 366     -77.665 -33.548  12.869  1.00136.24           C  
ANISOU 2210  CG  ASP A 366    15505  19100  17160  -1448   -958   3676       C  
ATOM   2211  OD1 ASP A 366     -78.475 -34.430  12.518  1.00138.35           O  
ANISOU 2211  OD1 ASP A 366    15666  19321  17580  -1709  -1145   3919       O  
ATOM   2212  OD2 ASP A 366     -77.016 -33.617  13.933  1.00135.66           O  
ANISOU 2212  OD2 ASP A 366    15542  19081  16921  -1306   -773   3593       O  
ATOM   2213  N   VAL A 367     -78.050 -29.687  13.859  1.00135.45           N  
ANISOU 2213  N   VAL A 367    14985  19422  17059   -710   -265   3428       N  
ATOM   2214  CA  VAL A 367     -77.988 -29.118  15.199  1.00136.11           C  
ANISOU 2214  CA  VAL A 367    15005  19688  17024   -472     65   3365       C  
ATOM   2215  C   VAL A 367     -79.358 -28.667  15.673  1.00139.20           C  
ANISOU 2215  C   VAL A 367    15001  20308  17579   -400    267   3615       C  
ATOM   2216  O   VAL A 367     -79.749 -28.896  16.821  1.00141.15           O  
ANISOU 2216  O   VAL A 367    15128  20756  17746   -343    502   3734       O  
ATOM   2217  CB  VAL A 367     -77.031 -27.929  15.260  1.00134.06           C  
ANISOU 2217  CB  VAL A 367    14911  19368  16658   -218    178   3023       C  
ATOM   2218  CG1 VAL A 367     -77.155 -27.234  16.592  1.00135.37           C  
ANISOU 2218  CG1 VAL A 367    14987  19731  16718     33    511   2952       C  
ATOM   2219  CG2 VAL A 367     -75.597 -28.400  15.032  1.00131.38           C  
ANISOU 2219  CG2 VAL A 367    14931  18848  16139   -264     32   2772       C  
ATOM   2220  N   SER A 368     -80.101 -28.071  14.751  1.00139.92           N  
ANISOU 2220  N   SER A 368    14886  20379  17900   -410    167   3711       N  
ATOM   2221  CA  SER A 368     -81.420 -27.507  15.033  1.00143.03           C  
ANISOU 2221  CA  SER A 368    14866  20979  18502   -312    341   3936       C  
ATOM   2222  C   SER A 368     -82.578 -28.513  14.889  1.00145.83           C  
ANISOU 2222  C   SER A 368    14930  21440  19040   -585    227   4321       C  
ATOM   2223  O   SER A 368     -83.749 -28.129  14.857  1.00148.65           O  
ANISOU 2223  O   SER A 368    14897  21956  19626   -549    305   4544       O  
ATOM   2224  CB  SER A 368     -81.633 -26.279  14.137  1.00142.77           C  
ANISOU 2224  CB  SER A 368    14740  20862  18644   -160    278   3858       C  
ATOM   2225  OG  SER A 368     -81.324 -26.560  12.781  1.00141.17           O  
ANISOU 2225  OG  SER A 368    14696  20454  18488   -360    -74   3850       O  
ATOM   2226  N   ARG A 369     -82.224 -29.794  14.787  1.00145.26           N  
ANISOU 2226  N   ARG A 369    15044  21262  18884   -857     32   4392       N  
ATOM   2227  CA  ARG A 369     -83.184 -30.893  14.756  1.00148.02           C  
ANISOU 2227  CA  ARG A 369    15170  21676  19394  -1157    -89   4747       C  
ATOM   2228  C   ARG A 369     -84.107 -30.838  13.556  1.00149.46           C  
ANISOU 2228  C   ARG A 369    15108  21818  19860  -1328   -365   4930       C  
ATOM   2229  O   ARG A 369     -85.285 -31.137  13.678  1.00152.78           O  
ANISOU 2229  O   ARG A 369    15151  22398  20499  -1462   -353   5249       O  
ATOM   2230  CB  ARG A 369     -84.016 -30.902  16.041  1.00151.24           C  
ANISOU 2230  CB  ARG A 369    15262  22386  19817  -1077    265   4976       C  
ATOM   2231  CG  ARG A 369     -83.222 -31.132  17.319  1.00150.60           C  
ANISOU 2231  CG  ARG A 369    15413  22380  19426   -950    520   4854       C  
ATOM   2232  CD  ARG A 369     -82.915 -32.610  17.551  1.00150.87           C  
ANISOU 2232  CD  ARG A 369    15639  22309  19376  -1243    360   5008       C  
ATOM   2233  NE  ARG A 369     -81.800 -33.071  16.737  1.00147.62           N  
ANISOU 2233  NE  ARG A 369    15628  21581  18881  -1339     43   4774       N  
ATOM   2234  CZ  ARG A 369     -81.908 -33.991  15.783  1.00147.66           C  
ANISOU 2234  CZ  ARG A 369    15705  21372  19028  -1638   -307   4872       C  
ATOM   2235  NH1 ARG A 369     -83.081 -34.566  15.541  1.00150.76           N  
ANISOU 2235  NH1 ARG A 369    15793  21825  19665  -1895   -409   5214       N  
ATOM   2236  NH2 ARG A 369     -80.838 -34.349  15.083  1.00144.90           N  
ANISOU 2236  NH2 ARG A 369    15725  20751  18577  -1682   -553   4621       N  
ATOM   2237  N   LEU A 370     -83.578 -30.489  12.391  1.00147.26           N  
ANISOU 2237  N   LEU A 370    15039  21339  19575  -1339   -623   4744       N  
ATOM   2238  CA  LEU A 370     -84.437 -30.308  11.229  1.00148.81           C  
ANISOU 2238  CA  LEU A 370    15017  21514  20010  -1475   -899   4909       C  
ATOM   2239  C   LEU A 370     -84.163 -31.341  10.149  1.00148.22           C  
ANISOU 2239  C   LEU A 370    15183  21218  19916  -1804  -1315   4900       C  
ATOM   2240  O   LEU A 370     -83.386 -32.273  10.352  1.00146.88           O  
ANISOU 2240  O   LEU A 370    15319  20907  19583  -1928  -1375   4790       O  
ATOM   2241  CB  LEU A 370     -84.283 -28.904  10.651  1.00147.70           C  
ANISOU 2241  CB  LEU A 370    14869  21349  19900  -1211   -869   4750       C  
ATOM   2242  CG  LEU A 370     -84.420 -27.769  11.663  1.00148.23           C  
ANISOU 2242  CG  LEU A 370    14759  21583  19978   -848   -466   4683       C  
ATOM   2243  CD1 LEU A 370     -84.286 -26.429  10.969  1.00147.45           C  
ANISOU 2243  CD1 LEU A 370    14671  21402  19950   -617   -490   4547       C  
ATOM   2244  CD2 LEU A 370     -85.713 -27.865  12.428  1.00152.07           C  
ANISOU 2244  CD2 LEU A 370    14774  22337  20671   -834   -266   4989       C  
ATOM   2245  N   GLU A 371     -84.839 -31.184   9.013  1.00149.61           N  
ANISOU 2245  N   GLU A 371    15216  21366  20262  -1937  -1608   5020       N  
ATOM   2246  CA  GLU A 371     -84.679 -32.089   7.877  1.00149.59           C  
ANISOU 2246  CA  GLU A 371    15438  21165  20235  -2248  -2027   4996       C  
ATOM   2247  C   GLU A 371     -83.241 -32.116   7.406  1.00146.02           C  
ANISOU 2247  C   GLU A 371    15485  20499  19498  -2184  -2087   4634       C  
ATOM   2248  O   GLU A 371     -82.531 -31.117   7.520  1.00143.75           O  
ANISOU 2248  O   GLU A 371    15318  20216  19085  -1910  -1892   4427       O  
ATOM   2249  CB  GLU A 371     -85.596 -31.693   6.713  1.00151.81           C  
ANISOU 2249  CB  GLU A 371    15494  21480  20709  -2355  -2330   5161       C  
ATOM   2250  CG  GLU A 371     -87.101 -31.691   7.032  1.00155.89           C  
ANISOU 2250  CG  GLU A 371    15460  22217  21555  -2441  -2319   5541       C  
ATOM   2251  CD  GLU A 371     -87.633 -30.329   7.459  1.00156.69           C  
ANISOU 2251  CD  GLU A 371    15220  22520  21797  -2098  -2033   5616       C  
ATOM   2252  OE1 GLU A 371     -86.819 -29.423   7.748  1.00154.06           O  
ANISOU 2252  OE1 GLU A 371    15081  22153  21300  -1793  -1794   5373       O  
ATOM   2253  OE2 GLU A 371     -88.871 -30.162   7.489  1.00160.24           O  
ANISOU 2253  OE2 GLU A 371    15195  23152  22536  -2135  -2056   5915       O  
ATOM   2254  N   VAL A 372     -82.804 -33.263   6.891  1.00148.57           N  
ANISOU 2254  N   VAL A 372    16090  20627  19731  -2434  -2351   4553       N  
ATOM   2255  CA  VAL A 372     -81.423 -33.400   6.446  1.00145.56           C  
ANISOU 2255  CA  VAL A 372    16166  20051  19088  -2375  -2398   4206       C  
ATOM   2256  C   VAL A 372     -81.383 -33.837   4.977  1.00146.17           C  
ANISOU 2256  C   VAL A 372    16448  19973  19116  -2597  -2795   4127       C  
ATOM   2257  O   VAL A 372     -80.355 -33.714   4.310  1.00144.10           O  
ANISOU 2257  O   VAL A 372    16527  19585  18638  -2535  -2849   3846       O  
ATOM   2258  CB  VAL A 372     -80.654 -34.414   7.318  1.00145.72           C  
ANISOU 2258  CB  VAL A 372    16413  19959  18993  -2406  -2300   4106       C  
ATOM   2259  CG1 VAL A 372     -79.173 -34.371   6.994  1.00142.63           C  
ANISOU 2259  CG1 VAL A 372    16439  19406  18350  -2275  -2285   3737       C  
ATOM   2260  CG2 VAL A 372     -80.843 -34.091   8.783  1.00145.86           C  
ANISOU 2260  CG2 VAL A 372    16220  20162  19040  -2225  -1934   4224       C  
ATOM   2261  N   ARG A 373     -82.514 -34.327   4.467  1.00148.11           N  
ANISOU 2261  N   ARG A 373    16476  20243  19554  -2858  -3073   4375       N  
ATOM   2262  CA  ARG A 373     -82.590 -34.748   3.067  1.00149.28           C  
ANISOU 2262  CA  ARG A 373    16813  20264  19644  -3085  -3480   4306       C  
ATOM   2263  C   ARG A 373     -83.846 -34.245   2.353  1.00152.19           C  
ANISOU 2263  C   ARG A 373    16843  20774  20207  -3193  -3709   4572       C  
ATOM   2264  O   ARG A 373     -84.006 -34.451   1.149  1.00153.54           O  
ANISOU 2264  O   ARG A 373    17148  20877  20315  -3373  -4065   4535       O  
ATOM   2265  CB  ARG A 373     -82.497 -36.275   2.954  1.00155.54           C  
ANISOU 2265  CB  ARG A 373    17813  20845  20439  -3381  -3726   4268       C  
ATOM   2266  CG  ARG A 373     -83.733 -37.065   3.395  1.00159.11           C  
ANISOU 2266  CG  ARG A 373    17932  21337  21186  -3656  -3858   4611       C  
ATOM   2267  CD  ARG A 373     -83.447 -38.566   3.272  1.00160.35           C  
ANISOU 2267  CD  ARG A 373    18371  21220  21334  -3934  -4101   4528       C  
ATOM   2268  NE  ARG A 373     -84.587 -39.400   3.638  1.00164.09           N  
ANISOU 2268  NE  ARG A 373    18548  21697  22103  -4244  -4255   4862       N  
ATOM   2269  CZ  ARG A 373     -84.590 -40.729   3.590  1.00166.08           C  
ANISOU 2269  CZ  ARG A 373    18978  21698  22426  -4533  -4494   4864       C  
ATOM   2270  NH1 ARG A 373     -83.514 -41.386   3.188  1.00164.68           N  
ANISOU 2270  NH1 ARG A 373    19278  21247  22046  -4525  -4604   4534       N  
ATOM   2271  NH2 ARG A 373     -85.671 -41.404   3.948  1.00169.74           N  
ANISOU 2271  NH2 ARG A 373    19134  22176  23184  -4830  -4620   5201       N  
ATOM   2272  N   GLY A 374     -84.741 -33.603   3.093  1.00151.90           N  
ANISOU 2272  N   GLY A 374    16367  20945  20404  -3078  -3510   4836       N  
ATOM   2273  CA  GLY A 374     -86.001 -33.168   2.520  1.00155.10           C  
ANISOU 2273  CA  GLY A 374    16390  21498  21044  -3168  -3724   5119       C  
ATOM   2274  C   GLY A 374     -85.851 -32.163   1.394  1.00154.65           C  
ANISOU 2274  C   GLY A 374    16433  21452  20874  -3050  -3878   5043       C  
ATOM   2275  O   GLY A 374     -84.770 -31.619   1.177  1.00151.67           O  
ANISOU 2275  O   GLY A 374    16384  20994  20251  -2860  -3744   4781       O  
ATOM   2276  N   GLY A 375     -86.936 -31.930   0.662  1.00157.88           N  
ANISOU 2276  N   GLY A 375    16555  21964  21469  -3175  -4174   5289       N  
ATOM   2277  CA  GLY A 375     -86.930 -30.950  -0.409  1.00158.10           C  
ANISOU 2277  CA  GLY A 375    16645  22018  21407  -3070  -4346   5282       C  
ATOM   2278  C   GLY A 375     -86.825 -29.558   0.176  1.00156.67           C  
ANISOU 2278  C   GLY A 375    16290  21937  21299  -2681  -3980   5306       C  
ATOM   2279  O   GLY A 375     -86.190 -28.671  -0.392  1.00155.09           O  
ANISOU 2279  O   GLY A 375    16310  21687  20930  -2506  -3952   5176       O  
ATOM   2280  N   THR A 376     -87.468 -29.384   1.328  1.00157.56           N  
ANISOU 2280  N   THR A 376    16009  22188  21668  -2553  -3696   5477       N  
ATOM   2281  CA  THR A 376     -87.418 -28.138   2.082  1.00156.58           C  
ANISOU 2281  CA  THR A 376    15705  22152  21635  -2171  -3311   5477       C  
ATOM   2282  C   THR A 376     -85.990 -27.881   2.521  1.00152.42           C  
ANISOU 2282  C   THR A 376    15595  21493  20824  -1984  -3020   5132       C  
ATOM   2283  O   THR A 376     -85.521 -26.745   2.521  1.00150.99           O  
ANISOU 2283  O   THR A 376    15489  21285  20596  -1711  -2841   5025       O  
ATOM   2284  CB  THR A 376     -88.339 -28.179   3.318  1.00158.63           C  
ANISOU 2284  CB  THR A 376    15486  22602  22182  -2085  -3032   5694       C  
ATOM   2285  OG1 THR A 376     -89.682 -28.458   2.907  1.00162.83           O  
ANISOU 2285  OG1 THR A 376    15588  23270  23010  -2278  -3311   6029       O  
ATOM   2286  CG2 THR A 376     -88.307 -26.847   4.059  1.00158.03           C  
ANISOU 2286  CG2 THR A 376    15244  22607  22194  -1667  -2641   5659       C  
ATOM   2287  N   PHE A 377     -85.311 -28.952   2.910  1.00150.77           N  
ANISOU 2287  N   PHE A 377    15645  21192  20447  -2139  -2984   4968       N  
ATOM   2288  CA  PHE A 377     -83.910 -28.879   3.267  1.00147.06           C  
ANISOU 2288  CA  PHE A 377    15574  20596  19707  -1999  -2758   4638       C  
ATOM   2289  C   PHE A 377     -83.084 -28.295   2.125  1.00145.49           C  
ANISOU 2289  C   PHE A 377    15714  20277  19289  -1960  -2901   4450       C  
ATOM   2290  O   PHE A 377     -82.440 -27.256   2.285  1.00143.68           O  
ANISOU 2290  O   PHE A 377    15578  20022  18991  -1707  -2678   4314       O  
ATOM   2291  CB  PHE A 377     -83.400 -30.269   3.639  1.00148.24           C  
ANISOU 2291  CB  PHE A 377    15949  20644  19731  -2210  -2796   4525       C  
ATOM   2292  CG  PHE A 377     -81.911 -30.350   3.799  1.00144.75           C  
ANISOU 2292  CG  PHE A 377    15934  20059  19008  -2102  -2644   4180       C  
ATOM   2293  CD1 PHE A 377     -81.288 -29.844   4.931  1.00142.74           C  
ANISOU 2293  CD1 PHE A 377    15692  19841  18701  -1845  -2270   4051       C  
ATOM   2294  CD2 PHE A 377     -81.132 -30.941   2.817  1.00143.81           C  
ANISOU 2294  CD2 PHE A 377    16194  19777  18672  -2255  -2880   3976       C  
ATOM   2295  CE1 PHE A 377     -79.924 -29.926   5.078  1.00139.83           C  
ANISOU 2295  CE1 PHE A 377    15683  19351  18095  -1754  -2153   3743       C  
ATOM   2296  CE2 PHE A 377     -79.765 -31.024   2.959  1.00140.93           C  
ANISOU 2296  CE2 PHE A 377    16181  19294  18071  -2148  -2733   3664       C  
ATOM   2297  CZ  PHE A 377     -79.161 -30.515   4.093  1.00138.91           C  
ANISOU 2297  CZ  PHE A 377    15910  19079  17792  -1902  -2378   3557       C  
ATOM   2298  N   GLU A 378     -83.132 -28.930   0.959  1.00146.55           N  
ANISOU 2298  N   GLU A 378    16029  20340  19313  -2216  -3273   4448       N  
ATOM   2299  CA  GLU A 378     -82.325 -28.452  -0.161  1.00145.41           C  
ANISOU 2299  CA  GLU A 378    16227  20104  18917  -2199  -3397   4276       C  
ATOM   2300  C   GLU A 378     -82.773 -27.071  -0.639  1.00146.50           C  
ANISOU 2300  C   GLU A 378    16192  20311  19159  -2018  -3405   4439       C  
ATOM   2301  O   GLU A 378     -81.989 -26.323  -1.220  1.00145.16           O  
ANISOU 2301  O   GLU A 378    16270  20076  18810  -1910  -3363   4308       O  
ATOM   2302  CB  GLU A 378     -82.334 -29.447  -1.325  1.00146.84           C  
ANISOU 2302  CB  GLU A 378    16651  20212  18930  -2510  -3799   4229       C  
ATOM   2303  CG  GLU A 378     -81.442 -30.665  -1.078  1.00145.23           C  
ANISOU 2303  CG  GLU A 378    16770  19866  18546  -2635  -3775   3964       C  
ATOM   2304  CD  GLU A 378     -81.293 -31.564  -2.297  1.00146.70           C  
ANISOU 2304  CD  GLU A 378    17262  19953  18526  -2906  -4152   3845       C  
ATOM   2305  OE1 GLU A 378     -82.116 -31.462  -3.234  1.00149.48           O  
ANISOU 2305  OE1 GLU A 378    17525  20367  18905  -3059  -4481   4016       O  
ATOM   2306  OE2 GLU A 378     -80.337 -32.370  -2.317  1.00145.30           O  
ANISOU 2306  OE2 GLU A 378    17420  19634  18154  -2953  -4123   3570       O  
ATOM   2307  N   SER A 379     -84.033 -26.739  -0.389  1.00149.19           N  
ANISOU 2307  N   SER A 379    16100  20781  19805  -1984  -3457   4737       N  
ATOM   2308  CA  SER A 379     -84.531 -25.397  -0.649  1.00150.53           C  
ANISOU 2308  CA  SER A 379    16057  21003  20137  -1763  -3434   4910       C  
ATOM   2309  C   SER A 379     -83.809 -24.409   0.259  1.00148.11           C  
ANISOU 2309  C   SER A 379    15789  20647  19839  -1434  -3009   4745       C  
ATOM   2310  O   SER A 379     -83.388 -23.335  -0.181  1.00147.62           O  
ANISOU 2310  O   SER A 379    15846  20511  19732  -1267  -2963   4709       O  
ATOM   2311  CB  SER A 379     -86.039 -25.335  -0.424  1.00154.18           C  
ANISOU 2311  CB  SER A 379    15999  21623  20959  -1773  -3547   5253       C  
ATOM   2312  OG  SER A 379     -86.697 -26.367  -1.139  1.00156.57           O  
ANISOU 2312  OG  SER A 379    16253  21966  21270  -2112  -3947   5390       O  
ATOM   2313  N   ARG A 380     -83.659 -24.799   1.525  1.00146.86           N  
ANISOU 2313  N   ARG A 380    15545  20524  19729  -1356  -2711   4648       N  
ATOM   2314  CA  ARG A 380     -82.938 -24.012   2.520  1.00144.69           C  
ANISOU 2314  CA  ARG A 380    15327  20210  19437  -1066  -2312   4454       C  
ATOM   2315  C   ARG A 380     -81.508 -23.788   2.078  1.00141.73           C  
ANISOU 2315  C   ARG A 380    15398  19679  18772  -1052  -2269   4164       C  
ATOM   2316  O   ARG A 380     -80.968 -22.694   2.221  1.00140.74           O  
ANISOU 2316  O   ARG A 380    15348  19478  18646   -831  -2081   4057       O  
ATOM   2317  CB  ARG A 380     -82.945 -24.707   3.889  1.00144.02           C  
ANISOU 2317  CB  ARG A 380    15135  20208  19378  -1041  -2047   4393       C  
ATOM   2318  CG  ARG A 380     -84.275 -24.686   4.612  1.00147.02           C  
ANISOU 2318  CG  ARG A 380    15033  20771  20056   -979  -1954   4662       C  
ATOM   2319  CD  ARG A 380     -84.113 -25.029   6.092  1.00146.30           C  
ANISOU 2319  CD  ARG A 380    14872  20771  19945   -873  -1596   4575       C  
ATOM   2320  NE  ARG A 380     -83.747 -26.427   6.324  1.00145.36           N  
ANISOU 2320  NE  ARG A 380    14927  20630  19672  -1134  -1673   4529       N  
ATOM   2321  CZ  ARG A 380     -84.622 -27.380   6.637  1.00147.62           C  
ANISOU 2321  CZ  ARG A 380    14968  21030  20092  -1337  -1747   4759       C  
ATOM   2322  NH1 ARG A 380     -85.906 -27.082   6.752  1.00150.93           N  
ANISOU 2322  NH1 ARG A 380    14933  21619  20796  -1308  -1743   5047       N  
ATOM   2323  NH2 ARG A 380     -84.221 -28.629   6.837  1.00146.87           N  
ANISOU 2323  NH2 ARG A 380    15067  20870  19867  -1568  -1826   4712       N  
ATOM   2324  N   ILE A 381     -80.895 -24.836   1.545  1.00143.17           N  
ANISOU 2324  N   ILE A 381    15869  19805  18722  -1289  -2440   4033       N  
ATOM   2325  CA  ILE A 381     -79.530 -24.727   1.048  1.00140.71           C  
ANISOU 2325  CA  ILE A 381    15963  19369  18132  -1292  -2401   3760       C  
ATOM   2326  C   ILE A 381     -79.432 -23.784  -0.144  1.00141.55           C  
ANISOU 2326  C   ILE A 381    16179  19427  18176  -1275  -2550   3829       C  
ATOM   2327  O   ILE A 381     -78.561 -22.914  -0.180  1.00140.09           O  
ANISOU 2327  O   ILE A 381    16160  19158  17910  -1129  -2376   3687       O  
ATOM   2328  CB  ILE A 381     -78.968 -26.100   0.668  1.00138.01           C  
ANISOU 2328  CB  ILE A 381    15894  18977  17568  -1538  -2563   3604       C  
ATOM   2329  CG1 ILE A 381     -78.607 -26.879   1.934  1.00136.52           C  
ANISOU 2329  CG1 ILE A 381    15699  18786  17386  -1507  -2350   3475       C  
ATOM   2330  CG2 ILE A 381     -77.723 -25.945  -0.173  1.00136.38           C  
ANISOU 2330  CG2 ILE A 381    16072  18671  17077  -1559  -2575   3366       C  
ATOM   2331  CD1 ILE A 381     -78.146 -28.282   1.658  1.00136.13           C  
ANISOU 2331  CD1 ILE A 381    15894  18657  17172  -1731  -2516   3341       C  
ATOM   2332  N   GLN A 382     -80.333 -23.943  -1.106  1.00141.64           N  
ANISOU 2332  N   GLN A 382    16093  19494  18229  -1431  -2880   4062       N  
ATOM   2333  CA  GLN A 382     -80.350 -23.065  -2.270  1.00142.98           C  
ANISOU 2333  CA  GLN A 382    16360  19637  18330  -1424  -3055   4179       C  
ATOM   2334  C   GLN A 382     -80.408 -21.624  -1.820  1.00143.08           C  
ANISOU 2334  C   GLN A 382    16217  19600  18545  -1132  -2830   4252       C  
ATOM   2335  O   GLN A 382     -79.633 -20.786  -2.271  1.00142.33           O  
ANISOU 2335  O   GLN A 382    16337  19407  18337  -1053  -2755   4178       O  
ATOM   2336  CB  GLN A 382     -81.541 -23.371  -3.178  1.00152.73           C  
ANISOU 2336  CB  GLN A 382    17426  20965  19639  -1604  -3456   4467       C  
ATOM   2337  CG  GLN A 382     -81.451 -24.733  -3.820  1.00153.13           C  
ANISOU 2337  CG  GLN A 382    17686  21031  19467  -1912  -3729   4375       C  
ATOM   2338  CD  GLN A 382     -80.188 -24.899  -4.634  1.00151.57           C  
ANISOU 2338  CD  GLN A 382    17951  20754  18883  -1992  -3732   4116       C  
ATOM   2339  OE1 GLN A 382     -79.619 -25.990  -4.695  1.00150.57           O  
ANISOU 2339  OE1 GLN A 382    18057  20588  18566  -2146  -3766   3895       O  
ATOM   2340  NE2 GLN A 382     -79.756 -23.824  -5.294  1.00151.69           N  
ANISOU 2340  NE2 GLN A 382    18102  20744  18791  -1889  -3698   4153       N  
ATOM   2341  N   GLY A 383     -81.327 -21.349  -0.906  1.00144.31           N  
ANISOU 2341  N   GLY A 383    16000  19822  19010   -974  -2712   4394       N  
ATOM   2342  CA  GLY A 383     -81.435 -20.026  -0.343  1.00144.70           C  
ANISOU 2342  CA  GLY A 383    15892  19808  19280   -669  -2479   4430       C  
ATOM   2343  C   GLY A 383     -80.155 -19.595   0.336  1.00141.74           C  
ANISOU 2343  C   GLY A 383    15760  19312  18781   -530  -2153   4118       C  
ATOM   2344  O   GLY A 383     -79.742 -18.457   0.190  1.00141.76           O  
ANISOU 2344  O   GLY A 383    15844  19186  18831   -370  -2053   4093       O  
ATOM   2345  N   ALA A 384     -79.504 -20.513   1.043  1.00140.72           N  
ANISOU 2345  N   ALA A 384    15755  19212  18499   -604  -2010   3888       N  
ATOM   2346  CA  ALA A 384     -78.263 -20.202   1.758  1.00138.03           C  
ANISOU 2346  CA  ALA A 384    15629  18776  18041   -484  -1721   3582       C  
ATOM   2347  C   ALA A 384     -77.163 -19.726   0.819  1.00136.94           C  
ANISOU 2347  C   ALA A 384    15822  18512  17699   -546  -1762   3462       C  
ATOM   2348  O   ALA A 384     -76.495 -18.736   1.086  1.00136.24           O  
ANISOU 2348  O   ALA A 384    15815  18305  17645   -390  -1574   3342       O  
ATOM   2349  CB  ALA A 384     -77.789 -21.405   2.540  1.00137.64           C  
ANISOU 2349  CB  ALA A 384    15662  18788  17849   -579  -1626   3394       C  
ATOM   2350  N   VAL A 385     -76.954 -20.464  -0.261  1.00135.84           N  
ANISOU 2350  N   VAL A 385    15876  18400  17338   -782  -2002   3484       N  
ATOM   2351  CA  VAL A 385     -75.917 -20.123  -1.217  1.00135.17           C  
ANISOU 2351  CA  VAL A 385    16104  18233  17021   -863  -2029   3381       C  
ATOM   2352  C   VAL A 385     -76.293 -18.866  -2.012  1.00137.31           C  
ANISOU 2352  C   VAL A 385    16343  18435  17394   -792  -2123   3614       C  
ATOM   2353  O   VAL A 385     -75.438 -18.021  -2.301  1.00136.85           O  
ANISOU 2353  O   VAL A 385    16459  18265  17273   -743  -2005   3541       O  
ATOM   2354  CB  VAL A 385     -75.645 -21.296  -2.164  1.00136.44           C  
ANISOU 2354  CB  VAL A 385    16489  18457  16895  -1122  -2254   3325       C  
ATOM   2355  CG1 VAL A 385     -74.435 -21.006  -3.018  1.00135.72           C  
ANISOU 2355  CG1 VAL A 385    16721  18311  16535  -1189  -2210   3177       C  
ATOM   2356  CG2 VAL A 385     -75.413 -22.562  -1.357  1.00134.81           C  
ANISOU 2356  CG2 VAL A 385    16295  18288  16639  -1183  -2192   3135       C  
ATOM   2357  N   LEU A 386     -77.570 -18.746  -2.364  1.00139.71           N  
ANISOU 2357  N   LEU A 386    16412  18802  17870   -790  -2343   3909       N  
ATOM   2358  CA  LEU A 386     -78.069 -17.554  -3.052  1.00142.20           C  
ANISOU 2358  CA  LEU A 386    16660  19045  18327   -695  -2459   4172       C  
ATOM   2359  C   LEU A 386     -77.840 -16.294  -2.235  1.00141.99           C  
ANISOU 2359  C   LEU A 386    16544  18859  18545   -420  -2184   4121       C  
ATOM   2360  O   LEU A 386     -77.332 -15.302  -2.748  1.00142.59           O  
ANISOU 2360  O   LEU A 386    16771  18793  18615   -374  -2157   4164       O  
ATOM   2361  CB  LEU A 386     -79.547 -17.700  -3.379  1.00145.22           C  
ANISOU 2361  CB  LEU A 386    16740  19535  18902   -712  -2739   4493       C  
ATOM   2362  CG  LEU A 386     -79.777 -18.547  -4.624  1.00146.57           C  
ANISOU 2362  CG  LEU A 386    17058  19817  18814   -997  -3102   4605       C  
ATOM   2363  CD1 LEU A 386     -81.225 -19.009  -4.726  1.00149.32           C  
ANISOU 2363  CD1 LEU A 386    17072  20300  19365  -1056  -3382   4872       C  
ATOM   2364  CD2 LEU A 386     -79.378 -17.733  -5.841  1.00148.02           C  
ANISOU 2364  CD2 LEU A 386    17483  19934  18822  -1040  -3239   4737       C  
ATOM   2365  N   ALA A 387     -78.267 -16.318  -0.980  1.00141.54           N  
ANISOU 2365  N   ALA A 387    16243  18826  18708   -241  -1987   4040       N  
ATOM   2366  CA  ALA A 387     -77.993 -15.231  -0.053  1.00141.33           C  
ANISOU 2366  CA  ALA A 387    16156  18650  18892     27  -1705   3918       C  
ATOM   2367  C   ALA A 387     -76.490 -15.058   0.181  1.00138.71           C  
ANISOU 2367  C   ALA A 387    16129  18204  18369     -5  -1499   3608       C  
ATOM   2368  O   ALA A 387     -76.023 -13.949   0.439  1.00138.97           O  
ANISOU 2368  O   ALA A 387    16220  18055  18529    147  -1347   3534       O  
ATOM   2369  CB  ALA A 387     -78.708 -15.465   1.252  1.00141.50           C  
ANISOU 2369  CB  ALA A 387    15881  18767  19115    203  -1524   3865       C  
ATOM   2370  N   ASP A 388     -75.740 -16.153   0.107  1.00136.44           N  
ANISOU 2370  N   ASP A 388    16026  18013  17802   -199  -1502   3424       N  
ATOM   2371  CA  ASP A 388     -74.290 -16.071   0.230  1.00134.21           C  
ANISOU 2371  CA  ASP A 388    16010  17648  17338   -245  -1331   3143       C  
ATOM   2372  C   ASP A 388     -73.742 -15.137  -0.826  1.00135.27           C  
ANISOU 2372  C   ASP A 388    16330  17645  17420   -302  -1387   3240       C  
ATOM   2373  O   ASP A 388     -73.186 -14.090  -0.503  1.00135.37           O  
ANISOU 2373  O   ASP A 388    16389  17487  17558   -184  -1224   3158       O  
ATOM   2374  CB  ASP A 388     -73.637 -17.460   0.116  1.00134.90           C  
ANISOU 2374  CB  ASP A 388    16260  17860  17137   -444  -1368   2964       C  
ATOM   2375  CG  ASP A 388     -72.095 -17.407   0.059  1.00132.98           C  
ANISOU 2375  CG  ASP A 388    16275  17550  16701   -503  -1214   2692       C  
ATOM   2376  OD1 ASP A 388     -71.447 -17.194   1.108  1.00131.55           O  
ANISOU 2376  OD1 ASP A 388    16087  17318  16577   -383   -996   2462       O  
ATOM   2377  OD2 ASP A 388     -71.526 -17.625  -1.037  1.00133.12           O  
ANISOU 2377  OD2 ASP A 388    16499  17584  16497   -674  -1313   2702       O  
ATOM   2378  N   GLY A 389     -73.957 -15.476  -2.089  1.00136.46           N  
ANISOU 2378  N   GLY A 389    16586  17868  17393   -486  -1627   3431       N  
ATOM   2379  CA  GLY A 389     -73.410 -14.655  -3.148  1.00137.73           C  
ANISOU 2379  CA  GLY A 389    16947  17928  17457   -565  -1677   3550       C  
ATOM   2380  C   GLY A 389     -74.035 -13.273  -3.249  1.00140.28           C  
ANISOU 2380  C   GLY A 389    17150  18075  18074   -395  -1707   3799       C  
ATOM   2381  O   GLY A 389     -73.337 -12.289  -3.522  1.00140.90           O  
ANISOU 2381  O   GLY A 389    17368  17981  18185   -381  -1613   3811       O  
ATOM   2382  N   ILE A 390     -75.345 -13.194  -3.024  1.00142.03           N  
ANISOU 2382  N   ILE A 390    17103  18331  18531   -264  -1837   4005       N  
ATOM   2383  CA  ILE A 390     -76.048 -11.909  -2.985  1.00144.74           C  
ANISOU 2383  CA  ILE A 390    17289  18495  19209    -49  -1861   4231       C  
ATOM   2384  C   ILE A 390     -75.416 -10.968  -1.971  1.00144.01           C  
ANISOU 2384  C   ILE A 390    17207  18184  19327    150  -1568   4007       C  
ATOM   2385  O   ILE A 390     -75.140  -9.808  -2.274  1.00145.65           O  
ANISOU 2385  O   ILE A 390    17502  18163  19677    220  -1545   4103       O  
ATOM   2386  CB  ILE A 390     -77.531 -12.089  -2.661  1.00146.62           C  
ANISOU 2386  CB  ILE A 390    17178  18834  19698     93  -1996   4431       C  
ATOM   2387  CG1 ILE A 390     -78.272 -12.528  -3.921  1.00148.77           C  
ANISOU 2387  CG1 ILE A 390    17439  19246  19840    -85  -2362   4749       C  
ATOM   2388  CG2 ILE A 390     -78.127 -10.791  -2.133  1.00148.98           C  
ANISOU 2388  CG2 ILE A 390    17277  18928  20401    402  -1906   4538       C  
ATOM   2389  CD1 ILE A 390     -79.719 -12.823  -3.688  1.00150.84           C  
ANISOU 2389  CD1 ILE A 390    17332  19638  20344     12  -2526   4959       C  
ATOM   2390  N   ASN A 391     -75.196 -11.470  -0.762  1.00141.84           N  
ANISOU 2390  N   ASN A 391    16850  17972  19069    234  -1357   3715       N  
ATOM   2391  CA  ASN A 391     -74.537 -10.687   0.269  1.00141.15           C  
ANISOU 2391  CA  ASN A 391    16793  17701  19137    407  -1090   3453       C  
ATOM   2392  C   ASN A 391     -73.073 -10.446  -0.044  1.00139.70           C  
ANISOU 2392  C   ASN A 391    16899  17409  18773    248   -992   3274       C  
ATOM   2393  O   ASN A 391     -72.462  -9.526   0.484  1.00139.95           O  
ANISOU 2393  O   ASN A 391    16992  17228  18955    350   -830   3118       O  
ATOM   2394  CB  ASN A 391     -74.640 -11.380   1.616  1.00139.37           C  
ANISOU 2394  CB  ASN A 391    16429  17611  18916    516   -905   3193       C  
ATOM   2395  CG  ASN A 391     -76.044 -11.428   2.128  1.00141.22           C  
ANISOU 2395  CG  ASN A 391    16341  17938  19379    710   -928   3347       C  
ATOM   2396  OD1 ASN A 391     -76.894 -10.636   1.715  1.00144.06           O  
ANISOU 2396  OD1 ASN A 391    16557  18197  19982    845  -1036   3598       O  
ATOM   2397  ND2 ASN A 391     -76.296 -12.336   3.063  1.00139.92           N  
ANISOU 2397  ND2 ASN A 391    16047  17966  19150    735   -818   3208       N  
ATOM   2398  N   SER A 392     -72.495 -11.282  -0.891  1.00138.44           N  
ANISOU 2398  N   SER A 392    16911  17397  18294     -5  -1087   3282       N  
ATOM   2399  CA  SER A 392     -71.141 -11.012  -1.323  1.00137.62           C  
ANISOU 2399  CA  SER A 392    17053  17211  18026   -161   -991   3153       C  
ATOM   2400  C   SER A 392     -71.123  -9.749  -2.189  1.00140.39           C  
ANISOU 2400  C   SER A 392    17494  17344  18504   -172  -1061   3415       C  
ATOM   2401  O   SER A 392     -70.321  -8.845  -1.949  1.00140.75           O  
ANISOU 2401  O   SER A 392    17632  17177  18670   -154   -915   3311       O  
ATOM   2402  CB  SER A 392     -70.568 -12.219  -2.060  1.00136.06           C  
ANISOU 2402  CB  SER A 392    17012  17233  17452   -405  -1062   3095       C  
ATOM   2403  OG  SER A 392     -70.401 -13.309  -1.166  1.00133.59           O  
ANISOU 2403  OG  SER A 392    16640  17067  17050   -389   -978   2833       O  
ATOM   2404  N   VAL A 393     -72.037  -9.652  -3.152  1.00142.65           N  
ANISOU 2404  N   VAL A 393    17748  17668  18785   -201  -1297   3764       N  
ATOM   2405  CA  VAL A 393     -72.129  -8.426  -3.955  1.00145.73           C  
ANISOU 2405  CA  VAL A 393    18218  17838  19314   -193  -1387   4061       C  
ATOM   2406  C   VAL A 393     -72.495  -7.217  -3.098  1.00147.31           C  
ANISOU 2406  C   VAL A 393    18284  17742  19945     80  -1286   4048       C  
ATOM   2407  O   VAL A 393     -71.869  -6.161  -3.191  1.00148.65           O  
ANISOU 2407  O   VAL A 393    18577  17646  20256     81  -1204   4065       O  
ATOM   2408  CB  VAL A 393     -73.169  -8.540  -5.091  1.00148.28           C  
ANISOU 2408  CB  VAL A 393    18507  18265  19566   -246  -1697   4460       C  
ATOM   2409  CG1 VAL A 393     -73.395  -7.181  -5.743  1.00151.84           C  
ANISOU 2409  CG1 VAL A 393    19011  18455  20226   -183  -1797   4792       C  
ATOM   2410  CG2 VAL A 393     -72.722  -9.544  -6.125  1.00147.52           C  
ANISOU 2410  CG2 VAL A 393    18609  18421  19022   -529  -1810   4482       C  
ATOM   2411  N   VAL A 394     -73.513  -7.382  -2.260  1.00147.43           N  
ANISOU 2411  N   VAL A 394    18045  17801  20172    308  -1286   4012       N  
ATOM   2412  CA  VAL A 394     -73.967  -6.308  -1.386  1.00149.23           C  
ANISOU 2412  CA  VAL A 394    18130  17768  20804    606  -1178   3966       C  
ATOM   2413  C   VAL A 394     -72.819  -5.790  -0.531  1.00147.96           C  
ANISOU 2413  C   VAL A 394    18102  17415  20700    627   -925   3612       C  
ATOM   2414  O   VAL A 394     -72.598  -4.587  -0.447  1.00150.08           O  
ANISOU 2414  O   VAL A 394    18435  17360  21228    728   -878   3631       O  
ATOM   2415  CB  VAL A 394     -75.121  -6.768  -0.468  1.00149.26           C  
ANISOU 2415  CB  VAL A 394    17826  17920  20968    839  -1151   3915       C  
ATOM   2416  CG1 VAL A 394     -75.421  -5.713   0.584  1.00151.02           C  
ANISOU 2416  CG1 VAL A 394    17926  17887  21566   1164   -977   3771       C  
ATOM   2417  CG2 VAL A 394     -76.358  -7.095  -1.288  1.00151.30           C  
ANISOU 2417  CG2 VAL A 394    17905  18330  21254    838  -1426   4292       C  
ATOM   2418  N   ALA A 395     -72.070  -6.704   0.074  1.00144.75           N  
ANISOU 2418  N   ALA A 395    17743  17196  20058    522   -785   3297       N  
ATOM   2419  CA  ALA A 395     -70.935  -6.328   0.906  1.00143.52           C  
ANISOU 2419  CA  ALA A 395    17703  16898  19932    521   -572   2946       C  
ATOM   2420  C   ALA A 395     -69.849  -5.628   0.090  1.00144.35           C  
ANISOU 2420  C   ALA A 395    18035  16812  20000    312   -571   3012       C  
ATOM   2421  O   ALA A 395     -69.272  -4.633   0.534  1.00145.50           O  
ANISOU 2421  O   ALA A 395    18251  16674  20360    364   -464   2876       O  
ATOM   2422  CB  ALA A 395     -70.366  -7.548   1.602  1.00140.13           C  
ANISOU 2422  CB  ALA A 395    17273  16735  19236    438   -463   2641       C  
ATOM   2423  N   ALA A 396     -69.574  -6.149  -1.102  1.00144.07           N  
ANISOU 2423  N   ALA A 396    18115  16934  19689     69   -688   3219       N  
ATOM   2424  CA  ALA A 396     -68.581  -5.549  -1.993  1.00145.21           C  
ANISOU 2424  CA  ALA A 396    18467  16947  19761   -153   -674   3331       C  
ATOM   2425  C   ALA A 396     -68.916  -4.104  -2.356  1.00148.89           C  
ANISOU 2425  C   ALA A 396    18969  17051  20552    -66   -740   3598       C  
ATOM   2426  O   ALA A 396     -68.044  -3.249  -2.393  1.00150.07           O  
ANISOU 2426  O   ALA A 396    19244  16955  20821   -157   -647   3559       O  
ATOM   2427  CB  ALA A 396     -68.434  -6.387  -3.240  1.00144.82           C  
ANISOU 2427  CB  ALA A 396    18530  17161  19333   -395   -792   3527       C  
ATOM   2428  N   LEU A 397     -70.183  -3.827  -2.622  1.00150.98           N  
ANISOU 2428  N   LEU A 397    19113  17272  20981    109   -911   3878       N  
ATOM   2429  CA  LEU A 397     -70.588  -2.454  -2.875  1.00154.76           C  
ANISOU 2429  CA  LEU A 397    19610  17378  21814    239   -987   4129       C  
ATOM   2430  C   LEU A 397     -70.307  -1.623  -1.627  1.00155.17           C  
ANISOU 2430  C   LEU A 397    19626  17123  22209    441   -807   3811       C  
ATOM   2431  O   LEU A 397     -69.935  -0.457  -1.709  1.00157.75           O  
ANISOU 2431  O   LEU A 397    20063  17080  22795    449   -789   3874       O  
ATOM   2432  CB  LEU A 397     -72.066  -2.395  -3.258  1.00156.98           C  
ANISOU 2432  CB  LEU A 397    19719  17693  22234    432  -1208   4460       C  
ATOM   2433  CG  LEU A 397     -72.436  -3.240  -4.478  1.00156.94           C  
ANISOU 2433  CG  LEU A 397    19750  17999  21880    233  -1428   4763       C  
ATOM   2434  CD1 LEU A 397     -73.924  -3.154  -4.763  1.00159.41           C  
ANISOU 2434  CD1 LEU A 397    19852  18344  22373    433  -1668   5079       C  
ATOM   2435  CD2 LEU A 397     -71.629  -2.814  -5.697  1.00158.54           C  
ANISOU 2435  CD2 LEU A 397    20219  18134  21886    -41  -1485   5016       C  
ATOM   2436  N   ALA A 398     -70.447  -2.259  -0.471  1.00152.78           N  
ANISOU 2436  N   ALA A 398    19187  16977  21887    588   -677   3461       N  
ATOM   2437  CA  ALA A 398     -70.175  -1.631   0.814  1.00153.04           C  
ANISOU 2437  CA  ALA A 398    19195  16780  22173    782   -502   3099       C  
ATOM   2438  C   ALA A 398     -68.693  -1.683   1.158  1.00151.23           C  
ANISOU 2438  C   ALA A 398    19125  16524  21811    565   -354   2789       C  
ATOM   2439  O   ALA A 398     -68.316  -1.554   2.323  1.00150.51           O  
ANISOU 2439  O   ALA A 398    19018  16364  21807    677   -210   2413       O  
ATOM   2440  CB  ALA A 398     -70.986  -2.304   1.900  1.00151.65           C  
ANISOU 2440  CB  ALA A 398    18805  16817  21996   1029   -422   2882       C  
ATOM   2441  N   THR A 399     -67.874  -1.901   0.130  1.00150.74           N  
ANISOU 2441  N   THR A 399    19207  16541  21524    257   -392   2952       N  
ATOM   2442  CA  THR A 399     -66.406  -1.943   0.216  1.00149.48           C  
ANISOU 2442  CA  THR A 399    19179  16376  21240     10   -263   2724       C  
ATOM   2443  C   THR A 399     -65.887  -3.159   0.999  1.00145.72           C  
ANISOU 2443  C   THR A 399    18643  16231  20494    -20   -153   2363       C  
ATOM   2444  O   THR A 399     -64.769  -3.128   1.514  1.00144.80           O  
ANISOU 2444  O   THR A 399    18578  16085  20354   -132    -35   2077       O  
ATOM   2445  CB  THR A 399     -65.802  -0.647   0.837  1.00151.81           C  
ANISOU 2445  CB  THR A 399    19550  16243  21888     48   -183   2550       C  
ATOM   2446  OG1 THR A 399     -66.169  -0.533   2.218  1.00151.46           O  
ANISOU 2446  OG1 THR A 399    19409  16127  22012    323   -103   2198       O  
ATOM   2447  CG2 THR A 399     -66.263   0.587   0.072  1.00155.87           C  
ANISOU 2447  CG2 THR A 399    20141  16383  22699     77   -299   2919       C  
ATOM   2448  N   MET A 400     -66.687  -4.225   1.067  1.00143.84           N  
ANISOU 2448  N   MET A 400    18291  16297  20065     68   -206   2392       N  
ATOM   2449  CA  MET A 400     -66.313  -5.426   1.817  1.00140.55           C  
ANISOU 2449  CA  MET A 400    17820  16179  19405     56   -121   2088       C  
ATOM   2450  C   MET A 400     -65.983  -6.623   0.925  1.00138.58           C  
ANISOU 2450  C   MET A 400    17620  16248  18788   -166   -175   2186       C  
ATOM   2451  O   MET A 400     -66.576  -6.801  -0.133  1.00139.48           O  
ANISOU 2451  O   MET A 400    17755  16440  18800   -237   -312   2502       O  
ATOM   2452  CB  MET A 400     -67.440  -5.819   2.768  1.00140.04           C  
ANISOU 2452  CB  MET A 400    17582  16217  19409    327   -116   2003       C  
ATOM   2453  CG  MET A 400     -67.667  -4.868   3.919  1.00141.66           C  
ANISOU 2453  CG  MET A 400    17739  16172  19915    578    -15   1786       C  
ATOM   2454  SD  MET A 400     -66.212  -4.735   4.944  1.00140.49           S  
ANISOU 2454  SD  MET A 400    17692  15956  19730    503    136   1327       S  
ATOM   2455  CE  MET A 400     -65.904  -6.455   5.299  1.00136.65           C  
ANISOU 2455  CE  MET A 400    17155  15912  18853    414    164   1170       C  
ATOM   2456  N   THR A 401     -65.053  -7.457   1.388  1.00137.92           N  
ANISOU 2456  N   THR A 401    17555  16345  18504   -260    -77   1899       N  
ATOM   2457  CA  THR A 401     -64.604  -8.636   0.646  1.00136.16           C  
ANISOU 2457  CA  THR A 401    17389  16407  17938   -450   -105   1921       C  
ATOM   2458  C   THR A 401     -65.626  -9.767   0.754  1.00134.76           C  
ANISOU 2458  C   THR A 401    17120  16465  17617   -363   -208   1976       C  
ATOM   2459  O   THR A 401     -66.488  -9.718   1.627  1.00134.75           O  
ANISOU 2459  O   THR A 401    16987  16442  17769   -157   -210   1935       O  
ATOM   2460  CB  THR A 401     -63.238  -9.119   1.170  1.00133.74           C  
ANISOU 2460  CB  THR A 401    17114  16192  17511   -551     30   1587       C  
ATOM   2461  OG1 THR A 401     -63.414  -9.773   2.432  1.00131.86           O  
ANISOU 2461  OG1 THR A 401    16779  16057  17266   -390     68   1323       O  
ATOM   2462  CG2 THR A 401     -62.288  -7.937   1.329  1.00135.36           C  
ANISOU 2462  CG2 THR A 401    17366  16142  17924   -625    129   1497       C  
ATOM   2463  N   PRO A 402     -65.536 -10.786  -0.130  1.00135.03           N  
ANISOU 2463  N   PRO A 402    17221  16724  17359   -522   -288   2063       N  
ATOM   2464  CA  PRO A 402     -66.459 -11.928  -0.085  1.00133.93           C  
ANISOU 2464  CA  PRO A 402    17005  16794  17088   -480   -407   2114       C  
ATOM   2465  C   PRO A 402     -66.627 -12.556   1.295  1.00132.08           C  
ANISOU 2465  C   PRO A 402    16648  16637  16901   -327   -331   1865       C  
ATOM   2466  O   PRO A 402     -65.671 -12.704   2.070  1.00130.72           O  
ANISOU 2466  O   PRO A 402    16499  16467  16704   -318   -198   1579       O  
ATOM   2467  CB  PRO A 402     -65.819 -12.929  -1.046  1.00133.43           C  
ANISOU 2467  CB  PRO A 402    17082  16926  16691   -691   -449   2101       C  
ATOM   2468  CG  PRO A 402     -65.187 -12.080  -2.054  1.00135.25           C  
ANISOU 2468  CG  PRO A 402    17444  17060  16886   -834   -421   2247       C  
ATOM   2469  CD  PRO A 402     -64.674 -10.857  -1.325  1.00135.93           C  
ANISOU 2469  CD  PRO A 402    17494  16898  17257   -754   -281   2150       C  
ATOM   2470  N   MET A 403     -67.865 -12.935   1.578  1.00130.44           N  
ANISOU 2470  N   MET A 403    16300  16505  16756   -213   -422   1995       N  
ATOM   2471  CA  MET A 403     -68.216 -13.461   2.875  1.00129.27           C  
ANISOU 2471  CA  MET A 403    16021  16440  16654    -61   -344   1820       C  
ATOM   2472  C   MET A 403     -69.024 -14.734   2.716  1.00128.61           C  
ANISOU 2472  C   MET A 403    15864  16566  16434   -114   -474   1933       C  
ATOM   2473  O   MET A 403     -69.715 -14.933   1.715  1.00129.69           O  
ANISOU 2473  O   MET A 403    15996  16751  16529   -206   -648   2185       O  
ATOM   2474  CB  MET A 403     -69.000 -12.419   3.673  1.00129.89           C  
ANISOU 2474  CB  MET A 403    15955  16372  17025    176   -272   1849       C  
ATOM   2475  CG  MET A 403     -70.275 -11.942   2.999  1.00132.17           C  
ANISOU 2475  CG  MET A 403    16124  16616  17477    241   -412   2187       C  
ATOM   2476  SD  MET A 403     -70.939 -10.478   3.817  1.00134.69           S  
ANISOU 2476  SD  MET A 403    16307  16694  18174    543   -301   2183       S  
ATOM   2477  CE  MET A 403     -71.303 -11.115   5.452  1.00133.64           C  
ANISOU 2477  CE  MET A 403    16019  16728  18030    732   -130   1931       C  
ATOM   2478  N   THR A 404     -68.901 -15.605   3.706  1.00127.31           N  
ANISOU 2478  N   THR A 404    15655  16520  16197    -68   -403   1747       N  
ATOM   2479  CA  THR A 404     -69.611 -16.864   3.711  1.00126.80           C  
ANISOU 2479  CA  THR A 404    15522  16631  16026   -128   -515   1837       C  
ATOM   2480  C   THR A 404     -69.976 -17.296   5.127  1.00126.25           C  
ANISOU 2480  C   THR A 404    15316  16647  16006     17   -400   1723       C  
ATOM   2481  O   THR A 404     -69.719 -16.592   6.111  1.00126.35           O  
ANISOU 2481  O   THR A 404    15294  16596  16118    180   -235   1561       O  
ATOM   2482  CB  THR A 404     -68.805 -17.965   3.022  1.00127.83           C  
ANISOU 2482  CB  THR A 404    15826  16846  15896   -326   -598   1746       C  
ATOM   2483  OG1 THR A 404     -69.584 -19.167   2.992  1.00127.74           O  
ANISOU 2483  OG1 THR A 404    15756  16967  15813   -397   -735   1848       O  
ATOM   2484  CG2 THR A 404     -67.511 -18.218   3.768  1.00126.11           C  
ANISOU 2484  CG2 THR A 404    15703  16626  15588   -306   -449   1434       C  
ATOM   2485  N   THR A 405     -70.560 -18.482   5.204  1.00125.07           N  
ANISOU 2485  N   THR A 405    15106  16644  15773    -58   -494   1809       N  
ATOM   2486  CA  THR A 405     -71.225 -18.951   6.403  1.00125.23           C  
ANISOU 2486  CA  THR A 405    14962  16775  15843     56   -405   1806       C  
ATOM   2487  C   THR A 405     -70.261 -19.280   7.521  1.00123.74           C  
ANISOU 2487  C   THR A 405    14863  16615  15539    120   -255   1526       C  
ATOM   2488  O   THR A 405     -69.313 -20.030   7.331  1.00122.26           O  
ANISOU 2488  O   THR A 405    14834  16438  15183      5   -298   1386       O  
ATOM   2489  CB  THR A 405     -72.076 -20.199   6.096  1.00128.19           C  
ANISOU 2489  CB  THR A 405    15257  17283  16168    -87   -571   2000       C  
ATOM   2490  OG1 THR A 405     -72.847 -19.974   4.907  1.00129.66           O  
ANISOU 2490  OG1 THR A 405    15389  17450  16426   -181   -762   2249       O  
ATOM   2491  CG2 THR A 405     -73.004 -20.515   7.261  1.00129.10           C  
ANISOU 2491  CG2 THR A 405    15151  17524  16377     27   -466   2078       C  
ATOM   2492  N   PHE A 406     -70.541 -18.735   8.698  1.00124.00           N  
ANISOU 2492  N   PHE A 406    14787  16670  15658    315    -84   1445       N  
ATOM   2493  CA  PHE A 406     -69.738 -18.994   9.883  1.00123.06           C  
ANISOU 2493  CA  PHE A 406    14741  16599  15417    393     48   1191       C  
ATOM   2494  C   PHE A 406     -70.185 -20.245  10.613  1.00122.91           C  
ANISOU 2494  C   PHE A 406    14660  16753  15286    366     45   1261       C  
ATOM   2495  O   PHE A 406     -71.348 -20.362  10.988  1.00124.36           O  
ANISOU 2495  O   PHE A 406    14655  17040  15554    424     86   1447       O  
ATOM   2496  CB  PHE A 406     -69.824 -17.811  10.830  1.00127.22           C  
ANISOU 2496  CB  PHE A 406    15209  17072  16056    618    231   1051       C  
ATOM   2497  CG  PHE A 406     -68.728 -16.822  10.652  1.00126.88           C  
ANISOU 2497  CG  PHE A 406    15310  16851  16049    632    263    833       C  
ATOM   2498  CD1 PHE A 406     -68.283 -16.490   9.387  1.00126.51           C  
ANISOU 2498  CD1 PHE A 406    15351  16673  16042    490    154    902       C  
ATOM   2499  CD2 PHE A 406     -68.139 -16.229  11.751  1.00127.26           C  
ANISOU 2499  CD2 PHE A 406    15405  16866  16080    774    399    564       C  
ATOM   2500  CE1 PHE A 406     -67.267 -15.588   9.223  1.00126.49           C  
ANISOU 2500  CE1 PHE A 406    15464  16508  16087    477    192    726       C  
ATOM   2501  CE2 PHE A 406     -67.134 -15.324  11.597  1.00127.24           C  
ANISOU 2501  CE2 PHE A 406    15521  16688  16137    761    413    368       C  
ATOM   2502  CZ  PHE A 406     -66.692 -14.996  10.330  1.00126.85           C  
ANISOU 2502  CZ  PHE A 406    15542  16504  16153    607    316    458       C  
ATOM   2503  N   ALA A 407     -69.236 -21.126  10.909  1.00122.27           N  
ANISOU 2503  N   ALA A 407    14724  16704  15030    291     13   1110       N  
ATOM   2504  CA  ALA A 407     -69.566 -22.460  11.392  1.00122.19           C  
ANISOU 2504  CA  ALA A 407    14693  16818  14915    220    -35   1208       C  
ATOM   2505  C   ALA A 407     -69.387 -22.666  12.900  1.00122.54           C  
ANISOU 2505  C   ALA A 407    14729  16980  14850    354    113   1095       C  
ATOM   2506  O   ALA A 407     -69.649 -23.755  13.402  1.00122.75           O  
ANISOU 2506  O   ALA A 407    14744  17108  14787    298     84   1198       O  
ATOM   2507  CB  ALA A 407     -68.748 -23.480  10.634  1.00122.49           C  
ANISOU 2507  CB  ALA A 407    14901  16803  14836     46   -200   1156       C  
ATOM   2508  N   GLN A 408     -68.912 -21.649  13.613  1.00122.17           N  
ANISOU 2508  N   GLN A 408    14707  16913  14800    521    257    884       N  
ATOM   2509  CA  GLN A 408     -68.801 -21.721  15.076  1.00122.97           C  
ANISOU 2509  CA  GLN A 408    14811  17146  14767    664    400    766       C  
ATOM   2510  C   GLN A 408     -70.159 -21.959  15.727  1.00124.90           C  
ANISOU 2510  C   GLN A 408    14863  17558  15034    732    518    991       C  
ATOM   2511  O   GLN A 408     -70.291 -22.755  16.662  1.00125.53           O  
ANISOU 2511  O   GLN A 408    14942  17792  14962    742    571   1042       O  
ATOM   2512  CB  GLN A 408     -68.213 -20.436  15.664  1.00124.06           C  
ANISOU 2512  CB  GLN A 408    15001  17218  14918    833    526    491       C  
ATOM   2513  CG  GLN A 408     -66.894 -19.977  15.096  1.00122.68           C  
ANISOU 2513  CG  GLN A 408    14975  16881  14758    771    441    267       C  
ATOM   2514  CD  GLN A 408     -67.070 -19.105  13.866  1.00122.63           C  
ANISOU 2514  CD  GLN A 408    14940  16701  14951    717    399    339       C  
ATOM   2515  OE1 GLN A 408     -67.799 -19.460  12.943  1.00122.53           O  
ANISOU 2515  OE1 GLN A 408    14858  16683  15014    616    315    580       O  
ATOM   2516  NE2 GLN A 408     -66.440 -17.935  13.871  1.00123.02           N  
ANISOU 2516  NE2 GLN A 408    15047  16605  15092    778    448    142       N  
ATOM   2517  N   ASN A 409     -71.158 -21.233  15.224  1.00125.94           N  
ANISOU 2517  N   ASN A 409    14824  17663  15364    782    561   1137       N  
ATOM   2518  CA  ASN A 409     -72.490 -21.148  15.828  1.00128.30           C  
ANISOU 2518  CA  ASN A 409    14888  18124  15736    890    714   1330       C  
ATOM   2519  C   ASN A 409     -73.146 -22.487  16.118  1.00128.88           C  
ANISOU 2519  C   ASN A 409    14867  18365  15737    754    681   1585       C  
ATOM   2520  O   ASN A 409     -73.811 -22.648  17.132  1.00130.80           O  
ANISOU 2520  O   ASN A 409    14982  18799  15918    849    860   1669       O  
ATOM   2521  CB  ASN A 409     -73.413 -20.326  14.916  1.00130.76           C  
ANISOU 2521  CB  ASN A 409    15019  18352  16313    925    689   1492       C  
ATOM   2522  CG  ASN A 409     -73.900 -21.112  13.691  1.00130.20           C  
ANISOU 2522  CG  ASN A 409    14885  18251  16333    692    458   1760       C  
ATOM   2523  OD1 ASN A 409     -73.294 -22.109  13.292  1.00128.56           O  
ANISOU 2523  OD1 ASN A 409    14828  18015  16003    501    299   1760       O  
ATOM   2524  ND2 ASN A 409     -74.984 -20.646  13.080  1.00131.82           N  
ANISOU 2524  ND2 ASN A 409    14874  18455  16758    716    427   1978       N  
ATOM   2525  N   ASN A 410     -72.939 -23.441  15.218  1.00127.49           N  
ANISOU 2525  N   ASN A 410    14764  18112  15565    526    456   1702       N  
ATOM   2526  CA  ASN A 410     -73.571 -24.744  15.303  1.00128.20           C  
ANISOU 2526  CA  ASN A 410    14776  18304  15632    355    376   1959       C  
ATOM   2527  C   ASN A 410     -73.209 -25.409  16.610  1.00128.67           C  
ANISOU 2527  C   ASN A 410    14916  18498  15475    400    491   1915       C  
ATOM   2528  O   ASN A 410     -73.959 -26.222  17.133  1.00130.27           O  
ANISOU 2528  O   ASN A 410    15000  18842  15657    325    533   2151       O  
ATOM   2529  CB  ASN A 410     -73.171 -25.616  14.117  1.00126.65           C  
ANISOU 2529  CB  ASN A 410    14713  17957  15451    119    100   2008       C  
ATOM   2530  CG  ASN A 410     -73.711 -25.085  12.804  1.00126.75           C  
ANISOU 2530  CG  ASN A 410    14637  17874  15648     48    -34   2113       C  
ATOM   2531  OD1 ASN A 410     -74.713 -24.375  12.780  1.00128.42           O  
ANISOU 2531  OD1 ASN A 410    14621  18152  16023    134     47   2257       O  
ATOM   2532  ND2 ASN A 410     -73.053 -25.428  11.706  1.00125.25           N  
ANISOU 2532  ND2 ASN A 410    14625  17538  15428   -100   -238   2045       N  
ATOM   2533  N   VAL A 411     -72.038 -25.072  17.130  1.00127.49           N  
ANISOU 2533  N   VAL A 411    14969  18308  15165    510    530   1626       N  
ATOM   2534  CA  VAL A 411     -71.640 -25.548  18.445  1.00128.24           C  
ANISOU 2534  CA  VAL A 411    15154  18545  15026    583    635   1566       C  
ATOM   2535  C   VAL A 411     -72.546 -24.951  19.515  1.00130.86           C  
ANISOU 2535  C   VAL A 411    15314  19094  15315    764    910   1621       C  
ATOM   2536  O   VAL A 411     -73.215 -25.678  20.261  1.00132.73           O  
ANISOU 2536  O   VAL A 411    15456  19515  15460    730   1007   1840       O  
ATOM   2537  CB  VAL A 411     -70.168 -25.195  18.754  1.00128.54           C  
ANISOU 2537  CB  VAL A 411    15426  18499  14913    670    596   1225       C  
ATOM   2538  CG1 VAL A 411     -69.873 -25.348  20.233  1.00129.93           C  
ANISOU 2538  CG1 VAL A 411    15677  18855  14835    798    729   1141       C  
ATOM   2539  CG2 VAL A 411     -69.222 -26.052  17.913  1.00126.44           C  
ANISOU 2539  CG2 VAL A 411    15324  18067  14649    504    353   1183       C  
ATOM   2540  N   VAL A 412     -72.583 -23.620  19.546  1.00131.28           N  
ANISOU 2540  N   VAL A 412    15324  19113  15443    953   1040   1429       N  
ATOM   2541  CA  VAL A 412     -73.325 -22.863  20.548  1.00133.99           C  
ANISOU 2541  CA  VAL A 412    15527  19639  15744   1176   1321   1399       C  
ATOM   2542  C   VAL A 412     -74.761 -23.369  20.668  1.00136.33           C  
ANISOU 2542  C   VAL A 412    15537  20123  16137   1130   1436   1756       C  
ATOM   2543  O   VAL A 412     -75.193 -23.761  21.754  1.00138.52           O  
ANISOU 2543  O   VAL A 412    15755  20638  16240   1186   1626   1852       O  
ATOM   2544  CB  VAL A 412     -73.352 -21.361  20.206  1.00134.28           C  
ANISOU 2544  CB  VAL A 412    15527  19537  15954   1362   1399   1187       C  
ATOM   2545  CG1 VAL A 412     -73.999 -20.585  21.337  1.00137.37           C  
ANISOU 2545  CG1 VAL A 412    15811  20107  16277   1626   1701   1093       C  
ATOM   2546  CG2 VAL A 412     -71.951 -20.850  20.002  1.00132.20           C  
ANISOU 2546  CG2 VAL A 412    15520  19077  15634   1370   1276    860       C  
ATOM   2547  N   ILE A 413     -75.471 -23.392  19.540  1.00136.05           N  
ANISOU 2547  N   ILE A 413    15327  19993  16373   1012   1311   1962       N  
ATOM   2548  CA  ILE A 413     -76.835 -23.902  19.483  1.00138.33           C  
ANISOU 2548  CA  ILE A 413    15310  20443  16807    929   1371   2321       C  
ATOM   2549  C   ILE A 413     -76.898 -25.281  20.108  1.00138.97           C  
ANISOU 2549  C   ILE A 413    15421  20666  16716    750   1356   2529       C  
ATOM   2550  O   ILE A 413     -77.694 -25.522  21.013  1.00141.76           O  
ANISOU 2550  O   ILE A 413    15597  21266  17002    797   1579   2706       O  
ATOM   2551  CB  ILE A 413     -77.357 -24.003  18.046  1.00137.58           C  
ANISOU 2551  CB  ILE A 413    15083  20197  16994    756   1132   2512       C  
ATOM   2552  CG1 ILE A 413     -77.328 -22.651  17.347  1.00137.20           C  
ANISOU 2552  CG1 ILE A 413    15009  19991  17131    919   1124   2356       C  
ATOM   2553  CG2 ILE A 413     -78.769 -24.520  18.033  1.00140.29           C  
ANISOU 2553  CG2 ILE A 413    15082  20716  17505    659   1178   2882       C  
ATOM   2554  CD1 ILE A 413     -77.513 -22.779  15.852  1.00136.05           C  
ANISOU 2554  CD1 ILE A 413    14833  19673  17186    731    837   2502       C  
ATOM   2555  N   ALA A 414     -76.031 -26.175  19.643  1.00136.65           N  
ANISOU 2555  N   ALA A 414    15359  20214  16349    554   1104   2507       N  
ATOM   2556  CA  ALA A 414     -76.025 -27.551  20.121  1.00137.28           C  
ANISOU 2556  CA  ALA A 414    15497  20364  16298    368   1041   2717       C  
ATOM   2557  C   ALA A 414     -75.784 -27.592  21.627  1.00138.95           C  
ANISOU 2557  C   ALA A 414    15787  20794  16213    517   1278   2659       C  
ATOM   2558  O   ALA A 414     -76.303 -28.462  22.338  1.00141.09           O  
ANISOU 2558  O   ALA A 414    15986  21235  16387    420   1361   2923       O  
ATOM   2559  CB  ALA A 414     -74.966 -28.361  19.386  1.00134.57           C  
ANISOU 2559  CB  ALA A 414    15424  19781  15926    193    737   2628       C  
ATOM   2560  N   LEU A 415     -74.998 -26.636  22.106  1.00138.23           N  
ANISOU 2560  N   LEU A 415    15850  20700  15973    743   1379   2317       N  
ATOM   2561  CA  LEU A 415     -74.655 -26.576  23.515  1.00139.90           C  
ANISOU 2561  CA  LEU A 415    16175  21117  15863    899   1577   2207       C  
ATOM   2562  C   LEU A 415     -75.642 -25.724  24.299  1.00143.09           C  
ANISOU 2562  C   LEU A 415    16361  21770  16237   1115   1923   2218       C  
ATOM   2563  O   LEU A 415     -75.675 -25.782  25.525  1.00145.41           O  
ANISOU 2563  O   LEU A 415    16701  22302  16245   1231   2134   2202       O  
ATOM   2564  CB  LEU A 415     -73.236 -26.038  23.691  1.00138.94           C  
ANISOU 2564  CB  LEU A 415    16343  20866  15581   1018   1482   1812       C  
ATOM   2565  CG  LEU A 415     -72.133 -26.898  23.065  1.00136.18           C  
ANISOU 2565  CG  LEU A 415    16211  20300  15229    843   1171   1770       C  
ATOM   2566  CD1 LEU A 415     -70.765 -26.369  23.446  1.00134.88           C  
ANISOU 2566  CD1 LEU A 415    16288  20066  14894    971   1109   1396       C  
ATOM   2567  CD2 LEU A 415     -72.269 -28.368  23.466  1.00137.13           C  
ANISOU 2567  CD2 LEU A 415    16375  20490  15240    666   1087   2069       C  
ATOM   2568  N   THR A 416     -76.439 -24.928  23.592  1.00143.48           N  
ANISOU 2568  N   THR A 416    16175  21769  16573   1183   1981   2244       N  
ATOM   2569  CA  THR A 416     -77.429 -24.074  24.250  1.00146.80           C  
ANISOU 2569  CA  THR A 416    16356  22409  17014   1419   2317   2245       C  
ATOM   2570  C   THR A 416     -78.883 -24.519  24.018  1.00149.30           C  
ANISOU 2570  C   THR A 416    16288  22889  17552   1317   2419   2652       C  
ATOM   2571  O   THR A 416     -79.808 -23.955  24.605  1.00152.59           O  
ANISOU 2571  O   THR A 416    16455  23527  17994   1507   2725   2700       O  
ATOM   2572  CB  THR A 416     -77.275 -22.603  23.805  1.00146.25           C  
ANISOU 2572  CB  THR A 416    16285  22166  17117   1649   2351   1935       C  
ATOM   2573  OG1 THR A 416     -77.434 -22.506  22.382  1.00144.21           O  
ANISOU 2573  OG1 THR A 416    15935  21667  17190   1512   2108   2038       O  
ATOM   2574  CG2 THR A 416     -75.900 -22.063  24.226  1.00144.60           C  
ANISOU 2574  CG2 THR A 416    16424  21831  16685   1761   2292   1521       C  
ATOM   2575  N   ARG A 417     -79.069 -25.517  23.154  1.00148.00           N  
ANISOU 2575  N   ARG A 417    16068  22610  17555   1019   2161   2928       N  
ATOM   2576  CA  ARG A 417     -80.394 -26.041  22.826  1.00150.35           C  
ANISOU 2576  CA  ARG A 417    15997  23036  18093    864   2192   3328       C  
ATOM   2577  C   ARG A 417     -81.314 -24.931  22.387  1.00151.94           C  
ANISOU 2577  C   ARG A 417    15885  23265  18581   1055   2319   3322       C  
ATOM   2578  O   ARG A 417     -82.416 -24.806  22.903  1.00155.52           O  
ANISOU 2578  O   ARG A 417    16006  23975  19111   1142   2583   3519       O  
ATOM   2579  CB  ARG A 417     -81.021 -26.781  24.008  1.00153.82           C  
ANISOU 2579  CB  ARG A 417    16305  23800  18340    822   2452   3592       C  
ATOM   2580  CG  ARG A 417     -80.249 -27.983  24.456  1.00152.88           C  
ANISOU 2580  CG  ARG A 417    16468  23652  17965    619   2313   3675       C  
ATOM   2581  CD  ARG A 417     -80.988 -28.717  25.547  1.00156.77           C  
ANISOU 2581  CD  ARG A 417    16805  24468  18292    549   2570   4001       C  
ATOM   2582  NE  ARG A 417     -80.367 -30.008  25.811  1.00156.12           N  
ANISOU 2582  NE  ARG A 417    16971  24311  18036    309   2381   4161       N  
ATOM   2583  CZ  ARG A 417     -80.794 -30.873  26.723  1.00159.25           C  
ANISOU 2583  CZ  ARG A 417    17314  24935  18261    186   2537   4481       C  
ATOM   2584  NH1 ARG A 417     -81.856 -30.589  27.464  1.00163.30           N  
ANISOU 2584  NH1 ARG A 417    17517  25794  18737    277   2908   4671       N  
ATOM   2585  NH2 ARG A 417     -80.158 -32.024  26.892  1.00158.61           N  
ANISOU 2585  NH2 ARG A 417    17485  24731  18049    -23   2326   4619       N  
ATOM   2586  N   CYS A 418     -80.855 -24.109  21.457  1.00149.58           N  
ANISOU 2586  N   CYS A 418    15686  22706  18441   1129   2141   3105       N  
ATOM   2587  CA  CYS A 418     -81.673 -23.015  20.971  1.00151.14           C  
ANISOU 2587  CA  CYS A 418    15607  22886  18934   1323   2224   3105       C  
ATOM   2588  C   CYS A 418     -81.290 -22.585  19.580  1.00148.42           C  
ANISOU 2588  C   CYS A 418    15356  22230  18808   1249   1906   3032       C  
ATOM   2589  O   CYS A 418     -80.210 -22.055  19.377  1.00145.91           O  
ANISOU 2589  O   CYS A 418    15340  21706  18391   1317   1815   2729       O  
ATOM   2590  CB  CYS A 418     -81.563 -21.809  21.895  1.00152.86           C  
ANISOU 2590  CB  CYS A 418    15856  23184  19039   1699   2544   2795       C  
ATOM   2591  SG  CYS A 418     -82.303 -20.337  21.163  1.00154.38           S  
ANISOU 2591  SG  CYS A 418    15792  23242  19623   1968   2586   2731       S  
ATOM   2592  N   ALA A 419     -82.173 -22.793  18.618  1.00149.20           N  
ANISOU 2592  N   ALA A 419    15189  22304  19198   1103   1733   3315       N  
ATOM   2593  CA  ALA A 419     -81.890 -22.325  17.275  1.00147.13           C  
ANISOU 2593  CA  ALA A 419    15010  21772  19122   1043   1438   3269       C  
ATOM   2594  C   ALA A 419     -82.833 -21.203  16.869  1.00149.54           C  
ANISOU 2594  C   ALA A 419    15005  22073  19739   1262   1506   3340       C  
ATOM   2595  O   ALA A 419     -83.051 -20.993  15.679  1.00148.99           O  
ANISOU 2595  O   ALA A 419    14880  21847  19880   1169   1243   3452       O  
ATOM   2596  CB  ALA A 419     -81.971 -23.475  16.283  1.00145.86           C  
ANISOU 2596  CB  ALA A 419    14867  21531  19023    678   1095   3506       C  
ATOM   2597  N   ASN A 420     -83.348 -20.457  17.852  1.00152.38           N  
ANISOU 2597  N   ASN A 420    15183  22598  20118   1569   1854   3259       N  
ATOM   2598  CA  ASN A 420     -84.295 -19.360  17.587  1.00155.27           C  
ANISOU 2598  CA  ASN A 420    15228  22963  20805   1830   1952   3319       C  
ATOM   2599  C   ASN A 420     -83.703 -18.230  16.769  1.00153.70           C  
ANISOU 2599  C   ASN A 420    15222  22443  20733   1963   1794   3111       C  
ATOM   2600  O   ASN A 420     -82.612 -17.754  17.059  1.00151.69           O  
ANISOU 2600  O   ASN A 420    15313  22028  20293   2050   1831   2782       O  
ATOM   2601  CB  ASN A 420     -84.830 -18.755  18.892  1.00158.82           C  
ANISOU 2601  CB  ASN A 420    15492  23641  21210   2170   2391   3205       C  
ATOM   2602  CG  ASN A 420     -86.026 -19.497  19.445  1.00162.31           C  
ANISOU 2602  CG  ASN A 420    15520  24435  21715   2111   2584   3537       C  
ATOM   2603  OD1 ASN A 420     -85.885 -20.499  20.139  1.00162.22           O  
ANISOU 2603  OD1 ASN A 420    15570  24611  21454   1935   2672   3622       O  
ATOM   2604  ND2 ASN A 420     -87.217 -18.992  19.151  1.00165.72           N  
ANISOU 2604  ND2 ASN A 420    15514  24959  22494   2260   2652   3740       N  
ATOM   2605  N   ARG A 421     -84.458 -17.762  15.781  1.00155.03           N  
ANISOU 2605  N   ARG A 421    15152  22524  21229   1984   1622   3316       N  
ATOM   2606  CA  ARG A 421     -84.006 -16.675  14.929  1.00154.06           C  
ANISOU 2606  CA  ARG A 421    15191  22092  21254   2099   1460   3183       C  
ATOM   2607  C   ARG A 421     -83.806 -15.394  15.731  1.00155.68           C  
ANISOU 2607  C   ARG A 421    15454  22205  21490   2490   1749   2871       C  
ATOM   2608  O   ARG A 421     -83.200 -14.449  15.244  1.00154.78           O  
ANISOU 2608  O   ARG A 421    15549  21803  21455   2591   1654   2696       O  
ATOM   2609  CB  ARG A 421     -84.997 -16.420  13.797  1.00155.95           C  
ANISOU 2609  CB  ARG A 421    15125  22288  21842   2070   1223   3504       C  
ATOM   2610  CG  ARG A 421     -86.319 -15.833  14.268  1.00160.58           C  
ANISOU 2610  CG  ARG A 421    15242  23044  22726   2366   1450   3653       C  
ATOM   2611  CD  ARG A 421     -87.257 -15.553  13.108  1.00162.61           C  
ANISOU 2611  CD  ARG A 421    15194  23249  23341   2341   1173   3980       C  
ATOM   2612  NE  ARG A 421     -88.518 -14.988  13.570  1.00167.34           N  
ANISOU 2612  NE  ARG A 421    15309  24018  24253   2648   1396   4122       N  
ATOM   2613  CZ  ARG A 421     -89.519 -15.724  14.040  1.00169.98           C  
ANISOU 2613  CZ  ARG A 421    15238  24680  24668   2587   1525   4365       C  
ATOM   2614  NH1 ARG A 421     -89.380 -17.040  14.116  1.00168.27           N  
ANISOU 2614  NH1 ARG A 421    15074  24622  24240   2223   1437   4490       N  
ATOM   2615  NH2 ARG A 421     -90.652 -15.154  14.442  1.00174.59           N  
ANISOU 2615  NH2 ARG A 421    15356  25427  25553   2890   1748   4487       N  
ATOM   2616  N   TRP A 422     -84.345 -15.350  16.946  1.00158.43           N  
ANISOU 2616  N   TRP A 422    15619  22796  21783   2706   2102   2807       N  
ATOM   2617  CA  TRP A 422     -84.238 -14.157  17.780  1.00160.59           C  
ANISOU 2617  CA  TRP A 422    15944  22996  22075   3097   2394   2484       C  
ATOM   2618  C   TRP A 422     -82.856 -14.014  18.390  1.00157.99           C  
ANISOU 2618  C   TRP A 422    16073  22540  21416   3090   2441   2089       C  
ATOM   2619  O   TRP A 422     -82.387 -12.900  18.623  1.00158.63           O  
ANISOU 2619  O   TRP A 422    16329  22401  21541   3329   2524   1782       O  
ATOM   2620  CB  TRP A 422     -85.312 -14.163  18.865  1.00164.89           C  
ANISOU 2620  CB  TRP A 422    16131  23872  22647   3343   2776   2540       C  
ATOM   2621  CG  TRP A 422     -86.673 -14.140  18.270  1.00167.96           C  
ANISOU 2621  CG  TRP A 422    16029  24372  23414   3388   2732   2910       C  
ATOM   2622  CD1 TRP A 422     -87.679 -15.027  18.488  1.00170.11           C  
ANISOU 2622  CD1 TRP A 422    15914  24981  23737   3269   2820   3239       C  
ATOM   2623  CD2 TRP A 422     -87.164 -13.200  17.309  1.00169.40           C  
ANISOU 2623  CD2 TRP A 422    16048  24323  23995   3544   2558   3014       C  
ATOM   2624  NE1 TRP A 422     -88.778 -14.686  17.740  1.00172.87           N  
ANISOU 2624  NE1 TRP A 422    15846  25337  24500   3348   2711   3528       N  
ATOM   2625  CE2 TRP A 422     -88.483 -13.568  17.005  1.00172.48           C  
ANISOU 2625  CE2 TRP A 422    15932  24940  24662   3526   2543   3400       C  
ATOM   2626  CE3 TRP A 422     -86.618 -12.073  16.686  1.00168.68           C  
ANISOU 2626  CE3 TRP A 422    16183  23849  24059   3692   2408   2835       C  
ATOM   2627  CZ2 TRP A 422     -89.265 -12.851  16.106  1.00174.82           C  
ANISOU 2627  CZ2 TRP A 422    15944  25102  25378   3668   2368   3605       C  
ATOM   2628  CZ3 TRP A 422     -87.392 -11.368  15.793  1.00170.99           C  
ANISOU 2628  CZ3 TRP A 422    16214  23995  24759   3828   2243   3053       C  
ATOM   2629  CH2 TRP A 422     -88.700 -11.757  15.510  1.00174.01           C  
ANISOU 2629  CH2 TRP A 422    16093  24618  25405   3825   2217   3431       C  
ATOM   2630  N   ALA A 423     -82.215 -15.146  18.655  1.00155.35           N  
ANISOU 2630  N   ALA A 423    15924  22335  20768   2815   2376   2101       N  
ATOM   2631  CA  ALA A 423     -80.810 -15.150  19.045  1.00152.53           C  
ANISOU 2631  CA  ALA A 423    15994  21849  20110   2751   2340   1768       C  
ATOM   2632  C   ALA A 423     -79.962 -14.568  17.910  1.00149.87           C  
ANISOU 2632  C   ALA A 423    15894  21149  19902   2651   2050   1676       C  
ATOM   2633  O   ALA A 423     -79.056 -13.766  18.145  1.00149.21           O  
ANISOU 2633  O   ALA A 423    16076  20860  19759   2759   2072   1349       O  
ATOM   2634  CB  ALA A 423     -80.353 -16.561  19.393  1.00150.39           C  
ANISOU 2634  CB  ALA A 423    15845  21770  19527   2465   2279   1859       C  
ATOM   2635  N   GLY A 424     -80.267 -14.984  16.682  1.00148.65           N  
ANISOU 2635  N   GLY A 424    15640  20926  19915   2430   1778   1973       N  
ATOM   2636  CA  GLY A 424     -79.586 -14.493  15.495  1.00146.56           C  
ANISOU 2636  CA  GLY A 424    15570  20353  19762   2315   1507   1951       C  
ATOM   2637  C   GLY A 424     -79.804 -13.017  15.210  1.00148.67           C  
ANISOU 2637  C   GLY A 424    15802  20369  20317   2582   1543   1861       C  
ATOM   2638  O   GLY A 424     -78.876 -12.306  14.836  1.00147.37           O  
ANISOU 2638  O   GLY A 424    15901  19930  20162   2575   1451   1666       O  
ATOM   2639  N   TYR A 425     -81.039 -12.557  15.373  1.00152.21           N  
ANISOU 2639  N   TYR A 425    15911  20904  21020   2818   1676   2015       N  
ATOM   2640  CA  TYR A 425     -81.384 -11.162  15.131  1.00154.85           C  
ANISOU 2640  CA  TYR A 425    16179  20988  21671   3110   1712   1954       C  
ATOM   2641  C   TYR A 425     -80.826 -10.255  16.221  1.00156.12           C  
ANISOU 2641  C   TYR A 425    16531  21031  21757   3387   1970   1528       C  
ATOM   2642  O   TYR A 425     -80.326  -9.168  15.927  1.00156.55           O  
ANISOU 2642  O   TYR A 425    16764  20752  21965   3503   1916   1354       O  
ATOM   2643  CB  TYR A 425     -82.901 -11.028  14.988  1.00158.57           C  
ANISOU 2643  CB  TYR A 425    16193  21606  22450   3289   1772   2256       C  
ATOM   2644  CG  TYR A 425     -83.386 -11.508  13.634  1.00157.86           C  
ANISOU 2644  CG  TYR A 425    15953  21508  22518   3041   1431   2654       C  
ATOM   2645  CD1 TYR A 425     -82.725 -11.126  12.476  1.00155.97           C  
ANISOU 2645  CD1 TYR A 425    15951  20982  22327   2888   1138   2696       C  
ATOM   2646  CD2 TYR A 425     -84.453 -12.386  13.513  1.00159.21           C  
ANISOU 2646  CD2 TYR A 425    15762  21968  22761   2934   1395   2983       C  
ATOM   2647  CE1 TYR A 425     -83.142 -11.559  11.238  1.00155.59           C  
ANISOU 2647  CE1 TYR A 425    15798  20941  22377   2661    818   3042       C  
ATOM   2648  CE2 TYR A 425     -84.867 -12.836  12.272  1.00158.77           C  
ANISOU 2648  CE2 TYR A 425    15592  21904  22829   2692   1052   3323       C  
ATOM   2649  CZ  TYR A 425     -84.206 -12.414  11.141  1.00156.97           C  
ANISOU 2649  CZ  TYR A 425    15624  21394  22622   2564    764   3342       C  
ATOM   2650  OH  TYR A 425     -84.596 -12.841   9.898  1.00156.81           O  
ANISOU 2650  OH  TYR A 425    15522  21376  22683   2326    415   3663       O  
ATOM   2651  N   CYS A 426     -80.898 -10.707  17.470  1.00156.95           N  
ANISOU 2651  N   CYS A 426    16612  21405  21617   3479   2239   1366       N  
ATOM   2652  CA  CYS A 426     -80.257  -9.995  18.573  1.00158.05           C  
ANISOU 2652  CA  CYS A 426    16982  21469  21602   3704   2462    928       C  
ATOM   2653  C   CYS A 426     -78.764  -9.893  18.337  1.00154.68           C  
ANISOU 2653  C   CYS A 426    16964  20804  21004   3501   2277    685       C  
ATOM   2654  O   CYS A 426     -78.152  -8.849  18.556  1.00155.54           O  
ANISOU 2654  O   CYS A 426    17282  20638  21178   3649   2304    375       O  
ATOM   2655  CB  CYS A 426     -80.506 -10.691  19.903  1.00159.30           C  
ANISOU 2655  CB  CYS A 426    17077  22004  21446   3778   2752    831       C  
ATOM   2656  SG  CYS A 426     -82.128 -10.392  20.581  1.00164.66           S  
ANISOU 2656  SG  CYS A 426    17301  22950  22312   4141   3103    956       S  
ATOM   2657  N   CYS A 427     -78.184 -11.005  17.907  1.00151.12           N  
ANISOU 2657  N   CYS A 427    16616  20459  20344   3161   2090    825       N  
ATOM   2658  CA  CYS A 427     -76.788 -11.044  17.528  1.00147.87           C  
ANISOU 2658  CA  CYS A 427    16542  19851  19790   2939   1897    649       C  
ATOM   2659  C   CYS A 427     -76.504  -9.950  16.514  1.00148.01           C  
ANISOU 2659  C   CYS A 427    16648  19489  20102   2953   1732    648       C  
ATOM   2660  O   CYS A 427     -75.690  -9.060  16.764  1.00148.35           O  
ANISOU 2660  O   CYS A 427    16915  19283  20167   3030   1748    345       O  
ATOM   2661  CB  CYS A 427     -76.442 -12.417  16.956  1.00144.51           C  
ANISOU 2661  CB  CYS A 427    16151  19581  19176   2590   1702    871       C  
ATOM   2662  SG  CYS A 427     -74.753 -12.598  16.413  1.00140.72           S  
ANISOU 2662  SG  CYS A 427    16036  18902  18528   2317   1477    684       S  
ATOM   2663  N   CYS A 428     -77.232  -9.994  15.400  1.00148.21           N  
ANISOU 2663  N   CYS A 428    16486  19469  20357   2883   1572   1000       N  
ATOM   2664  CA  CYS A 428     -77.076  -9.031  14.312  1.00148.61           C  
ANISOU 2664  CA  CYS A 428    16604  19178  20684   2875   1392   1086       C  
ATOM   2665  C   CYS A 428     -77.106  -7.591  14.800  1.00151.74           C  
ANISOU 2665  C   CYS A 428    17052  19292  21310   3193   1532    835       C  
ATOM   2666  O   CYS A 428     -76.187  -6.819  14.520  1.00151.31           O  
ANISOU 2666  O   CYS A 428    17246  18927  21317   3146   1448    659       O  
ATOM   2667  CB  CYS A 428     -78.171  -9.222  13.258  1.00149.59           C  
ANISOU 2667  CB  CYS A 428    16456  19348  21032   2834   1231   1514       C  
ATOM   2668  SG  CYS A 428     -78.041 -10.728  12.276  1.00146.19           S  
ANISOU 2668  SG  CYS A 428    16027  19127  20390   2418    970   1818       S  
ATOM   2669  N   LEU A 429     -78.157  -7.243  15.540  1.00155.15           N  
ANISOU 2669  N   LEU A 429    17247  19829  21875   3513   1753    812       N  
ATOM   2670  CA  LEU A 429     -78.297  -5.892  16.073  1.00158.71           C  
ANISOU 2670  CA  LEU A 429    17737  20009  22558   3859   1906    549       C  
ATOM   2671  C   LEU A 429     -77.112  -5.534  16.961  1.00158.10           C  
ANISOU 2671  C   LEU A 429    17994  19812  22266   3862   1994     88       C  
ATOM   2672  O   LEU A 429     -76.589  -4.423  16.876  1.00159.46           O  
ANISOU 2672  O   LEU A 429    18355  19610  22623   3952   1955   -123       O  
ATOM   2673  CB  LEU A 429     -79.609  -5.744  16.858  1.00162.64           C  
ANISOU 2673  CB  LEU A 429    17908  20711  23176   4215   2176    569       C  
ATOM   2674  CG  LEU A 429     -80.943  -5.766  16.106  1.00164.73           C  
ANISOU 2674  CG  LEU A 429    17783  21049  23758   4313   2114    988       C  
ATOM   2675  CD1 LEU A 429     -82.086  -6.028  17.074  1.00167.97           C  
ANISOU 2675  CD1 LEU A 429    17853  21800  24168   4588   2424    999       C  
ATOM   2676  CD2 LEU A 429     -81.158  -4.446  15.376  1.00167.34           C  
ANISOU 2676  CD2 LEU A 429    18117  20954  24510   4510   1993   1040       C  
ATOM   2677  N   ILE A 430     -76.683  -6.480  17.796  1.00156.28           N  
ANISOU 2677  N   ILE A 430    17836  19889  21655   3750   2092    -55       N  
ATOM   2678  CA  ILE A 430     -75.536  -6.267  18.673  1.00155.72           C  
ANISOU 2678  CA  ILE A 430    18071  19753  21343   3731   2145   -482       C  
ATOM   2679  C   ILE A 430     -74.285  -5.944  17.852  1.00153.24           C  
ANISOU 2679  C   ILE A 430    18017  19128  21077   3463   1893   -538       C  
ATOM   2680  O   ILE A 430     -73.500  -5.063  18.214  1.00154.31           O  
ANISOU 2680  O   ILE A 430    18378  18993  21258   3515   1891   -871       O  
ATOM   2681  CB  ILE A 430     -75.286  -7.488  19.578  1.00154.03           C  
ANISOU 2681  CB  ILE A 430    17881  19944  20699   3620   2244   -546       C  
ATOM   2682  CG1 ILE A 430     -76.352  -7.560  20.667  1.00157.41           C  
ANISOU 2682  CG1 ILE A 430    18106  20659  21044   3922   2556   -596       C  
ATOM   2683  CG2 ILE A 430     -73.929  -7.396  20.237  1.00152.84           C  
ANISOU 2683  CG2 ILE A 430    18055  19721  20295   3521   2204   -932       C  
ATOM   2684  CD1 ILE A 430     -76.418  -8.885  21.364  1.00156.10           C  
ANISOU 2684  CD1 ILE A 430    17890  20923  20500   3795   2649   -505       C  
ATOM   2685  N   LEU A 431     -74.115  -6.636  16.732  1.00150.26           N  
ANISOU 2685  N   LEU A 431    17605  18788  20698   3174   1685   -214       N  
ATOM   2686  CA  LEU A 431     -72.972  -6.384  15.860  1.00148.11           C  
ANISOU 2686  CA  LEU A 431    17551  18260  20465   2910   1470   -225       C  
ATOM   2687  C   LEU A 431     -73.048  -5.016  15.188  1.00150.49           C  
ANISOU 2687  C   LEU A 431    17899  18135  21145   3013   1398   -199       C  
ATOM   2688  O   LEU A 431     -72.067  -4.280  15.170  1.00150.69           O  
ANISOU 2688  O   LEU A 431    18147  17875  21234   2940   1338   -422       O  
ATOM   2689  CB  LEU A 431     -72.844  -7.466  14.789  1.00144.81           C  
ANISOU 2689  CB  LEU A 431    17087  17999  19934   2597   1281    113       C  
ATOM   2690  CG  LEU A 431     -72.485  -8.869  15.269  1.00142.09           C  
ANISOU 2690  CG  LEU A 431    16757  18003  19229   2428   1292     94       C  
ATOM   2691  CD1 LEU A 431     -72.335  -9.792  14.075  1.00139.31           C  
ANISOU 2691  CD1 LEU A 431    16388  17731  18813   2131   1087    401       C  
ATOM   2692  CD2 LEU A 431     -71.218  -8.857  16.114  1.00141.14           C  
ANISOU 2692  CD2 LEU A 431    16872  17866  18889   2374   1323   -286       C  
ATOM   2693  N   ILE A 432     -74.204  -4.695  14.615  1.00152.48           N  
ANISOU 2693  N   ILE A 432    17933  18341  21662   3169   1388     94       N  
ATOM   2694  CA  ILE A 432     -74.394  -3.422  13.924  1.00155.12           C  
ANISOU 2694  CA  ILE A 432    18295  18261  22381   3284   1301    179       C  
ATOM   2695  C   ILE A 432     -74.157  -2.258  14.882  1.00158.33           C  
ANISOU 2695  C   ILE A 432    18843  18381  22935   3551   1448   -232       C  
ATOM   2696  O   ILE A 432     -73.451  -1.305  14.546  1.00159.32           O  
ANISOU 2696  O   ILE A 432    19170  18115  23251   3497   1351   -341       O  
ATOM   2697  CB  ILE A 432     -75.804  -3.320  13.302  1.00157.25           C  
ANISOU 2697  CB  ILE A 432    18267  18570  22913   3459   1271    558       C  
ATOM   2698  CG1 ILE A 432     -76.012  -4.452  12.291  1.00154.35           C  
ANISOU 2698  CG1 ILE A 432    17786  18463  22398   3167   1086    951       C  
ATOM   2699  CG2 ILE A 432     -75.988  -1.976  12.632  1.00160.34           C  
ANISOU 2699  CG2 ILE A 432    18700  18511  23712   3600   1170    654       C  
ATOM   2700  CD1 ILE A 432     -77.440  -4.664  11.869  1.00156.24           C  
ANISOU 2700  CD1 ILE A 432    17685  18857  22822   3308   1055   1311       C  
ATOM   2701  N   VAL A 433     -74.721  -2.362  16.082  1.00160.16           N  
ANISOU 2701  N   VAL A 433    18978  18813  23061   3824   1685   -466       N  
ATOM   2702  CA  VAL A 433     -74.507  -1.371  17.132  1.00163.44           C  
ANISOU 2702  CA  VAL A 433    19545  19006  23548   4091   1842   -915       C  
ATOM   2703  C   VAL A 433     -73.029  -1.267  17.504  1.00161.79           C  
ANISOU 2703  C   VAL A 433    19656  18670  23146   3864   1763  -1258       C  
ATOM   2704  O   VAL A 433     -72.489  -0.165  17.633  1.00164.04           O  
ANISOU 2704  O   VAL A 433    20139  18555  23634   3923   1725  -1518       O  
ATOM   2705  CB  VAL A 433     -75.325  -1.703  18.396  1.00165.53           C  
ANISOU 2705  CB  VAL A 433    19657  19605  23633   4396   2133  -1104       C  
ATOM   2706  CG1 VAL A 433     -74.795  -0.936  19.602  1.00168.24           C  
ANISOU 2706  CG1 VAL A 433    20236  19793  23894   4595   2280  -1645       C  
ATOM   2707  CG2 VAL A 433     -76.791  -1.404  18.168  1.00168.69           C  
ANISOU 2707  CG2 VAL A 433    19731  20032  24330   4706   2243   -851       C  
ATOM   2708  N   ALA A 434     -72.376  -2.414  17.673  1.00158.13           N  
ANISOU 2708  N   ALA A 434    19235  18535  22311   3603   1725  -1255       N  
ATOM   2709  CA  ALA A 434     -70.950  -2.431  17.980  1.00156.48           C  
ANISOU 2709  CA  ALA A 434    19288  18248  21917   3371   1629  -1548       C  
ATOM   2710  C   ALA A 434     -70.152  -1.738  16.874  1.00155.94           C  
ANISOU 2710  C   ALA A 434    19353  17789  22107   3136   1417  -1440       C  
ATOM   2711  O   ALA A 434     -69.131  -1.102  17.134  1.00156.65           O  
ANISOU 2711  O   ALA A 434    19654  17628  22236   3038   1352  -1732       O  
ATOM   2712  CB  ALA A 434     -70.464  -3.856  18.177  1.00152.68           C  
ANISOU 2712  CB  ALA A 434    18794  18183  21034   3137   1601  -1487       C  
ATOM   2713  N   GLY A 435     -70.636  -1.861  15.642  1.00154.98           N  
ANISOU 2713  N   GLY A 435    19104  17628  22155   3037   1307  -1011       N  
ATOM   2714  CA  GLY A 435     -70.011  -1.232  14.496  1.00154.80           C  
ANISOU 2714  CA  GLY A 435    19192  17265  22361   2815   1122   -835       C  
ATOM   2715  C   GLY A 435     -70.193   0.270  14.470  1.00158.96           C  
ANISOU 2715  C   GLY A 435    19807  17300  23292   3010   1118   -939       C  
ATOM   2716  O   GLY A 435     -69.283   0.999  14.091  1.00159.61           O  
ANISOU 2716  O   GLY A 435    20072  17044  23530   2833   1005  -1011       O  
ATOM   2717  N   ILE A 436     -71.372   0.736  14.868  1.00162.07           N  
ANISOU 2717  N   ILE A 436    20061  17644  23874   3377   1243   -940       N  
ATOM   2718  CA  ILE A 436     -71.639   2.168  14.944  1.00166.56           C  
ANISOU 2718  CA  ILE A 436    20712  17723  24850   3621   1251  -1067       C  
ATOM   2719  C   ILE A 436     -70.683   2.864  15.899  1.00168.27           C  
ANISOU 2719  C   ILE A 436    21186  17693  25056   3630   1286  -1582       C  
ATOM   2720  O   ILE A 436     -69.998   3.809  15.525  1.00169.93           O  
ANISOU 2720  O   ILE A 436    21580  17461  25525   3512   1161  -1646       O  
ATOM   2721  CB  ILE A 436     -73.079   2.440  15.398  1.00169.84           C  
ANISOU 2721  CB  ILE A 436    20906  18188  25436   4060   1419  -1041       C  
ATOM   2722  CG1 ILE A 436     -74.069   1.928  14.349  1.00168.91           C  
ANISOU 2722  CG1 ILE A 436    20519  18249  25410   4050   1337   -507       C  
ATOM   2723  CG2 ILE A 436     -73.284   3.926  15.672  1.00174.91           C  
ANISOU 2723  CG2 ILE A 436    21662  18304  26491   4357   1448  -1265       C  
ATOM   2724  CD1 ILE A 436     -75.516   1.941  14.808  1.00171.77           C  
ANISOU 2724  CD1 ILE A 436    20588  18774  25901   4454   1513   -443       C  
ATOM   2725  N   PHE A 437     -70.615   2.354  17.123  1.00167.98           N  
ANISOU 2725  N   PHE A 437    21165  17954  24705   3744   1443  -1935       N  
ATOM   2726  CA  PHE A 437     -69.709   2.877  18.138  1.00169.62           C  
ANISOU 2726  CA  PHE A 437    21618  17999  24831   3747   1462  -2453       C  
ATOM   2727  C   PHE A 437     -68.257   2.601  17.759  1.00166.72           C  
ANISOU 2727  C   PHE A 437    21408  17600  24336   3313   1276  -2483       C  
ATOM   2728  O   PHE A 437     -67.636   1.674  18.281  1.00164.00           O  
ANISOU 2728  O   PHE A 437    21084  17610  23617   3158   1282  -2617       O  
ATOM   2729  CB  PHE A 437     -70.028   2.261  19.501  1.00169.96           C  
ANISOU 2729  CB  PHE A 437    21633  18443  24502   3962   1671  -2774       C  
ATOM   2730  CG  PHE A 437     -71.352   2.696  20.068  1.00173.80           C  
ANISOU 2730  CG  PHE A 437    21980  18939  25118   4419   1896  -2845       C  
ATOM   2731  CD1 PHE A 437     -71.763   4.019  19.980  1.00178.31           C  
ANISOU 2731  CD1 PHE A 437    22611  19020  26117   4681   1907  -2961       C  
ATOM   2732  CD2 PHE A 437     -72.191   1.779  20.683  1.00173.21           C  
ANISOU 2732  CD2 PHE A 437    21703  19357  24752   4591   2103  -2784       C  
ATOM   2733  CE1 PHE A 437     -72.981   4.421  20.501  1.00182.17           C  
ANISOU 2733  CE1 PHE A 437    22951  19523  26742   5131   2129  -3038       C  
ATOM   2734  CE2 PHE A 437     -73.415   2.176  21.206  1.00177.07           C  
ANISOU 2734  CE2 PHE A 437    22030  19883  25366   5018   2338  -2845       C  
ATOM   2735  CZ  PHE A 437     -73.809   3.500  21.113  1.00181.56           C  
ANISOU 2735  CZ  PHE A 437    22650  19972  26364   5301   2355  -2982       C  
ATOM   2736  N   ALA A 438     -67.724   3.403  16.840  1.00167.55           N  
ANISOU 2736  N   ALA A 438    21612  17285  24764   3121   1114  -2339       N  
ATOM   2737  CA  ALA A 438     -66.405   3.143  16.259  1.00164.96           C  
ANISOU 2737  CA  ALA A 438    21381  16937  24357   2692    949  -2281       C  
ATOM   2738  C   ALA A 438     -65.215   3.437  17.187  1.00165.88           C  
ANISOU 2738  C   ALA A 438    21696  16957  24374   2565    901  -2767       C  
ATOM   2739  O   ALA A 438     -64.145   3.850  16.726  1.00165.93           O  
ANISOU 2739  O   ALA A 438    21810  16720  24516   2260    756  -2780       O  
ATOM   2740  CB  ALA A 438     -66.257   3.939  14.971  1.00166.06           C  
ANISOU 2740  CB  ALA A 438    21557  16669  24870   2521    809  -1940       C  
ATOM   2741  N   LYS A 439     -65.392   3.187  18.481  1.00166.75           N  
ANISOU 2741  N   LYS A 439    21843  17284  24232   2784   1018  -3150       N  
ATOM   2742  CA  LYS A 439     -64.301   3.282  19.444  1.00167.49           C  
ANISOU 2742  CA  LYS A 439    22111  17376  24151   2668    952  -3613       C  
ATOM   2743  C   LYS A 439     -63.883   1.869  19.780  1.00163.46           C  
ANISOU 2743  C   LYS A 439    21517  17411  23178   2525    962  -3585       C  
ATOM   2744  O   LYS A 439     -62.741   1.608  20.147  1.00162.54           O  
ANISOU 2744  O   LYS A 439    21486  17375  22898   2297    846  -3801       O  
ATOM   2745  CB  LYS A 439     -64.728   4.016  20.713  1.00171.83           C  
ANISOU 2745  CB  LYS A 439    22801  17787  24701   3014   1062  -4095       C  
ATOM   2746  CG  LYS A 439     -64.796   5.530  20.589  1.00176.56           C  
ANISOU 2746  CG  LYS A 439    23555  17761  25771   3124   1008  -4263       C  
ATOM   2747  CD  LYS A 439     -63.423   6.157  20.437  1.00177.52           C  
ANISOU 2747  CD  LYS A 439    23852  17534  26063   2773    789  -4450       C  
ATOM   2748  CE  LYS A 439     -63.524   7.667  20.567  1.00182.95           C  
ANISOU 2748  CE  LYS A 439    24729  17583  27200   2914    738  -4701       C  
ATOM   2749  NZ  LYS A 439     -62.204   8.338  20.445  1.00184.44           N  
ANISOU 2749  NZ  LYS A 439    25083  17401  27594   2551    516  -4884       N  
ATOM   2750  N   PHE A 440     -64.841   0.958  19.666  1.00161.34           N  
ANISOU 2750  N   PHE A 440    21072  17509  22721   2666   1092  -3311       N  
ATOM   2751  CA  PHE A 440     -64.576  -0.460  19.839  1.00157.49           C  
ANISOU 2751  CA  PHE A 440    20492  17519  21829   2533   1097  -3204       C  
ATOM   2752  C   PHE A 440     -63.684  -0.930  18.699  1.00154.22           C  
ANISOU 2752  C   PHE A 440    20036  17109  21450   2156    937  -2921       C  
ATOM   2753  O   PHE A 440     -62.694  -1.621  18.930  1.00152.17           O  
ANISOU 2753  O   PHE A 440    19804  17056  20958   1947    850  -3024       O  
ATOM   2754  CB  PHE A 440     -65.885  -1.258  19.873  1.00156.43           C  
ANISOU 2754  CB  PHE A 440    20166  17726  21546   2751   1266  -2936       C  
ATOM   2755  CG  PHE A 440     -65.708  -2.718  20.200  1.00153.06           C  
ANISOU 2755  CG  PHE A 440    19662  17789  20705   2643   1280  -2846       C  
ATOM   2756  CD1 PHE A 440     -65.309  -3.115  21.468  1.00153.61           C  
ANISOU 2756  CD1 PHE A 440    19830  18103  20433   2708   1323  -3181       C  
ATOM   2757  CD2 PHE A 440     -65.949  -3.691  19.244  1.00149.66           C  
ANISOU 2757  CD2 PHE A 440    19076  17565  20223   2480   1239  -2425       C  
ATOM   2758  CE1 PHE A 440     -65.152  -4.451  21.774  1.00150.82           C  
ANISOU 2758  CE1 PHE A 440    19416  18173  19717   2615   1324  -3073       C  
ATOM   2759  CE2 PHE A 440     -65.792  -5.030  19.544  1.00146.87           C  
ANISOU 2759  CE2 PHE A 440    18666  17621  19518   2385   1241  -2343       C  
ATOM   2760  CZ  PHE A 440     -65.393  -5.410  20.812  1.00147.45           C  
ANISOU 2760  CZ  PHE A 440    18832  17917  19274   2454   1285  -2655       C  
ATOM   2761  N   ALA A 441     -64.027  -0.526  17.477  1.00154.09           N  
ANISOU 2761  N   ALA A 441    19957  16866  21724   2081    897  -2568       N  
ATOM   2762  CA  ALA A 441     -63.232  -0.864  16.303  1.00151.56           C  
ANISOU 2762  CA  ALA A 441    19607  16536  21442   1734    769  -2288       C  
ATOM   2763  C   ALA A 441     -61.767  -0.472  16.492  1.00152.10           C  
ANISOU 2763  C   ALA A 441    19801  16442  21549   1475    647  -2557       C  
ATOM   2764  O   ALA A 441     -60.859  -1.262  16.218  1.00149.49           O  
ANISOU 2764  O   ALA A 441    19431  16330  21037   1225    577  -2512       O  
ATOM   2765  CB  ALA A 441     -63.810  -0.192  15.065  1.00152.55           C  
ANISOU 2765  CB  ALA A 441    19694  16372  21898   1715    738  -1913       C  
ATOM   2766  N   ALA A 442     -61.545   0.742  16.981  1.00155.79           N  
ANISOU 2766  N   ALA A 442    20407  16521  22266   1541    617  -2849       N  
ATOM   2767  CA  ALA A 442     -60.190   1.230  17.224  1.00157.00           C  
ANISOU 2767  CA  ALA A 442    20669  16484  22500   1289    483  -3126       C  
ATOM   2768  C   ALA A 442     -59.531   0.464  18.360  1.00155.96           C  
ANISOU 2768  C   ALA A 442    20558  16691  22008   1281    455  -3469       C  
ATOM   2769  O   ALA A 442     -58.329   0.224  18.330  1.00155.12           O  
ANISOU 2769  O   ALA A 442    20447  16644  21849   1011    334  -3565       O  
ATOM   2770  CB  ALA A 442     -60.200   2.717  17.531  1.00161.64           C  
ANISOU 2770  CB  ALA A 442    21417  16547  23453   1373    443  -3374       C  
ATOM   2771  N   ALA A 443     -60.321   0.094  19.364  1.00156.32           N  
ANISOU 2771  N   ALA A 443    20619  16967  21808   1580    567  -3642       N  
ATOM   2772  CA  ALA A 443     -59.810  -0.678  20.491  1.00155.59           C  
ANISOU 2772  CA  ALA A 443    20560  17224  21334   1600    541  -3935       C  
ATOM   2773  C   ALA A 443     -59.301  -2.025  19.996  1.00151.35           C  
ANISOU 2773  C   ALA A 443    19885  17069  20553   1395    497  -3676       C  
ATOM   2774  O   ALA A 443     -58.336  -2.573  20.527  1.00150.57           O  
ANISOU 2774  O   ALA A 443    19798  17168  20244   1263    391  -3862       O  
ATOM   2775  CB  ALA A 443     -60.881  -0.862  21.545  1.00156.92           C  
ANISOU 2775  CB  ALA A 443    20758  17594  21268   1962    706  -4093       C  
ATOM   2776  N   ILE A 444     -59.970  -2.556  18.980  1.00150.69           N  
ANISOU 2776  N   ILE A 444    19671  17080  20503   1380    569  -3254       N  
ATOM   2777  CA  ILE A 444     -59.541  -3.775  18.305  1.00146.92           C  
ANISOU 2777  CA  ILE A 444    19074  16905  19843   1182    528  -2986       C  
ATOM   2778  C   ILE A 444     -58.263  -3.554  17.501  1.00146.45           C  
ANISOU 2778  C   ILE A 444    19001  16697  19946    851    400  -2950       C  
ATOM   2779  O   ILE A 444     -57.325  -4.356  17.562  1.00144.67           O  
ANISOU 2779  O   ILE A 444    18725  16700  19545    686    321  -2995       O  
ATOM   2780  CB  ILE A 444     -60.651  -4.309  17.387  1.00146.17           C  
ANISOU 2780  CB  ILE A 444    18861  16919  19757   1249    621  -2559       C  
ATOM   2781  CG1 ILE A 444     -61.659  -5.098  18.219  1.00145.63           C  
ANISOU 2781  CG1 ILE A 444    18744  17170  19418   1501    741  -2556       C  
ATOM   2782  CG2 ILE A 444     -60.081  -5.214  16.320  1.00143.02           C  
ANISOU 2782  CG2 ILE A 444    18373  16684  19284    992    556  -2277       C  
ATOM   2783  CD1 ILE A 444     -62.902  -5.459  17.466  1.00144.59           C  
ANISOU 2783  CD1 ILE A 444    18483  17116  19339   1597    827  -2171       C  
ATOM   2784  N   VAL A 445     -58.234  -2.462  16.746  1.00148.04           N  
ANISOU 2784  N   VAL A 445    19238  16517  20494    758    384  -2854       N  
ATOM   2785  CA  VAL A 445     -57.040  -2.084  16.005  1.00148.36           C  
ANISOU 2785  CA  VAL A 445    19261  16387  20720    433    285  -2816       C  
ATOM   2786  C   VAL A 445     -55.856  -1.869  16.963  1.00149.92           C  
ANISOU 2786  C   VAL A 445    19505  16570  20888    323    163  -3228       C  
ATOM   2787  O   VAL A 445     -54.709  -2.156  16.618  1.00149.20           O  
ANISOU 2787  O   VAL A 445    19333  16554  20801     61     81  -3228       O  
ATOM   2788  CB  VAL A 445     -57.294  -0.811  15.163  1.00149.41           C  
ANISOU 2788  CB  VAL A 445    19452  16068  21249    369    288  -2646       C  
ATOM   2789  CG1 VAL A 445     -56.040  -0.394  14.418  1.00150.16           C  
ANISOU 2789  CG1 VAL A 445    19522  15995  21538      9    205  -2588       C  
ATOM   2790  CG2 VAL A 445     -58.426  -1.053  14.179  1.00148.05           C  
ANISOU 2790  CG2 VAL A 445    19224  15934  21096    467    374  -2221       C  
ATOM   2791  N   ALA A 446     -56.148  -1.411  18.180  1.00150.75           N  
ANISOU 2791  N   ALA A 446    19731  16606  20943    532    151  -3584       N  
ATOM   2792  CA  ALA A 446     -55.116  -1.108  19.178  1.00152.87           C  
ANISOU 2792  CA  ALA A 446    20068  16841  21175    445      5  -4008       C  
ATOM   2793  C   ALA A 446     -54.714  -2.313  20.032  1.00150.95           C  
ANISOU 2793  C   ALA A 446    19780  17049  20526    491    -45  -4152       C  
ATOM   2794  O   ALA A 446     -54.202  -2.160  21.144  1.00152.94           O  
ANISOU 2794  O   ALA A 446    20118  17342  20652    524   -157  -4530       O  
ATOM   2795  CB  ALA A 446     -55.580   0.028  20.076  1.00156.88           C  
ANISOU 2795  CB  ALA A 446    20759  17036  21813    645      1  -4355       C  
ATOM   2796  N   ILE A 447     -54.978  -3.511  19.529  1.00147.37           N  
ANISOU 2796  N   ILE A 447    19205  16923  19864    499     26  -3851       N  
ATOM   2797  CA  ILE A 447     -54.482  -4.715  20.171  1.00145.53           C  
ANISOU 2797  CA  ILE A 447    18918  17090  19286    507    -39  -3928       C  
ATOM   2798  C   ILE A 447     -53.103  -5.015  19.613  1.00144.72           C  
ANISOU 2798  C   ILE A 447    18686  17032  19268    210   -167  -3903       C  
ATOM   2799  O   ILE A 447     -52.912  -4.985  18.396  1.00143.53           O  
ANISOU 2799  O   ILE A 447    18440  16792  19304     34   -121  -3626       O  
ATOM   2800  CB  ILE A 447     -55.411  -5.925  19.943  1.00145.56           C  
ANISOU 2800  CB  ILE A 447    18858  17411  19036    657     86  -3627       C  
ATOM   2801  CG1 ILE A 447     -56.776  -5.687  20.586  1.00146.67           C  
ANISOU 2801  CG1 ILE A 447    19087  17558  19083    959    229  -3653       C  
ATOM   2802  CG2 ILE A 447     -54.787  -7.197  20.502  1.00143.80           C  
ANISOU 2802  CG2 ILE A 447    18582  17563  18494    639     -2  -3672       C  
ATOM   2803  CD1 ILE A 447     -57.751  -6.809  20.340  1.00143.99           C  
ANISOU 2803  CD1 ILE A 447    18664  17508  18536   1081    349  -3337       C  
ATOM   2804  N   PRO A 448     -52.134  -5.276  20.504  1.00147.63           N  
ANISOU 2804  N   PRO A 448    19046  17548  19499    156   -329  -4192       N  
ATOM   2805  CA  PRO A 448     -50.761  -5.614  20.110  1.00147.26           C  
ANISOU 2805  CA  PRO A 448    18839  17582  19531   -106   -459  -4198       C  
ATOM   2806  C   PRO A 448     -50.744  -6.778  19.125  1.00143.73           C  
ANISOU 2806  C   PRO A 448    18245  17375  18990   -157   -372  -3846       C  
ATOM   2807  O   PRO A 448     -51.625  -7.642  19.197  1.00141.53           O  
ANISOU 2807  O   PRO A 448    17998  17302  18476     28   -282  -3683       O  
ATOM   2808  CB  PRO A 448     -50.101  -5.997  21.437  1.00147.13           C  
ANISOU 2808  CB  PRO A 448    18851  17779  19273    -48   -644  -4534       C  
ATOM   2809  CG  PRO A 448     -50.865  -5.221  22.467  1.00149.71           C  
ANISOU 2809  CG  PRO A 448    19392  17969  19521    158   -634  -4805       C  
ATOM   2810  CD  PRO A 448     -52.284  -5.179  21.969  1.00148.26           C  
ANISOU 2810  CD  PRO A 448    19269  17720  19343    346   -404  -4545       C  
ATOM   2811  N   ASN A 449     -49.772  -6.802  18.218  1.00142.74           N  
ANISOU 2811  N   ASN A 449    17963  17224  19047   -406   -393  -3737       N  
ATOM   2812  CA  ASN A 449     -49.710  -7.864  17.223  1.00139.81           C  
ANISOU 2812  CA  ASN A 449    17468  17066  18588   -453   -303  -3435       C  
ATOM   2813  C   ASN A 449     -49.478  -9.235  17.831  1.00138.04           C  
ANISOU 2813  C   ASN A 449    17193  17196  18059   -329   -376  -3474       C  
ATOM   2814  O   ASN A 449     -49.733 -10.239  17.188  1.00135.56           O  
ANISOU 2814  O   ASN A 449    16828  17057  17620   -295   -299  -3240       O  
ATOM   2815  CB  ASN A 449     -48.636  -7.562  16.182  1.00140.88           C  
ANISOU 2815  CB  ASN A 449    17439  17119  18969   -742   -291  -3339       C  
ATOM   2816  CG  ASN A 449     -49.146  -6.667  15.073  1.00141.41           C  
ANISOU 2816  CG  ASN A 449    17553  16908  19270   -855   -156  -3094       C  
ATOM   2817  OD1 ASN A 449     -50.344  -6.639  14.792  1.00140.29           O  
ANISOU 2817  OD1 ASN A 449    17527  16706  19070   -706    -57  -2911       O  
ATOM   2818  ND2 ASN A 449     -48.245  -5.920  14.449  1.00143.43           N  
ANISOU 2818  ND2 ASN A 449    17709  16991  19796  -1123   -158  -3074       N  
ATOM   2819  N   SER A 450     -49.007  -9.269  19.073  1.00141.32           N  
ANISOU 2819  N   SER A 450    17638  17705  18354   -261   -537  -3769       N  
ATOM   2820  CA  SER A 450     -48.718 -10.525  19.761  1.00140.18           C  
ANISOU 2820  CA  SER A 450    17456  17882  17923   -141   -637  -3808       C  
ATOM   2821  C   SER A 450     -49.963 -11.213  20.296  1.00138.65           C  
ANISOU 2821  C   SER A 450    17405  17836  17438    108   -558  -3699       C  
ATOM   2822  O   SER A 450     -50.126 -12.423  20.142  1.00136.52           O  
ANISOU 2822  O   SER A 450    17098  17783  16989    181   -541  -3520       O  
ATOM   2823  CB  SER A 450     -47.759 -10.272  20.911  1.00143.33           C  
ANISOU 2823  CB  SER A 450    17841  18336  18283   -165   -864  -4152       C  
ATOM   2824  OG  SER A 450     -46.541  -9.767  20.411  1.00144.86           O  
ANISOU 2824  OG  SER A 450    17856  18428  18758   -414   -946  -4232       O  
ATOM   2825  N   VAL A 451     -50.828 -10.435  20.939  1.00138.69           N  
ANISOU 2825  N   VAL A 451    17569  17718  17409    237   -505  -3812       N  
ATOM   2826  CA  VAL A 451     -52.117 -10.925  21.419  1.00137.73           C  
ANISOU 2826  CA  VAL A 451    17563  17725  17043    468   -389  -3696       C  
ATOM   2827  C   VAL A 451     -52.921 -11.457  20.236  1.00135.00           C  
ANISOU 2827  C   VAL A 451    17162  17380  16753    460   -231  -3324       C  
ATOM   2828  O   VAL A 451     -53.348 -12.629  20.195  1.00133.02           O  
ANISOU 2828  O   VAL A 451    16893  17345  16303    539   -203  -3129       O  
ATOM   2829  CB  VAL A 451     -52.897  -9.796  22.123  1.00138.64           C  
ANISOU 2829  CB  VAL A 451    17834  17664  17180    604   -323  -3889       C  
ATOM   2830  CG1 VAL A 451     -54.261 -10.258  22.521  1.00137.91           C  
ANISOU 2830  CG1 VAL A 451    17818  17714  16866    836   -166  -3743       C  
ATOM   2831  CG2 VAL A 451     -52.143  -9.310  23.344  1.00141.66           C  
ANISOU 2831  CG2 VAL A 451    18302  18058  17464    616   -497  -4285       C  
ATOM   2832  N   MET A 452     -53.056 -10.575  19.250  1.00135.79           N  
ANISOU 2832  N   MET A 452    17237  17224  17132    344   -150  -3226       N  
ATOM   2833  CA  MET A 452     -53.606 -10.890  17.941  1.00133.70           C  
ANISOU 2833  CA  MET A 452    16916  16926  16957    282    -34  -2887       C  
ATOM   2834  C   MET A 452     -52.980 -12.146  17.375  1.00131.55           C  
ANISOU 2834  C   MET A 452    16540  16867  16578    196    -75  -2748       C  
ATOM   2835  O   MET A 452     -53.641 -12.957  16.747  1.00129.57           O  
ANISOU 2835  O   MET A 452    16278  16715  16238    229     -7  -2495       O  
ATOM   2836  CB  MET A 452     -53.361  -9.727  16.979  1.00139.12           C  
ANISOU 2836  CB  MET A 452    17582  17312  17964    111      7  -2836       C  
ATOM   2837  CG  MET A 452     -54.263  -8.536  17.194  1.00141.03           C  
ANISOU 2837  CG  MET A 452    17933  17293  18361    217     76  -2877       C  
ATOM   2838  SD  MET A 452     -55.985  -9.040  17.102  1.00139.56           S  
ANISOU 2838  SD  MET A 452    17781  17210  18035    450    217  -2609       S  
ATOM   2839  CE  MET A 452     -55.994  -9.754  15.454  1.00136.99           C  
ANISOU 2839  CE  MET A 452    17359  16943  17749    276    252  -2221       C  
ATOM   2840  N   GLY A 453     -51.679 -12.273  17.591  1.00134.71           N  
ANISOU 2840  N   GLY A 453    16855  17324  17006     86   -195  -2927       N  
ATOM   2841  CA  GLY A 453     -50.900 -13.394  17.114  1.00133.27           C  
ANISOU 2841  CA  GLY A 453    16555  17328  16754     20   -241  -2848       C  
ATOM   2842  C   GLY A 453     -51.334 -14.720  17.690  1.00131.79           C  
ANISOU 2842  C   GLY A 453    16407  17376  16290    186   -281  -2773       C  
ATOM   2843  O   GLY A 453     -51.658 -15.635  16.939  1.00129.90           O  
ANISOU 2843  O   GLY A 453    16149  17219  15990    187   -228  -2553       O  
ATOM   2844  N   GLY A 454     -51.330 -14.829  19.017  1.00132.66           N  
ANISOU 2844  N   GLY A 454    16585  17592  16227    317   -381  -2952       N  
ATOM   2845  CA  GLY A 454     -51.762 -16.051  19.671  1.00131.69           C  
ANISOU 2845  CA  GLY A 454    16514  17689  15833    469   -421  -2861       C  
ATOM   2846  C   GLY A 454     -53.171 -16.426  19.244  1.00130.10           C  
ANISOU 2846  C   GLY A 454    16378  17490  15564    546   -273  -2588       C  
ATOM   2847  O   GLY A 454     -53.442 -17.570  18.834  1.00128.44           O  
ANISOU 2847  O   GLY A 454    16154  17387  15261    562   -269  -2384       O  
ATOM   2848  N   MET A 455     -54.063 -15.440  19.305  1.00131.45           N  
ANISOU 2848  N   MET A 455    16612  17526  15806    592   -159  -2587       N  
ATOM   2849  CA  MET A 455     -55.468 -15.667  18.974  1.00130.42           C  
ANISOU 2849  CA  MET A 455    16515  17402  15637    674    -23  -2334       C  
ATOM   2850  C   MET A 455     -55.649 -16.176  17.532  1.00128.43           C  
ANISOU 2850  C   MET A 455    16198  17106  15492    553     17  -2069       C  
ATOM   2851  O   MET A 455     -56.267 -17.227  17.297  1.00127.05           O  
ANISOU 2851  O   MET A 455    16024  17048  15201    583     28  -1858       O  
ATOM   2852  CB  MET A 455     -56.251 -14.369  19.210  1.00131.57           C  
ANISOU 2852  CB  MET A 455    16714  17380  15898    751     86  -2407       C  
ATOM   2853  CG  MET A 455     -57.750 -14.445  18.995  1.00131.13           C  
ANISOU 2853  CG  MET A 455    16660  17335  15829    862    228  -2165       C  
ATOM   2854  SD  MET A 455     -58.273 -14.052  17.312  1.00129.95           S  
ANISOU 2854  SD  MET A 455    16444  16990  15940    735    294  -1884       S  
ATOM   2855  CE  MET A 455     -57.798 -12.331  17.202  1.00132.17           C  
ANISOU 2855  CE  MET A 455    16761  16963  16496    689    305  -2095       C  
ATOM   2856  N   LYS A 456     -55.066 -15.461  16.574  1.00127.79           N  
ANISOU 2856  N   LYS A 456    16070  16862  15623    403     32  -2083       N  
ATOM   2857  CA  LYS A 456     -55.203 -15.811  15.161  1.00126.37           C  
ANISOU 2857  CA  LYS A 456    15850  16644  15520    282     77  -1850       C  
ATOM   2858  C   LYS A 456     -54.574 -17.154  14.867  1.00125.05           C  
ANISOU 2858  C   LYS A 456    15646  16638  15230    247      7  -1809       C  
ATOM   2859  O   LYS A 456     -55.096 -17.937  14.076  1.00123.75           O  
ANISOU 2859  O   LYS A 456    15492  16515  15012    223     27  -1601       O  
ATOM   2860  CB  LYS A 456     -54.583 -14.739  14.264  1.00130.49           C  
ANISOU 2860  CB  LYS A 456    16335  16975  16271    118    115  -1874       C  
ATOM   2861  CG  LYS A 456     -55.394 -13.453  14.224  1.00131.80           C  
ANISOU 2861  CG  LYS A 456    16550  16928  16599    149    188  -1837       C  
ATOM   2862  CD  LYS A 456     -54.820 -12.449  13.244  1.00132.86           C  
ANISOU 2862  CD  LYS A 456    16659  16855  16966    -34    221  -1804       C  
ATOM   2863  CE  LYS A 456     -53.318 -12.362  13.343  1.00133.67           C  
ANISOU 2863  CE  LYS A 456    16684  16974  17131   -175    162  -2010       C  
ATOM   2864  NZ  LYS A 456     -52.784 -11.669  12.139  1.00134.51           N  
ANISOU 2864  NZ  LYS A 456    16746  16932  17428   -386    222  -1892       N  
ATOM   2865  N   THR A 457     -53.438 -17.406  15.498  1.00128.20           N  
ANISOU 2865  N   THR A 457    15999  17114  15595    249    -90  -2017       N  
ATOM   2866  CA  THR A 457     -52.768 -18.687  15.368  1.00127.37           C  
ANISOU 2866  CA  THR A 457    15853  17151  15392    254   -170  -2006       C  
ATOM   2867  C   THR A 457     -53.701 -19.825  15.771  1.00126.35           C  
ANISOU 2867  C   THR A 457    15801  17133  15073    373   -196  -1842       C  
ATOM   2868  O   THR A 457     -53.836 -20.817  15.042  1.00125.24           O  
ANISOU 2868  O   THR A 457    15667  17026  14892    348   -204  -1694       O  
ATOM   2869  CB  THR A 457     -51.503 -18.737  16.235  1.00129.04           C  
ANISOU 2869  CB  THR A 457    15992  17440  15595    275   -299  -2256       C  
ATOM   2870  OG1 THR A 457     -50.466 -17.959  15.621  1.00130.01           O  
ANISOU 2870  OG1 THR A 457    15999  17479  15919    124   -279  -2376       O  
ATOM   2871  CG2 THR A 457     -51.041 -20.175  16.424  1.00128.47           C  
ANISOU 2871  CG2 THR A 457    15898  17518  15395    351   -404  -2231       C  
ATOM   2872  N   PHE A 458     -54.375 -19.661  16.908  1.00127.36           N  
ANISOU 2872  N   PHE A 458    15993  17314  15085    494   -200  -1864       N  
ATOM   2873  CA  PHE A 458     -55.365 -20.653  17.337  1.00126.77           C  
ANISOU 2873  CA  PHE A 458    15980  17346  14839    589   -202  -1675       C  
ATOM   2874  C   PHE A 458     -56.454 -20.848  16.275  1.00125.59           C  
ANISOU 2874  C   PHE A 458    15836  17134  14748    529   -116  -1415       C  
ATOM   2875  O   PHE A 458     -56.882 -21.973  15.967  1.00124.74           O  
ANISOU 2875  O   PHE A 458    15750  17078  14566    520   -153  -1239       O  
ATOM   2876  CB  PHE A 458     -56.020 -20.236  18.654  1.00130.63           C  
ANISOU 2876  CB  PHE A 458    16529  17912  15192    723   -169  -1732       C  
ATOM   2877  CG  PHE A 458     -56.823 -21.326  19.286  1.00130.52           C  
ANISOU 2877  CG  PHE A 458    16566  18045  14983    809   -177  -1545       C  
ATOM   2878  CD1 PHE A 458     -56.319 -22.024  20.366  1.00131.44           C  
ANISOU 2878  CD1 PHE A 458    16730  18305  14905    891   -288  -1612       C  
ATOM   2879  CD2 PHE A 458     -58.073 -21.656  18.809  1.00129.81           C  
ANISOU 2879  CD2 PHE A 458    16468  17950  14905    797    -86  -1286       C  
ATOM   2880  CE1 PHE A 458     -57.035 -23.037  20.957  1.00131.65           C  
ANISOU 2880  CE1 PHE A 458    16810  18459  14752    954   -294  -1411       C  
ATOM   2881  CE2 PHE A 458     -58.794 -22.675  19.387  1.00130.01           C  
ANISOU 2881  CE2 PHE A 458    16525  18104  14770    849    -93  -1095       C  
ATOM   2882  CZ  PHE A 458     -58.276 -23.365  20.470  1.00130.95           C  
ANISOU 2882  CZ  PHE A 458    16704  18357  14693    925   -188  -1150       C  
ATOM   2883  N   LEU A 459     -56.901 -19.719  15.738  1.00125.56           N  
ANISOU 2883  N   LEU A 459    15814  17005  14887    486    -19  -1395       N  
ATOM   2884  CA  LEU A 459     -57.965 -19.668  14.742  1.00124.87           C  
ANISOU 2884  CA  LEU A 459    15722  16854  14871    432     47  -1151       C  
ATOM   2885  C   LEU A 459     -57.619 -20.513  13.490  1.00123.71           C  
ANISOU 2885  C   LEU A 459    15577  16700  14729    306     -3  -1041       C  
ATOM   2886  O   LEU A 459     -58.378 -21.430  13.103  1.00123.03           O  
ANISOU 2886  O   LEU A 459    15514  16655  14577    290    -34   -847       O  
ATOM   2887  CB  LEU A 459     -58.203 -18.199  14.372  1.00124.57           C  
ANISOU 2887  CB  LEU A 459    15666  16654  15011    409    133  -1178       C  
ATOM   2888  CG  LEU A 459     -59.319 -17.682  13.473  1.00124.59           C  
ANISOU 2888  CG  LEU A 459    15652  16557  15129    380    198   -948       C  
ATOM   2889  CD1 LEU A 459     -60.643 -18.098  14.045  1.00124.75           C  
ANISOU 2889  CD1 LEU A 459    15650  16673  15075    498    232   -787       C  
ATOM   2890  CD2 LEU A 459     -59.234 -16.160  13.327  1.00125.95           C  
ANISOU 2890  CD2 LEU A 459    15822  16539  15496    375    261  -1030       C  
ATOM   2891  N   PHE A 460     -56.464 -20.215  12.882  1.00120.15           N  
ANISOU 2891  N   PHE A 460    15099  16200  14353    215     -7  -1175       N  
ATOM   2892  CA  PHE A 460     -55.980 -20.911  11.680  1.00119.51           C  
ANISOU 2892  CA  PHE A 460    15023  16124  14262    107    -25  -1119       C  
ATOM   2893  C   PHE A 460     -55.618 -22.378  11.916  1.00119.00           C  
ANISOU 2893  C   PHE A 460    14984  16157  14075    158   -122  -1140       C  
ATOM   2894  O   PHE A 460     -55.825 -23.234  11.040  1.00118.49           O  
ANISOU 2894  O   PHE A 460    14966  16094  13963    106   -149  -1032       O  
ATOM   2895  CB  PHE A 460     -54.771 -20.170  11.121  1.00119.74           C  
ANISOU 2895  CB  PHE A 460    14991  16102  14403      6     24  -1267       C  
ATOM   2896  CG  PHE A 460     -55.089 -18.812  10.586  1.00120.45           C  
ANISOU 2896  CG  PHE A 460    15076  16057  14633    -78    111  -1202       C  
ATOM   2897  CD1 PHE A 460     -54.659 -17.673  11.246  1.00121.62           C  
ANISOU 2897  CD1 PHE A 460    15185  16116  14908    -74    134  -1357       C  
ATOM   2898  CD2 PHE A 460     -55.858 -18.675   9.445  1.00120.24           C  
ANISOU 2898  CD2 PHE A 460    15096  15978  14612   -160    151   -981       C  
ATOM   2899  CE1 PHE A 460     -54.963 -16.421  10.765  1.00122.57           C  
ANISOU 2899  CE1 PHE A 460    15314  16072  15183   -147    203  -1288       C  
ATOM   2900  CE2 PHE A 460     -56.156 -17.433   8.951  1.00121.16           C  
ANISOU 2900  CE2 PHE A 460    15215  15955  14867   -228    215   -893       C  
ATOM   2901  CZ  PHE A 460     -55.714 -16.301   9.612  1.00122.33           C  
ANISOU 2901  CZ  PHE A 460    15326  15989  15164   -219    246  -1042       C  
ATOM   2902  N   ALA A 461     -55.051 -22.656  13.088  1.00119.17           N  
ANISOU 2902  N   ALA A 461    14986  16249  14046    260   -187  -1284       N  
ATOM   2903  CA  ALA A 461     -54.773 -24.032  13.486  1.00119.02           C  
ANISOU 2903  CA  ALA A 461    14998  16303  13922    333   -298  -1281       C  
ATOM   2904  C   ALA A 461     -56.063 -24.830  13.437  1.00118.47           C  
ANISOU 2904  C   ALA A 461    15008  16235  13772    339   -321  -1044       C  
ATOM   2905  O   ALA A 461     -56.116 -25.932  12.860  1.00118.17           O  
ANISOU 2905  O   ALA A 461    15020  16177  13700    313   -387   -964       O  
ATOM   2906  CB  ALA A 461     -54.180 -24.080  14.874  1.00121.29           C  
ANISOU 2906  CB  ALA A 461    15265  16673  14147    448   -378  -1429       C  
ATOM   2907  N   SER A 462     -57.105 -24.248  14.034  1.00117.20           N  
ANISOU 2907  N   SER A 462    14847  16091  13593    372   -264   -939       N  
ATOM   2908  CA  SER A 462     -58.443 -24.834  14.012  1.00117.01           C  
ANISOU 2908  CA  SER A 462    14855  16082  13522    362   -267   -692       C  
ATOM   2909  C   SER A 462     -58.969 -25.025  12.586  1.00116.43           C  
ANISOU 2909  C   SER A 462    14798  15929  13509    234   -272   -545       C  
ATOM   2910  O   SER A 462     -59.638 -26.017  12.299  1.00116.33           O  
ANISOU 2910  O   SER A 462    14827  15913  13459    190   -344   -380       O  
ATOM   2911  CB  SER A 462     -59.411 -23.974  14.810  1.00118.02           C  
ANISOU 2911  CB  SER A 462    14944  16252  13646    432   -168   -628       C  
ATOM   2912  OG  SER A 462     -60.683 -24.583  14.819  1.00118.13           O  
ANISOU 2912  OG  SER A 462    14950  16303  13630    416   -166   -377       O  
ATOM   2913  N   VAL A 463     -58.693 -24.067  11.704  1.00114.99           N  
ANISOU 2913  N   VAL A 463    14591  15682  13417    164   -205   -595       N  
ATOM   2914  CA  VAL A 463     -59.056 -24.233  10.296  1.00114.74           C  
ANISOU 2914  CA  VAL A 463    14596  15595  13404     39   -221   -469       C  
ATOM   2915  C   VAL A 463     -58.427 -25.495   9.688  1.00114.57           C  
ANISOU 2915  C   VAL A 463    14650  15573  13309     -1   -310   -522       C  
ATOM   2916  O   VAL A 463     -59.118 -26.299   9.056  1.00114.58           O  
ANISOU 2916  O   VAL A 463    14715  15551  13269    -69   -388   -382       O  
ATOM   2917  CB  VAL A 463     -58.635 -23.020   9.448  1.00114.99           C  
ANISOU 2917  CB  VAL A 463    14604  15564  13523    -35   -132   -517       C  
ATOM   2918  CG1 VAL A 463     -58.826 -23.320   7.967  1.00115.03           C  
ANISOU 2918  CG1 VAL A 463    14673  15542  13491   -166   -159   -404       C  
ATOM   2919  CG2 VAL A 463     -59.450 -21.803   9.836  1.00115.46           C  
ANISOU 2919  CG2 VAL A 463    14608  15577  13684      5    -60   -435       C  
ATOM   2920  N   VAL A 464     -57.116 -25.658   9.880  1.00116.98           N  
ANISOU 2920  N   VAL A 464    14940  15897  13611     46   -304   -735       N  
ATOM   2921  CA  VAL A 464     -56.377 -26.834   9.381  1.00117.19           C  
ANISOU 2921  CA  VAL A 464    15024  15914  13587     51   -374   -826       C  
ATOM   2922  C   VAL A 464     -56.940 -28.153   9.892  1.00117.25           C  
ANISOU 2922  C   VAL A 464    15108  15903  13541     96   -506   -724       C  
ATOM   2923  O   VAL A 464     -57.168 -29.099   9.127  1.00117.51           O  
ANISOU 2923  O   VAL A 464    15234  15877  13538     44   -582   -678       O  
ATOM   2924  CB  VAL A 464     -54.902 -26.806   9.791  1.00116.76           C  
ANISOU 2924  CB  VAL A 464    14896  15901  13568    131   -357  -1065       C  
ATOM   2925  CG1 VAL A 464     -54.181 -27.976   9.152  1.00117.30           C  
ANISOU 2925  CG1 VAL A 464    15012  15950  13605    158   -410  -1163       C  
ATOM   2926  CG2 VAL A 464     -54.254 -25.515   9.376  1.00117.03           C  
ANISOU 2926  CG2 VAL A 464    14840  15946  13681     65   -231  -1164       C  
ATOM   2927  N   ILE A 465     -57.104 -28.221  11.210  1.00116.84           N  
ANISOU 2927  N   ILE A 465    15024  15896  13473    190   -535   -698       N  
ATOM   2928  CA  ILE A 465     -57.661 -29.407  11.852  1.00117.21           C  
ANISOU 2928  CA  ILE A 465    15138  15928  13470    224   -651   -563       C  
ATOM   2929  C   ILE A 465     -59.065 -29.703  11.313  1.00117.18           C  
ANISOU 2929  C   ILE A 465    15172  15883  13469    107   -680   -321       C  
ATOM   2930  O   ILE A 465     -59.418 -30.857  11.061  1.00117.66           O  
ANISOU 2930  O   ILE A 465    15318  15869  13519     61   -797   -226       O  
ATOM   2931  CB  ILE A 465     -57.706 -29.246  13.385  1.00121.66           C  
ANISOU 2931  CB  ILE A 465    15662  16582  13979    335   -651   -547       C  
ATOM   2932  CG1 ILE A 465     -56.290 -29.190  13.954  1.00122.06           C  
ANISOU 2932  CG1 ILE A 465    15680  16673  14027    446   -684   -779       C  
ATOM   2933  CG2 ILE A 465     -58.438 -30.403  14.020  1.00122.32           C  
ANISOU 2933  CG2 ILE A 465    15813  16655  14006    342   -751   -346       C  
ATOM   2934  CD1 ILE A 465     -55.401 -30.323  13.476  1.00122.52           C  
ANISOU 2934  CD1 ILE A 465    15783  16657  14111    483   -792   -870       C  
ATOM   2935  N   SER A 466     -59.862 -28.658  11.124  1.00116.88           N  
ANISOU 2935  N   SER A 466    15065  15881  13464     59   -587   -222       N  
ATOM   2936  CA  SER A 466     -61.204 -28.849  10.598  1.00117.11           C  
ANISOU 2936  CA  SER A 466    15093  15888  13517    -52   -626     15       C  
ATOM   2937  C   SER A 466     -61.154 -29.417   9.181  1.00117.24           C  
ANISOU 2937  C   SER A 466    15205  15818  13523   -173   -716      9       C  
ATOM   2938  O   SER A 466     -61.935 -30.302   8.831  1.00117.83           O  
ANISOU 2938  O   SER A 466    15333  15839  13596   -267   -836    156       O  
ATOM   2939  CB  SER A 466     -61.991 -27.535  10.622  1.00121.84           C  
ANISOU 2939  CB  SER A 466    15583  16535  14176    -52   -511    109       C  
ATOM   2940  OG  SER A 466     -63.381 -27.753  10.842  1.00122.46           O  
ANISOU 2940  OG  SER A 466    15596  16647  14287    -95   -533    361       O  
ATOM   2941  N   GLY A 467     -60.232 -28.920   8.367  1.00115.19           N  
ANISOU 2941  N   GLY A 467    14971  15548  13249   -180   -657   -165       N  
ATOM   2942  CA  GLY A 467     -60.026 -29.494   7.051  1.00115.66           C  
ANISOU 2942  CA  GLY A 467    15144  15548  13253   -276   -723   -213       C  
ATOM   2943  C   GLY A 467     -59.692 -30.972   7.139  1.00116.28           C  
ANISOU 2943  C   GLY A 467    15332  15545  13303   -250   -852   -281       C  
ATOM   2944  O   GLY A 467     -60.099 -31.773   6.296  1.00117.06           O  
ANISOU 2944  O   GLY A 467    15546  15566  13363   -345   -967   -245       O  
ATOM   2945  N   GLN A 468     -58.927 -31.330   8.165  1.00117.12           N  
ANISOU 2945  N   GLN A 468    15412  15657  13430   -117   -848   -386       N  
ATOM   2946  CA  GLN A 468     -58.560 -32.728   8.400  1.00117.96           C  
ANISOU 2946  CA  GLN A 468    15620  15662  13538    -63   -980   -439       C  
ATOM   2947  C   GLN A 468     -59.764 -33.600   8.773  1.00118.57           C  
ANISOU 2947  C   GLN A 468    15751  15664  13637   -145  -1119   -198       C  
ATOM   2948  O   GLN A 468     -59.909 -34.737   8.299  1.00119.62           O  
ANISOU 2948  O   GLN A 468    16014  15659  13779   -197  -1260   -193       O  
ATOM   2949  CB  GLN A 468     -57.499 -32.798   9.496  1.00119.39           C  
ANISOU 2949  CB  GLN A 468    15741  15882  13739    105   -960   -573       C  
ATOM   2950  CG  GLN A 468     -57.017 -34.190   9.826  1.00120.52           C  
ANISOU 2950  CG  GLN A 468    15981  15906  13904    193  -1104   -620       C  
ATOM   2951  CD  GLN A 468     -55.916 -34.171  10.852  1.00120.75           C  
ANISOU 2951  CD  GLN A 468    15935  15993  13952    365  -1103   -749       C  
ATOM   2952  OE1 GLN A 468     -55.304 -33.129  11.091  1.00120.15           O  
ANISOU 2952  OE1 GLN A 468    15737  16038  13874    407   -991   -866       O  
ATOM   2953  NE2 GLN A 468     -55.639 -35.325  11.453  1.00121.90           N  
ANISOU 2953  NE2 GLN A 468    16154  16039  14125    459  -1247   -726       N  
ATOM   2954  N   ALA A 469     -60.620 -33.065   9.636  1.00117.29           N  
ANISOU 2954  N   ALA A 469    15484  15590  13491   -158  -1072     -6       N  
ATOM   2955  CA  ALA A 469     -61.859 -33.737   9.987  1.00118.09           C  
ANISOU 2955  CA  ALA A 469    15589  15656  13626   -259  -1170    258       C  
ATOM   2956  C   ALA A 469     -62.691 -33.952   8.724  1.00118.61           C  
ANISOU 2956  C   ALA A 469    15706  15649  13711   -435  -1266    346       C  
ATOM   2957  O   ALA A 469     -63.317 -34.993   8.562  1.00119.79           O  
ANISOU 2957  O   ALA A 469    15931  15686  13899   -545  -1422    471       O  
ATOM   2958  CB  ALA A 469     -62.630 -32.945  11.012  1.00120.27           C  
ANISOU 2958  CB  ALA A 469    15717  16075  13905   -230  -1056    429       C  
ATOM   2959  N   ILE A 470     -62.704 -32.964   7.833  1.00117.99           N  
ANISOU 2959  N   ILE A 470    15593  15632  13607   -473  -1188    291       N  
ATOM   2960  CA  ILE A 470     -63.340 -33.149   6.531  1.00118.73           C  
ANISOU 2960  CA  ILE A 470    15759  15672  13681   -634  -1299    347       C  
ATOM   2961  C   ILE A 470     -62.729 -34.327   5.788  1.00119.75           C  
ANISOU 2961  C   ILE A 470    16085  15654  13759   -661  -1432    176       C  
ATOM   2962  O   ILE A 470     -63.450 -35.138   5.207  1.00121.04           O  
ANISOU 2962  O   ILE A 470    16342  15715  13932   -803  -1606    261       O  
ATOM   2963  CB  ILE A 470     -63.202 -31.917   5.619  1.00118.17           C  
ANISOU 2963  CB  ILE A 470    15654  15685  13561   -654  -1195    296       C  
ATOM   2964  CG1 ILE A 470     -63.749 -30.650   6.287  1.00117.42           C  
ANISOU 2964  CG1 ILE A 470    15376  15703  13537   -603  -1059    434       C  
ATOM   2965  CG2 ILE A 470     -63.891 -32.183   4.289  1.00119.30           C  
ANISOU 2965  CG2 ILE A 470    15892  15788  13649   -824  -1340    369       C  
ATOM   2966  CD1 ILE A 470     -63.329 -29.361   5.581  1.00116.95           C  
ANISOU 2966  CD1 ILE A 470    15290  15693  13452   -592   -937    361       C  
ATOM   2967  N   VAL A 471     -61.394 -34.396   5.803  1.00119.43           N  
ANISOU 2967  N   VAL A 471    16097  15603  13677   -521  -1350    -77       N  
ATOM   2968  CA  VAL A 471     -60.632 -35.464   5.136  1.00120.64           C  
ANISOU 2968  CA  VAL A 471    16427  15620  13789   -493  -1439   -290       C  
ATOM   2969  C   VAL A 471     -61.045 -36.863   5.568  1.00121.97           C  
ANISOU 2969  C   VAL A 471    16703  15605  14036   -524  -1633   -211       C  
ATOM   2970  O   VAL A 471     -61.273 -37.743   4.733  1.00123.51           O  
ANISOU 2970  O   VAL A 471    17064  15652  14213   -616  -1785   -268       O  
ATOM   2971  CB  VAL A 471     -59.117 -35.342   5.405  1.00121.20           C  
ANISOU 2971  CB  VAL A 471    16475  15725  13851   -301  -1310   -549       C  
ATOM   2972  CG1 VAL A 471     -58.391 -36.563   4.881  1.00122.82           C  
ANISOU 2972  CG1 VAL A 471    16846  15774  14046   -233  -1402   -762       C  
ATOM   2973  CG2 VAL A 471     -58.546 -34.085   4.794  1.00120.41           C  
ANISOU 2973  CG2 VAL A 471    16292  15776  13681   -294  -1123   -654       C  
ATOM   2974  N   ALA A 472     -61.115 -37.059   6.883  1.00121.78           N  
ANISOU 2974  N   ALA A 472    16596  15584  14091   -451  -1632    -81       N  
ATOM   2975  CA  ALA A 472     -61.361 -38.379   7.472  1.00123.25           C  
ANISOU 2975  CA  ALA A 472    16879  15586  14363   -465  -1804     19       C  
ATOM   2976  C   ALA A 472     -62.711 -39.024   7.107  1.00124.60           C  
ANISOU 2976  C   ALA A 472    17104  15646  14594   -693  -1981    245       C  
ATOM   2977  O   ALA A 472     -62.959 -40.181   7.450  1.00126.22           O  
ANISOU 2977  O   ALA A 472    17409  15660  14888   -742  -2144    336       O  
ATOM   2978  CB  ALA A 472     -61.236 -38.287   8.982  1.00123.47           C  
ANISOU 2978  CB  ALA A 472    16798  15689  14424   -354  -1746    152       C  
ATOM   2979  N   LYS A 473     -63.576 -38.282   6.422  1.00124.73           N  
ANISOU 2979  N   LYS A 473    17045  15770  14576   -836  -1964    348       N  
ATOM   2980  CA  LYS A 473     -64.882 -38.788   6.000  1.00126.21           C  
ANISOU 2980  CA  LYS A 473    17245  15879  14830  -1068  -2146    565       C  
ATOM   2981  C   LYS A 473     -64.763 -39.868   4.923  1.00128.16           C  
ANISOU 2981  C   LYS A 473    17732  15901  15064  -1165  -2356    400       C  
ATOM   2982  O   LYS A 473     -65.658 -40.692   4.749  1.00130.01           O  
ANISOU 2982  O   LYS A 473    18022  15989  15387  -1355  -2564    548       O  
ATOM   2983  CB  LYS A 473     -65.750 -37.634   5.489  1.00124.84           C  
ANISOU 2983  CB  LYS A 473    16916  15891  14626  -1168  -2083    703       C  
ATOM   2984  CG  LYS A 473     -66.142 -36.618   6.557  1.00123.50           C  
ANISOU 2984  CG  LYS A 473    16509  15918  14497  -1089  -1895    888       C  
ATOM   2985  CD  LYS A 473     -66.938 -35.468   5.954  1.00123.09           C  
ANISOU 2985  CD  LYS A 473    16312  16017  14439  -1159  -1843   1006       C  
ATOM   2986  CE  LYS A 473     -67.299 -34.410   6.997  1.00122.05           C  
ANISOU 2986  CE  LYS A 473    15955  16064  14355  -1050  -1642   1150       C  
ATOM   2987  NZ  LYS A 473     -68.076 -33.289   6.391  1.00121.96           N  
ANISOU 2987  NZ  LYS A 473    15802  16169  14370  -1097  -1603   1269       N  
ATOM   2988  N   ALA A 474     -63.644 -39.861   4.209  1.00131.81           N  
ANISOU 2988  N   ALA A 474    18330  16336  15416  -1036  -2298     83       N  
ATOM   2989  CA  ALA A 474     -63.397 -40.824   3.138  1.00133.91           C  
ANISOU 2989  CA  ALA A 474    18845  16401  15634  -1088  -2465   -138       C  
ATOM   2990  C   ALA A 474     -62.472 -41.944   3.611  1.00135.06           C  
ANISOU 2990  C   ALA A 474    19131  16322  15863   -928  -2518   -309       C  
ATOM   2991  O   ALA A 474     -61.445 -41.680   4.242  1.00133.93           O  
ANISOU 2991  O   ALA A 474    18919  16247  15722   -711  -2360   -420       O  
ATOM   2992  CB  ALA A 474     -62.813 -40.129   1.918  1.00134.85           C  
ANISOU 2992  CB  ALA A 474    19032  16647  15556  -1052  -2356   -378       C  
ATOM   2993  N   PRO A 475     -62.865 -43.203   3.343  1.00135.89           N  
ANISOU 2993  N   PRO A 475    19427  16148  16058  -1038  -2760   -318       N  
ATOM   2994  CA  PRO A 475     -62.129 -44.406   3.748  1.00137.61           C  
ANISOU 2994  CA  PRO A 475    19805  16089  16394   -898  -2858   -455       C  
ATOM   2995  C   PRO A 475     -60.638 -44.283   3.470  1.00137.32           C  
ANISOU 2995  C   PRO A 475    19813  16087  16274   -619  -2695   -807       C  
ATOM   2996  O   PRO A 475     -60.249 -44.160   2.309  1.00138.03           O  
ANISOU 2996  O   PRO A 475    20018  16206  16220   -600  -2652  -1075       O  
ATOM   2997  CB  PRO A 475     -62.748 -45.506   2.879  1.00140.17           C  
ANISOU 2997  CB  PRO A 475    20371  16123  16763  -1085  -3134   -523       C  
ATOM   2998  CG  PRO A 475     -64.129 -45.027   2.614  1.00139.95           C  
ANISOU 2998  CG  PRO A 475    20234  16216  16723  -1370  -3222   -250       C  
ATOM   2999  CD  PRO A 475     -64.013 -43.531   2.477  1.00137.14           C  
ANISOU 2999  CD  PRO A 475    19677  16222  16210  -1310  -2976   -227       C  
ATOM   3000  N   PHE A 476     -59.822 -44.314   4.518  1.00137.03           N  
ANISOU 3000  N   PHE A 476    19680  16065  16321   -409  -2604   -799       N  
ATOM   3001  CA  PHE A 476     -58.379 -44.180   4.356  1.00136.94           C  
ANISOU 3001  CA  PHE A 476    19658  16106  16268   -138  -2450  -1113       C  
ATOM   3002  C   PHE A 476     -57.766 -45.419   3.706  1.00139.95           C  
ANISOU 3002  C   PHE A 476    20280  16187  16706    -20  -2577  -1403       C  
ATOM   3003  O   PHE A 476     -57.334 -46.348   4.390  1.00141.44           O  
ANISOU 3003  O   PHE A 476    20532  16147  17061    122  -2691  -1405       O  
ATOM   3004  CB  PHE A 476     -57.695 -43.906   5.697  1.00136.05           C  
ANISOU 3004  CB  PHE A 476    19368  16089  16236     50  -2359  -1018       C  
ATOM   3005  CG  PHE A 476     -57.421 -42.447   5.954  1.00133.36           C  
ANISOU 3005  CG  PHE A 476    18795  16087  15786     82  -2124   -993       C  
ATOM   3006  CD1 PHE A 476     -58.168 -41.730   6.874  1.00131.62           C  
ANISOU 3006  CD1 PHE A 476    18419  16026  15564    -14  -2082   -701       C  
ATOM   3007  CD2 PHE A 476     -56.392 -41.797   5.285  1.00132.89           C  
ANISOU 3007  CD2 PHE A 476    18675  16183  15637    210  -1937  -1269       C  
ATOM   3008  CE1 PHE A 476     -57.902 -40.388   7.108  1.00129.46           C  
ANISOU 3008  CE1 PHE A 476    17953  16027  15208     22  -1879   -704       C  
ATOM   3009  CE2 PHE A 476     -56.124 -40.459   5.514  1.00130.73           C  
ANISOU 3009  CE2 PHE A 476    18196  16185  15290    221  -1737  -1244       C  
ATOM   3010  CZ  PHE A 476     -56.879 -39.754   6.426  1.00129.01           C  
ANISOU 3010  CZ  PHE A 476    17845  16091  15080    131  -1718   -971       C  
ATOM   3011  N   THR A 477     -57.763 -45.435   2.377  1.00139.29           N  
ANISOU 3011  N   THR A 477    20344  16101  16480    -77  -2565  -1644       N  
ATOM   3012  CA  THR A 477     -57.096 -46.487   1.617  1.00142.40           C  
ANISOU 3012  CA  THR A 477    20973  16242  16890     64  -2642  -1989       C  
ATOM   3013  C   THR A 477     -55.717 -46.017   1.170  1.00142.34           C  
ANISOU 3013  C   THR A 477    20884  16420  16780    324  -2381  -2313       C  
ATOM   3014  O   THR A 477     -55.380 -44.836   1.295  1.00139.93           O  
ANISOU 3014  O   THR A 477    20360  16433  16376    343  -2160  -2264       O  
ATOM   3015  CB  THR A 477     -57.911 -46.902   0.370  1.00143.10           C  
ANISOU 3015  CB  THR A 477    21308  16209  16853   -153  -2799  -2097       C  
ATOM   3016  OG1 THR A 477     -57.909 -45.836  -0.587  1.00141.96           O  
ANISOU 3016  OG1 THR A 477    21115  16377  16448   -225  -2618  -2185       O  
ATOM   3017  CG2 THR A 477     -59.341 -47.243   0.750  1.00143.24           C  
ANISOU 3017  CG2 THR A 477    21358  16085  16982   -450  -3051  -1753       C  
ATOM   3018  N   ARG A 478     -54.916 -46.951   0.669  1.00144.49           N  
ANISOU 3018  N   ARG A 478    21323  16484  17094    527  -2405  -2644       N  
ATOM   3019  CA  ARG A 478     -53.634 -46.609   0.069  1.00145.19           C  
ANISOU 3019  CA  ARG A 478    21338  16749  17080    768  -2147  -2980       C  
ATOM   3020  C   ARG A 478     -53.834 -45.584  -1.052  1.00144.34           C  
ANISOU 3020  C   ARG A 478    21221  16947  16675    614  -1959  -3049       C  
ATOM   3021  O   ARG A 478     -53.020 -44.677  -1.228  1.00143.27           O  
ANISOU 3021  O   ARG A 478    20895  17101  16442    712  -1690  -3136       O  
ATOM   3022  CB  ARG A 478     -52.935 -47.873  -0.447  1.00150.10           C  
ANISOU 3022  CB  ARG A 478    22179  17069  17783    998  -2218  -3342       C  
ATOM   3023  CG  ARG A 478     -51.796 -47.641  -1.435  1.00151.80           C  
ANISOU 3023  CG  ARG A 478    22372  17466  17838   1211  -1942  -3739       C  
ATOM   3024  CD  ARG A 478     -50.723 -46.722  -0.866  1.00149.89           C  
ANISOU 3024  CD  ARG A 478    21780  17533  17637   1390  -1677  -3724       C  
ATOM   3025  NE  ARG A 478     -49.593 -46.537  -1.776  1.00151.90           N  
ANISOU 3025  NE  ARG A 478    21980  17972  17765   1593  -1394  -4087       N  
ATOM   3026  CZ  ARG A 478     -48.631 -45.635  -1.597  1.00150.77           C  
ANISOU 3026  CZ  ARG A 478    21529  18142  17616   1709  -1125  -4116       C  
ATOM   3027  NH1 ARG A 478     -48.683 -44.808  -0.558  1.00147.56           N  
ANISOU 3027  NH1 ARG A 478    20870  17887  17310   1638  -1121  -3825       N  
ATOM   3028  NH2 ARG A 478     -47.625 -45.548  -2.461  1.00153.12           N  
ANISOU 3028  NH2 ARG A 478    21771  18605  17803   1887   -857  -4442       N  
ATOM   3029  N   ARG A 479     -54.940 -45.722  -1.780  1.00144.41           N  
ANISOU 3029  N   ARG A 479    21430  16889  16551    357  -2119  -2983       N  
ATOM   3030  CA  ARG A 479     -55.323 -44.771  -2.818  1.00143.79           C  
ANISOU 3030  CA  ARG A 479    21366  17087  16182    177  -1997  -2983       C  
ATOM   3031  C   ARG A 479     -55.554 -43.373  -2.248  1.00140.13           C  
ANISOU 3031  C   ARG A 479    20616  16925  15703     77  -1846  -2678       C  
ATOM   3032  O   ARG A 479     -54.964 -42.390  -2.705  1.00139.32           O  
ANISOU 3032  O   ARG A 479    20389  17102  15443    111  -1594  -2744       O  
ATOM   3033  CB  ARG A 479     -56.581 -45.248  -3.533  1.00146.27           C  
ANISOU 3033  CB  ARG A 479    21931  17249  16396    -93  -2265  -2921       C  
ATOM   3034  CG  ARG A 479     -57.057 -44.320  -4.627  1.00146.03           C  
ANISOU 3034  CG  ARG A 479    21937  17492  16055   -286  -2187  -2894       C  
ATOM   3035  CD  ARG A 479     -58.362 -44.815  -5.209  1.00147.66           C  
ANISOU 3035  CD  ARG A 479    22364  17546  16195   -565  -2503  -2802       C  
ATOM   3036  NE  ARG A 479     -58.756 -44.059  -6.393  1.00148.22           N  
ANISOU 3036  NE  ARG A 479    22516  17865  15937   -731  -2461  -2812       N  
ATOM   3037  CZ  ARG A 479     -59.495 -42.952  -6.360  1.00145.95           C  
ANISOU 3037  CZ  ARG A 479    22057  17808  15588   -914  -2444  -2490       C  
ATOM   3038  NH1 ARG A 479     -59.908 -42.457  -5.197  1.00142.94           N  
ANISOU 3038  NH1 ARG A 479    21412  17452  15446   -944  -2440  -2160       N  
ATOM   3039  NH2 ARG A 479     -59.813 -42.333  -7.490  1.00146.95           N  
ANISOU 3039  NH2 ARG A 479    22284  18143  15407  -1053  -2428  -2499       N  
ATOM   3040  N   ASN A 480     -56.440 -43.281  -1.263  1.00139.69           N  
ANISOU 3040  N   ASN A 480    20460  16807  15809    -54  -1999  -2342       N  
ATOM   3041  CA  ASN A 480     -56.740 -41.994  -0.640  1.00136.50           C  
ANISOU 3041  CA  ASN A 480    19798  16657  15407   -135  -1871  -2062       C  
ATOM   3042  C   ASN A 480     -55.515 -41.397   0.071  1.00135.10           C  
ANISOU 3042  C   ASN A 480    19390  16637  15305     90  -1637  -2138       C  
ATOM   3043  O   ASN A 480     -55.287 -40.190  -0.009  1.00133.39           O  
ANISOU 3043  O   ASN A 480    19003  16675  15004     62  -1440  -2080       O  
ATOM   3044  CB  ASN A 480     -57.926 -42.122   0.329  1.00135.58           C  
ANISOU 3044  CB  ASN A 480    19621  16442  15451   -296  -2066  -1704       C  
ATOM   3045  CG  ASN A 480     -59.285 -42.134  -0.393  1.00136.26           C  
ANISOU 3045  CG  ASN A 480    19821  16502  15450   -579  -2251  -1542       C  
ATOM   3046  OD1 ASN A 480     -59.359 -42.078  -1.625  1.00137.72           O  
ANISOU 3046  OD1 ASN A 480    20161  16732  15434   -659  -2260  -1701       O  
ATOM   3047  ND2 ASN A 480     -60.362 -42.188   0.382  1.00135.45           N  
ANISOU 3047  ND2 ASN A 480    19630  16346  15488   -732  -2397  -1219       N  
ATOM   3048  N   ARG A 481     -54.736 -42.233   0.760  1.00134.62           N  
ANISOU 3048  N   ARG A 481    19321  16413  15415    306  -1677  -2259       N  
ATOM   3049  CA  ARG A 481     -53.500 -41.778   1.413  1.00133.84           C  
ANISOU 3049  CA  ARG A 481    18996  16455  15401    529  -1491  -2356       C  
ATOM   3050  C   ARG A 481     -52.468 -41.227   0.419  1.00134.75           C  
ANISOU 3050  C   ARG A 481    19053  16775  15370    624  -1228  -2633       C  
ATOM   3051  O   ARG A 481     -51.787 -40.232   0.690  1.00133.40           O  
ANISOU 3051  O   ARG A 481    18650  16834  15201    671  -1029  -2626       O  
ATOM   3052  CB  ARG A 481     -52.874 -42.913   2.227  1.00136.59           C  
ANISOU 3052  CB  ARG A 481    19367  16567  15962    754  -1622  -2438       C  
ATOM   3053  CG  ARG A 481     -53.653 -43.284   3.483  1.00135.61           C  
ANISOU 3053  CG  ARG A 481    19234  16300  15990    687  -1829  -2123       C  
ATOM   3054  CD  ARG A 481     -52.907 -44.309   4.327  1.00137.30           C  
ANISOU 3054  CD  ARG A 481    19460  16301  16408    928  -1952  -2180       C  
ATOM   3055  NE  ARG A 481     -52.853 -45.612   3.673  1.00140.45           N  
ANISOU 3055  NE  ARG A 481    20112  16379  16872   1000  -2102  -2376       N  
ATOM   3056  CZ  ARG A 481     -53.648 -46.634   3.969  1.00141.85           C  
ANISOU 3056  CZ  ARG A 481    20483  16246  17166    907  -2358  -2226       C  
ATOM   3057  NH1 ARG A 481     -54.566 -46.509   4.918  1.00140.37           N  
ANISOU 3057  NH1 ARG A 481    20247  16056  17030    738  -2472  -1860       N  
ATOM   3058  NH2 ARG A 481     -53.522 -47.784   3.316  1.00145.02           N  
ANISOU 3058  NH2 ARG A 481    21129  16336  17638    982  -2493  -2446       N  
ATOM   3059  N   PHE A 482     -52.348 -41.902  -0.717  1.00137.37           N  
ANISOU 3059  N   PHE A 482    19602  17021  15574    647  -1229  -2880       N  
ATOM   3060  CA  PHE A 482     -51.473 -41.475  -1.798  1.00138.85           C  
ANISOU 3060  CA  PHE A 482    19769  17412  15576    719   -967  -3141       C  
ATOM   3061  C   PHE A 482     -51.924 -40.125  -2.354  1.00137.12           C  
ANISOU 3061  C   PHE A 482    19477  17467  15155    496   -821  -2971       C  
ATOM   3062  O   PHE A 482     -51.128 -39.185  -2.447  1.00136.55           O  
ANISOU 3062  O   PHE A 482    19202  17635  15047    535   -571  -3003       O  
ATOM   3063  CB  PHE A 482     -51.461 -42.548  -2.894  1.00142.35           C  
ANISOU 3063  CB  PHE A 482    20511  17688  15888    771  -1028  -3436       C  
ATOM   3064  CG  PHE A 482     -50.805 -42.122  -4.175  1.00144.29           C  
ANISOU 3064  CG  PHE A 482    20792  18168  15864    799   -758  -3684       C  
ATOM   3065  CD1 PHE A 482     -49.454 -41.837  -4.225  1.00145.27           C  
ANISOU 3065  CD1 PHE A 482    20704  18472  16019   1016   -475  -3886       C  
ATOM   3066  CD2 PHE A 482     -51.547 -42.024  -5.342  1.00145.49           C  
ANISOU 3066  CD2 PHE A 482    21185  18373  15721    600   -791  -3706       C  
ATOM   3067  CE1 PHE A 482     -48.858 -41.453  -5.414  1.00147.41           C  
ANISOU 3067  CE1 PHE A 482    21002  18981  16028   1031   -199  -4096       C  
ATOM   3068  CE2 PHE A 482     -50.957 -41.641  -6.532  1.00147.62           C  
ANISOU 3068  CE2 PHE A 482    21508  18880  15701    619   -533  -3919       C  
ATOM   3069  CZ  PHE A 482     -49.613 -41.355  -6.567  1.00148.60           C  
ANISOU 3069  CZ  PHE A 482    21417  19189  15854    833   -222  -4109       C  
ATOM   3070  N   ILE A 483     -53.204 -40.029  -2.707  1.00136.52           N  
ANISOU 3070  N   ILE A 483    19558  17345  14970    258   -989  -2776       N  
ATOM   3071  CA  ILE A 483     -53.777 -38.777  -3.214  1.00135.08           C  
ANISOU 3071  CA  ILE A 483    19320  17389  14616     47   -896  -2575       C  
ATOM   3072  C   ILE A 483     -53.591 -37.615  -2.232  1.00132.19           C  
ANISOU 3072  C   ILE A 483    18661  17172  14393     43   -775  -2361       C  
ATOM   3073  O   ILE A 483     -53.219 -36.510  -2.633  1.00131.68           O  
ANISOU 3073  O   ILE A 483    18477  17324  14229    -10   -566  -2328       O  
ATOM   3074  CB  ILE A 483     -55.271 -38.937  -3.546  1.00134.96           C  
ANISOU 3074  CB  ILE A 483    19480  17276  14523   -194  -1150  -2363       C  
ATOM   3075  CG1 ILE A 483     -55.450 -39.964  -4.666  1.00138.20           C  
ANISOU 3075  CG1 ILE A 483    20204  17557  14751   -221  -1275  -2601       C  
ATOM   3076  CG2 ILE A 483     -55.869 -37.603  -3.964  1.00133.54           C  
ANISOU 3076  CG2 ILE A 483    19217  17316  14204   -386  -1071  -2124       C  
ATOM   3077  CD1 ILE A 483     -56.869 -40.389  -4.876  1.00138.61           C  
ANISOU 3077  CD1 ILE A 483    20425  17461  14782   -450  -1584  -2422       C  
ATOM   3078  N   LEU A 484     -53.851 -37.865  -0.952  1.00130.60           N  
ANISOU 3078  N   LEU A 484    18359  16848  14416     93   -909  -2216       N  
ATOM   3079  CA  LEU A 484     -53.609 -36.866   0.087  1.00128.24           C  
ANISOU 3079  CA  LEU A 484    17802  16673  14250    117   -810  -2059       C  
ATOM   3080  C   LEU A 484     -52.157 -36.428   0.135  1.00128.70           C  
ANISOU 3080  C   LEU A 484    17674  16879  14346    280   -577  -2261       C  
ATOM   3081  O   LEU A 484     -51.863 -35.238   0.229  1.00127.54           O  
ANISOU 3081  O   LEU A 484    17353  16908  14197    225   -415  -2188       O  
ATOM   3082  CB  LEU A 484     -54.000 -37.410   1.454  1.00127.16           C  
ANISOU 3082  CB  LEU A 484    17618  16385  14312    175   -991  -1912       C  
ATOM   3083  CG  LEU A 484     -55.489 -37.559   1.703  1.00126.35           C  
ANISOU 3083  CG  LEU A 484    17602  16185  14219     -8  -1188  -1635       C  
ATOM   3084  CD1 LEU A 484     -55.707 -38.128   3.080  1.00125.73           C  
ANISOU 3084  CD1 LEU A 484    17470  15983  14320     65  -1326  -1495       C  
ATOM   3085  CD2 LEU A 484     -56.141 -36.206   1.565  1.00124.64           C  
ANISOU 3085  CD2 LEU A 484    17275  16147  13937   -163  -1095  -1431       C  
ATOM   3086  N   THR A 485     -51.261 -37.411   0.108  1.00130.63           N  
ANISOU 3086  N   THR A 485    17946  17035  14652    482   -574  -2511       N  
ATOM   3087  CA  THR A 485     -49.826 -37.167   0.106  1.00131.68           C  
ANISOU 3087  CA  THR A 485    17879  17306  14846    657   -361  -2725       C  
ATOM   3088  C   THR A 485     -49.386 -36.245  -1.022  1.00132.49           C  
ANISOU 3088  C   THR A 485    17933  17643  14763    561    -95  -2797       C  
ATOM   3089  O   THR A 485     -48.776 -35.196  -0.780  1.00131.71           O  
ANISOU 3089  O   THR A 485    17604  17721  14719    536     76  -2755       O  
ATOM   3090  CB  THR A 485     -49.058 -38.479  -0.001  1.00134.29           C  
ANISOU 3090  CB  THR A 485    18281  17489  15255    898   -403  -2998       C  
ATOM   3091  OG1 THR A 485     -49.337 -39.281   1.152  1.00133.74           O  
ANISOU 3091  OG1 THR A 485    18234  17203  15380    993   -647  -2902       O  
ATOM   3092  CG2 THR A 485     -47.571 -38.214  -0.092  1.00135.78           C  
ANISOU 3092  CG2 THR A 485    18227  17849  15514   1082   -168  -3221       C  
ATOM   3093  N   ALA A 486     -49.694 -36.638  -2.254  1.00134.34           N  
ANISOU 3093  N   ALA A 486    18395  17875  14774    498    -68  -2900       N  
ATOM   3094  CA  ALA A 486     -49.306 -35.839  -3.406  1.00135.61           C  
ANISOU 3094  CA  ALA A 486    18545  18269  14712    401    188  -2953       C  
ATOM   3095  C   ALA A 486     -49.939 -34.448  -3.355  1.00133.42           C  
ANISOU 3095  C   ALA A 486    18185  18115  14394    173    227  -2654       C  
ATOM   3096  O   ALA A 486     -49.263 -33.449  -3.589  1.00133.61           O  
ANISOU 3096  O   ALA A 486    18034  18330  14400    126    456  -2634       O  
ATOM   3097  CB  ALA A 486     -49.685 -36.542  -4.688  1.00138.13           C  
ANISOU 3097  CB  ALA A 486    19167  18559  14758    362    168  -3101       C  
ATOM   3098  N   SER A 487     -51.226 -34.389  -3.016  1.00131.60           N  
ANISOU 3098  N   SER A 487    18064  17764  14173     37      1  -2417       N  
ATOM   3099  CA  SER A 487     -51.970 -33.125  -2.989  1.00129.80           C  
ANISOU 3099  CA  SER A 487    17776  17621  13921   -160     12  -2129       C  
ATOM   3100  C   SER A 487     -51.431 -32.139  -1.965  1.00128.02           C  
ANISOU 3100  C   SER A 487    17274  17460  13907   -130    115  -2045       C  
ATOM   3101  O   SER A 487     -51.227 -30.964  -2.274  1.00127.86           O  
ANISOU 3101  O   SER A 487    17150  17573  13858   -240    276  -1944       O  
ATOM   3102  CB  SER A 487     -53.437 -33.388  -2.703  1.00128.49           C  
ANISOU 3102  CB  SER A 487    17744  17309  13769   -276   -257  -1908       C  
ATOM   3103  OG  SER A 487     -53.959 -34.307  -3.636  1.00130.38           O  
ANISOU 3103  OG  SER A 487    18243  17473  13823   -326   -388  -1993       O  
ATOM   3104  N   MET A 488     -51.222 -32.612  -0.744  1.00126.93           N  
ANISOU 3104  N   MET A 488    17030  17218  13979     10      7  -2080       N  
ATOM   3105  CA  MET A 488     -50.644 -31.782   0.302  1.00125.60           C  
ANISOU 3105  CA  MET A 488    16613  17108  14002     53     75  -2042       C  
ATOM   3106  C   MET A 488     -49.245 -31.316  -0.086  1.00127.15           C  
ANISOU 3106  C   MET A 488    16626  17467  14219    104    321  -2222       C  
ATOM   3107  O   MET A 488     -48.949 -30.106  -0.092  1.00126.81           O  
ANISOU 3107  O   MET A 488    16434  17532  14215     -3    462  -2138       O  
ATOM   3108  CB  MET A 488     -50.596 -32.539   1.632  1.00127.28           C  
ANISOU 3108  CB  MET A 488    16772  17195  14393    209   -100  -2064       C  
ATOM   3109  CG  MET A 488     -51.955 -32.829   2.232  1.00125.77           C  
ANISOU 3109  CG  MET A 488    16702  16870  14214    141   -315  -1845       C  
ATOM   3110  SD  MET A 488     -52.885 -31.302   2.409  1.00123.90           S  
ANISOU 3110  SD  MET A 488    16396  16707  13975    -43   -272  -1576       S  
ATOM   3111  CE  MET A 488     -51.770 -30.306   3.402  1.00123.34           C  
ANISOU 3111  CE  MET A 488    16060  16736  14067     36   -143  -1658       C  
ATOM   3112  N   ALA A 489     -48.399 -32.284  -0.430  1.00129.16           N  
ANISOU 3112  N   ALA A 489    16886  17728  14461    266    374  -2466       N  
ATOM   3113  CA  ALA A 489     -47.002 -32.005  -0.716  1.00131.04           C  
ANISOU 3113  CA  ALA A 489    16908  18131  14751    346    611  -2654       C  
ATOM   3114  C   ALA A 489     -46.833 -31.012  -1.859  1.00132.17           C  
ANISOU 3114  C   ALA A 489    17040  18455  14723    166    857  -2595       C  
ATOM   3115  O   ALA A 489     -46.056 -30.061  -1.753  1.00132.56           O  
ANISOU 3115  O   ALA A 489    16857  18637  14871    107   1029  -2580       O  
ATOM   3116  CB  ALA A 489     -46.280 -33.287  -1.041  1.00133.41           C  
ANISOU 3116  CB  ALA A 489    17246  18398  15046    567    630  -2927       C  
ATOM   3117  N   LEU A 490     -47.582 -31.211  -2.937  1.00132.91           N  
ANISOU 3117  N   LEU A 490    17389  18550  14560     62    856  -2546       N  
ATOM   3118  CA  LEU A 490     -47.440 -30.360  -4.108  1.00134.45           C  
ANISOU 3118  CA  LEU A 490    17612  18927  14547   -107   1083  -2474       C  
ATOM   3119  C   LEU A 490     -48.117 -29.002  -3.936  1.00132.68           C  
ANISOU 3119  C   LEU A 490    17350  18703  14357   -321   1064  -2170       C  
ATOM   3120  O   LEU A 490     -47.655 -27.994  -4.474  1.00133.77           O  
ANISOU 3120  O   LEU A 490    17391  18983  14454   -454   1273  -2084       O  
ATOM   3121  CB  LEU A 490     -47.986 -31.064  -5.342  1.00136.30           C  
ANISOU 3121  CB  LEU A 490    18151  19174  14462   -140   1069  -2537       C  
ATOM   3122  CG  LEU A 490     -47.104 -32.220  -5.815  1.00139.10           C  
ANISOU 3122  CG  LEU A 490    18540  19566  14744     69   1180  -2876       C  
ATOM   3123  CD1 LEU A 490     -47.475 -32.668  -7.220  1.00141.66           C  
ANISOU 3123  CD1 LEU A 490    19166  19962  14697     10   1232  -2962       C  
ATOM   3124  CD2 LEU A 490     -45.633 -31.865  -5.732  1.00140.76           C  
ANISOU 3124  CD2 LEU A 490    18440  19959  15084    169   1467  -3026       C  
ATOM   3125  N   GLY A 491     -49.217 -28.966  -3.197  1.00130.22           N  
ANISOU 3125  N   GLY A 491    17116  18230  14133   -352    821  -2000       N  
ATOM   3126  CA  GLY A 491     -49.851 -27.691  -2.927  1.00128.72           C  
ANISOU 3126  CA  GLY A 491    16875  18018  14014   -514    799  -1734       C  
ATOM   3127  C   GLY A 491     -48.930 -26.799  -2.123  1.00128.36           C  
ANISOU 3127  C   GLY A 491    16553  18010  14207   -506    919  -1758       C  
ATOM   3128  O   GLY A 491     -48.636 -25.664  -2.509  1.00129.11           O  
ANISOU 3128  O   GLY A 491    16561  18178  14315   -652   1075  -1643       O  
ATOM   3129  N   TYR A 492     -48.442 -27.336  -1.013  1.00127.53           N  
ANISOU 3129  N   TYR A 492    16312  17850  14292   -343    833  -1907       N  
ATOM   3130  CA  TYR A 492     -47.563 -26.587  -0.125  1.00127.35           C  
ANISOU 3130  CA  TYR A 492    16024  17858  14503   -328    896  -1956       C  
ATOM   3131  C   TYR A 492     -46.224 -26.242  -0.790  1.00129.87           C  
ANISOU 3131  C   TYR A 492    16155  18352  14837   -361   1159  -2084       C  
ATOM   3132  O   TYR A 492     -45.633 -25.175  -0.547  1.00130.33           O  
ANISOU 3132  O   TYR A 492    16017  18456  15047   -469   1265  -2042       O  
ATOM   3133  CB  TYR A 492     -47.346 -27.387   1.156  1.00127.32           C  
ANISOU 3133  CB  TYR A 492    15942  17775  14659   -134    719  -2086       C  
ATOM   3134  CG  TYR A 492     -46.347 -26.785   2.106  1.00127.54           C  
ANISOU 3134  CG  TYR A 492    15697  17848  14913    -99    746  -2178       C  
ATOM   3135  CD1 TYR A 492     -46.675 -25.698   2.898  1.00126.29           C  
ANISOU 3135  CD1 TYR A 492    15473  17633  14879   -193    689  -2060       C  
ATOM   3136  CD2 TYR A 492     -45.074 -27.321   2.219  1.00129.29           C  
ANISOU 3136  CD2 TYR A 492    15723  18166  15235     37    815  -2396       C  
ATOM   3137  CE1 TYR A 492     -45.756 -25.155   3.770  1.00126.80           C  
ANISOU 3137  CE1 TYR A 492    15302  17734  15144   -175    686  -2165       C  
ATOM   3138  CE2 TYR A 492     -44.152 -26.791   3.085  1.00129.78           C  
ANISOU 3138  CE2 TYR A 492    15522  18279  15511     58    809  -2481       C  
ATOM   3139  CZ  TYR A 492     -44.493 -25.710   3.860  1.00128.54           C  
ANISOU 3139  CZ  TYR A 492    15320  18061  15458    -58    736  -2369       C  
ATOM   3140  OH  TYR A 492     -43.557 -25.187   4.725  1.00129.34           O  
ANISOU 3140  OH  TYR A 492    15168  18209  15767    -49    704  -2475       O  
ATOM   3141  N   GLY A 493     -45.753 -27.146  -1.640  1.00131.80           N  
ANISOU 3141  N   GLY A 493    16456  18692  14928   -272   1270  -2245       N  
ATOM   3142  CA  GLY A 493     -44.560 -26.877  -2.414  1.00134.63           C  
ANISOU 3142  CA  GLY A 493    16641  19249  15263   -303   1557  -2356       C  
ATOM   3143  C   GLY A 493     -44.794 -25.695  -3.333  1.00135.52           C  
ANISOU 3143  C   GLY A 493    16802  19443  15245   -555   1727  -2136       C  
ATOM   3144  O   GLY A 493     -43.947 -24.814  -3.458  1.00137.03           O  
ANISOU 3144  O   GLY A 493    16775  19745  15547   -671   1922  -2107       O  
ATOM   3145  N   ALA A 494     -45.976 -25.650  -3.936  1.00134.71           N  
ANISOU 3145  N   ALA A 494    16981  19275  14929   -651   1632  -1960       N  
ATOM   3146  CA  ALA A 494     -46.351 -24.523  -4.778  1.00135.56           C  
ANISOU 3146  CA  ALA A 494    17166  19433  14910   -885   1746  -1706       C  
ATOM   3147  C   ALA A 494     -46.373 -23.239  -3.955  1.00134.32           C  
ANISOU 3147  C   ALA A 494    16843  19169  15023  -1005   1710  -1541       C  
ATOM   3148  O   ALA A 494     -46.082 -22.162  -4.469  1.00135.81           O  
ANISOU 3148  O   ALA A 494    16970  19411  15223  -1192   1872  -1380       O  
ATOM   3149  CB  ALA A 494     -47.698 -24.766  -5.433  1.00134.89           C  
ANISOU 3149  CB  ALA A 494    17399  19279  14573   -944   1586  -1543       C  
ATOM   3150  N   THR A 495     -46.746 -23.351  -2.683  1.00131.85           N  
ANISOU 3150  N   THR A 495    16478  18698  14920   -901   1494  -1576       N  
ATOM   3151  CA  THR A 495     -46.665 -22.203  -1.777  1.00130.96           C  
ANISOU 3151  CA  THR A 495    16207  18479  15072   -983   1453  -1486       C  
ATOM   3152  C   THR A 495     -45.237 -21.703  -1.601  1.00132.89           C  
ANISOU 3152  C   THR A 495    16157  18829  15507  -1032   1635  -1609       C  
ATOM   3153  O   THR A 495     -44.987 -20.496  -1.670  1.00133.85           O  
ANISOU 3153  O   THR A 495    16181  18920  15757  -1215   1726  -1476       O  
ATOM   3154  CB  THR A 495     -47.236 -22.531  -0.382  1.00133.23           C  
ANISOU 3154  CB  THR A 495    16492  18615  15515   -838   1202  -1540       C  
ATOM   3155  OG1 THR A 495     -48.669 -22.564  -0.445  1.00131.59           O  
ANISOU 3155  OG1 THR A 495    16507  18289  15201   -851   1043  -1354       O  
ATOM   3156  CG2 THR A 495     -46.808 -21.476   0.638  1.00132.97           C  
ANISOU 3156  CG2 THR A 495    16265  18502  15756   -889   1179  -1548       C  
ATOM   3157  N   LEU A 496     -44.305 -22.637  -1.398  1.00133.76           N  
ANISOU 3157  N   LEU A 496    16118  19054  15649   -872   1680  -1855       N  
ATOM   3158  CA  LEU A 496     -42.891 -22.308  -1.121  1.00135.79           C  
ANISOU 3158  CA  LEU A 496    16044  19431  16120   -892   1827  -1997       C  
ATOM   3159  C   LEU A 496     -42.184 -21.416  -2.157  1.00138.76           C  
ANISOU 3159  C   LEU A 496    16299  19951  16472  -1115   2123  -1887       C  
ATOM   3160  O   LEU A 496     -41.426 -20.514  -1.791  1.00140.00           O  
ANISOU 3160  O   LEU A 496    16211  20114  16868  -1249   2191  -1872       O  
ATOM   3161  CB  LEU A 496     -42.093 -23.599  -0.965  1.00136.69           C  
ANISOU 3161  CB  LEU A 496    16039  19659  16238   -653   1839  -2265       C  
ATOM   3162  CG  LEU A 496     -42.398 -24.383   0.308  1.00134.46           C  
ANISOU 3162  CG  LEU A 496    15778  19245  16067   -441   1553  -2382       C  
ATOM   3163  CD1 LEU A 496     -41.777 -25.759   0.222  1.00135.64           C  
ANISOU 3163  CD1 LEU A 496    15879  19475  16184   -196   1562  -2613       C  
ATOM   3164  CD2 LEU A 496     -41.901 -23.641   1.534  1.00134.06           C  
ANISOU 3164  CD2 LEU A 496    15496  19144  16299   -473   1436  -2414       C  
ATOM   3165  N   VAL A 497     -42.413 -21.690  -3.437  1.00140.18           N  
ANISOU 3165  N   VAL A 497    16653  20250  16357  -1162   2293  -1812       N  
ATOM   3166  CA  VAL A 497     -41.798 -20.940  -4.530  1.00143.36           C  
ANISOU 3166  CA  VAL A 497    16977  20821  16673  -1374   2597  -1680       C  
ATOM   3167  C   VAL A 497     -42.381 -19.533  -4.681  1.00143.22           C  
ANISOU 3167  C   VAL A 497    17042  20663  16714  -1633   2580  -1368       C  
ATOM   3168  O   VAL A 497     -43.603 -19.361  -4.647  1.00141.14           O  
ANISOU 3168  O   VAL A 497    17036  20234  16359  -1644   2392  -1207       O  
ATOM   3169  CB  VAL A 497     -41.960 -21.693  -5.868  1.00145.15           C  
ANISOU 3169  CB  VAL A 497    17415  21228  16508  -1336   2769  -1696       C  
ATOM   3170  CG1 VAL A 497     -41.501 -20.838  -7.039  1.00148.56           C  
ANISOU 3170  CG1 VAL A 497    17816  21839  16791  -1580   3082  -1500       C  
ATOM   3171  CG2 VAL A 497     -41.198 -22.997  -5.823  1.00146.17           C  
ANISOU 3171  CG2 VAL A 497    17435  21495  16610  -1081   2836  -2022       C  
ATOM   3172  N   PRO A 498     -41.503 -18.519  -4.827  1.00150.10           N  
ANISOU 3172  N   PRO A 498    17679  21586  17766  -1843   2769  -1275       N  
ATOM   3173  CA  PRO A 498     -41.883 -17.118  -5.077  1.00150.83           C  
ANISOU 3173  CA  PRO A 498    17834  21533  17943  -2109   2787   -967       C  
ATOM   3174  C   PRO A 498     -42.600 -16.881  -6.412  1.00152.12           C  
ANISOU 3174  C   PRO A 498    18282  21754  17761  -2238   2897   -692       C  
ATOM   3175  O   PRO A 498     -43.708 -16.339  -6.390  1.00150.61           O  
ANISOU 3175  O   PRO A 498    18314  21363  17547  -2290   2718   -478       O  
ATOM   3176  CB  PRO A 498     -40.542 -16.383  -5.047  1.00149.56           C  
ANISOU 3176  CB  PRO A 498    17321  21468  18036  -2294   3002   -978       C  
ATOM   3177  CG  PRO A 498     -39.697 -17.214  -4.162  1.00149.08           C  
ANISOU 3177  CG  PRO A 498    16994  21496  18153  -2091   2949  -1310       C  
ATOM   3178  CD  PRO A 498     -40.079 -18.633  -4.474  1.00147.81           C  
ANISOU 3178  CD  PRO A 498    17009  21451  17700  -1824   2920  -1478       C  
ATOM   3179  N   THR A 499     -41.987 -17.253  -7.537  1.00156.50           N  
ANISOU 3179  N   THR A 499    18826  22585  18052  -2284   3182   -695       N  
ATOM   3180  CA  THR A 499     -42.611 -17.044  -8.848  1.00158.22           C  
ANISOU 3180  CA  THR A 499    19329  22893  17894  -2413   3287   -434       C  
ATOM   3181  C   THR A 499     -41.971 -17.799 -10.014  1.00161.42           C  
ANISOU 3181  C   THR A 499    19757  23640  17934  -2385   3591   -533       C  
ATOM   3182  O   THR A 499     -40.832 -18.247  -9.926  1.00163.14           O  
ANISOU 3182  O   THR A 499    19703  24047  18235  -2312   3800   -762       O  
ATOM   3183  CB  THR A 499     -42.617 -15.558  -9.228  1.00161.23           C  
ANISOU 3183  CB  THR A 499    19703  23173  18386  -2718   3374    -68       C  
ATOM   3184  OG1 THR A 499     -43.092 -15.427 -10.573  1.00163.51           O  
ANISOU 3184  OG1 THR A 499    20258  23596  18270  -2840   3495    191       O  
ATOM   3185  CG2 THR A 499     -41.214 -14.994  -9.154  1.00164.26           C  
ANISOU 3185  CG2 THR A 499    19725  23673  19015  -2881   3642    -97       C  
ATOM   3186  N   TRP A 500     -42.722 -17.929 -11.107  1.00166.79           N  
ANISOU 3186  N   TRP A 500    20762  24407  18204  -2436   3609   -363       N  
ATOM   3187  CA  TRP A 500     -42.214 -18.532 -12.339  1.00170.38           C  
ANISOU 3187  CA  TRP A 500    21296  25196  18243  -2430   3909   -434       C  
ATOM   3188  C   TRP A 500     -42.139 -17.514 -13.468  1.00174.10           C  
ANISOU 3188  C   TRP A 500    21861  25801  18488  -2722   4140    -61       C  
ATOM   3189  O   TRP A 500     -42.825 -16.497 -13.458  1.00173.54           O  
ANISOU 3189  O   TRP A 500    21904  25530  18504  -2902   3994    275       O  
ATOM   3190  CB  TRP A 500     -43.079 -19.720 -12.777  1.00173.84           C  
ANISOU 3190  CB  TRP A 500    22067  25667  18316  -2234   3742   -594       C  
ATOM   3191  CG  TRP A 500     -42.588 -20.440 -14.033  1.00177.75           C  
ANISOU 3191  CG  TRP A 500    22684  26505  18349  -2194   4039   -728       C  
ATOM   3192  CD1 TRP A 500     -43.339 -20.780 -15.126  1.00179.27           C  
ANISOU 3192  CD1 TRP A 500    23251  26810  18056  -2222   4008   -646       C  
ATOM   3193  CD2 TRP A 500     -41.251 -20.905 -14.312  1.00180.95           C  
ANISOU 3193  CD2 TRP A 500    22834  27189  18728  -2110   4408   -979       C  
ATOM   3194  NE1 TRP A 500     -42.559 -21.420 -16.061  1.00183.22           N  
ANISOU 3194  NE1 TRP A 500    23770  27639  18208  -2159   4342   -846       N  
ATOM   3195  CE2 TRP A 500     -41.277 -21.509 -15.587  1.00184.33           C  
ANISOU 3195  CE2 TRP A 500    23517  27888  18630  -2081   4604  -1050       C  
ATOM   3196  CE3 TRP A 500     -40.042 -20.868 -13.609  1.00181.54           C  
ANISOU 3196  CE3 TRP A 500    22481  27320  19175  -2052   4584  -1155       C  
ATOM   3197  CZ2 TRP A 500     -40.144 -22.075 -16.166  1.00188.26           C  
ANISOU 3197  CZ2 TRP A 500    23856  28708  18965  -1978   4995  -1301       C  
ATOM   3198  CZ3 TRP A 500     -38.921 -21.424 -14.191  1.00185.40           C  
ANISOU 3198  CZ3 TRP A 500    22787  28130  19528  -1957   4958  -1382       C  
ATOM   3199  CH2 TRP A 500     -38.979 -22.020 -15.455  1.00188.73           C  
ANISOU 3199  CH2 TRP A 500    23468  28816  19424  -1912   5175  -1457       C  
ATOM   3200  N   PHE A 501     -41.288 -17.808 -14.441  1.00180.71           N  
ANISOU 3200  N   PHE A 501    22648  26981  19032  -2758   4509   -120       N  
ATOM   3201  CA  PHE A 501     -40.942 -16.860 -15.479  1.00185.00           C  
ANISOU 3201  CA  PHE A 501    23215  27704  19372  -3048   4801    228       C  
ATOM   3202  C   PHE A 501     -40.468 -17.586 -16.735  1.00189.17           C  
ANISOU 3202  C   PHE A 501    23860  28641  19376  -3005   5142    114       C  
ATOM   3203  O   PHE A 501     -40.804 -17.200 -17.852  1.00192.17           O  
ANISOU 3203  O   PHE A 501    24498  29175  19342  -3176   5259    393       O  
ATOM   3204  CB  PHE A 501     -39.862 -15.909 -14.954  1.00185.40           C  
ANISOU 3204  CB  PHE A 501    22852  27728  19864  -3238   4997    325       C  
ATOM   3205  CG  PHE A 501     -38.756 -16.608 -14.201  1.00185.18           C  
ANISOU 3205  CG  PHE A 501    22434  27804  20121  -3052   5117    -70       C  
ATOM   3206  CD1 PHE A 501     -37.631 -17.071 -14.865  1.00189.29           C  
ANISOU 3206  CD1 PHE A 501    22746  28701  20476  -3024   5531   -227       C  
ATOM   3207  CD2 PHE A 501     -38.856 -16.823 -12.832  1.00181.12           C  
ANISOU 3207  CD2 PHE A 501    21764  27024  20029  -2890   4815   -285       C  
ATOM   3208  CE1 PHE A 501     -36.621 -17.722 -14.178  1.00189.36           C  
ANISOU 3208  CE1 PHE A 501    22375  28804  20768  -2832   5625   -582       C  
ATOM   3209  CE2 PHE A 501     -37.853 -17.477 -12.139  1.00181.14           C  
ANISOU 3209  CE2 PHE A 501    21413  27122  20289  -2710   4894   -629       C  
ATOM   3210  CZ  PHE A 501     -36.733 -17.925 -12.812  1.00185.25           C  
ANISOU 3210  CZ  PHE A 501    21708  28004  20674  -2677   5291   -776       C  
ATOM   3211  N   GLY A 502     -39.729 -18.671 -16.525  1.00186.95           N  
ANISOU 3211  N   GLY A 502    23406  28524  19104  -2756   5282   -308       N  
ATOM   3212  CA  GLY A 502     -38.937 -19.313 -17.562  1.00191.57           C  
ANISOU 3212  CA  GLY A 502    23983  29517  19289  -2691   5690   -483       C  
ATOM   3213  C   GLY A 502     -39.560 -19.635 -18.910  1.00194.34           C  
ANISOU 3213  C   GLY A 502    24773  30083  18985  -2722   5765   -397       C  
ATOM   3214  O   GLY A 502     -38.862 -20.108 -19.810  1.00198.73           O  
ANISOU 3214  O   GLY A 502    25329  31003  19177  -2673   6142   -546       O  
ATOM   3215  N   ASN A 503     -40.854 -19.378 -19.071  1.00191.24           N  
ANISOU 3215  N   ASN A 503    24747  29487  18429  -2799   5414   -163       N  
ATOM   3216  CA  ASN A 503     -41.520 -19.742 -20.312  1.00193.85           C  
ANISOU 3216  CA  ASN A 503    25514  30013  18127  -2822   5419    -97       C  
ATOM   3217  C   ASN A 503     -41.819 -18.550 -21.215  1.00196.93           C  
ANISOU 3217  C   ASN A 503    26077  30496  18253  -3153   5512    426       C  
ATOM   3218  O   ASN A 503     -41.052 -18.255 -22.134  1.00201.95           O  
ANISOU 3218  O   ASN A 503    26676  31473  18581  -3294   5929    542       O  
ATOM   3219  CB  ASN A 503     -42.807 -20.502 -20.008  1.00192.75           C  
ANISOU 3219  CB  ASN A 503    25695  29623  17919  -2655   4941   -232       C  
ATOM   3220  CG  ASN A 503     -42.553 -21.958 -19.696  1.00191.79           C  
ANISOU 3220  CG  ASN A 503    25564  29522  17786  -2327   4915   -761       C  
ATOM   3221  OD1 ASN A 503     -42.818 -22.424 -18.587  1.00187.55           O  
ANISOU 3221  OD1 ASN A 503    24916  28705  17641  -2156   4636   -950       O  
ATOM   3222  ND2 ASN A 503     -42.022 -22.686 -20.672  1.00196.05           N  
ANISOU 3222  ND2 ASN A 503    26227  30392  17872  -2231   5215  -1003       N  
ATOM   3223  N   VAL A 504     -42.946 -17.888 -20.977  1.00196.43           N  
ANISOU 3223  N   VAL A 504    26203  30135  18296  -3269   5129    748       N  
ATOM   3224  CA  VAL A 504     -43.330 -16.739 -21.788  1.00199.30           C  
ANISOU 3224  CA  VAL A 504    26750  30534  18440  -3569   5158   1277       C  
ATOM   3225  C   VAL A 504     -42.673 -15.448 -21.298  1.00199.85           C  
ANISOU 3225  C   VAL A 504    26490  30466  18979  -3804   5313   1590       C  
ATOM   3226  O   VAL A 504     -42.584 -14.464 -22.036  1.00203.51           O  
ANISOU 3226  O   VAL A 504    27026  31015  19283  -4080   5473   2025       O  
ATOM   3227  CB  VAL A 504     -44.863 -16.560 -21.807  1.00194.48           C  
ANISOU 3227  CB  VAL A 504    26484  29661  17749  -3581   4667   1509       C  
ATOM   3228  CG1 VAL A 504     -45.349 -16.323 -23.225  1.00198.92           C  
ANISOU 3228  CG1 VAL A 504    27432  30472  17675  -3746   4704   1823       C  
ATOM   3229  CG2 VAL A 504     -45.544 -17.779 -21.207  1.00190.41           C  
ANISOU 3229  CG2 VAL A 504    26067  29001  17279  -3292   4336   1102       C  
ATOM   3230  N   PHE A 505     -42.191 -15.469 -20.059  1.00199.06           N  
ANISOU 3230  N   PHE A 505    26034  30151  19449  -3703   5260   1366       N  
ATOM   3231  CA  PHE A 505     -41.654 -14.271 -19.421  1.00199.13           C  
ANISOU 3231  CA  PHE A 505    25733  29960  19968  -3918   5327   1615       C  
ATOM   3232  C   PHE A 505     -40.208 -14.418 -18.884  1.00200.26           C  
ANISOU 3232  C   PHE A 505    25404  30244  20443  -3895   5656   1349       C  
ATOM   3233  O   PHE A 505     -39.833 -13.729 -17.937  1.00198.77           O  
ANISOU 3233  O   PHE A 505    24920  29812  20790  -3983   5589   1392       O  
ATOM   3234  CB  PHE A 505     -42.613 -13.847 -18.296  1.00199.42           C  
ANISOU 3234  CB  PHE A 505    25791  29525  20454  -3861   4863   1676       C  
ATOM   3235  CG  PHE A 505     -42.340 -12.477 -17.721  1.00199.68           C  
ANISOU 3235  CG  PHE A 505    25610  29281  20978  -4100   4852   1980       C  
ATOM   3236  CD1 PHE A 505     -42.550 -11.335 -18.480  1.00203.05           C  
ANISOU 3236  CD1 PHE A 505    26180  29665  21303  -4391   4916   2484       C  
ATOM   3237  CD2 PHE A 505     -41.937 -12.331 -16.402  1.00196.68           C  
ANISOU 3237  CD2 PHE A 505    24912  28656  21161  -4029   4742   1765       C  
ATOM   3238  CE1 PHE A 505     -42.324 -10.075 -17.947  1.00203.53           C  
ANISOU 3238  CE1 PHE A 505    26066  29426  21843  -4612   4885   2756       C  
ATOM   3239  CE2 PHE A 505     -41.707 -11.075 -15.866  1.00197.18           C  
ANISOU 3239  CE2 PHE A 505    24801  28440  21677  -4250   4708   2015       C  
ATOM   3240  CZ  PHE A 505     -41.902  -9.948 -16.637  1.00200.60           C  
ANISOU 3240  CZ  PHE A 505    25378  28809  22032  -4542   4780   2504       C  
ATOM   3241  N   PRO A 506     -39.384 -15.317 -19.462  1.00199.80           N  
ANISOU 3241  N   PRO A 506    25259  30575  20081  -3769   6003   1059       N  
ATOM   3242  CA  PRO A 506     -38.083 -15.438 -18.794  1.00200.51           C  
ANISOU 3242  CA  PRO A 506    24856  30757  20572  -3724   6252    808       C  
ATOM   3243  C   PRO A 506     -37.162 -14.254 -19.090  1.00204.81           C  
ANISOU 3243  C   PRO A 506    25115  31407  21297  -4075   6591   1157       C  
ATOM   3244  O   PRO A 506     -36.261 -13.957 -18.304  1.00204.82           O  
ANISOU 3244  O   PRO A 506    24684  31352  21786  -4123   6678   1060       O  
ATOM   3245  CB  PRO A 506     -37.506 -16.720 -19.386  1.00198.65           C  
ANISOU 3245  CB  PRO A 506    24615  30903  19960  -3471   6535    409       C  
ATOM   3246  CG  PRO A 506     -38.089 -16.798 -20.756  1.00201.85           C  
ANISOU 3246  CG  PRO A 506    25455  31544  19695  -3552   6644    602       C  
ATOM   3247  CD  PRO A 506     -39.408 -16.064 -20.736  1.00199.26           C  
ANISOU 3247  CD  PRO A 506    25471  30894  19346  -3701   6236    978       C  
ATOM   3248  N   GLN A 507     -37.404 -13.595 -20.222  1.00204.86           N  
ANISOU 3248  N   GLN A 507    25366  31563  20908  -4327   6764   1569       N  
ATOM   3249  CA  GLN A 507     -36.568 -12.496 -20.695  1.00209.78           C  
ANISOU 3249  CA  GLN A 507    25765  32318  21625  -4692   7120   1954       C  
ATOM   3250  C   GLN A 507     -37.204 -11.159 -20.337  1.00208.60           C  
ANISOU 3250  C   GLN A 507    25709  31743  21807  -4965   6836   2407       C  
ATOM   3251  O   GLN A 507     -36.790 -10.112 -20.848  1.00212.80           O  
ANISOU 3251  O   GLN A 507    26169  32309  22376  -5310   7060   2832       O  
ATOM   3252  CB  GLN A 507     -36.371 -12.588 -22.211  1.00208.88           C  
ANISOU 3252  CB  GLN A 507    25869  32659  20838  -4811   7523   2156       C  
ATOM   3253  CG  GLN A 507     -36.062 -13.988 -22.719  1.00210.05           C  
ANISOU 3253  CG  GLN A 507    26074  33197  20538  -4495   7744   1695       C  
ATOM   3254  CD  GLN A 507     -34.704 -14.491 -22.282  1.00211.61           C  
ANISOU 3254  CD  GLN A 507    25751  33620  21030  -4370   8088   1332       C  
ATOM   3255  OE1 GLN A 507     -33.735 -13.735 -22.225  1.00214.85           O  
ANISOU 3255  OE1 GLN A 507    25771  34128  21733  -4617   8388   1527       O  
ATOM   3256  NE2 GLN A 507     -34.629 -15.777 -21.959  1.00209.51           N  
ANISOU 3256  NE2 GLN A 507    25465  33425  20713  -3986   8032    809       N  
ATOM   3257  N   THR A 508     -38.213 -11.216 -19.466  1.00207.94           N  
ANISOU 3257  N   THR A 508    25786  31257  21964  -4804   6351   2314       N  
ATOM   3258  CA  THR A 508     -39.039 -10.062 -19.119  1.00206.45           C  
ANISOU 3258  CA  THR A 508    25751  30633  22058  -4987   6027   2699       C  
ATOM   3259  C   THR A 508     -39.702  -9.518 -20.392  1.00209.95           C  
ANISOU 3259  C   THR A 508    26589  31171  22011  -5185   6072   3182       C  
ATOM   3260  O   THR A 508     -39.421  -8.400 -20.837  1.00213.79           O  
ANISOU 3260  O   THR A 508    27051  31607  22574  -5514   6224   3632       O  
ATOM   3261  CB  THR A 508     -38.218  -8.960 -18.401  1.00210.99           C  
ANISOU 3261  CB  THR A 508    25946  30979  23244  -5249   6099   2848       C  
ATOM   3262  OG1 THR A 508     -37.471  -9.548 -17.328  1.00208.55           O  
ANISOU 3262  OG1 THR A 508    25253  30664  23323  -5068   6090   2390       O  
ATOM   3263  CG2 THR A 508     -39.130  -7.888 -17.827  1.00208.80           C  
ANISOU 3263  CG2 THR A 508    25829  30183  23324  -5361   5710   3140       C  
ATOM   3264  N   GLU A 509     -40.577 -10.336 -20.978  1.00208.94           N  
ANISOU 3264  N   GLU A 509    26830  31180  21379  -4987   5925   3091       N  
ATOM   3265  CA  GLU A 509     -41.272  -9.976 -22.212  1.00212.28           C  
ANISOU 3265  CA  GLU A 509    27659  31732  21268  -5138   5923   3513       C  
ATOM   3266  C   GLU A 509     -42.618  -9.313 -21.940  1.00209.56           C  
ANISOU 3266  C   GLU A 509    27589  30959  21075  -5149   5441   3814       C  
ATOM   3267  O   GLU A 509     -43.119  -9.330 -20.816  1.00204.70           O  
ANISOU 3267  O   GLU A 509    26887  29981  20909  -4989   5107   3630       O  
ATOM   3268  CB  GLU A 509     -41.473 -11.214 -23.090  1.00205.86           C  
ANISOU 3268  CB  GLU A 509    27109  31322  19786  -4935   6020   3250       C  
ATOM   3269  CG  GLU A 509     -40.183 -11.858 -23.572  1.00209.61           C  
ANISOU 3269  CG  GLU A 509    27355  32265  20023  -4911   6541   2980       C  
ATOM   3270  CD  GLU A 509     -39.512 -11.076 -24.690  1.00216.33           C  
ANISOU 3270  CD  GLU A 509    28211  33431  20554  -5243   6977   3415       C  
ATOM   3271  OE1 GLU A 509     -40.098 -10.081 -25.171  1.00218.19           O  
ANISOU 3271  OE1 GLU A 509    28678  33521  20701  -5490   6854   3940       O  
ATOM   3272  OE2 GLU A 509     -38.393 -11.460 -25.090  1.00220.03           O  
ANISOU 3272  OE2 GLU A 509    28444  34296  20862  -5253   7451   3241       O  
ATOM   3273  N   ASN A 510     -43.214  -8.751 -22.984  1.00210.17           N  
ANISOU 3273  N   ASN A 510    27999  31097  20760  -5324   5408   4279       N  
ATOM   3274  CA  ASN A 510     -44.479  -8.047 -22.838  1.00208.42           C  
ANISOU 3274  CA  ASN A 510    28028  30485  20678  -5339   4965   4617       C  
ATOM   3275  C   ASN A 510     -45.352  -8.290 -24.057  1.00210.96           C  
ANISOU 3275  C   ASN A 510    28791  31029  20334  -5346   4848   4870       C  
ATOM   3276  O   ASN A 510     -45.311  -7.534 -25.028  1.00215.88           O  
ANISOU 3276  O   ASN A 510    29590  31766  20670  -5600   4981   5356       O  
ATOM   3277  CB  ASN A 510     -44.239  -6.543 -22.642  1.00212.27           C  
ANISOU 3277  CB  ASN A 510    28398  30643  21614  -5635   4988   5084       C  
ATOM   3278  CG  ASN A 510     -45.499  -5.782 -22.237  1.00210.04           C  
ANISOU 3278  CG  ASN A 510    28305  29879  21621  -5599   4515   5370       C  
ATOM   3279  OD1 ASN A 510     -46.619  -6.259 -22.411  1.00207.97           O  
ANISOU 3279  OD1 ASN A 510    28310  29596  21114  -5410   4193   5350       O  
ATOM   3280  ND2 ASN A 510     -45.311  -4.573 -21.716  1.00210.85           N  
ANISOU 3280  ND2 ASN A 510    28264  29589  22259  -5785   4475   5643       N  
ATOM   3281  N   ARG A 511     -46.131  -9.362 -24.007  1.00206.91           N  
ANISOU 3281  N   ARG A 511    28461  30583  19573  -5076   4589   4545       N  
ATOM   3282  CA  ARG A 511     -47.092  -9.654 -25.057  1.00208.91           C  
ANISOU 3282  CA  ARG A 511    29137  31013  19226  -5064   4388   4743       C  
ATOM   3283  C   ARG A 511     -48.479  -9.606 -24.438  1.00204.62           C  
ANISOU 3283  C   ARG A 511    28716  30086  18942  -4901   3840   4784       C  
ATOM   3284  O   ARG A 511     -48.607  -9.425 -23.228  1.00200.28           O  
ANISOU 3284  O   ARG A 511    27931  29180  18988  -4788   3674   4623       O  
ATOM   3285  CB  ARG A 511     -46.809 -11.013 -25.697  1.00202.18           C  
ANISOU 3285  CB  ARG A 511    28419  30609  17791  -4909   4565   4322       C  
ATOM   3286  CG  ARG A 511     -45.405 -11.144 -26.278  1.00206.61           C  
ANISOU 3286  CG  ARG A 511    28822  31581  18098  -5029   5144   4231       C  
ATOM   3287  CD  ARG A 511     -45.141 -10.059 -27.310  1.00212.64           C  
ANISOU 3287  CD  ARG A 511    29719  32501  18573  -5366   5377   4826       C  
ATOM   3288  NE  ARG A 511     -43.822 -10.184 -27.925  1.00217.41           N  
ANISOU 3288  NE  ARG A 511    30164  33540  18901  -5492   5960   4764       N  
ATOM   3289  CZ  ARG A 511     -42.824  -9.324 -27.742  1.00219.79           C  
ANISOU 3289  CZ  ARG A 511    30145  33819  19545  -5727   6301   4987       C  
ATOM   3290  NH1 ARG A 511     -42.988  -8.265 -26.958  1.00217.83           N  
ANISOU 3290  NH1 ARG A 511    29729  33111  19927  -5863   6101   5271       N  
ATOM   3291  NH2 ARG A 511     -41.660  -9.517 -28.350  1.00224.44           N  
ANISOU 3291  NH2 ARG A 511    30578  34847  19853  -5830   6844   4922       N  
ATOM   3292  N   ASP A 512     -49.513  -9.774 -25.256  1.00207.34           N  
ANISOU 3292  N   ASP A 512    29421  30519  18839  -4889   3561   4995       N  
ATOM   3293  CA  ASP A 512     -50.887  -9.751 -24.759  1.00203.82           C  
ANISOU 3293  CA  ASP A 512    29078  29746  18616  -4736   3040   5060       C  
ATOM   3294  C   ASP A 512     -51.139 -10.850 -23.731  1.00198.25           C  
ANISOU 3294  C   ASP A 512    28224  28943  18160  -4450   2873   4501       C  
ATOM   3295  O   ASP A 512     -51.918 -10.671 -22.794  1.00194.31           O  
ANISOU 3295  O   ASP A 512    27625  28087  18116  -4319   2549   4480       O  
ATOM   3296  CB  ASP A 512     -51.880  -9.888 -25.918  1.00200.93           C  
ANISOU 3296  CB  ASP A 512    29117  29565  17662  -4777   2775   5349       C  
ATOM   3297  CG  ASP A 512     -52.060  -8.595 -26.696  1.00205.64           C  
ANISOU 3297  CG  ASP A 512    29875  30102  18158  -5028   2761   6013       C  
ATOM   3298  OD1 ASP A 512     -51.698  -7.521 -26.173  1.00205.69           O  
ANISOU 3298  OD1 ASP A 512    29682  29806  18666  -5145   2851   6266       O  
ATOM   3299  OD2 ASP A 512     -52.559  -8.657 -27.840  1.00209.58           O  
ANISOU 3299  OD2 ASP A 512    30711  30850  18070  -5114   2648   6284       O  
ATOM   3300  N   LEU A 513     -50.461 -11.981 -23.902  1.00202.05           N  
ANISOU 3300  N   LEU A 513    28687  29738  18346  -4350   3107   4054       N  
ATOM   3301  CA  LEU A 513     -50.582 -13.097 -22.970  1.00197.27           C  
ANISOU 3301  CA  LEU A 513    27948  29052  17955  -4086   2978   3523       C  
ATOM   3302  C   LEU A 513     -49.987 -12.779 -21.604  1.00193.57           C  
ANISOU 3302  C   LEU A 513    27091  28300  18158  -4017   3061   3339       C  
ATOM   3303  O   LEU A 513     -50.612 -13.054 -20.575  1.00189.07           O  
ANISOU 3303  O   LEU A 513    26420  27456  17964  -3839   2775   3156       O  
ATOM   3304  CB  LEU A 513     -49.913 -14.350 -23.541  1.00199.79           C  
ANISOU 3304  CB  LEU A 513    28349  29761  17801  -3990   3230   3095       C  
ATOM   3305  CG  LEU A 513     -49.816 -15.532 -22.570  1.00195.37           C  
ANISOU 3305  CG  LEU A 513    27628  29117  17485  -3721   3152   2537       C  
ATOM   3306  CD1 LEU A 513     -51.196 -16.018 -22.144  1.00191.86           C  
ANISOU 3306  CD1 LEU A 513    27324  28441  17131  -3579   2651   2488       C  
ATOM   3307  CD2 LEU A 513     -49.010 -16.666 -23.186  1.00197.72           C  
ANISOU 3307  CD2 LEU A 513    27995  29787  17343  -3626   3451   2126       C  
ATOM   3308  N   GLU A 514     -48.788 -12.196 -21.618  1.00195.91           N  
ANISOU 3308  N   GLU A 514    27173  28678  18587  -4169   3448   3398       N  
ATOM   3309  CA  GLU A 514     -47.975 -11.963 -20.422  1.00193.28           C  
ANISOU 3309  CA  GLU A 514    26457  28148  18834  -4128   3580   3179       C  
ATOM   3310  C   GLU A 514     -48.758 -11.403 -19.226  1.00189.06           C  
ANISOU 3310  C   GLU A 514    25813  27152  18868  -4041   3226   3233       C  
ATOM   3311  O   GLU A 514     -48.516 -11.797 -18.076  1.00185.31           O  
ANISOU 3311  O   GLU A 514    25104  26528  18778  -3877   3178   2884       O  
ATOM   3312  CB  GLU A 514     -46.810 -11.034 -20.785  1.00201.65           C  
ANISOU 3312  CB  GLU A 514    27339  29311  19969  -4393   3981   3421       C  
ATOM   3313  CG  GLU A 514     -45.779 -10.853 -19.690  1.00199.90           C  
ANISOU 3313  CG  GLU A 514    26704  28959  20291  -4382   4156   3173       C  
ATOM   3314  CD  GLU A 514     -46.000  -9.583 -18.896  1.00198.80           C  
ANISOU 3314  CD  GLU A 514    26436  28381  20718  -4505   3985   3444       C  
ATOM   3315  OE1 GLU A 514     -46.595  -8.636 -19.456  1.00201.09           O  
ANISOU 3315  OE1 GLU A 514    26922  28528  20954  -4675   3876   3912       O  
ATOM   3316  OE2 GLU A 514     -45.593  -9.534 -17.714  1.00195.88           O  
ANISOU 3316  OE2 GLU A 514    25782  27803  20843  -4423   3946   3185       O  
ATOM   3317  N   GLY A 515     -49.705 -10.510 -19.499  1.00189.66           N  
ANISOU 3317  N   GLY A 515    26066  27012  18985  -4134   2978   3663       N  
ATOM   3318  CA  GLY A 515     -50.565  -9.982 -18.456  1.00186.16           C  
ANISOU 3318  CA  GLY A 515    25547  26145  19040  -4027   2643   3721       C  
ATOM   3319  C   GLY A 515     -51.414 -11.031 -17.748  1.00181.67           C  
ANISOU 3319  C   GLY A 515    24993  25515  18516  -3751   2347   3379       C  
ATOM   3320  O   GLY A 515     -51.734 -10.880 -16.565  1.00178.12           O  
ANISOU 3320  O   GLY A 515    24376  24774  18527  -3617   2179   3242       O  
ATOM   3321  N   PHE A 516     -51.770 -12.104 -18.452  1.00182.20           N  
ANISOU 3321  N   PHE A 516    25266  25856  18106  -3673   2287   3233       N  
ATOM   3322  CA  PHE A 516     -52.596 -13.157 -17.853  1.00178.38           C  
ANISOU 3322  CA  PHE A 516    24809  25315  17652  -3438   1999   2929       C  
ATOM   3323  C   PHE A 516     -51.762 -14.412 -17.607  1.00177.12           C  
ANISOU 3323  C   PHE A 516    24554  25369  17375  -3306   2192   2430       C  
ATOM   3324  O   PHE A 516     -52.174 -15.324 -16.882  1.00173.73           O  
ANISOU 3324  O   PHE A 516    24085  24865  17061  -3109   2008   2123       O  
ATOM   3325  CB  PHE A 516     -53.814 -13.466 -18.728  1.00179.73           C  
ANISOU 3325  CB  PHE A 516    25288  25569  17433  -3437   1694   3131       C  
ATOM   3326  CG  PHE A 516     -54.851 -12.371 -18.727  1.00180.20           C  
ANISOU 3326  CG  PHE A 516    25404  25362  17701  -3491   1415   3584       C  
ATOM   3327  CD1 PHE A 516     -54.657 -11.208 -19.462  1.00184.05           C  
ANISOU 3327  CD1 PHE A 516    25977  25833  18122  -3698   1516   4030       C  
ATOM   3328  CD2 PHE A 516     -56.003 -12.490 -17.963  1.00177.04           C  
ANISOU 3328  CD2 PHE A 516    24956  24721  17589  -3328   1061   3571       C  
ATOM   3329  CE1 PHE A 516     -55.601 -10.197 -19.455  1.00184.77           C  
ANISOU 3329  CE1 PHE A 516    26118  25652  18434  -3724   1250   4448       C  
ATOM   3330  CE2 PHE A 516     -56.948 -11.483 -17.950  1.00177.75           C  
ANISOU 3330  CE2 PHE A 516    25074  24564  17898  -3347    815   3974       C  
ATOM   3331  CZ  PHE A 516     -56.745 -10.333 -18.699  1.00181.62           C  
ANISOU 3331  CZ  PHE A 516    25660  25018  18328  -3537    900   4410       C  
ATOM   3332  N   GLU A 517     -50.574 -14.437 -18.204  1.00179.18           N  
ANISOU 3332  N   GLU A 517    24766  25890  17422  -3412   2572   2364       N  
ATOM   3333  CA  GLU A 517     -49.499 -15.287 -17.715  1.00178.15           C  
ANISOU 3333  CA  GLU A 517    24426  25897  17367  -3288   2816   1916       C  
ATOM   3334  C   GLU A 517     -49.336 -14.937 -16.244  1.00174.36           C  
ANISOU 3334  C   GLU A 517    23646  25109  17495  -3198   2732   1791       C  
ATOM   3335  O   GLU A 517     -49.145 -15.813 -15.408  1.00171.46           O  
ANISOU 3335  O   GLU A 517    23145  24708  17292  -3002   2683   1417       O  
ATOM   3336  CB  GLU A 517     -48.197 -15.051 -18.504  1.00181.63           C  
ANISOU 3336  CB  GLU A 517    24787  26641  17584  -3444   3270   1941       C  
ATOM   3337  CG  GLU A 517     -46.879 -15.376 -17.768  1.00180.95           C  
ANISOU 3337  CG  GLU A 517    24345  26618  17789  -3366   3558   1591       C  
ATOM   3338  CD  GLU A 517     -46.603 -16.869 -17.604  1.00179.65           C  
ANISOU 3338  CD  GLU A 517    24174  26611  17473  -3113   3583   1096       C  
ATOM   3339  OE1 GLU A 517     -47.331 -17.693 -18.194  1.00179.81           O  
ANISOU 3339  OE1 GLU A 517    24485  26725  17110  -3020   3423   1004       O  
ATOM   3340  OE2 GLU A 517     -45.646 -17.216 -16.879  1.00178.70           O  
ANISOU 3340  OE2 GLU A 517    23756  26510  17633  -3006   3750    798       O  
ATOM   3341  N   ASN A 518     -49.464 -13.646 -15.938  1.00176.38           N  
ANISOU 3341  N   ASN A 518    23819  25126  18073  -3339   2693   2115       N  
ATOM   3342  CA  ASN A 518     -49.434 -13.176 -14.555  1.00173.16           C  
ANISOU 3342  CA  ASN A 518    23167  24401  18226  -3264   2580   2019       C  
ATOM   3343  C   ASN A 518     -50.591 -13.721 -13.712  1.00169.05           C  
ANISOU 3343  C   ASN A 518    22699  23680  17854  -3045   2217   1885       C  
ATOM   3344  O   ASN A 518     -50.439 -13.935 -12.508  1.00165.99           O  
ANISOU 3344  O   ASN A 518    22116  23138  17814  -2905   2151   1632       O  
ATOM   3345  CB  ASN A 518     -49.442 -11.645 -14.512  1.00176.65           C  
ANISOU 3345  CB  ASN A 518    23561  24599  18959  -3465   2590   2406       C  
ATOM   3346  CG  ASN A 518     -48.126 -11.042 -14.985  1.00180.37           C  
ANISOU 3346  CG  ASN A 518    23881  25215  19435  -3694   2964   2504       C  
ATOM   3347  OD1 ASN A 518     -47.090 -11.710 -14.999  1.00180.95           O  
ANISOU 3347  OD1 ASN A 518    23792  25535  19426  -3668   3221   2217       O  
ATOM   3348  ND2 ASN A 518     -48.163  -9.772 -15.376  1.00183.17           N  
ANISOU 3348  ND2 ASN A 518    24279  25413  19906  -3919   2997   2920       N  
ATOM   3349  N   ALA A 519     -51.747 -13.933 -14.337  1.00168.79           N  
ANISOU 3349  N   ALA A 519    22920  23658  17557  -3026   1981   2068       N  
ATOM   3350  CA  ALA A 519     -52.897 -14.534 -13.650  1.00165.38           C  
ANISOU 3350  CA  ALA A 519    22530  23073  17233  -2835   1646   1962       C  
ATOM   3351  C   ALA A 519     -52.654 -16.011 -13.317  1.00163.37           C  
ANISOU 3351  C   ALA A 519    22255  22963  16855  -2660   1644   1531       C  
ATOM   3352  O   ALA A 519     -52.969 -16.486 -12.212  1.00160.01           O  
ANISOU 3352  O   ALA A 519    21712  22387  16697  -2492   1492   1322       O  
ATOM   3353  CB  ALA A 519     -54.158 -14.383 -14.496  1.00167.89           C  
ANISOU 3353  CB  ALA A 519    23103  23390  17297  -2881   1386   2285       C  
ATOM   3354  N   ILE A 520     -52.098 -16.733 -14.287  1.00163.09           N  
ANISOU 3354  N   ILE A 520    22346  23216  16404  -2694   1818   1405       N  
ATOM   3355  CA  ILE A 520     -51.702 -18.118 -14.062  1.00161.90           C  
ANISOU 3355  CA  ILE A 520    22182  23193  16140  -2526   1854    984       C  
ATOM   3356  C   ILE A 520     -50.690 -18.142 -12.924  1.00160.00           C  
ANISOU 3356  C   ILE A 520    21630  22876  16286  -2430   2013    724       C  
ATOM   3357  O   ILE A 520     -50.717 -19.036 -12.084  1.00157.37           O  
ANISOU 3357  O   ILE A 520    21219  22477  16098  -2247   1906    433       O  
ATOM   3358  CB  ILE A 520     -51.094 -18.764 -15.319  1.00161.15           C  
ANISOU 3358  CB  ILE A 520    22260  23426  15544  -2574   2076    870       C  
ATOM   3359  CG1 ILE A 520     -52.065 -18.676 -16.493  1.00163.54           C  
ANISOU 3359  CG1 ILE A 520    22888  23825  15423  -2688   1903   1141       C  
ATOM   3360  CG2 ILE A 520     -50.699 -20.207 -15.039  1.00160.09           C  
ANISOU 3360  CG2 ILE A 520    22114  23377  15337  -2371   2098    415       C  
ATOM   3361  CD1 ILE A 520     -51.450 -19.069 -17.815  1.00167.84           C  
ANISOU 3361  CD1 ILE A 520    23628  24713  15430  -2767   2152   1080       C  
ATOM   3362  N   GLU A 521     -49.803 -17.146 -12.907  1.00162.99           N  
ANISOU 3362  N   GLU A 521    21834  23261  16834  -2569   2253    848       N  
ATOM   3363  CA  GLU A 521     -48.849 -16.966 -11.816  1.00161.59           C  
ANISOU 3363  CA  GLU A 521    21342  22998  17056  -2514   2375    643       C  
ATOM   3364  C   GLU A 521     -49.595 -16.804 -10.493  1.00157.78           C  
ANISOU 3364  C   GLU A 521    20778  22218  16953  -2391   2092    611       C  
ATOM   3365  O   GLU A 521     -49.156 -17.319  -9.463  1.00155.64           O  
ANISOU 3365  O   GLU A 521    20327  21896  16913  -2243   2071    327       O  
ATOM   3366  CB  GLU A 521     -47.946 -15.743 -12.051  1.00168.13           C  
ANISOU 3366  CB  GLU A 521    22008  23840  18033  -2733   2633    849       C  
ATOM   3367  CG  GLU A 521     -46.983 -15.818 -13.241  1.00172.34           C  
ANISOU 3367  CG  GLU A 521    22551  24699  18231  -2868   2987    877       C  
ATOM   3368  CD  GLU A 521     -45.937 -16.910 -13.111  1.00172.66           C  
ANISOU 3368  CD  GLU A 521    22424  24964  18213  -2715   3194    469       C  
ATOM   3369  OE1 GLU A 521     -45.354 -17.050 -12.015  1.00170.71           O  
ANISOU 3369  OE1 GLU A 521    21910  24619  18333  -2610   3181    238       O  
ATOM   3370  OE2 GLU A 521     -45.679 -17.613 -14.115  1.00175.18           O  
ANISOU 3370  OE2 GLU A 521    22881  25561  18117  -2694   3368    377       O  
ATOM   3371  N   LEU A 522     -50.715 -16.080 -10.525  1.00157.25           N  
ANISOU 3371  N   LEU A 522    20839  21964  16943  -2444   1881    908       N  
ATOM   3372  CA  LEU A 522     -51.523 -15.860  -9.322  1.00154.06           C  
ANISOU 3372  CA  LEU A 522    20367  21292  16878  -2321   1632    898       C  
ATOM   3373  C   LEU A 522     -52.102 -17.151  -8.763  1.00151.32           C  
ANISOU 3373  C   LEU A 522    20061  20956  16477  -2115   1441    651       C  
ATOM   3374  O   LEU A 522     -51.995 -17.413  -7.563  1.00148.87           O  
ANISOU 3374  O   LEU A 522    19598  20534  16431  -1978   1373    449       O  
ATOM   3375  CB  LEU A 522     -52.662 -14.877  -9.597  1.00152.75           C  
ANISOU 3375  CB  LEU A 522    20330  20942  16767  -2397   1451   1274       C  
ATOM   3376  CG  LEU A 522     -52.287 -13.412  -9.771  1.00155.00           C  
ANISOU 3376  CG  LEU A 522    20557  21085  17252  -2578   1569   1547       C  
ATOM   3377  CD1 LEU A 522     -53.521 -12.587 -10.053  1.00155.59           C  
ANISOU 3377  CD1 LEU A 522    20775  20966  17377  -2607   1354   1911       C  
ATOM   3378  CD2 LEU A 522     -51.615 -12.933  -8.506  1.00153.58           C  
ANISOU 3378  CD2 LEU A 522    20133  20726  17495  -2538   1621   1357       C  
ATOM   3379  N   VAL A 523     -52.736 -17.945  -9.621  1.00150.70           N  
ANISOU 3379  N   VAL A 523    20199  21006  16055  -2105   1341    677       N  
ATOM   3380  CA  VAL A 523     -53.315 -19.212  -9.166  1.00148.51           C  
ANISOU 3380  CA  VAL A 523    19978  20721  15729  -1937   1147    461       C  
ATOM   3381  C   VAL A 523     -52.211 -20.148  -8.691  1.00147.95           C  
ANISOU 3381  C   VAL A 523    19779  20745  15689  -1812   1295     87       C  
ATOM   3382  O   VAL A 523     -52.311 -20.762  -7.625  1.00145.49           O  
ANISOU 3382  O   VAL A 523    19372  20333  15575  -1658   1178   -101       O  
ATOM   3383  CB  VAL A 523     -54.132 -19.913 -10.263  1.00149.41           C  
ANISOU 3383  CB  VAL A 523    20359  20953  15458  -1974   1001    537       C  
ATOM   3384  CG1 VAL A 523     -54.513 -21.316  -9.818  1.00147.63           C  
ANISOU 3384  CG1 VAL A 523    20183  20713  15197  -1819    831    274       C  
ATOM   3385  CG2 VAL A 523     -55.384 -19.113 -10.584  1.00149.76           C  
ANISOU 3385  CG2 VAL A 523    20505  20886  15510  -2060    785    907       C  
ATOM   3386  N   LEU A 524     -51.170 -20.253  -9.515  1.00148.93           N  
ANISOU 3386  N   LEU A 524    19901  21075  15610  -1876   1556     -4       N  
ATOM   3387  CA  LEU A 524     -49.993 -21.074  -9.243  1.00149.23           C  
ANISOU 3387  CA  LEU A 524    19796  21233  15670  -1756   1736   -347       C  
ATOM   3388  C   LEU A 524     -49.405 -20.778  -7.868  1.00147.17           C  
ANISOU 3388  C   LEU A 524    19256  20841  15822  -1671   1740   -474       C  
ATOM   3389  O   LEU A 524     -49.049 -21.691  -7.122  1.00145.80           O  
ANISOU 3389  O   LEU A 524    18990  20653  15754  -1496   1692   -744       O  
ATOM   3390  CB  LEU A 524     -48.928 -20.838 -10.319  1.00150.30           C  
ANISOU 3390  CB  LEU A 524    19913  21616  15577  -1870   2068   -354       C  
ATOM   3391  CG  LEU A 524     -47.701 -21.749 -10.299  1.00151.50           C  
ANISOU 3391  CG  LEU A 524    19923  21940  15699  -1733   2287   -710       C  
ATOM   3392  CD1 LEU A 524     -48.071 -23.132 -10.820  1.00151.91           C  
ANISOU 3392  CD1 LEU A 524    20206  22064  15448  -1589   2194   -932       C  
ATOM   3393  CD2 LEU A 524     -46.526 -21.146 -11.075  1.00155.11           C  
ANISOU 3393  CD2 LEU A 524    20246  22628  16060  -1870   2660   -668       C  
ATOM   3394  N   GLU A 525     -49.309 -19.495  -7.542  1.00146.06           N  
ANISOU 3394  N   GLU A 525    18993  20592  15910  -1799   1782   -276       N  
ATOM   3395  CA  GLU A 525     -48.756 -19.076  -6.266  1.00144.55           C  
ANISOU 3395  CA  GLU A 525    18552  20274  16097  -1745   1772   -393       C  
ATOM   3396  C   GLU A 525     -49.633 -19.554  -5.119  1.00141.31           C  
ANISOU 3396  C   GLU A 525    18162  19689  15839  -1577   1500   -469       C  
ATOM   3397  O   GLU A 525     -49.128 -19.988  -4.084  1.00139.96           O  
ANISOU 3397  O   GLU A 525    17835  19488  15856  -1443   1463   -693       O  
ATOM   3398  CB  GLU A 525     -48.596 -17.558  -6.237  1.00147.01           C  
ANISOU 3398  CB  GLU A 525    18774  20470  16615  -1934   1849   -155       C  
ATOM   3399  CG  GLU A 525     -47.634 -17.060  -5.183  1.00146.76           C  
ANISOU 3399  CG  GLU A 525    18463  20363  16935  -1933   1907   -309       C  
ATOM   3400  CD  GLU A 525     -47.163 -15.653  -5.461  1.00149.07           C  
ANISOU 3400  CD  GLU A 525    18663  20581  17395  -2165   2048    -98       C  
ATOM   3401  OE1 GLU A 525     -47.453 -15.131  -6.561  1.00151.13           O  
ANISOU 3401  OE1 GLU A 525    19070  20880  17471  -2324   2137    175       O  
ATOM   3402  OE2 GLU A 525     -46.520 -15.062  -4.569  1.00149.04           O  
ANISOU 3402  OE2 GLU A 525    18449  20468  17709  -2195   2051   -195       O  
ATOM   3403  N   THR A 526     -50.946 -19.477  -5.319  1.00142.14           N  
ANISOU 3403  N   THR A 526    18454  19695  15858  -1587   1310   -268       N  
ATOM   3404  CA  THR A 526     -51.920 -19.981  -4.352  1.00139.44           C  
ANISOU 3404  CA  THR A 526    18141  19215  15625  -1441   1066   -302       C  
ATOM   3405  C   THR A 526     -51.709 -21.457  -4.029  1.00138.48           C  
ANISOU 3405  C   THR A 526    18035  19161  15418  -1278   1004   -568       C  
ATOM   3406  O   THR A 526     -51.664 -22.295  -4.932  1.00139.68           O  
ANISOU 3406  O   THR A 526    18329  19435  15310  -1276   1030   -636       O  
ATOM   3407  CB  THR A 526     -53.355 -19.796  -4.869  1.00139.45           C  
ANISOU 3407  CB  THR A 526    18329  19145  15509  -1490    884    -33       C  
ATOM   3408  OG1 THR A 526     -53.649 -18.398  -4.968  1.00140.24           O  
ANISOU 3408  OG1 THR A 526    18405  19128  15751  -1604    905    223       O  
ATOM   3409  CG2 THR A 526     -54.347 -20.456  -3.937  1.00137.04           C  
ANISOU 3409  CG2 THR A 526    18035  18733  15300  -1348    656    -68       C  
ATOM   3410  N   GLY A 527     -51.596 -21.773  -2.742  1.00133.14           N  
ANISOU 3410  N   GLY A 527    17233  18399  14955  -1138    912   -718       N  
ATOM   3411  CA  GLY A 527     -51.337 -23.138  -2.327  1.00132.42           C  
ANISOU 3411  CA  GLY A 527    17148  18342  14824   -976    842   -952       C  
ATOM   3412  C   GLY A 527     -52.523 -24.074  -2.485  1.00131.52           C  
ANISOU 3412  C   GLY A 527    17229  18173  14570   -931    634   -892       C  
ATOM   3413  O   GLY A 527     -52.400 -25.156  -3.062  1.00132.38           O  
ANISOU 3413  O   GLY A 527    17457  18341  14500   -883    617  -1025       O  
ATOM   3414  N   PHE A 528     -53.677 -23.671  -1.959  1.00127.40           N  
ANISOU 3414  N   PHE A 528    16732  17533  14141   -945    475   -700       N  
ATOM   3415  CA  PHE A 528     -54.827 -24.568  -1.917  1.00126.58           C  
ANISOU 3415  CA  PHE A 528    16765  17372  13959   -910    262   -634       C  
ATOM   3416  C   PHE A 528     -55.425 -24.853  -3.290  1.00128.15           C  
ANISOU 3416  C   PHE A 528    17166  17630  13894  -1025    207   -524       C  
ATOM   3417  O   PHE A 528     -55.937 -25.935  -3.517  1.00128.28           O  
ANISOU 3417  O   PHE A 528    17314  17630  13796  -1002     59   -575       O  
ATOM   3418  CB  PHE A 528     -55.915 -24.007  -0.994  1.00124.44           C  
ANISOU 3418  CB  PHE A 528    16432  16985  13866   -890    130   -447       C  
ATOM   3419  CG  PHE A 528     -56.572 -22.744  -1.502  1.00125.04           C  
ANISOU 3419  CG  PHE A 528    16516  17029  13967  -1005    143   -190       C  
ATOM   3420  CD1 PHE A 528     -57.631 -22.795  -2.397  1.00125.85           C  
ANISOU 3420  CD1 PHE A 528    16751  17137  13928  -1096     16     20       C  
ATOM   3421  CD2 PHE A 528     -56.147 -21.503  -1.055  1.00125.06           C  
ANISOU 3421  CD2 PHE A 528    16392  16975  14149  -1019    260   -155       C  
ATOM   3422  CE1 PHE A 528     -58.226 -21.636  -2.857  1.00126.67           C  
ANISOU 3422  CE1 PHE A 528    16858  17201  14070  -1184     10    274       C  
ATOM   3423  CE2 PHE A 528     -56.750 -20.342  -1.501  1.00125.88           C  
ANISOU 3423  CE2 PHE A 528    16511  17013  14305  -1110    261     89       C  
ATOM   3424  CZ  PHE A 528     -57.789 -20.409  -2.403  1.00126.68           C  
ANISOU 3424  CZ  PHE A 528    16740  17127  14266  -1184    137    313       C  
ATOM   3425  N   ALA A 529     -55.357 -23.894  -4.204  1.00126.15           N  
ANISOU 3425  N   ALA A 529    16949  17440  13541  -1158    313   -370       N  
ATOM   3426  CA  ALA A 529     -55.851 -24.108  -5.558  1.00128.06           C  
ANISOU 3426  CA  ALA A 529    17399  17768  13491  -1275    260   -263       C  
ATOM   3427  C   ALA A 529     -55.077 -25.253  -6.198  1.00129.53           C  
ANISOU 3427  C   ALA A 529    17699  18063  13452  -1230    335   -534       C  
ATOM   3428  O   ALA A 529     -55.655 -26.143  -6.831  1.00130.44           O  
ANISOU 3428  O   ALA A 529    18006  18191  13364  -1249    187   -569       O  
ATOM   3429  CB  ALA A 529     -55.722 -22.839  -6.377  1.00132.06           C  
ANISOU 3429  CB  ALA A 529    17919  18334  13926  -1420    388    -45       C  
ATOM   3430  N   VAL A 530     -53.758 -25.207  -6.026  1.00130.52           N  
ANISOU 3430  N   VAL A 530    17698  18264  13631  -1167    564   -733       N  
ATOM   3431  CA  VAL A 530     -52.859 -26.257  -6.491  1.00132.10           C  
ANISOU 3431  CA  VAL A 530    17956  18564  13671  -1077    675  -1025       C  
ATOM   3432  C   VAL A 530     -53.183 -27.585  -5.809  1.00130.91           C  
ANISOU 3432  C   VAL A 530    17857  18288  13595   -929    478  -1201       C  
ATOM   3433  O   VAL A 530     -53.328 -28.621  -6.477  1.00132.34           O  
ANISOU 3433  O   VAL A 530    18232  18479  13574   -902    405  -1344       O  
ATOM   3434  CB  VAL A 530     -51.379 -25.891  -6.230  1.00132.33           C  
ANISOU 3434  CB  VAL A 530    17765  18692  13822  -1021    949  -1190       C  
ATOM   3435  CG1 VAL A 530     -50.474 -27.057  -6.576  1.00134.03           C  
ANISOU 3435  CG1 VAL A 530    18008  18998  13919   -880   1058  -1511       C  
ATOM   3436  CG2 VAL A 530     -50.995 -24.656  -7.022  1.00134.10           C  
ANISOU 3436  CG2 VAL A 530    17952  19041  13959  -1194   1161  -1009       C  
ATOM   3437  N   THR A 531     -53.301 -27.538  -4.481  1.00129.31           N  
ANISOU 3437  N   THR A 531    17494  17962  13675   -839    389  -1186       N  
ATOM   3438  CA  THR A 531     -53.651 -28.710  -3.685  1.00128.19           C  
ANISOU 3438  CA  THR A 531    17387  17686  13633   -711    196  -1296       C  
ATOM   3439  C   THR A 531     -54.858 -29.414  -4.272  1.00128.66           C  
ANISOU 3439  C   THR A 531    17673  17677  13536   -791    -30  -1205       C  
ATOM   3440  O   THR A 531     -54.834 -30.614  -4.542  1.00129.72           O  
ANISOU 3440  O   THR A 531    17953  17756  13580   -729   -124  -1381       O  
ATOM   3441  CB  THR A 531     -53.994 -28.329  -2.227  1.00125.95           C  
ANISOU 3441  CB  THR A 531    16933  17296  13625   -653    105  -1191       C  
ATOM   3442  OG1 THR A 531     -52.871 -27.713  -1.595  1.00125.67           O  
ANISOU 3442  OG1 THR A 531    16687  17314  13749   -585    275  -1296       O  
ATOM   3443  CG2 THR A 531     -54.415 -29.554  -1.438  1.00125.13           C  
ANISOU 3443  CG2 THR A 531    16879  17061  13603   -542    -93  -1259       C  
ATOM   3444  N   ALA A 532     -55.902 -28.626  -4.493  1.00129.30           N  
ANISOU 3444  N   ALA A 532    17777  17754  13598   -929   -125   -928       N  
ATOM   3445  CA  ALA A 532     -57.173 -29.112  -4.996  1.00129.82           C  
ANISOU 3445  CA  ALA A 532    18013  17764  13548  -1031   -369   -789       C  
ATOM   3446  C   ALA A 532     -57.068 -29.655  -6.406  1.00132.52           C  
ANISOU 3446  C   ALA A 532    18595  18193  13563  -1106   -377   -903       C  
ATOM   3447  O   ALA A 532     -57.647 -30.693  -6.700  1.00133.43           O  
ANISOU 3447  O   ALA A 532    18879  18230  13587  -1127   -579   -973       O  
ATOM   3448  CB  ALA A 532     -58.217 -28.004  -4.943  1.00126.99           C  
ANISOU 3448  CB  ALA A 532    17585  17402  13263  -1144   -448   -460       C  
ATOM   3449  N   PHE A 533     -56.328 -28.971  -7.274  1.00131.74           N  
ANISOU 3449  N   PHE A 533    18520  18255  13280  -1153   -159   -924       N  
ATOM   3450  CA  PHE A 533     -56.189 -29.450  -8.645  1.00134.72           C  
ANISOU 3450  CA  PHE A 533    19142  18749  13296  -1218   -140  -1043       C  
ATOM   3451  C   PHE A 533     -55.530 -30.820  -8.656  1.00135.82           C  
ANISOU 3451  C   PHE A 533    19382  18839  13385  -1073   -128  -1402       C  
ATOM   3452  O   PHE A 533     -55.969 -31.733  -9.368  1.00137.71           O  
ANISOU 3452  O   PHE A 533    19863  19046  13416  -1105   -288  -1520       O  
ATOM   3453  CB  PHE A 533     -55.390 -28.485  -9.507  1.00136.51           C  
ANISOU 3453  CB  PHE A 533    19359  19178  13330  -1288    138   -999       C  
ATOM   3454  CG  PHE A 533     -55.103 -29.020 -10.880  1.00139.95           C  
ANISOU 3454  CG  PHE A 533    20050  19769  13355  -1332    204  -1158       C  
ATOM   3455  CD1 PHE A 533     -56.073 -28.975 -11.868  1.00141.71           C  
ANISOU 3455  CD1 PHE A 533    20506  20045  13293  -1488     11   -997       C  
ATOM   3456  CD2 PHE A 533     -53.874 -29.587 -11.182  1.00141.73           C  
ANISOU 3456  CD2 PHE A 533    20283  20099  13471  -1207    452  -1478       C  
ATOM   3457  CE1 PHE A 533     -55.821 -29.474 -13.136  1.00145.22           C  
ANISOU 3457  CE1 PHE A 533    21214  20646  13316  -1529     65  -1161       C  
ATOM   3458  CE2 PHE A 533     -53.615 -30.089 -12.451  1.00145.27           C  
ANISOU 3458  CE2 PHE A 533    20980  20704  13513  -1232    534  -1650       C  
ATOM   3459  CZ  PHE A 533     -54.591 -30.031 -13.427  1.00147.02           C  
ANISOU 3459  CZ  PHE A 533    21461  20980  13420  -1397    339  -1497       C  
ATOM   3460  N   VAL A 534     -54.451 -30.944  -7.889  1.00136.20           N  
ANISOU 3460  N   VAL A 534    19245  18875  13628   -910     53  -1582       N  
ATOM   3461  CA  VAL A 534     -53.767 -32.226  -7.758  1.00137.28           C  
ANISOU 3461  CA  VAL A 534    19443  18937  13780   -732     63  -1917       C  
ATOM   3462  C   VAL A 534     -54.732 -33.285  -7.218  1.00136.46           C  
ANISOU 3462  C   VAL A 534    19455  18600  13791   -718   -261  -1914       C  
ATOM   3463  O   VAL A 534     -54.816 -34.395  -7.750  1.00138.48           O  
ANISOU 3463  O   VAL A 534    19930  18771  13914   -682   -373  -2122       O  
ATOM   3464  CB  VAL A 534     -52.538 -32.127  -6.819  1.00135.07           C  
ANISOU 3464  CB  VAL A 534    18898  18668  13755   -553    262  -2062       C  
ATOM   3465  CG1 VAL A 534     -51.857 -33.483  -6.671  1.00136.47           C  
ANISOU 3465  CG1 VAL A 534    19131  18746  13974   -343    250  -2395       C  
ATOM   3466  CG2 VAL A 534     -51.562 -31.092  -7.338  1.00136.20           C  
ANISOU 3466  CG2 VAL A 534    18898  19035  13815   -591    583  -2056       C  
ATOM   3467  N   ALA A 535     -55.492 -32.909  -6.190  1.00135.86           N  
ANISOU 3467  N   ALA A 535    19239  18423  13960   -759   -406  -1672       N  
ATOM   3468  CA  ALA A 535     -56.422 -33.821  -5.531  1.00135.06           C  
ANISOU 3468  CA  ALA A 535    19199  18112  14004   -764   -691  -1616       C  
ATOM   3469  C   ALA A 535     -57.467 -34.371  -6.491  1.00136.91           C  
ANISOU 3469  C   ALA A 535    19686  18299  14033   -923   -929  -1573       C  
ATOM   3470  O   ALA A 535     -57.629 -35.584  -6.609  1.00138.33           O  
ANISOU 3470  O   ALA A 535    20038  18321  14199   -896  -1097  -1742       O  
ATOM   3471  CB  ALA A 535     -57.100 -33.122  -4.367  1.00129.87           C  
ANISOU 3471  CB  ALA A 535    18334  17412  13599   -794   -758  -1335       C  
ATOM   3472  N   MET A 536     -58.164 -33.473  -7.178  1.00136.16           N  
ANISOU 3472  N   MET A 536    19616  18329  13788  -1092   -960  -1346       N  
ATOM   3473  CA  MET A 536     -59.213 -33.852  -8.116  1.00138.11           C  
ANISOU 3473  CA  MET A 536    20084  18559  13830  -1265  -1214  -1272       C  
ATOM   3474  C   MET A 536     -58.670 -34.643  -9.293  1.00141.40           C  
ANISOU 3474  C   MET A 536    20782  19017  13926  -1251  -1189  -1584       C  
ATOM   3475  O   MET A 536     -59.277 -35.632  -9.712  1.00143.23           O  
ANISOU 3475  O   MET A 536    21229  19123  14070  -1320  -1441  -1684       O  
ATOM   3476  CB  MET A 536     -59.943 -32.617  -8.633  1.00141.29           C  
ANISOU 3476  CB  MET A 536    20441  19109  14136  -1425  -1237   -954       C  
ATOM   3477  CG  MET A 536     -60.672 -31.832  -7.573  1.00138.59           C  
ANISOU 3477  CG  MET A 536    19842  18718  14096  -1440  -1286   -647       C  
ATOM   3478  SD  MET A 536     -61.532 -30.434  -8.299  1.00139.11           S  
ANISOU 3478  SD  MET A 536    19873  18926  14057  -1603  -1334   -282       S  
ATOM   3479  CE  MET A 536     -62.867 -31.266  -9.164  1.00141.55           C  
ANISOU 3479  CE  MET A 536    20391  19195  14196  -1788  -1731   -201       C  
ATOM   3480  N   LEU A 537     -57.536 -34.199  -9.834  1.00140.72           N  
ANISOU 3480  N   LEU A 537    20695  19109  13665  -1167   -883  -1740       N  
ATOM   3481  CA  LEU A 537     -56.944 -34.875 -10.985  1.00144.24           C  
ANISOU 3481  CA  LEU A 537    21400  19632  13771  -1131   -804  -2054       C  
ATOM   3482  C   LEU A 537     -56.570 -36.315 -10.625  1.00145.18           C  
ANISOU 3482  C   LEU A 537    21624  19532  14006   -968   -888  -2387       C  
ATOM   3483  O   LEU A 537     -56.863 -37.256 -11.378  1.00147.99           O  
ANISOU 3483  O   LEU A 537    22265  19804  14162   -999  -1056  -2593       O  
ATOM   3484  CB  LEU A 537     -55.731 -34.103 -11.501  1.00144.68           C  
ANISOU 3484  CB  LEU A 537    21379  19936  13658  -1062   -415  -2141       C  
ATOM   3485  CG  LEU A 537     -55.026 -34.741 -12.695  1.00148.69           C  
ANISOU 3485  CG  LEU A 537    22137  20569  13788  -1001   -268  -2480       C  
ATOM   3486  CD1 LEU A 537     -56.027 -35.048 -13.800  1.00151.30           C  
ANISOU 3486  CD1 LEU A 537    22796  20925  13765  -1183   -528  -2452       C  
ATOM   3487  CD2 LEU A 537     -53.937 -33.810 -13.210  1.00149.81           C  
ANISOU 3487  CD2 LEU A 537    22164  20994  13765   -975    133  -2484       C  
ATOM   3488  N   LEU A 538     -55.926 -36.477  -9.472  1.00144.19           N  
ANISOU 3488  N   LEU A 538    21278  19302  14206   -793   -788  -2436       N  
ATOM   3489  CA  LEU A 538     -55.562 -37.803  -8.984  1.00145.01           C  
ANISOU 3489  CA  LEU A 538    21455  19168  14474   -620   -880  -2707       C  
ATOM   3490  C   LEU A 538     -56.784 -38.672  -8.716  1.00145.06           C  
ANISOU 3490  C   LEU A 538    21611  18915  14592   -743  -1266  -2614       C  
ATOM   3491  O   LEU A 538     -56.861 -39.802  -9.188  1.00147.72           O  
ANISOU 3491  O   LEU A 538    22199  19079  14848   -717  -1421  -2861       O  
ATOM   3492  CB  LEU A 538     -54.736 -37.690  -7.706  1.00141.29           C  
ANISOU 3492  CB  LEU A 538    20696  18649  14337   -428   -736  -2708       C  
ATOM   3493  CG  LEU A 538     -53.303 -37.191  -7.882  1.00141.96           C  
ANISOU 3493  CG  LEU A 538    20621  18940  14379   -264   -368  -2889       C  
ATOM   3494  CD1 LEU A 538     -52.613 -37.096  -6.536  1.00139.72           C  
ANISOU 3494  CD1 LEU A 538    20047  18596  14443    -96   -297  -2866       C  
ATOM   3495  CD2 LEU A 538     -52.532 -38.109  -8.824  1.00145.77           C  
ANISOU 3495  CD2 LEU A 538    21304  19429  14651   -115   -256  -3286       C  
ATOM   3496  N   ASN A 539     -57.744 -38.127  -7.973  1.00143.17           N  
ANISOU 3496  N   ASN A 539    21211  18646  14540   -879  -1415  -2261       N  
ATOM   3497  CA  ASN A 539     -58.971 -38.844  -7.634  1.00143.20           C  
ANISOU 3497  CA  ASN A 539    21295  18430  14683  -1024  -1767  -2113       C  
ATOM   3498  C   ASN A 539     -59.728 -39.291  -8.885  1.00146.29           C  
ANISOU 3498  C   ASN A 539    21982  18807  14794  -1209  -1997  -2184       C  
ATOM   3499  O   ASN A 539     -60.392 -40.327  -8.889  1.00147.84           O  
ANISOU 3499  O   ASN A 539    22340  18770  15061  -1294  -2287  -2236       O  
ATOM   3500  CB  ASN A 539     -59.873 -37.971  -6.758  1.00141.97           C  
ANISOU 3500  CB  ASN A 539    20888  18319  14735  -1139  -1831  -1708       C  
ATOM   3501  CG  ASN A 539     -61.069 -38.726  -6.225  1.00142.02           C  
ANISOU 3501  CG  ASN A 539    20913  18110  14936  -1276  -2157  -1532       C  
ATOM   3502  OD1 ASN A 539     -60.929 -39.805  -5.645  1.00142.56           O  
ANISOU 3502  OD1 ASN A 539    21042  17949  15177  -1202  -2263  -1648       O  
ATOM   3503  ND2 ASN A 539     -62.258 -38.166  -6.419  1.00141.72           N  
ANISOU 3503  ND2 ASN A 539    20814  18145  14888  -1480  -2320  -1236       N  
ATOM   3504  N   ALA A 540     -59.612 -38.500  -9.946  1.00145.04           N  
ANISOU 3504  N   ALA A 540    21900  18897  14311  -1282  -1876  -2180       N  
ATOM   3505  CA  ALA A 540     -60.196 -38.841 -11.234  1.00148.40           C  
ANISOU 3505  CA  ALA A 540    22627  19359  14399  -1446  -2075  -2273       C  
ATOM   3506  C   ALA A 540     -59.452 -39.986 -11.912  1.00151.86           C  
ANISOU 3506  C   ALA A 540    23360  19691  14649  -1318  -2051  -2732       C  
ATOM   3507  O   ALA A 540     -60.046 -41.016 -12.233  1.00154.24           O  
ANISOU 3507  O   ALA A 540    23900  19781  14925  -1406  -2349  -2872       O  
ATOM   3508  CB  ALA A 540     -60.211 -37.622 -12.139  1.00148.86           C  
ANISOU 3508  CB  ALA A 540    22686  19730  14146  -1547  -1934  -2113       C  
ATOM   3509  N   ILE A 541     -58.149 -39.811 -12.119  1.00152.41           N  
ANISOU 3509  N   ILE A 541    23404  19899  14606  -1108  -1695  -2972       N  
ATOM   3510  CA  ILE A 541     -57.391 -40.757 -12.941  1.00156.28           C  
ANISOU 3510  CA  ILE A 541    24174  20345  14859   -965  -1617  -3429       C  
ATOM   3511  C   ILE A 541     -56.907 -41.992 -12.180  1.00156.67           C  
ANISOU 3511  C   ILE A 541    24245  20069  15214   -755  -1674  -3690       C  
ATOM   3512  O   ILE A 541     -56.509 -42.980 -12.799  1.00160.25           O  
ANISOU 3512  O   ILE A 541    24966  20395  15526   -642  -1697  -4078       O  
ATOM   3513  CB  ILE A 541     -56.165 -40.086 -13.588  1.00157.51           C  
ANISOU 3513  CB  ILE A 541    24285  20814  14747   -821  -1184  -3590       C  
ATOM   3514  CG1 ILE A 541     -55.146 -39.691 -12.515  1.00154.67           C  
ANISOU 3514  CG1 ILE A 541    23575  20478  14715   -611   -896  -3558       C  
ATOM   3515  CG2 ILE A 541     -56.589 -38.883 -14.424  1.00157.70           C  
ANISOU 3515  CG2 ILE A 541    24323  21151  14444  -1029  -1124  -3323       C  
ATOM   3516  CD1 ILE A 541     -53.866 -39.106 -13.071  1.00156.09           C  
ANISOU 3516  CD1 ILE A 541    23664  20952  14689   -470   -462  -3722       C  
ATOM   3517  N   MET A 542     -56.920 -41.940 -10.851  1.00154.30           N  
ANISOU 3517  N   MET A 542    23675  19630  15321   -692  -1695  -3486       N  
ATOM   3518  CA  MET A 542     -56.535 -43.112 -10.072  1.00154.79           C  
ANISOU 3518  CA  MET A 542    23761  19366  15688   -504  -1786  -3678       C  
ATOM   3519  C   MET A 542     -57.675 -44.119 -10.035  1.00156.21           C  
ANISOU 3519  C   MET A 542    24160  19222  15972   -681  -2209  -3643       C  
ATOM   3520  O   MET A 542     -58.826 -43.749  -9.792  1.00154.62           O  
ANISOU 3520  O   MET A 542    23889  19021  15838   -927  -2429  -3302       O  
ATOM   3521  CB  MET A 542     -56.131 -42.733  -8.644  1.00153.41           C  
ANISOU 3521  CB  MET A 542    23237  19169  15882   -377  -1673  -3465       C  
ATOM   3522  CG  MET A 542     -54.820 -41.988  -8.560  1.00152.59           C  
ANISOU 3522  CG  MET A 542    22911  19318  15750   -170  -1278  -3565       C  
ATOM   3523  SD  MET A 542     -53.509 -42.949  -9.336  1.00156.92           S  
ANISOU 3523  SD  MET A 542    23639  19823  16160    127  -1078  -4107       S  
ATOM   3524  CE  MET A 542     -53.505 -44.405  -8.290  1.00157.45           C  
ANISOU 3524  CE  MET A 542    23763  19429  16632    300  -1343  -4214       C  
ATOM   3525  N   PRO A 543     -57.349 -45.404 -10.243  1.00158.48           N  
ANISOU 3525  N   PRO A 543    24697  19216  16304   -550  -2324  -3995       N  
ATOM   3526  CA  PRO A 543     -58.359 -46.467 -10.239  1.00160.46           C  
ANISOU 3526  CA  PRO A 543    25179  19111  16679   -726  -2740  -3996       C  
ATOM   3527  C   PRO A 543     -58.934 -46.700  -8.843  1.00157.73           C  
ANISOU 3527  C   PRO A 543    24622  18543  16766   -788  -2918  -3652       C  
ATOM   3528  O   PRO A 543     -58.255 -46.455  -7.843  1.00155.24           O  
ANISOU 3528  O   PRO A 543    24056  18251  16675   -597  -2726  -3557       O  
ATOM   3529  CB  PRO A 543     -57.582 -47.691 -10.735  1.00164.68           C  
ANISOU 3529  CB  PRO A 543    26009  19385  17176   -501  -2742  -4495       C  
ATOM   3530  CG  PRO A 543     -56.158 -47.402 -10.375  1.00163.75           C  
ANISOU 3530  CG  PRO A 543    25689  19413  17116   -158  -2346  -4655       C  
ATOM   3531  CD  PRO A 543     -56.002 -45.919 -10.555  1.00160.91           C  
ANISOU 3531  CD  PRO A 543    25083  19506  16551   -229  -2066  -4423       C  
ATOM   3532  N   ALA A 544     -60.187 -47.143  -8.791  1.00159.04           N  
ANISOU 3532  N   ALA A 544    24880  18517  17033  -1065  -3280  -3457       N  
ATOM   3533  CA  ALA A 544     -60.878 -47.390  -7.528  1.00156.98           C  
ANISOU 3533  CA  ALA A 544    24428  18062  17155  -1165  -3455  -3100       C  
ATOM   3534  C   ALA A 544     -60.334 -48.630  -6.819  1.00158.52           C  
ANISOU 3534  C   ALA A 544    24721  17861  17649   -977  -3537  -3264       C  
ATOM   3535  O   ALA A 544     -60.394 -49.738  -7.354  1.00162.32           O  
ANISOU 3535  O   ALA A 544    25513  18026  18137   -989  -3752  -3542       O  
ATOM   3536  CB  ALA A 544     -62.372 -47.534  -7.769  1.00158.94           C  
ANISOU 3536  CB  ALA A 544    24731  18231  17427  -1530  -3816  -2848       C  
ATOM   3537  N   GLU A 545     -59.809 -48.434  -5.613  1.00157.99           N  
ANISOU 3537  N   GLU A 545    24399  17802  17826   -803  -3379  -3091       N  
ATOM   3538  CA  GLU A 545     -59.229 -49.528  -4.838  1.00159.36           C  
ANISOU 3538  CA  GLU A 545    24636  17618  18294   -599  -3449  -3198       C  
ATOM   3539  C   GLU A 545     -60.299 -50.421  -4.210  1.00160.49           C  
ANISOU 3539  C   GLU A 545    24853  17406  18721   -829  -3807  -2941       C  
ATOM   3540  O   GLU A 545     -60.201 -51.651  -4.255  1.00163.83           O  
ANISOU 3540  O   GLU A 545    25521  17420  19306   -783  -4014  -3129       O  
ATOM   3541  CB  GLU A 545     -58.303 -48.974  -3.749  1.00153.66           C  
ANISOU 3541  CB  GLU A 545    23614  17055  17716   -344  -3179  -3082       C  
ATOM   3542  CG  GLU A 545     -57.540 -50.045  -2.970  1.00155.28           C  
ANISOU 3542  CG  GLU A 545    23871  16921  18208    -85  -3236  -3200       C  
ATOM   3543  CD  GLU A 545     -56.585 -49.458  -1.943  1.00152.57           C  
ANISOU 3543  CD  GLU A 545    23225  16766  17978    166  -2990  -3100       C  
ATOM   3544  OE1 GLU A 545     -56.140 -48.304  -2.129  1.00150.22           O  
ANISOU 3544  OE1 GLU A 545    22725  16850  17500    213  -2716  -3103       O  
ATOM   3545  OE2 GLU A 545     -56.288 -50.148  -0.944  1.00153.02           O  
ANISOU 3545  OE2 GLU A 545    23251  16583  18305    305  -3086  -3008       O  
TER    3546      GLU A 545                                                      
ATOM   3547  N   PRO B  66     -53.909 -66.446  -4.591  1.00222.01           N  
ANISOU 3547  N   PRO B  66    26204  15475  42677  -1429  -4505  -2935       N  
ATOM   3548  CA  PRO B  66     -53.501 -67.522  -3.681  1.00226.27           C  
ANISOU 3548  CA  PRO B  66    26617  15342  44012  -1633  -4688  -2392       C  
ATOM   3549  C   PRO B  66     -52.643 -67.017  -2.519  1.00221.68           C  
ANISOU 3549  C   PRO B  66    25904  15137  43187  -1576  -4283  -1680       C  
ATOM   3550  O   PRO B  66     -51.463 -66.719  -2.706  1.00219.25           O  
ANISOU 3550  O   PRO B  66    25761  14932  42610  -1110  -4024  -1884       O  
ATOM   3551  CB  PRO B  66     -52.702 -68.459  -4.590  1.00231.44           C  
ANISOU 3551  CB  PRO B  66    27582  15241  45115  -1211  -4946  -3086       C  
ATOM   3552  CG  PRO B  66     -52.187 -67.578  -5.676  1.00227.56           C  
ANISOU 3552  CG  PRO B  66    27360  15257  43846   -670  -4658  -3805       C  
ATOM   3553  CD  PRO B  66     -53.256 -66.551  -5.907  1.00223.46           C  
ANISOU 3553  CD  PRO B  66    26755  15462  42689   -883  -4545  -3835       C  
ATOM   3554  N   PHE B  67     -53.236 -66.928  -1.332  1.00220.91           N  
ANISOU 3554  N   PHE B  67    25496  15265  43177  -2045  -4235   -857       N  
ATOM   3555  CA  PHE B  67     -52.537 -66.401  -0.161  1.00216.77           C  
ANISOU 3555  CA  PHE B  67    24833  15160  42368  -2016  -3878   -162       C  
ATOM   3556  C   PHE B  67     -51.595 -67.426   0.475  1.00220.88           C  
ANISOU 3556  C   PHE B  67    25366  15008  43550  -1940  -4020    202       C  
ATOM   3557  O   PHE B  67     -51.996 -68.551   0.781  1.00227.14           O  
ANISOU 3557  O   PHE B  67    26083  15109  45112  -2258  -4388    482       O  
ATOM   3558  CB  PHE B  67     -53.533 -65.897   0.887  1.00214.78           C  
ANISOU 3558  CB  PHE B  67    24250  15462  41895  -2507  -3759    576       C  
ATOM   3559  CG  PHE B  67     -52.877 -65.245   2.073  1.00210.44           C  
ANISOU 3559  CG  PHE B  67    23575  15430  40951  -2456  -3398   1240       C  
ATOM   3560  CD1 PHE B  67     -52.394 -63.951   1.984  1.00203.66           C  
ANISOU 3560  CD1 PHE B  67    22799  15308  39274  -2142  -3000   1069       C  
ATOM   3561  CD2 PHE B  67     -52.727 -65.931   3.267  1.00213.55           C  
ANISOU 3561  CD2 PHE B  67    23784  15558  41796  -2718  -3476   2031       C  
ATOM   3562  CE1 PHE B  67     -51.781 -63.347   3.066  1.00200.04           C  
ANISOU 3562  CE1 PHE B  67    22231  15310  38463  -2093  -2708   1634       C  
ATOM   3563  CE2 PHE B  67     -52.111 -65.337   4.350  1.00209.92           C  
ANISOU 3563  CE2 PHE B  67    23222  15591  40946  -2646  -3175   2610       C  
ATOM   3564  CZ  PHE B  67     -51.642 -64.042   4.251  1.00203.14           C  
ANISOU 3564  CZ  PHE B  67    22438  15466  39281  -2335  -2801   2390       C  
ATOM   3565  N   PHE B  68     -50.345 -67.015   0.676  1.00217.61           N  
ANISOU 3565  N   PHE B  68    25039  14802  42840  -1521  -3733    210       N  
ATOM   3566  CA  PHE B  68     -49.313 -67.859   1.273  1.00221.04           C  
ANISOU 3566  CA  PHE B  68    25482  14686  43816  -1355  -3836    530       C  
ATOM   3567  C   PHE B  68     -49.146 -67.602   2.764  1.00219.12           C  
ANISOU 3567  C   PHE B  68    24998  14795  43463  -1583  -3663   1473       C  
ATOM   3568  O   PHE B  68     -48.916 -66.471   3.184  1.00213.07           O  
ANISOU 3568  O   PHE B  68    24153  14810  41994  -1505  -3292   1654       O  
ATOM   3569  CB  PHE B  68     -47.968 -67.635   0.587  1.00219.44           C  
ANISOU 3569  CB  PHE B  68    25483  14493  43400   -729  -3645    -46       C  
ATOM   3570  CG  PHE B  68     -47.914 -68.121  -0.824  1.00222.84           C  
ANISOU 3570  CG  PHE B  68    26179  14466  44026   -419  -3845   -961       C  
ATOM   3571  CD1 PHE B  68     -48.276 -67.292  -1.868  1.00219.49           C  
ANISOU 3571  CD1 PHE B  68    25895  14516  42984   -269  -3676  -1597       C  
ATOM   3572  CD2 PHE B  68     -47.485 -69.404  -1.109  1.00229.77           C  
ANISOU 3572  CD2 PHE B  68    27181  14436  45684   -247  -4212  -1195       C  
ATOM   3573  CE1 PHE B  68     -48.219 -67.732  -3.172  1.00222.98           C  
ANISOU 3573  CE1 PHE B  68    26596  14578  43546     47  -3861  -2452       C  
ATOM   3574  CE2 PHE B  68     -47.423 -69.852  -2.414  1.00233.31           C  
ANISOU 3574  CE2 PHE B  68    27889  14479  46280     78  -4405  -2084       C  
ATOM   3575  CZ  PHE B  68     -47.792 -69.014  -3.447  1.00229.91           C  
ANISOU 3575  CZ  PHE B  68    27594  14572  45189    225  -4225  -2715       C  
ATOM   3576  N   GLY B  69     -49.218 -68.663   3.557  1.00224.69           N  
ANISOU 3576  N   GLY B  69    25605  14902  44864  -1843  -3945   2065       N  
ATOM   3577  CA  GLY B  69     -49.052 -68.541   4.991  1.00223.91           C  
ANISOU 3577  CA  GLY B  69    25295  15096  44684  -2045  -3816   2989       C  
ATOM   3578  C   GLY B  69     -47.592 -68.335   5.356  1.00221.95           C  
ANISOU 3578  C   GLY B  69    25099  14950  44281  -1574  -3640   3045       C  
ATOM   3579  O   GLY B  69     -46.719 -68.348   4.489  1.00221.57           O  
ANISOU 3579  O   GLY B  69    25230  14717  44241  -1105  -3611   2383       O  
ATOM   3580  N   LEU B  70     -47.336 -68.110   6.641  1.00220.86           N  
ANISOU 3580  N   LEU B  70    24788  15161  43969  -1690  -3515   3830       N  
ATOM   3581  CA  LEU B  70     -45.986 -67.853   7.143  1.00219.08           C  
ANISOU 3581  CA  LEU B  70    24558  15112  43570  -1282  -3363   3965       C  
ATOM   3582  C   LEU B  70     -44.979 -68.945   6.817  1.00224.45           C  
ANISOU 3582  C   LEU B  70    25371  14961  44950   -914  -3634   3742       C  
ATOM   3583  O   LEU B  70     -43.966 -68.692   6.161  1.00222.81           O  
ANISOU 3583  O   LEU B  70    25257  14789  44614   -427  -3509   3170       O  
ATOM   3584  CB  LEU B  70     -46.003 -67.666   8.656  1.00218.74           C  
ANISOU 3584  CB  LEU B  70    24313  15467  43331  -1512  -3286   4910       C  
ATOM   3585  CG  LEU B  70     -47.093 -66.814   9.290  1.00215.21           C  
ANISOU 3585  CG  LEU B  70    23695  15777  42299  -1923  -3072   5333       C  
ATOM   3586  CD1 LEU B  70     -46.743 -66.598  10.753  1.00215.00           C  
ANISOU 3586  CD1 LEU B  70    23507  16169  42013  -1984  -2977   6173       C  
ATOM   3587  CD2 LEU B  70     -47.260 -65.496   8.547  1.00208.29           C  
ANISOU 3587  CD2 LEU B  70    22868  15599  40675  -1778  -2751   4713       C  
ATOM   3588  N   ASN B  71     -45.263 -70.154   7.295  1.00231.25           N  
ANISOU 3588  N   ASN B  71    26229  15079  46556  -1146  -3999   4216       N  
ATOM   3589  CA  ASN B  71     -44.327 -71.265   7.183  1.00237.19           C  
ANISOU 3589  CA  ASN B  71    27103  14992  48029   -801  -4299   4128       C  
ATOM   3590  C   ASN B  71     -44.742 -72.259   6.110  1.00242.77           C  
ANISOU 3590  C   ASN B  71    28010  14817  49415   -801  -4653   3535       C  
ATOM   3591  O   ASN B  71     -45.460 -73.228   6.368  1.00248.77           O  
ANISOU 3591  O   ASN B  71    28785  14912  50824  -1181  -5002   3903       O  
ATOM   3592  CB  ASN B  71     -44.198 -71.986   8.522  1.00241.79           C  
ANISOU 3592  CB  ASN B  71    27580  15275  49015   -999  -4499   5109       C  
ATOM   3593  CG  ASN B  71     -43.275 -73.180   8.450  1.00248.57           C  
ANISOU 3593  CG  ASN B  71    28572  15212  50662   -636  -4851   5061       C  
ATOM   3594  OD1 ASN B  71     -42.277 -73.166   7.730  1.00248.14           O  
ANISOU 3594  OD1 ASN B  71    28609  15037  50635    -90  -4815   4405       O  
ATOM   3595  ND2 ASN B  71     -43.609 -74.228   9.191  1.00255.31           N  
ANISOU 3595  ND2 ASN B  71    29432  15404  52169   -930  -5189   5766       N  
ATOM   3596  N   GLU B  72     -44.262 -72.000   4.902  1.00241.08           N  
ANISOU 3596  N   GLU B  72    27950  14612  49036   -368  -4562   2612       N  
ATOM   3597  CA  GLU B  72     -44.444 -72.878   3.764  1.00246.35           C  
ANISOU 3597  CA  GLU B  72    28843  14487  50272   -226  -4888   1890       C  
ATOM   3598  C   GLU B  72     -43.348 -72.577   2.750  1.00244.72           C  
ANISOU 3598  C   GLU B  72    28771  14392  49818    445  -4704   1029       C  
ATOM   3599  O   GLU B  72     -43.027 -71.410   2.523  1.00238.09           O  
ANISOU 3599  O   GLU B  72    27872  14383  48210    616  -4283    800       O  
ATOM   3600  CB  GLU B  72     -45.822 -72.660   3.146  1.00245.55           C  
ANISOU 3600  CB  GLU B  72    28768  14490  50040   -661  -4949   1617       C  
ATOM   3601  CG  GLU B  72     -46.068 -73.436   1.873  1.00250.65           C  
ANISOU 3601  CG  GLU B  72    29660  14408  51169   -506  -5288    766       C  
ATOM   3602  CD  GLU B  72     -47.388 -73.064   1.235  1.00249.26           C  
ANISOU 3602  CD  GLU B  72    29482  14468  50758   -900  -5328    454       C  
ATOM   3603  OE1 GLU B  72     -48.145 -72.280   1.850  1.00244.78           O  
ANISOU 3603  OE1 GLU B  72    28704  14582  49720  -1314  -5104    959       O  
ATOM   3604  OE2 GLU B  72     -47.669 -73.555   0.122  1.00252.94           O  
ANISOU 3604  OE2 GLU B  72    30152  14453  51502   -775  -5597   -312       O  
ATOM   3605  N   LYS B  73     -42.767 -73.601   2.137  1.00251.00           N  
ANISOU 3605  N   LYS B  73    29746  14371  51251    832  -5006    551       N  
ATOM   3606  CA  LYS B  73     -41.776 -73.327   1.108  1.00250.01           C  
ANISOU 3606  CA  LYS B  73    29731  14395  50865   1480  -4805   -301       C  
ATOM   3607  C   LYS B  73     -42.460 -72.966  -0.205  1.00248.63           C  
ANISOU 3607  C   LYS B  73    29739  14376  50354   1495  -4753  -1138       C  
ATOM   3608  O   LYS B  73     -43.389 -73.641  -0.654  1.00252.90           O  
ANISOU 3608  O   LYS B  73    30421  14351  51319   1230  -5117  -1361       O  
ATOM   3609  CB  LYS B  73     -40.820 -74.504   0.899  1.00257.42           C  
ANISOU 3609  CB  LYS B  73    30787  14468  52551   1984  -5118   -570       C  
ATOM   3610  CG  LYS B  73     -39.489 -74.078   0.274  1.00255.80           C  
ANISOU 3610  CG  LYS B  73    30562  14630  52001   2688  -4795  -1173       C  
ATOM   3611  CD  LYS B  73     -38.623 -75.270  -0.092  1.00263.76           C  
ANISOU 3611  CD  LYS B  73    31697  14772  53749   3241  -5119  -1571       C  
ATOM   3612  CE  LYS B  73     -37.332 -74.821  -0.758  1.00262.49           C  
ANISOU 3612  CE  LYS B  73    31469  15047  53217   3942  -4759  -2188       C  
ATOM   3613  NZ  LYS B  73     -36.435 -75.968  -1.086  1.00270.53           N  
ANISOU 3613  NZ  LYS B  73    32582  15265  54943   4546  -5059  -2590       N  
ATOM   3614  N   ILE B  74     -41.980 -71.883  -0.806  1.00242.94           N  
ANISOU 3614  N   ILE B  74    29009  14432  48864   1802  -4307  -1582       N  
ATOM   3615  CA  ILE B  74     -42.477 -71.394  -2.084  1.00241.23           C  
ANISOU 3615  CA  ILE B  74    28976  14487  48192   1902  -4194  -2381       C  
ATOM   3616  C   ILE B  74     -41.356 -71.556  -3.107  1.00243.58           C  
ANISOU 3616  C   ILE B  74    29416  14695  48438   2614  -4067  -3191       C  
ATOM   3617  O   ILE B  74     -40.213 -71.817  -2.718  1.00245.12           O  
ANISOU 3617  O   ILE B  74    29503  14785  48845   2984  -3992  -3058       O  
ATOM   3618  CB  ILE B  74     -42.928 -69.919  -1.982  1.00232.86           C  
ANISOU 3618  CB  ILE B  74    27810  14450  46218   1656  -3754  -2209       C  
ATOM   3619  CG1 ILE B  74     -41.766 -69.014  -1.564  1.00227.93           C  
ANISOU 3619  CG1 ILE B  74    27022  14499  45083   1953  -3292  -2010       C  
ATOM   3620  CG2 ILE B  74     -44.053 -69.782  -0.979  1.00231.09           C  
ANISOU 3620  CG2 ILE B  74    27426  14346  46033    992  -3868  -1438       C  
ATOM   3621  CD1 ILE B  74     -42.136 -67.547  -1.489  1.00220.14           C  
ANISOU 3621  CD1 ILE B  74    25962  14464  43218   1747  -2873  -1875       C  
ATOM   3622  N   PRO B  75     -41.676 -71.476  -4.414  1.00244.64           N  
ANISOU 3622  N   PRO B  75    29784  14848  48320   2828  -4070  -4037       N  
ATOM   3623  CA  PRO B  75     -40.602 -71.493  -5.414  1.00246.63           C  
ANISOU 3623  CA  PRO B  75    30154  15166  48388   3527  -3864  -4806       C  
ATOM   3624  C   PRO B  75     -39.532 -70.457  -5.077  1.00241.06           C  
ANISOU 3624  C   PRO B  75    29227  15269  47095   3768  -3308  -4573       C  
ATOM   3625  O   PRO B  75     -39.845 -69.269  -4.979  1.00234.35           O  
ANISOU 3625  O   PRO B  75    28304  15198  45540   3526  -2952  -4368       O  
ATOM   3626  CB  PRO B  75     -41.330 -71.146  -6.713  1.00246.37           C  
ANISOU 3626  CB  PRO B  75    30377  15342  47890   3584  -3845  -5578       C  
ATOM   3627  CG  PRO B  75     -42.688 -71.692  -6.511  1.00248.59           C  
ANISOU 3627  CG  PRO B  75    30726  15134  48594   3024  -4315  -5391       C  
ATOM   3628  CD  PRO B  75     -43.005 -71.485  -5.050  1.00245.17           C  
ANISOU 3628  CD  PRO B  75    30016  14826  48311   2477  -4302  -4350       C  
ATOM   3629  N   VAL B  76     -38.294 -70.903  -4.895  1.00244.15           N  
ANISOU 3629  N   VAL B  76    29505  15465  47798   4237  -3254  -4607       N  
ATOM   3630  CA  VAL B  76     -37.234 -70.026  -4.410  1.00239.66           C  
ANISOU 3630  CA  VAL B  76    28666  15595  46801   4418  -2788  -4300       C  
ATOM   3631  C   VAL B  76     -36.957 -68.831  -5.326  1.00235.06           C  
ANISOU 3631  C   VAL B  76    28112  15854  45346   4622  -2256  -4769       C  
ATOM   3632  O   VAL B  76     -36.435 -67.807  -4.875  1.00229.75           O  
ANISOU 3632  O   VAL B  76    27224  15882  44187   4562  -1852  -4421       O  
ATOM   3633  CB  VAL B  76     -35.943 -70.821  -4.204  1.00244.97           C  
ANISOU 3633  CB  VAL B  76    29201  15867  48011   4952  -2863  -4364       C  
ATOM   3634  CG1 VAL B  76     -36.125 -71.810  -3.063  1.00248.66           C  
ANISOU 3634  CG1 VAL B  76    29605  15610  49267   4707  -3336  -3698       C  
ATOM   3635  CG2 VAL B  76     -35.562 -71.544  -5.485  1.00251.30           C  
ANISOU 3635  CG2 VAL B  76    30220  16255  49007   5545  -2952  -5307       C  
ATOM   3636  N   LEU B  77     -37.343 -68.943  -6.595  1.00237.32           N  
ANISOU 3636  N   LEU B  77    28675  16070  45425   4839  -2272  -5537       N  
ATOM   3637  CA  LEU B  77     -37.324 -67.792  -7.491  1.00233.10           C  
ANISOU 3637  CA  LEU B  77    28224  16320  44021   4953  -1801  -5929       C  
ATOM   3638  C   LEU B  77     -38.301 -66.737  -6.996  1.00226.01           C  
ANISOU 3638  C   LEU B  77    27306  15954  42615   4362  -1681  -5426       C  
ATOM   3639  O   LEU B  77     -37.974 -65.551  -6.939  1.00220.58           O  
ANISOU 3639  O   LEU B  77    26514  16013  41283   4320  -1231  -5255       O  
ATOM   3640  CB  LEU B  77     -37.669 -68.192  -8.927  1.00237.53           C  
ANISOU 3640  CB  LEU B  77    29121  16674  44455   5293  -1906  -6840       C  
ATOM   3641  CG  LEU B  77     -37.751 -67.019  -9.911  1.00233.67           C  
ANISOU 3641  CG  LEU B  77    28766  16987  43030   5403  -1441  -7228       C  
ATOM   3642  CD1 LEU B  77     -36.402 -66.329 -10.042  1.00232.22           C  
ANISOU 3642  CD1 LEU B  77    28372  17408  42453   5792   -874  -7248       C  
ATOM   3643  CD2 LEU B  77     -38.260 -67.462 -11.275  1.00238.38           C  
ANISOU 3643  CD2 LEU B  77    29726  17363  43486   5701  -1620  -8100       C  
ATOM   3644  N   LEU B  78     -39.502 -67.177  -6.638  1.00226.51           N  
ANISOU 3644  N   LEU B  78    27457  15620  42985   3907  -2092  -5191       N  
ATOM   3645  CA  LEU B  78     -40.508 -66.277  -6.090  1.00220.47           C  
ANISOU 3645  CA  LEU B  78    26645  15322  41802   3351  -2021  -4694       C  
ATOM   3646  C   LEU B  78     -40.007 -65.636  -4.801  1.00215.80           C  
ANISOU 3646  C   LEU B  78    25754  15138  41101   3134  -1792  -3903       C  
ATOM   3647  O   LEU B  78     -40.072 -64.419  -4.653  1.00209.88           O  
ANISOU 3647  O   LEU B  78    24946  15101  39697   2983  -1436  -3703       O  
ATOM   3648  CB  LEU B  78     -41.822 -67.019  -5.830  1.00222.96           C  
ANISOU 3648  CB  LEU B  78    27038  15088  42588   2898  -2525  -4531       C  
ATOM   3649  CG  LEU B  78     -42.952 -66.199  -5.199  1.00217.52           C  
ANISOU 3649  CG  LEU B  78    26261  14856  41532   2320  -2486  -3997       C  
ATOM   3650  CD1 LEU B  78     -43.393 -65.071  -6.121  1.00213.31           C  
ANISOU 3650  CD1 LEU B  78    25889  14991  40168   2370  -2190  -4415       C  
ATOM   3651  CD2 LEU B  78     -44.130 -67.080  -4.823  1.00221.08           C  
ANISOU 3651  CD2 LEU B  78    26709  14716  42575   1862  -2988  -3760       C  
ATOM   3652  N   ALA B  79     -39.486 -66.451  -3.886  1.00218.83           N  
ANISOU 3652  N   ALA B  79    25965  15061  42120   3143  -2013  -3474       N  
ATOM   3653  CA  ALA B  79     -38.976 -65.947  -2.614  1.00215.23           C  
ANISOU 3653  CA  ALA B  79    25226  14957  41593   2965  -1854  -2727       C  
ATOM   3654  C   ALA B  79     -37.905 -64.885  -2.832  1.00211.45           C  
ANISOU 3654  C   ALA B  79    24623  15181  40538   3257  -1348  -2858       C  
ATOM   3655  O   ALA B  79     -37.880 -63.864  -2.142  1.00206.06           O  
ANISOU 3655  O   ALA B  79    23794  15092  39408   3012  -1102  -2407       O  
ATOM   3656  CB  ALA B  79     -38.429 -67.089  -1.769  1.00220.27           C  
ANISOU 3656  CB  ALA B  79    25729  14948  43015   3048  -2186  -2343       C  
ATOM   3657  N   PHE B  80     -37.026 -65.128  -3.799  1.00214.71           N  
ANISOU 3657  N   PHE B  80    25088  15526  40967   3781  -1194  -3485       N  
ATOM   3658  CA  PHE B  80     -36.009 -64.145  -4.156  1.00211.95           C  
ANISOU 3658  CA  PHE B  80    24608  15840  40082   4057   -687  -3657       C  
ATOM   3659  C   PHE B  80     -36.621 -62.862  -4.694  1.00206.40           C  
ANISOU 3659  C   PHE B  80    24051  15798  38575   3846   -356  -3776       C  
ATOM   3660  O   PHE B  80     -36.181 -61.776  -4.340  1.00201.88           O  
ANISOU 3660  O   PHE B  80    23329  15834  37544   3749     -7  -3504       O  
ATOM   3661  CB  PHE B  80     -35.033 -64.705  -5.193  1.00217.29           C  
ANISOU 3661  CB  PHE B  80    25314  16335  40912   4679   -569  -4348       C  
ATOM   3662  CG  PHE B  80     -34.122 -63.661  -5.779  1.00214.98           C  
ANISOU 3662  CG  PHE B  80    24909  16761  40012   4937     -6  -4588       C  
ATOM   3663  CD1 PHE B  80     -32.984 -63.261  -5.099  1.00213.95           C  
ANISOU 3663  CD1 PHE B  80    24424  16962  39905   5035    232  -4246       C  
ATOM   3664  CD2 PHE B  80     -34.411 -63.068  -7.001  1.00214.16           C  
ANISOU 3664  CD2 PHE B  80    25047  17011  39313   5064    276  -5132       C  
ATOM   3665  CE1 PHE B  80     -32.146 -62.297  -5.629  1.00212.28           C  
ANISOU 3665  CE1 PHE B  80    24079  17402  39176   5225    752  -4436       C  
ATOM   3666  CE2 PHE B  80     -33.580 -62.104  -7.534  1.00212.49           C  
ANISOU 3666  CE2 PHE B  80    24732  17453  38549   5269    811  -5296       C  
ATOM   3667  CZ  PHE B  80     -32.445 -61.718  -6.848  1.00211.59           C  
ANISOU 3667  CZ  PHE B  80    24243  17647  38505   5332   1055  -4944       C  
ATOM   3668  N   ILE B  81     -37.602 -63.000  -5.583  1.00207.23           N  
ANISOU 3668  N   ILE B  81    24454  15762  38523   3797   -487  -4210       N  
ATOM   3669  CA  ILE B  81     -38.245 -61.850  -6.223  1.00202.73           C  
ANISOU 3669  CA  ILE B  81    24065  15771  37191   3648   -214  -4380       C  
ATOM   3670  C   ILE B  81     -38.979 -60.968  -5.216  1.00196.77           C  
ANISOU 3670  C   ILE B  81    23219  15397  36149   3127   -194  -3728       C  
ATOM   3671  O   ILE B  81     -38.846 -59.746  -5.238  1.00192.11           O  
ANISOU 3671  O   ILE B  81    22619  15426  34949   3049    166  -3618       O  
ATOM   3672  CB  ILE B  81     -39.233 -62.295  -7.315  1.00205.49           C  
ANISOU 3672  CB  ILE B  81    24745  15844  37488   3699   -448  -4967       C  
ATOM   3673  CG1 ILE B  81     -38.471 -62.779  -8.546  1.00210.63           C  
ANISOU 3673  CG1 ILE B  81    25539  16360  38130   4282   -329  -5723       C  
ATOM   3674  CG2 ILE B  81     -40.158 -61.152  -7.698  1.00200.60           C  
ANISOU 3674  CG2 ILE B  81    24297  15773  36147   3443   -278  -4979       C  
ATOM   3675  CD1 ILE B  81     -39.357 -63.423  -9.581  1.00214.64           C  
ANISOU 3675  CD1 ILE B  81    26373  16495  38685   4384   -647  -6352       C  
ATOM   3676  N   LEU B  82     -39.769 -61.589  -4.349  1.00197.36           N  
ANISOU 3676  N   LEU B  82    23232  15094  36660   2775   -580  -3301       N  
ATOM   3677  CA  LEU B  82     -40.448 -60.859  -3.288  1.00192.45           C  
ANISOU 3677  CA  LEU B  82    22493  14828  35802   2309   -574  -2659       C  
ATOM   3678  C   LEU B  82     -39.425 -60.265  -2.328  1.00189.76           C  
ANISOU 3678  C   LEU B  82    21890  14850  35360   2322   -331  -2187       C  
ATOM   3679  O   LEU B  82     -39.621 -59.170  -1.801  1.00184.79           O  
ANISOU 3679  O   LEU B  82    21204  14763  34243   2089   -128  -1856       O  
ATOM   3680  CB  LEU B  82     -41.414 -61.771  -2.528  1.00194.71           C  
ANISOU 3680  CB  LEU B  82    22730  14621  36631   1946  -1023  -2264       C  
ATOM   3681  CG  LEU B  82     -42.659 -62.221  -3.291  1.00196.88           C  
ANISOU 3681  CG  LEU B  82    23216  14599  36990   1795  -1307  -2629       C  
ATOM   3682  CD1 LEU B  82     -43.548 -63.065  -2.400  1.00199.28           C  
ANISOU 3682  CD1 LEU B  82    23407  14453  37858   1374  -1715  -2128       C  
ATOM   3683  CD2 LEU B  82     -43.423 -61.032  -3.848  1.00192.23           C  
ANISOU 3683  CD2 LEU B  82    22769  14617  35652   1675  -1084  -2813       C  
ATOM   3684  N   GLY B  83     -38.327 -60.989  -2.120  1.00193.42           N  
ANISOU 3684  N   GLY B  83    22194  15007  36290   2618   -374  -2188       N  
ATOM   3685  CA  GLY B  83     -37.211 -60.480  -1.345  1.00191.72           C  
ANISOU 3685  CA  GLY B  83    21708  15130  36007   2697   -157  -1836       C  
ATOM   3686  C   GLY B  83     -36.691 -59.196  -1.954  1.00188.06           C  
ANISOU 3686  C   GLY B  83    21261  15312  34881   2808    315  -2084       C  
ATOM   3687  O   GLY B  83     -36.343 -58.253  -1.248  1.00184.27           O  
ANISOU 3687  O   GLY B  83    20625  15304  34085   2647    509  -1715       O  
ATOM   3688  N   LEU B  84     -36.654 -59.167  -3.281  1.00189.61           N  
ANISOU 3688  N   LEU B  84    21662  15520  34862   3083    488  -2714       N  
ATOM   3689  CA  LEU B  84     -36.221 -57.996  -4.021  1.00186.92           C  
ANISOU 3689  CA  LEU B  84    21381  15760  33881   3194    949  -2970       C  
ATOM   3690  C   LEU B  84     -37.210 -56.858  -3.888  1.00181.50           C  
ANISOU 3690  C   LEU B  84    20855  15501  32606   2823   1040  -2766       C  
ATOM   3691  O   LEU B  84     -36.812 -55.715  -3.700  1.00177.96           O  
ANISOU 3691  O   LEU B  84    20343  15557  31717   2734   1351  -2594       O  
ATOM   3692  CB  LEU B  84     -36.025 -58.325  -5.498  1.00190.61           C  
ANISOU 3692  CB  LEU B  84    22058  16131  34234   3598   1095  -3689       C  
ATOM   3693  CG  LEU B  84     -35.566 -57.119  -6.319  1.00188.44           C  
ANISOU 3693  CG  LEU B  84    21858  16466  33274   3713   1602  -3920       C  
ATOM   3694  CD1 LEU B  84     -34.193 -56.653  -5.858  1.00188.26           C  
ANISOU 3694  CD1 LEU B  84    21489  16759  33281   3819   1917  -3696       C  
ATOM   3695  CD2 LEU B  84     -35.574 -57.425  -7.806  1.00192.22           C  
ANISOU 3695  CD2 LEU B  84    22597  16894  33542   4099   1732  -4622       C  
ATOM   3696  N   GLN B  85     -38.497 -57.164  -4.019  1.00181.24           N  
ANISOU 3696  N   GLN B  85    21026  15258  32580   2617    761  -2807       N  
ATOM   3697  CA  GLN B  85     -39.526 -56.139  -3.898  1.00176.53           C  
ANISOU 3697  CA  GLN B  85    20573  15056  31445   2296    814  -2632       C  
ATOM   3698  C   GLN B  85     -39.512 -55.513  -2.510  1.00172.76           C  
ANISOU 3698  C   GLN B  85    19880  14859  30900   1979    816  -1980       C  
ATOM   3699  O   GLN B  85     -39.663 -54.300  -2.379  1.00168.62           O  
ANISOU 3699  O   GLN B  85    19407  14821  29839   1838   1040  -1846       O  
ATOM   3700  CB  GLN B  85     -40.912 -56.701  -4.214  1.00177.66           C  
ANISOU 3700  CB  GLN B  85    20904  14906  31692   2127    472  -2777       C  
ATOM   3701  CG  GLN B  85     -42.023 -55.675  -4.048  1.00173.15           C  
ANISOU 3701  CG  GLN B  85    20447  14755  30589   1819    505  -2591       C  
ATOM   3702  CD  GLN B  85     -43.363 -56.164  -4.552  1.00174.71           C  
ANISOU 3702  CD  GLN B  85    20811  14720  30850   1687    191  -2820       C  
ATOM   3703  OE1 GLN B  85     -43.514 -57.327  -4.917  1.00179.23           O  
ANISOU 3703  OE1 GLN B  85    21412  14767  31919   1772    -95  -3078       O  
ATOM   3704  NE2 GLN B  85     -44.345 -55.271  -4.580  1.00171.30           N  
ANISOU 3704  NE2 GLN B  85    20485  14671  29930   1483    222  -2744       N  
ATOM   3705  N   HIS B  86     -39.333 -56.339  -1.481  1.00174.55           N  
ANISOU 3705  N   HIS B  86    19888  14773  31662   1885    552  -1581       N  
ATOM   3706  CA  HIS B  86     -39.201 -55.833  -0.121  1.00171.73           C  
ANISOU 3706  CA  HIS B  86    19318  14689  31244   1635    538   -968       C  
ATOM   3707  C   HIS B  86     -37.949 -54.978   0.012  1.00170.14           C  
ANISOU 3707  C   HIS B  86    18967  14875  30802   1779    864   -940       C  
ATOM   3708  O   HIS B  86     -37.989 -53.881   0.573  1.00166.27           O  
ANISOU 3708  O   HIS B  86    18447  14838  29890   1590   1009   -678       O  
ATOM   3709  CB  HIS B  86     -39.144 -56.975   0.893  1.00174.88           C  
ANISOU 3709  CB  HIS B  86    19521  14654  32272   1555    191   -544       C  
ATOM   3710  CG  HIS B  86     -40.431 -57.713   1.047  1.00176.36           C  
ANISOU 3710  CG  HIS B  86    19797  14503  32710   1300   -138   -409       C  
ATOM   3711  ND1 HIS B  86     -41.647 -57.077   1.180  1.00173.24           N  
ANISOU 3711  ND1 HIS B  86    19496  14403  31922    994   -148   -278       N  
ATOM   3712  CD2 HIS B  86     -40.695 -59.042   1.118  1.00181.06           C  
ANISOU 3712  CD2 HIS B  86    20378  14477  33941   1290   -480   -366       C  
ATOM   3713  CE1 HIS B  86     -42.601 -57.976   1.312  1.00175.94           C  
ANISOU 3713  CE1 HIS B  86    19851  14355  32644    792   -465   -159       C  
ATOM   3714  NE2 HIS B  86     -42.053 -59.176   1.278  1.00180.73           N  
ANISOU 3714  NE2 HIS B  86    20405  14380  33885    949   -677   -202       N  
ATOM   3715  N   ALA B  87     -36.841 -55.487  -0.517  1.00173.53           N  
ANISOU 3715  N   ALA B  87    19293  15123  31516   2118    971  -1230       N  
ATOM   3716  CA  ALA B  87     -35.578 -54.776  -0.458  1.00172.92           C  
ANISOU 3716  CA  ALA B  87    19018  15397  31287   2259   1281  -1226       C  
ATOM   3717  C   ALA B  87     -35.718 -53.390  -1.060  1.00169.20           C  
ANISOU 3717  C   ALA B  87    18718  15427  30145   2171   1636  -1387       C  
ATOM   3718  O   ALA B  87     -35.430 -52.399  -0.403  1.00166.20           O  
ANISOU 3718  O   ALA B  87    18236  15427  29486   1990   1763  -1096       O  
ATOM   3719  CB  ALA B  87     -34.490 -55.562  -1.171  1.00177.71           C  
ANISOU 3719  CB  ALA B  87    19501  15754  32269   2680   1375  -1608       C  
ATOM   3720  N   LEU B  88     -36.221 -53.321  -2.286  1.00169.66           N  
ANISOU 3720  N   LEU B  88    19058  15465  29939   2292   1763  -1842       N  
ATOM   3721  CA  LEU B  88     -36.385 -52.045  -2.965  1.00166.72           C  
ANISOU 3721  CA  LEU B  88    18892  15531  28923   2237   2093  -1997       C  
ATOM   3722  C   LEU B  88     -37.386 -51.161  -2.254  1.00162.15           C  
ANISOU 3722  C   LEU B  88    18429  15204  27978   1882   1996  -1653       C  
ATOM   3723  O   LEU B  88     -37.220 -49.950  -2.208  1.00159.30           O  
ANISOU 3723  O   LEU B  88    18121  15232  27175   1770   2233  -1558       O  
ATOM   3724  CB  LEU B  88     -36.841 -52.247  -4.407  1.00168.60           C  
ANISOU 3724  CB  LEU B  88    19440  15685  28936   2459   2193  -2544       C  
ATOM   3725  CG  LEU B  88     -35.857 -52.888  -5.371  1.00173.30           C  
ANISOU 3725  CG  LEU B  88    19981  16146  29717   2871   2386  -2992       C  
ATOM   3726  CD1 LEU B  88     -36.490 -53.048  -6.738  1.00175.12           C  
ANISOU 3726  CD1 LEU B  88    20566  16325  29648   3077   2435  -3528       C  
ATOM   3727  CD2 LEU B  88     -34.621 -52.024  -5.456  1.00173.09           C  
ANISOU 3727  CD2 LEU B  88    19763  16522  29483   2944   2814  -2932       C  
ATOM   3728  N   ALA B  89     -38.415 -51.780  -1.685  1.00162.56           N  
ANISOU 3728  N   ALA B  89    18507  15026  28232   1709   1647  -1461       N  
ATOM   3729  CA  ALA B  89     -39.491 -51.047  -1.030  1.00158.79           C  
ANISOU 3729  CA  ALA B  89    18123  14796  27414   1404   1542  -1160       C  
ATOM   3730  C   ALA B  89     -38.961 -50.299   0.177  1.00156.37           C  
ANISOU 3730  C   ALA B  89    17614  14792  27008   1235   1588   -711       C  
ATOM   3731  O   ALA B  89     -39.264 -49.121   0.377  1.00153.06           O  
ANISOU 3731  O   ALA B  89    17302  14741  26111   1092   1713   -608       O  
ATOM   3732  CB  ALA B  89     -40.595 -51.982  -0.614  1.00160.83           C  
ANISOU 3732  CB  ALA B  89    18377  14749  27983   1248   1171  -1009       C  
ATOM   3733  N   MET B  90     -38.178 -51.001   0.988  1.00157.73           N  
ANISOU 3733  N   MET B  90    17501  14791  27637   1269   1457   -456       N  
ATOM   3734  CA  MET B  90     -37.641 -50.437   2.218  1.00156.14           C  
ANISOU 3734  CA  MET B  90    17085  14855  27387   1127   1436    -29       C  
ATOM   3735  C   MET B  90     -36.350 -49.657   1.977  1.00156.06           C  
ANISOU 3735  C   MET B  90    16956  15088  27251   1237   1734   -148       C  
ATOM   3736  O   MET B  90     -35.857 -48.961   2.867  1.00154.65           O  
ANISOU 3736  O   MET B  90    16623  15179  26959   1113   1741    132       O  
ATOM   3737  CB  MET B  90     -37.387 -51.546   3.228  1.00158.79           C  
ANISOU 3737  CB  MET B  90    17168  14908  28257   1122   1134    331       C  
ATOM   3738  CG  MET B  90     -36.274 -52.480   2.841  1.00162.88           C  
ANISOU 3738  CG  MET B  90    17507  15097  29281   1411   1139    146       C  
ATOM   3739  SD  MET B  90     -36.169 -53.763   4.073  1.00166.15           S  
ANISOU 3739  SD  MET B  90    17685  15145  30300   1391    735    629       S  
ATOM   3740  CE  MET B  90     -35.554 -52.809   5.451  1.00163.87           C  
ANISOU 3740  CE  MET B  90    17171  15340  29753   1238    736   1099       C  
ATOM   3741  N   LEU B  91     -35.803 -49.806   0.775  1.00158.04           N  
ANISOU 3741  N   LEU B  91    17265  15250  27533   1471   1973   -569       N  
ATOM   3742  CA  LEU B  91     -34.550 -49.171   0.381  1.00158.87           C  
ANISOU 3742  CA  LEU B  91    17225  15577  27560   1584   2299   -705       C  
ATOM   3743  C   LEU B  91     -34.509 -47.675   0.696  1.00155.49           C  
ANISOU 3743  C   LEU B  91    16865  15563  26651   1354   2472   -552       C  
ATOM   3744  O   LEU B  91     -33.570 -47.198   1.326  1.00155.68           O  
ANISOU 3744  O   LEU B  91    16637  15771  26743   1290   2527   -368       O  
ATOM   3745  CB  LEU B  91     -34.308 -49.391  -1.112  1.00161.23           C  
ANISOU 3745  CB  LEU B  91    17673  15796  27792   1851   2574  -1201       C  
ATOM   3746  CG  LEU B  91     -33.036 -48.760  -1.662  1.00162.76           C  
ANISOU 3746  CG  LEU B  91    17704  16248  27891   1971   2971  -1350       C  
ATOM   3747  CD1 LEU B  91     -31.840 -49.419  -0.997  1.00165.77           C  
ANISOU 3747  CD1 LEU B  91    17646  16540  28800   2102   2896  -1212       C  
ATOM   3748  CD2 LEU B  91     -32.976 -48.913  -3.172  1.00165.15           C  
ANISOU 3748  CD2 LEU B  91    18209  16531  28010   2238   3262  -1831       C  
ATOM   3749  N   ALA B  92     -35.540 -46.952   0.271  1.00152.75           N  
ANISOU 3749  N   ALA B  92    16857  15343  25837   1238   2525   -636       N  
ATOM   3750  CA  ALA B  92     -35.614 -45.508   0.468  1.00149.82           C  
ANISOU 3750  CA  ALA B  92    16619  15312  24995   1043   2672   -527       C  
ATOM   3751  C   ALA B  92     -35.593 -45.171   1.956  1.00148.17           C  
ANISOU 3751  C   ALA B  92    16231  15246  24822    837   2434   -119       C  
ATOM   3752  O   ALA B  92     -34.890 -44.259   2.398  1.00147.58           O  
ANISOU 3752  O   ALA B  92    16052  15393  24627    722   2526     -2       O  
ATOM   3753  CB  ALA B  92     -36.857 -44.943  -0.194  1.00151.47           C  
ANISOU 3753  CB  ALA B  92    17229  15590  24733    998   2702   -680       C  
ATOM   3754  N   GLY B  93     -36.398 -45.895   2.720  1.00148.83           N  
ANISOU 3754  N   GLY B  93    16285  15207  25055    785   2121     97       N  
ATOM   3755  CA  GLY B  93     -36.503 -45.669   4.149  1.00147.66           C  
ANISOU 3755  CA  GLY B  93    15991  15222  24892    619   1883    494       C  
ATOM   3756  C   GLY B  93     -35.250 -45.990   4.946  1.00149.84           C  
ANISOU 3756  C   GLY B  93    15901  15499  25531    655   1802    693       C  
ATOM   3757  O   GLY B  93     -35.013 -45.382   5.987  1.00148.95           O  
ANISOU 3757  O   GLY B  93    15681  15621  25292    525   1683    947       O  
ATOM   3758  N   VAL B  94     -34.471 -46.966   4.480  1.00151.95           N  
ANISOU 3758  N   VAL B  94    15978  15509  26249    855   1838    562       N  
ATOM   3759  CA  VAL B  94     -33.201 -47.346   5.113  1.00154.64           C  
ANISOU 3759  CA  VAL B  94    15939  15839  26980    943   1763    712       C  
ATOM   3760  C   VAL B  94     -32.070 -46.384   4.753  1.00155.05           C  
ANISOU 3760  C   VAL B  94    15850  16132  26932    930   2043    557       C  
ATOM   3761  O   VAL B  94     -31.265 -45.992   5.596  1.00155.71           O  
ANISOU 3761  O   VAL B  94    15673  16397  27093    855   1955    749       O  
ATOM   3762  CB  VAL B  94     -32.788 -48.770   4.709  1.00158.41           C  
ANISOU 3762  CB  VAL B  94    16258  15932  27999   1204   1692    603       C  
ATOM   3763  CG1 VAL B  94     -31.419 -49.102   5.262  1.00161.51           C  
ANISOU 3763  CG1 VAL B  94    16243  16338  28787   1337   1631    722       C  
ATOM   3764  CG2 VAL B  94     -33.804 -49.760   5.215  1.00158.73           C  
ANISOU 3764  CG2 VAL B  94    16393  15697  28222   1170   1375    827       C  
ATOM   3765  N   VAL B  95     -32.012 -46.050   3.470  1.00155.13           N  
ANISOU 3765  N   VAL B  95    16026  16139  26779   1003   2377    212       N  
ATOM   3766  CA  VAL B  95     -30.996 -45.184   2.889  1.00156.12           C  
ANISOU 3766  CA  VAL B  95    16037  16472  26810    983   2713     53       C  
ATOM   3767  C   VAL B  95     -31.087 -43.717   3.317  1.00153.51           C  
ANISOU 3767  C   VAL B  95    15828  16430  26069    699   2759    178       C  
ATOM   3768  O   VAL B  95     -30.073 -43.094   3.622  1.00154.77           O  
ANISOU 3768  O   VAL B  95    15735  16763  26308    598   2839    239       O  
ATOM   3769  CB  VAL B  95     -31.078 -45.255   1.349  1.00157.18           C  
ANISOU 3769  CB  VAL B  95    16377  16536  26806   1151   3065   -331       C  
ATOM   3770  CG1 VAL B  95     -30.533 -43.998   0.710  1.00157.07           C  
ANISOU 3770  CG1 VAL B  95    16419  16786  26473   1026   3437   -430       C  
ATOM   3771  CG2 VAL B  95     -30.366 -46.490   0.843  1.00161.24           C  
ANISOU 3771  CG2 VAL B  95    16648  16833  27783   1470   3113   -527       C  
ATOM   3772  N   THR B  96     -32.300 -43.168   3.350  1.00150.24           N  
ANISOU 3772  N   THR B  96    15789  16056  25239    576   2690    205       N  
ATOM   3773  CA  THR B  96     -32.470 -41.717   3.503  1.00148.06           C  
ANISOU 3773  CA  THR B  96    15713  16005  24540    351   2770    246       C  
ATOM   3774  C   THR B  96     -31.947 -41.110   4.829  1.00147.92           C  
ANISOU 3774  C   THR B  96    15479  16169  24553    170   2541    502       C  
ATOM   3775  O   THR B  96     -31.242 -40.097   4.787  1.00148.48           O  
ANISOU 3775  O   THR B  96    15501  16378  24539     17   2679    478       O  
ATOM   3776  CB  THR B  96     -33.957 -41.311   3.314  1.00144.86           C  
ANISOU 3776  CB  THR B  96    15745  15608  23686    305   2706    214       C  
ATOM   3777  OG1 THR B  96     -34.315 -41.417   1.930  1.00145.14           O  
ANISOU 3777  OG1 THR B  96    16033  15545  23571    436   2967    -71       O  
ATOM   3778  CG2 THR B  96     -34.177 -39.884   3.760  1.00142.85           C  
ANISOU 3778  CG2 THR B  96    15684  15558  23035    100   2690    295       C  
ATOM   3779  N   PRO B  97     -32.276 -41.705   6.000  1.00147.57           N  
ANISOU 3779  N   PRO B  97    15313  16131  24628    180   2187    751       N  
ATOM   3780  CA  PRO B  97     -31.771 -41.095   7.240  1.00147.82           C  
ANISOU 3780  CA  PRO B  97    15160  16367  24635     34   1956    962       C  
ATOM   3781  C   PRO B  97     -30.243 -40.997   7.353  1.00150.97           C  
ANISOU 3781  C   PRO B  97    15149  16826  25386     14   2012    949       C  
ATOM   3782  O   PRO B  97     -29.765 -39.976   7.853  1.00151.14           O  
ANISOU 3782  O   PRO B  97    15116  17023  25287   -171   1959    981       O  
ATOM   3783  CB  PRO B  97     -32.320 -42.014   8.337  1.00147.79           C  
ANISOU 3783  CB  PRO B  97    15069  16349  24733    104   1602   1245       C  
ATOM   3784  CG  PRO B  97     -33.499 -42.601   7.756  1.00146.26           C  
ANISOU 3784  CG  PRO B  97    15139  15995  24438    180   1644   1189       C  
ATOM   3785  CD  PRO B  97     -33.206 -42.805   6.300  1.00147.07           C  
ANISOU 3785  CD  PRO B  97    15307  15913  24660    289   1972    871       C  
ATOM   3786  N   PRO B  98     -29.487 -42.032   6.935  1.00153.77           N  
ANISOU 3786  N   PRO B  98    15205  17038  26184    205   2094    894       N  
ATOM   3787  CA  PRO B  98     -28.052 -41.754   6.941  1.00156.92           C  
ANISOU 3787  CA  PRO B  98    15198  17547  26878    170   2193    855       C  
ATOM   3788  C   PRO B  98     -27.698 -40.521   6.119  1.00156.85           C  
ANISOU 3788  C   PRO B  98    15297  17647  26651    -23   2539    677       C  
ATOM   3789  O   PRO B  98     -26.963 -39.683   6.625  1.00158.02           O  
ANISOU 3789  O   PRO B  98    15256  17956  26829   -223   2483    733       O  
ATOM   3790  CB  PRO B  98     -27.455 -43.023   6.338  1.00159.95           C  
ANISOU 3790  CB  PRO B  98    15312  17749  27714    457   2303    753       C  
ATOM   3791  CG  PRO B  98     -28.386 -44.084   6.783  1.00158.91           C  
ANISOU 3791  CG  PRO B  98    15327  17415  27638    602   2028    897       C  
ATOM   3792  CD  PRO B  98     -29.754 -43.463   6.709  1.00154.91           C  
ANISOU 3792  CD  PRO B  98    15292  16934  26633    451   2025    902       C  
ATOM   3793  N   LEU B  99     -28.249 -40.378   4.920  1.00155.73           N  
ANISOU 3793  N   LEU B  99    15473  17416  26280     21   2861    483       N  
ATOM   3794  CA  LEU B  99     -27.962 -39.200   4.108  1.00155.99           C  
ANISOU 3794  CA  LEU B  99    15650  17540  26078   -165   3201    362       C  
ATOM   3795  C   LEU B  99     -28.311 -37.902   4.843  1.00154.01           C  
ANISOU 3795  C   LEU B  99    15616  17393  25508   -449   3023    473       C  
ATOM   3796  O   LEU B  99     -27.536 -36.934   4.820  1.00155.70           O  
ANISOU 3796  O   LEU B  99    15714  17698  25746   -677   3136    477       O  
ATOM   3797  CB  LEU B  99     -28.714 -39.269   2.779  1.00154.90           C  
ANISOU 3797  CB  LEU B  99    15900  17300  25656    -42   3516    159       C  
ATOM   3798  CG  LEU B  99     -28.407 -40.488   1.913  1.00157.27           C  
ANISOU 3798  CG  LEU B  99    16043  17485  26225    264   3709    -23       C  
ATOM   3799  CD1 LEU B  99     -29.191 -40.454   0.614  1.00156.40           C  
ANISOU 3799  CD1 LEU B  99    16353  17304  25768    383   3987   -248       C  
ATOM   3800  CD2 LEU B  99     -26.925 -40.558   1.642  1.00161.53           C  
ANISOU 3800  CD2 LEU B  99    16103  18144  27128    289   3951    -66       C  
ATOM   3801  N   ILE B 100     -29.455 -37.898   5.521  1.00150.88           N  
ANISOU 3801  N   ILE B 100    15513  16982  24834   -434   2737    562       N  
ATOM   3802  CA  ILE B 100     -29.920 -36.708   6.230  1.00149.09           C  
ANISOU 3802  CA  ILE B 100    15534  16852  24263   -641   2547    628       C  
ATOM   3803  C   ILE B 100     -29.017 -36.357   7.414  1.00151.02           C  
ANISOU 3803  C   ILE B 100    15437  17233  24711   -789   2263    754       C  
ATOM   3804  O   ILE B 100     -28.613 -35.205   7.550  1.00151.83           O  
ANISOU 3804  O   ILE B 100    15584  17385  24722  -1021   2265    723       O  
ATOM   3805  CB  ILE B 100     -31.376 -36.864   6.728  1.00145.75           C  
ANISOU 3805  CB  ILE B 100    15454  16434  23489   -551   2312    692       C  
ATOM   3806  CG1 ILE B 100     -32.353 -36.898   5.552  1.00143.88           C  
ANISOU 3806  CG1 ILE B 100    15606  16084  22980   -448   2558    537       C  
ATOM   3807  CG2 ILE B 100     -31.760 -35.705   7.624  1.00144.53           C  
ANISOU 3807  CG2 ILE B 100    15502  16409  23002   -712   2076    746       C  
ATOM   3808  CD1 ILE B 100     -33.779 -37.098   5.978  1.00141.05           C  
ANISOU 3808  CD1 ILE B 100    15525  15752  22317   -363   2343    594       C  
ATOM   3809  N   ILE B 101     -28.716 -37.329   8.275  1.00152.07           N  
ANISOU 3809  N   ILE B 101    15247  17414  25119   -657   1994    897       N  
ATOM   3810  CA  ILE B 101     -27.800 -37.095   9.396  1.00154.42           C  
ANISOU 3810  CA  ILE B 101    15189  17864  25619   -762   1693   1009       C  
ATOM   3811  C   ILE B 101     -26.397 -36.663   8.932  1.00157.98           C  
ANISOU 3811  C   ILE B 101    15267  18344  26415   -916   1896    917       C  
ATOM   3812  O   ILE B 101     -25.808 -35.727   9.486  1.00159.54           O  
ANISOU 3812  O   ILE B 101    15351  18643  26625  -1148   1747    915       O  
ATOM   3813  CB  ILE B 101     -27.650 -38.340  10.302  1.00155.55           C  
ANISOU 3813  CB  ILE B 101    15035  18043  26024   -554   1385   1206       C  
ATOM   3814  CG1 ILE B 101     -28.938 -38.608  11.070  1.00152.82           C  
ANISOU 3814  CG1 ILE B 101    14994  17739  25331   -470   1128   1366       C  
ATOM   3815  CG2 ILE B 101     -26.557 -38.127  11.322  1.00158.65           C  
ANISOU 3815  CG2 ILE B 101    15022  18608  26651   -636   1088   1296       C  
ATOM   3816  CD1 ILE B 101     -28.917 -39.919  11.828  1.00154.12           C  
ANISOU 3816  CD1 ILE B 101    14923  17893  25744   -267    868   1609       C  
ATOM   3817  N   SER B 102     -25.855 -37.350   7.931  1.00159.70           N  
ANISOU 3817  N   SER B 102    15276  18483  26920   -786   2228    832       N  
ATOM   3818  CA  SER B 102     -24.512 -37.035   7.463  1.00163.61           C  
ANISOU 3818  CA  SER B 102    15354  19052  27760   -914   2462    762       C  
ATOM   3819  C   SER B 102     -24.436 -35.625   6.913  1.00163.73           C  
ANISOU 3819  C   SER B 102    15591  19068  27553  -1233   2696    687       C  
ATOM   3820  O   SER B 102     -23.577 -34.852   7.317  1.00166.36           O  
ANISOU 3820  O   SER B 102    15665  19491  28055  -1492   2613    708       O  
ATOM   3821  CB  SER B 102     -24.055 -38.005   6.376  1.00165.58           C  
ANISOU 3821  CB  SER B 102    15387  19241  28287   -672   2828    653       C  
ATOM   3822  OG  SER B 102     -24.785 -37.801   5.176  1.00163.74           O  
ANISOU 3822  OG  SER B 102    15572  18901  27739   -640   3198    519       O  
ATOM   3823  N   SER B 103     -25.369 -35.273   6.032  1.00161.14           N  
ANISOU 3823  N   SER B 103    15754  18625  26847  -1222   2951    609       N  
ATOM   3824  CA  SER B 103     -25.317 -33.959   5.397  1.00161.64           C  
ANISOU 3824  CA  SER B 103    16070  18649  26697  -1506   3199    566       C  
ATOM   3825  C   SER B 103     -25.427 -32.828   6.422  1.00161.23           C  
ANISOU 3825  C   SER B 103    16156  18604  26500  -1774   2840    616       C  
ATOM   3826  O   SER B 103     -24.823 -31.767   6.256  1.00163.59           O  
ANISOU 3826  O   SER B 103    16424  18877  26857  -2083   2935    613       O  
ATOM   3827  CB  SER B 103     -26.422 -33.821   4.346  1.00158.87           C  
ANISOU 3827  CB  SER B 103    16266  18177  25921  -1397   3473    482       C  
ATOM   3828  OG  SER B 103     -27.682 -33.579   4.945  1.00155.04           O  
ANISOU 3828  OG  SER B 103    16214  17639  25055  -1345   3173    498       O  
ATOM   3829  N   SER B 104     -26.184 -33.070   7.487  1.00158.69           N  
ANISOU 3829  N   SER B 104    15980  18318  25997  -1654   2425    662       N  
ATOM   3830  CA  SER B 104     -26.397 -32.065   8.522  1.00158.37           C  
ANISOU 3830  CA  SER B 104    16108  18305  25760  -1839   2051    669       C  
ATOM   3831  C   SER B 104     -25.297 -32.044   9.569  1.00161.69           C  
ANISOU 3831  C   SER B 104    16038  18865  26532  -1964   1721    714       C  
ATOM   3832  O   SER B 104     -25.401 -31.321  10.558  1.00161.94           O  
ANISOU 3832  O   SER B 104    16167  18945  26416  -2084   1347    696       O  
ATOM   3833  CB  SER B 104     -27.729 -32.301   9.229  1.00155.44           C  
ANISOU 3833  CB  SER B 104    16104  17973  24985  -1634   1765    700       C  
ATOM   3834  OG  SER B 104     -27.661 -33.467  10.027  1.00155.46           O  
ANISOU 3834  OG  SER B 104    15808  18103  25158  -1424   1521    821       O  
ATOM   3835  N   LEU B 105     -24.252 -32.838   9.373  1.00164.54           N  
ANISOU 3835  N   LEU B 105    15871  19303  27346  -1910   1836    753       N  
ATOM   3836  CA  LEU B 105     -23.168 -32.877  10.350  1.00168.11           C  
ANISOU 3836  CA  LEU B 105    15811  19908  28154  -2005   1502    792       C  
ATOM   3837  C   LEU B 105     -21.787 -32.836   9.707  1.00172.63           C  
ANISOU 3837  C   LEU B 105    15851  20526  29215  -2173   1783    767       C  
ATOM   3838  O   LEU B 105     -20.893 -32.160  10.204  1.00176.11           O  
ANISOU 3838  O   LEU B 105    15977  21039  29898  -2443   1597    749       O  
ATOM   3839  CB  LEU B 105     -23.292 -34.128  11.229  1.00167.59           C  
ANISOU 3839  CB  LEU B 105    15536  19963  28176  -1685   1185    914       C  
ATOM   3840  CG  LEU B 105     -22.307 -34.279  12.395  1.00171.18           C  
ANISOU 3840  CG  LEU B 105    15499  20608  28933  -1710    752    975       C  
ATOM   3841  CD1 LEU B 105     -22.383 -33.110  13.365  1.00171.74           C  
ANISOU 3841  CD1 LEU B 105    15736  20749  28770  -1947    360    913       C  
ATOM   3842  CD2 LEU B 105     -22.539 -35.596  13.121  1.00170.69           C  
ANISOU 3842  CD2 LEU B 105    15299  20628  28926  -1360    489   1144       C  
ATOM   3843  N   SER B 106     -21.626 -33.540   8.592  1.00172.93           N  
ANISOU 3843  N   SER B 106    15782  20534  29391  -2012   2230    752       N  
ATOM   3844  CA  SER B 106     -20.321 -33.695   7.962  1.00177.59           C  
ANISOU 3844  CA  SER B 106    15806  21226  30444  -2096   2539    734       C  
ATOM   3845  C   SER B 106     -20.429 -33.554   6.454  1.00177.68           C  
ANISOU 3845  C   SER B 106    16001  21163  30346  -2109   3145    679       C  
ATOM   3846  O   SER B 106     -21.500 -33.306   5.910  1.00174.14           O  
ANISOU 3846  O   SER B 106    16124  20570  29473  -2060   3293    651       O  
ATOM   3847  CB  SER B 106     -19.702 -35.057   8.284  1.00179.49           C  
ANISOU 3847  CB  SER B 106    15538  21590  31070  -1762   2425    764       C  
ATOM   3848  OG  SER B 106     -20.245 -36.071   7.458  1.00177.63           O  
ANISOU 3848  OG  SER B 106    15469  21262  30761  -1418   2712    724       O  
ATOM   3849  N   LEU B 107     -19.293 -33.680   5.790  1.00182.17           N  
ANISOU 3849  N   LEU B 107    16066  21862  31288  -2170   3493    666       N  
ATOM   3850  CA  LEU B 107     -19.236 -33.693   4.338  1.00183.26           C  
ANISOU 3850  CA  LEU B 107    16293  22001  31337  -2129   4103    619       C  
ATOM   3851  C   LEU B 107     -18.694 -35.021   3.758  1.00185.45           C  
ANISOU 3851  C   LEU B 107    16160  22405  31898  -1732   4361    536       C  
ATOM   3852  O   LEU B 107     -19.322 -35.558   2.846  1.00183.73           O  
ANISOU 3852  O   LEU B 107    16255  22117  31438  -1466   4658    443       O  
ATOM   3853  CB  LEU B 107     -18.392 -32.516   3.834  1.00187.46           C  
ANISOU 3853  CB  LEU B 107    16633  22592  32002  -2578   4410    686       C  
ATOM   3854  CG  LEU B 107     -18.170 -32.358   2.329  1.00189.79           C  
ANISOU 3854  CG  LEU B 107    16974  22946  32191  -2596   5087    688       C  
ATOM   3855  CD1 LEU B 107     -19.485 -32.136   1.597  1.00185.44           C  
ANISOU 3855  CD1 LEU B 107    17192  22203  31062  -2479   5254    657       C  
ATOM   3856  CD2 LEU B 107     -17.200 -31.214   2.060  1.00194.83           C  
ANISOU 3856  CD2 LEU B 107    17317  23655  33054  -3095   5327    816       C  
ATOM   3857  N   PRO B 108     -17.556 -35.562   4.291  1.00189.47           N  
ANISOU 3857  N   PRO B 108    15980  23095  32916  -1666   4220    545       N  
ATOM   3858  CA  PRO B 108     -16.825 -36.639   3.596  1.00192.95           C  
ANISOU 3858  CA  PRO B 108    15963  23678  33672  -1313   4542    444       C  
ATOM   3859  C   PRO B 108     -17.670 -37.746   2.985  1.00190.20           C  
ANISOU 3859  C   PRO B 108    15966  23183  33119   -854   4662    317       C  
ATOM   3860  O   PRO B 108     -18.358 -38.477   3.695  1.00187.09           O  
ANISOU 3860  O   PRO B 108    15769  22631  32685   -625   4259    332       O  
ATOM   3861  CB  PRO B 108     -15.935 -37.219   4.700  1.00195.81           C  
ANISOU 3861  CB  PRO B 108    15703  24170  34526  -1213   4112    486       C  
ATOM   3862  CG  PRO B 108     -15.638 -36.071   5.554  1.00196.48           C  
ANISOU 3862  CG  PRO B 108    15707  24298  34650  -1672   3803    594       C  
ATOM   3863  CD  PRO B 108     -16.914 -35.272   5.592  1.00191.26           C  
ANISOU 3863  CD  PRO B 108    15816  23409  33443  -1859   3717    626       C  
ATOM   3864  N   SER B 109     -17.590 -37.858   1.663  1.00191.87           N  
ANISOU 3864  N   SER B 109    16241  23456  33206   -729   5217    195       N  
ATOM   3865  CA  SER B 109     -18.311 -38.879   0.921  1.00190.15           C  
ANISOU 3865  CA  SER B 109    16341  23104  32805   -294   5366     20       C  
ATOM   3866  C   SER B 109     -17.916 -40.285   1.366  1.00191.88           C  
ANISOU 3866  C   SER B 109    16173  23286  33444    140   5120    -64       C  
ATOM   3867  O   SER B 109     -18.712 -41.216   1.264  1.00189.51           O  
ANISOU 3867  O   SER B 109    16185  22767  33053    468   4983   -165       O  
ATOM   3868  CB  SER B 109     -18.060 -38.700  -0.579  1.00193.00           C  
ANISOU 3868  CB  SER B 109    16747  23610  32974   -228   6025   -110       C  
ATOM   3869  OG  SER B 109     -16.689 -38.894  -0.889  1.00199.10           O  
ANISOU 3869  OG  SER B 109    16822  24672  34155   -173   6332   -144       O  
ATOM   3870  N   ASP B 110     -16.698 -40.421   1.883  1.00196.27           N  
ANISOU 3870  N   ASP B 110    16051  24041  34480    130   5035    -15       N  
ATOM   3871  CA  ASP B 110     -16.228 -41.684   2.429  1.00198.46           C  
ANISOU 3871  CA  ASP B 110    15927  24281  35196    537   4746    -62       C  
ATOM   3872  C   ASP B 110     -17.178 -42.188   3.502  1.00194.04           C  
ANISOU 3872  C   ASP B 110    15722  23447  34556    619   4162     65       C  
ATOM   3873  O   ASP B 110     -17.668 -43.323   3.448  1.00193.23           O  
ANISOU 3873  O   ASP B 110    15779  23121  34520   1000   4028    -10       O  
ATOM   3874  CB  ASP B 110     -14.824 -41.530   3.014  1.00203.64           C  
ANISOU 3874  CB  ASP B 110    15805  25216  36352    441   4655     12       C  
ATOM   3875  CG  ASP B 110     -13.790 -41.176   1.971  1.00208.99           C  
ANISOU 3875  CG  ASP B 110    16023  26209  37176    390   5255    -94       C  
ATOM   3876  OD1 ASP B 110     -14.024 -41.465   0.781  1.00209.58           O  
ANISOU 3876  OD1 ASP B 110    16303  26289  37037    610   5730   -269       O  
ATOM   3877  OD2 ASP B 110     -12.741 -40.609   2.344  1.00212.97           O  
ANISOU 3877  OD2 ASP B 110    15947  26972  38001    128   5250     -2       O  
ATOM   3878  N   LEU B 111     -17.471 -41.314   4.457  1.00191.46           N  
ANISOU 3878  N   LEU B 111    15540  23135  34071    253   3825    257       N  
ATOM   3879  CA  LEU B 111     -18.298 -41.688   5.588  1.00187.87           C  
ANISOU 3879  CA  LEU B 111    15369  22498  33514    303   3279    416       C  
ATOM   3880  C   LEU B 111     -19.752 -41.901   5.180  1.00182.92           C  
ANISOU 3880  C   LEU B 111    15432  21617  32453    381   3313    379       C  
ATOM   3881  O   LEU B 111     -20.424 -42.761   5.738  1.00181.06           O  
ANISOU 3881  O   LEU B 111    15379  21188  32229    592   2983    462       O  
ATOM   3882  CB  LEU B 111     -18.201 -40.625   6.681  1.00186.95           C  
ANISOU 3882  CB  LEU B 111    15226  22507  33300    -92   2927    589       C  
ATOM   3883  CG  LEU B 111     -16.863 -40.576   7.414  1.00191.81           C  
ANISOU 3883  CG  LEU B 111    15146  23354  34380   -146   2705    649       C  
ATOM   3884  CD1 LEU B 111     -16.805 -39.391   8.357  1.00191.17           C  
ANISOU 3884  CD1 LEU B 111    15093  23384  34159   -567   2380    760       C  
ATOM   3885  CD2 LEU B 111     -16.659 -41.869   8.175  1.00193.31           C  
ANISOU 3885  CD2 LEU B 111    15079  23480  34889    254   2313    735       C  
ATOM   3886  N   GLN B 112     -20.230 -41.153   4.188  1.00181.23           N  
ANISOU 3886  N   GLN B 112    15586  21404  31869    217   3709    267       N  
ATOM   3887  CA  GLN B 112     -21.610 -41.312   3.727  1.00176.88           C  
ANISOU 3887  CA  GLN B 112    15668  20638  30900    295   3743    208       C  
ATOM   3888  C   GLN B 112     -21.795 -42.657   3.039  1.00178.01           C  
ANISOU 3888  C   GLN B 112    15827  20601  31207    729   3849     31       C  
ATOM   3889  O   GLN B 112     -22.746 -43.383   3.339  1.00175.43           O  
ANISOU 3889  O   GLN B 112    15803  20042  30811    883   3581     63       O  
ATOM   3890  CB  GLN B 112     -22.030 -40.175   2.786  1.00175.35           C  
ANISOU 3890  CB  GLN B 112    15863  20496  30266     44   4133    132       C  
ATOM   3891  CG  GLN B 112     -22.264 -38.833   3.482  1.00173.26           C  
ANISOU 3891  CG  GLN B 112    15786  20293  29752   -375   3952    291       C  
ATOM   3892  CD  GLN B 112     -22.663 -37.708   2.530  1.00172.24           C  
ANISOU 3892  CD  GLN B 112    16063  20172  29210   -608   4326    241       C  
ATOM   3893  OE1 GLN B 112     -22.122 -37.580   1.432  1.00175.09           O  
ANISOU 3893  OE1 GLN B 112    16321  20625  29581   -591   4797    143       O  
ATOM   3894  NE2 GLN B 112     -23.625 -36.890   2.953  1.00168.50           N  
ANISOU 3894  NE2 GLN B 112    16059  19610  28353   -806   4118    317       N  
ATOM   3895  N   GLN B 113     -20.888 -42.981   2.120  1.00182.25           N  
ANISOU 3895  N   GLN B 113    16031  21248  31966    924   4239   -161       N  
ATOM   3896  CA  GLN B 113     -20.902 -44.279   1.451  1.00184.33           C  
ANISOU 3896  CA  GLN B 113    16263  21342  32434   1381   4334   -383       C  
ATOM   3897  C   GLN B 113     -20.855 -45.388   2.500  1.00184.93           C  
ANISOU 3897  C   GLN B 113    16138  21216  32913   1611   3835   -254       C  
ATOM   3898  O   GLN B 113     -21.624 -46.368   2.450  1.00183.83           O  
ANISOU 3898  O   GLN B 113    16268  20769  32809   1858   3649   -310       O  
ATOM   3899  CB  GLN B 113     -19.720 -44.399   0.481  1.00189.76           C  
ANISOU 3899  CB  GLN B 113    16508  22258  33335   1570   4814   -595       C  
ATOM   3900  CG  GLN B 113     -19.736 -43.374  -0.656  1.00189.98           C  
ANISOU 3900  CG  GLN B 113    16739  22495  32950   1365   5357   -691       C  
ATOM   3901  CD  GLN B 113     -18.343 -43.002  -1.154  1.00195.56           C  
ANISOU 3901  CD  GLN B 113    16862  23558  33884   1333   5788   -731       C  
ATOM   3902  OE1 GLN B 113     -17.336 -43.320  -0.523  1.00198.95           O  
ANISOU 3902  OE1 GLN B 113    16699  24108  34783   1397   5644   -670       O  
ATOM   3903  NE2 GLN B 113     -18.287 -42.311  -2.289  1.00196.87           N  
ANISOU 3903  NE2 GLN B 113    17181  23911  33709   1230   6322   -816       N  
ATOM   3904  N   TYR B 114     -19.958 -45.203   3.465  1.00186.99           N  
ANISOU 3904  N   TYR B 114    15928  21642  33478   1513   3601    -67       N  
ATOM   3905  CA  TYR B 114     -19.830 -46.133   4.574  1.00187.96           C  
ANISOU 3905  CA  TYR B 114    15845  21614  33959   1708   3101    117       C  
ATOM   3906  C   TYR B 114     -21.153 -46.353   5.313  1.00183.37           C  
ANISOU 3906  C   TYR B 114    15761  20788  33124   1623   2713    321       C  
ATOM   3907  O   TYR B 114     -21.574 -47.483   5.467  1.00183.76           O  
ANISOU 3907  O   TYR B 114    15910  20544  33365   1896   2492    350       O  
ATOM   3908  CB  TYR B 114     -18.757 -45.659   5.551  1.00190.53           C  
ANISOU 3908  CB  TYR B 114    15638  22209  34548   1550   2879    299       C  
ATOM   3909  CG  TYR B 114     -18.843 -46.338   6.891  1.00190.62           C  
ANISOU 3909  CG  TYR B 114    15557  22100  34768   1662   2299    570       C  
ATOM   3910  CD1 TYR B 114     -18.488 -47.669   7.036  1.00193.95           C  
ANISOU 3910  CD1 TYR B 114    15747  22317  35626   2091   2107    571       C  
ATOM   3911  CD2 TYR B 114     -19.262 -45.645   8.014  1.00187.83           C  
ANISOU 3911  CD2 TYR B 114    15358  21843  34167   1357   1938    827       C  
ATOM   3912  CE1 TYR B 114     -18.564 -48.294   8.261  1.00194.45           C  
ANISOU 3912  CE1 TYR B 114    15747  22268  35867   2196   1577    865       C  
ATOM   3913  CE2 TYR B 114     -19.338 -46.261   9.243  1.00188.33           C  
ANISOU 3913  CE2 TYR B 114    15348  21839  34371   1472   1421   1100       C  
ATOM   3914  CZ  TYR B 114     -18.991 -47.583   9.361  1.00191.63           C  
ANISOU 3914  CZ  TYR B 114    15545  22049  35218   1881   1246   1141       C  
ATOM   3915  OH  TYR B 114     -19.071 -48.190  10.591  1.00192.50           O  
ANISOU 3915  OH  TYR B 114    15604  22088  35449   1993    731   1460       O  
ATOM   3916  N   LEU B 115     -21.802 -45.286   5.773  1.00179.46           N  
ANISOU 3916  N   LEU B 115    15565  20408  32213   1251   2630    466       N  
ATOM   3917  CA  LEU B 115     -23.044 -45.409   6.554  1.00175.43           C  
ANISOU 3917  CA  LEU B 115    15480  19743  31434   1161   2277    679       C  
ATOM   3918  C   LEU B 115     -24.261 -45.887   5.763  1.00172.78           C  
ANISOU 3918  C   LEU B 115    15637  19142  30870   1263   2401    547       C  
ATOM   3919  O   LEU B 115     -25.177 -46.475   6.332  1.00170.93           O  
ANISOU 3919  O   LEU B 115    15641  18715  30588   1298   2101    718       O  
ATOM   3920  CB  LEU B 115     -23.380 -44.073   7.221  1.00172.44           C  
ANISOU 3920  CB  LEU B 115    15278  19585  30655    769   2170    822       C  
ATOM   3921  CG  LEU B 115     -22.742 -43.812   8.585  1.00173.90           C  
ANISOU 3921  CG  LEU B 115    15137  19960  30977    661   1767   1061       C  
ATOM   3922  CD1 LEU B 115     -23.156 -42.459   9.110  1.00171.12           C  
ANISOU 3922  CD1 LEU B 115    15027  19793  30197    297   1679   1126       C  
ATOM   3923  CD2 LEU B 115     -23.167 -44.900   9.550  1.00174.05           C  
ANISOU 3923  CD2 LEU B 115    15170  19826  31135    869   1339   1317       C  
ATOM   3924  N   VAL B 116     -24.288 -45.622   4.462  1.00172.91           N  
ANISOU 3924  N   VAL B 116    15800  19166  30733   1301   2836    255       N  
ATOM   3925  CA  VAL B 116     -25.338 -46.183   3.622  1.00171.26           C  
ANISOU 3925  CA  VAL B 116    16015  18705  30351   1446   2935     74       C  
ATOM   3926  C   VAL B 116     -25.159 -47.705   3.549  1.00174.42           C  
ANISOU 3926  C   VAL B 116    16258  18794  31217   1828   2777      2       C  
ATOM   3927  O   VAL B 116     -26.109 -48.455   3.810  1.00173.07           O  
ANISOU 3927  O   VAL B 116    16347  18338  31072   1889   2512     84       O  
ATOM   3928  CB  VAL B 116     -25.339 -45.569   2.209  1.00171.35           C  
ANISOU 3928  CB  VAL B 116    16220  18822  30063   1439   3435   -231       C  
ATOM   3929  CG1 VAL B 116     -26.293 -46.325   1.300  1.00170.67           C  
ANISOU 3929  CG1 VAL B 116    16517  18471  29859   1658   3499   -471       C  
ATOM   3930  CG2 VAL B 116     -25.725 -44.109   2.273  1.00168.14           C  
ANISOU 3930  CG2 VAL B 116    16067  18631  29186   1065   3546   -137       C  
ATOM   3931  N   SER B 117     -23.947 -48.150   3.198  1.00178.98           N  
ANISOU 3931  N   SER B 117    16402  19421  32179   2082   2934   -150       N  
ATOM   3932  CA  SER B 117     -23.644 -49.585   3.080  1.00182.78           C  
ANISOU 3932  CA  SER B 117    16714  19588  33144   2496   2787   -258       C  
ATOM   3933  C   SER B 117     -23.748 -50.334   4.413  1.00183.18           C  
ANISOU 3933  C   SER B 117    16650  19438  33512   2532   2260    103       C  
ATOM   3934  O   SER B 117     -24.190 -51.493   4.470  1.00184.51           O  
ANISOU 3934  O   SER B 117    16937  19214  33953   2760   2023    114       O  
ATOM   3935  CB  SER B 117     -22.253 -49.774   2.493  1.00187.90           C  
ANISOU 3935  CB  SER B 117    16873  20404  34115   2769   3078   -489       C  
ATOM   3936  OG  SER B 117     -21.286 -49.215   3.359  1.00189.18           O  
ANISOU 3936  OG  SER B 117    16581  20860  34439   2617   2978   -262       O  
ATOM   3937  N   THR B 118     -23.310 -49.663   5.471  1.00182.51           N  
ANISOU 3937  N   THR B 118    16334  19619  33392   2307   2072    398       N  
ATOM   3938  CA  THR B 118     -23.382 -50.169   6.828  1.00182.90           C  
ANISOU 3938  CA  THR B 118    16282  19576  33637   2306   1580    788       C  
ATOM   3939  C   THR B 118     -24.824 -50.341   7.198  1.00179.14           C  
ANISOU 3939  C   THR B 118    16285  18898  32884   2143   1370    985       C  
ATOM   3940  O   THR B 118     -25.221 -51.341   7.789  1.00180.29           O  
ANISOU 3940  O   THR B 118    16485  18748  33270   2269   1038   1214       O  
ATOM   3941  CB  THR B 118     -22.785 -49.191   7.846  1.00182.45           C  
ANISOU 3941  CB  THR B 118    15962  19902  33458   2050   1428   1025       C  
ATOM   3942  OG1 THR B 118     -21.456 -48.840   7.467  1.00185.91           O  
ANISOU 3942  OG1 THR B 118    15924  20586  34128   2123   1658    840       O  
ATOM   3943  CG2 THR B 118     -22.800 -49.782   9.251  1.00183.56           C  
ANISOU 3943  CG2 THR B 118    15991  19979  33775   2101    910   1432       C  
ATOM   3944  N   SER B 119     -25.620 -49.345   6.824  1.00174.95           N  
ANISOU 3944  N   SER B 119    16096  18529  31848   1860   1574    904       N  
ATOM   3945  CA  SER B 119     -27.032 -49.391   7.127  1.00171.39           C  
ANISOU 3945  CA  SER B 119    16073  17951  31097   1692   1409   1070       C  
ATOM   3946  C   SER B 119     -27.665 -50.568   6.415  1.00172.59           C  
ANISOU 3946  C   SER B 119    16426  17670  31479   1911   1394    917       C  
ATOM   3947  O   SER B 119     -28.350 -51.357   7.044  1.00172.77           O  
ANISOU 3947  O   SER B 119    16560  17443  31641   1914   1081   1179       O  
ATOM   3948  CB  SER B 119     -27.719 -48.089   6.733  1.00167.15           C  
ANISOU 3948  CB  SER B 119    15855  17663  29991   1400   1646    960       C  
ATOM   3949  OG  SER B 119     -29.052 -48.080   7.198  1.00163.99           O  
ANISOU 3949  OG  SER B 119    15804  17205  29299   1241   1455   1154       O  
ATOM   3950  N   LEU B 120     -27.376 -50.728   5.127  1.00174.04           N  
ANISOU 3950  N   LEU B 120    16637  17761  31728   2102   1720    499       N  
ATOM   3951  CA  LEU B 120     -27.940 -51.838   4.364  1.00175.68           C  
ANISOU 3951  CA  LEU B 120    17049  17543  32159   2332   1692    277       C  
ATOM   3952  C   LEU B 120     -27.643 -53.172   5.031  1.00179.53           C  
ANISOU 3952  C   LEU B 120    17343  17654  33216   2567   1324    480       C  
ATOM   3953  O   LEU B 120     -28.555 -53.950   5.331  1.00179.48           O  
ANISOU 3953  O   LEU B 120    17554  17303  33338   2535   1049    648       O  
ATOM   3954  CB  LEU B 120     -27.404 -51.835   2.933  1.00177.79           C  
ANISOU 3954  CB  LEU B 120    17304  17824  32426   2575   2098   -223       C  
ATOM   3955  CG  LEU B 120     -27.753 -50.606   2.097  1.00174.62           C  
ANISOU 3955  CG  LEU B 120    17152  17740  31458   2374   2482   -431       C  
ATOM   3956  CD1 LEU B 120     -26.973 -50.572   0.803  1.00177.66           C  
ANISOU 3956  CD1 LEU B 120    17438  18222  31841   2632   2911   -861       C  
ATOM   3957  CD2 LEU B 120     -29.231 -50.608   1.799  1.00171.38           C  
ANISOU 3957  CD2 LEU B 120    17217  17169  30732   2231   2395   -469       C  
ATOM   3958  N   ILE B 121     -26.365 -53.408   5.300  1.00183.15           N  
ANISOU 3958  N   ILE B 121    17380  18184  34024   2790   1307    493       N  
ATOM   3959  CA  ILE B 121     -25.939 -54.647   5.942  1.00187.42           C  
ANISOU 3959  CA  ILE B 121    17713  18371  35128   3060    947    694       C  
ATOM   3960  C   ILE B 121     -26.623 -54.875   7.295  1.00186.12           C  
ANISOU 3960  C   ILE B 121    17644  18125  34948   2842    524   1247       C  
ATOM   3961  O   ILE B 121     -27.229 -55.928   7.527  1.00187.83           O  
ANISOU 3961  O   ILE B 121    18017  17898  35453   2915    247   1417       O  
ATOM   3962  CB  ILE B 121     -24.424 -54.659   6.133  1.00191.34           C  
ANISOU 3962  CB  ILE B 121    17693  19063  35943   3310    988    652       C  
ATOM   3963  CG1 ILE B 121     -23.734 -54.608   4.770  1.00193.66           C  
ANISOU 3963  CG1 ILE B 121    17862  19428  36291   3575   1424    116       C  
ATOM   3964  CG2 ILE B 121     -24.006 -55.880   6.924  1.00195.81           C  
ANISOU 3964  CG2 ILE B 121    18058  19273  37068   3594    567    917       C  
ATOM   3965  CD1 ILE B 121     -22.265 -54.304   4.845  1.00197.05           C  
ANISOU 3965  CD1 ILE B 121    17745  20194  36933   3743   1570     48       C  
ATOM   3966  N   VAL B 122     -26.502 -53.895   8.188  1.00183.59           N  
ANISOU 3966  N   VAL B 122    17225  18235  34297   2580    475   1529       N  
ATOM   3967  CA  VAL B 122     -27.034 -53.996   9.546  1.00182.76           C  
ANISOU 3967  CA  VAL B 122    17175  18165  34102   2396    100   2064       C  
ATOM   3968  C   VAL B 122     -28.542 -54.245   9.547  1.00180.14           C  
ANISOU 3968  C   VAL B 122    17260  17624  33561   2182     24   2208       C  
ATOM   3969  O   VAL B 122     -29.060 -55.060  10.318  1.00181.68           O  
ANISOU 3969  O   VAL B 122    17521  17570  33940   2162   -296   2604       O  
ATOM   3970  CB  VAL B 122     -26.726 -52.720  10.361  1.00180.25           C  
ANISOU 3970  CB  VAL B 122    16730  18392  33364   2144     99   2238       C  
ATOM   3971  CG1 VAL B 122     -27.470 -52.729  11.684  1.00179.10           C  
ANISOU 3971  CG1 VAL B 122    16713  18342  32994   1951   -242   2753       C  
ATOM   3972  CG2 VAL B 122     -25.239 -52.607  10.611  1.00183.67           C  
ANISOU 3972  CG2 VAL B 122    16689  19020  34078   2333     70   2190       C  
ATOM   3973  N   CYS B 123     -29.243 -53.538   8.671  1.00176.53           N  
ANISOU 3973  N   CYS B 123    17072  17280  32724   2018    319   1899       N  
ATOM   3974  CA  CYS B 123     -30.682 -53.687   8.556  1.00174.11           C  
ANISOU 3974  CA  CYS B 123    17128  16820  32206   1814    271   1977       C  
ATOM   3975  C   CYS B 123     -31.060 -55.071   8.060  1.00177.41           C  
ANISOU 3975  C   CYS B 123    17648  16652  33106   1993    123   1900       C  
ATOM   3976  O   CYS B 123     -31.981 -55.683   8.588  1.00177.78           O  
ANISOU 3976  O   CYS B 123    17839  16469  33238   1853   -121   2225       O  
ATOM   3977  CB  CYS B 123     -31.244 -52.625   7.617  1.00170.07           C  
ANISOU 3977  CB  CYS B 123    16867  16552  31199   1655    615   1615       C  
ATOM   3978  SG  CYS B 123     -31.334 -50.991   8.366  1.00165.78           S  
ANISOU 3978  SG  CYS B 123    16345  16612  30033   1351    698   1787       S  
ATOM   3979  N   GLY B 124     -30.326 -55.579   7.074  1.00180.30           N  
ANISOU 3979  N   GLY B 124    17927  16776  33804   2306    264   1478       N  
ATOM   3980  CA  GLY B 124     -30.539 -56.944   6.623  1.00184.29           C  
ANISOU 3980  CA  GLY B 124    18517  16677  34828   2526     82   1362       C  
ATOM   3981  C   GLY B 124     -30.404 -57.907   7.787  1.00187.74           C  
ANISOU 3981  C   GLY B 124    18817  16816  35698   2572   -332   1884       C  
ATOM   3982  O   GLY B 124     -31.268 -58.759   8.028  1.00189.21           O  
ANISOU 3982  O   GLY B 124    19183  16590  36119   2474   -587   2116       O  
ATOM   3983  N   LEU B 125     -29.320 -57.742   8.537  1.00189.29           N  
ANISOU 3983  N   LEU B 125    18688  17239  35994   2704   -410   2095       N  
ATOM   3984  CA  LEU B 125     -29.031 -58.619   9.664  1.00193.09           C  
ANISOU 3984  CA  LEU B 125    19020  17479  36867   2799   -810   2607       C  
ATOM   3985  C   LEU B 125     -30.098 -58.601  10.758  1.00191.42           C  
ANISOU 3985  C   LEU B 125    18979  17331  36421   2448  -1043   3196       C  
ATOM   3986  O   LEU B 125     -30.536 -59.654  11.220  1.00194.68           O  
ANISOU 3986  O   LEU B 125    19474  17298  37197   2451  -1343   3552       O  
ATOM   3987  CB  LEU B 125     -27.676 -58.248  10.275  1.00194.74           C  
ANISOU 3987  CB  LEU B 125    18829  18030  37133   2987   -845   2702       C  
ATOM   3988  CG  LEU B 125     -26.445 -58.483   9.403  1.00198.04           C  
ANISOU 3988  CG  LEU B 125    18969  18376  37899   3394   -667   2221       C  
ATOM   3989  CD1 LEU B 125     -25.218 -57.912  10.080  1.00199.15           C  
ANISOU 3989  CD1 LEU B 125    18685  18958  38024   3490   -695   2342       C  
ATOM   3990  CD2 LEU B 125     -26.283 -59.966   9.155  1.00203.61           C  
ANISOU 3990  CD2 LEU B 125    19689  18413  39260   3753   -913   2179       C  
ATOM   3991  N   LEU B 126     -30.546 -57.417  11.154  1.00186.74           N  
ANISOU 3991  N   LEU B 126    18446  17281  35224   2149   -899   3300       N  
ATOM   3992  CA  LEU B 126     -31.460 -57.336  12.286  1.00185.59           C  
ANISOU 3992  CA  LEU B 126    18414  17296  34806   1856  -1099   3868       C  
ATOM   3993  C   LEU B 126     -32.909 -57.602  11.873  1.00184.03           C  
ANISOU 3993  C   LEU B 126    18525  16875  34522   1603  -1066   3875       C  
ATOM   3994  O   LEU B 126     -33.742 -58.022  12.691  1.00184.94           O  
ANISOU 3994  O   LEU B 126    18723  16926  34620   1398  -1269   4380       O  
ATOM   3995  CB  LEU B 126     -31.312 -55.977  12.965  1.00181.87           C  
ANISOU 3995  CB  LEU B 126    17871  17501  33731   1679   -997   3965       C  
ATOM   3996  CG  LEU B 126     -29.852 -55.796  13.381  1.00184.15           C  
ANISOU 3996  CG  LEU B 126    17814  17982  34173   1918  -1076   3956       C  
ATOM   3997  CD1 LEU B 126     -29.621 -54.491  14.099  1.00181.23           C  
ANISOU 3997  CD1 LEU B 126    17361  18238  33260   1747  -1034   4035       C  
ATOM   3998  CD2 LEU B 126     -29.417 -56.953  14.250  1.00189.38           C  
ANISOU 3998  CD2 LEU B 126    18324  18336  35294   2118  -1460   4417       C  
ATOM   3999  N   SER B 127     -33.199 -57.393  10.594  1.00182.17           N  
ANISOU 3999  N   SER B 127    18445  16530  34243   1622   -815   3325       N  
ATOM   4000  CA  SER B 127     -34.453 -57.869  10.038  1.00181.88           C  
ANISOU 4000  CA  SER B 127    18667  16174  34264   1445   -833   3251       C  
ATOM   4001  C   SER B 127     -34.445 -59.381  10.152  1.00187.42           C  
ANISOU 4001  C   SER B 127    19362  16198  35650   1571  -1148   3455       C  
ATOM   4002  O   SER B 127     -35.416 -59.977  10.608  1.00188.78           O  
ANISOU 4002  O   SER B 127    19642  16136  35949   1338  -1345   3839       O  
ATOM   4003  CB  SER B 127     -34.632 -57.443   8.582  1.00179.67           C  
ANISOU 4003  CB  SER B 127    18555  15880  33832   1509   -537   2584       C  
ATOM   4004  OG  SER B 127     -34.877 -56.061   8.467  1.00174.69           O  
ANISOU 4004  OG  SER B 127    17994  15816  32565   1343   -268   2446       O  
ATOM   4005  N   MET B 128     -33.333 -59.999   9.762  1.00191.03           N  
ANISOU 4005  N   MET B 128    19678  16340  36565   1943  -1197   3214       N  
ATOM   4006  CA  MET B 128     -33.181 -61.438   9.946  1.00196.92           C  
ANISOU 4006  CA  MET B 128    20414  16406  38002   2116  -1533   3419       C  
ATOM   4007  C   MET B 128     -33.372 -61.819  11.411  1.00198.95           C  
ANISOU 4007  C   MET B 128    20594  16673  38324   1953  -1835   4208       C  
ATOM   4008  O   MET B 128     -33.948 -62.864  11.712  1.00202.76           O  
ANISOU 4008  O   MET B 128    21180  16636  39224   1860  -2109   4556       O  
ATOM   4009  CB  MET B 128     -31.817 -61.910   9.448  1.00200.61           C  
ANISOU 4009  CB  MET B 128    20689  16639  38895   2596  -1534   3059       C  
ATOM   4010  CG  MET B 128     -31.847 -62.432   8.033  1.00202.40           C  
ANISOU 4010  CG  MET B 128    21063  16433  39406   2826  -1427   2394       C  
ATOM   4011  SD  MET B 128     -30.467 -63.520   7.656  1.00209.16           S  
ANISOU 4011  SD  MET B 128    21718  16784  40969   3426  -1574   2107       S  
ATOM   4012  CE  MET B 128     -29.073 -62.488   8.097  1.00207.40           C  
ANISOU 4012  CE  MET B 128    21090  17274  40438   3604  -1348   2120       C  
ATOM   4013  N   VAL B 129     -32.906 -60.962  12.316  1.00196.73           N  
ANISOU 4013  N   VAL B 129    20143  16985  37620   1909  -1791   4494       N  
ATOM   4014  CA  VAL B 129     -33.088 -61.201  13.746  1.00198.60           C  
ANISOU 4014  CA  VAL B 129    20318  17343  37797   1768  -2057   5247       C  
ATOM   4015  C   VAL B 129     -34.568 -61.236  14.169  1.00197.38           C  
ANISOU 4015  C   VAL B 129    20359  17232  37405   1345  -2085   5650       C  
ATOM   4016  O   VAL B 129     -34.982 -62.151  14.884  1.00201.44           O  
ANISOU 4016  O   VAL B 129    20906  17414  38219   1243  -2351   6217       O  
ATOM   4017  CB  VAL B 129     -32.342 -60.146  14.585  1.00196.29           C  
ANISOU 4017  CB  VAL B 129    19821  17742  37020   1801  -2003   5393       C  
ATOM   4018  CG1 VAL B 129     -32.701 -60.276  16.054  1.00197.94           C  
ANISOU 4018  CG1 VAL B 129    20010  18171  37026   1636  -2251   6157       C  
ATOM   4019  CG2 VAL B 129     -30.854 -60.306  14.403  1.00198.93           C  
ANISOU 4019  CG2 VAL B 129    19890  18011  37683   2207  -2052   5143       C  
ATOM   4020  N   GLN B 130     -35.376 -60.269  13.734  1.00192.28           N  
ANISOU 4020  N   GLN B 130    19833  16985  36241   1103  -1813   5384       N  
ATOM   4021  CA  GLN B 130     -36.779 -60.264  14.180  1.00191.42           C  
ANISOU 4021  CA  GLN B 130    19855  16984  35891    715  -1829   5774       C  
ATOM   4022  C   GLN B 130     -37.737 -61.062  13.279  1.00192.96           C  
ANISOU 4022  C   GLN B 130    20223  16614  36480    565  -1866   5574       C  
ATOM   4023  O   GLN B 130     -38.885 -61.295  13.654  1.00193.56           O  
ANISOU 4023  O   GLN B 130    20363  16681  36501    237  -1924   5945       O  
ATOM   4024  CB  GLN B 130     -37.315 -58.834  14.332  1.00185.68           C  
ANISOU 4024  CB  GLN B 130    19166  16995  34390    519  -1564   5665       C  
ATOM   4025  CG  GLN B 130     -38.619 -58.775  15.152  1.00185.50           C  
ANISOU 4025  CG  GLN B 130    19196  17232  34052    164  -1596   6199       C  
ATOM   4026  CD  GLN B 130     -39.158 -57.379  15.350  1.00180.34           C  
ANISOU 4026  CD  GLN B 130    18584  17298  32638     18  -1357   6084       C  
ATOM   4027  OE1 GLN B 130     -38.419 -56.453  15.686  1.00178.00           O  
ANISOU 4027  OE1 GLN B 130    18224  17446  31961    148  -1277   5968       O  
ATOM   4028  NE2 GLN B 130     -40.461 -57.219  15.142  1.00178.87           N  
ANISOU 4028  NE2 GLN B 130    18498  17221  32245   -252  -1259   6104       N  
ATOM   4029  N   ILE B 131     -37.285 -61.497  12.107  1.00194.06           N  
ANISOU 4029  N   ILE B 131    20424  16294  37016    803  -1841   4989       N  
ATOM   4030  CA  ILE B 131     -38.148 -62.328  11.269  1.00196.29           C  
ANISOU 4030  CA  ILE B 131    20876  15994  37709    681  -1937   4771       C  
ATOM   4031  C   ILE B 131     -38.289 -63.692  11.955  1.00202.63           C  
ANISOU 4031  C   ILE B 131    21666  16175  39149    617  -2305   5346       C  
ATOM   4032  O   ILE B 131     -39.238 -64.442  11.708  1.00205.30           O  
ANISOU 4032  O   ILE B 131    22118  16054  39833    375  -2457   5438       O  
ATOM   4033  CB  ILE B 131     -37.608 -62.470   9.829  1.00196.43           C  
ANISOU 4033  CB  ILE B 131    20984  15690  37960    995  -1828   3967       C  
ATOM   4034  CG1 ILE B 131     -37.806 -61.169   9.061  1.00190.53           C  
ANISOU 4034  CG1 ILE B 131    20310  15510  36575    965  -1464   3455       C  
ATOM   4035  CG2 ILE B 131     -38.354 -63.531   9.050  1.00200.15           C  
ANISOU 4035  CG2 ILE B 131    21629  15457  38962    923  -2023   3748       C  
ATOM   4036  CD1 ILE B 131     -37.221 -61.197   7.689  1.00190.75           C  
ANISOU 4036  CD1 ILE B 131    20419  15334  36724   1287  -1308   2701       C  
ATOM   4037  N   THR B 132     -37.359 -63.988  12.859  1.00205.32           N  
ANISOU 4037  N   THR B 132    21863  16510  39639    817  -2464   5763       N  
ATOM   4038  CA  THR B 132     -37.366 -65.262  13.570  1.00211.80           C  
ANISOU 4038  CA  THR B 132    22682  16734  41056    796  -2825   6362       C  
ATOM   4039  C   THR B 132     -37.416 -65.064  15.083  1.00212.49           C  
ANISOU 4039  C   THR B 132    22655  17259  40824    639  -2911   7189       C  
ATOM   4040  O   THR B 132     -37.045 -64.005  15.597  1.00208.55           O  
ANISOU 4040  O   THR B 132    22044  17477  39718    680  -2738   7221       O  
ATOM   4041  CB  THR B 132     -36.141 -66.101  13.227  1.00216.32           C  
ANISOU 4041  CB  THR B 132    23211  16738  42241   1265  -3023   6125       C  
ATOM   4042  OG1 THR B 132     -36.247 -67.378  13.866  1.00223.04           O  
ANISOU 4042  OG1 THR B 132    24106  16929  43710   1231  -3399   6715       O  
ATOM   4043  CG2 THR B 132     -34.870 -65.400  13.687  1.00214.59           C  
ANISOU 4043  CG2 THR B 132    22777  17037  41720   1590  -2932   6094       C  
ATOM   4044  N   SER B 145     -40.234 -61.564  16.818  1.00198.07           N  
ANISOU 4044  N   SER B 145    20770  17922  36565   -337  -2173   7818       N  
ATOM   4045  CA  SER B 145     -41.444 -61.999  16.126  1.00198.63           C  
ANISOU 4045  CA  SER B 145    20932  17667  36871   -637  -2147   7713       C  
ATOM   4046  C   SER B 145     -41.184 -63.185  15.204  1.00202.59           C  
ANISOU 4046  C   SER B 145    21521  17267  38189   -527  -2351   7426       C  
ATOM   4047  O   SER B 145     -40.037 -63.507  14.894  1.00203.93           O  
ANISOU 4047  O   SER B 145    21686  17118  38682   -170  -2447   7161       O  
ATOM   4048  CB  SER B 145     -42.043 -60.852  15.317  1.00192.63           C  
ANISOU 4048  CB  SER B 145    20239  17358  35592   -713  -1850   7120       C  
ATOM   4049  OG  SER B 145     -42.913 -61.349  14.313  1.00193.37           O  
ANISOU 4049  OG  SER B 145    20428  17012  36030   -891  -1867   6802       O  
ATOM   4050  N   GLY B 146     -42.258 -63.836  14.772  1.00204.86           N  
ANISOU 4050  N   GLY B 146    21873  17149  38814   -829  -2428   7464       N  
ATOM   4051  CA  GLY B 146     -42.144 -64.992  13.904  1.00209.19           C  
ANISOU 4051  CA  GLY B 146    22528  16804  40149   -752  -2659   7175       C  
ATOM   4052  C   GLY B 146     -42.854 -64.810  12.578  1.00206.91           C  
ANISOU 4052  C   GLY B 146    22360  16368  39890   -840  -2558   6467       C  
ATOM   4053  O   GLY B 146     -43.172 -65.782  11.900  1.00210.95           O  
ANISOU 4053  O   GLY B 146    22967  16161  41021   -899  -2771   6272       O  
ATOM   4054  N   VAL B 147     -43.091 -63.560  12.201  1.00200.78           N  
ANISOU 4054  N   VAL B 147    21591  16255  38443   -834  -2255   6069       N  
ATOM   4055  CA  VAL B 147     -43.786 -63.254  10.959  1.00198.37           C  
ANISOU 4055  CA  VAL B 147    21407  15906  38057   -896  -2148   5404       C  
ATOM   4056  C   VAL B 147     -43.026 -62.097  10.331  1.00192.82           C  
ANISOU 4056  C   VAL B 147    20761  15677  36826   -576  -1860   4801       C  
ATOM   4057  O   VAL B 147     -42.262 -61.443  11.034  1.00190.63           O  
ANISOU 4057  O   VAL B 147    20392  15848  36191   -430  -1742   4999       O  
ATOM   4058  CB  VAL B 147     -45.265 -62.898  11.226  1.00197.20           C  
ANISOU 4058  CB  VAL B 147    21199  16128  37601  -1337  -2078   5673       C  
ATOM   4059  CG1 VAL B 147     -45.355 -61.741  12.205  1.00193.02           C  
ANISOU 4059  CG1 VAL B 147    20557  16470  36313  -1392  -1838   6032       C  
ATOM   4060  CG2 VAL B 147     -46.015 -62.578   9.945  1.00195.00           C  
ANISOU 4060  CG2 VAL B 147    21041  15821  37230  -1388  -2003   4987       C  
ATOM   4061  N   LEU B 148     -43.226 -61.842   9.035  1.00190.95           N  
ANISOU 4061  N   LEU B 148    20672  15347  36534   -476  -1758   4087       N  
ATOM   4062  CA  LEU B 148     -42.469 -60.814   8.308  1.00186.43           C  
ANISOU 4062  CA  LEU B 148    20170  15158  35507   -172  -1473   3505       C  
ATOM   4063  C   LEU B 148     -42.315 -59.518   9.088  1.00181.60           C  
ANISOU 4063  C   LEU B 148    19473  15333  34195   -212  -1234   3743       C  
ATOM   4064  O   LEU B 148     -43.145 -58.621   8.996  1.00177.92           O  
ANISOU 4064  O   LEU B 148    19054  15335  33212   -385  -1071   3668       O  
ATOM   4065  CB  LEU B 148     -43.114 -60.499   6.961  1.00184.61           C  
ANISOU 4065  CB  LEU B 148    20124  14903  35118   -164  -1367   2833       C  
ATOM   4066  CG  LEU B 148     -42.737 -61.426   5.814  1.00188.37           C  
ANISOU 4066  CG  LEU B 148    20736  14710  36127     87  -1507   2270       C  
ATOM   4067  CD1 LEU B 148     -43.257 -60.884   4.504  1.00186.04           C  
ANISOU 4067  CD1 LEU B 148    20634  14544  35509    147  -1360   1587       C  
ATOM   4068  CD2 LEU B 148     -41.245 -61.592   5.765  1.00189.55           C  
ANISOU 4068  CD2 LEU B 148    20831  14729  36461    495  -1450   2120       C  
ATOM   4069  N   SER B 149     -41.208 -59.413   9.812  1.00181.92           N  
ANISOU 4069  N   SER B 149    19389  15501  34231    -22  -1234   3984       N  
ATOM   4070  CA  SER B 149     -40.942 -58.267  10.665  1.00178.19           C  
ANISOU 4070  CA  SER B 149    18829  15724  33152    -45  -1068   4225       C  
ATOM   4071  C   SER B 149     -39.730 -57.537  10.147  1.00175.83           C  
ANISOU 4071  C   SER B 149    18519  15617  32672    263   -871   3769       C  
ATOM   4072  O   SER B 149     -38.627 -57.693  10.663  1.00177.42           O  
ANISOU 4072  O   SER B 149    18573  15804  33035    460   -937   3922       O  
ATOM   4073  CB  SER B 149     -40.697 -58.692  12.113  1.00180.98           C  
ANISOU 4073  CB  SER B 149    19018  16148  33599   -113  -1260   4959       C  
ATOM   4074  OG  SER B 149     -41.904 -59.013  12.766  1.00182.41           O  
ANISOU 4074  OG  SER B 149    19181  16385  33742   -451  -1355   5461       O  
ATOM   4075  N   VAL B 150     -39.954 -56.735   9.116  1.00172.35           N  
ANISOU 4075  N   VAL B 150    18225  15368  31895    296   -630   3224       N  
ATOM   4076  CA  VAL B 150     -38.902 -55.960   8.481  1.00170.21           C  
ANISOU 4076  CA  VAL B 150    17953  15300  31420    547   -392   2774       C  
ATOM   4077  C   VAL B 150     -38.448 -54.827   9.399  1.00167.25           C  
ANISOU 4077  C   VAL B 150    17473  15522  30554    503   -287   3016       C  
ATOM   4078  O   VAL B 150     -39.267 -54.075   9.919  1.00164.52           O  
ANISOU 4078  O   VAL B 150    17185  15584  29740    290   -243   3212       O  
ATOM   4079  CB  VAL B 150     -39.382 -55.387   7.134  1.00167.65           C  
ANISOU 4079  CB  VAL B 150    17848  15030  30819    573   -164   2177       C  
ATOM   4080  CG1 VAL B 150     -38.483 -54.268   6.671  1.00164.81           C  
ANISOU 4080  CG1 VAL B 150    17494  15042  30082    735    134   1838       C  
ATOM   4081  CG2 VAL B 150     -39.485 -56.492   6.086  1.00171.17           C  
ANISOU 4081  CG2 VAL B 150    18394  14874  31768    715   -268   1803       C  
ATOM   4082  N   MET B 151     -37.140 -54.702   9.590  1.00168.15           N  
ANISOU 4082  N   MET B 151    17419  15689  30782    715   -259   2976       N  
ATOM   4083  CA  MET B 151     -36.599 -53.666  10.458  1.00165.99           C  
ANISOU 4083  CA  MET B 151    17030  15942  30097    680   -204   3168       C  
ATOM   4084  C   MET B 151     -35.723 -52.707   9.658  1.00163.87           C  
ANISOU 4084  C   MET B 151    16753  15889  29622    814     77   2689       C  
ATOM   4085  O   MET B 151     -35.113 -53.088   8.664  1.00165.39           O  
ANISOU 4085  O   MET B 151    16927  15806  30107   1019    196   2303       O  
ATOM   4086  CB  MET B 151     -35.816 -54.280  11.618  1.00169.39           C  
ANISOU 4086  CB  MET B 151    17222  16323  30815    772   -464   3637       C  
ATOM   4087  CG  MET B 151     -36.658 -55.180  12.508  1.00171.95           C  
ANISOU 4087  CG  MET B 151    17554  16469  31309    616   -729   4201       C  
ATOM   4088  SD  MET B 151     -36.042 -55.301  14.198  1.00174.51           S  
ANISOU 4088  SD  MET B 151    17663  17060  31582    644   -997   4862       S  
ATOM   4089  CE  MET B 151     -36.640 -53.758  14.873  1.00169.89           C  
ANISOU 4089  CE  MET B 151    17155  17238  30158    436   -852   4929       C  
ATOM   4090  N   GLY B 152     -35.702 -51.447  10.075  1.00161.37           N  
ANISOU 4090  N   GLY B 152    16458  16064  28791    695    191   2711       N  
ATOM   4091  CA  GLY B 152     -34.899 -50.444   9.403  1.00159.62           C  
ANISOU 4091  CA  GLY B 152    16227  16059  28362    763    458   2323       C  
ATOM   4092  C   GLY B 152     -34.818 -49.174  10.224  1.00157.08           C  
ANISOU 4092  C   GLY B 152    15899  16235  27551    614    471   2465       C  
ATOM   4093  O   GLY B 152     -35.557 -49.015  11.181  1.00156.23           O  
ANISOU 4093  O   GLY B 152    15842  16336  27184    474    309   2802       O  
ATOM   4094  N   VAL B 153     -33.900 -48.283   9.866  1.00158.93           N  
ANISOU 4094  N   VAL B 153    16061  16658  27667    645    659   2209       N  
ATOM   4095  CA  VAL B 153     -33.635 -47.075  10.646  1.00157.25           C  
ANISOU 4095  CA  VAL B 153    15823  16866  27059    512    635   2303       C  
ATOM   4096  C   VAL B 153     -34.873 -46.174  10.803  1.00153.76           C  
ANISOU 4096  C   VAL B 153    15686  16678  26058    334    674   2316       C  
ATOM   4097  O   VAL B 153     -35.575 -45.889   9.831  1.00151.79           O  
ANISOU 4097  O   VAL B 153    15683  16360  25633    306    873   2050       O  
ATOM   4098  CB  VAL B 153     -32.503 -46.266  10.006  1.00154.11           C  
ANISOU 4098  CB  VAL B 153    15311  16568  26675    537    869   1985       C  
ATOM   4099  CG1 VAL B 153     -32.048 -45.167  10.953  1.00153.47           C  
ANISOU 4099  CG1 VAL B 153    15146  16859  26307    401    761   2102       C  
ATOM   4100  CG2 VAL B 153     -31.355 -47.183   9.694  1.00157.79           C  
ANISOU 4100  CG2 VAL B 153    15462  16798  27693    751    873   1919       C  
ATOM   4101  N   SER B 154     -35.122 -45.720  12.030  1.00155.19           N  
ANISOU 4101  N   SER B 154    15847  17173  25945    243    474   2611       N  
ATOM   4102  CA  SER B 154     -36.290 -44.897  12.341  1.00152.45           C  
ANISOU 4102  CA  SER B 154    15755  17107  25062    116    483   2646       C  
ATOM   4103  C   SER B 154     -36.077 -43.450  11.894  1.00150.14           C  
ANISOU 4103  C   SER B 154    15633  17008  24406     49    665   2323       C  
ATOM   4104  O   SER B 154     -34.938 -43.004  11.758  1.00151.03           O  
ANISOU 4104  O   SER B 154    15607  17130  24648     54    721   2182       O  
ATOM   4105  CB  SER B 154     -36.589 -44.950  13.840  1.00155.12           C  
ANISOU 4105  CB  SER B 154    16007  17741  25190     81    210   3070       C  
ATOM   4106  OG  SER B 154     -37.770 -44.239  14.164  1.00152.95           O  
ANISOU 4106  OG  SER B 154    15954  17762  24400     -4    226   3103       O  
ATOM   4107  N   PHE B 155     -37.164 -42.719  11.654  1.00147.43           N  
ANISOU 4107  N   PHE B 155    15576  16809  23631    -16    752   2213       N  
ATOM   4108  CA  PHE B 155     -37.056 -41.322  11.228  1.00145.52           C  
ANISOU 4108  CA  PHE B 155    15545  16708  23038    -76    905   1929       C  
ATOM   4109  C   PHE B 155     -37.190 -40.337  12.390  1.00145.10           C  
ANISOU 4109  C   PHE B 155    15543  17013  22574   -133    724   2042       C  
ATOM   4110  O   PHE B 155     -37.037 -39.136  12.197  1.00144.02           O  
ANISOU 4110  O   PHE B 155    15582  16971  22169   -190    797   1828       O  
ATOM   4111  CB  PHE B 155     -38.118 -40.991  10.182  1.00147.22           C  
ANISOU 4111  CB  PHE B 155    16077  16856  23005    -73   1099   1694       C  
ATOM   4112  CG  PHE B 155     -37.946 -41.711   8.871  1.00147.73           C  
ANISOU 4112  CG  PHE B 155    16155  16590  23385     -1   1299   1478       C  
ATOM   4113  CD1 PHE B 155     -36.890 -42.579   8.659  1.00150.10           C  
ANISOU 4113  CD1 PHE B 155    16194  16669  24169     71   1319   1483       C  
ATOM   4114  CD2 PHE B 155     -38.858 -41.514   7.845  1.00146.16           C  
ANISOU 4114  CD2 PHE B 155    16235  16320  22979     25   1452   1247       C  
ATOM   4115  CE1 PHE B 155     -36.754 -43.246   7.451  1.00150.97           C  
ANISOU 4115  CE1 PHE B 155    16331  16492  24537    176   1500   1245       C  
ATOM   4116  CE2 PHE B 155     -38.725 -42.168   6.635  1.00146.98           C  
ANISOU 4116  CE2 PHE B 155    16375  16145  23326    117   1619   1015       C  
ATOM   4117  CZ  PHE B 155     -37.666 -43.030   6.434  1.00149.42           C  
ANISOU 4117  CZ  PHE B 155    16432  16236  24103    197   1650   1004       C  
ATOM   4118  N   SER B 156     -37.510 -40.837  13.581  1.00146.51           N  
ANISOU 4118  N   SER B 156    15593  17386  22690   -109    484   2378       N  
ATOM   4119  CA  SER B 156     -37.687 -39.979  14.755  1.00146.63           C  
ANISOU 4119  CA  SER B 156    15660  17782  22271   -120    292   2477       C  
ATOM   4120  C   SER B 156     -36.351 -39.444  15.247  1.00148.32           C  
ANISOU 4120  C   SER B 156    15709  18057  22591   -149    162   2419       C  
ATOM   4121  O   SER B 156     -36.237 -38.299  15.746  1.00148.16           O  
ANISOU 4121  O   SER B 156    15808  18254  22232   -187     66   2289       O  
ATOM   4122  CB  SER B 156     -38.378 -40.745  15.884  1.00145.76           C  
ANISOU 4122  CB  SER B 156    15441  17896  22045    -74     93   2888       C  
ATOM   4123  OG  SER B 156     -37.667 -41.926  16.211  1.00148.33           O  
ANISOU 4123  OG  SER B 156    15483  18054  22820    -41    -30   3162       O  
ATOM   4124  N   ILE B 157     -35.332 -40.281  15.096  1.00145.12           N  
ANISOU 4124  N   ILE B 157    15016  17446  22676   -125    142   2497       N  
ATOM   4125  CA  ILE B 157     -34.020 -39.953  15.606  1.00147.36           C  
ANISOU 4125  CA  ILE B 157    15060  17799  23132   -148    -11   2475       C  
ATOM   4126  C   ILE B 157     -33.487 -38.731  14.865  1.00146.44           C  
ANISOU 4126  C   ILE B 157    15059  17625  22957   -273    163   2112       C  
ATOM   4127  O   ILE B 157     -32.762 -37.935  15.442  1.00147.81           O  
ANISOU 4127  O   ILE B 157    15152  17945  23063   -349      4   2040       O  
ATOM   4128  CB  ILE B 157     -33.036 -41.157  15.479  1.00151.21           C  
ANISOU 4128  CB  ILE B 157    15191  18061  24199    -60    -50   2614       C  
ATOM   4129  CG1 ILE B 157     -31.886 -41.036  16.486  1.00154.27           C  
ANISOU 4129  CG1 ILE B 157    15278  18631  24707    -42   -340   2726       C  
ATOM   4130  CG2 ILE B 157     -32.548 -41.350  14.037  1.00150.80           C  
ANISOU 4130  CG2 ILE B 157    15106  17685  24507    -62    271   2336       C  
ATOM   4131  CD1 ILE B 157     -32.337 -41.073  17.931  1.00155.43           C  
ANISOU 4131  CD1 ILE B 157    15443  19111  24500     13   -669   3038       C  
ATOM   4132  N   ILE B 158     -33.920 -38.531  13.625  1.00144.39           N  
ANISOU 4132  N   ILE B 158    15013  17162  22685   -303    472   1893       N  
ATOM   4133  CA  ILE B 158     -33.504 -37.359  12.865  1.00143.77           C  
ANISOU 4133  CA  ILE B 158    15086  17015  22526   -433    664   1596       C  
ATOM   4134  C   ILE B 158     -34.023 -36.081  13.513  1.00142.86           C  
ANISOU 4134  C   ILE B 158    15244  17112  21925   -501    515   1514       C  
ATOM   4135  O   ILE B 158     -33.254 -35.174  13.827  1.00144.26           O  
ANISOU 4135  O   ILE B 158    15381  17337  22094   -623    416   1399       O  
ATOM   4136  CB  ILE B 158     -34.008 -37.421  11.412  1.00141.95           C  
ANISOU 4136  CB  ILE B 158    15080  16553  22300   -418   1015   1404       C  
ATOM   4137  CG1 ILE B 158     -33.378 -38.602  10.670  1.00143.39           C  
ANISOU 4137  CG1 ILE B 158    15005  16509  22967   -328   1175   1408       C  
ATOM   4138  CG2 ILE B 158     -33.724 -36.107  10.698  1.00141.51           C  
ANISOU 4138  CG2 ILE B 158    15244  16446  22078   -558   1208   1154       C  
ATOM   4139  CD1 ILE B 158     -34.013 -38.894   9.329  1.00141.95           C  
ANISOU 4139  CD1 ILE B 158    15049  16124  22762   -261   1469   1227       C  
ATOM   4140  N   SER B 159     -35.335 -36.027  13.719  1.00145.80           N  
ANISOU 4140  N   SER B 159    15880  17608  21910   -415    486   1561       N  
ATOM   4141  CA  SER B 159     -35.989 -34.889  14.361  1.00145.12           C  
ANISOU 4141  CA  SER B 159    16070  17742  21325   -412    339   1469       C  
ATOM   4142  C   SER B 159     -35.357 -34.579  15.719  1.00147.50           C  
ANISOU 4142  C   SER B 159    16206  18292  21547   -421     -2   1556       C  
ATOM   4143  O   SER B 159     -35.273 -33.413  16.104  1.00148.03           O  
ANISOU 4143  O   SER B 159    16448  18447  21348   -471   -135   1373       O  
ATOM   4144  CB  SER B 159     -37.495 -35.126  14.513  1.00138.64           C  
ANISOU 4144  CB  SER B 159    15455  17084  20137   -279    347   1559       C  
ATOM   4145  OG  SER B 159     -38.121 -33.974  15.055  1.00138.24           O  
ANISOU 4145  OG  SER B 159    15678  17249  19597   -235    225   1425       O  
ATOM   4146  N   VAL B 160     -34.962 -35.607  16.469  1.00146.28           N  
ANISOU 4146  N   VAL B 160    15736  18246  21599   -355   -173   1830       N  
ATOM   4147  CA  VAL B 160     -34.213 -35.340  17.707  1.00149.07           C  
ANISOU 4147  CA  VAL B 160    15908  18837  21895   -353   -518   1900       C  
ATOM   4148  C   VAL B 160     -32.808 -34.746  17.448  1.00151.01           C  
ANISOU 4148  C   VAL B 160    15968  18930  22480   -519   -553   1700       C  
ATOM   4149  O   VAL B 160     -32.407 -33.728  18.047  1.00152.55           O  
ANISOU 4149  O   VAL B 160    16219  19241  22501   -596   -775   1536       O  
ATOM   4150  CB  VAL B 160     -34.082 -36.617  18.566  1.00151.69           C  
ANISOU 4150  CB  VAL B 160    15948  19315  22373   -229   -706   2280       C  
ATOM   4151  CG1 VAL B 160     -32.917 -36.499  19.533  1.00155.11           C  
ANISOU 4151  CG1 VAL B 160    16109  19906  22920   -235  -1037   2326       C  
ATOM   4152  CG2 VAL B 160     -35.374 -36.875  19.319  1.00151.09           C  
ANISOU 4152  CG2 VAL B 160    16034  19535  21839    -96   -780   2505       C  
ATOM   4153  N   ALA B 161     -32.067 -35.391  16.554  1.00150.01           N  
ANISOU 4153  N   ALA B 161    15607  18546  22843   -572   -337   1705       N  
ATOM   4154  CA  ALA B 161     -30.693 -35.011  16.257  1.00152.35           C  
ANISOU 4154  CA  ALA B 161    15636  18725  23527   -730   -327   1563       C  
ATOM   4155  C   ALA B 161     -30.557 -33.619  15.644  1.00151.95           C  
ANISOU 4155  C   ALA B 161    15826  18548  23361   -936   -194   1268       C  
ATOM   4156  O   ALA B 161     -29.483 -33.034  15.686  1.00154.49           O  
ANISOU 4156  O   ALA B 161    15946  18829  23922  -1114   -267   1152       O  
ATOM   4157  CB  ALA B 161     -30.052 -36.050  15.336  1.00152.30           C  
ANISOU 4157  CB  ALA B 161    15339  18494  24035   -696    -71   1619       C  
ATOM   4158  N   SER B 162     -31.625 -33.084  15.068  1.00149.59           N  
ANISOU 4158  N   SER B 162    15946  18173  22717   -921     -9   1158       N  
ATOM   4159  CA  SER B 162     -31.538 -31.736  14.521  1.00149.57           C  
ANISOU 4159  CA  SER B 162    16217  18020  22595  -1105     93    910       C  
ATOM   4160  C   SER B 162     -31.264 -30.763  15.653  1.00151.71           C  
ANISOU 4160  C   SER B 162    16534  18444  22665  -1178   -296    803       C  
ATOM   4161  O   SER B 162     -30.279 -30.023  15.630  1.00154.27           O  
ANISOU 4161  O   SER B 162    16736  18663  23217  -1400   -369    671       O  
ATOM   4162  CB  SER B 162     -32.816 -31.342  13.790  1.00154.10           C  
ANISOU 4162  CB  SER B 162    17252  18506  22795  -1024    309    820       C  
ATOM   4163  OG  SER B 162     -33.883 -31.159  14.705  1.00153.02           O  
ANISOU 4163  OG  SER B 162    17338  18607  22195   -857     75    847       O  
ATOM   4164  N   GLY B 163     -32.132 -30.793  16.658  1.00152.10           N  
ANISOU 4164  N   GLY B 163    16742  18758  22292   -989   -551    860       N  
ATOM   4165  CA  GLY B 163     -31.998 -29.926  17.810  1.00154.35           C  
ANISOU 4165  CA  GLY B 163    17107  19231  22307   -994   -950    731       C  
ATOM   4166  C   GLY B 163     -30.741 -30.256  18.582  1.00157.87           C  
ANISOU 4166  C   GLY B 163    17114  19792  23076  -1070  -1238    799       C  
ATOM   4167  O   GLY B 163     -30.029 -29.351  19.055  1.00160.72           O  
ANISOU 4167  O   GLY B 163    17443  20143  23481  -1224  -1505    604       O  
ATOM   4168  N   ALA B 164     -30.458 -31.552  18.701  1.00155.95           N  
ANISOU 4168  N   ALA B 164    16530  19639  23085   -960  -1207   1068       N  
ATOM   4169  CA  ALA B 164     -29.241 -31.981  19.379  1.00159.51           C  
ANISOU 4169  CA  ALA B 164    16530  20201  23877   -995  -1481   1156       C  
ATOM   4170  C   ALA B 164     -28.024 -31.302  18.764  1.00161.77           C  
ANISOU 4170  C   ALA B 164    16601  20260  24606  -1285  -1416    954       C  
ATOM   4171  O   ALA B 164     -27.350 -30.523  19.426  1.00164.86           O  
ANISOU 4171  O   ALA B 164    16903  20720  25018  -1420  -1741    794       O  
ATOM   4172  CB  ALA B 164     -29.095 -33.492  19.317  1.00163.10           C  
ANISOU 4172  CB  ALA B 164    16670  20681  24617   -834  -1391   1470       C  
ATOM   4173  N   PHE B 165     -27.793 -31.557  17.480  1.00160.51           N  
ANISOU 4173  N   PHE B 165    16373  19836  24777  -1387   -990    952       N  
ATOM   4174  CA  PHE B 165     -26.640 -31.013  16.770  1.00162.94           C  
ANISOU 4174  CA  PHE B 165    16434  19949  25527  -1672   -841    813       C  
ATOM   4175  C   PHE B 165     -26.601 -29.506  16.791  1.00164.08           C  
ANISOU 4175  C   PHE B 165    16856  19969  25517  -1924   -946    563       C  
ATOM   4176  O   PHE B 165     -25.537 -28.917  16.925  1.00167.70           O  
ANISOU 4176  O   PHE B 165    17050  20378  26291  -2176  -1090    452       O  
ATOM   4177  CB  PHE B 165     -26.629 -31.460  15.311  1.00161.23           C  
ANISOU 4177  CB  PHE B 165    16200  19500  25559  -1699   -313    843       C  
ATOM   4178  CG  PHE B 165     -26.220 -32.875  15.118  1.00161.61           C  
ANISOU 4178  CG  PHE B 165    15862  19588  25953  -1511   -202   1029       C  
ATOM   4179  CD1 PHE B 165     -25.709 -33.606  16.174  1.00163.85           C  
ANISOU 4179  CD1 PHE B 165    15794  20079  26383  -1372   -561   1180       C  
ATOM   4180  CD2 PHE B 165     -26.309 -33.466  13.871  1.00160.19           C  
ANISOU 4180  CD2 PHE B 165    15680  19230  25954  -1457    245   1042       C  
ATOM   4181  CE1 PHE B 165     -25.323 -34.908  15.999  1.00164.60           C  
ANISOU 4181  CE1 PHE B 165    15553  20167  26822  -1178   -481   1353       C  
ATOM   4182  CE2 PHE B 165     -25.923 -34.764  13.689  1.00160.96           C  
ANISOU 4182  CE2 PHE B 165    15441  19328  26390  -1260    325   1177       C  
ATOM   4183  CZ  PHE B 165     -25.432 -35.490  14.756  1.00163.16           C  
ANISOU 4183  CZ  PHE B 165    15378  19778  26839  -1120    -41   1340       C  
ATOM   4184  N   ASN B 166     -27.758 -28.880  16.635  1.00161.33           N  
ANISOU 4184  N   ASN B 166    17033  19552  24712  -1858   -881    470       N  
ATOM   4185  CA  ASN B 166     -27.805 -27.432  16.675  1.00162.63           C  
ANISOU 4185  CA  ASN B 166    17521  19551  24719  -2064  -1010    226       C  
ATOM   4186  C   ASN B 166     -27.278 -26.897  18.005  1.00166.23           C  
ANISOU 4186  C   ASN B 166    17858  20182  25121  -2111  -1556     90       C  
ATOM   4187  O   ASN B 166     -26.555 -25.897  18.043  1.00169.48           O  
ANISOU 4187  O   ASN B 166    18242  20421  25731  -2400  -1716   -100       O  
ATOM   4188  CB  ASN B 166     -29.214 -26.934  16.409  1.00159.29           C  
ANISOU 4188  CB  ASN B 166    17677  19065  23781  -1904   -899    149       C  
ATOM   4189  CG  ASN B 166     -29.261 -25.443  16.239  1.00160.78           C  
ANISOU 4189  CG  ASN B 166    18238  18995  23857  -2108   -982    -98       C  
ATOM   4190  OD1 ASN B 166     -28.261 -24.818  15.884  1.00163.82           O  
ANISOU 4190  OD1 ASN B 166    18468  19157  24619  -2435   -963   -172       O  
ATOM   4191  ND2 ASN B 166     -30.426 -24.859  16.472  1.00159.01           N  
ANISOU 4191  ND2 ASN B 166    18499  18786  23132  -1917  -1072   -221       N  
ATOM   4192  N   GLN B 167     -27.650 -27.549  19.100  1.00166.06           N  
ANISOU 4192  N   GLN B 167    17774  20501  24822  -1833  -1856    190       N  
ATOM   4193  CA  GLN B 167     -27.119 -27.136  20.396  1.00169.89           C  
ANISOU 4193  CA  GLN B 167    18130  21201  25219  -1836  -2399     59       C  
ATOM   4194  C   GLN B 167     -25.640 -27.518  20.590  1.00173.81           C  
ANISOU 4194  C   GLN B 167    18030  21737  26275  -2016  -2562    109       C  
ATOM   4195  O   GLN B 167     -24.894 -26.808  21.269  1.00177.88           O  
ANISOU 4195  O   GLN B 167    18411  22283  26893  -2181  -2964    -89       O  
ATOM   4196  CB  GLN B 167     -27.963 -27.714  21.534  1.00169.97           C  
ANISOU 4196  CB  GLN B 167    18257  21612  24711  -1468  -2659    181       C  
ATOM   4197  CG  GLN B 167     -27.643 -27.115  22.910  1.00173.99           C  
ANISOU 4197  CG  GLN B 167    18765  22380  24963  -1413  -3239    -10       C  
ATOM   4198  CD  GLN B 167     -27.707 -25.585  22.948  1.00175.75           C  
ANISOU 4198  CD  GLN B 167    19352  22384  25041  -1588  -3431   -407       C  
ATOM   4199  OE1 GLN B 167     -27.036 -24.950  23.759  1.00179.99           O  
ANISOU 4199  OE1 GLN B 167    19804  22984  25600  -1681  -3889   -636       O  
ATOM   4200  NE2 GLN B 167     -28.527 -24.994  22.083  1.00172.83           N  
ANISOU 4200  NE2 GLN B 167    19399  21743  24524  -1620  -3109   -497       N  
ATOM   4201  N   MET B 168     -25.222 -28.639  20.005  1.00172.95           N  
ANISOU 4201  N   MET B 168    17553  21628  26532  -1968  -2274    351       N  
ATOM   4202  CA  MET B 168     -23.824 -29.065  20.081  1.00176.78           C  
ANISOU 4202  CA  MET B 168    17432  22158  27578  -2103  -2383    403       C  
ATOM   4203  C   MET B 168     -22.940 -28.058  19.348  1.00179.44           C  
ANISOU 4203  C   MET B 168    17637  22217  28324  -2523  -2256    206       C  
ATOM   4204  O   MET B 168     -21.805 -27.821  19.737  1.00183.92           O  
ANISOU 4204  O   MET B 168    17779  22838  29265  -2721  -2526    123       O  
ATOM   4205  CB  MET B 168     -23.642 -30.474  19.488  1.00175.33           C  
ANISOU 4205  CB  MET B 168    16926  21993  27699  -1925  -2059    680       C  
ATOM   4206  CG  MET B 168     -24.606 -31.510  20.062  1.00172.71           C  
ANISOU 4206  CG  MET B 168    16754  21865  27003  -1551  -2123    925       C  
ATOM   4207  SD  MET B 168     -24.364 -33.248  19.611  1.00172.03           S  
ANISOU 4207  SD  MET B 168    16293  21771  27300  -1308  -1879   1250       S  
ATOM   4208  CE  MET B 168     -23.088 -33.727  20.757  1.00177.41           C  
ANISOU 4208  CE  MET B 168    16402  22717  28287  -1232  -2389   1345       C  
ATOM   4209  N   TYR B 169     -23.472 -27.465  18.286  1.00177.01           N  
ANISOU 4209  N   TYR B 169    17690  21619  27945  -2665  -1850    147       N  
ATOM   4210  CA  TYR B 169     -22.756 -26.446  17.533  1.00179.64           C  
ANISOU 4210  CA  TYR B 169    17970  21661  28624  -3083  -1687      8       C  
ATOM   4211  C   TYR B 169     -22.917 -25.079  18.166  1.00181.78           C  
ANISOU 4211  C   TYR B 169    18588  21803  28679  -3270  -2079   -261       C  
ATOM   4212  O   TYR B 169     -22.143 -24.169  17.893  1.00185.46           O  
ANISOU 4212  O   TYR B 169    18942  22042  29484  -3660  -2116   -390       O  
ATOM   4213  CB  TYR B 169     -23.257 -26.403  16.091  1.00176.55           C  
ANISOU 4213  CB  TYR B 169    17847  21013  28222  -3136  -1081     86       C  
ATOM   4214  CG  TYR B 169     -22.641 -27.449  15.202  1.00176.48           C  
ANISOU 4214  CG  TYR B 169    17400  21043  28613  -3097   -654    272       C  
ATOM   4215  CD1 TYR B 169     -23.382 -28.539  14.780  1.00172.55           C  
ANISOU 4215  CD1 TYR B 169    17005  20612  27944  -2763   -384    424       C  
ATOM   4216  CD2 TYR B 169     -21.310 -27.381  14.829  1.00180.80           C  
ANISOU 4216  CD2 TYR B 169    17402  21573  29719  -3378   -544    283       C  
ATOM   4217  CE1 TYR B 169     -22.830 -29.516  13.985  1.00172.85           C  
ANISOU 4217  CE1 TYR B 169    16665  20672  28340  -2686    -22    551       C  
ATOM   4218  CE2 TYR B 169     -20.746 -28.355  14.023  1.00181.12           C  
ANISOU 4218  CE2 TYR B 169    17032  21678  30107  -3291   -147    425       C  
ATOM   4219  CZ  TYR B 169     -21.514 -29.422  13.609  1.00177.12           C  
ANISOU 4219  CZ  TYR B 169    16681  21213  29403  -2929    103    545       C  
ATOM   4220  OH  TYR B 169     -20.972 -30.402  12.814  1.00177.76           O  
ANISOU 4220  OH  TYR B 169    16381  21339  29819  -2805    474    644       O  
ATOM   4221  N   SER B 170     -23.924 -24.933  19.016  1.00179.89           N  
ANISOU 4221  N   SER B 170    18763  21706  27881  -2991  -2374   -350       N  
ATOM   4222  CA  SER B 170     -24.155 -23.647  19.657  1.00182.12           C  
ANISOU 4222  CA  SER B 170    19418  21866  27915  -3102  -2772   -651       C  
ATOM   4223  C   SER B 170     -23.351 -23.521  20.944  1.00186.84           C  
ANISOU 4223  C   SER B 170    19697  22695  28597  -3131  -3385   -805       C  
ATOM   4224  O   SER B 170     -22.375 -22.777  21.007  1.00191.43           O  
ANISOU 4224  O   SER B 170    20053  23106  29576  -3494  -3606   -974       O  
ATOM   4225  CB  SER B 170     -25.644 -23.448  19.947  1.00178.41           C  
ANISOU 4225  CB  SER B 170    19555  21463  26770  -2761  -2794   -716       C  
ATOM   4226  OG  SER B 170     -25.874 -22.207  20.594  1.00180.95           O  
ANISOU 4226  OG  SER B 170    20252  21664  26837  -2817  -3199  -1045       O  
ATOM   4227  N   ASN B 171     -23.773 -24.248  21.972  1.00186.04           N  
ANISOU 4227  N   ASN B 171    19578  22993  28116  -2754  -3667   -735       N  
ATOM   4228  CA  ASN B 171     -23.109 -24.200  23.270  1.00190.57           C  
ANISOU 4228  CA  ASN B 171    19889  23852  28668  -2708  -4280   -872       C  
ATOM   4229  C   ASN B 171     -22.282 -25.448  23.502  1.00191.74           C  
ANISOU 4229  C   ASN B 171    19424  24278  29150  -2609  -4308   -604       C  
ATOM   4230  O   ASN B 171     -21.566 -25.549  24.497  1.00195.90           O  
ANISOU 4230  O   ASN B 171    19637  25060  29737  -2573  -4806   -674       O  
ATOM   4231  CB  ASN B 171     -24.121 -24.043  24.403  1.00189.99           C  
ANISOU 4231  CB  ASN B 171    20241  24078  27870  -2330  -4638   -993       C  
ATOM   4232  CG  ASN B 171     -24.799 -22.685  24.401  1.00190.29           C  
ANISOU 4232  CG  ASN B 171    20859  23858  27587  -2395  -4754  -1343       C  
ATOM   4233  OD1 ASN B 171     -24.144 -21.644  24.329  1.00194.07           O  
ANISOU 4233  OD1 ASN B 171    21347  24031  28358  -2736  -4978  -1622       O  
ATOM   4234  ND2 ASN B 171     -26.124 -22.692  24.499  1.00186.71           N  
ANISOU 4234  ND2 ASN B 171    20881  23519  26541  -2064  -4617  -1329       N  
ATOM   4235  N   GLY B 172     -22.402 -26.405  22.590  1.00188.32           N  
ANISOU 4235  N   GLY B 172    18838  23795  28919  -2536  -3797   -309       N  
ATOM   4236  CA  GLY B 172     -21.697 -27.665  22.716  1.00189.28           C  
ANISOU 4236  CA  GLY B 172    18413  24136  29368  -2392  -3787    -44       C  
ATOM   4237  C   GLY B 172     -20.232 -27.522  22.345  1.00193.71           C  
ANISOU 4237  C   GLY B 172    18380  24599  30623  -2727  -3809   -104       C  
ATOM   4238  O   GLY B 172     -19.681 -26.416  22.351  1.00197.07           O  
ANISOU 4238  O   GLY B 172    18781  24854  31244  -3080  -3995   -363       O  
ATOM   4239  N   PHE B 173     -19.589 -28.648  22.054  1.00194.20           N  
ANISOU 4239  N   PHE B 173    17942  24769  31076  -2614  -3638    132       N  
ATOM   4240  CA  PHE B 173     -18.157 -28.657  21.774  1.00198.91           C  
ANISOU 4240  CA  PHE B 173    17880  25354  32341  -2876  -3664     97       C  
ATOM   4241  C   PHE B 173     -17.767 -28.451  20.307  1.00198.38           C  
ANISOU 4241  C   PHE B 173    17665  24995  32714  -3174  -3056    115       C  
ATOM   4242  O   PHE B 173     -16.652 -28.020  20.007  1.00202.79           O  
ANISOU 4242  O   PHE B 173    17756  25500  33793  -3512  -3052     27       O  
ATOM   4243  CB  PHE B 173     -17.559 -29.965  22.291  1.00200.70           C  
ANISOU 4243  CB  PHE B 173    17597  25875  32783  -2562  -3843    324       C  
ATOM   4244  CG  PHE B 173     -18.433 -31.179  22.072  1.00196.14           C  
ANISOU 4244  CG  PHE B 173    17225  25337  31962  -2163  -3553    620       C  
ATOM   4245  CD1 PHE B 173     -18.433 -31.849  20.860  1.00193.78           C  
ANISOU 4245  CD1 PHE B 173    16817  24852  31958  -2133  -2978    757       C  
ATOM   4246  CD2 PHE B 173     -19.217 -31.677  23.103  1.00194.83           C  
ANISOU 4246  CD2 PHE B 173    17337  25406  31283  -1818  -3871    764       C  
ATOM   4247  CE1 PHE B 173     -19.215 -32.972  20.673  1.00190.13           C  
ANISOU 4247  CE1 PHE B 173    16534  24389  31315  -1785  -2758   1005       C  
ATOM   4248  CE2 PHE B 173     -19.995 -32.797  22.919  1.00191.25           C  
ANISOU 4248  CE2 PHE B 173    17044  24963  30658  -1495  -3623   1058       C  
ATOM   4249  CZ  PHE B 173     -19.987 -33.446  21.708  1.00188.92           C  
ANISOU 4249  CZ  PHE B 173    16644  24437  30700  -1486  -3086   1167       C  
ATOM   4250  N   CYS B 174     -18.684 -28.767  19.403  1.00193.37           N  
ANISOU 4250  N   CYS B 174    17415  24196  31860  -3047  -2546    237       N  
ATOM   4251  CA  CYS B 174     -18.416 -28.721  17.966  1.00192.68           C  
ANISOU 4251  CA  CYS B 174    17229  23878  32103  -3250  -1929    285       C  
ATOM   4252  C   CYS B 174     -18.114 -27.310  17.454  1.00194.94           C  
ANISOU 4252  C   CYS B 174    17644  23893  32530  -3733  -1833    104       C  
ATOM   4253  O   CYS B 174     -18.441 -26.328  18.101  1.00195.71           O  
ANISOU 4253  O   CYS B 174    18083  23904  32373  -3871  -2201    -82       O  
ATOM   4254  CB  CYS B 174     -19.593 -29.320  17.206  1.00186.92           C  
ANISOU 4254  CB  CYS B 174    16955  23041  31025  -2982  -1482    422       C  
ATOM   4255  SG  CYS B 174     -19.742 -31.101  17.429  1.00185.15           S  
ANISOU 4255  SG  CYS B 174    16481  23030  30838  -2490  -1455    679       S  
ATOM   4256  N   GLN B 175     -17.472 -27.215  16.296  1.00196.46           N  
ANISOU 4256  N   GLN B 175    17564  23950  33133  -3985  -1340    164       N  
ATOM   4257  CA  GLN B 175     -16.959 -25.933  15.808  1.00199.92           C  
ANISOU 4257  CA  GLN B 175    18007  24136  33819  -4499  -1245     53       C  
ATOM   4258  C   GLN B 175     -17.569 -25.433  14.496  1.00197.31           C  
ANISOU 4258  C   GLN B 175    18128  23506  33336  -4639   -653    120       C  
ATOM   4259  O   GLN B 175     -18.137 -26.205  13.747  1.00193.46           O  
ANISOU 4259  O   GLN B 175    17794  23040  32670  -4360   -228    251       O  
ATOM   4260  CB  GLN B 175     -15.447 -26.033  15.670  1.00205.94           C  
ANISOU 4260  CB  GLN B 175    17958  25030  35260  -4777  -1224     77       C  
ATOM   4261  CG  GLN B 175     -14.783 -26.374  16.978  1.00209.33           C  
ANISOU 4261  CG  GLN B 175    17939  25744  35852  -4672  -1868    -11       C  
ATOM   4262  CD  GLN B 175     -13.552 -27.222  16.794  1.00213.32           C  
ANISOU 4262  CD  GLN B 175    17607  26508  36936  -4639  -1760     93       C  
ATOM   4263  OE1 GLN B 175     -12.832 -27.078  15.808  1.00216.00           O  
ANISOU 4263  OE1 GLN B 175    17574  26798  37698  -4910  -1299    158       O  
ATOM   4264  NE2 GLN B 175     -13.305 -28.125  17.739  1.00214.06           N  
ANISOU 4264  NE2 GLN B 175    17396  26896  37043  -4287  -2177    121       N  
ATOM   4265  N   LEU B 176     -17.419 -24.132  14.229  1.00199.93           N  
ANISOU 4265  N   LEU B 176    18669  23545  33750  -5076   -655     29       N  
ATOM   4266  CA  LEU B 176     -17.984 -23.468  13.037  1.00198.24           C  
ANISOU 4266  CA  LEU B 176    18938  23015  33371  -5244   -149    105       C  
ATOM   4267  C   LEU B 176     -16.991 -22.631  12.204  1.00203.64           C  
ANISOU 4267  C   LEU B 176    19330  23502  34542  -5795    163    182       C  
ATOM   4268  O   LEU B 176     -15.964 -22.207  12.701  1.00209.04           O  
ANISOU 4268  O   LEU B 176    19535  24211  35679  -6139   -128    115       O  
ATOM   4269  CB  LEU B 176     -19.119 -22.523  13.461  1.00195.73           C  
ANISOU 4269  CB  LEU B 176    19390  22435  32545  -5210   -440    -53       C  
ATOM   4270  CG  LEU B 176     -20.201 -23.032  14.406  1.00191.18           C  
ANISOU 4270  CG  LEU B 176    19177  22036  31427  -4732   -799   -147       C  
ATOM   4271  CD1 LEU B 176     -20.754 -21.828  15.133  1.00191.99           C  
ANISOU 4271  CD1 LEU B 176    19797  21917  31234  -4833  -1255   -385       C  
ATOM   4272  CD2 LEU B 176     -21.305 -23.788  13.680  1.00185.33           C  
ANISOU 4272  CD2 LEU B 176    18805  21330  30281  -4350   -377    -12       C  
ATOM   4273  N   ASP B 177     -17.297 -22.430  10.922  1.00202.49           N  
ANISOU 4273  N   ASP B 177    19455  23182  34300  -5874    763    341       N  
ATOM   4274  CA  ASP B 177     -16.502 -21.568  10.031  1.00207.63           C  
ANISOU 4274  CA  ASP B 177    19925  23629  35336  -6404   1130    474       C  
ATOM   4275  C   ASP B 177     -17.337 -20.704   9.088  1.00206.03           C  
ANISOU 4275  C   ASP B 177    20440  23053  34788  -6522   1476    569       C  
ATOM   4276  O   ASP B 177     -18.466 -21.054   8.749  1.00200.55           O  
ANISOU 4276  O   ASP B 177    20281  22339  33581  -6133   1632    572       O  
ATOM   4277  CB  ASP B 177     -15.531 -22.378   9.193  1.00210.25           C  
ANISOU 4277  CB  ASP B 177    19574  24248  36064  -6426   1662    656       C  
ATOM   4278  CG  ASP B 177     -14.188 -22.542   9.869  1.00215.92           C  
ANISOU 4278  CG  ASP B 177    19449  25200  37389  -6658   1376    610       C  
ATOM   4279  OD1 ASP B 177     -13.465 -21.532  10.066  1.00221.45           O  
ANISOU 4279  OD1 ASP B 177    19942  25728  38472  -7191   1192    593       O  
ATOM   4280  OD2 ASP B 177     -13.879 -23.697  10.228  1.00215.02           O  
ANISOU 4280  OD2 ASP B 177    18887  25433  37380  -6298   1303    587       O  
ATOM   4281  N   GLU B 178     -16.762 -19.566   8.693  1.00211.26           N  
ANISOU 4281  N   GLU B 178    21097  23416  35756  -7071   1568    656       N  
ATOM   4282  CA  GLU B 178     -17.354 -18.606   7.747  1.00211.33           C  
ANISOU 4282  CA  GLU B 178    21742  23027  35525  -7267   1900    798       C  
ATOM   4283  C   GLU B 178     -18.840 -18.256   7.939  1.00205.88           C  
ANISOU 4283  C   GLU B 178    21930  22096  34198  -6925   1685    665       C  
ATOM   4284  O   GLU B 178     -19.606 -18.277   6.966  1.00202.97           O  
ANISOU 4284  O   GLU B 178    22029  21637  33453  -6742   2111    800       O  
ATOM   4285  CB  GLU B 178     -17.173 -19.107   6.304  1.00211.43           C  
ANISOU 4285  CB  GLU B 178    21628  23190  35514  -7227   2691   1080       C  
ATOM   4286  CG  GLU B 178     -15.784 -18.994   5.714  1.00218.26           C  
ANISOU 4286  CG  GLU B 178    21779  24181  36969  -7692   3080   1293       C  
ATOM   4287  CD  GLU B 178     -15.786 -19.272   4.220  1.00218.62           C  
ANISOU 4287  CD  GLU B 178    21871  24333  36860  -7640   3879   1568       C  
ATOM   4288  OE1 GLU B 178     -16.867 -19.612   3.698  1.00213.31           O  
ANISOU 4288  OE1 GLU B 178    21777  23636  35634  -7223   4074   1563       O  
ATOM   4289  OE2 GLU B 178     -14.726 -19.140   3.567  1.00224.47           O  
ANISOU 4289  OE2 GLU B 178    22073  25201  38015  -8009   4308   1786       O  
ATOM   4290  N   ALA B 179     -19.244 -17.967   9.177  1.00204.77           N  
ANISOU 4290  N   ALA B 179    21992  21890  33920  -6809   1030    392       N  
ATOM   4291  CA  ALA B 179     -20.630 -17.593   9.497  1.00200.21           C  
ANISOU 4291  CA  ALA B 179    22197  21124  32750  -6469    777    231       C  
ATOM   4292  C   ALA B 179     -21.662 -18.709   9.282  1.00193.40           C  
ANISOU 4292  C   ALA B 179    21542  20558  31384  -5876    986    247       C  
ATOM   4293  O   ALA B 179     -22.636 -18.804  10.032  1.00189.62           O  
ANISOU 4293  O   ALA B 179    21438  20130  30481  -5515    632     64       O  
ATOM   4294  CB  ALA B 179     -21.044 -16.335   8.693  1.00202.09           C  
ANISOU 4294  CB  ALA B 179    23057  20851  32878  -6739    961    331       C  
ATOM   4295  N   GLY B 180     -21.462 -19.555   8.277  1.00192.19           N  
ANISOU 4295  N   GLY B 180    21141  20607  31277  -5771   1552    455       N  
ATOM   4296  CA  GLY B 180     -22.438 -20.592   7.991  1.00186.26           C  
ANISOU 4296  CA  GLY B 180    20597  20084  30090  -5246   1746    462       C  
ATOM   4297  C   GLY B 180     -21.928 -22.016   8.059  1.00185.15           C  
ANISOU 4297  C   GLY B 180    19851  20351  30146  -5006   1885    509       C  
ATOM   4298  O   GLY B 180     -22.556 -22.881   8.665  1.00181.15           O  
ANISOU 4298  O   GLY B 180    19373  20058  29399  -4603   1675    428       O  
ATOM   4299  N   ASN B 181     -20.773 -22.252   7.450  1.00189.14           N  
ANISOU 4299  N   ASN B 181    19798  20962  31106  -5254   2236    649       N  
ATOM   4300  CA  ASN B 181     -20.289 -23.605   7.212  1.00188.53           C  
ANISOU 4300  CA  ASN B 181    19180  21236  31217  -4993   2484    706       C  
ATOM   4301  C   ASN B 181     -19.852 -24.319   8.497  1.00188.69           C  
ANISOU 4301  C   ASN B 181    18728  21509  31456  -4842   1985    594       C  
ATOM   4302  O   ASN B 181     -18.960 -23.844   9.212  1.00192.95           O  
ANISOU 4302  O   ASN B 181    18882  22059  32370  -5150   1658    542       O  
ATOM   4303  CB  ASN B 181     -19.111 -23.564   6.228  1.00193.64           C  
ANISOU 4303  CB  ASN B 181    19324  21955  32295  -5302   3002    875       C  
ATOM   4304  CG  ASN B 181     -19.479 -22.939   4.885  1.00194.06           C  
ANISOU 4304  CG  ASN B 181    19824  21805  32107  -5433   3546   1034       C  
ATOM   4305  OD1 ASN B 181     -20.590 -23.121   4.375  1.00189.65           O  
ANISOU 4305  OD1 ASN B 181    19826  21174  31057  -5120   3693   1021       O  
ATOM   4306  ND2 ASN B 181     -18.544 -22.176   4.318  1.00199.80           N  
ANISOU 4306  ND2 ASN B 181    20295  22443  33177  -5909   3834   1199       N  
ATOM   4307  N   ARG B 182     -20.503 -25.438   8.807  1.00184.37           N  
ANISOU 4307  N   ARG B 182    18226  21154  30672  -4376   1902    565       N  
ATOM   4308  CA  ARG B 182     -20.130 -26.232   9.978  1.00184.61           C  
ANISOU 4308  CA  ARG B 182    17831  21436  30876  -4184   1456    510       C  
ATOM   4309  C   ARG B 182     -19.060 -27.278   9.710  1.00187.29           C  
ANISOU 4309  C   ARG B 182    17454  22028  31681  -4096   1669    590       C  
ATOM   4310  O   ARG B 182     -19.111 -27.983   8.703  1.00186.29           O  
ANISOU 4310  O   ARG B 182    17276  21949  31555  -3910   2151    663       O  
ATOM   4311  CB  ARG B 182     -21.341 -26.938  10.549  1.00180.94           C  
ANISOU 4311  CB  ARG B 182    17748  21049  29953  -3740   1228    478       C  
ATOM   4312  CG  ARG B 182     -22.414 -26.005  10.973  1.00178.49           C  
ANISOU 4312  CG  ARG B 182    18089  20558  29172  -3751    967    374       C  
ATOM   4313  CD  ARG B 182     -23.502 -26.754  11.698  1.00174.05           C  
ANISOU 4313  CD  ARG B 182    17784  20149  28199  -3328    713    362       C  
ATOM   4314  NE  ARG B 182     -24.609 -25.858  11.996  1.00171.77           N  
ANISOU 4314  NE  ARG B 182    18125  19714  27425  -3294    521    249       N  
ATOM   4315  CZ  ARG B 182     -25.763 -26.245  12.516  1.00167.95           C  
ANISOU 4315  CZ  ARG B 182    17972  19345  26498  -2958    350    235       C  
ATOM   4316  NH1 ARG B 182     -25.973 -27.527  12.793  1.00165.97           N  
ANISOU 4316  NH1 ARG B 182    17499  19321  26239  -2657    343    352       N  
ATOM   4317  NH2 ARG B 182     -26.707 -25.346  12.753  1.00166.50           N  
ANISOU 4317  NH2 ARG B 182    18331  19041  25892  -2923    189    110       N  
ATOM   4318  N   LEU B 183     -18.114 -27.400  10.636  1.00190.92           N  
ANISOU 4318  N   LEU B 183    17364  22657  32518  -4193   1283    554       N  
ATOM   4319  CA  LEU B 183     -17.116 -28.457  10.577  1.00193.66           C  
ANISOU 4319  CA  LEU B 183    17003  23269  33311  -4041   1387    612       C  
ATOM   4320  C   LEU B 183     -17.685 -29.799  11.012  1.00190.02           C  
ANISOU 4320  C   LEU B 183    16570  22951  32679  -3519   1240    643       C  
ATOM   4321  O   LEU B 183     -18.332 -29.879  12.055  1.00187.65           O  
ANISOU 4321  O   LEU B 183    16528  22675  32096  -3359    772    616       O  
ATOM   4322  CB  LEU B 183     -15.927 -28.100  11.456  1.00199.15           C  
ANISOU 4322  CB  LEU B 183    17096  24102  34469  -4317    973    559       C  
ATOM   4323  CG  LEU B 183     -15.288 -26.766  11.102  1.00203.61           C  
ANISOU 4323  CG  LEU B 183    17580  24498  35284  -4891   1071    540       C  
ATOM   4324  CD1 LEU B 183     -14.151 -26.495  12.064  1.00209.19           C  
ANISOU 4324  CD1 LEU B 183    17665  25355  36461  -5145    585    458       C  
ATOM   4325  CD2 LEU B 183     -14.815 -26.781   9.656  1.00205.65           C  
ANISOU 4325  CD2 LEU B 183    17640  24753  35747  -5039   1794    673       C  
ATOM   4326  N   PRO B 184     -17.377 -30.869  10.262  1.00190.25           N  
ANISOU 4326  N   PRO B 184    16297  23083  32905  -3255   1621    703       N  
ATOM   4327  CA  PRO B 184     -17.837 -32.206  10.637  1.00187.54           C  
ANISOU 4327  CA  PRO B 184    15949  22826  32481  -2775   1477    750       C  
ATOM   4328  C   PRO B 184     -17.385 -32.540  12.050  1.00189.42           C  
ANISOU 4328  C   PRO B 184    15845  23241  32884  -2684    866    771       C  
ATOM   4329  O   PRO B 184     -16.264 -32.205  12.422  1.00194.22           O  
ANISOU 4329  O   PRO B 184    15920  23984  33889  -2902    691    740       O  
ATOM   4330  CB  PRO B 184     -17.160 -33.114   9.604  1.00189.70           C  
ANISOU 4330  CB  PRO B 184    15798  23185  33096  -2584   1961    765       C  
ATOM   4331  CG  PRO B 184     -16.030 -32.303   9.056  1.00194.82           C  
ANISOU 4331  CG  PRO B 184    16011  23907  34104  -2979   2237    747       C  
ATOM   4332  CD  PRO B 184     -16.546 -30.905   9.050  1.00193.66           C  
ANISOU 4332  CD  PRO B 184    16359  23564  33659  -3380   2197    730       C  
ATOM   4333  N   CYS B 185     -18.270 -33.120  12.849  1.00186.00           N  
ANISOU 4333  N   CYS B 185    15724  22819  32127  -2388    531    833       N  
ATOM   4334  CA  CYS B 185     -17.974 -33.332  14.258  1.00187.76           C  
ANISOU 4334  CA  CYS B 185    15722  23226  32391  -2296    -76    874       C  
ATOM   4335  C   CYS B 185     -18.454 -34.707  14.702  1.00185.82           C  
ANISOU 4335  C   CYS B 185    15495  23039  32071  -1841   -226   1035       C  
ATOM   4336  O   CYS B 185     -19.537 -34.837  15.257  1.00182.28           O  
ANISOU 4336  O   CYS B 185    15508  22569  31182  -1691   -422   1109       O  
ATOM   4337  CB  CYS B 185     -18.614 -32.232  15.105  1.00186.45           C  
ANISOU 4337  CB  CYS B 185    16003  23034  31805  -2493   -460    791       C  
ATOM   4338  SG  CYS B 185     -18.164 -32.253  16.853  1.00189.60           S  
ANISOU 4338  SG  CYS B 185    16141  23702  32196  -2422  -1234    795       S  
ATOM   4339  N   PRO B 186     -17.632 -35.737  14.473  1.00188.61           N  
ANISOU 4339  N   PRO B 186    15328  23465  32870  -1617   -140   1098       N  
ATOM   4340  CA  PRO B 186     -17.996 -37.134  14.714  1.00187.46           C  
ANISOU 4340  CA  PRO B 186    15176  23301  32749  -1182   -231   1264       C  
ATOM   4341  C   PRO B 186     -18.247 -37.447  16.184  1.00187.73           C  
ANISOU 4341  C   PRO B 186    15254  23486  32590  -1021   -833   1427       C  
ATOM   4342  O   PRO B 186     -18.923 -38.430  16.477  1.00185.85           O  
ANISOU 4342  O   PRO B 186    15205  23192  32219   -714   -925   1612       O  
ATOM   4343  CB  PRO B 186     -16.781 -37.902  14.199  1.00191.87           C  
ANISOU 4343  CB  PRO B 186    15081  23923  33898  -1027    -51   1244       C  
ATOM   4344  CG  PRO B 186     -15.645 -36.950  14.361  1.00196.29           C  
ANISOU 4344  CG  PRO B 186    15176  24658  34746  -1370   -140   1127       C  
ATOM   4345  CD  PRO B 186     -16.219 -35.596  14.079  1.00193.87           C  
ANISOU 4345  CD  PRO B 186    15329  24249  34085  -1773     -2   1018       C  
ATOM   4346  N   GLU B 187     -17.693 -36.651  17.093  1.00190.51           N  
ANISOU 4346  N   GLU B 187    15424  24027  32932  -1223  -1243   1368       N  
ATOM   4347  CA  GLU B 187     -17.903 -36.891  18.516  1.00191.30           C  
ANISOU 4347  CA  GLU B 187    15576  24321  32790  -1056  -1826   1515       C  
ATOM   4348  C   GLU B 187     -19.377 -36.721  18.880  1.00186.51           C  
ANISOU 4348  C   GLU B 187    15647  23667  31552   -997  -1872   1596       C  
ATOM   4349  O   GLU B 187     -19.852 -37.310  19.852  1.00186.29           O  
ANISOU 4349  O   GLU B 187    15743  23772  31268   -756  -2213   1807       O  
ATOM   4350  CB  GLU B 187     -17.030 -35.962  19.361  1.00195.54           C  
ANISOU 4350  CB  GLU B 187    15810  25072  33413  -1300  -2269   1373       C  
ATOM   4351  CG  GLU B 187     -15.544 -36.084  19.049  1.00200.86           C  
ANISOU 4351  CG  GLU B 187    15747  25836  34736  -1383  -2244   1293       C  
ATOM   4352  CD  GLU B 187     -14.713 -34.950  19.624  1.00205.06           C  
ANISOU 4352  CD  GLU B 187    15995  26521  35398  -1739  -2602   1095       C  
ATOM   4353  OE1 GLU B 187     -15.216 -33.809  19.693  1.00203.48           O  
ANISOU 4353  OE1 GLU B 187    16200  26235  34877  -2040  -2636    941       O  
ATOM   4354  OE2 GLU B 187     -13.548 -35.204  20.005  1.00210.30           O  
ANISOU 4354  OE2 GLU B 187    16021  27378  36505  -1714  -2870   1083       O  
ATOM   4355  N   ALA B 188     -20.091 -35.922  18.085  1.00183.05           N  
ANISOU 4355  N   ALA B 188    15631  23056  30862  -1208  -1518   1446       N  
ATOM   4356  CA  ALA B 188     -21.542 -35.740  18.224  1.00178.42           C  
ANISOU 4356  CA  ALA B 188    15673  22418  29701  -1146  -1480   1496       C  
ATOM   4357  C   ALA B 188     -22.300 -37.017  17.882  1.00175.78           C  
ANISOU 4357  C   ALA B 188    15479  21970  29340   -841  -1280   1715       C  
ATOM   4358  O   ALA B 188     -23.221 -37.421  18.590  1.00173.99           O  
ANISOU 4358  O   ALA B 188    15535  21827  28748   -668  -1472   1902       O  
ATOM   4359  CB  ALA B 188     -22.020 -34.599  17.340  1.00175.92           C  
ANISOU 4359  CB  ALA B 188    15735  21921  29188  -1426  -1140   1277       C  
ATOM   4360  N   TYR B 189     -21.905 -37.635  16.776  1.00175.94           N  
ANISOU 4360  N   TYR B 189    15294  21803  29753   -784   -889   1684       N  
ATOM   4361  CA  TYR B 189     -22.456 -38.906  16.348  1.00174.30           C  
ANISOU 4361  CA  TYR B 189    15165  21432  29630   -500   -712   1848       C  
ATOM   4362  C   TYR B 189     -22.152 -39.975  17.383  1.00176.95           C  
ANISOU 4362  C   TYR B 189    15234  21875  30124   -225  -1115   2123       C  
ATOM   4363  O   TYR B 189     -23.003 -40.797  17.706  1.00175.37           O  
ANISOU 4363  O   TYR B 189    15262  21614  29758    -29  -1193   2355       O  
ATOM   4364  CB  TYR B 189     -21.857 -39.301  15.003  1.00175.17           C  
ANISOU 4364  CB  TYR B 189    15039  21353  30163   -471   -253   1704       C  
ATOM   4365  CG  TYR B 189     -22.456 -40.527  14.366  1.00173.60           C  
ANISOU 4365  CG  TYR B 189    14970  20927  30062   -193    -39   1791       C  
ATOM   4366  CD1 TYR B 189     -23.569 -40.448  13.545  1.00169.62           C  
ANISOU 4366  CD1 TYR B 189    14936  20248  29264   -216    273   1716       C  
ATOM   4367  CD2 TYR B 189     -21.907 -41.778  14.610  1.00176.50           C  
ANISOU 4367  CD2 TYR B 189    14990  21237  30834    103   -187   1941       C  
ATOM   4368  CE1 TYR B 189     -24.104 -41.589  12.961  1.00168.66           C  
ANISOU 4368  CE1 TYR B 189    14922  19897  29263     26    430   1767       C  
ATOM   4369  CE2 TYR B 189     -22.437 -42.919  14.041  1.00175.60           C  
ANISOU 4369  CE2 TYR B 189    15003  20863  30852    354    -30   2002       C  
ATOM   4370  CZ  TYR B 189     -23.532 -42.823  13.219  1.00171.71           C  
ANISOU 4370  CZ  TYR B 189    14968  20197  30075    303    274   1906       C  
ATOM   4371  OH  TYR B 189     -24.040 -43.975  12.662  1.00171.29           O  
ANISOU 4371  OH  TYR B 189    15029  19867  30185    541    390   1940       O  
ATOM   4372  N   GLY B 190     -20.932 -39.944  17.908  1.00181.35           N  
ANISOU 4372  N   GLY B 190    15299  22596  31010   -222  -1382   2112       N  
ATOM   4373  CA  GLY B 190     -20.524 -40.866  18.950  1.00184.58           C  
ANISOU 4373  CA  GLY B 190    15435  23132  31566     47  -1815   2378       C  
ATOM   4374  C   GLY B 190     -21.356 -40.706  20.204  1.00183.60           C  
ANISOU 4374  C   GLY B 190    15644  23212  30905     87  -2207   2589       C  
ATOM   4375  O   GLY B 190     -21.736 -41.688  20.842  1.00184.24           O  
ANISOU 4375  O   GLY B 190    15774  23302  30927    339  -2415   2911       O  
ATOM   4376  N   ALA B 191     -21.677 -39.462  20.534  1.00182.30           N  
ANISOU 4376  N   ALA B 191    15728  23203  30335   -157  -2293   2413       N  
ATOM   4377  CA  ALA B 191     -22.529 -39.189  21.679  1.00181.46           C  
ANISOU 4377  CA  ALA B 191    15966  23332  29648   -107  -2624   2562       C  
ATOM   4378  C   ALA B 191     -23.910 -39.749  21.407  1.00177.41           C  
ANISOU 4378  C   ALA B 191    15891  22689  28830      1  -2382   2754       C  
ATOM   4379  O   ALA B 191     -24.505 -40.406  22.259  1.00177.79           O  
ANISOU 4379  O   ALA B 191    16062  22871  28621    190  -2603   3075       O  
ATOM   4380  CB  ALA B 191     -22.598 -37.697  21.957  1.00181.08           C  
ANISOU 4380  CB  ALA B 191    16117  23429  29255   -375  -2740   2267       C  
ATOM   4381  N   LEU B 192     -24.387 -39.508  20.193  1.00173.97           N  
ANISOU 4381  N   LEU B 192    15664  21997  28439   -125  -1925   2569       N  
ATOM   4382  CA  LEU B 192     -25.681 -39.995  19.742  1.00170.20           C  
ANISOU 4382  CA  LEU B 192    15572  21366  27729    -53  -1665   2693       C  
ATOM   4383  C   LEU B 192     -25.813 -41.506  19.897  1.00171.38           C  
ANISOU 4383  C   LEU B 192    15596  21387  28134    203  -1720   3039       C  
ATOM   4384  O   LEU B 192     -26.825 -42.006  20.400  1.00170.23           O  
ANISOU 4384  O   LEU B 192    15698  21288  27692    298  -1792   3314       O  
ATOM   4385  CB  LEU B 192     -25.899 -39.597  18.282  1.00168.78           C  
ANISOU 4385  CB  LEU B 192    15551  20916  27663   -201  -1178   2414       C  
ATOM   4386  CG  LEU B 192     -27.132 -40.173  17.592  1.00165.24           C  
ANISOU 4386  CG  LEU B 192    15447  20268  27069   -126   -889   2488       C  
ATOM   4387  CD1 LEU B 192     -28.374 -39.839  18.394  1.00163.16           C  
ANISOU 4387  CD1 LEU B 192    15559  20209  26224   -122  -1043   2628       C  
ATOM   4388  CD2 LEU B 192     -27.249 -39.644  16.172  1.00162.89           C  
ANISOU 4388  CD2 LEU B 192    15309  19749  26834   -264   -442   2184       C  
ATOM   4389  N   ILE B 193     -24.785 -42.224  19.460  1.00174.07           N  
ANISOU 4389  N   ILE B 193    15541  21559  29038    316  -1683   3029       N  
ATOM   4390  CA  ILE B 193     -24.799 -43.677  19.487  1.00175.74           C  
ANISOU 4390  CA  ILE B 193    15627  21565  29581    574  -1736   3322       C  
ATOM   4391  C   ILE B 193     -24.649 -44.200  20.910  1.00179.04           C  
ANISOU 4391  C   ILE B 193    15929  22208  29889    745  -2217   3707       C  
ATOM   4392  O   ILE B 193     -25.261 -45.198  21.278  1.00179.52           O  
ANISOU 4392  O   ILE B 193    16105  22165  29941    902  -2308   4066       O  
ATOM   4393  CB  ILE B 193     -23.696 -44.254  18.591  1.00178.16           C  
ANISOU 4393  CB  ILE B 193    15534  21638  30521    690  -1559   3158       C  
ATOM   4394  CG1 ILE B 193     -23.926 -43.812  17.148  1.00175.18           C  
ANISOU 4394  CG1 ILE B 193    15309  21057  30193    547  -1055   2810       C  
ATOM   4395  CG2 ILE B 193     -23.667 -45.767  18.674  1.00180.50           C  
ANISOU 4395  CG2 ILE B 193    15712  21679  31191    990  -1667   3446       C  
ATOM   4396  CD1 ILE B 193     -25.317 -44.136  16.633  1.00171.31           C  
ANISOU 4396  CD1 ILE B 193    15279  20364  29446    541   -833   2860       C  
ATOM   4397  N   GLY B 194     -23.841 -43.519  21.714  1.00181.66           N  
ANISOU 4397  N   GLY B 194    16040  22851  30133    706  -2537   3643       N  
ATOM   4398  CA  GLY B 194     -23.653 -43.935  23.091  1.00185.22           C  
ANISOU 4398  CA  GLY B 194    16389  23567  30420    884  -3019   3994       C  
ATOM   4399  C   GLY B 194     -24.945 -43.802  23.866  1.00183.29           C  
ANISOU 4399  C   GLY B 194    16576  23528  29540    869  -3100   4247       C  
ATOM   4400  O   GLY B 194     -25.359 -44.710  24.590  1.00185.05           O  
ANISOU 4400  O   GLY B 194    16856  23789  29665   1049  -3288   4686       O  
ATOM   4401  N   THR B 195     -25.583 -42.653  23.696  1.00180.00           N  
ANISOU 4401  N   THR B 195    16456  23243  28692    658  -2946   3976       N  
ATOM   4402  CA  THR B 195     -26.844 -42.343  24.351  1.00178.09           C  
ANISOU 4402  CA  THR B 195    16615  23243  27806    643  -2975   4137       C  
ATOM   4403  C   THR B 195     -27.986 -43.253  23.893  1.00175.69           C  
ANISOU 4403  C   THR B 195    16542  22707  27505    684  -2699   4409       C  
ATOM   4404  O   THR B 195     -28.797 -43.715  24.703  1.00176.43           O  
ANISOU 4404  O   THR B 195    16796  22986  27252    775  -2820   4792       O  
ATOM   4405  CB  THR B 195     -27.228 -40.883  24.092  1.00175.19           C  
ANISOU 4405  CB  THR B 195    16511  23002  27053    427  -2846   3724       C  
ATOM   4406  OG1 THR B 195     -26.125 -40.033  24.444  1.00177.81           O  
ANISOU 4406  OG1 THR B 195    16612  23489  27458    345  -3112   3449       O  
ATOM   4407  CG2 THR B 195     -28.445 -40.504  24.908  1.00174.03           C  
ANISOU 4407  CG2 THR B 195    16736  23180  26208    463  -2922   3864       C  
ATOM   4408  N   SER B 196     -28.052 -43.498  22.589  1.00173.19           N  
ANISOU 4408  N   SER B 196    16235  21999  27570    611  -2329   4207       N  
ATOM   4409  CA  SER B 196     -29.102 -44.338  22.033  1.00171.12           C  
ANISOU 4409  CA  SER B 196    16177  21473  27366    627  -2080   4398       C  
ATOM   4410  C   SER B 196     -28.916 -45.798  22.453  1.00174.56           C  
ANISOU 4410  C   SER B 196    16438  21728  28159    826  -2264   4852       C  
ATOM   4411  O   SER B 196     -29.889 -46.487  22.759  1.00174.52           O  
ANISOU 4411  O   SER B 196    16608  21686  28015    847  -2257   5211       O  
ATOM   4412  CB  SER B 196     -29.140 -44.207  20.515  1.00168.10           C  
ANISOU 4412  CB  SER B 196    15853  20731  27286    524  -1669   4025       C  
ATOM   4413  OG  SER B 196     -27.928 -44.627  19.920  1.00170.25           O  
ANISOU 4413  OG  SER B 196    15784  20768  28134    605  -1634   3878       O  
ATOM   4414  N   ALA B 197     -27.667 -46.264  22.452  1.00177.88           N  
ANISOU 4414  N   ALA B 197    16502  22025  29058    967  -2430   4841       N  
ATOM   4415  CA  ALA B 197     -27.327 -47.595  22.955  1.00181.97           C  
ANISOU 4415  CA  ALA B 197    16838  22370  29932   1196  -2674   5275       C  
ATOM   4416  C   ALA B 197     -27.709 -47.709  24.428  1.00184.50           C  
ANISOU 4416  C   ALA B 197    17243  23070  29788   1268  -3026   5746       C  
ATOM   4417  O   ALA B 197     -28.157 -48.760  24.890  1.00186.75           O  
ANISOU 4417  O   ALA B 197    17582  23232  30141   1377  -3140   6231       O  
ATOM   4418  CB  ALA B 197     -25.853 -47.883  22.765  1.00185.39           C  
ANISOU 4418  CB  ALA B 197    16845  22686  30908   1360  -2816   5131       C  
ATOM   4419  N   CYS B 198     -27.476 -46.628  25.165  1.00184.66           N  
ANISOU 4419  N   CYS B 198    17270  23548  29345   1215  -3211   5603       N  
ATOM   4420  CA  CYS B 198     -27.911 -46.516  26.552  1.00186.92           C  
ANISOU 4420  CA  CYS B 198    17681  24289  29053   1287  -3517   5974       C  
ATOM   4421  C   CYS B 198     -29.413 -46.704  26.738  1.00184.90           C  
ANISOU 4421  C   CYS B 198    17771  24115  28367   1205  -3327   6266       C  
ATOM   4422  O   CYS B 198     -29.843 -47.525  27.549  1.00187.81           O  
ANISOU 4422  O   CYS B 198    18183  24578  28597   1312  -3483   6810       O  
ATOM   4423  CB  CYS B 198     -27.508 -45.154  27.120  1.00186.94           C  
ANISOU 4423  CB  CYS B 198    17683  24736  28610   1221  -3707   5633       C  
ATOM   4424  SG  CYS B 198     -28.384 -44.708  28.640  1.00188.60           S  
ANISOU 4424  SG  CYS B 198    18168  25570  27921   1292  -3966   5942       S  
ATOM   4425  N   CYS B 199     -30.204 -45.940  25.986  1.00180.28           N  
ANISOU 4425  N   CYS B 199    17417  23505  27576   1015  -2991   5922       N  
ATOM   4426  CA  CYS B 199     -31.652 -45.888  26.199  1.00178.38           C  
ANISOU 4426  CA  CYS B 199    17477  23439  26858    931  -2813   6129       C  
ATOM   4427  C   CYS B 199     -32.447 -46.975  25.478  1.00177.38           C  
ANISOU 4427  C   CYS B 199    17419  22888  27089    871  -2564   6375       C  
ATOM   4428  O   CYS B 199     -33.634 -47.169  25.751  1.00176.85           O  
ANISOU 4428  O   CYS B 199    17534  22960  26700    802  -2449   6655       O  
ATOM   4429  CB  CYS B 199     -32.189 -44.527  25.755  1.00174.22           C  
ANISOU 4429  CB  CYS B 199    17177  23092  25926    781  -2599   5640       C  
ATOM   4430  SG  CYS B 199     -31.506 -43.115  26.646  1.00175.51           S  
ANISOU 4430  SG  CYS B 199    17341  23749  25596    817  -2905   5314       S  
ATOM   4431  N   ALA B 200     -31.801 -47.688  24.563  1.00177.53           N  
ANISOU 4431  N   ALA B 200    17277  22400  27778    901  -2488   6260       N  
ATOM   4432  CA  ALA B 200     -32.429 -48.850  23.949  1.00177.64           C  
ANISOU 4432  CA  ALA B 200    17339  21957  28198    871  -2331   6497       C  
ATOM   4433  C   ALA B 200     -32.737 -49.867  25.032  1.00182.03           C  
ANISOU 4433  C   ALA B 200    17873  22579  28711    958  -2574   7184       C  
ATOM   4434  O   ALA B 200     -33.740 -50.572  24.982  1.00182.34           O  
ANISOU 4434  O   ALA B 200    18035  22460  28785    860  -2465   7516       O  
ATOM   4435  CB  ALA B 200     -31.532 -49.451  22.886  1.00177.98           C  
ANISOU 4435  CB  ALA B 200    17200  21472  28952    953  -2257   6233       C  
ATOM   4436  N   LEU B 201     -31.855 -49.912  26.022  1.00185.79           N  
ANISOU 4436  N   LEU B 201    18184  23301  29106   1134  -2916   7402       N  
ATOM   4437  CA  LEU B 201     -32.012 -50.763  27.189  1.00190.64           C  
ANISOU 4437  CA  LEU B 201    18782  24056  29596   1247  -3186   8086       C  
ATOM   4438  C   LEU B 201     -33.166 -50.252  28.042  1.00190.27           C  
ANISOU 4438  C   LEU B 201    18947  24555  28792   1147  -3127   8353       C  
ATOM   4439  O   LEU B 201     -33.983 -51.026  28.555  1.00192.72           O  
ANISOU 4439  O   LEU B 201    19338  24884  29004   1104  -3119   8924       O  
ATOM   4440  CB  LEU B 201     -30.710 -50.787  27.994  1.00194.75           C  
ANISOU 4440  CB  LEU B 201    19069  24758  30169   1487  -3587   8175       C  
ATOM   4441  CG  LEU B 201     -29.441 -51.120  27.205  1.00195.45           C  
ANISOU 4441  CG  LEU B 201    18884  24415  30964   1620  -3650   7846       C  
ATOM   4442  CD1 LEU B 201     -28.214 -50.717  27.999  1.00198.74           C  
ANISOU 4442  CD1 LEU B 201    19052  25166  31296   1813  -4031   7791       C  
ATOM   4443  CD2 LEU B 201     -29.386 -52.598  26.847  1.00198.39           C  
ANISOU 4443  CD2 LEU B 201    19197  24190  31990   1728  -3684   8200       C  
ATOM   4444  N   VAL B 202     -33.226 -48.930  28.166  1.00187.49           N  
ANISOU 4444  N   VAL B 202    18681  24639  27919   1109  -3076   7928       N  
ATOM   4445  CA  VAL B 202     -34.322 -48.255  28.840  1.00186.72           C  
ANISOU 4445  CA  VAL B 202    18788  25084  27073   1045  -2981   8038       C  
ATOM   4446  C   VAL B 202     -35.657 -48.696  28.237  1.00184.59           C  
ANISOU 4446  C   VAL B 202    18656  24619  26858    852  -2641   8193       C  
ATOM   4447  O   VAL B 202     -36.648 -48.852  28.953  1.00186.22           O  
ANISOU 4447  O   VAL B 202    18955  25178  26623    813  -2585   8616       O  
ATOM   4448  CB  VAL B 202     -34.167 -46.715  28.760  1.00183.54           C  
ANISOU 4448  CB  VAL B 202    18480  25029  26226   1028  -2951   7420       C  
ATOM   4449  CG1 VAL B 202     -35.457 -46.009  29.158  1.00182.04           C  
ANISOU 4449  CG1 VAL B 202    18524  25312  25330    970  -2773   7430       C  
ATOM   4450  CG2 VAL B 202     -33.008 -46.251  29.630  1.00186.66           C  
ANISOU 4450  CG2 VAL B 202    18741  25733  26448   1204  -3344   7337       C  
ATOM   4451  N   GLU B 203     -35.684 -48.923  26.926  1.00181.38           N  
ANISOU 4451  N   GLU B 203    18249  23674  26994    733  -2417   7859       N  
ATOM   4452  CA  GLU B 203     -36.920 -49.394  26.307  1.00179.74           C  
ANISOU 4452  CA  GLU B 203    18152  23250  26892    546  -2136   7980       C  
ATOM   4453  C   GLU B 203     -37.144 -50.903  26.388  1.00183.52           C  
ANISOU 4453  C   GLU B 203    18554  23311  27864    506  -2202   8563       C  
ATOM   4454  O   GLU B 203     -38.274 -51.334  26.609  1.00184.53           O  
ANISOU 4454  O   GLU B 203    18743  23515  27853    357  -2078   8948       O  
ATOM   4455  CB  GLU B 203     -37.004 -48.961  24.848  1.00175.46           C  
ANISOU 4455  CB  GLU B 203    17682  22338  26648    438  -1869   7362       C  
ATOM   4456  CG  GLU B 203     -38.360 -49.283  24.240  1.00173.74           C  
ANISOU 4456  CG  GLU B 203    17582  21977  26453    247  -1605   7426       C  
ATOM   4457  CD  GLU B 203     -39.523 -48.843  25.129  1.00174.26           C  
ANISOU 4457  CD  GLU B 203    17738  22636  25838    188  -1537   7718       C  
ATOM   4458  OE1 GLU B 203     -39.416 -47.787  25.793  1.00173.67           O  
ANISOU 4458  OE1 GLU B 203    17726  23086  25174    288  -1593   7558       O  
ATOM   4459  OE2 GLU B 203     -40.538 -49.574  25.185  1.00175.74           O  
ANISOU 4459  OE2 GLU B 203    17918  22768  26087     45  -1435   8111       O  
ATOM   4460  N   ILE B 204     -36.100 -51.709  26.203  1.00185.96           N  
ANISOU 4460  N   ILE B 204    18719  23171  28765    635  -2397   8632       N  
ATOM   4461  CA  ILE B 204     -36.272 -53.161  26.279  1.00190.06           C  
ANISOU 4461  CA  ILE B 204    19191  23223  29799    613  -2495   9183       C  
ATOM   4462  C   ILE B 204     -36.747 -53.558  27.668  1.00194.70           C  
ANISOU 4462  C   ILE B 204    19792  24217  29970    620  -2652   9935       C  
ATOM   4463  O   ILE B 204     -37.488 -54.529  27.820  1.00197.63           O  
ANISOU 4463  O   ILE B 204    20188  24356  30547    482  -2625  10468       O  
ATOM   4464  CB  ILE B 204     -34.984 -53.949  25.938  1.00192.58           C  
ANISOU 4464  CB  ILE B 204    19349  23012  30812    817  -2717   9131       C  
ATOM   4465  CG1 ILE B 204     -33.874 -53.682  26.951  1.00195.58           C  
ANISOU 4465  CG1 ILE B 204    19587  23748  30978   1062  -3044   9268       C  
ATOM   4466  CG2 ILE B 204     -34.514 -53.626  24.554  1.00188.66           C  
ANISOU 4466  CG2 ILE B 204    18825  22141  30716    824  -2530   8422       C  
ATOM   4467  CD1 ILE B 204     -32.627 -54.509  26.722  1.00198.84           C  
ANISOU 4467  CD1 ILE B 204    19802  23682  32064   1298  -3286   9271       C  
ATOM   4468  N   LEU B 205     -36.329 -52.801  28.680  1.00195.75           N  
ANISOU 4468  N   LEU B 205    19910  24960  29507    774  -2818   9981       N  
ATOM   4469  CA  LEU B 205     -36.727 -53.109  30.045  1.00200.57           C  
ANISOU 4469  CA  LEU B 205    20542  26039  29625    820  -2964  10687       C  
ATOM   4470  C   LEU B 205     -38.140 -52.598  30.319  1.00199.19           C  
ANISOU 4470  C   LEU B 205    20489  26354  28840    634  -2681  10808       C  
ATOM   4471  O   LEU B 205     -38.798 -53.026  31.267  1.00203.30           O  
ANISOU 4471  O   LEU B 205    21026  27213  29006    600  -2689  11462       O  
ATOM   4472  CB  LEU B 205     -35.730 -52.518  31.042  1.00202.80           C  
ANISOU 4472  CB  LEU B 205    20766  26812  29479   1086  -3285  10667       C  
ATOM   4473  CG  LEU B 205     -34.336 -53.147  30.971  1.00205.52           C  
ANISOU 4473  CG  LEU B 205    20938  26741  30411   1301  -3609  10670       C  
ATOM   4474  CD1 LEU B 205     -33.490 -52.725  32.164  1.00209.12           C  
ANISOU 4474  CD1 LEU B 205    21324  27735  30396   1559  -3979  10800       C  
ATOM   4475  CD2 LEU B 205     -34.422 -54.669  30.865  1.00209.62           C  
ANISOU 4475  CD2 LEU B 205    21426  26655  31565   1282  -3683  11258       C  
ATOM   4476  N   LEU B 206     -38.603 -51.683  29.476  1.00193.73           N  
ANISOU 4476  N   LEU B 206    19874  25710  28025    527  -2422  10188       N  
ATOM   4477  CA  LEU B 206     -40.000 -51.269  29.488  1.00192.14           C  
ANISOU 4477  CA  LEU B 206    19761  25872  27371    351  -2127  10233       C  
ATOM   4478  C   LEU B 206     -40.774 -51.913  28.334  1.00190.15           C  
ANISOU 4478  C   LEU B 206    19509  25053  27688     97  -1890  10165       C  
ATOM   4479  O   LEU B 206     -41.900 -51.512  28.027  1.00187.96           O  
ANISOU 4479  O   LEU B 206    19281  24982  27154    -60  -1630  10050       O  
ATOM   4480  CB  LEU B 206     -40.106 -49.742  29.424  1.00187.95           C  
ANISOU 4480  CB  LEU B 206    19339  25834  26239    429  -2024   9605       C  
ATOM   4481  CG  LEU B 206     -39.567 -48.987  30.649  1.00190.26           C  
ANISOU 4481  CG  LEU B 206    19657  26778  25854    667  -2260   9639       C  
ATOM   4482  CD1 LEU B 206     -39.621 -47.485  30.408  1.00186.06           C  
ANISOU 4482  CD1 LEU B 206    19256  26583  24857    728  -2178   8937       C  
ATOM   4483  CD2 LEU B 206     -40.313 -49.370  31.927  1.00195.31           C  
ANISOU 4483  CD2 LEU B 206    20293  27988  25929    704  -2272  10351       C  
ATOM   4484  N   ALA B 207     -40.157 -52.901  27.690  1.00191.22           N  
ANISOU 4484  N   ALA B 207    19583  24476  28594     81  -2002  10205       N  
ATOM   4485  CA  ALA B 207     -40.820 -53.663  26.636  1.00190.33           C  
ANISOU 4485  CA  ALA B 207    19476  23767  29074   -143  -1842  10160       C  
ATOM   4486  C   ALA B 207     -41.574 -54.847  27.215  1.00195.63           C  
ANISOU 4486  C   ALA B 207    20093  24303  29935   -324  -1874  10959       C  
ATOM   4487  O   ALA B 207     -42.403 -55.457  26.540  1.00195.72           O  
ANISOU 4487  O   ALA B 207    20098  23926  30339   -567  -1741  11019       O  
ATOM   4488  CB  ALA B 207     -39.808 -54.144  25.603  1.00189.26           C  
ANISOU 4488  CB  ALA B 207    19314  22918  29677    -48  -1941   9761       C  
ATOM   4489  N   PHE B 208     -41.288 -55.158  28.475  1.00200.42           N  
ANISOU 4489  N   PHE B 208    20660  25238  30253   -215  -2061  11581       N  
ATOM   4490  CA  PHE B 208     -41.843 -56.343  29.123  1.00206.46           C  
ANISOU 4490  CA  PHE B 208    21376  25851  31218   -377  -2120  12437       C  
ATOM   4491  C   PHE B 208     -43.248 -56.153  29.691  1.00207.83           C  
ANISOU 4491  C   PHE B 208    21521  26594  30853   -607  -1865  12849       C  
ATOM   4492  O   PHE B 208     -43.473 -55.344  30.591  1.00208.13           O  
ANISOU 4492  O   PHE B 208    21567  27417  30094   -493  -1803  12947       O  
ATOM   4493  CB  PHE B 208     -40.913 -56.817  30.236  1.00211.71           C  
ANISOU 4493  CB  PHE B 208    22019  26621  31799   -142  -2440  12984       C  
ATOM   4494  CG  PHE B 208     -39.729 -57.593  29.744  1.00212.99           C  
ANISOU 4494  CG  PHE B 208    22157  26047  32724     27  -2716  12874       C  
ATOM   4495  CD1 PHE B 208     -38.444 -57.103  29.910  1.00212.11           C  
ANISOU 4495  CD1 PHE B 208    22009  26046  32537    347  -2940  12527       C  
ATOM   4496  CD2 PHE B 208     -39.902 -58.814  29.112  1.00215.50           C  
ANISOU 4496  CD2 PHE B 208    22472  25557  33849   -127  -2762  13099       C  
ATOM   4497  CE1 PHE B 208     -37.348 -57.820  29.458  1.00213.68           C  
ANISOU 4497  CE1 PHE B 208    22146  25604  33440    532  -3183  12417       C  
ATOM   4498  CE2 PHE B 208     -38.813 -59.535  28.657  1.00217.08           C  
ANISOU 4498  CE2 PHE B 208    22649  25083  34748     75  -3018  12969       C  
ATOM   4499  CZ  PHE B 208     -37.533 -59.037  28.831  1.00216.16           C  
ANISOU 4499  CZ  PHE B 208    22471  25124  34533    416  -3216  12632       C  
ATOM   4500  N   VAL B 209     -44.186 -56.900  29.117  1.00208.91           N  
ANISOU 4500  N   VAL B 209    21608  26322  31447   -927  -1723  13053       N  
ATOM   4501  CA  VAL B 209     -45.574 -56.987  29.579  1.00211.37           C  
ANISOU 4501  CA  VAL B 209    21826  27066  31420  -1205  -1478  13541       C  
ATOM   4502  C   VAL B 209     -46.271 -55.633  29.816  1.00207.75           C  
ANISOU 4502  C   VAL B 209    21362  27470  30102  -1139  -1219  13181       C  
ATOM   4503  O   VAL B 209     -46.705 -55.343  30.931  1.00210.86           O  
ANISOU 4503  O   VAL B 209    21709  28596  29810  -1091  -1136  13637       O  
ATOM   4504  CB  VAL B 209     -45.676 -57.831  30.885  1.00219.01           C  
ANISOU 4504  CB  VAL B 209    22736  28245  32234  -1253  -1581  14565       C  
ATOM   4505  CG1 VAL B 209     -47.093 -58.378  31.055  1.00222.72           C  
ANISOU 4505  CG1 VAL B 209    23060  28834  32728  -1650  -1337  15149       C  
ATOM   4506  CG2 VAL B 209     -44.695 -58.991  30.855  1.00222.83           C  
ANISOU 4506  CG2 VAL B 209    23266  27948  33449  -1185  -1912  14894       C  
ATOM   4507  N   PRO B 210     -46.347 -54.776  28.786  1.00201.48           N  
ANISOU 4507  N   PRO B 210    20633  26606  29315  -1104  -1099  12354       N  
ATOM   4508  CA  PRO B 210     -47.304 -53.691  28.997  1.00199.22           C  
ANISOU 4508  CA  PRO B 210    20325  27075  28295  -1096   -837  12132       C  
ATOM   4509  C   PRO B 210     -48.271 -53.437  27.824  1.00195.37           C  
ANISOU 4509  C   PRO B 210    19807  26395  28031  -1303   -614  11653       C  
ATOM   4510  O   PRO B 210     -48.619 -52.280  27.601  1.00191.35           O  
ANISOU 4510  O   PRO B 210    19357  26326  27022  -1181   -465  11125       O  
ATOM   4511  CB  PRO B 210     -46.378 -52.488  29.180  1.00195.50           C  
ANISOU 4511  CB  PRO B 210    20001  26951  27328   -747   -937  11557       C  
ATOM   4512  CG  PRO B 210     -45.066 -52.886  28.401  1.00193.60           C  
ANISOU 4512  CG  PRO B 210    19834  25941  27785   -655  -1174  11207       C  
ATOM   4513  CD  PRO B 210     -45.259 -54.310  27.916  1.00196.66           C  
ANISOU 4513  CD  PRO B 210    20143  25594  28986   -901  -1226  11609       C  
ATOM   4514  N   PRO B 211     -48.730 -54.493  27.122  1.00197.04           N  
ANISOU 4514  N   PRO B 211    19931  25969  28965  -1603   -614  11841       N  
ATOM   4515  CA  PRO B 211     -49.293 -54.359  25.767  1.00193.07           C  
ANISOU 4515  CA  PRO B 211    19441  25078  28838  -1752   -504  11249       C  
ATOM   4516  C   PRO B 211     -50.406 -53.317  25.594  1.00190.20           C  
ANISOU 4516  C   PRO B 211    19028  25336  27904  -1768   -240  10915       C  
ATOM   4517  O   PRO B 211     -50.146 -52.228  25.074  1.00185.06           O  
ANISOU 4517  O   PRO B 211    18526  24838  26950  -1555   -192  10230       O  
ATOM   4518  CB  PRO B 211     -49.837 -55.766  25.487  1.00197.64           C  
ANISOU 4518  CB  PRO B 211    19885  25048  30159  -2109   -561  11743       C  
ATOM   4519  CG  PRO B 211     -49.027 -56.657  26.369  1.00202.65           C  
ANISOU 4519  CG  PRO B 211    20527  25462  31009  -2063   -778  12401       C  
ATOM   4520  CD  PRO B 211     -48.901 -55.866  27.627  1.00203.49           C  
ANISOU 4520  CD  PRO B 211    20630  26443  30245  -1841   -714  12668       C  
ATOM   4521  N   LYS B 212     -51.625 -53.658  26.001  1.00193.83           N  
ANISOU 4521  N   LYS B 212    19269  26130  28246  -2018    -74  11398       N  
ATOM   4522  CA  LYS B 212     -52.772 -52.771  25.836  1.00191.88           C  
ANISOU 4522  CA  LYS B 212    18926  26475  27504  -2030    174  11117       C  
ATOM   4523  C   LYS B 212     -52.650 -51.519  26.707  1.00190.47           C  
ANISOU 4523  C   LYS B 212    18828  27140  26401  -1689    268  10967       C  
ATOM   4524  O   LYS B 212     -53.296 -50.497  26.447  1.00187.51           O  
ANISOU 4524  O   LYS B 212    18466  27209  25570  -1567    429  10512       O  
ATOM   4525  CB  LYS B 212     -54.063 -53.519  26.166  1.00197.10           C  
ANISOU 4525  CB  LYS B 212    19274  27328  28287  -2392    331  11746       C  
ATOM   4526  CG  LYS B 212     -54.429 -54.603  25.162  1.00198.37           C  
ANISOU 4526  CG  LYS B 212    19345  26677  29349  -2756    238  11765       C  
ATOM   4527  CD  LYS B 212     -55.644 -55.393  25.633  1.00204.54           C  
ANISOU 4527  CD  LYS B 212    19784  27655  30279  -3158    375  12484       C  
ATOM   4528  CE  LYS B 212     -56.102 -56.407  24.593  1.00206.06           C  
ANISOU 4528  CE  LYS B 212    19880  27038  31376  -3541    255  12436       C  
ATOM   4529  NZ  LYS B 212     -57.232 -57.242  25.091  1.00212.84           N  
ANISOU 4529  NZ  LYS B 212    20378  28038  32452  -3986    369  13196       N  
ATOM   4530  N   VAL B 213     -51.815 -51.609  27.738  1.00192.94           N  
ANISOU 4530  N   VAL B 213    19206  27656  26445  -1517    140  11336       N  
ATOM   4531  CA  VAL B 213     -51.585 -50.491  28.648  1.00192.36           C  
ANISOU 4531  CA  VAL B 213    19230  28351  25505  -1178    170  11198       C  
ATOM   4532  C   VAL B 213     -51.042 -49.296  27.876  1.00185.97           C  
ANISOU 4532  C   VAL B 213    18659  27455  24548   -930    123  10299       C  
ATOM   4533  O   VAL B 213     -51.535 -48.174  28.010  1.00184.04           O  
ANISOU 4533  O   VAL B 213    18468  27773  23687   -740    251   9928       O  
ATOM   4534  CB  VAL B 213     -50.593 -50.860  29.773  1.00196.10           C  
ANISOU 4534  CB  VAL B 213    19760  28948  25801  -1023    -35  11689       C  
ATOM   4535  CG1 VAL B 213     -50.408 -49.687  30.725  1.00195.97           C  
ANISOU 4535  CG1 VAL B 213    19850  29750  24860   -665    -30  11505       C  
ATOM   4536  CG2 VAL B 213     -51.075 -52.084  30.530  1.00202.92           C  
ANISOU 4536  CG2 VAL B 213    20418  29847  26835  -1276      4  12641       C  
ATOM   4537  N   ILE B 214     -50.023 -49.553  27.061  1.00183.12           N  
ANISOU 4537  N   ILE B 214    18436  26376  24764   -927    -58   9963       N  
ATOM   4538  CA  ILE B 214     -49.437 -48.520  26.219  1.00177.43           C  
ANISOU 4538  CA  ILE B 214    17934  25483  23999   -741    -92   9154       C  
ATOM   4539  C   ILE B 214     -50.462 -47.965  25.239  1.00174.11           C  
ANISOU 4539  C   ILE B 214    17524  25079  23549   -813    107   8689       C  
ATOM   4540  O   ILE B 214     -50.520 -46.755  25.009  1.00170.66           O  
ANISOU 4540  O   ILE B 214    17245  24923  22677   -613    164   8145       O  
ATOM   4541  CB  ILE B 214     -48.225 -49.055  25.432  1.00176.52           C  
ANISOU 4541  CB  ILE B 214    17913  24580  24578   -755   -281   8927       C  
ATOM   4542  CG1 ILE B 214     -47.255 -49.776  26.366  1.00180.49           C  
ANISOU 4542  CG1 ILE B 214    18369  25010  25198   -689   -505   9442       C  
ATOM   4543  CG2 ILE B 214     -47.501 -47.923  24.730  1.00171.40           C  
ANISOU 4543  CG2 ILE B 214    17476  23839  23811   -559   -304   8165       C  
ATOM   4544  CD1 ILE B 214     -46.232 -50.611  25.634  1.00180.15           C  
ANISOU 4544  CD1 ILE B 214    18347  24167  25936   -724   -680   9353       C  
ATOM   4545  N   GLN B 215     -51.279 -48.851  24.675  1.00175.52           N  
ANISOU 4545  N   GLN B 215    17539  24950  24202  -1098    189   8908       N  
ATOM   4546  CA  GLN B 215     -52.354 -48.426  23.789  1.00173.16           C  
ANISOU 4546  CA  GLN B 215    17209  24703  23883  -1176    355   8523       C  
ATOM   4547  C   GLN B 215     -53.259 -47.422  24.497  1.00173.65           C  
ANISOU 4547  C   GLN B 215    17211  25623  23146  -1010    531   8501       C  
ATOM   4548  O   GLN B 215     -53.737 -46.470  23.878  1.00170.30           O  
ANISOU 4548  O   GLN B 215    16887  25355  22463   -880    622   7955       O  
ATOM   4549  CB  GLN B 215     -53.163 -49.626  23.292  1.00178.67           C  
ANISOU 4549  CB  GLN B 215    17684  25009  25193  -1536    384   8860       C  
ATOM   4550  CG  GLN B 215     -52.376 -50.589  22.401  1.00178.16           C  
ANISOU 4550  CG  GLN B 215    17703  24043  25948  -1670    205   8760       C  
ATOM   4551  CD  GLN B 215     -53.235 -51.723  21.857  1.00181.19           C  
ANISOU 4551  CD  GLN B 215    17888  24005  26952  -2031    199   9023       C  
ATOM   4552  OE1 GLN B 215     -54.040 -52.321  22.582  1.00185.90           O  
ANISOU 4552  OE1 GLN B 215    18232  24864  27537  -2258    267   9645       O  
ATOM   4553  NE2 GLN B 215     -53.064 -52.028  20.573  1.00178.91           N  
ANISOU 4553  NE2 GLN B 215    17708  23062  27207  -2090    114   8548       N  
ATOM   4554  N   LYS B 216     -53.483 -47.633  25.794  1.00178.16           N  
ANISOU 4554  N   LYS B 216    17629  26755  23310   -988    576   9093       N  
ATOM   4555  CA  LYS B 216     -54.304 -46.714  26.586  1.00179.44           C  
ANISOU 4555  CA  LYS B 216    17723  27795  22662   -783    750   9093       C  
ATOM   4556  C   LYS B 216     -53.575 -45.411  26.923  1.00176.60           C  
ANISOU 4556  C   LYS B 216    17649  27737  21715   -396    660   8583       C  
ATOM   4557  O   LYS B 216     -54.188 -44.340  26.963  1.00175.31           O  
ANISOU 4557  O   LYS B 216    17543  28060  21006   -174    770   8202       O  
ATOM   4558  CB  LYS B 216     -54.762 -47.385  27.887  1.00185.83           C  
ANISOU 4558  CB  LYS B 216    18276  29147  23184   -873    845   9918       C  
ATOM   4559  CG  LYS B 216     -55.533 -46.460  28.823  1.00187.92           C  
ANISOU 4559  CG  LYS B 216    18464  30391  22547   -608   1033   9937       C  
ATOM   4560  CD  LYS B 216     -56.304 -47.230  29.882  1.00194.74           C  
ANISOU 4560  CD  LYS B 216    18998  31806  23186   -769   1215  10786       C  
ATOM   4561  CE  LYS B 216     -57.006 -46.282  30.841  1.00197.18           C  
ANISOU 4561  CE  LYS B 216    19236  33143  22541   -447   1413  10769       C  
ATOM   4562  NZ  LYS B 216     -58.134 -46.933  31.555  1.00203.58           N  
ANISOU 4562  NZ  LYS B 216    19644  34543  23164   -646   1692  11507       N  
ATOM   4563  N   ILE B 217     -52.273 -45.509  27.174  1.00176.05           N  
ANISOU 4563  N   ILE B 217    17745  27370  21776   -312    441   8573       N  
ATOM   4564  CA  ILE B 217     -51.465 -44.343  27.530  1.00173.95           C  
ANISOU 4564  CA  ILE B 217    17735  27332  21027     13    308   8111       C  
ATOM   4565  C   ILE B 217     -51.179 -43.445  26.323  1.00168.31           C  
ANISOU 4565  C   ILE B 217    17260  26213  20478     87    288   7332       C  
ATOM   4566  O   ILE B 217     -51.128 -42.216  26.442  1.00166.52           O  
ANISOU 4566  O   ILE B 217    17228  26290  19754    342    270   6862       O  
ATOM   4567  CB  ILE B 217     -50.143 -44.783  28.181  1.00175.67           C  
ANISOU 4567  CB  ILE B 217    18009  27364  21373     61     59   8367       C  
ATOM   4568  CG1 ILE B 217     -50.438 -45.519  29.488  1.00181.73           C  
ANISOU 4568  CG1 ILE B 217    18584  28628  21837     42     75   9150       C  
ATOM   4569  CG2 ILE B 217     -49.235 -43.589  28.440  1.00173.56           C  
ANISOU 4569  CG2 ILE B 217    17991  27249  20704    354   -118   7837       C  
ATOM   4570  CD1 ILE B 217     -49.244 -46.218  30.084  1.00184.22           C  
ANISOU 4570  CD1 ILE B 217    18916  28703  22377     58   -183   9522       C  
ATOM   4571  N   PHE B 218     -51.032 -44.057  25.153  1.00165.92           N  
ANISOU 4571  N   PHE B 218    16954  25226  20864   -130    292   7200       N  
ATOM   4572  CA  PHE B 218     -50.846 -43.300  23.921  1.00161.03           C  
ANISOU 4572  CA  PHE B 218    16553  24222  20409    -80    306   6517       C  
ATOM   4573  C   PHE B 218     -51.916 -43.644  22.881  1.00159.88           C  
ANISOU 4573  C   PHE B 218    16315  23864  20570   -257    461   6413       C  
ATOM   4574  O   PHE B 218     -51.643 -44.378  21.928  1.00158.68           O  
ANISOU 4574  O   PHE B 218    16158  23091  21042   -442    431   6348       O  
ATOM   4575  CB  PHE B 218     -49.447 -43.555  23.352  1.00159.00           C  
ANISOU 4575  CB  PHE B 218    16424  23326  20664   -116    144   6321       C  
ATOM   4576  CG  PHE B 218     -48.328 -43.331  24.346  1.00160.56           C  
ANISOU 4576  CG  PHE B 218    16669  23693  20645     34    -50   6437       C  
ATOM   4577  CD1 PHE B 218     -47.618 -44.401  24.867  1.00163.54           C  
ANISOU 4577  CD1 PHE B 218    16903  23866  21367    -53   -192   6922       C  
ATOM   4578  CD2 PHE B 218     -48.001 -42.051  24.769  1.00159.47           C  
ANISOU 4578  CD2 PHE B 218    16720  23906  19964    271   -120   6057       C  
ATOM   4579  CE1 PHE B 218     -46.602 -44.198  25.780  1.00165.28           C  
ANISOU 4579  CE1 PHE B 218    17153  24267  21380    101   -400   7022       C  
ATOM   4580  CE2 PHE B 218     -46.982 -41.844  25.682  1.00161.27           C  
ANISOU 4580  CE2 PHE B 218    16979  24297  20000    403   -336   6136       C  
ATOM   4581  CZ  PHE B 218     -46.286 -42.918  26.188  1.00164.15           C  
ANISOU 4581  CZ  PHE B 218    17183  24494  20693    322   -476   6620       C  
ATOM   4582  N   PRO B 219     -53.142 -43.115  23.068  1.00160.63           N  
ANISOU 4582  N   PRO B 219    16324  24492  20216   -180    615   6377       N  
ATOM   4583  CA  PRO B 219     -54.259 -43.334  22.141  1.00159.96           C  
ANISOU 4583  CA  PRO B 219    16121  24299  20356   -324    741   6253       C  
ATOM   4584  C   PRO B 219     -54.040 -42.562  20.843  1.00155.23           C  
ANISOU 4584  C   PRO B 219    15804  23300  19876   -225    722   5566       C  
ATOM   4585  O   PRO B 219     -53.171 -41.698  20.824  1.00152.84           O  
ANISOU 4585  O   PRO B 219    15770  22929  19371    -32    647   5213       O  
ATOM   4586  CB  PRO B 219     -55.457 -42.789  22.918  1.00162.48           C  
ANISOU 4586  CB  PRO B 219    16269  25419  20047   -185    897   6388       C  
ATOM   4587  CG  PRO B 219     -54.879 -41.719  23.753  1.00162.11           C  
ANISOU 4587  CG  PRO B 219    16435  25779  19380    143    837   6192       C  
ATOM   4588  CD  PRO B 219     -53.516 -42.198  24.160  1.00162.36           C  
ANISOU 4588  CD  PRO B 219    16558  25473  19658     89    660   6392       C  
ATOM   4589  N   PRO B 220     -54.847 -42.818  19.801  1.00154.29           N  
ANISOU 4589  N   PRO B 220    15625  22954  20045   -350    784   5383       N  
ATOM   4590  CA  PRO B 220     -54.709 -42.092  18.531  1.00150.23           C  
ANISOU 4590  CA  PRO B 220    15393  22090  19599   -242    774   4757       C  
ATOM   4591  C   PRO B 220     -54.823 -40.570  18.682  1.00148.30           C  
ANISOU 4591  C   PRO B 220    15396  22231  18720     86    803   4337       C  
ATOM   4592  O   PRO B 220     -54.353 -39.857  17.799  1.00145.07           O  
ANISOU 4592  O   PRO B 220    15287  21500  18333    194    775   3859       O  
ATOM   4593  CB  PRO B 220     -55.844 -42.664  17.671  1.00150.92           C  
ANISOU 4593  CB  PRO B 220    15300  22059  19985   -416    824   4729       C  
ATOM   4594  CG  PRO B 220     -56.782 -43.305  18.647  1.00155.31           C  
ANISOU 4594  CG  PRO B 220    15469  23094  20449   -561    899   5292       C  
ATOM   4595  CD  PRO B 220     -55.890 -43.850  19.714  1.00157.37           C  
ANISOU 4595  CD  PRO B 220    15678  23366  20750   -620    847   5762       C  
ATOM   4596  N   ILE B 221     -55.484 -40.084  19.732  1.00150.60           N  
ANISOU 4596  N   ILE B 221    15568  23192  18460    248    862   4504       N  
ATOM   4597  CA  ILE B 221     -55.573 -38.641  19.968  1.00149.37           C  
ANISOU 4597  CA  ILE B 221    15664  23388  17701    592    857   4095       C  
ATOM   4598  C   ILE B 221     -54.241 -38.067  20.453  1.00148.29           C  
ANISOU 4598  C   ILE B 221    15788  23124  17431    707    725   3961       C  
ATOM   4599  O   ILE B 221     -53.990 -36.870  20.343  1.00146.61           O  
ANISOU 4599  O   ILE B 221    15872  22945  16889    941    672   3527       O  
ATOM   4600  CB  ILE B 221     -56.662 -38.281  20.994  1.00152.70           C  
ANISOU 4600  CB  ILE B 221    15876  24607  17538    779    960   4282       C  
ATOM   4601  CG1 ILE B 221     -57.009 -36.798  20.873  1.00151.34           C  
ANISOU 4601  CG1 ILE B 221    15979  24695  16828   1154    949   3747       C  
ATOM   4602  CG2 ILE B 221     -56.195 -38.584  22.410  1.00155.90           C  
ANISOU 4602  CG2 ILE B 221    16157  25399  17680    799    935   4726       C  
ATOM   4603  CD1 ILE B 221     -57.344 -36.383  19.463  1.00148.23           C  
ANISOU 4603  CD1 ILE B 221    15775  23899  16646   1176    947   3294       C  
ATOM   4604  N   VAL B 222     -53.387 -38.923  20.999  1.00149.62           N  
ANISOU 4604  N   VAL B 222    15840  23134  17877    541    651   4339       N  
ATOM   4605  CA  VAL B 222     -52.044 -38.510  21.381  1.00148.85           C  
ANISOU 4605  CA  VAL B 222    15939  22866  17751    613    498   4220       C  
ATOM   4606  C   VAL B 222     -51.112 -38.922  20.263  1.00146.13           C  
ANISOU 4606  C   VAL B 222    15701  21798  18022    436    461   4041       C  
ATOM   4607  O   VAL B 222     -50.258 -38.163  19.826  1.00143.89           O  
ANISOU 4607  O   VAL B 222    15670  21244  17757    507    396   3660       O  
ATOM   4608  CB  VAL B 222     -51.586 -39.149  22.708  1.00152.40           C  
ANISOU 4608  CB  VAL B 222    16198  23615  18093    587    412   4734       C  
ATOM   4609  CG1 VAL B 222     -50.080 -39.004  22.886  1.00151.64           C  
ANISOU 4609  CG1 VAL B 222    16246  23205  18164    595    223   4631       C  
ATOM   4610  CG2 VAL B 222     -52.346 -38.551  23.884  1.00155.38           C  
ANISOU 4610  CG2 VAL B 222    16518  24771  17750    827    449   4847       C  
ATOM   4611  N   THR B 223     -51.312 -40.143  19.796  1.00146.76           N  
ANISOU 4611  N   THR B 223    15578  21573  18612    202    506   4320       N  
ATOM   4612  CA  THR B 223     -50.488 -40.732  18.762  1.00144.93           C  
ANISOU 4612  CA  THR B 223    15407  20676  18986     49    480   4185       C  
ATOM   4613  C   THR B 223     -50.469 -39.937  17.466  1.00141.48           C  
ANISOU 4613  C   THR B 223    15244  19934  18579    117    544   3625       C  
ATOM   4614  O   THR B 223     -49.425 -39.468  17.044  1.00139.70           O  
ANISOU 4614  O   THR B 223    15211  19408  18461    153    510   3350       O  
ATOM   4615  CB  THR B 223     -50.955 -42.157  18.469  1.00146.78           C  
ANISOU 4615  CB  THR B 223    15387  20653  19731   -194    505   4547       C  
ATOM   4616  OG1 THR B 223     -50.834 -42.940  19.664  1.00150.37           O  
ANISOU 4616  OG1 THR B 223    15609  21330  20194   -271    440   5121       O  
ATOM   4617  CG2 THR B 223     -50.086 -42.766  17.428  1.00145.33           C  
ANISOU 4617  CG2 THR B 223    15275  19799  20145   -301    470   4369       C  
ATOM   4618  N   GLY B 224     -51.621 -39.783  16.836  1.00140.90           N  
ANISOU 4618  N   GLY B 224    15178  19954  18406    135    636   3473       N  
ATOM   4619  CA  GLY B 224     -51.702 -39.074  15.571  1.00138.06           C  
ANISOU 4619  CA  GLY B 224    15090  19319  18047    214    691   2976       C  
ATOM   4620  C   GLY B 224     -51.040 -37.706  15.389  1.00135.96           C  
ANISOU 4620  C   GLY B 224    15167  19023  17470    399    677   2574       C  
ATOM   4621  O   GLY B 224     -50.317 -37.510  14.405  1.00134.06           O  
ANISOU 4621  O   GLY B 224    15124  18348  17464    370    709   2295       O  
ATOM   4622  N   PRO B 225     -51.275 -36.752  16.317  1.00136.70           N  
ANISOU 4622  N   PRO B 225    15335  19567  17037    589    631   2537       N  
ATOM   4623  CA  PRO B 225     -50.683 -35.415  16.164  1.00135.22           C  
ANISOU 4623  CA  PRO B 225    15490  19307  16578    749    586   2147       C  
ATOM   4624  C   PRO B 225     -49.166 -35.456  16.207  1.00134.77           C  
ANISOU 4624  C   PRO B 225    15488  18909  16811    637    517   2134       C  
ATOM   4625  O   PRO B 225     -48.497 -34.826  15.388  1.00133.09           O  
ANISOU 4625  O   PRO B 225    15519  18346  16705    627    544   1825       O  
ATOM   4626  CB  PRO B 225     -51.212 -34.631  17.375  1.00137.06           C  
ANISOU 4626  CB  PRO B 225    15733  20116  16228    974    513   2169       C  
ATOM   4627  CG  PRO B 225     -52.138 -35.509  18.073  1.00139.38           C  
ANISOU 4627  CG  PRO B 225    15685  20822  16452    939    562   2570       C  
ATOM   4628  CD  PRO B 225     -51.935 -36.905  17.621  1.00139.46           C  
ANISOU 4628  CD  PRO B 225    15458  20493  17038    659    606   2872       C  
ATOM   4629  N   THR B 226     -48.638 -36.195  17.176  1.00136.67           N  
ANISOU 4629  N   THR B 226    15487  19271  17171    555    429   2489       N  
ATOM   4630  CA  THR B 226     -47.206 -36.362  17.310  1.00136.81           C  
ANISOU 4630  CA  THR B 226    15482  19007  17493    456    340   2515       C  
ATOM   4631  C   THR B 226     -46.597 -36.780  15.976  1.00135.01           C  
ANISOU 4631  C   THR B 226    15302  18223  17772    318    451   2351       C  
ATOM   4632  O   THR B 226     -45.787 -36.046  15.416  1.00133.83           O  
ANISOU 4632  O   THR B 226    15345  17823  17681    313    470   2058       O  
ATOM   4633  CB  THR B 226     -46.890 -37.385  18.418  1.00139.47           C  
ANISOU 4633  CB  THR B 226    15515  19529  17948    390    231   2989       C  
ATOM   4634  OG1 THR B 226     -47.282 -36.825  19.676  1.00141.45           O  
ANISOU 4634  OG1 THR B 226    15761  20331  17653    552    128   3093       O  
ATOM   4635  CG2 THR B 226     -45.422 -37.667  18.492  1.00139.88           C  
ANISOU 4635  CG2 THR B 226    15500  19280  18368    302    126   3020       C  
ATOM   4636  N   VAL B 227     -47.079 -37.880  15.410  1.00135.07           N  
ANISOU 4636  N   VAL B 227    15154  18051  18113    216    533   2509       N  
ATOM   4637  CA  VAL B 227     -46.570 -38.390  14.134  1.00133.86           C  
ANISOU 4637  CA  VAL B 227    15042  17396  18424    119    637   2339       C  
ATOM   4638  C   VAL B 227     -46.724 -37.398  12.972  1.00131.66           C  
ANISOU 4638  C   VAL B 227    15085  16953  17986    192    760   1904       C  
ATOM   4639  O   VAL B 227     -45.809 -37.217  12.146  1.00130.83           O  
ANISOU 4639  O   VAL B 227    15094  16508  18107    153    844   1694       O  
ATOM   4640  CB  VAL B 227     -47.266 -39.707  13.779  1.00134.81           C  
ANISOU 4640  CB  VAL B 227    14961  17373  18888     13    664   2555       C  
ATOM   4641  CG1 VAL B 227     -46.711 -40.279  12.489  1.00134.06           C  
ANISOU 4641  CG1 VAL B 227    14916  16768  19254    -47    753   2344       C  
ATOM   4642  CG2 VAL B 227     -47.102 -40.684  14.922  1.00137.44           C  
ANISOU 4642  CG2 VAL B 227    15000  17834  19386    -67    543   3035       C  
ATOM   4643  N   MET B 228     -47.890 -36.769  12.906  1.00131.09           N  
ANISOU 4643  N   MET B 228    15148  17139  17520    307    779   1786       N  
ATOM   4644  CA  MET B 228     -48.152 -35.762  11.895  1.00129.40           C  
ANISOU 4644  CA  MET B 228    15267  16805  17095    410    868   1407       C  
ATOM   4645  C   MET B 228     -47.086 -34.681  11.925  1.00128.93           C  
ANISOU 4645  C   MET B 228    15431  16623  16935    428    859   1212       C  
ATOM   4646  O   MET B 228     -46.522 -34.319  10.892  1.00128.01           O  
ANISOU 4646  O   MET B 228    15511  16182  16946    396    973    988       O  
ATOM   4647  CB  MET B 228     -49.523 -35.137  12.113  1.00129.43           C  
ANISOU 4647  CB  MET B 228    15357  17181  16641    579    842   1335       C  
ATOM   4648  CG  MET B 228     -50.661 -35.972  11.620  1.00129.77           C  
ANISOU 4648  CG  MET B 228    15241  17271  16792    553    878   1407       C  
ATOM   4649  SD  MET B 228     -52.159 -35.030  11.769  1.00129.99           S  
ANISOU 4649  SD  MET B 228    15376  17747  16268    794    856   1255       S  
ATOM   4650  CE  MET B 228     -51.751 -33.674  10.675  1.00128.14           C  
ANISOU 4650  CE  MET B 228    15636  17214  15835    944    900    808       C  
ATOM   4651  N   LEU B 229     -46.807 -34.178  13.123  1.00129.99           N  
ANISOU 4651  N   LEU B 229    15526  17026  16838    471    719   1304       N  
ATOM   4652  CA  LEU B 229     -45.859 -33.091  13.272  1.00130.09           C  
ANISOU 4652  CA  LEU B 229    15738  16934  16755    470    662   1110       C  
ATOM   4653  C   LEU B 229     -44.426 -33.584  13.045  1.00130.46           C  
ANISOU 4653  C   LEU B 229    15635  16667  17268    289    692   1169       C  
ATOM   4654  O   LEU B 229     -43.553 -32.796  12.677  1.00130.46           O  
ANISOU 4654  O   LEU B 229    15790  16452  17325    226    717    979       O  
ATOM   4655  CB  LEU B 229     -45.987 -32.433  14.645  1.00131.60           C  
ANISOU 4655  CB  LEU B 229    15931  17516  16554    590    465   1151       C  
ATOM   4656  CG  LEU B 229     -45.316 -31.057  14.618  1.00131.83           C  
ANISOU 4656  CG  LEU B 229    16261  17402  16425    612    386    853       C  
ATOM   4657  CD1 LEU B 229     -46.097 -30.142  13.682  1.00130.64           C  
ANISOU 4657  CD1 LEU B 229    16472  17133  16035    739    480    571       C  
ATOM   4658  CD2 LEU B 229     -45.178 -30.427  15.987  1.00133.84           C  
ANISOU 4658  CD2 LEU B 229    16520  17988  16344    721    149    845       C  
ATOM   4659  N   ILE B 230     -44.166 -34.865  13.301  1.00131.21           N  
ANISOU 4659  N   ILE B 230    15413  16735  17706    206    680   1443       N  
ATOM   4660  CA  ILE B 230     -42.874 -35.444  12.922  1.00131.75           C  
ANISOU 4660  CA  ILE B 230    15317  16489  18254     74    729   1476       C  
ATOM   4661  C   ILE B 230     -42.635 -35.330  11.419  1.00130.55           C  
ANISOU 4661  C   ILE B 230    15334  15978  18291     37    955   1225       C  
ATOM   4662  O   ILE B 230     -41.672 -34.700  10.976  1.00130.74           O  
ANISOU 4662  O   ILE B 230    15443  15816  18415    -33   1033   1064       O  
ATOM   4663  CB  ILE B 230     -42.765 -36.915  13.355  1.00133.04           C  
ANISOU 4663  CB  ILE B 230    15142  16638  18772     28    670   1810       C  
ATOM   4664  CG1 ILE B 230     -42.534 -36.976  14.861  1.00134.92           C  
ANISOU 4664  CG1 ILE B 230    15201  17204  18860     51    445   2081       C  
ATOM   4665  CG2 ILE B 230     -41.581 -37.569  12.710  1.00133.65           C  
ANISOU 4665  CG2 ILE B 230    15065  16355  19359    -55    752   1787       C  
ATOM   4666  CD1 ILE B 230     -42.445 -38.371  15.420  1.00136.73           C  
ANISOU 4666  CD1 ILE B 230    15119  17429  19403     13    362   2471       C  
ATOM   4667  N   GLY B 231     -43.557 -35.881  10.640  1.00129.66           N  
ANISOU 4667  N   GLY B 231    15276  15795  18195     83   1058   1189       N  
ATOM   4668  CA  GLY B 231     -43.470 -35.794   9.193  1.00128.83           C  
ANISOU 4668  CA  GLY B 231    15360  15398  18191     87   1265    941       C  
ATOM   4669  C   GLY B 231     -43.404 -34.366   8.691  1.00128.09           C  
ANISOU 4669  C   GLY B 231    15620  15273  17778    121   1345    693       C  
ATOM   4670  O   GLY B 231     -42.693 -34.061   7.737  1.00128.21           O  
ANISOU 4670  O   GLY B 231    15759  15043  17911     73   1522    538       O  
ATOM   4671  N   ILE B 232     -44.193 -33.495   9.309  1.00127.70           N  
ANISOU 4671  N   ILE B 232    15739  15470  17310    216   1222    660       N  
ATOM   4672  CA  ILE B 232     -44.212 -32.089   8.929  1.00127.41           C  
ANISOU 4672  CA  ILE B 232    16070  15375  16964    266   1254    436       C  
ATOM   4673  C   ILE B 232     -42.856 -31.458   9.151  1.00128.51           C  
ANISOU 4673  C   ILE B 232    16208  15362  17260    118   1252    408       C  
ATOM   4674  O   ILE B 232     -42.269 -30.906   8.229  1.00128.76           O  
ANISOU 4674  O   ILE B 232    16424  15139  17359     43   1417    274       O  
ATOM   4675  CB  ILE B 232     -45.255 -31.286   9.708  1.00127.32           C  
ANISOU 4675  CB  ILE B 232    16217  15668  16490    433   1086    393       C  
ATOM   4676  CG1 ILE B 232     -46.666 -31.706   9.296  1.00126.50           C  
ANISOU 4676  CG1 ILE B 232    16137  15719  16210    582   1109    377       C  
ATOM   4677  CG2 ILE B 232     -45.077 -29.807   9.422  1.00127.60           C  
ANISOU 4677  CG2 ILE B 232    16641  15573  16267    477   1078    167       C  
ATOM   4678  CD1 ILE B 232     -47.745 -31.130  10.182  1.00126.86           C  
ANISOU 4678  CD1 ILE B 232    16232  16147  15823    771    956    370       C  
ATOM   4679  N   SER B 233     -42.357 -31.545  10.378  1.00129.56           N  
ANISOU 4679  N   SER B 233    16118  15664  17445     68   1061    546       N  
ATOM   4680  CA  SER B 233     -41.097 -30.906  10.721  1.00131.05           C  
ANISOU 4680  CA  SER B 233    16269  15739  17784    -82   1002    507       C  
ATOM   4681  C   SER B 233     -39.940 -31.472   9.909  1.00131.69           C  
ANISOU 4681  C   SER B 233    16158  15551  18325   -241   1203    530       C  
ATOM   4682  O   SER B 233     -38.974 -30.767   9.627  1.00132.92           O  
ANISOU 4682  O   SER B 233    16358  15534  18612   -389   1265    442       O  
ATOM   4683  CB  SER B 233     -40.801 -31.080  12.207  1.00132.38           C  
ANISOU 4683  CB  SER B 233    16196  16177  17925    -79    730    657       C  
ATOM   4684  OG  SER B 233     -40.630 -32.451  12.513  1.00132.60           O  
ANISOU 4684  OG  SER B 233    15865  16274  18242    -93    723    905       O  
ATOM   4685  N   LEU B 234     -40.061 -32.725   9.486  1.00131.20           N  
ANISOU 4685  N   LEU B 234    15888  15446  18514   -208   1311    636       N  
ATOM   4686  CA  LEU B 234     -39.017 -33.332   8.667  1.00132.11           C  
ANISOU 4686  CA  LEU B 234    15818  15328  19052   -302   1516    627       C  
ATOM   4687  C   LEU B 234     -39.149 -32.994   7.181  1.00131.63           C  
ANISOU 4687  C   LEU B 234    16029  15055  18927   -288   1806    438       C  
ATOM   4688  O   LEU B 234     -38.176 -33.095   6.441  1.00132.88           O  
ANISOU 4688  O   LEU B 234    16097  15045  19349   -373   2017    390       O  
ATOM   4689  CB  LEU B 234     -39.005 -34.855   8.832  1.00132.40           C  
ANISOU 4689  CB  LEU B 234    15526  15362  19419   -250   1487    800       C  
ATOM   4690  CG  LEU B 234     -38.546 -35.463  10.162  1.00133.70           C  
ANISOU 4690  CG  LEU B 234    15353  15687  19761   -270   1238   1044       C  
ATOM   4691  CD1 LEU B 234     -38.391 -36.971  10.024  1.00134.50           C  
ANISOU 4691  CD1 LEU B 234    15169  15666  20267   -223   1254   1200       C  
ATOM   4692  CD2 LEU B 234     -37.283 -34.817  10.696  1.00135.46           C  
ANISOU 4692  CD2 LEU B 234    15432  15923  20113   -393   1153   1032       C  
ATOM   4693  N   ILE B 235     -40.352 -32.642   6.733  1.00130.15           N  
ANISOU 4693  N   ILE B 235    16158  14907  18385   -161   1821    339       N  
ATOM   4694  CA  ILE B 235     -40.599 -32.437   5.302  1.00129.90           C  
ANISOU 4694  CA  ILE B 235    16401  14703  18251   -107   2072    172       C  
ATOM   4695  C   ILE B 235     -39.772 -31.269   4.748  1.00131.17           C  
ANISOU 4695  C   ILE B 235    16775  14706  18358   -234   2239     90       C  
ATOM   4696  O   ILE B 235     -39.483 -31.204   3.542  1.00131.91           O  
ANISOU 4696  O   ILE B 235    17009  14647  18465   -235   2509      3       O  
ATOM   4697  CB  ILE B 235     -42.118 -32.219   5.014  1.00128.35           C  
ANISOU 4697  CB  ILE B 235    16497  14611  17661     73   2004     81       C  
ATOM   4698  CG1 ILE B 235     -42.464 -32.682   3.601  1.00128.30           C  
ANISOU 4698  CG1 ILE B 235    16639  14465  17645    170   2211    -62       C  
ATOM   4699  CG2 ILE B 235     -42.515 -30.769   5.174  1.00128.21           C  
ANISOU 4699  CG2 ILE B 235    16839  14624  17250    109   1930     -6       C  
ATOM   4700  CD1 ILE B 235     -43.930 -32.736   3.322  1.00127.15           C  
ANISOU 4700  CD1 ILE B 235    16681  14435  17197    346   2112   -149       C  
ATOM   4701  N   GLY B 236     -39.385 -30.364   5.644  1.00131.84           N  
ANISOU 4701  N   GLY B 236    16880  14829  18384   -344   2071    125       N  
ATOM   4702  CA  GLY B 236     -38.595 -29.196   5.297  1.00133.56           C  
ANISOU 4702  CA  GLY B 236    17281  14871  18594   -514   2177     76       C  
ATOM   4703  C   GLY B 236     -37.251 -29.509   4.661  1.00135.60           C  
ANISOU 4703  C   GLY B 236    17287  14995  19239   -691   2440    118       C  
ATOM   4704  O   GLY B 236     -36.782 -28.782   3.792  1.00137.13           O  
ANISOU 4704  O   GLY B 236    17672  15025  19407   -804   2673     87       O  
ATOM   4705  N   THR B 237     -36.614 -30.580   5.119  1.00136.01           N  
ANISOU 4705  N   THR B 237    16900  15128  19651   -709   2405    204       N  
ATOM   4706  CA  THR B 237     -35.311 -30.962   4.598  1.00138.31           C  
ANISOU 4706  CA  THR B 237    16881  15334  20335   -840   2645    234       C  
ATOM   4707  C   THR B 237     -35.433 -31.557   3.198  1.00138.45           C  
ANISOU 4707  C   THR B 237    16986  15269  20348   -716   2986    149       C  
ATOM   4708  O   THR B 237     -34.570 -31.355   2.336  1.00140.67           O  
ANISOU 4708  O   THR B 237    17218  15470  20759   -812   3294    131       O  
ATOM   4709  CB  THR B 237     -34.643 -31.989   5.520  1.00138.98           C  
ANISOU 4709  CB  THR B 237    16473  15527  20805   -840   2472    345       C  
ATOM   4710  OG1 THR B 237     -35.450 -33.171   5.590  1.00137.29           O  
ANISOU 4710  OG1 THR B 237    16198  15370  20596   -632   2396    374       O  
ATOM   4711  CG2 THR B 237     -34.481 -31.409   6.916  1.00139.30           C  
ANISOU 4711  CG2 THR B 237    16430  15686  20812   -943   2119    415       C  
ATOM   4712  N   GLY B 238     -36.541 -32.257   2.975  1.00138.43           N  
ANISOU 4712  N   GLY B 238    17116  15304  20177   -502   2924     93       N  
ATOM   4713  CA  GLY B 238     -36.860 -32.829   1.681  1.00138.58           C  
ANISOU 4713  CA  GLY B 238    17270  15253  20130   -346   3180    -34       C  
ATOM   4714  C   GLY B 238     -37.079 -31.708   0.692  1.00139.14           C  
ANISOU 4714  C   GLY B 238    17775  15249  19842   -366   3394   -107       C  
ATOM   4715  O   GLY B 238     -36.493 -31.701  -0.395  1.00141.13           O  
ANISOU 4715  O   GLY B 238    18068  15441  20113   -368   3725   -157       O  
ATOM   4716  N   PHE B 239     -37.922 -30.749   1.069  1.00140.20           N  
ANISOU 4716  N   PHE B 239    18241  15394  19633   -361   3209   -104       N  
ATOM   4717  CA  PHE B 239     -38.131 -29.586   0.213  1.00141.07           C  
ANISOU 4717  CA  PHE B 239    18800  15398  19404   -378   3373   -139       C  
ATOM   4718  C   PHE B 239     -36.839 -28.797  -0.010  1.00143.97           C  
ANISOU 4718  C   PHE B 239    19110  15648  19945   -642   3594    -41       C  
ATOM   4719  O   PHE B 239     -36.597 -28.323  -1.114  1.00145.85           O  
ANISOU 4719  O   PHE B 239    19583  15798  20037   -667   3895    -35       O  
ATOM   4720  CB  PHE B 239     -39.207 -28.660   0.788  1.00135.82           C  
ANISOU 4720  CB  PHE B 239    18479  14748  18377   -306   3096   -161       C  
ATOM   4721  CG  PHE B 239     -40.611 -29.045   0.409  1.00133.90           C  
ANISOU 4721  CG  PHE B 239    18452  14598  17825    -36   2998   -275       C  
ATOM   4722  CD1 PHE B 239     -41.534 -29.408   1.374  1.00131.88           C  
ANISOU 4722  CD1 PHE B 239    18093  14511  17506     75   2697   -280       C  
ATOM   4723  CD2 PHE B 239     -41.013 -29.022  -0.920  1.00134.52           C  
ANISOU 4723  CD2 PHE B 239    18829  14621  17663    107   3206   -371       C  
ATOM   4724  CE1 PHE B 239     -42.836 -29.751   1.020  1.00130.54           C  
ANISOU 4724  CE1 PHE B 239    18076  14443  17079    301   2605   -381       C  
ATOM   4725  CE2 PHE B 239     -42.308 -29.365  -1.281  1.00133.12           C  
ANISOU 4725  CE2 PHE B 239    18827  14537  17214    351   3083   -496       C  
ATOM   4726  CZ  PHE B 239     -43.222 -29.729  -0.306  1.00131.12           C  
ANISOU 4726  CZ  PHE B 239    18433  14444  16944    436   2781   -501       C  
ATOM   4727  N   LYS B 240     -36.002 -28.672   1.016  1.00143.02           N  
ANISOU 4727  N   LYS B 240    18664  15540  20135   -845   3447     47       N  
ATOM   4728  CA  LYS B 240     -34.749 -27.926   0.876  1.00146.21           C  
ANISOU 4728  CA  LYS B 240    18953  15837  20762  -1138   3629    144       C  
ATOM   4729  C   LYS B 240     -33.790 -28.580  -0.115  1.00148.63           C  
ANISOU 4729  C   LYS B 240    18992  16173  21306  -1166   4037    164       C  
ATOM   4730  O   LYS B 240     -33.202 -27.905  -0.956  1.00151.41           O  
ANISOU 4730  O   LYS B 240    19463  16443  21624  -1318   4351    234       O  
ATOM   4731  CB  LYS B 240     -34.057 -27.758   2.231  1.00147.63           C  
ANISOU 4731  CB  LYS B 240    18795  16053  21245  -1332   3336    203       C  
ATOM   4732  CG  LYS B 240     -34.618 -26.632   3.086  1.00147.02           C  
ANISOU 4732  CG  LYS B 240    19025  15902  20934  -1388   3001    178       C  
ATOM   4733  CD  LYS B 240     -34.087 -26.695   4.505  1.00147.42           C  
ANISOU 4733  CD  LYS B 240    18731  16051  21230  -1503   2657    197       C  
ATOM   4734  CE  LYS B 240     -34.721 -25.632   5.378  1.00147.03           C  
ANISOU 4734  CE  LYS B 240    19005  15954  20906  -1499   2305    122       C  
ATOM   4735  NZ  LYS B 240     -34.301 -25.757   6.799  1.00147.54           N  
ANISOU 4735  NZ  LYS B 240    18755  16164  21138  -1560   1941    118       N  
ATOM   4736  N   ASP B 241     -33.641 -29.896  -0.018  1.00145.22           N  
ANISOU 4736  N   ASP B 241    18204  15859  21112  -1009   4037    110       N  
ATOM   4737  CA  ASP B 241     -32.779 -30.623  -0.942  1.00147.72           C  
ANISOU 4737  CA  ASP B 241    18255  16225  21648   -965   4412     81       C  
ATOM   4738  C   ASP B 241     -33.359 -30.513  -2.342  1.00148.15           C  
ANISOU 4738  C   ASP B 241    18716  16256  21316   -795   4713     -7       C  
ATOM   4739  O   ASP B 241     -32.640 -30.334  -3.324  1.00151.26           O  
ANISOU 4739  O   ASP B 241    19096  16674  21703   -845   5110     18       O  
ATOM   4740  CB  ASP B 241     -32.650 -32.093  -0.541  1.00148.39           C  
ANISOU 4740  CB  ASP B 241    17935  16393  22055   -779   4296     15       C  
ATOM   4741  CG  ASP B 241     -31.733 -32.296   0.641  1.00149.29           C  
ANISOU 4741  CG  ASP B 241    17568  16558  22596   -935   4083    124       C  
ATOM   4742  OD1 ASP B 241     -31.074 -31.323   1.072  1.00150.84           O  
ANISOU 4742  OD1 ASP B 241    17700  16740  22874  -1206   4054    223       O  
ATOM   4743  OD2 ASP B 241     -31.644 -33.443   1.119  1.00148.83           O  
ANISOU 4743  OD2 ASP B 241    17196  16545  22810   -787   3934    110       O  
ATOM   4744  N   TRP B 242     -34.678 -30.647  -2.414  1.00145.42           N  
ANISOU 4744  N   TRP B 242    18718  15896  20640   -584   4516   -108       N  
ATOM   4745  CA  TRP B 242     -35.422 -30.491  -3.656  1.00145.64           C  
ANISOU 4745  CA  TRP B 242    19183  15913  20243   -392   4711   -210       C  
ATOM   4746  C   TRP B 242     -35.022 -29.169  -4.314  1.00148.21           C  
ANISOU 4746  C   TRP B 242    19819  16156  20339   -575   4973    -73       C  
ATOM   4747  O   TRP B 242     -34.728 -29.118  -5.512  1.00150.82           O  
ANISOU 4747  O   TRP B 242    20292  16520  20491   -514   5345    -79       O  
ATOM   4748  CB  TRP B 242     -36.935 -30.575  -3.360  1.00142.14           C  
ANISOU 4748  CB  TRP B 242    19039  15469  19499   -194   4373   -310       C  
ATOM   4749  CG  TRP B 242     -37.855 -30.639  -4.555  1.00142.18           C  
ANISOU 4749  CG  TRP B 242    19450  15487  19083     57   4481   -458       C  
ATOM   4750  CD1 TRP B 242     -37.559 -30.304  -5.842  1.00144.89           C  
ANISOU 4750  CD1 TRP B 242    20043  15832  19177    113   4839   -476       C  
ATOM   4751  CD2 TRP B 242     -39.204 -31.125  -4.573  1.00139.81           C  
ANISOU 4751  CD2 TRP B 242    19323  15229  18568    291   4222   -609       C  
ATOM   4752  NE1 TRP B 242     -38.647 -30.513  -6.653  1.00144.29           N  
ANISOU 4752  NE1 TRP B 242    20315  15792  18718    385   4791   -644       N  
ATOM   4753  CE2 TRP B 242     -39.668 -31.028  -5.898  1.00141.18           C  
ANISOU 4753  CE2 TRP B 242    19862  15418  18363    489   4408   -737       C  
ATOM   4754  CE3 TRP B 242     -40.071 -31.618  -3.594  1.00137.03           C  
ANISOU 4754  CE3 TRP B 242    18840  14925  18299    346   3854   -633       C  
ATOM   4755  CZ2 TRP B 242     -40.954 -31.402  -6.270  1.00139.83           C  
ANISOU 4755  CZ2 TRP B 242    19913  15294  17922    734   4207   -915       C  
ATOM   4756  CZ3 TRP B 242     -41.348 -31.992  -3.967  1.00135.75           C  
ANISOU 4756  CZ3 TRP B 242    18879  14815  17887    568   3687   -786       C  
ATOM   4757  CH2 TRP B 242     -41.776 -31.883  -5.291  1.00137.12           C  
ANISOU 4757  CH2 TRP B 242    19400  14989  17712    757   3847   -938       C  
ATOM   4758  N   ALA B 243     -34.945 -28.123  -3.495  1.00151.53           N  
ANISOU 4758  N   ALA B 243    20326  16464  20783   -805   4775     58       N  
ATOM   4759  CA  ALA B 243     -34.518 -26.801  -3.941  1.00154.34           C  
ANISOU 4759  CA  ALA B 243    20966  16675  21003  -1037   4966    223       C  
ATOM   4760  C   ALA B 243     -33.090 -26.834  -4.467  1.00158.45           C  
ANISOU 4760  C   ALA B 243    21146  17240  21816  -1262   5378    350       C  
ATOM   4761  O   ALA B 243     -32.779 -26.178  -5.461  1.00161.60           O  
ANISOU 4761  O   ALA B 243    21784  17596  22022  -1351   5727    478       O  
ATOM   4762  CB  ALA B 243     -34.649 -25.782  -2.806  1.00157.77           C  
ANISOU 4762  CB  ALA B 243    21505  16954  21488  -1239   4610    294       C  
ATOM   4763  N   GLY B 244     -32.229 -27.580  -3.775  1.00156.72           N  
ANISOU 4763  N   GLY B 244    20362  17124  22060  -1350   5334    335       N  
ATOM   4764  CA  GLY B 244     -30.840 -27.774  -4.174  1.00160.75           C  
ANISOU 4764  CA  GLY B 244    20436  17734  22909  -1530   5707    430       C  
ATOM   4765  C   GLY B 244     -29.912 -27.611  -2.986  1.00161.63           C  
ANISOU 4765  C   GLY B 244    20076  17831  23505  -1822   5491    512       C  
ATOM   4766  O   GLY B 244     -28.689 -27.607  -3.126  1.00165.34           O  
ANISOU 4766  O   GLY B 244    20125  18380  24316  -2032   5745    610       O  
ATOM   4767  N   GLY B 245     -30.518 -27.525  -1.805  1.00160.47           N  
ANISOU 4767  N   GLY B 245    19980  17617  23376  -1809   5011    460       N  
ATOM   4768  CA  GLY B 245     -29.817 -27.263  -0.563  1.00161.14           C  
ANISOU 4768  CA  GLY B 245    19703  17686  23837  -2059   4711    513       C  
ATOM   4769  C   GLY B 245     -29.519 -28.525   0.223  1.00159.87           C  
ANISOU 4769  C   GLY B 245    19043  17694  24007  -1905   4514    439       C  
ATOM   4770  O   GLY B 245     -29.428 -29.604  -0.360  1.00159.88           O  
ANISOU 4770  O   GLY B 245    18857  17809  24080  -1675   4721    367       O  
ATOM   4771  N   SER B 246     -29.330 -28.397   1.537  1.00163.44           N  
ANISOU 4771  N   SER B 246    19284  18156  24662  -2020   4107    454       N  
ATOM   4772  CA  SER B 246     -29.385 -27.110   2.226  1.00164.01           C  
ANISOU 4772  CA  SER B 246    19579  18079  24658  -2279   3843    493       C  
ATOM   4773  C   SER B 246     -28.110 -26.296   1.992  1.00168.76           C  
ANISOU 4773  C   SER B 246    19942  18602  25579  -2676   4040    609       C  
ATOM   4774  O   SER B 246     -28.002 -25.154   2.429  1.00170.24           O  
ANISOU 4774  O   SER B 246    20308  18611  25764  -2943   3850    642       O  
ATOM   4775  CB  SER B 246     -29.627 -27.306   3.724  1.00160.67           C  
ANISOU 4775  CB  SER B 246    19010  17734  24305  -2231   3328    445       C  
ATOM   4776  OG  SER B 246     -28.583 -28.039   4.324  1.00162.46           O  
ANISOU 4776  OG  SER B 246    18639  18109  24979  -2290   3249    480       O  
ATOM   4777  N   ALA B 247     -27.141 -26.898   1.312  1.00164.83           N  
ANISOU 4777  N   ALA B 247    19022  18235  25371  -2713   4416    664       N  
ATOM   4778  CA  ALA B 247     -25.966 -26.165   0.867  1.00169.87           C  
ANISOU 4778  CA  ALA B 247    19416  18833  26293  -3093   4703    804       C  
ATOM   4779  C   ALA B 247     -25.810 -26.359  -0.634  1.00171.83           C  
ANISOU 4779  C   ALA B 247    19747  19150  26391  -3016   5292    873       C  
ATOM   4780  O   ALA B 247     -25.533 -27.463  -1.107  1.00172.01           O  
ANISOU 4780  O   ALA B 247    19470  19378  26509  -2768   5530    806       O  
ATOM   4781  CB  ALA B 247     -24.737 -26.629   1.605  1.00171.39           C  
ANISOU 4781  CB  ALA B 247    18902  19189  27031  -3242   4589    815       C  
ATOM   4782  N   CYS B 248     -25.967 -25.265  -1.370  1.00177.45           N  
ANISOU 4782  N   CYS B 248    20878  19682  26862  -3220   5516   1007       N  
ATOM   4783  CA  CYS B 248     -25.924 -25.292  -2.826  1.00179.64           C  
ANISOU 4783  CA  CYS B 248    21334  20030  26891  -3143   6074   1099       C  
ATOM   4784  C   CYS B 248     -24.550 -25.704  -3.318  1.00184.53           C  
ANISOU 4784  C   CYS B 248    21331  20886  27897  -3288   6508   1193       C  
ATOM   4785  O   CYS B 248     -23.560 -25.484  -2.625  1.00187.28           O  
ANISOU 4785  O   CYS B 248    21186  21256  28713  -3597   6396   1259       O  
ATOM   4786  CB  CYS B 248     -26.301 -23.922  -3.399  1.00192.47           C  
ANISOU 4786  CB  CYS B 248    23537  21387  28207  -3373   6187   1280       C  
ATOM   4787  SG  CYS B 248     -28.003 -23.372  -3.093  1.00187.42           S  
ANISOU 4787  SG  CYS B 248    23686  20492  27032  -3128   5758   1163       S  
ATOM   4788  N   MET B 249     -24.497 -26.299  -4.509  1.00183.22           N  
ANISOU 4788  N   MET B 249    21176  20915  27525  -3047   6991   1181       N  
ATOM   4789  CA  MET B 249     -23.275 -26.935  -5.027  1.00187.76           C  
ANISOU 4789  CA  MET B 249    21126  21788  28425  -3057   7430   1212       C  
ATOM   4790  C   MET B 249     -22.003 -26.071  -4.987  1.00193.63           C  
ANISOU 4790  C   MET B 249    21448  22556  29568  -3574   7655   1465       C  
ATOM   4791  O   MET B 249     -22.053 -24.852  -5.162  1.00195.61           O  
ANISOU 4791  O   MET B 249    22025  22585  29712  -3934   7703   1683       O  
ATOM   4792  CB  MET B 249     -23.495 -27.395  -6.464  1.00187.06           C  
ANISOU 4792  CB  MET B 249    21255  21887  27933  -2746   7957   1178       C  
ATOM   4793  CG  MET B 249     -24.839 -28.006  -6.727  1.00182.10           C  
ANISOU 4793  CG  MET B 249    21146  21194  26848  -2298   7770    954       C  
ATOM   4794  SD  MET B 249     -24.623 -29.123  -8.107  1.00184.74           S  
ANISOU 4794  SD  MET B 249    21371  21857  26966  -1857   8314    783       S  
ATOM   4795  CE  MET B 249     -23.762 -30.442  -7.265  1.00184.85           C  
ANISOU 4795  CE  MET B 249    20596  22032  27607  -1695   8141    588       C  
ATOM   4796  N   ASP B 250     -20.865 -26.725  -4.763  1.00194.61           N  
ANISOU 4796  N   ASP B 250    20831  22939  30172  -3605   7780   1436       N  
ATOM   4797  CA  ASP B 250     -19.590 -26.030  -4.623  1.00200.52           C  
ANISOU 4797  CA  ASP B 250    21052  23752  31383  -4101   7956   1655       C  
ATOM   4798  C   ASP B 250     -18.828 -25.880  -5.940  1.00206.61           C  
ANISOU 4798  C   ASP B 250    21627  24781  32092  -4201   8696   1856       C  
ATOM   4799  O   ASP B 250     -19.346 -26.164  -7.017  1.00206.32           O  
ANISOU 4799  O   ASP B 250    21962  24849  31580  -3895   9074   1837       O  
ATOM   4800  CB  ASP B 250     -18.703 -26.744  -3.599  1.00201.33           C  
ANISOU 4800  CB  ASP B 250    20398  24024  32073  -4102   7664   1530       C  
ATOM   4801  CG  ASP B 250     -17.793 -25.782  -2.854  1.00205.34           C  
ANISOU 4801  CG  ASP B 250    20521  24436  33061  -4674   7467   1695       C  
ATOM   4802  OD1 ASP B 250     -17.350 -24.798  -3.478  1.00209.98           O  
ANISOU 4802  OD1 ASP B 250    21151  24963  33669  -5090   7817   1952       O  
ATOM   4803  OD2 ASP B 250     -17.495 -26.013  -1.664  1.00204.34           O  
ANISOU 4803  OD2 ASP B 250    20042  24297  33299  -4718   6964   1579       O  
ATOM   4804  N   ASP B 251     -17.581 -25.437  -5.817  1.00212.49           N  
ANISOU 4804  N   ASP B 251    21761  25652  33323  -4632   8888   2048       N  
ATOM   4805  CA  ASP B 251     -16.729 -25.080  -6.946  1.00219.42           C  
ANISOU 4805  CA  ASP B 251    22381  26784  34203  -4852   9599   2315       C  
ATOM   4806  C   ASP B 251     -16.102 -26.298  -7.591  1.00221.89           C  
ANISOU 4806  C   ASP B 251    22159  27577  34574  -4434  10046   2161       C  
ATOM   4807  O   ASP B 251     -15.681 -27.234  -6.906  1.00220.90           O  
ANISOU 4807  O   ASP B 251    21501  27605  34826  -4205   9798   1929       O  
ATOM   4808  CB  ASP B 251     -15.603 -24.128  -6.514  1.00225.37           C  
ANISOU 4808  CB  ASP B 251    22618  27494  35519  -5518   9616   2586       C  
ATOM   4809  CG  ASP B 251     -16.121 -22.813  -5.989  1.00224.29           C  
ANISOU 4809  CG  ASP B 251    23020  26853  35348  -5965   9219   2748       C  
ATOM   4810  OD1 ASP B 251     -17.176 -22.352  -6.476  1.00221.40           O  
ANISOU 4810  OD1 ASP B 251    23449  26233  34440  -5848   9226   2803       O  
ATOM   4811  OD2 ASP B 251     -15.489 -22.261  -5.064  1.00226.46           O  
ANISOU 4811  OD2 ASP B 251    22924  26980  36140  -6405   8863   2791       O  
ATOM   4812  N   GLY B 252     -16.112 -26.309  -8.920  1.00225.12           N  
ANISOU 4812  N   GLY B 252    22760  28214  34562  -4286  10684   2275       N  
ATOM   4813  CA  GLY B 252     -15.420 -27.328  -9.683  1.00228.93           C  
ANISOU 4813  CA  GLY B 252    22734  29184  35064  -3907  11201   2142       C  
ATOM   4814  C   GLY B 252     -16.203 -28.615  -9.688  1.00223.61           C  
ANISOU 4814  C   GLY B 252    22280  28535  34147  -3232  10976   1726       C  
ATOM   4815  O   GLY B 252     -15.888 -29.541 -10.436  1.00226.08           O  
ANISOU 4815  O   GLY B 252    22348  29199  34355  -2800  11369   1543       O  
ATOM   4816  N   MET B 253     -17.229 -28.667  -8.848  1.00216.68           N  
ANISOU 4816  N   MET B 253    21862  27280  33185  -3143  10337   1575       N  
ATOM   4817  CA  MET B 253     -18.088 -29.826  -8.777  1.00211.48           C  
ANISOU 4817  CA  MET B 253    21457  26579  32316  -2564  10064   1214       C  
ATOM   4818  C   MET B 253     -19.022 -29.727  -9.963  1.00210.59           C  
ANISOU 4818  C   MET B 253    22056  26461  31497  -2303  10367   1188       C  
ATOM   4819  O   MET B 253     -19.406 -28.627 -10.357  1.00211.13           O  
ANISOU 4819  O   MET B 253    22607  26376  31236  -2599  10488   1449       O  
ATOM   4820  CB  MET B 253     -18.860 -29.855  -7.468  1.00209.32           C  
ANISOU 4820  CB  MET B 253    21407  25945  32181  -2594   9310   1108       C  
ATOM   4821  CG  MET B 253     -17.989 -29.715  -6.234  1.00210.43           C  
ANISOU 4821  CG  MET B 253    20927  26065  32960  -2914   8953   1171       C  
ATOM   4822  SD  MET B 253     -18.924 -30.076  -4.738  1.00203.06           S  
ANISOU 4822  SD  MET B 253    20231  24808  32115  -2791   8098    994       S  
ATOM   4823  CE  MET B 253     -19.175 -31.840  -4.955  1.00201.10           C  
ANISOU 4823  CE  MET B 253    19830  24709  31868  -2111   8086    661       C  
ATOM   4824  N   LEU B 254     -19.402 -30.865 -10.527  1.00209.50           N  
ANISOU 4824  N   LEU B 254    22002  26468  31129  -1742  10460    870       N  
ATOM   4825  CA  LEU B 254     -20.091 -30.867 -11.810  1.00210.19           C  
ANISOU 4825  CA  LEU B 254    22666  26650  30546  -1452  10825    814       C  
ATOM   4826  C   LEU B 254     -21.481 -30.238 -11.739  1.00204.83           C  
ANISOU 4826  C   LEU B 254    22809  25611  29406  -1489  10462    852       C  
ATOM   4827  O   LEU B 254     -22.203 -30.418 -10.759  1.00199.15           O  
ANISOU 4827  O   LEU B 254    22247  24600  28822  -1468   9870    729       O  
ATOM   4828  CB  LEU B 254     -20.175 -32.295 -12.341  1.00210.43           C  
ANISOU 4828  CB  LEU B 254    22578  26887  30490   -828  10927    402       C  
ATOM   4829  CG  LEU B 254     -18.784 -32.932 -12.362  1.00216.01           C  
ANISOU 4829  CG  LEU B 254    22440  27954  31679   -747  11263    343       C  
ATOM   4830  CD1 LEU B 254     -18.812 -34.393 -12.762  1.00216.52           C  
ANISOU 4830  CD1 LEU B 254    22357  28167  31743   -106  11297   -102       C  
ATOM   4831  CD2 LEU B 254     -17.877 -32.142 -13.297  1.00223.25           C  
ANISOU 4831  CD2 LEU B 254    23144  29234  32445  -1007  11981    651       C  
ATOM   4832  N   CYS B 255     -21.822 -29.473 -12.775  1.00207.14           N  
ANISOU 4832  N   CYS B 255    23605  25948  29149  -1544  10832   1044       N  
ATOM   4833  CA  CYS B 255     -23.141 -28.848 -12.915  1.00203.00           C  
ANISOU 4833  CA  CYS B 255    23887  25125  28119  -1521  10553   1082       C  
ATOM   4834  C   CYS B 255     -23.579 -27.962 -11.750  1.00198.93           C  
ANISOU 4834  C   CYS B 255    23557  24205  27824  -1912  10011   1242       C  
ATOM   4835  O   CYS B 255     -24.643 -28.188 -11.175  1.00193.19           O  
ANISOU 4835  O   CYS B 255    23175  23240  26987  -1735   9501   1053       O  
ATOM   4836  CB  CYS B 255     -24.210 -29.918 -13.156  1.00198.73           C  
ANISOU 4836  CB  CYS B 255    23680  24562  27267   -961  10291    668       C  
ATOM   4837  SG  CYS B 255     -24.017 -30.821 -14.700  1.00203.49           S  
ANISOU 4837  SG  CYS B 255    24308  25589  27419   -431  10871    420       S  
ATOM   4838  N   PRO B 256     -22.749 -26.986 -11.368  1.00202.22           N  
ANISOU 4838  N   PRO B 256    23715  24548  28570  -2438  10108   1572       N  
ATOM   4839  CA  PRO B 256     -23.285 -26.041 -10.391  1.00198.80           C  
ANISOU 4839  CA  PRO B 256    23585  23706  28243  -2769   9593   1696       C  
ATOM   4840  C   PRO B 256     -24.315 -25.132 -11.050  1.00197.98           C  
ANISOU 4840  C   PRO B 256    24302  23380  27540  -2758   9604   1846       C  
ATOM   4841  O   PRO B 256     -23.984 -24.491 -12.047  1.00202.96           O  
ANISOU 4841  O   PRO B 256    25111  24101  27904  -2903  10095   2128       O  
ATOM   4842  CB  PRO B 256     -22.058 -25.253  -9.945  1.00203.58           C  
ANISOU 4842  CB  PRO B 256    23690  24294  29368  -3337   9723   1992       C  
ATOM   4843  CG  PRO B 256     -21.023 -25.456 -11.018  1.00210.32           C  
ANISOU 4843  CG  PRO B 256    24147  25549  30218  -3355  10440   2144       C  
ATOM   4844  CD  PRO B 256     -21.495 -26.511 -11.977  1.00209.54           C  
ANISOU 4844  CD  PRO B 256    24223  25731  29663  -2760  10705   1876       C  
ATOM   4845  N   SER B 257     -25.525 -25.061 -10.504  1.00192.24           N  
ANISOU 4845  N   SER B 257    24052  22386  26606  -2587   9081   1683       N  
ATOM   4846  CA  SER B 257     -26.545 -24.143 -11.015  1.00191.42           C  
ANISOU 4846  CA  SER B 257    24721  22044  25964  -2561   9016   1815       C  
ATOM   4847  C   SER B 257     -26.901 -23.128  -9.933  1.00189.13           C  
ANISOU 4847  C   SER B 257    24648  21348  25866  -2884   8512   1915       C  
ATOM   4848  O   SER B 257     -27.530 -22.101 -10.190  1.00189.50           O  
ANISOU 4848  O   SER B 257    25286  21125  25592  -2976   8434   2089       O  
ATOM   4849  CB  SER B 257     -27.774 -24.916 -11.489  1.00187.33           C  
ANISOU 4849  CB  SER B 257    24625  21599  24954  -2015   8866   1511       C  
ATOM   4850  OG  SER B 257     -28.334 -25.660 -10.428  1.00181.73           O  
ANISOU 4850  OG  SER B 257    23760  20814  24475  -1838   8339   1213       O  
ATOM   4851  N   ALA B 258     -26.487 -23.447  -8.713  1.00189.35           N  
ANISOU 4851  N   ALA B 258    24196  21337  26409  -3026   8155   1788       N  
ATOM   4852  CA  ALA B 258     -26.507 -22.512  -7.599  1.00188.44           C  
ANISOU 4852  CA  ALA B 258    24141  20885  26570  -3379   7705   1866       C  
ATOM   4853  C   ALA B 258     -25.258 -22.801  -6.768  1.00190.50           C  
ANISOU 4853  C   ALA B 258    23638  21260  27484  -3678   7662   1870       C  
ATOM   4854  O   ALA B 258     -25.133 -23.872  -6.172  1.00187.86           O  
ANISOU 4854  O   ALA B 258    22880  21116  27381  -3458   7479   1635       O  
ATOM   4855  CB  ALA B 258     -27.764 -22.659  -6.777  1.00184.86           C  
ANISOU 4855  CB  ALA B 258    24041  20271  25927  -3101   7127   1615       C  
ATOM   4856  N   THR B 259     -24.312 -21.868  -6.790  1.00195.78           N  
ANISOU 4856  N   THR B 259    24118  21813  28457  -4181   7842   2152       N  
ATOM   4857  CA  THR B 259     -23.092 -21.972  -5.999  1.00198.53           C  
ANISOU 4857  CA  THR B 259    23734  22252  29448  -4521   7771   2173       C  
ATOM   4858  C   THR B 259     -22.977 -20.817  -5.019  1.00199.45           C  
ANISOU 4858  C   THR B 259    23950  21981  29850  -4967   7325   2258       C  
ATOM   4859  O   THR B 259     -22.862 -19.652  -5.426  1.00203.29           O  
ANISOU 4859  O   THR B 259    24755  22189  30295  -5330   7459   2530       O  
ATOM   4860  CB  THR B 259     -21.840 -21.996  -6.894  1.00202.99           C  
ANISOU 4860  CB  THR B 259    23806  23091  30228  -4765   8419   2420       C  
ATOM   4861  OG1 THR B 259     -21.858 -23.170  -7.710  1.00202.47           O  
ANISOU 4861  OG1 THR B 259    23583  23414  29933  -4307   8801   2275       O  
ATOM   4862  CG2 THR B 259     -20.579 -22.007  -6.046  1.00206.30           C  
ANISOU 4862  CG2 THR B 259    23445  23597  31344  -5146   8307   2447       C  
ATOM   4863  N   ALA B 260     -22.970 -21.147  -3.731  1.00201.32           N  
ANISOU 4863  N   ALA B 260    23911  22198  30383  -4940   6792   2030       N  
ATOM   4864  CA  ALA B 260     -22.936 -20.132  -2.688  1.00201.93           C  
ANISOU 4864  CA  ALA B 260    24098  21925  30702  -5295   6288   2027       C  
ATOM   4865  C   ALA B 260     -22.731 -20.743  -1.309  1.00199.30           C  
ANISOU 4865  C   ALA B 260    23320  21704  30701  -5218   5765   1770       C  
ATOM   4866  O   ALA B 260     -23.094 -21.899  -1.069  1.00195.20           O  
ANISOU 4866  O   ALA B 260    22642  21442  30083  -4798   5681   1576       O  
ATOM   4867  CB  ALA B 260     -24.222 -19.301  -2.705  1.00200.78           C  
ANISOU 4867  CB  ALA B 260    24793  21414  30078  -5167   6020   2002       C  
ATOM   4868  N   PRO B 261     -22.090 -19.974  -0.413  1.00204.36           N  
ANISOU 4868  N   PRO B 261    23741  22150  31756  -5640   5414   1782       N  
ATOM   4869  CA  PRO B 261     -22.080 -20.261   1.024  1.00202.01           C  
ANISOU 4869  CA  PRO B 261    23193  21888  31676  -5577   4803   1535       C  
ATOM   4870  C   PRO B 261     -23.362 -19.736   1.675  1.00197.70           C  
ANISOU 4870  C   PRO B 261    23324  21072  30721  -5369   4316   1362       C  
ATOM   4871  O   PRO B 261     -23.847 -18.677   1.270  1.00198.84           O  
ANISOU 4871  O   PRO B 261    24035  20869  30645  -5512   4333   1457       O  
ATOM   4872  CB  PRO B 261     -20.838 -19.515   1.527  1.00200.18           C  
ANISOU 4872  CB  PRO B 261    22486  21543  32032  -6148   4669   1624       C  
ATOM   4873  CG  PRO B 261     -20.668 -18.372   0.574  1.00204.77           C  
ANISOU 4873  CG  PRO B 261    23397  21815  32592  -6548   5026   1908       C  
ATOM   4874  CD  PRO B 261     -21.208 -18.838  -0.759  1.00203.12           C  
ANISOU 4874  CD  PRO B 261    23495  21757  31926  -6231   5606   2048       C  
ATOM   4875  N   ARG B 262     -23.944 -20.537   2.568  1.00202.61           N  
ANISOU 4875  N   ARG B 262    23894  21877  31210  -4995   3939   1133       N  
ATOM   4876  CA  ARG B 262     -25.159 -20.225   3.346  1.00198.43           C  
ANISOU 4876  CA  ARG B 262    23899  21202  30293  -4735   3461    940       C  
ATOM   4877  C   ARG B 262     -26.477 -19.977   2.556  1.00195.18           C  
ANISOU 4877  C   ARG B 262    24204  20651  29305  -4434   3615    950       C  
ATOM   4878  O   ARG B 262     -27.304 -19.164   2.975  1.00194.03           O  
ANISOU 4878  O   ARG B 262    24575  20257  28890  -4374   3284    850       O  
ATOM   4879  CB  ARG B 262     -24.877 -19.025   4.291  1.00193.58           C  
ANISOU 4879  CB  ARG B 262    23392  20279  29880  -5085   2981    857       C  
ATOM   4880  CG  ARG B 262     -24.928 -17.614   3.694  1.00197.27           C  
ANISOU 4880  CG  ARG B 262    24352  20287  30313  -5424   3071    993       C  
ATOM   4881  CD  ARG B 262     -24.128 -16.590   4.494  1.00202.30           C  
ANISOU 4881  CD  ARG B 262    24848  20635  31382  -5903   2683    943       C  
ATOM   4882  NE  ARG B 262     -23.972 -15.347   3.738  1.00206.87           N  
ANISOU 4882  NE  ARG B 262    25813  20757  32031  -6293   2867   1150       N  
ATOM   4883  CZ  ARG B 262     -23.545 -14.195   4.249  1.00211.56           C  
ANISOU 4883  CZ  ARG B 262    26513  20942  32929  -6715   2521   1115       C  
ATOM   4884  NH1 ARG B 262     -23.227 -14.105   5.535  1.00212.30           N  
ANISOU 4884  NH1 ARG B 262    26353  21052  33259  -6787   1954    845       N  
ATOM   4885  NH2 ARG B 262     -23.443 -13.126   3.469  1.00215.89           N  
ANISOU 4885  NH2 ARG B 262    27438  21050  33539  -7062   2727   1352       N  
ATOM   4886  N   PRO B 263     -26.716 -20.705   1.443  1.00195.89           N  
ANISOU 4886  N   PRO B 263    24327  20915  29187  -4203   4084   1041       N  
ATOM   4887  CA  PRO B 263     -28.113 -20.639   1.005  1.00192.04           C  
ANISOU 4887  CA  PRO B 263    24472  20354  28140  -3837   4071    975       C  
ATOM   4888  C   PRO B 263     -28.886 -21.932   1.280  1.00186.92           C  
ANISOU 4888  C   PRO B 263    23726  20007  27288  -3373   3969    808       C  
ATOM   4889  O   PRO B 263     -28.785 -22.895   0.519  1.00186.23           O  
ANISOU 4889  O   PRO B 263    23445  20134  27181  -3189   4316    832       O  
ATOM   4890  CB  PRO B 263     -27.977 -20.380  -0.497  1.00191.79           C  
ANISOU 4890  CB  PRO B 263    24663  20261  27947  -3905   4631   1192       C  
ATOM   4891  CG  PRO B 263     -26.739 -21.143  -0.866  1.00194.63           C  
ANISOU 4891  CG  PRO B 263    24360  20888  28703  -4056   5008   1291       C  
ATOM   4892  CD  PRO B 263     -25.850 -21.197   0.354  1.00196.03           C  
ANISOU 4892  CD  PRO B 263    23986  21109  29386  -4305   4660   1219       C  
ATOM   4893  N   LEU B 264     -29.644 -21.955   2.371  1.00187.85           N  
ANISOU 4893  N   LEU B 264    23971  20142  27260  -3187   3493    638       N  
ATOM   4894  CA  LEU B 264     -30.372 -23.163   2.751  1.00183.47           C  
ANISOU 4894  CA  LEU B 264    23297  19860  26551  -2795   3367    517       C  
ATOM   4895  C   LEU B 264     -31.582 -23.488   1.852  1.00180.43           C  
ANISOU 4895  C   LEU B 264    23347  19503  25705  -2446   3549    481       C  
ATOM   4896  O   LEU B 264     -31.789 -24.656   1.506  1.00178.45           O  
ANISOU 4896  O   LEU B 264    22904  19460  25440  -2204   3698    446       O  
ATOM   4897  CB  LEU B 264     -30.821 -23.063   4.218  1.00181.89           C  
ANISOU 4897  CB  LEU B 264    23091  19715  26304  -2707   2823    375       C  
ATOM   4898  CG  LEU B 264     -29.742 -22.890   5.293  1.00184.60           C  
ANISOU 4898  CG  LEU B 264    22989  20086  27064  -2983   2537    361       C  
ATOM   4899  CD1 LEU B 264     -30.378 -22.664   6.659  1.00182.93           C  
ANISOU 4899  CD1 LEU B 264    22901  19939  26665  -2839   2004    204       C  
ATOM   4900  CD2 LEU B 264     -28.829 -24.108   5.335  1.00185.15           C  
ANISOU 4900  CD2 LEU B 264    22419  20411  27518  -2978   2684    425       C  
ATOM   4901  N   PRO B 265     -32.376 -22.471   1.451  1.00186.32           N  
ANISOU 4901  N   PRO B 265    24677  20027  26088  -2409   3518    479       N  
ATOM   4902  CA  PRO B 265     -33.481 -22.860   0.569  1.00183.76           C  
ANISOU 4902  CA  PRO B 265    24711  19768  25343  -2064   3677    435       C  
ATOM   4903  C   PRO B 265     -33.371 -22.371  -0.877  1.00186.31           C  
ANISOU 4903  C   PRO B 265    25355  19953  25480  -2119   4106    574       C  
ATOM   4904  O   PRO B 265     -34.409 -22.195  -1.517  1.00184.90           O  
ANISOU 4904  O   PRO B 265    25637  19738  24877  -1862   4133    534       O  
ATOM   4905  CB  PRO B 265     -34.680 -22.198   1.247  1.00182.38           C  
ANISOU 4905  CB  PRO B 265    24967  19507  24821  -1872   3277    308       C  
ATOM   4906  CG  PRO B 265     -34.105 -20.883   1.722  1.00185.66           C  
ANISOU 4906  CG  PRO B 265    25530  19629  25384  -2192   3106    352       C  
ATOM   4907  CD  PRO B 265     -32.637 -21.153   2.066  1.00188.38           C  
ANISOU 4907  CD  PRO B 265    25306  20018  26254  -2546   3193    442       C  
ATOM   4908  N   TRP B 266     -32.164 -22.139  -1.383  1.00180.12           N  
ANISOU 4908  N   TRP B 266    24334  19116  24988  -2439   4435    744       N  
ATOM   4909  CA  TRP B 266     -32.034 -21.630  -2.747  1.00183.15           C  
ANISOU 4909  CA  TRP B 266    25033  19395  25161  -2501   4868    920       C  
ATOM   4910  C   TRP B 266     -31.821 -22.744  -3.780  1.00183.27           C  
ANISOU 4910  C   TRP B 266    24833  19687  25113  -2302   5296    912       C  
ATOM   4911  O   TRP B 266     -31.475 -23.878  -3.437  1.00181.85           O  
ANISOU 4911  O   TRP B 266    24174  19738  25183  -2196   5291    797       O  
ATOM   4912  CB  TRP B 266     -30.896 -20.602  -2.847  1.00192.48           C  
ANISOU 4912  CB  TRP B 266    26133  20351  26650  -2986   5032   1152       C  
ATOM   4913  CG  TRP B 266     -31.282 -19.183  -2.438  1.00193.83           C  
ANISOU 4913  CG  TRP B 266    26794  20127  26727  -3158   4726   1200       C  
ATOM   4914  CD1 TRP B 266     -30.813 -18.483  -1.359  1.00195.32           C  
ANISOU 4914  CD1 TRP B 266    26861  20109  27243  -3455   4367   1167       C  
ATOM   4915  CD2 TRP B 266     -32.242 -18.324  -3.082  1.00194.06           C  
ANISOU 4915  CD2 TRP B 266    27522  19910  26303  -3005   4713   1260       C  
ATOM   4916  NE1 TRP B 266     -31.396 -17.237  -1.311  1.00196.63           N  
ANISOU 4916  NE1 TRP B 266    27612  19891  27207  -3502   4144   1194       N  
ATOM   4917  CE2 TRP B 266     -32.280 -17.116  -2.352  1.00195.85           C  
ANISOU 4917  CE2 TRP B 266    28022  19759  26633  -3222   4351   1263       C  
ATOM   4918  CE3 TRP B 266     -33.066 -18.456  -4.209  1.00193.28           C  
ANISOU 4918  CE3 TRP B 266    27847  19870  25720  -2688   4951   1299       C  
ATOM   4919  CZ2 TRP B 266     -33.107 -16.048  -2.712  1.00196.88           C  
ANISOU 4919  CZ2 TRP B 266    28836  19550  26417  -3121   4228   1315       C  
ATOM   4920  CZ3 TRP B 266     -33.888 -17.393  -4.564  1.00194.23           C  
ANISOU 4920  CZ3 TRP B 266    28634  19685  25481  -2592   4825   1366       C  
ATOM   4921  CH2 TRP B 266     -33.901 -16.207  -3.817  1.00196.01           C  
ANISOU 4921  CH2 TRP B 266    29121  19517  25838  -2802   4472   1380       C  
ATOM   4922  N   GLY B 267     -32.064 -22.399  -5.044  1.00174.63           N  
ANISOU 4922  N   GLY B 267    24129  18557  23663  -2223   5645   1026       N  
ATOM   4923  CA  GLY B 267     -31.875 -23.298  -6.169  1.00175.64           C  
ANISOU 4923  CA  GLY B 267    24141  18939  23653  -2017   6076   1005       C  
ATOM   4924  C   GLY B 267     -32.531 -22.783  -7.440  1.00177.19           C  
ANISOU 4924  C   GLY B 267    24932  19084  23307  -1847   6326   1099       C  
ATOM   4925  O   GLY B 267     -33.541 -22.086  -7.386  1.00175.65           O  
ANISOU 4925  O   GLY B 267    25255  18701  22783  -1726   6065   1085       O  
ATOM   4926  N   SER B 268     -31.941 -23.106  -8.587  1.00171.61           N  
ANISOU 4926  N   SER B 268    24149  18562  22492  -1818   6832   1195       N  
ATOM   4927  CA  SER B 268     -32.446 -22.655  -9.885  1.00173.92           C  
ANISOU 4927  CA  SER B 268    24993  18855  22235  -1648   7116   1312       C  
ATOM   4928  C   SER B 268     -33.627 -23.535 -10.344  1.00170.47           C  
ANISOU 4928  C   SER B 268    24797  18584  21390  -1142   6976   1015       C  
ATOM   4929  O   SER B 268     -33.890 -24.569  -9.726  1.00166.85           O  
ANISOU 4929  O   SER B 268    24016  18247  21133   -966   6735    750       O  
ATOM   4930  CB  SER B 268     -31.307 -22.656 -10.915  1.00178.53           C  
ANISOU 4930  CB  SER B 268    25377  19623  22835  -1813   7737   1539       C  
ATOM   4931  OG  SER B 268     -30.929 -23.972 -11.271  1.00178.39           O  
ANISOU 4931  OG  SER B 268    24933  19948  22899  -1568   7964   1321       O  
ATOM   4932  N   PRO B 269     -34.341 -23.130 -11.420  1.00170.85           N  
ANISOU 4932  N   PRO B 269    25408  18632  20876   -916   7108   1068       N  
ATOM   4933  CA  PRO B 269     -35.463 -23.922 -11.949  1.00168.28           C  
ANISOU 4933  CA  PRO B 269    25317  18468  20152   -445   6964    776       C  
ATOM   4934  C   PRO B 269     -35.147 -25.393 -12.251  1.00167.82           C  
ANISOU 4934  C   PRO B 269    24829  18708  20228   -223   7125    505       C  
ATOM   4935  O   PRO B 269     -36.022 -26.256 -12.115  1.00164.45           O  
ANISOU 4935  O   PRO B 269    24399  18356  19729     83   6837    203       O  
ATOM   4936  CB  PRO B 269     -35.818 -23.178 -13.239  1.00171.96           C  
ANISOU 4936  CB  PRO B 269    26382  18929  20026   -310   7224    956       C  
ATOM   4937  CG  PRO B 269     -35.528 -21.769 -12.920  1.00174.12           C  
ANISOU 4937  CG  PRO B 269    26907  18879  20370   -665   7204   1304       C  
ATOM   4938  CD  PRO B 269     -34.289 -21.799 -12.057  1.00174.85           C  
ANISOU 4938  CD  PRO B 269    26416  18928  21092  -1091   7293   1410       C  
ATOM   4939  N   GLU B 270     -33.917 -25.670 -12.662  1.00171.57           N  
ANISOU 4939  N   GLU B 270    24938  19343  20909   -372   7575    610       N  
ATOM   4940  CA  GLU B 270     -33.521 -27.022 -13.029  1.00172.04           C  
ANISOU 4940  CA  GLU B 270    24603  19671  21095   -133   7759    346       C  
ATOM   4941  C   GLU B 270     -33.716 -28.013 -11.863  1.00167.50           C  
ANISOU 4941  C   GLU B 270    23599  19056  20987    -81   7343     95       C  
ATOM   4942  O   GLU B 270     -34.186 -29.141 -12.061  1.00165.96           O  
ANISOU 4942  O   GLU B 270    23322  18968  20767    241   7229   -213       O  
ATOM   4943  CB  GLU B 270     -32.059 -27.027 -13.512  1.00177.26           C  
ANISOU 4943  CB  GLU B 270    24874  20517  21959   -336   8316    531       C  
ATOM   4944  CG  GLU B 270     -31.801 -26.401 -14.913  1.00182.80           C  
ANISOU 4944  CG  GLU B 270    25942  21373  22139   -299   8841    754       C  
ATOM   4945  CD  GLU B 270     -31.949 -24.875 -14.972  1.00184.50           C  
ANISOU 4945  CD  GLU B 270    26617  21337  22148   -606   8855   1155       C  
ATOM   4946  OE1 GLU B 270     -31.927 -24.213 -13.912  1.00182.37           O  
ANISOU 4946  OE1 GLU B 270    26284  20781  22227   -923   8538   1283       O  
ATOM   4947  OE2 GLU B 270     -32.084 -24.335 -16.093  1.00188.38           O  
ANISOU 4947  OE2 GLU B 270    27551  21909  22115   -515   9176   1342       O  
ATOM   4948  N   PHE B 271     -33.377 -27.574 -10.651  1.00165.72           N  
ANISOU 4948  N   PHE B 271    23125  18666  21175   -398   7100    233       N  
ATOM   4949  CA  PHE B 271     -33.535 -28.381  -9.431  1.00161.76           C  
ANISOU 4949  CA  PHE B 271    22236  18128  21097   -382   6694     66       C  
ATOM   4950  C   PHE B 271     -35.008 -28.707  -9.099  1.00157.31           C  
ANISOU 4950  C   PHE B 271    21967  17499  20305   -119   6243   -138       C  
ATOM   4951  O   PHE B 271     -35.366 -29.850  -8.726  1.00154.96           O  
ANISOU 4951  O   PHE B 271    21426  17256  20195     71   6026   -359       O  
ATOM   4952  CB  PHE B 271     -32.890 -27.654  -8.244  1.00161.42           C  
ANISOU 4952  CB  PHE B 271    21937  17938  21456   -777   6520    271       C  
ATOM   4953  CG  PHE B 271     -31.381 -27.660  -8.262  1.00165.39           C  
ANISOU 4953  CG  PHE B 271    21942  18536  22362  -1046   6869    423       C  
ATOM   4954  CD1 PHE B 271     -30.661 -26.751  -7.503  1.00166.74           C  
ANISOU 4954  CD1 PHE B 271    21942  18571  22840  -1456   6801    644       C  
ATOM   4955  CD2 PHE B 271     -30.687 -28.590  -9.010  1.00168.08           C  
ANISOU 4955  CD2 PHE B 271    21964  19109  22791   -879   7241    319       C  
ATOM   4956  CE1 PHE B 271     -29.288 -26.761  -7.502  1.00170.70           C  
ANISOU 4956  CE1 PHE B 271    21938  19179  23739  -1718   7102    780       C  
ATOM   4957  CE2 PHE B 271     -29.312 -28.601  -9.017  1.00172.05           C  
ANISOU 4957  CE2 PHE B 271    21964  19737  23671  -1108   7568    453       C  
ATOM   4958  CZ  PHE B 271     -28.611 -27.685  -8.258  1.00173.34           C  
ANISOU 4958  CZ  PHE B 271    21932  19777  24154  -1542   7498    694       C  
ATOM   4959  N   ILE B 272     -35.849 -27.684  -9.236  1.00156.60           N  
ANISOU 4959  N   ILE B 272    22388  17284  19827   -115   6103    -49       N  
ATOM   4960  CA  ILE B 272     -37.288 -27.816  -9.065  1.00153.14           C  
ANISOU 4960  CA  ILE B 272    22259  16818  19110    141   5715   -222       C  
ATOM   4961  C   ILE B 272     -37.802 -28.862 -10.033  1.00153.47           C  
ANISOU 4961  C   ILE B 272    22367  17017  18927    494   5795   -486       C  
ATOM   4962  O   ILE B 272     -38.501 -29.800  -9.639  1.00150.75           O  
ANISOU 4962  O   ILE B 272    21875  16707  18696    667   5502   -704       O  
ATOM   4963  CB  ILE B 272     -38.019 -26.483  -9.320  1.00155.76           C  
ANISOU 4963  CB  ILE B 272    23168  17002  19010    140   5621    -84       C  
ATOM   4964  CG1 ILE B 272     -37.485 -25.389  -8.398  1.00156.08           C  
ANISOU 4964  CG1 ILE B 272    23181  16838  19284   -213   5523    150       C  
ATOM   4965  CG2 ILE B 272     -39.504 -26.639  -9.097  1.00152.44           C  
ANISOU 4965  CG2 ILE B 272    23001  16594  18326    421   5214   -275       C  
ATOM   4966  CD1 ILE B 272     -37.956 -23.992  -8.760  1.00157.68           C  
ANISOU 4966  CD1 ILE B 272    23964  16835  19112   -244   5492    323       C  
ATOM   4967  N   GLY B 273     -37.414 -28.709 -11.297  1.00157.27           N  
ANISOU 4967  N   GLY B 273    23060  17598  19098    589   6195   -460       N  
ATOM   4968  CA  GLY B 273     -37.781 -29.649 -12.341  1.00158.55           C  
ANISOU 4968  CA  GLY B 273    23312  17925  19005    940   6303   -738       C  
ATOM   4969  C   GLY B 273     -37.358 -31.072 -12.032  1.00157.93           C  
ANISOU 4969  C   GLY B 273    22727  17914  19366   1029   6271   -974       C  
ATOM   4970  O   GLY B 273     -38.077 -32.023 -12.353  1.00157.10           O  
ANISOU 4970  O   GLY B 273    22651  17849  19192   1309   6089  -1273       O  
ATOM   4971  N   LEU B 274     -36.190 -31.219 -11.411  1.00158.70           N  
ANISOU 4971  N   LEU B 274    22358  18006  19933    792   6426   -842       N  
ATOM   4972  CA  LEU B 274     -35.702 -32.538 -11.011  1.00158.39           C  
ANISOU 4972  CA  LEU B 274    21817  17998  20364    875   6375  -1032       C  
ATOM   4973  C   LEU B 274     -36.583 -33.211  -9.964  1.00154.07           C  
ANISOU 4973  C   LEU B 274    21140  17326  20072    912   5863  -1148       C  
ATOM   4974  O   LEU B 274     -37.128 -34.301 -10.196  1.00153.56           O  
ANISOU 4974  O   LEU B 274    21033  17257  20058   1159   5702  -1419       O  
ATOM   4975  CB  LEU B 274     -34.281 -32.429 -10.468  1.00160.24           C  
ANISOU 4975  CB  LEU B 274    21568  18260  21054    603   6607   -836       C  
ATOM   4976  CG  LEU B 274     -33.187 -32.280 -11.517  1.00165.44           C  
ANISOU 4976  CG  LEU B 274    22141  19108  21609    610   7174   -778       C  
ATOM   4977  CD1 LEU B 274     -31.869 -31.969 -10.838  1.00167.17           C  
ANISOU 4977  CD1 LEU B 274    21867  19348  22300    277   7346   -542       C  
ATOM   4978  CD2 LEU B 274     -33.083 -33.555 -12.344  1.00167.60           C  
ANISOU 4978  CD2 LEU B 274    22294  19522  21863    991   7328  -1120       C  
ATOM   4979  N   GLY B 275     -36.720 -32.561  -8.810  1.00151.37           N  
ANISOU 4979  N   GLY B 275    20736  16887  19890    664   5607   -941       N  
ATOM   4980  CA  GLY B 275     -37.487 -33.147  -7.721  1.00147.68           C  
ANISOU 4980  CA  GLY B 275    20111  16347  19655    674   5156   -994       C  
ATOM   4981  C   GLY B 275     -38.922 -33.398  -8.138  1.00146.03           C  
ANISOU 4981  C   GLY B 275    20242  16138  19104    915   4909  -1189       C  
ATOM   4982  O   GLY B 275     -39.527 -34.408  -7.763  1.00144.46           O  
ANISOU 4982  O   GLY B 275    19875  15908  19104   1025   4636  -1336       O  
ATOM   4983  N   PHE B 276     -39.456 -32.464  -8.923  1.00146.79           N  
ANISOU 4983  N   PHE B 276    20811  16263  18698    989   4999  -1173       N  
ATOM   4984  CA  PHE B 276     -40.806 -32.563  -9.456  1.00145.84           C  
ANISOU 4984  CA  PHE B 276    21040  16173  18200   1236   4776  -1363       C  
ATOM   4985  C   PHE B 276     -40.928 -33.740 -10.414  1.00147.75           C  
ANISOU 4985  C   PHE B 276    21251  16466  18421   1503   4843  -1676       C  
ATOM   4986  O   PHE B 276     -41.947 -34.427 -10.427  1.00146.53           O  
ANISOU 4986  O   PHE B 276    21124  16301  18249   1661   4539  -1884       O  
ATOM   4987  CB  PHE B 276     -41.205 -31.266 -10.157  1.00146.97           C  
ANISOU 4987  CB  PHE B 276    21707  16331  17805   1279   4880  -1258       C  
ATOM   4988  CG  PHE B 276     -42.629 -31.250 -10.643  1.00146.14           C  
ANISOU 4988  CG  PHE B 276    21955  16275  17297   1543   4611  -1442       C  
ATOM   4989  CD1 PHE B 276     -43.681 -31.052  -9.761  1.00143.06           C  
ANISOU 4989  CD1 PHE B 276    21571  15869  16914   1541   4215  -1435       C  
ATOM   4990  CD2 PHE B 276     -42.914 -31.422 -11.989  1.00148.84           C  
ANISOU 4990  CD2 PHE B 276    22610  16711  17233   1809   4752  -1629       C  
ATOM   4991  CE1 PHE B 276     -44.990 -31.035 -10.214  1.00142.66           C  
ANISOU 4991  CE1 PHE B 276    21798  15893  16514   1788   3962  -1609       C  
ATOM   4992  CE2 PHE B 276     -44.221 -31.403 -12.446  1.00148.43           C  
ANISOU 4992  CE2 PHE B 276    22862  16718  16815   2059   4473  -1812       C  
ATOM   4993  CZ  PHE B 276     -45.258 -31.210 -11.558  1.00145.32           C  
ANISOU 4993  CZ  PHE B 276    22438  16305  16473   2041   4076  -1800       C  
ATOM   4994  N   LEU B 277     -39.898 -33.979 -11.220  1.00151.14           N  
ANISOU 4994  N   LEU B 277    21613  16957  18857   1557   5234  -1723       N  
ATOM   4995  CA  LEU B 277     -39.906 -35.159 -12.077  1.00153.43           C  
ANISOU 4995  CA  LEU B 277    21848  17287  19160   1836   5291  -2063       C  
ATOM   4996  C   LEU B 277     -39.869 -36.439 -11.264  1.00152.01           C  
ANISOU 4996  C   LEU B 277    21228  16980  19550   1825   5032  -2188       C  
ATOM   4997  O   LEU B 277     -40.416 -37.445 -11.687  1.00152.77           O  
ANISOU 4997  O   LEU B 277    21328  17026  19693   2041   4859  -2493       O  
ATOM   4998  CB  LEU B 277     -38.741 -35.154 -13.063  1.00157.83           C  
ANISOU 4998  CB  LEU B 277    22388  17978  19601   1920   5798  -2089       C  
ATOM   4999  CG  LEU B 277     -39.024 -34.460 -14.394  1.00160.79           C  
ANISOU 4999  CG  LEU B 277    23272  18511  19311   2112   6044  -2130       C  
ATOM   5000  CD1 LEU B 277     -38.091 -34.998 -15.463  1.00165.64           C  
ANISOU 5000  CD1 LEU B 277    23815  19299  19821   2320   6484  -2302       C  
ATOM   5001  CD2 LEU B 277     -40.483 -34.620 -14.794  1.00159.56           C  
ANISOU 5001  CD2 LEU B 277    23479  18343  18804   2347   5673  -2370       C  
ATOM   5002  N   VAL B 278     -39.204 -36.409 -10.114  1.00150.40           N  
ANISOU 5002  N   VAL B 278    20653  16709  19784   1576   4993  -1952       N  
ATOM   5003  CA  VAL B 278     -39.230 -37.556  -9.207  1.00149.04           C  
ANISOU 5003  CA  VAL B 278    20081  16400  20146   1549   4709  -1999       C  
ATOM   5004  C   VAL B 278     -40.624 -37.806  -8.672  1.00146.13           C  
ANISOU 5004  C   VAL B 278    19808  15966  19751   1553   4268  -2037       C  
ATOM   5005  O   VAL B 278     -41.114 -38.933  -8.673  1.00146.39           O  
ANISOU 5005  O   VAL B 278    19717  15884  20020   1667   4038  -2232       O  
ATOM   5006  CB  VAL B 278     -38.286 -37.365  -8.016  1.00148.00           C  
ANISOU 5006  CB  VAL B 278    19556  16243  20435   1285   4721  -1708       C  
ATOM   5007  CG1 VAL B 278     -38.508 -38.457  -6.971  1.00146.42           C  
ANISOU 5007  CG1 VAL B 278    19003  15903  20727   1254   4371  -1693       C  
ATOM   5008  CG2 VAL B 278     -36.855 -37.347  -8.498  1.00151.40           C  
ANISOU 5008  CG2 VAL B 278    19775  16748  21003   1282   5141  -1691       C  
ATOM   5009  N   PHE B 279     -41.249 -36.731  -8.212  1.00145.01           N  
ANISOU 5009  N   PHE B 279    19874  15890  19331   1426   4151  -1846       N  
ATOM   5010  CA  PHE B 279     -42.563 -36.798  -7.594  1.00142.37           C  
ANISOU 5010  CA  PHE B 279    19593  15554  18947   1416   3759  -1838       C  
ATOM   5011  C   PHE B 279     -43.586 -37.316  -8.595  1.00143.51           C  
ANISOU 5011  C   PHE B 279    19980  15705  18844   1659   3625  -2153       C  
ATOM   5012  O   PHE B 279     -44.336 -38.261  -8.322  1.00143.05           O  
ANISOU 5012  O   PHE B 279    19765  15571  19017   1690   3328  -2274       O  
ATOM   5013  CB  PHE B 279     -42.963 -35.418  -7.090  1.00139.14           C  
ANISOU 5013  CB  PHE B 279    19411  15235  18219   1296   3708  -1619       C  
ATOM   5014  CG  PHE B 279     -43.836 -35.446  -5.890  1.00136.34           C  
ANISOU 5014  CG  PHE B 279    18913  14914  17977   1200   3353  -1494       C  
ATOM   5015  CD1 PHE B 279     -43.285 -35.309  -4.630  1.00134.96           C  
ANISOU 5015  CD1 PHE B 279    18449  14737  18091    991   3288  -1250       C  
ATOM   5016  CD2 PHE B 279     -45.191 -35.612  -6.008  1.00135.49           C  
ANISOU 5016  CD2 PHE B 279    18934  14870  17675   1324   3086  -1618       C  
ATOM   5017  CE1 PHE B 279     -44.065 -35.328  -3.512  1.00132.82           C  
ANISOU 5017  CE1 PHE B 279    18045  14544  17876    922   2989  -1123       C  
ATOM   5018  CE2 PHE B 279     -45.984 -35.637  -4.884  1.00133.35           C  
ANISOU 5018  CE2 PHE B 279    18494  14679  17495   1238   2797  -1482       C  
ATOM   5019  CZ  PHE B 279     -45.417 -35.495  -3.632  1.00132.04           C  
ANISOU 5019  CZ  PHE B 279    18061  14526  17581   1043   2760  -1229       C  
ATOM   5020  N   VAL B 280     -43.591 -36.682  -9.761  1.00144.18           N  
ANISOU 5020  N   VAL B 280    20445  15879  18457   1823   3841  -2274       N  
ATOM   5021  CA  VAL B 280     -44.413 -37.087 -10.888  1.00146.05           C  
ANISOU 5021  CA  VAL B 280    20955  16152  18387   2090   3746  -2604       C  
ATOM   5022  C   VAL B 280     -44.105 -38.522 -11.303  1.00148.36           C  
ANISOU 5022  C   VAL B 280    21028  16321  19023   2222   3722  -2901       C  
ATOM   5023  O   VAL B 280     -45.002 -39.270 -11.671  1.00149.12           O  
ANISOU 5023  O   VAL B 280    21168  16364  19129   2359   3443  -3175       O  
ATOM   5024  CB  VAL B 280     -44.206 -36.134 -12.079  1.00148.40           C  
ANISOU 5024  CB  VAL B 280    21699  16584  18103   2248   4049  -2634       C  
ATOM   5025  CG1 VAL B 280     -44.716 -36.745 -13.374  1.00151.43           C  
ANISOU 5025  CG1 VAL B 280    22328  17022  18186   2566   4012  -3023       C  
ATOM   5026  CG2 VAL B 280     -44.889 -34.812 -11.803  1.00146.54           C  
ANISOU 5026  CG2 VAL B 280    21762  16419  17496   2188   3953  -2416       C  
ATOM   5027  N   SER B 281     -42.834 -38.903 -11.249  1.00149.84           N  
ANISOU 5027  N   SER B 281    20972  16454  19508   2188   3998  -2862       N  
ATOM   5028  CA  SER B 281     -42.437 -40.269 -11.568  1.00152.37           C  
ANISOU 5028  CA  SER B 281    21068  16625  20200   2338   3974  -3146       C  
ATOM   5029  C   SER B 281     -43.062 -41.267 -10.603  1.00150.70           C  
ANISOU 5029  C   SER B 281    20556  16205  20500   2222   3557  -3136       C  
ATOM   5030  O   SER B 281     -43.473 -42.350 -11.010  1.00152.65           O  
ANISOU 5030  O   SER B 281    20769  16291  20941   2367   3350  -3442       O  
ATOM   5031  CB  SER B 281     -40.917 -40.412 -11.553  1.00154.31           C  
ANISOU 5031  CB  SER B 281    21055  16877  20697   2323   4349  -3066       C  
ATOM   5032  OG  SER B 281     -40.308 -39.497 -12.448  1.00156.38           O  
ANISOU 5032  OG  SER B 281    21568  17349  20501   2398   4769  -3033       O  
ATOM   5033  N   ILE B 282     -43.134 -40.895  -9.329  1.00149.43           N  
ANISOU 5033  N   ILE B 282    20184  16042  20549   1958   3430  -2779       N  
ATOM   5034  CA  ILE B 282     -43.785 -41.726  -8.320  1.00147.95           C  
ANISOU 5034  CA  ILE B 282    19717  15700  20796   1818   3054  -2684       C  
ATOM   5035  C   ILE B 282     -45.275 -41.834  -8.618  1.00147.55           C  
ANISOU 5035  C   ILE B 282    19853  15674  20536   1869   2734  -2849       C  
ATOM   5036  O   ILE B 282     -45.857 -42.924  -8.577  1.00148.73           O  
ANISOU 5036  O   ILE B 282    19860  15639  21011   1878   2451  -3003       O  
ATOM   5037  CB  ILE B 282     -43.584 -41.161  -6.903  1.00146.49           C  
ANISOU 5037  CB  ILE B 282    19307  15584  20770   1550   3003  -2260       C  
ATOM   5038  CG1 ILE B 282     -42.090 -41.062  -6.579  1.00147.22           C  
ANISOU 5038  CG1 ILE B 282    19173  15661  21102   1486   3282  -2104       C  
ATOM   5039  CG2 ILE B 282     -44.311 -42.020  -5.882  1.00145.44           C  
ANISOU 5039  CG2 ILE B 282    18896  15331  21033   1411   2637  -2123       C  
ATOM   5040  CD1 ILE B 282     -41.794 -40.342  -5.289  1.00144.66           C  
ANISOU 5040  CD1 ILE B 282    18675  15433  20856   1242   3243  -1725       C  
ATOM   5041  N   ILE B 283     -45.884 -40.690  -8.923  1.00147.92           N  
ANISOU 5041  N   ILE B 283    20209  15936  20058   1901   2769  -2812       N  
ATOM   5042  CA  ILE B 283     -47.307 -40.649  -9.248  1.00147.76           C  
ANISOU 5042  CA  ILE B 283    20362  15991  19790   1975   2471  -2971       C  
ATOM   5043  C   ILE B 283     -47.653 -41.528 -10.444  1.00151.15           C  
ANISOU 5043  C   ILE B 283    20929  16315  20187   2205   2364  -3417       C  
ATOM   5044  O   ILE B 283     -48.578 -42.331 -10.380  1.00151.89           O  
ANISOU 5044  O   ILE B 283    20907  16305  20500   2184   2020  -3568       O  
ATOM   5045  CB  ILE B 283     -47.773 -39.219  -9.549  1.00146.86           C  
ANISOU 5045  CB  ILE B 283    20608  16115  19077   2041   2553  -2888       C  
ATOM   5046  CG1 ILE B 283     -47.568 -38.327  -8.326  1.00143.79           C  
ANISOU 5046  CG1 ILE B 283    20103  15816  18714   1826   2594  -2494       C  
ATOM   5047  CG2 ILE B 283     -49.238 -39.214  -9.946  1.00147.17           C  
ANISOU 5047  CG2 ILE B 283    20799  16255  18863   2156   2229  -3080       C  
ATOM   5048  CD1 ILE B 283     -47.730 -36.854  -8.619  1.00143.05           C  
ANISOU 5048  CD1 ILE B 283    20386  15885  18080   1892   2722  -2396       C  
ATOM   5049  N   LEU B 284     -46.889 -41.403 -11.520  1.00150.05           N  
ANISOU 5049  N   LEU B 284    21022  16204  19784   2420   2658  -3629       N  
ATOM   5050  CA  LEU B 284     -47.116 -42.217 -12.703  1.00153.80           C  
ANISOU 5050  CA  LEU B 284    21658  16600  20179   2683   2572  -4095       C  
ATOM   5051  C   LEU B 284     -46.833 -43.667 -12.390  1.00155.48           C  
ANISOU 5051  C   LEU B 284    21541  16500  21035   2648   2399  -4246       C  
ATOM   5052  O   LEU B 284     -47.461 -44.567 -12.947  1.00158.09           O  
ANISOU 5052  O   LEU B 284    21904  16677  21487   2768   2117  -4610       O  
ATOM   5053  CB  LEU B 284     -46.237 -41.753 -13.865  1.00156.50           C  
ANISOU 5053  CB  LEU B 284    22300  17086  20075   2934   2981  -4254       C  
ATOM   5054  CG  LEU B 284     -46.481 -40.349 -14.402  1.00155.93           C  
ANISOU 5054  CG  LEU B 284    22630  17287  19329   3008   3164  -4123       C  
ATOM   5055  CD1 LEU B 284     -45.438 -40.003 -15.442  1.00159.11           C  
ANISOU 5055  CD1 LEU B 284    23262  17825  19366   3211   3624  -4205       C  
ATOM   5056  CD2 LEU B 284     -47.869 -40.298 -15.003  1.00156.67           C  
ANISOU 5056  CD2 LEU B 284    22987  17466  19076   3167   2811  -4374       C  
ATOM   5057  N   CYS B 285     -45.907 -43.884 -11.464  1.00156.37           N  
ANISOU 5057  N   CYS B 285    21337  16501  21574   2478   2537  -3961       N  
ATOM   5058  CA  CYS B 285     -45.565 -45.229 -11.032  1.00158.01           C  
ANISOU 5058  CA  CYS B 285    21224  16381  22434   2439   2369  -4034       C  
ATOM   5059  C   CYS B 285     -46.758 -45.863 -10.341  1.00157.19           C  
ANISOU 5059  C   CYS B 285    20946  16116  22662   2241   1914  -3968       C  
ATOM   5060  O   CYS B 285     -46.953 -47.078 -10.411  1.00159.79           O  
ANISOU 5060  O   CYS B 285    21139  16131  23443   2258   1656  -4176       O  
ATOM   5061  CB  CYS B 285     -44.348 -45.215 -10.104  1.00156.52           C  
ANISOU 5061  CB  CYS B 285    20725  16144  22600   2301   2592  -3693       C  
ATOM   5062  SG  CYS B 285     -43.582 -46.829  -9.849  1.00159.73           S  
ANISOU 5062  SG  CYS B 285    20794  16141  23754   2370   2476  -3829       S  
ATOM   5063  N   GLU B 286     -47.548 -45.038  -9.663  1.00154.74           N  
ANISOU 5063  N   GLU B 286    20635  16019  22142   2053   1818  -3671       N  
ATOM   5064  CA  GLU B 286     -48.780 -45.517  -9.050  1.00154.24           C  
ANISOU 5064  CA  GLU B 286    20395  15888  22322   1862   1420  -3587       C  
ATOM   5065  C   GLU B 286     -49.887 -45.732 -10.097  1.00156.59           C  
ANISOU 5065  C   GLU B 286    20915  16201  22383   2014   1161  -4005       C  
ATOM   5066  O   GLU B 286     -50.594 -46.738 -10.064  1.00158.71           O  
ANISOU 5066  O   GLU B 286    21024  16241  23036   1929    816  -4152       O  
ATOM   5067  CB  GLU B 286     -49.258 -44.535  -7.977  1.00153.02           C  
ANISOU 5067  CB  GLU B 286    20150  16006  21985   1653   1420  -3156       C  
ATOM   5068  CG  GLU B 286     -50.248 -45.129  -6.989  1.00152.58           C  
ANISOU 5068  CG  GLU B 286    19779  15900  22294   1402   1084  -2932       C  
ATOM   5069  CD  GLU B 286     -49.572 -45.958  -5.913  1.00152.63           C  
ANISOU 5069  CD  GLU B 286    19433  15676  22884   1206   1062  -2619       C  
ATOM   5070  OE1 GLU B 286     -48.322 -45.953  -5.860  1.00152.58           O  
ANISOU 5070  OE1 GLU B 286    19412  15583  22980   1272   1306  -2569       O  
ATOM   5071  OE2 GLU B 286     -50.287 -46.626  -5.132  1.00153.09           O  
ANISOU 5071  OE2 GLU B 286    19219  15648  23300    990    801  -2411       O  
ATOM   5072  N   ARG B 287     -50.026 -44.775 -11.015  1.00158.19           N  
ANISOU 5072  N   ARG B 287    21483  16665  21956   2230   1314  -4182       N  
ATOM   5073  CA  ARG B 287     -51.069 -44.784 -12.052  1.00160.45           C  
ANISOU 5073  CA  ARG B 287    22020  17038  21906   2414   1071  -4574       C  
ATOM   5074  C   ARG B 287     -51.018 -46.005 -12.945  1.00164.93           C  
ANISOU 5074  C   ARG B 287    22624  17319  22721   2581    888  -5063       C  
ATOM   5075  O   ARG B 287     -52.051 -46.556 -13.313  1.00167.13           O  
ANISOU 5075  O   ARG B 287    22896  17521  23084   2584    505  -5340       O  
ATOM   5076  CB  ARG B 287     -50.962 -43.523 -12.924  1.00162.29           C  
ANISOU 5076  CB  ARG B 287    22681  17586  21395   2657   1328  -4640       C  
ATOM   5077  CG  ARG B 287     -51.965 -43.427 -14.090  1.00164.98           C  
ANISOU 5077  CG  ARG B 287    23332  18060  21292   2905   1087  -5050       C  
ATOM   5078  CD  ARG B 287     -51.840 -42.062 -14.785  1.00164.46           C  
ANISOU 5078  CD  ARG B 287    23696  18306  20484   3122   1357  -4996       C  
ATOM   5079  NE  ARG B 287     -52.737 -41.875 -15.929  1.00167.26           N  
ANISOU 5079  NE  ARG B 287    24384  18824  20342   3400   1137  -5363       N  
ATOM   5080  CZ  ARG B 287     -52.824 -40.745 -16.631  1.00167.55           C  
ANISOU 5080  CZ  ARG B 287    24832  19123  19705   3620   1298  -5334       C  
ATOM   5081  NH1 ARG B 287     -52.084 -39.696 -16.294  1.00165.22           N  
ANISOU 5081  NH1 ARG B 287    24659  18927  19188   3563   1678  -4953       N  
ATOM   5082  NH2 ARG B 287     -53.660 -40.654 -17.660  1.00170.48           N  
ANISOU 5082  NH2 ARG B 287    25497  19645  19632   3891   1057  -5675       N  
ATOM   5083  N   PHE B 288     -49.807 -46.410 -13.301  1.00162.03           N  
ANISOU 5083  N   PHE B 288    22290  16804  22472   2730   1155  -5187       N  
ATOM   5084  CA  PHE B 288     -49.602 -47.582 -14.132  1.00166.69           C  
ANISOU 5084  CA  PHE B 288    22925  17103  23305   2936   1009  -5682       C  
ATOM   5085  C   PHE B 288     -48.925 -48.677 -13.314  1.00167.35           C  
ANISOU 5085  C   PHE B 288    22652  16793  24142   2782    955  -5553       C  
ATOM   5086  O   PHE B 288     -48.058 -49.401 -13.810  1.00170.54           O  
ANISOU 5086  O   PHE B 288    23072  16983  24742   2995   1062  -5835       O  
ATOM   5087  CB  PHE B 288     -48.768 -47.206 -15.360  1.00169.16           C  
ANISOU 5087  CB  PHE B 288    23589  17593  23091   3315   1367  -5996       C  
ATOM   5088  CG  PHE B 288     -49.357 -46.077 -16.169  1.00168.82           C  
ANISOU 5088  CG  PHE B 288    23934  17935  22275   3483   1441  -6068       C  
ATOM   5089  CD1 PHE B 288     -48.879 -44.781 -16.025  1.00165.97           C  
ANISOU 5089  CD1 PHE B 288    23716  17878  21469   3462   1830  -5702       C  
ATOM   5090  CD2 PHE B 288     -50.424 -46.299 -17.028  1.00171.57           C  
ANISOU 5090  CD2 PHE B 288    24500  18325  22365   3648   1086  -6482       C  
ATOM   5091  CE1 PHE B 288     -49.426 -43.732 -16.750  1.00165.98           C  
ANISOU 5091  CE1 PHE B 288    24097  18195  20772   3623   1882  -5732       C  
ATOM   5092  CE2 PHE B 288     -50.974 -45.254 -17.759  1.00171.53           C  
ANISOU 5092  CE2 PHE B 288    24860  18675  21637   3828   1131  -6527       C  
ATOM   5093  CZ  PHE B 288     -50.476 -43.969 -17.618  1.00168.72           C  
ANISOU 5093  CZ  PHE B 288    24668  18599  20840   3820   1533  -6138       C  
ATOM   5094  N   GLY B 289     -49.331 -48.785 -12.051  1.00166.89           N  
ANISOU 5094  N   GLY B 289    22273  16653  24485   2433    790  -5116       N  
ATOM   5095  CA  GLY B 289     -48.659 -49.649 -11.098  1.00167.06           C  
ANISOU 5095  CA  GLY B 289    21956  16343  25177   2264    763  -4864       C  
ATOM   5096  C   GLY B 289     -49.141 -51.090 -11.070  1.00170.87           C  
ANISOU 5096  C   GLY B 289    22277  16346  26299   2183    337  -5079       C  
ATOM   5097  O   GLY B 289     -50.294 -51.373 -10.740  1.00171.08           O  
ANISOU 5097  O   GLY B 289    22184  16307  26510   1950    -16  -5011       O  
ATOM   5098  N   ALA B 290     -48.232 -51.999 -11.410  1.00172.01           N  
ANISOU 5098  N   ALA B 290    22405  16150  26802   2379    373  -5335       N  
ATOM   5099  CA  ALA B 290     -48.450 -53.440 -11.331  1.00176.19           C  
ANISOU 5099  CA  ALA B 290    22788  16127  28029   2322    -17  -5528       C  
ATOM   5100  C   ALA B 290     -48.094 -53.915  -9.918  1.00174.81           C  
ANISOU 5100  C   ALA B 290    22244  15717  28459   2024    -64  -4967       C  
ATOM   5101  O   ALA B 290     -47.406 -53.197  -9.194  1.00171.23           O  
ANISOU 5101  O   ALA B 290    21677  15524  27860   1962    248  -4550       O  
ATOM   5102  CB  ALA B 290     -47.618 -54.160 -12.383  1.00180.91           C  
ANISOU 5102  CB  ALA B 290    23567  16474  28696   2731     42  -6097       C  
ATOM   5103  N   PRO B 291     -48.589 -55.099  -9.501  1.00177.91           N  
ANISOU 5103  N   PRO B 291    22452  15619  29525   1825   -469  -4934       N  
ATOM   5104  CA  PRO B 291     -48.333 -55.624  -8.148  1.00177.25           C  
ANISOU 5104  CA  PRO B 291    22032  15295  30019   1537   -548  -4363       C  
ATOM   5105  C   PRO B 291     -46.872 -55.600  -7.658  1.00176.39           C  
ANISOU 5105  C   PRO B 291    21812  15166  30040   1694   -234  -4142       C  
ATOM   5106  O   PRO B 291     -46.661 -55.587  -6.442  1.00174.42           O  
ANISOU 5106  O   PRO B 291    21306  14928  30038   1457   -217  -3579       O  
ATOM   5107  CB  PRO B 291     -48.808 -57.074  -8.256  1.00182.65           C  
ANISOU 5107  CB  PRO B 291    22647  15337  31417   1441  -1012  -4566       C  
ATOM   5108  CG  PRO B 291     -49.909 -57.010  -9.231  1.00184.36           C  
ANISOU 5108  CG  PRO B 291    23058  15616  31375   1460  -1253  -5033       C  
ATOM   5109  CD  PRO B 291     -49.494 -55.987 -10.254  1.00182.53           C  
ANISOU 5109  CD  PRO B 291    23137  15849  30365   1830   -906  -5407       C  
ATOM   5110  N   ILE B 292     -45.896 -55.601  -8.566  1.00178.17           N  
ANISOU 5110  N   ILE B 292    22208  15392  30096   2089      4  -4569       N  
ATOM   5111  CA  ILE B 292     -44.486 -55.515  -8.179  1.00177.68           C  
ANISOU 5111  CA  ILE B 292    22006  15368  30135   2256    320  -4391       C  
ATOM   5112  C   ILE B 292     -44.068 -54.085  -7.826  1.00172.60           C  
ANISOU 5112  C   ILE B 292    21351  15311  28916   2197    729  -4062       C  
ATOM   5113  O   ILE B 292     -43.401 -53.855  -6.818  1.00170.53           O  
ANISOU 5113  O   ILE B 292    20853  15134  28806   2074    856  -3608       O  
ATOM   5114  CB  ILE B 292     -43.568 -56.037  -9.306  1.00182.03           C  
ANISOU 5114  CB  ILE B 292    22709  15747  30709   2722    458  -4980       C  
ATOM   5115  CG1 ILE B 292     -43.963 -57.457  -9.710  1.00187.63           C  
ANISOU 5115  CG1 ILE B 292    23466  15826  31998   2814     19  -5373       C  
ATOM   5116  CG2 ILE B 292     -42.110 -55.997  -8.873  1.00182.01           C  
ANISOU 5116  CG2 ILE B 292    22496  15795  30865   2892    772  -4787       C  
ATOM   5117  CD1 ILE B 292     -43.248 -57.959 -10.948  1.00192.47           C  
ANISOU 5117  CD1 ILE B 292    24277  16297  32554   3317    119  -6056       C  
ATOM   5118  N   MET B 293     -44.483 -53.129  -8.654  1.00172.98           N  
ANISOU 5118  N   MET B 293    21667  15745  28311   2284    905  -4294       N  
ATOM   5119  CA  MET B 293     -44.160 -51.707  -8.478  1.00168.69           C  
ANISOU 5119  CA  MET B 293    21179  15723  27193   2237   1277  -4035       C  
ATOM   5120  C   MET B 293     -44.693 -51.101  -7.177  1.00164.45           C  
ANISOU 5120  C   MET B 293    20459  15379  26645   1867   1200  -3455       C  
ATOM   5121  O   MET B 293     -44.417 -49.939  -6.867  1.00161.01           O  
ANISOU 5121  O   MET B 293    20053  15328  25797   1804   1465  -3211       O  
ATOM   5122  CB  MET B 293     -44.700 -50.894  -9.661  1.00172.03           C  
ANISOU 5122  CB  MET B 293    21967  16460  26937   2403   1405  -4394       C  
ATOM   5123  CG  MET B 293     -44.148 -51.300 -11.025  1.00176.33           C  
ANISOU 5123  CG  MET B 293    22735  16933  27328   2811   1546  -4977       C  
ATOM   5124  SD  MET B 293     -45.099 -50.571 -12.389  1.00176.91           S  
ANISOU 5124  SD  MET B 293    23261  17321  26636   2994   1551  -5403       S  
ATOM   5125  CE  MET B 293     -44.592 -48.854 -12.358  1.00172.83           C  
ANISOU 5125  CE  MET B 293    22876  17356  25435   2961   2048  -5059       C  
ATOM   5126  N   LYS B 294     -45.490 -51.875  -6.446  1.00167.64           N  
ANISOU 5126  N   LYS B 294    20687  15521  27488   1626    836  -3246       N  
ATOM   5127  CA  LYS B 294     -46.080 -51.422  -5.189  1.00164.34           C  
ANISOU 5127  CA  LYS B 294    20078  15302  27062   1291    748  -2702       C  
ATOM   5128  C   LYS B 294     -44.998 -51.159  -4.139  1.00162.58           C  
ANISOU 5128  C   LYS B 294    19629  15170  26974   1232    937  -2273       C  
ATOM   5129  O   LYS B 294     -44.065 -51.953  -3.988  1.00165.00           O  
ANISOU 5129  O   LYS B 294    19789  15181  27725   1342    936  -2271       O  
ATOM   5130  CB  LYS B 294     -47.089 -52.450  -4.668  1.00167.63           C  
ANISOU 5130  CB  LYS B 294    20323  15397  27974   1043    336  -2554       C  
ATOM   5131  CG  LYS B 294     -48.346 -52.585  -5.527  1.00169.14           C  
ANISOU 5131  CG  LYS B 294    20681  15563  28021   1027     98  -2919       C  
ATOM   5132  CD  LYS B 294     -48.675 -51.285  -6.251  1.00166.37           C  
ANISOU 5132  CD  LYS B 294    20603  15689  26922   1165    312  -3125       C  
ATOM   5133  CE  LYS B 294     -49.870 -51.449  -7.177  1.00168.37           C  
ANISOU 5133  CE  LYS B 294    21023  15925  27025   1196     49  -3529       C  
ATOM   5134  NZ  LYS B 294     -50.167 -50.181  -7.904  1.00166.05           N  
ANISOU 5134  NZ  LYS B 294    21020  16083  25986   1366    244  -3713       N  
ATOM   5135  N   SER B 295     -45.134 -50.043  -3.424  1.00164.89           N  
ANISOU 5135  N   SER B 295    19897  15870  26883   1078   1074  -1933       N  
ATOM   5136  CA  SER B 295     -44.171 -49.585  -2.409  1.00163.02           C  
ANISOU 5136  CA  SER B 295    19465  15794  26680   1010   1237  -1540       C  
ATOM   5137  C   SER B 295     -42.775 -49.296  -2.979  1.00163.74           C  
ANISOU 5137  C   SER B 295    19586  15917  26711   1246   1559  -1740       C  
ATOM   5138  O   SER B 295     -41.871 -48.871  -2.259  1.00162.59           O  
ANISOU 5138  O   SER B 295    19270  15913  26593   1204   1702  -1469       O  
ATOM   5139  CB  SER B 295     -44.043 -50.611  -1.274  1.00161.27           C  
ANISOU 5139  CB  SER B 295    18936  15298  27040    855    994  -1152       C  
ATOM   5140  OG  SER B 295     -45.308 -51.030  -0.800  1.00161.54           O  
ANISOU 5140  OG  SER B 295    18908  15276  27195    623    710   -956       O  
ATOM   5141  N   CYS B 296     -42.615 -49.502  -4.280  1.00158.95           N  
ANISOU 5141  N   CYS B 296    19183  15209  25999   1494   1673  -2218       N  
ATOM   5142  CA  CYS B 296     -41.371 -49.191  -4.958  1.00160.14           C  
ANISOU 5142  CA  CYS B 296    19364  15450  26034   1731   2023  -2429       C  
ATOM   5143  C   CYS B 296     -41.528 -47.872  -5.682  1.00158.08           C  
ANISOU 5143  C   CYS B 296    19391  15567  25104   1766   2304  -2551       C  
ATOM   5144  O   CYS B 296     -40.552 -47.297  -6.161  1.00158.59           O  
ANISOU 5144  O   CYS B 296    19485  15804  24966   1893   2650  -2632       O  
ATOM   5145  CB  CYS B 296     -40.995 -50.303  -5.936  1.00162.11           C  
ANISOU 5145  CB  CYS B 296    19652  15362  26580   2029   1996  -2885       C  
ATOM   5146  SG  CYS B 296     -40.504 -51.849  -5.143  1.00165.43           S  
ANISOU 5146  SG  CYS B 296    19742  15273  27842   2048   1700  -2746       S  
ATOM   5147  N   SER B 297     -42.772 -47.403  -5.743  1.00157.20           N  
ANISOU 5147  N   SER B 297    19478  15585  24668   1650   2149  -2543       N  
ATOM   5148  CA  SER B 297     -43.127 -46.182  -6.456  1.00155.53           C  
ANISOU 5148  CA  SER B 297    19588  15695  23813   1699   2350  -2656       C  
ATOM   5149  C   SER B 297     -42.251 -44.997  -6.056  1.00153.41           C  
ANISOU 5149  C   SER B 297    19297  15699  23291   1617   2663  -2391       C  
ATOM   5150  O   SER B 297     -41.897 -44.164  -6.891  1.00153.68           O  
ANISOU 5150  O   SER B 297    19567  15922  22904   1730   2957  -2527       O  
ATOM   5151  CB  SER B 297     -44.602 -45.844  -6.215  1.00154.25           C  
ANISOU 5151  CB  SER B 297    19547  15643  23418   1555   2083  -2582       C  
ATOM   5152  OG  SER B 297     -44.855 -45.592  -4.842  1.00151.62           O  
ANISOU 5152  OG  SER B 297    18990  15402  23216   1298   1953  -2138       O  
ATOM   5153  N   VAL B 298     -41.900 -44.930  -4.777  1.00150.53           N  
ANISOU 5153  N   VAL B 298    18655  15351  23190   1415   2587  -2006       N  
ATOM   5154  CA  VAL B 298     -41.011 -43.888  -4.288  1.00148.98           C  
ANISOU 5154  CA  VAL B 298    18394  15373  22836   1312   2828  -1763       C  
ATOM   5155  C   VAL B 298     -39.615 -44.130  -4.812  1.00151.70           C  
ANISOU 5155  C   VAL B 298    18602  15671  23366   1460   3124  -1893       C  
ATOM   5156  O   VAL B 298     -38.947 -43.223  -5.298  1.00151.91           O  
ANISOU 5156  O   VAL B 298    18730  15887  23102   1477   3446  -1912       O  
ATOM   5157  CB  VAL B 298     -40.994 -43.846  -2.760  1.00148.64           C  
ANISOU 5157  CB  VAL B 298    18079  15369  23028   1084   2629  -1348       C  
ATOM   5158  CG1 VAL B 298     -40.097 -42.755  -2.269  1.00147.41           C  
ANISOU 5158  CG1 VAL B 298    17865  15424  22719    972   2832  -1142       C  
ATOM   5159  CG2 VAL B 298     -42.395 -43.633  -2.250  1.00146.44           C  
ANISOU 5159  CG2 VAL B 298    17903  15184  22552    959   2366  -1222       C  
ATOM   5160  N   VAL B 299     -39.193 -45.382  -4.721  1.00150.51           N  
ANISOU 5160  N   VAL B 299    18212  15259  23715   1572   3012  -1979       N  
ATOM   5161  CA  VAL B 299     -37.872 -45.783  -5.161  1.00153.66           C  
ANISOU 5161  CA  VAL B 299    18420  15609  24356   1758   3266  -2123       C  
ATOM   5162  C   VAL B 299     -37.776 -45.807  -6.681  1.00156.36           C  
ANISOU 5162  C   VAL B 299    19020  15990  24401   2032   3529  -2556       C  
ATOM   5163  O   VAL B 299     -36.730 -45.495  -7.243  1.00158.45           O  
ANISOU 5163  O   VAL B 299    19220  16402  24581   2154   3892  -2646       O  
ATOM   5164  CB  VAL B 299     -37.518 -47.161  -4.589  1.00155.91           C  
ANISOU 5164  CB  VAL B 299    18393  15567  25280   1836   3024  -2093       C  
ATOM   5165  CG1 VAL B 299     -36.069 -47.522  -4.887  1.00159.29           C  
ANISOU 5165  CG1 VAL B 299    18558  15979  25986   2043   3280  -2210       C  
ATOM   5166  CG2 VAL B 299     -37.774 -47.156  -3.098  1.00153.49           C  
ANISOU 5166  CG2 VAL B 299    17875  15247  25196   1572   2742  -1641       C  
ATOM   5167  N   ILE B 300     -38.869 -46.161  -7.346  1.00156.67           N  
ANISOU 5167  N   ILE B 300    19340  15926  24263   2128   3348  -2821       N  
ATOM   5168  CA  ILE B 300     -38.897 -46.150  -8.803  1.00159.42           C  
ANISOU 5168  CA  ILE B 300    19981  16344  24248   2408   3562  -3249       C  
ATOM   5169  C   ILE B 300     -38.921 -44.724  -9.335  1.00157.96           C  
ANISOU 5169  C   ILE B 300    20078  16509  23432   2355   3872  -3173       C  
ATOM   5170  O   ILE B 300     -38.275 -44.420 -10.329  1.00160.57           O  
ANISOU 5170  O   ILE B 300    20531  17004  23473   2545   4235  -3362       O  
ATOM   5171  CB  ILE B 300     -40.085 -46.954  -9.350  1.00160.57           C  
ANISOU 5171  CB  ILE B 300    20341  16272  24398   2523   3225  -3577       C  
ATOM   5172  CG1 ILE B 300     -39.881 -48.435  -9.027  1.00163.30           C  
ANISOU 5172  CG1 ILE B 300    20432  16210  25403   2615   2958  -3701       C  
ATOM   5173  CG2 ILE B 300     -40.187 -46.801 -10.855  1.00163.41           C  
ANISOU 5173  CG2 ILE B 300    21049  16763  24276   2823   3428  -4021       C  
ATOM   5174  CD1 ILE B 300     -41.067 -49.303  -9.347  1.00164.62           C  
ANISOU 5174  CD1 ILE B 300    20749  16094  25706   2648   2555  -3970       C  
ATOM   5175  N   GLY B 301     -39.664 -43.850  -8.675  1.00154.20           N  
ANISOU 5175  N   GLY B 301    19709  16145  22734   2107   3735  -2887       N  
ATOM   5176  CA  GLY B 301     -39.644 -42.449  -9.043  1.00152.93           C  
ANISOU 5176  CA  GLY B 301    19816  16262  22030   2037   3999  -2764       C  
ATOM   5177  C   GLY B 301     -38.245 -41.886  -8.848  1.00153.83           C  
ANISOU 5177  C   GLY B 301    19715  16507  22227   1952   4367  -2562       C  
ATOM   5178  O   GLY B 301     -37.701 -41.209  -9.724  1.00155.75           O  
ANISOU 5178  O   GLY B 301    20126  16934  22119   2030   4742  -2617       O  
ATOM   5179  N   LEU B 302     -37.659 -42.204  -7.696  1.00152.87           N  
ANISOU 5179  N   LEU B 302    19205  16297  22581   1789   4252  -2319       N  
ATOM   5180  CA  LEU B 302     -36.295 -41.819  -7.367  1.00154.05           C  
ANISOU 5180  CA  LEU B 302    19058  16555  22920   1693   4534  -2132       C  
ATOM   5181  C   LEU B 302     -35.364 -42.233  -8.488  1.00158.47           C  
ANISOU 5181  C   LEU B 302    19557  17177  23476   1956   4908  -2406       C  
ATOM   5182  O   LEU B 302     -34.577 -41.437  -8.988  1.00160.13           O  
ANISOU 5182  O   LEU B 302    19778  17602  23465   1922   5301  -2341       O  
ATOM   5183  CB  LEU B 302     -35.878 -42.467  -6.049  1.00153.20           C  
ANISOU 5183  CB  LEU B 302    18526  16308  23375   1568   4277  -1910       C  
ATOM   5184  CG  LEU B 302     -34.422 -42.466  -5.600  1.00155.13           C  
ANISOU 5184  CG  LEU B 302    18349  16620  23974   1517   4471  -1763       C  
ATOM   5185  CD1 LEU B 302     -33.949 -41.076  -5.249  1.00153.90           C  
ANISOU 5185  CD1 LEU B 302    18200  16680  23595   1246   4652  -1498       C  
ATOM   5186  CD2 LEU B 302     -34.275 -43.381  -4.401  1.00154.68           C  
ANISOU 5186  CD2 LEU B 302    17937  16378  24455   1475   4125  -1595       C  
ATOM   5187  N   LEU B 303     -35.494 -43.487  -8.899  1.00160.73           N  
ANISOU 5187  N   LEU B 303    19790  17276  24006   2224   4783  -2718       N  
ATOM   5188  CA  LEU B 303     -34.697 -44.044  -9.984  1.00165.44           C  
ANISOU 5188  CA  LEU B 303    20336  17927  24598   2549   5104  -3051       C  
ATOM   5189  C   LEU B 303     -34.891 -43.295 -11.298  1.00167.10           C  
ANISOU 5189  C   LEU B 303    20949  18386  24157   2683   5443  -3227       C  
ATOM   5190  O   LEU B 303     -33.921 -42.937 -11.942  1.00170.24           O  
ANISOU 5190  O   LEU B 303    21269  19014  24402   2773   5888  -3249       O  
ATOM   5191  CB  LEU B 303     -35.029 -45.524 -10.181  1.00167.60           C  
ANISOU 5191  CB  LEU B 303    20559  17891  25228   2823   4819  -3398       C  
ATOM   5192  CG  LEU B 303     -34.359 -46.144 -11.400  1.00172.88           C  
ANISOU 5192  CG  LEU B 303    21240  18617  25830   3229   5118  -3831       C  
ATOM   5193  CD1 LEU B 303     -32.869 -46.199 -11.181  1.00175.55           C  
ANISOU 5193  CD1 LEU B 303    21134  19087  26480   3282   5444  -3727       C  
ATOM   5194  CD2 LEU B 303     -34.919 -47.522 -11.674  1.00175.05           C  
ANISOU 5194  CD2 LEU B 303    21573  18536  26403   3495   4768  -4224       C  
ATOM   5195  N   VAL B 304     -36.139 -43.087 -11.703  1.00165.42           N  
ANISOU 5195  N   VAL B 304    21149  18143  23561   2706   5233  -3345       N  
ATOM   5196  CA  VAL B 304     -36.447 -42.397 -12.955  1.00167.16           C  
ANISOU 5196  CA  VAL B 304    21799  18592  23120   2859   5499  -3505       C  
ATOM   5197  C   VAL B 304     -35.827 -41.010 -12.994  1.00166.83           C  
ANISOU 5197  C   VAL B 304    21815  18812  22761   2642   5887  -3156       C  
ATOM   5198  O   VAL B 304     -35.128 -40.646 -13.946  1.00170.48           O  
ANISOU 5198  O   VAL B 304    22358  19509  22906   2777   6336  -3214       O  
ATOM   5199  CB  VAL B 304     -37.961 -42.261 -13.173  1.00164.90           C  
ANISOU 5199  CB  VAL B 304    21917  18237  22500   2871   5142  -3620       C  
ATOM   5200  CG1 VAL B 304     -38.239 -41.367 -14.373  1.00166.61           C  
ANISOU 5200  CG1 VAL B 304    22594  18715  21995   3012   5412  -3705       C  
ATOM   5201  CG2 VAL B 304     -38.585 -43.621 -13.385  1.00166.34           C  
ANISOU 5201  CG2 VAL B 304    22084  18162  22954   3093   4785  -4015       C  
ATOM   5202  N   GLY B 305     -36.101 -40.233 -11.953  1.00162.83           N  
ANISOU 5202  N   GLY B 305    21271  18261  22336   2304   5708  -2793       N  
ATOM   5203  CA  GLY B 305     -35.559 -38.894 -11.846  1.00162.50           C  
ANISOU 5203  CA  GLY B 305    21284  18392  22067   2051   6001  -2449       C  
ATOM   5204  C   GLY B 305     -34.045 -38.933 -11.820  1.00165.65           C  
ANISOU 5204  C   GLY B 305    21268  18914  22760   2001   6390  -2346       C  
ATOM   5205  O   GLY B 305     -33.380 -38.002 -12.272  1.00167.74           O  
ANISOU 5205  O   GLY B 305    21583  19371  22778   1884   6787  -2162       O  
ATOM   5206  N   CYS B 306     -33.501 -40.029 -11.305  1.00166.43           N  
ANISOU 5206  N   CYS B 306    20940  18894  23400   2093   6272  -2458       N  
ATOM   5207  CA  CYS B 306     -32.059 -40.209 -11.239  1.00169.77           C  
ANISOU 5207  CA  CYS B 306    20899  19443  24163   2090   6603  -2396       C  
ATOM   5208  C   CYS B 306     -31.453 -40.514 -12.627  1.00175.15           C  
ANISOU 5208  C   CYS B 306    21624  20347  24579   2423   7072  -2678       C  
ATOM   5209  O   CYS B 306     -30.363 -40.044 -12.953  1.00178.48           O  
ANISOU 5209  O   CYS B 306    21819  21013  24985   2364   7522  -2547       O  
ATOM   5210  CB  CYS B 306     -31.751 -41.321 -10.228  1.00169.08           C  
ANISOU 5210  CB  CYS B 306    20370  19141  24732   2126   6279  -2426       C  
ATOM   5211  SG  CYS B 306     -30.080 -41.967 -10.200  1.00173.88           S  
ANISOU 5211  SG  CYS B 306    20359  19866  25841   2266   6591  -2472       S  
ATOM   5212  N   ILE B 307     -32.178 -41.267 -13.449  1.00176.34           N  
ANISOU 5212  N   ILE B 307    22066  20434  24501   2769   6967  -3067       N  
ATOM   5213  CA  ILE B 307     -31.774 -41.563 -14.825  1.00181.63           C  
ANISOU 5213  CA  ILE B 307    22859  21336  24816   3140   7376  -3388       C  
ATOM   5214  C   ILE B 307     -31.820 -40.317 -15.686  1.00182.96           C  
ANISOU 5214  C   ILE B 307    23399  21797  24321   3051   7770  -3206       C  
ATOM   5215  O   ILE B 307     -30.890 -40.033 -16.431  1.00187.52           O  
ANISOU 5215  O   ILE B 307    23872  22677  24700   3139   8293  -3179       O  
ATOM   5216  CB  ILE B 307     -32.671 -42.630 -15.465  1.00182.58           C  
ANISOU 5216  CB  ILE B 307    23256  21289  24829   3522   7086  -3878       C  
ATOM   5217  CG1 ILE B 307     -32.387 -43.995 -14.844  1.00183.17           C  
ANISOU 5217  CG1 ILE B 307    22945  21072  25579   3680   6790  -4094       C  
ATOM   5218  CG2 ILE B 307     -32.465 -42.669 -16.974  1.00187.90           C  
ANISOU 5218  CG2 ILE B 307    24196  22257  24942   3902   7496  -4202       C  
ATOM   5219  CD1 ILE B 307     -33.443 -45.034 -15.157  1.00183.23           C  
ANISOU 5219  CD1 ILE B 307    23210  20790  25621   3937   6356  -4515       C  
ATOM   5220  N   VAL B 308     -32.924 -39.584 -15.603  1.00179.37           N  
ANISOU 5220  N   VAL B 308    23380  21256  23517   2892   7520  -3073       N  
ATOM   5221  CA  VAL B 308     -33.017 -38.305 -16.296  1.00180.43           C  
ANISOU 5221  CA  VAL B 308    23899  21610  23049   2775   7841  -2831       C  
ATOM   5222  C   VAL B 308     -31.892 -37.383 -15.822  1.00181.31           C  
ANISOU 5222  C   VAL B 308    23695  21841  23352   2407   8192  -2393       C  
ATOM   5223  O   VAL B 308     -31.279 -36.671 -16.623  1.00185.23           O  
ANISOU 5223  O   VAL B 308    24282  22603  23493   2379   8688  -2231       O  
ATOM   5224  CB  VAL B 308     -34.390 -37.627 -16.068  1.00176.10           C  
ANISOU 5224  CB  VAL B 308    23821  20908  22180   2649   7448  -2729       C  
ATOM   5225  CG1 VAL B 308     -34.430 -36.255 -16.728  1.00177.51           C  
ANISOU 5225  CG1 VAL B 308    24406  21268  21773   2524   7764  -2435       C  
ATOM   5226  CG2 VAL B 308     -35.510 -38.508 -16.596  1.00175.81           C  
ANISOU 5226  CG2 VAL B 308    24070  20774  21955   2991   7098  -3166       C  
ATOM   5227  N   ALA B 309     -31.598 -37.435 -14.523  1.00178.13           N  
ANISOU 5227  N   ALA B 309    22908  21253  23521   2125   7931  -2203       N  
ATOM   5228  CA  ALA B 309     -30.528 -36.625 -13.948  1.00179.01           C  
ANISOU 5228  CA  ALA B 309    22670  21448  23897   1753   8181  -1820       C  
ATOM   5229  C   ALA B 309     -29.178 -36.951 -14.578  1.00184.81           C  
ANISOU 5229  C   ALA B 309    22996  22470  24753   1878   8717  -1869       C  
ATOM   5230  O   ALA B 309     -28.411 -36.049 -14.914  1.00187.91           O  
ANISOU 5230  O   ALA B 309    23316  23070  25012   1655   9151  -1581       O  
ATOM   5231  CB  ALA B 309     -30.464 -36.822 -12.444  1.00175.01           C  
ANISOU 5231  CB  ALA B 309    21804  20712  23982   1503   7754  -1681       C  
ATOM   5232  N   ALA B 310     -28.894 -38.241 -14.740  1.00186.65           N  
ANISOU 5232  N   ALA B 310    22956  22711  25253   2237   8686  -2230       N  
ATOM   5233  CA  ALA B 310     -27.664 -38.678 -15.402  1.00192.65           C  
ANISOU 5233  CA  ALA B 310    23317  23773  26108   2449   9194  -2348       C  
ATOM   5234  C   ALA B 310     -27.666 -38.267 -16.874  1.00197.25           C  
ANISOU 5234  C   ALA B 310    24268  24683  25995   2662   9699  -2422       C  
ATOM   5235  O   ALA B 310     -26.619 -37.977 -17.445  1.00202.44           O  
ANISOU 5235  O   ALA B 310    24664  25681  26574   2660  10257  -2305       O  
ATOM   5236  CB  ALA B 310     -27.482 -40.180 -15.265  1.00193.74           C  
ANISOU 5236  CB  ALA B 310    23148  23795  26668   2842   8991  -2761       C  
ATOM   5237  N   ALA B 311     -28.845 -38.261 -17.488  1.00195.71           N  
ANISOU 5237  N   ALA B 311    24665  24409  25287   2856   9503  -2611       N  
ATOM   5238  CA  ALA B 311     -28.974 -37.854 -18.882  1.00200.04           C  
ANISOU 5238  CA  ALA B 311    25635  25268  25101   3084   9927  -2676       C  
ATOM   5239  C   ALA B 311     -28.587 -36.390 -19.070  1.00201.43           C  
ANISOU 5239  C   ALA B 311    25940  25618  24977   2689  10320  -2152       C  
ATOM   5240  O   ALA B 311     -27.859 -36.056 -20.003  1.00207.15           O  
ANISOU 5240  O   ALA B 311    26641  26713  25355   2766  10907  -2052       O  
ATOM   5241  CB  ALA B 311     -30.395 -38.093 -19.376  1.00197.77           C  
ANISOU 5241  CB  ALA B 311    25953  24832  24358   3341   9543  -2970       C  
ATOM   5242  N   CYS B 312     -29.075 -35.522 -18.184  1.00196.62           N  
ANISOU 5242  N   CYS B 312    25468  24739  24501   2272   9997  -1815       N  
ATOM   5243  CA  CYS B 312     -28.737 -34.093 -18.230  1.00197.85           C  
ANISOU 5243  CA  CYS B 312    25757  24959  24457   1852  10292  -1304       C  
ATOM   5244  C   CYS B 312     -27.267 -33.823 -17.903  1.00201.46           C  
ANISOU 5244  C   CYS B 312    25593  25595  25358   1552  10708  -1025       C  
ATOM   5245  O   CYS B 312     -26.660 -32.887 -18.430  1.00205.63           O  
ANISOU 5245  O   CYS B 312    26151  26326  25653   1317  11186   -666       O  
ATOM   5246  CB  CYS B 312     -29.634 -33.298 -17.274  1.00191.92           C  
ANISOU 5246  CB  CYS B 312    25291  23842  23788   1519   9785  -1076       C  
ATOM   5247  SG  CYS B 312     -31.395 -33.318 -17.698  1.00188.25           S  
ANISOU 5247  SG  CYS B 312    25565  23211  22753   1809   9331  -1315       S  
ATOM   5248  N   GLY B 313     -26.706 -34.647 -17.025  1.00200.17           N  
ANISOU 5248  N   GLY B 313    24858  25351  25847   1555  10512  -1174       N  
ATOM   5249  CA  GLY B 313     -25.294 -34.578 -16.697  1.00203.90           C  
ANISOU 5249  CA  GLY B 313    24660  26018  26794   1333  10861   -981       C  
ATOM   5250  C   GLY B 313     -25.005 -34.280 -15.237  1.00200.13           C  
ANISOU 5250  C   GLY B 313    23809  25277  26956    910  10472   -760       C  
ATOM   5251  O   GLY B 313     -23.899 -33.881 -14.882  1.00203.06           O  
ANISOU 5251  O   GLY B 313    23674  25778  27702    601  10717   -508       O  
ATOM   5252  N   TYR B 314     -25.997 -34.497 -14.384  1.00194.00           N  
ANISOU 5252  N   TYR B 314    23260  24151  26300    903   9860   -861       N  
ATOM   5253  CA  TYR B 314     -25.848 -34.252 -12.958  1.00190.28           C  
ANISOU 5253  CA  TYR B 314    22491  23439  26367    549   9439   -680       C  
ATOM   5254  C   TYR B 314     -25.332 -35.510 -12.271  1.00190.00           C  
ANISOU 5254  C   TYR B 314    21895  23383  26911    757   9225   -920       C  
ATOM   5255  O   TYR B 314     -26.108 -36.317 -11.762  1.00186.08           O  
ANISOU 5255  O   TYR B 314    21505  22661  26535    961   8764  -1142       O  
ATOM   5256  CB  TYR B 314     -27.178 -33.810 -12.347  1.00184.25           C  
ANISOU 5256  CB  TYR B 314    22243  22351  25414    444   8908   -641       C  
ATOM   5257  CG  TYR B 314     -27.588 -32.400 -12.703  1.00184.34           C  
ANISOU 5257  CG  TYR B 314    22750  22308  24983    161   9027   -336       C  
ATOM   5258  CD1 TYR B 314     -28.126 -32.107 -13.949  1.00186.36           C  
ANISOU 5258  CD1 TYR B 314    23526  22681  24603    367   9306   -369       C  
ATOM   5259  CD2 TYR B 314     -27.470 -31.368 -11.781  1.00182.65           C  
ANISOU 5259  CD2 TYR B 314    22513  21906  24980   -288   8822    -27       C  
ATOM   5260  CE1 TYR B 314     -28.509 -30.822 -14.280  1.00186.80           C  
ANISOU 5260  CE1 TYR B 314    24059  22657  24258    129   9396    -66       C  
ATOM   5261  CE2 TYR B 314     -27.855 -30.080 -12.101  1.00183.09           C  
ANISOU 5261  CE2 TYR B 314    23050  21857  24661   -531   8901    247       C  
ATOM   5262  CZ  TYR B 314     -28.374 -29.811 -13.352  1.00185.16           C  
ANISOU 5262  CZ  TYR B 314    23823  22224  24305   -321   9191    243       C  
ATOM   5263  OH  TYR B 314     -28.761 -28.528 -13.678  1.00185.96           O  
ANISOU 5263  OH  TYR B 314    24427  22194  24036   -544   9255    541       O  
ATOM   5264  N   PHE B 315     -24.020 -35.696 -12.285  1.00194.60           N  
ANISOU 5264  N   PHE B 315    21874  24205  27859    715   9565   -865       N  
ATOM   5265  CA  PHE B 315     -23.433 -36.877 -11.672  1.00195.10           C  
ANISOU 5265  CA  PHE B 315    21385  24258  28487    944   9378  -1080       C  
ATOM   5266  C   PHE B 315     -21.995 -36.604 -11.254  1.00199.21           C  
ANISOU 5266  C   PHE B 315    21201  24997  29493    688   9628   -869       C  
ATOM   5267  O   PHE B 315     -21.355 -35.704 -11.785  1.00203.10           O  
ANISOU 5267  O   PHE B 315    21606  25724  29840    424  10090   -623       O  
ATOM   5268  CB  PHE B 315     -23.499 -38.072 -12.633  1.00197.90           C  
ANISOU 5268  CB  PHE B 315    21772  24732  28691   1517   9563  -1507       C  
ATOM   5269  CG  PHE B 315     -22.755 -37.869 -13.942  1.00204.46           C  
ANISOU 5269  CG  PHE B 315    22525  25981  29177   1673  10265  -1538       C  
ATOM   5270  CD1 PHE B 315     -21.434 -38.277 -14.081  1.00210.02           C  
ANISOU 5270  CD1 PHE B 315    22567  26994  30238   1784  10644  -1576       C  
ATOM   5271  CD2 PHE B 315     -23.390 -37.315 -15.045  1.00205.44           C  
ANISOU 5271  CD2 PHE B 315    23231  26220  28605   1745  10545  -1536       C  
ATOM   5272  CE1 PHE B 315     -20.759 -38.109 -15.278  1.00216.47           C  
ANISOU 5272  CE1 PHE B 315    23290  28246  30714   1944  11319  -1597       C  
ATOM   5273  CE2 PHE B 315     -22.711 -37.147 -16.250  1.00211.91           C  
ANISOU 5273  CE2 PHE B 315    23988  27464  29062   1906  11209  -1543       C  
ATOM   5274  CZ  PHE B 315     -21.395 -37.545 -16.361  1.00217.45           C  
ANISOU 5274  CZ  PHE B 315    24013  28491  30117   2001  11610  -1571       C  
ATOM   5275  N   SER B 316     -21.485 -37.379 -10.303  1.00198.72           N  
ANISOU 5275  N   SER B 316    20629  24860  30017    759   9317   -947       N  
ATOM   5276  CA  SER B 316     -20.075 -37.278  -9.935  1.00203.23           C  
ANISOU 5276  CA  SER B 316    20459  25671  31087    584   9532   -801       C  
ATOM   5277  C   SER B 316     -19.400 -38.632 -10.045  1.00206.57           C  
ANISOU 5277  C   SER B 316    20388  26221  31880   1067   9588  -1115       C  
ATOM   5278  O   SER B 316     -19.064 -39.258  -9.040  1.00205.60           O  
ANISOU 5278  O   SER B 316    19866  25970  32282   1117   9195  -1144       O  
ATOM   5279  CB  SER B 316     -19.918 -36.739  -8.515  1.00200.66           C  
ANISOU 5279  CB  SER B 316    19908  25156  31176    154   9061   -544       C  
ATOM   5280  OG  SER B 316     -18.548 -36.686  -8.155  1.00205.35           O  
ANISOU 5280  OG  SER B 316    19753  25992  32278     -5   9230   -427       O  
ATOM   5281  N   HIS B 317     -19.131 -39.043 -11.277  1.00211.16           N  
ANISOU 5281  N   HIS B 317    20977  27075  32181   1433  10093  -1340       N  
ATOM   5282  CA  HIS B 317     -18.581 -40.363 -11.525  1.00214.77           C  
ANISOU 5282  CA  HIS B 317    21042  27633  32930   1972  10159  -1704       C  
ATOM   5283  C   HIS B 317     -17.189 -40.469 -10.919  1.00218.99           C  
ANISOU 5283  C   HIS B 317    20728  28396  34084   1879  10256  -1586       C  
ATOM   5284  O   HIS B 317     -16.669 -41.566 -10.736  1.00221.44           O  
ANISOU 5284  O   HIS B 317    20622  28718  34797   2287  10156  -1842       O  
ATOM   5285  CB  HIS B 317     -18.554 -40.661 -13.027  1.00219.49           C  
ANISOU 5285  CB  HIS B 317    21840  28528  33028   2388  10720  -1983       C  
ATOM   5286  CG  HIS B 317     -17.674 -39.745 -13.811  1.00225.15           C  
ANISOU 5286  CG  HIS B 317    22313  29720  33513   2166  11416  -1741       C  
ATOM   5287  ND1 HIS B 317     -17.987 -38.419 -14.044  1.00224.04           N  
ANISOU 5287  ND1 HIS B 317    22534  29613  32978   1685  11605  -1365       N  
ATOM   5288  CD2 HIS B 317     -16.480 -39.952 -14.426  1.00232.48           C  
ANISOU 5288  CD2 HIS B 317    22659  31117  34554   2356  11987  -1799       C  
ATOM   5289  CE1 HIS B 317     -17.035 -37.858 -14.762  1.00230.41           C  
ANISOU 5289  CE1 HIS B 317    23005  30869  33674   1558  12258  -1176       C  
ATOM   5290  NE2 HIS B 317     -16.106 -38.770 -15.005  1.00235.64           N  
ANISOU 5290  NE2 HIS B 317    23071  31828  34631   1959  12515  -1435       N  
ATOM   5291  N   ALA B 318     -16.605 -39.318 -10.590  1.00220.06           N  
ANISOU 5291  N   ALA B 318    20611  28689  34312   1339  10417  -1202       N  
ATOM   5292  CA  ALA B 318     -15.279 -39.245  -9.980  1.00224.29           C  
ANISOU 5292  CA  ALA B 318    20315  29463  35441   1162  10491  -1053       C  
ATOM   5293  C   ALA B 318     -15.266 -39.868  -8.584  1.00220.94           C  
ANISOU 5293  C   ALA B 318    19625  28745  35578   1187   9806  -1073       C  
ATOM   5294  O   ALA B 318     -14.410 -40.707  -8.276  1.00224.48           O  
ANISOU 5294  O   ALA B 318    19461  29316  36515   1479   9758  -1216       O  
ATOM   5295  CB  ALA B 318     -14.806 -37.797  -9.921  1.00225.95           C  
ANISOU 5295  CB  ALA B 318    20399  29836  35614    514  10751   -629       C  
ATOM   5296  N   ASP B 319     -16.203 -39.436  -7.740  1.00214.53           N  
ANISOU 5296  N   ASP B 319    19269  27565  34678    896   9285   -919       N  
ATOM   5297  CA  ASP B 319     -16.331 -39.971  -6.388  1.00211.12           C  
ANISOU 5297  CA  ASP B 319    18674  26856  34685    907   8620   -898       C  
ATOM   5298  C   ASP B 319     -16.882 -41.391  -6.421  1.00209.69           C  
ANISOU 5298  C   ASP B 319    18661  26438  34574   1474   8350  -1222       C  
ATOM   5299  O   ASP B 319     -16.671 -42.170  -5.491  1.00209.19           O  
ANISOU 5299  O   ASP B 319    18300  26218  34965   1636   7909  -1247       O  
ATOM   5300  CB  ASP B 319     -17.220 -39.078  -5.523  1.00205.10           C  
ANISOU 5300  CB  ASP B 319    18374  25808  33745    459   8177   -651       C  
ATOM   5301  CG  ASP B 319     -16.501 -37.833  -5.041  1.00206.82           C  
ANISOU 5301  CG  ASP B 319    18285  26172  34126   -112   8232   -337       C  
ATOM   5302  OD1 ASP B 319     -15.360 -37.950  -4.545  1.00210.85           O  
ANISOU 5302  OD1 ASP B 319    18090  26881  35143   -180   8218   -281       O  
ATOM   5303  OD2 ASP B 319     -17.089 -36.737  -5.139  1.00204.39           O  
ANISOU 5303  OD2 ASP B 319    18440  25759  33458   -489   8258   -155       O  
ATOM   5304  N   ILE B 320     -17.628 -41.705  -7.474  1.00209.18           N  
ANISOU 5304  N   ILE B 320    19103  26323  34053   1762   8582  -1458       N  
ATOM   5305  CA  ILE B 320     -18.093 -43.068  -7.693  1.00208.97           C  
ANISOU 5305  CA  ILE B 320    19231  26067  34101   2312   8379  -1813       C  
ATOM   5306  C   ILE B 320     -16.905 -44.008  -7.920  1.00215.37           C  
ANISOU 5306  C   ILE B 320    19382  27090  35360   2747   8587  -2038       C  
ATOM   5307  O   ILE B 320     -16.820 -45.079  -7.319  1.00215.56           O  
ANISOU 5307  O   ILE B 320    19210  26880  35814   3066   8196  -2174       O  
ATOM   5308  CB  ILE B 320     -19.060 -43.147  -8.890  1.00208.05           C  
ANISOU 5308  CB  ILE B 320    19769  25901  33380   2532   8613  -2058       C  
ATOM   5309  CG1 ILE B 320     -20.368 -42.427  -8.554  1.00201.47           C  
ANISOU 5309  CG1 ILE B 320    19591  24799  32159   2189   8294  -1876       C  
ATOM   5310  CG2 ILE B 320     -19.350 -44.596  -9.246  1.00209.42           C  
ANISOU 5310  CG2 ILE B 320    20026  25859  33685   3124   8452  -2481       C  
ATOM   5311  CD1 ILE B 320     -21.320 -42.293  -9.725  1.00200.67           C  
ANISOU 5311  CD1 ILE B 320    20134  24689  31422   2344   8518  -2073       C  
ATOM   5312  N   ASP B 321     -15.987 -43.594  -8.787  1.00220.98           N  
ANISOU 5312  N   ASP B 321    19745  28249  35968   2765   9209  -2060       N  
ATOM   5313  CA  ASP B 321     -14.767 -44.346  -9.045  1.00227.80           C  
ANISOU 5313  CA  ASP B 321    19913  29403  37238   3167   9479  -2263       C  
ATOM   5314  C   ASP B 321     -13.885 -44.391  -7.806  1.00228.73           C  
ANISOU 5314  C   ASP B 321    19360  29537  38008   2995   9139  -2047       C  
ATOM   5315  O   ASP B 321     -13.249 -45.404  -7.523  1.00232.11           O  
ANISOU 5315  O   ASP B 321    19329  29955  38909   3416   8990  -2236       O  
ATOM   5316  CB  ASP B 321     -13.998 -43.721 -10.212  1.00233.77           C  
ANISOU 5316  CB  ASP B 321    20426  30701  37694   3144  10264  -2262       C  
ATOM   5317  CG  ASP B 321     -14.782 -43.744 -11.505  1.00233.87           C  
ANISOU 5317  CG  ASP B 321    21079  30754  37026   3389  10618  -2501       C  
ATOM   5318  OD1 ASP B 321     -15.733 -44.548 -11.609  1.00230.78           O  
ANISOU 5318  OD1 ASP B 321    21188  29996  36501   3725  10278  -2790       O  
ATOM   5319  OD2 ASP B 321     -14.474 -42.932 -12.401  1.00237.19           O  
ANISOU 5319  OD2 ASP B 321    21513  31569  37041   3224  11219  -2381       O  
ATOM   5320  N   ALA B 322     -13.868 -43.290  -7.062  1.00225.92           N  
ANISOU 5320  N   ALA B 322    18972  29194  37674   2391   8986  -1666       N  
ATOM   5321  CA  ALA B 322     -12.987 -43.145  -5.908  1.00227.24           C  
ANISOU 5321  CA  ALA B 322    18495  29434  38412   2163   8676  -1447       C  
ATOM   5322  C   ALA B 322     -13.440 -43.952  -4.691  1.00223.34           C  
ANISOU 5322  C   ALA B 322    18077  28527  38254   2313   7936  -1439       C  
ATOM   5323  O   ALA B 322     -12.723 -44.033  -3.694  1.00224.75           O  
ANISOU 5323  O   ALA B 322    17728  28752  38915   2227   7610  -1294       O  
ATOM   5324  CB  ALA B 322     -12.861 -41.672  -5.537  1.00225.88           C  
ANISOU 5324  CB  ALA B 322    18311  29382  38133   1464   8730  -1072       C  
ATOM   5325  N   ALA B 323     -14.630 -44.534  -4.762  1.00218.77           N  
ANISOU 5325  N   ALA B 323    18148  27558  37417   2523   7664  -1575       N  
ATOM   5326  CA  ALA B 323     -15.161 -45.301  -3.640  1.00215.21           C  
ANISOU 5326  CA  ALA B 323    17820  26704  37245   2640   6985  -1522       C  
ATOM   5327  C   ALA B 323     -14.671 -46.749  -3.651  1.00219.28           C  
ANISOU 5327  C   ALA B 323    18001  27103  38213   3256   6850  -1787       C  
ATOM   5328  O   ALA B 323     -14.443 -47.319  -4.717  1.00223.18           O  
ANISOU 5328  O   ALA B 323    18464  27695  38639   3675   7238  -2117       O  
ATOM   5329  CB  ALA B 323     -16.683 -45.254  -3.651  1.00208.79           C  
ANISOU 5329  CB  ALA B 323    17819  25522  35990   2545   6735  -1515       C  
ATOM   5330  N   PRO B 324     -14.523 -47.354  -2.459  1.00218.71           N  
ANISOU 5330  N   PRO B 324    17700  26811  38588   3333   6284  -1646       N  
ATOM   5331  CA  PRO B 324     -14.137 -48.765  -2.352  1.00222.49           C  
ANISOU 5331  CA  PRO B 324    17915  27089  39531   3924   6066  -1861       C  
ATOM   5332  C   PRO B 324     -15.290 -49.710  -2.666  1.00219.85           C  
ANISOU 5332  C   PRO B 324    18211  26267  39053   4231   5843  -2067       C  
ATOM   5333  O   PRO B 324     -16.433 -49.384  -2.381  1.00214.09           O  
ANISOU 5333  O   PRO B 324    18051  25294  37999   3938   5610  -1917       O  
ATOM   5334  CB  PRO B 324     -13.710 -48.895  -0.888  1.00222.22           C  
ANISOU 5334  CB  PRO B 324    17507  26983  39945   3807   5500  -1554       C  
ATOM   5335  CG  PRO B 324     -14.488 -47.859  -0.183  1.00216.13           C  
ANISOU 5335  CG  PRO B 324    17122  26164  38834   3225   5269  -1231       C  
ATOM   5336  CD  PRO B 324     -14.583 -46.703  -1.139  1.00215.36           C  
ANISOU 5336  CD  PRO B 324    17204  26354  38268   2885   5829  -1270       C  
ATOM   5337  N   ALA B 325     -14.989 -50.880  -3.218  1.00224.37           N  
ANISOU 5337  N   ALA B 325    18666  26693  39892   4821   5892  -2414       N  
ATOM   5338  CA  ALA B 325     -16.031 -51.837  -3.568  1.00222.77           C  
ANISOU 5338  CA  ALA B 325    19034  25994  39613   5121   5664  -2649       C  
ATOM   5339  C   ALA B 325     -16.128 -52.930  -2.517  1.00223.06           C  
ANISOU 5339  C   ALA B 325    19008  25569  40176   5347   5030  -2521       C  
ATOM   5340  O   ALA B 325     -16.241 -54.113  -2.840  1.00226.08           O  
ANISOU 5340  O   ALA B 325    19490  25586  40823   5837   4881  -2807       O  
ATOM   5341  CB  ALA B 325     -15.762 -52.440  -4.936  1.00227.82           C  
ANISOU 5341  CB  ALA B 325    19687  26712  40162   5643   6105  -3160       C  
ATOM   5342  N   ALA B 326     -16.093 -52.521  -1.254  1.00220.25           N  
ANISOU 5342  N   ALA B 326    18507  25217  39960   4990   4646  -2087       N  
ATOM   5343  CA  ALA B 326     -16.220 -53.450  -0.145  1.00220.40           C  
ANISOU 5343  CA  ALA B 326    18489  24828  40424   5146   4029  -1871       C  
ATOM   5344  C   ALA B 326     -16.676 -52.714   1.101  1.00215.30           C  
ANISOU 5344  C   ALA B 326    17952  24211  39641   4624   3657  -1387       C  
ATOM   5345  O   ALA B 326     -16.393 -51.528   1.266  1.00213.50           O  
ANISOU 5345  O   ALA B 326    17574  24381  39165   4213   3848  -1230       O  
ATOM   5346  CB  ALA B 326     -14.908 -54.162   0.109  1.00227.05           C  
ANISOU 5346  CB  ALA B 326    18657  25761  41851   5593   3958  -1948       C  
ATOM   5347  N   SER B 327     -17.353 -53.428   1.991  1.00213.50           N  
ANISOU 5347  N   SER B 327    17974  23561  39586   4649   3122  -1147       N  
ATOM   5348  CA  SER B 327     -17.784 -52.842   3.248  1.00209.30           C  
ANISOU 5348  CA  SER B 327    17538  23070  38918   4219   2741   -689       C  
ATOM   5349  C   SER B 327     -18.056 -53.882   4.325  1.00210.08           C  
ANISOU 5349  C   SER B 327    17683  22760  39378   4392   2147   -397       C  
ATOM   5350  O   SER B 327     -18.977 -54.698   4.225  1.00209.08           O  
ANISOU 5350  O   SER B 327    17980  22175  39286   4509   1951   -407       O  
ATOM   5351  CB  SER B 327     -19.030 -51.988   3.040  1.00203.01           C  
ANISOU 5351  CB  SER B 327    17327  22277  37530   3780   2848   -624       C  
ATOM   5352  OG  SER B 327     -19.454 -51.435   4.272  1.00199.34           O  
ANISOU 5352  OG  SER B 327    16954  21871  36913   3405   2481   -207       O  
ATOM   5353  N   PHE B 328     -17.245 -53.816   5.369  1.00212.17           N  
ANISOU 5353  N   PHE B 328    17504  23203  39907   4386   1852   -117       N  
ATOM   5354  CA  PHE B 328     -17.438 -54.615   6.560  1.00212.97           C  
ANISOU 5354  CA  PHE B 328    17628  23003  40287   4491   1272    259       C  
ATOM   5355  C   PHE B 328     -18.127 -53.708   7.557  1.00207.83           C  
ANISOU 5355  C   PHE B 328    17215  22535  39216   3985   1049    649       C  
ATOM   5356  O   PHE B 328     -18.166 -52.492   7.374  1.00204.76           O  
ANISOU 5356  O   PHE B 328    16850  22513  38435   3613   1314    601       O  
ATOM   5357  CB  PHE B 328     -16.107 -55.148   7.115  1.00219.04           C  
ANISOU 5357  CB  PHE B 328    17761  23873  41592   4854   1046    321       C  
ATOM   5358  CG  PHE B 328     -15.418 -56.144   6.212  1.00224.79           C  
ANISOU 5358  CG  PHE B 328    18240  24403  42769   5429   1224    -69       C  
ATOM   5359  CD1 PHE B 328     -14.539 -55.721   5.227  1.00227.58           C  
ANISOU 5359  CD1 PHE B 328    18204  25127  43139   5558   1732   -458       C  
ATOM   5360  CD2 PHE B 328     -15.658 -57.504   6.349  1.00227.83           C  
ANISOU 5360  CD2 PHE B 328    18784  24224  43557   5845    883    -45       C  
ATOM   5361  CE1 PHE B 328     -13.920 -56.633   4.401  1.00233.21           C  
ANISOU 5361  CE1 PHE B 328    18688  25693  44229   6125   1907   -843       C  
ATOM   5362  CE2 PHE B 328     -15.042 -58.418   5.524  1.00233.44           C  
ANISOU 5362  CE2 PHE B 328    19291  24728  44678   6407   1024   -442       C  
ATOM   5363  CZ  PHE B 328     -14.173 -57.983   4.550  1.00236.12           C  
ANISOU 5363  CZ  PHE B 328    19236  25481  44996   6567   1541   -858       C  
ATOM   5364  N   ILE B 329     -18.712 -54.299   8.585  1.00207.18           N  
ANISOU 5364  N   ILE B 329    17334  22185  39199   3978    571   1034       N  
ATOM   5365  CA  ILE B 329     -19.540 -53.544   9.508  1.00202.42           C  
ANISOU 5365  CA  ILE B 329    17025  21737  38150   3541    363   1390       C  
ATOM   5366  C   ILE B 329     -18.774 -52.402  10.173  1.00202.19           C  
ANISOU 5366  C   ILE B 329    16640  22228  37956   3282    331   1494       C  
ATOM   5367  O   ILE B 329     -19.324 -51.333  10.400  1.00197.91           O  
ANISOU 5367  O   ILE B 329    16329  21926  36943   2879    398   1564       O  
ATOM   5368  CB  ILE B 329     -20.123 -54.461  10.594  1.00203.09           C  
ANISOU 5368  CB  ILE B 329    17298  21494  38373   3622   -153   1838       C  
ATOM   5369  CG1 ILE B 329     -20.987 -55.555   9.962  1.00203.38           C  
ANISOU 5369  CG1 ILE B 329    17719  20968  38589   3808   -153   1751       C  
ATOM   5370  CG2 ILE B 329     -20.928 -53.658  11.607  1.00198.74           C  
ANISOU 5370  CG2 ILE B 329    17010  21179  37321   3204   -354   2206       C  
ATOM   5371  CD1 ILE B 329     -21.473 -56.596  10.947  1.00205.22           C  
ANISOU 5371  CD1 ILE B 329    18104  20814  39057   3907   -644   2213       C  
ATOM   5372  N   TRP B 330     -17.491 -52.608  10.443  1.00207.14           N  
ANISOU 5372  N   TRP B 330    16694  23025  38985   3520    225   1472       N  
ATOM   5373  CA  TRP B 330     -16.700 -51.587  11.126  1.00207.73           C  
ANISOU 5373  CA  TRP B 330    16383  23576  38969   3275    131   1562       C  
ATOM   5374  C   TRP B 330     -15.514 -51.056  10.324  1.00210.90           C  
ANISOU 5374  C   TRP B 330    16258  24298  39576   3305    523   1223       C  
ATOM   5375  O   TRP B 330     -14.439 -50.860  10.883  1.00214.71           O  
ANISOU 5375  O   TRP B 330    16192  25067  40319   3348    344   1277       O  
ATOM   5376  CB  TRP B 330     -16.184 -52.142  12.455  1.00211.22           C  
ANISOU 5376  CB  TRP B 330    16543  24039  39671   3461   -443   1923       C  
ATOM   5377  CG  TRP B 330     -17.254 -52.392  13.453  1.00208.40           C  
ANISOU 5377  CG  TRP B 330    16644  23512  39027   3340   -832   2336       C  
ATOM   5378  CD1 TRP B 330     -17.765 -51.497  14.335  1.00205.09           C  
ANISOU 5378  CD1 TRP B 330    16427  23361  38136   2973  -1022   2566       C  
ATOM   5379  CD2 TRP B 330     -17.966 -53.618  13.663  1.00209.07           C  
ANISOU 5379  CD2 TRP B 330    17040  23125  39272   3583  -1065   2573       C  
ATOM   5380  NE1 TRP B 330     -18.742 -52.088  15.096  1.00203.70           N  
ANISOU 5380  NE1 TRP B 330    16646  22962  37789   2982  -1334   2947       N  
ATOM   5381  CE2 TRP B 330     -18.886 -53.390  14.701  1.00206.11           C  
ANISOU 5381  CE2 TRP B 330    17022  22799  38492   3329  -1366   2978       C  
ATOM   5382  CE3 TRP B 330     -17.905 -54.887  13.081  1.00212.31           C  
ANISOU 5382  CE3 TRP B 330    17461  23067  40142   3991  -1057   2478       C  
ATOM   5383  CZ2 TRP B 330     -19.746 -54.381  15.168  1.00206.33           C  
ANISOU 5383  CZ2 TRP B 330    17392  22439  38565   3434  -1632   3333       C  
ATOM   5384  CZ3 TRP B 330     -18.763 -55.872  13.544  1.00212.49           C  
ANISOU 5384  CZ3 TRP B 330    17850  22648  40239   4089  -1357   2812       C  
ATOM   5385  CH2 TRP B 330     -19.669 -55.612  14.580  1.00209.55           C  
ANISOU 5385  CH2 TRP B 330    17805  22351  39463   3794  -1630   3257       C  
ATOM   5386  N   VAL B 331     -15.713 -50.787   9.036  1.00209.62           N  
ANISOU 5386  N   VAL B 331    16247  24121  39278   3267   1055    889       N  
ATOM   5387  CA  VAL B 331     -14.662 -50.170   8.229  1.00212.63           C  
ANISOU 5387  CA  VAL B 331    16151  24854  39785   3237   1495    602       C  
ATOM   5388  C   VAL B 331     -14.205 -48.851   8.856  1.00211.88           C  
ANISOU 5388  C   VAL B 331    15814  25176  39514   2774   1434    730       C  
ATOM   5389  O   VAL B 331     -13.008 -48.573   8.946  1.00216.34           O  
ANISOU 5389  O   VAL B 331    15752  26057  40389   2787   1470    670       O  
ATOM   5390  CB  VAL B 331     -15.131 -49.913   6.785  1.00210.76           C  
ANISOU 5390  CB  VAL B 331    16227  24571  39281   3199   2085    274       C  
ATOM   5391  CG1 VAL B 331     -14.068 -49.161   6.004  1.00214.05           C  
ANISOU 5391  CG1 VAL B 331    16154  25403  39772   3106   2571     46       C  
ATOM   5392  CG2 VAL B 331     -15.456 -51.219   6.097  1.00212.46           C  
ANISOU 5392  CG2 VAL B 331    16632  24384  39710   3683   2139     73       C  
ATOM   5393  N   LYS B 332     -15.176 -48.063   9.310  1.00206.58           N  
ANISOU 5393  N   LYS B 332    15633  24494  38363   2376   1316    895       N  
ATOM   5394  CA  LYS B 332     -14.934 -46.814  10.032  1.00205.53           C  
ANISOU 5394  CA  LYS B 332    15389  24682  38023   1930   1167   1017       C  
ATOM   5395  C   LYS B 332     -15.618 -46.932  11.396  1.00203.15           C  
ANISOU 5395  C   LYS B 332    15372  24301  37515   1869    590   1349       C  
ATOM   5396  O   LYS B 332     -16.610 -47.645  11.520  1.00200.54           O  
ANISOU 5396  O   LYS B 332    15489  23668  37038   2014    464   1478       O  
ATOM   5397  CB  LYS B 332     -15.499 -45.605   9.278  1.00201.64           C  
ANISOU 5397  CB  LYS B 332    15262  24271  37080   1508   1585    883       C  
ATOM   5398  CG  LYS B 332     -15.180 -45.512   7.790  1.00203.09           C  
ANISOU 5398  CG  LYS B 332    15362  24496  37308   1567   2219    586       C  
ATOM   5399  CD  LYS B 332     -13.737 -45.200   7.500  1.00208.76           C  
ANISOU 5399  CD  LYS B 332    15355  25552  38414   1550   2442    469       C  
ATOM   5400  CE  LYS B 332     -13.542 -44.984   6.008  1.00210.05           C  
ANISOU 5400  CE  LYS B 332    15502  25801  38507   1570   3121    206       C  
ATOM   5401  NZ  LYS B 332     -12.130 -44.676   5.658  1.00216.11           N  
ANISOU 5401  NZ  LYS B 332    15519  26940  39653   1541   3404    108       N  
ATOM   5402  N   THR B 333     -15.096 -46.274  12.427  1.00204.48           N  
ANISOU 5402  N   THR B 333    15276  24747  37671   1662    233   1492       N  
ATOM   5403  CA  THR B 333     -15.718 -46.368  13.752  1.00202.76           C  
ANISOU 5403  CA  THR B 333    15324  24514  37201   1630   -308   1809       C  
ATOM   5404  C   THR B 333     -15.884 -44.996  14.396  1.00200.64           C  
ANISOU 5404  C   THR B 333    15185  24513  36538   1181   -458   1834       C  
ATOM   5405  O   THR B 333     -15.354 -44.003  13.906  1.00201.26           O  
ANISOU 5405  O   THR B 333    15068  24772  36629    888   -200   1630       O  
ATOM   5406  CB  THR B 333     -14.928 -47.275  14.713  1.00207.70           C  
ANISOU 5406  CB  THR B 333    15514  25182  38221   1978   -799   2019       C  
ATOM   5407  OG1 THR B 333     -13.598 -46.771  14.869  1.00212.31           O  
ANISOU 5407  OG1 THR B 333    15444  26100  39124   1915   -863   1896       O  
ATOM   5408  CG2 THR B 333     -14.886 -48.710  14.194  1.00209.94           C  
ANISOU 5408  CG2 THR B 333    15750  25123  38894   2458   -728   2019       C  
ATOM   5409  N   PHE B 334     -16.649 -44.948  15.484  1.00198.46           N  
ANISOU 5409  N   PHE B 334    15252  24250  35902   1132   -869   2088       N  
ATOM   5410  CA  PHE B 334     -17.014 -43.685  16.122  1.00196.15           C  
ANISOU 5410  CA  PHE B 334    15193  24175  35162    751  -1033   2088       C  
ATOM   5411  C   PHE B 334     -16.857 -43.751  17.644  1.00198.25           C  
ANISOU 5411  C   PHE B 334    15364  24653  35311    817  -1657   2341       C  
ATOM   5412  O   PHE B 334     -16.882 -44.835  18.219  1.00200.06           O  
ANISOU 5412  O   PHE B 334    15537  24802  35674   1147  -1940   2599       O  
ATOM   5413  CB  PHE B 334     -18.456 -43.318  15.750  1.00190.30           C  
ANISOU 5413  CB  PHE B 334    15136  23267  33902    590   -804   2087       C  
ATOM   5414  CG  PHE B 334     -18.650 -43.049  14.287  1.00188.26           C  
ANISOU 5414  CG  PHE B 334    15022  22847  33662    490   -218   1826       C  
ATOM   5415  CD1 PHE B 334     -19.147 -44.031  13.447  1.00187.12           C  
ANISOU 5415  CD1 PHE B 334    15053  22417  33625    744     53   1801       C  
ATOM   5416  CD2 PHE B 334     -18.326 -41.816  13.748  1.00187.94           C  
ANISOU 5416  CD2 PHE B 334    14950  22931  33529    143     48   1609       C  
ATOM   5417  CE1 PHE B 334     -19.322 -43.786  12.099  1.00185.62           C  
ANISOU 5417  CE1 PHE B 334    15010  22113  33405    680    577   1549       C  
ATOM   5418  CE2 PHE B 334     -18.499 -41.567  12.400  1.00186.49           C  
ANISOU 5418  CE2 PHE B 334    14913  22623  33320     64    593   1403       C  
ATOM   5419  CZ  PHE B 334     -18.998 -42.554  11.576  1.00185.30           C  
ANISOU 5419  CZ  PHE B 334    14941  22231  33233    347    858   1365       C  
ATOM   5420  N   PRO B 335     -16.695 -42.587  18.298  1.00198.40           N  
ANISOU 5420  N   PRO B 335    15380  24932  35069    511  -1884   2268       N  
ATOM   5421  CA  PRO B 335     -16.440 -42.481  19.742  1.00201.02           C  
ANISOU 5421  CA  PRO B 335    15599  25531  35247    558  -2494   2447       C  
ATOM   5422  C   PRO B 335     -17.374 -43.268  20.674  1.00199.72           C  
ANISOU 5422  C   PRO B 335    15811  25339  34735    805  -2811   2812       C  
ATOM   5423  O   PRO B 335     -18.592 -43.305  20.498  1.00195.30           O  
ANISOU 5423  O   PRO B 335    15780  24635  33792    765  -2627   2900       O  
ATOM   5424  CB  PRO B 335     -16.586 -40.981  19.991  1.00199.63           C  
ANISOU 5424  CB  PRO B 335    15606  25532  34712    144  -2552   2240       C  
ATOM   5425  CG  PRO B 335     -16.073 -40.377  18.736  1.00199.57           C  
ANISOU 5425  CG  PRO B 335    15406  25426  34996   -107  -2055   1951       C  
ATOM   5426  CD  PRO B 335     -16.535 -41.282  17.629  1.00197.19           C  
ANISOU 5426  CD  PRO B 335    15255  24837  34833    104  -1578   1976       C  
ATOM   5427  N   LEU B 336     -16.756 -43.893  21.675  1.00204.12           N  
ANISOU 5427  N   LEU B 336    16060  26055  35440   1060  -3295   3040       N  
ATOM   5428  CA  LEU B 336     -17.443 -44.640  22.730  1.00204.36           C  
ANISOU 5428  CA  LEU B 336    16367  26121  35158   1300  -3662   3450       C  
ATOM   5429  C   LEU B 336     -17.094 -44.051  24.100  1.00207.39           C  
ANISOU 5429  C   LEU B 336    16659  26915  35224   1271  -4231   3527       C  
ATOM   5430  O   LEU B 336     -16.136 -43.279  24.221  1.00210.17           O  
ANISOU 5430  O   LEU B 336    16631  27480  35744   1113  -4393   3265       O  
ATOM   5431  CB  LEU B 336     -17.082 -46.131  22.683  1.00207.52           C  
ANISOU 5431  CB  LEU B 336    16538  26291  36021   1711  -3747   3720       C  
ATOM   5432  CG  LEU B 336     -17.478 -46.924  21.436  1.00205.28           C  
ANISOU 5432  CG  LEU B 336    16377  25572  36049   1820  -3262   3662       C  
ATOM   5433  CD1 LEU B 336     -17.038 -48.385  21.559  1.00209.43           C  
ANISOU 5433  CD1 LEU B 336    16667  25856  37050   2257  -3449   3926       C  
ATOM   5434  CD2 LEU B 336     -18.982 -46.818  21.188  1.00199.73           C  
ANISOU 5434  CD2 LEU B 336    16309  24705  34876   1660  -3006   3749       C  
ATOM   5435  N   SER B 337     -17.879 -44.425  25.115  1.00207.20           N  
ANISOU 5435  N   SER B 337    16977  27010  34739   1418  -4530   3886       N  
ATOM   5436  CA  SER B 337     -17.859 -43.800  26.444  1.00209.42           C  
ANISOU 5436  CA  SER B 337    17326  27712  34532   1398  -5040   3958       C  
ATOM   5437  C   SER B 337     -18.334 -42.364  26.288  1.00206.02           C  
ANISOU 5437  C   SER B 337    17186  27403  33688   1026  -4895   3598       C  
ATOM   5438  O   SER B 337     -18.034 -41.494  27.112  1.00208.15           O  
ANISOU 5438  O   SER B 337    17424  27997  33668    922  -5274   3448       O  
ATOM   5439  CB  SER B 337     -16.462 -43.842  27.091  1.00215.70           C  
ANISOU 5439  CB  SER B 337    17541  28755  35661   1536  -5527   3914       C  
ATOM   5440  OG  SER B 337     -16.000 -45.167  27.282  1.00219.35           O  
ANISOU 5440  OG  SER B 337    17739  29099  36507   1922  -5702   4255       O  
ATOM   5441  N   VAL B 338     -19.100 -42.138  25.224  1.00200.98           N  
ANISOU 5441  N   VAL B 338    16853  26488  33023    846  -4365   3456       N  
ATOM   5442  CA  VAL B 338     -19.536 -40.803  24.842  1.00197.68           C  
ANISOU 5442  CA  VAL B 338    16717  26095  32299    500  -4159   3103       C  
ATOM   5443  C   VAL B 338     -21.051 -40.743  24.768  1.00192.77           C  
ANISOU 5443  C   VAL B 338    16696  25407  31140    478  -3918   3222       C  
ATOM   5444  O   VAL B 338     -21.690 -41.500  24.041  1.00189.98           O  
ANISOU 5444  O   VAL B 338    16505  24779  30901    557  -3564   3368       O  
ATOM   5445  CB  VAL B 338     -18.942 -40.371  23.488  1.00196.64           C  
ANISOU 5445  CB  VAL B 338    16356  25713  32647    265  -3713   2763       C  
ATOM   5446  CG1 VAL B 338     -19.356 -38.954  23.160  1.00193.88           C  
ANISOU 5446  CG1 VAL B 338    16315  25367  31984    -94  -3547   2434       C  
ATOM   5447  CG2 VAL B 338     -17.427 -40.475  23.512  1.00201.93           C  
ANISOU 5447  CG2 VAL B 338    16361  26473  33889    287  -3914   2653       C  
ATOM   5448  N   TYR B 339     -21.616 -39.824  25.530  1.00192.09           N  
ANISOU 5448  N   TYR B 339    16926  25587  30473    380  -4128   3136       N  
ATOM   5449  CA  TYR B 339     -23.053 -39.654  25.607  1.00188.05           C  
ANISOU 5449  CA  TYR B 339    16953  25099  29397    376  -3945   3234       C  
ATOM   5450  C   TYR B 339     -23.364 -38.169  25.639  1.00186.47           C  
ANISOU 5450  C   TYR B 339    17032  25010  28808    130  -3950   2849       C  
ATOM   5451  O   TYR B 339     -22.500 -37.360  25.994  1.00189.42           O  
ANISOU 5451  O   TYR B 339    17201  25513  29258     -1  -4238   2585       O  
ATOM   5452  CB  TYR B 339     -23.608 -40.359  26.845  1.00189.94           C  
ANISOU 5452  CB  TYR B 339    17328  25629  29211    644  -4273   3666       C  
ATOM   5453  CG  TYR B 339     -23.094 -39.776  28.146  1.00194.18           C  
ANISOU 5453  CG  TYR B 339    17780  26599  29401    711  -4826   3618       C  
ATOM   5454  CD1 TYR B 339     -23.938 -39.078  29.000  1.00193.79           C  
ANISOU 5454  CD1 TYR B 339    18113  26889  28630    733  -4992   3593       C  
ATOM   5455  CD2 TYR B 339     -21.751 -39.896  28.507  1.00198.94           C  
ANISOU 5455  CD2 TYR B 339    17907  27289  30393    767  -5192   3564       C  
ATOM   5456  CE1 TYR B 339     -23.463 -38.533  30.188  1.00198.08           C  
ANISOU 5456  CE1 TYR B 339    18597  27839  28824    818  -5521   3506       C  
ATOM   5457  CE2 TYR B 339     -21.268 -39.357  29.688  1.00203.19           C  
ANISOU 5457  CE2 TYR B 339    18365  28228  30611    831  -5736   3488       C  
ATOM   5458  CZ  TYR B 339     -22.127 -38.676  30.525  1.00202.76           C  
ANISOU 5458  CZ  TYR B 339    18725  28498  29815    859  -5904   3451       C  
ATOM   5459  OH  TYR B 339     -21.649 -38.140  31.700  1.00207.36           O  
ANISOU 5459  OH  TYR B 339    19249  29491  30047    949  -6466   3339       O  
ATOM   5460  N   GLY B 340     -24.585 -37.809  25.255  1.00182.17           N  
ANISOU 5460  N   GLY B 340    16944  24395  27877     69  -3649   2808       N  
ATOM   5461  CA  GLY B 340     -25.017 -36.428  25.316  1.00180.76           C  
ANISOU 5461  CA  GLY B 340    17092  24297  27291   -115  -3664   2459       C  
ATOM   5462  C   GLY B 340     -26.053 -36.213  26.397  1.00180.63           C  
ANISOU 5462  C   GLY B 340    17443  24638  26551     53  -3883   2582       C  
ATOM   5463  O   GLY B 340     -26.318 -37.112  27.195  1.00182.22           O  
ANISOU 5463  O   GLY B 340    17607  25064  26564    290  -4056   2965       O  
ATOM   5464  N   PRO B 341     -26.633 -35.006  26.439  1.00179.19           N  
ANISOU 5464  N   PRO B 341    17617  24515  25951    -58  -3876   2262       N  
ATOM   5465  CA  PRO B 341     -27.750 -34.689  27.333  1.00178.84           C  
ANISOU 5465  CA  PRO B 341    17955  24821  25174    118  -4007   2320       C  
ATOM   5466  C   PRO B 341     -29.092 -34.899  26.639  1.00174.17           C  
ANISOU 5466  C   PRO B 341    17696  24109  24373    143  -3557   2429       C  
ATOM   5467  O   PRO B 341     -30.132 -34.533  27.177  1.00173.44           O  
ANISOU 5467  O   PRO B 341    17928  24286  23685    270  -3575   2435       O  
ATOM   5468  CB  PRO B 341     -27.516 -33.216  27.658  1.00180.34           C  
ANISOU 5468  CB  PRO B 341    18323  25082  25118    -11  -4265   1845       C  
ATOM   5469  CG  PRO B 341     -26.927 -32.677  26.389  1.00178.66           C  
ANISOU 5469  CG  PRO B 341    18018  24412  25452   -325  -3984   1565       C  
ATOM   5470  CD  PRO B 341     -26.076 -33.794  25.810  1.00179.12           C  
ANISOU 5470  CD  PRO B 341    17623  24281  26152   -348  -3832   1813       C  
ATOM   5471  N   MET B 342     -29.057 -35.485  25.447  1.00172.32           N  
ANISOU 5471  N   MET B 342    17363  23491  24620     36  -3166   2496       N  
ATOM   5472  CA  MET B 342     -30.271 -35.769  24.694  1.00168.17           C  
ANISOU 5472  CA  MET B 342    17111  22821  23964     49  -2756   2589       C  
ATOM   5473  C   MET B 342     -30.819 -37.139  25.091  1.00168.50           C  
ANISOU 5473  C   MET B 342    17070  22972  23980    236  -2727   3086       C  
ATOM   5474  O   MET B 342     -31.615 -37.735  24.372  1.00165.70           O  
ANISOU 5474  O   MET B 342    16819  22426  23712    231  -2399   3228       O  
ATOM   5475  CB  MET B 342     -30.003 -35.689  23.181  1.00171.05           C  
ANISOU 5475  CB  MET B 342    17446  22725  24819   -149  -2357   2387       C  
ATOM   5476  CG  MET B 342     -29.375 -36.930  22.534  1.00171.39           C  
ANISOU 5476  CG  MET B 342    17149  22504  25466   -129  -2194   2605       C  
ATOM   5477  SD  MET B 342     -27.587 -37.084  22.744  1.00175.79           S  
ANISOU 5477  SD  MET B 342    17183  23028  26582   -178  -2460   2551       S  
ATOM   5478  CE  MET B 342     -26.989 -35.917  21.526  1.00174.62           C  
ANISOU 5478  CE  MET B 342    17045  22588  26715   -486  -2179   2096       C  
ATOM   5479  N   VAL B 343     -30.404 -37.610  26.263  1.00171.42           N  
ANISOU 5479  N   VAL B 343    17263  23650  24219    395  -3094   3356       N  
ATOM   5480  CA  VAL B 343     -30.832 -38.897  26.805  1.00172.79           C  
ANISOU 5480  CA  VAL B 343    17354  23940  24359    569  -3125   3889       C  
ATOM   5481  C   VAL B 343     -32.344 -39.091  26.788  1.00170.36           C  
ANISOU 5481  C   VAL B 343    17340  23753  23636    611  -2868   4086       C  
ATOM   5482  O   VAL B 343     -32.855 -40.085  26.262  1.00169.04           O  
ANISOU 5482  O   VAL B 343    17144  23356  23728    602  -2629   4372       O  
ATOM   5483  CB  VAL B 343     -30.340 -39.067  28.253  1.00177.67           C  
ANISOU 5483  CB  VAL B 343    17840  24987  24678    758  -3594   4126       C  
ATOM   5484  CG1 VAL B 343     -30.799 -40.396  28.821  1.00179.55           C  
ANISOU 5484  CG1 VAL B 343    18016  25330  24875    925  -3617   4736       C  
ATOM   5485  CG2 VAL B 343     -28.829 -38.953  28.316  1.00180.63           C  
ANISOU 5485  CG2 VAL B 343    17868  25267  25494    725  -3886   3949       C  
ATOM   5486  N   LEU B 344     -33.056 -38.130  27.365  1.00170.14           N  
ANISOU 5486  N   LEU B 344    17583  24086  22976    663  -2931   3914       N  
ATOM   5487  CA  LEU B 344     -34.509 -38.197  27.435  1.00168.34           C  
ANISOU 5487  CA  LEU B 344    17602  24057  22302    721  -2700   4076       C  
ATOM   5488  C   LEU B 344     -35.203 -38.182  26.059  1.00163.78           C  
ANISOU 5488  C   LEU B 344    17158  23087  21983    571  -2276   3907       C  
ATOM   5489  O   LEU B 344     -36.074 -39.010  25.827  1.00162.77           O  
ANISOU 5489  O   LEU B 344    17042  22916  21888    574  -2064   4218       O  
ATOM   5490  CB  LEU B 344     -35.041 -37.067  28.319  1.00169.47           C  
ANISOU 5490  CB  LEU B 344    17998  24683  21711    850  -2867   3849       C  
ATOM   5491  CG  LEU B 344     -36.555 -36.911  28.330  1.00167.69           C  
ANISOU 5491  CG  LEU B 344    18017  24702  20995    925  -2608   3922       C  
ATOM   5492  CD1 LEU B 344     -37.185 -38.152  28.939  1.00169.65           C  
ANISOU 5492  CD1 LEU B 344    18138  25190  21132   1014  -2552   4548       C  
ATOM   5493  CD2 LEU B 344     -36.936 -35.669  29.105  1.00169.04           C  
ANISOU 5493  CD2 LEU B 344    18441  25307  20480   1084  -2786   3590       C  
ATOM   5494  N   PRO B 345     -34.831 -37.255  25.148  1.00163.92           N  
ANISOU 5494  N   PRO B 345    17279  22820  22183    432  -2162   3431       N  
ATOM   5495  CA  PRO B 345     -35.381 -37.364  23.789  1.00160.05           C  
ANISOU 5495  CA  PRO B 345    16899  21946  21965    309  -1773   3301       C  
ATOM   5496  C   PRO B 345     -35.131 -38.719  23.145  1.00159.83           C  
ANISOU 5496  C   PRO B 345    16642  21573  22513    268  -1622   3584       C  
ATOM   5497  O   PRO B 345     -35.960 -39.186  22.369  1.00157.50           O  
ANISOU 5497  O   PRO B 345    16437  21085  22319    229  -1347   3642       O  
ATOM   5498  CB  PRO B 345     -34.642 -36.274  23.023  1.00159.29           C  
ANISOU 5498  CB  PRO B 345    16879  21589  22054    162  -1730   2820       C  
ATOM   5499  CG  PRO B 345     -34.380 -35.246  24.031  1.00161.58           C  
ANISOU 5499  CG  PRO B 345    17266  22204  21924    221  -2055   2625       C  
ATOM   5500  CD  PRO B 345     -34.138 -35.968  25.334  1.00165.23           C  
ANISOU 5500  CD  PRO B 345    17529  23034  22217    383  -2368   2993       C  
ATOM   5501  N   ILE B 346     -33.992 -39.329  23.452  1.00161.37           N  
ANISOU 5501  N   ILE B 346    16541  21680  23091    292  -1820   3732       N  
ATOM   5502  CA  ILE B 346     -33.696 -40.666  22.959  1.00161.95           C  
ANISOU 5502  CA  ILE B 346    16394  21421  23719    303  -1728   4005       C  
ATOM   5503  C   ILE B 346     -34.689 -41.670  23.524  1.00162.92           C  
ANISOU 5503  C   ILE B 346    16545  21673  23684    384  -1729   4494       C  
ATOM   5504  O   ILE B 346     -35.207 -42.524  22.801  1.00161.75           O  
ANISOU 5504  O   ILE B 346    16397  21219  23841    342  -1518   4631       O  
ATOM   5505  CB  ILE B 346     -32.274 -41.114  23.339  1.00168.06           C  
ANISOU 5505  CB  ILE B 346    16825  22129  24901    363  -1990   4089       C  
ATOM   5506  CG1 ILE B 346     -31.225 -40.194  22.717  1.00167.65           C  
ANISOU 5506  CG1 ILE B 346    16677  21934  25088    242  -1966   3634       C  
ATOM   5507  CG2 ILE B 346     -32.040 -42.528  22.892  1.00169.11           C  
ANISOU 5507  CG2 ILE B 346    16756  21909  25590    423  -1918   4376       C  
ATOM   5508  CD1 ILE B 346     -31.284 -40.133  21.223  1.00164.58           C  
ANISOU 5508  CD1 ILE B 346    16351  21146  25036    119  -1573   3360       C  
ATOM   5509  N   ILE B 347     -34.958 -41.548  24.820  1.00164.11           N  
ANISOU 5509  N   ILE B 347    16720  22285  23348    495  -1969   4754       N  
ATOM   5510  CA  ILE B 347     -35.946 -42.395  25.475  1.00165.64           C  
ANISOU 5510  CA  ILE B 347    16938  22682  23315    553  -1957   5265       C  
ATOM   5511  C   ILE B 347     -37.321 -42.239  24.829  1.00162.45           C  
ANISOU 5511  C   ILE B 347    16744  22261  22720    463  -1635   5194       C  
ATOM   5512  O   ILE B 347     -38.020 -43.224  24.586  1.00162.63           O  
ANISOU 5512  O   ILE B 347    16728  22120  22944    410  -1498   5524       O  
ATOM   5513  CB  ILE B 347     -36.046 -42.069  26.976  1.00169.05           C  
ANISOU 5513  CB  ILE B 347    17396  23708  23128    707  -2240   5501       C  
ATOM   5514  CG1 ILE B 347     -34.690 -42.269  27.651  1.00172.68           C  
ANISOU 5514  CG1 ILE B 347    17632  24205  23773    812  -2605   5582       C  
ATOM   5515  CG2 ILE B 347     -37.097 -42.941  27.642  1.00171.08           C  
ANISOU 5515  CG2 ILE B 347    17663  24209  23132    747  -2182   6078       C  
ATOM   5516  CD1 ILE B 347     -34.592 -41.657  29.024  1.00176.00           C  
ANISOU 5516  CD1 ILE B 347    18105  25216  23551    975  -2927   5643       C  
ATOM   5517  N   ALA B 348     -37.674 -40.996  24.517  1.00161.11           N  
ANISOU 5517  N   ALA B 348    16789  22227  22199    443  -1534   4751       N  
ATOM   5518  CA  ALA B 348     -38.916 -40.666  23.831  1.00158.05           C  
ANISOU 5518  CA  ALA B 348    16605  21833  21616    384  -1249   4601       C  
ATOM   5519  C   ALA B 348     -38.985 -41.350  22.473  1.00155.71           C  
ANISOU 5519  C   ALA B 348    16276  20996  21893    255  -1007   4521       C  
ATOM   5520  O   ALA B 348     -40.021 -41.907  22.095  1.00154.87           O  
ANISOU 5520  O   ALA B 348    16203  20825  21815    200   -831   4680       O  
ATOM   5521  CB  ALA B 348     -39.045 -39.162  23.676  1.00158.11           C  
ANISOU 5521  CB  ALA B 348    16857  22001  21218    411  -1229   4100       C  
ATOM   5522  N   VAL B 349     -37.884 -41.268  21.733  1.00156.39           N  
ANISOU 5522  N   VAL B 349    16289  20714  22419    209  -1000   4248       N  
ATOM   5523  CA  VAL B 349     -37.735 -41.971  20.465  1.00154.89           C  
ANISOU 5523  CA  VAL B 349    16050  20017  22787    130   -793   4147       C  
ATOM   5524  C   VAL B 349     -37.971 -43.472  20.616  1.00157.06           C  
ANISOU 5524  C   VAL B 349    16154  20097  23424    135   -829   4602       C  
ATOM   5525  O   VAL B 349     -38.654 -44.080  19.796  1.00155.89           O  
ANISOU 5525  O   VAL B 349    16052  19667  23511     67   -649   4605       O  
ATOM   5526  CB  VAL B 349     -36.350 -41.723  19.859  1.00157.92           C  
ANISOU 5526  CB  VAL B 349    16311  20119  23573    111   -800   3848       C  
ATOM   5527  CG1 VAL B 349     -36.036 -42.741  18.775  1.00157.76           C  
ANISOU 5527  CG1 VAL B 349    16173  19612  24156     95   -636   3828       C  
ATOM   5528  CG2 VAL B 349     -36.276 -40.312  19.318  1.00155.50           C  
ANISOU 5528  CG2 VAL B 349    16213  19856  23013     45   -682   3382       C  
ATOM   5529  N   PHE B 350     -37.424 -44.072  21.670  1.00157.89           N  
ANISOU 5529  N   PHE B 350    16074  20337  23578    215  -1082   4990       N  
ATOM   5530  CA  PHE B 350     -37.590 -45.512  21.854  1.00160.55           C  
ANISOU 5530  CA  PHE B 350    16266  20441  24295    219  -1144   5462       C  
ATOM   5531  C   PHE B 350     -39.006 -45.885  22.255  1.00160.99           C  
ANISOU 5531  C   PHE B 350    16404  20704  24060    145  -1063   5819       C  
ATOM   5532  O   PHE B 350     -39.485 -46.956  21.887  1.00162.00           O  
ANISOU 5532  O   PHE B 350    16480  20509  24563     66  -1005   6071       O  
ATOM   5533  CB  PHE B 350     -36.607 -46.045  22.891  1.00166.38           C  
ANISOU 5533  CB  PHE B 350    16795  21272  25152    345  -1456   5814       C  
ATOM   5534  CG  PHE B 350     -35.235 -46.260  22.346  1.00167.07           C  
ANISOU 5534  CG  PHE B 350    16697  21007  25773    415  -1528   5585       C  
ATOM   5535  CD1 PHE B 350     -34.159 -45.533  22.823  1.00168.08           C  
ANISOU 5535  CD1 PHE B 350    16711  21352  25801    490  -1719   5402       C  
ATOM   5536  CD2 PHE B 350     -35.027 -47.168  21.320  1.00166.98           C  
ANISOU 5536  CD2 PHE B 350    16613  20457  26373    409  -1402   5519       C  
ATOM   5537  CE1 PHE B 350     -32.896 -45.730  22.301  1.00169.07           C  
ANISOU 5537  CE1 PHE B 350    16613  21188  26437    549  -1765   5194       C  
ATOM   5538  CE2 PHE B 350     -33.767 -47.365  20.794  1.00167.95           C  
ANISOU 5538  CE2 PHE B 350    16540  20297  26979    503  -1438   5292       C  
ATOM   5539  CZ  PHE B 350     -32.702 -46.642  21.283  1.00168.99           C  
ANISOU 5539  CZ  PHE B 350    16521  20674  27014    567  -1608   5141       C  
ATOM   5540  N   ILE B 351     -39.685 -44.998  22.978  1.00160.54           N  
ANISOU 5540  N   ILE B 351    16465  21179  23353    171  -1059   5821       N  
ATOM   5541  CA  ILE B 351     -41.107 -45.185  23.251  1.00160.79           C  
ANISOU 5541  CA  ILE B 351    16554  21471  23069     99   -927   6093       C  
ATOM   5542  C   ILE B 351     -41.917 -45.163  21.961  1.00157.53           C  
ANISOU 5542  C   ILE B 351    16248  20754  22854    -24   -670   5786       C  
ATOM   5543  O   ILE B 351     -42.710 -46.072  21.693  1.00158.47           O  
ANISOU 5543  O   ILE B 351    16305  20690  23219   -145   -587   6054       O  
ATOM   5544  CB  ILE B 351     -41.656 -44.100  24.183  1.00160.93           C  
ANISOU 5544  CB  ILE B 351    16685  22146  22315    201   -950   6052       C  
ATOM   5545  CG1 ILE B 351     -41.123 -44.285  25.601  1.00165.07           C  
ANISOU 5545  CG1 ILE B 351    17107  23058  22555    332  -1214   6455       C  
ATOM   5546  CG2 ILE B 351     -43.159 -44.159  24.213  1.00160.74           C  
ANISOU 5546  CG2 ILE B 351    16699  22386  21989    132   -752   6222       C  
ATOM   5547  CD1 ILE B 351     -41.493 -43.143  26.524  1.00165.60           C  
ANISOU 5547  CD1 ILE B 351    17303  23774  21844    481  -1272   6327       C  
ATOM   5548  N   ILE B 352     -41.673 -44.136  21.152  1.00154.13           N  
ANISOU 5548  N   ILE B 352    15976  20250  22336      0   -563   5229       N  
ATOM   5549  CA  ILE B 352     -42.277 -44.022  19.830  1.00151.08           C  
ANISOU 5549  CA  ILE B 352    15717  19564  22122    -83   -338   4878       C  
ATOM   5550  C   ILE B 352     -42.101 -45.321  19.059  1.00152.02           C  
ANISOU 5550  C   ILE B 352    15721  19131  22908   -168   -313   4994       C  
ATOM   5551  O   ILE B 352     -43.049 -45.865  18.494  1.00151.77           O  
ANISOU 5551  O   ILE B 352    15703  18937  23024   -272   -206   5039       O  
ATOM   5552  CB  ILE B 352     -41.672 -42.869  19.026  1.00149.00           C  
ANISOU 5552  CB  ILE B 352    15630  19200  21783    -41   -251   4311       C  
ATOM   5553  CG1 ILE B 352     -42.095 -41.534  19.624  1.00148.02           C  
ANISOU 5553  CG1 ILE B 352    15679  19557  21006     40   -268   4133       C  
ATOM   5554  CG2 ILE B 352     -42.114 -42.946  17.578  1.00146.47           C  
ANISOU 5554  CG2 ILE B 352    15432  18510  21708   -106    -34   3984       C  
ATOM   5555  CD1 ILE B 352     -41.409 -40.366  19.001  1.00145.81           C  
ANISOU 5555  CD1 ILE B 352    15575  19166  20660     61   -225   3638       C  
ATOM   5556  N   CYS B 353     -40.870 -45.810  19.034  1.00155.96           N  
ANISOU 5556  N   CYS B 353    16097  19340  23821   -112   -431   5016       N  
ATOM   5557  CA  CYS B 353     -40.562 -47.036  18.320  1.00157.34           C  
ANISOU 5557  CA  CYS B 353    16169  18963  24649   -141   -434   5081       C  
ATOM   5558  C   CYS B 353     -41.318 -48.223  18.919  1.00160.59           C  
ANISOU 5558  C   CYS B 353    16470  19311  25235   -234   -532   5639       C  
ATOM   5559  O   CYS B 353     -41.701 -49.135  18.196  1.00161.33           O  
ANISOU 5559  O   CYS B 353    16550  18974  25774   -317   -494   5658       O  
ATOM   5560  CB  CYS B 353     -39.052 -47.293  18.335  1.00157.48           C  
ANISOU 5560  CB  CYS B 353    16039  18751  25044    -19   -561   5021       C  
ATOM   5561  SG  CYS B 353     -38.093 -46.033  17.468  1.00154.40           S  
ANISOU 5561  SG  CYS B 353    15732  18356  24578     35   -413   4391       S  
ATOM   5562  N   ALA B 354     -41.557 -48.203  20.227  1.00160.32           N  
ANISOU 5562  N   ALA B 354    16365  19707  24844   -226   -658   6094       N  
ATOM   5563  CA  ALA B 354     -42.311 -49.283  20.854  1.00163.92           C  
ANISOU 5563  CA  ALA B 354    16711  20141  25429   -342   -727   6691       C  
ATOM   5564  C   ALA B 354     -43.750 -49.301  20.345  1.00162.74           C  
ANISOU 5564  C   ALA B 354    16616  20038  25179   -517   -543   6659       C  
ATOM   5565  O   ALA B 354     -44.230 -50.331  19.849  1.00164.39           O  
ANISOU 5565  O   ALA B 354    16769  19828  25863   -663   -542   6819       O  
ATOM   5566  CB  ALA B 354     -42.280 -49.156  22.371  1.00166.88           C  
ANISOU 5566  CB  ALA B 354    17011  21051  25345   -277   -873   7185       C  
ATOM   5567  N   CYS B 355     -44.429 -48.158  20.460  1.00164.02           N  
ANISOU 5567  N   CYS B 355    16883  20696  24743   -494   -408   6433       N  
ATOM   5568  CA  CYS B 355     -45.822 -48.046  20.006  1.00162.98           C  
ANISOU 5568  CA  CYS B 355    16777  20687  24462   -630   -239   6371       C  
ATOM   5569  C   CYS B 355     -45.946 -48.415  18.531  1.00161.05           C  
ANISOU 5569  C   CYS B 355    16607  19880  24706   -707   -160   5965       C  
ATOM   5570  O   CYS B 355     -46.836 -49.186  18.124  1.00162.43           O  
ANISOU 5570  O   CYS B 355    16709  19840  25167   -881   -133   6104       O  
ATOM   5571  CB  CYS B 355     -46.356 -46.623  20.215  1.00156.51           C  
ANISOU 5571  CB  CYS B 355    16089  20439  22939   -520   -121   6070       C  
ATOM   5572  SG  CYS B 355     -46.351 -46.017  21.918  1.00158.92           S  
ANISOU 5572  SG  CYS B 355    16346  21494  22543   -381   -207   6439       S  
ATOM   5573  N   GLU B 356     -45.031 -47.861  17.741  1.00162.10           N  
ANISOU 5573  N   GLU B 356    16876  19787  24929   -579   -128   5466       N  
ATOM   5574  CA  GLU B 356     -44.965 -48.134  16.316  1.00160.46           C  
ANISOU 5574  CA  GLU B 356    16764  19077  25128   -597    -47   5034       C  
ATOM   5575  C   GLU B 356     -44.812 -49.620  16.032  1.00163.67           C  
ANISOU 5575  C   GLU B 356    17048  18922  26215   -686   -164   5266       C  
ATOM   5576  O   GLU B 356     -45.482 -50.162  15.162  1.00163.88           O  
ANISOU 5576  O   GLU B 356    17103  18629  26534   -789   -133   5117       O  
ATOM   5577  CB  GLU B 356     -43.816 -47.369  15.681  1.00164.87           C  
ANISOU 5577  CB  GLU B 356    17448  19517  25677   -440     14   4558       C  
ATOM   5578  CG  GLU B 356     -43.759 -47.554  14.189  1.00163.37           C  
ANISOU 5578  CG  GLU B 356    17379  18885  25811   -427    132   4096       C  
ATOM   5579  CD  GLU B 356     -42.704 -46.696  13.550  1.00161.13           C  
ANISOU 5579  CD  GLU B 356    17212  18552  25458   -294    243   3656       C  
ATOM   5580  OE1 GLU B 356     -42.029 -45.947  14.286  1.00160.73           O  
ANISOU 5580  OE1 GLU B 356    17139  18791  25142   -235    204   3701       O  
ATOM   5581  OE2 GLU B 356     -42.554 -46.765  12.313  1.00160.11           O  
ANISOU 5581  OE2 GLU B 356    17193  18108  25534   -253    366   3266       O  
ATOM   5582  N   CYS B 357     -43.908 -50.266  16.758  1.00160.77           N  
ANISOU 5582  N   CYS B 357    16555  18422  26110   -629   -326   5610       N  
ATOM   5583  CA  CYS B 357     -43.717 -51.704  16.638  1.00164.52           C  
ANISOU 5583  CA  CYS B 357    16923  18342  27245   -690   -476   5885       C  
ATOM   5584  C   CYS B 357     -45.026 -52.446  16.877  1.00167.06           C  
ANISOU 5584  C   CYS B 357    17168  18635  27673   -936   -502   6284       C  
ATOM   5585  O   CYS B 357     -45.406 -53.311  16.083  1.00168.51           O  
ANISOU 5585  O   CYS B 357    17356  18316  28356  -1046   -544   6195       O  
ATOM   5586  CB  CYS B 357     -42.634 -52.184  17.609  1.00165.89           C  
ANISOU 5586  CB  CYS B 357    16967  18479  27585   -571   -670   6279       C  
ATOM   5587  SG  CYS B 357     -40.942 -51.843  17.049  1.00164.56           S  
ANISOU 5587  SG  CYS B 357    16799  18091  27636   -305   -684   5812       S  
ATOM   5588  N   ILE B 358     -45.709 -52.102  17.965  1.00166.01           N  
ANISOU 5588  N   ILE B 358    16954  19052  27070  -1023   -479   6710       N  
ATOM   5589  CA  ILE B 358     -46.993 -52.720  18.284  1.00168.81           C  
ANISOU 5589  CA  ILE B 358    17186  19478  27477  -1282   -469   7138       C  
ATOM   5590  C   ILE B 358     -47.972 -52.618  17.106  1.00166.88           C  
ANISOU 5590  C   ILE B 358    16999  19073  27335  -1407   -360   6709       C  
ATOM   5591  O   ILE B 358     -48.512 -53.634  16.635  1.00169.57           O  
ANISOU 5591  O   ILE B 358    17272  18961  28197  -1605   -442   6818       O  
ATOM   5592  CB  ILE B 358     -47.621 -52.079  19.534  1.00169.54           C  
ANISOU 5592  CB  ILE B 358    17190  20329  26899  -1305   -391   7547       C  
ATOM   5593  CG1 ILE B 358     -46.732 -52.322  20.755  1.00172.39           C  
ANISOU 5593  CG1 ILE B 358    17489  20850  27162  -1189   -538   8032       C  
ATOM   5594  CG2 ILE B 358     -49.013 -52.630  19.775  1.00172.52           C  
ANISOU 5594  CG2 ILE B 358    17399  20840  27310  -1587   -330   7961       C  
ATOM   5595  CD1 ILE B 358     -47.044 -51.424  21.928  1.00172.50           C  
ANISOU 5595  CD1 ILE B 358    17476  21667  26401  -1102   -468   8264       C  
ATOM   5596  N   GLY B 359     -48.172 -51.396  16.613  1.00168.36           N  
ANISOU 5596  N   GLY B 359    17323  19604  27042  -1285   -202   6209       N  
ATOM   5597  CA  GLY B 359     -49.098 -51.168  15.512  1.00166.49           C  
ANISOU 5597  CA  GLY B 359    17156  19286  26816  -1361   -110   5783       C  
ATOM   5598  C   GLY B 359     -48.718 -51.878  14.218  1.00166.55           C  
ANISOU 5598  C   GLY B 359    17264  18599  27416  -1353   -182   5380       C  
ATOM   5599  O   GLY B 359     -49.566 -52.469  13.539  1.00167.94           O  
ANISOU 5599  O   GLY B 359    17407  18506  27898  -1519   -226   5290       O  
ATOM   5600  N   ASP B 360     -47.434 -51.814  13.880  1.00165.04           N  
ANISOU 5600  N   ASP B 360    17185  18139  27384  -1149   -198   5122       N  
ATOM   5601  CA  ASP B 360     -46.892 -52.419  12.666  1.00165.28           C  
ANISOU 5601  CA  ASP B 360    17320  17556  27922  -1068   -242   4696       C  
ATOM   5602  C   ASP B 360     -47.041 -53.942  12.662  1.00170.05           C  
ANISOU 5602  C   ASP B 360    17808  17580  29222  -1222   -450   4996       C  
ATOM   5603  O   ASP B 360     -47.451 -54.541  11.660  1.00171.13           O  
ANISOU 5603  O   ASP B 360    18005  17282  29736  -1281   -512   4693       O  
ATOM   5604  CB  ASP B 360     -45.414 -52.052  12.508  1.00171.34           C  
ANISOU 5604  CB  ASP B 360    18164  18233  28707   -815   -201   4448       C  
ATOM   5605  CG  ASP B 360     -45.195 -50.587  12.142  1.00166.89           C  
ANISOU 5605  CG  ASP B 360    17762  18075  27573   -676      0   4026       C  
ATOM   5606  OD1 ASP B 360     -46.148 -49.925  11.686  1.00164.75           O  
ANISOU 5606  OD1 ASP B 360    17600  18041  26956   -726    105   3801       O  
ATOM   5607  OD2 ASP B 360     -44.053 -50.100  12.295  1.00165.85           O  
ANISOU 5607  OD2 ASP B 360    17644  18008  27362   -517     40   3919       O  
ATOM   5608  N   VAL B 361     -46.678 -54.560  13.785  1.00167.76           N  
ANISOU 5608  N   VAL B 361    17370  17270  29101  -1274   -577   5586       N  
ATOM   5609  CA  VAL B 361     -46.814 -56.003  13.972  1.00172.95           C  
ANISOU 5609  CA  VAL B 361    17922  17371  30419  -1436   -795   5983       C  
ATOM   5610  C   VAL B 361     -48.272 -56.447  13.887  1.00175.07           C  
ANISOU 5610  C   VAL B 361    18095  17621  30804  -1766   -827   6181       C  
ATOM   5611  O   VAL B 361     -48.585 -57.417  13.187  1.00177.98           O  
ANISOU 5611  O   VAL B 361    18472  17396  31755  -1892   -979   6072       O  
ATOM   5612  CB  VAL B 361     -46.228 -56.451  15.324  1.00176.12           C  
ANISOU 5612  CB  VAL B 361    18192  17855  30871  -1427   -917   6659       C  
ATOM   5613  CG1 VAL B 361     -46.734 -57.838  15.705  1.00181.95           C  
ANISOU 5613  CG1 VAL B 361    18815  18122  32196  -1679  -1123   7218       C  
ATOM   5614  CG2 VAL B 361     -44.715 -56.424  15.266  1.00175.61           C  
ANISOU 5614  CG2 VAL B 361    18176  17598  30951  -1115   -972   6463       C  
ATOM   5615  N   THR B 362     -49.157 -55.756  14.610  1.00174.09           N  
ANISOU 5615  N   THR B 362    17862  18142  30140  -1903   -695   6463       N  
ATOM   5616  CA  THR B 362     -50.582 -56.090  14.559  1.00176.28           C  
ANISOU 5616  CA  THR B 362    17990  18493  30494  -2224   -699   6657       C  
ATOM   5617  C   THR B 362     -51.122 -56.012  13.132  1.00174.60           C  
ANISOU 5617  C   THR B 362    17890  18007  30443  -2236   -707   5996       C  
ATOM   5618  O   THR B 362     -51.820 -56.916  12.652  1.00178.00           O  
ANISOU 5618  O   THR B 362    18243  18007  31383  -2476   -859   6015       O  
ATOM   5619  CB  THR B 362     -51.410 -55.151  15.445  1.00174.98           C  
ANISOU 5619  CB  THR B 362    17694  19164  29627  -2288   -511   6940       C  
ATOM   5620  OG1 THR B 362     -50.868 -55.141  16.770  1.00176.58           O  
ANISOU 5620  OG1 THR B 362    17821  19680  29594  -2234   -507   7512       O  
ATOM   5621  CG2 THR B 362     -52.853 -55.616  15.500  1.00178.22           C  
ANISOU 5621  CG2 THR B 362    17875  19667  30175  -2640   -514   7227       C  
ATOM   5622  N   ALA B 363     -50.753 -54.936  12.447  1.00171.03           N  
ANISOU 5622  N   ALA B 363    17631  17788  29564  -1973   -559   5411       N  
ATOM   5623  CA  ALA B 363     -51.128 -54.751  11.054  1.00169.27           C  
ANISOU 5623  CA  ALA B 363    17561  17350  29404  -1917   -557   4751       C  
ATOM   5624  C   ALA B 363     -50.671 -55.936  10.212  1.00172.32           C  
ANISOU 5624  C   ALA B 363    18024  16935  30516  -1914   -761   4522       C  
ATOM   5625  O   ALA B 363     -51.439 -56.476   9.419  1.00174.29           O  
ANISOU 5625  O   ALA B 363    18271  16867  31085  -2062   -890   4284       O  
ATOM   5626  CB  ALA B 363     -50.541 -53.453  10.513  1.00173.69           C  
ANISOU 5626  CB  ALA B 363    18348  18228  29417  -1609   -362   4226       C  
ATOM   5627  N   THR B 364     -49.420 -56.345  10.403  1.00171.97           N  
ANISOU 5627  N   THR B 364    18038  16567  30735  -1730   -810   4580       N  
ATOM   5628  CA  THR B 364     -48.878 -57.493   9.684  1.00175.35           C  
ANISOU 5628  CA  THR B 364    18542  16224  31859  -1668  -1011   4364       C  
ATOM   5629  C   THR B 364     -49.716 -58.741   9.943  1.00180.89           C  
ANISOU 5629  C   THR B 364    19091  16480  33158  -2012  -1260   4769       C  
ATOM   5630  O   THR B 364     -50.028 -59.495   9.020  1.00183.50           O  
ANISOU 5630  O   THR B 364    19490  16261  33969  -2070  -1440   4427       O  
ATOM   5631  CB  THR B 364     -47.416 -57.774  10.088  1.00175.82           C  
ANISOU 5631  CB  THR B 364    18624  16063  32116  -1415  -1036   4480       C  
ATOM   5632  OG1 THR B 364     -46.611 -56.619   9.819  1.00171.12           O  
ANISOU 5632  OG1 THR B 364    18144  15862  31013  -1132   -808   4105       O  
ATOM   5633  CG2 THR B 364     -46.873 -58.962   9.313  1.00179.70           C  
ANISOU 5633  CG2 THR B 364    19196  15753  33328  -1302  -1247   4214       C  
ATOM   5634  N   CYS B 365     -50.096 -58.929  11.204  1.00182.78           N  
ANISOU 5634  N   CYS B 365    19126  16976  33348  -2245  -1270   5498       N  
ATOM   5635  CA  CYS B 365     -50.919 -60.062  11.613  1.00188.52           C  
ANISOU 5635  CA  CYS B 365    19675  17336  34617  -2626  -1478   6012       C  
ATOM   5636  C   CYS B 365     -52.253 -60.087  10.868  1.00189.21           C  
ANISOU 5636  C   CYS B 365    19692  17429  34771  -2890  -1522   5743       C  
ATOM   5637  O   CYS B 365     -52.729 -61.159  10.484  1.00194.00           O  
ANISOU 5637  O   CYS B 365    20250  17429  36030  -3133  -1770   5773       O  
ATOM   5638  CB  CYS B 365     -51.142 -60.038  13.125  1.00190.32           C  
ANISOU 5638  CB  CYS B 365    19691  18010  34610  -2811  -1409   6857       C  
ATOM   5639  SG  CYS B 365     -49.641 -60.388  14.077  1.00191.66           S  
ANISOU 5639  SG  CYS B 365    19912  18023  34888  -2553  -1477   7284       S  
ATOM   5640  N   ASP B 366     -52.866 -58.918  10.680  1.00184.86           N  
ANISOU 5640  N   ASP B 366    19128  17544  33566  -2844  -1309   5483       N  
ATOM   5641  CA  ASP B 366     -54.092 -58.858   9.874  1.00185.35           C  
ANISOU 5641  CA  ASP B 366    19123  17644  33656  -3040  -1365   5150       C  
ATOM   5642  C   ASP B 366     -53.813 -59.110   8.390  1.00184.94           C  
ANISOU 5642  C   ASP B 366    19321  17056  33892  -2852  -1510   4362       C  
ATOM   5643  O   ASP B 366     -54.631 -59.703   7.684  1.00188.00           O  
ANISOU 5643  O   ASP B 366    19660  17104  34665  -3058  -1716   4133       O  
ATOM   5644  CB  ASP B 366     -54.787 -57.504  10.030  1.00187.91           C  
ANISOU 5644  CB  ASP B 366    19388  18819  33191  -2980  -1112   5047       C  
ATOM   5645  CG  ASP B 366     -56.148 -57.466   9.348  1.00189.08           C  
ANISOU 5645  CG  ASP B 366    19400  19072  33368  -3198  -1188   4793       C  
ATOM   5646  OD1 ASP B 366     -57.111 -58.059   9.880  1.00193.38           O  
ANISOU 5646  OD1 ASP B 366    19637  19654  34184  -3582  -1269   5268       O  
ATOM   5647  OD2 ASP B 366     -56.250 -56.855   8.262  1.00186.05           O  
ANISOU 5647  OD2 ASP B 366    19209  18738  32743  -2987  -1173   4125       O  
ATOM   5648  N   VAL B 367     -52.663 -58.635   7.924  1.00181.47           N  
ANISOU 5648  N   VAL B 367    19134  16573  33241  -2457  -1400   3944       N  
ATOM   5649  CA  VAL B 367     -52.233 -58.812   6.540  1.00181.13           C  
ANISOU 5649  CA  VAL B 367    19348  16088  33386  -2209  -1487   3196       C  
ATOM   5650  C   VAL B 367     -51.888 -60.273   6.261  1.00186.75           C  
ANISOU 5650  C   VAL B 367    20085  15934  34938  -2272  -1794   3193       C  
ATOM   5651  O   VAL B 367     -52.126 -60.793   5.168  1.00188.93           O  
ANISOU 5651  O   VAL B 367    20490  15752  35544  -2239  -1985   2660       O  
ATOM   5652  CB  VAL B 367     -51.029 -57.915   6.216  1.00176.74           C  
ANISOU 5652  CB  VAL B 367    19014  15757  32383  -1787  -1247   2831       C  
ATOM   5653  CG1 VAL B 367     -50.517 -58.212   4.841  1.00177.28           C  
ANISOU 5653  CG1 VAL B 367    19330  15369  32659  -1518  -1316   2115       C  
ATOM   5654  CG2 VAL B 367     -51.430 -56.454   6.295  1.00171.57           C  
ANISOU 5654  CG2 VAL B 367    18389  15867  30931  -1714   -983   2731       C  
ATOM   5655  N   SER B 368     -51.292 -60.911   7.264  1.00189.32           N  
ANISOU 5655  N   SER B 368    20307  16036  35590  -2334  -1855   3778       N  
ATOM   5656  CA  SER B 368     -50.860 -62.303   7.185  1.00195.05           C  
ANISOU 5656  CA  SER B 368    21063  15916  37133  -2369  -2156   3872       C  
ATOM   5657  C   SER B 368     -51.932 -63.319   7.619  1.00200.92           C  
ANISOU 5657  C   SER B 368    21603  16290  38448  -2859  -2421   4365       C  
ATOM   5658  O   SER B 368     -51.643 -64.508   7.774  1.00206.37           O  
ANISOU 5658  O   SER B 368    22302  16259  39851  -2946  -2691   4593       O  
ATOM   5659  CB  SER B 368     -49.597 -62.484   8.029  1.00195.27           C  
ANISOU 5659  CB  SER B 368    21093  15865  37236  -2151  -2110   4259       C  
ATOM   5660  OG  SER B 368     -49.778 -61.972   9.337  1.00193.88           O  
ANISOU 5660  OG  SER B 368    20728  16277  36662  -2313  -1952   4953       O  
ATOM   5661  N   ARG B 369     -53.159 -62.839   7.809  1.00200.13           N  
ANISOU 5661  N   ARG B 369    21311  16682  38048  -3173  -2344   4533       N  
ATOM   5662  CA  ARG B 369     -54.313 -63.681   8.132  1.00205.74           C  
ANISOU 5662  CA  ARG B 369    21776  17136  39260  -3683  -2561   4970       C  
ATOM   5663  C   ARG B 369     -54.153 -64.419   9.456  1.00210.03           C  
ANISOU 5663  C   ARG B 369    22144  17517  40141  -3934  -2612   5891       C  
ATOM   5664  O   ARG B 369     -54.551 -65.577   9.577  1.00216.46           O  
ANISOU 5664  O   ARG B 369    22867  17694  41683  -4271  -2893   6216       O  
ATOM   5665  CB  ARG B 369     -54.581 -64.693   7.012  1.00210.40           C  
ANISOU 5665  CB  ARG B 369    22483  16894  40566  -3766  -2930   4451       C  
ATOM   5666  CG  ARG B 369     -54.915 -64.082   5.660  1.00207.34           C  
ANISOU 5666  CG  ARG B 369    22262  16649  39870  -3558  -2928   3559       C  
ATOM   5667  CD  ARG B 369     -56.346 -63.584   5.603  1.00207.01           C  
ANISOU 5667  CD  ARG B 369    21973  17121  39560  -3891  -2900   3594       C  
ATOM   5668  NE  ARG B 369     -56.487 -62.267   6.215  1.00201.24           N  
ANISOU 5668  NE  ARG B 369    21145  17332  37984  -3787  -2520   3808       N  
ATOM   5669  CZ  ARG B 369     -57.183 -62.029   7.321  1.00201.80           C  
ANISOU 5669  CZ  ARG B 369    20899  17918  37856  -4093  -2375   4500       C  
ATOM   5670  NH1 ARG B 369     -57.790 -63.028   7.952  1.00207.91           N  
ANISOU 5670  NH1 ARG B 369    21408  18366  39221  -4553  -2555   5101       N  
ATOM   5671  NH2 ARG B 369     -57.263 -60.796   7.806  1.00196.65           N  
ANISOU 5671  NH2 ARG B 369    20200  18103  36416  -3935  -2047   4598       N  
ATOM   5672  N   LEU B 370     -53.602 -63.738  10.455  1.00206.86           N  
ANISOU 5672  N   LEU B 370    21701  17694  39204  -3781  -2353   6324       N  
ATOM   5673  CA  LEU B 370     -53.297 -64.385  11.727  1.00210.86           C  
ANISOU 5673  CA  LEU B 370    22083  18088  39947  -3941  -2394   7196       C  
ATOM   5674  C   LEU B 370     -54.115 -63.844  12.893  1.00210.73           C  
ANISOU 5674  C   LEU B 370    21778  18865  39423  -4220  -2161   7899       C  
ATOM   5675  O   LEU B 370     -54.992 -62.997  12.714  1.00207.76           O  
ANISOU 5675  O   LEU B 370    21273  19110  38554  -4304  -1979   7706       O  
ATOM   5676  CB  LEU B 370     -51.811 -64.237  12.045  1.00208.69           C  
ANISOU 5676  CB  LEU B 370    21996  17755  39542  -3499  -2344   7181       C  
ATOM   5677  CG  LEU B 370     -50.844 -64.678  10.950  1.00208.70           C  
ANISOU 5677  CG  LEU B 370    22265  17070  39961  -3138  -2517   6478       C  
ATOM   5678  CD1 LEU B 370     -49.425 -64.444  11.415  1.00206.73           C  
ANISOU 5678  CD1 LEU B 370    22118  16897  39535  -2725  -2435   6547       C  
ATOM   5679  CD2 LEU B 370     -51.052 -66.143  10.581  1.00215.85           C  
ANISOU 5679  CD2 LEU B 370    23207  16992  41815  -3349  -2901   6536       C  
ATOM   5680  N   GLU B 371     -53.816 -64.357  14.085  1.00214.38           N  
ANISOU 5680  N   GLU B 371    22144  19309  40003  -4337  -2175   8716       N  
ATOM   5681  CA  GLU B 371     -54.478 -63.931  15.313  1.00215.13           C  
ANISOU 5681  CA  GLU B 371    21973  20170  39597  -4564  -1945   9456       C  
ATOM   5682  C   GLU B 371     -54.267 -62.436  15.518  1.00208.08           C  
ANISOU 5682  C   GLU B 371    21118  20195  37749  -4229  -1626   9163       C  
ATOM   5683  O   GLU B 371     -53.235 -61.885  15.115  1.00203.49           O  
ANISOU 5683  O   GLU B 371    20776  19606  36935  -3810  -1593   8654       O  
ATOM   5684  CB  GLU B 371     -53.954 -64.703  16.526  1.00220.14           C  
ANISOU 5684  CB  GLU B 371    22569  20616  40459  -4647  -2023  10345       C  
ATOM   5685  CG  GLU B 371     -54.079 -66.219  16.422  1.00227.81           C  
ANISOU 5685  CG  GLU B 371    23534  20607  42416  -4972  -2362  10713       C  
ATOM   5686  CD  GLU B 371     -52.815 -66.877  15.881  1.00228.46           C  
ANISOU 5686  CD  GLU B 371    23919  19850  43033  -4623  -2632  10350       C  
ATOM   5687  OE1 GLU B 371     -51.927 -66.150  15.380  1.00222.73           O  
ANISOU 5687  OE1 GLU B 371    23384  19295  41948  -4158  -2545   9711       O  
ATOM   5688  OE2 GLU B 371     -52.710 -68.122  15.954  1.00235.05           O  
ANISOU 5688  OE2 GLU B 371    24795  19852  44662  -4810  -2931  10708       O  
ATOM   5689  N   VAL B 372     -55.245 -61.777  16.131  1.00207.58           N  
ANISOU 5689  N   VAL B 372    20810  20916  37146  -4411  -1394   9473       N  
ATOM   5690  CA  VAL B 372     -55.160 -60.337  16.326  1.00201.40           C  
ANISOU 5690  CA  VAL B 372    20069  20988  35465  -4101  -1114   9177       C  
ATOM   5691  C   VAL B 372     -55.301 -59.980  17.815  1.00202.83           C  
ANISOU 5691  C   VAL B 372    20071  21907  35087  -4137   -912   9933       C  
ATOM   5692  O   VAL B 372     -54.988 -58.860  18.224  1.00198.44           O  
ANISOU 5692  O   VAL B 372    19584  22020  33793  -3837   -715   9783       O  
ATOM   5693  CB  VAL B 372     -56.233 -59.598  15.493  1.00203.51           C  
ANISOU 5693  CB  VAL B 372    20247  21618  35458  -4162  -1007   8632       C  
ATOM   5694  CG1 VAL B 372     -55.983 -58.098  15.513  1.00196.94           C  
ANISOU 5694  CG1 VAL B 372    19543  21521  33763  -3779   -761   8211       C  
ATOM   5695  CG2 VAL B 372     -56.191 -60.073  14.054  1.00203.24           C  
ANISOU 5695  CG2 VAL B 372    20380  20855  35986  -4155  -1235   7938       C  
ATOM   5696  N   ARG B 373     -55.770 -60.931  18.625  1.00209.36           N  
ANISOU 5696  N   ARG B 373    20680  22610  36259  -4502   -966  10747       N  
ATOM   5697  CA  ARG B 373     -55.897 -60.697  20.063  1.00211.66           C  
ANISOU 5697  CA  ARG B 373    20806  23602  36013  -4532   -775  11519       C  
ATOM   5698  C   ARG B 373     -55.393 -61.851  20.944  1.00218.00           C  
ANISOU 5698  C   ARG B 373    21601  23967  37261  -4688   -936  12354       C  
ATOM   5699  O   ARG B 373     -55.343 -61.718  22.167  1.00220.31           O  
ANISOU 5699  O   ARG B 373    21800  24811  37095  -4669   -801  13020       O  
ATOM   5700  CB  ARG B 373     -57.351 -60.384  20.417  1.00213.76           C  
ANISOU 5700  CB  ARG B 373    20712  24550  35958  -4842   -547  11817       C  
ATOM   5701  CG  ARG B 373     -58.291 -61.580  20.378  1.00220.91           C  
ANISOU 5701  CG  ARG B 373    21338  25011  37589  -5400   -659  12341       C  
ATOM   5702  CD  ARG B 373     -59.716 -61.147  20.684  1.00222.75           C  
ANISOU 5702  CD  ARG B 373    21165  26013  37454  -5674   -402  12571       C  
ATOM   5703  NE  ARG B 373     -60.628 -62.284  20.714  1.00230.21           N  
ANISOU 5703  NE  ARG B 373    21795  26567  39108  -6257   -500  13130       N  
ATOM   5704  CZ  ARG B 373     -61.925 -62.198  20.988  1.00233.69           C  
ANISOU 5704  CZ  ARG B 373    21804  27566  39424  -6604   -306  13456       C  
ATOM   5705  NH1 ARG B 373     -62.475 -61.021  21.254  1.00230.29           N  
ANISOU 5705  NH1 ARG B 373    21217  28117  38166  -6384     -4  13255       N  
ATOM   5706  NH2 ARG B 373     -62.675 -63.292  20.995  1.00240.97           N  
ANISOU 5706  NH2 ARG B 373    22435  28052  41071  -7171   -420  13980       N  
ATOM   5707  N   GLY B 374     -55.027 -62.973  20.331  1.00221.16           N  
ANISOU 5707  N   GLY B 374    22113  23384  38533  -4819  -1233  12315       N  
ATOM   5708  CA  GLY B 374     -54.636 -64.162  21.076  1.00227.94           C  
ANISOU 5708  CA  GLY B 374    22976  23717  39914  -4992  -1424  13116       C  
ATOM   5709  C   GLY B 374     -53.414 -63.996  21.964  1.00227.32           C  
ANISOU 5709  C   GLY B 374    23073  23812  39487  -4610  -1449  13412       C  
ATOM   5710  O   GLY B 374     -52.725 -62.981  21.898  1.00221.32           O  
ANISOU 5710  O   GLY B 374    22452  23485  38153  -4197  -1348  12907       O  
ATOM   5711  N   GLY B 375     -53.157 -64.983  22.818  1.00233.92           N  
ANISOU 5711  N   GLY B 375    23894  24316  40669  -4757  -1595  14252       N  
ATOM   5712  CA  GLY B 375     -51.991 -64.951  23.683  1.00234.31           C  
ANISOU 5712  CA  GLY B 375    24101  24479  40447  -4397  -1674  14582       C  
ATOM   5713  C   GLY B 375     -50.721 -65.083  22.862  1.00231.14           C  
ANISOU 5713  C   GLY B 375    23969  23409  40445  -4001  -1919  13903       C  
ATOM   5714  O   GLY B 375     -49.685 -64.482  23.175  1.00227.79           O  
ANISOU 5714  O   GLY B 375    23670  23277  39602  -3578  -1921  13704       O  
ATOM   5715  N   THR B 376     -50.814 -65.875  21.797  1.00232.59           N  
ANISOU 5715  N   THR B 376    24226  22704  41445  -4140  -2129  13528       N  
ATOM   5716  CA  THR B 376     -49.717 -66.055  20.853  1.00230.04           C  
ANISOU 5716  CA  THR B 376    24137  21720  41546  -3770  -2341  12809       C  
ATOM   5717  C   THR B 376     -49.388 -64.723  20.173  1.00221.61           C  
ANISOU 5717  C   THR B 376    23140  21192  39869  -3433  -2132  11915       C  
ATOM   5718  O   THR B 376     -48.218 -64.375  19.968  1.00218.43           O  
ANISOU 5718  O   THR B 376    22885  20739  39368  -3011  -2181  11500       O  
ATOM   5719  CB  THR B 376     -50.071 -67.117  19.789  1.00233.57           C  
ANISOU 5719  CB  THR B 376    24645  21162  42938  -4002  -2595  12523       C  
ATOM   5720  OG1 THR B 376     -50.391 -68.353  20.437  1.00241.90           O  
ANISOU 5720  OG1 THR B 376    25644  21669  44599  -4348  -2802  13388       O  
ATOM   5721  CG2 THR B 376     -48.911 -67.342  18.837  1.00231.59           C  
ANISOU 5721  CG2 THR B 376    24633  20258  43104  -3576  -2799  11784       C  
ATOM   5722  N   PHE B 377     -50.441 -63.980  19.846  1.00218.45           N  
ANISOU 5722  N   PHE B 377    22620  21314  39069  -3630  -1899  11652       N  
ATOM   5723  CA  PHE B 377     -50.336 -62.645  19.272  1.00210.92           C  
ANISOU 5723  CA  PHE B 377    21729  20931  37480  -3363  -1679  10890       C  
ATOM   5724  C   PHE B 377     -49.501 -61.729  20.169  1.00207.84           C  
ANISOU 5724  C   PHE B 377    21379  21223  36368  -3021  -1555  11003       C  
ATOM   5725  O   PHE B 377     -48.490 -61.171  19.737  1.00203.61           O  
ANISOU 5725  O   PHE B 377    20996  20672  35696  -2654  -1562  10445       O  
ATOM   5726  CB  PHE B 377     -51.743 -62.074  19.066  1.00209.51           C  
ANISOU 5726  CB  PHE B 377    21371  21273  36961  -3657  -1464  10801       C  
ATOM   5727  CG  PHE B 377     -51.777 -60.624  18.680  1.00202.39           C  
ANISOU 5727  CG  PHE B 377    20528  21053  35317  -3399  -1224  10151       C  
ATOM   5728  CD1 PHE B 377     -51.470 -60.226  17.390  1.00197.89           C  
ANISOU 5728  CD1 PHE B 377    20138  20207  34845  -3197  -1240   9281       C  
ATOM   5729  CD2 PHE B 377     -52.142 -59.660  19.606  1.00200.64           C  
ANISOU 5729  CD2 PHE B 377    20196  21748  34291  -3351   -984  10417       C  
ATOM   5730  CE1 PHE B 377     -51.516 -58.891  17.035  1.00191.79           C  
ANISOU 5730  CE1 PHE B 377    19439  20027  33404  -2974  -1025   8728       C  
ATOM   5731  CE2 PHE B 377     -52.189 -58.324  19.258  1.00194.53           C  
ANISOU 5731  CE2 PHE B 377    19498  21549  32865  -3110   -788   9822       C  
ATOM   5732  CZ  PHE B 377     -51.875 -57.939  17.969  1.00190.10           C  
ANISOU 5732  CZ  PHE B 377    19123  20670  32435  -2934   -811   8995       C  
ATOM   5733  N   GLU B 378     -49.912 -61.601  21.428  1.00210.48           N  
ANISOU 5733  N   GLU B 378    21568  22155  36251  -3145  -1449  11733       N  
ATOM   5734  CA  GLU B 378     -49.227 -60.719  22.368  1.00208.21           C  
ANISOU 5734  CA  GLU B 378    21311  22570  35228  -2835  -1354  11857       C  
ATOM   5735  C   GLU B 378     -47.807 -61.193  22.650  1.00209.71           C  
ANISOU 5735  C   GLU B 378    21631  22347  35701  -2531  -1598  11955       C  
ATOM   5736  O   GLU B 378     -46.923 -60.388  22.965  1.00206.43           O  
ANISOU 5736  O   GLU B 378    21286  22326  34821  -2193  -1579  11716       O  
ATOM   5737  CB  GLU B 378     -50.017 -60.614  23.675  1.00211.85           C  
ANISOU 5737  CB  GLU B 378    21589  23748  35157  -3028  -1200  12660       C  
ATOM   5738  CG  GLU B 378     -51.252 -59.726  23.576  1.00209.25           C  
ANISOU 5738  CG  GLU B 378    21109  24117  34279  -3185   -906  12471       C  
ATOM   5739  CD  GLU B 378     -51.960 -59.542  24.906  1.00213.01           C  
ANISOU 5739  CD  GLU B 378    21391  25397  34144  -3310   -720  13232       C  
ATOM   5740  OE1 GLU B 378     -51.735 -60.356  25.826  1.00218.79           O  
ANISOU 5740  OE1 GLU B 378    22083  26034  35014  -3400   -823  14023       O  
ATOM   5741  OE2 GLU B 378     -52.736 -58.571  25.034  1.00210.45           O  
ANISOU 5741  OE2 GLU B 378    20961  25818  33181  -3294   -468  13040       O  
ATOM   5742  N   SER B 379     -47.586 -62.496  22.520  1.00214.95           N  
ANISOU 5742  N   SER B 379    22321  22198  37152  -2645  -1846  12288       N  
ATOM   5743  CA  SER B 379     -46.232 -63.030  22.595  1.00216.60           C  
ANISOU 5743  CA  SER B 379    22647  21909  37741  -2322  -2105  12289       C  
ATOM   5744  C   SER B 379     -45.395 -62.511  21.421  1.00211.10           C  
ANISOU 5744  C   SER B 379    22074  20972  37164  -2003  -2104  11325       C  
ATOM   5745  O   SER B 379     -44.237 -62.108  21.592  1.00209.25           O  
ANISOU 5745  O   SER B 379    21884  20861  36760  -1641  -2164  11113       O  
ATOM   5746  CB  SER B 379     -46.263 -64.556  22.612  1.00223.75           C  
ANISOU 5746  CB  SER B 379    23574  21928  39515  -2510  -2384  12811       C  
ATOM   5747  OG  SER B 379     -47.140 -65.025  23.622  1.00229.15           O  
ANISOU 5747  OG  SER B 379    24131  22836  40099  -2864  -2347  13726       O  
ATOM   5748  N   ARG B 380     -46.001 -62.513  20.234  1.00208.87           N  
ANISOU 5748  N   ARG B 380    21830  20375  37157  -2143  -2032  10754       N  
ATOM   5749  CA  ARG B 380     -45.368 -61.988  19.022  1.00203.86           C  
ANISOU 5749  CA  ARG B 380    21316  19559  36583  -1871  -1982   9835       C  
ATOM   5750  C   ARG B 380     -45.009 -60.518  19.193  1.00197.80           C  
ANISOU 5750  C   ARG B 380    20557  19589  35009  -1651  -1753   9470       C  
ATOM   5751  O   ARG B 380     -43.948 -60.077  18.756  1.00194.91           O  
ANISOU 5751  O   ARG B 380    20260  19186  34613  -1331  -1752   8975       O  
ATOM   5752  CB  ARG B 380     -46.287 -62.152  17.804  1.00202.78           C  
ANISOU 5752  CB  ARG B 380    21221  19076  36752  -2088  -1933   9336       C  
ATOM   5753  CG  ARG B 380     -46.455 -63.582  17.314  1.00208.48           C  
ANISOU 5753  CG  ARG B 380    21980  18855  38376  -2248  -2205   9451       C  
ATOM   5754  CD  ARG B 380     -47.035 -63.616  15.903  1.00206.71           C  
ANISOU 5754  CD  ARG B 380    21839  18273  38426  -2331  -2191   8723       C  
ATOM   5755  NE  ARG B 380     -48.417 -63.141  15.873  1.00205.39           N  
ANISOU 5755  NE  ARG B 380    21556  18559  37925  -2684  -2024   8780       N  
ATOM   5756  CZ  ARG B 380     -49.485 -63.936  15.899  1.00210.02           C  
ANISOU 5756  CZ  ARG B 380    22031  18838  38929  -3103  -2137   9137       C  
ATOM   5757  NH1 ARG B 380     -49.337 -65.253  15.956  1.00216.33           N  
ANISOU 5757  NH1 ARG B 380    22855  18827  40514  -3233  -2429   9476       N  
ATOM   5758  NH2 ARG B 380     -50.705 -63.414  15.869  1.00208.71           N  
ANISOU 5758  NH2 ARG B 380    21716  19164  38420  -3392  -1969   9155       N  
ATOM   5759  N   ILE B 381     -45.910 -59.759  19.811  1.00196.25           N  
ANISOU 5759  N   ILE B 381    20281  20109  34177  -1825  -1559   9705       N  
ATOM   5760  CA  ILE B 381     -45.656 -58.347  20.074  1.00191.11           C  
ANISOU 5760  CA  ILE B 381    19654  20211  32747  -1629  -1367   9393       C  
ATOM   5761  C   ILE B 381     -44.493 -58.155  21.039  1.00192.01           C  
ANISOU 5761  C   ILE B 381    19758  20568  32630  -1356  -1484   9656       C  
ATOM   5762  O   ILE B 381     -43.593 -57.362  20.772  1.00188.33           O  
ANISOU 5762  O   ILE B 381    19350  20264  31944  -1090  -1452   9168       O  
ATOM   5763  CB  ILE B 381     -46.905 -57.647  20.639  1.00190.21           C  
ANISOU 5763  CB  ILE B 381    19448  20820  32002  -1842  -1155   9632       C  
ATOM   5764  CG1 ILE B 381     -47.923 -57.402  19.527  1.00187.58           C  
ANISOU 5764  CG1 ILE B 381    19132  20400  31740  -2021  -1014   9140       C  
ATOM   5765  CG2 ILE B 381     -46.540 -56.310  21.243  1.00186.43           C  
ANISOU 5765  CG2 ILE B 381    19005  21109  30721  -1611  -1023   9462       C  
ATOM   5766  CD1 ILE B 381     -49.204 -56.803  20.024  1.00187.30           C  
ANISOU 5766  CD1 ILE B 381    18966  21046  31154  -2220   -813   9367       C  
ATOM   5767  N   GLN B 382     -44.506 -58.880  22.152  1.00197.27           N  
ANISOU 5767  N   GLN B 382    20342  21261  33351  -1428  -1630  10437       N  
ATOM   5768  CA  GLN B 382     -43.396 -58.806  23.104  1.00198.95           C  
ANISOU 5768  CA  GLN B 382    20539  21682  33369  -1155  -1795  10724       C  
ATOM   5769  C   GLN B 382     -42.046 -59.135  22.475  1.00198.64           C  
ANISOU 5769  C   GLN B 382    20541  21087  33845   -859  -1976  10315       C  
ATOM   5770  O   GLN B 382     -41.077 -58.396  22.655  1.00196.29           O  
ANISOU 5770  O   GLN B 382    20235  21092  33255   -588  -1999  10028       O  
ATOM   5771  CB  GLN B 382     -43.661 -59.713  24.303  1.00205.55           C  
ANISOU 5771  CB  GLN B 382    21302  22535  34261  -1284  -1944  11675       C  
ATOM   5772  CG  GLN B 382     -44.790 -59.194  25.172  1.00206.14           C  
ANISOU 5772  CG  GLN B 382    21300  23375  33649  -1495  -1737  12113       C  
ATOM   5773  CD  GLN B 382     -44.503 -57.796  25.708  1.00202.12           C  
ANISOU 5773  CD  GLN B 382    20811  23706  32278  -1262  -1619  11822       C  
ATOM   5774  OE1 GLN B 382     -45.412 -56.983  25.883  1.00199.97           O  
ANISOU 5774  OE1 GLN B 382    20509  24043  31427  -1364  -1386  11744       O  
ATOM   5775  NE2 GLN B 382     -43.231 -57.518  25.987  1.00201.52           N  
ANISOU 5775  NE2 GLN B 382    20775  23660  32132   -942  -1799  11655       N  
ATOM   5776  N   GLY B 383     -41.988 -60.242  21.741  1.00201.38           N  
ANISOU 5776  N   GLY B 383    20919  20629  34968   -907  -2109  10276       N  
ATOM   5777  CA  GLY B 383     -40.777 -60.609  21.031  1.00201.46           C  
ANISOU 5777  CA  GLY B 383    20953  20095  35499   -604  -2256   9837       C  
ATOM   5778  C   GLY B 383     -40.365 -59.531  20.045  1.00195.30           C  
ANISOU 5778  C   GLY B 383    20212  19518  34473   -446  -2046   8980       C  
ATOM   5779  O   GLY B 383     -39.184 -59.230  19.894  1.00194.25           O  
ANISOU 5779  O   GLY B 383    20038  19388  34381   -149  -2095   8659       O  
ATOM   5780  N   ALA B 384     -41.350 -58.943  19.376  1.00191.56           N  
ANISOU 5780  N   ALA B 384    19807  19228  33747   -649  -1814   8631       N  
ATOM   5781  CA  ALA B 384     -41.100 -57.892  18.404  1.00185.93           C  
ANISOU 5781  CA  ALA B 384    19165  18711  32770   -530  -1597   7859       C  
ATOM   5782  C   ALA B 384     -40.429 -56.698  19.056  1.00182.99           C  
ANISOU 5782  C   ALA B 384    18753  19002  31773   -365  -1527   7774       C  
ATOM   5783  O   ALA B 384     -39.430 -56.210  18.555  1.00180.85           O  
ANISOU 5783  O   ALA B 384    18473  18714  31528   -143  -1489   7303       O  
ATOM   5784  CB  ALA B 384     -42.391 -57.466  17.742  1.00183.05           C  
ANISOU 5784  CB  ALA B 384    18883  18485  32183   -780  -1392   7602       C  
ATOM   5785  N   VAL B 385     -40.978 -56.230  20.173  1.00183.29           N  
ANISOU 5785  N   VAL B 385    18758  19629  31255   -474  -1512   8225       N  
ATOM   5786  CA  VAL B 385     -40.443 -55.045  20.840  1.00180.81           C  
ANISOU 5786  CA  VAL B 385    18427  19962  30310   -328  -1473   8120       C  
ATOM   5787  C   VAL B 385     -39.078 -55.330  21.478  1.00183.60           C  
ANISOU 5787  C   VAL B 385    18669  20254  30836    -72  -1717   8299       C  
ATOM   5788  O   VAL B 385     -38.159 -54.494  21.449  1.00181.38           O  
ANISOU 5788  O   VAL B 385    18352  20215  30347    108  -1714   7929       O  
ATOM   5789  CB  VAL B 385     -41.415 -54.520  21.911  1.00181.11           C  
ANISOU 5789  CB  VAL B 385    18464  20670  29682   -472  -1406   8550       C  
ATOM   5790  CG1 VAL B 385     -40.946 -53.181  22.432  1.00178.23           C  
ANISOU 5790  CG1 VAL B 385    18124  20941  28655   -316  -1367   8298       C  
ATOM   5791  CG2 VAL B 385     -42.805 -54.372  21.325  1.00179.22           C  
ANISOU 5791  CG2 VAL B 385    18282  20481  29331   -721  -1190   8430       C  
ATOM   5792  N   LEU B 386     -38.948 -56.518  22.053  1.00188.85           N  
ANISOU 5792  N   LEU B 386    19270  20583  31903    -63  -1943   8876       N  
ATOM   5793  CA  LEU B 386     -37.683 -56.937  22.638  1.00192.24           C  
ANISOU 5793  CA  LEU B 386    19584  20898  32561    204  -2213   9082       C  
ATOM   5794  C   LEU B 386     -36.579 -56.948  21.592  1.00190.82           C  
ANISOU 5794  C   LEU B 386    19346  20308  32847    429  -2212   8464       C  
ATOM   5795  O   LEU B 386     -35.546 -56.314  21.777  1.00189.91           O  
ANISOU 5795  O   LEU B 386    19123  20453  32580    632  -2268   8225       O  
ATOM   5796  CB  LEU B 386     -37.829 -58.313  23.277  1.00198.51           C  
ANISOU 5796  CB  LEU B 386    20353  21286  33785    170  -2454   9811       C  
ATOM   5797  CG  LEU B 386     -38.529 -58.222  24.630  1.00201.07           C  
ANISOU 5797  CG  LEU B 386    20681  22170  33548     36  -2492  10523       C  
ATOM   5798  CD1 LEU B 386     -39.014 -59.587  25.115  1.00207.28           C  
ANISOU 5798  CD1 LEU B 386    21475  22521  34761   -107  -2656  11289       C  
ATOM   5799  CD2 LEU B 386     -37.603 -57.560  25.644  1.00201.71           C  
ANISOU 5799  CD2 LEU B 386    20686  22812  33142    288  -2658  10623       C  
ATOM   5800  N   ALA B 387     -36.821 -57.651  20.488  1.00190.92           N  
ANISOU 5800  N   ALA B 387    19420  19706  33414    388  -2143   8193       N  
ATOM   5801  CA  ALA B 387     -35.889 -57.693  19.363  1.00189.79           C  
ANISOU 5801  CA  ALA B 387    19232  19184  33695    608  -2088   7568       C  
ATOM   5802  C   ALA B 387     -35.659 -56.304  18.780  1.00184.26           C  
ANISOU 5802  C   ALA B 387    18546  18924  32539    617  -1823   6953       C  
ATOM   5803  O   ALA B 387     -34.589 -56.015  18.244  1.00183.56           O  
ANISOU 5803  O   ALA B 387    18349  18780  32616    828  -1783   6526       O  
ATOM   5804  CB  ALA B 387     -36.399 -58.641  18.286  1.00190.99           C  
ANISOU 5804  CB  ALA B 387    19490  18646  34430    546  -2055   7366       C  
ATOM   5805  N   ASP B 388     -36.680 -55.460  18.865  1.00180.72           N  
ANISOU 5805  N   ASP B 388    18227  18900  31537    389  -1638   6918       N  
ATOM   5806  CA  ASP B 388     -36.571 -54.074  18.437  1.00175.78           C  
ANISOU 5806  CA  ASP B 388    17654  18705  30429    377  -1407   6404       C  
ATOM   5807  C   ASP B 388     -35.460 -53.366  19.199  1.00176.02           C  
ANISOU 5807  C   ASP B 388    17535  19136  30208    538  -1525   6409       C  
ATOM   5808  O   ASP B 388     -34.497 -52.881  18.599  1.00174.72           O  
ANISOU 5808  O   ASP B 388    17283  18947  30156    672  -1447   5959       O  
ATOM   5809  CB  ASP B 388     -37.906 -53.349  18.624  1.00172.83           C  
ANISOU 5809  CB  ASP B 388    17438  18745  29487    138  -1245   6460       C  
ATOM   5810  CG  ASP B 388     -37.818 -51.869  18.325  1.00168.22           C  
ANISOU 5810  CG  ASP B 388    16936  18605  28374    137  -1046   5985       C  
ATOM   5811  OD1 ASP B 388     -37.786 -51.510  17.131  1.00165.44           O  
ANISOU 5811  OD1 ASP B 388    16677  18067  28117    143   -844   5459       O  
ATOM   5812  OD2 ASP B 388     -37.809 -51.065  19.281  1.00167.69           O  
ANISOU 5812  OD2 ASP B 388    16861  19067  27787    135  -1099   6141       O  
ATOM   5813  N   GLY B 389     -35.583 -53.320  20.521  1.00178.11           N  
ANISOU 5813  N   GLY B 389    17758  19781  30134    525  -1716   6922       N  
ATOM   5814  CA  GLY B 389     -34.578 -52.641  21.324  1.00178.78           C  
ANISOU 5814  CA  GLY B 389    17704  20274  29950    674  -1879   6926       C  
ATOM   5815  C   GLY B 389     -33.213 -53.327  21.347  1.00182.38           C  
ANISOU 5815  C   GLY B 389    17928  20424  30944    927  -2099   6944       C  
ATOM   5816  O   GLY B 389     -32.164 -52.664  21.378  1.00182.01           O  
ANISOU 5816  O   GLY B 389    17723  20578  30855   1052  -2147   6654       O  
ATOM   5817  N   ILE B 390     -33.227 -54.658  21.360  1.00186.30           N  
ANISOU 5817  N   ILE B 390    18392  20429  31965   1004  -2250   7297       N  
ATOM   5818  CA  ILE B 390     -32.002 -55.445  21.258  1.00190.14           C  
ANISOU 5818  CA  ILE B 390    18665  20541  33038   1285  -2457   7294       C  
ATOM   5819  C   ILE B 390     -31.235 -55.053  20.006  1.00187.79           C  
ANISOU 5819  C   ILE B 390    18268  20062  33022   1391  -2242   6601       C  
ATOM   5820  O   ILE B 390     -30.056 -54.725  20.075  1.00188.80           O  
ANISOU 5820  O   ILE B 390    18160  20325  33252   1576  -2324   6401       O  
ATOM   5821  CB  ILE B 390     -32.295 -56.958  21.237  1.00194.60           C  
ANISOU 5821  CB  ILE B 390    19273  20488  34180   1337  -2622   7710       C  
ATOM   5822  CG1 ILE B 390     -32.530 -57.464  22.659  1.00198.86           C  
ANISOU 5822  CG1 ILE B 390    19816  21209  34532   1332  -2914   8488       C  
ATOM   5823  CG2 ILE B 390     -31.139 -57.724  20.626  1.00197.68           C  
ANISOU 5823  CG2 ILE B 390    19480  20372  35259   1650  -2738   7474       C  
ATOM   5824  CD1 ILE B 390     -32.901 -58.925  22.730  1.00203.74           C  
ANISOU 5824  CD1 ILE B 390    20502  21204  35705   1335  -3088   8981       C  
ATOM   5825  N   ASN B 391     -31.918 -55.053  18.866  1.00184.91           N  
ANISOU 5825  N   ASN B 391    18073  19428  32757   1267  -1963   6239       N  
ATOM   5826  CA  ASN B 391     -31.293 -54.650  17.614  1.00182.79           C  
ANISOU 5826  CA  ASN B 391    17743  19024  32686   1360  -1711   5590       C  
ATOM   5827  C   ASN B 391     -30.969 -53.169  17.570  1.00179.00           C  
ANISOU 5827  C   ASN B 391    17231  19074  31706   1264  -1534   5246       C  
ATOM   5828  O   ASN B 391     -30.164 -52.746  16.757  1.00178.16           O  
ANISOU 5828  O   ASN B 391    16999  18948  31746   1355  -1357   4787       O  
ATOM   5829  CB  ASN B 391     -32.175 -55.017  16.426  1.00181.00           C  
ANISOU 5829  CB  ASN B 391    17737  18402  32632   1260  -1480   5297       C  
ATOM   5830  CG  ASN B 391     -32.262 -56.505  16.216  1.00185.32           C  
ANISOU 5830  CG  ASN B 391    18295  18309  33810   1388  -1657   5492       C  
ATOM   5831  OD1 ASN B 391     -31.387 -57.255  16.650  1.00189.65           O  
ANISOU 5831  OD1 ASN B 391    18657  18639  34765   1630  -1902   5706       O  
ATOM   5832  ND2 ASN B 391     -33.318 -56.946  15.544  1.00184.54           N  
ANISOU 5832  ND2 ASN B 391    18415  17885  33817   1235  -1561   5411       N  
ATOM   5833  N   SER B 392     -31.616 -52.371  18.411  1.00176.99           N  
ANISOU 5833  N   SER B 392    17098  19287  30865   1080  -1569   5458       N  
ATOM   5834  CA  SER B 392     -31.216 -50.974  18.541  1.00174.26           C  
ANISOU 5834  CA  SER B 392    16720  19418  30072   1005  -1479   5166       C  
ATOM   5835  C   SER B 392     -29.829 -50.913  19.177  1.00177.47           C  
ANISOU 5835  C   SER B 392    16804  19979  30649   1188  -1723   5214       C  
ATOM   5836  O   SER B 392     -28.959 -50.161  18.720  1.00176.64           O  
ANISOU 5836  O   SER B 392    16540  19995  30580   1203  -1612   4818       O  
ATOM   5837  CB  SER B 392     -32.232 -50.177  19.353  1.00172.01           C  
ANISOU 5837  CB  SER B 392    16645  19592  29119    813  -1494   5367       C  
ATOM   5838  OG  SER B 392     -33.453 -50.059  18.641  1.00168.83           O  
ANISOU 5838  OG  SER B 392    16503  19093  28553    646  -1244   5234       O  
ATOM   5839  N   VAL B 393     -29.625 -51.710  20.227  1.00181.51           N  
ANISOU 5839  N   VAL B 393    17207  20488  31271   1321  -2060   5715       N  
ATOM   5840  CA  VAL B 393     -28.303 -51.807  20.850  1.00185.30           C  
ANISOU 5840  CA  VAL B 393    17356  21088  31961   1535  -2345   5789       C  
ATOM   5841  C   VAL B 393     -27.276 -52.363  19.867  1.00187.13           C  
ANISOU 5841  C   VAL B 393    17333  20927  32843   1744  -2256   5460       C  
ATOM   5842  O   VAL B 393     -26.200 -51.801  19.699  1.00187.78           O  
ANISOU 5842  O   VAL B 393    17137  21181  33029   1816  -2249   5159       O  
ATOM   5843  CB  VAL B 393     -28.320 -52.706  22.104  1.00189.89           C  
ANISOU 5843  CB  VAL B 393    17896  21689  32563   1676  -2735   6434       C  
ATOM   5844  CG1 VAL B 393     -26.906 -52.973  22.581  1.00194.31           C  
ANISOU 5844  CG1 VAL B 393    18093  22291  33446   1949  -3045   6479       C  
ATOM   5845  CG2 VAL B 393     -29.140 -52.069  23.208  1.00188.93           C  
ANISOU 5845  CG2 VAL B 393    17968  22078  31738   1517  -2836   6754       C  
ATOM   5846  N   VAL B 394     -27.633 -53.465  19.214  1.00188.31           N  
ANISOU 5846  N   VAL B 394    17570  20552  33427   1840  -2187   5508       N  
ATOM   5847  CA  VAL B 394     -26.775 -54.130  18.239  1.00190.54           C  
ANISOU 5847  CA  VAL B 394    17645  20425  34328   2087  -2095   5186       C  
ATOM   5848  C   VAL B 394     -26.361 -53.186  17.118  1.00187.42           C  
ANISOU 5848  C   VAL B 394    17180  20158  33872   2016  -1717   4573       C  
ATOM   5849  O   VAL B 394     -25.190 -53.114  16.758  1.00189.52           O  
ANISOU 5849  O   VAL B 394    17115  20450  34445   2197  -1680   4308       O  
ATOM   5850  CB  VAL B 394     -27.473 -55.363  17.633  1.00191.86           C  
ANISOU 5850  CB  VAL B 394    18010  19987  34902   2157  -2065   5274       C  
ATOM   5851  CG1 VAL B 394     -26.654 -55.936  16.485  1.00193.93           C  
ANISOU 5851  CG1 VAL B 394    18095  19851  35737   2434  -1920   4831       C  
ATOM   5852  CG2 VAL B 394     -27.710 -56.417  18.705  1.00196.12           C  
ANISOU 5852  CG2 VAL B 394    18581  20324  35612   2247  -2450   5921       C  
ATOM   5853  N   ALA B 395     -27.331 -52.463  16.575  1.00182.75           N  
ANISOU 5853  N   ALA B 395    16892  19663  32883   1755  -1434   4373       N  
ATOM   5854  CA  ALA B 395     -27.082 -51.495  15.522  1.00179.73           C  
ANISOU 5854  CA  ALA B 395    16510  19411  32368   1654  -1062   3846       C  
ATOM   5855  C   ALA B 395     -26.184 -50.390  16.050  1.00179.74           C  
ANISOU 5855  C   ALA B 395    16266  19873  32152   1578  -1118   3757       C  
ATOM   5856  O   ALA B 395     -25.306 -49.916  15.334  1.00180.10           O  
ANISOU 5856  O   ALA B 395    16089  19982  32357   1607   -906   3391       O  
ATOM   5857  CB  ALA B 395     -28.376 -50.927  14.994  1.00175.06           C  
ANISOU 5857  CB  ALA B 395    16316  18850  31350   1401   -813   3716       C  
ATOM   5858  N   ALA B 396     -26.417 -49.964  17.289  1.00179.66           N  
ANISOU 5858  N   ALA B 396    16296  20198  31768   1472  -1399   4084       N  
ATOM   5859  CA  ALA B 396     -25.553 -48.962  17.904  1.00180.35           C  
ANISOU 5859  CA  ALA B 396    16149  20706  31669   1403  -1533   4001       C  
ATOM   5860  C   ALA B 396     -24.095 -49.447  17.960  1.00185.07           C  
ANISOU 5860  C   ALA B 396    16262  21261  32794   1653  -1691   3956       C  
ATOM   5861  O   ALA B 396     -23.165 -48.700  17.658  1.00185.67           O  
ANISOU 5861  O   ALA B 396    16062  21531  32954   1601  -1594   3655       O  
ATOM   5862  CB  ALA B 396     -26.058 -48.613  19.295  1.00180.37           C  
ANISOU 5862  CB  ALA B 396    16284  21062  31188   1317  -1861   4374       C  
ATOM   5863  N   LEU B 397     -23.905 -50.706  18.336  1.00188.77           N  
ANISOU 5863  N   LEU B 397    16620  21466  33639   1923  -1938   4265       N  
ATOM   5864  CA  LEU B 397     -22.580 -51.310  18.334  1.00193.67           C  
ANISOU 5864  CA  LEU B 397    16780  22002  34804   2222  -2095   4224       C  
ATOM   5865  C   LEU B 397     -22.036 -51.391  16.913  1.00193.69           C  
ANISOU 5865  C   LEU B 397    16619  21784  35191   2314  -1697   3749       C  
ATOM   5866  O   LEU B 397     -20.850 -51.215  16.680  1.00196.50           O  
ANISOU 5866  O   LEU B 397    16545  22268  35848   2437  -1668   3528       O  
ATOM   5867  CB  LEU B 397     -22.620 -52.703  18.966  1.00197.77           C  
ANISOU 5867  CB  LEU B 397    17285  22208  35650   2511  -2439   4672       C  
ATOM   5868  CG  LEU B 397     -23.155 -52.777  20.397  1.00198.65           C  
ANISOU 5868  CG  LEU B 397    17559  22543  35377   2458  -2829   5216       C  
ATOM   5869  CD1 LEU B 397     -23.151 -54.212  20.907  1.00203.29           C  
ANISOU 5869  CD1 LEU B 397    18138  22756  36347   2745  -3143   5686       C  
ATOM   5870  CD2 LEU B 397     -22.371 -51.861  21.326  1.00199.98           C  
ANISOU 5870  CD2 LEU B 397    17470  23243  35270   2415  -3093   5221       C  
ATOM   5871  N   ALA B 398     -22.927 -51.637  15.962  1.00190.81           N  
ANISOU 5871  N   ALA B 398    16589  21118  34791   2254  -1386   3587       N  
ATOM   5872  CA  ALA B 398     -22.573 -51.687  14.549  1.00190.67           C  
ANISOU 5872  CA  ALA B 398    16493  20915  35038   2345   -974   3123       C  
ATOM   5873  C   ALA B 398     -22.572 -50.297  13.924  1.00187.07           C  
ANISOU 5873  C   ALA B 398    16093  20776  34211   2044   -614   2781       C  
ATOM   5874  O   ALA B 398     -22.700 -50.160  12.709  1.00185.67           O  
ANISOU 5874  O   ALA B 398    16018  20477  34052   2034   -216   2430       O  
ATOM   5875  CB  ALA B 398     -23.522 -52.597  13.803  1.00189.73           C  
ANISOU 5875  CB  ALA B 398    16721  20325  35045   2431   -843   3082       C  
ATOM   5876  N   THR B 399     -22.465 -49.279  14.775  1.00185.89           N  
ANISOU 5876  N   THR B 399    15905  21018  33708   1806   -773   2894       N  
ATOM   5877  CA  THR B 399     -22.379 -47.867  14.381  1.00183.14           C  
ANISOU 5877  CA  THR B 399    15598  20965  33023   1497   -510   2620       C  
ATOM   5878  C   THR B 399     -23.670 -47.298  13.781  1.00178.02           C  
ANISOU 5878  C   THR B 399    15469  20255  31915   1266   -234   2508       C  
ATOM   5879  O   THR B 399     -23.626 -46.292  13.066  1.00176.01           O  
ANISOU 5879  O   THR B 399    15291  20125  31458   1062     79   2227       O  
ATOM   5880  CB  THR B 399     -21.227 -47.608  13.366  1.00185.48           C  
ANISOU 5880  CB  THR B 399    15506  21308  33660   1553   -174   2251       C  
ATOM   5881  OG1 THR B 399     -21.522 -48.246  12.116  1.00185.09           O  
ANISOU 5881  OG1 THR B 399    15598  20948  33779   1718    183   2017       O  
ATOM   5882  CG2 THR B 399     -19.892 -48.108  13.911  1.00190.92           C  
ANISOU 5882  CG2 THR B 399    15618  22098  34824   1793   -437   2325       C  
ATOM   5883  N   MET B 400     -24.811 -47.925  14.076  1.00176.28           N  
ANISOU 5883  N   MET B 400    15592  19849  31539   1292   -357   2743       N  
ATOM   5884  CA  MET B 400     -26.099 -47.443  13.571  1.00171.74           C  
ANISOU 5884  CA  MET B 400    15485  19235  30536   1094   -136   2653       C  
ATOM   5885  C   MET B 400     -26.979 -46.849  14.658  1.00169.42           C  
ANISOU 5885  C   MET B 400    15442  19198  29733    904   -369   2924       C  
ATOM   5886  O   MET B 400     -26.951 -47.267  15.812  1.00171.34           O  
ANISOU 5886  O   MET B 400    15595  19541  29965    972   -725   3280       O  
ATOM   5887  CB  MET B 400     -26.888 -48.552  12.865  1.00171.47           C  
ANISOU 5887  CB  MET B 400    15668  18789  30695   1239    -36   2646       C  
ATOM   5888  CG  MET B 400     -26.378 -48.989  11.504  1.00172.85           C  
ANISOU 5888  CG  MET B 400    15747  18707  31221   1419    287   2268       C  
ATOM   5889  SD  MET B 400     -26.363 -47.621  10.333  1.00169.80           S  
ANISOU 5889  SD  MET B 400    15509  18528  30480   1209    765   1838       S  
ATOM   5890  CE  MET B 400     -28.019 -47.022  10.469  1.00164.76           C  
ANISOU 5890  CE  MET B 400    15405  17939  29256    956    763   1928       C  
ATOM   5891  N   THR B 401     -27.775 -45.871  14.247  1.00167.44           N  
ANISOU 5891  N   THR B 401    15516  19062  29040    689   -155   2747       N  
ATOM   5892  CA  THR B 401     -28.702 -45.174  15.122  1.00165.07           C  
ANISOU 5892  CA  THR B 401    15486  19028  28204    526   -314   2923       C  
ATOM   5893  C   THR B 401     -29.930 -46.072  15.345  1.00164.21           C  
ANISOU 5893  C   THR B 401    15613  18763  28016    572   -388   3205       C  
ATOM   5894  O   THR B 401     -30.094 -47.068  14.635  1.00164.96           O  
ANISOU 5894  O   THR B 401    15712  18503  28461    690   -286   3183       O  
ATOM   5895  CB  THR B 401     -29.110 -43.822  14.509  1.00164.73           C  
ANISOU 5895  CB  THR B 401    15710  19122  27757    311    -53   2612       C  
ATOM   5896  OG1 THR B 401     -30.110 -44.017  13.498  1.00162.05           O  
ANISOU 5896  OG1 THR B 401    15680  18569  27322    300    222   2472       O  
ATOM   5897  CG2 THR B 401     -27.878 -43.118  13.934  1.00166.09           C  
ANISOU 5897  CG2 THR B 401    15635  19337  28136    244    114   2321       C  
ATOM   5898  N   PRO B 402     -30.778 -45.747  16.343  1.00166.71           N  
ANISOU 5898  N   PRO B 402    16109  19347  27886    483   -573   3469       N  
ATOM   5899  CA  PRO B 402     -31.981 -46.547  16.611  1.00166.31           C  
ANISOU 5899  CA  PRO B 402    16246  19195  27748    486   -629   3777       C  
ATOM   5900  C   PRO B 402     -32.829 -46.866  15.383  1.00164.06           C  
ANISOU 5900  C   PRO B 402    16183  18601  27552    447   -346   3561       C  
ATOM   5901  O   PRO B 402     -32.994 -46.029  14.488  1.00161.34           O  
ANISOU 5901  O   PRO B 402    16002  18276  27022    364    -84   3190       O  
ATOM   5902  CB  PRO B 402     -32.771 -45.664  17.577  1.00164.41           C  
ANISOU 5902  CB  PRO B 402    16194  19389  26884    368   -741   3926       C  
ATOM   5903  CG  PRO B 402     -31.727 -44.967  18.337  1.00166.06           C  
ANISOU 5903  CG  PRO B 402    16214  19881  27002    388   -944   3893       C  
ATOM   5904  CD  PRO B 402     -30.598 -44.703  17.370  1.00166.33           C  
ANISOU 5904  CD  PRO B 402    16060  19722  27416    394   -772   3517       C  
ATOM   5905  N   MET B 403     -33.348 -48.090  15.358  1.00164.48           N  
ANISOU 5905  N   MET B 403    16243  18354  27896    507   -422   3804       N  
ATOM   5906  CA  MET B 403     -34.121 -48.588  14.233  1.00163.22           C  
ANISOU 5906  CA  MET B 403    16267  17857  27894    488   -220   3605       C  
ATOM   5907  C   MET B 403     -35.396 -49.260  14.717  1.00163.53           C  
ANISOU 5907  C   MET B 403    16436  17846  27852    390   -338   3971       C  
ATOM   5908  O   MET B 403     -35.439 -49.810  15.816  1.00166.02           O  
ANISOU 5908  O   MET B 403    16644  18237  28199    398   -583   4435       O  
ATOM   5909  CB  MET B 403     -33.298 -49.571  13.405  1.00162.97           C  
ANISOU 5909  CB  MET B 403    16073  17378  28469    679   -178   3429       C  
ATOM   5910  CG  MET B 403     -32.792 -50.764  14.187  1.00167.27           C  
ANISOU 5910  CG  MET B 403    16396  17704  29453    827   -477   3822       C  
ATOM   5911  SD  MET B 403     -31.593 -51.682  13.220  1.00170.66           S  
ANISOU 5911  SD  MET B 403    16602  17676  30565   1118   -418   3521       S  
ATOM   5912  CE  MET B 403     -32.627 -52.208  11.854  1.00169.36           C  
ANISOU 5912  CE  MET B 403    16729  17102  30519   1092   -205   3197       C  
ATOM   5913  N   THR B 404     -36.423 -49.226  13.876  1.00163.59           N  
ANISOU 5913  N   THR B 404    16662  17733  27760    295   -164   3771       N  
ATOM   5914  CA  THR B 404     -37.731 -49.780  14.198  1.00163.88           C  
ANISOU 5914  CA  THR B 404    16802  17740  27723    162   -239   4074       C  
ATOM   5915  C   THR B 404     -38.421 -50.376  12.966  1.00163.52           C  
ANISOU 5915  C   THR B 404    16896  17292  27942    136   -116   3799       C  
ATOM   5916  O   THR B 404     -37.824 -50.476  11.884  1.00163.42           O  
ANISOU 5916  O   THR B 404    16905  17005  28181    260     20   3387       O  
ATOM   5917  CB  THR B 404     -38.654 -48.713  14.831  1.00165.16           C  
ANISOU 5917  CB  THR B 404    17100  18421  27231     24   -197   4167       C  
ATOM   5918  OG1 THR B 404     -39.895 -49.320  15.218  1.00166.12           O  
ANISOU 5918  OG1 THR B 404    17256  18555  27308   -111   -263   4512       O  
ATOM   5919  CG2 THR B 404     -38.931 -47.586  13.848  1.00161.37           C  
ANISOU 5919  CG2 THR B 404    16832  18057  26424     -1     54   3666       C  
ATOM   5920  N   THR B 405     -39.669 -50.800  13.166  1.00165.19           N  
ANISOU 5920  N   THR B 405    17182  17488  28096    -22   -173   4036       N  
ATOM   5921  CA  THR B 405     -40.418 -51.585  12.189  1.00165.92           C  
ANISOU 5921  CA  THR B 405    17373  17164  28506    -74   -149   3858       C  
ATOM   5922  C   THR B 405     -40.893 -50.797  10.972  1.00162.60           C  
ANISOU 5922  C   THR B 405    17167  16802  27811    -73     84   3319       C  
ATOM   5923  O   THR B 405     -41.554 -49.768  11.109  1.00159.70           O  
ANISOU 5923  O   THR B 405    16914  16845  26921   -158    189   3266       O  
ATOM   5924  CB  THR B 405     -41.649 -52.215  12.841  1.00162.86           C  
ANISOU 5924  CB  THR B 405    16958  16788  28135   -287   -286   4310       C  
ATOM   5925  OG1 THR B 405     -41.283 -52.783  14.104  1.00165.98           O  
ANISOU 5925  OG1 THR B 405    17179  17228  28656   -297   -488   4882       O  
ATOM   5926  CG2 THR B 405     -42.239 -53.278  11.933  1.00164.94           C  
ANISOU 5926  CG2 THR B 405    17273  16509  28886   -348   -346   4168       C  
ATOM   5927  N   PHE B 406     -40.596 -51.315   9.784  1.00161.11           N  
ANISOU 5927  N   PHE B 406    17045  16200  27969     45    150   2924       N  
ATOM   5928  CA  PHE B 406     -41.030 -50.691   8.538  1.00158.63           C  
ANISOU 5928  CA  PHE B 406    16954  15908  27409     73    358   2416       C  
ATOM   5929  C   PHE B 406     -42.420 -51.178   8.137  1.00159.05           C  
ANISOU 5929  C   PHE B 406    17110  15820  27500    -73    278   2396       C  
ATOM   5930  O   PHE B 406     -42.715 -52.369   8.226  1.00162.29           O  
ANISOU 5930  O   PHE B 406    17438  15844  28381   -133     85   2576       O  
ATOM   5931  CB  PHE B 406     -40.026 -50.958   7.419  1.00161.98           C  
ANISOU 5931  CB  PHE B 406    17404  16021  28120    299    489   1971       C  
ATOM   5932  CG  PHE B 406     -38.990 -49.878   7.269  1.00160.09           C  
ANISOU 5932  CG  PHE B 406    17154  16068  27605    401    708   1774       C  
ATOM   5933  CD1 PHE B 406     -38.428 -49.286   8.387  1.00159.46           C  
ANISOU 5933  CD1 PHE B 406    16924  16308  27354    351    655   2079       C  
ATOM   5934  CD2 PHE B 406     -38.585 -49.447   6.017  1.00159.37           C  
ANISOU 5934  CD2 PHE B 406    17200  15935  27418    536    960   1294       C  
ATOM   5935  CE1 PHE B 406     -37.473 -48.294   8.266  1.00158.19           C  
ANISOU 5935  CE1 PHE B 406    16733  16384  26986    405    831   1901       C  
ATOM   5936  CE2 PHE B 406     -37.628 -48.451   5.884  1.00158.14           C  
ANISOU 5936  CE2 PHE B 406    17013  16033  27039    588   1174   1154       C  
ATOM   5937  CZ  PHE B 406     -37.070 -47.872   7.011  1.00157.55           C  
ANISOU 5937  CZ  PHE B 406    16772  16242  26848    507   1100   1454       C  
ATOM   5938  N   ALA B 407     -43.280 -50.249   7.734  1.00156.76           N  
ANISOU 5938  N   ALA B 407    16992  15837  26732   -138    404   2195       N  
ATOM   5939  CA  ALA B 407     -44.675 -50.563   7.485  1.00157.13           C  
ANISOU 5939  CA  ALA B 407    17091  15855  26756   -295    317   2206       C  
ATOM   5940  C   ALA B 407     -45.013 -50.667   6.000  1.00157.04           C  
ANISOU 5940  C   ALA B 407    17282  15595  26791   -202    381   1662       C  
ATOM   5941  O   ALA B 407     -46.141 -51.000   5.647  1.00157.80           O  
ANISOU 5941  O   ALA B 407    17413  15622  26922   -323    278   1603       O  
ATOM   5942  CB  ALA B 407     -45.556 -49.522   8.150  1.00158.52           C  
ANISOU 5942  CB  ALA B 407    17291  16579  26360   -410    372   2383       C  
ATOM   5943  N   GLN B 408     -44.048 -50.377   5.132  1.00155.82           N  
ANISOU 5943  N   GLN B 408    17248  15335  26623     12    550   1267       N  
ATOM   5944  CA  GLN B 408     -44.269 -50.536   3.698  1.00156.35           C  
ANISOU 5944  CA  GLN B 408    17520  15174  26711    142    614    743       C  
ATOM   5945  C   GLN B 408     -44.595 -51.982   3.363  1.00160.32           C  
ANISOU 5945  C   GLN B 408    17963  15152  27799    119    376    691       C  
ATOM   5946  O   GLN B 408     -45.461 -52.245   2.534  1.00161.15           O  
ANISOU 5946  O   GLN B 408    18199  15119  27912     98    296    399       O  
ATOM   5947  CB  GLN B 408     -43.065 -50.090   2.863  1.00157.93           C  
ANISOU 5947  CB  GLN B 408    17825  15356  26825    387    862    372       C  
ATOM   5948  CG  GLN B 408     -42.558 -48.675   3.094  1.00154.66           C  
ANISOU 5948  CG  GLN B 408    17476  15380  25909    401   1097    395       C  
ATOM   5949  CD  GLN B 408     -41.496 -48.593   4.176  1.00154.86           C  
ANISOU 5949  CD  GLN B 408    17265  15499  26075    385   1091    733       C  
ATOM   5950  OE1 GLN B 408     -41.645 -49.156   5.258  1.00155.93           O  
ANISOU 5950  OE1 GLN B 408    17209  15606  26431    271    885   1140       O  
ATOM   5951  NE2 GLN B 408     -40.408 -47.891   3.880  1.00154.20           N  
ANISOU 5951  NE2 GLN B 408    17185  15540  25865    496   1314    574       N  
ATOM   5952  N   ASN B 409     -43.858 -52.914   3.967  1.00160.99           N  
ANISOU 5952  N   ASN B 409    17861  14923  28384    141    245    950       N  
ATOM   5953  CA  ASN B 409     -43.966 -54.335   3.620  1.00165.42           C  
ANISOU 5953  CA  ASN B 409    18386  14891  29574    157      4    877       C  
ATOM   5954  C   ASN B 409     -45.383 -54.904   3.717  1.00167.00           C  
ANISOU 5954  C   ASN B 409    18569  14951  29931   -116   -232   1022       C  
ATOM   5955  O   ASN B 409     -45.767 -55.733   2.906  1.00169.96           O  
ANISOU 5955  O   ASN B 409    19026  14895  30657    -97   -397    713       O  
ATOM   5956  CB  ASN B 409     -43.014 -55.183   4.485  1.00167.24           C  
ANISOU 5956  CB  ASN B 409    18406  14833  30303    209   -130   1246       C  
ATOM   5957  CG  ASN B 409     -43.523 -55.404   5.908  1.00167.77           C  
ANISOU 5957  CG  ASN B 409    18286  15027  30434    -64   -298   1926       C  
ATOM   5958  OD1 ASN B 409     -44.337 -54.639   6.423  1.00165.14           O  
ANISOU 5958  OD1 ASN B 409    17944  15142  29661   -258   -239   2144       O  
ATOM   5959  ND2 ASN B 409     -43.047 -56.474   6.542  1.00171.63           N  
ANISOU 5959  ND2 ASN B 409    18626  15120  31465    -57   -509   2268       N  
ATOM   5960  N   ASN B 410     -46.153 -54.466   4.710  1.00164.59           N  
ANISOU 5960  N   ASN B 410    18144  15020  29373   -368   -253   1479       N  
ATOM   5961  CA  ASN B 410     -47.486 -55.015   4.921  1.00166.58           C  
ANISOU 5961  CA  ASN B 410    18308  15187  29797   -660   -460   1691       C  
ATOM   5962  C   ASN B 410     -48.352 -54.813   3.690  1.00166.17           C  
ANISOU 5962  C   ASN B 410    18434  15118  29586   -641   -475   1158       C  
ATOM   5963  O   ASN B 410     -49.186 -55.656   3.356  1.00169.41           O  
ANISOU 5963  O   ASN B 410    18805  15193  30368   -808   -710   1100       O  
ATOM   5964  CB  ASN B 410     -48.142 -54.375   6.141  1.00163.06           C  
ANISOU 5964  CB  ASN B 410    17700  15278  28978   -881   -410   2227       C  
ATOM   5965  CG  ASN B 410     -47.449 -54.747   7.436  1.00164.46           C  
ANISOU 5965  CG  ASN B 410    17692  15458  29338   -927   -459   2811       C  
ATOM   5966  OD1 ASN B 410     -46.804 -55.791   7.533  1.00167.90           O  
ANISOU 5966  OD1 ASN B 410    18071  15396  30329   -886   -615   2931       O  
ATOM   5967  ND2 ASN B 410     -47.579 -53.889   8.441  1.00162.13           N  
ANISOU 5967  ND2 ASN B 410    17311  15726  28564   -987   -343   3164       N  
ATOM   5968  N   VAL B 411     -48.100 -53.714   2.985  1.00165.23           N  
ANISOU 5968  N   VAL B 411    18516  15332  28932   -432   -240    764       N  
ATOM   5969  CA  VAL B 411     -48.771 -53.431   1.724  1.00164.88           C  
ANISOU 5969  CA  VAL B 411    18684  15299  28664   -344   -240    221       C  
ATOM   5970  C   VAL B 411     -48.383 -54.502   0.722  1.00168.70           C  
ANISOU 5970  C   VAL B 411    19274  15193  29632   -189   -388   -210       C  
ATOM   5971  O   VAL B 411     -49.239 -55.159   0.128  1.00171.48           O  
ANISOU 5971  O   VAL B 411    19655  15270  30229   -283   -623   -439       O  
ATOM   5972  CB  VAL B 411     -48.401 -52.046   1.166  1.00166.11           C  
ANISOU 5972  CB  VAL B 411    19066  15890  28158   -124     60    -77       C  
ATOM   5973  CG1 VAL B 411     -48.815 -51.928  -0.295  1.00166.66           C  
ANISOU 5973  CG1 VAL B 411    19397  15882  28044     46     56   -681       C  
ATOM   5974  CG2 VAL B 411     -49.029 -50.938   2.008  1.00162.72           C  
ANISOU 5974  CG2 VAL B 411    18579  16029  27220   -257    159    248       C  
ATOM   5975  N   VAL B 412     -47.079 -54.655   0.534  1.00164.04           N  
ANISOU 5975  N   VAL B 412    18729  14424  29173     62   -256   -341       N  
ATOM   5976  CA  VAL B 412     -46.523 -55.621  -0.401  1.00167.87           C  
ANISOU 5976  CA  VAL B 412    19320  14379  30085    290   -359   -785       C  
ATOM   5977  C   VAL B 412     -47.120 -57.010  -0.160  1.00172.65           C  
ANISOU 5977  C   VAL B 412    19805  14415  31379     89   -743   -644       C  
ATOM   5978  O   VAL B 412     -47.655 -57.622  -1.073  1.00175.64           O  
ANISOU 5978  O   VAL B 412    20308  14456  31969    121   -944  -1070       O  
ATOM   5979  CB  VAL B 412     -44.991 -55.682  -0.285  1.00168.83           C  
ANISOU 5979  CB  VAL B 412    19398  14416  30334    558   -174   -792       C  
ATOM   5980  CG1 VAL B 412     -44.428 -56.642  -1.315  1.00173.12           C  
ANISOU 5980  CG1 VAL B 412    20055  14449  31275    851   -260  -1307       C  
ATOM   5981  CG2 VAL B 412     -44.398 -54.298  -0.481  1.00164.56           C  
ANISOU 5981  CG2 VAL B 412    18952  14419  29156    700    201   -889       C  
ATOM   5982  N   ILE B 413     -47.035 -57.486   1.078  1.00173.61           N  
ANISOU 5982  N   ILE B 413    19692  14432  31839   -124   -855    -36       N  
ATOM   5983  CA  ILE B 413     -47.610 -58.758   1.485  1.00178.38           C  
ANISOU 5983  CA  ILE B 413    20163  14502  33110   -375  -1210    233       C  
ATOM   5984  C   ILE B 413     -49.078 -58.849   1.101  1.00179.39           C  
ANISOU 5984  C   ILE B 413    20293  14644  33223   -652  -1399    122       C  
ATOM   5985  O   ILE B 413     -49.505 -59.815   0.468  1.00183.78           O  
ANISOU 5985  O   ILE B 413    20901  14667  34261   -704  -1691   -163       O  
ATOM   5986  CB  ILE B 413     -47.531 -58.959   3.004  1.00178.65           C  
ANISOU 5986  CB  ILE B 413    19945  14618  33317   -617  -1250   1018       C  
ATOM   5987  CG1 ILE B 413     -46.113 -58.777   3.526  1.00177.58           C  
ANISOU 5987  CG1 ILE B 413    19765  14548  33159   -361  -1085   1181       C  
ATOM   5988  CG2 ILE B 413     -48.078 -60.317   3.384  1.00184.25           C  
ANISOU 5988  CG2 ILE B 413    20532  14723  34753   -887  -1611   1332       C  
ATOM   5989  CD1 ILE B 413     -46.061 -58.618   5.032  1.00176.83           C  
ANISOU 5989  CD1 ILE B 413    19450  14737  33000   -564  -1075   1929       C  
ATOM   5990  N   ALA B 414     -49.844 -57.835   1.502  1.00175.63           N  
ANISOU 5990  N   ALA B 414    19746  14780  32204   -821  -1250    335       N  
ATOM   5991  CA  ALA B 414     -51.291 -57.825   1.297  1.00176.53           C  
ANISOU 5991  CA  ALA B 414    19788  15011  32272  -1100  -1416    306       C  
ATOM   5992  C   ALA B 414     -51.685 -57.906  -0.173  1.00177.80           C  
ANISOU 5992  C   ALA B 414    20181  14990  32385   -936  -1537   -431       C  
ATOM   5993  O   ALA B 414     -52.675 -58.549  -0.523  1.00181.29           O  
ANISOU 5993  O   ALA B 414    20559  15172  33150  -1155  -1832   -555       O  
ATOM   5994  CB  ALA B 414     -51.895 -56.574   1.924  1.00172.06           C  
ANISOU 5994  CB  ALA B 414    19129  15196  31050  -1205  -1192    594       C  
ATOM   5995  N   LEU B 415     -50.888 -57.279  -1.028  1.00175.44           N  
ANISOU 5995  N   LEU B 415    20142  14826  31689   -553  -1316   -912       N  
ATOM   5996  CA  LEU B 415     -51.175 -57.229  -2.457  1.00176.54           C  
ANISOU 5996  CA  LEU B 415    20542  14880  31656   -336  -1389  -1624       C  
ATOM   5997  C   LEU B 415     -50.543 -58.381  -3.228  1.00181.35           C  
ANISOU 5997  C   LEU B 415    21285  14819  32800   -125  -1586  -2064       C  
ATOM   5998  O   LEU B 415     -50.866 -58.608  -4.392  1.00183.66           O  
ANISOU 5998  O   LEU B 415    21782  14942  33057     36  -1734  -2669       O  
ATOM   5999  CB  LEU B 415     -50.712 -55.895  -3.031  1.00179.69           C  
ANISOU 5999  CB  LEU B 415    21170  15813  31290    -32  -1027  -1898       C  
ATOM   6000  CG  LEU B 415     -51.435 -54.681  -2.442  1.00175.29           C  
ANISOU 6000  CG  LEU B 415    20538  15901  30164   -186   -866  -1578       C  
ATOM   6001  CD1 LEU B 415     -51.030 -53.409  -3.172  1.00171.58           C  
ANISOU 6001  CD1 LEU B 415    20348  15864  28980    116   -552  -1899       C  
ATOM   6002  CD2 LEU B 415     -52.944 -54.881  -2.492  1.00177.00           C  
ANISOU 6002  CD2 LEU B 415    20625  16176  30452   -461  -1145  -1568       C  
ATOM   6003  N   THR B 416     -49.622 -59.082  -2.578  1.00183.08           N  
ANISOU 6003  N   THR B 416    21398  14675  33487    -93  -1596  -1776       N  
ATOM   6004  CA  THR B 416     -48.926 -60.221  -3.173  1.00188.03           C  
ANISOU 6004  CA  THR B 416    22134  14636  34673    142  -1786  -2155       C  
ATOM   6005  C   THR B 416     -49.372 -61.550  -2.566  1.00193.26           C  
ANISOU 6005  C   THR B 416    22624  14647  36159   -169  -2194  -1835       C  
ATOM   6006  O   THR B 416     -48.980 -62.621  -3.038  1.00198.29           O  
ANISOU 6006  O   THR B 416    23356  14632  37353    -12  -2439  -2152       O  
ATOM   6007  CB  THR B 416     -47.408 -60.081  -3.013  1.00186.93           C  
ANISOU 6007  CB  THR B 416    22014  14517  34493    487  -1504  -2133       C  
ATOM   6008  OG1 THR B 416     -47.093 -59.926  -1.621  1.00184.93           O  
ANISOU 6008  OG1 THR B 416    21513  14425  34329    281  -1417  -1406       O  
ATOM   6009  CG2 THR B 416     -46.915 -58.862  -3.778  1.00182.84           C  
ANISOU 6009  CG2 THR B 416    21686  14562  33225    794  -1108  -2500       C  
ATOM   6010  N   ARG B 417     -50.188 -61.463  -1.519  1.00192.40           N  
ANISOU 6010  N   ARG B 417    22266  14721  36115   -602  -2258  -1200       N  
ATOM   6011  CA  ARG B 417     -50.709 -62.633  -0.824  1.00197.42           C  
ANISOU 6011  CA  ARG B 417    22709  14801  37501   -973  -2613   -767       C  
ATOM   6012  C   ARG B 417     -49.597 -63.582  -0.357  1.00200.81           C  
ANISOU 6012  C   ARG B 417    23129  14651  38518   -819  -2704   -558       C  
ATOM   6013  O   ARG B 417     -49.662 -64.785  -0.607  1.00206.71           O  
ANISOU 6013  O   ARG B 417    23917  14654  39969   -865  -3062   -692       O  
ATOM   6014  CB  ARG B 417     -51.700 -63.387  -1.723  1.00202.26           C  
ANISOU 6014  CB  ARG B 417    23391  14957  38500  -1127  -3008  -1232       C  
ATOM   6015  CG  ARG B 417     -52.932 -62.590  -2.155  1.00199.96           C  
ANISOU 6015  CG  ARG B 417    23065  15192  37719  -1309  -2998  -1415       C  
ATOM   6016  CD  ARG B 417     -53.901 -63.476  -2.948  1.00205.70           C  
ANISOU 6016  CD  ARG B 417    23815  15406  38936  -1502  -3459  -1840       C  
ATOM   6017  NE  ARG B 417     -55.205 -62.851  -3.170  1.00204.41           N  
ANISOU 6017  NE  ARG B 417    23527  15721  38419  -1750  -3511  -1900       N  
ATOM   6018  CZ  ARG B 417     -56.212 -63.425  -3.826  1.00208.98           C  
ANISOU 6018  CZ  ARG B 417    24072  16000  39332  -1962  -3909  -2253       C  
ATOM   6019  NH1 ARG B 417     -56.074 -64.643  -4.326  1.00215.21           N  
ANISOU 6019  NH1 ARG B 417    24968  15978  40825  -1967  -4300  -2592       N  
ATOM   6020  NH2 ARG B 417     -57.363 -62.782  -3.982  1.00207.68           N  
ANISOU 6020  NH2 ARG B 417    23758  16338  38812  -2160  -3939  -2286       N  
ATOM   6021  N   CYS B 418     -48.575 -63.041   0.305  1.00197.42           N  
ANISOU 6021  N   CYS B 418    22648  14546  37816   -625  -2405   -249       N  
ATOM   6022  CA  CYS B 418     -47.479 -63.857   0.831  1.00200.49           C  
ANISOU 6022  CA  CYS B 418    22998  14458  38721   -450  -2484     -9       C  
ATOM   6023  C   CYS B 418     -46.769 -63.200   2.008  1.00196.75           C  
ANISOU 6023  C   CYS B 418    22354  14464  37940   -440  -2214    601       C  
ATOM   6024  O   CYS B 418     -46.108 -62.176   1.847  1.00192.12           O  
ANISOU 6024  O   CYS B 418    21811  14409  36779   -190  -1878    427       O  
ATOM   6025  CB  CYS B 418     -46.453 -64.161  -0.259  1.00202.30           C  
ANISOU 6025  CB  CYS B 418    23446  14367  39051     66  -2456   -724       C  
ATOM   6026  SG  CYS B 418     -44.921 -64.897   0.383  1.00205.22           S  
ANISOU 6026  SG  CYS B 418    23736  14319  39919    390  -2473   -464       S  
ATOM   6027  N   ALA B 419     -46.890 -63.803   3.185  1.00199.21           N  
ANISOU 6027  N   ALA B 419    22477  14575  38641   -713  -2375   1319       N  
ATOM   6028  CA  ALA B 419     -46.206 -63.299   4.368  1.00196.57           C  
ANISOU 6028  CA  ALA B 419    21982  14655  38049   -693  -2179   1914       C  
ATOM   6029  C   ALA B 419     -45.117 -64.260   4.816  1.00200.79           C  
ANISOU 6029  C   ALA B 419    22484  14640  39167   -478  -2347   2136       C  
ATOM   6030  O   ALA B 419     -44.774 -64.302   5.996  1.00201.01           O  
ANISOU 6030  O   ALA B 419    22354  14800  39223   -564  -2345   2793       O  
ATOM   6031  CB  ALA B 419     -47.192 -63.063   5.497  1.00195.81           C  
ANISOU 6031  CB  ALA B 419    21683  14926  37790  -1148  -2183   2635       C  
ATOM   6032  N   ASN B 420     -44.568 -65.015   3.866  1.00204.40           N  
ANISOU 6032  N   ASN B 420    23097  14501  40063   -164  -2498   1570       N  
ATOM   6033  CA  ASN B 420     -43.520 -65.999   4.152  1.00209.12           C  
ANISOU 6033  CA  ASN B 420    23679  14508  41268    109  -2688   1688       C  
ATOM   6034  C   ASN B 420     -42.242 -65.380   4.680  1.00206.25           C  
ANISOU 6034  C   ASN B 420    23199  14570  40596    427  -2433   1839       C  
ATOM   6035  O   ASN B 420     -41.786 -64.351   4.184  1.00201.63           O  
ANISOU 6035  O   ASN B 420    22636  14534  39439    639  -2101   1455       O  
ATOM   6036  CB  ASN B 420     -43.182 -66.816   2.905  1.00213.48           C  
ANISOU 6036  CB  ASN B 420    24435  14403  42273    451  -2871    930       C  
ATOM   6037  CG  ASN B 420     -44.103 -67.991   2.715  1.00219.47           C  
ANISOU 6037  CG  ASN B 420    25278  14392  43717    171  -3304    945       C  
ATOM   6038  OD1 ASN B 420     -45.192 -67.858   2.164  1.00219.06           O  
ANISOU 6038  OD1 ASN B 420    25293  14384  43555    -99  -3372    702       O  
ATOM   6039  ND2 ASN B 420     -43.671 -69.157   3.179  1.00225.46           N  
ANISOU 6039  ND2 ASN B 420    26030  14421  45215    229  -3622   1237       N  
ATOM   6040  N   ARG B 421     -41.664 -66.021   5.688  1.00209.44           N  
ANISOU 6040  N   ARG B 421    23475  14706  41397    452  -2605   2412       N  
ATOM   6041  CA  ARG B 421     -40.430 -65.540   6.281  1.00207.58           C  
ANISOU 6041  CA  ARG B 421    23094  14836  40942    746  -2428   2592       C  
ATOM   6042  C   ARG B 421     -39.294 -65.558   5.258  1.00208.25           C  
ANISOU 6042  C   ARG B 421    23231  14796  41098   1276  -2302   1876       C  
ATOM   6043  O   ARG B 421     -38.281 -64.878   5.432  1.00205.73           O  
ANISOU 6043  O   ARG B 421    22779  14920  40469   1532  -2064   1833       O  
ATOM   6044  CB  ARG B 421     -40.063 -66.392   7.497  1.00212.02           C  
ANISOU 6044  CB  ARG B 421    23529  15046  41984    701  -2705   3332       C  
ATOM   6045  CG  ARG B 421     -39.660 -67.821   7.158  1.00219.23           C  
ANISOU 6045  CG  ARG B 421    24534  15014  43751    935  -3064   3197       C  
ATOM   6046  CD  ARG B 421     -39.267 -68.601   8.405  1.00223.73           C  
ANISOU 6046  CD  ARG B 421    24992  15260  44756    906  -3337   3986       C  
ATOM   6047  NE  ARG B 421     -38.848 -69.972   8.110  1.00231.07           N  
ANISOU 6047  NE  ARG B 421    26027  15235  46534   1158  -3707   3870       N  
ATOM   6048  CZ  ARG B 421     -39.681 -70.997   7.946  1.00236.25           C  
ANISOU 6048  CZ  ARG B 421    26829  15147  47789    900  -4038   3972       C  
ATOM   6049  NH1 ARG B 421     -40.992 -70.811   8.042  1.00234.89           N  
ANISOU 6049  NH1 ARG B 421    26677  15110  47459    367  -4032   4202       N  
ATOM   6050  NH2 ARG B 421     -39.205 -72.208   7.689  1.00243.18           N  
ANISOU 6050  NH2 ARG B 421    27819  15134  49444   1175  -4389   3840       N  
ATOM   6051  N   TRP B 422     -39.485 -66.312   4.178  1.00211.92           N  
ANISOU 6051  N   TRP B 422    23880  14686  41956   1434  -2457   1298       N  
ATOM   6052  CA  TRP B 422     -38.456 -66.466   3.153  1.00213.65           C  
ANISOU 6052  CA  TRP B 422    24156  14750  42273   1970  -2347    590       C  
ATOM   6053  C   TRP B 422     -38.325 -65.248   2.249  1.00208.38           C  
ANISOU 6053  C   TRP B 422    23541  14751  40882   2098  -1918     42       C  
ATOM   6054  O   TRP B 422     -37.235 -64.945   1.773  1.00208.18           O  
ANISOU 6054  O   TRP B 422    23449  14928  40722   2506  -1680   -328       O  
ATOM   6055  CB  TRP B 422     -38.733 -67.711   2.310  1.00219.98           C  
ANISOU 6055  CB  TRP B 422    25162  14696  43725   2120  -2685    128       C  
ATOM   6056  CG  TRP B 422     -38.710 -68.971   3.118  1.00226.09           C  
ANISOU 6056  CG  TRP B 422    25905  14716  45281   2049  -3117    637       C  
ATOM   6057  CD1 TRP B 422     -39.708 -69.898   3.223  1.00230.39           C  
ANISOU 6057  CD1 TRP B 422    26574  14609  46356   1711  -3502    837       C  
ATOM   6058  CD2 TRP B 422     -37.641 -69.435   3.953  1.00228.97           C  
ANISOU 6058  CD2 TRP B 422    26104  14896  45998   2312  -3223   1046       C  
ATOM   6059  NE1 TRP B 422     -39.321 -70.915   4.064  1.00235.87           N  
ANISOU 6059  NE1 TRP B 422    27213  14694  47712   1743  -3831   1365       N  
ATOM   6060  CE2 TRP B 422     -38.058 -70.653   4.525  1.00235.05           C  
ANISOU 6060  CE2 TRP B 422    26938  14872  47499   2128  -3674   1499       C  
ATOM   6061  CE3 TRP B 422     -36.371 -68.941   4.267  1.00227.36           C  
ANISOU 6061  CE3 TRP B 422    25691  15117  45577   2679  -2994   1079       C  
ATOM   6062  CZ2 TRP B 422     -37.252 -71.381   5.393  1.00239.47           C  
ANISOU 6062  CZ2 TRP B 422    27389  15051  48547   2330  -3905   1988       C  
ATOM   6063  CZ3 TRP B 422     -35.576 -69.664   5.129  1.00231.67           C  
ANISOU 6063  CZ3 TRP B 422    26100  15312  46611   2880  -3234   1536       C  
ATOM   6064  CH2 TRP B 422     -36.018 -70.871   5.682  1.00237.63           C  
ANISOU 6064  CH2 TRP B 422    26951  15274  48063   2720  -3686   1989       C  
ATOM   6065  N   ALA B 423     -39.432 -64.556   2.006  1.00204.50           N  
ANISOU 6065  N   ALA B 423    23160  14607  39935   1755  -1820      4       N  
ATOM   6066  CA  ALA B 423     -39.378 -63.283   1.297  1.00199.23           C  
ANISOU 6066  CA  ALA B 423    22555  14615  38529   1828  -1415   -392       C  
ATOM   6067  C   ALA B 423     -38.553 -62.292   2.106  1.00195.12           C  
ANISOU 6067  C   ALA B 423    21820  14718  37598   1849  -1130    -22       C  
ATOM   6068  O   ALA B 423     -37.692 -61.595   1.575  1.00193.29           O  
ANISOU 6068  O   ALA B 423    21554  14854  37034   2125   -809   -364       O  
ATOM   6069  CB  ALA B 423     -40.780 -62.744   1.048  1.00196.15           C  
ANISOU 6069  CB  ALA B 423    22303  14470  37753   1446  -1413   -413       C  
ATOM   6070  N   GLY B 424     -38.806 -62.268   3.408  1.00194.24           N  
ANISOU 6070  N   GLY B 424    21557  14715  37529   1553  -1260    687       N  
ATOM   6071  CA  GLY B 424     -38.088 -61.398   4.313  1.00190.92           C  
ANISOU 6071  CA  GLY B 424    20934  14854  36753   1547  -1066   1072       C  
ATOM   6072  C   GLY B 424     -36.616 -61.731   4.383  1.00193.65           C  
ANISOU 6072  C   GLY B 424    21101  15080  37399   1955  -1038    988       C  
ATOM   6073  O   GLY B 424     -35.784 -60.836   4.396  1.00190.95           O  
ANISOU 6073  O   GLY B 424    20626  15231  36693   2092   -758    899       O  
ATOM   6074  N   TYR B 425     -36.287 -63.017   4.410  1.00199.40           N  
ANISOU 6074  N   TYR B 425    21812  15139  38810   2155  -1338   1006       N  
ATOM   6075  CA  TYR B 425     -34.889 -63.427   4.497  1.00202.72           C  
ANISOU 6075  CA  TYR B 425    22036  15418  39569   2585  -1346    926       C  
ATOM   6076  C   TYR B 425     -34.155 -63.124   3.197  1.00202.86           C  
ANISOU 6076  C   TYR B 425    22078  15560  39439   2980  -1040    170       C  
ATOM   6077  O   TYR B 425     -32.995 -62.710   3.215  1.00202.75           O  
ANISOU 6077  O   TYR B 425    21839  15861  39335   3253   -829     75       O  
ATOM   6078  CB  TYR B 425     -34.772 -64.915   4.835  1.00209.36           C  
ANISOU 6078  CB  TYR B 425    22884  15458  41205   2725  -1773   1131       C  
ATOM   6079  CG  TYR B 425     -35.135 -65.222   6.265  1.00210.14           C  
ANISOU 6079  CG  TYR B 425    22893  15489  41461   2414  -2044   1974       C  
ATOM   6080  CD1 TYR B 425     -34.738 -64.377   7.291  1.00206.78           C  
ANISOU 6080  CD1 TYR B 425    22263  15678  40625   2303  -1923   2446       C  
ATOM   6081  CD2 TYR B 425     -35.851 -66.364   6.595  1.00214.74           C  
ANISOU 6081  CD2 TYR B 425    23596  15393  42601   2235  -2427   2302       C  
ATOM   6082  CE1 TYR B 425     -35.061 -64.645   8.596  1.00207.85           C  
ANISOU 6082  CE1 TYR B 425    22329  15804  40841   2049  -2158   3215       C  
ATOM   6083  CE2 TYR B 425     -36.176 -66.641   7.902  1.00215.90           C  
ANISOU 6083  CE2 TYR B 425    23663  15512  42858   1951  -2646   3116       C  
ATOM   6084  CZ  TYR B 425     -35.777 -65.778   8.896  1.00212.43           C  
ANISOU 6084  CZ  TYR B 425    23029  15737  41946   1876  -2502   3566       C  
ATOM   6085  OH  TYR B 425     -36.096 -66.044  10.199  1.00213.93           O  
ANISOU 6085  OH  TYR B 425    23150  15948  42184   1621  -2710   4376       O  
ATOM   6086  N   CYS B 426     -34.838 -63.343   2.076  1.00203.52           N  
ANISOU 6086  N   CYS B 426    22422  15413  39494   3005  -1020   -359       N  
ATOM   6087  CA  CYS B 426     -34.307 -63.007   0.759  1.00203.73           C  
ANISOU 6087  CA  CYS B 426    22520  15611  39276   3361   -703  -1086       C  
ATOM   6088  C   CYS B 426     -34.001 -61.530   0.694  1.00198.11           C  
ANISOU 6088  C   CYS B 426    21720  15697  37854   3262   -266  -1088       C  
ATOM   6089  O   CYS B 426     -32.945 -61.118   0.221  1.00198.49           O  
ANISOU 6089  O   CYS B 426    21619  16039  37760   3569     39  -1381       O  
ATOM   6090  CB  CYS B 426     -35.306 -63.365  -0.337  1.00204.89           C  
ANISOU 6090  CB  CYS B 426    22997  15451  39403   3333   -788  -1598       C  
ATOM   6091  SG  CYS B 426     -35.412 -65.121  -0.714  1.00212.93           S  
ANISOU 6091  SG  CYS B 426    24155  15463  41287   3593  -1262  -1882       S  
ATOM   6092  N   CYS B 427     -34.951 -60.746   1.188  1.00193.28           N  
ANISOU 6092  N   CYS B 427    21196  15423  36819   2825   -244   -748       N  
ATOM   6093  CA  CYS B 427     -34.798 -59.311   1.328  1.00187.90           C  
ANISOU 6093  CA  CYS B 427    20457  15452  35484   2665    105   -654       C  
ATOM   6094  C   CYS