HEADER    SIGNALING PROTEIN                       05-DEC-16   5WS3              
TITLE     CRYSTAL STRUCTURES OF HUMAN OREXIN 2 RECEPTOR BOUND TO THE SELECTIVE  
TITLE    2 ANTAGONIST EMPA DETERMINED BY SERIAL FEMTOSECOND CRYSTALLOGRAPHY AT  
TITLE    3 SACLA                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OREXIN RECEPTOR TYPE 2,GLGA GLYCOGEN SYNTHASE,OREXIN       
COMPND   3 RECEPTOR TYPE 2;                                                     
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: UNP RESIDUES 3-254,UNP RESIDUES 218-413,UNP RESIDUES 294-  
COMPND   6 388;                                                                 
COMPND   7 SYNONYM: OX2R,HYPOCRETIN RECEPTOR TYPE 2,GLYCOGEN SYNTHASE;          
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: CHIMERA PROTEIN OF UNP RESIDUES 3-254 FROM OREXIN     
COMPND  10 RECEPTOR TYPE 2 (O43614), UNP RESIDUES 218-413 FROM GLGA GLYCOGEN    
COMPND  11 SYNTHASE (Q9V2J8), UNP RESIDUES 294-388 FROM OREXIN RECEPTOR TYPE 2  
COMPND  12 (O43614)                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, PYROCOCCUS ABYSSI (STRAIN GE5 /   
SOURCE   3 ORSAY);                                                              
SOURCE   4 ORGANISM_COMMON: HUMAN;                                              
SOURCE   5 ORGANISM_TAXID: 9606, 272844;                                        
SOURCE   6 STRAIN: GE5 / ORSAY;                                                 
SOURCE   7 GENE: HCRTR2, PAB2292;                                               
SOURCE   8 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    RECEPTOR, SIGNALING PROTEIN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.SUNO,K.KIMURA,T.NAKANE,K.YAMASHITA,J.WANG,T.FUJIWARA,Y.YAMANAKA,    
AUTHOR   2 D.IM,H.TSUJIMOTO,M.SASANUMA,S.HORITA,T.HIROKAWA,E.NANGO,K.TONO,      
AUTHOR   3 T.KAMESHIMA,T.HATSUI,Y.JOTI,M.YABASHI,K.SHIMAMOTO,M.YAMAMOTO,        
AUTHOR   4 D.M.ROSENBAUM,S.IWATA,T.SHIMAMURA,T.KOBAYASHI                        
REVDAT   3   20-JUN-18 5WS3    1       JRNL                                     
REVDAT   2   31-JAN-18 5WS3    1       REMARK                                   
REVDAT   1   13-DEC-17 5WS3    0                                                
JRNL        AUTH   R.SUNO,K.T.KIMURA,T.NAKANE,K.YAMASHITA,J.WANG,T.FUJIWARA,    
JRNL        AUTH 2 Y.YAMANAKA,D.IM,S.HORITA,H.TSUJIMOTO,M.S.TAWARAMOTO,         
JRNL        AUTH 3 T.HIROKAWA,E.NANGO,K.TONO,T.KAMESHIMA,T.HATSUI,Y.JOTI,       
JRNL        AUTH 4 M.YABASHI,K.SHIMAMOTO,M.YAMAMOTO,D.M.ROSENBAUM,S.IWATA,      
JRNL        AUTH 5 T.SHIMAMURA,T.KOBAYASHI                                      
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN OREXIN 2 RECEPTOR BOUND TO THE   
JRNL        TITL 2 SUBTYPE-SELECTIVE ANTAGONIST EMPA.                           
JRNL        REF    STRUCTURE                     V.  26     7 2018              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   29225076                                                     
JRNL        DOI    10.1016/J.STR.2017.11.005                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_2747: ???)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.11                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 28958                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1440                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 45.1173 -  4.9532    0.99     2804   162  0.1971 0.2028        
REMARK   3     2  4.9532 -  3.9322    1.00     2768   145  0.1748 0.1930        
REMARK   3     3  3.9322 -  3.4354    1.00     2752   131  0.1798 0.1930        
REMARK   3     4  3.4354 -  3.1214    1.00     2763   159  0.1939 0.2386        
REMARK   3     5  3.1214 -  2.8977    1.00     2748   151  0.1978 0.2323        
REMARK   3     6  2.8977 -  2.7269    1.00     2734   139  0.2002 0.2264        
REMARK   3     7  2.7269 -  2.5903    1.00     2748   144  0.2380 0.2970        
REMARK   3     8  2.5903 -  2.4776    1.00     2719   145  0.2646 0.3122        
REMARK   3     9  2.4776 -  2.3822    1.00     2740   130  0.3202 0.3679        
REMARK   3    10  2.3822 -  2.3000    1.00     2742   134  0.3974 0.4361        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.500           
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      :  0.005           4310                                  
REMARK   3   ANGLE     :  0.714           5814                                  
REMARK   3   CHIRALITY :  0.047            651                                  
REMARK   3   PLANARITY :  0.004            708                                  
REMARK   3   DIHEDRAL  : 11.864           2586                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 35 THROUGH 251 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  46.2769  40.0896 -46.8419              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5561 T22:   0.4614                                     
REMARK   3      T33:   0.5701 T12:   0.0067                                     
REMARK   3      T13:   0.0971 T23:   0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1586 L22:   2.4917                                     
REMARK   3      L33:   3.0250 L12:   0.0548                                     
REMARK   3      L13:  -0.0566 L23:  -0.1264                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0879 S12:   0.1059 S13:  -0.0111                       
REMARK   3      S21:  -0.0685 S22:  -0.0104 S23:  -0.0417                       
REMARK   3      S31:  -0.0711 S32:  -0.0662 S33:   0.0888                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 252 THROUGH 383 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   39.600   47.049  -39.435              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7632 T22:   0.5345                                     
REMARK   3      T33:   0.5803 T12:   0.0068                                     
REMARK   3      T13:   0.0661 T23:  -0.0133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3297 L22:   0.0966                                     
REMARK   3      L33:   3.6996 L12:   0.1314                                     
REMARK   3      L13:  -1.0812 L23:  -0.5477                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0115 S12:   0.0157 S13:  -0.0280                       
REMARK   3      S21:  -0.0572 S22:  -0.0494 S23:  -0.0457                       
REMARK   3      S31:  -0.0962 S32:  -0.0989 S33:   0.0482                       
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 5WS3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-DEC-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300002299.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : FREE ELECTRON LASER                
REMARK 200  BEAMLINE                       : BL3                                
REMARK 200  X-RAY GENERATOR MODEL          : SACLA BEAMLINE BL3                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.77                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MPCCD                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28958                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 77.60                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 4S0V                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 0.1M SODIUM MALONATE, 27-30%   
REMARK 280  PEG 300, PH 6.0, LIPIDIC CUBIC PHASE, TEMPERATURE 293K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       48.75500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.99000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       48.75500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       37.99000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 310 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 25810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A    -6                                                      
REMARK 465     TYR A    -5                                                      
REMARK 465     LYS A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     ASP A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     MET A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     CYS A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     ASN A    14                                                      
REMARK 465     TRP A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     GLU A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     ASN A    22                                                      
REMARK 465     GLU A    23                                                      
REMARK 465     THR A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     GLU A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     PHE A    28                                                      
REMARK 465     LEU A    29                                                      
REMARK 465     ASN A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     THR A    32                                                      
REMARK 465     ASP A    33                                                      
REMARK 465     TYR A    34                                                      
REMARK 465     LEU A   384                                                      
REMARK 465     GLY A   385                                                      
REMARK 465     VAL A   386                                                      
REMARK 465     HIS A   387                                                      
REMARK 465     HIS A   388                                                      
REMARK 465     HIS A   389                                                      
REMARK 465     HIS A   390                                                      
REMARK 465     HIS A   391                                                      
REMARK 465     HIS A   392                                                      
REMARK 465     HIS A   393                                                      
REMARK 465     HIS A   394                                                      
REMARK 465     HIS A   395                                                      
REMARK 465     HIS A   396                                                      
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    TYR A 232      -57.65   -126.16                                   
REMARK 500    SER A1111      -31.96   -132.99                                   
REMARK 500    PRO A1118       49.60    -89.72                                   
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     OLA A 2002                                                       
REMARK 610     OLA A 2003                                                       
REMARK 610     OLA A 2004                                                       
REMARK 610     OLA A 2005                                                       
REMARK 610     1PE A 2006                                                       
REMARK 610     1PE A 2007                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7MA A 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 2006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 2007                
DBREF  5WS3 A    3   254  UNP    O43614   OX2R_HUMAN       3    254             
DBREF  5WS3 A 1001  1196  UNP    Q9V2J8   Q9V2J8_PYRAB   218    413             
DBREF  5WS3 A  294   388  UNP    O43614   OX2R_HUMAN     294    388             
SEQADV 5WS3 ASP A   -6  UNP  O43614              EXPRESSION TAG                 
SEQADV 5WS3 TYR A   -5  UNP  O43614              EXPRESSION TAG                 
SEQADV 5WS3 LYS A   -4  UNP  O43614              EXPRESSION TAG                 
SEQADV 5WS3 ASP A   -3  UNP  O43614              EXPRESSION TAG                 
SEQADV 5WS3 ASP A   -2  UNP  O43614              EXPRESSION TAG                 
SEQADV 5WS3 ASP A   -1  UNP  O43614              EXPRESSION TAG                 
SEQADV 5WS3 ASP A    0  UNP  O43614              EXPRESSION TAG                 
SEQADV 5WS3 ALA A    1  UNP  O43614              EXPRESSION TAG                 
SEQADV 5WS3 MET A    2  UNP  O43614              EXPRESSION TAG                 
SEQADV 5WS3 VAL A  308  UNP  O43614    ILE   308 VARIANT                        
SEQADV 5WS3 HIS A  389  UNP  O43614              EXPRESSION TAG                 
SEQADV 5WS3 HIS A  390  UNP  O43614              EXPRESSION TAG                 
SEQADV 5WS3 HIS A  391  UNP  O43614              EXPRESSION TAG                 
SEQADV 5WS3 HIS A  392  UNP  O43614              EXPRESSION TAG                 
SEQADV 5WS3 HIS A  393  UNP  O43614              EXPRESSION TAG                 
SEQADV 5WS3 HIS A  394  UNP  O43614              EXPRESSION TAG                 
SEQADV 5WS3 HIS A  395  UNP  O43614              EXPRESSION TAG                 
SEQADV 5WS3 HIS A  396  UNP  O43614              EXPRESSION TAG                 
SEQRES   1 A  560  ASP TYR LYS ASP ASP ASP ASP ALA MET GLY THR LYS LEU          
SEQRES   2 A  560  GLU ASP SER PRO PRO CYS ARG ASN TRP SER SER ALA SER          
SEQRES   3 A  560  GLU LEU ASN GLU THR GLN GLU PRO PHE LEU ASN PRO THR          
SEQRES   4 A  560  ASP TYR ASP ASP GLU GLU PHE LEU ARG TYR LEU TRP ARG          
SEQRES   5 A  560  GLU TYR LEU HIS PRO LYS GLU TYR GLU TRP VAL LEU ILE          
SEQRES   6 A  560  ALA GLY TYR ILE ILE VAL PHE VAL VAL ALA LEU ILE GLY          
SEQRES   7 A  560  ASN VAL LEU VAL CYS VAL ALA VAL TRP LYS ASN HIS HIS          
SEQRES   8 A  560  MET ARG THR VAL THR ASN TYR PHE ILE VAL ASN LEU SER          
SEQRES   9 A  560  LEU ALA ASP VAL LEU VAL THR ILE THR CYS LEU PRO ALA          
SEQRES  10 A  560  THR LEU VAL VAL ASP ILE THR GLU THR TRP PHE PHE GLY          
SEQRES  11 A  560  GLN SER LEU CYS LYS VAL ILE PRO TYR LEU GLN THR VAL          
SEQRES  12 A  560  SER VAL SER VAL SER VAL LEU THR LEU SER CYS ILE ALA          
SEQRES  13 A  560  LEU ASP ARG TRP TYR ALA ILE CYS HIS PRO LEU MET PHE          
SEQRES  14 A  560  LYS SER THR ALA LYS ARG ALA ARG ASN SER ILE VAL ILE          
SEQRES  15 A  560  ILE TRP ILE VAL SER CYS ILE ILE MET ILE PRO GLN ALA          
SEQRES  16 A  560  ILE VAL MET GLU CYS SER THR VAL PHE PRO GLY LEU ALA          
SEQRES  17 A  560  ASN LYS THR THR LEU PHE THR VAL CYS ASP GLU ARG TRP          
SEQRES  18 A  560  GLY GLY GLU ILE TYR PRO LYS MET TYR HIS ILE CYS PHE          
SEQRES  19 A  560  PHE LEU VAL THR TYR MET ALA PRO LEU CYS LEU MET VAL          
SEQRES  20 A  560  LEU ALA TYR LEU GLN ILE PHE ARG LYS LEU TRP CYS ARG          
SEQRES  21 A  560  GLN GLY ILE ASP CYS SER PHE TRP ASN GLU SER TYR LEU          
SEQRES  22 A  560  THR GLY SER ARG ASP GLU ARG LYS LYS SER LEU LEU SER          
SEQRES  23 A  560  LYS PHE GLY MET ASP GLU GLY VAL THR PHE MET PHE ILE          
SEQRES  24 A  560  GLY ARG PHE ASP ARG GLY GLN LYS GLY VAL ASP VAL LEU          
SEQRES  25 A  560  LEU LYS ALA ILE GLU ILE LEU SER SER LYS LYS GLU PHE          
SEQRES  26 A  560  GLN GLU MET ARG PHE ILE ILE ILE GLY LYS GLY ASP PRO          
SEQRES  27 A  560  GLU LEU GLU GLY TRP ALA ARG SER LEU GLU GLU LYS HIS          
SEQRES  28 A  560  GLY ASN VAL LYS VAL ILE THR GLU MET LEU SER ARG GLU          
SEQRES  29 A  560  PHE VAL ARG GLU LEU TYR GLY SER VAL ASP PHE VAL ILE          
SEQRES  30 A  560  ILE PRO SER TYR PHE GLU PRO PHE GLY LEU VAL ALA LEU          
SEQRES  31 A  560  GLU ALA MET CYS LEU GLY ALA ILE PRO ILE ALA SER ALA          
SEQRES  32 A  560  VAL GLY GLY LEU ARG ASP ILE ILE THR ASN GLU THR GLY          
SEQRES  33 A  560  ILE LEU VAL LYS ALA GLY ASP PRO GLY GLU LEU ALA ASN          
SEQRES  34 A  560  ALA ILE LEU LYS ALA LEU GLU LEU SER ARG SER ASP LEU          
SEQRES  35 A  560  SER LYS PHE ARG GLU ASN CYS LYS LYS ARG ALA MET SER          
SEQRES  36 A  560  PHE SER LYS GLN ILE ARG ALA ARG ARG LYS THR ALA ARG          
SEQRES  37 A  560  MET LEU MET VAL VAL LEU LEU VAL PHE ALA ILE CYS TYR          
SEQRES  38 A  560  LEU PRO ILE SER ILE LEU ASN VAL LEU LYS ARG VAL PHE          
SEQRES  39 A  560  GLY MET PHE ALA HIS THR GLU ASP ARG GLU THR VAL TYR          
SEQRES  40 A  560  ALA TRP PHE THR PHE SER HIS TRP LEU VAL TYR ALA ASN          
SEQRES  41 A  560  SER ALA ALA ASN PRO ILE ILE TYR ASN PHE LEU SER GLY          
SEQRES  42 A  560  LYS PHE ARG GLU GLU PHE LYS ALA ALA PHE SER CYS CYS          
SEQRES  43 A  560  CYS LEU GLY VAL HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES  44 A  560  HIS                                                          
HET    7MA  A2001      32                                                       
HET    OLA  A2002      15                                                       
HET    OLA  A2003      16                                                       
HET    OLA  A2004      15                                                       
HET    OLA  A2005      17                                                       
HET    1PE  A2006      13                                                       
HET    1PE  A2007      13                                                       
HETNAM     7MA N-ETHYL-2-[(6-METHOXYPYRIDIN-3-YL)-(2-METHYLPHENYL)              
HETNAM   2 7MA  SULFONYL-AMINO]-N-(PYRIDIN-3-YLMETHYL)ETHANAMIDE                
HETNAM     OLA OLEIC ACID                                                       
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETSYN     1PE PEG400                                                           
FORMUL   2  7MA    C23 H26 N4 O4 S                                              
FORMUL   3  OLA    4(C18 H34 O2)                                                
FORMUL   7  1PE    2(C10 H22 O6)                                                
FORMUL   9  HOH   *12(H2 O)                                                     
HELIX    1 AA1 ASP A   35  LEU A   48  1                                  14    
HELIX    2 AA2 TYR A   53  ASN A   82  1                                  30    
HELIX    3 AA3 HIS A   83  ARG A   86  5                                   4    
HELIX    4 AA4 THR A   87  CYS A  107  1                                  21    
HELIX    5 AA5 CYS A  107  GLU A  118  1                                  12    
HELIX    6 AA6 PHE A  122  CYS A  157  1                                  36    
HELIX    7 AA7 THR A  165  MET A  184  1                                  20    
HELIX    8 AA8 MET A  184  VAL A  190  1                                   7    
HELIX    9 AA9 GLU A  217  TYR A  232  1                                  16    
HELIX   10 AB1 TYR A  232  CYS A  252  1                                  21    
HELIX   11 AB2 ASN A 1008  LEU A 1012  5                                   5    
HELIX   12 AB3 SER A 1015  GLY A 1028  1                                  14    
HELIX   13 AB4 GLY A 1047  SER A 1059  1                                  13    
HELIX   14 AB5 SER A 1060  GLN A 1065  5                                   6    
HELIX   15 AB6 ASP A 1076  HIS A 1090  1                                  15    
HELIX   16 AB7 SER A 1101  GLY A 1110  1                                  10    
HELIX   17 AB8 GLY A 1125  LEU A 1134  1                                  10    
HELIX   18 AB9 GLY A 1144  ILE A 1150  1                                   7    
HELIX   19 AC1 ASP A 1162  ARG A 1178  1                                  17    
HELIX   20 AC2 LEU A 1181  VAL A  329  1                                  52    
HELIX   21 AC3 ASP A  338  SER A  368  1                                  31    
HELIX   22 AC4 SER A  368  CYS A  383  1                                  16    
SHEET    1 AA1 2 MET A 191  VAL A 196  0                                        
SHEET    2 AA1 2 PHE A 207  GLU A 212 -1  O  PHE A 207   N  VAL A 196           
SHEET    1 AA2 6 VAL A1093  ILE A1096  0                                        
SHEET    2 AA2 6 MET A1067  ILE A1072  1  N  ILE A1071   O  ILE A1096           
SHEET    3 AA2 6 VAL A1033  ILE A1038  1  N  PHE A1035   O  ARG A1068           
SHEET    4 AA2 6 PHE A1114  ILE A1117  1  O  ILE A1116   N  MET A1036           
SHEET    5 AA2 6 ILE A1137  SER A1141  1  O  ILE A1139   N  ILE A1117           
SHEET    6 AA2 6 ILE A1156  VAL A1158  1  O  VAL A1158   N  ALA A1140           
SSBOND   1 CYS A  127    CYS A  210                          1555   1555  2.04  
SITE     1 AC1 11 THR A 111  PRO A 131  GLN A 134  GLN A 187                    
SITE     2 AC1 11 GLU A 212  PHE A 227  ILE A 320  SER A 321                    
SITE     3 AC1 11 ASN A 324  HIS A 350  TYR A 354                               
SITE     1 AC2  1 OLA A2004                                                     
SITE     1 AC3  6 GLU A  54  TRP A  55  ILE A  62  LEU A 150                    
SITE     2 AC3  6 TYR A 154  LEU A 238                                          
SITE     1 AC4  1 OLA A2002                                                     
SITE     1 AC5  6 TYR A  53  VAL A  56  LEU A  57  VAL A 179                    
SITE     2 AC5  6 ALA A 344  TRP A 351                                          
SITE     1 AC6  8 LEU A  43  TYR A  47  THR A 204  THR A 205                    
SITE     2 AC6  8 SER A1022  LYS A1026  PHE A1104  GLU A1107                    
SITE     1 AC7  4 CYS A 210  LYS A 327  PHE A 333  PHE A 346                    
CRYST1   97.510   75.980   96.100  90.00 112.30  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010255  0.000000  0.004206        0.00000                         
SCALE2      0.000000  0.013161  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011247        0.00000                         
ATOM      1  N   ASP A  35      64.551  65.983 -72.867  1.00168.46           N  
ANISOU    1  N   ASP A  35    25862  18997  19147  -4212   3812   3031       N  
ATOM      2  CA  ASP A  35      64.832  65.428 -74.186  1.00170.02           C  
ANISOU    2  CA  ASP A  35    26082  19372  19147  -4175   4035   3069       C  
ATOM      3  C   ASP A  35      64.588  63.928 -74.219  1.00168.98           C  
ANISOU    3  C   ASP A  35    25727  19474  19003  -3973   4113   2948       C  
ATOM      4  O   ASP A  35      63.472  63.483 -74.466  1.00168.41           O  
ANISOU    4  O   ASP A  35    25869  19350  18770  -3720   3981   2918       O  
ATOM      5  CB  ASP A  35      66.270  65.733 -74.601  1.00172.70           C  
ANISOU    5  CB  ASP A  35    26202  19854  19562  -4468   4295   3131       C  
ATOM      6  CG  ASP A  35      66.506  67.209 -74.814  1.00177.61           C  
ANISOU    6  CG  ASP A  35    27096  20241  20147  -4671   4248   3264       C  
ATOM      7  OD1 ASP A  35      65.555  67.903 -75.230  1.00178.98           O  
ANISOU    7  OD1 ASP A  35    27701  20172  20131  -4544   4082   3332       O  
ATOM      8  OD2 ASP A  35      67.637  67.675 -74.564  1.00180.90           O  
ANISOU    8  OD2 ASP A  35    27292  20714  20727  -4953   4371   3300       O  
ATOM      9  N   ASP A  36      65.642  63.150 -73.965  1.00169.61           N  
ANISOU    9  N   ASP A  36    25373  19814  19256  -4080   4325   2876       N  
ATOM     10  CA  ASP A  36      65.514  61.697 -74.011  1.00168.81           C  
ANISOU   10  CA  ASP A  36    25050  19938  19153  -3887   4426   2751       C  
ATOM     11  C   ASP A  36      64.755  61.168 -72.802  1.00169.70           C  
ANISOU   11  C   ASP A  36    25014  20026  19439  -3692   4172   2617       C  
ATOM     12  O   ASP A  36      63.813  60.380 -72.946  1.00167.66           O  
ANISOU   12  O   ASP A  36    24800  19806  19099  -3394   4031   2519       O  
ATOM     13  CB  ASP A  36      66.895  61.050 -74.112  1.00168.32           C  
ANISOU   13  CB  ASP A  36    24546  20167  19241  -4020   4715   2710       C  
ATOM     14  CG  ASP A  36      67.354  60.891 -75.546  1.00170.60           C  
ANISOU   14  CG  ASP A  36    24929  20579  19313  -4024   4958   2767       C  
ATOM     15  OD1 ASP A  36      66.487  60.671 -76.420  1.00170.11           O  
ANISOU   15  OD1 ASP A  36    25201  20452  18981  -3841   4918   2775       O  
ATOM     16  OD2 ASP A  36      68.573  60.985 -75.803  1.00172.99           O  
ANISOU   16  OD2 ASP A  36    24972  21045  19711  -4209   5183   2805       O  
ATOM     17  N   GLU A  37      65.154  61.585 -71.597  1.00173.59           N  
ANISOU   17  N   GLU A  37    25286  20477  20192  -3823   4060   2587       N  
ATOM     18  CA  GLU A  37      64.471  61.116 -70.395  1.00173.65           C  
ANISOU   18  CA  GLU A  37    25108  20483  20388  -3601   3775   2438       C  
ATOM     19  C   GLU A  37      63.023  61.593 -70.359  1.00172.54           C  
ANISOU   19  C   GLU A  37    25338  20107  20113  -3382   3489   2446       C  
ATOM     20  O   GLU A  37      62.128  60.852 -69.933  1.00168.97           O  
ANISOU   20  O   GLU A  37    24806  19699  19697  -3100   3299   2323       O  
ATOM     21  CB  GLU A  37      65.221  61.580 -69.148  1.00176.58           C  
ANISOU   21  CB  GLU A  37    25216  20842  21036  -3810   3712   2415       C  
ATOM     22  CG  GLU A  37      64.613  61.083 -67.849  1.00175.69           C  
ANISOU   22  CG  GLU A  37    24904  20737  21113  -3598   3439   2262       C  
ATOM     23  CD  GLU A  37      65.361  61.580 -66.632  1.00178.89           C  
ANISOU   23  CD  GLU A  37    25081  21124  21765  -3814   3362   2240       C  
ATOM     24  OE1 GLU A  37      66.291  62.397 -66.797  1.00183.19           O  
ANISOU   24  OE1 GLU A  37    25639  21629  22335  -4143   3501   2347       O  
ATOM     25  OE2 GLU A  37      65.019  61.152 -65.510  1.00177.57           O  
ANISOU   25  OE2 GLU A  37    24727  20983  21759  -3667   3161   2117       O  
ATOM     26  N   GLU A  38      62.774  62.831 -70.799  1.00175.29           N  
ANISOU   26  N   GLU A  38    26090  20204  20307  -3505   3457   2596       N  
ATOM     27  CA  GLU A  38      61.406  63.334 -70.879  1.00173.69           C  
ANISOU   27  CA  GLU A  38    26252  19780  19963  -3277   3196   2621       C  
ATOM     28  C   GLU A  38      60.605  62.599 -71.948  1.00171.01           C  
ANISOU   28  C   GLU A  38    26063  19527  19386  -3031   3192   2609       C  
ATOM     29  O   GLU A  38      59.379  62.483 -71.832  1.00170.26           O  
ANISOU   29  O   GLU A  38    26098  19361  19233  -2759   2947   2562       O  
ATOM     30  CB  GLU A  38      61.418  64.842 -71.152  1.00177.19           C  
ANISOU   30  CB  GLU A  38    27112  19921  20290  -3470   3179   2795       C  
ATOM     31  CG  GLU A  38      60.041  65.508 -71.208  1.00177.69           C  
ANISOU   31  CG  GLU A  38    27568  19731  20214  -3226   2906   2838       C  
ATOM     32  CD  GLU A  38      59.317  65.509 -69.869  1.00175.99           C  
ANISOU   32  CD  GLU A  38    27220  19447  20202  -3038   2633   2709       C  
ATOM     33  OE1 GLU A  38      59.970  65.290 -68.828  1.00175.19           O  
ANISOU   33  OE1 GLU A  38    26796  19429  20341  -3158   2645   2613       O  
ATOM     34  OE2 GLU A  38      58.087  65.729 -69.858  1.00175.43           O  
ANISOU   34  OE2 GLU A  38    27365  19245  20044  -2766   2408   2704       O  
ATOM     35  N   PHE A  39      61.280  62.095 -72.985  1.00168.67           N  
ANISOU   35  N   PHE A  39    25747  19392  18949  -3124   3463   2647       N  
ATOM     36  CA  PHE A  39      60.596  61.354 -74.040  1.00164.95           C  
ANISOU   36  CA  PHE A  39    25432  19010  18234  -2912   3469   2626       C  
ATOM     37  C   PHE A  39      60.023  60.040 -73.521  1.00163.09           C  
ANISOU   37  C   PHE A  39    24899  18953  18115  -2646   3339   2433       C  
ATOM     38  O   PHE A  39      58.908  59.655 -73.891  1.00161.77           O  
ANISOU   38  O   PHE A  39    24885  18774  17807  -2405   3158   2390       O  
ATOM     39  CB  PHE A  39      61.554  61.094 -75.199  1.00163.65           C  
ANISOU   39  CB  PHE A  39    25303  18980  17896  -3084   3818   2699       C  
ATOM     40  CG  PHE A  39      61.017  60.146 -76.224  1.00161.07           C  
ANISOU   40  CG  PHE A  39    25090  18781  17330  -2881   3853   2646       C  
ATOM     41  CD1 PHE A  39      60.094  60.573 -77.159  1.00161.17           C  
ANISOU   41  CD1 PHE A  39    25541  18655  17040  -2770   3730   2740       C  
ATOM     42  CD2 PHE A  39      61.435  58.825 -76.254  1.00159.32           C  
ANISOU   42  CD2 PHE A  39    24548  18809  17179  -2796   4000   2499       C  
ATOM     43  CE1 PHE A  39      59.595  59.703 -78.107  1.00160.64           C  
ANISOU   43  CE1 PHE A  39    25591  18705  16739  -2598   3744   2685       C  
ATOM     44  CE2 PHE A  39      60.938  57.949 -77.199  1.00158.60           C  
ANISOU   44  CE2 PHE A  39    24588  18818  16856  -2620   4028   2438       C  
ATOM     45  CZ  PHE A  39      60.019  58.390 -78.129  1.00159.57           C  
ANISOU   45  CZ  PHE A  39    25148  18809  16671  -2531   3897   2529       C  
ATOM     46  N   LEU A  40      60.777  59.329 -72.679  1.00162.83           N  
ANISOU   46  N   LEU A  40    24442  19088  18337  -2692   3424   2317       N  
ATOM     47  CA  LEU A  40      60.292  58.054 -72.160  1.00160.70           C  
ANISOU   47  CA  LEU A  40    23901  18975  18181  -2453   3315   2139       C  
ATOM     48  C   LEU A  40      59.138  58.257 -71.187  1.00157.38           C  
ANISOU   48  C   LEU A  40    23501  18431  17867  -2267   2981   2077       C  
ATOM     49  O   LEU A  40      58.173  57.483 -71.189  1.00155.14           O  
ANISOU   49  O   LEU A  40    23202  18200  17545  -2029   2825   1977       O  
ATOM     50  CB  LEU A  40      61.431  57.287 -71.491  1.00161.20           C  
ANISOU   50  CB  LEU A  40    23522  19240  18489  -2541   3488   2047       C  
ATOM     51  CG  LEU A  40      61.061  55.902 -70.953  1.00159.23           C  
ANISOU   51  CG  LEU A  40    22994  19146  18359  -2308   3404   1868       C  
ATOM     52  CD1 LEU A  40      60.534  55.016 -72.073  1.00159.45           C  
ANISOU   52  CD1 LEU A  40    23175  19257  18153  -2142   3464   1820       C  
ATOM     53  CD2 LEU A  40      62.250  55.252 -70.262  1.00159.33           C  
ANISOU   53  CD2 LEU A  40    22580  19342  18616  -2390   3566   1797       C  
ATOM     54  N   ARG A  41      59.224  59.288 -70.340  1.00156.94           N  
ANISOU   54  N   ARG A  41    23477  18209  17943  -2377   2874   2130       N  
ATOM     55  CA  ARG A  41      58.109  59.612 -69.456  1.00154.10           C  
ANISOU   55  CA  ARG A  41    23175  17713  17663  -2194   2576   2081       C  
ATOM     56  C   ARG A  41      56.865  59.968 -70.258  1.00148.72           C  
ANISOU   56  C   ARG A  41    22852  16910  16746  -2006   2413   2143       C  
ATOM     57  O   ARG A  41      55.748  59.585 -69.893  1.00146.62           O  
ANISOU   57  O   ARG A  41    22561  16649  16500  -1765   2195   2059       O  
ATOM     58  CB  ARG A  41      58.496  60.761 -68.525  1.00159.19           C  
ANISOU   58  CB  ARG A  41    23854  18176  18456  -2365   2516   2135       C  
ATOM     59  CG  ARG A  41      59.682  60.452 -67.625  1.00162.79           C  
ANISOU   59  CG  ARG A  41    23939  18758  19155  -2552   2631   2072       C  
ATOM     60  CD  ARG A  41      60.046  61.638 -66.745  1.00166.72           C  
ANISOU   60  CD  ARG A  41    24507  19061  19776  -2744   2554   2123       C  
ATOM     61  NE  ARG A  41      58.929  62.076 -65.910  1.00167.87           N  
ANISOU   61  NE  ARG A  41    24787  19034  19961  -2552   2284   2074       N  
ATOM     62  CZ  ARG A  41      58.660  61.595 -64.700  1.00168.02           C  
ANISOU   62  CZ  ARG A  41    24567  19108  20164  -2435   2141   1941       C  
ATOM     63  NH1 ARG A  41      59.425  60.648 -64.173  1.00168.15           N  
ANISOU   63  NH1 ARG A  41    24203  19342  20343  -2484   2225   1847       N  
ATOM     64  NH2 ARG A  41      57.622  62.058 -64.014  1.00167.01           N  
ANISOU   64  NH2 ARG A  41    24586  18819  20052  -2258   1920   1905       N  
ATOM     65  N   TYR A  42      57.047  60.692 -71.364  1.00146.23           N  
ANISOU   65  N   TYR A  42    22867  16492  16204  -2116   2516   2295       N  
ATOM     66  CA  TYR A  42      55.932  61.028 -72.243  1.00143.36           C  
ANISOU   66  CA  TYR A  42    22858  16022  15589  -1938   2361   2370       C  
ATOM     67  C   TYR A  42      55.286  59.774 -72.822  1.00141.01           C  
ANISOU   67  C   TYR A  42    22475  15919  15184  -1737   2317   2263       C  
ATOM     68  O   TYR A  42      54.056  59.698 -72.945  1.00138.01           O  
ANISOU   68  O   TYR A  42    22210  15508  14721  -1508   2080   2241       O  
ATOM     69  CB  TYR A  42      56.436  61.949 -73.357  1.00145.11           C  
ANISOU   69  CB  TYR A  42    23447  16114  15575  -2125   2520   2559       C  
ATOM     70  CG  TYR A  42      55.423  62.320 -74.417  1.00145.24           C  
ANISOU   70  CG  TYR A  42    23863  16026  15297  -1960   2377   2661       C  
ATOM     71  CD1 TYR A  42      55.192  61.491 -75.509  1.00144.66           C  
ANISOU   71  CD1 TYR A  42    23859  16107  14999  -1875   2433   2641       C  
ATOM     72  CD2 TYR A  42      54.722  63.514 -74.342  1.00147.04           C  
ANISOU   72  CD2 TYR A  42    24415  15995  15460  -1887   2184   2780       C  
ATOM     73  CE1 TYR A  42      54.275  61.830 -76.481  1.00146.51           C  
ANISOU   73  CE1 TYR A  42    24460  16256  14952  -1728   2282   2737       C  
ATOM     74  CE2 TYR A  42      53.805  63.865 -75.313  1.00149.39           C  
ANISOU   74  CE2 TYR A  42    25073  16202  15485  -1722   2038   2883       C  
ATOM     75  CZ  TYR A  42      53.584  63.020 -76.381  1.00149.10           C  
ANISOU   75  CZ  TYR A  42    25087  16337  15227  -1647   2079   2863       C  
ATOM     76  OH  TYR A  42      52.668  63.372 -77.347  1.00150.89           O  
ANISOU   76  OH  TYR A  42    25676  16483  15173  -1484   1910   2968       O  
ATOM     77  N   LEU A  43      56.103  58.783 -73.185  1.00143.06           N  
ANISOU   77  N   LEU A  43    22532  16378  15445  -1818   2544   2193       N  
ATOM     78  CA  LEU A  43      55.590  57.583 -73.842  1.00144.27           C  
ANISOU   78  CA  LEU A  43    22648  16699  15470  -1656   2530   2090       C  
ATOM     79  C   LEU A  43      54.684  56.784 -72.908  1.00138.71           C  
ANISOU   79  C   LEU A  43    21698  16065  14941  -1444   2303   1932       C  
ATOM     80  O   LEU A  43      53.593  56.352 -73.299  1.00136.29           O  
ANISOU   80  O   LEU A  43    21485  15787  14513  -1258   2119   1886       O  
ATOM     81  CB  LEU A  43      56.761  56.733 -74.342  1.00148.59           C  
ANISOU   81  CB  LEU A  43    23030  17427  16000  -1786   2848   2045       C  
ATOM     82  CG  LEU A  43      56.477  55.534 -75.250  1.00150.56           C  
ANISOU   82  CG  LEU A  43    23308  17833  16067  -1664   2904   1949       C  
ATOM     83  CD1 LEU A  43      55.587  55.935 -76.415  1.00153.54           C  
ANISOU   83  CD1 LEU A  43    24098  18127  16115  -1583   2780   2040       C  
ATOM     84  CD2 LEU A  43      57.782  54.934 -75.760  1.00151.69           C  
ANISOU   84  CD2 LEU A  43    23321  18126  16189  -1806   3262   1930       C  
ATOM     85  N   TRP A  44      55.119  56.578 -71.663  1.00137.13           N  
ANISOU   85  N   TRP A  44    21183  15898  15022  -1479   2309   1849       N  
ATOM     86  CA  TRP A  44      54.267  55.884 -70.703  1.00134.56           C  
ANISOU   86  CA  TRP A  44    20638  15627  14863  -1291   2105   1710       C  
ATOM     87  C   TRP A  44      53.014  56.687 -70.376  1.00133.53           C  
ANISOU   87  C   TRP A  44    20677  15345  14714  -1137   1826   1751       C  
ATOM     88  O   TRP A  44      51.959  56.098 -70.115  1.00131.41           O  
ANISOU   88  O   TRP A  44    20328  15133  14468   -946   1638   1660       O  
ATOM     89  CB  TRP A  44      55.044  55.572 -69.425  1.00132.96           C  
ANISOU   89  CB  TRP A  44    20092  15481  14948  -1367   2170   1628       C  
ATOM     90  CG  TRP A  44      55.874  54.341 -69.535  1.00133.30           C  
ANISOU   90  CG  TRP A  44    19883  15716  15050  -1401   2369   1530       C  
ATOM     91  CD1 TRP A  44      57.227  54.276 -69.686  1.00136.13           C  
ANISOU   91  CD1 TRP A  44    20111  16151  15460  -1580   2626   1559       C  
ATOM     92  CD2 TRP A  44      55.407  52.987 -69.515  1.00130.93           C  
ANISOU   92  CD2 TRP A  44    19433  15551  14764  -1244   2331   1389       C  
ATOM     93  NE1 TRP A  44      57.633  52.966 -69.755  1.00135.92           N  
ANISOU   93  NE1 TRP A  44    19864  16299  15481  -1518   2753   1443       N  
ATOM     94  CE2 TRP A  44      56.533  52.154 -69.652  1.00132.17           C  
ANISOU   94  CE2 TRP A  44    19390  15850  14980  -1318   2575   1337       C  
ATOM     95  CE3 TRP A  44      54.145  52.399 -69.394  1.00127.81           C  
ANISOU   95  CE3 TRP A  44    19050  15171  14342  -1054   2118   1302       C  
ATOM     96  CZ2 TRP A  44      56.437  50.765 -69.673  1.00129.71           C  
ANISOU   96  CZ2 TRP A  44    18925  15667  14691  -1199   2609   1200       C  
ATOM     97  CZ3 TRP A  44      54.052  51.019 -69.416  1.00125.89           C  
ANISOU   97  CZ3 TRP A  44    18649  15062  14122   -966   2152   1168       C  
ATOM     98  CH2 TRP A  44      55.191  50.218 -69.555  1.00126.46           C  
ANISOU   98  CH2 TRP A  44    18557  15248  14244  -1034   2395   1117       C  
ATOM     99  N   ARG A  45      53.108  58.022 -70.378  1.00134.01           N  
ANISOU   99  N   ARG A  45    20969  15212  14736  -1215   1799   1887       N  
ATOM    100  CA  ARG A  45      51.919  58.839 -70.153  1.00133.34           C  
ANISOU  100  CA  ARG A  45    21073  14972  14619  -1041   1544   1935       C  
ATOM    101  C   ARG A  45      50.904  58.650 -71.273  1.00134.44           C  
ANISOU  101  C   ARG A  45    21428  15140  14512   -875   1409   1970       C  
ATOM    102  O   ARG A  45      49.698  58.550 -71.016  1.00133.74           O  
ANISOU  102  O   ARG A  45    21318  15058  14438   -659   1175   1926       O  
ATOM    103  CB  ARG A  45      52.296  60.313 -70.025  1.00135.64           C  
ANISOU  103  CB  ARG A  45    21615  15024  14899  -1164   1559   2079       C  
ATOM    104  CG  ARG A  45      53.010  60.689 -68.739  1.00134.54           C  
ANISOU  104  CG  ARG A  45    21292  14820  15008  -1298   1605   2039       C  
ATOM    105  CD  ARG A  45      53.288  62.192 -68.711  1.00137.67           C  
ANISOU  105  CD  ARG A  45    21994  14949  15364  -1425   1603   2184       C  
ATOM    106  NE  ARG A  45      54.217  62.574 -67.651  1.00136.79           N  
ANISOU  106  NE  ARG A  45    21732  14781  15463  -1626   1681   2155       N  
ATOM    107  CZ  ARG A  45      54.640  63.816 -67.438  1.00137.43           C  
ANISOU  107  CZ  ARG A  45    22039  14629  15548  -1789   1696   2258       C  
ATOM    108  NH1 ARG A  45      54.213  64.806 -68.211  1.00138.17           N  
ANISOU  108  NH1 ARG A  45    22535  14514  15450  -1762   1647   2404       N  
ATOM    109  NH2 ARG A  45      55.487  64.067 -66.449  1.00138.10           N  
ANISOU  109  NH2 ARG A  45    21963  14685  15825  -1983   1751   2215       N  
ATOM    110  N   GLU A  46      51.371  58.610 -72.525  1.00135.49           N  
ANISOU  110  N   GLU A  46    21769  15300  14412   -976   1553   2052       N  
ATOM    111  CA  GLU A  46      50.471  58.265 -73.623  1.00135.14           C  
ANISOU  111  CA  GLU A  46    21918  15313  14118   -832   1424   2068       C  
ATOM    112  C   GLU A  46      49.924  56.853 -73.466  1.00130.66           C  
ANISOU  112  C   GLU A  46    21087  14951  13609   -711   1351   1893       C  
ATOM    113  O   GLU A  46      48.778  56.583 -73.846  1.00132.01           O  
ANISOU  113  O   GLU A  46    21319  15166  13671   -537   1131   1868       O  
ATOM    114  CB  GLU A  46      51.185  58.406 -74.966  1.00138.61           C  
ANISOU  114  CB  GLU A  46    22632  15750  14283   -981   1624   2178       C  
ATOM    115  CG  GLU A  46      51.187  59.813 -75.519  1.00144.05           C  
ANISOU  115  CG  GLU A  46    23711  16219  14802  -1031   1601   2379       C  
ATOM    116  CD  GLU A  46      51.611  59.858 -76.971  1.00150.32           C  
ANISOU  116  CD  GLU A  46    24816  17025  15273  -1136   1758   2488       C  
ATOM    117  OE1 GLU A  46      52.080  58.820 -77.486  1.00151.40           O  
ANISOU  117  OE1 GLU A  46    24845  17343  15338  -1193   1927   2399       O  
ATOM    118  OE2 GLU A  46      51.471  60.930 -77.599  1.00154.44           O  
ANISOU  118  OE2 GLU A  46    25708  17368  15603  -1155   1718   2663       O  
ATOM    119  N   TYR A  47      50.720  55.945 -72.902  1.00124.58           N  
ANISOU  119  N   TYR A  47    20023  14304  13009   -804   1524   1773       N  
ATOM    120  CA  TYR A  47      50.266  54.573 -72.720  1.00119.43           C  
ANISOU  120  CA  TYR A  47    19138  13824  12417   -704   1471   1607       C  
ATOM    121  C   TYR A  47      49.245  54.472 -71.587  1.00116.06           C  
ANISOU  121  C   TYR A  47    18510  13396  12191   -544   1236   1526       C  
ATOM    122  O   TYR A  47      48.124  53.997 -71.796  1.00115.37           O  
ANISOU  122  O   TYR A  47    18415  13376  12044   -395   1038   1470       O  
ATOM    123  CB  TYR A  47      51.474  53.664 -72.469  1.00117.31           C  
ANISOU  123  CB  TYR A  47    18636  13671  12266   -835   1736   1515       C  
ATOM    124  CG  TYR A  47      51.144  52.212 -72.213  1.00115.67           C  
ANISOU  124  CG  TYR A  47    18201  13615  12133   -746   1708   1343       C  
ATOM    125  CD1 TYR A  47      50.942  51.323 -73.263  1.00115.53           C  
ANISOU  125  CD1 TYR A  47    18295  13694  11908   -719   1741   1283       C  
ATOM    126  CD2 TYR A  47      51.048  51.728 -70.916  1.00115.62           C  
ANISOU  126  CD2 TYR A  47    17893  13644  12393   -699   1652   1240       C  
ATOM    127  CE1 TYR A  47      50.643  49.993 -73.023  1.00115.75           C  
ANISOU  127  CE1 TYR A  47    18140  13836  12003   -650   1716   1123       C  
ATOM    128  CE2 TYR A  47      50.750  50.405 -70.663  1.00115.82           C  
ANISOU  128  CE2 TYR A  47    17733  13788  12486   -627   1631   1090       C  
ATOM    129  CZ  TYR A  47      50.551  49.539 -71.717  1.00116.71           C  
ANISOU  129  CZ  TYR A  47    17962  13983  12400   -607   1663   1031       C  
ATOM    130  OH  TYR A  47      50.256  48.221 -71.451  1.00116.67           O  
ANISOU  130  OH  TYR A  47    17795  14072  12462   -548   1642    880       O  
ATOM    131  N   LEU A  48      49.604  54.946 -70.392  1.00113.95           N  
ANISOU  131  N   LEU A  48    18084  13056  12155   -578   1254   1521       N  
ATOM    132  CA  LEU A  48      48.783  54.787 -69.193  1.00110.78           C  
ANISOU  132  CA  LEU A  48    17470  12664  11959   -441   1079   1434       C  
ATOM    133  C   LEU A  48      47.757  55.911 -69.091  1.00113.94           C  
ANISOU  133  C   LEU A  48    18047  12925  12321   -294    862   1523       C  
ATOM    134  O   LEU A  48      48.128  57.086 -69.008  1.00117.78           O  
ANISOU  134  O   LEU A  48    18713  13240  12796   -350    888   1637       O  
ATOM    135  CB  LEU A  48      49.665  54.778 -67.945  1.00106.21           C  
ANISOU  135  CB  LEU A  48    16661  12069  11626   -542   1197   1385       C  
ATOM    136  CG  LEU A  48      50.680  53.645 -67.785  1.00104.36           C  
ANISOU  136  CG  LEU A  48    16196  11974  11482   -653   1396   1289       C  
ATOM    137  CD1 LEU A  48      51.629  53.943 -66.634  1.00103.39           C  
ANISOU  137  CD1 LEU A  48    15891  11813  11578   -767   1491   1279       C  
ATOM    138  CD2 LEU A  48      49.964  52.325 -67.556  1.00101.86           C  
ANISOU  138  CD2 LEU A  48    15691  11796  11213   -531   1314   1147       C  
ATOM    139  N   HIS A  49      46.473  55.553 -69.053  1.00113.50           N  
ANISOU  139  N   HIS A  49    17929  12939  12257   -106    648   1469       N  
ATOM    140  CA  HIS A  49      45.410  56.546 -68.943  1.00116.83           C  
ANISOU  140  CA  HIS A  49    18485  13252  12655     75    432   1546       C  
ATOM    141  C   HIS A  49      45.127  56.840 -67.475  1.00114.41           C  
ANISOU  141  C   HIS A  49    17988  12892  12593    153    381   1487       C  
ATOM    142  O   HIS A  49      44.769  55.918 -66.730  1.00114.39           O  
ANISOU  142  O   HIS A  49    17707  13019  12736    197    355   1358       O  
ATOM    143  CB  HIS A  49      44.146  56.060 -69.634  1.00122.23           C  
ANISOU  143  CB  HIS A  49    19174  14055  13212    241    220   1523       C  
ATOM    144  CG  HIS A  49      44.309  55.843 -71.107  1.00129.51           C  
ANISOU  144  CG  HIS A  49    20328  15019  13860    181    240   1583       C  
ATOM    145  ND1 HIS A  49      44.092  56.840 -72.034  1.00133.61           N  
ANISOU  145  ND1 HIS A  49    21180  15420  14166    230    158   1738       N  
ATOM    146  CD2 HIS A  49      44.672  54.745 -71.814  1.00130.71           C  
ANISOU  146  CD2 HIS A  49    20450  15309  13904     79    338   1507       C  
ATOM    147  CE1 HIS A  49      44.310  56.365 -73.248  1.00135.47           C  
ANISOU  147  CE1 HIS A  49    21578  15729  14164    156    202   1757       C  
ATOM    148  NE2 HIS A  49      44.664  55.097 -73.142  1.00133.33           N  
ANISOU  148  NE2 HIS A  49    21095  15613  13952     64    315   1613       N  
ATOM    149  N   PRO A  50      45.263  58.082 -67.020  1.00113.22           N  
ANISOU  149  N   PRO A  50    17992  12544  12481    170    368   1574       N  
ATOM    150  CA  PRO A  50      45.102  58.367 -65.592  1.00110.27           C  
ANISOU  150  CA  PRO A  50    17462  12110  12326    229    341   1508       C  
ATOM    151  C   PRO A  50      43.645  58.413 -65.159  1.00104.88           C  
ANISOU  151  C   PRO A  50    16686  11466  11696    492    132   1469       C  
ATOM    152  O   PRO A  50      42.739  58.712 -65.939  1.00103.59           O  
ANISOU  152  O   PRO A  50    16652  11308  11400    650    -25   1534       O  
ATOM    153  CB  PRO A  50      45.764  59.742 -65.435  1.00113.71           C  
ANISOU  153  CB  PRO A  50    18157  12300  12748    144    398   1622       C  
ATOM    154  CG  PRO A  50      45.572  60.392 -66.757  1.00115.90           C  
ANISOU  154  CG  PRO A  50    18755  12491  12792    171    350   1767       C  
ATOM    155  CD  PRO A  50      45.638  59.284 -67.786  1.00116.30           C  
ANISOU  155  CD  PRO A  50    18737  12742  12709    118    391   1737       C  
ATOM    156  N   LYS A  51      43.434  58.114 -63.884  1.00103.04           N  
ANISOU  156  N   LYS A  51    16221  11269  11659    539    132   1362       N  
ATOM    157  CA  LYS A  51      42.120  58.180 -63.263  1.00101.21           C  
ANISOU  157  CA  LYS A  51    15865  11080  11511    779    -30   1315       C  
ATOM    158  C   LYS A  51      41.992  59.469 -62.463  1.00 99.91           C  
ANISOU  158  C   LYS A  51    15851  10699  11412    884    -59   1359       C  
ATOM    159  O   LYS A  51      42.967  59.967 -61.896  1.00 97.91           O  
ANISOU  159  O   LYS A  51    15683  10302  11214    735     60   1367       O  
ATOM    160  CB  LYS A  51      41.882  56.969 -62.359  1.00 97.59           C  
ANISOU  160  CB  LYS A  51    15065  10802  11211    769     -1   1166       C  
ATOM    161  CG  LYS A  51      42.018  55.652 -63.092  1.00 96.15           C  
ANISOU  161  CG  LYS A  51    14752  10810  10968    664     32   1110       C  
ATOM    162  CD  LYS A  51      41.814  54.473 -62.181  1.00 94.56           C  
ANISOU  162  CD  LYS A  51    14247  10760  10923    645     65    972       C  
ATOM    163  CE  LYS A  51      42.109  53.194 -62.927  1.00 95.49           C  
ANISOU  163  CE  LYS A  51    14282  11027  10972    524    119    915       C  
ATOM    164  NZ  LYS A  51      41.220  53.069 -64.105  1.00 98.09           N  
ANISOU  164  NZ  LYS A  51    14691  11438  11140    607    -32    949       N  
ATOM    165  N   GLU A  52      40.771  60.007 -62.426  1.00101.79           N  
ANISOU  165  N   GLU A  52    16119  10914  11642   1146   -221   1386       N  
ATOM    166  CA  GLU A  52      40.560  61.317 -61.820  1.00102.64           C  
ANISOU  166  CA  GLU A  52    16425  10791  11784   1284   -257   1436       C  
ATOM    167  C   GLU A  52      40.765  61.289 -60.311  1.00 97.80           C  
ANISOU  167  C   GLU A  52    15666  10142  11353   1266   -175   1325       C  
ATOM    168  O   GLU A  52      41.102  62.319 -59.715  1.00 96.35           O  
ANISOU  168  O   GLU A  52    15681   9733  11195   1270   -144   1351       O  
ATOM    169  CB  GLU A  52      39.159  61.821 -62.151  1.00107.43           C  
ANISOU  169  CB  GLU A  52    17070  11404  12345   1601   -451   1487       C  
ATOM    170  CG  GLU A  52      38.043  60.948 -61.603  1.00108.69           C  
ANISOU  170  CG  GLU A  52    16873  11800  12623   1763   -531   1375       C  
ATOM    171  CD  GLU A  52      36.668  61.444 -62.003  1.00114.91           C  
ANISOU  171  CD  GLU A  52    17666  12623  13373   2080   -730   1433       C  
ATOM    172  OE1 GLU A  52      36.571  62.185 -63.009  1.00121.65           O  
ANISOU  172  OE1 GLU A  52    18788  13365  14069   2158   -830   1565       O  
ATOM    173  OE2 GLU A  52      35.687  61.099 -61.313  1.00115.14           O  
ANISOU  173  OE2 GLU A  52    17427  12794  13525   2254   -786   1351       O  
ATOM    174  N   TYR A  53      40.582  60.128 -59.682  1.00 94.67           N  
ANISOU  174  N   TYR A  53    14947   9954  11070   1236   -140   1202       N  
ATOM    175  CA  TYR A  53      40.645  59.988 -58.234  1.00 91.29           C  
ANISOU  175  CA  TYR A  53    14368   9519  10800   1238    -74   1093       C  
ATOM    176  C   TYR A  53      41.960  59.386 -57.756  1.00 88.21           C  
ANISOU  176  C   TYR A  53    13897   9148  10470    962     75   1038       C  
ATOM    177  O   TYR A  53      42.057  58.972 -56.596  1.00 92.19           O  
ANISOU  177  O   TYR A  53    14238   9695  11096    940    127    939       O  
ATOM    178  CB  TYR A  53      39.473  59.134 -57.740  1.00 91.80           C  
ANISOU  178  CB  TYR A  53    14129   9796  10954   1406   -135    999       C  
ATOM    179  CG  TYR A  53      39.410  57.738 -58.347  1.00 89.93           C  
ANISOU  179  CG  TYR A  53    13666   9799  10704   1300   -134    954       C  
ATOM    180  CD1 TYR A  53      40.053  56.663 -57.748  1.00 87.18           C  
ANISOU  180  CD1 TYR A  53    13125   9557  10441   1124    -21    861       C  
ATOM    181  CD2 TYR A  53      38.707  57.499 -59.519  1.00 93.15           C  
ANISOU  181  CD2 TYR A  53    14071  10317  11004   1380   -256   1005       C  
ATOM    182  CE1 TYR A  53      39.993  55.394 -58.297  1.00 86.12           C  
ANISOU  182  CE1 TYR A  53    12816   9616  10291   1034    -17    816       C  
ATOM    183  CE2 TYR A  53      38.643  56.232 -60.073  1.00 92.85           C  
ANISOU  183  CE2 TYR A  53    13855  10480  10942   1274   -259    954       C  
ATOM    184  CZ  TYR A  53      39.285  55.187 -59.457  1.00 89.90           C  
ANISOU  184  CZ  TYR A  53    13307  10192  10660   1103   -133    858       C  
ATOM    185  OH  TYR A  53      39.225  53.928 -60.014  1.00 93.54           O  
ANISOU  185  OH  TYR A  53    13622  10827  11092   1003   -132    803       O  
ATOM    186  N   GLU A  54      42.973  59.318 -58.619  1.00 81.96           N  
ANISOU  186  N   GLU A  54    13212   8335   9594    757    147   1103       N  
ATOM    187  CA  GLU A  54      44.207  58.652 -58.219  1.00 79.04           C  
ANISOU  187  CA  GLU A  54    12720   8018   9292    514    286   1051       C  
ATOM    188  C   GLU A  54      45.020  59.480 -57.234  1.00 79.90           C  
ANISOU  188  C   GLU A  54    12939   7945   9473    403    343   1044       C  
ATOM    189  O   GLU A  54      45.882  58.928 -56.546  1.00 83.50           O  
ANISOU  189  O   GLU A  54    13247   8458  10021    241    429    981       O  
ATOM    190  CB  GLU A  54      45.053  58.313 -59.443  1.00 78.20           C  
ANISOU  190  CB  GLU A  54    12676   7960   9077    335    366   1118       C  
ATOM    191  CG  GLU A  54      45.644  59.504 -60.148  1.00 83.25           C  
ANISOU  191  CG  GLU A  54    13629   8401   9603    245    392   1248       C  
ATOM    192  CD  GLU A  54      46.525  59.109 -61.321  1.00 87.20           C  
ANISOU  192  CD  GLU A  54    14176   8966   9991     59    503   1311       C  
ATOM    193  OE1 GLU A  54      47.234  59.993 -61.855  1.00 91.05           O  
ANISOU  193  OE1 GLU A  54    14901   9301  10392    -74    565   1418       O  
ATOM    194  OE2 GLU A  54      46.507  57.914 -61.703  1.00 86.52           O  
ANISOU  194  OE2 GLU A  54    13900   9078   9897     42    537   1250       O  
ATOM    195  N   TRP A  55      44.757  60.781 -57.132  1.00 75.34           N  
ANISOU  195  N   TRP A  55    12624   7147   8856    489    287   1106       N  
ATOM    196  CA  TRP A  55      45.508  61.601 -56.189  1.00 74.38           C  
ANISOU  196  CA  TRP A  55    12633   6835   8792    369    329   1091       C  
ATOM    197  C   TRP A  55      45.136  61.251 -54.757  1.00 71.51           C  
ANISOU  197  C   TRP A  55    12099   6519   8551    456    317    963       C  
ATOM    198  O   TRP A  55      46.012  61.049 -53.907  1.00 71.09           O  
ANISOU  198  O   TRP A  55    11970   6465   8576    285    377    904       O  
ATOM    199  CB  TRP A  55      45.285  63.093 -56.471  1.00 73.63           C  
ANISOU  199  CB  TRP A  55    12903   6463   8611    444    272   1187       C  
ATOM    200  CG  TRP A  55      43.864  63.613 -56.337  1.00 75.36           C  
ANISOU  200  CG  TRP A  55    13203   6620   8811    778    153   1187       C  
ATOM    201  CD1 TRP A  55      42.909  63.655 -57.314  1.00 78.84           C  
ANISOU  201  CD1 TRP A  55    13684   7110   9161    982     58   1258       C  
ATOM    202  CD2 TRP A  55      43.268  64.205 -55.173  1.00 75.79           C  
ANISOU  202  CD2 TRP A  55    13313   6552   8933    953    116   1113       C  
ATOM    203  NE1 TRP A  55      41.755  64.221 -56.831  1.00 76.32           N  
ANISOU  203  NE1 TRP A  55    13414   6720   8866   1280    -36   1238       N  
ATOM    204  CE2 TRP A  55      41.948  64.572 -55.522  1.00 75.66           C  
ANISOU  204  CE2 TRP A  55    13347   6525   8875   1273     10   1147       C  
ATOM    205  CE3 TRP A  55      43.713  64.437 -53.862  1.00 73.89           C  
ANISOU  205  CE3 TRP A  55    13082   6217   8777    875    161   1019       C  
ATOM    206  CZ2 TRP A  55      41.072  65.161 -54.612  1.00 76.59           C  
ANISOU  206  CZ2 TRP A  55    13516   6544   9042   1527    -31   1089       C  
ATOM    207  CZ3 TRP A  55      42.847  65.024 -52.964  1.00 73.12           C  
ANISOU  207  CZ3 TRP A  55    13065   6009   8709   1115    119    957       C  
ATOM    208  CH2 TRP A  55      41.538  65.384 -53.343  1.00 74.94           C  
ANISOU  208  CH2 TRP A  55    13337   6233   8906   1444     35    992       C  
ATOM    209  N   VAL A  56      43.837  61.155 -54.476  1.00 73.48           N  
ANISOU  209  N   VAL A  56    12278   6823   8816    722    241    922       N  
ATOM    210  CA  VAL A  56      43.407  60.791 -53.135  1.00 78.62           C  
ANISOU  210  CA  VAL A  56    12771   7530   9570    813    247    804       C  
ATOM    211  C   VAL A  56      43.744  59.334 -52.843  1.00 74.62           C  
ANISOU  211  C   VAL A  56    11955   7261   9137    697    307    729       C  
ATOM    212  O   VAL A  56      44.040  58.978 -51.700  1.00 73.96           O  
ANISOU  212  O   VAL A  56    11767   7203   9131    645    346    644       O  
ATOM    213  CB  VAL A  56      41.906  61.095 -52.965  1.00 86.48           C  
ANISOU  213  CB  VAL A  56    13757   8535  10566   1133    167    787       C  
ATOM    214  CG1 VAL A  56      41.058  60.193 -53.856  1.00 85.89           C  
ANISOU  214  CG1 VAL A  56    13474   8687  10472   1238    115    803       C  
ATOM    215  CG2 VAL A  56      41.499  60.968 -51.505  1.00 89.20           C  
ANISOU  215  CG2 VAL A  56    14001   8894  10999   1229    197    671       C  
ATOM    216  N   LEU A  57      43.743  58.479 -53.867  1.00 69.62           N  
ANISOU  216  N   LEU A  57    11195   6789   8469    653    314    759       N  
ATOM    217  CA  LEU A  57      44.125  57.087 -53.665  1.00 68.59           C  
ANISOU  217  CA  LEU A  57    10802   6857   8401    542    375    692       C  
ATOM    218  C   LEU A  57      45.594  56.975 -53.278  1.00 65.28           C  
ANISOU  218  C   LEU A  57    10376   6403   8023    300    463    685       C  
ATOM    219  O   LEU A  57      45.949  56.247 -52.347  1.00 62.52           O  
ANISOU  219  O   LEU A  57     9862   6134   7759    242    500    609       O  
ATOM    220  CB  LEU A  57      43.842  56.286 -54.932  1.00 72.57           C  
ANISOU  220  CB  LEU A  57    11222   7514   8839    543    363    724       C  
ATOM    221  CG  LEU A  57      43.990  54.772 -54.841  1.00 69.61           C  
ANISOU  221  CG  LEU A  57    10594   7337   8518    469    416    650       C  
ATOM    222  CD1 LEU A  57      42.911  54.207 -53.912  1.00 67.23           C  
ANISOU  222  CD1 LEU A  57    10113   7135   8296    614    379    564       C  
ATOM    223  CD2 LEU A  57      43.878  54.189 -56.212  1.00 70.51           C  
ANISOU  223  CD2 LEU A  57    10700   7554   8536    444    407    687       C  
ATOM    224  N   ILE A  58      46.465  57.689 -53.992  1.00 65.37           N  
ANISOU  224  N   ILE A  58    10562   6301   7975    155    494    770       N  
ATOM    225  CA  ILE A  58      47.886  57.678 -53.663  1.00 64.51           C  
ANISOU  225  CA  ILE A  58    10428   6168   7914    -85    574    772       C  
ATOM    226  C   ILE A  58      48.118  58.257 -52.275  1.00 66.23           C  
ANISOU  226  C   ILE A  58    10696   6268   8201   -111    545    714       C  
ATOM    227  O   ILE A  58      48.878  57.694 -51.474  1.00 65.75           O  
ANISOU  227  O   ILE A  58    10484   6278   8220   -231    577    658       O  
ATOM    228  CB  ILE A  58      48.682  58.443 -54.733  1.00 64.44           C  
ANISOU  228  CB  ILE A  58    10609   6055   7822   -242    621    884       C  
ATOM    229  CG1 ILE A  58      48.715  57.656 -56.039  1.00 63.62           C  
ANISOU  229  CG1 ILE A  58    10433   6098   7643   -257    676    926       C  
ATOM    230  CG2 ILE A  58      50.093  58.738 -54.254  1.00 66.04           C  
ANISOU  230  CG2 ILE A  58    10803   6204   8085   -495    689    891       C  
ATOM    231  CD1 ILE A  58      49.278  58.479 -57.196  1.00 66.81           C  
ANISOU  231  CD1 ILE A  58    11062   6391   7931   -379    726   1049       C  
ATOM    232  N   ALA A  59      47.479  59.396 -51.974  1.00 67.88           N  
ANISOU  232  N   ALA A  59    11130   6288   8371      7    481    727       N  
ATOM    233  CA  ALA A  59      47.603  59.992 -50.646  1.00 67.40           C  
ANISOU  233  CA  ALA A  59    11157   6098   8355     -1    451    660       C  
ATOM    234  C   ALA A  59      47.165  59.013 -49.560  1.00 66.09           C  
ANISOU  234  C   ALA A  59    10769   6083   8262     92    451    552       C  
ATOM    235  O   ALA A  59      47.871  58.815 -48.560  1.00 67.48           O  
ANISOU  235  O   ALA A  59    10887   6264   8490    -28    458    494       O  
ATOM    236  CB  ALA A  59      46.783  61.279 -50.567  1.00 64.11           C  
ANISOU  236  CB  ALA A  59    11025   5457   7877    169    390    682       C  
ATOM    237  N   GLY A  60      45.999  58.389 -49.743  1.00 65.58           N  
ANISOU  237  N   GLY A  60    10578   6143   8195    297    439    528       N  
ATOM    238  CA  GLY A  60      45.508  57.451 -48.751  1.00 67.05           C  
ANISOU  238  CA  GLY A  60    10564   6468   8442    379    452    434       C  
ATOM    239  C   GLY A  60      46.420  56.253 -48.587  1.00 66.16           C  
ANISOU  239  C   GLY A  60    10239   6512   8388    212    501    409       C  
ATOM    240  O   GLY A  60      46.648  55.785 -47.469  1.00 65.74           O  
ANISOU  240  O   GLY A  60    10099   6498   8382    184    510    341       O  
ATOM    241  N   TYR A  61      46.981  55.757 -49.697  1.00 65.03           N  
ANISOU  241  N   TYR A  61    10024   6452   8233    106    537    465       N  
ATOM    242  CA  TYR A  61      47.901  54.628 -49.607  1.00 63.06           C  
ANISOU  242  CA  TYR A  61     9577   6342   8041    -33    593    444       C  
ATOM    243  C   TYR A  61      49.188  55.011 -48.893  1.00 63.22           C  
ANISOU  243  C   TYR A  61     9623   6296   8104   -218    598    442       C  
ATOM    244  O   TYR A  61      49.733  54.216 -48.130  1.00 63.19           O  
ANISOU  244  O   TYR A  61     9466   6382   8161   -275    609    396       O  
ATOM    245  CB  TYR A  61      48.218  54.082 -50.994  1.00 60.94           C  
ANISOU  245  CB  TYR A  61     9250   6167   7737    -91    644    500       C  
ATOM    246  CG  TYR A  61      47.355  52.913 -51.388  1.00 60.97           C  
ANISOU  246  CG  TYR A  61     9103   6326   7739     22    651    464       C  
ATOM    247  CD1 TYR A  61      46.106  53.108 -51.951  1.00 59.70           C  
ANISOU  247  CD1 TYR A  61     8990   6173   7522    178    595    475       C  
ATOM    248  CD2 TYR A  61      47.787  51.609 -51.189  1.00 62.29           C  
ANISOU  248  CD2 TYR A  61     9081   6627   7961    -29    704    419       C  
ATOM    249  CE1 TYR A  61      45.314  52.042 -52.305  1.00 59.77           C  
ANISOU  249  CE1 TYR A  61     8854   6326   7529    254    589    438       C  
ATOM    250  CE2 TYR A  61      47.004  50.536 -51.555  1.00 60.47           C  
ANISOU  250  CE2 TYR A  61     8735   6519   7723     51    708    382       C  
ATOM    251  CZ  TYR A  61      45.765  50.760 -52.107  1.00 60.43           C  
ANISOU  251  CZ  TYR A  61     8773   6526   7662    180    648    389       C  
ATOM    252  OH  TYR A  61      44.973  49.705 -52.480  1.00 62.07           O  
ANISOU  252  OH  TYR A  61     8862   6858   7864    235    640    349       O  
ATOM    253  N   ILE A  62      49.699  56.216 -49.133  1.00 65.19           N  
ANISOU  253  N   ILE A  62    10066   6385   8318   -320    581    494       N  
ATOM    254  CA  ILE A  62      50.924  56.630 -48.455  1.00 66.01           C  
ANISOU  254  CA  ILE A  62    10187   6428   8465   -522    571    491       C  
ATOM    255  C   ILE A  62      50.682  56.763 -46.958  1.00 64.56           C  
ANISOU  255  C   ILE A  62    10035   6192   8302   -473    506    405       C  
ATOM    256  O   ILE A  62      51.507  56.338 -46.134  1.00 66.71           O  
ANISOU  256  O   ILE A  62    10196   6524   8628   -587    487    369       O  
ATOM    257  CB  ILE A  62      51.450  57.944 -49.054  1.00 68.03           C  
ANISOU  257  CB  ILE A  62    10670   6504   8673   -661    568    568       C  
ATOM    258  CG1 ILE A  62      51.994  57.709 -50.456  1.00 65.95           C  
ANISOU  258  CG1 ILE A  62    10356   6316   8386   -760    654    655       C  
ATOM    259  CG2 ILE A  62      52.532  58.537 -48.158  1.00 69.93           C  
ANISOU  259  CG2 ILE A  62    10956   6657   8956   -871    528    548       C  
ATOM    260  CD1 ILE A  62      52.491  58.996 -51.079  1.00 67.83           C  
ANISOU  260  CD1 ILE A  62    10835   6371   8568   -910    664    744       C  
ATOM    261  N   ILE A  63      49.548  57.366 -46.588  1.00 62.13           N  
ANISOU  261  N   ILE A  63     9885   5775   7945   -292    471    373       N  
ATOM    262  CA  ILE A  63      49.200  57.516 -45.180  1.00 63.27           C  
ANISOU  262  CA  ILE A  63    10086   5866   8087   -222    428    286       C  
ATOM    263  C   ILE A  63      49.083  56.152 -44.520  1.00 65.89           C  
ANISOU  263  C   ILE A  63    10182   6388   8466   -176    449    231       C  
ATOM    264  O   ILE A  63      49.693  55.897 -43.474  1.00 67.30           O  
ANISOU  264  O   ILE A  63    10324   6583   8663   -260    417    185       O  
ATOM    265  CB  ILE A  63      47.900  58.322 -45.033  1.00 65.73           C  
ANISOU  265  CB  ILE A  63    10585   6048   8339      2    414    263       C  
ATOM    266  CG1 ILE A  63      48.126  59.757 -45.503  1.00 71.89           C  
ANISOU  266  CG1 ILE A  63    11652   6596   9067    -51    382    316       C  
ATOM    267  CG2 ILE A  63      47.422  58.286 -43.604  1.00 67.24           C  
ANISOU  267  CG2 ILE A  63    10811   6217   8518    102    400    166       C  
ATOM    268  CD1 ILE A  63      46.888  60.624 -45.418  1.00 74.99           C  
ANISOU  268  CD1 ILE A  63    12246   6844   9403    195    367    301       C  
ATOM    269  N   VAL A  64      48.303  55.253 -45.131  1.00 63.76           N  
ANISOU  269  N   VAL A  64     9762   6257   8208    -49    496    239       N  
ATOM    270  CA  VAL A  64      48.107  53.927 -44.558  1.00 65.70           C  
ANISOU  270  CA  VAL A  64     9805   6664   8494     -6    523    193       C  
ATOM    271  C   VAL A  64      49.430  53.177 -44.489  1.00 66.12           C  
ANISOU  271  C   VAL A  64     9714   6808   8602   -178    529    207       C  
ATOM    272  O   VAL A  64      49.710  52.480 -43.510  1.00 67.50           O  
ANISOU  272  O   VAL A  64     9802   7045   8802   -192    515    166       O  
ATOM    273  CB  VAL A  64      47.042  53.157 -45.358  1.00 65.45           C  
ANISOU  273  CB  VAL A  64     9652   6752   8463    133    565    201       C  
ATOM    274  CG1 VAL A  64      47.151  51.678 -45.109  1.00 63.47           C  
ANISOU  274  CG1 VAL A  64     9196   6660   8258    116    603    174       C  
ATOM    275  CG2 VAL A  64      45.654  53.661 -44.982  1.00 66.05           C  
ANISOU  275  CG2 VAL A  64     9806   6784   8505    330    557    167       C  
ATOM    276  N   PHE A  65      50.285  53.350 -45.496  1.00 60.39           N  
ANISOU  276  N   PHE A  65     8966   6087   7893   -306    550    271       N  
ATOM    277  CA  PHE A  65      51.589  52.700 -45.495  1.00 58.23           C  
ANISOU  277  CA  PHE A  65     8533   5909   7681   -458    565    289       C  
ATOM    278  C   PHE A  65      52.410  53.118 -44.279  1.00 58.01           C  
ANISOU  278  C   PHE A  65     8538   5828   7673   -573    487    260       C  
ATOM    279  O   PHE A  65      52.910  52.272 -43.526  1.00 56.86           O  
ANISOU  279  O   PHE A  65     8256   5779   7571   -591    464    233       O  
ATOM    280  CB  PHE A  65      52.340  53.025 -46.794  1.00 58.60           C  
ANISOU  280  CB  PHE A  65     8573   5960   7732   -581    619    365       C  
ATOM    281  CG  PHE A  65      53.710  52.426 -46.852  1.00 59.47           C  
ANISOU  281  CG  PHE A  65     8499   6181   7917   -727    650    387       C  
ATOM    282  CD1 PHE A  65      53.891  51.126 -47.293  1.00 57.59           C  
ANISOU  282  CD1 PHE A  65     8072   6094   7717   -678    720    384       C  
ATOM    283  CD2 PHE A  65      54.812  53.146 -46.426  1.00 61.68           C  
ANISOU  283  CD2 PHE A  65     8790   6413   8231   -911    606    406       C  
ATOM    284  CE1 PHE A  65      55.147  50.558 -47.325  1.00 58.67           C  
ANISOU  284  CE1 PHE A  65     8026   6337   7929   -782    755    404       C  
ATOM    285  CE2 PHE A  65      56.074  52.581 -46.453  1.00 62.82           C  
ANISOU  285  CE2 PHE A  65     8729   6683   8458  -1035    631    429       C  
ATOM    286  CZ  PHE A  65      56.237  51.280 -46.902  1.00 62.71           C  
ANISOU  286  CZ  PHE A  65     8518   6824   8485   -955    710    429       C  
ATOM    287  N   VAL A  66      52.564  54.431 -44.072  1.00 59.71           N  
ANISOU  287  N   VAL A  66     8953   5882   7851   -653    435    264       N  
ATOM    288  CA  VAL A  66      53.421  54.881 -42.978  1.00 64.97           C  
ANISOU  288  CA  VAL A  66     9665   6494   8528   -795    345    233       C  
ATOM    289  C   VAL A  66      52.802  54.524 -41.627  1.00 65.97           C  
ANISOU  289  C   VAL A  66     9829   6620   8617   -675    296    153       C  
ATOM    290  O   VAL A  66      53.501  54.056 -40.717  1.00 65.46           O  
ANISOU  290  O   VAL A  66     9680   6619   8573   -746    232    127       O  
ATOM    291  CB  VAL A  66      53.735  56.389 -43.100  1.00 73.30           C  
ANISOU  291  CB  VAL A  66    10955   7353   9544   -930    301    252       C  
ATOM    292  CG1 VAL A  66      54.607  56.650 -44.320  1.00 74.01           C  
ANISOU  292  CG1 VAL A  66    10985   7463   9673  -1098    356    340       C  
ATOM    293  CG2 VAL A  66      52.472  57.218 -43.184  1.00 78.98           C  
ANISOU  293  CG2 VAL A  66    11917   7909  10182   -762    310    232       C  
ATOM    294  N   VAL A  67      51.484  54.698 -41.482  1.00 66.49           N  
ANISOU  294  N   VAL A  67    10011   6627   8624   -486    328    117       N  
ATOM    295  CA  VAL A  67      50.849  54.450 -40.188  1.00 67.92           C  
ANISOU  295  CA  VAL A  67    10248   6801   8756   -374    306     42       C  
ATOM    296  C   VAL A  67      50.895  52.966 -39.840  1.00 71.43           C  
ANISOU  296  C   VAL A  67    10477   7423   9240   -331    332     36       C  
ATOM    297  O   VAL A  67      51.267  52.591 -38.725  1.00 75.58           O  
ANISOU  297  O   VAL A  67    10996   7975   9745   -359    278      1       O  
ATOM    298  CB  VAL A  67      49.408  54.987 -40.175  1.00 65.87           C  
ANISOU  298  CB  VAL A  67    10135   6454   8436   -172    354      8       C  
ATOM    299  CG1 VAL A  67      48.696  54.543 -38.912  1.00 66.64           C  
ANISOU  299  CG1 VAL A  67    10254   6581   8484    -48    368    -65       C  
ATOM    300  CG2 VAL A  67      49.408  56.513 -40.268  1.00 65.28           C  
ANISOU  300  CG2 VAL A  67    10327   6167   8311   -201    315      5       C  
ATOM    301  N   ALA A  68      50.510  52.099 -40.779  1.00 67.12           N  
ANISOU  301  N   ALA A  68     9773   6990   8739   -262    410     71       N  
ATOM    302  CA  ALA A  68      50.544  50.662 -40.529  1.00 62.72           C  
ANISOU  302  CA  ALA A  68     9035   6578   8219   -222    441     69       C  
ATOM    303  C   ALA A  68      51.960  50.190 -40.230  1.00 64.49           C  
ANISOU  303  C   ALA A  68     9141   6867   8495   -359    384     92       C  
ATOM    304  O   ALA A  68      52.175  49.401 -39.305  1.00 64.56           O  
ANISOU  304  O   ALA A  68     9095   6934   8502   -341    352     74       O  
ATOM    305  CB  ALA A  68      49.963  49.906 -41.726  1.00 59.08           C  
ANISOU  305  CB  ALA A  68     8450   6206   7790   -150    527     98       C  
ATOM    306  N   LEU A  69      52.950  50.678 -40.987  1.00 65.30           N  
ANISOU  306  N   LEU A  69     9202   6965   8644   -497    370    138       N  
ATOM    307  CA  LEU A  69      54.325  50.243 -40.763  1.00 68.66           C  
ANISOU  307  CA  LEU A  69     9475   7476   9136   -622    318    165       C  
ATOM    308  C   LEU A  69      54.814  50.650 -39.378  1.00 66.15           C  
ANISOU  308  C   LEU A  69     9238   7113   8783   -694    189    129       C  
ATOM    309  O   LEU A  69      55.226  49.804 -38.572  1.00 72.43           O  
ANISOU  309  O   LEU A  69     9940   7991   9590   -675    136    122       O  
ATOM    310  CB  LEU A  69      55.231  50.817 -41.851  1.00 73.89           C  
ANISOU  310  CB  LEU A  69    10078   8144   9852   -768    346    223       C  
ATOM    311  CG  LEU A  69      56.629  50.213 -41.877  1.00 75.66           C  
ANISOU  311  CG  LEU A  69    10080   8500  10169   -875    325    260       C  
ATOM    312  CD1 LEU A  69      56.527  48.737 -42.203  1.00 75.27           C  
ANISOU  312  CD1 LEU A  69     9861   8578  10161   -743    403    267       C  
ATOM    313  CD2 LEU A  69      57.483  50.938 -42.885  1.00 78.79           C  
ANISOU  313  CD2 LEU A  69    10432   8896  10610  -1040    368    316       C  
ATOM    314  N   ILE A  70      54.788  51.952 -39.090  1.00 64.20           N  
ANISOU  314  N   ILE A  70     9185   6724   8483   -778    131    105       N  
ATOM    315  CA  ILE A  70      55.269  52.447 -37.804  1.00 65.89           C  
ANISOU  315  CA  ILE A  70     9510   6879   8645   -867     -4     60       C  
ATOM    316  C   ILE A  70      54.490  51.813 -36.659  1.00 65.74           C  
ANISOU  316  C   ILE A  70     9561   6871   8547   -719    -14      6       C  
ATOM    317  O   ILE A  70      55.072  51.325 -35.684  1.00 67.86           O  
ANISOU  317  O   ILE A  70     9790   7197   8798   -752   -110     -5       O  
ATOM    318  CB  ILE A  70      55.171  53.980 -37.756  1.00 67.37           C  
ANISOU  318  CB  ILE A  70     9946   6877   8773   -965    -47     32       C  
ATOM    319  CG1 ILE A  70      56.034  54.597 -38.860  1.00 64.99           C  
ANISOU  319  CG1 ILE A  70     9584   6564   8546  -1143    -32     97       C  
ATOM    320  CG2 ILE A  70      55.570  54.496 -36.373  1.00 67.44           C  
ANISOU  320  CG2 ILE A  70    10110   6810   8705  -1055   -191    -31       C  
ATOM    321  CD1 ILE A  70      55.980  56.094 -38.871  1.00 65.18           C  
ANISOU  321  CD1 ILE A  70     9874   6379   8512  -1254    -73     79       C  
ATOM    322  N   GLY A  71      53.161  51.822 -36.754  1.00 61.91           N  
ANISOU  322  N   GLY A  71     9178   6337   8009   -555     84    -23       N  
ATOM    323  CA  GLY A  71      52.357  51.339 -35.654  1.00 63.71           C  
ANISOU  323  CA  GLY A  71     9487   6567   8152   -426     97    -73       C  
ATOM    324  C   GLY A  71      52.602  49.874 -35.360  1.00 64.02           C  
ANISOU  324  C   GLY A  71     9348   6752   8226   -383    105    -45       C  
ATOM    325  O   GLY A  71      52.800  49.499 -34.202  1.00 64.71           O  
ANISOU  325  O   GLY A  71     9485   6853   8247   -379     37    -66       O  
ATOM    326  N   ASN A  72      52.629  49.026 -36.395  1.00 61.35           N  
ANISOU  326  N   ASN A  72     8820   6511   7978   -350    184      5       N  
ATOM    327  CA  ASN A  72      52.778  47.601 -36.121  1.00 60.98           C  
ANISOU  327  CA  ASN A  72     8635   6576   7960   -292    202     30       C  
ATOM    328  C   ASN A  72      54.198  47.264 -35.677  1.00 64.48           C  
ANISOU  328  C   ASN A  72     8971   7083   8444   -390     80     63       C  
ATOM    329  O   ASN A  72      54.403  46.389 -34.820  1.00 69.15           O  
ANISOU  329  O   ASN A  72     9540   7723   9009   -345     34     72       O  
ATOM    330  CB  ASN A  72      52.338  46.798 -37.342  1.00 56.61           C  
ANISOU  330  CB  ASN A  72     7941   6091   7479   -225    322     61       C  
ATOM    331  CG  ASN A  72      50.832  46.806 -37.508  1.00 57.86           C  
ANISOU  331  CG  ASN A  72     8173   6220   7591   -109    423     29       C  
ATOM    332  OD1 ASN A  72      50.118  46.197 -36.717  1.00 62.75           O  
ANISOU  332  OD1 ASN A  72     8831   6853   8160    -32    457      7       O  
ATOM    333  ND2 ASN A  72      50.339  47.527 -38.502  1.00 58.37           N  
ANISOU  333  ND2 ASN A  72     8260   6249   7670    -98    468     31       N  
ATOM    334  N   VAL A  73      55.193  47.981 -36.199  1.00 66.94           N  
ANISOU  334  N   VAL A  73     9218   7397   8818   -527     21     86       N  
ATOM    335  CA  VAL A  73      56.539  47.817 -35.668  1.00 69.67           C  
ANISOU  335  CA  VAL A  73     9451   7815   9205   -630   -115    112       C  
ATOM    336  C   VAL A  73      56.581  48.197 -34.191  1.00 71.27           C  
ANISOU  336  C   VAL A  73     9824   7961   9294   -660   -254     68       C  
ATOM    337  O   VAL A  73      57.220  47.513 -33.381  1.00 73.18           O  
ANISOU  337  O   VAL A  73    10003   8276   9527   -654   -361     87       O  
ATOM    338  CB  VAL A  73      57.542  48.627 -36.510  1.00 72.73           C  
ANISOU  338  CB  VAL A  73     9736   8218   9681   -798   -140    144       C  
ATOM    339  CG1 VAL A  73      58.889  48.713 -35.810  1.00 75.32           C  
ANISOU  339  CG1 VAL A  73     9955   8619  10046   -933   -308    162       C  
ATOM    340  CG2 VAL A  73      57.704  47.975 -37.864  1.00 71.61           C  
ANISOU  340  CG2 VAL A  73     9404   8164   9640   -757     -5    194       C  
ATOM    341  N   LEU A  74      55.889  49.277 -33.807  1.00 71.40           N  
ANISOU  341  N   LEU A  74    10075   7842   9213   -681   -258      8       N  
ATOM    342  CA  LEU A  74      55.908  49.662 -32.397  1.00 72.30           C  
ANISOU  342  CA  LEU A  74    10383   7892   9196   -708   -383    -45       C  
ATOM    343  C   LEU A  74      55.187  48.634 -31.534  1.00 70.80           C  
ANISOU  343  C   LEU A  74    10246   7735   8919   -553   -342    -53       C  
ATOM    344  O   LEU A  74      55.604  48.370 -30.405  1.00 71.80           O  
ANISOU  344  O   LEU A  74    10440   7879   8961   -570   -465    -61       O  
ATOM    345  CB  LEU A  74      55.292  51.043 -32.196  1.00 71.14           C  
ANISOU  345  CB  LEU A  74    10499   7575   8956   -744   -377   -116       C  
ATOM    346  CG  LEU A  74      56.148  52.238 -32.619  1.00 72.67           C  
ANISOU  346  CG  LEU A  74    10725   7695   9192   -945   -467   -118       C  
ATOM    347  CD1 LEU A  74      55.451  53.514 -32.243  1.00 73.60           C  
ANISOU  347  CD1 LEU A  74    11153   7615   9195   -950   -462   -196       C  
ATOM    348  CD2 LEU A  74      57.542  52.174 -32.013  1.00 73.52           C  
ANISOU  348  CD2 LEU A  74    10731   7880   9323  -1119   -660   -101       C  
ATOM    349  N   VAL A  75      54.096  48.060 -32.040  1.00 67.64           N  
ANISOU  349  N   VAL A  75     9824   7343   8532   -413   -174    -48       N  
ATOM    350  CA  VAL A  75      53.421  46.990 -31.310  1.00 70.19           C  
ANISOU  350  CA  VAL A  75    10181   7702   8785   -287   -116    -43       C  
ATOM    351  C   VAL A  75      54.408  45.872 -30.999  1.00 70.60           C  
ANISOU  351  C   VAL A  75    10088   7859   8880   -293   -210     19       C  
ATOM    352  O   VAL A  75      54.529  45.410 -29.852  1.00 72.19           O  
ANISOU  352  O   VAL A  75    10384   8066   8979   -266   -288     23       O  
ATOM    353  CB  VAL A  75      52.222  46.460 -32.117  1.00 62.87           C  
ANISOU  353  CB  VAL A  75     9197   6792   7900   -169     71    -38       C  
ATOM    354  CG1 VAL A  75      51.691  45.180 -31.488  1.00 59.09           C  
ANISOU  354  CG1 VAL A  75     8717   6361   7374    -72    134    -17       C  
ATOM    355  CG2 VAL A  75      51.137  47.504 -32.200  1.00 59.96           C  
ANISOU  355  CG2 VAL A  75     8981   6328   7473   -123    155    -99       C  
ATOM    356  N   CYS A  76      55.148  45.444 -32.022  1.00 65.35           N  
ANISOU  356  N   CYS A  76     9198   7273   8358   -319   -203     72       N  
ATOM    357  CA  CYS A  76      56.094  44.352 -31.835  1.00 66.77           C  
ANISOU  357  CA  CYS A  76     9220   7552   8595   -293   -280    135       C  
ATOM    358  C   CYS A  76      57.168  44.721 -30.822  1.00 70.58           C  
ANISOU  358  C   CYS A  76     9726   8059   9031   -385   -494    140       C  
ATOM    359  O   CYS A  76      57.435  43.960 -29.887  1.00 69.72           O  
ANISOU  359  O   CYS A  76     9648   7982   8858   -327   -584    169       O  
ATOM    360  CB  CYS A  76      56.712  43.963 -33.174  1.00 64.55           C  
ANISOU  360  CB  CYS A  76     8699   7351   8475   -300   -216    180       C  
ATOM    361  SG  CYS A  76      55.512  43.255 -34.288  1.00 65.95           S  
ANISOU  361  SG  CYS A  76     8853   7513   8691   -188      4    177       S  
ATOM    362  N   VAL A  77      57.784  45.893 -30.975  1.00 73.40           N  
ANISOU  362  N   VAL A  77    10081   8396   9410   -538   -586    113       N  
ATOM    363  CA  VAL A  77      58.875  46.235 -30.066  1.00 77.81           C  
ANISOU  363  CA  VAL A  77    10637   8993   9934   -651   -810    116       C  
ATOM    364  C   VAL A  77      58.349  46.452 -28.646  1.00 76.56           C  
ANISOU  364  C   VAL A  77    10761   8752   9577   -631   -894     65       C  
ATOM    365  O   VAL A  77      59.037  46.135 -27.666  1.00 76.18           O  
ANISOU  365  O   VAL A  77    10730   8753   9463   -648  -1074     84       O  
ATOM    366  CB  VAL A  77      59.658  47.458 -30.586  1.00 80.23           C  
ANISOU  366  CB  VAL A  77    10882   9290  10313   -851   -886     99       C  
ATOM    367  CG1 VAL A  77      60.146  47.217 -32.000  1.00 79.07           C  
ANISOU  367  CG1 VAL A  77    10468   9229  10345   -867   -777    154       C  
ATOM    368  CG2 VAL A  77      58.813  48.713 -30.520  1.00 81.39           C  
ANISOU  368  CG2 VAL A  77    11291   9271  10360   -912   -836     20       C  
ATOM    369  N   ALA A  78      57.116  46.948 -28.504  1.00 71.03           N  
ANISOU  369  N   ALA A  78    10283   7931   8773   -579   -764      2       N  
ATOM    370  CA  ALA A  78      56.540  47.139 -27.182  1.00 72.57           C  
ANISOU  370  CA  ALA A  78    10757   8048   8767   -546   -806    -52       C  
ATOM    371  C   ALA A  78      56.384  45.812 -26.468  1.00 81.42           C  
ANISOU  371  C   ALA A  78    11883   9229   9822   -418   -803      1       C  
ATOM    372  O   ALA A  78      56.777  45.672 -25.302  1.00 86.42           O  
ANISOU  372  O   ALA A  78    12647   9868  10321   -433   -956      2       O  
ATOM    373  CB  ALA A  78      55.182  47.830 -27.295  1.00 67.87           C  
ANISOU  373  CB  ALA A  78    10360   7330   8097   -482   -629   -124       C  
ATOM    374  N   VAL A  79      55.827  44.817 -27.158  1.00 78.53           N  
ANISOU  374  N   VAL A  79    11392   8904   9544   -300   -637     49       N  
ATOM    375  CA  VAL A  79      55.646  43.537 -26.490  1.00 76.52           C  
ANISOU  375  CA  VAL A  79    11168   8683   9223   -186   -623    105       C  
ATOM    376  C   VAL A  79      56.989  42.835 -26.292  1.00 82.31           C  
ANISOU  376  C   VAL A  79    11740   9515  10018   -192   -811    183       C  
ATOM    377  O   VAL A  79      57.203  42.172 -25.271  1.00 82.52           O  
ANISOU  377  O   VAL A  79    11869   9553   9932   -138   -912    223       O  
ATOM    378  CB  VAL A  79      54.634  42.687 -27.273  1.00 69.91           C  
ANISOU  378  CB  VAL A  79    10262   7846   8456    -78   -396    128       C  
ATOM    379  CG1 VAL A  79      54.548  41.284 -26.708  1.00 71.38           C  
ANISOU  379  CG1 VAL A  79    10474   8053   8594     24   -379    198       C  
ATOM    380  CG2 VAL A  79      53.272  43.361 -27.244  1.00 63.60           C  
ANISOU  380  CG2 VAL A  79     9621   6966   7577    -56   -231     55       C  
ATOM    381  N   TRP A  80      57.941  43.023 -27.208  1.00 87.17           N  
ANISOU  381  N   TRP A  80    12108  10206  10805   -256   -868    207       N  
ATOM    382  CA  TRP A  80      59.194  42.281 -27.111  1.00 94.57           C  
ANISOU  382  CA  TRP A  80    12848  11258  11827   -232  -1027    285       C  
ATOM    383  C   TRP A  80      60.115  42.844 -26.035  1.00100.16           C  
ANISOU  383  C   TRP A  80    13614  12000  12442   -336  -1294    279       C  
ATOM    384  O   TRP A  80      60.748  42.079 -25.301  1.00100.96           O  
ANISOU  384  O   TRP A  80    13693  12165  12504   -268  -1447    342       O  
ATOM    385  CB  TRP A  80      59.902  42.261 -28.467  1.00 98.79           C  
ANISOU  385  CB  TRP A  80    13081  11877  12576   -261   -975    314       C  
ATOM    386  CG  TRP A  80      59.238  41.356 -29.479  1.00103.27           C  
ANISOU  386  CG  TRP A  80    13570  12435  13233   -136   -752    337       C  
ATOM    387  CD1 TRP A  80      58.332  40.361 -29.225  1.00104.00           C  
ANISOU  387  CD1 TRP A  80    13787  12472  13258     -6   -634    354       C  
ATOM    388  CD2 TRP A  80      59.420  41.376 -30.903  1.00105.32           C  
ANISOU  388  CD2 TRP A  80    13627  12737  13654   -148   -623    342       C  
ATOM    389  NE1 TRP A  80      57.945  39.760 -30.399  1.00104.04           N  
ANISOU  389  NE1 TRP A  80    13677  12480  13376     58   -454    363       N  
ATOM    390  CE2 TRP A  80      58.597  40.364 -31.443  1.00104.70           C  
ANISOU  390  CE2 TRP A  80    13565  12623  13592    -19   -443    355       C  
ATOM    391  CE3 TRP A  80      60.197  42.153 -31.773  1.00107.25           C  
ANISOU  391  CE3 TRP A  80    13687  13042  14020   -267   -636    338       C  
ATOM    392  CZ2 TRP A  80      58.532  40.107 -32.812  1.00104.73           C  
ANISOU  392  CZ2 TRP A  80    13422  12652  13721      4   -290    358       C  
ATOM    393  CZ3 TRP A  80      60.130  41.897 -33.130  1.00107.48           C  
ANISOU  393  CZ3 TRP A  80    13568  13099  14170   -238   -469    349       C  
ATOM    394  CH2 TRP A  80      59.304  40.881 -33.636  1.00106.52           C  
ANISOU  394  CH2 TRP A  80    13480  12941  14052    -99   -303    355       C  
ATOM    395  N   LYS A  81      60.203  44.166 -25.914  1.00105.08           N  
ANISOU  395  N   LYS A  81    14327  12575  13022   -499  -1364    205       N  
ATOM    396  CA  LYS A  81      61.174  44.769 -25.013  1.00110.63           C  
ANISOU  396  CA  LYS A  81    15066  13316  13652   -633  -1636    191       C  
ATOM    397  C   LYS A  81      60.655  44.960 -23.591  1.00111.56           C  
ANISOU  397  C   LYS A  81    15529  13345  13515   -624  -1726    144       C  
ATOM    398  O   LYS A  81      61.452  45.275 -22.701  1.00113.00           O  
ANISOU  398  O   LYS A  81    15767  13563  13605   -720  -1977    137       O  
ATOM    399  CB  LYS A  81      61.651  46.116 -25.577  1.00115.30           C  
ANISOU  399  CB  LYS A  81    15597  13889  14322   -844  -1685    134       C  
ATOM    400  CG  LYS A  81      62.431  46.001 -26.894  1.00119.54           C  
ANISOU  400  CG  LYS A  81    15779  14539  15101   -886  -1630    188       C  
ATOM    401  CD  LYS A  81      62.991  47.348 -27.342  1.00123.73           C  
ANISOU  401  CD  LYS A  81    16268  15049  15695  -1124  -1695    143       C  
ATOM    402  CE  LYS A  81      63.808  47.228 -28.625  1.00125.57           C  
ANISOU  402  CE  LYS A  81    16148  15406  16157  -1175  -1626    203       C  
ATOM    403  NZ  LYS A  81      64.400  48.542 -29.034  1.00127.56           N  
ANISOU  403  NZ  LYS A  81    16367  15635  16467  -1434  -1688    169       N  
ATOM    404  N   ASN A  82      59.360  44.763 -23.346  1.00111.18           N  
ANISOU  404  N   ASN A  82    15707  13191  13345   -516  -1530    111       N  
ATOM    405  CA  ASN A  82      58.765  44.979 -22.029  1.00112.71           C  
ANISOU  405  CA  ASN A  82    16246  13295  13282   -501  -1570     61       C  
ATOM    406  C   ASN A  82      58.131  43.685 -21.543  1.00107.13           C  
ANISOU  406  C   ASN A  82    15623  12594  12489   -327  -1464    128       C  
ATOM    407  O   ASN A  82      57.189  43.180 -22.161  1.00104.61           O  
ANISOU  407  O   ASN A  82    15273  12245  12229   -228  -1221    140       O  
ATOM    408  CB  ASN A  82      57.727  46.100 -22.071  1.00118.75           C  
ANISOU  408  CB  ASN A  82    17239  13922  13960   -542  -1416    -51       C  
ATOM    409  CG  ASN A  82      58.328  47.431 -22.473  1.00126.36           C  
ANISOU  409  CG  ASN A  82    18178  14846  14987   -726  -1525   -118       C  
ATOM    410  OD1 ASN A  82      58.742  48.219 -21.621  1.00132.94           O  
ANISOU  410  OD1 ASN A  82    19204  15628  15679   -849  -1707   -181       O  
ATOM    411  ND2 ASN A  82      58.383  47.688 -23.779  1.00126.84           N  
ANISOU  411  ND2 ASN A  82    18020  14923  15251   -758  -1414   -104       N  
ATOM    412  N   HIS A  83      58.628  43.169 -20.419  1.00106.16           N  
ANISOU  412  N   HIS A  83    15621  12500  12214   -300  -1650    174       N  
ATOM    413  CA  HIS A  83      58.199  41.863 -19.939  1.00 99.81           C  
ANISOU  413  CA  HIS A  83    14898  11697  11328   -144  -1574    259       C  
ATOM    414  C   HIS A  83      56.802  41.879 -19.335  1.00 88.50           C  
ANISOU  414  C   HIS A  83    13767  10155   9703    -91  -1357    212       C  
ATOM    415  O   HIS A  83      56.161  40.826 -19.270  1.00 80.26           O  
ANISOU  415  O   HIS A  83    12764   9097   8636     23  -1203    277       O  
ATOM    416  CB  HIS A  83      59.199  41.317 -18.924  1.00105.87           C  
ANISOU  416  CB  HIS A  83    15712  12530  11984   -123  -1856    335       C  
ATOM    417  CG  HIS A  83      59.187  39.825 -18.830  1.00113.12           C  
ANISOU  417  CG  HIS A  83    16595  13470  12916     45  -1815    458       C  
ATOM    418  ND1 HIS A  83      59.253  39.011 -19.941  1.00113.65           N  
ANISOU  418  ND1 HIS A  83    16400  13574  13209    136  -1683    518       N  
ATOM    419  CD2 HIS A  83      59.102  38.998 -17.761  1.00116.51           C  
ANISOU  419  CD2 HIS A  83    17244  13873  13150    138  -1882    532       C  
ATOM    420  CE1 HIS A  83      59.214  37.748 -19.559  1.00114.19           C  
ANISOU  420  CE1 HIS A  83    16531  13627  13228    278  -1674    621       C  
ATOM    421  NE2 HIS A  83      59.125  37.712 -18.242  1.00114.90           N  
ANISOU  421  NE2 HIS A  83    16911  13680  13066    282  -1794    638       N  
ATOM    422  N   HIS A  84      56.306  43.040 -18.914  1.00 90.36           N  
ANISOU  422  N   HIS A  84    14216  10312   9806   -171  -1330    101       N  
ATOM    423  CA  HIS A  84      54.940  43.113 -18.417  1.00 95.29           C  
ANISOU  423  CA  HIS A  84    15095  10847  10265   -107  -1094     50       C  
ATOM    424  C   HIS A  84      53.913  42.940 -19.531  1.00 90.44           C  
ANISOU  424  C   HIS A  84    14325  10221   9816    -44   -806     41       C  
ATOM    425  O   HIS A  84      52.748  42.652 -19.240  1.00 89.00           O  
ANISOU  425  O   HIS A  84    14280   9998   9539     29   -585     29       O  
ATOM    426  CB  HIS A  84      54.717  44.444 -17.686  1.00106.00           C  
ANISOU  426  CB  HIS A  84    16727  12114  11433   -190  -1139    -77       C  
ATOM    427  CG  HIS A  84      55.046  45.652 -18.512  1.00116.08           C  
ANISOU  427  CG  HIS A  84    17889  13361  12853   -301  -1184   -157       C  
ATOM    428  ND1 HIS A  84      54.164  46.191 -19.424  1.00117.66           N  
ANISOU  428  ND1 HIS A  84    18025  13510  13170   -271   -958   -211       N  
ATOM    429  CD2 HIS A  84      56.158  46.423 -18.566  1.00119.94           C  
ANISOU  429  CD2 HIS A  84    18323  13864  13387   -449  -1430   -187       C  
ATOM    430  CE1 HIS A  84      54.717  47.242 -20.004  1.00118.76           C  
ANISOU  430  CE1 HIS A  84    18096  13617  13410   -389  -1057   -266       C  
ATOM    431  NE2 HIS A  84      55.927  47.405 -19.500  1.00119.41           N  
ANISOU  431  NE2 HIS A  84    18179  13738  13455   -510  -1338   -255       N  
ATOM    432  N   MET A  85      54.315  43.102 -20.796  1.00 86.56           N  
ANISOU  432  N   MET A  85    13551   9773   9566    -76   -804     49       N  
ATOM    433  CA  MET A  85      53.416  42.903 -21.928  1.00 87.70           C  
ANISOU  433  CA  MET A  85    13538   9915   9867    -21   -561     46       C  
ATOM    434  C   MET A  85      53.270  41.435 -22.333  1.00 87.83           C  
ANISOU  434  C   MET A  85    13414   9981   9977     69   -466    147       C  
ATOM    435  O   MET A  85      52.481  41.133 -23.237  1.00 85.13           O  
ANISOU  435  O   MET A  85    12951   9641   9752    108   -270    146       O  
ATOM    436  CB  MET A  85      53.904  43.706 -23.137  1.00 90.90           C  
ANISOU  436  CB  MET A  85    13729  10337  10471    -98   -594     15       C  
ATOM    437  CG  MET A  85      54.128  45.185 -22.867  1.00 95.02           C  
ANISOU  437  CG  MET A  85    14392  10790  10923   -205   -694    -81       C  
ATOM    438  SD  MET A  85      52.604  46.126 -22.701  1.00 94.12           S  
ANISOU  438  SD  MET A  85    14509  10558  10694   -148   -469   -190       S  
ATOM    439  CE  MET A  85      51.928  46.033 -24.354  1.00 87.24           C  
ANISOU  439  CE  MET A  85    13377   9715  10056    -96   -267   -171       C  
ATOM    440  N   ARG A  86      53.994  40.519 -21.690  1.00 88.74           N  
ANISOU  440  N   ARG A  86    13555  10127  10036    104   -607    232       N  
ATOM    441  CA  ARG A  86      54.027  39.116 -22.101  1.00 88.70           C  
ANISOU  441  CA  ARG A  86    13428  10147  10126    192   -541    331       C  
ATOM    442  C   ARG A  86      52.739  38.428 -21.664  1.00 87.62           C  
ANISOU  442  C   ARG A  86    13464   9954   9874    246   -318    346       C  
ATOM    443  O   ARG A  86      52.647  37.869 -20.572  1.00 94.49           O  
ANISOU  443  O   ARG A  86    14546  10793  10563    278   -345    395       O  
ATOM    444  CB  ARG A  86      55.251  38.422 -21.519  1.00 92.25           C  
ANISOU  444  CB  ARG A  86    13860  10640  10550    230   -778    421       C  
ATOM    445  CG  ARG A  86      56.576  39.030 -21.946  1.00 95.53           C  
ANISOU  445  CG  ARG A  86    14063  11138  11097    167   -999    415       C  
ATOM    446  CD  ARG A  86      56.741  38.989 -23.460  1.00 97.48           C  
ANISOU  446  CD  ARG A  86    14013  11429  11595    166   -895    411       C  
ATOM    447  NE  ARG A  86      58.005  39.582 -23.894  1.00100.67           N  
ANISOU  447  NE  ARG A  86    14199  11922  12129     91  -1082    410       N  
ATOM    448  CZ  ARG A  86      59.159  38.926 -23.949  1.00105.37           C  
ANISOU  448  CZ  ARG A  86    14611  12607  12819    145  -1241    489       C  
ATOM    449  NH1 ARG A  86      59.219  37.649 -23.592  1.00110.57           N  
ANISOU  449  NH1 ARG A  86    15305  13258  13449    288  -1244    578       N  
ATOM    450  NH2 ARG A  86      60.257  39.547 -24.357  1.00105.85           N  
ANISOU  450  NH2 ARG A  86    14451  12764  13004     58  -1393    483       N  
ATOM    451  N   THR A  87      51.737  38.457 -22.540  1.00 81.92           N  
ANISOU  451  N   THR A  87    12645   9224   9255    248    -97    308       N  
ATOM    452  CA  THR A  87      50.510  37.692 -22.373  1.00 76.44           C  
ANISOU  452  CA  THR A  87    12041   8499   8505    282    130    329       C  
ATOM    453  C   THR A  87      50.186  36.967 -23.674  1.00 75.30           C  
ANISOU  453  C   THR A  87    11676   8372   8563    296    257    352       C  
ATOM    454  O   THR A  87      50.672  37.332 -24.747  1.00 76.16           O  
ANISOU  454  O   THR A  87    11579   8517   8840    283    211    328       O  
ATOM    455  CB  THR A  87      49.323  38.578 -21.973  1.00 75.82           C  
ANISOU  455  CB  THR A  87    12096   8400   8312    265    296    240       C  
ATOM    456  OG1 THR A  87      49.000  39.469 -23.046  1.00 76.85           O  
ANISOU  456  OG1 THR A  87    12056   8550   8591    247    357    164       O  
ATOM    457  CG2 THR A  87      49.652  39.391 -20.732  1.00 77.84           C  
ANISOU  457  CG2 THR A  87    12596   8624   8354    247    173    198       C  
ATOM    458  N   VAL A  88      49.332  35.946 -23.565  1.00 73.01           N  
ANISOU  458  N   VAL A  88    11444   8052   8244    312    425    397       N  
ATOM    459  CA  VAL A  88      48.898  35.188 -24.738  1.00 71.30           C  
ANISOU  459  CA  VAL A  88    11054   7841   8196    310    552    411       C  
ATOM    460  C   VAL A  88      48.173  36.095 -25.720  1.00 70.27           C  
ANISOU  460  C   VAL A  88    10769   7755   8175    278    657    322       C  
ATOM    461  O   VAL A  88      48.376  36.005 -26.942  1.00 77.42           O  
ANISOU  461  O   VAL A  88    11484   8686   9246    274    659    312       O  
ATOM    462  CB  VAL A  88      48.016  33.999 -24.302  1.00 70.36           C  
ANISOU  462  CB  VAL A  88    11060   7671   8004    301    716    470       C  
ATOM    463  CG1 VAL A  88      47.542  33.196 -25.502  1.00 66.91           C  
ANISOU  463  CG1 VAL A  88    10463   7230   7731    280    837    476       C  
ATOM    464  CG2 VAL A  88      48.781  33.116 -23.343  1.00 71.54           C  
ANISOU  464  CG2 VAL A  88    11385   7761   8036    348    597    570       C  
ATOM    465  N   THR A  89      47.312  36.976 -25.204  1.00 69.22           N  
ANISOU  465  N   THR A  89    10727   7630   7942    265    749    259       N  
ATOM    466  CA  THR A  89      46.617  37.921 -26.070  1.00 70.43           C  
ANISOU  466  CA  THR A  89    10751   7821   8189    259    834    179       C  
ATOM    467  C   THR A  89      47.613  38.774 -26.846  1.00 67.62           C  
ANISOU  467  C   THR A  89    10276   7476   7941    249    678    150       C  
ATOM    468  O   THR A  89      47.501  38.912 -28.065  1.00 65.96           O  
ANISOU  468  O   THR A  89     9891   7294   7876    242    710    133       O  
ATOM    469  CB  THR A  89      45.675  38.800 -25.248  1.00 70.13           C  
ANISOU  469  CB  THR A  89    10853   7781   8013    277    942    115       C  
ATOM    470  OG1 THR A  89      44.703  37.974 -24.609  1.00 72.54           O  
ANISOU  470  OG1 THR A  89    11241   8092   8228    271   1116    147       O  
ATOM    471  CG2 THR A  89      44.957  39.796 -26.139  1.00 70.30           C  
ANISOU  471  CG2 THR A  89    10744   7834   8133    297   1020     39       C  
ATOM    472  N   ASN A  90      48.628  39.305 -26.160  1.00 69.52           N  
ANISOU  472  N   ASN A  90    10611   7697   8108    238    503    150       N  
ATOM    473  CA  ASN A  90      49.611  40.161 -26.816  1.00 69.28           C  
ANISOU  473  CA  ASN A  90    10470   7678   8174    202    356    126       C  
ATOM    474  C   ASN A  90      50.519  39.378 -27.757  1.00 70.41           C  
ANISOU  474  C   ASN A  90    10417   7861   8476    203    290    185       C  
ATOM    475  O   ASN A  90      51.004  39.936 -28.746  1.00 69.75           O  
ANISOU  475  O   ASN A  90    10183   7802   8515    171    251    167       O  
ATOM    476  CB  ASN A  90      50.438  40.894 -25.764  1.00 68.26           C  
ANISOU  476  CB  ASN A  90    10494   7523   7918    168    177    108       C  
ATOM    477  CG  ASN A  90      49.682  42.023 -25.131  1.00 69.43           C  
ANISOU  477  CG  ASN A  90    10826   7621   7934    166    235     22       C  
ATOM    478  OD1 ASN A  90      48.509  42.235 -25.424  1.00 72.26           O  
ANISOU  478  OD1 ASN A  90    11183   7973   8299    207    416    -18       O  
ATOM    479  ND2 ASN A  90      50.345  42.761 -24.260  1.00 70.98           N  
ANISOU  479  ND2 ASN A  90    11181   7780   8008    122     78    -11       N  
ATOM    480  N   TYR A  91      50.759  38.094 -27.479  1.00 66.80           N  
ANISOU  480  N   TYR A  91     9969   7401   8011    243    287    258       N  
ATOM    481  CA  TYR A  91      51.472  37.253 -28.435  1.00 64.27           C  
ANISOU  481  CA  TYR A  91     9471   7106   7841    270    264    307       C  
ATOM    482  C   TYR A  91      50.684  37.129 -29.730  1.00 61.35           C  
ANISOU  482  C   TYR A  91     8973   6749   7590    261    421    275       C  
ATOM    483  O   TYR A  91      51.235  37.261 -30.833  1.00 64.33           O  
ANISOU  483  O   TYR A  91     9186   7160   8098    253    402    270       O  
ATOM    484  CB  TYR A  91      51.732  35.877 -27.829  1.00 69.07           C  
ANISOU  484  CB  TYR A  91    10158   7682   8404    333    246    390       C  
ATOM    485  CG  TYR A  91      52.843  35.867 -26.816  1.00 73.18           C  
ANISOU  485  CG  TYR A  91    10752   8211   8844    360     42    439       C  
ATOM    486  CD1 TYR A  91      53.979  36.644 -26.997  1.00 75.89           C  
ANISOU  486  CD1 TYR A  91    10969   8614   9250    332   -129    427       C  
ATOM    487  CD2 TYR A  91      52.756  35.085 -25.674  1.00 75.73           C  
ANISOU  487  CD2 TYR A  91    11269   8485   9020    405     15    502       C  
ATOM    488  CE1 TYR A  91      55.006  36.631 -26.071  1.00 80.53           C  
ANISOU  488  CE1 TYR A  91    11604   9228   9768    349   -338    472       C  
ATOM    489  CE2 TYR A  91      53.773  35.070 -24.739  1.00 79.32           C  
ANISOU  489  CE2 TYR A  91    11794   8955   9390    436   -194    552       C  
ATOM    490  CZ  TYR A  91      54.895  35.844 -24.939  1.00 81.44           C  
ANISOU  490  CZ  TYR A  91    11917   9297   9732    408   -378    534       C  
ATOM    491  OH  TYR A  91      55.904  35.823 -24.005  1.00 84.11           O  
ANISOU  491  OH  TYR A  91    12307   9665   9986    431   -608    584       O  
ATOM    492  N   PHE A  92      49.377  36.894 -29.614  1.00 58.19           N  
ANISOU  492  N   PHE A  92     8643   6329   7140    255    577    254       N  
ATOM    493  CA  PHE A  92      48.557  36.840 -30.815  1.00 59.01           C  
ANISOU  493  CA  PHE A  92     8623   6454   7345    238    706    219       C  
ATOM    494  C   PHE A  92      48.525  38.195 -31.520  1.00 64.29           C  
ANISOU  494  C   PHE A  92     9211   7153   8064    216    684    160       C  
ATOM    495  O   PHE A  92      48.584  38.262 -32.756  1.00 65.14           O  
ANISOU  495  O   PHE A  92     9182   7287   8282    206    707    148       O  
ATOM    496  CB  PHE A  92      47.153  36.356 -30.453  1.00 63.65           C  
ANISOU  496  CB  PHE A  92     9281   7032   7869    225    868    211       C  
ATOM    497  CG  PHE A  92      47.077  34.872 -30.143  1.00 69.91           C  
ANISOU  497  CG  PHE A  92    10139   7780   8642    225    919    274       C  
ATOM    498  CD1 PHE A  92      47.825  33.960 -30.862  1.00 71.84           C  
ANISOU  498  CD1 PHE A  92    10315   7999   8981    245    878    311       C  
ATOM    499  CD2 PHE A  92      46.272  34.400 -29.119  1.00 73.46           C  
ANISOU  499  CD2 PHE A  92    10736   8202   8972    206   1016    297       C  
ATOM    500  CE1 PHE A  92      47.761  32.608 -30.571  1.00 74.67           C  
ANISOU  500  CE1 PHE A  92    10766   8289   9318    252    924    370       C  
ATOM    501  CE2 PHE A  92      46.203  33.056 -28.835  1.00 73.10           C  
ANISOU  501  CE2 PHE A  92    10776   8095   8903    194   1065    362       C  
ATOM    502  CZ  PHE A  92      46.947  32.161 -29.555  1.00 72.46           C  
ANISOU  502  CZ  PHE A  92    10643   7972   8919    219   1013    398       C  
ATOM    503  N   ILE A  93      48.454  39.285 -30.744  1.00 65.27           N  
ANISOU  503  N   ILE A  93     9442   7261   8097    210    639    123       N  
ATOM    504  CA  ILE A  93      48.454  40.627 -31.318  1.00 64.97           C  
ANISOU  504  CA  ILE A  93     9368   7222   8094    191    611     71       C  
ATOM    505  C   ILE A  93      49.746  40.879 -32.093  1.00 62.92           C  
ANISOU  505  C   ILE A  93     8990   6981   7937    149    492     93       C  
ATOM    506  O   ILE A  93      49.732  41.475 -33.176  1.00 59.45           O  
ANISOU  506  O   ILE A  93     8457   6552   7580    128    511     74       O  
ATOM    507  CB  ILE A  93      48.229  41.672 -30.209  1.00 65.79           C  
ANISOU  507  CB  ILE A  93     9651   7282   8065    194    579     24       C  
ATOM    508  CG1 ILE A  93      46.773  41.643 -29.753  1.00 64.42           C  
ANISOU  508  CG1 ILE A  93     9552   7109   7815    246    742     -9       C  
ATOM    509  CG2 ILE A  93      48.597  43.072 -30.692  1.00 67.66           C  
ANISOU  509  CG2 ILE A  93     9887   7486   8333    161    507    -20       C  
ATOM    510  CD1 ILE A  93      46.484  42.570 -28.576  1.00 62.76           C  
ANISOU  510  CD1 ILE A  93     9545   6848   7452    271    739    -62       C  
ATOM    511  N   VAL A  94      50.878  40.407 -31.563  1.00 62.97           N  
ANISOU  511  N   VAL A  94     8990   6996   7938    140    371    137       N  
ATOM    512  CA  VAL A  94      52.143  40.550 -32.272  1.00 62.89           C  
ANISOU  512  CA  VAL A  94     8833   7026   8036    102    271    163       C  
ATOM    513  C   VAL A  94      52.105  39.773 -33.576  1.00 65.56           C  
ANISOU  513  C   VAL A  94     9018   7398   8494    129    368    184       C  
ATOM    514  O   VAL A  94      52.551  40.271 -34.618  1.00 64.78           O  
ANISOU  514  O   VAL A  94     8802   7326   8483     91    369    178       O  
ATOM    515  CB  VAL A  94      53.312  40.102 -31.379  1.00 64.57           C  
ANISOU  515  CB  VAL A  94     9050   7261   8223    106    116    212       C  
ATOM    516  CG1 VAL A  94      54.577  39.902 -32.203  1.00 58.45           C  
ANISOU  516  CG1 VAL A  94     8069   6552   7585     92     48    251       C  
ATOM    517  CG2 VAL A  94      53.549  41.133 -30.290  1.00 69.66           C  
ANISOU  517  CG2 VAL A  94     9840   7876   8752     48    -10    180       C  
ATOM    518  N   ASN A  95      51.582  38.536 -33.541  1.00 64.56           N  
ANISOU  518  N   ASN A  95     8907   7261   8363    186    453    207       N  
ATOM    519  CA  ASN A  95      51.443  37.768 -34.779  1.00 58.85           C  
ANISOU  519  CA  ASN A  95     8072   6553   7735    207    548    212       C  
ATOM    520  C   ASN A  95      50.623  38.535 -35.815  1.00 58.46           C  
ANISOU  520  C   ASN A  95     7981   6516   7715    171    630    164       C  
ATOM    521  O   ASN A  95      50.980  38.590 -37.002  1.00 58.48           O  
ANISOU  521  O   ASN A  95     7876   6546   7797    158    654    162       O  
ATOM    522  CB  ASN A  95      50.793  36.422 -34.489  1.00 57.08           C  
ANISOU  522  CB  ASN A  95     7914   6291   7481    249    632    234       C  
ATOM    523  CG  ASN A  95      50.837  35.487 -35.683  1.00 63.42           C  
ANISOU  523  CG  ASN A  95     8630   7094   8374    270    711    237       C  
ATOM    524  OD1 ASN A  95      51.898  35.248 -36.262  1.00 62.66           O  
ANISOU  524  OD1 ASN A  95     8434   7019   8353    303    673    257       O  
ATOM    525  ND2 ASN A  95      49.674  34.962 -36.068  1.00 65.70           N  
ANISOU  525  ND2 ASN A  95     8952   7360   8652    248    824    211       N  
ATOM    526  N   LEU A  96      49.517  39.131 -35.377  1.00 58.30           N  
ANISOU  526  N   LEU A  96     8049   6477   7624    165    675    128       N  
ATOM    527  CA  LEU A  96      48.666  39.901 -36.276  1.00 63.59           C  
ANISOU  527  CA  LEU A  96     8686   7160   8317    154    737     88       C  
ATOM    528  C   LEU A  96      49.439  41.071 -36.880  1.00 64.24           C  
ANISOU  528  C   LEU A  96     8731   7240   8436    115    666     84       C  
ATOM    529  O   LEU A  96      49.383  41.317 -38.092  1.00 65.15           O  
ANISOU  529  O   LEU A  96     8773   7375   8606    101    699     80       O  
ATOM    530  CB  LEU A  96      47.439  40.388 -35.507  1.00 67.71           C  
ANISOU  530  CB  LEU A  96     9304   7666   8755    179    793     52       C  
ATOM    531  CG  LEU A  96      46.322  41.117 -36.244  1.00 72.64           C  
ANISOU  531  CG  LEU A  96     9896   8309   9393    201    859     14       C  
ATOM    532  CD1 LEU A  96      45.702  40.230 -37.313  1.00 72.99           C  
ANISOU  532  CD1 LEU A  96     9832   8401   9499    192    932     17       C  
ATOM    533  CD2 LEU A  96      45.262  41.551 -35.234  1.00 72.34           C  
ANISOU  533  CD2 LEU A  96     9950   8264   9271    246    920    -19       C  
ATOM    534  N   SER A  97      50.197  41.784 -36.042  1.00 59.84           N  
ANISOU  534  N   SER A  97     8237   6658   7842     84    564     86       N  
ATOM    535  CA  SER A  97      50.999  42.905 -36.521  1.00 61.15           C  
ANISOU  535  CA  SER A  97     8380   6813   8043     17    492     86       C  
ATOM    536  C   SER A  97      52.084  42.454 -37.485  1.00 61.88           C  
ANISOU  536  C   SER A  97     8317   6960   8235    -17    482    126       C  
ATOM    537  O   SER A  97      52.452  43.206 -38.391  1.00 60.79           O  
ANISOU  537  O   SER A  97     8133   6825   8141    -73    484    130       O  
ATOM    538  CB  SER A  97      51.616  43.658 -35.340  1.00 60.80           C  
ANISOU  538  CB  SER A  97     8441   6729   7933    -31    371     75       C  
ATOM    539  OG  SER A  97      50.600  44.288 -34.584  1.00 65.72           O  
ANISOU  539  OG  SER A  97     9225   7292   8456      6    399     27       O  
ATOM    540  N   LEU A  98      52.615  41.241 -37.302  1.00 60.35           N  
ANISOU  540  N   LEU A  98     8051   6805   8074     23    480    158       N  
ATOM    541  CA  LEU A  98      53.630  40.732 -38.219  1.00 65.34           C  
ANISOU  541  CA  LEU A  98     8530   7494   8803     19    493    191       C  
ATOM    542  C   LEU A  98      53.027  40.465 -39.595  1.00 63.41           C  
ANISOU  542  C   LEU A  98     8245   7258   8589     34    615    177       C  
ATOM    543  O   LEU A  98      53.592  40.865 -40.620  1.00 62.24           O  
ANISOU  543  O   LEU A  98     8016   7142   8492     -7    641    187       O  
ATOM    544  CB  LEU A  98      54.275  39.461 -37.658  1.00 68.52           C  
ANISOU  544  CB  LEU A  98     8885   7921   9228     90    464    228       C  
ATOM    545  CG  LEU A  98      55.255  39.605 -36.490  1.00 72.39           C  
ANISOU  545  CG  LEU A  98     9369   8433   9704     78    314    259       C  
ATOM    546  CD1 LEU A  98      55.741  38.226 -36.028  1.00 74.25           C  
ANISOU  546  CD1 LEU A  98     9573   8681   9956    182    293    304       C  
ATOM    547  CD2 LEU A  98      56.428  40.491 -36.847  1.00 70.69           C  
ANISOU  547  CD2 LEU A  98     9025   8277   9559    -13    235    273       C  
ATOM    548  N   ALA A  99      51.873  39.787 -39.627  1.00 59.32           N  
ANISOU  548  N   ALA A  99     7787   6716   8034     84    689    153       N  
ATOM    549  CA  ALA A  99      51.168  39.584 -40.893  1.00 57.41           C  
ANISOU  549  CA  ALA A  99     7523   6484   7806     87    782    132       C  
ATOM    550  C   ALA A  99      50.890  40.914 -41.581  1.00 64.23           C  
ANISOU  550  C   ALA A  99     8405   7344   8657     41    776    121       C  
ATOM    551  O   ALA A  99      51.080  41.056 -42.802  1.00 69.02           O  
ANISOU  551  O   ALA A  99     8967   7973   9287     20    819    126       O  
ATOM    552  CB  ALA A  99      49.858  38.832 -40.651  1.00 49.11           C  
ANISOU  552  CB  ALA A  99     6532   5414   6713    120    842    106       C  
ATOM    553  N   ASP A 100      50.460  41.906 -40.799  1.00 59.64           N  
ANISOU  553  N   ASP A 100     7909   6724   8029     30    725    108       N  
ATOM    554  CA  ASP A 100      50.142  43.212 -41.353  1.00 61.86           C  
ANISOU  554  CA  ASP A 100     8240   6973   8290      2    715    100       C  
ATOM    555  C   ASP A 100      51.382  43.906 -41.910  1.00 61.40           C  
ANISOU  555  C   ASP A 100     8140   6917   8272    -82    679    133       C  
ATOM    556  O   ASP A 100      51.325  44.506 -42.987  1.00 62.91           O  
ANISOU  556  O   ASP A 100     8337   7101   8465   -111    710    146       O  
ATOM    557  CB  ASP A 100      49.441  44.058 -40.292  1.00 59.74           C  
ANISOU  557  CB  ASP A 100     8092   6648   7958     27    677     71       C  
ATOM    558  CG  ASP A 100      47.995  43.678 -40.154  1.00 57.21           C  
ANISOU  558  CG  ASP A 100     7792   6341   7604    105    743     41       C  
ATOM    559  OD1 ASP A 100      47.588  42.709 -40.843  1.00 59.01           O  
ANISOU  559  OD1 ASP A 100     7944   6620   7859    119    800     43       O  
ATOM    560  OD2 ASP A 100      47.256  44.312 -39.381  1.00 58.31           O  
ANISOU  560  OD2 ASP A 100     8020   6444   7689    149    742     13       O  
ATOM    561  N   VAL A 101      52.517  43.811 -41.209  1.00 61.31           N  
ANISOU  561  N   VAL A 101     8081   6922   8292   -127    614    153       N  
ATOM    562  CA  VAL A 101      53.765  44.380 -41.715  1.00 64.36           C  
ANISOU  562  CA  VAL A 101     8390   7333   8732   -226    587    188       C  
ATOM    563  C   VAL A 101      54.174  43.691 -43.010  1.00 67.31           C  
ANISOU  563  C   VAL A 101     8646   7772   9157   -216    684    211       C  
ATOM    564  O   VAL A 101      54.656  44.332 -43.955  1.00 70.36           O  
ANISOU  564  O   VAL A 101     9006   8168   9561   -289    720    237       O  
ATOM    565  CB  VAL A 101      54.861  44.265 -40.640  1.00 64.28           C  
ANISOU  565  CB  VAL A 101     8322   7352   8751   -269    482    204       C  
ATOM    566  CG1 VAL A 101      56.215  44.599 -41.228  1.00 66.04           C  
ANISOU  566  CG1 VAL A 101     8403   7635   9053   -372    469    245       C  
ATOM    567  CG2 VAL A 101      54.563  45.196 -39.490  1.00 64.57           C  
ANISOU  567  CG2 VAL A 101     8507   7310   8716   -306    383    175       C  
ATOM    568  N   LEU A 102      53.978  42.375 -43.073  1.00 65.70           N  
ANISOU  568  N   LEU A 102     8391   7604   8968   -128    736    202       N  
ATOM    569  CA  LEU A 102      54.299  41.622 -44.274  1.00 64.08           C  
ANISOU  569  CA  LEU A 102     8104   7448   8796   -103    838    210       C  
ATOM    570  C   LEU A 102      53.529  42.156 -45.476  1.00 62.78           C  
ANISOU  570  C   LEU A 102     8009   7264   8582   -123    901    200       C  
ATOM    571  O   LEU A 102      54.119  42.450 -46.523  1.00 61.67           O  
ANISOU  571  O   LEU A 102     7829   7153   8451   -170    961    223       O  
ATOM    572  CB  LEU A 102      53.991  40.140 -44.052  1.00 64.54           C  
ANISOU  572  CB  LEU A 102     8150   7511   8860     -3    878    191       C  
ATOM    573  CG  LEU A 102      54.245  39.220 -45.252  1.00 64.43           C  
ANISOU  573  CG  LEU A 102     8086   7529   8867     39    989    183       C  
ATOM    574  CD1 LEU A 102      55.712  39.286 -45.645  1.00 61.58           C  
ANISOU  574  CD1 LEU A 102     7584   7236   8577     23   1018    219       C  
ATOM    575  CD2 LEU A 102      53.854  37.780 -44.897  1.00 69.67           C  
ANISOU  575  CD2 LEU A 102     8780   8162   9529    129   1017    160       C  
ATOM    576  N   VAL A 103      52.204  42.286 -45.347  1.00 63.96           N  
ANISOU  576  N   VAL A 103     8258   7370   8672    -85    889    169       N  
ATOM    577  CA  VAL A 103      51.425  42.749 -46.500  1.00 65.61           C  
ANISOU  577  CA  VAL A 103     8529   7570   8830    -88    926    164       C  
ATOM    578  C   VAL A 103      51.686  44.216 -46.787  1.00 66.56           C  
ANISOU  578  C   VAL A 103     8712   7648   8931   -157    893    198       C  
ATOM    579  O   VAL A 103      51.523  44.665 -47.923  1.00 68.15           O  
ANISOU  579  O   VAL A 103     8956   7846   9092   -178    929    217       O  
ATOM    580  CB  VAL A 103      49.912  42.521 -46.328  1.00 67.59           C  
ANISOU  580  CB  VAL A 103     8840   7807   9036    -25    915    126       C  
ATOM    581  CG1 VAL A 103      49.527  41.166 -46.842  1.00 70.29           C  
ANISOU  581  CG1 VAL A 103     9147   8184   9376      7    974     97       C  
ATOM    582  CG2 VAL A 103      49.474  42.744 -44.893  1.00 68.04           C  
ANISOU  582  CG2 VAL A 103     8931   7830   9090      3    860    111       C  
ATOM    583  N   THR A 104      52.035  44.997 -45.766  1.00 63.19           N  
ANISOU  583  N   THR A 104     8316   7176   8517   -197    820    204       N  
ATOM    584  CA  THR A 104      52.295  46.412 -45.980  1.00 63.04           C  
ANISOU  584  CA  THR A 104     8386   7091   8477   -276    785    234       C  
ATOM    585  C   THR A 104      53.560  46.599 -46.805  1.00 64.38           C  
ANISOU  585  C   THR A 104     8479   7299   8685   -384    833    282       C  
ATOM    586  O   THR A 104      53.626  47.485 -47.664  1.00 64.75           O  
ANISOU  586  O   THR A 104     8602   7305   8697   -447    858    318       O  
ATOM    587  CB  THR A 104      52.413  47.124 -44.626  1.00 61.73           C  
ANISOU  587  CB  THR A 104     8287   6858   8309   -304    691    217       C  
ATOM    588  OG1 THR A 104      51.160  47.057 -43.943  1.00 60.03           O  
ANISOU  588  OG1 THR A 104     8152   6609   8047   -197    673    173       O  
ATOM    589  CG2 THR A 104      52.825  48.572 -44.793  1.00 61.12           C  
ANISOU  589  CG2 THR A 104     8319   6689   8213   -409    651    245       C  
ATOM    590  N   ILE A 105      54.568  45.756 -46.572  1.00 63.76           N  
ANISOU  590  N   ILE A 105     8249   7302   8675   -400    855    288       N  
ATOM    591  CA  ILE A 105      55.826  45.913 -47.293  1.00 66.31           C  
ANISOU  591  CA  ILE A 105     8464   7685   9047   -500    916    334       C  
ATOM    592  C   ILE A 105      55.773  45.236 -48.662  1.00 65.55           C  
ANISOU  592  C   ILE A 105     8338   7642   8925   -458   1046    340       C  
ATOM    593  O   ILE A 105      56.253  45.792 -49.650  1.00 65.15           O  
ANISOU  593  O   ILE A 105     8297   7602   8856   -540   1119    382       O  
ATOM    594  CB  ILE A 105      56.983  45.383 -46.430  1.00 70.64           C  
ANISOU  594  CB  ILE A 105     8844   8310   9687   -523    874    341       C  
ATOM    595  CG1 ILE A 105      57.187  46.282 -45.210  1.00 74.26           C  
ANISOU  595  CG1 ILE A 105     9354   8710  10149   -606    735    338       C  
ATOM    596  CG2 ILE A 105      58.258  45.313 -47.220  1.00 71.57           C  
ANISOU  596  CG2 ILE A 105     8800   8522   9870   -601    962    386       C  
ATOM    597  CD1 ILE A 105      58.287  45.787 -44.295  1.00 77.57           C  
ANISOU  597  CD1 ILE A 105     9610   9214  10649   -627    660    348       C  
ATOM    598  N   THR A 106      55.182  44.044 -48.764  1.00 65.63           N  
ANISOU  598  N   THR A 106     8335   7680   8924   -341   1081    299       N  
ATOM    599  CA  THR A 106      55.326  43.250 -49.984  1.00 63.36           C  
ANISOU  599  CA  THR A 106     8019   7445   8612   -303   1204    293       C  
ATOM    600  C   THR A 106      54.126  43.295 -50.919  1.00 66.71           C  
ANISOU  600  C   THR A 106     8583   7832   8932   -268   1223    272       C  
ATOM    601  O   THR A 106      54.257  42.870 -52.075  1.00 70.76           O  
ANISOU  601  O   THR A 106     9110   8378   9397   -261   1321    270       O  
ATOM    602  CB  THR A 106      55.594  41.776 -49.639  1.00 58.22           C  
ANISOU  602  CB  THR A 106     7270   6839   8012   -202   1239    258       C  
ATOM    603  OG1 THR A 106      54.473  41.238 -48.915  1.00 57.84           O  
ANISOU  603  OG1 THR A 106     7295   6742   7940   -130   1172    215       O  
ATOM    604  CG2 THR A 106      56.861  41.631 -48.820  1.00 53.24           C  
ANISOU  604  CG2 THR A 106     6480   6264   7486   -215   1214    285       C  
ATOM    605  N   CYS A 107      52.966  43.750 -50.457  1.00 60.65           N  
ANISOU  605  N   CYS A 107     7913   7005   8125   -238   1132    255       N  
ATOM    606  CA  CYS A 107      51.740  43.650 -51.244  1.00 59.24           C  
ANISOU  606  CA  CYS A 107     7836   6814   7861   -189   1127    232       C  
ATOM    607  C   CYS A 107      51.065  44.983 -51.503  1.00 62.54           C  
ANISOU  607  C   CYS A 107     8376   7169   8216   -206   1064    266       C  
ATOM    608  O   CYS A 107      50.508  45.193 -52.586  1.00 68.03           O  
ANISOU  608  O   CYS A 107     9156   7864   8827   -194   1073    278       O  
ATOM    609  CB  CYS A 107      50.734  42.725 -50.553  1.00 59.50           C  
ANISOU  609  CB  CYS A 107     7853   6851   7904   -110   1086    175       C  
ATOM    610  SG  CYS A 107      51.247  41.049 -50.440  1.00 59.92           S  
ANISOU  610  SG  CYS A 107     7820   6943   8003    -71   1159    135       S  
ATOM    611  N   LEU A 108      51.089  45.884 -50.533  1.00 59.26           N  
ANISOU  611  N   LEU A 108     7990   6694   7834   -224    993    280       N  
ATOM    612  CA  LEU A 108      50.415  47.165 -50.698  1.00 57.62           C  
ANISOU  612  CA  LEU A 108     7920   6403   7568   -216    932    309       C  
ATOM    613  C   LEU A 108      50.947  47.952 -51.893  1.00 59.19           C  
ANISOU  613  C   LEU A 108     8208   6573   7708   -295    977    374       C  
ATOM    614  O   LEU A 108      50.129  48.430 -52.701  1.00 60.05           O  
ANISOU  614  O   LEU A 108     8432   6651   7732   -248    951    397       O  
ATOM    615  CB  LEU A 108      50.527  47.950 -49.388  1.00 53.34           C  
ANISOU  615  CB  LEU A 108     7412   5786   7068   -230    861    303       C  
ATOM    616  CG  LEU A 108      49.967  49.357 -49.355  1.00 53.62           C  
ANISOU  616  CG  LEU A 108     7613   5706   7055   -214    800    328       C  
ATOM    617  CD1 LEU A 108      49.654  49.666 -47.939  1.00 56.91           C  
ANISOU  617  CD1 LEU A 108     8057   6070   7498   -174    738    286       C  
ATOM    618  CD2 LEU A 108      50.984  50.370 -49.888  1.00 54.07           C  
ANISOU  618  CD2 LEU A 108     7753   5693   7099   -350    818    394       C  
ATOM    619  N   PRO A 109      52.266  48.129 -52.074  1.00 56.78           N  
ANISOU  619  N   PRO A 109     7854   6282   7439   -414   1043    413       N  
ATOM    620  CA  PRO A 109      52.732  48.899 -53.243  1.00 61.50           C  
ANISOU  620  CA  PRO A 109     8550   6850   7967   -503   1104    483       C  
ATOM    621  C   PRO A 109      52.278  48.305 -54.563  1.00 63.93           C  
ANISOU  621  C   PRO A 109     8901   7212   8177   -452   1165    484       C  
ATOM    622  O   PRO A 109      51.840  49.044 -55.456  1.00 67.56           O  
ANISOU  622  O   PRO A 109     9517   7619   8534   -454   1154    534       O  
ATOM    623  CB  PRO A 109      54.261  48.863 -53.097  1.00 61.07           C  
ANISOU  623  CB  PRO A 109     8369   6844   7991   -638   1183    511       C  
ATOM    624  CG  PRO A 109      54.506  48.566 -51.639  1.00 59.35           C  
ANISOU  624  CG  PRO A 109     8036   6636   7876   -626   1107    466       C  
ATOM    625  CD  PRO A 109      53.394  47.664 -51.241  1.00 54.26           C  
ANISOU  625  CD  PRO A 109     7381   6013   7221   -475   1063    401       C  
ATOM    626  N   ALA A 110      52.350  46.979 -54.700  1.00 63.44           N  
ANISOU  626  N   ALA A 110     8724   7244   8135   -403   1222    429       N  
ATOM    627  CA  ALA A 110      51.903  46.327 -55.926  1.00 62.04           C  
ANISOU  627  CA  ALA A 110     8604   7114   7854   -361   1273    414       C  
ATOM    628  C   ALA A 110      50.422  46.569 -56.168  1.00 61.02           C  
ANISOU  628  C   ALA A 110     8585   6953   7645   -272   1158    401       C  
ATOM    629  O   ALA A 110      50.003  46.834 -57.301  1.00 63.83           O  
ANISOU  629  O   ALA A 110     9066   7307   7879   -265   1154    430       O  
ATOM    630  CB  ALA A 110      52.187  44.828 -55.853  1.00 60.88           C  
ANISOU  630  CB  ALA A 110     8333   7048   7752   -317   1343    345       C  
ATOM    631  N   THR A 111      49.615  46.468 -55.114  1.00 57.11           N  
ANISOU  631  N   THR A 111     8040   6445   7214   -200   1063    359       N  
ATOM    632  CA  THR A 111      48.179  46.665 -55.256  1.00 58.45           C  
ANISOU  632  CA  THR A 111     8269   6609   7330   -105    956    345       C  
ATOM    633  C   THR A 111      47.861  48.100 -55.665  1.00 62.25           C  
ANISOU  633  C   THR A 111     8907   7004   7742    -91    894    419       C  
ATOM    634  O   THR A 111      46.987  48.330 -56.509  1.00 62.01           O  
ANISOU  634  O   THR A 111     8965   6981   7615    -30    830    438       O  
ATOM    635  CB  THR A 111      47.489  46.304 -53.945  1.00 57.69           C  
ANISOU  635  CB  THR A 111     8075   6521   7324    -39    897    290       C  
ATOM    636  OG1 THR A 111      47.724  44.921 -53.660  1.00 58.94           O  
ANISOU  636  OG1 THR A 111     8119   6744   7531    -50    951    230       O  
ATOM    637  CG2 THR A 111      45.997  46.574 -54.025  1.00 57.94           C  
ANISOU  637  CG2 THR A 111     8133   6565   7317     64    794    278       C  
ATOM    638  N   LEU A 112      48.567  49.076 -55.083  1.00 61.07           N  
ANISOU  638  N   LEU A 112     8802   6765   7635   -150    903    462       N  
ATOM    639  CA  LEU A 112      48.388  50.461 -55.500  1.00 61.60           C  
ANISOU  639  CA  LEU A 112     9052   6720   7633   -148    856    539       C  
ATOM    640  C   LEU A 112      48.730  50.628 -56.979  1.00 63.70           C  
ANISOU  640  C   LEU A 112     9436   6991   7775   -206    912    604       C  
ATOM    641  O   LEU A 112      47.978  51.254 -57.737  1.00 64.37           O  
ANISOU  641  O   LEU A 112     9671   7032   7754   -139    842    653       O  
ATOM    642  CB  LEU A 112      49.246  51.381 -54.636  1.00 59.88           C  
ANISOU  642  CB  LEU A 112     8872   6397   7483   -239    866    566       C  
ATOM    643  CG  LEU A 112      49.317  52.827 -55.141  1.00 62.33           C  
ANISOU  643  CG  LEU A 112     9404   6562   7718   -276    840    655       C  
ATOM    644  CD1 LEU A 112      47.925  53.417 -55.244  1.00 64.70           C  
ANISOU  644  CD1 LEU A 112     9824   6800   7958   -102    727    663       C  
ATOM    645  CD2 LEU A 112      50.184  53.677 -54.220  1.00 62.12           C  
ANISOU  645  CD2 LEU A 112     9418   6425   7761   -394    843    669       C  
ATOM    646  N   VAL A 113      49.857  50.053 -57.412  1.00 62.59           N  
ANISOU  646  N   VAL A 113     9232   6910   7639   -319   1040    608       N  
ATOM    647  CA  VAL A 113      50.292  50.245 -58.791  1.00 64.06           C  
ANISOU  647  CA  VAL A 113     9542   7101   7696   -387   1122    672       C  
ATOM    648  C   VAL A 113      49.289  49.630 -59.758  1.00 63.93           C  
ANISOU  648  C   VAL A 113     9585   7148   7557   -291   1070    647       C  
ATOM    649  O   VAL A 113      48.928  50.241 -60.772  1.00 66.64           O  
ANISOU  649  O   VAL A 113    10109   7453   7757   -278   1038    714       O  
ATOM    650  CB  VAL A 113      51.708  49.676 -58.997  1.00 69.76           C  
ANISOU  650  CB  VAL A 113    10154   7893   8460   -513   1290    671       C  
ATOM    651  CG1 VAL A 113      52.039  49.624 -60.472  1.00 71.78           C  
ANISOU  651  CG1 VAL A 113    10531   8178   8562   -563   1398    720       C  
ATOM    652  CG2 VAL A 113      52.731  50.545 -58.269  1.00 70.51           C  
ANISOU  652  CG2 VAL A 113    10217   7922   8650   -641   1324    719       C  
ATOM    653  N   VAL A 114      48.807  48.428 -59.448  1.00 62.08           N  
ANISOU  653  N   VAL A 114     9212   7006   7369   -229   1050    554       N  
ATOM    654  CA  VAL A 114      47.836  47.760 -60.312  1.00 65.30           C  
ANISOU  654  CA  VAL A 114     9664   7481   7667   -160    986    517       C  
ATOM    655  C   VAL A 114      46.518  48.517 -60.327  1.00 67.31           C  
ANISOU  655  C   VAL A 114     9995   7702   7877    -49    815    546       C  
ATOM    656  O   VAL A 114      45.868  48.636 -61.374  1.00 67.07           O  
ANISOU  656  O   VAL A 114    10084   7692   7705     -9    742    574       O  
ATOM    657  CB  VAL A 114      47.629  46.304 -59.859  1.00 67.68           C  
ANISOU  657  CB  VAL A 114     9804   7870   8042   -139   1003    409       C  
ATOM    658  CG1 VAL A 114      46.526  45.636 -60.683  1.00 64.83           C  
ANISOU  658  CG1 VAL A 114     9488   7574   7571    -89    912    362       C  
ATOM    659  CG2 VAL A 114      48.927  45.534 -59.964  1.00 70.84           C  
ANISOU  659  CG2 VAL A 114    10139   8302   8476   -216   1173    384       C  
ATOM    660  N   ASP A 115      46.079  49.017 -59.166  1.00 66.36           N  
ANISOU  660  N   ASP A 115     9806   7537   7872     15    746    538       N  
ATOM    661  CA  ASP A 115      44.828  49.759 -59.141  1.00 65.98           C  
ANISOU  661  CA  ASP A 115     9814   7462   7794    148    595    565       C  
ATOM    662  C   ASP A 115      44.934  51.067 -59.918  1.00 64.43           C  
ANISOU  662  C   ASP A 115     9843   7153   7482    159    562    677       C  
ATOM    663  O   ASP A 115      43.947  51.510 -60.515  1.00 68.77           O  
ANISOU  663  O   ASP A 115    10482   7703   7943    272    436    715       O  
ATOM    664  CB  ASP A 115      44.416  49.995 -57.700  1.00 66.58           C  
ANISOU  664  CB  ASP A 115     9779   7509   8011    219    558    526       C  
ATOM    665  CG  ASP A 115      44.018  48.716 -57.019  1.00 70.92           C  
ANISOU  665  CG  ASP A 115    10129   8168   8649    226    569    428       C  
ATOM    666  OD1 ASP A 115      44.011  47.680 -57.718  1.00 73.66           O  
ANISOU  666  OD1 ASP A 115    10437   8603   8949    180    592    389       O  
ATOM    667  OD2 ASP A 115      43.707  48.735 -55.812  1.00 68.79           O  
ANISOU  667  OD2 ASP A 115     9763   7890   8484    274    558    389       O  
ATOM    668  N   ILE A 116      46.117  51.676 -59.954  1.00 59.85           N  
ANISOU  668  N   ILE A 116     9359   6482   6901     40    670    734       N  
ATOM    669  CA  ILE A 116      46.296  52.895 -60.737  1.00 64.18           C  
ANISOU  669  CA  ILE A 116    10150   6907   7329     24    656    850       C  
ATOM    670  C   ILE A 116      46.363  52.582 -62.230  1.00 68.49           C  
ANISOU  670  C   ILE A 116    10819   7508   7697    -13    682    893       C  
ATOM    671  O   ILE A 116      45.684  53.217 -63.046  1.00 73.92           O  
ANISOU  671  O   ILE A 116    11686   8153   8249     68    579    966       O  
ATOM    672  CB  ILE A 116      47.559  53.638 -60.275  1.00 67.26           C  
ANISOU  672  CB  ILE A 116    10595   7182   7777   -126    769    898       C  
ATOM    673  CG1 ILE A 116      47.354  54.258 -58.900  1.00 67.42           C  
ANISOU  673  CG1 ILE A 116    10578   7108   7929    -76    710    869       C  
ATOM    674  CG2 ILE A 116      47.949  54.706 -61.301  1.00 71.77           C  
ANISOU  674  CG2 ILE A 116    11431   7633   8205   -194    797   1024       C  
ATOM    675  CD1 ILE A 116      48.604  54.947 -58.410  1.00 69.59           C  
ANISOU  675  CD1 ILE A 116    10901   7278   8263   -247    800    906       C  
ATOM    676  N   THR A 117      47.196  51.609 -62.612  1.00 68.66           N  
ANISOU  676  N   THR A 117    10760   7621   7707   -126    821    849       N  
ATOM    677  CA  THR A 117      47.538  51.375 -64.011  1.00 70.00           C  
ANISOU  677  CA  THR A 117    11075   7828   7694   -189    892    889       C  
ATOM    678  C   THR A 117      46.695  50.307 -64.685  1.00 71.64           C  
ANISOU  678  C   THR A 117    11253   8159   7809   -119    816    816       C  
ATOM    679  O   THR A 117      46.642  50.285 -65.917  1.00 73.91           O  
ANISOU  679  O   THR A 117    11713   8465   7906   -136    819    855       O  
ATOM    680  CB  THR A 117      49.007  50.957 -64.143  1.00 68.83           C  
ANISOU  680  CB  THR A 117    10871   7709   7573   -348   1112    884       C  
ATOM    681  OG1 THR A 117      49.203  49.694 -63.484  1.00 65.50           O  
ANISOU  681  OG1 THR A 117    10218   7391   7279   -342   1163    767       O  
ATOM    682  CG2 THR A 117      49.925  52.008 -63.521  1.00 67.31           C  
ANISOU  682  CG2 THR A 117    10699   7405   7471   -455   1185    958       C  
ATOM    683  N   GLU A 118      46.061  49.418 -63.920  1.00 74.08           N  
ANISOU  683  N   GLU A 118    11361   8548   8237    -57    750    710       N  
ATOM    684  CA  GLU A 118      45.291  48.294 -64.446  1.00 77.02           C  
ANISOU  684  CA  GLU A 118    11687   9035   8542    -23    679    625       C  
ATOM    685  C   GLU A 118      46.160  47.333 -65.242  1.00 76.84           C  
ANISOU  685  C   GLU A 118    11703   9064   8429   -123    839    579       C  
ATOM    686  O   GLU A 118      45.651  46.570 -66.068  1.00 77.44           O  
ANISOU  686  O   GLU A 118    11837   9209   8378   -117    789    525       O  
ATOM    687  CB  GLU A 118      44.114  48.766 -65.306  1.00 84.20           C  
ANISOU  687  CB  GLU A 118    12732   9961   9299     73    488    673       C  
ATOM    688  CG  GLU A 118      43.167  49.709 -64.598  1.00 92.34           C  
ANISOU  688  CG  GLU A 118    13724  10948  10414    208    330    717       C  
ATOM    689  CD  GLU A 118      41.841  49.854 -65.322  1.00100.83           C  
ANISOU  689  CD  GLU A 118    14851  12087  11372    327    116    738       C  
ATOM    690  OE1 GLU A 118      41.269  48.819 -65.730  1.00103.06           O  
ANISOU  690  OE1 GLU A 118    15055  12492  11611    310     49    656       O  
ATOM    691  OE2 GLU A 118      41.372  51.000 -65.490  1.00103.99           O  
ANISOU  691  OE2 GLU A 118    15374  12412  11724    437      6    836       O  
ATOM    692  N   THR A 119      47.470  47.344 -65.009  1.00 74.02           N  
ANISOU  692  N   THR A 119    11314   8678   8134   -213   1030    594       N  
ATOM    693  CA  THR A 119      48.373  46.443 -65.706  1.00 77.52           C  
ANISOU  693  CA  THR A 119    11777   9171   8505   -286   1209    548       C  
ATOM    694  C   THR A 119      49.380  45.882 -64.714  1.00 73.92           C  
ANISOU  694  C   THR A 119    11117   8730   8240   -326   1352    500       C  
ATOM    695  O   THR A 119      49.703  46.517 -63.706  1.00 72.60           O  
ANISOU  695  O   THR A 119    10847   8516   8220   -338   1345    537       O  
ATOM    696  CB  THR A 119      49.096  47.136 -66.878  1.00 82.23           C  
ANISOU  696  CB  THR A 119    12588   9736   8920   -361   1327    645       C  
ATOM    697  OG1 THR A 119      49.634  48.390 -66.448  1.00 84.02           O  
ANISOU  697  OG1 THR A 119    12839   9874   9213   -411   1357    754       O  
ATOM    698  CG2 THR A 119      48.132  47.376 -68.034  1.00 85.02           C  
ANISOU  698  CG2 THR A 119    13164  10093   9045   -316   1187    678       C  
ATOM    699  N   TRP A 120      49.861  44.677 -65.008  1.00 68.77           N  
ANISOU  699  N   TRP A 120    10417   8136   7575   -337   1474    415       N  
ATOM    700  CA  TRP A 120      50.817  43.979 -64.161  1.00 67.55           C  
ANISOU  700  CA  TRP A 120    10071   8004   7590   -349   1606    366       C  
ATOM    701  C   TRP A 120      52.197  44.090 -64.788  1.00 67.00           C  
ANISOU  701  C   TRP A 120    10020   7956   7480   -421   1830    408       C  
ATOM    702  O   TRP A 120      52.444  43.522 -65.857  1.00 71.70           O  
ANISOU  702  O   TRP A 120    10730   8586   7926   -426   1944    377       O  
ATOM    703  CB  TRP A 120      50.426  42.510 -63.984  1.00 64.86           C  
ANISOU  703  CB  TRP A 120     9663   7701   7279   -295   1597    242       C  
ATOM    704  CG  TRP A 120      51.297  41.766 -63.023  1.00 65.26           C  
ANISOU  704  CG  TRP A 120     9524   7765   7508   -280   1703    197       C  
ATOM    705  CD1 TRP A 120      52.340  40.944 -63.326  1.00 66.16           C  
ANISOU  705  CD1 TRP A 120     9598   7909   7629   -273   1890    157       C  
ATOM    706  CD2 TRP A 120      51.207  41.792 -61.591  1.00 66.11           C  
ANISOU  706  CD2 TRP A 120     9460   7856   7803   -255   1627    193       C  
ATOM    707  NE1 TRP A 120      52.900  40.445 -62.175  1.00 67.07           N  
ANISOU  707  NE1 TRP A 120     9522   8029   7932   -239   1919    133       N  
ATOM    708  CE2 TRP A 120      52.230  40.955 -61.095  1.00 64.88           C  
ANISOU  708  CE2 TRP A 120     9169   7723   7760   -236   1758    155       C  
ATOM    709  CE3 TRP A 120      50.354  42.435 -60.682  1.00 65.00           C  
ANISOU  709  CE3 TRP A 120     9274   7685   7738   -236   1464    216       C  
ATOM    710  CZ2 TRP A 120      52.427  40.746 -59.729  1.00 63.89           C  
ANISOU  710  CZ2 TRP A 120     8877   7589   7809   -208   1715    146       C  
ATOM    711  CZ3 TRP A 120      50.547  42.225 -59.329  1.00 63.34           C  
ANISOU  711  CZ3 TRP A 120     8906   7465   7695   -215   1441    199       C  
ATOM    712  CH2 TRP A 120      51.577  41.389 -58.864  1.00 63.51           C  
ANISOU  712  CH2 TRP A 120     8807   7507   7815   -206   1558    167       C  
ATOM    713  N   PHE A 121      53.098  44.784 -64.107  1.00 64.86           N  
ANISOU  713  N   PHE A 121     9631   7671   7340   -482   1897    473       N  
ATOM    714  CA  PHE A 121      54.442  45.011 -64.607  1.00 66.97           C  
ANISOU  714  CA  PHE A 121     9876   7976   7595   -569   2113    527       C  
ATOM    715  C   PHE A 121      55.474  44.068 -64.023  1.00 63.77           C  
ANISOU  715  C   PHE A 121     9244   7642   7345   -547   2253    468       C  
ATOM    716  O   PHE A 121      56.622  44.086 -64.476  1.00 67.28           O  
ANISOU  716  O   PHE A 121     9632   8143   7787   -604   2453    500       O  
ATOM    717  CB  PHE A 121      54.887  46.442 -64.301  1.00 73.56           C  
ANISOU  717  CB  PHE A 121    10723   8753   8475   -680   2103    644       C  
ATOM    718  CG  PHE A 121      54.059  47.481 -64.960  1.00 80.90           C  
ANISOU  718  CG  PHE A 121    11896   9598   9245   -696   1991    724       C  
ATOM    719  CD1 PHE A 121      54.200  47.729 -66.313  1.00 87.03           C  
ANISOU  719  CD1 PHE A 121    12880  10376   9812   -742   2092    779       C  
ATOM    720  CD2 PHE A 121      53.150  48.222 -64.229  1.00 82.29           C  
ANISOU  720  CD2 PHE A 121    12104   9688   9473   -654   1788    747       C  
ATOM    721  CE1 PHE A 121      53.444  48.693 -66.930  1.00 92.01           C  
ANISOU  721  CE1 PHE A 121    13751  10922  10286   -744   1976    863       C  
ATOM    722  CE2 PHE A 121      52.388  49.189 -64.836  1.00 87.16           C  
ANISOU  722  CE2 PHE A 121    12948  10222   9948   -642   1679    825       C  
ATOM    723  CZ  PHE A 121      52.538  49.430 -66.191  1.00 92.90           C  
ANISOU  723  CZ  PHE A 121    13885  10948  10465   -688   1765    889       C  
ATOM    724  N   PHE A 122      55.100  43.261 -63.035  1.00 60.33           N  
ANISOU  724  N   PHE A 122     8677   7207   7040   -462   2158    389       N  
ATOM    725  CA  PHE A 122      56.057  42.576 -62.183  1.00 66.92           C  
ANISOU  725  CA  PHE A 122     9281   8092   8051   -432   2243    356       C  
ATOM    726  C   PHE A 122      56.345  41.140 -62.610  1.00 72.38           C  
ANISOU  726  C   PHE A 122     9955   8826   8719   -334   2370    261       C  
ATOM    727  O   PHE A 122      57.024  40.417 -61.875  1.00 74.69           O  
ANISOU  727  O   PHE A 122    10068   9153   9158   -272   2422    227       O  
ATOM    728  CB  PHE A 122      55.559  42.592 -60.731  1.00 67.11           C  
ANISOU  728  CB  PHE A 122     9187   8079   8231   -397   2066    338       C  
ATOM    729  CG  PHE A 122      55.147  43.951 -60.239  1.00 69.10           C  
ANISOU  729  CG  PHE A 122     9484   8268   8501   -470   1931    413       C  
ATOM    730  CD1 PHE A 122      56.067  44.976 -60.148  1.00 73.15           C  
ANISOU  730  CD1 PHE A 122     9953   8781   9059   -587   1989    499       C  
ATOM    731  CD2 PHE A 122      53.837  44.202 -59.869  1.00 71.72           C  
ANISOU  731  CD2 PHE A 122     9905   8540   8806   -423   1752    395       C  
ATOM    732  CE1 PHE A 122      55.694  46.231 -59.689  1.00 74.41           C  
ANISOU  732  CE1 PHE A 122    10188   8857   9229   -652   1867    562       C  
ATOM    733  CE2 PHE A 122      53.454  45.447 -59.405  1.00 71.59           C  
ANISOU  733  CE2 PHE A 122     9945   8452   8804   -464   1637    458       C  
ATOM    734  CZ  PHE A 122      54.384  46.463 -59.313  1.00 73.28           C  
ANISOU  734  CZ  PHE A 122    10146   8642   9054   -578   1693    539       C  
ATOM    735  N   GLY A 123      55.817  40.691 -63.742  1.00 72.11           N  
ANISOU  735  N   GLY A 123    10116   8781   8500   -309   2408    214       N  
ATOM    736  CA  GLY A 123      56.146  39.369 -64.230  1.00 70.95           C  
ANISOU  736  CA  GLY A 123     9991   8655   8313   -219   2546    118       C  
ATOM    737  C   GLY A 123      55.333  38.254 -63.594  1.00 68.53           C  
ANISOU  737  C   GLY A 123     9681   8297   8060   -133   2424     18       C  
ATOM    738  O   GLY A 123      54.510  38.442 -62.689  1.00 66.59           O  
ANISOU  738  O   GLY A 123     9391   8015   7896   -139   2238     22       O  
ATOM    739  N   GLN A 124      55.631  37.045 -64.077  1.00 72.24           N  
ANISOU  739  N   GLN A 124    10206   8761   8483    -51   2552    -74       N  
ATOM    740  CA  GLN A 124      54.807  35.867 -63.804  1.00 72.74           C  
ANISOU  740  CA  GLN A 124    10341   8755   8544     11   2461   -180       C  
ATOM    741  C   GLN A 124      54.983  35.376 -62.369  1.00 63.10           C  
ANISOU  741  C   GLN A 124     8929   7511   7536     72   2399   -185       C  
ATOM    742  O   GLN A 124      54.004  35.045 -61.683  1.00 66.55           O  
ANISOU  742  O   GLN A 124     9379   7895   8013     66   2237   -217       O  
ATOM    743  CB  GLN A 124      55.158  34.759 -64.810  1.00 79.18           C  
ANISOU  743  CB  GLN A 124    11308   9547   9229     80   2631   -279       C  
ATOM    744  CG  GLN A 124      54.548  33.381 -64.547  1.00 85.14           C  
ANISOU  744  CG  GLN A 124    12151  10210   9991    143   2577   -397       C  
ATOM    745  CD  GLN A 124      53.112  33.260 -65.016  1.00 92.84           C  
ANISOU  745  CD  GLN A 124    13316  11138  10819     59   2396   -452       C  
ATOM    746  OE1 GLN A 124      52.529  34.221 -65.521  1.00100.45           O  
ANISOU  746  OE1 GLN A 124    14346  12144  11678    -25   2297   -399       O  
ATOM    747  NE2 GLN A 124      52.533  32.070 -64.855  1.00 95.16           N  
ANISOU  747  NE2 GLN A 124    13703  11345  11107     80   2347   -557       N  
ATOM    748  N   SER A 125      56.231  35.291 -61.906  1.00 60.51           N  
ANISOU  748  N   SER A 125     8420   7229   7341    132   2528   -151       N  
ATOM    749  CA  SER A 125      56.481  34.761 -60.572  1.00 59.47           C  
ANISOU  749  CA  SER A 125     8123   7078   7396    204   2467   -152       C  
ATOM    750  C   SER A 125      55.833  35.637 -59.519  1.00 61.29           C  
ANISOU  750  C   SER A 125     8274   7303   7709    128   2271    -90       C  
ATOM    751  O   SER A 125      55.120  35.139 -58.647  1.00 59.39           O  
ANISOU  751  O   SER A 125     8033   7006   7528    151   2147   -121       O  
ATOM    752  CB  SER A 125      57.982  34.653 -60.312  1.00 60.63           C  
ANISOU  752  CB  SER A 125     8066   7300   7669    281   2624   -113       C  
ATOM    753  OG  SER A 125      58.515  33.537 -60.985  1.00 69.06           O  
ANISOU  753  OG  SER A 125     9195   8353   8693    405   2801   -189       O  
ATOM    754  N   LEU A 126      56.026  36.950 -59.617  1.00 64.70           N  
ANISOU  754  N   LEU A 126     8663   7783   8136     33   2248     -6       N  
ATOM    755  CA  LEU A 126      55.363  37.849 -58.679  1.00 64.44           C  
ANISOU  755  CA  LEU A 126     8590   7730   8164    -30   2068     44       C  
ATOM    756  C   LEU A 126      53.850  37.827 -58.854  1.00 64.48           C  
ANISOU  756  C   LEU A 126     8748   7681   8071    -51   1925      5       C  
ATOM    757  O   LEU A 126      53.124  38.019 -57.875  1.00 67.64           O  
ANISOU  757  O   LEU A 126     9109   8052   8538    -55   1784     10       O  
ATOM    758  CB  LEU A 126      55.925  39.267 -58.821  1.00 64.51           C  
ANISOU  758  CB  LEU A 126     8553   7780   8179   -132   2082    140       C  
ATOM    759  CG  LEU A 126      57.372  39.377 -58.325  1.00 67.04           C  
ANISOU  759  CG  LEU A 126     8663   8170   8637   -135   2182    186       C  
ATOM    760  CD1 LEU A 126      57.882  40.816 -58.371  1.00 67.54           C  
ANISOU  760  CD1 LEU A 126     8687   8260   8713   -271   2181    281       C  
ATOM    761  CD2 LEU A 126      57.473  38.821 -56.906  1.00 66.94           C  
ANISOU  761  CD2 LEU A 126     8510   8147   8777    -67   2082    168       C  
ATOM    762  N   CYS A 127      53.353  37.550 -60.065  1.00 62.73           N  
ANISOU  762  N   CYS A 127     8693   7451   7689    -62   1958    -38       N  
ATOM    763  CA  CYS A 127      51.912  37.355 -60.220  1.00 63.18           C  
ANISOU  763  CA  CYS A 127     8867   7474   7665    -80   1810    -84       C  
ATOM    764  C   CYS A 127      51.414  36.177 -59.387  1.00 63.81           C  
ANISOU  764  C   CYS A 127     8911   7508   7826    -36   1758   -158       C  
ATOM    765  O   CYS A 127      50.255  36.169 -58.948  1.00 62.66           O  
ANISOU  765  O   CYS A 127     8775   7346   7685    -61   1616   -175       O  
ATOM    766  CB  CYS A 127      51.551  37.160 -61.698  1.00 62.33           C  
ANISOU  766  CB  CYS A 127     8953   7370   7357   -105   1847   -124       C  
ATOM    767  SG  CYS A 127      49.763  36.822 -61.995  1.00 61.57           S  
ANISOU  767  SG  CYS A 127     8980   7255   7157   -140   1644   -189       S  
ATOM    768  N   LYS A 128      52.260  35.163 -59.189  1.00 62.70           N  
ANISOU  768  N   LYS A 128     8732   7344   7745     33   1879   -198       N  
ATOM    769  CA  LYS A 128      51.906  34.101 -58.245  1.00 63.64           C  
ANISOU  769  CA  LYS A 128     8825   7403   7954     76   1833   -248       C  
ATOM    770  C   LYS A 128      52.090  34.563 -56.803  1.00 60.70           C  
ANISOU  770  C   LYS A 128     8291   7040   7734     89   1759   -184       C  
ATOM    771  O   LYS A 128      51.194  34.418 -55.967  1.00 57.88           O  
ANISOU  771  O   LYS A 128     7922   6653   7416     69   1646   -193       O  
ATOM    772  CB  LYS A 128      52.757  32.859 -58.481  1.00 66.34           C  
ANISOU  772  CB  LYS A 128     9201   7699   8308    170   1982   -307       C  
ATOM    773  CG  LYS A 128      52.772  32.331 -59.880  1.00 67.90           C  
ANISOU  773  CG  LYS A 128     9575   7877   8347    172   2085   -380       C  
ATOM    774  CD  LYS A 128      51.488  31.647 -60.190  1.00 65.49           C  
ANISOU  774  CD  LYS A 128     9432   7506   7947    108   1981   -462       C  
ATOM    775  CE  LYS A 128      51.674  30.521 -61.216  1.00 63.02           C  
ANISOU  775  CE  LYS A 128     9315   7121   7508    143   2098   -568       C  
ATOM    776  NZ  LYS A 128      50.330  29.968 -61.519  1.00 62.77           N  
ANISOU  776  NZ  LYS A 128     9436   7035   7380     41   1965   -647       N  
ATOM    777  N   VAL A 129      53.255  35.128 -56.499  1.00 61.08           N  
ANISOU  777  N   VAL A 129     8211   7134   7861    114   1823   -122       N  
ATOM    778  CA  VAL A 129      53.695  35.282 -55.118  1.00 61.33           C  
ANISOU  778  CA  VAL A 129     8099   7171   8034    142   1766    -75       C  
ATOM    779  C   VAL A 129      52.859  36.320 -54.388  1.00 62.84           C  
ANISOU  779  C   VAL A 129     8274   7364   8240     74   1621    -35       C  
ATOM    780  O   VAL A 129      52.426  36.094 -53.249  1.00 65.87           O  
ANISOU  780  O   VAL A 129     8624   7718   8687     89   1536    -36       O  
ATOM    781  CB  VAL A 129      55.191  35.643 -55.056  1.00 60.92           C  
ANISOU  781  CB  VAL A 129     7899   7185   8063    170   1862    -21       C  
ATOM    782  CG1 VAL A 129      55.554  36.081 -53.632  1.00 58.81           C  
ANISOU  782  CG1 VAL A 129     7492   6933   7922    169   1761     34       C  
ATOM    783  CG2 VAL A 129      56.040  34.470 -55.479  1.00 58.39           C  
ANISOU  783  CG2 VAL A 129     7565   6861   7760    282   2008    -62       C  
ATOM    784  N   ILE A 130      52.639  37.481 -55.004  1.00 59.84           N  
ANISOU  784  N   ILE A 130     7930   7012   7794      6   1596      3       N  
ATOM    785  CA  ILE A 130      52.001  38.588 -54.284  1.00 60.02           C  
ANISOU  785  CA  ILE A 130     7940   7027   7838    -37   1471     46       C  
ATOM    786  C   ILE A 130      50.565  38.257 -53.882  1.00 56.00           C  
ANISOU  786  C   ILE A 130     7482   6489   7305    -29   1368      4       C  
ATOM    787  O   ILE A 130      50.201  38.499 -52.721  1.00 53.61           O  
ANISOU  787  O   ILE A 130     7131   6172   7068    -20   1292     16       O  
ATOM    788  CB  ILE A 130      52.128  39.885 -55.083  1.00 57.86           C  
ANISOU  788  CB  ILE A 130     7719   6770   7496   -101   1474    103       C  
ATOM    789  CG1 ILE A 130      53.603  40.298 -55.133  1.00 58.83           C  
ANISOU  789  CG1 ILE A 130     7747   6928   7675   -135   1572    155       C  
ATOM    790  CG2 ILE A 130      51.246  40.972 -54.473  1.00 56.32           C  
ANISOU  790  CG2 ILE A 130     7553   6544   7302   -122   1342    134       C  
ATOM    791  CD1 ILE A 130      53.867  41.602 -55.863  1.00 65.75           C  
ANISOU  791  CD1 ILE A 130     8685   7808   8489   -222   1591    223       C  
ATOM    792  N   PRO A 131      49.716  37.710 -54.758  1.00 56.67           N  
ANISOU  792  N   PRO A 131     7660   6574   7299    -38   1361    -47       N  
ATOM    793  CA  PRO A 131      48.392  37.272 -54.285  1.00 59.32           C  
ANISOU  793  CA  PRO A 131     8006   6898   7634    -44   1268    -88       C  
ATOM    794  C   PRO A 131      48.469  36.169 -53.245  1.00 59.94           C  
ANISOU  794  C   PRO A 131     8042   6937   7795    -18   1288   -119       C  
ATOM    795  O   PRO A 131      47.607  36.086 -52.360  1.00 61.72           O  
ANISOU  795  O   PRO A 131     8239   7157   8057    -27   1221   -125       O  
ATOM    796  CB  PRO A 131      47.698  36.813 -55.578  1.00 61.02           C  
ANISOU  796  CB  PRO A 131     8329   7127   7729    -76   1260   -140       C  
ATOM    797  CG  PRO A 131      48.375  37.597 -56.646  1.00 59.88           C  
ANISOU  797  CG  PRO A 131     8244   7004   7502    -84   1311   -100       C  
ATOM    798  CD  PRO A 131      49.812  37.625 -56.224  1.00 56.53           C  
ANISOU  798  CD  PRO A 131     7746   6573   7161    -57   1421    -65       C  
ATOM    799  N   TYR A 132      49.494  35.322 -53.321  1.00 59.92           N  
ANISOU  799  N   TYR A 132     8040   6905   7821     22   1385   -133       N  
ATOM    800  CA  TYR A 132      49.653  34.276 -52.321  1.00 61.99           C  
ANISOU  800  CA  TYR A 132     8284   7114   8157     62   1399   -150       C  
ATOM    801  C   TYR A 132      49.953  34.874 -50.952  1.00 61.31           C  
ANISOU  801  C   TYR A 132     8102   7036   8156     82   1344    -92       C  
ATOM    802  O   TYR A 132      49.313  34.512 -49.959  1.00 55.04           O  
ANISOU  802  O   TYR A 132     7309   6212   7390     78   1298    -96       O  
ATOM    803  CB  TYR A 132      50.746  33.298 -52.752  1.00 60.44           C  
ANISOU  803  CB  TYR A 132     8110   6881   7972    131   1515   -173       C  
ATOM    804  CG  TYR A 132      51.016  32.221 -51.743  1.00 59.55           C  
ANISOU  804  CG  TYR A 132     7995   6698   7931    193   1527   -178       C  
ATOM    805  CD1 TYR A 132      50.111  31.190 -51.547  1.00 62.29           C  
ANISOU  805  CD1 TYR A 132     8444   6967   8255    164   1511   -228       C  
ATOM    806  CD2 TYR A 132      52.173  32.237 -50.987  1.00 58.88           C  
ANISOU  806  CD2 TYR A 132     7811   6625   7936    275   1546   -127       C  
ATOM    807  CE1 TYR A 132      50.350  30.199 -50.618  1.00 62.77           C  
ANISOU  807  CE1 TYR A 132     8533   6945   8372    220   1524   -222       C  
ATOM    808  CE2 TYR A 132      52.431  31.251 -50.074  1.00 61.84           C  
ANISOU  808  CE2 TYR A 132     8200   6929   8366    347   1545   -121       C  
ATOM    809  CZ  TYR A 132      51.514  30.233 -49.882  1.00 62.19           C  
ANISOU  809  CZ  TYR A 132     8372   6879   8378    322   1538   -166       C  
ATOM    810  OH  TYR A 132      51.769  29.251 -48.950  1.00 58.63           O  
ANISOU  810  OH  TYR A 132     7963   6340   7973    394   1539   -149       O  
ATOM    811  N   LEU A 133      50.920  35.798 -50.887  1.00 61.57           N  
ANISOU  811  N   LEU A 133     8062   7109   8224     91   1351    -40       N  
ATOM    812  CA  LEU A 133      51.213  36.494 -49.636  1.00 60.73           C  
ANISOU  812  CA  LEU A 133     7884   7009   8183     93   1282      9       C  
ATOM    813  C   LEU A 133      49.998  37.241 -49.112  1.00 61.11           C  
ANISOU  813  C   LEU A 133     7962   7053   8202     57   1195      9       C  
ATOM    814  O   LEU A 133      49.724  37.225 -47.903  1.00 59.18           O  
ANISOU  814  O   LEU A 133     7706   6789   7989     69   1146     17       O  
ATOM    815  CB  LEU A 133      52.373  37.469 -49.825  1.00 59.58           C  
ANISOU  815  CB  LEU A 133     7662   6908   8069     73   1297     60       C  
ATOM    816  CG  LEU A 133      53.708  36.806 -50.163  1.00 61.71           C  
ANISOU  816  CG  LEU A 133     7852   7206   8389    123   1391     69       C  
ATOM    817  CD1 LEU A 133      54.822  37.856 -50.261  1.00 64.80           C  
ANISOU  817  CD1 LEU A 133     8139   7658   8824     73   1402    126       C  
ATOM    818  CD2 LEU A 133      54.036  35.762 -49.130  1.00 56.78           C  
ANISOU  818  CD2 LEU A 133     7193   6551   7830    204   1373     66       C  
ATOM    819  N   GLN A 134      49.260  37.909 -49.997  1.00 60.92           N  
ANISOU  819  N   GLN A 134     7983   7050   8115     23   1176      1       N  
ATOM    820  CA  GLN A 134      48.093  38.659 -49.540  1.00 61.11           C  
ANISOU  820  CA  GLN A 134     8021   7079   8119     16   1098      2       C  
ATOM    821  C   GLN A 134      47.065  37.725 -48.915  1.00 61.62           C  
ANISOU  821  C   GLN A 134     8085   7137   8192     18   1087    -38       C  
ATOM    822  O   GLN A 134      46.581  37.968 -47.802  1.00 64.85           O  
ANISOU  822  O   GLN A 134     8475   7539   8624     32   1054    -30       O  
ATOM    823  CB  GLN A 134      47.478  39.449 -50.697  1.00 58.76           C  
ANISOU  823  CB  GLN A 134     7771   6807   7748     -1   1070      7       C  
ATOM    824  CG  GLN A 134      46.261  40.296 -50.327  1.00 55.99           C  
ANISOU  824  CG  GLN A 134     7424   6468   7382     21    989     11       C  
ATOM    825  CD  GLN A 134      46.596  41.476 -49.392  1.00 60.98           C  
ANISOU  825  CD  GLN A 134     8060   7063   8047     41    954     51       C  
ATOM    826  OE1 GLN A 134      47.604  42.167 -49.562  1.00 62.69           O  
ANISOU  826  OE1 GLN A 134     8297   7252   8268     14    965     90       O  
ATOM    827  NE2 GLN A 134      45.740  41.696 -48.395  1.00 59.78           N  
ANISOU  827  NE2 GLN A 134     7892   6908   7912     79    918     38       N  
ATOM    828  N   THR A 135      46.721  36.635 -49.612  1.00 58.42           N  
ANISOU  828  N   THR A 135     7711   6728   7759     -4   1122    -82       N  
ATOM    829  CA  THR A 135      45.683  35.760 -49.084  1.00 58.87           C  
ANISOU  829  CA  THR A 135     7770   6776   7821    -32   1114   -118       C  
ATOM    830  C   THR A 135      46.159  35.024 -47.840  1.00 58.50           C  
ANISOU  830  C   THR A 135     7725   6675   7827    -10   1145   -104       C  
ATOM    831  O   THR A 135      45.374  34.807 -46.909  1.00 59.43           O  
ANISOU  831  O   THR A 135     7834   6789   7957    -27   1135   -105       O  
ATOM    832  CB  THR A 135      45.222  34.788 -50.162  1.00 65.20           C  
ANISOU  832  CB  THR A 135     8627   7572   8574    -83   1134   -175       C  
ATOM    833  OG1 THR A 135      46.362  34.104 -50.706  1.00 65.77           O  
ANISOU  833  OG1 THR A 135     8754   7595   8640    -57   1207   -186       O  
ATOM    834  CG2 THR A 135      44.527  35.576 -51.259  1.00 69.41           C  
ANISOU  834  CG2 THR A 135     9160   8171   9040   -105   1074   -182       C  
ATOM    835  N   VAL A 136      47.442  34.655 -47.796  1.00 55.59           N  
ANISOU  835  N   VAL A 136     7364   6269   7488     35   1185    -85       N  
ATOM    836  CA  VAL A 136      47.995  34.034 -46.604  1.00 57.49           C  
ANISOU  836  CA  VAL A 136     7610   6460   7773     75   1193    -59       C  
ATOM    837  C   VAL A 136      47.893  34.983 -45.418  1.00 61.70           C  
ANISOU  837  C   VAL A 136     8110   7015   8318     84   1135    -20       C  
ATOM    838  O   VAL A 136      47.538  34.572 -44.308  1.00 60.30           O  
ANISOU  838  O   VAL A 136     7961   6808   8142     86   1128     -9       O  
ATOM    839  CB  VAL A 136      49.446  33.596 -46.864  1.00 58.52           C  
ANISOU  839  CB  VAL A 136     7725   6570   7941    142   1236    -41       C  
ATOM    840  CG1 VAL A 136      50.186  33.383 -45.554  1.00 59.32           C  
ANISOU  840  CG1 VAL A 136     7806   6645   8089    200   1204      7       C  
ATOM    841  CG2 VAL A 136      49.459  32.320 -47.688  1.00 61.27           C  
ANISOU  841  CG2 VAL A 136     8150   6861   8270    154   1309    -88       C  
ATOM    842  N   SER A 137      48.179  36.265 -45.634  1.00 61.89           N  
ANISOU  842  N   SER A 137     8095   7080   8341     83   1096     -1       N  
ATOM    843  CA  SER A 137      48.091  37.214 -44.536  1.00 68.09           C  
ANISOU  843  CA  SER A 137     8877   7868   9125     89   1040     24       C  
ATOM    844  C   SER A 137      46.654  37.384 -44.076  1.00 70.31           C  
ANISOU  844  C   SER A 137     9178   8161   9375     78   1036      1       C  
ATOM    845  O   SER A 137      46.395  37.527 -42.878  1.00 77.02           O  
ANISOU  845  O   SER A 137    10053   8998  10214     92   1023     11       O  
ATOM    846  CB  SER A 137      48.677  38.554 -44.951  1.00 74.83           C  
ANISOU  846  CB  SER A 137     9710   8741   9981     77   1003     47       C  
ATOM    847  OG  SER A 137      50.048  38.402 -45.265  1.00 86.53           O  
ANISOU  847  OG  SER A 137    11144  10230  11502     79   1017     72       O  
ATOM    848  N   VAL A 138      45.707  37.371 -45.012  1.00 61.53           N  
ANISOU  848  N   VAL A 138     8051   7084   8242     54   1047    -28       N  
ATOM    849  CA  VAL A 138      44.305  37.440 -44.613  1.00 58.85           C  
ANISOU  849  CA  VAL A 138     7693   6781   7888     45   1049    -49       C  
ATOM    850  C   VAL A 138      43.951  36.244 -43.738  1.00 60.37           C  
ANISOU  850  C   VAL A 138     7905   6947   8086     15   1097    -56       C  
ATOM    851  O   VAL A 138      43.310  36.379 -42.690  1.00 56.67           O  
ANISOU  851  O   VAL A 138     7438   6489   7606     20   1115    -51       O  
ATOM    852  CB  VAL A 138      43.400  37.518 -45.852  1.00 57.79           C  
ANISOU  852  CB  VAL A 138     7521   6703   7734     20   1032    -78       C  
ATOM    853  CG1 VAL A 138      41.939  37.367 -45.448  1.00 54.60           C  
ANISOU  853  CG1 VAL A 138     7058   6358   7331      2   1039   -100       C  
ATOM    854  CG2 VAL A 138      43.624  38.854 -46.566  1.00 57.56           C  
ANISOU  854  CG2 VAL A 138     7497   6688   7684     60    982    -57       C  
ATOM    855  N   SER A 139      44.358  35.051 -44.174  1.00 59.77           N  
ANISOU  855  N   SER A 139     7862   6828   8019    -17   1129    -66       N  
ATOM    856  CA  SER A 139      44.073  33.832 -43.432  1.00 58.94           C  
ANISOU  856  CA  SER A 139     7807   6672   7914    -54   1178    -65       C  
ATOM    857  C   SER A 139      44.717  33.865 -42.049  1.00 60.17           C  
ANISOU  857  C   SER A 139     8011   6784   8065     -6   1174    -20       C  
ATOM    858  O   SER A 139      44.065  33.555 -41.048  1.00 58.78           O  
ANISOU  858  O   SER A 139     7868   6599   7866    -30   1207     -9       O  
ATOM    859  CB  SER A 139      44.568  32.626 -44.233  1.00 57.46           C  
ANISOU  859  CB  SER A 139     7678   6420   7734    -76   1209    -86       C  
ATOM    860  OG  SER A 139      44.367  31.422 -43.518  1.00 57.39           O  
ANISOU  860  OG  SER A 139     7749   6334   7723   -111   1255    -79       O  
ATOM    861  N   VAL A 140      45.999  34.239 -41.982  1.00 60.56           N  
ANISOU  861  N   VAL A 140     8064   6815   8132     55   1133      8       N  
ATOM    862  CA  VAL A 140      46.692  34.393 -40.709  1.00 60.67           C  
ANISOU  862  CA  VAL A 140     8119   6801   8134    100   1098     51       C  
ATOM    863  C   VAL A 140      45.937  35.356 -39.806  1.00 64.46           C  
ANISOU  863  C   VAL A 140     8608   7313   8570     96   1085     49       C  
ATOM    864  O   VAL A 140      45.732  35.084 -38.623  1.00 62.16           O  
ANISOU  864  O   VAL A 140     8385   6995   8236    100   1098     69       O  
ATOM    865  CB  VAL A 140      48.132  34.884 -40.940  1.00 54.47           C  
ANISOU  865  CB  VAL A 140     7291   6021   7383    148   1039     76       C  
ATOM    866  CG1 VAL A 140      48.732  35.375 -39.621  1.00 53.13           C  
ANISOU  866  CG1 VAL A 140     7154   5843   7191    177    969    113       C  
ATOM    867  CG2 VAL A 140      48.978  33.783 -41.530  1.00 52.27           C  
ANISOU  867  CG2 VAL A 140     7011   5705   7145    185   1068     83       C  
ATOM    868  N   SER A 141      45.512  36.494 -40.353  1.00 62.53           N  
ANISOU  868  N   SER A 141     8313   7119   8328     97   1066     25       N  
ATOM    869  CA  SER A 141      44.809  37.491 -39.562  1.00 59.31           C  
ANISOU  869  CA  SER A 141     7924   6733   7880    117   1062     15       C  
ATOM    870  C   SER A 141      43.529  36.917 -38.978  1.00 60.54           C  
ANISOU  870  C   SER A 141     8083   6912   8009     93   1142      2       C  
ATOM    871  O   SER A 141      43.250  37.063 -37.783  1.00 60.37           O  
ANISOU  871  O   SER A 141     8123   6881   7935    110   1169     10       O  
ATOM    872  CB  SER A 141      44.496  38.713 -40.429  1.00 58.11           C  
ANISOU  872  CB  SER A 141     7724   6616   7738    137   1032     -5       C  
ATOM    873  OG  SER A 141      45.682  39.391 -40.787  1.00 59.36           O  
ANISOU  873  OG  SER A 141     7892   6748   7913    141    969     14       O  
ATOM    874  N   VAL A 142      42.726  36.270 -39.817  1.00 61.75           N  
ANISOU  874  N   VAL A 142     8170   7101   8190     43   1183    -19       N  
ATOM    875  CA  VAL A 142      41.415  35.834 -39.361  1.00 64.54           C  
ANISOU  875  CA  VAL A 142     8491   7500   8531     -1   1262    -33       C  
ATOM    876  C   VAL A 142      41.558  34.682 -38.367  1.00 65.48           C  
ANISOU  876  C   VAL A 142     8705   7556   8619    -46   1320     -2       C  
ATOM    877  O   VAL A 142      40.821  34.602 -37.381  1.00 66.09           O  
ANISOU  877  O   VAL A 142     8805   7652   8655    -63   1392      6       O  
ATOM    878  CB  VAL A 142      40.528  35.481 -40.573  1.00 66.58           C  
ANISOU  878  CB  VAL A 142     8646   7823   8829    -62   1268    -66       C  
ATOM    879  CG1 VAL A 142      40.818  34.087 -41.094  1.00 64.98           C  
ANISOU  879  CG1 VAL A 142     8485   7562   8642   -146   1285    -69       C  
ATOM    880  CG2 VAL A 142      39.058  35.644 -40.231  1.00 70.65           C  
ANISOU  880  CG2 VAL A 142     9063   8434   9347    -85   1329    -84       C  
ATOM    881  N   LEU A 143      42.560  33.816 -38.565  1.00 67.91           N  
ANISOU  881  N   LEU A 143     9081   7783   8939    -53   1293     21       N  
ATOM    882  CA  LEU A 143      42.796  32.709 -37.641  1.00 65.29           C  
ANISOU  882  CA  LEU A 143     8866   7370   8571    -77   1333     62       C  
ATOM    883  C   LEU A 143      43.455  33.183 -36.351  1.00 65.05           C  
ANISOU  883  C   LEU A 143     8926   7311   8478    -10   1298    102       C  
ATOM    884  O   LEU A 143      43.260  32.574 -35.293  1.00 62.83           O  
ANISOU  884  O   LEU A 143     8752   6987   8135    -29   1346    138       O  
ATOM    885  CB  LEU A 143      43.663  31.640 -38.311  1.00 63.55           C  
ANISOU  885  CB  LEU A 143     8696   7065   8386    -77   1313     72       C  
ATOM    886  CG  LEU A 143      43.047  30.925 -39.510  1.00 63.47           C  
ANISOU  886  CG  LEU A 143     8648   7054   8415   -160   1348     28       C  
ATOM    887  CD1 LEU A 143      43.980  29.831 -39.991  1.00 63.25           C  
ANISOU  887  CD1 LEU A 143     8709   6917   8406   -137   1344     35       C  
ATOM    888  CD2 LEU A 143      41.675  30.356 -39.154  1.00 61.65           C  
ANISOU  888  CD2 LEU A 143     8415   6842   8167   -280   1431     18       C  
ATOM    889  N   THR A 144      44.223  34.276 -36.415  1.00 62.48           N  
ANISOU  889  N   THR A 144     8574   7007   8157     57   1213     96       N  
ATOM    890  CA  THR A 144      44.760  34.875 -35.204  1.00 60.64           C  
ANISOU  890  CA  THR A 144     8429   6756   7854    105   1163    120       C  
ATOM    891  C   THR A 144      43.642  35.466 -34.360  1.00 61.56           C  
ANISOU  891  C   THR A 144     8578   6911   7900    100   1238    100       C  
ATOM    892  O   THR A 144      43.568  35.210 -33.152  1.00 61.99           O  
ANISOU  892  O   THR A 144     8752   6936   7865    102   1267    127       O  
ATOM    893  CB  THR A 144      45.792  35.934 -35.573  1.00 58.57           C  
ANISOU  893  CB  THR A 144     8125   6506   7622    148   1054    112       C  
ATOM    894  OG1 THR A 144      46.867  35.307 -36.276  1.00 56.35           O  
ANISOU  894  OG1 THR A 144     7802   6202   7406    161   1006    135       O  
ATOM    895  CG2 THR A 144      46.345  36.603 -34.314  1.00 59.20           C  
ANISOU  895  CG2 THR A 144     8307   6566   7621    179    982    127       C  
ATOM    896  N   LEU A 145      42.745  36.228 -34.987  1.00 58.88           N  
ANISOU  896  N   LEU A 145     8137   6640   7594    102   1275     54       N  
ATOM    897  CA  LEU A 145      41.578  36.720 -34.265  1.00 58.03           C  
ANISOU  897  CA  LEU A 145     8034   6583   7433    114   1370     30       C  
ATOM    898  C   LEU A 145      40.768  35.564 -33.699  1.00 61.91           C  
ANISOU  898  C   LEU A 145     8549   7080   7893     41   1490     54       C  
ATOM    899  O   LEU A 145      40.260  35.640 -32.570  1.00 63.62           O  
ANISOU  899  O   LEU A 145     8846   7305   8023     47   1574     62       O  
ATOM    900  CB  LEU A 145      40.718  37.579 -35.188  1.00 57.72           C  
ANISOU  900  CB  LEU A 145     7857   6623   7452    144   1384    -15       C  
ATOM    901  CG  LEU A 145      41.430  38.860 -35.637  1.00 56.70           C  
ANISOU  901  CG  LEU A 145     7737   6470   7335    212   1279    -33       C  
ATOM    902  CD1 LEU A 145      40.641  39.599 -36.697  1.00 53.35           C  
ANISOU  902  CD1 LEU A 145     7192   6111   6968    249   1278    -65       C  
ATOM    903  CD2 LEU A 145      41.682  39.764 -34.420  1.00 57.67           C  
ANISOU  903  CD2 LEU A 145     7995   6551   7366    272   1268    -45       C  
ATOM    904  N   SER A 146      40.650  34.472 -34.463  1.00 62.16           N  
ANISOU  904  N   SER A 146     8531   7100   7988    -38   1506     66       N  
ATOM    905  CA  SER A 146      39.886  33.333 -33.977  1.00 62.25           C  
ANISOU  905  CA  SER A 146     8578   7100   7974   -136   1621     92       C  
ATOM    906  C   SER A 146      40.538  32.724 -32.745  1.00 60.39           C  
ANISOU  906  C   SER A 146     8536   6769   7640   -130   1629    153       C  
ATOM    907  O   SER A 146      39.855  32.420 -31.766  1.00 60.05           O  
ANISOU  907  O   SER A 146     8566   6732   7520   -172   1740    177       O  
ATOM    908  CB  SER A 146      39.730  32.305 -35.087  1.00 63.25           C  
ANISOU  908  CB  SER A 146     8645   7208   8180   -230   1620     85       C  
ATOM    909  OG  SER A 146      38.808  32.783 -36.045  1.00 63.29           O  
ANISOU  909  OG  SER A 146     8474   7321   8251   -256   1627     33       O  
ATOM    910  N   CYS A 147      41.864  32.576 -32.756  1.00 59.73           N  
ANISOU  910  N   CYS A 147     8535   6606   7555    -71   1511    182       N  
ATOM    911  CA  CYS A 147      42.536  32.028 -31.583  1.00 60.58           C  
ANISOU  911  CA  CYS A 147     8827   6627   7563    -47   1489    246       C  
ATOM    912  C   CYS A 147      42.476  32.984 -30.399  1.00 63.09           C  
ANISOU  912  C   CYS A 147     9232   6973   7765      5   1490    243       C  
ATOM    913  O   CYS A 147      42.433  32.538 -29.252  1.00 68.15           O  
ANISOU  913  O   CYS A 147    10036   7569   8290     -5   1532    292       O  
ATOM    914  CB  CYS A 147      43.982  31.674 -31.924  1.00 63.36           C  
ANISOU  914  CB  CYS A 147     9211   6908   7955     20   1352    278       C  
ATOM    915  SG  CYS A 147      44.095  30.207 -33.012  1.00 67.88           S  
ANISOU  915  SG  CYS A 147     9771   7401   8621    -28   1380    290       S  
ATOM    916  N   ILE A 148      42.477  34.293 -30.653  1.00 61.85           N  
ANISOU  916  N   ILE A 148     8995   6879   7628     59   1444    187       N  
ATOM    917  CA  ILE A 148      42.284  35.261 -29.581  1.00 58.86           C  
ANISOU  917  CA  ILE A 148     8714   6517   7133    108   1460    166       C  
ATOM    918  C   ILE A 148      40.933  35.039 -28.922  1.00 61.08           C  
ANISOU  918  C   ILE A 148     9015   6844   7346     68   1646    162       C  
ATOM    919  O   ILE A 148      40.828  34.923 -27.693  1.00 70.69           O  
ANISOU  919  O   ILE A 148    10399   8035   8423     71   1703    189       O  
ATOM    920  CB  ILE A 148      42.417  36.696 -30.124  1.00 56.10           C  
ANISOU  920  CB  ILE A 148     8281   6207   6828    169   1391    101       C  
ATOM    921  CG1 ILE A 148      43.863  36.985 -30.476  1.00 56.72           C  
ANISOU  921  CG1 ILE A 148     8365   6240   6944    193   1214    114       C  
ATOM    922  CG2 ILE A 148      41.922  37.711 -29.108  1.00 56.51           C  
ANISOU  922  CG2 ILE A 148     8439   6271   6761    223   1443     61       C  
ATOM    923  CD1 ILE A 148      44.076  38.337 -31.113  1.00 60.05           C  
ANISOU  923  CD1 ILE A 148     8719   6682   7415    228   1144     61       C  
ATOM    924  N   ALA A 149      39.879  34.978 -29.740  1.00 56.29           N  
ANISOU  924  N   ALA A 149     8235   6317   6836     26   1744    130       N  
ATOM    925  CA  ALA A 149      38.529  34.754 -29.230  1.00 59.47           C  
ANISOU  925  CA  ALA A 149     8602   6793   7202    -24   1932    125       C  
ATOM    926  C   ALA A 149      38.442  33.434 -28.464  1.00 66.29           C  
ANISOU  926  C   ALA A 149     9604   7594   7988   -124   2020    198       C  
ATOM    927  O   ALA A 149      37.824  33.360 -27.396  1.00 67.29           O  
ANISOU  927  O   ALA A 149     9828   7739   8000   -144   2159    217       O  
ATOM    928  CB  ALA A 149      37.537  34.764 -30.395  1.00 55.87           C  
ANISOU  928  CB  ALA A 149     7906   6440   6882    -67   1983     86       C  
ATOM    929  N   LEU A 150      39.072  32.384 -28.994  1.00 65.49           N  
ANISOU  929  N   LEU A 150     9532   7409   7942   -183   1947    242       N  
ATOM    930  CA  LEU A 150      39.021  31.072 -28.357  1.00 69.52           C  
ANISOU  930  CA  LEU A 150    10198   7831   8384   -277   2022    318       C  
ATOM    931  C   LEU A 150      39.740  31.085 -27.019  1.00 65.31           C  
ANISOU  931  C   LEU A 150     9908   7221   7684   -215   1986    375       C  
ATOM    932  O   LEU A 150      39.260  30.499 -26.043  1.00 60.15           O  
ANISOU  932  O   LEU A 150     9403   6537   6912   -277   2112    429       O  
ATOM    933  CB  LEU A 150      39.639  30.015 -29.280  1.00 71.98           C  
ANISOU  933  CB  LEU A 150    10509   8050   8791   -322   1938    344       C  
ATOM    934  CG  LEU A 150      39.149  28.574 -29.126  1.00 82.61           C  
ANISOU  934  CG  LEU A 150    11954   9312  10124   -463   2047    403       C  
ATOM    935  CD1 LEU A 150      37.733  28.448 -29.689  1.00 86.41           C  
ANISOU  935  CD1 LEU A 150    12252   9899  10683   -604   2186    359       C  
ATOM    936  CD2 LEU A 150      40.090  27.571 -29.809  1.00 84.24           C  
ANISOU  936  CD2 LEU A 150    12237   9379  10389   -455   1941    433       C  
ATOM    937  N   ASP A 151      40.909  31.722 -26.965  1.00 63.47           N  
ANISOU  937  N   ASP A 151     9724   6957   7437   -104   1811    367       N  
ATOM    938  CA  ASP A 151      41.645  31.800 -25.714  1.00 65.31           C  
ANISOU  938  CA  ASP A 151    10183   7126   7505    -46   1742    415       C  
ATOM    939  C   ASP A 151      40.836  32.548 -24.661  1.00 65.50           C  
ANISOU  939  C   ASP A 151    10294   7208   7384    -37   1871    387       C  
ATOM    940  O   ASP A 151      40.708  32.075 -23.524  1.00 63.89           O  
ANISOU  940  O   ASP A 151    10299   6960   7018    -61   1943    446       O  
ATOM    941  CB  ASP A 151      42.999  32.463 -25.953  1.00 66.49           C  
ANISOU  941  CB  ASP A 151    10321   7257   7685     53   1521    400       C  
ATOM    942  CG  ASP A 151      43.696  32.833 -24.675  1.00 69.84           C  
ANISOU  942  CG  ASP A 151    10955   7644   7935    110   1424    429       C  
ATOM    943  OD1 ASP A 151      44.344  31.956 -24.072  1.00 75.34           O  
ANISOU  943  OD1 ASP A 151    11811   8260   8555    123   1355    514       O  
ATOM    944  OD2 ASP A 151      43.603  34.006 -24.270  1.00 71.83           O  
ANISOU  944  OD2 ASP A 151    11229   7941   8122    147   1408    367       O  
ATOM    945  N   ARG A 152      40.246  33.697 -25.030  1.00 65.06           N  
ANISOU  945  N   ARG A 152    10094   7249   7379      3   1915    299       N  
ATOM    946  CA  ARG A 152      39.405  34.411 -24.067  1.00 69.88           C  
ANISOU  946  CA  ARG A 152    10782   7915   7855     31   2064    263       C  
ATOM    947  C   ARG A 152      38.211  33.565 -23.637  1.00 71.45           C  
ANISOU  947  C   ARG A 152    10983   8154   8012    -71   2300    302       C  
ATOM    948  O   ARG A 152      37.794  33.613 -22.472  1.00 74.10           O  
ANISOU  948  O   ARG A 152    11486   8493   8174    -72   2431    319       O  
ATOM    949  CB  ARG A 152      38.910  35.739 -24.640  1.00 69.36           C  
ANISOU  949  CB  ARG A 152    10551   7934   7867    110   2079    164       C  
ATOM    950  CG  ARG A 152      39.982  36.752 -25.008  1.00 68.41           C  
ANISOU  950  CG  ARG A 152    10442   7774   7777    194   1870    119       C  
ATOM    951  CD  ARG A 152      40.733  37.296 -23.808  1.00 66.07           C  
ANISOU  951  CD  ARG A 152    10398   7410   7295    244   1782    115       C  
ATOM    952  NE  ARG A 152      41.826  36.406 -23.430  1.00 67.60           N  
ANISOU  952  NE  ARG A 152    10722   7526   7437    209   1639    197       N  
ATOM    953  CZ  ARG A 152      41.992  35.896 -22.215  1.00 71.95           C  
ANISOU  953  CZ  ARG A 152    11506   8028   7803    196   1656    252       C  
ATOM    954  NH1 ARG A 152      41.138  36.195 -21.248  1.00 74.44           N  
ANISOU  954  NH1 ARG A 152    11957   8367   7959    206   1826    229       N  
ATOM    955  NH2 ARG A 152      43.013  35.085 -21.970  1.00 75.62           N  
ANISOU  955  NH2 ARG A 152    12072   8423   8237    185   1507    333       N  
ATOM    956  N   TRP A 153      37.634  32.794 -24.568  1.00 71.35           N  
ANISOU  956  N   TRP A 153    10789   8174   8148   -170   2361    316       N  
ATOM    957  CA  TRP A 153      36.465  31.987 -24.228  1.00 75.62           C  
ANISOU  957  CA  TRP A 153    11304   8760   8666   -300   2586    353       C  
ATOM    958  C   TRP A 153      36.833  30.882 -23.250  1.00 71.49           C  
ANISOU  958  C   TRP A 153    11053   8116   7993   -374   2621    457       C  
ATOM    959  O   TRP A 153      36.099  30.626 -22.291  1.00 67.36           O  
ANISOU  959  O   TRP A 153    10639   7616   7339   -436   2814    493       O  
ATOM    960  CB  TRP A 153      35.827  31.401 -25.492  1.00 78.68           C  
ANISOU  960  CB  TRP A 153    11446   9203   9247   -410   2613    338       C  
ATOM    961  CG  TRP A 153      34.540  30.657 -25.226  1.00 81.19           C  
ANISOU  961  CG  TRP A 153    11694   9592   9564   -569   2844    368       C  
ATOM    962  CD1 TRP A 153      33.278  31.171 -25.250  1.00 80.13           C  
ANISOU  962  CD1 TRP A 153    11348   9624   9473   -588   3015    320       C  
ATOM    963  CD2 TRP A 153      34.402  29.271 -24.881  1.00 84.46           C  
ANISOU  963  CD2 TRP A 153    12246   9911   9933   -737   2931    456       C  
ATOM    964  NE1 TRP A 153      32.361  30.194 -24.946  1.00 81.91           N  
ANISOU  964  NE1 TRP A 153    11550   9881   9690   -773   3207    372       N  
ATOM    965  CE2 TRP A 153      33.025  29.019 -24.712  1.00 86.44           C  
ANISOU  965  CE2 TRP A 153    12352  10285  10205   -876   3161    457       C  
ATOM    966  CE3 TRP A 153      35.308  28.219 -24.702  1.00 84.26           C  
ANISOU  966  CE3 TRP A 153    12454   9704   9855   -777   2838    538       C  
ATOM    967  CZ2 TRP A 153      32.531  27.757 -24.368  1.00 90.16           C  
ANISOU  967  CZ2 TRP A 153    12917  10696  10642  -1081   3303    537       C  
ATOM    968  CZ3 TRP A 153      34.814  26.969 -24.352  1.00 89.86           C  
ANISOU  968  CZ3 TRP A 153    13280  10338  10524   -958   2976    619       C  
ATOM    969  CH2 TRP A 153      33.439  26.751 -24.191  1.00 90.44           C  
ANISOU  969  CH2 TRP A 153    13217  10530  10616  -1121   3207    617       C  
ATOM    970  N   TYR A 154      37.964  30.212 -23.483  1.00 72.48           N  
ANISOU  970  N   TYR A 154    11293   8111   8133   -361   2443    511       N  
ATOM    971  CA  TYR A 154      38.424  29.182 -22.559  1.00 75.43           C  
ANISOU  971  CA  TYR A 154    11949   8353   8360   -402   2445    620       C  
ATOM    972  C   TYR A 154      38.798  29.781 -21.208  1.00 72.76           C  
ANISOU  972  C   TYR A 154    11847   8000   7798   -313   2429    638       C  
ATOM    973  O   TYR A 154      38.567  29.162 -20.163  1.00 68.78           O  
ANISOU  973  O   TYR A 154    11574   7439   7120   -368   2540    718       O  
ATOM    974  CB  TYR A 154      39.616  28.428 -23.157  1.00 76.70           C  
ANISOU  974  CB  TYR A 154    12160   8384   8597   -366   2243    668       C  
ATOM    975  CG  TYR A 154      39.248  27.359 -24.167  1.00 81.90           C  
ANISOU  975  CG  TYR A 154    12717   8994   9406   -485   2291    683       C  
ATOM    976  CD1 TYR A 154      38.282  26.397 -23.878  1.00 86.80           C  
ANISOU  976  CD1 TYR A 154    13405   9581   9993   -653   2484    737       C  
ATOM    977  CD2 TYR A 154      39.866  27.311 -25.412  1.00 81.33           C  
ANISOU  977  CD2 TYR A 154    12495   8906   9502   -443   2147    641       C  
ATOM    978  CE1 TYR A 154      37.946  25.416 -24.801  1.00 86.20           C  
ANISOU  978  CE1 TYR A 154    13257   9447  10048   -782   2517    742       C  
ATOM    979  CE2 TYR A 154      39.539  26.334 -26.338  1.00 84.41           C  
ANISOU  979  CE2 TYR A 154    12820   9240  10011   -553   2187    644       C  
ATOM    980  CZ  TYR A 154      38.576  25.393 -26.030  1.00 87.49           C  
ANISOU  980  CZ  TYR A 154    13287   9589  10367   -726   2364    691       C  
ATOM    981  OH  TYR A 154      38.251  24.426 -26.955  1.00 90.12           O  
ANISOU  981  OH  TYR A 154    13574   9853  10813   -854   2392    685       O  
ATOM    982  N   ALA A 155      39.381  30.979 -21.207  1.00 71.55           N  
ANISOU  982  N   ALA A 155    11661   7889   7636   -186   2291    565       N  
ATOM    983  CA  ALA A 155      39.818  31.567 -19.951  1.00 74.68           C  
ANISOU  983  CA  ALA A 155    12303   8262   7811   -109   2246    570       C  
ATOM    984  C   ALA A 155      38.633  32.043 -19.122  1.00 82.77           C  
ANISOU  984  C   ALA A 155    13381   9368   8698   -131   2498    536       C  
ATOM    985  O   ALA A 155      38.648  31.917 -17.890  1.00 82.67           O  
ANISOU  985  O   ALA A 155    13638   9315   8455   -130   2559    582       O  
ATOM    986  CB  ALA A 155      40.789  32.720 -20.220  1.00 69.77           C  
ANISOU  986  CB  ALA A 155    11636   7651   7223      9   2021    496       C  
ATOM    987  N   ILE A 156      37.580  32.522 -19.785  1.00 86.77           N  
ANISOU  987  N   ILE A 156    13634   9996   9340   -149   2652    461       N  
ATOM    988  CA  ILE A 156      36.460  33.188 -19.125  1.00 89.09           C  
ANISOU  988  CA  ILE A 156    13921  10394   9534   -131   2891    407       C  
ATOM    989  C   ILE A 156      35.237  32.279 -19.044  1.00 95.42           C  
ANISOU  989  C   ILE A 156    14637  11261  10358   -278   3161    459       C  
ATOM    990  O   ILE A 156      34.720  32.006 -17.951  1.00 95.79           O  
ANISOU  990  O   ILE A 156    14865  11313  10216   -324   3356    503       O  
ATOM    991  CB  ILE A 156      36.124  34.521 -19.836  1.00 80.28           C  
ANISOU  991  CB  ILE A 156    12580   9377   8546    -17   2873    284       C  
ATOM    992  CG1 ILE A 156      37.305  35.491 -19.724  1.00 79.37           C  
ANISOU  992  CG1 ILE A 156    12594   9187   8375    104   2629    233       C  
ATOM    993  CG2 ILE A 156      34.852  35.134 -19.277  1.00 77.58           C  
ANISOU  993  CG2 ILE A 156    12188   9156   8134     21   3145    227       C  
ATOM    994  CD1 ILE A 156      37.243  36.650 -20.701  1.00 76.57           C  
ANISOU  994  CD1 ILE A 156    12025   8887   8182    199   2552    132       C  
ATOM    995  N  ACYS A 157      34.736  31.796 -20.187  0.50 96.77           N  
ANISOU  995  N  ACYS A 157    14536  11486  10749   -369   3181    455       N  
ATOM    996  N  BCYS A 157      34.742  31.791 -20.185  0.50 96.77           N  
ANISOU  996  N  BCYS A 157    14537  11484  10748   -369   3180    455       N  
ATOM    997  CA ACYS A 157      33.490  31.036 -20.208  0.50 99.52           C  
ANISOU  997  CA ACYS A 157    14754  11918  11143   -531   3432    491       C  
ATOM    998  CA BCYS A 157      33.500  31.030 -20.186  0.50 99.55           C  
ANISOU  998  CA BCYS A 157    14763  11919  11141   -531   3433    492       C  
ATOM    999  C  ACYS A 157      33.684  29.588 -19.770  0.50102.52           C  
ANISOU  999  C  ACYS A 157    15346  12168  11441   -693   3473    616       C  
ATOM   1000  C  BCYS A 157      33.706  29.593 -19.726  0.50102.55           C  
ANISOU 1000  C  BCYS A 157    15362  12168  11436   -690   3472    618       C  
ATOM   1001  O  ACYS A 157      32.756  28.981 -19.222  0.50104.99           O  
ANISOU 1001  O  ACYS A 157    15683  12521  11688   -835   3716    669       O  
ATOM   1002  O  BCYS A 157      32.805  29.003 -19.118  0.50105.09           O  
ANISOU 1002  O  BCYS A 157    15722  12526  11679   -827   3715    672       O  
ATOM   1003  CB ACYS A 157      32.867  31.086 -21.609  0.50 97.48           C  
ANISOU 1003  CB ACYS A 157    14128  11767  11141   -579   3417    434       C  
ATOM   1004  CB BCYS A 157      32.870  31.067 -21.576  0.50 97.54           C  
ANISOU 1004  CB BCYS A 157    14143  11773  11143   -581   3420    436       C  
ATOM   1005  SG ACYS A 157      31.162  30.442 -21.739  0.50101.50           S  
ANISOU 1005  SG ACYS A 157    14384  12442  11741   -778   3720    450       S  
ATOM   1006  SG BCYS A 157      32.165  32.670 -21.986  0.50 94.81           S  
ANISOU 1006  SG BCYS A 157    13529  11608  10888   -409   3463    306       S  
ATOM   1007  N   HIS A 158      34.862  29.019 -19.997  1.00102.93           N  
ANISOU 1007  N   HIS A 158    15552  12061  11495   -672   3247    669       N  
ATOM   1008  CA  HIS A 158      35.105  27.642 -19.591  1.00104.47           C  
ANISOU 1008  CA  HIS A 158    15979  12106  11610   -799   3271    793       C  
ATOM   1009  C   HIS A 158      35.543  27.609 -18.130  1.00105.02           C  
ANISOU 1009  C   HIS A 158    16409  12093  11401   -747   3294    868       C  
ATOM   1010  O   HIS A 158      36.377  28.426 -17.722  1.00100.39           O  
ANISOU 1010  O   HIS A 158    15934  11493  10718   -587   3130    833       O  
ATOM   1011  CB  HIS A 158      36.164  26.997 -20.481  1.00104.31           C  
ANISOU 1011  CB  HIS A 158    15968  11950  11716   -776   3028    819       C  
ATOM   1012  CG  HIS A 158      36.112  25.500 -20.491  1.00105.99           C  
ANISOU 1012  CG  HIS A 158    16334  12014  11925   -932   3080    927       C  
ATOM   1013  ND1 HIS A 158      36.585  24.729 -19.451  1.00107.38           N  
ANISOU 1013  ND1 HIS A 158    16859  12036  11905   -942   3083   1048       N  
ATOM   1014  CD2 HIS A 158      35.646  24.631 -21.420  1.00105.94           C  
ANISOU 1014  CD2 HIS A 158    16199  11974  12078  -1086   3125    931       C  
ATOM   1015  CE1 HIS A 158      36.416  23.451 -19.739  1.00107.56           C  
ANISOU 1015  CE1 HIS A 158    16970  11927  11973  -1090   3134   1126       C  
ATOM   1016  NE2 HIS A 158      35.844  23.364 -20.926  1.00106.68           N  
ANISOU 1016  NE2 HIS A 158    16574  11883  12076  -1187   3162   1052       N  
ATOM   1017  N   PRO A 159      35.000  26.694 -17.313  1.00109.84           N  
ANISOU 1017  N   PRO A 159    17219  12647  11867   -890   3491    971       N  
ATOM   1018  CA  PRO A 159      35.383  26.657 -15.893  1.00112.56           C  
ANISOU 1018  CA  PRO A 159    17934  12914  11918   -841   3516   1048       C  
ATOM   1019  C   PRO A 159      36.822  26.244 -15.658  1.00115.57           C  
ANISOU 1019  C   PRO A 159    18574  13122  12216   -735   3229   1124       C  
ATOM   1020  O   PRO A 159      37.374  26.569 -14.600  1.00118.09           O  
ANISOU 1020  O   PRO A 159    19166  13401  12304   -640   3160   1156       O  
ATOM   1021  CB  PRO A 159      34.407  25.638 -15.293  1.00114.00           C  
ANISOU 1021  CB  PRO A 159    18243  13071  12001  -1050   3805   1152       C  
ATOM   1022  CG  PRO A 159      33.992  24.790 -16.446  1.00112.72           C  
ANISOU 1022  CG  PRO A 159    17857  12888  12082  -1208   3824   1160       C  
ATOM   1023  CD  PRO A 159      33.965  25.694 -17.630  1.00110.21           C  
ANISOU 1023  CD  PRO A 159    17169  12704  12002  -1116   3706   1021       C  
ATOM   1024  N   LEU A 160      37.446  25.542 -16.592  1.00118.37           N  
ANISOU 1024  N   LEU A 160    18853  13376  12745   -740   3059   1151       N  
ATOM   1025  CA  LEU A 160      38.838  25.153 -16.445  1.00124.03           C  
ANISOU 1025  CA  LEU A 160    19772  13945  13411   -615   2782   1221       C  
ATOM   1026  C   LEU A 160      39.740  26.151 -17.170  1.00130.46           C  
ANISOU 1026  C   LEU A 160    20382  14825  14362   -452   2531   1116       C  
ATOM   1027  O   LEU A 160      39.285  27.022 -17.917  1.00127.64           O  
ANISOU 1027  O   LEU A 160    19740  14602  14156   -445   2568    997       O  
ATOM   1028  CB  LEU A 160      39.059  23.727 -16.965  1.00121.83           C  
ANISOU 1028  CB  LEU A 160    19570  13496  13225   -698   2755   1320       C  
ATOM   1029  CG  LEU A 160      38.292  22.604 -16.251  1.00122.34           C  
ANISOU 1029  CG  LEU A 160    19883  13453  13148   -879   2985   1444       C  
ATOM   1030  CD1 LEU A 160      38.671  21.245 -16.812  1.00122.08           C  
ANISOU 1030  CD1 LEU A 160    19958  13218  13210   -936   2919   1534       C  
ATOM   1031  CD2 LEU A 160      38.506  22.639 -14.734  1.00122.72           C  
ANISOU 1031  CD2 LEU A 160    20296  13452  12880   -833   3012   1540       C  
ATOM   1032  N   MET A 161      41.040  26.023 -16.917  1.00139.15           N  
ANISOU 1032  N   MET A 161    21635  15831  15404   -321   2273   1168       N  
ATOM   1033  CA  MET A 161      42.049  26.879 -17.519  1.00143.49           C  
ANISOU 1033  CA  MET A 161    22016  16432  16072   -180   2021   1088       C  
ATOM   1034  C   MET A 161      43.180  26.018 -18.058  1.00144.66           C  
ANISOU 1034  C   MET A 161    22180  16459  16323   -103   1808   1160       C  
ATOM   1035  O   MET A 161      43.445  24.924 -17.553  1.00147.19           O  
ANISOU 1035  O   MET A 161    22742  16639  16546   -107   1795   1284       O  
ATOM   1036  CB  MET A 161      42.603  27.900 -16.510  1.00149.04           C  
ANISOU 1036  CB  MET A 161    22870  17180  16576    -78   1895   1060       C  
ATOM   1037  CG  MET A 161      43.213  27.279 -15.260  1.00155.76           C  
ANISOU 1037  CG  MET A 161    24089  17921  17174    -37   1801   1187       C  
ATOM   1038  SD  MET A 161      44.006  28.503 -14.199  1.00159.44           S  
ANISOU 1038  SD  MET A 161    24724  18440  17415     76   1595   1138       S  
ATOM   1039  CE  MET A 161      45.341  29.053 -15.257  1.00157.58           C  
ANISOU 1039  CE  MET A 161    24213  18242  17419    188   1272   1075       C  
ATOM   1040  N   PHE A 162      43.842  26.521 -19.093  1.00143.49           N  
ANISOU 1040  N   PHE A 162    21783  16365  16373    -26   1650   1083       N  
ATOM   1041  CA  PHE A 162      44.995  25.836 -19.657  1.00143.58           C  
ANISOU 1041  CA  PHE A 162    21775  16285  16496     75   1449   1136       C  
ATOM   1042  C   PHE A 162      46.211  26.043 -18.763  1.00147.17           C  
ANISOU 1042  C   PHE A 162    22396  16716  16807    214   1204   1197       C  
ATOM   1043  O   PHE A 162      46.489  27.166 -18.327  1.00148.06           O  
ANISOU 1043  O   PHE A 162    22484  16927  16844    251   1108   1135       O  
ATOM   1044  CB  PHE A 162      45.282  26.342 -21.071  1.00139.61           C  
ANISOU 1044  CB  PHE A 162    20945  15860  16242    103   1381   1033       C  
ATOM   1045  CG  PHE A 162      44.345  25.796 -22.110  1.00137.09           C  
ANISOU 1045  CG  PHE A 162    20477  15531  16078    -17   1560    996       C  
ATOM   1046  CD1 PHE A 162      44.553  24.538 -22.656  1.00136.54           C  
ANISOU 1046  CD1 PHE A 162    20464  15325  16092    -28   1565   1056       C  
ATOM   1047  CD2 PHE A 162      43.261  26.538 -22.546  1.00134.94           C  
ANISOU 1047  CD2 PHE A 162    20019  15383  15870   -114   1715    898       C  
ATOM   1048  CE1 PHE A 162      43.694  24.030 -23.610  1.00135.00           C  
ANISOU 1048  CE1 PHE A 162    20148  15116  16028   -157   1714   1013       C  
ATOM   1049  CE2 PHE A 162      42.397  26.034 -23.501  1.00133.63           C  
ANISOU 1049  CE2 PHE A 162    19708  15222  15844   -233   1857    863       C  
ATOM   1050  CZ  PHE A 162      42.615  24.778 -24.033  1.00133.91           C  
ANISOU 1050  CZ  PHE A 162    19809  15120  15951   -267   1853    918       C  
ATOM   1051  N   LYS A 163      46.929  24.952 -18.481  1.00149.83           N  
ANISOU 1051  N   LYS A 163    22910  16917  17102    291   1095   1320       N  
ATOM   1052  CA  LYS A 163      48.159  25.058 -17.704  1.00152.54           C  
ANISOU 1052  CA  LYS A 163    23385  17247  17326    437    830   1388       C  
ATOM   1053  C   LYS A 163      49.234  25.827 -18.460  1.00154.46           C  
ANISOU 1053  C   LYS A 163    23351  17595  17744    541    610   1313       C  
ATOM   1054  O   LYS A 163      50.033  26.541 -17.845  1.00157.19           O  
ANISOU 1054  O   LYS A 163    23720  18008  17998    611    404   1308       O  
ATOM   1055  CB  LYS A 163      48.671  23.666 -17.332  1.00153.98           C  
ANISOU 1055  CB  LYS A 163    23805  17254  17444    520    763   1542       C  
ATOM   1056  CG  LYS A 163      47.654  22.789 -16.617  1.00154.90           C  
ANISOU 1056  CG  LYS A 163    24221  17244  17390    400    987   1634       C  
ATOM   1057  CD  LYS A 163      48.212  21.393 -16.357  1.00155.92           C  
ANISOU 1057  CD  LYS A 163    24599  17173  17472    493    911   1792       C  
ATOM   1058  CE  LYS A 163      47.187  20.502 -15.669  1.00156.87           C  
ANISOU 1058  CE  LYS A 163    25033  17151  17420    347   1147   1891       C  
ATOM   1059  NZ  LYS A 163      47.718  19.137 -15.396  1.00158.54           N  
ANISOU 1059  NZ  LYS A 163    25526  17137  17573    442   1074   2052       N  
ATOM   1060  N   SER A 164      49.269  25.695 -19.784  1.00158.05           N  
ANISOU 1060  N   SER A 164    23548  18064  18439    540    650   1254       N  
ATOM   1061  CA  SER A 164      50.266  26.341 -20.624  1.00150.68           C  
ANISOU 1061  CA  SER A 164    22339  17227  17684    626    474   1190       C  
ATOM   1062  C   SER A 164      49.719  27.636 -21.208  1.00145.70           C  
ANISOU 1062  C   SER A 164    21494  16730  17135    534    550   1050       C  
ATOM   1063  O   SER A 164      48.569  27.694 -21.653  1.00147.84           O  
ANISOU 1063  O   SER A 164    21715  17010  17447    424    765    994       O  
ATOM   1064  CB  SER A 164      50.700  25.412 -21.758  1.00151.40           C  
ANISOU 1064  CB  SER A 164    22299  17249  17978    696    477   1210       C  
ATOM   1065  OG  SER A 164      51.152  26.165 -22.865  1.00150.72           O  
ANISOU 1065  OG  SER A 164    21907  17275  18086    712    424   1112       O  
ATOM   1066  N   THR A 165      50.547  28.677 -21.201  1.00130.86           N  
ANISOU 1066  N   THR A 165    19489  14953  15281    577    367    998       N  
ATOM   1067  CA  THR A 165      50.174  29.949 -21.805  1.00118.54           C  
ANISOU 1067  CA  THR A 165    17736  13500  13804    506    415    872       C  
ATOM   1068  C   THR A 165      51.082  30.338 -22.961  1.00109.49           C  
ANISOU 1068  C   THR A 165    16310  12422  12872    550    296    827       C  
ATOM   1069  O   THR A 165      50.592  30.565 -24.072  1.00107.98           O  
ANISOU 1069  O   THR A 165    15937  12261  12829    503    416    758       O  
ATOM   1070  CB  THR A 165      50.164  31.063 -20.742  1.00119.22           C  
ANISOU 1070  CB  THR A 165    17953  13639  13708    479    339    830       C  
ATOM   1071  OG1 THR A 165      51.451  31.152 -20.120  1.00120.78           O  
ANISOU 1071  OG1 THR A 165    18201  13850  13840    556     71    881       O  
ATOM   1072  CG2 THR A 165      49.103  30.786 -19.685  1.00121.14           C  
ANISOU 1072  CG2 THR A 165    18462  13829  13735    425    510    859       C  
ATOM   1073  N   ALA A 166      52.397  30.395 -22.745  1.00101.94           N  
ANISOU 1073  N   ALA A 166    15305  11495  11931    638     64    870       N  
ATOM   1074  CA  ALA A 166      53.294  30.890 -23.785  1.00 94.43           C  
ANISOU 1074  CA  ALA A 166    14075  10628  11176    666    -38    826       C  
ATOM   1075  C   ALA A 166      53.512  29.856 -24.884  1.00 88.16           C  
ANISOU 1075  C   ALA A 166    13150   9791  10555    735     33    855       C  
ATOM   1076  O   ALA A 166      53.395  30.171 -26.076  1.00 82.59           O  
ANISOU 1076  O   ALA A 166    12246   9129  10005    702    115    787       O  
ATOM   1077  CB  ALA A 166      54.630  31.316 -23.175  1.00 96.12           C  
ANISOU 1077  CB  ALA A 166    14253  10909  11357    724   -310    860       C  
ATOM   1078  N   LYS A 167      53.843  28.615 -24.511  1.00 86.85           N  
ANISOU 1078  N   LYS A 167    13114   9531  10355    839      3    956       N  
ATOM   1079  CA  LYS A 167      54.039  27.611 -25.546  1.00 88.72           C  
ANISOU 1079  CA  LYS A 167    13259   9705  10746    914     79    975       C  
ATOM   1080  C   LYS A 167      52.723  27.247 -26.221  1.00 84.34           C  
ANISOU 1080  C   LYS A 167    12743   9082  10220    804    322    924       C  
ATOM   1081  O   LYS A 167      52.722  26.868 -27.397  1.00 83.80           O  
ANISOU 1081  O   LYS A 167    12543   8999  10299    816    405    887       O  
ATOM   1082  CB  LYS A 167      54.734  26.374 -24.980  1.00 95.00           C  
ANISOU 1082  CB  LYS A 167    14203  10395  11498   1069    -18   1098       C  
ATOM   1083  CG  LYS A 167      53.995  25.670 -23.886  1.00103.46           C  
ANISOU 1083  CG  LYS A 167    15597  11339  12374   1042     43   1177       C  
ATOM   1084  CD  LYS A 167      54.730  24.415 -23.451  1.00111.10           C  
ANISOU 1084  CD  LYS A 167    16719  12183  13310   1214    -58   1306       C  
ATOM   1085  CE  LYS A 167      53.997  23.729 -22.307  1.00116.87           C  
ANISOU 1085  CE  LYS A 167    17803  12776  13825   1174      6   1397       C  
ATOM   1086  NZ  LYS A 167      54.656  22.451 -21.901  1.00120.44           N  
ANISOU 1086  NZ  LYS A 167    18443  13080  14238   1350    -86   1534       N  
ATOM   1087  N   ARG A 168      51.596  27.387 -25.515  1.00 78.60           N  
ANISOU 1087  N   ARG A 168    12185   8326   9353    693    440    917       N  
ATOM   1088  CA  ARG A 168      50.298  27.226 -26.165  1.00 75.87           C  
ANISOU 1088  CA  ARG A 168    11825   7956   9046    567    659    859       C  
ATOM   1089  C   ARG A 168      50.121  28.254 -27.275  1.00 75.54           C  
ANISOU 1089  C   ARG A 168    11532   8029   9139    514    691    748       C  
ATOM   1090  O   ARG A 168      49.693  27.922 -28.390  1.00 74.07           O  
ANISOU 1090  O   ARG A 168    11241   7832   9071    474    798    702       O  
ATOM   1091  CB  ARG A 168      49.169  27.348 -25.142  1.00 78.15           C  
ANISOU 1091  CB  ARG A 168    12304   8227   9163    462    781    869       C  
ATOM   1092  CG  ARG A 168      47.780  27.526 -25.758  1.00 82.31           C  
ANISOU 1092  CG  ARG A 168    12753   8784   9736    322    993    794       C  
ATOM   1093  CD  ARG A 168      46.672  27.213 -24.764  1.00 89.28           C  
ANISOU 1093  CD  ARG A 168    13835   9627  10458    223   1150    830       C  
ATOM   1094  NE  ARG A 168      46.801  28.021 -23.554  1.00 94.63           N  
ANISOU 1094  NE  ARG A 168    14638  10353  10965    248   1088    839       N  
ATOM   1095  CZ  ARG A 168      46.161  29.167 -23.345  1.00 92.04           C  
ANISOU 1095  CZ  ARG A 168    14251  10126  10593    202   1151    759       C  
ATOM   1096  NH1 ARG A 168      45.333  29.646 -24.266  1.00 87.57           N  
ANISOU 1096  NH1 ARG A 168    13488   9635  10151    136   1272    672       N  
ATOM   1097  NH2 ARG A 168      46.357  29.831 -22.215  1.00 91.92           N  
ANISOU 1097  NH2 ARG A 168    14387  10134  10405    230   1087    764       N  
ATOM   1098  N   ALA A 169      50.443  29.521 -26.983  1.00 72.51           N  
ANISOU 1098  N   ALA A 169    11071   7750   8730    506    593    703       N  
ATOM   1099  CA  ALA A 169      50.340  30.554 -28.005  1.00 70.23           C  
ANISOU 1099  CA  ALA A 169    10569   7557   8559    461    612    609       C  
ATOM   1100  C   ALA A 169      51.300  30.286 -29.153  1.00 68.03           C  
ANISOU 1100  C   ALA A 169    10106   7296   8444    528    553    606       C  
ATOM   1101  O   ALA A 169      50.946  30.478 -30.317  1.00 66.43           O  
ANISOU 1101  O   ALA A 169     9767   7124   8351    487    640    545       O  
ATOM   1102  CB  ALA A 169      50.606  31.931 -27.405  1.00 69.92           C  
ANISOU 1102  CB  ALA A 169    10518   7596   8451    439    506    568       C  
ATOM   1103  N   ARG A 170      52.520  29.845 -28.842  1.00 71.34           N  
ANISOU 1103  N   ARG A 170    10520   7705   8879    639    406    672       N  
ATOM   1104  CA  ARG A 170      53.498  29.562 -29.888  1.00 78.42           C  
ANISOU 1104  CA  ARG A 170    11232   8630   9932    721    365    671       C  
ATOM   1105  C   ARG A 170      53.012  28.448 -30.811  1.00 77.37           C  
ANISOU 1105  C   ARG A 170    11121   8405   9870    736    516    663       C  
ATOM   1106  O   ARG A 170      53.085  28.565 -32.042  1.00 80.77           O  
ANISOU 1106  O   ARG A 170    11402   8870  10417    727    579    607       O  
ATOM   1107  CB  ARG A 170      54.840  29.190 -29.258  1.00 88.31           C  
ANISOU 1107  CB  ARG A 170    12473   9894  11184    856    181    753       C  
ATOM   1108  CG  ARG A 170      55.949  28.976 -30.264  1.00 95.94           C  
ANISOU 1108  CG  ARG A 170    13221  10915  12317    958    142    754       C  
ATOM   1109  CD  ARG A 170      57.196  28.425 -29.601  1.00105.46           C  
ANISOU 1109  CD  ARG A 170    14410  12133  13529   1116    -35    846       C  
ATOM   1110  NE  ARG A 170      58.321  28.362 -30.529  1.00112.70           N  
ANISOU 1110  NE  ARG A 170    15076  13132  14612   1217    -68    844       N  
ATOM   1111  CZ  ARG A 170      59.516  27.868 -30.224  1.00118.46           C  
ANISOU 1111  CZ  ARG A 170    15717  13900  15393   1382   -210    919       C  
ATOM   1112  NH1 ARG A 170      59.745  27.389 -29.006  1.00121.01           N  
ANISOU 1112  NH1 ARG A 170    16200  14175  15604   1464   -352   1006       N  
ATOM   1113  NH2 ARG A 170      60.479  27.850 -31.138  1.00119.57           N  
ANISOU 1113  NH2 ARG A 170    15607  14132  15694   1470   -208    909       N  
ATOM   1114  N   ASN A 171      52.514  27.356 -30.228  1.00 75.27           N  
ANISOU 1114  N   ASN A 171    11062   8012   9524    750    575    720       N  
ATOM   1115  CA  ASN A 171      51.968  26.266 -31.028  1.00 73.62           C  
ANISOU 1115  CA  ASN A 171    10913   7692   9366    737    717    708       C  
ATOM   1116  C   ASN A 171      50.783  26.734 -31.861  1.00 69.28           C  
ANISOU 1116  C   ASN A 171    10290   7184   8848    585    858    615       C  
ATOM   1117  O   ASN A 171      50.658  26.368 -33.039  1.00 71.43           O  
ANISOU 1117  O   ASN A 171    10491   7437   9213    573    934    565       O  
ATOM   1118  CB  ASN A 171      51.566  25.108 -30.118  1.00 73.50           C  
ANISOU 1118  CB  ASN A 171    11162   7524   9242    747    755    791       C  
ATOM   1119  CG  ASN A 171      52.757  24.477 -29.434  1.00 76.85           C  
ANISOU 1119  CG  ASN A 171    11668   7890   9643    927    609    892       C  
ATOM   1120  OD1 ASN A 171      53.893  24.608 -29.897  1.00 80.80           O  
ANISOU 1120  OD1 ASN A 171    12004   8450  10244   1057    505    893       O  
ATOM   1121  ND2 ASN A 171      52.509  23.796 -28.324  1.00 75.88           N  
ANISOU 1121  ND2 ASN A 171    11793   7655   9383    938    599    982       N  
ATOM   1122  N   SER A 172      49.908  27.554 -31.270  1.00 63.34           N  
ANISOU 1122  N   SER A 172     9558   6494   8015    479    891    591       N  
ATOM   1123  CA  SER A 172      48.778  28.090 -32.019  1.00 61.71           C  
ANISOU 1123  CA  SER A 172     9259   6347   7842    354   1008    508       C  
ATOM   1124  C   SER A 172      49.248  28.917 -33.204  1.00 62.01           C  
ANISOU 1124  C   SER A 172     9089   6480   7993    371    971    442       C  
ATOM   1125  O   SER A 172      48.714  28.786 -34.308  1.00 63.09           O  
ANISOU 1125  O   SER A 172     9152   6624   8196    316   1053    386       O  
ATOM   1126  CB  SER A 172      47.891  28.935 -31.106  1.00 63.24           C  
ANISOU 1126  CB  SER A 172     9498   6601   7932    276   1044    495       C  
ATOM   1127  OG  SER A 172      47.286  28.144 -30.098  1.00 66.46           O  
ANISOU 1127  OG  SER A 172    10101   6924   8226    235   1117    554       O  
ATOM   1128  N   ILE A 173      50.260  29.761 -32.996  1.00 62.06           N  
ANISOU 1128  N   ILE A 173     9008   6558   8016    436    845    451       N  
ATOM   1129  CA  ILE A 173      50.735  30.650 -34.054  1.00 60.03           C  
ANISOU 1129  CA  ILE A 173     8562   6390   7854    435    817    397       C  
ATOM   1130  C   ILE A 173      51.379  29.850 -35.186  1.00 64.68           C  
ANISOU 1130  C   ILE A 173     9079   6951   8546    500    847    392       C  
ATOM   1131  O   ILE A 173      51.179  30.145 -36.378  1.00 65.23           O  
ANISOU 1131  O   ILE A 173     9046   7059   8679    462    906    335       O  
ATOM   1132  CB  ILE A 173      51.702  31.690 -33.459  1.00 57.82           C  
ANISOU 1132  CB  ILE A 173     8219   6186   7564    465    671    414       C  
ATOM   1133  CG1 ILE A 173      50.940  32.682 -32.575  1.00 60.14           C  
ANISOU 1133  CG1 ILE A 173     8591   6507   7754    394    664    390       C  
ATOM   1134  CG2 ILE A 173      52.443  32.445 -34.556  1.00 57.31           C  
ANISOU 1134  CG2 ILE A 173     7965   6202   7607    465    641    378       C  
ATOM   1135  CD1 ILE A 173      51.837  33.615 -31.811  1.00 61.53           C  
ANISOU 1135  CD1 ILE A 173     8757   6730   7891    405    509    403       C  
ATOM   1136  N   VAL A 174      52.160  28.826 -34.835  1.00 64.63           N  
ANISOU 1136  N   VAL A 174     9138   6871   8548    609    808    453       N  
ATOM   1137  CA  VAL A 174      52.764  27.990 -35.865  1.00 67.48           C  
ANISOU 1137  CA  VAL A 174     9453   7189   8998    694    855    443       C  
ATOM   1138  C   VAL A 174      51.685  27.277 -36.665  1.00 68.00           C  
ANISOU 1138  C   VAL A 174     9604   7172   9060    612    993    390       C  
ATOM   1139  O   VAL A 174      51.748  27.211 -37.900  1.00 64.25           O  
ANISOU 1139  O   VAL A 174     9054   6711   8646    608   1055    333       O  
ATOM   1140  CB  VAL A 174      53.751  26.986 -35.248  1.00 67.64           C  
ANISOU 1140  CB  VAL A 174     9545   7132   9024    853    786    523       C  
ATOM   1141  CG1 VAL A 174      54.346  26.136 -36.353  1.00 67.09           C  
ANISOU 1141  CG1 VAL A 174     9435   7011   9046    960    855    503       C  
ATOM   1142  CG2 VAL A 174      54.837  27.710 -34.489  1.00 67.09           C  
ANISOU 1142  CG2 VAL A 174     9366   7165   8961    922    625    574       C  
ATOM   1143  N   ILE A 175      50.680  26.732 -35.976  1.00 68.26           N  
ANISOU 1143  N   ILE A 175     9799   7122   9014    534   1045    408       N  
ATOM   1144  CA  ILE A 175      49.570  26.098 -36.678  1.00 68.24           C  
ANISOU 1144  CA  ILE A 175     9866   7055   9009    421   1165    355       C  
ATOM   1145  C   ILE A 175      48.897  27.091 -37.612  1.00 64.96           C  
ANISOU 1145  C   ILE A 175     9302   6757   8623    320   1196    275       C  
ATOM   1146  O   ILE A 175      48.579  26.773 -38.763  1.00 62.37           O  
ANISOU 1146  O   ILE A 175     8952   6416   8331    277   1256    215       O  
ATOM   1147  CB  ILE A 175      48.572  25.512 -35.664  1.00 70.61           C  
ANISOU 1147  CB  ILE A 175    10338   7271   9217    327   1218    395       C  
ATOM   1148  CG1 ILE A 175      49.175  24.264 -35.016  1.00 75.07           C  
ANISOU 1148  CG1 ILE A 175    11094   7676   9751    427   1203    475       C  
ATOM   1149  CG2 ILE A 175      47.214  25.236 -36.331  1.00 71.35           C  
ANISOU 1149  CG2 ILE A 175    10442   7355   9312    159   1331    331       C  
ATOM   1150  CD1 ILE A 175      48.306  23.625 -33.961  1.00 78.77           C  
ANISOU 1150  CD1 ILE A 175    11763   8048  10118    333   1262    532       C  
ATOM   1151  N   ILE A 176      48.659  28.306 -37.121  1.00 62.27           N  
ANISOU 1151  N   ILE A 176     8878   6526   8257    287   1151    273       N  
ATOM   1152  CA  ILE A 176      47.980  29.321 -37.917  1.00 63.15           C  
ANISOU 1152  CA  ILE A 176     8864   6741   8389    209   1172    209       C  
ATOM   1153  C   ILE A 176      48.734  29.563 -39.215  1.00 61.05           C  
ANISOU 1153  C   ILE A 176     8489   6513   8194    254   1160    172       C  
ATOM   1154  O   ILE A 176      48.151  29.564 -40.305  1.00 62.30           O  
ANISOU 1154  O   ILE A 176     8611   6691   8369    193   1210    115       O  
ATOM   1155  CB  ILE A 176      47.826  30.614 -37.100  1.00 60.55           C  
ANISOU 1155  CB  ILE A 176     8489   6499   8019    200   1118    217       C  
ATOM   1156  CG1 ILE A 176      46.703  30.434 -36.086  1.00 60.99           C  
ANISOU 1156  CG1 ILE A 176     8640   6537   7995    131   1177    231       C  
ATOM   1157  CG2 ILE A 176      47.577  31.820 -38.022  1.00 56.13           C  
ANISOU 1157  CG2 ILE A 176     7795   6037   7496    169   1108    163       C  
ATOM   1158  CD1 ILE A 176      46.529  31.612 -35.166  1.00 65.84           C  
ANISOU 1158  CD1 ILE A 176     9250   7217   8550    137   1139    233       C  
ATOM   1159  N   TRP A 177      50.051  29.738 -39.112  1.00 56.53           N  
ANISOU 1159  N   TRP A 177     7863   5957   7660    358   1095    207       N  
ATOM   1160  CA  TRP A 177      50.852  30.000 -40.298  1.00 57.95           C  
ANISOU 1160  CA  TRP A 177     7930   6184   7904    401   1103    179       C  
ATOM   1161  C   TRP A 177      50.875  28.799 -41.249  1.00 62.88           C  
ANISOU 1161  C   TRP A 177     8620   6724   8549    430   1188    146       C  
ATOM   1162  O   TRP A 177      50.781  28.967 -42.468  1.00 62.78           O  
ANISOU 1162  O   TRP A 177     8561   6742   8550    401   1237     92       O  
ATOM   1163  CB  TRP A 177      52.262  30.402 -39.876  1.00 59.86           C  
ANISOU 1163  CB  TRP A 177     8077   6475   8190    497   1017    229       C  
ATOM   1164  CG  TRP A 177      52.371  31.857 -39.527  1.00 65.76           C  
ANISOU 1164  CG  TRP A 177     8737   7319   8930    442    941    233       C  
ATOM   1165  CD1 TRP A 177      52.332  32.412 -38.277  1.00 65.20           C  
ANISOU 1165  CD1 TRP A 177     8704   7261   8810    427    854    265       C  
ATOM   1166  CD2 TRP A 177      52.526  32.945 -40.446  1.00 66.07           C  
ANISOU 1166  CD2 TRP A 177     8665   7440   9000    391    946    202       C  
ATOM   1167  NE1 TRP A 177      52.458  33.777 -38.361  1.00 63.27           N  
ANISOU 1167  NE1 TRP A 177     8382   7090   8568    369    803    248       N  
ATOM   1168  CE2 TRP A 177      52.578  34.134 -39.679  1.00 65.28           C  
ANISOU 1168  CE2 TRP A 177     8545   7385   8874    344    858    215       C  
ATOM   1169  CE3 TRP A 177      52.633  33.028 -41.840  1.00 66.61           C  
ANISOU 1169  CE3 TRP A 177     8672   7536   9102    378   1019    165       C  
ATOM   1170  CZ2 TRP A 177      52.732  35.397 -40.259  1.00 63.66           C  
ANISOU 1170  CZ2 TRP A 177     8262   7240   8684    283    840    198       C  
ATOM   1171  CZ3 TRP A 177      52.790  34.276 -42.418  1.00 65.65           C  
ANISOU 1171  CZ3 TRP A 177     8468   7486   8989    318   1003    155       C  
ATOM   1172  CH2 TRP A 177      52.838  35.449 -41.624  1.00 66.41           C  
ANISOU 1172  CH2 TRP A 177     8549   7615   9069    270    914    174       C  
ATOM   1173  N   ILE A 178      50.993  27.578 -40.712  1.00 67.07           N  
ANISOU 1173  N   ILE A 178     9282   7135   9068    487   1207    176       N  
ATOM   1174  CA  ILE A 178      51.082  26.395 -41.568  1.00 65.79           C  
ANISOU 1174  CA  ILE A 178     9215   6864   8920    525   1288    140       C  
ATOM   1175  C   ILE A 178      49.772  26.181 -42.312  1.00 64.50           C  
ANISOU 1175  C   ILE A 178     9116   6675   8716    374   1353     68       C  
ATOM   1176  O   ILE A 178      49.750  25.969 -43.532  1.00 68.23           O  
ANISOU 1176  O   ILE A 178     9591   7140   9193    360   1405      3       O  
ATOM   1177  CB  ILE A 178      51.461  25.154 -40.742  1.00 70.31           C  
ANISOU 1177  CB  ILE A 178     9943   7289   9483    624   1287    197       C  
ATOM   1178  CG1 ILE A 178      52.909  25.251 -40.269  1.00 70.92           C  
ANISOU 1178  CG1 ILE A 178     9931   7404   9612    802   1213    262       C  
ATOM   1179  CG2 ILE A 178      51.258  23.875 -41.567  1.00 74.07           C  
ANISOU 1179  CG2 ILE A 178    10575   7614   9954    634   1382    147       C  
ATOM   1180  CD1 ILE A 178      53.290  24.105 -39.344  1.00 77.12           C  
ANISOU 1180  CD1 ILE A 178    10876   8046  10379    921   1188    334       C  
ATOM   1181  N   VAL A 179      48.661  26.217 -41.583  1.00 63.04           N  
ANISOU 1181  N   VAL A 179     8982   6482   8487    257   1350     79       N  
ATOM   1182  CA  VAL A 179      47.354  26.097 -42.214  1.00 66.57           C  
ANISOU 1182  CA  VAL A 179     9450   6936   8906     99   1396     15       C  
ATOM   1183  C   VAL A 179      47.171  27.193 -43.259  1.00 66.66           C  
ANISOU 1183  C   VAL A 179     9317   7081   8928     67   1376    -36       C  
ATOM   1184  O   VAL A 179      46.710  26.929 -44.375  1.00 62.71           O  
ANISOU 1184  O   VAL A 179     8834   6578   8415      0   1404   -102       O  
ATOM   1185  CB  VAL A 179      46.247  26.126 -41.140  1.00 71.79           C  
ANISOU 1185  CB  VAL A 179    10146   7604   9528    -12   1404     45       C  
ATOM   1186  CG1 VAL A 179      44.863  26.236 -41.775  1.00 74.20           C  
ANISOU 1186  CG1 VAL A 179    10405   7965   9820   -177   1435    -17       C  
ATOM   1187  CG2 VAL A 179      46.326  24.874 -40.276  1.00 76.03           C  
ANISOU 1187  CG2 VAL A 179    10869   7981  10037     -3   1439     97       C  
ATOM   1188  N   SER A 180      47.557  28.432 -42.926  1.00 65.04           N  
ANISOU 1188  N   SER A 180     8988   6987   8739    111   1320     -6       N  
ATOM   1189  CA  SER A 180      47.341  29.545 -43.842  1.00 60.22           C  
ANISOU 1189  CA  SER A 180     8263   6488   8129     79   1298    -42       C  
ATOM   1190  C   SER A 180      48.131  29.368 -45.128  1.00 60.39           C  
ANISOU 1190  C   SER A 180     8277   6506   8164    128   1329    -77       C  
ATOM   1191  O   SER A 180      47.593  29.553 -46.226  1.00 61.67           O  
ANISOU 1191  O   SER A 180     8431   6703   8296     66   1342   -130       O  
ATOM   1192  CB  SER A 180      47.719  30.852 -43.157  1.00 55.46           C  
ANISOU 1192  CB  SER A 180     7564   5970   7537    117   1235      0       C  
ATOM   1193  OG  SER A 180      46.687  31.266 -42.294  1.00 56.71           O  
ANISOU 1193  OG  SER A 180     7723   6158   7665     58   1223      8       O  
ATOM   1194  N   CYS A 181      49.402  28.987 -45.009  1.00 60.51           N  
ANISOU 1194  N   CYS A 181     8293   6483   8216    246   1343    -48       N  
ATOM   1195  CA  CYS A 181      50.237  28.770 -46.182  1.00 64.79           C  
ANISOU 1195  CA  CYS A 181     8824   7025   8770    310   1399    -80       C  
ATOM   1196  C   CYS A 181      49.751  27.599 -47.023  1.00 66.16           C  
ANISOU 1196  C   CYS A 181     9140   7096   8902    277   1468   -149       C  
ATOM   1197  O   CYS A 181      49.911  27.614 -48.250  1.00 72.04           O  
ANISOU 1197  O   CYS A 181     9898   7859   9617    275   1516   -202       O  
ATOM   1198  CB  CYS A 181      51.682  28.534 -45.752  1.00 66.50           C  
ANISOU 1198  CB  CYS A 181     8987   7233   9047    457   1403    -29       C  
ATOM   1199  SG  CYS A 181      52.470  30.012 -45.147  1.00 65.20           S  
ANISOU 1199  SG  CYS A 181     8643   7203   8928    471   1319     34       S  
ATOM   1200  N  AILE A 182      49.168  26.577 -46.392  0.50 62.41           N  
ANISOU 1200  N  AILE A 182     8793   6506   8415    242   1477   -150       N  
ATOM   1201  N  BILE A 182      49.151  26.585 -46.402  0.50 62.40           N  
ANISOU 1201  N  BILE A 182     8790   6505   8412    240   1477   -151       N  
ATOM   1202  CA AILE A 182      48.702  25.424 -47.153  0.50 63.03           C  
ANISOU 1202  CA AILE A 182     9033   6465   8451    191   1536   -221       C  
ATOM   1203  CA BILE A 182      48.716  25.434 -47.181  0.50 63.02           C  
ANISOU 1203  CA BILE A 182     9031   6466   8450    192   1537   -222       C  
ATOM   1204  C  AILE A 182      47.410  25.746 -47.892  0.50 62.32           C  
ANISOU 1204  C  AILE A 182     8939   6434   8307     21   1511   -284       C  
ATOM   1205  C  BILE A 182      47.397  25.721 -47.888  0.50 62.36           C  
ANISOU 1205  C  BILE A 182     8946   6436   8311     19   1512   -284       C  
ATOM   1206  O  AILE A 182      47.259  25.424 -49.075  0.50 63.05           O  
ANISOU 1206  O  AILE A 182     9102   6506   8350    -17   1540   -358       O  
ATOM   1207  O  BILE A 182      47.219  25.363 -49.057  0.50 63.09           O  
ANISOU 1207  O  BILE A 182     9114   6503   8353    -22   1541   -359       O  
ATOM   1208  CB AILE A 182      48.529  24.200 -46.235  0.50 63.50           C  
ANISOU 1208  CB AILE A 182     9251   6364   8513    195   1555   -195       C  
ATOM   1209  CB BILE A 182      48.622  24.182 -46.288  0.50 63.58           C  
ANISOU 1209  CB BILE A 182     9261   6371   8524    207   1558   -196       C  
ATOM   1210  CG1AILE A 182      49.891  23.704 -45.763  0.50 63.88           C  
ANISOU 1210  CG1AILE A 182     9322   6340   8608    395   1575   -142       C  
ATOM   1211  CG1BILE A 182      50.017  23.758 -45.825  0.50 63.87           C  
ANISOU 1211  CG1BILE A 182     9309   6348   8611    410   1577   -142       C  
ATOM   1212  CG2AILE A 182      47.806  23.094 -46.983  0.50 64.87           C  
ANISOU 1212  CG2AILE A 182     9607   6406   8636     89   1604   -276       C  
ATOM   1213  CG2BILE A 182      47.952  23.048 -47.046  0.50 64.87           C  
ANISOU 1213  CG2BILE A 182     9612   6398   8637    110   1610   -278       C  
ATOM   1214  CD1AILE A 182      50.822  23.354 -46.896  0.50 65.52           C  
ANISOU 1214  CD1AILE A 182     9549   6521   8824    518   1649   -193       C  
ATOM   1215  CD1BILE A 182      50.025  22.545 -44.924  0.50 63.76           C  
ANISOU 1215  CD1BILE A 182     9474   6156   8594    452   1590   -101       C  
ATOM   1216  N   ILE A 183      46.455  26.382 -47.213  1.00 61.19           N  
ANISOU 1216  N   ILE A 183     8713   6370   8167    -77   1456   -256       N  
ATOM   1217  CA  ILE A 183      45.135  26.540 -47.810  1.00 66.68           C  
ANISOU 1217  CA  ILE A 183     9389   7123   8822   -233   1424   -310       C  
ATOM   1218  C   ILE A 183      45.132  27.530 -48.960  1.00 65.47           C  
ANISOU 1218  C   ILE A 183     9150   7089   8637   -231   1388   -341       C  
ATOM   1219  O   ILE A 183      44.239  27.467 -49.807  1.00 67.43           O  
ANISOU 1219  O   ILE A 183     9413   7372   8836   -341   1356   -400       O  
ATOM   1220  CB  ILE A 183      44.082  26.947 -46.764  1.00 66.76           C  
ANISOU 1220  CB  ILE A 183     9317   7198   8849   -322   1391   -272       C  
ATOM   1221  CG1 ILE A 183      44.412  28.297 -46.138  1.00 63.95           C  
ANISOU 1221  CG1 ILE A 183     8821   6955   8520   -237   1351   -213       C  
ATOM   1222  CG2 ILE A 183      43.940  25.868 -45.690  1.00 72.25           C  
ANISOU 1222  CG2 ILE A 183    10130   7767   9555   -355   1436   -239       C  
ATOM   1223  CD1 ILE A 183      43.331  28.758 -45.213  1.00 63.23           C  
ANISOU 1223  CD1 ILE A 183     8655   6934   8435   -308   1335   -188       C  
ATOM   1224  N   MET A 184      46.099  28.442 -49.023  1.00 63.62           N  
ANISOU 1224  N   MET A 184     8832   6918   8424   -119   1387   -301       N  
ATOM   1225  CA  MET A 184      46.147  29.414 -50.109  1.00 64.55           C  
ANISOU 1225  CA  MET A 184     8891   7134   8501   -119   1362   -317       C  
ATOM   1226  C   MET A 184      46.984  28.939 -51.297  1.00 66.34           C  
ANISOU 1226  C   MET A 184     9207   7317   8681    -68   1431   -364       C  
ATOM   1227  O   MET A 184      47.271  29.734 -52.197  1.00 68.25           O  
ANISOU 1227  O   MET A 184     9417   7633   8882    -54   1430   -365       O  
ATOM   1228  CB  MET A 184      46.672  30.760 -49.601  1.00 60.41           C  
ANISOU 1228  CB  MET A 184     8239   6698   8017    -54   1328   -249       C  
ATOM   1229  CG  MET A 184      45.729  31.479 -48.650  1.00 56.67           C  
ANISOU 1229  CG  MET A 184     7685   6282   7563    -97   1263   -217       C  
ATOM   1230  SD  MET A 184      44.021  31.462 -49.231  1.00 59.44           S  
ANISOU 1230  SD  MET A 184     8022   6695   7869   -222   1209   -268       S  
ATOM   1231  CE  MET A 184      43.175  32.333 -47.916  1.00 60.43           C  
ANISOU 1231  CE  MET A 184     8036   6891   8035   -223   1171   -222       C  
ATOM   1232  N  AILE A 185      47.369  27.667 -51.323  0.50 65.00           N  
ANISOU 1232  N  AILE A 185     9165   7022   8511    -36   1498   -400       N  
ATOM   1233  N  BILE A 185      47.385  27.663 -51.300  0.50 65.00           N  
ANISOU 1233  N  BILE A 185     9164   7020   8512    -34   1499   -399       N  
ATOM   1234  CA AILE A 185      48.116  27.119 -52.455  0.50 65.47           C  
ANISOU 1234  CA AILE A 185     9330   7028   8516     25   1584   -457       C  
ATOM   1235  CA BILE A 185      48.109  27.125 -52.456  0.50 65.46           C  
ANISOU 1235  CA BILE A 185     9328   7028   8515     24   1583   -457       C  
ATOM   1236  C  AILE A 185      47.281  27.180 -53.737  0.50 65.23           C  
ANISOU 1236  C  AILE A 185     9380   7029   8375    -89   1554   -534       C  
ATOM   1237  C  BILE A 185      47.269  27.191 -53.725  0.50 65.19           C  
ANISOU 1237  C  BILE A 185     9373   7026   8371    -90   1552   -533       C  
ATOM   1238  O  AILE A 185      47.814  27.593 -54.778  0.50 66.13           O  
ANISOU 1238  O  AILE A 185     9513   7189   8426    -49   1596   -553       O  
ATOM   1239  O  BILE A 185      47.796  27.622 -54.760  0.50 66.09           O  
ANISOU 1239  O  BILE A 185     9502   7186   8421    -51   1594   -551       O  
ATOM   1240  CB AILE A 185      48.603  25.691 -52.161  0.50 67.15           C  
ANISOU 1240  CB AILE A 185     9690   7076   8749     96   1661   -485       C  
ATOM   1241  CB BILE A 185      48.618  25.704 -52.143  0.50 67.13           C  
ANISOU 1241  CB BILE A 185     9684   7074   8748     98   1660   -483       C  
ATOM   1242  CG1AILE A 185      49.700  25.740 -51.086  0.50 66.11           C  
ANISOU 1242  CG1AILE A 185     9466   6936   8717    246   1684   -401       C  
ATOM   1243  CG1BILE A 185      49.671  25.752 -51.035  0.50 66.04           C  
ANISOU 1243  CG1BILE A 185     9454   6928   8710    244   1680   -398       C  
ATOM   1244  CG2AILE A 185      49.093  25.018 -53.444  0.50 67.81           C  
ANISOU 1244  CG2AILE A 185     9922   7090   8753    143   1756   -570       C  
ATOM   1245  CG2BILE A 185      49.161  25.045 -53.410  0.50 67.83           C  
ANISOU 1245  CG2BILE A 185     9917   7095   8760    152   1758   -565       C  
ATOM   1246  CD1AILE A 185      50.289  24.379 -50.732  0.50 66.43           C  
ANISOU 1246  CD1AILE A 185     9649   6809   8783    357   1753   -411       C  
ATOM   1247  CD1BILE A 185      50.883  26.570 -51.369  0.50 65.53           C  
ANISOU 1247  CD1BILE A 185     9253   6967   8679    361   1722   -360       C  
ATOM   1248  N   PRO A 186      45.989  26.802 -53.725  1.00 63.53           N  
ANISOU 1248  N   PRO A 186     9210   6800   8128   -235   1478   -575       N  
ATOM   1249  CA  PRO A 186      45.193  26.966 -54.963  1.00 63.89           C  
ANISOU 1249  CA  PRO A 186     9314   6900   8063   -344   1419   -644       C  
ATOM   1250  C   PRO A 186      45.179  28.384 -55.485  1.00 66.47           C  
ANISOU 1250  C   PRO A 186     9523   7374   8357   -323   1364   -599       C  
ATOM   1251  O   PRO A 186      45.217  28.593 -56.707  1.00 69.05           O  
ANISOU 1251  O   PRO A 186     9928   7732   8574   -338   1361   -640       O  
ATOM   1252  CB  PRO A 186      43.785  26.527 -54.536  1.00 64.15           C  
ANISOU 1252  CB  PRO A 186     9336   6931   8105   -509   1328   -669       C  
ATOM   1253  CG  PRO A 186      44.014  25.587 -53.419  1.00 63.60           C  
ANISOU 1253  CG  PRO A 186     9317   6733   8114   -493   1389   -650       C  
ATOM   1254  CD  PRO A 186      45.211  26.100 -52.681  1.00 59.76           C  
ANISOU 1254  CD  PRO A 186     8747   6255   7702   -320   1450   -567       C  
ATOM   1255  N   GLN A 187      45.143  29.369 -54.584  1.00 65.74           N  
ANISOU 1255  N   GLN A 187     9269   7363   8348   -287   1324   -516       N  
ATOM   1256  CA  GLN A 187      45.169  30.761 -55.007  1.00 61.90           C  
ANISOU 1256  CA  GLN A 187     8692   6991   7835   -260   1275   -466       C  
ATOM   1257  C   GLN A 187      46.404  31.047 -55.851  1.00 61.99           C  
ANISOU 1257  C   GLN A 187     8755   7000   7797   -177   1368   -458       C  
ATOM   1258  O   GLN A 187      46.312  31.653 -56.925  1.00 61.13           O  
ANISOU 1258  O   GLN A 187     8690   6948   7589   -196   1348   -463       O  
ATOM   1259  CB  GLN A 187      45.121  31.684 -53.787  1.00 60.18           C  
ANISOU 1259  CB  GLN A 187     8324   6825   7716   -220   1238   -385       C  
ATOM   1260  CG  GLN A 187      44.955  33.155 -54.162  1.00 62.79           C  
ANISOU 1260  CG  GLN A 187     8583   7253   8019   -201   1173   -334       C  
ATOM   1261  CD  GLN A 187      43.617  33.422 -54.846  1.00 63.24           C  
ANISOU 1261  CD  GLN A 187     8638   7383   8006   -276   1062   -362       C  
ATOM   1262  OE1 GLN A 187      42.561  32.982 -54.382  1.00 63.14           O  
ANISOU 1262  OE1 GLN A 187     8578   7390   8023   -343   1007   -388       O  
ATOM   1263  NE2 GLN A 187      43.663  34.111 -55.968  1.00 60.26           N  
ANISOU 1263  NE2 GLN A 187     8310   7051   7534   -269   1028   -354       N  
ATOM   1264  N   ALA A 188      47.570  30.613 -55.377  1.00 61.02           N  
ANISOU 1264  N   ALA A 188     8624   6819   7742    -82   1474   -440       N  
ATOM   1265  CA  ALA A 188      48.796  30.825 -56.127  1.00 61.14           C  
ANISOU 1265  CA  ALA A 188     8658   6846   7725     -2   1585   -430       C  
ATOM   1266  C   ALA A 188      48.810  30.007 -57.413  1.00 65.40           C  
ANISOU 1266  C   ALA A 188     9376   7335   8138    -15   1654   -520       C  
ATOM   1267  O   ALA A 188      49.381  30.452 -58.415  1.00 61.24           O  
ANISOU 1267  O   ALA A 188     8890   6851   7528      9   1724   -520       O  
ATOM   1268  CB  ALA A 188      50.005  30.484 -55.258  1.00 60.29           C  
ANISOU 1268  CB  ALA A 188     8472   6703   7733    113   1670   -390       C  
ATOM   1269  N   ILE A 189      48.174  28.830 -57.413  1.00 66.60           N  
ANISOU 1269  N   ILE A 189     9652   7390   8264    -64   1638   -599       N  
ATOM   1270  CA  ILE A 189      48.156  28.015 -58.627  1.00 63.74           C  
ANISOU 1270  CA  ILE A 189     9492   6962   7765    -85   1697   -699       C  
ATOM   1271  C   ILE A 189      47.366  28.702 -59.732  1.00 60.93           C  
ANISOU 1271  C   ILE A 189     9191   6693   7267   -185   1606   -721       C  
ATOM   1272  O   ILE A 189      47.793  28.719 -60.893  1.00 62.53           O  
ANISOU 1272  O   ILE A 189     9519   6900   7338   -166   1678   -760       O  
ATOM   1273  CB  ILE A 189      47.611  26.611 -58.326  1.00 66.50           C  
ANISOU 1273  CB  ILE A 189     9981   7169   8119   -137   1689   -779       C  
ATOM   1274  CG1 ILE A 189      48.602  25.846 -57.465  1.00 70.37           C  
ANISOU 1274  CG1 ILE A 189    10465   7552   8719      0   1799   -758       C  
ATOM   1275  CG2 ILE A 189      47.378  25.829 -59.608  1.00 68.17           C  
ANISOU 1275  CG2 ILE A 189    10428   7305   8169   -192   1718   -897       C  
ATOM   1276  CD1 ILE A 189      48.110  24.485 -57.083  1.00 76.12           C  
ANISOU 1276  CD1 ILE A 189    11353   8116   9454    -48   1797   -822       C  
ATOM   1277  N   VAL A 190      46.218  29.296 -59.403  1.00 58.24           N  
ANISOU 1277  N   VAL A 190     8759   6426   6943   -282   1449   -691       N  
ATOM   1278  CA  VAL A 190      45.387  29.831 -60.480  1.00 59.94           C  
ANISOU 1278  CA  VAL A 190     9036   6720   7017   -368   1339   -714       C  
ATOM   1279  C   VAL A 190      45.862  31.187 -61.005  1.00 64.78           C  
ANISOU 1279  C   VAL A 190     9602   7431   7582   -313   1347   -632       C  
ATOM   1280  O   VAL A 190      45.419  31.607 -62.084  1.00 63.69           O  
ANISOU 1280  O   VAL A 190     9558   7344   7295   -359   1279   -646       O  
ATOM   1281  CB  VAL A 190      43.919  29.968 -60.058  1.00 57.70           C  
ANISOU 1281  CB  VAL A 190     8661   6497   6764   -483   1162   -714       C  
ATOM   1282  CG1 VAL A 190      43.357  28.637 -59.674  1.00 53.60           C  
ANISOU 1282  CG1 VAL A 190     8209   5882   6273   -578   1151   -795       C  
ATOM   1283  CG2 VAL A 190      43.793  30.967 -58.923  1.00 59.46           C  
ANISOU 1283  CG2 VAL A 190     8675   6791   7125   -434   1122   -613       C  
ATOM   1284  N   MET A 191      46.755  31.885 -60.304  1.00 62.88           N  
ANISOU 1284  N   MET A 191     9231   7210   7451   -226   1421   -547       N  
ATOM   1285  CA  MET A 191      47.165  33.205 -60.774  1.00 62.81           C  
ANISOU 1285  CA  MET A 191     9189   7277   7398   -199   1427   -465       C  
ATOM   1286  C   MET A 191      48.037  33.071 -62.017  1.00 67.57           C  
ANISOU 1286  C   MET A 191     9940   7872   7862   -173   1564   -491       C  
ATOM   1287  O   MET A 191      49.016  32.319 -62.019  1.00 71.08           O  
ANISOU 1287  O   MET A 191    10412   8263   8333   -108   1720   -526       O  
ATOM   1288  CB  MET A 191      47.913  33.965 -59.678  1.00 59.41           C  
ANISOU 1288  CB  MET A 191     8588   6864   7120   -138   1466   -373       C  
ATOM   1289  CG  MET A 191      47.104  34.162 -58.403  1.00 54.17           C  
ANISOU 1289  CG  MET A 191     7794   6209   6580   -153   1349   -347       C  
ATOM   1290  SD  MET A 191      45.473  34.851 -58.731  1.00 58.25           S  
ANISOU 1290  SD  MET A 191     8307   6797   7027   -221   1159   -342       S  
ATOM   1291  CE  MET A 191      45.933  36.435 -59.379  1.00 53.27           C  
ANISOU 1291  CE  MET A 191     7694   6214   6330   -187   1153   -248       C  
ATOM   1292  N   GLU A 192      47.675  33.794 -63.081  1.00 65.56           N  
ANISOU 1292  N   GLU A 192     9787   7670   7452   -214   1510   -472       N  
ATOM   1293  CA  GLU A 192      48.423  33.763 -64.329  1.00 71.26           C  
ANISOU 1293  CA  GLU A 192    10671   8393   8011   -199   1645   -491       C  
ATOM   1294  C   GLU A 192      48.504  35.155 -64.937  1.00 72.17           C  
ANISOU 1294  C   GLU A 192    10808   8576   8038   -215   1619   -390       C  
ATOM   1295  O   GLU A 192      47.577  35.965 -64.823  1.00 75.91           O  
ANISOU 1295  O   GLU A 192    11250   9089   8504   -248   1446   -338       O  
ATOM   1296  CB  GLU A 192      47.796  32.805 -65.369  1.00 74.23           C  
ANISOU 1296  CB  GLU A 192    11267   8731   8205   -254   1610   -608       C  
ATOM   1297  CG  GLU A 192      47.682  31.345 -64.933  1.00 74.97           C  
ANISOU 1297  CG  GLU A 192    11400   8727   8357   -254   1641   -718       C  
ATOM   1298  CD  GLU A 192      49.026  30.646 -64.827  1.00 79.82           C  
ANISOU 1298  CD  GLU A 192    12031   9275   9024   -144   1870   -746       C  
ATOM   1299  OE1 GLU A 192      50.048  31.246 -65.206  1.00 82.81           O  
ANISOU 1299  OE1 GLU A 192    12383   9699   9382    -80   2016   -689       O  
ATOM   1300  OE2 GLU A 192      49.060  29.487 -64.357  1.00 83.96           O  
ANISOU 1300  OE2 GLU A 192    12589   9698   9613   -119   1908   -821       O  
ATOM   1301  N   CYS A 193      49.634  35.413 -65.584  1.00 71.49           N  
ANISOU 1301  N   CYS A 193    10778   8499   7885   -187   1801   -360       N  
ATOM   1302  CA  CYS A 193      49.799  36.558 -66.468  1.00 73.92           C  
ANISOU 1302  CA  CYS A 193    11180   8853   8054   -217   1814   -274       C  
ATOM   1303  C   CYS A 193      49.194  36.247 -67.830  1.00 74.15           C  
ANISOU 1303  C   CYS A 193    11460   8884   7829   -257   1768   -334       C  
ATOM   1304  O   CYS A 193      49.479  35.208 -68.432  1.00 75.15           O  
ANISOU 1304  O   CYS A 193    11720   8977   7858   -246   1877   -436       O  
ATOM   1305  CB  CYS A 193      51.276  36.915 -66.624  1.00 76.37           C  
ANISOU 1305  CB  CYS A 193    11443   9182   8393   -191   2047   -216       C  
ATOM   1306  SG  CYS A 193      51.952  37.790 -65.234  1.00 74.88           S  
ANISOU 1306  SG  CYS A 193    10987   9011   8454   -182   2052   -111       S  
ATOM   1307  N   SER A 194      48.326  37.126 -68.296  1.00 76.64           N  
ANISOU 1307  N   SER A 194    11852   9234   8035   -297   1596   -275       N  
ATOM   1308  CA  SER A 194      47.803  37.011 -69.644  1.00 77.90           C  
ANISOU 1308  CA  SER A 194    12261   9408   7931   -338   1534   -312       C  
ATOM   1309  C   SER A 194      48.037  38.337 -70.353  1.00 78.39           C  
ANISOU 1309  C   SER A 194    12426   9497   7859   -348   1542   -183       C  
ATOM   1310  O   SER A 194      47.769  39.404 -69.790  1.00 78.45           O  
ANISOU 1310  O   SER A 194    12328   9515   7965   -337   1441    -77       O  
ATOM   1311  CB  SER A 194      46.323  36.609 -69.638  1.00 80.66           C  
ANISOU 1311  CB  SER A 194    12625   9776   8246   -380   1274   -376       C  
ATOM   1312  OG  SER A 194      45.549  37.491 -68.850  1.00 89.80           O  
ANISOU 1312  OG  SER A 194    13613  10971   9535   -365   1095   -292       O  
ATOM   1313  N   THR A 195      48.587  38.267 -71.562  1.00 81.24           N  
ANISOU 1313  N   THR A 195    13012   9861   7996   -365   1681   -192       N  
ATOM   1314  CA  THR A 195      48.847  39.442 -72.381  1.00 84.27           C  
ANISOU 1314  CA  THR A 195    13544  10259   8214   -388   1710    -67       C  
ATOM   1315  C   THR A 195      47.732  39.585 -73.406  1.00 91.07           C  
ANISOU 1315  C   THR A 195    14636  11141   8825   -414   1494    -74       C  
ATOM   1316  O   THR A 195      47.367  38.613 -74.073  1.00 95.40           O  
ANISOU 1316  O   THR A 195    15335  11692   9219   -436   1463   -194       O  
ATOM   1317  CB  THR A 195      50.196  39.330 -73.094  1.00 86.35           C  
ANISOU 1317  CB  THR A 195    13913  10523   8372   -396   2019    -60       C  
ATOM   1318  OG1 THR A 195      51.239  39.091 -72.142  1.00 86.32           O  
ANISOU 1318  OG1 THR A 195    13670  10518   8611   -365   2206    -61       O  
ATOM   1319  CG2 THR A 195      50.508  40.602 -73.870  1.00 90.86           C  
ANISOU 1319  CG2 THR A 195    14640  11101   8780   -440   2066     86       C  
ATOM   1320  N   VAL A 196      47.204  40.793 -73.536  1.00 94.69           N  
ANISOU 1320  N   VAL A 196    15132  11609   9236   -409   1338     53       N  
ATOM   1321  CA  VAL A 196      46.170  41.109 -74.510  1.00 97.48           C  
ANISOU 1321  CA  VAL A 196    15697  11992   9350   -417   1111     75       C  
ATOM   1322  C   VAL A 196      46.752  42.079 -75.528  1.00 93.32           C  
ANISOU 1322  C   VAL A 196    15416  11445   8597   -434   1215    201       C  
ATOM   1323  O   VAL A 196      47.495  43.003 -75.172  1.00 86.71           O  
ANISOU 1323  O   VAL A 196    14522  10571   7852   -436   1345    320       O  
ATOM   1324  CB  VAL A 196      44.915  41.695 -73.832  1.00105.65           C  
ANISOU 1324  CB  VAL A 196    16578  13054  10510   -370    814    124       C  
ATOM   1325  CG1 VAL A 196      43.803  41.908 -74.852  1.00112.11           C  
ANISOU 1325  CG1 VAL A 196    17590  13922  11085   -367    554    139       C  
ATOM   1326  CG2 VAL A 196      44.443  40.772 -72.712  1.00105.14           C  
ANISOU 1326  CG2 VAL A 196    16255  13008  10687   -367    752     11       C  
ATOM   1327  N   PHE A 197      46.428  41.853 -76.799  1.00 99.49           N  
ANISOU 1327  N   PHE A 197    16485  12246   9071   -460   1159    175       N  
ATOM   1328  CA  PHE A 197      46.921  42.680 -77.893  1.00106.18           C  
ANISOU 1328  CA  PHE A 197    17615  13075   9655   -485   1259    292       C  
ATOM   1329  C   PHE A 197      45.776  43.500 -78.468  1.00113.66           C  
ANISOU 1329  C   PHE A 197    18722  14036  10428   -453    948    388       C  
ATOM   1330  O   PHE A 197      44.994  42.987 -79.284  1.00117.47           O  
ANISOU 1330  O   PHE A 197    19380  14563  10692   -463    768    318       O  
ATOM   1331  CB  PHE A 197      47.557  41.813 -78.983  1.00107.71           C  
ANISOU 1331  CB  PHE A 197    18056  13276   9592   -530   1467    195       C  
ATOM   1332  CG  PHE A 197      48.848  41.171 -78.572  1.00105.76           C  
ANISOU 1332  CG  PHE A 197    17677  13016   9491   -537   1810    129       C  
ATOM   1333  CD1 PHE A 197      48.852  40.052 -77.761  1.00102.92           C  
ANISOU 1333  CD1 PHE A 197    17109  12656   9341   -511   1832    -15       C  
ATOM   1334  CD2 PHE A 197      50.058  41.673 -79.017  1.00107.52           C  
ANISOU 1334  CD2 PHE A 197    17984  13231   9638   -569   2112    215       C  
ATOM   1335  CE1 PHE A 197      50.040  39.457 -77.382  1.00103.32           C  
ANISOU 1335  CE1 PHE A 197    17033  12696   9527   -492   2135    -69       C  
ATOM   1336  CE2 PHE A 197      51.250  41.079 -78.648  1.00107.08           C  
ANISOU 1336  CE2 PHE A 197    17776  13184   9725   -561   2423    156       C  
ATOM   1337  CZ  PHE A 197      51.241  39.970 -77.827  1.00105.85           C  
ANISOU 1337  CZ  PHE A 197    17410  13027   9781   -511   2428     15       C  
ATOM   1338  N   PRO A 198      45.626  44.760 -78.082  1.00116.26           N  
ANISOU 1338  N   PRO A 198    19007  14325  10841   -410    865    544       N  
ATOM   1339  CA  PRO A 198      44.610  45.611 -78.703  1.00121.82           C  
ANISOU 1339  CA  PRO A 198    19889  15034  11365   -354    579    653       C  
ATOM   1340  C   PRO A 198      45.062  46.073 -80.082  1.00127.21           C  
ANISOU 1340  C   PRO A 198    20958  15687  11690   -396    673    745       C  
ATOM   1341  O   PRO A 198      46.201  45.863 -80.501  1.00127.43           O  
ANISOU 1341  O   PRO A 198    21098  15690  11627   -473    981    738       O  
ATOM   1342  CB  PRO A 198      44.493  46.788 -77.729  1.00121.42           C  
ANISOU 1342  CB  PRO A 198    19670  14920  11544   -285    516    785       C  
ATOM   1343  CG  PRO A 198      45.831  46.857 -77.072  1.00118.60           C  
ANISOU 1343  CG  PRO A 198    19188  14508  11367   -352    838    795       C  
ATOM   1344  CD  PRO A 198      46.346  45.448 -76.997  1.00115.42           C  
ANISOU 1344  CD  PRO A 198    18684  14161  11009   -406   1010    624       C  
ATOM   1345  N   GLY A 199      44.143  46.711 -80.782  1.00133.17           N  
ANISOU 1345  N   GLY A 199    21912  16449  12238   -340    403    837       N  
ATOM   1346  CA  GLY A 199      44.407  47.168 -82.130  1.00139.83           C  
ANISOU 1346  CA  GLY A 199    23156  17265  12709   -373    446    935       C  
ATOM   1347  C   GLY A 199      43.577  46.404 -83.146  1.00145.01           C  
ANISOU 1347  C   GLY A 199    24016  18005  13074   -378    228    838       C  
ATOM   1348  O   GLY A 199      43.234  45.228 -82.957  1.00144.19           O  
ANISOU 1348  O   GLY A 199    23780  17972  13033   -408    176    659       O  
ATOM   1349  N   LEU A 200      43.242  47.082 -84.243  1.00150.94           N  
ANISOU 1349  N   LEU A 200    25112  18743  13495   -356     91    960       N  
ATOM   1350  CA  LEU A 200      42.361  46.479 -85.238  1.00157.30           C  
ANISOU 1350  CA  LEU A 200    26130  19633  14002   -360   -170    882       C  
ATOM   1351  C   LEU A 200      43.081  45.392 -86.029  1.00160.39           C  
ANISOU 1351  C   LEU A 200    26734  20041  14165   -474     71    734       C  
ATOM   1352  O   LEU A 200      42.713  44.213 -85.963  1.00161.40           O  
ANISOU 1352  O   LEU A 200    26773  20233  14319   -515      2    545       O  
ATOM   1353  CB  LEU A 200      41.803  47.558 -86.169  1.00161.35           C  
ANISOU 1353  CB  LEU A 200    26964  20124  14217   -290   -401   1068       C  
ATOM   1354  CG  LEU A 200      40.777  48.505 -85.540  1.00161.05           C  
ANISOU 1354  CG  LEU A 200    26743  20087  14362   -140   -727   1193       C  
ATOM   1355  CD1 LEU A 200      40.191  49.438 -86.591  1.00163.91           C  
ANISOU 1355  CD1 LEU A 200    27460  20428  14389    -55   -978   1368       C  
ATOM   1356  CD2 LEU A 200      39.674  47.728 -84.824  1.00159.40           C  
ANISOU 1356  CD2 LEU A 200    26178  20004  14383    -98  -1003   1045       C  
ATOM   1357  N   ALA A 201      44.124  45.763 -86.774  1.00161.46           N  
ANISOU 1357  N   ALA A 201    27157  20114  14076   -528    371    816       N  
ATOM   1358  CA  ALA A 201      44.806  44.823 -87.656  1.00162.65           C  
ANISOU 1358  CA  ALA A 201    27559  20278  13962   -615    615    686       C  
ATOM   1359  C   ALA A 201      46.223  44.505 -87.192  1.00160.78           C  
ANISOU 1359  C   ALA A 201    27186  20003  13902   -666   1077    644       C  
ATOM   1360  O   ALA A 201      46.543  43.340 -86.937  1.00161.30           O  
ANISOU 1360  O   ALA A 201    27133  20092  14062   -690   1221    457       O  
ATOM   1361  CB  ALA A 201      44.825  45.372 -89.090  1.00165.82           C  
ANISOU 1361  CB  ALA A 201    28451  20663  13891   -637    594    800       C  
ATOM   1362  N   ASN A 202      47.082  45.511 -87.058  1.00157.79           N  
ANISOU 1362  N   ASN A 202    26815  19562  13577   -684   1309    813       N  
ATOM   1363  CA  ASN A 202      48.476  45.305 -86.689  1.00154.10           C  
ANISOU 1363  CA  ASN A 202    26209  19076  13265   -739   1748    792       C  
ATOM   1364  C   ASN A 202      48.667  45.699 -85.234  1.00149.17           C  
ANISOU 1364  C   ASN A 202    25158  18428  13092   -714   1757    831       C  
ATOM   1365  O   ASN A 202      48.354  46.829 -84.845  1.00149.90           O  
ANISOU 1365  O   ASN A 202    25208  18467  13281   -690   1612    992       O  
ATOM   1366  CB  ASN A 202      49.408  46.108 -87.593  1.00156.92           C  
ANISOU 1366  CB  ASN A 202    26873  19393  13357   -812   2036    948       C  
ATOM   1367  CG  ASN A 202      49.363  45.636 -89.027  1.00160.70           C  
ANISOU 1367  CG  ASN A 202    27790  19897  13372   -841   2082    896       C  
ATOM   1368  OD1 ASN A 202      48.938  44.514 -89.304  1.00161.68           O  
ANISOU 1368  OD1 ASN A 202    27964  20067  13398   -822   1993    707       O  
ATOM   1369  ND2 ASN A 202      49.799  46.487 -89.949  1.00163.14           N  
ANISOU 1369  ND2 ASN A 202    28440  20166  13379   -897   2223   1062       N  
ATOM   1370  N   LYS A 203      49.181  44.768 -84.437  1.00144.12           N  
ANISOU 1370  N   LYS A 203    24224  17818  12716   -712   1925    684       N  
ATOM   1371  CA  LYS A 203      49.365  44.996 -83.010  1.00137.12           C  
ANISOU 1371  CA  LYS A 203    22933  16915  12250   -688   1928    700       C  
ATOM   1372  C   LYS A 203      50.650  45.787 -82.793  1.00135.49           C  
ANISOU 1372  C   LYS A 203    22663  16673  12143   -757   2254    830       C  
ATOM   1373  O   LYS A 203      51.749  45.294 -83.068  1.00133.26           O  
ANISOU 1373  O   LYS A 203    22380  16423  11831   -803   2598    781       O  
ATOM   1374  CB  LYS A 203      49.394  43.667 -82.263  1.00133.76           C  
ANISOU 1374  CB  LYS A 203    22242  16531  12049   -657   1964    499       C  
ATOM   1375  CG  LYS A 203      48.250  42.728 -82.624  1.00131.91           C  
ANISOU 1375  CG  LYS A 203    22104  16333  11684   -629   1688    351       C  
ATOM   1376  CD  LYS A 203      46.900  43.342 -82.305  1.00129.19           C  
ANISOU 1376  CD  LYS A 203    21698  15997  11391   -582   1280    418       C  
ATOM   1377  CE  LYS A 203      45.765  42.407 -82.679  1.00127.06           C  
ANISOU 1377  CE  LYS A 203    21500  15781  10996   -580    998    272       C  
ATOM   1378  NZ  LYS A 203      44.441  43.032 -82.418  1.00124.84           N  
ANISOU 1378  NZ  LYS A 203    21135  15535  10765   -525    602    345       N  
ATOM   1379  N   THR A 204      50.507  47.024 -82.314  1.00136.84           N  
ANISOU 1379  N   THR A 204    22785  16779  12430   -765   2149    996       N  
ATOM   1380  CA  THR A 204      51.643  47.850 -81.931  1.00137.17           C  
ANISOU 1380  CA  THR A 204    22730  16778  12612   -854   2416   1123       C  
ATOM   1381  C   THR A 204      51.828  47.948 -80.422  1.00136.00           C  
ANISOU 1381  C   THR A 204    22175  16617  12880   -838   2391   1102       C  
ATOM   1382  O   THR A 204      52.933  48.266 -79.970  1.00137.33           O  
ANISOU 1382  O   THR A 204    22186  16781  13212   -922   2645   1152       O  
ATOM   1383  CB  THR A 204      51.497  49.267 -82.502  1.00136.00           C  
ANISOU 1383  CB  THR A 204    22864  16532  12276   -899   2349   1338       C  
ATOM   1384  OG1 THR A 204      50.573  50.012 -81.700  1.00132.79           O  
ANISOU 1384  OG1 THR A 204    22353  16057  12046   -821   2033   1405       O  
ATOM   1385  CG2 THR A 204      50.988  49.217 -83.932  1.00139.11           C  
ANISOU 1385  CG2 THR A 204    23681  16933  12241   -887   2268   1365       C  
ATOM   1386  N   THR A 205      50.781  47.691 -79.637  1.00133.50           N  
ANISOU 1386  N   THR A 205    21688  16303  12733   -739   2093   1031       N  
ATOM   1387  CA  THR A 205      50.861  47.716 -78.183  1.00130.74           C  
ANISOU 1387  CA  THR A 205    20974  15943  12757   -715   2053   1001       C  
ATOM   1388  C   THR A 205      50.158  46.495 -77.608  1.00125.95           C  
ANISOU 1388  C   THR A 205    20169  15401  12285   -630   1904    821       C  
ATOM   1389  O   THR A 205      49.462  45.754 -78.308  1.00126.58           O  
ANISOU 1389  O   THR A 205    20395  15522  12176   -594   1783    729       O  
ATOM   1390  CB  THR A 205      50.236  48.987 -77.588  1.00132.13           C  
ANISOU 1390  CB  THR A 205    21140  16025  13039   -683   1831   1137       C  
ATOM   1391  OG1 THR A 205      48.896  49.138 -78.075  1.00133.07           O  
ANISOU 1391  OG1 THR A 205    21429  16140  12992   -584   1514   1151       O  
ATOM   1392  CG2 THR A 205      51.055  50.216 -77.946  1.00135.84           C  
ANISOU 1392  CG2 THR A 205    21780  16405  13429   -791   2000   1317       C  
ATOM   1393  N   LEU A 206      50.340  46.305 -76.308  1.00120.81           N  
ANISOU 1393  N   LEU A 206    19194  14752  11957   -610   1907    775       N  
ATOM   1394  CA  LEU A 206      49.722  45.202 -75.589  1.00117.04           C  
ANISOU 1394  CA  LEU A 206    18508  14320  11640   -542   1780    620       C  
ATOM   1395  C   LEU A 206      49.597  45.606 -74.127  1.00113.55           C  
ANISOU 1395  C   LEU A 206    17773  13850  11520   -511   1690    641       C  
ATOM   1396  O   LEU A 206      50.024  46.692 -73.724  1.00112.61           O  
ANISOU 1396  O   LEU A 206    17625  13672  11489   -545   1729    764       O  
ATOM   1397  CB  LEU A 206      50.538  43.916 -75.760  1.00115.21           C  
ANISOU 1397  CB  LEU A 206    18224  14139  11412   -555   2021    482       C  
ATOM   1398  CG  LEU A 206      52.035  44.001 -75.448  1.00115.32           C  
ANISOU 1398  CG  LEU A 206    18097  14163  11556   -607   2346    514       C  
ATOM   1399  CD1 LEU A 206      52.303  43.862 -73.960  1.00112.67           C  
ANISOU 1399  CD1 LEU A 206    17414  13827  11569   -582   2335    487       C  
ATOM   1400  CD2 LEU A 206      52.799  42.944 -76.214  1.00118.72           C  
ANISOU 1400  CD2 LEU A 206    18615  14640  11852   -605   2604    409       C  
ATOM   1401  N   PHE A 207      49.020  44.716 -73.327  1.00111.25           N  
ANISOU 1401  N   PHE A 207    17281  13594  11396   -456   1576    519       N  
ATOM   1402  CA  PHE A 207      49.071  44.911 -71.886  1.00110.02           C  
ANISOU 1402  CA  PHE A 207    16844  13418  11542   -431   1540    521       C  
ATOM   1403  C   PHE A 207      48.879  43.570 -71.198  1.00100.89           C  
ANISOU 1403  C   PHE A 207    15496  12305  10534   -397   1532    368       C  
ATOM   1404  O   PHE A 207      48.076  42.747 -71.638  1.00 98.46           O  
ANISOU 1404  O   PHE A 207    15259  12030  10122   -378   1413    273       O  
ATOM   1405  CB  PHE A 207      48.035  45.934 -71.396  1.00115.78           C  
ANISOU 1405  CB  PHE A 207    17557  14105  12328   -373   1286    604       C  
ATOM   1406  CG  PHE A 207      46.617  45.610 -71.761  1.00122.19           C  
ANISOU 1406  CG  PHE A 207    18427  14961  13037   -304   1023    556       C  
ATOM   1407  CD1 PHE A 207      46.112  45.948 -73.006  1.00127.29           C  
ANISOU 1407  CD1 PHE A 207    19339  15615  13410   -297    917    608       C  
ATOM   1408  CD2 PHE A 207      45.775  45.008 -70.841  1.00123.73           C  
ANISOU 1408  CD2 PHE A 207    18407  15197  13409   -252    873    466       C  
ATOM   1409  CE1 PHE A 207      44.798  45.666 -73.338  1.00130.89           C  
ANISOU 1409  CE1 PHE A 207    19826  16129  13778   -239    651    566       C  
ATOM   1410  CE2 PHE A 207      44.460  44.723 -71.165  1.00127.49           C  
ANISOU 1410  CE2 PHE A 207    18904  15733  13805   -204    628    424       C  
ATOM   1411  CZ  PHE A 207      43.971  45.052 -72.416  1.00131.02           C  
ANISOU 1411  CZ  PHE A 207    19597  16197  13987   -197    508    472       C  
ATOM   1412  N   THR A 208      49.643  43.354 -70.136  1.00 92.81           N  
ANISOU 1412  N   THR A 208    14245  11276   9744   -400   1655    349       N  
ATOM   1413  CA  THR A 208      49.573  42.123 -69.370  1.00 89.53           C  
ANISOU 1413  CA  THR A 208    13652  10882   9483   -365   1662    221       C  
ATOM   1414  C   THR A 208      48.814  42.373 -68.073  1.00 80.48           C  
ANISOU 1414  C   THR A 208    12310   9723   8547   -324   1481    225       C  
ATOM   1415  O   THR A 208      49.067  43.362 -67.376  1.00 75.74           O  
ANISOU 1415  O   THR A 208    11623   9090   8065   -328   1469    315       O  
ATOM   1416  CB  THR A 208      50.972  41.581 -69.079  1.00 94.39           C  
ANISOU 1416  CB  THR A 208    14149  11509  10207   -375   1925    192       C  
ATOM   1417  OG1 THR A 208      51.573  41.146 -70.304  1.00100.42           O  
ANISOU 1417  OG1 THR A 208    15095  12294  10766   -395   2108    163       O  
ATOM   1418  CG2 THR A 208      50.903  40.408 -68.113  1.00 94.25           C  
ANISOU 1418  CG2 THR A 208    13949  11494  10370   -324   1916     80       C  
ATOM   1419  N   VAL A 209      47.871  41.491 -67.769  1.00 76.94           N  
ANISOU 1419  N   VAL A 209    11805   9296   8133   -295   1344    126       N  
ATOM   1420  CA  VAL A 209      47.161  41.508 -66.502  1.00 72.48           C  
ANISOU 1420  CA  VAL A 209    11043   8730   7767   -258   1205    112       C  
ATOM   1421  C   VAL A 209      47.528  40.255 -65.729  1.00 68.53           C  
ANISOU 1421  C   VAL A 209    10401   8226   7409   -253   1297     10       C  
ATOM   1422  O   VAL A 209      47.874  39.214 -66.304  1.00 68.43           O  
ANISOU 1422  O   VAL A 209    10468   8213   7318   -267   1399    -76       O  
ATOM   1423  CB  VAL A 209      45.631  41.601 -66.686  1.00 76.23           C  
ANISOU 1423  CB  VAL A 209    11543   9242   8180   -232    957     97       C  
ATOM   1424  CG1 VAL A 209      45.266  42.911 -67.365  1.00 77.78           C  
ANISOU 1424  CG1 VAL A 209    11880   9430   8244   -207    852    214       C  
ATOM   1425  CG2 VAL A 209      45.127  40.413 -67.498  1.00 80.17           C  
ANISOU 1425  CG2 VAL A 209    12144   9776   8540   -270    916    -16       C  
ATOM   1426  N   CYS A 210      47.456  40.373 -64.405  1.00 65.97           N  
ANISOU 1426  N   CYS A 210     9887   7890   7288   -227   1260     20       N  
ATOM   1427  CA  CYS A 210      47.644  39.261 -63.487  1.00 65.76           C  
ANISOU 1427  CA  CYS A 210     9726   7851   7408   -214   1311    -61       C  
ATOM   1428  C   CYS A 210      46.279  38.912 -62.909  1.00 67.31           C  
ANISOU 1428  C   CYS A 210     9851   8066   7659   -210   1130   -108       C  
ATOM   1429  O   CYS A 210      45.694  39.708 -62.171  1.00 71.33           O  
ANISOU 1429  O   CYS A 210    10264   8585   8253   -183   1021    -55       O  
ATOM   1430  CB  CYS A 210      48.635  39.623 -62.384  1.00 63.14           C  
ANISOU 1430  CB  CYS A 210     9237   7499   7255   -195   1407    -11       C  
ATOM   1431  SG  CYS A 210      48.777  38.357 -61.076  1.00 63.09           S  
ANISOU 1431  SG  CYS A 210     9070   7469   7431   -161   1437    -90       S  
ATOM   1432  N   ASP A 211      45.765  37.731 -63.234  1.00 64.42           N  
ANISOU 1432  N   ASP A 211     9532   7702   7241   -241   1104   -208       N  
ATOM   1433  CA  ASP A 211      44.423  37.400 -62.782  1.00 62.25           C  
ANISOU 1433  CA  ASP A 211     9181   7461   7011   -263    934   -250       C  
ATOM   1434  C   ASP A 211      44.286  35.893 -62.634  1.00 66.15           C  
ANISOU 1434  C   ASP A 211     9690   7919   7526   -312    970   -363       C  
ATOM   1435  O   ASP A 211      45.142  35.120 -63.070  1.00 69.31           O  
ANISOU 1435  O   ASP A 211    10192   8265   7877   -312   1113   -415       O  
ATOM   1436  CB  ASP A 211      43.369  37.955 -63.741  1.00 62.49           C  
ANISOU 1436  CB  ASP A 211     9296   7554   6892   -280    760   -232       C  
ATOM   1437  CG  ASP A 211      42.018  38.082 -63.094  1.00 66.28           C  
ANISOU 1437  CG  ASP A 211     9629   8097   7457   -278    581   -236       C  
ATOM   1438  OD1 ASP A 211      41.893  37.704 -61.920  1.00 66.50           O  
ANISOU 1438  OD1 ASP A 211     9507   8113   7648   -276    607   -255       O  
ATOM   1439  OD2 ASP A 211      41.079  38.561 -63.750  1.00 72.28           O  
ANISOU 1439  OD2 ASP A 211    10418   8925   8121   -274    416   -215       O  
ATOM   1440  N   GLU A 212      43.187  35.479 -62.012  1.00 69.21           N  
ANISOU 1440  N   GLU A 212     9976   8332   7987   -352    848   -399       N  
ATOM   1441  CA  GLU A 212      42.907  34.060 -61.849  1.00 70.48           C  
ANISOU 1441  CA  GLU A 212    10167   8445   8166   -423    865   -503       C  
ATOM   1442  C   GLU A 212      42.515  33.435 -63.178  1.00 73.82           C  
ANISOU 1442  C   GLU A 212    10777   8870   8400   -501    811   -586       C  
ATOM   1443  O   GLU A 212      41.687  33.982 -63.910  1.00 76.58           O  
ANISOU 1443  O   GLU A 212    11154   9300   8641   -532    657   -573       O  
ATOM   1444  CB  GLU A 212      41.784  33.858 -60.840  1.00 69.23           C  
ANISOU 1444  CB  GLU A 212     9846   8326   8133   -468    754   -510       C  
ATOM   1445  CG  GLU A 212      41.982  34.563 -59.530  1.00 64.75           C  
ANISOU 1445  CG  GLU A 212     9112   7765   7727   -393    785   -432       C  
ATOM   1446  CD  GLU A 212      40.777  34.405 -58.636  1.00 64.50           C  
ANISOU 1446  CD  GLU A 212     8926   7787   7795   -437    688   -440       C  
ATOM   1447  OE1 GLU A 212      40.836  34.847 -57.462  1.00 65.01           O  
ANISOU 1447  OE1 GLU A 212     8866   7851   7983   -383    718   -389       O  
ATOM   1448  OE2 GLU A 212      39.770  33.832 -59.112  1.00 63.18           O  
ANISOU 1448  OE2 GLU A 212     8762   7666   7576   -534    583   -499       O  
ATOM   1449  N   ARG A 213      43.087  32.272 -63.472  1.00 73.81           N  
ANISOU 1449  N   ARG A 213    10913   8776   8356   -527    928   -676       N  
ATOM   1450  CA  ARG A 213      42.785  31.520 -64.683  1.00 76.89           C  
ANISOU 1450  CA  ARG A 213    11517   9142   8557   -609    891   -777       C  
ATOM   1451  C   ARG A 213      42.040  30.247 -64.299  1.00 77.35           C  
ANISOU 1451  C   ARG A 213    11589   9140   8659   -723    835   -879       C  
ATOM   1452  O   ARG A 213      42.589  29.385 -63.603  1.00 76.69           O  
ANISOU 1452  O   ARG A 213    11515   8948   8675   -703    962   -913       O  
ATOM   1453  CB  ARG A 213      44.063  31.190 -65.453  1.00 82.18           C  
ANISOU 1453  CB  ARG A 213    12374   9736   9116   -543   1090   -810       C  
ATOM   1454  CG  ARG A 213      43.837  30.393 -66.733  1.00 91.30           C  
ANISOU 1454  CG  ARG A 213    13791  10850  10049   -619   1072   -926       C  
ATOM   1455  CD  ARG A 213      45.133  30.210 -67.507  1.00101.21           C  
ANISOU 1455  CD  ARG A 213    15223  12045  11188   -532   1296   -950       C  
ATOM   1456  NE  ARG A 213      45.736  31.496 -67.855  1.00110.03           N  
ANISOU 1456  NE  ARG A 213    16298  13244  12264   -461   1351   -834       N  
ATOM   1457  CZ  ARG A 213      45.529  32.140 -69.000  1.00117.23           C  
ANISOU 1457  CZ  ARG A 213    17359  14214  12967   -488   1294   -812       C  
ATOM   1458  NH1 ARG A 213      44.734  31.616 -69.928  1.00121.85           N  
ANISOU 1458  NH1 ARG A 213    18141  14798  13359   -580   1165   -904       N  
ATOM   1459  NH2 ARG A 213      46.121  33.307 -69.221  1.00117.97           N  
ANISOU 1459  NH2 ARG A 213    17421  14364  13038   -432   1359   -695       N  
ATOM   1460  N   TRP A 214      40.795  30.131 -64.749  1.00 78.08           N  
ANISOU 1460  N   TRP A 214    11686   9303   8678   -847    640   -922       N  
ATOM   1461  CA  TRP A 214      39.942  29.002 -64.411  1.00 79.39           C  
ANISOU 1461  CA  TRP A 214    11851   9426   8886   -995    565  -1013       C  
ATOM   1462  C   TRP A 214      39.610  28.197 -65.662  1.00 87.44           C  
ANISOU 1462  C   TRP A 214    13119  10405   9699  -1118    493  -1136       C  
ATOM   1463  O   TRP A 214      39.441  28.756 -66.752  1.00 86.85           O  
ANISOU 1463  O   TRP A 214    13144  10405   9449  -1119    399  -1135       O  
ATOM   1464  CB  TRP A 214      38.654  29.468 -63.731  1.00 76.33           C  
ANISOU 1464  CB  TRP A 214    11216   9172   8615  -1063    389   -965       C  
ATOM   1465  CG  TRP A 214      38.895  30.094 -62.397  1.00 77.00           C  
ANISOU 1465  CG  TRP A 214    11084   9277   8896   -958    464   -864       C  
ATOM   1466  CD1 TRP A 214      38.904  31.426 -62.108  1.00 75.65           C  
ANISOU 1466  CD1 TRP A 214    10766   9202   8775   -841    431   -756       C  
ATOM   1467  CD2 TRP A 214      39.180  29.412 -61.168  1.00 75.53           C  
ANISOU 1467  CD2 TRP A 214    10833   8998   8866   -960    581   -864       C  
ATOM   1468  NE1 TRP A 214      39.182  31.617 -60.775  1.00 75.57           N  
ANISOU 1468  NE1 TRP A 214    10604   9169   8939   -776    521   -697       N  
ATOM   1469  CE2 TRP A 214      39.350  30.396 -60.176  1.00 75.27           C  
ANISOU 1469  CE2 TRP A 214    10610   9023   8966   -845    611   -758       C  
ATOM   1470  CE3 TRP A 214      39.308  28.065 -60.813  1.00 73.98           C  
ANISOU 1470  CE3 TRP A 214    10745   8665   8701  -1045    662   -942       C  
ATOM   1471  CZ2 TRP A 214      39.629  30.074 -58.850  1.00 73.36           C  
ANISOU 1471  CZ2 TRP A 214    10277   8720   8876   -817    710   -728       C  
ATOM   1472  CZ3 TRP A 214      39.596  27.749 -59.494  1.00 72.01           C  
ANISOU 1472  CZ3 TRP A 214    10404   8349   8609  -1009    763   -901       C  
ATOM   1473  CH2 TRP A 214      39.754  28.747 -58.534  1.00 72.98           C  
ANISOU 1473  CH2 TRP A 214    10333   8545   8851   -898    783   -796       C  
ATOM   1474  N   GLY A 215      39.502  26.884 -65.491  1.00 92.85           N  
ANISOU 1474  N   GLY A 215    13923  10960  10395  -1227    532  -1243       N  
ATOM   1475  CA  GLY A 215      39.177  26.000 -66.590  1.00 98.79           C  
ANISOU 1475  CA  GLY A 215    14938  11647  10953  -1363    465  -1378       C  
ATOM   1476  C   GLY A 215      37.715  25.615 -66.596  1.00102.53           C  
ANISOU 1476  C   GLY A 215    15330  12195  11430  -1582    235  -1430       C  
ATOM   1477  O   GLY A 215      37.377  24.444 -66.792  1.00107.65           O  
ANISOU 1477  O   GLY A 215    16144  12729  12028  -1744    211  -1550       O  
ATOM   1478  N   GLY A 216      36.844  26.584 -66.368  1.00 98.61           N  
ANISOU 1478  N   GLY A 216    14578  11889  11000  -1589     67  -1342       N  
ATOM   1479  CA  GLY A 216      35.420  26.324 -66.355  1.00 98.74           C  
ANISOU 1479  CA  GLY A 216    14458  12017  11039  -1789   -158  -1379       C  
ATOM   1480  C   GLY A 216      34.691  27.374 -65.555  1.00 98.31           C  
ANISOU 1480  C   GLY A 216    14053  12149  11151  -1729   -253  -1257       C  
ATOM   1481  O   GLY A 216      35.290  28.200 -64.869  1.00 98.43           O  
ANISOU 1481  O   GLY A 216    13947  12176  11274  -1548   -136  -1151       O  
ATOM   1482  N   GLU A 217      33.366  27.323 -65.650  1.00 99.10           N  
ANISOU 1482  N   GLU A 217    13987  12396  11269  -1887   -470  -1277       N  
ATOM   1483  CA  GLU A 217      32.518  28.294 -64.976  1.00100.88           C  
ANISOU 1483  CA  GLU A 217    13869  12817  11645  -1827   -575  -1171       C  
ATOM   1484  C   GLU A 217      32.205  27.912 -63.533  1.00 96.80           C  
ANISOU 1484  C   GLU A 217    13138  12287  11355  -1875   -470  -1144       C  
ATOM   1485  O   GLU A 217      31.961  28.803 -62.708  1.00 94.80           O  
ANISOU 1485  O   GLU A 217    12638  12141  11243  -1749   -452  -1042       O  
ATOM   1486  CB  GLU A 217      31.212  28.469 -65.758  1.00110.54           C  
ANISOU 1486  CB  GLU A 217    14977  14235  12789  -1956   -864  -1196       C  
ATOM   1487  CG  GLU A 217      30.355  29.637 -65.307  1.00118.67           C  
ANISOU 1487  CG  GLU A 217    15665  15482  13942  -1842   -990  -1082       C  
ATOM   1488  CD  GLU A 217      29.117  29.813 -66.166  1.00127.85           C  
ANISOU 1488  CD  GLU A 217    16708  16849  15019  -1949  -1293  -1104       C  
ATOM   1489  OE1 GLU A 217      28.954  29.052 -67.143  1.00132.21           O  
ANISOU 1489  OE1 GLU A 217    17462  17371  15401  -2124  -1415  -1210       O  
ATOM   1490  OE2 GLU A 217      28.308  30.716 -65.861  1.00130.57           O  
ANISOU 1490  OE2 GLU A 217    16760  17385  15465  -1850  -1415  -1016       O  
ATOM   1491  N   ILE A 218      32.232  26.617 -63.207  1.00 92.02           N  
ANISOU 1491  N   ILE A 218    12648  11539  10778  -2050   -390  -1232       N  
ATOM   1492  CA  ILE A 218      31.834  26.165 -61.879  1.00 83.69           C  
ANISOU 1492  CA  ILE A 218    11412  10470   9918  -2128   -298  -1206       C  
ATOM   1493  C   ILE A 218      32.975  26.300 -60.879  1.00 77.45           C  
ANISOU 1493  C   ILE A 218    10662   9540   9224  -1945    -61  -1138       C  
ATOM   1494  O   ILE A 218      32.738  26.551 -59.690  1.00 81.18           O  
ANISOU 1494  O   ILE A 218    10932  10056   9857  -1908     12  -1066       O  
ATOM   1495  CB  ILE A 218      31.323  24.716 -61.962  1.00 85.50           C  
ANISOU 1495  CB  ILE A 218    11764  10594  10128  -2413   -324  -1322       C  
ATOM   1496  CG1 ILE A 218      30.231  24.602 -63.020  1.00 89.78           C  
ANISOU 1496  CG1 ILE A 218    12269  11283  10561  -2608   -583  -1395       C  
ATOM   1497  CG2 ILE A 218      30.780  24.248 -60.622  1.00 87.01           C  
ANISOU 1497  CG2 ILE A 218    11765  10783  10509  -2523   -235  -1286       C  
ATOM   1498  CD1 ILE A 218      30.695  23.965 -64.313  1.00 92.46           C  
ANISOU 1498  CD1 ILE A 218    12969  11488  10674  -2681   -636  -1514       C  
ATOM   1499  N   TYR A 219      34.213  26.128 -61.330  1.00 71.71           N  
ANISOU 1499  N   TYR A 219    10192   8655   8401  -1829     61  -1161       N  
ATOM   1500  CA  TYR A 219      35.345  26.143 -60.409  1.00 71.29           C  
ANISOU 1500  CA  TYR A 219    10176   8470   8440  -1667    273  -1103       C  
ATOM   1501  C   TYR A 219      35.500  27.471 -59.679  1.00 68.94           C  
ANISOU 1501  C   TYR A 219     9655   8293   8248  -1480    297   -978       C  
ATOM   1502  O   TYR A 219      35.665  27.450 -58.449  1.00 67.28           O  
ANISOU 1502  O   TYR A 219     9339   8049   8176  -1435    405   -923       O  
ATOM   1503  CB  TYR A 219      36.631  25.773 -61.157  1.00 75.56           C  
ANISOU 1503  CB  TYR A 219    11006   8849   8856  -1567    393  -1152       C  
ATOM   1504  CG  TYR A 219      36.703  24.326 -61.566  1.00 83.50           C  
ANISOU 1504  CG  TYR A 219    12272   9673   9781  -1716    429  -1276       C  
ATOM   1505  CD1 TYR A 219      35.964  23.358 -60.898  1.00 87.32           C  
ANISOU 1505  CD1 TYR A 219    12737  10093  10348  -1907    414  -1315       C  
ATOM   1506  CD2 TYR A 219      37.504  23.926 -62.622  1.00 87.40           C  
ANISOU 1506  CD2 TYR A 219    13047  10051  10111  -1669    488  -1356       C  
ATOM   1507  CE1 TYR A 219      36.023  22.032 -61.271  1.00 91.04           C  
ANISOU 1507  CE1 TYR A 219    13477  10371  10742  -2052    445  -1431       C  
ATOM   1508  CE2 TYR A 219      37.571  22.601 -63.000  1.00 93.09           C  
ANISOU 1508  CE2 TYR A 219    14035  10584  10750  -1794    526  -1479       C  
ATOM   1509  CZ  TYR A 219      36.829  21.661 -62.320  1.00 95.40           C  
ANISOU 1509  CZ  TYR A 219    14319  10800  11131  -1987    499  -1516       C  
ATOM   1510  OH  TYR A 219      36.893  20.345 -62.699  1.00103.46           O  
ANISOU 1510  OH  TYR A 219    15635  11609  12067  -2119    534  -1640       O  
ATOM   1511  N   PRO A 220      35.499  28.636 -60.342  1.00 68.01           N  
ANISOU 1511  N   PRO A 220     9482   8296   8063  -1364    209   -928       N  
ATOM   1512  CA  PRO A 220      35.626  29.883 -59.570  1.00 66.97           C  
ANISOU 1512  CA  PRO A 220     9159   8250   8035  -1194    236   -814       C  
ATOM   1513  C   PRO A 220      34.470  30.098 -58.612  1.00 68.60           C  
ANISOU 1513  C   PRO A 220     9099   8585   8382  -1245    177   -778       C  
ATOM   1514  O   PRO A 220      34.680  30.571 -57.490  1.00 65.02           O  
ANISOU 1514  O   PRO A 220     8527   8131   8047  -1144    272   -709       O  
ATOM   1515  CB  PRO A 220      35.676  30.967 -60.655  1.00 66.12           C  
ANISOU 1515  CB  PRO A 220     9085   8235   7804  -1094    128   -778       C  
ATOM   1516  CG  PRO A 220      35.014  30.351 -61.834  1.00 68.45           C  
ANISOU 1516  CG  PRO A 220     9489   8566   7954  -1246    -22   -868       C  
ATOM   1517  CD  PRO A 220      35.418  28.911 -61.788  1.00 68.64           C  
ANISOU 1517  CD  PRO A 220     9695   8425   7960  -1376     84   -968       C  
ATOM   1518  N   LYS A 221      33.249  29.756 -59.025  1.00 70.04           N  
ANISOU 1518  N   LYS A 221     9180   8884   8548  -1403     22   -826       N  
ATOM   1519  CA  LYS A 221      32.104  29.892 -58.134  1.00 70.92           C  
ANISOU 1519  CA  LYS A 221     9013   9134   8798  -1462    -18   -795       C  
ATOM   1520  C   LYS A 221      32.301  29.069 -56.864  1.00 75.74           C  
ANISOU 1520  C   LYS A 221     9619   9634   9525  -1531    152   -794       C  
ATOM   1521  O   LYS A 221      32.147  29.575 -55.743  1.00 74.30           O  
ANISOU 1521  O   LYS A 221     9272   9498   9459  -1446    231   -726       O  
ATOM   1522  CB  LYS A 221      30.836  29.466 -58.866  1.00 68.45           C  
ANISOU 1522  CB  LYS A 221     8597   8962   8447  -1656   -213   -857       C  
ATOM   1523  CG  LYS A 221      30.551  30.282 -60.094  1.00 68.39           C  
ANISOU 1523  CG  LYS A 221     8594   9077   8315  -1583   -405   -849       C  
ATOM   1524  CD  LYS A 221      29.144  30.040 -60.578  1.00 75.77           C  
ANISOU 1524  CD  LYS A 221     9341  10200   9249  -1754   -620   -890       C  
ATOM   1525  CE  LYS A 221      28.797  30.986 -61.710  1.00 84.91           C  
ANISOU 1525  CE  LYS A 221    10481  11496  10285  -1648   -831   -861       C  
ATOM   1526  NZ  LYS A 221      27.339  30.958 -62.016  1.00 93.68           N  
ANISOU 1526  NZ  LYS A 221    11329  12837  11428  -1775  -1059   -879       N  
ATOM   1527  N   MET A 222      32.670  27.794 -57.026  1.00 76.37           N  
ANISOU 1527  N   MET A 222     9904   9552   9561  -1677    212   -870       N  
ATOM   1528  CA  MET A 222      32.881  26.933 -55.869  1.00 74.87           C  
ANISOU 1528  CA  MET A 222     9750   9233   9465  -1745    368   -863       C  
ATOM   1529  C   MET A 222      34.026  27.442 -55.009  1.00 69.22           C  
ANISOU 1529  C   MET A 222     9077   8426   8799  -1532    520   -787       C  
ATOM   1530  O   MET A 222      33.905  27.542 -53.778  1.00 72.55           O  
ANISOU 1530  O   MET A 222     9388   8854   9324  -1504    612   -729       O  
ATOM   1531  CB  MET A 222      33.154  25.507 -56.329  1.00 78.56           C  
ANISOU 1531  CB  MET A 222    10475   9514   9860  -1917    398   -959       C  
ATOM   1532  CG  MET A 222      31.992  24.894 -57.067  1.00 89.83           C  
ANISOU 1532  CG  MET A 222    11869  11020  11242  -2170    242  -1043       C  
ATOM   1533  SD  MET A 222      32.287  23.174 -57.517  1.00 97.09           S  
ANISOU 1533  SD  MET A 222    13132  11683  12074  -2387    286  -1165       S  
ATOM   1534  CE  MET A 222      32.366  22.426 -55.887  1.00 95.26           C  
ANISOU 1534  CE  MET A 222    12891  11317  11987  -2440    475  -1107       C  
ATOM   1535  N   TYR A 223      35.152  27.764 -55.644  1.00 62.59           N  
ANISOU 1535  N   TYR A 223     8399   7505   7878  -1389    551   -787       N  
ATOM   1536  CA  TYR A 223      36.327  28.167 -54.892  1.00 62.39           C  
ANISOU 1536  CA  TYR A 223     8416   7392   7899  -1207    685   -721       C  
ATOM   1537  C   TYR A 223      36.066  29.447 -54.114  1.00 66.60           C  
ANISOU 1537  C   TYR A 223     8739   8054   8512  -1079    674   -632       C  
ATOM   1538  O   TYR A 223      36.513  29.584 -52.975  1.00 64.34           O  
ANISOU 1538  O   TYR A 223     8423   7721   8302  -1001    776   -578       O  
ATOM   1539  CB  TYR A 223      37.520  28.346 -55.828  1.00 61.84           C  
ANISOU 1539  CB  TYR A 223     8525   7242   7729  -1091    718   -736       C  
ATOM   1540  CG  TYR A 223      38.717  28.972 -55.154  1.00 65.19           C  
ANISOU 1540  CG  TYR A 223     8948   7617   8206   -906    830   -661       C  
ATOM   1541  CD1 TYR A 223      39.646  28.187 -54.473  1.00 66.21           C  
ANISOU 1541  CD1 TYR A 223     9184   7595   8377   -863    959   -657       C  
ATOM   1542  CD2 TYR A 223      38.909  30.350 -55.178  1.00 64.92           C  
ANISOU 1542  CD2 TYR A 223     8807   7682   8179   -777    796   -592       C  
ATOM   1543  CE1 TYR A 223      40.739  28.756 -53.845  1.00 65.88           C  
ANISOU 1543  CE1 TYR A 223     9121   7526   8386   -705   1041   -589       C  
ATOM   1544  CE2 TYR A 223      39.995  30.927 -54.559  1.00 65.41           C  
ANISOU 1544  CE2 TYR A 223     8865   7701   8288   -636    886   -528       C  
ATOM   1545  CZ  TYR A 223      40.908  30.127 -53.891  1.00 66.52           C  
ANISOU 1545  CZ  TYR A 223     9089   7713   8473   -604   1003   -527       C  
ATOM   1546  OH  TYR A 223      41.993  30.701 -53.270  1.00 66.19           O  
ANISOU 1546  OH  TYR A 223     9024   7644   8482   -473   1072   -464       O  
ATOM   1547  N   HIS A 224      35.336  30.395 -54.702  1.00 67.22           N  
ANISOU 1547  N   HIS A 224     8684   8289   8566  -1049    547   -617       N  
ATOM   1548  CA  HIS A 224      35.154  31.671 -54.028  1.00 66.11           C  
ANISOU 1548  CA  HIS A 224     8379   8249   8493   -902    543   -537       C  
ATOM   1549  C   HIS A 224      34.026  31.626 -53.010  1.00 69.09           C  
ANISOU 1549  C   HIS A 224     8549   8729   8974   -962    552   -521       C  
ATOM   1550  O   HIS A 224      34.067  32.382 -52.034  1.00 69.57           O  
ANISOU 1550  O   HIS A 224     8515   8816   9101   -843    612   -462       O  
ATOM   1551  CB  HIS A 224      34.953  32.781 -55.056  1.00 62.90           C  
ANISOU 1551  CB  HIS A 224     7942   7945   8014   -808    414   -515       C  
ATOM   1552  CG  HIS A 224      36.216  33.151 -55.772  1.00 62.86           C  
ANISOU 1552  CG  HIS A 224     8122   7843   7919   -711    451   -501       C  
ATOM   1553  ND1 HIS A 224      37.241  33.841 -55.160  1.00 60.19           N  
ANISOU 1553  ND1 HIS A 224     7815   7437   7618   -575    549   -440       N  
ATOM   1554  CD2 HIS A 224      36.646  32.872 -57.027  1.00 63.23           C  
ANISOU 1554  CD2 HIS A 224     8335   7852   7839   -742    414   -543       C  
ATOM   1555  CE1 HIS A 224      38.225  34.018 -56.026  1.00 61.92           C  
ANISOU 1555  CE1 HIS A 224     8186   7593   7747   -530    574   -439       C  
ATOM   1556  NE2 HIS A 224      37.891  33.434 -57.163  1.00 62.38           N  
ANISOU 1556  NE2 HIS A 224     8336   7666   7700   -622    503   -501       N  
ATOM   1557  N   ILE A 225      33.052  30.723 -53.169  1.00 69.82           N  
ANISOU 1557  N   ILE A 225     8576   8872   9079  -1153    505   -574       N  
ATOM   1558  CA  ILE A 225      32.177  30.412 -52.042  1.00 68.20           C  
ANISOU 1558  CA  ILE A 225     8203   8734   8978  -1239    570   -557       C  
ATOM   1559  C   ILE A 225      33.001  29.918 -50.862  1.00 64.87           C  
ANISOU 1559  C   ILE A 225     7899   8155   8592  -1214    739   -527       C  
ATOM   1560  O   ILE A 225      32.894  30.438 -49.743  1.00 62.70           O  
ANISOU 1560  O   ILE A 225     7528   7916   8381  -1129    822   -472       O  
ATOM   1561  CB  ILE A 225      31.110  29.384 -52.440  1.00 70.35           C  
ANISOU 1561  CB  ILE A 225     8407   9068   9256  -1488    501   -621       C  
ATOM   1562  CG1 ILE A 225      30.032  30.057 -53.281  1.00 73.46           C  
ANISOU 1562  CG1 ILE A 225     8593   9676   9642  -1494    321   -631       C  
ATOM   1563  CG2 ILE A 225      30.496  28.774 -51.197  1.00 71.57           C  
ANISOU 1563  CG2 ILE A 225     8455   9233   9507  -1610    621   -602       C  
ATOM   1564  CD1 ILE A 225      28.931  29.118 -53.687  1.00 76.06           C  
ANISOU 1564  CD1 ILE A 225     8823  10093   9984  -1757    228   -696       C  
ATOM   1565  N   CYS A 226      33.857  28.924 -51.096  1.00 65.67           N  
ANISOU 1565  N   CYS A 226     8226   8079   8646  -1274    791   -562       N  
ATOM   1566  CA  CYS A 226      34.687  28.437 -50.000  1.00 68.05           C  
ANISOU 1566  CA  CYS A 226     8650   8230   8978  -1233    934   -525       C  
ATOM   1567  C   CYS A 226      35.592  29.537 -49.468  1.00 65.17           C  
ANISOU 1567  C   CYS A 226     8278   7859   8625  -1013    972   -460       C  
ATOM   1568  O   CYS A 226      35.808  29.643 -48.257  1.00 63.16           O  
ANISOU 1568  O   CYS A 226     8012   7574   8414   -959   1062   -409       O  
ATOM   1569  CB  CYS A 226      35.510  27.230 -50.449  1.00 70.16           C  
ANISOU 1569  CB  CYS A 226     9165   8301   9190  -1297    974   -573       C  
ATOM   1570  SG  CYS A 226      34.499  25.791 -50.805  1.00 76.75           S  
ANISOU 1570  SG  CYS A 226    10057   9091  10013  -1587    949   -651       S  
ATOM   1571  N   PHE A 227      36.119  30.373 -50.355  1.00 63.39           N  
ANISOU 1571  N   PHE A 227     8071   7662   8351   -897    904   -459       N  
ATOM   1572  CA  PHE A 227      37.022  31.436 -49.930  1.00 60.69           C  
ANISOU 1572  CA  PHE A 227     7735   7306   8020   -715    933   -400       C  
ATOM   1573  C   PHE A 227      36.314  32.405 -48.993  1.00 60.53           C  
ANISOU 1573  C   PHE A 227     7548   7395   8056   -644    938   -353       C  
ATOM   1574  O   PHE A 227      36.876  32.827 -47.976  1.00 60.28           O  
ANISOU 1574  O   PHE A 227     7534   7319   8051   -550   1006   -308       O  
ATOM   1575  CB  PHE A 227      37.575  32.179 -51.150  1.00 59.39           C  
ANISOU 1575  CB  PHE A 227     7621   7159   7787   -632    861   -404       C  
ATOM   1576  CG  PHE A 227      38.690  33.115 -50.814  1.00 57.45           C  
ANISOU 1576  CG  PHE A 227     7411   6871   7547   -479    899   -348       C  
ATOM   1577  CD1 PHE A 227      38.422  34.366 -50.285  1.00 56.12           C  
ANISOU 1577  CD1 PHE A 227     7140   6774   7410   -378    874   -299       C  
ATOM   1578  CD2 PHE A 227      40.001  32.728 -50.976  1.00 58.13           C  
ANISOU 1578  CD2 PHE A 227     7630   6843   7613   -440    965   -347       C  
ATOM   1579  CE1 PHE A 227      39.440  35.217 -49.943  1.00 58.69           C  
ANISOU 1579  CE1 PHE A 227     7510   7050   7740   -265    903   -251       C  
ATOM   1580  CE2 PHE A 227      41.030  33.587 -50.655  1.00 61.93           C  
ANISOU 1580  CE2 PHE A 227     8122   7299   8109   -323    994   -295       C  
ATOM   1581  CZ  PHE A 227      40.746  34.834 -50.133  1.00 61.30           C  
ANISOU 1581  CZ  PHE A 227     7953   7283   8055   -249    958   -248       C  
ATOM   1582  N   PHE A 228      35.080  32.782 -49.342  1.00 60.62           N  
ANISOU 1582  N   PHE A 228     7397   7555   8083   -681    861   -366       N  
ATOM   1583  CA  PHE A 228      34.284  33.660 -48.498  1.00 61.18           C  
ANISOU 1583  CA  PHE A 228     7298   7740   8210   -601    877   -330       C  
ATOM   1584  C   PHE A 228      33.955  32.998 -47.169  1.00 65.93           C  
ANISOU 1584  C   PHE A 228     7869   8320   8860   -673   1001   -318       C  
ATOM   1585  O   PHE A 228      33.989  33.648 -46.119  1.00 64.91           O  
ANISOU 1585  O   PHE A 228     7708   8202   8754   -570   1071   -279       O  
ATOM   1586  CB  PHE A 228      32.999  34.047 -49.226  1.00 60.81           C  
ANISOU 1586  CB  PHE A 228     7063   7868   8176   -625    763   -348       C  
ATOM   1587  CG  PHE A 228      32.064  34.873 -48.403  1.00 62.90           C  
ANISOU 1587  CG  PHE A 228     7131   8263   8505   -531    791   -317       C  
ATOM   1588  CD1 PHE A 228      32.382  36.179 -48.084  1.00 65.96           C  
ANISOU 1588  CD1 PHE A 228     7525   8645   8890   -331    792   -276       C  
ATOM   1589  CD2 PHE A 228      30.853  34.365 -47.982  1.00 65.21           C  
ANISOU 1589  CD2 PHE A 228     7233   8684   8860   -645    820   -333       C  
ATOM   1590  CE1 PHE A 228      31.515  36.963 -47.330  1.00 69.35           C  
ANISOU 1590  CE1 PHE A 228     7790   9186   9374   -221    829   -255       C  
ATOM   1591  CE2 PHE A 228      29.978  35.140 -47.230  1.00 70.53           C  
ANISOU 1591  CE2 PHE A 228     7713   9492   9596   -539    865   -307       C  
ATOM   1592  CZ  PHE A 228      30.311  36.446 -46.903  1.00 70.17           C  
ANISOU 1592  CZ  PHE A 228     7691   9430   9541   -314    871   -271       C  
ATOM   1593  N   LEU A 229      33.634  31.703 -47.192  1.00 69.11           N  
ANISOU 1593  N   LEU A 229     8305   8686   9268   -857   1033   -350       N  
ATOM   1594  CA  LEU A 229      33.293  31.015 -45.951  1.00 69.52           C  
ANISOU 1594  CA  LEU A 229     8349   8709   9354   -944   1159   -329       C  
ATOM   1595  C   LEU A 229      34.491  30.972 -45.012  1.00 66.43           C  
ANISOU 1595  C   LEU A 229     8134   8166   8941   -847   1247   -286       C  
ATOM   1596  O   LEU A 229      34.402  31.385 -43.854  1.00 64.30           O  
ANISOU 1596  O   LEU A 229     7836   7913   8682   -781   1328   -246       O  
ATOM   1597  CB  LEU A 229      32.792  29.599 -46.248  1.00 71.26           C  
ANISOU 1597  CB  LEU A 229     8610   8888   9578  -1178   1170   -370       C  
ATOM   1598  CG  LEU A 229      31.376  29.497 -46.827  1.00 75.34           C  
ANISOU 1598  CG  LEU A 229     8910   9581  10132  -1324   1097   -408       C  
ATOM   1599  CD1 LEU A 229      30.861  28.052 -46.804  1.00 75.11           C  
ANISOU 1599  CD1 LEU A 229     8933   9494  10113  -1590   1135   -442       C  
ATOM   1600  CD2 LEU A 229      30.415  30.417 -46.071  1.00 77.33           C  
ANISOU 1600  CD2 LEU A 229     8914  10018  10447  -1245   1138   -372       C  
ATOM   1601  N   VAL A 230      35.635  30.528 -45.520  1.00 67.11           N  
ANISOU 1601  N   VAL A 230     8396   8113   8989   -823   1226   -296       N  
ATOM   1602  CA  VAL A 230      36.812  30.317 -44.685  1.00 68.98           C  
ANISOU 1602  CA  VAL A 230     8789   8210   9210   -741   1292   -255       C  
ATOM   1603  C   VAL A 230      37.418  31.645 -44.234  1.00 67.97           C  
ANISOU 1603  C   VAL A 230     8633   8113   9079   -563   1275   -216       C  
ATOM   1604  O   VAL A 230      37.860  31.771 -43.091  1.00 68.55           O  
ANISOU 1604  O   VAL A 230     8762   8138   9146   -504   1333   -174       O  
ATOM   1605  CB  VAL A 230      37.841  29.445 -45.435  1.00 71.74           C  
ANISOU 1605  CB  VAL A 230     9312   8416   9531   -753   1278   -279       C  
ATOM   1606  CG1 VAL A 230      39.150  29.367 -44.671  1.00 70.12           C  
ANISOU 1606  CG1 VAL A 230     9234   8090   9318   -634   1322   -231       C  
ATOM   1607  CG2 VAL A 230      37.279  28.037 -45.660  1.00 74.82           C  
ANISOU 1607  CG2 VAL A 230     9780   8733   9916   -937   1308   -318       C  
ATOM   1608  N   THR A 231      37.504  32.641 -45.125  1.00 63.44           N  
ANISOU 1608  N   THR A 231     7998   7606   8499   -481   1192   -228       N  
ATOM   1609  CA  THR A 231      38.248  33.844 -44.759  1.00 60.65           C  
ANISOU 1609  CA  THR A 231     7659   7246   8139   -331   1175   -193       C  
ATOM   1610  C   THR A 231      37.395  34.879 -44.036  1.00 62.46           C  
ANISOU 1610  C   THR A 231     7776   7574   8384   -260   1187   -178       C  
ATOM   1611  O   THR A 231      37.944  35.746 -43.355  1.00 59.96           O  
ANISOU 1611  O   THR A 231     7500   7226   8054   -154   1194   -151       O  
ATOM   1612  CB  THR A 231      38.894  34.497 -45.984  1.00 62.34           C  
ANISOU 1612  CB  THR A 231     7897   7460   8331   -271   1095   -200       C  
ATOM   1613  OG1 THR A 231      37.882  35.006 -46.858  1.00 61.52           O  
ANISOU 1613  OG1 THR A 231     7684   7468   8221   -281   1023   -222       O  
ATOM   1614  CG2 THR A 231      39.766  33.507 -46.723  1.00 66.10           C  
ANISOU 1614  CG2 THR A 231     8487   7843   8785   -321   1103   -221       C  
ATOM   1615  N   TYR A 232      36.080  34.877 -44.232  1.00 64.41           N  
ANISOU 1615  N   TYR A 232     7877   7941   8656   -309   1183   -198       N  
ATOM   1616  CA  TYR A 232      35.257  35.907 -43.615  1.00 63.23           C  
ANISOU 1616  CA  TYR A 232     7608   7891   8524   -211   1204   -188       C  
ATOM   1617  C   TYR A 232      34.109  35.345 -42.789  1.00 66.04           C  
ANISOU 1617  C   TYR A 232     7847   8334   8910   -294   1303   -192       C  
ATOM   1618  O   TYR A 232      34.046  35.607 -41.584  1.00 66.65           O  
ANISOU 1618  O   TYR A 232     7948   8402   8975   -243   1398   -172       O  
ATOM   1619  CB  TYR A 232      34.738  36.864 -44.698  1.00 63.10           C  
ANISOU 1619  CB  TYR A 232     7490   7970   8515   -131   1096   -197       C  
ATOM   1620  CG  TYR A 232      34.090  38.109 -44.148  1.00 61.96           C  
ANISOU 1620  CG  TYR A 232     7256   7899   8386     22   1109   -184       C  
ATOM   1621  CD1 TYR A 232      34.860  39.172 -43.689  1.00 60.30           C  
ANISOU 1621  CD1 TYR A 232     7163   7603   8146    157   1110   -163       C  
ATOM   1622  CD2 TYR A 232      32.709  38.221 -44.087  1.00 65.69           C  
ANISOU 1622  CD2 TYR A 232     7527   8528   8905     32   1123   -196       C  
ATOM   1623  CE1 TYR A 232      34.268  40.325 -43.191  1.00 61.54           C  
ANISOU 1623  CE1 TYR A 232     7269   7804   8308    309   1127   -159       C  
ATOM   1624  CE2 TYR A 232      32.107  39.356 -43.573  1.00 67.99           C  
ANISOU 1624  CE2 TYR A 232     7740   8883   9211    199   1149   -188       C  
ATOM   1625  CZ  TYR A 232      32.893  40.405 -43.128  1.00 64.81           C  
ANISOU 1625  CZ  TYR A 232     7488   8369   8768    343   1153   -172       C  
ATOM   1626  OH  TYR A 232      32.290  41.534 -42.632  1.00 64.75           O  
ANISOU 1626  OH  TYR A 232     7431   8402   8767    519   1182   -171       O  
ATOM   1627  N   MET A 233      33.223  34.540 -43.377  1.00 65.77           N  
ANISOU 1627  N   MET A 233     7699   8382   8909   -437   1287   -218       N  
ATOM   1628  CA  MET A 233      31.911  34.353 -42.765  1.00 70.08           C  
ANISOU 1628  CA  MET A 233     8063   9065   9500   -501   1370   -221       C  
ATOM   1629  C   MET A 233      31.960  33.427 -41.553  1.00 72.03           C  
ANISOU 1629  C   MET A 233     8395   9242   9731   -609   1517   -198       C  
ATOM   1630  O   MET A 233      31.505  33.795 -40.466  1.00 72.87           O  
ANISOU 1630  O   MET A 233     8453   9399   9834   -556   1631   -179       O  
ATOM   1631  CB  MET A 233      30.903  33.829 -43.784  1.00 75.58           C  
ANISOU 1631  CB  MET A 233     8588   9888  10240   -640   1291   -256       C  
ATOM   1632  CG  MET A 233      29.552  33.597 -43.149  1.00 88.17           C  
ANISOU 1632  CG  MET A 233     9961  11644  11895   -725   1385   -255       C  
ATOM   1633  SD  MET A 233      28.342  32.934 -44.292  1.00101.19           S  
ANISOU 1633  SD  MET A 233    11386  13460  13603   -921   1274   -297       S  
ATOM   1634  CE  MET A 233      26.979  32.569 -43.190  1.00103.45           C  
ANISOU 1634  CE  MET A 233    11426  13916  13964  -1038   1442   -283       C  
ATOM   1635  N   ALA A 234      32.472  32.209 -41.728  1.00 70.86           N  
ANISOU 1635  N   ALA A 234     8387   8971   9564   -756   1522   -201       N  
ATOM   1636  CA  ALA A 234      32.426  31.240 -40.634  1.00 75.33           C  
ANISOU 1636  CA  ALA A 234     9049   9463  10110   -872   1657   -170       C  
ATOM   1637  C   ALA A 234      33.248  31.675 -39.427  1.00 74.17           C  
ANISOU 1637  C   ALA A 234     9054   9223   9903   -739   1727   -126       C  
ATOM   1638  O   ALA A 234      32.726  31.608 -38.298  1.00 73.48           O  
ANISOU 1638  O   ALA A 234     8956   9169   9795   -761   1857    -98       O  
ATOM   1639  CB  ALA A 234      32.851  29.858 -41.144  1.00 78.39           C  
ANISOU 1639  CB  ALA A 234     9587   9712  10487  -1039   1637   -182       C  
ATOM   1640  N   PRO A 235      34.507  32.110 -39.569  1.00 71.28           N  
ANISOU 1640  N   PRO A 235     8831   8749   9504   -612   1651   -117       N  
ATOM   1641  CA  PRO A 235      35.227  32.616 -38.389  1.00 68.59           C  
ANISOU 1641  CA  PRO A 235     8619   8339   9103   -494   1696    -79       C  
ATOM   1642  C   PRO A 235      34.557  33.811 -37.749  1.00 70.14           C  
ANISOU 1642  C   PRO A 235     8713   8648   9291   -378   1746    -85       C  
ATOM   1643  O   PRO A 235      34.571  33.923 -36.518  1.00 70.31           O  
ANISOU 1643  O   PRO A 235     8817   8645   9251   -345   1841    -59       O  
ATOM   1644  CB  PRO A 235      36.614  32.970 -38.939  1.00 68.95           C  
ANISOU 1644  CB  PRO A 235     8777   8283   9136   -393   1582    -78       C  
ATOM   1645  CG  PRO A 235      36.453  33.025 -40.427  1.00 70.58           C  
ANISOU 1645  CG  PRO A 235     8890   8536   9391   -420   1489   -118       C  
ATOM   1646  CD  PRO A 235      35.373  32.070 -40.763  1.00 69.74           C  
ANISOU 1646  CD  PRO A 235     8695   8486   9316   -586   1529   -140       C  
ATOM   1647  N   LEU A 236      33.942  34.693 -38.541  1.00 71.77           N  
ANISOU 1647  N   LEU A 236     8753   8969   9545   -308   1687   -118       N  
ATOM   1648  CA  LEU A 236      33.229  35.828 -37.967  1.00 72.09           C  
ANISOU 1648  CA  LEU A 236     8697   9112   9584   -174   1743   -127       C  
ATOM   1649  C   LEU A 236      32.057  35.363 -37.115  1.00 75.36           C  
ANISOU 1649  C   LEU A 236     8998   9631  10002   -253   1904   -121       C  
ATOM   1650  O   LEU A 236      31.839  35.870 -36.010  1.00 77.78           O  
ANISOU 1650  O   LEU A 236     9342   9953  10257   -169   2015   -114       O  
ATOM   1651  CB  LEU A 236      32.746  36.762 -39.076  1.00 77.22           C  
ANISOU 1651  CB  LEU A 236     9190   9860  10288    -78   1638   -155       C  
ATOM   1652  CG  LEU A 236      32.050  38.062 -38.672  1.00 87.57           C  
ANISOU 1652  CG  LEU A 236    10408  11261  11604    101   1676   -168       C  
ATOM   1653  CD1 LEU A 236      32.972  38.954 -37.832  1.00 87.51           C  
ANISOU 1653  CD1 LEU A 236    10602  11128  11519    236   1686   -162       C  
ATOM   1654  CD2 LEU A 236      31.574  38.811 -39.917  1.00 91.63           C  
ANISOU 1654  CD2 LEU A 236    10777  11865  12174    188   1550   -183       C  
ATOM   1655  N   CYS A 237      31.282  34.401 -37.617  1.00 75.20           N  
ANISOU 1655  N   CYS A 237     8846   9687  10041   -426   1923   -126       N  
ATOM   1656  CA  CYS A 237      30.147  33.908 -36.845  1.00 77.70           C  
ANISOU 1656  CA  CYS A 237     9036  10115  10371   -532   2088   -115       C  
ATOM   1657  C   CYS A 237      30.604  33.236 -35.562  1.00 72.52           C  
ANISOU 1657  C   CYS A 237     8590   9340   9624   -595   2220    -71       C  
ATOM   1658  O   CYS A 237      30.018  33.456 -34.495  1.00 73.23           O  
ANISOU 1658  O   CYS A 237     8658   9494   9673   -569   2378    -57       O  
ATOM   1659  CB  CYS A 237      29.315  32.959 -37.695  1.00 83.41           C  
ANISOU 1659  CB  CYS A 237     9588  10929  11174   -738   2062   -130       C  
ATOM   1660  SG  CYS A 237      28.518  33.853 -39.033  1.00 90.90           S  
ANISOU 1660  SG  CYS A 237    10259  12064  12217   -648   1913   -174       S  
ATOM   1661  N   LEU A 238      31.662  32.430 -35.640  1.00 70.74           N  
ANISOU 1661  N   LEU A 238     8580   8941   9359   -663   2159    -47       N  
ATOM   1662  CA  LEU A 238      32.168  31.779 -34.437  1.00 72.27           C  
ANISOU 1662  CA  LEU A 238     8995   9010   9455   -707   2260      6       C  
ATOM   1663  C   LEU A 238      32.652  32.802 -33.416  1.00 69.98           C  
ANISOU 1663  C   LEU A 238     8820   8695   9073   -524   2290     14       C  
ATOM   1664  O   LEU A 238      32.364  32.677 -32.215  1.00 65.12           O  
ANISOU 1664  O   LEU A 238     8291   8079   8373   -537   2435     45       O  
ATOM   1665  CB  LEU A 238      33.285  30.808 -34.806  1.00 72.85           C  
ANISOU 1665  CB  LEU A 238     9268   8900   9511   -772   2166     30       C  
ATOM   1666  CG  LEU A 238      32.748  29.673 -35.677  1.00 78.67           C  
ANISOU 1666  CG  LEU A 238     9940   9635  10317   -975   2158     16       C  
ATOM   1667  CD1 LEU A 238      33.891  28.851 -36.245  1.00 79.89           C  
ANISOU 1667  CD1 LEU A 238    10287   9607  10462   -996   2055     23       C  
ATOM   1668  CD2 LEU A 238      31.779  28.797 -34.893  1.00 79.52           C  
ANISOU 1668  CD2 LEU A 238    10033   9771  10408  -1164   2329     51       C  
ATOM   1669  N   MET A 239      33.377  33.831 -33.881  1.00 67.31           N  
ANISOU 1669  N   MET A 239     8500   8331   8742   -363   2157    -15       N  
ATOM   1670  CA  MET A 239      33.904  34.849 -32.980  1.00 68.28           C  
ANISOU 1670  CA  MET A 239     8753   8415   8777   -203   2162    -17       C  
ATOM   1671  C   MET A 239      32.787  35.687 -32.380  1.00 72.18           C  
ANISOU 1671  C   MET A 239     9127   9043   9256   -117   2298    -45       C  
ATOM   1672  O   MET A 239      32.847  36.060 -31.203  1.00 76.16           O  
ANISOU 1672  O   MET A 239     9766   9520   9651    -49   2393    -40       O  
ATOM   1673  CB  MET A 239      34.904  35.735 -33.716  1.00 68.44           C  
ANISOU 1673  CB  MET A 239     8812   8374   8819    -82   1988    -41       C  
ATOM   1674  CG  MET A 239      36.282  35.134 -33.811  1.00 68.48           C  
ANISOU 1674  CG  MET A 239     8988   8233   8799   -113   1880     -8       C  
ATOM   1675  SD  MET A 239      37.500  36.203 -34.602  1.00 69.90           S  
ANISOU 1675  SD  MET A 239     9200   8354   9004      7   1700    -29       S  
ATOM   1676  CE  MET A 239      36.884  36.256 -36.282  1.00 65.36           C  
ANISOU 1676  CE  MET A 239     8420   7869   8545    -23   1641    -63       C  
ATOM   1677  N   VAL A 240      31.747  35.972 -33.161  1.00 73.99           N  
ANISOU 1677  N   VAL A 240     9104   9420   9587   -111   2310    -77       N  
ATOM   1678  CA  VAL A 240      30.604  36.696 -32.621  1.00 75.54           C  
ANISOU 1678  CA  VAL A 240     9153   9762   9786    -15   2455   -102       C  
ATOM   1679  C   VAL A 240      29.932  35.877 -31.531  1.00 78.74           C  
ANISOU 1679  C   VAL A 240     9570  10214  10133   -138   2666    -70       C  
ATOM   1680  O   VAL A 240      29.606  36.400 -30.459  1.00 85.18           O  
ANISOU 1680  O   VAL A 240    10446  11059  10862    -43   2814    -77       O  
ATOM   1681  CB  VAL A 240      29.622  37.074 -33.745  1.00 77.77           C  
ANISOU 1681  CB  VAL A 240     9138  10210  10201     15   2405   -133       C  
ATOM   1682  CG1 VAL A 240      28.278  37.466 -33.162  1.00 79.73           C  
ANISOU 1682  CG1 VAL A 240     9180  10640  10472     80   2587   -150       C  
ATOM   1683  CG2 VAL A 240      30.193  38.223 -34.576  1.00 75.33           C  
ANISOU 1683  CG2 VAL A 240     8853   9854   9916    189   2232   -162       C  
ATOM   1684  N   LEU A 241      29.729  34.579 -31.769  1.00 78.32           N  
ANISOU 1684  N   LEU A 241     9484  10158  10117   -355   2692    -34       N  
ATOM   1685  CA  LEU A 241      29.122  33.764 -30.719  1.00 80.73           C  
ANISOU 1685  CA  LEU A 241     9825  10491  10358   -494   2901      9       C  
ATOM   1686  C   LEU A 241      29.997  33.739 -29.468  1.00 73.77           C  
ANISOU 1686  C   LEU A 241     9265   9457   9308   -444   2951     46       C  
ATOM   1687  O   LEU A 241      29.504  33.957 -28.353  1.00 74.27           O  
ANISOU 1687  O   LEU A 241     9379   9568   9273   -411   3137     55       O  
ATOM   1688  CB  LEU A 241      28.851  32.350 -31.225  1.00 87.22           C  
ANISOU 1688  CB  LEU A 241    10599  11297  11242   -753   2904     43       C  
ATOM   1689  CG  LEU A 241      27.718  32.210 -32.247  1.00 92.68           C  
ANISOU 1689  CG  LEU A 241    10956  12174  12086   -855   2890     10       C  
ATOM   1690  CD1 LEU A 241      27.507  30.748 -32.577  1.00 97.97           C  
ANISOU 1690  CD1 LEU A 241    11638  12796  12792  -1139   2904     42       C  
ATOM   1691  CD2 LEU A 241      26.417  32.840 -31.755  1.00 92.10           C  
ANISOU 1691  CD2 LEU A 241    10623  12325  12047   -797   3069     -7       C  
ATOM   1692  N   ALA A 242      31.305  33.511 -29.639  1.00 69.70           N  
ANISOU 1692  N   ALA A 242     8965   8766   8751   -429   2786     65       N  
ATOM   1693  CA  ALA A 242      32.205  33.464 -28.491  1.00 67.41           C  
ANISOU 1693  CA  ALA A 242     8977   8337   8301   -382   2796    104       C  
ATOM   1694  C   ALA A 242      32.180  34.767 -27.703  1.00 70.82           C  
ANISOU 1694  C   ALA A 242     9471   8800   8637   -192   2843     61       C  
ATOM   1695  O   ALA A 242      32.139  34.748 -26.466  1.00 74.25           O  
ANISOU 1695  O   ALA A 242    10084   9208   8921   -179   2971     84       O  
ATOM   1696  CB  ALA A 242      33.627  33.147 -28.947  1.00 63.64           C  
ANISOU 1696  CB  ALA A 242     8663   7694   7822   -368   2587    125       C  
ATOM   1697  N   TYR A 243      32.201  35.910 -28.393  1.00 67.84           N  
ANISOU 1697  N   TYR A 243     8975   8468   8332    -43   2743     -2       N  
ATOM   1698  CA  TYR A 243      32.230  37.182 -27.679  1.00 67.47           C  
ANISOU 1698  CA  TYR A 243     9023   8422   8192    142   2777    -51       C  
ATOM   1699  C   TYR A 243      30.877  37.520 -27.070  1.00 72.84           C  
ANISOU 1699  C   TYR A 243     9568   9254   8852    192   3015    -77       C  
ATOM   1700  O   TYR A 243      30.825  38.210 -26.049  1.00 74.91           O  
ANISOU 1700  O   TYR A 243     9982   9499   8980    309   3117   -105       O  
ATOM   1701  CB  TYR A 243      32.724  38.307 -28.596  1.00 68.48           C  
ANISOU 1701  CB  TYR A 243     9100   8523   8396    284   2597   -103       C  
ATOM   1702  CG  TYR A 243      34.233  38.335 -28.704  1.00 64.36           C  
ANISOU 1702  CG  TYR A 243     8780   7840   7833    282   2397    -86       C  
ATOM   1703  CD1 TYR A 243      35.016  38.540 -27.574  1.00 63.77           C  
ANISOU 1703  CD1 TYR A 243     8971   7658   7601    315   2382    -78       C  
ATOM   1704  CD2 TYR A 243      34.879  38.131 -29.920  1.00 62.02           C  
ANISOU 1704  CD2 TYR A 243     8406   7508   7650    241   2225    -77       C  
ATOM   1705  CE1 TYR A 243      36.397  38.550 -27.645  1.00 62.64           C  
ANISOU 1705  CE1 TYR A 243     8982   7390   7430    308   2192    -59       C  
ATOM   1706  CE2 TYR A 243      36.273  38.134 -29.999  1.00 59.63           C  
ANISOU 1706  CE2 TYR A 243     8262   7077   7319    239   2059    -58       C  
ATOM   1707  CZ  TYR A 243      37.023  38.349 -28.859  1.00 60.90           C  
ANISOU 1707  CZ  TYR A 243     8656   7145   7338    272   2038    -48       C  
ATOM   1708  OH  TYR A 243      38.392  38.362 -28.919  1.00 64.22           O  
ANISOU 1708  OH  TYR A 243     9201   7461   7740    268   1865    -28       O  
ATOM   1709  N   LEU A 244      29.779  37.024 -27.642  1.00 75.08           N  
ANISOU 1709  N   LEU A 244     9573   9693   9263    101   3110    -70       N  
ATOM   1710  CA  LEU A 244      28.496  37.146 -26.955  1.00 79.04           C  
ANISOU 1710  CA  LEU A 244     9929  10356   9746    121   3365    -81       C  
ATOM   1711  C   LEU A 244      28.515  36.381 -25.635  1.00 80.45           C  
ANISOU 1711  C   LEU A 244    10322  10485   9759      8   3547    -28       C  
ATOM   1712  O   LEU A 244      28.050  36.881 -24.598  1.00 82.63           O  
ANISOU 1712  O   LEU A 244    10672  10808   9914    104   3740    -48       O  
ATOM   1713  CB  LEU A 244      27.363  36.648 -27.851  1.00 86.77           C  
ANISOU 1713  CB  LEU A 244    10545  11521  10902      8   3411    -77       C  
ATOM   1714  CG  LEU A 244      26.902  37.610 -28.952  1.00 93.20           C  
ANISOU 1714  CG  LEU A 244    11102  12447  11862    166   3295   -132       C  
ATOM   1715  CD1 LEU A 244      25.858  36.945 -29.833  1.00 97.39           C  
ANISOU 1715  CD1 LEU A 244    11284  13162  12556     17   3309   -121       C  
ATOM   1716  CD2 LEU A 244      26.343  38.881 -28.335  1.00 94.98           C  
ANISOU 1716  CD2 LEU A 244    11298  12747  12043    417   3424   -187       C  
ATOM   1717  N   GLN A 245      29.052  35.161 -25.653  1.00 77.86           N  
ANISOU 1717  N   GLN A 245    10117  10055   9412   -188   3495     42       N  
ATOM   1718  CA  GLN A 245      29.134  34.403 -24.408  1.00 83.37           C  
ANISOU 1718  CA  GLN A 245    11054  10684   9937   -295   3653    107       C  
ATOM   1719  C   GLN A 245      30.069  35.079 -23.409  1.00 78.55           C  
ANISOU 1719  C   GLN A 245    10776   9940   9131   -146   3605     95       C  
ATOM   1720  O   GLN A 245      29.761  35.151 -22.210  1.00 78.05           O  
ANISOU 1720  O   GLN A 245    10873   9887   8897   -127   3795    107       O  
ATOM   1721  CB  GLN A 245      29.567  32.969 -24.690  1.00 87.63           C  
ANISOU 1721  CB  GLN A 245    11681  11115  10501   -517   3587    188       C  
ATOM   1722  CG  GLN A 245      28.535  32.174 -25.463  1.00 96.98           C  
ANISOU 1722  CG  GLN A 245    12577  12424  11845   -710   3668    201       C  
ATOM   1723  CD  GLN A 245      28.901  30.706 -25.571  1.00105.85           C  
ANISOU 1723  CD  GLN A 245    13843  13412  12964   -939   3637    281       C  
ATOM   1724  OE1 GLN A 245      29.763  30.220 -24.839  1.00109.99           O  
ANISOU 1724  OE1 GLN A 245    14681  13764  13345   -950   3609    341       O  
ATOM   1725  NE2 GLN A 245      28.250  29.991 -26.486  1.00107.17           N  
ANISOU 1725  NE2 GLN A 245    13789  13647  13283  -1121   3634    281       N  
ATOM   1726  N   ILE A 246      31.195  35.617 -23.893  1.00 74.14           N  
ANISOU 1726  N   ILE A 246    10318   9263   8587    -46   3356     68       N  
ATOM   1727  CA  ILE A 246      32.143  36.305 -23.017  1.00 74.21           C  
ANISOU 1727  CA  ILE A 246    10629   9149   8420     78   3274     50       C  
ATOM   1728  C   ILE A 246      31.516  37.565 -22.417  1.00 81.31           C  
ANISOU 1728  C   ILE A 246    11534  10121   9240    258   3411    -33       C  
ATOM   1729  O   ILE A 246      31.690  37.849 -21.225  1.00 85.58           O  
ANISOU 1729  O   ILE A 246    12332  10608   9576    312   3498    -40       O  
ATOM   1730  CB  ILE A 246      33.440  36.631 -23.780  1.00 70.12           C  
ANISOU 1730  CB  ILE A 246    10168   8510   7965    128   2980     37       C  
ATOM   1731  CG1 ILE A 246      34.235  35.349 -24.082  1.00 66.51           C  
ANISOU 1731  CG1 ILE A 246     9785   7951   7535    -19   2859    121       C  
ATOM   1732  CG2 ILE A 246      34.285  37.654 -22.995  1.00 66.11           C  
ANISOU 1732  CG2 ILE A 246     9917   7904   7300    266   2884     -7       C  
ATOM   1733  CD1 ILE A 246      35.356  35.554 -25.120  1.00 61.14           C  
ANISOU 1733  CD1 ILE A 246     9071   7193   6968     17   2598    108       C  
ATOM   1734  N   PHE A 247      30.789  38.341 -23.224  1.00 79.76           N  
ANISOU 1734  N   PHE A 247    11071  10040   9194    364   3430    -96       N  
ATOM   1735  CA  PHE A 247      30.112  39.524 -22.706  1.00 80.14           C  
ANISOU 1735  CA  PHE A 247    11114  10155   9180    559   3576   -176       C  
ATOM   1736  C   PHE A 247      29.101  39.140 -21.641  1.00 82.38           C  
ANISOU 1736  C   PHE A 247    11403  10548   9350    524   3888   -160       C  
ATOM   1737  O   PHE A 247      29.044  39.758 -20.572  1.00 84.41           O  
ANISOU 1737  O   PHE A 247    11874  10775   9422    640   4017   -202       O  
ATOM   1738  CB  PHE A 247      29.423  40.294 -23.837  1.00 81.62           C  
ANISOU 1738  CB  PHE A 247    10990  10457   9565    682   3540   -231       C  
ATOM   1739  CG  PHE A 247      28.481  41.371 -23.351  1.00 88.73           C  
ANISOU 1739  CG  PHE A 247    11831  11452  10428    894   3732   -307       C  
ATOM   1740  CD1 PHE A 247      28.953  42.641 -23.040  1.00 90.74           C  
ANISOU 1740  CD1 PHE A 247    12296  11591  10589   1094   3665   -384       C  
ATOM   1741  CD2 PHE A 247      27.123  41.115 -23.203  1.00 92.53           C  
ANISOU 1741  CD2 PHE A 247    12049  12138  10972    894   3985   -303       C  
ATOM   1742  CE1 PHE A 247      28.092  43.627 -22.583  1.00 92.91           C  
ANISOU 1742  CE1 PHE A 247    12543  11936  10825   1311   3851   -459       C  
ATOM   1743  CE2 PHE A 247      26.258  42.100 -22.739  1.00 94.48           C  
ANISOU 1743  CE2 PHE A 247    12234  12477  11187   1116   4177   -375       C  
ATOM   1744  CZ  PHE A 247      26.745  43.355 -22.433  1.00 93.61           C  
ANISOU 1744  CZ  PHE A 247    12357  12234  10976   1335   4112   -454       C  
ATOM   1745  N   ARG A 248      28.284  38.124 -21.925  1.00 82.78           N  
ANISOU 1745  N   ARG A 248    11223  10725   9503    356   4020   -101       N  
ATOM   1746  CA  ARG A 248      27.275  37.697 -20.964  1.00 88.32           C  
ANISOU 1746  CA  ARG A 248    11901  11548  10110    294   4338    -75       C  
ATOM   1747  C   ARG A 248      27.916  37.246 -19.655  1.00 90.11           C  
ANISOU 1747  C   ARG A 248    12526  11636  10075    231   4403    -26       C  
ATOM   1748  O   ARG A 248      27.387  37.518 -18.571  1.00 89.84           O  
ANISOU 1748  O   ARG A 248    12613  11651   9873    291   4646    -43       O  
ATOM   1749  CB  ARG A 248      26.416  36.587 -21.575  1.00 92.80           C  
ANISOU 1749  CB  ARG A 248    12163  12256  10842     76   4433    -12       C  
ATOM   1750  CG  ARG A 248      25.949  35.513 -20.615  1.00100.55           C  
ANISOU 1750  CG  ARG A 248    13240  13264  11701   -125   4680     70       C  
ATOM   1751  CD  ARG A 248      24.613  34.927 -21.059  1.00108.84           C  
ANISOU 1751  CD  ARG A 248    13900  14534  12920   -279   4871     93       C  
ATOM   1752  NE  ARG A 248      23.535  35.914 -20.976  1.00114.80           N  
ANISOU 1752  NE  ARG A 248    14386  15499  13734    -91   5060     19       N  
ATOM   1753  CZ  ARG A 248      22.803  36.137 -19.888  1.00120.23           C  
ANISOU 1753  CZ  ARG A 248    15102  16291  14289    -37   5374     12       C  
ATOM   1754  NH1 ARG A 248      23.026  35.436 -18.782  1.00122.01           N  
ANISOU 1754  NH1 ARG A 248    15627  16427  14303   -174   5532     80       N  
ATOM   1755  NH2 ARG A 248      21.848  37.060 -19.907  1.00123.31           N  
ANISOU 1755  NH2 ARG A 248    15227  16872  14752    164   5535    -60       N  
ATOM   1756  N   LYS A 249      29.078  36.591 -19.731  1.00 90.09           N  
ANISOU 1756  N   LYS A 249    12740  11464  10028    125   4184     34       N  
ATOM   1757  CA  LYS A 249      29.742  36.135 -18.513  1.00 91.51           C  
ANISOU 1757  CA  LYS A 249    13305  11510   9955     73   4210     91       C  
ATOM   1758  C   LYS A 249      30.383  37.295 -17.750  1.00 88.83           C  
ANISOU 1758  C   LYS A 249    13246  11078   9428    267   4140     14       C  
ATOM   1759  O   LYS A 249      30.205  37.427 -16.533  1.00 88.96           O  
ANISOU 1759  O   LYS A 249    13508  11082   9212    299   4313     12       O  
ATOM   1760  CB  LYS A 249      30.791  35.076 -18.864  1.00 94.70           C  
ANISOU 1760  CB  LYS A 249    13835  11764  10381    -75   3984    181       C  
ATOM   1761  CG  LYS A 249      31.447  34.411 -17.666  1.00101.12           C  
ANISOU 1761  CG  LYS A 249    15035  12442  10945   -143   3995    265       C  
ATOM   1762  CD  LYS A 249      31.046  32.958 -17.593  1.00109.77           C  
ANISOU 1762  CD  LYS A 249    16127  13529  12053   -367   4121    380       C  
ATOM   1763  CE  LYS A 249      31.905  32.190 -16.607  1.00115.51           C  
ANISOU 1763  CE  LYS A 249    17250  14087  12552   -427   4061    482       C  
ATOM   1764  NZ  LYS A 249      31.473  30.761 -16.484  1.00119.18           N  
ANISOU 1764  NZ  LYS A 249    17750  14519  13014   -651   4202    603       N  
ATOM   1765  N   LEU A 250      31.115  38.153 -18.458  1.00 87.43           N  
ANISOU 1765  N   LEU A 250    13045  10833   9341    387   3892    -51       N  
ATOM   1766  CA  LEU A 250      31.916  39.204 -17.842  1.00 85.92           C  
ANISOU 1766  CA  LEU A 250    13140  10522   8983    534   3769   -122       C  
ATOM   1767  C   LEU A 250      31.083  40.366 -17.331  1.00 86.17           C  
ANISOU 1767  C   LEU A 250    13182  10623   8936    722   3972   -228       C  
ATOM   1768  O   LEU A 250      31.474  41.008 -16.354  1.00 88.15           O  
ANISOU 1768  O   LEU A 250    13748  10782   8962    813   3977   -280       O  
ATOM   1769  CB  LEU A 250      32.946  39.737 -18.840  1.00 81.36           C  
ANISOU 1769  CB  LEU A 250    12516   9852   8545    578   3449   -153       C  
ATOM   1770  CG  LEU A 250      34.284  39.014 -18.909  1.00 80.14           C  
ANISOU 1770  CG  LEU A 250    12519   9565   8366    466   3192    -78       C  
ATOM   1771  CD1 LEU A 250      35.215  39.674 -19.910  1.00 78.95           C  
ANISOU 1771  CD1 LEU A 250    12293   9347   8358    517   2914   -117       C  
ATOM   1772  CD2 LEU A 250      34.916  38.970 -17.526  1.00 81.52           C  
ANISOU 1772  CD2 LEU A 250    13079   9638   8258    465   3176    -60       C  
ATOM   1773  N   TRP A 251      29.966  40.677 -17.983  1.00 88.82           N  
ANISOU 1773  N   TRP A 251    13185  11115   9447    794   4126   -265       N  
ATOM   1774  CA  TRP A 251      29.203  41.873 -17.647  1.00 94.06           C  
ANISOU 1774  CA  TRP A 251    13832  11838  10066   1015   4301   -372       C  
ATOM   1775  C   TRP A 251      27.890  41.578 -16.941  1.00101.37           C  
ANISOU 1775  C   TRP A 251    14645  12936  10933   1024   4676   -366       C  
ATOM   1776  O   TRP A 251      27.490  42.335 -16.053  1.00101.25           O  
ANISOU 1776  O   TRP A 251    14794  12927  10749   1184   4868   -441       O  
ATOM   1777  CB  TRP A 251      28.921  42.697 -18.907  1.00 88.91           C  
ANISOU 1777  CB  TRP A 251    12890  11236   9655   1151   4186   -429       C  
ATOM   1778  CG  TRP A 251      29.977  43.693 -19.214  1.00 84.08           C  
ANISOU 1778  CG  TRP A 251    12472  10449   9025   1254   3917   -491       C  
ATOM   1779  CD1 TRP A 251      30.069  44.965 -18.733  1.00 87.09           C  
ANISOU 1779  CD1 TRP A 251    13067  10737   9287   1453   3929   -596       C  
ATOM   1780  CD2 TRP A 251      31.103  43.506 -20.075  1.00 79.49           C  
ANISOU 1780  CD2 TRP A 251    11896   9759   8547   1155   3603   -454       C  
ATOM   1781  NE1 TRP A 251      31.180  45.587 -19.247  1.00 88.33           N  
ANISOU 1781  NE1 TRP A 251    13358  10733   9471   1463   3635   -622       N  
ATOM   1782  CE2 TRP A 251      31.837  44.712 -20.071  1.00 82.32           C  
ANISOU 1782  CE2 TRP A 251    12461   9969   8847   1285   3437   -534       C  
ATOM   1783  CE3 TRP A 251      31.565  42.436 -20.843  1.00 75.04           C  
ANISOU 1783  CE3 TRP A 251    11191   9206   8117    970   3457   -363       C  
ATOM   1784  CZ2 TRP A 251      33.008  44.880 -20.811  1.00 83.49           C  
ANISOU 1784  CZ2 TRP A 251    12652   9997   9072   1223   3138   -520       C  
ATOM   1785  CZ3 TRP A 251      32.727  42.600 -21.580  1.00 76.85           C  
ANISOU 1785  CZ3 TRP A 251    11465   9315   8417    934   3166   -354       C  
ATOM   1786  CH2 TRP A 251      33.433  43.818 -21.567  1.00 80.16           C  
ANISOU 1786  CH2 TRP A 251    12066   9606   8784   1055   3013   -429       C  
ATOM   1787  N   CYS A 252      27.209  40.507 -17.325  1.00 84.70           N  
ANISOU 1787  N   CYS A 252    12032  10311   9840    399    692   -123       N  
ATOM   1788  CA  CYS A 252      25.899  40.189 -16.775  1.00 91.43           C  
ANISOU 1788  CA  CYS A 252    12787  11343  10608    402    672   -114       C  
ATOM   1789  C   CYS A 252      25.943  39.155 -15.660  1.00 97.93           C  
ANISOU 1789  C   CYS A 252    13589  12136  11482    285    652   -145       C  
ATOM   1790  O   CYS A 252      25.111  39.215 -14.749  1.00103.09           O  
ANISOU 1790  O   CYS A 252    14192  12887  12091    310    640   -131       O  
ATOM   1791  CB  CYS A 252      24.970  39.694 -17.888  1.00 91.31           C  
ANISOU 1791  CB  CYS A 252    12672  11533  10488    363    662   -115       C  
ATOM   1792  SG  CYS A 252      24.874  40.838 -19.286  1.00 90.32           S  
ANISOU 1792  SG  CYS A 252    12562  11465  10292    514    689    -70       S  
ATOM   1793  N   ARG A 253      26.888  38.215 -15.704  1.00 97.70           N  
ANISOU 1793  N   ARG A 253    13605  11980  11536    174    656   -181       N  
ATOM   1794  CA  ARG A 253      26.994  37.176 -14.690  1.00 95.44           C  
ANISOU 1794  CA  ARG A 253    13321  11652  11290     77    652   -206       C  
ATOM   1795  C   ARG A 253      28.106  37.422 -13.681  1.00 91.79           C  
ANISOU 1795  C   ARG A 253    12917  11032  10925    102    658   -196       C  
ATOM   1796  O   ARG A 253      28.189  36.692 -12.690  1.00 91.26           O  
ANISOU 1796  O   ARG A 253    12850  10935  10889     49    656   -207       O  
ATOM   1797  CB  ARG A 253      27.209  35.806 -15.349  1.00 99.79           C  
ANISOU 1797  CB  ARG A 253    13901  12177  11837    -56    671   -244       C  
ATOM   1798  CG  ARG A 253      25.985  35.249 -16.065  1.00106.10           C  
ANISOU 1798  CG  ARG A 253    14639  13159  12514   -150    664   -265       C  
ATOM   1799  CD  ARG A 253      26.297  33.917 -16.744  1.00111.46           C  
ANISOU 1799  CD  ARG A 253    15398  13774  13178   -298    702   -309       C  
ATOM   1800  NE  ARG A 253      25.098  33.287 -17.293  1.00116.50           N  
ANISOU 1800  NE  ARG A 253    15988  14601  13677   -440    699   -339       N  
ATOM   1801  CZ  ARG A 253      25.103  32.214 -18.078  1.00119.23           C  
ANISOU 1801  CZ  ARG A 253    16414  14924  13962   -595    739   -382       C  
ATOM   1802  NH1 ARG A 253      26.250  31.641 -18.420  1.00119.15           N  
ANISOU 1802  NH1 ARG A 253    16542  14703  14026   -597    789   -393       N  
ATOM   1803  NH2 ARG A 253      23.957  31.716 -18.523  1.00121.54           N  
ANISOU 1803  NH2 ARG A 253    16655  15420  14105   -752    734   -411       N  
ATOM   1804  N   GLN A 254      28.964  38.412 -13.902  1.00 92.54           N  
ANISOU 1804  N   GLN A 254    13065  11040  11058    170    668   -176       N  
ATOM   1805  CA  GLN A 254      30.036  38.720 -12.968  1.00 92.41           C  
ANISOU 1805  CA  GLN A 254    13091  10912  11108    169    674   -165       C  
ATOM   1806  C   GLN A 254      29.997  40.199 -12.617  1.00 92.41           C  
ANISOU 1806  C   GLN A 254    13145  10887  11081    248    681   -144       C  
ATOM   1807  O   GLN A 254      29.144  40.958 -13.086  1.00 94.61           O  
ANISOU 1807  O   GLN A 254    13432  11226  11290    333    690   -130       O  
ATOM   1808  CB  GLN A 254      31.411  38.353 -13.535  1.00 95.95           C  
ANISOU 1808  CB  GLN A 254    13573  11273  11612    134    692   -162       C  
ATOM   1809  CG  GLN A 254      31.702  36.874 -13.541  1.00 98.83           C  
ANISOU 1809  CG  GLN A 254    13930  11620  12001     73    708   -173       C  
ATOM   1810  CD  GLN A 254      33.119  36.574 -13.963  1.00101.06           C  
ANISOU 1810  CD  GLN A 254    14240  11833  12324     74    735   -152       C  
ATOM   1811  OE1 GLN A 254      33.716  37.316 -14.741  1.00103.52           O  
ANISOU 1811  OE1 GLN A 254    14568  12127  12639     96    738   -141       O  
ATOM   1812  NE2 GLN A 254      33.673  35.488 -13.443  1.00101.90           N  
ANISOU 1812  NE2 GLN A 254    14356  11909  12452     58    762   -139       N  
ATOM   1813  N   GLY A1001      30.948  40.608 -11.788  1.00 89.84           N  
ANISOU 1813  N   GLY A1001    12865  10477  10792    221    688   -137       N  
ATOM   1814  CA  GLY A1001      30.996  41.985 -11.363  1.00 90.72           C  
ANISOU 1814  CA  GLY A1001    13069  10538  10863    266    710   -124       C  
ATOM   1815  C   GLY A1001      30.286  42.220 -10.052  1.00 90.24           C  
ANISOU 1815  C   GLY A1001    13012  10496  10780    292    705   -118       C  
ATOM   1816  O   GLY A1001      29.230  41.641  -9.774  1.00 89.25           O  
ANISOU 1816  O   GLY A1001    12811  10461  10637    321    685   -119       O  
ATOM   1817  N   ILE A1002      30.874  43.084  -9.238  1.00 87.24           N  
ANISOU 1817  N   ILE A1002    12725  10036  10387    267    727   -114       N  
ATOM   1818  CA  ILE A1002      30.341  43.438  -7.936  1.00 87.46           C  
ANISOU 1818  CA  ILE A1002    12783  10060  10389    287    731   -109       C  
ATOM   1819  C   ILE A1002      30.356  44.955  -7.828  1.00 85.65           C  
ANISOU 1819  C   ILE A1002    12731   9738  10076    335    790    -97       C  
ATOM   1820  O   ILE A1002      31.352  45.595  -8.187  1.00 85.00           O  
ANISOU 1820  O   ILE A1002    12746   9572   9978    266    819   -105       O  
ATOM   1821  CB  ILE A1002      31.162  42.785  -6.810  1.00 89.33           C  
ANISOU 1821  CB  ILE A1002    12969  10287  10685    175    704   -119       C  
ATOM   1822  CG1 ILE A1002      30.793  43.374  -5.459  1.00 84.08           C  
ANISOU 1822  CG1 ILE A1002    12364   9597   9986    180    715   -116       C  
ATOM   1823  CG2 ILE A1002      32.652  42.925  -7.094  1.00 93.05           C  
ANISOU 1823  CG2 ILE A1002    13462  10717  11174     74    712   -120       C  
ATOM   1824  CD1 ILE A1002      31.664  42.873  -4.351  1.00 82.97           C  
ANISOU 1824  CD1 ILE A1002    12176   9460   9890     70    693   -120       C  
ATOM   1825  N   ASP A1003      29.247  45.526  -7.352  1.00 82.15           N  
ANISOU 1825  N   ASP A1003    12340   9310   9562    454    818    -76       N  
ATOM   1826  CA  ASP A1003      29.139  46.965  -7.165  1.00 78.82           C  
ANISOU 1826  CA  ASP A1003    12129   8780   9039    526    897    -59       C  
ATOM   1827  C   ASP A1003      30.000  47.388  -5.983  1.00 78.43           C  
ANISOU 1827  C   ASP A1003    12186   8628   8987    391    914    -81       C  
ATOM   1828  O   ASP A1003      29.548  47.352  -4.834  1.00 81.50           O  
ANISOU 1828  O   ASP A1003    12575   9025   9367    402    911    -77       O  
ATOM   1829  CB  ASP A1003      27.675  47.364  -6.953  1.00 80.20           C  
ANISOU 1829  CB  ASP A1003    12321   9025   9126    720    930    -15       C  
ATOM   1830  CG  ASP A1003      27.455  48.878  -6.986  1.00 81.35           C  
ANISOU 1830  CG  ASP A1003    12720   9048   9141    847   1039     17       C  
ATOM   1831  OD1 ASP A1003      28.446  49.638  -7.051  1.00 81.77           O  
ANISOU 1831  OD1 ASP A1003    12955   8945   9170    749   1088     -6       O  
ATOM   1832  OD2 ASP A1003      26.280  49.308  -6.946  1.00 82.13           O  
ANISOU 1832  OD2 ASP A1003    12846   9215   9144   1046   1083     69       O  
ATOM   1833  N   CYS A1004      31.245  47.792  -6.255  1.00 77.26           N  
ANISOU 1833  N   CYS A1004    12120   8400   8835    252    932   -103       N  
ATOM   1834  CA  CYS A1004      32.155  48.182  -5.184  1.00 77.01           C  
ANISOU 1834  CA  CYS A1004    12175   8308   8779     86    945   -124       C  
ATOM   1835  C   CYS A1004      31.801  49.532  -4.577  1.00 75.99           C  
ANISOU 1835  C   CYS A1004    12308   8042   8523    117   1039   -122       C  
ATOM   1836  O   CYS A1004      32.232  49.817  -3.454  1.00 80.84           O  
ANISOU 1836  O   CYS A1004    12995   8616   9103     -8   1052   -139       O  
ATOM   1837  CB  CYS A1004      33.599  48.195  -5.693  1.00 82.03           C  
ANISOU 1837  CB  CYS A1004    12802   8941   9423    -87    937   -143       C  
ATOM   1838  SG  CYS A1004      34.317  46.545  -5.954  1.00 89.49           S  
ANISOU 1838  SG  CYS A1004    13462  10040  10501   -146    842   -138       S  
ATOM   1839  N   SER A1005      31.030  50.370  -5.278  1.00 69.88           N  
ANISOU 1839  N   SER A1005    11690   7197   7663    286   1114    -96       N  
ATOM   1840  CA  SER A1005      30.612  51.629  -4.668  1.00 72.49           C  
ANISOU 1840  CA  SER A1005    12306   7383   7856    349   1225    -84       C  
ATOM   1841  C   SER A1005      29.595  51.396  -3.555  1.00 70.71           C  
ANISOU 1841  C   SER A1005    12034   7204   7628    462   1216    -61       C  
ATOM   1842  O   SER A1005      29.533  52.178  -2.599  1.00 73.55           O  
ANISOU 1842  O   SER A1005    12600   7450   7897    441   1288    -64       O  
ATOM   1843  CB  SER A1005      30.051  52.589  -5.725  1.00 77.12           C  
ANISOU 1843  CB  SER A1005    13084   7884   8334    537   1324    -48       C  
ATOM   1844  OG  SER A1005      28.848  52.106  -6.299  1.00 82.42           O  
ANISOU 1844  OG  SER A1005    13597   8694   9026    770   1297      2       O  
ATOM   1845  N   PHE A1006      28.808  50.325  -3.644  1.00 69.63           N  
ANISOU 1845  N   PHE A1006    11642   7233   7580    564   1133    -40       N  
ATOM   1846  CA  PHE A1006      27.848  50.016  -2.591  1.00 70.76           C  
ANISOU 1846  CA  PHE A1006    11718   7445   7722    656   1117    -19       C  
ATOM   1847  C   PHE A1006      28.432  49.101  -1.521  1.00 69.84           C  
ANISOU 1847  C   PHE A1006    11452   7377   7709    476   1034    -56       C  
ATOM   1848  O   PHE A1006      28.337  49.404  -0.326  1.00 66.34           O  
ANISOU 1848  O   PHE A1006    11092   6884   7232    444   1056    -60       O  
ATOM   1849  CB  PHE A1006      26.589  49.378  -3.175  1.00 68.96           C  
ANISOU 1849  CB  PHE A1006    11302   7396   7506    848   1079     25       C  
ATOM   1850  CG  PHE A1006      25.538  49.094  -2.141  1.00 69.22           C  
ANISOU 1850  CG  PHE A1006    11259   7522   7519    947   1065     53       C  
ATOM   1851  CD1 PHE A1006      24.653  50.084  -1.751  1.00 70.24           C  
ANISOU 1851  CD1 PHE A1006    11559   7616   7513   1145   1160    107       C  
ATOM   1852  CD2 PHE A1006      25.457  47.846  -1.534  1.00 64.77           C  
ANISOU 1852  CD2 PHE A1006    10471   7077   7064    848    967     29       C  
ATOM   1853  CE1 PHE A1006      23.699  49.834  -0.790  1.00 71.56           C  
ANISOU 1853  CE1 PHE A1006    11651   7883   7657   1240   1148    137       C  
ATOM   1854  CE2 PHE A1006      24.501  47.594  -0.576  1.00 64.09           C  
ANISOU 1854  CE2 PHE A1006    10315   7079   6955    927    954     53       C  
ATOM   1855  CZ  PHE A1006      23.618  48.584  -0.211  1.00 68.71           C  
ANISOU 1855  CZ  PHE A1006    11049   7648   7409   1122   1040    107       C  
ATOM   1856  N   TRP A1007      29.004  47.967  -1.928  1.00 73.26           N  
ANISOU 1856  N   TRP A1007    11672   7906   8257    373    946    -77       N  
ATOM   1857  CA  TRP A1007      29.585  47.034  -0.971  1.00 72.51           C  
ANISOU 1857  CA  TRP A1007    11433   7867   8251    229    877   -101       C  
ATOM   1858  C   TRP A1007      30.908  47.585  -0.472  1.00 69.59           C  
ANISOU 1858  C   TRP A1007    11174   7417   7850     34    899   -127       C  
ATOM   1859  O   TRP A1007      31.981  47.101  -0.843  1.00 69.80           O  
ANISOU 1859  O   TRP A1007    11108   7489   7926    -93    862   -140       O  
ATOM   1860  CB  TRP A1007      29.753  45.642  -1.592  1.00 70.89           C  
ANISOU 1860  CB  TRP A1007    10998   7780   8155    204    798   -106       C  
ATOM   1861  CG  TRP A1007      28.452  45.107  -2.073  1.00 69.22           C  
ANISOU 1861  CG  TRP A1007    10682   7669   7948    350    778    -85       C  
ATOM   1862  CD1 TRP A1007      28.031  45.015  -3.360  1.00 68.71           C  
ANISOU 1862  CD1 TRP A1007    10580   7656   7870    432    780    -74       C  
ATOM   1863  CD2 TRP A1007      27.372  44.639  -1.264  1.00 69.11           C  
ANISOU 1863  CD2 TRP A1007    10585   7740   7932    419    755    -73       C  
ATOM   1864  NE1 TRP A1007      26.757  44.507  -3.410  1.00 66.02           N  
ANISOU 1864  NE1 TRP A1007    10129   7446   7509    537    758    -54       N  
ATOM   1865  CE2 TRP A1007      26.332  44.266  -2.132  1.00 68.39           C  
ANISOU 1865  CE2 TRP A1007    10399   7770   7815    529    743    -53       C  
ATOM   1866  CE3 TRP A1007      27.183  44.494   0.117  1.00 67.75           C  
ANISOU 1866  CE3 TRP A1007    10404   7568   7769    390    743    -76       C  
ATOM   1867  CZ2 TRP A1007      25.123  43.747  -1.667  1.00 72.96           C  
ANISOU 1867  CZ2 TRP A1007    10868   8483   8369    598    718    -35       C  
ATOM   1868  CZ3 TRP A1007      25.982  43.997   0.570  1.00 67.34           C  
ANISOU 1868  CZ3 TRP A1007    10253   7627   7705    474    720    -59       C  
ATOM   1869  CH2 TRP A1007      24.969  43.626  -0.316  1.00 70.19           C  
ANISOU 1869  CH2 TRP A1007    10515   8121   8032    572    708    -39       C  
ATOM   1870  N   ASN A1008      30.828  48.608   0.363  1.00 70.61           N  
ANISOU 1870  N   ASN A1008    11506   7440   7881      9    966   -132       N  
ATOM   1871  CA  ASN A1008      31.993  49.316   0.855  1.00 77.74           C  
ANISOU 1871  CA  ASN A1008    12554   8271   8714   -202   1003   -161       C  
ATOM   1872  C   ASN A1008      31.841  49.508   2.354  1.00 76.80           C  
ANISOU 1872  C   ASN A1008    12494   8129   8557   -264   1014   -170       C  
ATOM   1873  O   ASN A1008      30.739  49.766   2.846  1.00 75.72           O  
ANISOU 1873  O   ASN A1008    12430   7949   8391   -111   1047   -151       O  
ATOM   1874  CB  ASN A1008      32.153  50.675   0.128  1.00 82.73           C  
ANISOU 1874  CB  ASN A1008    13471   8747   9215   -204   1110   -168       C  
ATOM   1875  CG  ASN A1008      33.515  51.289   0.332  1.00 86.93           C  
ANISOU 1875  CG  ASN A1008    14127   9236   9665   -471   1141   -204       C  
ATOM   1876  OD1 ASN A1008      33.971  51.468   1.466  1.00 92.57           O  
ANISOU 1876  OD1 ASN A1008    14888   9953  10331   -634   1146   -224       O  
ATOM   1877  ND2 ASN A1008      34.185  51.604  -0.767  1.00 87.10           N  
ANISOU 1877  ND2 ASN A1008    14196   9237   9660   -532   1161   -212       N  
ATOM   1878  N   GLU A1009      32.945  49.359   3.080  1.00 78.32           N  
ANISOU 1878  N   GLU A1009    12642   8373   8742   -485    987   -192       N  
ATOM   1879  CA  GLU A1009      32.895  49.521   4.524  1.00 82.65           C  
ANISOU 1879  CA  GLU A1009    13240   8912   9250   -568    994   -202       C  
ATOM   1880  C   GLU A1009      32.850  50.982   4.958  1.00 84.43           C  
ANISOU 1880  C   GLU A1009    13810   8959   9310   -639   1111   -224       C  
ATOM   1881  O   GLU A1009      32.612  51.252   6.142  1.00 86.23           O  
ANISOU 1881  O   GLU A1009    14126   9150   9489   -682   1135   -232       O  
ATOM   1882  CB  GLU A1009      34.090  48.821   5.168  1.00 90.66           C  
ANISOU 1882  CB  GLU A1009    14070  10078  10297   -775    926   -209       C  
ATOM   1883  CG  GLU A1009      35.442  49.385   4.770  1.00100.27           C  
ANISOU 1883  CG  GLU A1009    15353  11324  11422  -1005    950   -228       C  
ATOM   1884  CD  GLU A1009      36.590  48.498   5.212  1.00108.84           C  
ANISOU 1884  CD  GLU A1009    16190  12624  12540  -1157    875   -212       C  
ATOM   1885  OE1 GLU A1009      37.340  48.016   4.336  1.00112.57           O  
ANISOU 1885  OE1 GLU A1009    16523  13201  13046  -1179    842   -194       O  
ATOM   1886  OE2 GLU A1009      36.731  48.269   6.435  1.00112.39           O  
ANISOU 1886  OE2 GLU A1009    16582  13148  12975  -1239    853   -210       O  
ATOM   1887  N   SER A1010      33.041  51.932   4.034  1.00 83.86           N  
ANISOU 1887  N   SER A1010    13957   8764   9142   -646   1194   -232       N  
ATOM   1888  CA  SER A1010      32.987  53.340   4.416  1.00 83.52           C  
ANISOU 1888  CA  SER A1010    14295   8521   8920   -711   1329   -253       C  
ATOM   1889  C   SER A1010      31.603  53.726   4.913  1.00 78.26           C  
ANISOU 1889  C   SER A1010    13772   7746   8215   -462   1395   -221       C  
ATOM   1890  O   SER A1010      31.472  54.662   5.706  1.00 78.06           O  
ANISOU 1890  O   SER A1010    14038   7570   8052   -512   1499   -234       O  
ATOM   1891  CB  SER A1010      33.385  54.235   3.245  1.00 89.44           C  
ANISOU 1891  CB  SER A1010    15265   9149   9571   -742   1415   -264       C  
ATOM   1892  OG  SER A1010      34.652  53.882   2.720  1.00 90.12           O  
ANISOU 1892  OG  SER A1010    15205   9355   9684   -963   1354   -287       O  
ATOM   1893  N   TYR A1011      30.560  53.023   4.468  1.00 76.53           N  
ANISOU 1893  N   TYR A1011    13361   7614   8102   -199   1343   -176       N  
ATOM   1894  CA  TYR A1011      29.212  53.324   4.929  1.00 74.76           C  
ANISOU 1894  CA  TYR A1011    13233   7341   7833     53   1400   -132       C  
ATOM   1895  C   TYR A1011      28.936  52.839   6.345  1.00 76.37           C  
ANISOU 1895  C   TYR A1011    13338   7603   8076     14   1353   -137       C  
ATOM   1896  O   TYR A1011      27.921  53.232   6.924  1.00 79.22           O  
ANISOU 1896  O   TYR A1011    13817   7910   8372    194   1414   -103       O  
ATOM   1897  CB  TYR A1011      28.183  52.722   3.976  1.00 71.50           C  
ANISOU 1897  CB  TYR A1011    12624   7047   7494    321   1357    -80       C  
ATOM   1898  CG  TYR A1011      28.238  53.320   2.591  1.00 72.12           C  
ANISOU 1898  CG  TYR A1011    12825   7061   7515    411   1421    -64       C  
ATOM   1899  CD1 TYR A1011      27.540  54.484   2.291  1.00 72.57           C  
ANISOU 1899  CD1 TYR A1011    13183   6975   7414    614   1565    -21       C  
ATOM   1900  CD2 TYR A1011      28.993  52.726   1.586  1.00 71.04           C  
ANISOU 1900  CD2 TYR A1011    12515   7005   7472    307   1346    -86       C  
ATOM   1901  CE1 TYR A1011      27.593  55.047   1.022  1.00 70.43           C  
ANISOU 1901  CE1 TYR A1011    13034   6643   7083    706   1630     -2       C  
ATOM   1902  CE2 TYR A1011      29.053  53.280   0.318  1.00 71.98           C  
ANISOU 1902  CE2 TYR A1011    12747   7065   7538    386   1403    -72       C  
ATOM   1903  CZ  TYR A1011      28.347  54.437   0.045  1.00 71.16           C  
ANISOU 1903  CZ  TYR A1011    12937   6820   7280    583   1543    -31       C  
ATOM   1904  OH  TYR A1011      28.398  54.974  -1.217  1.00 73.83           O  
ANISOU 1904  OH  TYR A1011    13389   7102   7562    673   1604    -12       O  
ATOM   1905  N   LEU A1012      29.800  52.009   6.916  1.00 78.30           N  
ANISOU 1905  N   LEU A1012    13372   7963   8414   -199   1252   -171       N  
ATOM   1906  CA  LEU A1012      29.572  51.486   8.254  1.00 82.67           C  
ANISOU 1906  CA  LEU A1012    13820   8582   9011   -236   1203   -174       C  
ATOM   1907  C   LEU A1012      30.168  52.419   9.298  1.00 84.51           C  
ANISOU 1907  C   LEU A1012    14314   8690   9107   -440   1282   -210       C  
ATOM   1908  O   LEU A1012      31.276  52.935   9.132  1.00 86.87           O  
ANISOU 1908  O   LEU A1012    14731   8949   9327   -677   1313   -248       O  
ATOM   1909  CB  LEU A1012      30.164  50.083   8.397  1.00 83.66           C  
ANISOU 1909  CB  LEU A1012    13596   8902   9291   -339   1066   -182       C  
ATOM   1910  CG  LEU A1012      29.712  49.109   7.308  1.00 83.12           C  
ANISOU 1910  CG  LEU A1012    13293   8946   9343   -184    996   -157       C  
ATOM   1911  CD1 LEU A1012      30.352  47.750   7.492  1.00 79.23           C  
ANISOU 1911  CD1 LEU A1012    12510   8614   8980   -281    887   -162       C  
ATOM   1912  CD2 LEU A1012      28.185  49.003   7.267  1.00 82.87           C  
ANISOU 1912  CD2 LEU A1012    13240   8932   9317     75   1007   -117       C  
ATOM   1913  N   THR A1013      29.421  52.641  10.369  1.00 86.01           N  
ANISOU 1913  N   THR A1013    14596   8828   9256   -361   1318   -199       N  
ATOM   1914  CA  THR A1013      29.878  53.494  11.453  1.00 90.37           C  
ANISOU 1914  CA  THR A1013    15409   9258   9670   -555   1398   -234       C  
ATOM   1915  C   THR A1013      30.364  52.652  12.623  1.00 88.60           C  
ANISOU 1915  C   THR A1013    14957   9182   9523   -725   1297   -254       C  
ATOM   1916  O   THR A1013      29.921  51.520  12.826  1.00 89.80           O  
ANISOU 1916  O   THR A1013    14812   9486   9824   -611   1192   -229       O  
ATOM   1917  CB  THR A1013      28.768  54.435  11.919  1.00 95.48           C  
ANISOU 1917  CB  THR A1013    16363   9724  10190   -350   1530   -205       C  
ATOM   1918  OG1 THR A1013      27.643  53.667  12.352  1.00 97.77           O  
ANISOU 1918  OG1 THR A1013    16439  10126  10582   -116   1466   -159       O  
ATOM   1919  CG2 THR A1013      28.344  55.345  10.786  1.00100.11           C  
ANISOU 1919  CG2 THR A1013    17204  10162  10672   -169   1650   -176       C  
ATOM   1920  N   GLY A1014      31.284  53.220  13.392  1.00 85.59           N  
ANISOU 1920  N   GLY A1014    14730   8765   9027  -1008   1335   -298       N  
ATOM   1921  CA  GLY A1014      31.791  52.558  14.577  1.00 79.02           C  
ANISOU 1921  CA  GLY A1014    13707   8080   8236  -1179   1254   -311       C  
ATOM   1922  C   GLY A1014      32.724  51.408  14.239  1.00 73.55           C  
ANISOU 1922  C   GLY A1014    12652   7627   7668  -1283   1124   -304       C  
ATOM   1923  O   GLY A1014      33.011  51.105  13.085  1.00 71.46           O  
ANISOU 1923  O   GLY A1014    12281   7409   7461  -1238   1095   -293       O  
ATOM   1924  N   SER A1015      33.211  50.765  15.291  1.00 71.51           N  
ANISOU 1924  N   SER A1015    12209   7522   7440  -1416   1054   -305       N  
ATOM   1925  CA  SER A1015      34.094  49.626  15.143  1.00 70.93           C  
ANISOU 1925  CA  SER A1015    11797   7688   7466  -1487    945   -284       C  
ATOM   1926  C   SER A1015      33.282  48.355  14.893  1.00 71.76           C  
ANISOU 1926  C   SER A1015    11644   7862   7759  -1225    864   -244       C  
ATOM   1927  O   SER A1015      32.073  48.288  15.146  1.00 72.32           O  
ANISOU 1927  O   SER A1015    11758   7842   7878  -1028    875   -235       O  
ATOM   1928  CB  SER A1015      34.958  49.470  16.388  1.00 73.13           C  
ANISOU 1928  CB  SER A1015    11986   8124   7678  -1726    914   -291       C  
ATOM   1929  OG  SER A1015      34.151  49.314  17.543  1.00 73.93           O  
ANISOU 1929  OG  SER A1015    12103   8181   7807  -1643    910   -289       O  
ATOM   1930  N   ARG A1016      33.968  47.323  14.404  1.00 71.47           N  
ANISOU 1930  N   ARG A1016    11345   7999   7813  -1229    787   -217       N  
ATOM   1931  CA  ARG A1016      33.274  46.083  14.087  1.00 65.47           C  
ANISOU 1931  CA  ARG A1016    10370   7292   7211  -1011    723   -186       C  
ATOM   1932  C   ARG A1016      32.680  45.435  15.332  1.00 65.76           C  
ANISOU 1932  C   ARG A1016    10311   7370   7304   -951    687   -175       C  
ATOM   1933  O   ARG A1016      31.585  44.873  15.262  1.00 64.88           O  
ANISOU 1933  O   ARG A1016    10146   7223   7281   -762    668   -164       O  
ATOM   1934  CB  ARG A1016      34.222  45.118  13.376  1.00 61.78           C  
ANISOU 1934  CB  ARG A1016     9678   6989   6808  -1032    668   -156       C  
ATOM   1935  CG  ARG A1016      33.503  43.931  12.750  1.00 56.05           C  
ANISOU 1935  CG  ARG A1016     8794   6278   6223   -820    624   -132       C  
ATOM   1936  CD  ARG A1016      34.444  43.006  12.017  1.00 56.04           C  
ANISOU 1936  CD  ARG A1016     8610   6413   6270   -824    590    -98       C  
ATOM   1937  NE  ARG A1016      33.672  42.126  11.143  1.00 57.72           N  
ANISOU 1937  NE  ARG A1016     8752   6590   6589   -644    571    -89       N  
ATOM   1938  CZ  ARG A1016      33.403  42.401   9.871  1.00 58.73           C  
ANISOU 1938  CZ  ARG A1016     8940   6646   6727   -581    589   -100       C  
ATOM   1939  NH1 ARG A1016      33.865  43.518   9.323  1.00 58.11           N  
ANISOU 1939  NH1 ARG A1016     9001   6512   6566   -671    627   -118       N  
ATOM   1940  NH2 ARG A1016      32.676  41.562   9.148  1.00 58.85           N  
ANISOU 1940  NH2 ARG A1016     8888   6648   6825   -441    572    -95       N  
ATOM   1941  N   ASP A1017      33.378  45.512  16.471  1.00 70.50           N  
ANISOU 1941  N   ASP A1017    10886   8061   7842  -1120    678   -177       N  
ATOM   1942  CA  ASP A1017      32.847  44.989  17.730  1.00 75.03           C  
ANISOU 1942  CA  ASP A1017    11385   8666   8457  -1076    650   -168       C  
ATOM   1943  C   ASP A1017      31.528  45.659  18.099  1.00 76.29           C  
ANISOU 1943  C   ASP A1017    11737   8649   8599   -954    697   -188       C  
ATOM   1944  O   ASP A1017      30.564  44.989  18.499  1.00 74.46           O  
ANISOU 1944  O   ASP A1017    11419   8419   8453   -797    667   -173       O  
ATOM   1945  CB  ASP A1017      33.856  45.206  18.862  1.00 83.49           C  
ANISOU 1945  CB  ASP A1017    12429   9862   9430  -1303    644   -170       C  
ATOM   1946  CG  ASP A1017      35.037  44.268  18.794  1.00 90.55           C  
ANISOU 1946  CG  ASP A1017    13068  10993  10343  -1369    590   -126       C  
ATOM   1947  OD1 ASP A1017      34.837  43.062  18.542  1.00 92.35           O  
ANISOU 1947  OD1 ASP A1017    13111  11286  10692  -1204    546    -88       O  
ATOM   1948  OD2 ASP A1017      36.170  44.740  19.012  1.00 94.74           O  
ANISOU 1948  OD2 ASP A1017    13592  11655  10749  -1590    599   -124       O  
ATOM   1949  N   GLU A1018      31.489  46.994  18.020  1.00 77.65           N  
ANISOU 1949  N   GLU A1018    12184   8675   8643  -1028    781   -217       N  
ATOM   1950  CA  GLU A1018      30.258  47.709  18.329  1.00 76.39           C  
ANISOU 1950  CA  GLU A1018    12233   8350   8443   -882    847   -221       C  
ATOM   1951  C   GLU A1018      29.136  47.284  17.399  1.00 71.55           C  
ANISOU 1951  C   GLU A1018    11553   7714   7919   -620    834   -194       C  
ATOM   1952  O   GLU A1018      28.002  47.067  17.838  1.00 73.28           O  
ANISOU 1952  O   GLU A1018    11755   7919   8170   -452    832   -175       O  
ATOM   1953  CB  GLU A1018      30.486  49.215  18.240  1.00 83.24           C  
ANISOU 1953  CB  GLU A1018    13446   9043   9137   -995    961   -252       C  
ATOM   1954  CG  GLU A1018      31.405  49.764  19.307  1.00 91.84           C  
ANISOU 1954  CG  GLU A1018    14645  10149  10102  -1277    988   -285       C  
ATOM   1955  CD  GLU A1018      31.680  51.253  19.140  1.00101.06           C  
ANISOU 1955  CD  GLU A1018    16196  11126  11075  -1422   1118   -323       C  
ATOM   1956  OE1 GLU A1018      31.591  51.761  17.997  1.00102.26           O  
ANISOU 1956  OE1 GLU A1018    16480  11175  11197  -1350   1171   -323       O  
ATOM   1957  OE2 GLU A1018      31.988  51.917  20.157  1.00106.51           O  
ANISOU 1957  OE2 GLU A1018    17071  11766  11633  -1616   1173   -355       O  
ATOM   1958  N   ARG A1019      29.435  47.134  16.110  1.00 68.62           N  
ANISOU 1958  N   ARG A1019    11132   7360   7580   -591    824   -189       N  
ATOM   1959  CA  ARG A1019      28.387  46.747  15.178  1.00 64.70           C  
ANISOU 1959  CA  ARG A1019    10568   6866   7150   -364    813   -164       C  
ATOM   1960  C   ARG A1019      27.893  45.340  15.464  1.00 61.00           C  
ANISOU 1960  C   ARG A1019     9836   6532   6810   -282    726   -146       C  
ATOM   1961  O   ARG A1019      26.687  45.093  15.442  1.00 62.42           O  
ANISOU 1961  O   ARG A1019     9980   6726   7011   -112    722   -127       O  
ATOM   1962  CB  ARG A1019      28.877  46.879  13.738  1.00 64.05           C  
ANISOU 1962  CB  ARG A1019    10491   6775   7070   -367    821   -165       C  
ATOM   1963  CG  ARG A1019      29.166  48.308  13.350  1.00 64.69           C  
ANISOU 1963  CG  ARG A1019    10867   6701   7011   -422    923   -181       C  
ATOM   1964  CD  ARG A1019      29.300  48.468  11.846  1.00 68.17           C  
ANISOU 1964  CD  ARG A1019    11323   7122   7456   -362    938   -175       C  
ATOM   1965  NE  ARG A1019      30.340  47.613  11.274  1.00 68.54           N  
ANISOU 1965  NE  ARG A1019    11162   7293   7586   -481    864   -182       N  
ATOM   1966  CZ  ARG A1019      31.618  47.962  11.174  1.00 66.83           C  
ANISOU 1966  CZ  ARG A1019    10985   7094   7314   -692    873   -202       C  
ATOM   1967  NH1 ARG A1019      32.025  49.148  11.612  1.00 67.00           N  
ANISOU 1967  NH1 ARG A1019    11260   7006   7192   -842    953   -229       N  
ATOM   1968  NH2 ARG A1019      32.485  47.122  10.636  1.00 60.79           N  
ANISOU 1968  NH2 ARG A1019    10015   6462   6619   -759    809   -194       N  
ATOM   1969  N   LYS A1020      28.799  44.413  15.762  1.00 62.61           N  
ANISOU 1969  N   LYS A1020     9863   6845   7082   -400    664   -149       N  
ATOM   1970  CA  LYS A1020      28.367  43.054  16.066  1.00 64.93           C  
ANISOU 1970  CA  LYS A1020     9945   7242   7483   -328    599   -133       C  
ATOM   1971  C   LYS A1020      27.515  43.007  17.327  1.00 63.06           C  
ANISOU 1971  C   LYS A1020     9717   7000   7243   -280    596   -130       C  
ATOM   1972  O   LYS A1020      26.482  42.329  17.351  1.00 63.54           O  
ANISOU 1972  O   LYS A1020     9687   7102   7354   -157    571   -119       O  
ATOM   1973  CB  LYS A1020      29.565  42.119  16.216  1.00 67.84           C  
ANISOU 1973  CB  LYS A1020    10150   7723   7903   -439    554   -123       C  
ATOM   1974  CG  LYS A1020      29.126  40.663  16.314  1.00 69.70           C  
ANISOU 1974  CG  LYS A1020    10209   8036   8238   -352    508   -106       C  
ATOM   1975  CD  LYS A1020      30.295  39.712  16.313  1.00 67.44           C  
ANISOU 1975  CD  LYS A1020     9781   7854   7987   -414    484    -81       C  
ATOM   1976  CE  LYS A1020      30.889  39.575  17.687  1.00 62.12           C  
ANISOU 1976  CE  LYS A1020     9055   7257   7291   -500    471    -66       C  
ATOM   1977  NZ  LYS A1020      31.892  38.476  17.695  1.00 60.69           N  
ANISOU 1977  NZ  LYS A1020     8719   7203   7137   -506    456    -23       N  
ATOM   1978  N   LYS A1021      27.927  43.710  18.381  1.00 65.32           N  
ANISOU 1978  N   LYS A1021    10113   7247   7460   -388    623   -142       N  
ATOM   1979  CA  LYS A1021      27.131  43.710  19.606  1.00 66.99           C  
ANISOU 1979  CA  LYS A1021    10343   7447   7665   -341    624   -139       C  
ATOM   1980  C   LYS A1021      25.762  44.328  19.363  1.00 63.79           C  
ANISOU 1980  C   LYS A1021    10056   6968   7213   -157    671   -125       C  
ATOM   1981  O   LYS A1021      24.749  43.807  19.828  1.00 61.96           O  
ANISOU 1981  O   LYS A1021     9739   6788   7015    -43    647   -109       O  
ATOM   1982  CB  LYS A1021      27.864  44.454  20.722  1.00 72.61           C  
ANISOU 1982  CB  LYS A1021    11176   8124   8291   -509    653   -157       C  
ATOM   1983  CG  LYS A1021      29.145  43.769  21.173  1.00 77.89           C  
ANISOU 1983  CG  LYS A1021    11685   8924   8985   -677    603   -155       C  
ATOM   1984  CD  LYS A1021      30.005  44.678  22.044  1.00 82.28           C  
ANISOU 1984  CD  LYS A1021    12374   9471   9419   -889    639   -176       C  
ATOM   1985  CE  LYS A1021      31.341  44.010  22.368  1.00 87.25           C  
ANISOU 1985  CE  LYS A1021    12814  10288  10051  -1048    590   -159       C  
ATOM   1986  NZ  LYS A1021      32.309  44.921  23.053  1.00 90.16           N  
ANISOU 1986  NZ  LYS A1021    13293  10693  10271  -1299    623   -180       N  
ATOM   1987  N   SER A1022      25.704  45.427  18.614  1.00 67.60           N  
ANISOU 1987  N   SER A1022    10734   7345   7606   -117    742   -125       N  
ATOM   1988  CA  SER A1022      24.413  46.028  18.304  1.00 69.66           C  
ANISOU 1988  CA  SER A1022    11103   7562   7803     95    799    -94       C  
ATOM   1989  C   SER A1022      23.551  45.078  17.482  1.00 71.22           C  
ANISOU 1989  C   SER A1022    11095   7891   8073    236    744    -70       C  
ATOM   1990  O   SER A1022      22.357  44.921  17.756  1.00 76.87           O  
ANISOU 1990  O   SER A1022    11762   8675   8771    387    744    -39       O  
ATOM   1991  CB  SER A1022      24.625  47.361  17.578  1.00 71.07           C  
ANISOU 1991  CB  SER A1022    11548   7595   7860    117    899    -94       C  
ATOM   1992  OG  SER A1022      23.397  47.889  17.122  1.00 77.67           O  
ANISOU 1992  OG  SER A1022    12473   8414   8623    359    961    -47       O  
ATOM   1993  N   LEU A1023      24.148  44.404  16.495  1.00 67.47           N  
ANISOU 1993  N   LEU A1023    10495   7469   7670    176    698    -82       N  
ATOM   1994  CA  LEU A1023      23.409  43.433  15.695  1.00 67.78           C  
ANISOU 1994  CA  LEU A1023    10353   7634   7769    268    649    -67       C  
ATOM   1995  C   LEU A1023      22.830  42.329  16.567  1.00 61.80           C  
ANISOU 1995  C   LEU A1023     9428   6980   7073    265    592    -67       C  
ATOM   1996  O   LEU A1023      21.626  42.056  16.522  1.00 61.52           O  
ANISOU 1996  O   LEU A1023     9320   7042   7013    382    583    -43       O  
ATOM   1997  CB  LEU A1023      24.317  42.831  14.623  1.00 73.19           C  
ANISOU 1997  CB  LEU A1023    10952   8338   8520    180    616    -85       C  
ATOM   1998  CG  LEU A1023      23.681  41.707  13.797  1.00 78.31           C  
ANISOU 1998  CG  LEU A1023    11427   9105   9223    232    570    -79       C  
ATOM   1999  CD1 LEU A1023      22.739  42.279  12.737  1.00 81.94           C  
ANISOU 1999  CD1 LEU A1023    11923   9602   9608    379    603    -53       C  
ATOM   2000  CD2 LEU A1023      24.735  40.825  13.160  1.00 79.04           C  
ANISOU 2000  CD2 LEU A1023    11430   9207   9394    123    536    -98       C  
ATOM   2001  N   LEU A1024      23.675  41.685  17.372  1.00 59.37           N  
ANISOU 2001  N   LEU A1024     9057   6670   6833    131    555    -88       N  
ATOM   2002  CA  LEU A1024      23.199  40.588  18.212  1.00 64.94           C  
ANISOU 2002  CA  LEU A1024     9620   7459   7595    123    507    -88       C  
ATOM   2003  C   LEU A1024      22.140  41.066  19.198  1.00 64.05           C  
ANISOU 2003  C   LEU A1024     9554   7356   7426    214    526    -71       C  
ATOM   2004  O   LEU A1024      21.128  40.384  19.401  1.00 64.93           O  
ANISOU 2004  O   LEU A1024     9556   7570   7545    274    499    -60       O  
ATOM   2005  CB  LEU A1024      24.378  39.927  18.939  1.00 63.79           C  
ANISOU 2005  CB  LEU A1024     9415   7311   7513    -14    479   -101       C  
ATOM   2006  CG  LEU A1024      25.339  39.248  17.949  1.00 60.74           C  
ANISOU 2006  CG  LEU A1024     8958   6944   7176    -73    463   -105       C  
ATOM   2007  CD1 LEU A1024      26.581  38.655  18.606  1.00 59.84           C  
ANISOU 2007  CD1 LEU A1024     8778   6860   7099   -178    447    -99       C  
ATOM   2008  CD2 LEU A1024      24.599  38.196  17.181  1.00 59.38           C  
ANISOU 2008  CD2 LEU A1024     8687   6834   7043    -17    443   -105       C  
ATOM   2009  N   SER A1025      22.312  42.261  19.756  1.00 64.21           N  
ANISOU 2009  N   SER A1025     9749   7275   7373    223    580    -67       N  
ATOM   2010  CA  SER A1025      21.292  42.818  20.634  1.00 69.55           C  
ANISOU 2010  CA  SER A1025    10498   7949   7979    335    613    -43       C  
ATOM   2011  C   SER A1025      19.957  42.941  19.910  1.00 71.17           C  
ANISOU 2011  C   SER A1025    10667   8253   8122    525    632     -1       C  
ATOM   2012  O   SER A1025      18.919  42.521  20.438  1.00 71.96           O  
ANISOU 2012  O   SER A1025    10668   8466   8207    605    612     22       O  
ATOM   2013  CB  SER A1025      21.747  44.182  21.163  1.00 69.06           C  
ANISOU 2013  CB  SER A1025    10685   7733   7824    313    692    -47       C  
ATOM   2014  OG  SER A1025      20.758  44.751  21.992  1.00 76.02           O  
ANISOU 2014  OG  SER A1025    11660   8598   8626    443    739    -17       O  
ATOM   2015  N   LYS A1026      19.971  43.483  18.686  1.00 67.48           N  
ANISOU 2015  N   LYS A1026    10263   7768   7608    593    668     13       N  
ATOM   2016  CA  LYS A1026      18.730  43.661  17.936  1.00 66.15           C  
ANISOU 2016  CA  LYS A1026    10049   7727   7358    783    689     64       C  
ATOM   2017  C   LYS A1026      18.104  42.331  17.556  1.00 65.23           C  
ANISOU 2017  C   LYS A1026     9686   7805   7295    753    612     60       C  
ATOM   2018  O   LYS A1026      16.891  42.261  17.341  1.00 68.76           O  
ANISOU 2018  O   LYS A1026    10042   8422   7662    883    614    105       O  
ATOM   2019  CB  LYS A1026      18.972  44.484  16.671  1.00 72.74           C  
ANISOU 2019  CB  LYS A1026    11003   8502   8132    856    746     80       C  
ATOM   2020  CG  LYS A1026      19.398  45.918  16.887  1.00 78.77           C  
ANISOU 2020  CG  LYS A1026    12057   9072   8801    903    848     89       C  
ATOM   2021  CD  LYS A1026      19.700  46.539  15.547  1.00 86.00           C  
ANISOU 2021  CD  LYS A1026    13072   9934   9669    955    897     99       C  
ATOM   2022  CE  LYS A1026      20.330  47.916  15.691  1.00 91.75           C  
ANISOU 2022  CE  LYS A1026    14123  10438  10299    949   1007     94       C  
ATOM   2023  NZ  LYS A1026      20.641  48.488  14.356  1.00 94.05           N  
ANISOU 2023  NZ  LYS A1026    14516  10675  10544    995   1056    102       N  
ATOM   2024  N   PHE A1027      18.911  41.285  17.418  1.00 63.50           N  
ANISOU 2024  N   PHE A1027     9367   7572   7188    584    552     13       N  
ATOM   2025  CA  PHE A1027      18.394  39.976  17.047  1.00 71.52           C  
ANISOU 2025  CA  PHE A1027    10195   8739   8241    527    495      1       C  
ATOM   2026  C   PHE A1027      17.932  39.171  18.258  1.00 72.51           C  
ANISOU 2026  C   PHE A1027    10230   8926   8394    475    459     -8       C  
ATOM   2027  O   PHE A1027      17.427  38.055  18.087  1.00 71.44           O  
ANISOU 2027  O   PHE A1027     9961   8912   8272    409    421    -22       O  
ATOM   2028  CB  PHE A1027      19.456  39.188  16.265  1.00 77.21           C  
ANISOU 2028  CB  PHE A1027    10880   9402   9052    390    467    -40       C  
ATOM   2029  CG  PHE A1027      19.499  39.503  14.789  1.00 81.75           C  
ANISOU 2029  CG  PHE A1027    11469   9996   9595    432    484    -32       C  
ATOM   2030  CD1 PHE A1027      19.321  40.790  14.322  1.00 85.95           C  
ANISOU 2030  CD1 PHE A1027    12120  10492  10045    562    537      1       C  
ATOM   2031  CD2 PHE A1027      19.745  38.506  13.872  1.00 86.00           C  
ANISOU 2031  CD2 PHE A1027    11921  10576  10177    344    456    -57       C  
ATOM   2032  CE1 PHE A1027      19.365  41.068  12.960  1.00 87.19           C  
ANISOU 2032  CE1 PHE A1027    12288  10669  10170    606    554     10       C  
ATOM   2033  CE2 PHE A1027      19.796  38.777  12.512  1.00 87.80           C  
ANISOU 2033  CE2 PHE A1027    12160  10825  10376    377    469    -51       C  
ATOM   2034  CZ  PHE A1027      19.603  40.063  12.057  1.00 86.53           C  
ANISOU 2034  CZ  PHE A1027    12097  10642  10140    509    514    -17       C  
ATOM   2035  N   GLY A1028      18.079  39.710  19.465  1.00 72.65           N  
ANISOU 2035  N   GLY A1028    10330   8863   8412    493    476     -3       N  
ATOM   2036  CA  GLY A1028      17.699  38.977  20.660  1.00 74.82           C  
ANISOU 2036  CA  GLY A1028    10526   9187   8717    445    444    -11       C  
ATOM   2037  C   GLY A1028      18.607  37.798  20.923  1.00 73.17           C  
ANISOU 2037  C   GLY A1028    10255   8931   8617    286    404    -53       C  
ATOM   2038  O   GLY A1028      18.130  36.728  21.323  1.00 71.01           O  
ANISOU 2038  O   GLY A1028     9879   8738   8364    231    374    -65       O  
ATOM   2039  N   MET A1029      19.904  37.959  20.670  1.00 72.61           N  
ANISOU 2039  N   MET A1029    10248   8740   8599    216    412    -71       N  
ATOM   2040  CA  MET A1029      20.880  36.902  20.859  1.00 70.07           C  
ANISOU 2040  CA  MET A1029     9874   8386   8364    100    389    -94       C  
ATOM   2041  C   MET A1029      21.987  37.419  21.758  1.00 67.67           C  
ANISOU 2041  C   MET A1029     9637   7993   8082     44    397    -95       C  
ATOM   2042  O   MET A1029      22.219  38.626  21.834  1.00 70.08           O  
ANISOU 2042  O   MET A1029    10057   8233   8337     63    427    -90       O  
ATOM   2043  CB  MET A1029      21.464  36.434  19.515  1.00 71.29           C  
ANISOU 2043  CB  MET A1029    10010   8532   8544     64    390   -104       C  
ATOM   2044  CG  MET A1029      20.421  36.210  18.420  1.00 75.15           C  
ANISOU 2044  CG  MET A1029    10451   9118   8985    107    388   -103       C  
ATOM   2045  SD  MET A1029      21.205  35.650  16.888  1.00 78.66           S  
ANISOU 2045  SD  MET A1029    10892   9535   9462     55    394   -119       S  
ATOM   2046  CE  MET A1029      21.916  34.106  17.467  1.00 70.63           C  
ANISOU 2046  CE  MET A1029     9841   8481   8516    -45    392   -134       C  
ATOM   2047  N   ASP A1030      22.651  36.498  22.451  1.00 63.74           N  
ANISOU 2047  N   ASP A1030     9078   7500   7641    -29    379    -99       N  
ATOM   2048  CA  ASP A1030      23.790  36.848  23.283  1.00 65.65           C  
ANISOU 2048  CA  ASP A1030     9348   7704   7890   -100    382    -93       C  
ATOM   2049  C   ASP A1030      25.003  37.128  22.404  1.00 68.53           C  
ANISOU 2049  C   ASP A1030     9737   8048   8255   -153    395    -90       C  
ATOM   2050  O   ASP A1030      25.032  36.788  21.223  1.00 73.19           O  
ANISOU 2050  O   ASP A1030    10308   8641   8860   -131    398    -92       O  
ATOM   2051  CB  ASP A1030      24.107  35.724  24.284  1.00 67.71           C  
ANISOU 2051  CB  ASP A1030     9523   8005   8198   -137    365    -85       C  
ATOM   2052  CG  ASP A1030      22.942  35.422  25.249  1.00 66.37           C  
ANISOU 2052  CG  ASP A1030     9329   7862   8027   -100    352    -90       C  
ATOM   2053  OD1 ASP A1030      22.141  36.322  25.577  1.00 66.87           O  
ANISOU 2053  OD1 ASP A1030     9448   7915   8044    -53    357    -91       O  
ATOM   2054  OD2 ASP A1030      22.834  34.263  25.678  1.00 67.76           O  
ANISOU 2054  OD2 ASP A1030     9439   8068   8239   -112    344    -87       O  
ATOM   2055  N   GLU A1031      26.011  37.758  22.994  1.00 71.68           N  
ANISOU 2055  N   GLU A1031    10174   8438   8624   -237    403    -86       N  
ATOM   2056  CA  GLU A1031      27.253  38.013  22.280  1.00 76.03           C  
ANISOU 2056  CA  GLU A1031    10729   9001   9157   -309    413    -78       C  
ATOM   2057  C   GLU A1031      27.999  36.706  22.039  1.00 74.50           C  
ANISOU 2057  C   GLU A1031    10408   8882   9015   -305    401    -51       C  
ATOM   2058  O   GLU A1031      28.013  35.814  22.888  1.00 77.53           O  
ANISOU 2058  O   GLU A1031    10718   9313   9428   -291    392    -33       O  
ATOM   2059  CB  GLU A1031      28.126  38.985  23.071  1.00 84.00           C  
ANISOU 2059  CB  GLU A1031    11805  10016  10094   -433    426    -80       C  
ATOM   2060  CG  GLU A1031      29.456  39.303  22.416  1.00 96.56           C  
ANISOU 2060  CG  GLU A1031    13389  11655  11643   -535    435    -70       C  
ATOM   2061  CD  GLU A1031      30.246  40.337  23.191  1.00109.12           C  
ANISOU 2061  CD  GLU A1031    15062  13267  13132   -698    453    -79       C  
ATOM   2062  OE1 GLU A1031      29.621  41.203  23.847  1.00110.54           O  
ANISOU 2062  OE1 GLU A1031    15383  13355  13261   -717    478   -105       O  
ATOM   2063  OE2 GLU A1031      31.494  40.271  23.153  1.00116.20           O  
ANISOU 2063  OE2 GLU A1031    15884  14282  13984   -812    447    -58       O  
ATOM   2064  N   GLY A1032      28.600  36.581  20.865  1.00 71.13           N  
ANISOU 2064  N   GLY A1032     9971   8461   8592   -303    411    -43       N  
ATOM   2065  CA  GLY A1032      29.301  35.354  20.530  1.00 69.00           C  
ANISOU 2065  CA  GLY A1032     9608   8251   8357   -273    418     -9       C  
ATOM   2066  C   GLY A1032      29.820  35.418  19.113  1.00 65.94           C  
ANISOU 2066  C   GLY A1032     9233   7855   7968   -265    432     -6       C  
ATOM   2067  O   GLY A1032      29.601  36.398  18.391  1.00 64.99           O  
ANISOU 2067  O   GLY A1032     9189   7682   7824   -285    434    -32       O  
ATOM   2068  N   VAL A1033      30.543  34.365  18.734  1.00 62.85           N  
ANISOU 2068  N   VAL A1033     8776   7512   7593   -224    452     33       N  
ATOM   2069  CA  VAL A1033      31.092  34.278  17.387  1.00 63.06           C  
ANISOU 2069  CA  VAL A1033     8809   7534   7618   -206    470     42       C  
ATOM   2070  C   VAL A1033      29.946  34.029  16.422  1.00 59.74           C  
ANISOU 2070  C   VAL A1033     8448   7019   7232   -160    473      1       C  
ATOM   2071  O   VAL A1033      29.207  33.050  16.550  1.00 62.69           O  
ANISOU 2071  O   VAL A1033     8824   7364   7630   -119    483     -7       O  
ATOM   2072  CB  VAL A1033      32.162  33.189  17.302  1.00 68.77           C  
ANISOU 2072  CB  VAL A1033     9458   8338   8332   -150    504    105       C  
ATOM   2073  CG1 VAL A1033      32.703  33.072  15.875  1.00 62.76           C  
ANISOU 2073  CG1 VAL A1033     8710   7568   7567   -122    527    117       C  
ATOM   2074  CG2 VAL A1033      33.278  33.547  18.274  1.00 73.87           C  
ANISOU 2074  CG2 VAL A1033    10017   9130   8919   -204    497    154       C  
ATOM   2075  N   THR A1034      29.767  34.934  15.476  1.00 58.36           N  
ANISOU 2075  N   THR A1034     8326   6806   7043   -177    467    -24       N  
ATOM   2076  CA  THR A1034      28.566  34.978  14.659  1.00 59.45           C  
ANISOU 2076  CA  THR A1034     8508   6890   7190   -139    464    -60       C  
ATOM   2077  C   THR A1034      28.884  34.469  13.259  1.00 57.10           C  
ANISOU 2077  C   THR A1034     8215   6578   6903   -118    484    -57       C  
ATOM   2078  O   THR A1034      29.834  34.933  12.620  1.00 57.70           O  
ANISOU 2078  O   THR A1034     8295   6661   6966   -136    492    -42       O  
ATOM   2079  CB  THR A1034      27.993  36.395  14.635  1.00 61.49           C  
ANISOU 2079  CB  THR A1034     8838   7116   7410   -144    454    -82       C  
ATOM   2080  OG1 THR A1034      27.627  36.765  15.973  1.00 61.31           O  
ANISOU 2080  OG1 THR A1034     8826   7097   7373   -158    444    -84       O  
ATOM   2081  CG2 THR A1034      26.759  36.470  13.756  1.00 60.08           C  
ANISOU 2081  CG2 THR A1034     8682   6925   7219    -85    453   -103       C  
ATOM   2082  N   PHE A1035      28.116  33.477  12.826  1.00 54.32           N  
ANISOU 2082  N   PHE A1035     7867   6210   6563    -96    496    -73       N  
ATOM   2083  CA  PHE A1035      28.206  32.849  11.518  1.00 57.50           C  
ANISOU 2083  CA  PHE A1035     8293   6589   6966    -85    521    -78       C  
ATOM   2084  C   PHE A1035      26.945  33.193  10.754  1.00 59.02           C  
ANISOU 2084  C   PHE A1035     8503   6790   7133    -90    505   -115       C  
ATOM   2085  O   PHE A1035      25.854  33.217  11.329  1.00 59.68           O  
ANISOU 2085  O   PHE A1035     8570   6907   7197    -94    486   -133       O  
ATOM   2086  CB  PHE A1035      28.329  31.321  11.627  1.00 56.94           C  
ANISOU 2086  CB  PHE A1035     8242   6494   6899    -75    566    -66       C  
ATOM   2087  CG  PHE A1035      29.573  30.862  12.326  1.00 57.35           C  
ANISOU 2087  CG  PHE A1035     8268   6565   6957    -34    595    -11       C  
ATOM   2088  CD1 PHE A1035      29.608  30.741  13.707  1.00 59.13           C  
ANISOU 2088  CD1 PHE A1035     8458   6822   7186    -30    587      7       C  
ATOM   2089  CD2 PHE A1035      30.710  30.555  11.600  1.00 55.44           C  
ANISOU 2089  CD2 PHE A1035     8029   6331   6705      9    634     31       C  
ATOM   2090  CE1 PHE A1035      30.761  30.307  14.341  1.00 62.02           C  
ANISOU 2090  CE1 PHE A1035     8783   7241   7540     18    616     69       C  
ATOM   2091  CE2 PHE A1035      31.858  30.129  12.227  1.00 55.82           C  
ANISOU 2091  CE2 PHE A1035     8033   6439   6736     67    665     97       C  
ATOM   2092  CZ  PHE A1035      31.887  29.998  13.595  1.00 58.21           C  
ANISOU 2092  CZ  PHE A1035     8293   6787   7036     72    657    118       C  
ATOM   2093  N   MET A1036      27.091  33.455   9.462  1.00 58.83           N  
ANISOU 2093  N   MET A1036     8499   6755   7099    -83    512   -122       N  
ATOM   2094  CA  MET A1036      25.965  33.875   8.651  1.00 58.01           C  
ANISOU 2094  CA  MET A1036     8397   6691   6955    -75    498   -146       C  
ATOM   2095  C   MET A1036      25.899  33.020   7.397  1.00 57.42           C  
ANISOU 2095  C   MET A1036     8339   6611   6865   -105    523   -161       C  
ATOM   2096  O   MET A1036      26.921  32.740   6.770  1.00 58.97           O  
ANISOU 2096  O   MET A1036     8564   6756   7086   -101    548   -148       O  
ATOM   2097  CB  MET A1036      26.076  35.352   8.289  1.00 61.77           C  
ANISOU 2097  CB  MET A1036     8898   7160   7411    -31    488   -138       C  
ATOM   2098  CG  MET A1036      24.989  35.857   7.371  1.00 69.08           C  
ANISOU 2098  CG  MET A1036     9821   8145   8280     12    483   -147       C  
ATOM   2099  SD  MET A1036      25.420  37.528   6.878  1.00 76.94           S  
ANISOU 2099  SD  MET A1036    10897   9090   9247     76    498   -131       S  
ATOM   2100  CE  MET A1036      24.203  37.841   5.601  1.00 81.32           C  
ANISOU 2100  CE  MET A1036    11431   9740   9726    150    501   -127       C  
ATOM   2101  N   PHE A1037      24.702  32.588   7.057  1.00 56.27           N  
ANISOU 2101  N   PHE A1037     8177   6534   6668   -143    518   -187       N  
ATOM   2102  CA  PHE A1037      24.409  32.024   5.756  1.00 57.63           C  
ANISOU 2102  CA  PHE A1037     8370   6727   6801   -191    537   -208       C  
ATOM   2103  C   PHE A1037      23.315  32.870   5.130  1.00 61.06           C  
ANISOU 2103  C   PHE A1037     8748   7284   7168   -167    507   -212       C  
ATOM   2104  O   PHE A1037      22.378  33.294   5.816  1.00 63.47           O  
ANISOU 2104  O   PHE A1037     9000   7683   7433   -142    482   -205       O  
ATOM   2105  CB  PHE A1037      23.972  30.565   5.869  1.00 55.71           C  
ANISOU 2105  CB  PHE A1037     8169   6477   6520   -291    572   -235       C  
ATOM   2106  CG  PHE A1037      23.430  30.005   4.602  1.00 57.90           C  
ANISOU 2106  CG  PHE A1037     8475   6797   6726   -376    592   -266       C  
ATOM   2107  CD1 PHE A1037      22.080  30.086   4.313  1.00 59.78           C  
ANISOU 2107  CD1 PHE A1037     8647   7195   6872   -444    566   -288       C  
ATOM   2108  CD2 PHE A1037      24.271  29.395   3.688  1.00 63.38           C  
ANISOU 2108  CD2 PHE A1037     9257   7392   7432   -390    642   -269       C  
ATOM   2109  CE1 PHE A1037      21.577  29.568   3.137  1.00 62.45           C  
ANISOU 2109  CE1 PHE A1037     9003   7598   7126   -547    584   -317       C  
ATOM   2110  CE2 PHE A1037      23.781  28.876   2.507  1.00 63.98           C  
ANISOU 2110  CE2 PHE A1037     9373   7503   7434   -484    665   -301       C  
ATOM   2111  CZ  PHE A1037      22.433  28.958   2.229  1.00 64.15           C  
ANISOU 2111  CZ  PHE A1037     9325   7689   7359   -575    635   -328       C  
ATOM   2112  N   ILE A1038      23.440  33.119   3.834  1.00 61.87           N  
ANISOU 2112  N   ILE A1038     8861   7397   7251   -160    514   -214       N  
ATOM   2113  CA  ILE A1038      22.418  33.841   3.094  1.00 62.42           C  
ANISOU 2113  CA  ILE A1038     8873   7606   7239   -122    495   -208       C  
ATOM   2114  C   ILE A1038      22.296  33.194   1.724  1.00 64.96           C  
ANISOU 2114  C   ILE A1038     9202   7964   7516   -199    511   -231       C  
ATOM   2115  O   ILE A1038      23.283  33.084   0.990  1.00 68.34           O  
ANISOU 2115  O   ILE A1038     9691   8283   7993   -197    533   -234       O  
ATOM   2116  CB  ILE A1038      22.744  35.346   2.994  1.00 61.37           C  
ANISOU 2116  CB  ILE A1038     8758   7442   7119      8    490   -175       C  
ATOM   2117  CG1 ILE A1038      21.675  36.089   2.186  1.00 66.07           C  
ANISOU 2117  CG1 ILE A1038     9302   8191   7613     83    485   -153       C  
ATOM   2118  CG2 ILE A1038      24.155  35.575   2.428  1.00 58.99           C  
ANISOU 2118  CG2 ILE A1038     8526   6998   6888     14    508   -173       C  
ATOM   2119  CD1 ILE A1038      21.887  37.596   2.122  1.00 68.95           C  
ANISOU 2119  CD1 ILE A1038     9725   8508   7965    227    501   -116       C  
ATOM   2120  N   GLY A1039      21.094  32.757   1.385  1.00 65.07           N  
ANISOU 2120  N   GLY A1039     9153   8147   7424   -276    502   -246       N  
ATOM   2121  CA  GLY A1039      20.874  32.135   0.097  1.00 68.73           C  
ANISOU 2121  CA  GLY A1039     9626   8667   7822   -376    519   -272       C  
ATOM   2122  C   GLY A1039      19.598  31.333   0.088  1.00 72.82           C  
ANISOU 2122  C   GLY A1039    10083   9375   8209   -524    514   -298       C  
ATOM   2123  O   GLY A1039      18.951  31.118   1.115  1.00 75.44           O  
ANISOU 2123  O   GLY A1039    10373   9781   8512   -555    500   -298       O  
ATOM   2124  N   ARG A1040      19.241  30.888  -1.109  1.00 75.22           N  
ANISOU 2124  N   ARG A1040    10384   9772   8423   -633    527   -322       N  
ATOM   2125  CA  ARG A1040      18.039  30.086  -1.264  1.00 80.83           C  
ANISOU 2125  CA  ARG A1040    11041  10694   8979   -820    526   -352       C  
ATOM   2126  C   ARG A1040      18.189  28.765  -0.515  1.00 74.50           C  
ANISOU 2126  C   ARG A1040    10361   9764   8179   -982    570   -401       C  
ATOM   2127  O   ARG A1040      19.275  28.180  -0.458  1.00 69.97           O  
ANISOU 2127  O   ARG A1040     9941   8945   7700   -979    619   -418       O  
ATOM   2128  CB  ARG A1040      17.750  29.833  -2.747  1.00 89.42           C  
ANISOU 2128  CB  ARG A1040    12119  11894   9962   -928    538   -373       C  
ATOM   2129  CG  ARG A1040      16.401  29.173  -3.022  1.00 99.83           C  
ANISOU 2129  CG  ARG A1040    13350  13501  11080  -1143    532   -399       C  
ATOM   2130  CD  ARG A1040      16.068  29.153  -4.507  1.00107.93           C  
ANISOU 2130  CD  ARG A1040    14336  14684  11990  -1233    535   -409       C  
ATOM   2131  NE  ARG A1040      17.016  28.356  -5.285  1.00114.45           N  
ANISOU 2131  NE  ARG A1040    15352  15270  12865  -1333    594   -460       N  
ATOM   2132  CZ  ARG A1040      18.008  28.866  -6.011  1.00118.64           C  
ANISOU 2132  CZ  ARG A1040    15938  15632  13506  -1193    603   -443       C  
ATOM   2133  NH1 ARG A1040      18.189  30.180  -6.057  1.00120.76           N  
ANISOU 2133  NH1 ARG A1040    16102  15934  13846   -962    560   -383       N  
ATOM   2134  NH2 ARG A1040      18.823  28.063  -6.687  1.00117.68           N  
ANISOU 2134  NH2 ARG A1040    15992  15307  13414  -1282    663   -484       N  
ATOM   2135  N   PHE A1041      17.087  28.311   0.078  1.00 73.45           N  
ANISOU 2135  N   PHE A1041    10163   9813   7932  -1112    557   -416       N  
ATOM   2136  CA  PHE A1041      17.027  27.002   0.722  1.00 74.60           C  
ANISOU 2136  CA  PHE A1041    10440   9863   8042  -1297    608   -467       C  
ATOM   2137  C   PHE A1041      16.707  25.958  -0.340  1.00 79.18           C  
ANISOU 2137  C   PHE A1041    11123  10481   8480  -1544    662   -526       C  
ATOM   2138  O   PHE A1041      15.589  25.923  -0.865  1.00 81.10           O  
ANISOU 2138  O   PHE A1041    11252  11006   8555  -1694    637   -539       O  
ATOM   2139  CB  PHE A1041      15.970  26.985   1.822  1.00 74.14           C  
ANISOU 2139  CB  PHE A1041    10270   9989   7909  -1347    574   -461       C  
ATOM   2140  CG  PHE A1041      16.315  27.826   3.013  1.00 74.02           C  
ANISOU 2140  CG  PHE A1041    10199   9900   8027  -1133    537   -412       C  
ATOM   2141  CD1 PHE A1041      17.551  28.429   3.107  1.00 72.50           C  
ANISOU 2141  CD1 PHE A1041    10066   9482   7996   -946    541   -385       C  
ATOM   2142  CD2 PHE A1041      15.411  28.000   4.043  1.00 75.89           C  
ANISOU 2142  CD2 PHE A1041    10325  10300   8211  -1133    502   -395       C  
ATOM   2143  CE1 PHE A1041      17.881  29.196   4.189  1.00 71.43           C  
ANISOU 2143  CE1 PHE A1041     9893   9283   7964   -781    512   -346       C  
ATOM   2144  CE2 PHE A1041      15.741  28.765   5.143  1.00 76.47           C  
ANISOU 2144  CE2 PHE A1041    10365  10292   8399   -945    475   -354       C  
ATOM   2145  CZ  PHE A1041      16.982  29.365   5.211  1.00 74.38           C  
ANISOU 2145  CZ  PHE A1041    10172   9798   8290   -778    481   -332       C  
ATOM   2146  N   ASP A1042      17.678  25.110  -0.664  1.00 80.81           N  
ANISOU 2146  N   ASP A1042    11548  10420   8736  -1588    742   -558       N  
ATOM   2147  CA  ASP A1042      17.455  24.063  -1.653  1.00 84.08           C  
ANISOU 2147  CA  ASP A1042    12112  10826   9008  -1831    813   -619       C  
ATOM   2148  C   ASP A1042      18.295  22.843  -1.298  1.00 83.82           C  
ANISOU 2148  C   ASP A1042    12364  10481   9002  -1886    926   -650       C  
ATOM   2149  O   ASP A1042      19.111  22.869  -0.376  1.00 81.66           O  
ANISOU 2149  O   ASP A1042    12142  10022   8864  -1717    942   -617       O  
ATOM   2150  CB  ASP A1042      17.776  24.559  -3.068  1.00 82.14           C  
ANISOU 2150  CB  ASP A1042    11836  10611   8763  -1786    802   -610       C  
ATOM   2151  CG  ASP A1042      19.151  25.177  -3.167  1.00 83.77           C  
ANISOU 2151  CG  ASP A1042    12081  10586   9162  -1529    804   -565       C  
ATOM   2152  OD1 ASP A1042      20.133  24.505  -2.792  1.00 83.80           O  
ANISOU 2152  OD1 ASP A1042    12267  10329   9244  -1485    876   -567       O  
ATOM   2153  OD2 ASP A1042      19.254  26.336  -3.626  1.00 84.83           O  
ANISOU 2153  OD2 ASP A1042    12066  10812   9355  -1370    740   -522       O  
ATOM   2154  N   ARG A1043      18.102  21.768  -2.053  1.00 88.78           N  
ANISOU 2154  N   ARG A1043    13189  11058   9486  -2122   1015   -711       N  
ATOM   2155  CA  ARG A1043      18.886  20.548  -1.883  1.00 88.50           C  
ANISOU 2155  CA  ARG A1043    13472  10711   9443  -2167   1151   -736       C  
ATOM   2156  C   ARG A1043      19.741  20.350  -3.125  1.00 85.94           C  
ANISOU 2156  C   ARG A1043    13295  10228   9132  -2128   1216   -738       C  
ATOM   2157  O   ARG A1043      19.229  19.990  -4.186  1.00 94.50           O  
ANISOU 2157  O   ARG A1043    14441  11396  10071  -2339   1244   -788       O  
ATOM   2158  CB  ARG A1043      17.987  19.341  -1.619  1.00 90.17           C  
ANISOU 2158  CB  ARG A1043    13863  10945   9454  -2486   1232   -810       C  
ATOM   2159  CG  ARG A1043      17.407  19.307  -0.218  1.00 89.04           C  
ANISOU 2159  CG  ARG A1043    13638  10878   9314  -2500   1197   -804       C  
ATOM   2160  CD  ARG A1043      16.675  18.008   0.038  1.00 92.25           C  
ANISOU 2160  CD  ARG A1043    14274  11260   9516  -2826   1300   -880       C  
ATOM   2161  NE  ARG A1043      16.152  17.930   1.399  1.00 93.14           N  
ANISOU 2161  NE  ARG A1043    14321  11435   9634  -2839   1271   -875       N  
ATOM   2162  CZ  ARG A1043      14.885  18.163   1.729  1.00 95.67           C  
ANISOU 2162  CZ  ARG A1043    14441  12073   9834  -3016   1192   -896       C  
ATOM   2163  NH1 ARG A1043      14.000  18.490   0.794  1.00 96.64           N  
ANISOU 2163  NH1 ARG A1043    14402  12503   9812  -3193   1134   -917       N  
ATOM   2164  NH2 ARG A1043      14.503  18.068   2.994  1.00 95.98           N  
ANISOU 2164  NH2 ARG A1043    14436  12144   9888  -3010   1173   -888       N  
ATOM   2165  N   GLY A1044      21.040  20.599  -2.993  1.00 79.02           N  
ANISOU 2165  N   GLY A1044    12465   9142   8418  -1865   1239   -680       N  
ATOM   2166  CA  GLY A1044      21.991  20.315  -4.046  1.00 76.24           C  
ANISOU 2166  CA  GLY A1044    12273   8613   8082  -1799   1316   -671       C  
ATOM   2167  C   GLY A1044      22.532  21.526  -4.774  1.00 80.63           C  
ANISOU 2167  C   GLY A1044    12630   9245   8762  -1611   1225   -624       C  
ATOM   2168  O   GLY A1044      23.367  21.354  -5.672  1.00 83.95           O  
ANISOU 2168  O   GLY A1044    13166   9529   9202  -1544   1283   -612       O  
ATOM   2169  N   GLN A1045      22.078  22.741  -4.448  1.00 80.12           N  
ANISOU 2169  N   GLN A1045    12287   9386   8768  -1524   1095   -597       N  
ATOM   2170  CA  GLN A1045      22.627  23.939  -5.077  1.00 80.80           C  
ANISOU 2170  CA  GLN A1045    12213   9523   8966  -1341   1021   -552       C  
ATOM   2171  C   GLN A1045      23.338  24.850  -4.081  1.00 74.28           C  
ANISOU 2171  C   GLN A1045    11262   8660   8301  -1105    962   -489       C  
ATOM   2172  O   GLN A1045      24.568  24.951  -4.123  1.00 77.96           O  
ANISOU 2172  O   GLN A1045    11782   8972   8867   -946    992   -447       O  
ATOM   2173  CB  GLN A1045      21.502  24.685  -5.813  1.00 90.61           C  
ANISOU 2173  CB  GLN A1045    13264  11042  10121  -1436    935   -570       C  
ATOM   2174  CG  GLN A1045      20.860  23.884  -6.956  1.00102.90           C  
ANISOU 2174  CG  GLN A1045    14924  12669  11503  -1686    987   -631       C  
ATOM   2175  CD  GLN A1045      19.589  24.524  -7.503  1.00112.84           C  
ANISOU 2175  CD  GLN A1045    15965  14267  12640  -1795    903   -640       C  
ATOM   2176  OE1 GLN A1045      18.968  25.362  -6.845  1.00117.87           O  
ANISOU 2176  OE1 GLN A1045    16398  15093  13294  -1707    820   -605       O  
ATOM   2177  NE2 GLN A1045      19.194  24.125  -8.712  1.00115.13           N  
ANISOU 2177  NE2 GLN A1045    16303  14650  12793  -1979    931   -681       N  
ATOM   2178  N   LYS A1046      22.621  25.437  -3.121  1.00 65.64           N  
ANISOU 2178  N   LYS A1046    10014   7706   7220  -1089    888   -480       N  
ATOM   2179  CA  LYS A1046      23.226  26.392  -2.201  1.00 70.13           C  
ANISOU 2179  CA  LYS A1046    10471   8251   7925   -889    833   -426       C  
ATOM   2180  C   LYS A1046      23.758  25.762  -0.921  1.00 71.12           C  
ANISOU 2180  C   LYS A1046    10682   8241   8101   -843    876   -409       C  
ATOM   2181  O   LYS A1046      24.586  26.384  -0.246  1.00 69.49           O  
ANISOU 2181  O   LYS A1046    10418   7982   8004   -683    850   -361       O  
ATOM   2182  CB  LYS A1046      22.224  27.492  -1.826  1.00 74.22           C  
ANISOU 2182  CB  LYS A1046    10788   8984   8428   -861    738   -414       C  
ATOM   2183  CG  LYS A1046      21.888  28.426  -2.967  1.00 77.16           C  
ANISOU 2183  CG  LYS A1046    11053   9494   8770   -826    692   -405       C  
ATOM   2184  CD  LYS A1046      23.148  28.962  -3.602  1.00 77.62           C  
ANISOU 2184  CD  LYS A1046    11150   9410   8932   -688    702   -376       C  
ATOM   2185  CE  LYS A1046      22.836  29.762  -4.847  1.00 80.40           C  
ANISOU 2185  CE  LYS A1046    11425   9881   9245   -663    670   -370       C  
ATOM   2186  NZ  LYS A1046      24.094  30.180  -5.527  1.00 83.18           N  
ANISOU 2186  NZ  LYS A1046    11829  10088   9689   -553    687   -347       N  
ATOM   2187  N   GLY A1047      23.291  24.569  -0.565  1.00 70.22           N  
ANISOU 2187  N   GLY A1047    10705   8078   7897   -988    944   -446       N  
ATOM   2188  CA  GLY A1047      23.888  23.821   0.519  1.00 67.07           C  
ANISOU 2188  CA  GLY A1047    10425   7527   7532   -932   1008   -425       C  
ATOM   2189  C   GLY A1047      23.403  24.150   1.910  1.00 63.57           C  
ANISOU 2189  C   GLY A1047     9871   7160   7124   -908    952   -414       C  
ATOM   2190  O   GLY A1047      24.145  23.918   2.865  1.00 65.23           O  
ANISOU 2190  O   GLY A1047    10122   7264   7399   -796    982   -376       O  
ATOM   2191  N   VAL A1048      22.186  24.680   2.067  1.00 59.84           N  
ANISOU 2191  N   VAL A1048     9253   6883   6599   -999    875   -440       N  
ATOM   2192  CA  VAL A1048      21.696  24.937   3.419  1.00 61.77           C  
ANISOU 2192  CA  VAL A1048     9405   7196   6869   -975    830   -429       C  
ATOM   2193  C   VAL A1048      21.418  23.624   4.144  1.00 67.47           C  
ANISOU 2193  C   VAL A1048    10287   7830   7518  -1102    909   -460       C  
ATOM   2194  O   VAL A1048      21.435  23.589   5.380  1.00 63.78           O  
ANISOU 2194  O   VAL A1048     9797   7341   7095  -1049    899   -442       O  
ATOM   2195  CB  VAL A1048      20.448  25.849   3.417  1.00 58.96           C  
ANISOU 2195  CB  VAL A1048     8852   7090   6460  -1012    737   -435       C  
ATOM   2196  CG1 VAL A1048      19.166  25.042   3.146  1.00 62.12           C  
ANISOU 2196  CG1 VAL A1048     9270   7641   6690  -1252    754   -490       C  
ATOM   2197  CG2 VAL A1048      20.340  26.604   4.739  1.00 60.22           C  
ANISOU 2197  CG2 VAL A1048     8896   7292   6694   -892    678   -400       C  
ATOM   2198  N   ASP A1049      21.182  22.538   3.393  1.00 67.06           N  
ANISOU 2198  N   ASP A1049    10417   7715   7347  -1275    996   -508       N  
ATOM   2199  CA  ASP A1049      21.011  21.214   3.986  1.00 65.26           C  
ANISOU 2199  CA  ASP A1049    10403   7362   7031  -1403   1099   -540       C  
ATOM   2200  C   ASP A1049      22.294  20.755   4.659  1.00 64.79           C  
ANISOU 2200  C   ASP A1049    10481   7075   7061  -1214   1179   -486       C  
ATOM   2201  O   ASP A1049      22.267  20.191   5.759  1.00 68.65           O  
ANISOU 2201  O   ASP A1049    11045   7496   7545  -1207   1220   -478       O  
ATOM   2202  CB  ASP A1049      20.573  20.214   2.910  1.00 69.55           C  
ANISOU 2202  CB  ASP A1049    11148   7869   7410  -1638   1191   -604       C  
ATOM   2203  CG  ASP A1049      21.486  20.226   1.670  1.00 76.47           C  
ANISOU 2203  CG  ASP A1049    12116   8627   8313  -1557   1238   -589       C  
ATOM   2204  OD1 ASP A1049      21.947  21.305   1.233  1.00 78.94           O  
ANISOU 2204  OD1 ASP A1049    12252   9007   8736  -1398   1155   -548       O  
ATOM   2205  OD2 ASP A1049      21.751  19.142   1.130  1.00 80.97           O  
ANISOU 2205  OD2 ASP A1049    12955   9025   8785  -1655   1366   -617       O  
ATOM   2206  N   VAL A1050      23.433  21.030   4.028  1.00 65.32           N  
ANISOU 2206  N   VAL A1050    10567   7047   7205  -1049   1199   -439       N  
ATOM   2207  CA  VAL A1050      24.719  20.724   4.639  1.00 68.48           C  
ANISOU 2207  CA  VAL A1050    11050   7290   7680   -841   1267   -369       C  
ATOM   2208  C   VAL A1050      24.904  21.536   5.913  1.00 69.26           C  
ANISOU 2208  C   VAL A1050    10955   7472   7889   -710   1178   -325       C  
ATOM   2209  O   VAL A1050      25.350  21.012   6.941  1.00 69.02           O  
ANISOU 2209  O   VAL A1050    10992   7361   7872   -624   1230   -287       O  
ATOM   2210  CB  VAL A1050      25.849  20.970   3.620  1.00 67.85           C  
ANISOU 2210  CB  VAL A1050    10991   7143   7646   -700   1294   -325       C  
ATOM   2211  CG1 VAL A1050      27.193  20.638   4.224  1.00 66.89           C  
ANISOU 2211  CG1 VAL A1050    10933   6908   7575   -477   1368   -237       C  
ATOM   2212  CG2 VAL A1050      25.596  20.159   2.371  1.00 57.09           C  
ANISOU 2212  CG2 VAL A1050     9834   5694   6165   -843   1386   -373       C  
ATOM   2213  N   LEU A1051      24.527  22.820   5.879  1.00 67.65           N  
ANISOU 2213  N   LEU A1051    10522   7430   7751   -695   1050   -327       N  
ATOM   2214  CA  LEU A1051      24.686  23.671   7.053  1.00 63.22           C  
ANISOU 2214  CA  LEU A1051     9797   6941   7284   -586    970   -290       C  
ATOM   2215  C   LEU A1051      23.779  23.231   8.196  1.00 64.42           C  
ANISOU 2215  C   LEU A1051     9954   7128   7396   -675    966   -316       C  
ATOM   2216  O   LEU A1051      24.210  23.207   9.353  1.00 62.67           O  
ANISOU 2216  O   LEU A1051     9711   6874   7226   -581    967   -279       O  
ATOM   2217  CB  LEU A1051      24.410  25.125   6.689  1.00 62.47           C  
ANISOU 2217  CB  LEU A1051     9506   6989   7242   -554    857   -289       C  
ATOM   2218  CG  LEU A1051      24.355  26.071   7.897  1.00 61.17           C  
ANISOU 2218  CG  LEU A1051     9196   6899   7148   -473    780   -262       C  
ATOM   2219  CD1 LEU A1051      25.692  26.106   8.615  1.00 59.32           C  
ANISOU 2219  CD1 LEU A1051     8966   6586   6988   -333    803   -202       C  
ATOM   2220  CD2 LEU A1051      23.958  27.465   7.449  1.00 59.70           C  
ANISOU 2220  CD2 LEU A1051     8867   6832   6984   -443    693   -263       C  
ATOM   2221  N   LEU A1052      22.521  22.885   7.899  1.00 65.93           N  
ANISOU 2221  N   LEU A1052    10164   7403   7485   -865    960   -378       N  
ATOM   2222  CA  LEU A1052      21.615  22.441   8.955  1.00 68.72           C  
ANISOU 2222  CA  LEU A1052    10519   7806   7786   -968    956   -405       C  
ATOM   2223  C   LEU A1052      22.083  21.122   9.557  1.00 69.14           C  
ANISOU 2223  C   LEU A1052    10798   7672   7800   -975   1079   -400       C  
ATOM   2224  O   LEU A1052      22.026  20.941  10.780  1.00 66.04           O  
ANISOU 2224  O   LEU A1052    10396   7265   7432   -938   1080   -383       O  
ATOM   2225  CB  LEU A1052      20.187  22.322   8.424  1.00 71.95           C  
ANISOU 2225  CB  LEU A1052    10890   8384   8066  -1188    928   -467       C  
ATOM   2226  CG  LEU A1052      19.576  23.612   7.849  1.00 72.20           C  
ANISOU 2226  CG  LEU A1052    10696   8629   8106  -1161    817   -461       C  
ATOM   2227  CD1 LEU A1052      18.162  23.373   7.319  1.00 70.26           C  
ANISOU 2227  CD1 LEU A1052    10398   8596   7700  -1382    798   -511       C  
ATOM   2228  CD2 LEU A1052      19.577  24.745   8.882  1.00 71.96           C  
ANISOU 2228  CD2 LEU A1052    10489   8675   8177  -1001    730   -416       C  
ATOM   2229  N   LYS A1053      22.580  20.198   8.722  1.00 70.99           N  
ANISOU 2229  N   LYS A1053    11252   7755   7969  -1005   1194   -408       N  
ATOM   2230  CA  LYS A1053      23.130  18.963   9.274  1.00 74.27           C  
ANISOU 2230  CA  LYS A1053    11914   7970   8334   -967   1334   -388       C  
ATOM   2231  C   LYS A1053      24.366  19.239  10.127  1.00 71.81           C  
ANISOU 2231  C   LYS A1053    11543   7605   8138   -705   1338   -297       C  
ATOM   2232  O   LYS A1053      24.527  18.649  11.202  1.00 71.97           O  
ANISOU 2232  O   LYS A1053    11642   7554   8148   -649   1394   -270       O  
ATOM   2233  CB  LYS A1053      23.457  17.981   8.150  1.00 78.68           C  
ANISOU 2233  CB  LYS A1053    12742   8366   8786  -1030   1470   -407       C  
ATOM   2234  CG  LYS A1053      23.589  16.547   8.605  1.00 82.23           C  
ANISOU 2234  CG  LYS A1053    13515   8607   9123  -1063   1641   -409       C  
ATOM   2235  CD  LYS A1053      22.272  16.050   9.164  1.00 87.96           C  
ANISOU 2235  CD  LYS A1053    14296   9386   9739  -1321   1642   -486       C  
ATOM   2236  CE  LYS A1053      22.280  14.543   9.379  1.00 94.02           C  
ANISOU 2236  CE  LYS A1053    15450   9919  10352  -1409   1836   -507       C  
ATOM   2237  NZ  LYS A1053      22.353  13.812   8.078  1.00 98.95           N  
ANISOU 2237  NZ  LYS A1053    16344  10408  10844  -1536   1959   -547       N  
ATOM   2238  N   ALA A1054      25.248  20.135   9.673  1.00 68.22           N  
ANISOU 2238  N   ALA A1054    10945   7198   7779   -552   1280   -247       N  
ATOM   2239  CA  ALA A1054      26.417  20.479  10.475  1.00 70.78           C  
ANISOU 2239  CA  ALA A1054    11181   7522   8189   -332   1274   -159       C  
ATOM   2240  C   ALA A1054      26.016  21.138  11.792  1.00 75.34           C  
ANISOU 2240  C   ALA A1054    11584   8209   8832   -324   1178   -155       C  
ATOM   2241  O   ALA A1054      26.689  20.942  12.810  1.00 81.40           O  
ANISOU 2241  O   ALA A1054    12343   8960   9627   -194   1205    -95       O  
ATOM   2242  CB  ALA A1054      27.352  21.391   9.682  1.00 71.20           C  
ANISOU 2242  CB  ALA A1054    11107   7633   8315   -214   1223   -116       C  
ATOM   2243  N   ILE A1055      24.925  21.911  11.793  1.00 70.42           N  
ANISOU 2243  N   ILE A1055    10822   7711   8222   -451   1071   -213       N  
ATOM   2244  CA  ILE A1055      24.436  22.518  13.030  1.00 69.01           C  
ANISOU 2244  CA  ILE A1055    10498   7630   8092   -448    988   -212       C  
ATOM   2245  C   ILE A1055      23.909  21.449  13.982  1.00 73.57           C  
ANISOU 2245  C   ILE A1055    11201   8143   8607   -515   1055   -228       C  
ATOM   2246  O   ILE A1055      24.190  21.481  15.185  1.00 73.39           O  
ANISOU 2246  O   ILE A1055    11133   8125   8627   -431   1046   -192       O  
ATOM   2247  CB  ILE A1055      23.368  23.582  12.722  1.00 66.53           C  
ANISOU 2247  CB  ILE A1055    10023   7472   7785   -540    875   -257       C  
ATOM   2248  CG1 ILE A1055      24.035  24.844  12.167  1.00 68.81           C  
ANISOU 2248  CG1 ILE A1055    10181   7815   8150   -435    807   -226       C  
ATOM   2249  CG2 ILE A1055      22.551  23.910  13.977  1.00 62.36           C  
ANISOU 2249  CG2 ILE A1055     9394   7034   7267   -569    815   -267       C  
ATOM   2250  CD1 ILE A1055      23.062  25.916  11.745  1.00 72.96           C  
ANISOU 2250  CD1 ILE A1055    10575   8481   8667   -486    718   -256       C  
ATOM   2251  N   GLU A1056      23.134  20.491  13.469  1.00 75.92           N  
ANISOU 2251  N   GLU A1056    11667   8385   8793   -682   1126   -286       N  
ATOM   2252  CA  GLU A1056      22.708  19.390  14.324  1.00 76.42           C  
ANISOU 2252  CA  GLU A1056    11894   8363   8781   -758   1210   -304       C  
ATOM   2253  C   GLU A1056      23.916  18.674  14.907  1.00 75.35           C  
ANISOU 2253  C   GLU A1056    11896   8073   8658   -568   1320   -229       C  
ATOM   2254  O   GLU A1056      23.951  18.373  16.106  1.00 73.03           O  
ANISOU 2254  O   GLU A1056    11612   7760   8375   -514   1338   -203       O  
ATOM   2255  CB  GLU A1056      21.817  18.416  13.551  1.00 79.94           C  
ANISOU 2255  CB  GLU A1056    12540   8758   9076   -993   1290   -380       C  
ATOM   2256  CG  GLU A1056      20.494  19.025  13.127  1.00 85.49           C  
ANISOU 2256  CG  GLU A1056    13084   9667   9732  -1191   1185   -445       C  
ATOM   2257  CD  GLU A1056      19.488  17.998  12.643  1.00 94.12           C  
ANISOU 2257  CD  GLU A1056    14360  10754  10647  -1471   1261   -524       C  
ATOM   2258  OE1 GLU A1056      18.290  18.155  12.966  1.00 97.55           O  
ANISOU 2258  OE1 GLU A1056    14683  11369  11013  -1643   1196   -568       O  
ATOM   2259  OE2 GLU A1056      19.887  17.040  11.948  1.00 96.12           O  
ANISOU 2259  OE2 GLU A1056    14873  10833  10814  -1527   1390   -540       O  
ATOM   2260  N   ILE A1057      24.945  18.451  14.091  1.00 74.57           N  
ANISOU 2260  N   ILE A1057    11890   7886   8558   -445   1392   -182       N  
ATOM   2261  CA  ILE A1057      26.139  17.778  14.594  1.00 74.21           C  
ANISOU 2261  CA  ILE A1057    11964   7730   8505   -230   1506    -91       C  
ATOM   2262  C   ILE A1057      26.780  18.599  15.703  1.00 73.27           C  
ANISOU 2262  C   ILE A1057    11614   7735   8490    -71   1418    -23       C  
ATOM   2263  O   ILE A1057      27.130  18.077  16.764  1.00 74.97           O  
ANISOU 2263  O   ILE A1057    11876   7918   8691     34   1475     29       O  
ATOM   2264  CB  ILE A1057      27.134  17.512  13.454  1.00 74.86           C  
ANISOU 2264  CB  ILE A1057    12155   7730   8560   -112   1591    -44       C  
ATOM   2265  CG1 ILE A1057      26.557  16.519  12.456  1.00 78.36           C  
ANISOU 2265  CG1 ILE A1057    12881   8018   8874   -274   1708   -110       C  
ATOM   2266  CG2 ILE A1057      28.434  16.981  14.011  1.00 74.38           C  
ANISOU 2266  CG2 ILE A1057    12163   7615   8484    151   1699     73       C  
ATOM   2267  CD1 ILE A1057      27.430  16.333  11.242  1.00 77.93           C  
ANISOU 2267  CD1 ILE A1057    12932   7885   8792   -171   1786    -72       C  
ATOM   2268  N   LEU A1058      26.940  19.901  15.478  1.00 74.47           N  
ANISOU 2268  N   LEU A1058    11526   8032   8736    -60   1284    -22       N  
ATOM   2269  CA  LEU A1058      27.591  20.755  16.465  1.00 71.26           C  
ANISOU 2269  CA  LEU A1058    10915   7748   8412     60   1204     37       C  
ATOM   2270  C   LEU A1058      26.755  20.932  17.727  1.00 72.29           C  
ANISOU 2270  C   LEU A1058    10973   7930   8566    -11   1143      6       C  
ATOM   2271  O   LEU A1058      27.309  21.280  18.774  1.00 71.49           O  
ANISOU 2271  O   LEU A1058    10759   7899   8505     89   1113     60       O  
ATOM   2272  CB  LEU A1058      27.901  22.130  15.856  1.00 64.55           C  
ANISOU 2272  CB  LEU A1058     9870   7019   7637     60   1089     34       C  
ATOM   2273  CG  LEU A1058      28.963  22.177  14.757  1.00 63.45           C  
ANISOU 2273  CG  LEU A1058     9751   6868   7490    157   1130     81       C  
ATOM   2274  CD1 LEU A1058      28.970  23.538  14.110  1.00 58.12           C  
ANISOU 2274  CD1 LEU A1058     8912   6294   6877    110   1017     56       C  
ATOM   2275  CD2 LEU A1058      30.339  21.817  15.309  1.00 66.42           C  
ANISOU 2275  CD2 LEU A1058    10112   7277   7847    354   1198    192       C  
ATOM   2276  N   SER A1059      25.439  20.725  17.650  1.00 72.90           N  
ANISOU 2276  N   SER A1059    11099   7992   8606   -188   1124    -76       N  
ATOM   2277  CA  SER A1059      24.579  21.001  18.794  1.00 72.71           C  
ANISOU 2277  CA  SER A1059    10986   8038   8602   -257   1057   -105       C  
ATOM   2278  C   SER A1059      24.896  20.110  19.984  1.00 80.46           C  
ANISOU 2278  C   SER A1059    12062   8949   9559   -179   1137    -62       C  
ATOM   2279  O   SER A1059      24.535  20.458  21.112  1.00 84.15           O  
ANISOU 2279  O   SER A1059    12426   9484  10062   -184   1077    -62       O  
ATOM   2280  CB  SER A1059      23.110  20.843  18.402  1.00 69.60           C  
ANISOU 2280  CB  SER A1059    10624   7676   8146   -466   1031   -193       C  
ATOM   2281  OG  SER A1059      22.757  19.485  18.199  1.00 70.50           O  
ANISOU 2281  OG  SER A1059    10975   7662   8150   -568   1153   -224       O  
ATOM   2282  N   SER A1060      25.570  18.985  19.768  1.00 83.85           N  
ANISOU 2282  N   SER A1060    12696   9243   9920    -92   1277    -19       N  
ATOM   2283  CA  SER A1060      25.916  18.095  20.865  1.00 86.67           C  
ANISOU 2283  CA  SER A1060    13164   9527  10237     11   1372     33       C  
ATOM   2284  C   SER A1060      27.230  18.462  21.541  1.00 85.83           C  
ANISOU 2284  C   SER A1060    12925   9508  10178    236   1366    142       C  
ATOM   2285  O   SER A1060      27.561  17.865  22.570  1.00 89.31           O  
ANISOU 2285  O   SER A1060    13414   9928  10590    344   1431    198       O  
ATOM   2286  CB  SER A1060      25.983  16.647  20.370  1.00 88.57           C  
ANISOU 2286  CB  SER A1060    13730   9570  10354     14   1553     36       C  
ATOM   2287  OG  SER A1060      26.919  16.513  19.316  1.00 89.01           O  
ANISOU 2287  OG  SER A1060    13856   9578  10388    132   1620     84       O  
ATOM   2288  N   LYS A1061      27.986  19.412  20.997  1.00 82.18           N  
ANISOU 2288  N   LYS A1061    12296   9156   9774    300   1293    174       N  
ATOM   2289  CA  LYS A1061      29.249  19.827  21.592  1.00 81.92           C  
ANISOU 2289  CA  LYS A1061    12113   9251   9763    478   1280    277       C  
ATOM   2290  C   LYS A1061      29.058  21.109  22.389  1.00 84.16           C  
ANISOU 2290  C   LYS A1061    12159   9687  10130    411   1132    256       C  
ATOM   2291  O   LYS A1061      28.111  21.868  22.172  1.00 87.10           O  
ANISOU 2291  O   LYS A1061    12470  10073  10551    261   1036    173       O  
ATOM   2292  CB  LYS A1061      30.321  20.024  20.518  1.00 82.37           C  
ANISOU 2292  CB  LYS A1061    12146   9345   9806    583   1308    334       C  
ATOM   2293  CG  LYS A1061      30.482  18.822  19.611  1.00 86.57           C  
ANISOU 2293  CG  LYS A1061    12935   9710  10248    649   1462    351       C  
ATOM   2294  CD  LYS A1061      31.575  19.020  18.570  1.00 90.45           C  
ANISOU 2294  CD  LYS A1061    13395  10249  10722    769   1492    415       C  
ATOM   2295  CE  LYS A1061      31.753  17.741  17.754  1.00 95.68           C  
ANISOU 2295  CE  LYS A1061    14349  10726  11280    854   1667    440       C  
ATOM   2296  NZ  LYS A1061      32.853  17.808  16.750  1.00 98.79           N  
ANISOU 2296  NZ  LYS A1061    14730  11162  11643    999   1714    515       N  
ATOM   2297  N   LYS A1062      29.965  21.340  23.340  1.00 84.53           N  
ANISOU 2297  N   LYS A1062    12081   9861  10177    529   1122    339       N  
ATOM   2298  CA  LYS A1062      29.827  22.526  24.179  1.00 84.32           C  
ANISOU 2298  CA  LYS A1062    11860   9966  10212    455    996    319       C  
ATOM   2299  C   LYS A1062      30.219  23.794  23.427  1.00 81.53           C  
ANISOU 2299  C   LYS A1062    11376   9706   9896    397    907    303       C  
ATOM   2300  O   LYS A1062      29.694  24.876  23.725  1.00 80.80           O  
ANISOU 2300  O   LYS A1062    11189   9659   9852    288    806    249       O  
ATOM   2301  CB  LYS A1062      30.648  22.375  25.462  1.00 86.54           C  
ANISOU 2301  CB  LYS A1062    12048  10371  10464    571   1013    408       C  
ATOM   2302  CG  LYS A1062      32.150  22.334  25.249  1.00 89.53           C  
ANISOU 2302  CG  LYS A1062    12343  10893  10783    726   1059    522       C  
ATOM   2303  CD  LYS A1062      32.898  22.355  26.576  1.00 91.11           C  
ANISOU 2303  CD  LYS A1062    12408  11270  10942    817   1057    610       C  
ATOM   2304  CE  LYS A1062      34.403  22.369  26.354  1.00 95.24           C  
ANISOU 2304  CE  LYS A1062    12811  11995  11380    964   1098    734       C  
ATOM   2305  NZ  LYS A1062      34.863  21.259  25.450  1.00 97.59           N  
ANISOU 2305  NZ  LYS A1062    13266  12204  11610   1142   1237    800       N  
ATOM   2306  N   GLU A1063      31.115  23.687  22.440  1.00 80.27           N  
ANISOU 2306  N   GLU A1063    11227   9566   9706    473    951    350       N  
ATOM   2307  CA  GLU A1063      31.465  24.859  21.646  1.00 76.09           C  
ANISOU 2307  CA  GLU A1063    10595   9111   9206    408    874    330       C  
ATOM   2308  C   GLU A1063      30.257  25.463  20.953  1.00 70.20           C  
ANISOU 2308  C   GLU A1063     9888   8274   8510    266    811    225       C  
ATOM   2309  O   GLU A1063      30.256  26.667  20.675  1.00 73.09           O  
ANISOU 2309  O   GLU A1063    10169   8696   8905    194    732    196       O  
ATOM   2310  CB  GLU A1063      32.525  24.508  20.611  1.00 77.78           C  
ANISOU 2310  CB  GLU A1063    10828   9350   9373    514    941    395       C  
ATOM   2311  CG  GLU A1063      33.871  24.175  21.202  1.00 81.70           C  
ANISOU 2311  CG  GLU A1063    11234  10009   9799    668    993    518       C  
ATOM   2312  CD  GLU A1063      33.998  22.710  21.571  1.00 86.07           C  
ANISOU 2312  CD  GLU A1063    11927  10487  10289    833   1125    585       C  
ATOM   2313  OE1 GLU A1063      32.997  21.970  21.429  1.00 88.01           O  
ANISOU 2313  OE1 GLU A1063    12353  10540  10548    793   1172    522       O  
ATOM   2314  OE2 GLU A1063      35.104  22.300  21.991  1.00 86.72           O  
ANISOU 2314  OE2 GLU A1063    11945  10714  10292   1001   1189    704       O  
ATOM   2315  N   PHE A1064      29.223  24.660  20.702  1.00 66.06           N  
ANISOU 2315  N   PHE A1064     9496   7623   7980    223    849    173       N  
ATOM   2316  CA  PHE A1064      27.997  25.168  20.098  1.00 69.09           C  
ANISOU 2316  CA  PHE A1064     9896   7966   8389     94    791     84       C  
ATOM   2317  C   PHE A1064      27.431  26.350  20.878  1.00 73.24           C  
ANISOU 2317  C   PHE A1064    10306   8568   8955     30    692     52       C  
ATOM   2318  O   PHE A1064      26.834  27.257  20.284  1.00 74.20           O  
ANISOU 2318  O   PHE A1064    10396   8704   9092    -33    633      7       O  
ATOM   2319  CB  PHE A1064      26.979  24.031  20.018  1.00 67.90           C  
ANISOU 2319  CB  PHE A1064     9891   7710   8197     33    851     39       C  
ATOM   2320  CG  PHE A1064      25.722  24.369  19.272  1.00 66.79           C  
ANISOU 2320  CG  PHE A1064     9760   7567   8050   -102    804    -42       C  
ATOM   2321  CD1 PHE A1064      25.741  24.568  17.892  1.00 63.43           C  
ANISOU 2321  CD1 PHE A1064     9361   7126   7613   -131    806    -64       C  
ATOM   2322  CD2 PHE A1064      24.508  24.438  19.948  1.00 61.42           C  
ANISOU 2322  CD2 PHE A1064     9056   6920   7362   -194    762    -90       C  
ATOM   2323  CE1 PHE A1064      24.571  24.853  17.207  1.00 63.40           C  
ANISOU 2323  CE1 PHE A1064     9350   7155   7585   -249    765   -128       C  
ATOM   2324  CE2 PHE A1064      23.338  24.733  19.274  1.00 63.17           C  
ANISOU 2324  CE2 PHE A1064     9263   7187   7553   -307    721   -150       C  
ATOM   2325  CZ  PHE A1064      23.367  24.946  17.902  1.00 65.28           C  
ANISOU 2325  CZ  PHE A1064     9547   7453   7803   -334    722   -168       C  
ATOM   2326  N   GLN A1065      27.636  26.379  22.200  1.00 73.39           N  
ANISOU 2326  N   GLN A1065    10271   8635   8981     57    679     82       N  
ATOM   2327  CA  GLN A1065      27.091  27.466  23.005  1.00 74.73           C  
ANISOU 2327  CA  GLN A1065    10357   8859   9176     -1    598     53       C  
ATOM   2328  C   GLN A1065      27.855  28.769  22.819  1.00 68.11           C  
ANISOU 2328  C   GLN A1065     9441   8093   8346    -14    549     67       C  
ATOM   2329  O   GLN A1065      27.304  29.837  23.094  1.00 64.25           O  
ANISOU 2329  O   GLN A1065     8928   7618   7866    -68    493     32       O  
ATOM   2330  CB  GLN A1065      27.073  27.067  24.483  1.00 83.06           C  
ANISOU 2330  CB  GLN A1065    11386   9941  10231     21    603     77       C  
ATOM   2331  CG  GLN A1065      26.024  26.010  24.814  1.00 91.23           C  
ANISOU 2331  CG  GLN A1065    12509  10903  11253     -4    640     45       C  
ATOM   2332  CD  GLN A1065      24.617  26.444  24.415  1.00 98.74           C  
ANISOU 2332  CD  GLN A1065    13466  11847  12205   -100    591    -27       C  
ATOM   2333  OE1 GLN A1065      24.200  27.573  24.679  1.00102.71           O  
ANISOU 2333  OE1 GLN A1065    13897  12403  12725   -124    524    -46       O  
ATOM   2334  NE2 GLN A1065      23.884  25.547  23.764  1.00101.36           N  
ANISOU 2334  NE2 GLN A1065    13891  12124  12498   -156    635    -63       N  
ATOM   2335  N   GLU A1066      29.103  28.703  22.362  1.00 68.72           N  
ANISOU 2335  N   GLU A1066     9490   8218   8403     32    577    119       N  
ATOM   2336  CA  GLU A1066      29.870  29.895  22.028  1.00 68.73           C  
ANISOU 2336  CA  GLU A1066     9432   8291   8392     -9    539    128       C  
ATOM   2337  C   GLU A1066      29.517  30.465  20.658  1.00 66.64           C  
ANISOU 2337  C   GLU A1066     9214   7967   8139    -41    525     85       C  
ATOM   2338  O   GLU A1066      30.029  31.533  20.299  1.00 64.02           O  
ANISOU 2338  O   GLU A1066     8861   7673   7792    -87    498     83       O  
ATOM   2339  CB  GLU A1066      31.366  29.584  22.072  1.00 72.85           C  
ANISOU 2339  CB  GLU A1066     9882   8928   8868     49    574    210       C  
ATOM   2340  CG  GLU A1066      31.888  29.364  23.453  1.00 80.13           C  
ANISOU 2340  CG  GLU A1066    10727   9961   9760     71    577    263       C  
ATOM   2341  CD  GLU A1066      33.361  29.049  23.467  1.00 91.51           C  
ANISOU 2341  CD  GLU A1066    12072  11566  11131    142    615    359       C  
ATOM   2342  OE1 GLU A1066      33.824  28.317  22.577  1.00 95.73           O  
ANISOU 2342  OE1 GLU A1066    12638  12087  11649    241    674    400       O  
ATOM   2343  OE2 GLU A1066      34.060  29.532  24.378  1.00 98.82           O  
ANISOU 2343  OE2 GLU A1066    12891  12652  12005     99    590    398       O  
ATOM   2344  N   MET A1067      28.664  29.787  19.894  1.00 67.88           N  
ANISOU 2344  N   MET A1067     9441   8041   8309    -29    548     51       N  
ATOM   2345  CA  MET A1067      28.393  30.140  18.507  1.00 64.13           C  
ANISOU 2345  CA  MET A1067     9004   7526   7836    -48    543     20       C  
ATOM   2346  C   MET A1067      27.002  30.746  18.367  1.00 62.23           C  
ANISOU 2346  C   MET A1067     8783   7265   7598    -93    503    -38       C  
ATOM   2347  O   MET A1067      26.083  30.433  19.133  1.00 62.73           O  
ANISOU 2347  O   MET A1067     8846   7328   7660   -108    493    -57       O  
ATOM   2348  CB  MET A1067      28.508  28.912  17.591  1.00 62.74           C  
ANISOU 2348  CB  MET A1067     8899   7292   7649    -10    608     28       C  
ATOM   2349  CG  MET A1067      29.819  28.132  17.709  1.00 64.89           C  
ANISOU 2349  CG  MET A1067     9167   7590   7899     79    670    102       C  
ATOM   2350  SD  MET A1067      29.725  26.615  16.734  1.00 71.40           S  
ANISOU 2350  SD  MET A1067    10136   8301   8690    128    771    106       S  
ATOM   2351  CE  MET A1067      31.329  25.864  17.031  1.00 72.08           C  
ANISOU 2351  CE  MET A1067    10211   8445   8731    285    855    218       C  
ATOM   2352  N   ARG A1068      26.863  31.621  17.373  1.00 61.62           N  
ANISOU 2352  N   ARG A1068     8717   7182   7513   -104    483    -58       N  
ATOM   2353  CA  ARG A1068      25.593  32.206  16.968  1.00 60.19           C  
ANISOU 2353  CA  ARG A1068     8549   7009   7314   -115    457    -96       C  
ATOM   2354  C   ARG A1068      25.440  32.009  15.466  1.00 63.38           C  
ANISOU 2354  C   ARG A1068     8979   7400   7703   -118    472   -112       C  
ATOM   2355  O   ARG A1068      26.399  32.181  14.712  1.00 62.74           O  
ANISOU 2355  O   ARG A1068     8909   7296   7631   -107    486    -96       O  
ATOM   2356  CB  ARG A1068      25.527  33.705  17.300  1.00 56.54           C  
ANISOU 2356  CB  ARG A1068     8095   6555   6835   -106    429    -97       C  
ATOM   2357  CG  ARG A1068      26.052  34.058  18.669  1.00 58.20           C  
ANISOU 2357  CG  ARG A1068     8291   6772   7048   -124    419    -80       C  
ATOM   2358  CD  ARG A1068      25.099  33.616  19.759  1.00 58.68           C  
ANISOU 2358  CD  ARG A1068     8331   6853   7113   -117    407    -89       C  
ATOM   2359  NE  ARG A1068      25.706  33.823  21.071  1.00 61.19           N  
ANISOU 2359  NE  ARG A1068     8632   7183   7436   -140    400    -70       N  
ATOM   2360  CZ  ARG A1068      26.119  32.839  21.859  1.00 59.73           C  
ANISOU 2360  CZ  ARG A1068     8404   7018   7271   -141    410    -48       C  
ATOM   2361  NH1 ARG A1068      25.969  31.578  21.483  1.00 57.00           N  
ANISOU 2361  NH1 ARG A1068     8058   6660   6941   -121    437    -46       N  
ATOM   2362  NH2 ARG A1068      26.669  33.113  23.027  1.00 60.87           N  
ANISOU 2362  NH2 ARG A1068     8523   7197   7410   -165    401    -28       N  
ATOM   2363  N   PHE A1069      24.234  31.674  15.028  1.00 61.77           N  
ANISOU 2363  N   PHE A1069     8775   7229   7465   -141    467   -141       N  
ATOM   2364  CA  PHE A1069      23.989  31.372  13.627  1.00 60.51           C  
ANISOU 2364  CA  PHE A1069     8637   7074   7278   -163    483   -159       C  
ATOM   2365  C   PHE A1069      22.846  32.230  13.120  1.00 60.52           C  
ANISOU 2365  C   PHE A1069     8604   7163   7228   -148    452   -172       C  
ATOM   2366  O   PHE A1069      21.789  32.301  13.754  1.00 61.89           O  
ANISOU 2366  O   PHE A1069     8738   7416   7363   -151    432   -178       O  
ATOM   2367  CB  PHE A1069      23.663  29.886  13.433  1.00 59.45           C  
ANISOU 2367  CB  PHE A1069     8549   6922   7119   -231    524   -179       C  
ATOM   2368  CG  PHE A1069      24.827  28.966  13.695  1.00 61.81           C  
ANISOU 2368  CG  PHE A1069     8907   7129   7447   -208    578   -152       C  
ATOM   2369  CD1 PHE A1069      25.016  28.401  14.952  1.00 63.77           C  
ANISOU 2369  CD1 PHE A1069     9161   7358   7709   -195    595   -134       C  
ATOM   2370  CD2 PHE A1069      25.730  28.668  12.691  1.00 60.15           C  
ANISOU 2370  CD2 PHE A1069     8745   6866   7242   -184    618   -136       C  
ATOM   2371  CE1 PHE A1069      26.077  27.546  15.192  1.00 62.29           C  
ANISOU 2371  CE1 PHE A1069     9028   7108   7531   -143    656    -94       C  
ATOM   2372  CE2 PHE A1069      26.801  27.823  12.929  1.00 61.66           C  
ANISOU 2372  CE2 PHE A1069     8990   6996   7442   -130    680    -95       C  
ATOM   2373  CZ  PHE A1069      26.973  27.265  14.186  1.00 61.42           C  
ANISOU 2373  CZ  PHE A1069     8965   6957   7417   -102    701    -70       C  
ATOM   2374  N   ILE A1070      23.061  32.875  11.982  1.00 60.55           N  
ANISOU 2374  N   ILE A1070     8620   7166   7221   -120    453   -170       N  
ATOM   2375  CA  ILE A1070      22.046  33.683  11.328  1.00 63.42           C  
ANISOU 2375  CA  ILE A1070     8954   7625   7519    -78    436   -169       C  
ATOM   2376  C   ILE A1070      21.856  33.095   9.944  1.00 60.06           C  
ANISOU 2376  C   ILE A1070     8526   7234   7059   -127    449   -188       C  
ATOM   2377  O   ILE A1070      22.755  33.171   9.105  1.00 63.77           O  
ANISOU 2377  O   ILE A1070     9038   7631   7562   -121    465   -186       O  
ATOM   2378  CB  ILE A1070      22.438  35.161  11.258  1.00 65.96           C  
ANISOU 2378  CB  ILE A1070     9314   7907   7840     12    435   -146       C  
ATOM   2379  CG1 ILE A1070      22.624  35.713  12.674  1.00 67.04           C  
ANISOU 2379  CG1 ILE A1070     9472   8004   7996     36    430   -134       C  
ATOM   2380  CG2 ILE A1070      21.384  35.953  10.512  1.00 64.51           C  
ANISOU 2380  CG2 ILE A1070     9112   7827   7573     90    434   -132       C  
ATOM   2381  CD1 ILE A1070      23.082  37.167  12.697  1.00 70.24           C  
ANISOU 2381  CD1 ILE A1070     9962   8344   8382     95    446   -117       C  
ATOM   2382  N   ILE A1071      20.714  32.466   9.721  1.00 59.29           N  
ANISOU 2382  N   ILE A1071     8382   7259   6886   -191    444   -205       N  
ATOM   2383  CA  ILE A1071      20.421  31.730   8.502  1.00 63.14           C  
ANISOU 2383  CA  ILE A1071     8875   7796   7320   -280    461   -231       C  
ATOM   2384  C   ILE A1071      19.328  32.504   7.784  1.00 65.37           C  
ANISOU 2384  C   ILE A1071     9072   8262   7505   -237    437   -215       C  
ATOM   2385  O   ILE A1071      18.205  32.617   8.289  1.00 69.70           O  
ANISOU 2385  O   ILE A1071     9539   8970   7974   -234    416   -204       O  
ATOM   2386  CB  ILE A1071      19.985  30.289   8.805  1.00 66.06           C  
ANISOU 2386  CB  ILE A1071     9274   8178   7648   -425    485   -267       C  
ATOM   2387  CG1 ILE A1071      21.001  29.625   9.730  1.00 68.73           C  
ANISOU 2387  CG1 ILE A1071     9695   8349   8071   -421    517   -264       C  
ATOM   2388  CG2 ILE A1071      19.829  29.489   7.524  1.00 66.10           C  
ANISOU 2388  CG2 ILE A1071     9324   8204   7586   -542    517   -299       C  
ATOM   2389  CD1 ILE A1071      20.547  28.274  10.254  1.00 72.59           C  
ANISOU 2389  CD1 ILE A1071    10243   8825   8511   -547    555   -295       C  
ATOM   2390  N   ILE A1072      19.652  33.060   6.623  1.00 62.24           N  
ANISOU 2390  N   ILE A1072     8688   7858   7103   -189    442   -206       N  
ATOM   2391  CA  ILE A1072      18.747  33.941   5.906  1.00 62.62           C  
ANISOU 2391  CA  ILE A1072     8660   8077   7054   -106    429   -176       C  
ATOM   2392  C   ILE A1072      18.451  33.330   4.550  1.00 60.25           C  
ANISOU 2392  C   ILE A1072     8336   7871   6685   -206    436   -198       C  
ATOM   2393  O   ILE A1072      19.372  33.060   3.775  1.00 60.62           O  
ANISOU 2393  O   ILE A1072     8458   7785   6789   -238    456   -218       O  
ATOM   2394  CB  ILE A1072      19.339  35.354   5.756  1.00 65.30           C  
ANISOU 2394  CB  ILE A1072     9053   8328   7432     56    438   -139       C  
ATOM   2395  CG1 ILE A1072      19.709  35.902   7.137  1.00 64.24           C  
ANISOU 2395  CG1 ILE A1072     8965   8087   7355    119    438   -125       C  
ATOM   2396  CG2 ILE A1072      18.349  36.285   5.046  1.00 65.39           C  
ANISOU 2396  CG2 ILE A1072     9001   8519   7325    179    440    -94       C  
ATOM   2397  CD1 ILE A1072      20.515  37.142   7.084  1.00 66.24           C  
ANISOU 2397  CD1 ILE A1072     9315   8211   7643    222    460   -103       C  
ATOM   2398  N   GLY A1073      17.176  33.131   4.257  1.00 60.98           N  
ANISOU 2398  N   GLY A1073     8320   8209   6642   -257    421   -192       N  
ATOM   2399  CA  GLY A1073      16.793  32.677   2.940  1.00 68.20           C  
ANISOU 2399  CA  GLY A1073     9199   9250   7463   -360    426   -210       C  
ATOM   2400  C   GLY A1073      15.390  32.126   2.931  1.00 77.53           C  
ANISOU 2400  C   GLY A1073    10255  10725   8478   -486    409   -213       C  
ATOM   2401  O   GLY A1073      14.699  32.083   3.948  1.00 79.01           O  
ANISOU 2401  O   GLY A1073    10378  11019   8624   -486    393   -199       O  
ATOM   2402  N   LYS A1074      14.975  31.724   1.734  1.00 83.35           N  
ANISOU 2402  N   LYS A1074    10952  11612   9106   -604    414   -230       N  
ATOM   2403  CA  LYS A1074      13.684  31.108   1.498  1.00 87.44           C  
ANISOU 2403  CA  LYS A1074    11345  12447   9433   -777    400   -239       C  
ATOM   2404  C   LYS A1074      13.876  29.953   0.529  1.00 84.56           C  
ANISOU 2404  C   LYS A1074    11069  12046   9015  -1025    432   -309       C  
ATOM   2405  O   LYS A1074      14.956  29.759  -0.041  1.00 78.02           O  
ANISOU 2405  O   LYS A1074    10382  10965   8296  -1019    463   -337       O  
ATOM   2406  CB  LYS A1074      12.676  32.116   0.931  1.00 94.02           C  
ANISOU 2406  CB  LYS A1074    11991  13614  10119   -635    374   -162       C  
ATOM   2407  CG  LYS A1074      12.377  33.300   1.833  1.00101.98           C  
ANISOU 2407  CG  LYS A1074    12935  14667  11145   -371    362    -83       C  
ATOM   2408  CD  LYS A1074      11.453  34.303   1.145  1.00109.89           C  
ANISOU 2408  CD  LYS A1074    13776  15990  11986   -191    358      7       C  
ATOM   2409  CE  LYS A1074      10.105  33.679   0.791  1.00115.56           C  
ANISOU 2409  CE  LYS A1074    14296  17140  12472   -359    335     20       C  
ATOM   2410  NZ  LYS A1074       9.229  34.608   0.007  1.00117.70           N  
ANISOU 2410  NZ  LYS A1074    14392  17764  12563   -171    336    121       N  
ATOM   2411  N   GLY A1075      12.801  29.209   0.311  1.00 88.50           N  
ANISOU 2411  N   GLY A1075    11487  12813   9326  -1250    429   -334       N  
ATOM   2412  CA  GLY A1075      12.827  28.167  -0.689  1.00 92.33           C  
ANISOU 2412  CA  GLY A1075    12065  13297   9718  -1509    467   -401       C  
ATOM   2413  C   GLY A1075      12.124  26.908  -0.245  1.00 93.88           C  
ANISOU 2413  C   GLY A1075    12308  13588   9774  -1815    493   -464       C  
ATOM   2414  O   GLY A1075      10.923  26.924   0.036  1.00 93.78           O  
ANISOU 2414  O   GLY A1075    12123  13917   9591  -1909    460   -444       O  
ATOM   2415  N   ASP A1076      12.871  25.815  -0.189  1.00 93.92           N  
ANISOU 2415  N   ASP A1076    12555  13297   9834  -1968    562   -534       N  
ATOM   2416  CA  ASP A1076      12.328  24.510   0.150  1.00 92.60           C  
ANISOU 2416  CA  ASP A1076    12503  13156   9524  -2283    613   -605       C  
ATOM   2417  C   ASP A1076      11.571  24.560   1.473  1.00 89.45           C  
ANISOU 2417  C   ASP A1076    11994  12902   9092  -2283    578   -585       C  
ATOM   2418  O   ASP A1076      12.186  24.800   2.523  1.00 87.43           O  
ANISOU 2418  O   ASP A1076    11786  12428   9005  -2100    575   -563       O  
ATOM   2419  CB  ASP A1076      13.459  23.491   0.219  1.00 93.69           C  
ANISOU 2419  CB  ASP A1076    12954  12882   9762  -2345    709   -662       C  
ATOM   2420  CG  ASP A1076      12.961  22.068   0.189  1.00 98.21           C  
ANISOU 2420  CG  ASP A1076    13716  13449  10152  -2704    792   -745       C  
ATOM   2421  OD1 ASP A1076      12.102  21.712   1.027  1.00101.20           O  
ANISOU 2421  OD1 ASP A1076    14042  13985  10424  -2849    782   -760       O  
ATOM   2422  OD2 ASP A1076      13.429  21.305  -0.683  1.00 98.71           O  
ANISOU 2422  OD2 ASP A1076    13995  13343  10167  -2846    875   -796       O  
ATOM   2423  N   PRO A1077      10.255  24.332   1.472  1.00 88.03           N  
ANISOU 2423  N   PRO A1077    11659  13101   8689  -2491    551   -590       N  
ATOM   2424  CA  PRO A1077       9.496  24.418   2.728  1.00 86.89           C  
ANISOU 2424  CA  PRO A1077    11392  13118   8505  -2482    516   -565       C  
ATOM   2425  C   PRO A1077       9.894  23.364   3.739  1.00 89.30           C  
ANISOU 2425  C   PRO A1077    11924  13139   8867  -2613    579   -626       C  
ATOM   2426  O   PRO A1077       9.751  23.591   4.947  1.00 88.50           O  
ANISOU 2426  O   PRO A1077    11768  13025   8834  -2502    553   -598       O  
ATOM   2427  CB  PRO A1077       8.043  24.244   2.269  1.00 87.81           C  
ANISOU 2427  CB  PRO A1077    11301  13731   8330  -2726    485   -562       C  
ATOM   2428  CG  PRO A1077       8.143  23.472   1.000  1.00 89.23           C  
ANISOU 2428  CG  PRO A1077    11613  13903   8386  -2996    537   -630       C  
ATOM   2429  CD  PRO A1077       9.406  23.945   0.333  1.00 87.81           C  
ANISOU 2429  CD  PRO A1077    11556  13389   8418  -2761    555   -619       C  
ATOM   2430  N   GLU A1078      10.395  22.216   3.293  1.00 91.71           N  
ANISOU 2430  N   GLU A1078    12499  13208   9139  -2833    671   -705       N  
ATOM   2431  CA  GLU A1078      10.896  21.242   4.253  1.00 93.71           C  
ANISOU 2431  CA  GLU A1078    13000  13153   9453  -2907    748   -752       C  
ATOM   2432  C   GLU A1078      12.160  21.755   4.931  1.00 84.89           C  
ANISOU 2432  C   GLU A1078    11948  11699   8606  -2570    747   -706       C  
ATOM   2433  O   GLU A1078      12.310  21.631   6.152  1.00 84.08           O  
ANISOU 2433  O   GLU A1078    11877  11483   8586  -2494    751   -695       O  
ATOM   2434  CB  GLU A1078      11.141  19.899   3.566  1.00100.52           C  
ANISOU 2434  CB  GLU A1078    14172  13828  10192  -3205    869   -840       C  
ATOM   2435  CG  GLU A1078      11.334  18.743   4.533  1.00105.76           C  
ANISOU 2435  CG  GLU A1078    15106  14240  10839  -3343    969   -891       C  
ATOM   2436  CD  GLU A1078      11.459  17.413   3.828  1.00113.55           C  
ANISOU 2436  CD  GLU A1078    16434  15047  11663  -3653   1108   -978       C  
ATOM   2437  OE1 GLU A1078      11.622  17.405   2.588  1.00115.66           O  
ANISOU 2437  OE1 GLU A1078    16744  15330  11872  -3725   1128   -997       O  
ATOM   2438  OE2 GLU A1078      11.392  16.376   4.517  1.00116.79           O  
ANISOU 2438  OE2 GLU A1078    17088  15293  11996  -3826   1206  -1027       O  
ATOM   2439  N   LEU A1079      13.071  22.354   4.158  1.00 81.71           N  
ANISOU 2439  N   LEU A1079    11557  11155   8332  -2375    741   -677       N  
ATOM   2440  CA  LEU A1079      14.274  22.935   4.746  1.00 78.55           C  
ANISOU 2440  CA  LEU A1079    11193  10486   8167  -2072    734   -628       C  
ATOM   2441  C   LEU A1079      13.951  24.161   5.587  1.00 78.42           C  
ANISOU 2441  C   LEU A1079    10943  10620   8234  -1851    638   -562       C  
ATOM   2442  O   LEU A1079      14.612  24.396   6.606  1.00 77.28           O  
ANISOU 2442  O   LEU A1079    10829  10297   8236  -1682    635   -535       O  
ATOM   2443  CB  LEU A1079      15.283  23.289   3.655  1.00 78.15           C  
ANISOU 2443  CB  LEU A1079    11204  10279   8211  -1944    750   -614       C  
ATOM   2444  CG  LEU A1079      15.744  22.121   2.774  1.00 80.83           C  
ANISOU 2444  CG  LEU A1079    11803  10433   8477  -2126    858   -673       C  
ATOM   2445  CD1 LEU A1079      16.732  22.595   1.723  1.00 78.68           C  
ANISOU 2445  CD1 LEU A1079    11560  10031   8304  -1972    864   -649       C  
ATOM   2446  CD2 LEU A1079      16.348  21.001   3.608  1.00 80.19           C  
ANISOU 2446  CD2 LEU A1079    11979  10067   8422  -2164    961   -697       C  
ATOM   2447  N   GLU A1080      12.939  24.944   5.191  1.00 80.64           N  
ANISOU 2447  N   GLU A1080    10998  11235   8408  -1842    569   -529       N  
ATOM   2448  CA  GLU A1080      12.480  26.041   6.041  1.00 82.33           C  
ANISOU 2448  CA  GLU A1080    11016  11603   8663  -1636    497   -462       C  
ATOM   2449  C   GLU A1080      11.959  25.514   7.372  1.00 84.03           C  
ANISOU 2449  C   GLU A1080    11232  11846   8850  -1720    498   -476       C  
ATOM   2450  O   GLU A1080      12.261  26.078   8.430  1.00 82.14           O  
ANISOU 2450  O   GLU A1080    10964  11512   8734  -1533    473   -438       O  
ATOM   2451  CB  GLU A1080      11.396  26.862   5.335  1.00 85.36           C  
ANISOU 2451  CB  GLU A1080    11167  12371   8897  -1606    441   -414       C  
ATOM   2452  CG  GLU A1080      11.911  27.798   4.242  1.00 89.01           C  
ANISOU 2452  CG  GLU A1080    11593  12811   9415  -1426    427   -375       C  
ATOM   2453  CD  GLU A1080      10.823  28.695   3.669  1.00 92.61           C  
ANISOU 2453  CD  GLU A1080    11815  13659   9716  -1342    380   -308       C  
ATOM   2454  OE1 GLU A1080      10.770  28.860   2.435  1.00 94.20           O  
ANISOU 2454  OE1 GLU A1080    11979  13966   9846  -1366    381   -304       O  
ATOM   2455  OE2 GLU A1080      10.019  29.237   4.455  1.00 96.17           O  
ANISOU 2455  OE2 GLU A1080    12116  14320  10106  -1238    346   -253       O  
ATOM   2456  N   GLY A1081      11.175  24.429   7.339  1.00 82.05           N  
ANISOU 2456  N   GLY A1081    11025  11724   8427  -2015    531   -532       N  
ATOM   2457  CA  GLY A1081      10.688  23.848   8.579  1.00 76.05           C  
ANISOU 2457  CA  GLY A1081    10284  10981   7631  -2116    539   -550       C  
ATOM   2458  C   GLY A1081      11.810  23.305   9.441  1.00 74.49           C  
ANISOU 2458  C   GLY A1081    10304  10395   7604  -2042    597   -570       C  
ATOM   2459  O   GLY A1081      11.804  23.474  10.659  1.00 74.79           O  
ANISOU 2459  O   GLY A1081    10311  10390   7716  -1943    577   -547       O  
ATOM   2460  N   TRP A1082      12.807  22.676   8.816  1.00 75.01           N  
ANISOU 2460  N   TRP A1082    10587  10187   7727  -2070    671   -603       N  
ATOM   2461  CA  TRP A1082      13.963  22.175   9.558  1.00 74.40           C  
ANISOU 2461  CA  TRP A1082    10709   9763   7798  -1964    734   -604       C  
ATOM   2462  C   TRP A1082      14.734  23.318  10.216  1.00 73.89           C  
ANISOU 2462  C   TRP A1082    10533   9612   7930  -1653    674   -536       C  
ATOM   2463  O   TRP A1082      15.127  23.227  11.391  1.00 73.09           O  
ANISOU 2463  O   TRP A1082    10468   9384   7920  -1561    681   -519       O  
ATOM   2464  CB  TRP A1082      14.858  21.380   8.607  1.00 74.58           C  
ANISOU 2464  CB  TRP A1082    10971   9546   7822  -2023    831   -637       C  
ATOM   2465  CG  TRP A1082      15.989  20.646   9.237  1.00 72.85           C  
ANISOU 2465  CG  TRP A1082    10978   8997   7703  -1931    922   -632       C  
ATOM   2466  CD1 TRP A1082      16.235  20.495  10.567  1.00 71.28           C  
ANISOU 2466  CD1 TRP A1082    10803   8700   7582  -1837    930   -610       C  
ATOM   2467  CD2 TRP A1082      17.040  19.962   8.550  1.00 73.48           C  
ANISOU 2467  CD2 TRP A1082    11293   8821   7806  -1903   1026   -638       C  
ATOM   2468  NE1 TRP A1082      17.372  19.748  10.754  1.00 71.29           N  
ANISOU 2468  NE1 TRP A1082    11030   8412   7643  -1747   1033   -597       N  
ATOM   2469  CE2 TRP A1082      17.883  19.406   9.529  1.00 71.62           C  
ANISOU 2469  CE2 TRP A1082    11210   8353   7651  -1779   1097   -611       C  
ATOM   2470  CE3 TRP A1082      17.353  19.775   7.195  1.00 74.41           C  
ANISOU 2470  CE3 TRP A1082    11506   8891   7875  -1960   1069   -658       C  
ATOM   2471  CZ2 TRP A1082      19.015  18.668   9.202  1.00 72.85           C  
ANISOU 2471  CZ2 TRP A1082    11605   8244   7830  -1693   1215   -595       C  
ATOM   2472  CZ3 TRP A1082      18.475  19.047   6.872  1.00 76.18           C  
ANISOU 2472  CZ3 TRP A1082    11977   8835   8132  -1885   1184   -649       C  
ATOM   2473  CH2 TRP A1082      19.295  18.499   7.873  1.00 76.87           C  
ANISOU 2473  CH2 TRP A1082    12210   8706   8290  -1744   1259   -613       C  
ATOM   2474  N   ALA A1083      14.945  24.414   9.475  1.00 71.33           N  
ANISOU 2474  N   ALA A1083    10082   9361   7658  -1501    619   -498       N  
ATOM   2475  CA  ALA A1083      15.636  25.572  10.032  1.00 70.47           C  
ANISOU 2475  CA  ALA A1083     9889   9179   7709  -1237    570   -439       C  
ATOM   2476  C   ALA A1083      14.836  26.207  11.164  1.00 72.61           C  
ANISOU 2476  C   ALA A1083    10010   9609   7970  -1168    510   -408       C  
ATOM   2477  O   ALA A1083      15.395  26.535  12.221  1.00 73.26           O  
ANISOU 2477  O   ALA A1083    10104   9565   8169  -1035    501   -382       O  
ATOM   2478  CB  ALA A1083      15.912  26.591   8.929  1.00 70.95           C  
ANISOU 2478  CB  ALA A1083     9870   9290   7797  -1114    536   -409       C  
ATOM   2479  N   ARG A1084      13.525  26.383  10.972  1.00 75.38           N  
ANISOU 2479  N   ARG A1084    10214  10255   8172  -1256    473   -404       N  
ATOM   2480  CA  ARG A1084      12.700  26.919  12.049  1.00 78.69           C  
ANISOU 2480  CA  ARG A1084    10494  10842   8563  -1186    425   -368       C  
ATOM   2481  C   ARG A1084      12.719  26.003  13.262  1.00 78.09           C  
ANISOU 2481  C   ARG A1084    10509  10654   8508  -1285    454   -399       C  
ATOM   2482  O   ARG A1084      12.684  26.483  14.397  1.00 77.79           O  
ANISOU 2482  O   ARG A1084    10419  10603   8536  -1162    426   -368       O  
ATOM   2483  CB  ARG A1084      11.258  27.128  11.579  1.00 82.28           C  
ANISOU 2483  CB  ARG A1084    10764  11679   8821  -1274    389   -351       C  
ATOM   2484  CG  ARG A1084      11.068  28.243  10.560  1.00 85.28           C  
ANISOU 2484  CG  ARG A1084    11021  12218   9165  -1119    358   -297       C  
ATOM   2485  CD  ARG A1084      11.401  29.606  11.151  1.00 87.53           C  
ANISOU 2485  CD  ARG A1084    11261  12437   9560   -822    332   -229       C  
ATOM   2486  NE  ARG A1084      11.182  30.675  10.176  1.00 91.58           N  
ANISOU 2486  NE  ARG A1084    11683  13094  10021   -662    318   -173       N  
ATOM   2487  CZ  ARG A1084      11.435  31.961  10.396  1.00 91.58           C  
ANISOU 2487  CZ  ARG A1084    11673  13041  10081   -405    313   -111       C  
ATOM   2488  NH1 ARG A1084      11.918  32.352  11.569  1.00 89.20           N  
ANISOU 2488  NH1 ARG A1084    11440  12558   9895   -294    315   -101       N  
ATOM   2489  NH2 ARG A1084      11.208  32.857   9.441  1.00 93.90           N  
ANISOU 2489  NH2 ARG A1084    11907  13462  10309   -264    315    -59       N  
ATOM   2490  N   SER A1085      12.780  24.689  13.041  1.00 80.43           N  
ANISOU 2490  N   SER A1085    10959  10859   8740  -1505    518   -460       N  
ATOM   2491  CA  SER A1085      12.865  23.743  14.147  1.00 80.59           C  
ANISOU 2491  CA  SER A1085    11103  10745   8772  -1595    563   -490       C  
ATOM   2492  C   SER A1085      14.164  23.920  14.919  1.00 77.04           C  
ANISOU 2492  C   SER A1085    10747  10013   8512  -1396    581   -462       C  
ATOM   2493  O   SER A1085      14.177  23.865  16.155  1.00 78.61           O  
ANISOU 2493  O   SER A1085    10942  10164   8762  -1345    575   -449       O  
ATOM   2494  CB  SER A1085      12.746  22.316  13.616  1.00 83.46           C  
ANISOU 2494  CB  SER A1085    11665  11036   9011  -1867    652   -560       C  
ATOM   2495  OG  SER A1085      13.239  21.394  14.567  1.00 88.67           O  
ANISOU 2495  OG  SER A1085    12510  11467   9713  -1897    723   -580       O  
ATOM   2496  N   LEU A1086      15.268  24.131  14.203  1.00 75.98           N  
ANISOU 2496  N   LEU A1086    10688   9708   8471  -1288    604   -449       N  
ATOM   2497  CA  LEU A1086      16.533  24.403  14.877  1.00 74.11           C  
ANISOU 2497  CA  LEU A1086    10507   9258   8395  -1099    616   -412       C  
ATOM   2498  C   LEU A1086      16.487  25.721  15.639  1.00 73.69           C  
ANISOU 2498  C   LEU A1086    10295   9282   8423   -923    537   -364       C  
ATOM   2499  O   LEU A1086      17.092  25.842  16.708  1.00 74.87           O  
ANISOU 2499  O   LEU A1086    10459   9323   8663   -824    536   -340       O  
ATOM   2500  CB  LEU A1086      17.675  24.409  13.864  1.00 74.64           C  
ANISOU 2500  CB  LEU A1086    10666   9171   8523  -1028    654   -403       C  
ATOM   2501  CG  LEU A1086      17.987  23.033  13.278  1.00 74.42           C  
ANISOU 2501  CG  LEU A1086    10852   8998   8426  -1165    758   -441       C  
ATOM   2502  CD1 LEU A1086      19.093  23.129  12.255  1.00 71.16           C  
ANISOU 2502  CD1 LEU A1086    10513   8454   8070  -1073    793   -423       C  
ATOM   2503  CD2 LEU A1086      18.375  22.084  14.410  1.00 70.94           C  
ANISOU 2503  CD2 LEU A1086    10553   8401   8002  -1163    829   -439       C  
ATOM   2504  N   GLU A1087      15.783  26.716  15.101  1.00 73.02           N  
ANISOU 2504  N   GLU A1087    10068   9383   8291   -877    480   -346       N  
ATOM   2505  CA  GLU A1087      15.675  28.004  15.776  1.00 72.84           C  
ANISOU 2505  CA  GLU A1087     9933   9420   8321   -704    424   -298       C  
ATOM   2506  C   GLU A1087      14.865  27.869  17.060  1.00 77.56           C  
ANISOU 2506  C   GLU A1087    10472  10110   8886   -726    404   -294       C  
ATOM   2507  O   GLU A1087      15.288  28.322  18.130  1.00 74.91           O  
ANISOU 2507  O   GLU A1087    10137   9688   8636   -617    390   -270       O  
ATOM   2508  CB  GLU A1087      15.034  29.026  14.835  1.00 70.04           C  
ANISOU 2508  CB  GLU A1087     9467   9247   7897   -633    388   -270       C  
ATOM   2509  CG  GLU A1087      14.825  30.402  15.419  1.00 72.44           C  
ANISOU 2509  CG  GLU A1087     9692   9608   8223   -442    353   -217       C  
ATOM   2510  CD  GLU A1087      14.172  31.349  14.429  1.00 79.62           C  
ANISOU 2510  CD  GLU A1087    10511  10697   9042   -350    337   -179       C  
ATOM   2511  OE1 GLU A1087      13.456  30.865  13.530  1.00 84.11           O  
ANISOU 2511  OE1 GLU A1087    11019  11443   9497   -461    336   -193       O  
ATOM   2512  OE2 GLU A1087      14.373  32.577  14.543  1.00 84.01           O  
ANISOU 2512  OE2 GLU A1087    11070  11224   9627   -170    332   -135       O  
ATOM   2513  N   GLU A1088      13.701  27.228  16.970  1.00 82.47           N  
ANISOU 2513  N   GLU A1088    11042  10921   9372   -882    403   -318       N  
ATOM   2514  CA  GLU A1088      12.891  26.967  18.152  1.00 84.90           C  
ANISOU 2514  CA  GLU A1088    11295  11331   9634   -928    387   -317       C  
ATOM   2515  C   GLU A1088      13.658  26.147  19.181  1.00 82.33           C  
ANISOU 2515  C   GLU A1088    11102  10780   9401   -954    427   -338       C  
ATOM   2516  O   GLU A1088      13.469  26.325  20.385  1.00 79.53           O  
ANISOU 2516  O   GLU A1088    10710  10429   9078   -899    407   -321       O  
ATOM   2517  CB  GLU A1088      11.609  26.247  17.741  1.00 90.19           C  
ANISOU 2517  CB  GLU A1088    11899  12250  10119  -1140    388   -346       C  
ATOM   2518  CG  GLU A1088      10.692  25.925  18.891  1.00 98.69           C  
ANISOU 2518  CG  GLU A1088    12909  13464  11127  -1211    373   -347       C  
ATOM   2519  CD  GLU A1088       9.526  25.066  18.468  1.00106.63           C  
ANISOU 2519  CD  GLU A1088    13867  14717  11930  -1473    382   -384       C  
ATOM   2520  OE1 GLU A1088       9.419  24.764  17.258  1.00110.61           O  
ANISOU 2520  OE1 GLU A1088    14388  15292  12346  -1597    400   -410       O  
ATOM   2521  OE2 GLU A1088       8.721  24.692  19.342  1.00109.20           O  
ANISOU 2521  OE2 GLU A1088    14138  15177  12175  -1568    373   -390       O  
ATOM   2522  N   LYS A1089      14.547  25.264  18.733  1.00 83.27           N  
ANISOU 2522  N   LYS A1089    11379  10704   9555  -1018    489   -367       N  
ATOM   2523  CA  LYS A1089      15.290  24.454  19.688  1.00 82.08           C  
ANISOU 2523  CA  LYS A1089    11359  10355   9474  -1015    540   -373       C  
ATOM   2524  C   LYS A1089      16.408  25.245  20.358  1.00 74.55           C  
ANISOU 2524  C   LYS A1089    10387   9271   8666   -813    519   -326       C  
ATOM   2525  O   LYS A1089      16.600  25.130  21.570  1.00 70.23           O  
ANISOU 2525  O   LYS A1089     9846   8670   8167   -768    519   -311       O  
ATOM   2526  CB  LYS A1089      15.852  23.220  18.984  1.00 90.50           C  
ANISOU 2526  CB  LYS A1089    12622  11260  10505  -1128    633   -408       C  
ATOM   2527  CG  LYS A1089      15.795  21.936  19.786  1.00 95.47           C  
ANISOU 2527  CG  LYS A1089    13409  11776  11088  -1238    711   -434       C  
ATOM   2528  CD  LYS A1089      16.035  20.739  18.879  1.00100.98           C  
ANISOU 2528  CD  LYS A1089    14327  12343  11696  -1382    818   -475       C  
ATOM   2529  CE  LYS A1089      15.038  20.728  17.719  1.00107.70           C  
ANISOU 2529  CE  LYS A1089    15135  13377  12410  -1576    800   -521       C  
ATOM   2530  NZ  LYS A1089      15.300  19.633  16.724  1.00112.83           N  
ANISOU 2530  NZ  LYS A1089    16019  13890  12962  -1730    909   -565       N  
ATOM   2531  N   HIS A1090      17.144  26.064  19.602  1.00 75.50           N  
ANISOU 2531  N   HIS A1090    10486   9354   8848   -704    502   -302       N  
ATOM   2532  CA  HIS A1090      18.369  26.688  20.096  1.00 74.55           C  
ANISOU 2532  CA  HIS A1090    10370   9111   8843   -555    495   -263       C  
ATOM   2533  C   HIS A1090      18.259  28.205  20.075  1.00 73.88           C  
ANISOU 2533  C   HIS A1090    10182   9104   8785   -442    433   -235       C  
ATOM   2534  O   HIS A1090      17.931  28.798  19.041  1.00 74.02           O  
ANISOU 2534  O   HIS A1090    10162   9196   8765   -429    416   -236       O  
ATOM   2535  CB  HIS A1090      19.572  26.253  19.267  1.00 74.34           C  
ANISOU 2535  CB  HIS A1090    10443   8947   8854   -529    548   -255       C  
ATOM   2536  CG  HIS A1090      19.719  24.773  19.168  1.00 73.82           C  
ANISOU 2536  CG  HIS A1090    10525   8780   8743   -619    633   -276       C  
ATOM   2537  ND1 HIS A1090      20.173  24.000  20.214  1.00 72.78           N  
ANISOU 2537  ND1 HIS A1090    10470   8552   8631   -593    682   -259       N  
ATOM   2538  CD2 HIS A1090      19.452  23.917  18.155  1.00 72.30           C  
ANISOU 2538  CD2 HIS A1090    10441   8560   8470   -736    690   -312       C  
ATOM   2539  CE1 HIS A1090      20.186  22.732  19.848  1.00 72.25           C  
ANISOU 2539  CE1 HIS A1090    10570   8387   8496   -677    774   -281       C  
ATOM   2540  NE2 HIS A1090      19.753  22.655  18.603  1.00 73.74           N  
ANISOU 2540  NE2 HIS A1090    10787   8611   8621   -776    781   -317       N  
ATOM   2541  N   GLY A1091      18.565  28.831  21.211  1.00 72.34           N  
ANISOU 2541  N   GLY A1091     9959   8882   8646   -360    410   -210       N  
ATOM   2542  CA  GLY A1091      18.517  30.283  21.304  1.00 71.92           C  
ANISOU 2542  CA  GLY A1091     9854   8867   8603   -255    371   -184       C  
ATOM   2543  C   GLY A1091      19.634  31.002  20.574  1.00 71.22           C  
ANISOU 2543  C   GLY A1091     9803   8694   8562   -197    378   -169       C  
ATOM   2544  O   GLY A1091      19.535  32.216  20.369  1.00 74.37           O  
ANISOU 2544  O   GLY A1091    10195   9114   8947   -122    361   -153       O  
ATOM   2545  N   ASN A1092      20.686  30.288  20.182  1.00 67.67           N  
ANISOU 2545  N   ASN A1092     9405   8151   8154   -223    410   -170       N  
ATOM   2546  CA  ASN A1092      21.787  30.843  19.411  1.00 62.67           C  
ANISOU 2546  CA  ASN A1092     8799   7457   7556   -183    418   -154       C  
ATOM   2547  C   ASN A1092      21.619  30.617  17.912  1.00 62.74           C  
ANISOU 2547  C   ASN A1092     8827   7479   7534   -209    433   -171       C  
ATOM   2548  O   ASN A1092      22.589  30.741  17.160  1.00 66.58           O  
ANISOU 2548  O   ASN A1092     9343   7907   8047   -190    450   -160       O  
ATOM   2549  CB  ASN A1092      23.101  30.227  19.874  1.00 62.46           C  
ANISOU 2549  CB  ASN A1092     8801   7354   7578   -174    449   -129       C  
ATOM   2550  CG  ASN A1092      23.113  28.719  19.707  1.00 64.19           C  
ANISOU 2550  CG  ASN A1092     9076   7530   7783   -213    502   -137       C  
ATOM   2551  OD1 ASN A1092      22.054  28.096  19.651  1.00 66.51           O  
ANISOU 2551  OD1 ASN A1092     9387   7851   8031   -280    509   -169       O  
ATOM   2552  ND2 ASN A1092      24.305  28.124  19.643  1.00 62.61           N  
ANISOU 2552  ND2 ASN A1092     8916   7270   7604   -173    549   -103       N  
ATOM   2553  N   VAL A1093      20.425  30.256  17.466  1.00 57.79           N  
ANISOU 2553  N   VAL A1093     8176   6942   6839   -264    428   -195       N  
ATOM   2554  CA  VAL A1093      20.146  30.056  16.055  1.00 61.88           C  
ANISOU 2554  CA  VAL A1093     8703   7497   7310   -306    440   -213       C  
ATOM   2555  C   VAL A1093      18.940  30.900  15.682  1.00 65.47           C  
ANISOU 2555  C   VAL A1093     9077   8109   7688   -278    404   -208       C  
ATOM   2556  O   VAL A1093      17.871  30.765  16.285  1.00 64.53           O  
ANISOU 2556  O   VAL A1093     8899   8109   7509   -305    387   -211       O  
ATOM   2557  CB  VAL A1093      19.890  28.574  15.724  1.00 60.68           C  
ANISOU 2557  CB  VAL A1093     8615   7328   7114   -431    485   -246       C  
ATOM   2558  CG1 VAL A1093      19.454  28.437  14.289  1.00 59.90           C  
ANISOU 2558  CG1 VAL A1093     8520   7293   6947   -496    493   -268       C  
ATOM   2559  CG2 VAL A1093      21.142  27.752  15.981  1.00 60.60           C  
ANISOU 2559  CG2 VAL A1093     8703   7161   7163   -414    539   -234       C  
ATOM   2560  N   LYS A1094      19.111  31.765  14.686  1.00 70.14           N  
ANISOU 2560  N   LYS A1094     9664   8714   8270   -214    399   -195       N  
ATOM   2561  CA  LYS A1094      18.023  32.595  14.202  1.00 73.69           C  
ANISOU 2561  CA  LYS A1094    10042   9325   8630   -153    379   -176       C  
ATOM   2562  C   LYS A1094      17.890  32.443  12.698  1.00 70.56           C  
ANISOU 2562  C   LYS A1094     9636   8989   8184   -190    387   -186       C  
ATOM   2563  O   LYS A1094      18.890  32.432  11.977  1.00 73.11           O  
ANISOU 2563  O   LYS A1094    10024   9190   8565   -190    405   -194       O  
ATOM   2564  CB  LYS A1094      18.229  34.067  14.562  1.00 81.15           C  
ANISOU 2564  CB  LYS A1094    11010  10234   9589     -3    375   -138       C  
ATOM   2565  CG  LYS A1094      16.965  34.872  14.362  1.00 92.26           C  
ANISOU 2565  CG  LYS A1094    12351  11822  10883    100    369   -100       C  
ATOM   2566  CD  LYS A1094      17.180  36.334  14.609  1.00103.44           C  
ANISOU 2566  CD  LYS A1094    13841  13169  12292    257    390    -61       C  
ATOM   2567  CE  LYS A1094      15.897  37.103  14.361  1.00111.98           C  
ANISOU 2567  CE  LYS A1094    14864  14443  13240    399    402     -7       C  
ATOM   2568  NZ  LYS A1094      15.282  36.787  13.032  1.00118.34           N  
ANISOU 2568  NZ  LYS A1094    15579  15423  13963    381    395      0       N  
ATOM   2569  N   VAL A1095      16.650  32.323  12.233  1.00 67.85           N  
ANISOU 2569  N   VAL A1095     9203   8855   7722   -224    375   -183       N  
ATOM   2570  CA  VAL A1095      16.336  32.139  10.824  1.00 68.43           C  
ANISOU 2570  CA  VAL A1095     9247   9031   7721   -278    380   -192       C  
ATOM   2571  C   VAL A1095      15.512  33.327  10.368  1.00 66.21           C  
ANISOU 2571  C   VAL A1095     8878   8933   7346   -132    366   -138       C  
ATOM   2572  O   VAL A1095      14.597  33.763  11.069  1.00 62.20           O  
ANISOU 2572  O   VAL A1095     8291   8576   6766    -58    353   -102       O  
ATOM   2573  CB  VAL A1095      15.566  30.826  10.564  1.00 71.35           C  
ANISOU 2573  CB  VAL A1095     9588   9529   7994   -481    386   -234       C  
ATOM   2574  CG1 VAL A1095      15.264  30.669   9.074  1.00 69.89           C  
ANISOU 2574  CG1 VAL A1095     9375   9461   7719   -553    393   -245       C  
ATOM   2575  CG2 VAL A1095      16.360  29.633  11.082  1.00 72.07           C  
ANISOU 2575  CG2 VAL A1095     9803   9418   8161   -599    422   -279       C  
ATOM   2576  N   ILE A1096      15.828  33.840   9.189  1.00 70.73           N  
ANISOU 2576  N   ILE A1096     9468   9498   7911    -78    377   -127       N  
ATOM   2577  CA  ILE A1096      15.173  35.010   8.639  1.00 70.23           C  
ANISOU 2577  CA  ILE A1096     9346   9587   7753     89    380    -68       C  
ATOM   2578  C   ILE A1096      14.696  34.629   7.249  1.00 69.60           C  
ANISOU 2578  C   ILE A1096     9193   9680   7574     13    377    -74       C  
ATOM   2579  O   ILE A1096      15.496  34.530   6.314  1.00 69.74           O  
ANISOU 2579  O   ILE A1096     9278   9572   7647    -22    389    -99       O  
ATOM   2580  CB  ILE A1096      16.100  36.224   8.596  1.00 70.96           C  
ANISOU 2580  CB  ILE A1096     9556   9483   7923    249    406    -43       C  
ATOM   2581  CG1 ILE A1096      16.621  36.528   9.999  1.00 74.22           C  
ANISOU 2581  CG1 ILE A1096    10048   9732   8421    285    409    -44       C  
ATOM   2582  CG2 ILE A1096      15.370  37.417   8.010  1.00 71.76           C  
ANISOU 2582  CG2 ILE A1096     9628   9731   7906    443    429     26       C  
ATOM   2583  CD1 ILE A1096      17.521  37.737  10.055  1.00 78.50           C  
ANISOU 2583  CD1 ILE A1096    10725  10087   9014    402    442    -26       C  
ATOM   2584  N   THR A1097      13.400  34.395   7.114  1.00 73.42           N  
ANISOU 2584  N   THR A1097     9530  10467   7900    -24    361    -49       N  
ATOM   2585  CA  THR A1097      12.794  34.176   5.813  1.00 77.08           C  
ANISOU 2585  CA  THR A1097     9898  11156   8234    -91    357    -43       C  
ATOM   2586  C   THR A1097      12.274  35.465   5.194  1.00 80.46           C  
ANISOU 2586  C   THR A1097    10256  11753   8562    145    370     43       C  
ATOM   2587  O   THR A1097      11.696  35.428   4.105  1.00 82.92           O  
ANISOU 2587  O   THR A1097    10466  12295   8746    121    367     64       O  
ATOM   2588  CB  THR A1097      11.666  33.147   5.934  1.00 80.54           C  
ANISOU 2588  CB  THR A1097    10204  11874   8522   -296    336    -63       C  
ATOM   2589  OG1 THR A1097      10.796  33.514   7.009  1.00 82.09           O  
ANISOU 2589  OG1 THR A1097    10302  12240   8648   -201    322    -12       O  
ATOM   2590  CG2 THR A1097      12.247  31.773   6.219  1.00 80.87           C  
ANISOU 2590  CG2 THR A1097    10362  11724   8641   -546    345   -154       C  
ATOM   2591  N   GLU A1098      12.471  36.598   5.857  1.00 84.20           N  
ANISOU 2591  N   GLU A1098    10797  12118   9077    372    394     95       N  
ATOM   2592  CA  GLU A1098      12.009  37.871   5.335  1.00 89.20           C  
ANISOU 2592  CA  GLU A1098    11409  12877   9604    628    429    185       C  
ATOM   2593  C   GLU A1098      13.008  38.415   4.322  1.00 88.15           C  
ANISOU 2593  C   GLU A1098    11405  12538   9551    681    456    172       C  
ATOM   2594  O   GLU A1098      14.211  38.157   4.399  1.00 85.02           O  
ANISOU 2594  O   GLU A1098    11141  11847   9314    584    454    108       O  
ATOM   2595  CB  GLU A1098      11.812  38.877   6.471  1.00 94.56           C  
ANISOU 2595  CB  GLU A1098    12156  13496  10277    847    464    246       C  
ATOM   2596  CG  GLU A1098      11.075  38.326   7.693  1.00 99.95           C  
ANISOU 2596  CG  GLU A1098    12744  14309  10924    786    437    247       C  
ATOM   2597  CD  GLU A1098       9.576  38.172   7.477  1.00108.24           C  
ANISOU 2597  CD  GLU A1098    13570  15800  11756    821    424    317       C  
ATOM   2598  OE1 GLU A1098       9.057  38.671   6.454  1.00111.93           O  
ANISOU 2598  OE1 GLU A1098    13954  16487  12087    943    443    382       O  
ATOM   2599  OE2 GLU A1098       8.915  37.553   8.340  1.00111.75           O  
ANISOU 2599  OE2 GLU A1098    13913  16392  12155    725    394    311       O  
ATOM   2600  N   MET A1099      12.502  39.161   3.353  1.00 92.71           N  
ANISOU 2600  N   MET A1099    11933  13288  10003    841    484    240       N  
ATOM   2601  CA  MET A1099      13.384  39.799   2.387  1.00 95.52           C  
ANISOU 2601  CA  MET A1099    12417  13457  10420    913    516    236       C  
ATOM   2602  C   MET A1099      14.036  41.011   3.042  1.00 91.85           C  
ANISOU 2602  C   MET A1099    12151  12728  10019   1101    573    263       C  
ATOM   2603  O   MET A1099      13.342  41.894   3.560  1.00 93.30           O  
ANISOU 2603  O   MET A1099    12352  13001  10096   1317    619    342       O  
ATOM   2604  CB  MET A1099      12.618  40.201   1.131  1.00102.30           C  
ANISOU 2604  CB  MET A1099    13164  14592  11114   1028    533    303       C  
ATOM   2605  CG  MET A1099      13.506  40.798   0.061  1.00110.17           C  
ANISOU 2605  CG  MET A1099    14290  15401  12169   1089    566    295       C  
ATOM   2606  SD  MET A1099      12.539  41.401  -1.328  1.00120.63           S  
ANISOU 2606  SD  MET A1099    15483  17068  13282   1271    596    392       S  
ATOM   2607  CE  MET A1099      13.826  42.095  -2.367  1.00121.36           C  
ANISOU 2607  CE  MET A1099    15778  16846  13487   1321    637    365       C  
ATOM   2608  N   LEU A1100      15.364  41.043   3.032  1.00 84.93           N  
ANISOU 2608  N   LEU A1100    11431  11538   9299   1013    577    201       N  
ATOM   2609  CA  LEU A1100      16.128  42.121   3.638  1.00 79.02           C  
ANISOU 2609  CA  LEU A1100    10890  10529   8606   1126    631    210       C  
ATOM   2610  C   LEU A1100      16.687  43.033   2.552  1.00 77.07           C  
ANISOU 2610  C   LEU A1100    10771  10170   8341   1229    684    229       C  
ATOM   2611  O   LEU A1100      17.104  42.565   1.489  1.00 82.99           O  
ANISOU 2611  O   LEU A1100    11479  10925   9130   1130    658    196       O  
ATOM   2612  CB  LEU A1100      17.269  41.560   4.489  1.00 74.97           C  
ANISOU 2612  CB  LEU A1100    10453   9772   8258    943    600    133       C  
ATOM   2613  CG  LEU A1100      16.910  40.516   5.562  1.00 71.78           C  
ANISOU 2613  CG  LEU A1100     9943   9437   7894    814    549    102       C  
ATOM   2614  CD1 LEU A1100      18.168  39.997   6.245  1.00 69.32           C  
ANISOU 2614  CD1 LEU A1100     9711   8891   7738    657    529     37       C  
ATOM   2615  CD2 LEU A1100      15.946  41.082   6.602  1.00 70.97           C  
ANISOU 2615  CD2 LEU A1100     9827   9439   7698    962    572    159       C  
ATOM   2616  N   SER A1101      16.697  44.333   2.822  1.00 71.23           N  
ANISOU 2616  N   SER A1101    10209   9320   7536   1425    766    282       N  
ATOM   2617  CA  SER A1101      17.276  45.276   1.879  1.00 69.29           C  
ANISOU 2617  CA  SER A1101    10125   8937   7266   1519    830    297       C  
ATOM   2618  C   SER A1101      18.786  45.088   1.807  1.00 68.21           C  
ANISOU 2618  C   SER A1101    10099   8532   7284   1319    809    213       C  
ATOM   2619  O   SER A1101      19.410  44.500   2.695  1.00 70.77           O  
ANISOU 2619  O   SER A1101    10417   8752   7719   1156    766    157       O  
ATOM   2620  CB  SER A1101      16.960  46.716   2.282  1.00 71.92           C  
ANISOU 2620  CB  SER A1101    10672   9181   7474   1768    943    372       C  
ATOM   2621  OG  SER A1101      17.765  47.119   3.380  1.00 71.59           O  
ANISOU 2621  OG  SER A1101    10820   8878   7502   1690    970    329       O  
ATOM   2622  N   ARG A1102      19.378  45.623   0.741  1.00 68.75           N  
ANISOU 2622  N   ARG A1102    10267   8507   7348   1343    844    212       N  
ATOM   2623  CA  ARG A1102      20.819  45.493   0.560  1.00 70.03           C  
ANISOU 2623  CA  ARG A1102    10520   8452   7635   1162    828    142       C  
ATOM   2624  C   ARG A1102      21.590  46.251   1.630  1.00 65.89           C  
ANISOU 2624  C   ARG A1102    10200   7705   7131   1122    874    123       C  
ATOM   2625  O   ARG A1102      22.688  45.836   2.002  1.00 65.23           O  
ANISOU 2625  O   ARG A1102    10127   7502   7155    935    838     65       O  
ATOM   2626  CB  ARG A1102      21.239  45.985  -0.827  1.00 75.36           C  
ANISOU 2626  CB  ARG A1102    11263   9083   8286   1203    862    149       C  
ATOM   2627  CG  ARG A1102      20.663  45.196  -1.983  1.00 81.96           C  
ANISOU 2627  CG  ARG A1102    11905  10130   9107   1201    813    158       C  
ATOM   2628  CD  ARG A1102      21.530  45.338  -3.249  1.00 90.74           C  
ANISOU 2628  CD  ARG A1102    13071  11147  10257   1150    821    134       C  
ATOM   2629  NE  ARG A1102      21.848  46.728  -3.575  1.00 95.14           N  
ANISOU 2629  NE  ARG A1102    13853  11555  10740   1285    915    166       N  
ATOM   2630  CZ  ARG A1102      22.804  47.099  -4.422  1.00 97.92           C  
ANISOU 2630  CZ  ARG A1102    14312  11768  11126   1230    937    141       C  
ATOM   2631  NH1 ARG A1102      23.547  46.182  -5.028  1.00 96.07           N  
ANISOU 2631  NH1 ARG A1102    13969  11531  11001   1060    871     89       N  
ATOM   2632  NH2 ARG A1102      23.018  48.388  -4.661  1.00100.94           N  
ANISOU 2632  NH2 ARG A1102    14925  12007  11420   1348   1035    171       N  
ATOM   2633  N   GLU A1103      21.044  47.362   2.128  1.00 65.87           N  
ANISOU 2633  N   GLU A1103    10366   7652   7009   1297    962    175       N  
ATOM   2634  CA  GLU A1103      21.700  48.069   3.221  1.00 69.78           C  
ANISOU 2634  CA  GLU A1103    11071   7939   7502   1236   1013    152       C  
ATOM   2635  C   GLU A1103      21.788  47.186   4.464  1.00 69.19           C  
ANISOU 2635  C   GLU A1103    10871   7896   7521   1097    939    115       C  
ATOM   2636  O   GLU A1103      22.831  47.130   5.130  1.00 71.70           O  
ANISOU 2636  O   GLU A1103    11254   8079   7909    920    924     64       O  
ATOM   2637  CB  GLU A1103      20.951  49.368   3.534  1.00 75.37           C  
ANISOU 2637  CB  GLU A1103    12004   8588   8044   1472   1137    222       C  
ATOM   2638  CG  GLU A1103      21.043  50.456   2.470  1.00 80.36           C  
ANISOU 2638  CG  GLU A1103    12844   9124   8566   1613   1241    259       C  
ATOM   2639  CD  GLU A1103      20.141  50.204   1.271  1.00 85.71           C  
ANISOU 2639  CD  GLU A1103    13351  10028   9188   1790   1228    320       C  
ATOM   2640  OE1 GLU A1103      19.157  49.450   1.405  1.00 87.76           O  
ANISOU 2640  OE1 GLU A1103    13371  10534   9439   1855   1167    353       O  
ATOM   2641  OE2 GLU A1103      20.420  50.767   0.188  1.00 88.71           O  
ANISOU 2641  OE2 GLU A1103    13836  10350   9521   1852   1281    334       O  
ATOM   2642  N   PHE A1104      20.711  46.470   4.779  1.00 65.35           N  
ANISOU 2642  N   PHE A1104    10197   7607   7025   1167    893    143       N  
ATOM   2643  CA  PHE A1104      20.741  45.578   5.931  1.00 67.39           C  
ANISOU 2643  CA  PHE A1104    10339   7898   7369   1041    826    109       C  
ATOM   2644  C   PHE A1104      21.734  44.443   5.709  1.00 67.69           C  
ANISOU 2644  C   PHE A1104    10254   7915   7549    822    746     45       C  
ATOM   2645  O   PHE A1104      22.485  44.074   6.624  1.00 66.45           O  
ANISOU 2645  O   PHE A1104    10102   7676   7470    684    718      7       O  
ATOM   2646  CB  PHE A1104      19.332  45.041   6.196  1.00 73.39           C  
ANISOU 2646  CB  PHE A1104    10922   8893   8070   1152    797    153       C  
ATOM   2647  CG  PHE A1104      19.170  44.352   7.521  1.00 78.47           C  
ANISOU 2647  CG  PHE A1104    11485   9561   8770   1063    750    131       C  
ATOM   2648  CD1 PHE A1104      19.550  43.033   7.685  1.00 82.60           C  
ANISOU 2648  CD1 PHE A1104    11854  10122   9409    876    667     77       C  
ATOM   2649  CD2 PHE A1104      18.589  45.006   8.588  1.00 85.21           C  
ANISOU 2649  CD2 PHE A1104    12426  10398   9549   1180    796    168       C  
ATOM   2650  CE1 PHE A1104      19.386  42.392   8.901  1.00 81.84           C  
ANISOU 2650  CE1 PHE A1104    11691  10046   9359    802    630     59       C  
ATOM   2651  CE2 PHE A1104      18.425  44.368   9.811  1.00 85.63           C  
ANISOU 2651  CE2 PHE A1104    12402  10478   9655   1099    751    148       C  
ATOM   2652  CZ  PHE A1104      18.829  43.062   9.965  1.00 81.30           C  
ANISOU 2652  CZ  PHE A1104    11697   9968   9227    908    667     93       C  
ATOM   2653  N   VAL A1105      21.764  43.883   4.491  1.00 64.15           N  
ANISOU 2653  N   VAL A1105     9702   7547   7124    799    715     38       N  
ATOM   2654  CA  VAL A1105      22.698  42.798   4.212  1.00 60.73           C  
ANISOU 2654  CA  VAL A1105     9176   7089   6809    619    657    -14       C  
ATOM   2655  C   VAL A1105      24.131  43.296   4.333  1.00 62.94           C  
ANISOU 2655  C   VAL A1105     9587   7190   7138    516    677    -41       C  
ATOM   2656  O   VAL A1105      25.005  42.591   4.858  1.00 61.03           O  
ANISOU 2656  O   VAL A1105     9296   6913   6981    379    641    -71       O  
ATOM   2657  CB  VAL A1105      22.412  42.197   2.826  1.00 60.67           C  
ANISOU 2657  CB  VAL A1105     9062   7193   6798    620    634    -14       C  
ATOM   2658  CG1 VAL A1105      23.459  41.159   2.457  1.00 53.71           C  
ANISOU 2658  CG1 VAL A1105     8125   6258   6024    458    595    -60       C  
ATOM   2659  CG2 VAL A1105      21.015  41.580   2.804  1.00 63.72           C  
ANISOU 2659  CG2 VAL A1105     9296   7798   7117    672    607      9       C  
ATOM   2660  N   ARG A1106      24.387  44.535   3.879  1.00 60.98           N  
ANISOU 2660  N   ARG A1106     9512   6840   6819    581    743    -26       N  
ATOM   2661  CA  ARG A1106      25.715  45.129   4.006  1.00 60.10           C  
ANISOU 2661  CA  ARG A1106     9538   6577   6721    458    770    -53       C  
ATOM   2662  C   ARG A1106      26.094  45.308   5.472  1.00 61.79           C  
ANISOU 2662  C   ARG A1106     9812   6728   6938    369    774    -68       C  
ATOM   2663  O   ARG A1106      27.250  45.072   5.854  1.00 62.46           O  
ANISOU 2663  O   ARG A1106     9885   6775   7070    206    751    -95       O  
ATOM   2664  CB  ARG A1106      25.770  46.464   3.257  1.00 62.20           C  
ANISOU 2664  CB  ARG A1106    10011   6737   6884    543    855    -35       C  
ATOM   2665  CG  ARG A1106      27.094  47.230   3.377  1.00 61.70           C  
ANISOU 2665  CG  ARG A1106    10121   6522   6800    390    896    -66       C  
ATOM   2666  CD  ARG A1106      27.116  48.511   2.520  1.00 62.72           C  
ANISOU 2666  CD  ARG A1106    10481   6532   6817    470    992    -51       C  
ATOM   2667  NE  ARG A1106      26.125  49.483   2.996  1.00 64.57           N  
ANISOU 2667  NE  ARG A1106    10902   6705   6928    647   1082    -11       N  
ATOM   2668  CZ  ARG A1106      25.737  50.575   2.342  1.00 62.64           C  
ANISOU 2668  CZ  ARG A1106    10870   6371   6560    800   1186     24       C  
ATOM   2669  NH1 ARG A1106      26.255  50.877   1.152  1.00 65.56           N  
ANISOU 2669  NH1 ARG A1106    11294   6697   6918    784   1209     18       N  
ATOM   2670  NH2 ARG A1106      24.818  51.357   2.893  1.00 60.89           N  
ANISOU 2670  NH2 ARG A1106    10814   6104   6218    984   1276     71       N  
ATOM   2671  N   GLU A1107      25.131  45.731   6.304  1.00 61.93           N  
ANISOU 2671  N   GLU A1107     9886   6751   6894    478    804    -43       N  
ATOM   2672  CA  GLU A1107      25.351  45.753   7.749  1.00 68.54           C  
ANISOU 2672  CA  GLU A1107    10757   7547   7738    397    799    -57       C  
ATOM   2673  C   GLU A1107      25.718  44.366   8.276  1.00 67.36           C  
ANISOU 2673  C   GLU A1107    10398   7490   7705    281    712    -79       C  
ATOM   2674  O   GLU A1107      26.602  44.230   9.129  1.00 67.50           O  
ANISOU 2674  O   GLU A1107    10418   7476   7753    144    697   -100       O  
ATOM   2675  CB  GLU A1107      24.105  46.257   8.471  1.00 77.56           C  
ANISOU 2675  CB  GLU A1107    11966   8707   8798    561    842    -20       C  
ATOM   2676  CG  GLU A1107      23.802  47.739   8.322  1.00 89.91           C  
ANISOU 2676  CG  GLU A1107    13798  10143  10219    690    957     10       C  
ATOM   2677  CD  GLU A1107      24.387  48.572   9.450  1.00 99.20           C  
ANISOU 2677  CD  GLU A1107    15195  11160  11338    588   1017    -12       C  
ATOM   2678  OE1 GLU A1107      25.610  48.474   9.694  1.00 99.90           O  
ANISOU 2678  OE1 GLU A1107    15297  11192  11468    369    992    -59       O  
ATOM   2679  OE2 GLU A1107      23.620  49.322  10.100  1.00105.74           O  
ANISOU 2679  OE2 GLU A1107    16183  11933  12063    724   1093     21       O  
ATOM   2680  N   LEU A1108      25.030  43.328   7.799  1.00 63.38           N  
ANISOU 2680  N   LEU A1108     9721   7109   7250    332    663    -72       N  
ATOM   2681  CA  LEU A1108      25.322  41.971   8.255  1.00 60.57           C  
ANISOU 2681  CA  LEU A1108     9204   6821   6989    236    600    -91       C  
ATOM   2682  C   LEU A1108      26.749  41.586   7.910  1.00 61.48           C  
ANISOU 2682  C   LEU A1108     9297   6899   7164    108    586   -108       C  
ATOM   2683  O   LEU A1108      27.516  41.148   8.775  1.00 60.23           O  
ANISOU 2683  O   LEU A1108     9099   6741   7044     13    567   -114       O  
ATOM   2684  CB  LEU A1108      24.344  40.977   7.628  1.00 58.83           C  
ANISOU 2684  CB  LEU A1108     8842   6727   6783    287    567    -86       C  
ATOM   2685  CG  LEU A1108      22.888  41.179   8.047  1.00 67.29           C  
ANISOU 2685  CG  LEU A1108     9885   7898   7783    406    573    -59       C  
ATOM   2686  CD1 LEU A1108      21.979  40.362   7.138  1.00 72.41           C  
ANISOU 2686  CD1 LEU A1108    10400   8702   8409    430    546    -55       C  
ATOM   2687  CD2 LEU A1108      22.683  40.784   9.486  1.00 68.45           C  
ANISOU 2687  CD2 LEU A1108     9998   8055   7955    370    552    -65       C  
ATOM   2688  N   TYR A1109      27.124  41.765   6.639  1.00 60.18           N  
ANISOU 2688  N   TYR A1109     9153   6718   6995    114    598   -109       N  
ATOM   2689  CA  TYR A1109      28.473  41.438   6.196  1.00 58.73           C  
ANISOU 2689  CA  TYR A1109     8943   6519   6853     10    589   -117       C  
ATOM   2690  C   TYR A1109      29.516  42.159   7.031  1.00 59.95           C  
ANISOU 2690  C   TYR A1109     9176   6627   6974   -103    607   -120       C  
ATOM   2691  O   TYR A1109      30.552  41.581   7.372  1.00 62.12           O  
ANISOU 2691  O   TYR A1109     9372   6950   7282   -198    586   -115       O  
ATOM   2692  CB  TYR A1109      28.647  41.812   4.729  1.00 61.19           C  
ANISOU 2692  CB  TYR A1109     9295   6808   7147     41    609   -117       C  
ATOM   2693  CG  TYR A1109      27.930  40.921   3.752  1.00 64.79           C  
ANISOU 2693  CG  TYR A1109     9653   7333   7632    104    588   -116       C  
ATOM   2694  CD1 TYR A1109      27.666  39.586   4.054  1.00 65.01           C  
ANISOU 2694  CD1 TYR A1109     9564   7425   7713     81    555   -122       C  
ATOM   2695  CD2 TYR A1109      27.541  41.405   2.505  1.00 65.77           C  
ANISOU 2695  CD2 TYR A1109     9815   7457   7717    175    608   -112       C  
ATOM   2696  CE1 TYR A1109      27.033  38.755   3.142  1.00 65.87           C  
ANISOU 2696  CE1 TYR A1109     9607   7594   7827    103    544   -129       C  
ATOM   2697  CE2 TYR A1109      26.904  40.584   1.590  1.00 69.26           C  
ANISOU 2697  CE2 TYR A1109    10166   7980   8171    207    589   -114       C  
ATOM   2698  CZ  TYR A1109      26.656  39.262   1.916  1.00 68.73           C  
ANISOU 2698  CZ  TYR A1109     9993   7973   8147    158    558   -126       C  
ATOM   2699  OH  TYR A1109      26.020  38.466   1.005  1.00 72.98           O  
ANISOU 2699  OH  TYR A1109    10466   8589   8675    157    548   -135       O  
ATOM   2700  N   GLY A1110      29.254  43.417   7.382  1.00 59.53           N  
ANISOU 2700  N   GLY A1110     9287   6492   6838    -94    653   -125       N  
ATOM   2701  CA  GLY A1110      30.201  44.235   8.104  1.00 56.91           C  
ANISOU 2701  CA  GLY A1110     9067   6111   6444   -234    682   -136       C  
ATOM   2702  C   GLY A1110      30.208  44.019   9.599  1.00 62.44           C  
ANISOU 2702  C   GLY A1110     9737   6841   7147   -293    664   -137       C  
ATOM   2703  O   GLY A1110      30.934  44.727  10.304  1.00 65.73           O  
ANISOU 2703  O   GLY A1110    10251   7229   7493   -430    690   -149       O  
ATOM   2704  N   SER A1111      29.423  43.071  10.117  1.00 59.97           N  
ANISOU 2704  N   SER A1111     9298   6587   6901   -211    624   -128       N  
ATOM   2705  CA  SER A1111      29.378  42.890  11.563  1.00 61.14           C  
ANISOU 2705  CA  SER A1111     9422   6758   7051   -258    610   -128       C  
ATOM   2706  C   SER A1111      29.505  41.420  11.974  1.00 59.61           C  
ANISOU 2706  C   SER A1111     9033   6667   6948   -257    555   -115       C  
ATOM   2707  O   SER A1111      30.088  41.124  13.021  1.00 60.28           O  
ANISOU 2707  O   SER A1111     9065   6801   7036   -337    539   -108       O  
ATOM   2708  CB  SER A1111      28.102  43.519  12.132  1.00 64.48           C  
ANISOU 2708  CB  SER A1111     9952   7122   7427   -148    641   -127       C  
ATOM   2709  OG  SER A1111      26.945  42.901  11.605  1.00 71.02           O  
ANISOU 2709  OG  SER A1111    10690   8002   8292     -2    620   -113       O  
ATOM   2710  N   VAL A1112      29.004  40.488  11.153  1.00 58.73           N  
ANISOU 2710  N   VAL A1112     8829   6591   6896   -173    534   -110       N  
ATOM   2711  CA  VAL A1112      29.184  39.068  11.453  1.00 55.51           C  
ANISOU 2711  CA  VAL A1112     8282   6254   6557   -174    504    -98       C  
ATOM   2712  C   VAL A1112      30.658  38.696  11.317  1.00 60.84           C  
ANISOU 2712  C   VAL A1112     8897   6980   7240   -251    504    -76       C  
ATOM   2713  O   VAL A1112      31.449  39.374  10.647  1.00 67.93           O  
ANISOU 2713  O   VAL A1112     9838   7871   8100   -304    519    -75       O  
ATOM   2714  CB  VAL A1112      28.308  38.177  10.556  1.00 53.92           C  
ANISOU 2714  CB  VAL A1112     8028   6068   6392    -96    495   -104       C  
ATOM   2715  CG1 VAL A1112      26.839  38.612  10.612  1.00 53.07           C  
ANISOU 2715  CG1 VAL A1112     7953   5963   6249    -16    495   -114       C  
ATOM   2716  CG2 VAL A1112      28.821  38.197   9.127  1.00 55.51           C  
ANISOU 2716  CG2 VAL A1112     8239   6258   6596    -93    507   -104       C  
ATOM   2717  N   ASP A1113      31.031  37.595  11.972  1.00 56.64           N  
ANISOU 2717  N   ASP A1113     8265   6512   6743   -248    493    -52       N  
ATOM   2718  CA  ASP A1113      32.419  37.142  11.977  1.00 55.94           C  
ANISOU 2718  CA  ASP A1113     8099   6513   6644   -289    499    -11       C  
ATOM   2719  C   ASP A1113      32.737  36.326  10.736  1.00 58.37           C  
ANISOU 2719  C   ASP A1113     8376   6822   6981   -228    517      6       C  
ATOM   2720  O   ASP A1113      33.783  36.511  10.103  1.00 62.81           O  
ANISOU 2720  O   ASP A1113     8915   7436   7515   -257    528     31       O  
ATOM   2721  CB  ASP A1113      32.698  36.302  13.225  1.00 53.49           C  
ANISOU 2721  CB  ASP A1113     7703   6278   6342   -282    495     22       C  
ATOM   2722  CG  ASP A1113      32.678  37.126  14.496  1.00 58.65           C  
ANISOU 2722  CG  ASP A1113     8378   6953   6954   -365    479     12       C  
ATOM   2723  OD1 ASP A1113      33.379  38.155  14.538  1.00 59.89           O  
ANISOU 2723  OD1 ASP A1113     8572   7140   7042   -474    483      8       O  
ATOM   2724  OD2 ASP A1113      31.952  36.753  15.448  1.00 60.71           O  
ANISOU 2724  OD2 ASP A1113     8630   7197   7240   -335    469      5       O  
ATOM   2725  N   PHE A1114      31.861  35.394  10.397  1.00 57.05           N  
ANISOU 2725  N   PHE A1114     8214   6605   6857   -155    523     -7       N  
ATOM   2726  CA  PHE A1114      32.101  34.489   9.292  1.00 55.87           C  
ANISOU 2726  CA  PHE A1114     8061   6441   6725   -104    551      6       C  
ATOM   2727  C   PHE A1114      30.831  34.356   8.477  1.00 54.74           C  
ANISOU 2727  C   PHE A1114     7970   6231   6598    -82    547    -39       C  
ATOM   2728  O   PHE A1114      29.716  34.385   9.010  1.00 53.81           O  
ANISOU 2728  O   PHE A1114     7863   6102   6482    -82    530    -67       O  
ATOM   2729  CB  PHE A1114      32.554  33.103   9.761  1.00 56.53           C  
ANISOU 2729  CB  PHE A1114     8107   6554   6817    -48    586     49       C  
ATOM   2730  CG  PHE A1114      33.817  33.117  10.563  1.00 59.46           C  
ANISOU 2730  CG  PHE A1114     8399   7040   7154    -49    594    110       C  
ATOM   2731  CD1 PHE A1114      35.048  32.947   9.946  1.00 59.11           C  
ANISOU 2731  CD1 PHE A1114     8309   7076   7076    -19    622    165       C  
ATOM   2732  CD2 PHE A1114      33.774  33.274  11.943  1.00 57.54           C  
ANISOU 2732  CD2 PHE A1114     8115   6848   6901    -78    574    119       C  
ATOM   2733  CE1 PHE A1114      36.212  32.941  10.688  1.00 60.03           C  
ANISOU 2733  CE1 PHE A1114     8324   7348   7136    -20    629    233       C  
ATOM   2734  CE2 PHE A1114      34.937  33.282  12.690  1.00 60.06           C  
ANISOU 2734  CE2 PHE A1114     8342   7309   7170    -89    579    181       C  
ATOM   2735  CZ  PHE A1114      36.160  33.126  12.059  1.00 61.64           C  
ANISOU 2735  CZ  PHE A1114     8481   7616   7324    -62    606    241       C  
ATOM   2736  N   VAL A1115      31.026  34.211   7.177  1.00 51.64           N  
ANISOU 2736  N   VAL A1115     7601   5816   6205    -67    564    -43       N  
ATOM   2737  CA  VAL A1115      29.962  33.875   6.250  1.00 56.87           C  
ANISOU 2737  CA  VAL A1115     8298   6445   6865    -58    567    -79       C  
ATOM   2738  C   VAL A1115      30.194  32.442   5.793  1.00 57.97           C  
ANISOU 2738  C   VAL A1115     8461   6556   7007    -42    613    -68       C  
ATOM   2739  O   VAL A1115      31.313  32.082   5.410  1.00 60.01           O  
ANISOU 2739  O   VAL A1115     8720   6813   7268    -10    647    -30       O  
ATOM   2740  CB  VAL A1115      29.931  34.850   5.063  1.00 59.65           C  
ANISOU 2740  CB  VAL A1115     8677   6785   7201    -55    559    -93       C  
ATOM   2741  CG1 VAL A1115      28.973  34.343   4.003  1.00 65.78           C  
ANISOU 2741  CG1 VAL A1115     9471   7560   7962    -50    565   -121       C  
ATOM   2742  CG2 VAL A1115      29.512  36.234   5.535  1.00 57.24           C  
ANISOU 2742  CG2 VAL A1115     8396   6481   6870    -56    535   -103       C  
ATOM   2743  N   ILE A1116      29.158  31.614   5.875  1.00 55.54           N  
ANISOU 2743  N   ILE A1116     8184   6234   6686    -67    624    -98       N  
ATOM   2744  CA  ILE A1116      29.243  30.224   5.447  1.00 56.98           C  
ANISOU 2744  CA  ILE A1116     8439   6363   6849    -71    686    -97       C  
ATOM   2745  C   ILE A1116      28.572  30.114   4.087  1.00 59.06           C  
ANISOU 2745  C   ILE A1116     8743   6618   7080   -118    692   -136       C  
ATOM   2746  O   ILE A1116      27.439  30.579   3.901  1.00 60.30           O  
ANISOU 2746  O   ILE A1116     8869   6833   7211   -164    653   -173       O  
ATOM   2747  CB  ILE A1116      28.609  29.254   6.460  1.00 55.69           C  
ANISOU 2747  CB  ILE A1116     8309   6182   6669    -99    710   -108       C  
ATOM   2748  CG1 ILE A1116      29.273  29.374   7.830  1.00 56.87           C  
ANISOU 2748  CG1 ILE A1116     8409   6354   6847    -48    703    -65       C  
ATOM   2749  CG2 ILE A1116      28.787  27.833   5.981  1.00 53.71           C  
ANISOU 2749  CG2 ILE A1116     8181   5847   6377   -104    797   -105       C  
ATOM   2750  CD1 ILE A1116      28.561  28.589   8.934  1.00 60.75           C  
ANISOU 2750  CD1 ILE A1116     8926   6833   7325    -74    717    -77       C  
ATOM   2751  N   ILE A1117      29.296  29.538   3.133  1.00 56.85           N  
ANISOU 2751  N   ILE A1117     8527   6283   6791    -97    744   -122       N  
ATOM   2752  CA  ILE A1117      28.850  29.399   1.753  1.00 58.31           C  
ANISOU 2752  CA  ILE A1117     8757   6457   6941   -145    757   -156       C  
ATOM   2753  C   ILE A1117      29.033  27.935   1.380  1.00 62.74           C  
ANISOU 2753  C   ILE A1117     9456   6926   7456   -167    847   -158       C  
ATOM   2754  O   ILE A1117      30.009  27.584   0.704  1.00 67.57           O  
ANISOU 2754  O   ILE A1117    10127   7479   8068   -106    901   -125       O  
ATOM   2755  CB  ILE A1117      29.634  30.341   0.824  1.00 59.92           C  
ANISOU 2755  CB  ILE A1117     8923   6672   7172    -95    736   -136       C  
ATOM   2756  CG1 ILE A1117      29.776  31.712   1.489  1.00 61.85           C  
ANISOU 2756  CG1 ILE A1117     9079   6972   7450    -66    674   -123       C  
ATOM   2757  CG2 ILE A1117      28.935  30.503  -0.509  1.00 58.22           C  
ANISOU 2757  CG2 ILE A1117     8725   6475   6920   -145    728   -175       C  
ATOM   2758  CD1 ILE A1117      30.663  32.665   0.774  1.00 65.37           C  
ANISOU 2758  CD1 ILE A1117     9504   7422   7911    -34    662   -102       C  
ATOM   2759  N   PRO A1118      28.157  27.042   1.835  1.00 63.34           N  
ANISOU 2759  N   PRO A1118     9603   6982   7480   -252    878   -192       N  
ATOM   2760  CA  PRO A1118      28.324  25.606   1.586  1.00 61.66           C  
ANISOU 2760  CA  PRO A1118     9572   6652   7203   -282    987   -196       C  
ATOM   2761  C   PRO A1118      27.648  25.170   0.286  1.00 64.73           C  
ANISOU 2761  C   PRO A1118    10053   7027   7514   -409   1016   -251       C  
ATOM   2762  O   PRO A1118      26.892  24.196   0.253  1.00 66.19           O  
ANISOU 2762  O   PRO A1118    10367   7174   7610   -541   1073   -296       O  
ATOM   2763  CB  PRO A1118      27.681  24.973   2.813  1.00 64.47           C  
ANISOU 2763  CB  PRO A1118     9965   6999   7533   -333   1003   -210       C  
ATOM   2764  CG  PRO A1118      26.583  25.935   3.195  1.00 63.17           C  
ANISOU 2764  CG  PRO A1118     9645   6975   7382   -403    897   -246       C  
ATOM   2765  CD  PRO A1118      26.979  27.310   2.686  1.00 65.52           C  
ANISOU 2765  CD  PRO A1118     9809   7343   7742   -326    822   -225       C  
ATOM   2766  N   SER A1119      27.917  25.890  -0.794  1.00 65.83           N  
ANISOU 2766  N   SER A1119    10135   7203   7676   -385    982   -250       N  
ATOM   2767  CA  SER A1119      27.336  25.556  -2.088  1.00 66.54           C  
ANISOU 2767  CA  SER A1119    10297   7297   7689   -504   1005   -298       C  
ATOM   2768  C   SER A1119      27.803  24.188  -2.556  1.00 68.37           C  
ANISOU 2768  C   SER A1119    10759   7368   7849   -530   1136   -300       C  
ATOM   2769  O   SER A1119      28.944  23.788  -2.314  1.00 67.71           O  
ANISOU 2769  O   SER A1119    10752   7177   7795   -388   1204   -241       O  
ATOM   2770  CB  SER A1119      27.729  26.595  -3.141  1.00 60.71           C  
ANISOU 2770  CB  SER A1119     9460   6611   6994   -443    953   -285       C  
ATOM   2771  OG  SER A1119      27.422  27.909  -2.740  1.00 63.87           O  
ANISOU 2771  OG  SER A1119     9689   7130   7449   -396    854   -275       O  
ATOM   2772  N   TYR A1120      26.910  23.462  -3.227  1.00 71.24           N  
ANISOU 2772  N   TYR A1120    11243   7726   8100   -713   1179   -364       N  
ATOM   2773  CA  TYR A1120      27.362  22.340  -4.044  1.00 73.77           C  
ANISOU 2773  CA  TYR A1120    11809   7883   8337   -747   1309   -372       C  
ATOM   2774  C   TYR A1120      27.957  22.840  -5.349  1.00 80.96           C  
ANISOU 2774  C   TYR A1120    12690   8794   9275   -688   1298   -358       C  
ATOM   2775  O   TYR A1120      28.966  22.311  -5.830  1.00 85.35           O  
ANISOU 2775  O   TYR A1120    13390   9213   9827   -582   1392   -318       O  
ATOM   2776  CB  TYR A1120      26.208  21.394  -4.348  1.00 70.51           C  
ANISOU 2776  CB  TYR A1120    11555   7465   7771  -1003   1367   -453       C  
ATOM   2777  CG  TYR A1120      25.733  20.579  -3.184  1.00 71.89           C  
ANISOU 2777  CG  TYR A1120    11839   7588   7888  -1080   1419   -470       C  
ATOM   2778  CD1 TYR A1120      24.895  21.128  -2.222  1.00 72.94           C  
ANISOU 2778  CD1 TYR A1120    11788   7879   8048  -1128   1319   -484       C  
ATOM   2779  CD2 TYR A1120      26.099  19.249  -3.055  1.00 72.37           C  
ANISOU 2779  CD2 TYR A1120    12205   7437   7856  -1100   1579   -470       C  
ATOM   2780  CE1 TYR A1120      24.449  20.375  -1.148  1.00 74.87           C  
ANISOU 2780  CE1 TYR A1120    12132   8078   8238  -1204   1367   -501       C  
ATOM   2781  CE2 TYR A1120      25.655  18.487  -1.991  1.00 74.48           C  
ANISOU 2781  CE2 TYR A1120    12593   7646   8062  -1173   1636   -487       C  
ATOM   2782  CZ  TYR A1120      24.831  19.052  -1.041  1.00 74.04           C  
ANISOU 2782  CZ  TYR A1120    12332   7757   8043  -1232   1524   -505       C  
ATOM   2783  OH  TYR A1120      24.386  18.298   0.009  1.00 73.36           O  
ANISOU 2783  OH  TYR A1120    12363   7615   7895  -1310   1580   -522       O  
ATOM   2784  N   PHE A1121      27.352  23.878  -5.918  1.00 83.72           N  
ANISOU 2784  N   PHE A1121    12856   9306   9648   -739   1189   -383       N  
ATOM   2785  CA  PHE A1121      27.726  24.425  -7.212  1.00 82.80           C  
ANISOU 2785  CA  PHE A1121    12701   9210   9548   -707   1169   -379       C  
ATOM   2786  C   PHE A1121      27.661  25.936  -7.077  1.00 80.40           C  
ANISOU 2786  C   PHE A1121    12156   9054   9339   -616   1044   -356       C  
ATOM   2787  O   PHE A1121      26.650  26.473  -6.617  1.00 78.23           O  
ANISOU 2787  O   PHE A1121    11755   8922   9047   -678    970   -378       O  
ATOM   2788  CB  PHE A1121      26.780  23.899  -8.301  1.00 84.07           C  
ANISOU 2788  CB  PHE A1121    12952   9415   9577   -920   1197   -449       C  
ATOM   2789  CG  PHE A1121      26.776  24.700  -9.571  1.00 90.71           C  
ANISOU 2789  CG  PHE A1121    13692  10346  10429   -913   1144   -454       C  
ATOM   2790  CD1 PHE A1121      27.825  24.610 -10.473  1.00 95.06           C  
ANISOU 2790  CD1 PHE A1121    14330  10777  11012   -816   1196   -426       C  
ATOM   2791  CD2 PHE A1121      25.696  25.506  -9.887  1.00 92.86           C  
ANISOU 2791  CD2 PHE A1121    13786  10833  10662   -996   1048   -480       C  
ATOM   2792  CE1 PHE A1121      27.807  25.336 -11.652  1.00 96.77           C  
ANISOU 2792  CE1 PHE A1121    14460  11073  11235   -813   1149   -431       C  
ATOM   2793  CE2 PHE A1121      25.671  26.235 -11.061  1.00 96.55           C  
ANISOU 2793  CE2 PHE A1121    14168  11387  11129   -978   1006   -479       C  
ATOM   2794  CZ  PHE A1121      26.729  26.150 -11.948  1.00 97.83           C  
ANISOU 2794  CZ  PHE A1121    14422  11414  11335   -894   1054   -459       C  
ATOM   2795  N   GLU A1122      28.752  26.617  -7.422  1.00 82.22           N  
ANISOU 2795  N   GLU A1122    12333   9250   9654   -465   1028   -306       N  
ATOM   2796  CA  GLU A1122      28.830  28.071  -7.277  1.00 82.10           C  
ANISOU 2796  CA  GLU A1122    12135   9342   9718   -379    929   -283       C  
ATOM   2797  C   GLU A1122      29.749  28.622  -8.357  1.00 81.30           C  
ANISOU 2797  C   GLU A1122    12023   9213   9656   -298    930   -256       C  
ATOM   2798  O   GLU A1122      30.959  28.781  -8.147  1.00 82.00           O  
ANISOU 2798  O   GLU A1122    12108   9245   9802   -182    949   -204       O  
ATOM   2799  CB  GLU A1122      29.327  28.467  -5.887  1.00 81.47           C  
ANISOU 2799  CB  GLU A1122    11985   9259   9710   -283    902   -241       C  
ATOM   2800  CG  GLU A1122      29.086  29.922  -5.521  1.00 80.07           C  
ANISOU 2800  CG  GLU A1122    11656   9185   9582   -235    810   -231       C  
ATOM   2801  CD  GLU A1122      27.618  30.218  -5.289  1.00 76.94           C  
ANISOU 2801  CD  GLU A1122    11192   8911   9132   -314    761   -269       C  
ATOM   2802  OE1 GLU A1122      27.008  30.898  -6.144  1.00 77.04           O  
ANISOU 2802  OE1 GLU A1122    11147   9016   9109   -326    726   -282       O  
ATOM   2803  OE2 GLU A1122      27.074  29.756  -4.257  1.00 71.00           O  
ANISOU 2803  OE2 GLU A1122    10438   8175   8362   -356    761   -279       O  
ATOM   2804  N   PRO A1123      29.206  28.933  -9.535  1.00 81.41           N  
ANISOU 2804  N   PRO A1123    12020   9285   9627   -359    910   -288       N  
ATOM   2805  CA  PRO A1123      30.075  29.432 -10.611  1.00 82.96           C  
ANISOU 2805  CA  PRO A1123    12215   9449   9858   -286    914   -265       C  
ATOM   2806  C   PRO A1123      30.685  30.792 -10.311  1.00 83.30           C  
ANISOU 2806  C   PRO A1123    12138   9532   9980   -175    852   -226       C  
ATOM   2807  O   PRO A1123      31.826  31.049 -10.714  1.00 79.36           O  
ANISOU 2807  O   PRO A1123    11646   8986   9522    -98    869   -189       O  
ATOM   2808  CB  PRO A1123      29.140  29.481 -11.827  1.00 83.52           C  
ANISOU 2808  CB  PRO A1123    12282   9599   9852   -390    901   -311       C  
ATOM   2809  CG  PRO A1123      27.775  29.606 -11.254  1.00 83.43           C  
ANISOU 2809  CG  PRO A1123    12193   9726   9781   -480    854   -342       C  
ATOM   2810  CD  PRO A1123      27.789  28.878  -9.933  1.00 82.91           C  
ANISOU 2810  CD  PRO A1123    12177   9600   9726   -497    882   -340       C  
ATOM   2811  N   PHE A1124      29.973  31.665  -9.604  1.00 89.52           N  
ANISOU 2811  N   PHE A1124    12829  10407  10776   -171    788   -231       N  
ATOM   2812  CA  PHE A1124      30.500  32.977  -9.245  1.00 95.02           C  
ANISOU 2812  CA  PHE A1124    13454  11122  11526    -87    744   -201       C  
ATOM   2813  C   PHE A1124      30.242  33.200  -7.764  1.00 91.51           C  
ANISOU 2813  C   PHE A1124    12968  10700  11101    -77    718   -192       C  
ATOM   2814  O   PHE A1124      29.087  33.313  -7.337  1.00 95.36           O  
ANISOU 2814  O   PHE A1124    13418  11261  11552   -109    690   -213       O  
ATOM   2815  CB  PHE A1124      29.856  34.071 -10.087  1.00107.46           C  
ANISOU 2815  CB  PHE A1124    14985  12772  13073    -70    706   -211       C  
ATOM   2816  CG  PHE A1124      29.740  33.707 -11.532  1.00122.04           C  
ANISOU 2816  CG  PHE A1124    16864  14625  14881   -105    728   -230       C  
ATOM   2817  CD1 PHE A1124      30.855  33.734 -12.353  1.00128.18           C  
ANISOU 2817  CD1 PHE A1124    17682  15327  15692    -70    755   -212       C  
ATOM   2818  CD2 PHE A1124      28.526  33.309 -12.070  1.00127.46           C  
ANISOU 2818  CD2 PHE A1124    17533  15410  15485   -183    722   -263       C  
ATOM   2819  CE1 PHE A1124      30.761  33.387 -13.679  1.00129.91           C  
ANISOU 2819  CE1 PHE A1124    17939  15545  15876   -103    777   -230       C  
ATOM   2820  CE2 PHE A1124      28.424  32.959 -13.404  1.00130.14           C  
ANISOU 2820  CE2 PHE A1124    17905  15765  15778   -232    743   -283       C  
ATOM   2821  CZ  PHE A1124      29.544  32.999 -14.209  1.00130.87           C  
ANISOU 2821  CZ  PHE A1124    18052  15756  15916   -188    771   -267       C  
ATOM   2822  N   GLY A1125      31.310  33.259  -6.978  1.00 86.57           N  
ANISOU 2822  N   GLY A1125    12338  10032  10522    -33    727   -156       N  
ATOM   2823  CA  GLY A1125      31.143  33.537  -5.567  1.00 79.87           C  
ANISOU 2823  CA  GLY A1125    11451   9206   9692    -27    702   -146       C  
ATOM   2824  C   GLY A1125      30.804  34.990  -5.309  1.00 72.37           C  
ANISOU 2824  C   GLY A1125    10463   8296   8739     -5    657   -148       C  
ATOM   2825  O   GLY A1125      31.612  35.714  -4.724  1.00 76.20           O  
ANISOU 2825  O   GLY A1125    10938   8769   9244     11    649   -124       O  
ATOM   2826  N   LEU A1126      29.625  35.440  -5.749  1.00 66.63           N  
ANISOU 2826  N   LEU A1126     9722   7624   7968     -2    636   -171       N  
ATOM   2827  CA  LEU A1126      29.243  36.828  -5.500  1.00 69.74           C  
ANISOU 2827  CA  LEU A1126    10113   8044   8341     50    614   -163       C  
ATOM   2828  C   LEU A1126      29.063  37.091  -4.008  1.00 68.65           C  
ANISOU 2828  C   LEU A1126     9964   7907   8212     54    600   -155       C  
ATOM   2829  O   LEU A1126      29.555  38.101  -3.491  1.00 69.31           O  
ANISOU 2829  O   LEU A1126    10083   7955   8298     73    600   -141       O  
ATOM   2830  CB  LEU A1126      27.969  37.178  -6.271  1.00 76.82           C  
ANISOU 2830  CB  LEU A1126    10986   9033   9169     83    605   -172       C  
ATOM   2831  CG  LEU A1126      27.381  38.576  -6.054  1.00 85.32           C  
ANISOU 2831  CG  LEU A1126    12082  10141  10196    177    602   -151       C  
ATOM   2832  CD1 LEU A1126      28.393  39.673  -6.380  1.00 85.46           C  
ANISOU 2832  CD1 LEU A1126    12185  10059  10229    209    624   -138       C  
ATOM   2833  CD2 LEU A1126      26.109  38.758  -6.879  1.00 89.77           C  
ANISOU 2833  CD2 LEU A1126    12595  10842  10670    230    599   -144       C  
ATOM   2834  N   VAL A1127      28.369  36.193  -3.300  1.00 68.86           N  
ANISOU 2834  N   VAL A1127     9955   7974   8235     23    592   -167       N  
ATOM   2835  CA  VAL A1127      28.239  36.325  -1.849  1.00 65.32           C  
ANISOU 2835  CA  VAL A1127     9494   7526   7800     24    579   -160       C  
ATOM   2836  C   VAL A1127      29.617  36.409  -1.203  1.00 61.56           C  
ANISOU 2836  C   VAL A1127     9032   6985   7371      8    588   -138       C  
ATOM   2837  O   VAL A1127      29.843  37.210  -0.292  1.00 63.82           O  
ANISOU 2837  O   VAL A1127     9331   7262   7656     11    579   -128       O  
ATOM   2838  CB  VAL A1127      27.402  35.161  -1.265  1.00 64.84           C  
ANISOU 2838  CB  VAL A1127     9398   7511   7726    -24    576   -177       C  
ATOM   2839  CG1 VAL A1127      27.563  35.077   0.258  1.00 61.40           C  
ANISOU 2839  CG1 VAL A1127     8952   7059   7320    -27    567   -167       C  
ATOM   2840  CG2 VAL A1127      25.924  35.327  -1.620  1.00 65.07           C  
ANISOU 2840  CG2 VAL A1127     9382   7661   7678    -18    558   -190       C  
ATOM   2841  N   ALA A1128      30.564  35.605  -1.682  1.00 59.57           N  
ANISOU 2841  N   ALA A1128     8782   6706   7146     -8    612   -126       N  
ATOM   2842  CA  ALA A1128      31.901  35.610  -1.099  1.00 60.08           C  
ANISOU 2842  CA  ALA A1128     8832   6761   7233    -15    622    -92       C  
ATOM   2843  C   ALA A1128      32.584  36.959  -1.294  1.00 64.37           C  
ANISOU 2843  C   ALA A1128     9396   7303   7759    -31    614    -83       C  
ATOM   2844  O   ALA A1128      33.187  37.497  -0.361  1.00 69.16           O  
ANISOU 2844  O   ALA A1128     9993   7929   8354    -68    607    -68       O  
ATOM   2845  CB  ALA A1128      32.739  34.478  -1.696  1.00 57.52           C  
ANISOU 2845  CB  ALA A1128     8511   6424   6920      2    663    -67       C  
ATOM   2846  N   LEU A1129      32.500  37.524  -2.501  1.00 62.26           N  
ANISOU 2846  N   LEU A1129     9166   7015   7477    -17    619    -95       N  
ATOM   2847  CA  LEU A1129      33.145  38.813  -2.761  1.00 63.61           C  
ANISOU 2847  CA  LEU A1129     9387   7167   7617    -45    623    -91       C  
ATOM   2848  C   LEU A1129      32.486  39.934  -1.977  1.00 62.01           C  
ANISOU 2848  C   LEU A1129     9250   6937   7374    -45    620   -105       C  
ATOM   2849  O   LEU A1129      33.178  40.793  -1.410  1.00 65.54           O  
ANISOU 2849  O   LEU A1129     9747   7370   7786   -109    630   -100       O  
ATOM   2850  CB  LEU A1129      33.124  39.141  -4.256  1.00 64.42           C  
ANISOU 2850  CB  LEU A1129     9525   7244   7708    -18    636   -100       C  
ATOM   2851  CG  LEU A1129      34.108  38.415  -5.161  1.00 69.73           C  
ANISOU 2851  CG  LEU A1129    10164   7929   8402    -24    651    -81       C  
ATOM   2852  CD1 LEU A1129      33.904  38.849  -6.609  1.00 75.26           C  
ANISOU 2852  CD1 LEU A1129    10907   8601   9089      3    660    -95       C  
ATOM   2853  CD2 LEU A1129      35.541  38.671  -4.721  1.00 69.09           C  
ANISOU 2853  CD2 LEU A1129    10054   7892   8306    -81    657    -47       C  
ATOM   2854  N   GLU A1130      31.151  39.954  -1.948  1.00 63.42           N  
ANISOU 2854  N   GLU A1130     9436   7120   7540     21    614   -118       N  
ATOM   2855  CA  GLU A1130      30.447  40.966  -1.167  1.00 68.01           C  
ANISOU 2855  CA  GLU A1130    10091   7678   8073     52    623   -121       C  
ATOM   2856  C   GLU A1130      30.798  40.872   0.310  1.00 67.86           C  
ANISOU 2856  C   GLU A1130    10057   7661   8064     -7    613   -117       C  
ATOM   2857  O   GLU A1130      31.003  41.897   0.974  1.00 69.66           O  
ANISOU 2857  O   GLU A1130    10379   7843   8244    -39    633   -119       O  
ATOM   2858  CB  GLU A1130      28.944  40.822  -1.367  1.00 69.53           C  
ANISOU 2858  CB  GLU A1130    10257   7924   8237    147    617   -122       C  
ATOM   2859  CG  GLU A1130      28.500  41.068  -2.794  1.00 70.40           C  
ANISOU 2859  CG  GLU A1130    10377   8057   8313    211    629   -120       C  
ATOM   2860  CD  GLU A1130      27.022  40.866  -2.946  1.00 73.13           C  
ANISOU 2860  CD  GLU A1130    10665   8513   8609    293    620   -112       C  
ATOM   2861  OE1 GLU A1130      26.435  40.182  -2.082  1.00 73.52           O  
ANISOU 2861  OE1 GLU A1130    10646   8620   8666    273    597   -116       O  
ATOM   2862  OE2 GLU A1130      26.442  41.413  -3.901  1.00 75.49           O  
ANISOU 2862  OE2 GLU A1130    10981   8856   8846    377    638    -96       O  
ATOM   2863  N   ALA A1131      30.886  39.651   0.843  1.00 62.58           N  
ANISOU 2863  N   ALA A1131     9290   7041   7448    -26    590   -113       N  
ATOM   2864  CA  ALA A1131      31.207  39.503   2.257  1.00 61.35           C  
ANISOU 2864  CA  ALA A1131     9110   6902   7301    -74    579   -105       C  
ATOM   2865  C   ALA A1131      32.649  39.906   2.532  1.00 62.74           C  
ANISOU 2865  C   ALA A1131     9289   7092   7457   -166    588    -88       C  
ATOM   2866  O   ALA A1131      32.932  40.576   3.533  1.00 62.11           O  
ANISOU 2866  O   ALA A1131     9248   7011   7338   -231    590    -89       O  
ATOM   2867  CB  ALA A1131      30.960  38.063   2.714  1.00 55.58           C  
ANISOU 2867  CB  ALA A1131     8287   6213   6618    -61    565   -100       C  
ATOM   2868  N   MET A1132      33.577  39.520   1.647  1.00 63.36           N  
ANISOU 2868  N   MET A1132     9328   7199   7547   -181    594    -71       N  
ATOM   2869  CA  MET A1132      34.982  39.814   1.886  1.00 63.68           C  
ANISOU 2869  CA  MET A1132     9340   7304   7550   -275    600    -45       C  
ATOM   2870  C   MET A1132      35.270  41.302   1.773  1.00 64.97           C  
ANISOU 2870  C   MET A1132     9623   7423   7638   -365    619    -65       C  
ATOM   2871  O   MET A1132      36.126  41.812   2.499  1.00 68.42           O  
ANISOU 2871  O   MET A1132    10064   7918   8014   -486    623    -57       O  
ATOM   2872  CB  MET A1132      35.849  39.010   0.922  1.00 63.80           C  
ANISOU 2872  CB  MET A1132     9283   7374   7586   -248    610    -13       C  
ATOM   2873  CG  MET A1132      35.801  37.502   1.168  1.00 63.05           C  
ANISOU 2873  CG  MET A1132     9106   7313   7538   -168    615     16       C  
ATOM   2874  SD  MET A1132      36.546  36.531  -0.166  1.00 69.10           S  
ANISOU 2874  SD  MET A1132     9839   8098   8317    -98    648     52       S  
ATOM   2875  CE  MET A1132      38.266  37.004   0.023  1.00 70.54           C  
ANISOU 2875  CE  MET A1132     9938   8434   8430   -166    654    111       C  
ATOM   2876  N   CYS A1133      34.552  42.021   0.903  1.00 62.77           N  
ANISOU 2876  N   CYS A1133     9454   7049   7346   -314    639    -91       N  
ATOM   2877  CA  CYS A1133      34.723  43.471   0.859  1.00 66.55           C  
ANISOU 2877  CA  CYS A1133    10095   7453   7736   -388    677   -111       C  
ATOM   2878  C   CYS A1133      34.417  44.111   2.207  1.00 65.51           C  
ANISOU 2878  C   CYS A1133    10050   7289   7552   -443    691   -123       C  
ATOM   2879  O   CYS A1133      35.001  45.146   2.550  1.00 64.50           O  
ANISOU 2879  O   CYS A1133    10051   7126   7331   -572    727   -137       O  
ATOM   2880  CB  CYS A1133      33.829  44.096  -0.217  1.00 69.31           C  
ANISOU 2880  CB  CYS A1133    10557   7706   8070   -281    707   -125       C  
ATOM   2881  SG  CYS A1133      34.382  43.773  -1.891  1.00 78.34           S  
ANISOU 2881  SG  CYS A1133    11654   8868   9244   -258    705   -118       S  
ATOM   2882  N   LEU A1134      33.521  43.511   2.988  1.00 61.09           N  
ANISOU 2882  N   LEU A1134     9433   6739   7040   -361    668   -121       N  
ATOM   2883  CA  LEU A1134      33.110  44.107   4.246  1.00 60.49           C  
ANISOU 2883  CA  LEU A1134     9444   6623   6916   -392    683   -131       C  
ATOM   2884  C   LEU A1134      33.817  43.478   5.428  1.00 57.47           C  
ANISOU 2884  C   LEU A1134     8945   6342   6548   -490    650   -118       C  
ATOM   2885  O   LEU A1134      33.514  43.824   6.568  1.00 58.50           O  
ANISOU 2885  O   LEU A1134     9128   6454   6647   -525    657   -126       O  
ATOM   2886  CB  LEU A1134      31.591  44.027   4.386  1.00 62.78           C  
ANISOU 2886  CB  LEU A1134     9757   6871   7228   -233    685   -132       C  
ATOM   2887  CG  LEU A1134      31.051  45.069   3.402  1.00 67.26           C  
ANISOU 2887  CG  LEU A1134    10483   7343   7729   -148    740   -135       C  
ATOM   2888  CD1 LEU A1134      29.794  44.634   2.684  1.00 65.19           C  
ANISOU 2888  CD1 LEU A1134    10157   7114   7495     24    728   -121       C  
ATOM   2889  CD2 LEU A1134      30.825  46.381   4.159  1.00 69.39           C  
ANISOU 2889  CD2 LEU A1134    10974   7501   7890   -166    808   -143       C  
ATOM   2890  N   GLY A1135      34.808  42.622   5.177  1.00 56.84           N  
ANISOU 2890  N   GLY A1135     8717   6378   6502   -531    623    -91       N  
ATOM   2891  CA  GLY A1135      35.637  42.082   6.232  1.00 56.87           C  
ANISOU 2891  CA  GLY A1135     8602   6510   6495   -614    601    -64       C  
ATOM   2892  C   GLY A1135      35.160  40.772   6.819  1.00 61.93           C  
ANISOU 2892  C   GLY A1135     9115   7196   7219   -508    572    -42       C  
ATOM   2893  O   GLY A1135      35.764  40.290   7.787  1.00 62.75           O  
ANISOU 2893  O   GLY A1135     9122   7409   7311   -553    559    -12       O  
ATOM   2894  N   ALA A1136      34.094  40.180   6.277  1.00 59.67           N  
ANISOU 2894  N   ALA A1136     8829   6840   7003   -378    567    -54       N  
ATOM   2895  CA  ALA A1136      33.603  38.909   6.787  1.00 60.92           C  
ANISOU 2895  CA  ALA A1136     8894   7027   7225   -298    550    -40       C  
ATOM   2896  C   ALA A1136      34.440  37.772   6.211  1.00 62.00           C  
ANISOU 2896  C   ALA A1136     8934   7235   7390   -260    558      1       C  
ATOM   2897  O   ALA A1136      34.699  37.724   5.004  1.00 60.81           O  
ANISOU 2897  O   ALA A1136     8794   7066   7244   -237    571      2       O  
ATOM   2898  CB  ALA A1136      32.124  38.726   6.446  1.00 59.32           C  
ANISOU 2898  CB  ALA A1136     8733   6750   7058   -205    546    -70       C  
ATOM   2899  N   ILE A1137      34.876  36.865   7.079  1.00 60.73           N  
ANISOU 2899  N   ILE A1137     8686   7151   7237   -241    560     39       N  
ATOM   2900  CA  ILE A1137      35.766  35.778   6.682  1.00 61.35           C  
ANISOU 2900  CA  ILE A1137     8688   7304   7318   -178    587     95       C  
ATOM   2901  C   ILE A1137      34.920  34.641   6.117  1.00 61.82           C  
ANISOU 2901  C   ILE A1137     8785   7272   7431    -81    609     81       C  
ATOM   2902  O   ILE A1137      34.055  34.104   6.823  1.00 56.94           O  
ANISOU 2902  O   ILE A1137     8182   6613   6838    -58    606     63       O  
ATOM   2903  CB  ILE A1137      36.631  35.308   7.863  1.00 65.86           C  
ANISOU 2903  CB  ILE A1137     9159   8014   7852   -180    593    155       C  
ATOM   2904  CG1 ILE A1137      37.466  36.477   8.409  1.00 67.83           C  
ANISOU 2904  CG1 ILE A1137     9373   8377   8022   -320    571    162       C  
ATOM   2905  CG2 ILE A1137      37.524  34.170   7.435  1.00 67.38           C  
ANISOU 2905  CG2 ILE A1137     9285   8287   8028    -73    638    228       C  
ATOM   2906  CD1 ILE A1137      38.134  36.204   9.764  1.00 65.48           C  
ANISOU 2906  CD1 ILE A1137     8969   8240   7672   -350    567    215       C  
ATOM   2907  N   PRO A1138      35.113  34.257   4.856  1.00 66.31           N  
ANISOU 2907  N   PRO A1138     9380   7809   8008    -38    634     85       N  
ATOM   2908  CA  PRO A1138      34.258  33.223   4.267  1.00 63.47           C  
ANISOU 2908  CA  PRO A1138     9080   7359   7678     18    662     62       C  
ATOM   2909  C   PRO A1138      34.685  31.830   4.678  1.00 60.15           C  
ANISOU 2909  C   PRO A1138     8660   6947   7247     97    719    111       C  
ATOM   2910  O   PRO A1138      35.869  31.549   4.877  1.00 60.92           O  
ANISOU 2910  O   PRO A1138     8702   7133   7311    151    749    181       O  
ATOM   2911  CB  PRO A1138      34.441  33.429   2.759  1.00 66.88           C  
ANISOU 2911  CB  PRO A1138     9547   7756   8107     24    673     50       C  
ATOM   2912  CG  PRO A1138      35.805  33.999   2.634  1.00 68.31           C  
ANISOU 2912  CG  PRO A1138     9668   8030   8256     12    675     98       C  
ATOM   2913  CD  PRO A1138      36.055  34.826   3.877  1.00 65.89           C  
ANISOU 2913  CD  PRO A1138     9313   7798   7926    -59    640    104       C  
ATOM   2914  N   ILE A1139      33.688  30.967   4.838  1.00 58.56           N  
ANISOU 2914  N   ILE A1139     8527   6665   7058    105    739     79       N  
ATOM   2915  CA  ILE A1139      33.862  29.526   4.991  1.00 59.18           C  
ANISOU 2915  CA  ILE A1139     8672   6700   7113    179    817    114       C  
ATOM   2916  C   ILE A1139      33.028  28.913   3.876  1.00 62.01           C  
ANISOU 2916  C   ILE A1139     9145   6952   7464    148    849     62       C  
ATOM   2917  O   ILE A1139      31.792  28.979   3.907  1.00 64.71           O  
ANISOU 2917  O   ILE A1139     9513   7263   7810     67    819     -1       O  
ATOM   2918  CB  ILE A1139      33.414  29.019   6.365  1.00 60.98           C  
ANISOU 2918  CB  ILE A1139     8900   6928   7342    183    821    117       C  
ATOM   2919  CG1 ILE A1139      34.086  29.804   7.494  1.00 66.69           C  
ANISOU 2919  CG1 ILE A1139     9502   7770   8067    181    776    156       C  
ATOM   2920  CG2 ILE A1139      33.717  27.553   6.518  1.00 56.58           C  
ANISOU 2920  CG2 ILE A1139     8440   6312   6744    275    921    162       C  
ATOM   2921  CD1 ILE A1139      33.631  29.359   8.878  1.00 68.25           C  
ANISOU 2921  CD1 ILE A1139     9692   7972   8267    185    776    159       C  
ATOM   2922  N   ALA A1140      33.689  28.356   2.866  1.00 59.11           N  
ANISOU 2922  N   ALA A1140     8841   6548   7071    205    911     91       N  
ATOM   2923  CA  ALA A1140      33.020  28.036   1.618  1.00 59.91           C  
ANISOU 2923  CA  ALA A1140     9039   6567   7157    151    933     39       C  
ATOM   2924  C   ALA A1140      33.432  26.666   1.107  1.00 66.38           C  
ANISOU 2924  C   ALA A1140    10011   7289   7921    217   1048     69       C  
ATOM   2925  O   ALA A1140      34.527  26.176   1.390  1.00 69.99           O  
ANISOU 2925  O   ALA A1140    10478   7762   8354    346   1113    150       O  
ATOM   2926  CB  ALA A1140      33.323  29.078   0.542  1.00 57.83           C  
ANISOU 2926  CB  ALA A1140     8717   6341   6914    134    885     28       C  
ATOM   2927  N   SER A1141      32.546  26.067   0.314  1.00 66.96           N  
ANISOU 2927  N   SER A1141    10212   7273   7958    129   1082      8       N  
ATOM   2928  CA  SER A1141      32.914  24.864  -0.419  1.00 68.95           C  
ANISOU 2928  CA  SER A1141    10650   7407   8143    174   1204     27       C  
ATOM   2929  C   SER A1141      33.938  25.203  -1.494  1.00 70.09           C  
ANISOU 2929  C   SER A1141    10769   7568   8293    260   1219     71       C  
ATOM   2930  O   SER A1141      33.871  26.260  -2.135  1.00 68.14           O  
ANISOU 2930  O   SER A1141    10411   7390   8091    212   1135     45       O  
ATOM   2931  CB  SER A1141      31.689  24.216  -1.056  1.00 66.48           C  
ANISOU 2931  CB  SER A1141    10481   7009   7769     15   1234    -58       C  
ATOM   2932  OG  SER A1141      30.737  23.871  -0.073  1.00 69.42           O  
ANISOU 2932  OG  SER A1141    10874   7382   8123    -77   1223    -98       O  
ATOM   2933  N   ALA A1142      34.907  24.304  -1.671  1.00 71.97           N  
ANISOU 2933  N   ALA A1142    11119   7748   8477    401   1333    146       N  
ATOM   2934  CA  ALA A1142      35.912  24.435  -2.724  1.00 74.39           C  
ANISOU 2934  CA  ALA A1142    11423   8071   8772    497   1367    197       C  
ATOM   2935  C   ALA A1142      35.279  23.952  -4.026  1.00 72.98           C  
ANISOU 2935  C   ALA A1142    11410   7765   8553    402   1414    130       C  
ATOM   2936  O   ALA A1142      35.419  22.801  -4.445  1.00 74.68           O  
ANISOU 2936  O   ALA A1142    11843   7846   8687    448   1545    146       O  
ATOM   2937  CB  ALA A1142      37.173  23.656  -2.375  1.00 76.04           C  
ANISOU 2937  CB  ALA A1142    11680   8292   8919    710   1480    317       C  
ATOM   2938  N   VAL A1143      34.527  24.853  -4.654  1.00 69.05           N  
ANISOU 2938  N   VAL A1143    10821   7314   8101    263   1312     55       N  
ATOM   2939  CA  VAL A1143      33.845  24.572  -5.910  1.00 68.04           C  
ANISOU 2939  CA  VAL A1143    10810   7112   7932    147   1334    -13       C  
ATOM   2940  C   VAL A1143      33.867  25.843  -6.743  1.00 71.99           C  
ANISOU 2940  C   VAL A1143    11153   7709   8492    115   1231    -33       C  
ATOM   2941  O   VAL A1143      33.482  26.914  -6.257  1.00 74.95           O  
ANISOU 2941  O   VAL A1143    11367   8187   8923     77   1125    -52       O  
ATOM   2942  CB  VAL A1143      32.397  24.086  -5.700  1.00 71.44           C  
ANISOU 2942  CB  VAL A1143    11326   7506   8312    -36   1331   -101       C  
ATOM   2943  CG1 VAL A1143      32.381  22.636  -5.208  1.00 69.30           C  
ANISOU 2943  CG1 VAL A1143    11290   7090   7952    -28   1469    -90       C  
ATOM   2944  CG2 VAL A1143      31.672  24.978  -4.712  1.00 77.18           C  
ANISOU 2944  CG2 VAL A1143    11873   8355   9098    -93   1214   -127       C  
ATOM   2945  N   GLY A1144      34.362  25.734  -7.975  1.00 70.57           N  
ANISOU 2945  N   GLY A1144    11035   7488   8291    144   1272    -24       N  
ATOM   2946  CA  GLY A1144      34.167  26.776  -8.970  1.00 63.74           C  
ANISOU 2946  CA  GLY A1144    10067   6690   7462     90   1191    -58       C  
ATOM   2947  C   GLY A1144      34.690  28.136  -8.554  1.00 66.11           C  
ANISOU 2947  C   GLY A1144    10173   7108   7837    141   1094    -27       C  
ATOM   2948  O   GLY A1144      35.860  28.307  -8.170  1.00 73.68           O  
ANISOU 2948  O   GLY A1144    11072   8110   8814    252   1107     46       O  
ATOM   2949  N   GLY A1145      33.810  29.132  -8.659  1.00 67.85           N  
ANISOU 2949  N   GLY A1145    10301   7395   8085     55   1003    -80       N  
ATOM   2950  CA  GLY A1145      34.209  30.498  -8.373  1.00 72.24           C  
ANISOU 2950  CA  GLY A1145    10719   8037   8693     83    925    -61       C  
ATOM   2951  C   GLY A1145      34.713  30.684  -6.956  1.00 79.98           C  
ANISOU 2951  C   GLY A1145    11629   9063   9697    126    909    -19       C  
ATOM   2952  O   GLY A1145      35.531  31.574  -6.697  1.00 86.47           O  
ANISOU 2952  O   GLY A1145    12364   9951  10540    154    875     16       O  
ATOM   2953  N   LEU A1146      34.228  29.864  -6.018  1.00 75.83           N  
ANISOU 2953  N   LEU A1146    11146   8510   9157    115    935    -25       N  
ATOM   2954  CA  LEU A1146      34.722  29.957  -4.651  1.00 74.42           C  
ANISOU 2954  CA  LEU A1146    10900   8381   8995    160    925     19       C  
ATOM   2955  C   LEU A1146      36.184  29.543  -4.579  1.00 76.95           C  
ANISOU 2955  C   LEU A1146    11208   8733   9296    276    983    105       C  
ATOM   2956  O   LEU A1146      36.975  30.167  -3.861  1.00 75.74           O  
ANISOU 2956  O   LEU A1146    10945   8684   9150    303    952    152       O  
ATOM   2957  CB  LEU A1146      33.859  29.109  -3.717  1.00 74.78           C  
ANISOU 2957  CB  LEU A1146    11004   8385   9024    127    946     -6       C  
ATOM   2958  CG  LEU A1146      32.382  29.511  -3.654  1.00 74.42           C  
ANISOU 2958  CG  LEU A1146    10943   8356   8978     16    887    -79       C  
ATOM   2959  CD1 LEU A1146      31.590  28.561  -2.762  1.00 77.44           C  
ANISOU 2959  CD1 LEU A1146    11387   8706   9330    -31    916   -102       C  
ATOM   2960  CD2 LEU A1146      32.245  30.929  -3.175  1.00 70.40           C  
ANISOU 2960  CD2 LEU A1146    10315   7928   8508     10    802    -83       C  
ATOM   2961  N   ARG A1147      36.563  28.499  -5.324  1.00 82.07           N  
ANISOU 2961  N   ARG A1147    11972   9309   9904    343   1074    132       N  
ATOM   2962  CA  ARG A1147      37.977  28.162  -5.454  1.00 89.79           C  
ANISOU 2962  CA  ARG A1147    12929  10341  10845    482   1136    228       C  
ATOM   2963  C   ARG A1147      38.745  29.306  -6.094  1.00 86.09           C  
ANISOU 2963  C   ARG A1147    12338   9977  10394    469   1078    246       C  
ATOM   2964  O   ARG A1147      39.884  29.592  -5.708  1.00 87.59           O  
ANISOU 2964  O   ARG A1147    12419  10303  10558    535   1079    323       O  
ATOM   2965  CB  ARG A1147      38.160  26.895  -6.287  1.00 99.95           C  
ANISOU 2965  CB  ARG A1147    14396  11508  12073    564   1257    251       C  
ATOM   2966  CG  ARG A1147      37.685  25.621  -5.638  1.00108.80           C  
ANISOU 2966  CG  ARG A1147    15678  12516  13144    594   1349    252       C  
ATOM   2967  CD  ARG A1147      38.258  24.409  -6.364  1.00116.29           C  
ANISOU 2967  CD  ARG A1147    16823  13351  14008    720   1497    306       C  
ATOM   2968  NE  ARG A1147      38.168  24.547  -7.816  1.00121.41           N  
ANISOU 2968  NE  ARG A1147    17534  13941  14654    668   1502    266       N  
ATOM   2969  CZ  ARG A1147      37.207  24.013  -8.564  1.00126.23           C  
ANISOU 2969  CZ  ARG A1147    18315  14413  15233    542   1537    183       C  
ATOM   2970  NH1 ARG A1147      36.246  23.290  -8.000  1.00129.25           N  
ANISOU 2970  NH1 ARG A1147    18829  14702  15578    446   1574    129       N  
ATOM   2971  NH2 ARG A1147      37.213  24.197  -9.880  1.00125.99           N  
ANISOU 2971  NH2 ARG A1147    18322  14350  15197    501   1538    153       N  
ATOM   2972  N   ASP A1148      38.143  29.969  -7.084  1.00 82.33           N  
ANISOU 2972  N   ASP A1148    11877   9456   9948    380   1031    178       N  
ATOM   2973  CA  ASP A1148      38.859  31.055  -7.754  1.00 84.21           C  
ANISOU 2973  CA  ASP A1148    12027   9775  10196    362    986    191       C  
ATOM   2974  C   ASP A1148      39.084  32.247  -6.835  1.00 85.74           C  
ANISOU 2974  C   ASP A1148    12099  10077  10403    295    911    192       C  
ATOM   2975  O   ASP A1148      40.060  32.987  -7.005  1.00 89.12           O  
ANISOU 2975  O   ASP A1148    12445  10610  10807    283    893    230       O  
ATOM   2976  CB  ASP A1148      38.105  31.505  -9.002  1.00 84.79           C  
ANISOU 2976  CB  ASP A1148    12154   9773  10291    292    960    121       C  
ATOM   2977  CG  ASP A1148      38.054  30.437 -10.056  1.00 88.42           C  
ANISOU 2977  CG  ASP A1148    12737  10135  10722    336   1037    120       C  
ATOM   2978  OD1 ASP A1148      39.026  29.660 -10.154  1.00 90.34           O  
ANISOU 2978  OD1 ASP A1148    13014  10385  10926    447   1114    192       O  
ATOM   2979  OD2 ASP A1148      37.038  30.366 -10.777  1.00 90.71           O  
ANISOU 2979  OD2 ASP A1148    13096  10356  11014    261   1027     52       O  
ATOM   2980  N   ILE A1149      38.194  32.454  -5.872  1.00 82.74           N  
ANISOU 2980  N   ILE A1149    11717   9675  10047    239    872    150       N  
ATOM   2981  CA  ILE A1149      38.220  33.656  -5.049  1.00 78.11           C  
ANISOU 2981  CA  ILE A1149    11054   9159   9465    160    808    137       C  
ATOM   2982  C   ILE A1149      39.018  33.441  -3.775  1.00 77.99           C  
ANISOU 2982  C   ILE A1149    10955   9258   9419    183    815    200       C  
ATOM   2983  O   ILE A1149      39.876  34.253  -3.420  1.00 76.49           O  
ANISOU 2983  O   ILE A1149    10682   9190   9192    131    790    230       O  
ATOM   2984  CB  ILE A1149      36.772  34.089  -4.743  1.00 76.01           C  
ANISOU 2984  CB  ILE A1149    10833   8818   9231    100    765     63       C  
ATOM   2985  CG1 ILE A1149      36.088  34.558  -6.026  1.00 77.26           C  
ANISOU 2985  CG1 ILE A1149    11045   8914   9398     78    752     14       C  
ATOM   2986  CG2 ILE A1149      36.732  35.153  -3.653  1.00 70.85           C  
ANISOU 2986  CG2 ILE A1149    10135   8213   8571     35    718     54       C  
ATOM   2987  CD1 ILE A1149      34.613  34.818  -5.867  1.00 78.32           C  
ANISOU 2987  CD1 ILE A1149    11208   9011   9538     46    721    -44       C  
ATOM   2988  N   ILE A1150      38.762  32.337  -3.085  1.00 79.73           N  
ANISOU 2988  N   ILE A1150    11201   9453   9640    252    855    221       N  
ATOM   2989  CA  ILE A1150      39.208  32.159  -1.710  1.00 83.22           C  
ANISOU 2989  CA  ILE A1150    11567   9997  10056    272    855    271       C  
ATOM   2990  C   ILE A1150      40.505  31.362  -1.686  1.00 87.56           C  
ANISOU 2990  C   ILE A1150    12061  10667  10541    400    923    378       C  
ATOM   2991  O   ILE A1150      40.633  30.338  -2.367  1.00 88.80           O  
ANISOU 2991  O   ILE A1150    12302  10756  10683    513    999    409       O  
ATOM   2992  CB  ILE A1150      38.113  31.475  -0.871  1.00 78.53           C  
ANISOU 2992  CB  ILE A1150    11036   9310   9493    277    861    234       C  
ATOM   2993  CG1 ILE A1150      36.827  32.304  -0.924  1.00 69.68           C  
ANISOU 2993  CG1 ILE A1150     9950   8108   8416    171    797    143       C  
ATOM   2994  CG2 ILE A1150      38.562  31.304   0.565  1.00 79.76           C  
ANISOU 2994  CG2 ILE A1150    11111   9571   9622    301    861    286       C  
ATOM   2995  CD1 ILE A1150      35.631  31.611  -0.395  1.00 66.47           C  
ANISOU 2995  CD1 ILE A1150     9607   7620   8030    161    803    100       C  
ATOM   2996  N   THR A1151      41.465  31.843  -0.902  1.00 91.64           N  
ANISOU 2996  N   THR A1151    12441  11375  11002    382    902    440       N  
ATOM   2997  CA  THR A1151      42.734  31.183  -0.632  1.00 97.10           C  
ANISOU 2997  CA  THR A1151    13037  12251  11606    513    962    561       C  
ATOM   2998  C   THR A1151      42.828  30.866   0.859  1.00105.26           C  
ANISOU 2998  C   THR A1151    13999  13387  12608    540    964    606       C  
ATOM   2999  O   THR A1151      41.972  31.261   1.657  1.00105.49           O  
ANISOU 2999  O   THR A1151    14050  13344  12687    440    912    537       O  
ATOM   3000  CB  THR A1151      43.914  32.058  -1.065  1.00 96.10           C  
ANISOU 3000  CB  THR A1151    12777  12330  11408    451    935    608       C  
ATOM   3001  OG1 THR A1151      43.989  33.207  -0.214  1.00 97.61           O  
ANISOU 3001  OG1 THR A1151    12882  12629  11578    274    860    576       O  
ATOM   3002  CG2 THR A1151      43.744  32.513  -2.508  1.00 93.26           C  
ANISOU 3002  CG2 THR A1151    12492  11858  11087    407    925    554       C  
ATOM   3003  N   ASN A1152      43.902  30.164   1.235  1.00110.74           N  
ANISOU 3003  N   ASN A1152    14600  14268  13206    689   1027    730       N  
ATOM   3004  CA  ASN A1152      44.085  29.726   2.617  1.00112.71           C  
ANISOU 3004  CA  ASN A1152    14777  14636  13410    749   1043    790       C  
ATOM   3005  C   ASN A1152      44.281  30.887   3.580  1.00110.34           C  
ANISOU 3005  C   ASN A1152    14334  14503  13087    562    951    768       C  
ATOM   3006  O   ASN A1152      44.094  30.711   4.789  1.00111.71           O  
ANISOU 3006  O   ASN A1152    14469  14726  13251    561    942    781       O  
ATOM   3007  CB  ASN A1152      45.281  28.780   2.719  1.00117.91           C  
ANISOU 3007  CB  ASN A1152    15356  15497  13947    975   1141    948       C  
ATOM   3008  CG  ASN A1152      46.583  29.440   2.299  1.00121.97           C  
ANISOU 3008  CG  ASN A1152    15684  16302  14357    949   1122   1028       C  
ATOM   3009  OD1 ASN A1152      46.953  29.415   1.122  1.00123.84           O  
ANISOU 3009  OD1 ASN A1152    15951  16519  14584    995   1150   1042       O  
ATOM   3010  ND2 ASN A1152      47.285  30.034   3.259  1.00122.70           N  
ANISOU 3010  ND2 ASN A1152    15582  16679  14361    862   1074   1079       N  
ATOM   3011  N   GLU A1153      44.678  32.052   3.083  1.00106.83           N  
ANISOU 3011  N   GLU A1153    13827  14142  12621    398    891    734       N  
ATOM   3012  CA  GLU A1153      44.860  33.229   3.916  1.00103.27           C  
ANISOU 3012  CA  GLU A1153    13286  13825  12129    189    816    701       C  
ATOM   3013  C   GLU A1153      43.679  34.185   3.855  1.00 95.11           C  
ANISOU 3013  C   GLU A1153    12387  12560  11191     24    755    564       C  
ATOM   3014  O   GLU A1153      43.720  35.240   4.495  1.00 92.96           O  
ANISOU 3014  O   GLU A1153    12090  12350  10880   -158    705    525       O  
ATOM   3015  CB  GLU A1153      46.136  33.958   3.507  1.00109.51           C  
ANISOU 3015  CB  GLU A1153    13933  14879  12796     89    802    757       C  
ATOM   3016  CG  GLU A1153      46.219  34.224   2.022  1.00113.90           C  
ANISOU 3016  CG  GLU A1153    14559  15337  13381     87    811    728       C  
ATOM   3017  CD  GLU A1153      47.447  35.018   1.659  1.00118.29           C  
ANISOU 3017  CD  GLU A1153    14978  16160  13808    -42    794    776       C  
ATOM   3018  OE1 GLU A1153      47.415  35.726   0.629  1.00120.53           O  
ANISOU 3018  OE1 GLU A1153    15330  16354  14111   -138    776    719       O  
ATOM   3019  OE2 GLU A1153      48.439  34.939   2.413  1.00119.35           O  
ANISOU 3019  OE2 GLU A1153    14930  16611  13809    -54    799    873       O  
ATOM   3020  N   THR A1154      42.629  33.846   3.103  1.00 91.44           N  
ANISOU 3020  N   THR A1154    12071  11842  10831     85    766    497       N  
ATOM   3021  CA  THR A1154      41.466  34.713   2.960  1.00 92.70           C  
ANISOU 3021  CA  THR A1154    12350  11806  11065    -33    718    383       C  
ATOM   3022  C   THR A1154      40.164  33.954   3.175  1.00 93.57           C  
ANISOU 3022  C   THR A1154    12563  11724  11264     46    728    335       C  
ATOM   3023  O   THR A1154      39.124  34.339   2.637  1.00 95.95           O  
ANISOU 3023  O   THR A1154    12966  11863  11625      9    706    256       O  
ATOM   3024  CB  THR A1154      41.448  35.390   1.591  1.00 96.94           C  
ANISOU 3024  CB  THR A1154    12952  12263  11617    -82    710    340       C  
ATOM   3025  OG1 THR A1154      41.514  34.391   0.565  1.00100.44           O  
ANISOU 3025  OG1 THR A1154    13427  12647  12088     62    760    369       O  
ATOM   3026  CG2 THR A1154      42.619  36.345   1.447  1.00 97.03           C  
ANISOU 3026  CG2 THR A1154    12880  12456  11530   -211    695    369       C  
ATOM   3027  N   GLY A1155      40.192  32.882   3.946  1.00 90.05           N  
ANISOU 3027  N   GLY A1155    12094  11308  10814    154    765    385       N  
ATOM   3028  CA  GLY A1155      38.986  32.135   4.221  1.00 85.59           C  
ANISOU 3028  CA  GLY A1155    11631  10575  10314    202    779    338       C  
ATOM   3029  C   GLY A1155      39.310  30.683   4.500  1.00 84.82           C  
ANISOU 3029  C   GLY A1155    11551  10487  10190    362    860    412       C  
ATOM   3030  O   GLY A1155      40.469  30.289   4.593  1.00 89.21           O  
ANISOU 3030  O   GLY A1155    12025  11198  10674    459    905    510       O  
ATOM   3031  N   ILE A1156      38.249  29.893   4.638  1.00 78.73           N  
ANISOU 3031  N   ILE A1156    10896   9557   9461    390    886    367       N  
ATOM   3032  CA  ILE A1156      38.353  28.476   4.957  1.00 75.04           C  
ANISOU 3032  CA  ILE A1156    10504   9048   8961    532    980    424       C  
ATOM   3033  C   ILE A1156      37.571  27.706   3.907  1.00 73.64           C  
ANISOU 3033  C   ILE A1156    10500   8679   8802    544   1034    372       C  
ATOM   3034  O   ILE A1156      36.363  27.918   3.750  1.00 71.31           O  
ANISOU 3034  O   ILE A1156    10267   8274   8554    433    992    279       O  
ATOM   3035  CB  ILE A1156      37.824  28.157   6.365  1.00 76.78           C  
ANISOU 3035  CB  ILE A1156    10718   9265   9189    527    972    419       C  
ATOM   3036  CG1 ILE A1156      38.658  28.865   7.429  1.00 77.88           C  
ANISOU 3036  CG1 ILE A1156    10687   9612   9294    505    925    475       C  
ATOM   3037  CG2 ILE A1156      37.820  26.660   6.611  1.00 76.21           C  
ANISOU 3037  CG2 ILE A1156    10770   9112   9075    672   1085    470       C  
ATOM   3038  CD1 ILE A1156      38.267  28.483   8.838  1.00 79.10           C  
ANISOU 3038  CD1 ILE A1156    10828   9777   9448    518    925    483       C  
ATOM   3039  N   LEU A1157      38.254  26.822   3.188  1.00 74.87           N  
ANISOU 3039  N   LEU A1157    10733   8809   8904    675   1131    435       N  
ATOM   3040  CA  LEU A1157      37.629  26.016   2.152  1.00 73.42           C  
ANISOU 3040  CA  LEU A1157    10738   8443   8715    675   1199    390       C  
ATOM   3041  C   LEU A1157      37.354  24.616   2.681  1.00 75.28           C  
ANISOU 3041  C   LEU A1157    11145   8561   8896    764   1313    415       C  
ATOM   3042  O   LEU A1157      38.201  24.013   3.344  1.00 76.50           O  
ANISOU 3042  O   LEU A1157    11291   8785   8991    925   1388    516       O  
ATOM   3043  CB  LEU A1157      38.510  25.951   0.905  1.00 69.72           C  
ANISOU 3043  CB  LEU A1157    10288   7991   8212    757   1247    437       C  
ATOM   3044  CG  LEU A1157      38.577  27.201   0.027  1.00 67.67           C  
ANISOU 3044  CG  LEU A1157     9926   7787   7999    649   1153    391       C  
ATOM   3045  CD1 LEU A1157      39.646  27.009  -1.032  1.00 72.01           C  
ANISOU 3045  CD1 LEU A1157    10480   8379   8501    757   1212    459       C  
ATOM   3046  CD2 LEU A1157      37.225  27.490  -0.626  1.00 62.81           C  
ANISOU 3046  CD2 LEU A1157     9392   7036   7436    502   1104    274       C  
ATOM   3047  N   VAL A1158      36.161  24.103   2.384  1.00 76.56           N  
ANISOU 3047  N   VAL A1158    11466   8560   9065    655   1332    325       N  
ATOM   3048  CA  VAL A1158      35.730  22.785   2.820  1.00 78.98           C  
ANISOU 3048  CA  VAL A1158    11977   8724   9307    692   1447    328       C  
ATOM   3049  C   VAL A1158      35.318  21.978   1.602  1.00 80.64           C  
ANISOU 3049  C   VAL A1158    12416   8762   9462    647   1540    282       C  
ATOM   3050  O   VAL A1158      34.976  22.520   0.548  1.00 80.66           O  
ANISOU 3050  O   VAL A1158    12395   8758   9493    541   1485    223       O  
ATOM   3051  CB  VAL A1158      34.558  22.842   3.826  1.00 80.08           C  
ANISOU 3051  CB  VAL A1158    12107   8841   9480    556   1389    254       C  
ATOM   3052  CG1 VAL A1158      34.854  23.818   4.924  1.00 81.01           C  
ANISOU 3052  CG1 VAL A1158    12001   9122   9656    565   1284    281       C  
ATOM   3053  CG2 VAL A1158      33.255  23.214   3.111  1.00 79.24           C  
ANISOU 3053  CG2 VAL A1158    12027   8681   9399    350   1321    136       C  
ATOM   3054  N   LYS A1159      35.344  20.661   1.771  1.00 85.69           N  
ANISOU 3054  N   LYS A1159    13294   9255  10007    725   1690    312       N  
ATOM   3055  CA  LYS A1159      34.823  19.756   0.761  1.00 85.82           C  
ANISOU 3055  CA  LYS A1159    13581   9082   9945    647   1798    258       C  
ATOM   3056  C   LYS A1159      33.312  19.911   0.682  1.00 82.51           C  
ANISOU 3056  C   LYS A1159    13185   8624   9541    378   1724    125       C  
ATOM   3057  O   LYS A1159      32.621  19.875   1.702  1.00 84.06           O  
ANISOU 3057  O   LYS A1159    13350   8839   9750    302   1686     93       O  
ATOM   3058  CB  LYS A1159      35.205  18.319   1.108  1.00 91.64           C  
ANISOU 3058  CB  LYS A1159    14603   9657  10558    797   1995    325       C  
ATOM   3059  CG  LYS A1159      34.417  17.258   0.378  1.00 96.60           C  
ANISOU 3059  CG  LYS A1159    15567  10057  11078    657   2121    248       C  
ATOM   3060  CD  LYS A1159      34.839  15.862   0.823  1.00101.97           C  
ANISOU 3060  CD  LYS A1159    16565  10557  11621    824   2336    322       C  
ATOM   3061  CE  LYS A1159      34.019  14.787   0.130  1.00106.13           C  
ANISOU 3061  CE  LYS A1159    17471  10838  12017    646   2477    234       C  
ATOM   3062  NZ  LYS A1159      34.509  13.421   0.466  1.00110.69           N  
ANISOU 3062  NZ  LYS A1159    18412  11206  12440    831   2715    313       N  
ATOM   3063  N   ALA A1160      32.801  20.106  -0.526  1.00 80.17           N  
ANISOU 3063  N   ALA A1160    12928   8299   9235    238   1700     54       N  
ATOM   3064  CA  ALA A1160      31.377  20.346  -0.692  1.00 74.85           C  
ANISOU 3064  CA  ALA A1160    12234   7649   8557    -13   1621    -60       C  
ATOM   3065  C   ALA A1160      30.581  19.109  -0.309  1.00 73.34           C  
ANISOU 3065  C   ALA A1160    12300   7316   8250   -140   1733   -109       C  
ATOM   3066  O   ALA A1160      31.040  17.979  -0.487  1.00 79.08           O  
ANISOU 3066  O   ALA A1160    13299   7870   8877    -68   1897    -76       O  
ATOM   3067  CB  ALA A1160      31.076  20.756  -2.135  1.00 70.84           C  
ANISOU 3067  CB  ALA A1160    11715   7158   8042   -123   1584   -114       C  
ATOM   3068  N   GLY A1161      29.393  19.332   0.249  1.00 70.07           N  
ANISOU 3068  N   GLY A1161    11809   6979   7837   -324   1651   -183       N  
ATOM   3069  CA  GLY A1161      28.465  18.268   0.579  1.00 67.68           C  
ANISOU 3069  CA  GLY A1161    11729   6574   7412   -503   1740   -246       C  
ATOM   3070  C   GLY A1161      28.763  17.489   1.840  1.00 72.71           C  
ANISOU 3070  C   GLY A1161    12492   7112   8023   -398   1832   -198       C  
ATOM   3071  O   GLY A1161      28.017  16.554   2.152  1.00 78.20           O  
ANISOU 3071  O   GLY A1161    13402   7705   8605   -553   1920   -251       O  
ATOM   3072  N   ASP A1162      29.796  17.856   2.601  1.00 70.69           N  
ANISOU 3072  N   ASP A1162    12105   6900   7854   -152   1815   -100       N  
ATOM   3073  CA  ASP A1162      30.185  17.080   3.775  1.00 70.80           C  
ANISOU 3073  CA  ASP A1162    12239   6830   7832    -19   1915    -38       C  
ATOM   3074  C   ASP A1162      29.833  17.807   5.072  1.00 72.63           C  
ANISOU 3074  C   ASP A1162    12227   7211   8158    -23   1785    -37       C  
ATOM   3075  O   ASP A1162      30.617  18.647   5.544  1.00 72.08           O  
ANISOU 3075  O   ASP A1162    11928   7271   8187    136   1702     33       O  
ATOM   3076  CB  ASP A1162      31.684  16.789   3.717  1.00 71.48           C  
ANISOU 3076  CB  ASP A1162    12375   6874   7910    281   2017     90       C  
ATOM   3077  CG  ASP A1162      32.092  15.651   4.629  1.00 75.87           C  
ANISOU 3077  CG  ASP A1162    13157   7298   8373    437   2181    162       C  
ATOM   3078  OD1 ASP A1162      31.485  15.489   5.708  1.00 79.17           O  
ANISOU 3078  OD1 ASP A1162    13566   7722   8794    369   2161    137       O  
ATOM   3079  OD2 ASP A1162      33.021  14.909   4.254  1.00 80.68           O  
ANISOU 3079  OD2 ASP A1162    13963   7795   8896    642   2340    250       O  
ATOM   3080  N   PRO A1163      28.704  17.488   5.714  1.00 74.63           N  
ANISOU 3080  N   PRO A1163    12529   7453   8372   -205   1771   -109       N  
ATOM   3081  CA  PRO A1163      28.357  18.191   6.961  1.00 76.25           C  
ANISOU 3081  CA  PRO A1163    12508   7798   8665   -201   1651   -106       C  
ATOM   3082  C   PRO A1163      29.412  18.055   8.047  1.00 78.36           C  
ANISOU 3082  C   PRO A1163    12738   8066   8968     40   1692      0       C  
ATOM   3083  O   PRO A1163      29.608  18.994   8.830  1.00 77.65           O  
ANISOU 3083  O   PRO A1163    12400   8126   8977    100   1573     28       O  
ATOM   3084  CB  PRO A1163      27.035  17.530   7.384  1.00 78.29           C  
ANISOU 3084  CB  PRO A1163    12896   8015   8836   -433   1674   -194       C  
ATOM   3085  CG  PRO A1163      26.520  16.852   6.155  1.00 78.76           C  
ANISOU 3085  CG  PRO A1163    13176   7976   8774   -617   1758   -263       C  
ATOM   3086  CD  PRO A1163      27.726  16.443   5.376  1.00 78.78           C  
ANISOU 3086  CD  PRO A1163    13330   7846   8756   -431   1873   -194       C  
ATOM   3087  N   GLY A1164      30.093  16.907   8.129  1.00 78.66           N  
ANISOU 3087  N   GLY A1164    13027   7949   8912    183   1865     65       N  
ATOM   3088  CA  GLY A1164      31.119  16.738   9.147  1.00 75.37           C  
ANISOU 3088  CA  GLY A1164    12563   7568   8507    433   1913    181       C  
ATOM   3089  C   GLY A1164      32.328  17.621   8.907  1.00 75.15           C  
ANISOU 3089  C   GLY A1164    12301   7700   8552    618   1846    271       C  
ATOM   3090  O   GLY A1164      32.885  18.203   9.846  1.00 78.67           O  
ANISOU 3090  O   GLY A1164    12536   8300   9057    729   1777    335       O  
ATOM   3091  N   GLU A1165      32.741  17.744   7.645  1.00 72.53           N  
ANISOU 3091  N   GLU A1165    12004   7346   8209    636   1867    275       N  
ATOM   3092  CA  GLU A1165      33.817  18.663   7.302  1.00 77.96           C  
ANISOU 3092  CA  GLU A1165    12462   8201   8960    770   1794    348       C  
ATOM   3093  C   GLU A1165      33.419  20.109   7.586  1.00 73.80           C  
ANISOU 3093  C   GLU A1165    11639   7846   8554    639   1597    293       C  
ATOM   3094  O   GLU A1165      34.240  20.911   8.052  1.00 75.97           O  
ANISOU 3094  O   GLU A1165    11697   8291   8878    734   1525    358       O  
ATOM   3095  CB  GLU A1165      34.187  18.494   5.833  1.00 86.24           C  
ANISOU 3095  CB  GLU A1165    13623   9175   9969    789   1853    348       C  
ATOM   3096  CG  GLU A1165      35.605  18.921   5.516  1.00 96.74           C  
ANISOU 3096  CG  GLU A1165    14807  10645  11305   1002   1857    464       C  
ATOM   3097  CD  GLU A1165      36.615  17.897   5.970  1.00105.02           C  
ANISOU 3097  CD  GLU A1165    15991  11670  12244   1276   2025    601       C  
ATOM   3098  OE1 GLU A1165      36.975  17.024   5.155  1.00107.57           O  
ANISOU 3098  OE1 GLU A1165    16554  11849  12469   1386   2178    639       O  
ATOM   3099  OE2 GLU A1165      37.028  17.951   7.152  1.00109.07           O  
ANISOU 3099  OE2 GLU A1165    16379  12306  12755   1389   2014    673       O  
ATOM   3100  N   LEU A1166      32.161  20.463   7.303  1.00 66.72           N  
ANISOU 3100  N   LEU A1166    10739   6920   7690    418   1516    178       N  
ATOM   3101  CA  LEU A1166      31.714  21.827   7.542  1.00 66.91           C  
ANISOU 3101  CA  LEU A1166    10519   7091   7813    315   1349    132       C  
ATOM   3102  C   LEU A1166      31.699  22.137   9.033  1.00 69.78           C  
ANISOU 3102  C   LEU A1166    10756   7543   8215    346   1296    157       C  
ATOM   3103  O   LEU A1166      32.112  23.222   9.456  1.00 68.49           O  
ANISOU 3103  O   LEU A1166    10389   7520   8114    367   1196    180       O  
ATOM   3104  CB  LEU A1166      30.329  22.047   6.932  1.00 66.53           C  
ANISOU 3104  CB  LEU A1166    10497   7017   7764    100   1291     19       C  
ATOM   3105  CG  LEU A1166      29.825  23.494   7.085  1.00 66.05           C  
ANISOU 3105  CG  LEU A1166    10208   7100   7787     24   1136    -20       C  
ATOM   3106  CD1 LEU A1166      30.872  24.459   6.542  1.00 61.13           C  
ANISOU 3106  CD1 LEU A1166     9454   6557   7216    118   1089     28       C  
ATOM   3107  CD2 LEU A1166      28.481  23.712   6.404  1.00 65.97           C  
ANISOU 3107  CD2 LEU A1166    10205   7106   7754   -156   1086   -112       C  
ATOM   3108  N   ALA A1167      31.239  21.185   9.844  1.00 69.73           N  
ANISOU 3108  N   ALA A1167    10883   7451   8160    340   1368    153       N  
ATOM   3109  CA  ALA A1167      31.283  21.356  11.288  1.00 68.69           C  
ANISOU 3109  CA  ALA A1167    10645   7397   8056    384   1331    185       C  
ATOM   3110  C   ALA A1167      32.713  21.520  11.777  1.00 70.08           C  
ANISOU 3110  C   ALA A1167    10709   7689   8231    585   1352    303       C  
ATOM   3111  O   ALA A1167      32.993  22.379  12.625  1.00 72.47           O  
ANISOU 3111  O   ALA A1167    10815   8136   8582    590   1260    325       O  
ATOM   3112  CB  ALA A1167      30.619  20.162  11.969  1.00 70.84           C  
ANISOU 3112  CB  ALA A1167    11115   7540   8261    354   1428    165       C  
ATOM   3113  N   ASN A1168      33.630  20.698  11.267  1.00 70.93           N  
ANISOU 3113  N   ASN A1168    10940   7747   8263    749   1479    384       N  
ATOM   3114  CA  ASN A1168      35.027  20.836  11.663  1.00 72.83           C  
ANISOU 3114  CA  ASN A1168    11050   8147   8475    950   1503    512       C  
ATOM   3115  C   ASN A1168      35.572  22.207  11.296  1.00 67.77           C  
ANISOU 3115  C   ASN A1168    10168   7685   7896    899   1375    513       C  
ATOM   3116  O   ASN A1168      36.321  22.807  12.069  1.00 72.21           O  
ANISOU 3116  O   ASN A1168    10541   8437   8460    950   1322    578       O  
ATOM   3117  CB  ASN A1168      35.872  19.738  11.026  1.00 75.14           C  
ANISOU 3117  CB  ASN A1168    11526   8362   8661   1154   1672    606       C  
ATOM   3118  CG  ASN A1168      35.575  18.386  11.608  1.00 82.79           C  
ANISOU 3118  CG  ASN A1168    12749   9166   9543   1242   1824    631       C  
ATOM   3119  OD1 ASN A1168      35.127  18.284  12.755  1.00 88.14           O  
ANISOU 3119  OD1 ASN A1168    13400   9855  10233   1212   1801    619       O  
ATOM   3120  ND2 ASN A1168      35.819  17.334  10.834  1.00 83.01           N  
ANISOU 3120  ND2 ASN A1168    13042   9028   9469   1352   1988    666       N  
ATOM   3121  N   ALA A1169      35.206  22.722  10.124  1.00 62.04           N  
ANISOU 3121  N   ALA A1169     9456   6907   7210    788   1328    443       N  
ATOM   3122  CA  ALA A1169      35.696  24.038   9.721  1.00 60.10           C  
ANISOU 3122  CA  ALA A1169     9015   6808   7012    731   1218    439       C  
ATOM   3123  C   ALA A1169      35.098  25.140  10.577  1.00 64.94           C  
ANISOU 3123  C   ALA A1169     9484   7498   7693    591   1089    380       C  
ATOM   3124  O   ALA A1169      35.759  26.146  10.845  1.00 69.56           O  
ANISOU 3124  O   ALA A1169     9903   8237   8288    569   1018    407       O  
ATOM   3125  CB  ALA A1169      35.379  24.293   8.254  1.00 56.11           C  
ANISOU 3125  CB  ALA A1169     8576   6216   6527    654   1206    378       C  
ATOM   3126  N   ILE A1170      33.857  24.962  11.022  1.00 65.48           N  
ANISOU 3126  N   ILE A1170     9622   7466   7792    490   1066    302       N  
ATOM   3127  CA  ILE A1170      33.237  25.923  11.924  1.00 66.00           C  
ANISOU 3127  CA  ILE A1170     9572   7595   7911    382    961    254       C  
ATOM   3128  C   ILE A1170      33.934  25.913  13.283  1.00 69.15           C  
ANISOU 3128  C   ILE A1170     9870   8115   8290    455    960    325       C  
ATOM   3129  O   ILE A1170      34.171  26.971  13.882  1.00 70.56           O  
ANISOU 3129  O   ILE A1170     9910   8412   8489    395    878    325       O  
ATOM   3130  CB  ILE A1170      31.736  25.613  12.035  1.00 65.02           C  
ANISOU 3130  CB  ILE A1170     9543   7358   7805    271    947    164       C  
ATOM   3131  CG1 ILE A1170      31.062  25.946  10.704  1.00 61.99           C  
ANISOU 3131  CG1 ILE A1170     9204   6918   7431    179    922     96       C  
ATOM   3132  CG2 ILE A1170      31.110  26.346  13.216  1.00 63.06           C  
ANISOU 3132  CG2 ILE A1170     9195   7170   7594    202    863    134       C  
ATOM   3133  CD1 ILE A1170      29.636  25.445  10.593  1.00 64.12           C  
ANISOU 3133  CD1 ILE A1170     9569   7111   7682     63    925     17       C  
ATOM   3134  N   LEU A1171      34.286  24.725  13.785  1.00 67.63           N  
ANISOU 3134  N   LEU A1171     9757   7897   8044    584   1060    391       N  
ATOM   3135  CA  LEU A1171      35.068  24.662  15.020  1.00 65.48           C  
ANISOU 3135  CA  LEU A1171     9374   7771   7736    676   1068    477       C  
ATOM   3136  C   LEU A1171      36.443  25.296  14.829  1.00 67.34           C  
ANISOU 3136  C   LEU A1171     9446   8214   7928    735   1049    561       C  
ATOM   3137  O   LEU A1171      36.944  26.007  15.713  1.00 68.39           O  
ANISOU 3137  O   LEU A1171     9418   8522   8046    699    989    593       O  
ATOM   3138  CB  LEU A1171      35.211  23.218  15.484  1.00 63.83           C  
ANISOU 3138  CB  LEU A1171     9304   7489   7460    833   1198    542       C  
ATOM   3139  CG  LEU A1171      33.951  22.454  15.900  1.00 65.75           C  
ANISOU 3139  CG  LEU A1171     9716   7548   7717    766   1232    469       C  
ATOM   3140  CD1 LEU A1171      34.248  20.962  15.867  1.00 70.12           C  
ANISOU 3140  CD1 LEU A1171    10479   7983   8178    930   1399    536       C  
ATOM   3141  CD2 LEU A1171      33.461  22.857  17.286  1.00 60.44           C  
ANISOU 3141  CD2 LEU A1171     8943   6940   7083    700   1159    447       C  
ATOM   3142  N   LYS A1172      37.071  25.044  13.681  1.00 69.65           N  
ANISOU 3142  N   LYS A1172     9777   8501   8186    812   1103    599       N  
ATOM   3143  CA  LYS A1172      38.327  25.710  13.371  1.00 74.07           C  
ANISOU 3143  CA  LYS A1172    10174   9274   8696    843   1080    674       C  
ATOM   3144  C   LYS A1172      38.155  27.226  13.408  1.00 74.14           C  
ANISOU 3144  C   LYS A1172    10062   9355   8754    642    952    600       C  
ATOM   3145  O   LYS A1172      38.973  27.934  14.007  1.00 74.51           O  
ANISOU 3145  O   LYS A1172     9947   9613   8751    600    907    648       O  
ATOM   3146  CB  LYS A1172      38.836  25.234  12.010  1.00 77.37           C  
ANISOU 3146  CB  LYS A1172    10675   9643   9080    944   1155    710       C  
ATOM   3147  CG  LYS A1172      39.990  26.029  11.427  1.00 83.96           C  
ANISOU 3147  CG  LYS A1172    11349  10684   9868    941   1121    767       C  
ATOM   3148  CD  LYS A1172      41.336  25.567  11.944  1.00 91.76           C  
ANISOU 3148  CD  LYS A1172    12207  11927  10731   1124   1188    922       C  
ATOM   3149  CE  LYS A1172      42.452  26.190  11.115  1.00 98.10           C  
ANISOU 3149  CE  LYS A1172    12871  12930  11471   1124   1170    981       C  
ATOM   3150  NZ  LYS A1172      43.801  25.735  11.546  1.00103.67           N  
ANISOU 3150  NZ  LYS A1172    13423  13936  12029   1315   1239   1148       N  
ATOM   3151  N   ALA A1173      37.067  27.734  12.815  1.00 70.86           N  
ANISOU 3151  N   ALA A1173     9734   8771   8419    514    899    488       N  
ATOM   3152  CA  ALA A1173      36.813  29.171  12.815  1.00 68.51           C  
ANISOU 3152  CA  ALA A1173     9366   8507   8156    345    798    420       C  
ATOM   3153  C   ALA A1173      36.608  29.708  14.231  1.00 68.42           C  
ANISOU 3153  C   ALA A1173     9280   8571   8144    268    745    409       C  
ATOM   3154  O   ALA A1173      37.049  30.816  14.545  1.00 67.21           O  
ANISOU 3154  O   ALA A1173     9041   8532   7964    155    688    403       O  
ATOM   3155  CB  ALA A1173      35.600  29.490  11.940  1.00 61.97           C  
ANISOU 3155  CB  ALA A1173     8652   7497   7398    264    768    317       C  
ATOM   3156  N   LEU A1174      35.934  28.950  15.095  1.00 67.51           N  
ANISOU 3156  N   LEU A1174     9214   8387   8050    313    767    403       N  
ATOM   3157  CA  LEU A1174      35.772  29.384  16.482  1.00 70.63           C  
ANISOU 3157  CA  LEU A1174     9538   8857   8442    251    721    399       C  
ATOM   3158  C   LEU A1174      37.125  29.509  17.173  1.00 75.46           C  
ANISOU 3158  C   LEU A1174     9996   9710   8963    279    727    497       C  
ATOM   3159  O   LEU A1174      37.413  30.509  17.851  1.00 76.03           O  
ANISOU 3159  O   LEU A1174     9980   9902   9005    152    668    486       O  
ATOM   3160  CB  LEU A1174      34.869  28.410  17.244  1.00 68.96           C  
ANISOU 3160  CB  LEU A1174     9407   8535   8261    307    753    383       C  
ATOM   3161  CG  LEU A1174      34.699  28.720  18.736  1.00 70.74           C  
ANISOU 3161  CG  LEU A1174     9562   8834   8483    260    713    385       C  
ATOM   3162  CD1 LEU A1174      34.002  30.075  18.943  1.00 71.57           C  
ANISOU 3162  CD1 LEU A1174     9660   8908   8625    102    626    301       C  
ATOM   3163  CD2 LEU A1174      33.934  27.618  19.452  1.00 66.23           C  
ANISOU 3163  CD2 LEU A1174     9072   8161   7931    330    758    381       C  
ATOM   3164  N   GLU A1175      37.974  28.492  17.007  1.00 77.49           N  
ANISOU 3164  N   GLU A1175    10228  10056   9160    447    808    598       N  
ATOM   3165  CA  GLU A1175      39.298  28.542  17.618  1.00 78.30           C  
ANISOU 3165  CA  GLU A1175    10158  10442   9151    495    820    710       C  
ATOM   3166  C   GLU A1175      40.109  29.712  17.079  1.00 76.67           C  
ANISOU 3166  C   GLU A1175     9842  10397   8892    355    765    709       C  
ATOM   3167  O   GLU A1175      40.815  30.387  17.836  1.00 78.98           O  
ANISOU 3167  O   GLU A1175     9992  10916   9102    252    725    743       O  
ATOM   3168  CB  GLU A1175      40.031  27.219  17.402  1.00 83.02           C  
ANISOU 3168  CB  GLU A1175    10765  11103   9677    740    934    831       C  
ATOM   3169  CG  GLU A1175      39.440  26.069  18.200  1.00 87.85           C  
ANISOU 3169  CG  GLU A1175    11482  11595  10301    873   1004    850       C  
ATOM   3170  CD  GLU A1175      39.349  26.382  19.688  1.00 91.07           C  
ANISOU 3170  CD  GLU A1175    11784  12121  10695    809    954    856       C  
ATOM   3171  OE1 GLU A1175      40.347  26.878  20.256  1.00 93.27           O  
ANISOU 3171  OE1 GLU A1175    11873  12683  10882    786    926    931       O  
ATOM   3172  OE2 GLU A1175      38.274  26.147  20.285  1.00 91.13           O  
ANISOU 3172  OE2 GLU A1175    11894  11956  10777    769    941    785       O  
ATOM   3173  N   LEU A1176      39.998  29.987  15.780  1.00 74.19           N  
ANISOU 3173  N   LEU A1176     9601   9973   8616    332    764    666       N  
ATOM   3174  CA  LEU A1176      40.654  31.168  15.224  1.00 75.65           C  
ANISOU 3174  CA  LEU A1176     9712  10277   8753    177    714    650       C  
ATOM   3175  C   LEU A1176      40.102  32.443  15.847  1.00 74.72           C  
ANISOU 3175  C   LEU A1176     9616  10119   8654    -42    636    557       C  
ATOM   3176  O   LEU A1176      40.862  33.362  16.182  1.00 71.73           O  
ANISOU 3176  O   LEU A1176     9144   9926   8183   -197    601    569       O  
ATOM   3177  CB  LEU A1176      40.481  31.216  13.705  1.00 71.75           C  
ANISOU 3177  CB  LEU A1176     9315   9639   8308    198    729    612       C  
ATOM   3178  CG  LEU A1176      41.328  30.249  12.890  1.00 73.53           C  
ANISOU 3178  CG  LEU A1176     9516   9941   8481    386    809    711       C  
ATOM   3179  CD1 LEU A1176      40.989  30.383  11.432  1.00 75.38           C  
ANISOU 3179  CD1 LEU A1176     9862  10005   8774    378    815    654       C  
ATOM   3180  CD2 LEU A1176      42.796  30.505  13.131  1.00 74.45           C  
ANISOU 3180  CD2 LEU A1176     9434  10396   8457    387    814    822       C  
ATOM   3181  N   SER A1177      38.779  32.515  16.004  1.00 72.03           N  
ANISOU 3181  N   SER A1177     9408   9544   8416    -62    615    467       N  
ATOM   3182  CA  SER A1177      38.154  33.709  16.540  1.00 72.56           C  
ANISOU 3182  CA  SER A1177     9530   9545   8497   -236    557    383       C  
ATOM   3183  C   SER A1177      38.534  33.942  17.985  1.00 74.28           C  
ANISOU 3183  C   SER A1177     9656   9923   8647   -314    537    412       C  
ATOM   3184  O   SER A1177      38.356  35.057  18.478  1.00 72.16           O  
ANISOU 3184  O   SER A1177     9426   9645   8347   -483    500    357       O  
ATOM   3185  CB  SER A1177      36.636  33.624  16.396  1.00 72.24           C  
ANISOU 3185  CB  SER A1177     9630   9254   8563   -206    547    298       C  
ATOM   3186  OG  SER A1177      36.122  32.536  17.143  1.00 77.02           O  
ANISOU 3186  OG  SER A1177    10235   9821   9207    -97    570    318       O  
ATOM   3187  N   ARG A1178      39.089  32.937  18.661  1.00 77.76           N  
ANISOU 3187  N   ARG A1178     9986  10513   9049   -191    569    502       N  
ATOM   3188  CA  ARG A1178      39.604  33.187  20.005  1.00 80.93           C  
ANISOU 3188  CA  ARG A1178    10272  11114   9364   -273    549    541       C  
ATOM   3189  C   ARG A1178      40.761  34.192  20.023  1.00 83.82           C  
ANISOU 3189  C   ARG A1178    10529  11729   9591   -461    524    567       C  
ATOM   3190  O   ARG A1178      41.077  34.737  21.088  1.00 88.38           O  
ANISOU 3190  O   ARG A1178    11040  12458  10084   -606    496    571       O  
ATOM   3191  CB  ARG A1178      40.027  31.867  20.650  1.00 79.45           C  
ANISOU 3191  CB  ARG A1178     9985  11057   9146    -76    600    647       C  
ATOM   3192  CG  ARG A1178      38.862  30.919  20.842  1.00 78.37           C  
ANISOU 3192  CG  ARG A1178     9975  10678   9123     63    629    613       C  
ATOM   3193  CD  ARG A1178      39.181  29.784  21.797  1.00 77.48           C  
ANISOU 3193  CD  ARG A1178     9794  10676   8967    229    683    709       C  
ATOM   3194  NE  ARG A1178      38.194  28.716  21.678  1.00 76.37           N  
ANISOU 3194  NE  ARG A1178     9804  10296   8916    368    734    682       N  
ATOM   3195  CZ  ARG A1178      36.969  28.768  22.189  1.00 76.61           C  
ANISOU 3195  CZ  ARG A1178     9935  10140   9034    309    704    595       C  
ATOM   3196  NH1 ARG A1178      36.568  29.842  22.859  1.00 74.41           N  
ANISOU 3196  NH1 ARG A1178     9632   9868   8770    140    628    530       N  
ATOM   3197  NH2 ARG A1178      36.142  27.746  22.022  1.00 78.36           N  
ANISOU 3197  NH2 ARG A1178    10292  10170   9311    413    757    574       N  
ATOM   3198  N  ASER A1179      41.382  34.459  18.880  0.50 82.02           N  
ANISOU 3198  N  ASER A1179    10287  11550   9328   -481    534    581       N  
ATOM   3199  N  BSER A1179      41.389  34.452  18.880  0.50 82.03           N  
ANISOU 3199  N  BSER A1179    10286  11552   9328   -480    534    581       N  
ATOM   3200  CA ASER A1179      42.463  35.429  18.774  0.50 82.90           C  
ANISOU 3200  CA ASER A1179    10306  11897   9294   -685    513    598       C  
ATOM   3201  CA BSER A1179      42.466  35.428  18.763  0.50 82.90           C  
ANISOU 3201  CA BSER A1179    10307  11898   9295   -685    514    599       C  
ATOM   3202  C  ASER A1179      42.057  36.544  17.804  0.50 81.62           C  
ANISOU 3202  C  ASER A1179    10308  11539   9164   -835    496    497       C  
ATOM   3203  C  BSER A1179      42.055  36.548  17.806  0.50 81.62           C  
ANISOU 3203  C  BSER A1179    10309  11538   9164   -835    496    496       C  
ATOM   3204  O  ASER A1179      40.930  36.585  17.302  0.50 79.83           O  
ANISOU 3204  O  ASER A1179    10245  11020   9066   -770    496    420       O  
ATOM   3205  O  BSER A1179      40.925  36.595  17.311  0.50 79.84           O  
ANISOU 3205  O  BSER A1179    10247  11020   9067   -772    495    419       O  
ATOM   3206  CB ASER A1179      43.761  34.745  18.335  0.50 84.46           C  
ANISOU 3206  CB ASER A1179    10314  12394   9385   -571    549    728       C  
ATOM   3207  CB BSER A1179      43.762  34.763  18.291  0.50 84.47           C  
ANISOU 3207  CB BSER A1179    10317  12391   9386   -573    549    727       C  
ATOM   3208  OG ASER A1179      43.692  34.327  16.982  0.50 85.37           O  
ANISOU 3208  OG ASER A1179    10492  12375   9569   -433    581    731       O  
ATOM   3209  OG BSER A1179      44.247  33.832  19.240  0.50 85.33           O  
ANISOU 3209  OG BSER A1179    10270  12720   9431   -429    576    837       O  
ATOM   3210  N   ASP A1180      42.997  37.446  17.537  1.00 82.69           N  
ANISOU 3210  N   ASP A1180    10397  11856   9165  -1037    487    502       N  
ATOM   3211  CA  ASP A1180      42.733  38.583  16.665  1.00 81.61           C  
ANISOU 3211  CA  ASP A1180    10430  11547   9031  -1193    482    411       C  
ATOM   3212  C   ASP A1180      42.560  38.127  15.224  1.00 81.30           C  
ANISOU 3212  C   ASP A1180    10431  11372   9086  -1028    502    414       C  
ATOM   3213  O   ASP A1180      43.432  37.458  14.667  1.00 83.87           O  
ANISOU 3213  O   ASP A1180    10615  11880   9370   -927    521    501       O  
ATOM   3214  CB  ASP A1180      43.877  39.592  16.768  1.00 83.17           C  
ANISOU 3214  CB  ASP A1180    10571  11995   9035  -1474    476    420       C  
ATOM   3215  CG  ASP A1180      43.669  40.818  15.889  1.00 83.59           C  
ANISOU 3215  CG  ASP A1180    10830  11863   9069  -1646    486    327       C  
ATOM   3216  OD1 ASP A1180      42.512  41.096  15.506  1.00 83.62           O  
ANISOU 3216  OD1 ASP A1180    11034  11542   9197  -1570    494    249       O  
ATOM   3217  OD2 ASP A1180      44.670  41.503  15.593  1.00 83.63           O  
ANISOU 3217  OD2 ASP A1180    10795  12063   8919  -1858    491    338       O  
ATOM   3218  N   LEU A1181      41.442  38.515  14.616  1.00 79.18           N  
ANISOU 3218  N   LEU A1181    10356  10799   8931   -999    502    325       N  
ATOM   3219  CA  LEU A1181      41.115  38.152  13.244  1.00 76.32           C  
ANISOU 3219  CA  LEU A1181    10052  10288   8660   -860    519    315       C  
ATOM   3220  C   LEU A1181      41.340  39.299  12.262  1.00 78.94           C  
ANISOU 3220  C   LEU A1181    10492  10558   8943  -1008    522    263       C  
ATOM   3221  O   LEU A1181      41.035  39.150  11.073  1.00 80.69           O  
ANISOU 3221  O   LEU A1181    10773  10649   9235   -910    534    246       O  
ATOM   3222  CB  LEU A1181      39.658  37.677  13.164  1.00 73.01           C  
ANISOU 3222  CB  LEU A1181     9752   9600   8387   -710    519    261       C  
ATOM   3223  CG  LEU A1181      39.290  36.425  13.971  1.00 71.84           C  
ANISOU 3223  CG  LEU A1181     9532   9465   8298   -551    526    303       C  
ATOM   3224  CD1 LEU A1181      37.774  36.237  14.084  1.00 65.74           C  
ANISOU 3224  CD1 LEU A1181     8887   8452   7640   -476    519    235       C  
ATOM   3225  CD2 LEU A1181      39.948  35.197  13.364  1.00 70.64           C  
ANISOU 3225  CD2 LEU A1181     9281   9409   8150   -378    565    389       C  
ATOM   3226  N   SER A1182      41.885  40.432  12.722  1.00 78.49           N  
ANISOU 3226  N   SER A1182    10474  10594   8756  -1250    518    236       N  
ATOM   3227  CA  SER A1182      41.892  41.638  11.896  1.00 80.69           C  
ANISOU 3227  CA  SER A1182    10921  10754   8983  -1401    536    171       C  
ATOM   3228  C   SER A1182      42.753  41.465  10.649  1.00 81.58           C  
ANISOU 3228  C   SER A1182    10953  10976   9069  -1382    544    212       C  
ATOM   3229  O   SER A1182      42.421  41.989   9.580  1.00 79.68           O  
ANISOU 3229  O   SER A1182    10848  10565   8862  -1378    560    165       O  
ATOM   3230  CB  SER A1182      42.363  42.837  12.718  1.00 82.15           C  
ANISOU 3230  CB  SER A1182    11191  11018   9006  -1693    545    134       C  
ATOM   3231  OG  SER A1182      43.650  42.617  13.260  1.00 85.31           O  
ANISOU 3231  OG  SER A1182    11382  11766   9265  -1825    530    206       O  
ATOM   3232  N   LYS A1183      43.862  40.735  10.759  1.00 85.10           N  
ANISOU 3232  N   LYS A1183    11174  11714   9444  -1356    538    308       N  
ATOM   3233  CA  LYS A1183      44.694  40.500   9.584  1.00 87.58           C  
ANISOU 3233  CA  LYS A1183    11401  12147   9728  -1314    551    358       C  
ATOM   3234  C   LYS A1183      43.966  39.640   8.560  1.00 83.82           C  
ANISOU 3234  C   LYS A1183    10972  11463   9414  -1056    564    357       C  
ATOM   3235  O   LYS A1183      44.089  39.867   7.353  1.00 81.85           O  
ANISOU 3235  O   LYS A1183    10774  11144   9180  -1043    576    342       O  
ATOM   3236  CB  LYS A1183      46.018  39.850   9.984  1.00 95.70           C  
ANISOU 3236  CB  LYS A1183    12168  13565  10629  -1306    551    478       C  
ATOM   3237  CG  LYS A1183      46.948  39.595   8.802  1.00104.76           C  
ANISOU 3237  CG  LYS A1183    13209  14868  11726  -1251    569    544       C  
ATOM   3238  CD  LYS A1183      48.234  38.900   9.232  1.00111.01           C  
ANISOU 3238  CD  LYS A1183    13726  16080  12374  -1203    577    683       C  
ATOM   3239  CE  LYS A1183      49.163  38.679   8.048  1.00112.82           C  
ANISOU 3239  CE  LYS A1183    13849  16475  12540  -1139    600    756       C  
ATOM   3240  NZ  LYS A1183      50.436  38.024   8.460  1.00114.85           N  
ANISOU 3240  NZ  LYS A1183    13823  17182  12631  -1069    616    909       N  
ATOM   3241  N   PHE A1184      43.190  38.657   9.020  1.00 84.53           N  
ANISOU 3241  N   PHE A1184    11053  11449   9614   -866    566    368       N  
ATOM   3242  CA  PHE A1184      42.394  37.861   8.092  1.00 82.63           C  
ANISOU 3242  CA  PHE A1184    10883  11002   9509   -660    583    354       C  
ATOM   3243  C   PHE A1184      41.339  38.709   7.399  1.00 77.52           C  
ANISOU 3243  C   PHE A1184    10431  10091   8933   -706    576    253       C  
ATOM   3244  O   PHE A1184      41.110  38.556   6.194  1.00 79.47           O  
ANISOU 3244  O   PHE A1184    10731  10230   9235   -625    589    239       O  
ATOM   3245  CB  PHE A1184      41.740  36.682   8.815  1.00 86.13           C  
ANISOU 3245  CB  PHE A1184    11303  11389  10034   -486    594    379       C  
ATOM   3246  CG  PHE A1184      42.484  35.400   8.648  1.00 95.81           C  
ANISOU 3246  CG  PHE A1184    12404  12760  11238   -303    636    484       C  
ATOM   3247  CD1 PHE A1184      42.200  34.551   7.592  1.00 99.27           C  
ANISOU 3247  CD1 PHE A1184    12903  13068  11747   -137    676    493       C  
ATOM   3248  CD2 PHE A1184      43.485  35.051   9.536  1.00103.79           C  
ANISOU 3248  CD2 PHE A1184    13247  14047  12142   -291    647    580       C  
ATOM   3249  CE1 PHE A1184      42.898  33.370   7.428  1.00104.45           C  
ANISOU 3249  CE1 PHE A1184    13482  13838  12368     50    736    596       C  
ATOM   3250  CE2 PHE A1184      44.188  33.874   9.382  1.00108.60           C  
ANISOU 3250  CE2 PHE A1184    13755  14797  12712    -86    703    693       C  
ATOM   3251  CZ  PHE A1184      43.897  33.031   8.324  1.00108.92           C  
ANISOU 3251  CZ  PHE A1184    13884  14676  12823     91    754    701       C  
ATOM   3252  N   ARG A1185      40.677  39.603   8.138  1.00 74.67           N  
ANISOU 3252  N   ARG A1185    10183   9627   8560   -822    561    189       N  
ATOM   3253  CA  ARG A1185      39.667  40.451   7.514  1.00 72.84           C  
ANISOU 3253  CA  ARG A1185    10141   9161   8373   -834    567    109       C  
ATOM   3254  C   ARG A1185      40.298  41.397   6.507  1.00 70.82           C  
ANISOU 3254  C   ARG A1185     9955   8908   8044   -952    584     91       C  
ATOM   3255  O   ARG A1185      39.734  41.637   5.435  1.00 70.80           O  
ANISOU 3255  O   ARG A1185    10054   8752   8093   -884    597     57       O  
ATOM   3256  CB  ARG A1185      38.896  41.236   8.570  1.00 72.36           C  
ANISOU 3256  CB  ARG A1185    10202   8999   8292   -915    565     56       C  
ATOM   3257  CG  ARG A1185      38.300  40.373   9.646  1.00 71.93           C  
ANISOU 3257  CG  ARG A1185    10077   8952   8300   -819    546     72       C  
ATOM   3258  CD  ARG A1185      37.354  41.192  10.510  1.00 69.41           C  
ANISOU 3258  CD  ARG A1185     9901   8500   7970   -871    549     17       C  
ATOM   3259  NE  ARG A1185      36.889  40.471  11.688  1.00 68.70           N  
ANISOU 3259  NE  ARG A1185     9741   8439   7925   -810    529     31       N  
ATOM   3260  CZ  ARG A1185      35.960  39.519  11.676  1.00 67.79           C  
ANISOU 3260  CZ  ARG A1185     9596   8251   7912   -648    520     33       C  
ATOM   3261  NH1 ARG A1185      35.380  39.152  10.541  1.00 62.20           N  
ANISOU 3261  NH1 ARG A1185     8916   7448   7270   -536    526     20       N  
ATOM   3262  NH2 ARG A1185      35.599  38.937  12.813  1.00 71.14           N  
ANISOU 3262  NH2 ARG A1185     9966   8703   8363   -613    506     45       N  
ATOM   3263  N   GLU A1186      41.478  41.927   6.825  1.00 74.80           N  
ANISOU 3263  N   GLU A1186    10401   9601   8417  -1136    587    116       N  
ATOM   3264  CA  GLU A1186      42.158  42.791   5.869  1.00 83.67           C  
ANISOU 3264  CA  GLU A1186    11590  10743   9456  -1269    606    100       C  
ATOM   3265  C   GLU A1186      42.572  42.011   4.624  1.00 79.41           C  
ANISOU 3265  C   GLU A1186    10948  10252   8973  -1128    607    146       C  
ATOM   3266  O   GLU A1186      42.432  42.511   3.502  1.00 79.32           O  
ANISOU 3266  O   GLU A1186    11041  10123   8975  -1128    623    113       O  
ATOM   3267  CB  GLU A1186      43.367  43.458   6.526  1.00 93.34           C  
ANISOU 3267  CB  GLU A1186    12758  12202  10505  -1528    609    119       C  
ATOM   3268  CG  GLU A1186      43.796  44.737   5.829  1.00102.90           C  
ANISOU 3268  CG  GLU A1186    14130  13367  11600  -1738    642     70       C  
ATOM   3269  CD  GLU A1186      42.727  45.822   5.899  1.00110.28           C  
ANISOU 3269  CD  GLU A1186    15360  14002  12539  -1779    681    -19       C  
ATOM   3270  OE1 GLU A1186      41.939  45.832   6.876  1.00110.65           O  
ANISOU 3270  OE1 GLU A1186    15470  13953  12619  -1742    680    -41       O  
ATOM   3271  OE2 GLU A1186      42.667  46.660   4.970  1.00113.68           O  
ANISOU 3271  OE2 GLU A1186    15965  14295  12934  -1834    721    -60       O  
ATOM   3272  N   ASN A1187      43.069  40.779   4.800  1.00 76.05           N  
ANISOU 3272  N   ASN A1187    10333   9990   8573   -994    599    226       N  
ATOM   3273  CA  ASN A1187      43.396  39.948   3.643  1.00 75.48           C  
ANISOU 3273  CA  ASN A1187    10189   9939   8550   -836    613    273       C  
ATOM   3274  C   ASN A1187      42.157  39.668   2.808  1.00 71.92           C  
ANISOU 3274  C   ASN A1187     9869   9221   8235   -689    619    218       C  
ATOM   3275  O   ASN A1187      42.218  39.656   1.577  1.00 72.84           O  
ANISOU 3275  O   ASN A1187    10020   9278   8378   -639    632    212       O  
ATOM   3276  CB  ASN A1187      44.040  38.637   4.087  1.00 76.43           C  
ANISOU 3276  CB  ASN A1187    10123  10256   8660   -687    625    374       C  
ATOM   3277  CG  ASN A1187      45.402  38.837   4.695  1.00 80.63           C  
ANISOU 3277  CG  ASN A1187    10482  11121   9034   -812    621    451       C  
ATOM   3278  OD1 ASN A1187      46.082  39.824   4.419  1.00 84.16           O  
ANISOU 3278  OD1 ASN A1187    10931  11675   9372  -1012    614    436       O  
ATOM   3279  ND2 ASN A1187      45.813  37.903   5.530  1.00 84.46           N  
ANISOU 3279  ND2 ASN A1187    10816  11787   9488   -700    631    538       N  
ATOM   3280  N   CYS A1188      41.015  39.459   3.458  1.00 69.06           N  
ANISOU 3280  N   CYS A1188     9575   8715   7948   -627    609    178       N  
ATOM   3281  CA  CYS A1188      39.793  39.236   2.699  1.00 69.48           C  
ANISOU 3281  CA  CYS A1188     9737   8559   8106   -509    613    128       C  
ATOM   3282  C   CYS A1188      39.429  40.471   1.889  1.00 69.70           C  
ANISOU 3282  C   CYS A1188     9910   8460   8113   -585    619     69       C  
ATOM   3283  O   CYS A1188      39.090  40.364   0.704  1.00 70.18           O  
ANISOU 3283  O   CYS A1188    10014   8432   8218   -509    628     54       O  
ATOM   3284  CB  CYS A1188      38.665  38.828   3.645  1.00 68.04           C  
ANISOU 3284  CB  CYS A1188     9583   8286   7984   -447    600    103       C  
ATOM   3285  SG  CYS A1188      38.977  37.206   4.396  1.00 65.23           S  
ANISOU 3285  SG  CYS A1188     9090   8037   7656   -321    612    173       S  
ATOM   3286  N   LYS A1189      39.526  41.656   2.506  1.00 67.58           N  
ANISOU 3286  N   LYS A1189     9734   8180   7764   -737    622     37       N  
ATOM   3287  CA  LYS A1189      39.188  42.895   1.810  1.00 67.76           C  
ANISOU 3287  CA  LYS A1189     9936   8065   7747   -801    648    -15       C  
ATOM   3288  C   LYS A1189      40.105  43.123   0.615  1.00 71.59           C  
ANISOU 3288  C   LYS A1189    10406   8603   8192   -849    661      0       C  
ATOM   3289  O   LYS A1189      39.646  43.470  -0.483  1.00 70.23           O  
ANISOU 3289  O   LYS A1189    10329   8307   8046   -789    678    -26       O  
ATOM   3290  CB  LYS A1189      39.278  44.074   2.770  1.00 69.41           C  
ANISOU 3290  CB  LYS A1189    10275   8249   7848   -973    669    -48       C  
ATOM   3291  CG  LYS A1189      38.309  44.002   3.931  1.00 75.00           C  
ANISOU 3291  CG  LYS A1189    11023   8887   8588   -924    662    -65       C  
ATOM   3292  CD  LYS A1189      38.640  45.098   4.930  1.00 80.64           C  
ANISOU 3292  CD  LYS A1189    11864   9599   9177  -1121    689    -92       C  
ATOM   3293  CE  LYS A1189      37.688  45.119   6.086  1.00 84.50           C  
ANISOU 3293  CE  LYS A1189    12407  10010   9688  -1072    688   -109       C  
ATOM   3294  NZ  LYS A1189      38.059  46.212   7.024  1.00 86.62           N  
ANISOU 3294  NZ  LYS A1189    12827  10266   9818  -1281    726   -139       N  
ATOM   3295  N   LYS A1190      41.414  42.942   0.821  1.00 72.56           N  
ANISOU 3295  N   LYS A1190    10398   8932   8240   -956    655     48       N  
ATOM   3296  CA  LYS A1190      42.376  43.134  -0.256  1.00 73.88           C  
ANISOU 3296  CA  LYS A1190    10530   9184   8355  -1010    666     70       C  
ATOM   3297  C   LYS A1190      42.149  42.132  -1.382  1.00 72.23           C  
ANISOU 3297  C   LYS A1190    10258   8934   8252   -814    664     95       C  
ATOM   3298  O   LYS A1190      42.174  42.496  -2.557  1.00 74.61           O  
ANISOU 3298  O   LYS A1190    10625   9163   8559   -803    679     77       O  
ATOM   3299  CB  LYS A1190      43.799  43.024   0.293  1.00 78.65           C  
ANISOU 3299  CB  LYS A1190    10971  10072   8842  -1151    658    131       C  
ATOM   3300  CG  LYS A1190      44.147  44.105   1.303  1.00 85.08           C  
ANISOU 3300  CG  LYS A1190    11861  10946   9518  -1400    666    100       C  
ATOM   3301  CD  LYS A1190      45.572  43.972   1.845  1.00 93.03           C  
ANISOU 3301  CD  LYS A1190    12673  12291  10383  -1556    654    168       C  
ATOM   3302  CE  LYS A1190      46.606  44.182   0.734  1.00100.26           C  
ANISOU 3302  CE  LYS A1190    13527  13348  11218  -1629    665    199       C  
ATOM   3303  NZ  LYS A1190      48.028  44.142   1.213  1.00104.62           N  
ANISOU 3303  NZ  LYS A1190    13873  14281  11598  -1798    655    274       N  
ATOM   3304  N   ARG A1191      41.902  40.871  -1.044  1.00 72.90           N  
ANISOU 3304  N   ARG A1191    10234   9052   8412   -662    654    134       N  
ATOM   3305  CA  ARG A1191      41.667  39.865  -2.073  1.00 72.13           C  
ANISOU 3305  CA  ARG A1191    10108   8901   8398   -492    666    154       C  
ATOM   3306  C   ARG A1191      40.402  40.154  -2.866  1.00 70.76           C  
ANISOU 3306  C   ARG A1191    10072   8516   8297   -430    666     88       C  
ATOM   3307  O   ARG A1191      40.381  39.972  -4.083  1.00 73.67           O  
ANISOU 3307  O   ARG A1191    10462   8835   8694   -368    678     85       O  
ATOM   3308  CB  ARG A1191      41.597  38.480  -1.437  1.00 71.53           C  
ANISOU 3308  CB  ARG A1191     9933   8879   8366   -357    672    204       C  
ATOM   3309  CG  ARG A1191      41.145  37.415  -2.386  1.00 73.90           C  
ANISOU 3309  CG  ARG A1191    10256   9081   8740   -198    697    211       C  
ATOM   3310  CD  ARG A1191      42.138  37.226  -3.487  1.00 77.01           C  
ANISOU 3310  CD  ARG A1191    10603   9556   9100   -165    723    258       C  
ATOM   3311  NE  ARG A1191      41.681  36.205  -4.416  1.00 83.58           N  
ANISOU 3311  NE  ARG A1191    11486  10277   9993    -25    757    259       N  
ATOM   3312  CZ  ARG A1191      42.220  35.988  -5.609  1.00 86.72           C  
ANISOU 3312  CZ  ARG A1191    11885  10682  10381     25    784    283       C  
ATOM   3313  NH1 ARG A1191      43.242  36.730  -6.021  1.00 90.85           N  
ANISOU 3313  NH1 ARG A1191    12349  11330  10839    -50    777    311       N  
ATOM   3314  NH2 ARG A1191      41.728  35.036  -6.393  1.00 85.43           N  
ANISOU 3314  NH2 ARG A1191    11792  10404  10265    136    821    277       N  
ATOM   3315  N   ALA A1192      39.333  40.594  -2.203  1.00 71.75           N  
ANISOU 3315  N   ALA A1192    10285   8533   8444   -435    656     41       N  
ATOM   3316  CA  ALA A1192      38.109  40.916  -2.934  1.00 74.97           C  
ANISOU 3316  CA  ALA A1192    10804   8785   8896   -363    660     -8       C  
ATOM   3317  C   ALA A1192      38.322  42.102  -3.864  1.00 74.30           C  
ANISOU 3317  C   ALA A1192    10832   8641   8759   -424    680    -33       C  
ATOM   3318  O   ALA A1192      37.868  42.093  -5.017  1.00 75.76           O  
ANISOU 3318  O   ALA A1192    11056   8755   8972   -348    689    -47       O  
ATOM   3319  CB  ALA A1192      36.965  41.211  -1.962  1.00 78.81           C  
ANISOU 3319  CB  ALA A1192    11353   9198   9392   -345    651    -40       C  
ATOM   3320  N   MET A1193      39.003  43.138  -3.377  1.00 70.90           N  
ANISOU 3320  N   MET A1193    10466   8237   8238   -572    695    -40       N  
ATOM   3321  CA  MET A1193      39.287  44.280  -4.233  1.00 71.50           C  
ANISOU 3321  CA  MET A1193    10676   8246   8246   -647    728    -64       C  
ATOM   3322  C   MET A1193      40.149  43.862  -5.420  1.00 71.66           C  
ANISOU 3322  C   MET A1193    10613   8339   8277   -638    726    -36       C  
ATOM   3323  O   MET A1193      39.867  44.237  -6.563  1.00 70.29           O  
ANISOU 3323  O   MET A1193    10519   8076   8112   -590    744    -55       O  
ATOM   3324  CB  MET A1193      39.953  45.379  -3.407  1.00 72.97           C  
ANISOU 3324  CB  MET A1193    10960   8455   8308   -847    753    -80       C  
ATOM   3325  CG  MET A1193      39.021  45.924  -2.323  1.00 84.18           C  
ANISOU 3325  CG  MET A1193    12506   9770   9708   -845    769   -110       C  
ATOM   3326  SD  MET A1193      39.787  46.933  -1.026  1.00 96.99           S  
ANISOU 3326  SD  MET A1193    14232  11438  11180  -1101    797   -128       S  
ATOM   3327  CE  MET A1193      38.382  47.287   0.028  1.00 97.63           C  
ANISOU 3327  CE  MET A1193    14455  11363  11276  -1007    818   -156       C  
ATOM   3328  N   SER A1194      41.168  43.038  -5.173  1.00 70.91           N  
ANISOU 3328  N   SER A1194    10352   8414   8176   -661    708     15       N  
ATOM   3329  CA  SER A1194      42.052  42.580  -6.239  1.00 72.93           C  
ANISOU 3329  CA  SER A1194    10521   8759   8432   -635    713     54       C  
ATOM   3330  C   SER A1194      41.295  41.755  -7.270  1.00 72.67           C  
ANISOU 3330  C   SER A1194    10489   8624   8499   -461    714     49       C  
ATOM   3331  O   SER A1194      41.530  41.881  -8.475  1.00 75.29           O  
ANISOU 3331  O   SER A1194    10844   8928   8833   -440    726     48       O  
ATOM   3332  CB  SER A1194      43.200  41.772  -5.637  1.00 73.94           C  
ANISOU 3332  CB  SER A1194    10466   9110   8519   -651    704    128       C  
ATOM   3333  OG  SER A1194      43.953  41.149  -6.651  1.00 82.83           O  
ANISOU 3333  OG  SER A1194    11503  10320   9647   -578    717    178       O  
ATOM   3334  N   PHE A1195      40.370  40.916  -6.815  1.00 72.60           N  
ANISOU 3334  N   PHE A1195    10461   8561   8561   -353    703     43       N  
ATOM   3335  CA  PHE A1195      39.567  40.131  -7.744  1.00 71.29           C  
ANISOU 3335  CA  PHE A1195    10309   8308   8468   -225    708     30       C  
ATOM   3336  C   PHE A1195      38.670  41.027  -8.589  1.00 69.35           C  
ANISOU 3336  C   PHE A1195    10184   7941   8224   -213    711    -20       C  
ATOM   3337  O   PHE A1195      38.506  40.800  -9.792  1.00 68.36           O  
ANISOU 3337  O   PHE A1195    10072   7779   8122   -156    720    -26       O  
ATOM   3338  CB  PHE A1195      38.733  39.111  -6.970  1.00 67.31           C  
ANISOU 3338  CB  PHE A1195     9775   7784   8017   -149    700     29       C  
ATOM   3339  CG  PHE A1195      38.239  37.983  -7.813  1.00 66.73           C  
ANISOU 3339  CG  PHE A1195     9701   7662   7992    -50    716     27       C  
ATOM   3340  CD1 PHE A1195      39.027  36.857  -8.012  1.00 67.51           C  
ANISOU 3340  CD1 PHE A1195     9746   7813   8093     10    748     78       C  
ATOM   3341  CD2 PHE A1195      36.991  38.046  -8.412  1.00 67.88           C  
ANISOU 3341  CD2 PHE A1195     9909   7722   8161    -19    709    -20       C  
ATOM   3342  CE1 PHE A1195      38.581  35.817  -8.791  1.00 71.99           C  
ANISOU 3342  CE1 PHE A1195    10352   8314   8686     83    778     72       C  
ATOM   3343  CE2 PHE A1195      36.538  37.007  -9.203  1.00 72.55           C  
ANISOU 3343  CE2 PHE A1195    10510   8279   8775     35    727    -27       C  
ATOM   3344  CZ  PHE A1195      37.334  35.891  -9.395  1.00 73.12           C  
ANISOU 3344  CZ  PHE A1195    10560   8370   8851     78    765     14       C  
ATOM   3345  N   SER A1196      38.062  42.037  -7.971  1.00 71.02           N  
ANISOU 3345  N   SER A1196    10490   8093   8402   -253    712    -51       N  
ATOM   3346  CA  SER A1196      37.252  42.981  -8.731  1.00 75.71           C  
ANISOU 3346  CA  SER A1196    11211   8583   8972   -215    732    -83       C  
ATOM   3347  C   SER A1196      38.101  43.716  -9.766  1.00 75.68           C  
ANISOU 3347  C   SER A1196    11265   8566   8923   -273    756    -82       C  
ATOM   3348  O   SER A1196      37.640  44.011 -10.875  1.00 73.07           O  
ANISOU 3348  O   SER A1196    10994   8175   8595   -205    771    -94       O  
ATOM   3349  CB  SER A1196      36.586  43.972  -7.775  1.00 77.93           C  
ANISOU 3349  CB  SER A1196    11607   8799   9201   -235    748   -103       C  
ATOM   3350  OG  SER A1196      35.774  43.277  -6.850  1.00 81.40           O  
ANISOU 3350  OG  SER A1196    11985   9261   9683   -179    723   -103       O  
ATOM   3351  N   LYS A 294      39.342  44.033  -9.399  1.00 78.36           N  
ANISOU 3351  N   LYS A 294    11584   8980   9208   -406    761    -65       N  
ATOM   3352  CA  LYS A 294      40.273  44.668 -10.319  1.00 82.86           C  
ANISOU 3352  CA  LYS A 294    12197   9565   9723   -488    783    -62       C  
ATOM   3353  C   LYS A 294      40.569  43.762 -11.509  1.00 84.45           C  
ANISOU 3353  C   LYS A 294    12299   9805   9984   -399    773    -38       C  
ATOM   3354  O   LYS A 294      40.579  44.222 -12.658  1.00 84.40           O  
ANISOU 3354  O   LYS A 294    12359   9742   9967   -382    791    -50       O  
ATOM   3355  CB  LYS A 294      41.551  45.028  -9.557  1.00 91.48           C  
ANISOU 3355  CB  LYS A 294    13249  10785  10727   -669    785    -43       C  
ATOM   3356  CG  LYS A 294      42.780  45.250 -10.404  1.00101.31           C  
ANISOU 3356  CG  LYS A 294    14455  12126  11912   -764    795    -20       C  
ATOM   3357  CD  LYS A 294      44.013  45.402  -9.517  1.00107.53           C  
ANISOU 3357  CD  LYS A 294    15152  13108  12596   -946    789     11       C  
ATOM   3358  CE  LYS A 294      45.288  45.434 -10.348  1.00111.33           C  
ANISOU 3358  CE  LYS A 294    15547  13743  13010  -1030    795     49       C  
ATOM   3359  NZ  LYS A 294      46.502  45.530  -9.495  1.00112.67           N  
ANISOU 3359  NZ  LYS A 294    15594  14162  13055  -1212    787     91       N  
ATOM   3360  N   GLN A 295      40.800  42.468 -11.253  1.00 84.48           N  
ANISOU 3360  N   GLN A 295    12162   9894  10041   -335    753     -2       N  
ATOM   3361  CA  GLN A 295      40.990  41.517 -12.346  1.00 84.38           C  
ANISOU 3361  CA  GLN A 295    12088   9896  10078   -239    758     21       C  
ATOM   3362  C   GLN A 295      39.767  41.465 -13.251  1.00 78.64           C  
ANISOU 3362  C   GLN A 295    11434   9050   9398   -145    760    -19       C  
ATOM   3363  O   GLN A 295      39.898  41.399 -14.481  1.00 80.60           O  
ANISOU 3363  O   GLN A 295    11696   9275   9655   -110    771    -19       O  
ATOM   3364  CB  GLN A 295      41.290  40.118 -11.808  1.00 92.54           C  
ANISOU 3364  CB  GLN A 295    13006  11010  11144   -167    758     67       C  
ATOM   3365  CG  GLN A 295      42.367  40.041 -10.744  1.00103.37           C  
ANISOU 3365  CG  GLN A 295    14277  12538  12459   -233    756    119       C  
ATOM   3366  CD  GLN A 295      43.770  40.164 -11.289  1.00112.67           C  
ANISOU 3366  CD  GLN A 295    15378  13863  13570   -278    771    172       C  
ATOM   3367  OE1 GLN A 295      43.984  40.675 -12.390  1.00117.17           O  
ANISOU 3367  OE1 GLN A 295    15994  14397  14128   -300    779    157       O  
ATOM   3368  NE2 GLN A 295      44.745  39.693 -10.515  1.00115.52           N  
ANISOU 3368  NE2 GLN A 295    15609  14410  13874   -287    775    242       N  
ATOM   3369  N   ILE A 296      38.570  41.468 -12.662  1.00 71.45           N  
ANISOU 3369  N   ILE A 296    10558   8084   8507   -105    748    -47       N  
ATOM   3370  CA  ILE A 296      37.356  41.439 -13.478  1.00 73.55           C  
ANISOU 3370  CA  ILE A 296    10868   8286   8791    -22    748    -75       C  
ATOM   3371  C   ILE A 296      37.301  42.661 -14.386  1.00 78.39           C  
ANISOU 3371  C   ILE A 296    11583   8843   9358    -22    769    -90       C  
ATOM   3372  O   ILE A 296      36.993  42.557 -15.583  1.00 80.76           O  
ANISOU 3372  O   ILE A 296    11894   9127   9666     32    775    -96       O  
ATOM   3373  CB  ILE A 296      36.097  41.347 -12.598  1.00 73.50           C  
ANISOU 3373  CB  ILE A 296    10867   8269   8789     17    733    -94       C  
ATOM   3374  CG1 ILE A 296      36.075  40.046 -11.796  1.00 71.23           C  
ANISOU 3374  CG1 ILE A 296    10495   8025   8545     19    720    -83       C  
ATOM   3375  CG2 ILE A 296      34.840  41.425 -13.459  1.00 72.35           C  
ANISOU 3375  CG2 ILE A 296    10747   8110   8633     97    733   -113       C  
ATOM   3376  CD1 ILE A 296      34.909  39.968 -10.852  1.00 71.56           C  
ANISOU 3376  CD1 ILE A 296    10535   8067   8586     42    703   -100       C  
ATOM   3377  N   ARG A 297      37.602  43.842 -13.830  1.00 76.64           N  
ANISOU 3377  N   ARG A 297    11457   8586   9077    -89    788    -96       N  
ATOM   3378  CA  ARG A 297      37.568  45.050 -14.647  1.00 79.78           C  
ANISOU 3378  CA  ARG A 297    11991   8907   9413    -88    826   -108       C  
ATOM   3379  C   ARG A 297      38.638  45.018 -15.740  1.00 76.53           C  
ANISOU 3379  C   ARG A 297    11558   8518   9001   -136    833    -98       C  
ATOM   3380  O   ARG A 297      38.400  45.478 -16.865  1.00 76.26           O  
ANISOU 3380  O   ARG A 297    11590   8433   8950    -85    854   -105       O  
ATOM   3381  CB  ARG A 297      37.715  46.291 -13.767  1.00 85.13           C  
ANISOU 3381  CB  ARG A 297    12816   9522  10007   -170    863   -120       C  
ATOM   3382  CG  ARG A 297      36.457  46.599 -12.947  1.00 91.63           C  
ANISOU 3382  CG  ARG A 297    13704  10298  10812    -81    874   -127       C  
ATOM   3383  CD  ARG A 297      36.536  47.953 -12.241  1.00 97.79           C  
ANISOU 3383  CD  ARG A 297    14688  10979  11487   -148    934   -139       C  
ATOM   3384  NE  ARG A 297      37.511  47.975 -11.150  1.00100.83           N  
ANISOU 3384  NE  ARG A 297    15057  11406  11848   -323    924   -145       N  
ATOM   3385  CZ  ARG A 297      37.217  47.751  -9.872  1.00100.39           C  
ANISOU 3385  CZ  ARG A 297    14971  11372  11799   -343    907   -146       C  
ATOM   3386  NH1 ARG A 297      35.967  47.480  -9.514  1.00100.76           N  
ANISOU 3386  NH1 ARG A 297    15003  11401  11878   -198    899   -142       N  
ATOM   3387  NH2 ARG A 297      38.175  47.794  -8.952  1.00 99.52           N  
ANISOU 3387  NH2 ARG A 297    14836  11323  11652   -513    898   -148       N  
ATOM   3388  N   ALA A 298      39.818  44.470 -15.433  1.00 72.89           N  
ANISOU 3388  N   ALA A 298    10997   8149   8548   -222    817    -74       N  
ATOM   3389  CA  ALA A 298      40.882  44.396 -16.430  1.00 70.09           C  
ANISOU 3389  CA  ALA A 298    10606   7842   8183   -261    825    -55       C  
ATOM   3390  C   ALA A 298      40.489  43.479 -17.582  1.00 71.14           C  
ANISOU 3390  C   ALA A 298    10685   7964   8382   -143    818    -50       C  
ATOM   3391  O   ALA A 298      40.703  43.811 -18.757  1.00 74.92           O  
ANISOU 3391  O   ALA A 298    11202   8413   8850   -130    833    -54       O  
ATOM   3392  CB  ALA A 298      42.182  43.919 -15.777  1.00 65.74           C  
ANISOU 3392  CB  ALA A 298     9935   7437   7608   -353    814    -13       C  
ATOM   3393  N   ARG A 299      39.905  42.323 -17.259  1.00 69.79           N  
ANISOU 3393  N   ARG A 299    10439   7811   8269    -69    800    -45       N  
ATOM   3394  CA  ARG A 299      39.401  41.427 -18.293  1.00 67.02           C  
ANISOU 3394  CA  ARG A 299    10063   7440   7960     17    801    -50       C  
ATOM   3395  C   ARG A 299      38.296  42.088 -19.106  1.00 66.17           C  
ANISOU 3395  C   ARG A 299    10032   7270   7838     69    804    -82       C  
ATOM   3396  O   ARG A 299      38.203  41.875 -20.321  1.00 71.66           O  
ANISOU 3396  O   ARG A 299    10732   7955   8540    107    812    -86       O  
ATOM   3397  CB  ARG A 299      38.901  40.120 -17.673  1.00 67.68           C  
ANISOU 3397  CB  ARG A 299    10088   7543   8085     59    794    -45       C  
ATOM   3398  CG  ARG A 299      39.992  39.236 -17.132  1.00 73.76           C  
ANISOU 3398  CG  ARG A 299    10784   8379   8860     56    808      3       C  
ATOM   3399  CD  ARG A 299      39.435  37.871 -16.795  1.00 81.83           C  
ANISOU 3399  CD  ARG A 299    11794   9387   9912    111    821      4       C  
ATOM   3400  NE  ARG A 299      40.491  36.911 -16.485  1.00 92.18           N  
ANISOU 3400  NE  ARG A 299    13055  10753  11214    152    855     64       N  
ATOM   3401  CZ  ARG A 299      40.317  35.592 -16.442  1.00 97.80           C  
ANISOU 3401  CZ  ARG A 299    13793  11434  11933    215    896     78       C  
ATOM   3402  NH1 ARG A 299      39.125  35.064 -16.694  1.00 97.92           N  
ANISOU 3402  NH1 ARG A 299    13873  11371  11962    208    899     28       N  
ATOM   3403  NH2 ARG A 299      41.339  34.798 -16.151  1.00101.53           N  
ANISOU 3403  NH2 ARG A 299    14232  11963  12380    284    942    147       N  
ATOM   3404  N   ARG A 300      37.455  42.905 -18.461  1.00 63.00           N  
ANISOU 3404  N   ARG A 300     9692   6840   7405     83    804    -98       N  
ATOM   3405  CA  ARG A 300      36.437  43.639 -19.209  1.00 68.76           C  
ANISOU 3405  CA  ARG A 300    10493   7536   8096    162    819   -111       C  
ATOM   3406  C   ARG A 300      37.074  44.590 -20.226  1.00 70.11           C  
ANISOU 3406  C   ARG A 300    10753   7657   8229    151    850   -109       C  
ATOM   3407  O   ARG A 300      36.652  44.652 -21.388  1.00 71.71           O  
ANISOU 3407  O   ARG A 300    10966   7857   8422    217    858   -111       O  
ATOM   3408  CB  ARG A 300      35.530  44.409 -18.253  1.00 72.59           C  
ANISOU 3408  CB  ARG A 300    11045   8001   8536    201    829   -115       C  
ATOM   3409  CG  ARG A 300      34.505  43.562 -17.542  1.00 77.37           C  
ANISOU 3409  CG  ARG A 300    11565   8670   9163    239    799   -118       C  
ATOM   3410  CD  ARG A 300      33.680  44.423 -16.586  1.00 80.75           C  
ANISOU 3410  CD  ARG A 300    12064   9081   9536    292    815   -113       C  
ATOM   3411  NE  ARG A 300      32.694  43.629 -15.862  1.00 83.87           N  
ANISOU 3411  NE  ARG A 300    12368   9553   9946    320    785   -115       N  
ATOM   3412  CZ  ARG A 300      31.717  44.144 -15.127  1.00 81.21           C  
ANISOU 3412  CZ  ARG A 300    12061   9238   9557    392    795   -104       C  
ATOM   3413  NH1 ARG A 300      31.587  45.455 -15.019  1.00 80.93           N  
ANISOU 3413  NH1 ARG A 300    12166   9134   9449    457    845    -89       N  
ATOM   3414  NH2 ARG A 300      30.861  43.346 -14.513  1.00 80.17           N  
ANISOU 3414  NH2 ARG A 300    11833   9193   9435    401    764   -107       N  
ATOM   3415  N   LYS A 301      38.093  45.342 -19.802  1.00 69.94           N  
ANISOU 3415  N   LYS A 301    10798   7604   8174     54    870   -106       N  
ATOM   3416  CA  LYS A 301      38.736  46.296 -20.710  1.00 73.08           C  
ANISOU 3416  CA  LYS A 301    11298   7948   8519     18    906   -108       C  
ATOM   3417  C   LYS A 301      39.380  45.579 -21.891  1.00 71.28           C  
ANISOU 3417  C   LYS A 301    10985   7764   8336     22    892    -98       C  
ATOM   3418  O   LYS A 301      39.270  46.022 -23.045  1.00 68.81           O  
ANISOU 3418  O   LYS A 301    10728   7412   8003     66    913   -102       O  
ATOM   3419  CB  LYS A 301      39.786  47.120 -19.967  1.00 76.44           C  
ANISOU 3419  CB  LYS A 301    11803   8359   8881   -133    930   -110       C  
ATOM   3420  CG  LYS A 301      39.244  48.263 -19.135  1.00 80.81           C  
ANISOU 3420  CG  LYS A 301    12530   8819   9353   -148    976   -126       C  
ATOM   3421  CD  LYS A 301      40.397  49.059 -18.534  1.00 84.51           C  
ANISOU 3421  CD  LYS A 301    13092   9281   9736   -345   1005   -135       C  
ATOM   3422  CE  LYS A 301      39.927  50.381 -17.966  1.00 90.10           C  
ANISOU 3422  CE  LYS A 301    14046   9853  10336   -368   1079   -156       C  
ATOM   3423  NZ  LYS A 301      41.074  51.245 -17.534  1.00 93.17           N  
ANISOU 3423  NZ  LYS A 301    14561  10228  10610   -602   1120   -175       N  
ATOM   3424  N   THR A 302      40.074  44.472 -21.611  1.00 70.08           N  
ANISOU 3424  N   THR A 302    10705   7690   8234    -12    865    -79       N  
ATOM   3425  CA  THR A 302      40.716  43.715 -22.676  1.00 66.03           C  
ANISOU 3425  CA  THR A 302    10124   7212   7753      7    864    -62       C  
ATOM   3426  C   THR A 302      39.688  43.157 -23.655  1.00 67.15           C  
ANISOU 3426  C   THR A 302    10260   7328   7926    107    860    -78       C  
ATOM   3427  O   THR A 302      39.840  43.310 -24.878  1.00 66.96           O  
ANISOU 3427  O   THR A 302    10259   7286   7897    131    872    -80       O  
ATOM   3428  CB  THR A 302      41.563  42.599 -22.071  1.00 62.10           C  
ANISOU 3428  CB  THR A 302     9510   6803   7284    -13    853    -26       C  
ATOM   3429  OG1 THR A 302      42.612  43.185 -21.290  1.00 64.99           O  
ANISOU 3429  OG1 THR A 302     9858   7237   7597   -122    856     -5       O  
ATOM   3430  CG2 THR A 302      42.168  41.728 -23.165  1.00 57.24           C  
ANISOU 3430  CG2 THR A 302     8843   6214   6692     35    867     -1       C  
ATOM   3431  N   ALA A 303      38.630  42.526 -23.134  1.00 64.22           N  
ANISOU 3431  N   ALA A 303     9857   6969   7575    151    843    -91       N  
ATOM   3432  CA  ALA A 303      37.580  42.005 -23.998  1.00 65.19           C  
ANISOU 3432  CA  ALA A 303     9966   7102   7700    213    838   -109       C  
ATOM   3433  C   ALA A 303      36.981  43.105 -24.861  1.00 67.35           C  
ANISOU 3433  C   ALA A 303    10308   7357   7923    270    852   -115       C  
ATOM   3434  O   ALA A 303      36.688  42.885 -26.041  1.00 69.32           O  
ANISOU 3434  O   ALA A 303    10549   7623   8165    304    856   -120       O  
ATOM   3435  CB  ALA A 303      36.492  41.336 -23.161  1.00 60.00           C  
ANISOU 3435  CB  ALA A 303     9268   6484   7047    226    819   -122       C  
ATOM   3436  N   ARG A 304      36.797  44.299 -24.295  1.00 67.98           N  
ANISOU 3436  N   ARG A 304    10473   7399   7958    285    870   -112       N  
ATOM   3437  CA  ARG A 304      36.255  45.407 -25.074  1.00 67.75           C  
ANISOU 3437  CA  ARG A 304    10539   7339   7863    366    903   -107       C  
ATOM   3438  C   ARG A 304      37.197  45.801 -26.213  1.00 65.00           C  
ANISOU 3438  C   ARG A 304    10239   6947   7512    339    924   -106       C  
ATOM   3439  O   ARG A 304      36.755  46.021 -27.349  1.00 65.95           O  
ANISOU 3439  O   ARG A 304    10376   7077   7606    412    938   -102       O  
ATOM   3440  CB  ARG A 304      35.979  46.590 -24.147  1.00 74.50           C  
ANISOU 3440  CB  ARG A 304    11518   8134   8654    389    939   -101       C  
ATOM   3441  CG  ARG A 304      35.728  47.920 -24.822  1.00 83.73           C  
ANISOU 3441  CG  ARG A 304    12846   9233   9736    473   1001    -88       C  
ATOM   3442  CD  ARG A 304      35.115  48.882 -23.825  1.00 94.09           C  
ANISOU 3442  CD  ARG A 304    14291  10489  10971    533   1048    -76       C  
ATOM   3443  NE  ARG A 304      35.468  50.272 -24.096  1.00104.20           N  
ANISOU 3443  NE  ARG A 304    15795  11638  12157    546   1131    -70       N  
ATOM   3444  CZ  ARG A 304      36.417  50.947 -23.451  1.00108.21           C  
ANISOU 3444  CZ  ARG A 304    16442  12043  12631    405   1167    -89       C  
ATOM   3445  NH1 ARG A 304      37.116  50.351 -22.490  1.00106.28           N  
ANISOU 3445  NH1 ARG A 304    16106  11834  12441    256   1119   -108       N  
ATOM   3446  NH2 ARG A 304      36.667  52.217 -23.772  1.00111.02           N  
ANISOU 3446  NH2 ARG A 304    17036  12267  12881    407   1257    -88       N  
ATOM   3447  N   MET A 305      38.499  45.896 -25.927  1.00 61.30           N  
ANISOU 3447  N   MET A 305     9783   6448   7059    231    928   -104       N  
ATOM   3448  CA  MET A 305      39.455  46.213 -26.984  1.00 62.56           C  
ANISOU 3448  CA  MET A 305     9974   6585   7211    192    946   -100       C  
ATOM   3449  C   MET A 305      39.404  45.169 -28.091  1.00 61.21           C  
ANISOU 3449  C   MET A 305     9709   6459   7089    235    926    -98       C  
ATOM   3450  O   MET A 305      39.320  45.506 -29.276  1.00 62.05           O  
ANISOU 3450  O   MET A 305     9851   6547   7177    278    943    -99       O  
ATOM   3451  CB  MET A 305      40.864  46.300 -26.407  1.00 66.63           C  
ANISOU 3451  CB  MET A 305    10477   7120   7721     57    947    -90       C  
ATOM   3452  CG  MET A 305      41.897  46.830 -27.383  1.00 67.93           C  
ANISOU 3452  CG  MET A 305    10684   7274   7853     -4    971    -84       C  
ATOM   3453  SD  MET A 305      43.558  46.682 -26.695  1.00 71.83           S  
ANISOU 3453  SD  MET A 305    11099   7872   8320   -168    963    -58       S  
ATOM   3454  CE  MET A 305      43.695  44.904 -26.577  1.00 68.67           C  
ANISOU 3454  CE  MET A 305    10513   7571   8009    -89    925    -25       C  
ATOM   3455  N   LEU A 306      39.425  43.895 -27.716  1.00 61.86           N  
ANISOU 3455  N   LEU A 306     9688   6592   7225    225    900    -95       N  
ATOM   3456  CA  LEU A 306      39.350  42.818 -28.694  1.00 62.13           C  
ANISOU 3456  CA  LEU A 306     9667   6651   7290    252    895    -97       C  
ATOM   3457  C   LEU A 306      38.053  42.884 -29.496  1.00 62.76           C  
ANISOU 3457  C   LEU A 306     9754   6751   7339    319    892   -115       C  
ATOM   3458  O   LEU A 306      38.048  42.599 -30.695  1.00 63.28           O  
ANISOU 3458  O   LEU A 306     9816   6825   7402    336    899   -120       O  
ATOM   3459  CB  LEU A 306      39.491  41.465 -27.982  1.00 61.18           C  
ANISOU 3459  CB  LEU A 306     9477   6559   7208    233    887    -90       C  
ATOM   3460  CG  LEU A 306      40.805  41.336 -27.211  1.00 62.52           C  
ANISOU 3460  CG  LEU A 306     9613   6752   7391    188    893    -55       C  
ATOM   3461  CD1 LEU A 306      40.837  40.083 -26.350  1.00 64.78           C  
ANISOU 3461  CD1 LEU A 306     9848   7062   7702    196    896    -40       C  
ATOM   3462  CD2 LEU A 306      42.000  41.352 -28.183  1.00 63.88           C  
ANISOU 3462  CD2 LEU A 306     9777   6936   7557    181    914    -28       C  
ATOM   3463  N   MET A 307      36.938  43.255 -28.862  1.00 64.45           N  
ANISOU 3463  N   MET A 307     9972   6997   7519    360    883   -121       N  
ATOM   3464  CA  MET A 307      35.687  43.330 -29.610  1.00 65.81           C  
ANISOU 3464  CA  MET A 307    10125   7242   7637    429    881   -126       C  
ATOM   3465  C   MET A 307      35.724  44.474 -30.608  1.00 67.61           C  
ANISOU 3465  C   MET A 307    10427   7444   7816    501    910   -112       C  
ATOM   3466  O   MET A 307      35.194  44.352 -31.716  1.00 66.75           O  
ANISOU 3466  O   MET A 307    10292   7398   7674    543    911   -111       O  
ATOM   3467  CB  MET A 307      34.498  43.483 -28.665  1.00 66.27           C  
ANISOU 3467  CB  MET A 307    10157   7371   7653    473    869   -122       C  
ATOM   3468  CG  MET A 307      34.105  42.198 -27.935  1.00 69.55           C  
ANISOU 3468  CG  MET A 307    10492   7840   8095    404    841   -140       C  
ATOM   3469  SD  MET A 307      33.042  42.581 -26.522  1.00 74.48           S  
ANISOU 3469  SD  MET A 307    11095   8524   8679    447    828   -130       S  
ATOM   3470  CE  MET A 307      33.108  41.043 -25.603  1.00 77.06           C  
ANISOU 3470  CE  MET A 307    11360   8860   9061    337    804   -156       C  
ATOM   3471  N   VAL A 308      36.343  45.597 -30.234  1.00 65.69           N  
ANISOU 3471  N   VAL A 308    10290   7112   7558    506    941   -101       N  
ATOM   3472  CA  VAL A 308      36.485  46.698 -31.182  1.00 63.97           C  
ANISOU 3472  CA  VAL A 308    10176   6843   7285    568    983    -88       C  
ATOM   3473  C   VAL A 308      37.367  46.274 -32.349  1.00 63.31           C  
ANISOU 3473  C   VAL A 308    10068   6745   7243    518    978    -96       C  
ATOM   3474  O   VAL A 308      37.062  46.560 -33.513  1.00 64.97           O  
ANISOU 3474  O   VAL A 308    10294   6972   7418    584    994    -89       O  
ATOM   3475  CB  VAL A 308      37.031  47.954 -30.474  1.00 64.01           C  
ANISOU 3475  CB  VAL A 308    10338   6736   7247    547   1031    -83       C  
ATOM   3476  CG1 VAL A 308      37.395  49.039 -31.493  1.00 60.13           C  
ANISOU 3476  CG1 VAL A 308     9986   6166   6696    585   1087    -74       C  
ATOM   3477  CG2 VAL A 308      35.993  48.492 -29.500  1.00 63.48           C  
ANISOU 3477  CG2 VAL A 308    10323   6676   7120    634   1052    -68       C  
ATOM   3478  N   VAL A 309      38.473  45.588 -32.053  1.00 60.15           N  
ANISOU 3478  N   VAL A 309     9624   6325   6906    416    961   -102       N  
ATOM   3479  CA  VAL A 309      39.336  45.073 -33.112  1.00 62.97           C  
ANISOU 3479  CA  VAL A 309     9951   6678   7297    383    960   -102       C  
ATOM   3480  C   VAL A 309      38.536  44.184 -34.051  1.00 62.87           C  
ANISOU 3480  C   VAL A 309     9874   6726   7287    425    946   -112       C  
ATOM   3481  O   VAL A 309      38.618  44.321 -35.278  1.00 60.46           O  
ANISOU 3481  O   VAL A 309     9584   6419   6968    451    958   -112       O  
ATOM   3482  CB  VAL A 309      40.537  44.322 -32.506  1.00 64.16           C  
ANISOU 3482  CB  VAL A 309    10045   6835   7497    297    950    -90       C  
ATOM   3483  CG1 VAL A 309      41.266  43.493 -33.576  1.00 56.06           C  
ANISOU 3483  CG1 VAL A 309     8978   5821   6501    294    956    -81       C  
ATOM   3484  CG2 VAL A 309      41.498  45.301 -31.845  1.00 66.65           C  
ANISOU 3484  CG2 VAL A 309    10418   7122   7782    220    966    -80       C  
ATOM   3485  N   LEU A 310      37.737  43.272 -33.489  1.00 60.25           N  
ANISOU 3485  N   LEU A 310     9478   6453   6963    416    924   -124       N  
ATOM   3486  CA  LEU A 310      36.919  42.396 -34.318  1.00 60.09           C  
ANISOU 3486  CA  LEU A 310     9407   6505   6919    415    915   -140       C  
ATOM   3487  C   LEU A 310      35.949  43.193 -35.185  1.00 62.07           C  
ANISOU 3487  C   LEU A 310     9660   6830   7095    497    920   -133       C  
ATOM   3488  O   LEU A 310      35.785  42.902 -36.371  1.00 66.36           O  
ANISOU 3488  O   LEU A 310    10186   7413   7613    497    923   -140       O  
ATOM   3489  CB  LEU A 310      36.161  41.408 -33.438  1.00 62.58           C  
ANISOU 3489  CB  LEU A 310     9670   6877   7232    370    896   -157       C  
ATOM   3490  CG  LEU A 310      35.186  40.495 -34.187  1.00 68.45           C  
ANISOU 3490  CG  LEU A 310    10371   7718   7920    328    891   -181       C  
ATOM   3491  CD1 LEU A 310      35.916  39.696 -35.293  1.00 67.61           C  
ANISOU 3491  CD1 LEU A 310    10301   7556   7832    281    916   -193       C  
ATOM   3492  CD2 LEU A 310      34.499  39.556 -33.210  1.00 69.13           C  
ANISOU 3492  CD2 LEU A 310    10423   7851   7992    259    879   -200       C  
ATOM   3493  N   LEU A 311      35.294  44.199 -34.608  1.00 62.89           N  
ANISOU 3493  N   LEU A 311     9789   6957   7148    578    927   -114       N  
ATOM   3494  CA  LEU A 311      34.317  44.979 -35.362  1.00 64.84           C  
ANISOU 3494  CA  LEU A 311    10037   7297   7301    694    944    -89       C  
ATOM   3495  C   LEU A 311      34.978  45.739 -36.509  1.00 63.25           C  
ANISOU 3495  C   LEU A 311     9914   7024   7093    738    976    -78       C  
ATOM   3496  O   LEU A 311      34.433  45.804 -37.622  1.00 60.82           O  
ANISOU 3496  O   LEU A 311     9575   6806   6728    794    982    -68       O  
ATOM   3497  CB  LEU A 311      33.587  45.939 -34.420  1.00 67.88           C  
ANISOU 3497  CB  LEU A 311    10465   7703   7624    799    965    -59       C  
ATOM   3498  CG  LEU A 311      32.710  47.025 -35.040  1.00 70.42           C  
ANISOU 3498  CG  LEU A 311    10826   8102   7830    972   1007    -11       C  
ATOM   3499  CD1 LEU A 311      31.605  46.431 -35.907  1.00 68.77           C  
ANISOU 3499  CD1 LEU A 311    10474   8113   7542   1003    983      1       C  
ATOM   3500  CD2 LEU A 311      32.112  47.883 -33.923  1.00 73.11           C  
ANISOU 3500  CD2 LEU A 311    11236   8435   8108   1081   1042     23       C  
ATOM   3501  N   VAL A 312      36.158  46.316 -36.254  1.00 63.29           N  
ANISOU 3501  N   VAL A 312    10018   6884   7144    701    999    -81       N  
ATOM   3502  CA  VAL A 312      36.866  47.075 -37.284  1.00 63.37           C  
ANISOU 3502  CA  VAL A 312    10116   6820   7143    723   1033    -73       C  
ATOM   3503  C   VAL A 312      37.384  46.140 -38.374  1.00 63.74           C  
ANISOU 3503  C   VAL A 312    10095   6887   7237    662   1012    -90       C  
ATOM   3504  O   VAL A 312      37.362  46.478 -39.559  1.00 63.20           O  
ANISOU 3504  O   VAL A 312    10048   6828   7138    710   1029    -83       O  
ATOM   3505  CB  VAL A 312      37.995  47.913 -36.650  1.00 64.12           C  
ANISOU 3505  CB  VAL A 312    10332   6778   7250    662   1064    -74       C  
ATOM   3506  CG1 VAL A 312      38.769  48.671 -37.721  1.00 65.61           C  
ANISOU 3506  CG1 VAL A 312    10618   6892   7417    661   1103    -70       C  
ATOM   3507  CG2 VAL A 312      37.417  48.906 -35.610  1.00 62.45           C  
ANISOU 3507  CG2 VAL A 312    10228   6527   6972    724   1102    -59       C  
ATOM   3508  N   PHE A 313      37.838  44.944 -37.997  1.00 64.62           N  
ANISOU 3508  N   PHE A 313    10138   7001   7415    567    983   -109       N  
ATOM   3509  CA  PHE A 313      38.204  43.945 -38.994  1.00 62.98           C  
ANISOU 3509  CA  PHE A 313     9888   6805   7235    521    977   -122       C  
ATOM   3510  C   PHE A 313      37.010  43.591 -39.872  1.00 64.73           C  
ANISOU 3510  C   PHE A 313    10057   7143   7393    550    968   -131       C  
ATOM   3511  O   PHE A 313      37.123  43.527 -41.106  1.00 67.02           O  
ANISOU 3511  O   PHE A 313    10350   7446   7667    557    977   -134       O  
ATOM   3512  CB  PHE A 313      38.755  42.688 -38.309  1.00 64.75           C  
ANISOU 3512  CB  PHE A 313    10076   7008   7518    440    967   -132       C  
ATOM   3513  CG  PHE A 313      39.063  41.563 -39.269  1.00 67.39           C  
ANISOU 3513  CG  PHE A 313    10402   7338   7864    401    979   -144       C  
ATOM   3514  CD1 PHE A 313      38.090  40.632 -39.612  1.00 68.18           C  
ANISOU 3514  CD1 PHE A 313    10478   7503   7923    361    976   -171       C  
ATOM   3515  CD2 PHE A 313      40.317  41.441 -39.834  1.00 67.00           C  
ANISOU 3515  CD2 PHE A 313    10380   7226   7851    397   1002   -127       C  
ATOM   3516  CE1 PHE A 313      38.365  39.618 -40.502  1.00 68.22           C  
ANISOU 3516  CE1 PHE A 313    10514   7485   7923    314   1001   -185       C  
ATOM   3517  CE2 PHE A 313      40.602  40.409 -40.710  1.00 67.38           C  
ANISOU 3517  CE2 PHE A 313    10444   7256   7901    377   1026   -133       C  
ATOM   3518  CZ  PHE A 313      39.623  39.505 -41.049  1.00 66.42           C  
ANISOU 3518  CZ  PHE A 313    10327   7173   7738    334   1030   -165       C  
ATOM   3519  N   ALA A 314      35.862  43.320 -39.243  1.00 62.60           N  
ANISOU 3519  N   ALA A 314     9728   6980   7076    554    949   -135       N  
ATOM   3520  CA  ALA A 314      34.679  42.897 -39.989  1.00 59.33           C  
ANISOU 3520  CA  ALA A 314     9240   6729   6576    552    936   -142       C  
ATOM   3521  C   ALA A 314      34.215  43.986 -40.953  1.00 61.69           C  
ANISOU 3521  C   ALA A 314     9543   7099   6798    675    954   -109       C  
ATOM   3522  O   ALA A 314      33.860  43.705 -42.104  1.00 64.26           O  
ANISOU 3522  O   ALA A 314     9827   7518   7070    663    953   -113       O  
ATOM   3523  CB  ALA A 314      33.562  42.506 -39.024  1.00 54.46           C  
ANISOU 3523  CB  ALA A 314     8548   6237   5906    530    913   -145       C  
ATOM   3524  N   ILE A 315      34.252  45.247 -40.518  1.00 63.53           N  
ANISOU 3524  N   ILE A 315     9844   7280   7013    794    980    -74       N  
ATOM   3525  CA  ILE A 315      33.890  46.341 -41.419  1.00 63.84           C  
ANISOU 3525  CA  ILE A 315     9924   7362   6971    937   1017    -34       C  
ATOM   3526  C   ILE A 315      34.907  46.482 -42.541  1.00 62.02           C  
ANISOU 3526  C   ILE A 315     9756   7023   6786    911   1033    -46       C  
ATOM   3527  O   ILE A 315      34.539  46.609 -43.713  1.00 66.69           O  
ANISOU 3527  O   ILE A 315    10319   7702   7318    963   1041    -33       O  
ATOM   3528  CB  ILE A 315      33.734  47.657 -40.639  1.00 66.51           C  
ANISOU 3528  CB  ILE A 315    10372   7634   7264   1072   1063      5       C  
ATOM   3529  CG1 ILE A 315      32.581  47.525 -39.653  1.00 68.57           C  
ANISOU 3529  CG1 ILE A 315    10555   8035   7462   1122   1049     27       C  
ATOM   3530  CG2 ILE A 315      33.516  48.814 -41.620  1.00 68.41           C  
ANISOU 3530  CG2 ILE A 315    10698   7881   7414   1234   1122     51       C  
ATOM   3531  CD1 ILE A 315      32.447  48.697 -38.730  1.00 75.19           C  
ANISOU 3531  CD1 ILE A 315    11523   8790   8257   1248   1103     63       C  
ATOM   3532  N   CYS A 316      36.201  46.466 -42.209  1.00 59.46           N  
ANISOU 3532  N   CYS A 316     9506   6529   6555    832   1038    -66       N  
ATOM   3533  CA  CYS A 316      37.223  46.714 -43.215  1.00 60.50           C  
ANISOU 3533  CA  CYS A 316     9698   6567   6721    812   1057    -71       C  
ATOM   3534  C   CYS A 316      37.219  45.647 -44.296  1.00 62.16           C  
ANISOU 3534  C   CYS A 316     9832   6841   6946    751   1035    -92       C  
ATOM   3535  O   CYS A 316      37.457  45.957 -45.467  1.00 56.95           O  
ANISOU 3535  O   CYS A 316     9197   6174   6268    784   1052    -86       O  
ATOM   3536  CB  CYS A 316      38.598  46.791 -42.557  1.00 59.34           C  
ANISOU 3536  CB  CYS A 316     9614   6278   6653    723   1063    -82       C  
ATOM   3537  SG  CYS A 316      38.877  48.359 -41.746  1.00 61.37           S  
ANISOU 3537  SG  CYS A 316    10027   6427   6865    765   1113    -62       S  
ATOM   3538  N   TYR A 317      36.910  44.398 -43.939  1.00 65.15           N  
ANISOU 3538  N   TYR A 317    10135   7275   7343    659   1006   -118       N  
ATOM   3539  CA  TYR A 317      36.940  43.322 -44.918  1.00 61.79           C  
ANISOU 3539  CA  TYR A 317     9677   6886   6916    580   1001   -144       C  
ATOM   3540  C   TYR A 317      35.587  42.992 -45.516  1.00 63.55           C  
ANISOU 3540  C   TYR A 317     9816   7298   7032    573    986   -149       C  
ATOM   3541  O   TYR A 317      35.533  42.144 -46.418  1.00 66.75           O  
ANISOU 3541  O   TYR A 317    10209   7741   7413    488    987   -175       O  
ATOM   3542  CB  TYR A 317      37.516  42.053 -44.309  1.00 60.14           C  
ANISOU 3542  CB  TYR A 317     9475   6607   6768    472    999   -169       C  
ATOM   3543  CG  TYR A 317      39.015  42.057 -44.224  1.00 58.91           C  
ANISOU 3543  CG  TYR A 317     9377   6311   6697    467   1019   -157       C  
ATOM   3544  CD1 TYR A 317      39.663  42.627 -43.144  1.00 60.66           C  
ANISOU 3544  CD1 TYR A 317     9614   6471   6961    482   1017   -138       C  
ATOM   3545  CD2 TYR A 317      39.787  41.482 -45.222  1.00 60.64           C  
ANISOU 3545  CD2 TYR A 317     9626   6478   6935    442   1042   -160       C  
ATOM   3546  CE1 TYR A 317      41.036  42.629 -43.060  1.00 64.03           C  
ANISOU 3546  CE1 TYR A 317    10069   6821   7441    465   1033   -119       C  
ATOM   3547  CE2 TYR A 317      41.165  41.480 -45.141  1.00 62.24           C  
ANISOU 3547  CE2 TYR A 317     9860   6591   7196    448   1062   -136       C  
ATOM   3548  CZ  TYR A 317      41.778  42.049 -44.055  1.00 62.10           C  
ANISOU 3548  CZ  TYR A 317     9838   6546   7211    455   1055   -114       C  
ATOM   3549  OH  TYR A 317      43.138  42.045 -43.955  1.00 62.29           O  
ANISOU 3549  OH  TYR A 317     9868   6530   7270    449   1073    -84       O  
ATOM   3550  N   LEU A 318      34.499  43.614 -45.045  1.00 59.70           N  
ANISOU 3550  N   LEU A 318     9272   6946   6464    653    977   -122       N  
ATOM   3551  CA  LEU A 318      33.216  43.372 -45.701  1.00 60.08           C  
ANISOU 3551  CA  LEU A 318     9214   7231   6382    648    962   -115       C  
ATOM   3552  C   LEU A 318      33.219  43.747 -47.181  1.00 59.28           C  
ANISOU 3552  C   LEU A 318     9108   7187   6230    698    977   -101       C  
ATOM   3553  O   LEU A 318      32.869  42.888 -48.009  1.00 62.98           O  
ANISOU 3553  O   LEU A 318     9524   7763   6641    585    966   -129       O  
ATOM   3554  CB  LEU A 318      32.111  44.102 -44.941  1.00 60.86           C  
ANISOU 3554  CB  LEU A 318     9246   7486   6391    767    959    -70       C  
ATOM   3555  CG  LEU A 318      30.664  43.853 -45.376  1.00 67.46           C  
ANISOU 3555  CG  LEU A 318     9933   8634   7063    764    940    -48       C  
ATOM   3556  CD1 LEU A 318      30.343  42.375 -45.352  1.00 70.31           C  
ANISOU 3556  CD1 LEU A 318    10237   9077   7402    537    910   -108       C  
ATOM   3557  CD2 LEU A 318      29.716  44.609 -44.425  1.00 67.36           C  
ANISOU 3557  CD2 LEU A 318     9866   8760   6969    911    945      9       C  
ATOM   3558  N   PRO A 319      33.605  44.962 -47.591  1.00 60.63           N  
ANISOU 3558  N   PRO A 319     9345   7287   6406    848   1008    -62       N  
ATOM   3559  CA  PRO A 319      33.400  45.326 -49.005  1.00 59.40           C  
ANISOU 3559  CA  PRO A 319     9168   7223   6179    910   1022    -41       C  
ATOM   3560  C   PRO A 319      34.125  44.407 -49.966  1.00 63.73           C  
ANISOU 3560  C   PRO A 319     9736   7698   6780    771   1016    -89       C  
ATOM   3561  O   PRO A 319      33.524  43.930 -50.933  1.00 68.46           O  
ANISOU 3561  O   PRO A 319    10262   8457   7291    717   1006    -97       O  
ATOM   3562  CB  PRO A 319      33.924  46.767 -49.071  1.00 57.24           C  
ANISOU 3562  CB  PRO A 319     9014   6816   5920   1081   1070      2       C  
ATOM   3563  CG  PRO A 319      33.756  47.277 -47.681  1.00 59.17           C  
ANISOU 3563  CG  PRO A 319     9300   7008   6174   1140   1081     20       C  
ATOM   3564  CD  PRO A 319      34.157  46.098 -46.830  1.00 57.47           C  
ANISOU 3564  CD  PRO A 319     9052   6731   6053    964   1039    -33       C  
ATOM   3565  N   ILE A 320      35.402  44.124 -49.725  1.00 62.63           N  
ANISOU 3565  N   ILE A 320     9691   7338   6767    712   1024   -116       N  
ATOM   3566  CA  ILE A 320      36.131  43.280 -50.663  1.00 62.01           C  
ANISOU 3566  CA  ILE A 320     9646   7184   6729    609   1031   -150       C  
ATOM   3567  C   ILE A 320      35.570  41.854 -50.659  1.00 64.34           C  
ANISOU 3567  C   ILE A 320     9903   7565   6979    446   1019   -194       C  
ATOM   3568  O   ILE A 320      35.485  41.217 -51.710  1.00 67.38           O  
ANISOU 3568  O   ILE A 320    10292   7993   7317    363   1028   -218       O  
ATOM   3569  CB  ILE A 320      37.637  43.321 -50.347  1.00 61.55           C  
ANISOU 3569  CB  ILE A 320     9684   6905   6797    602   1049   -153       C  
ATOM   3570  CG1 ILE A 320      38.449  42.700 -51.492  1.00 60.85           C  
ANISOU 3570  CG1 ILE A 320     9639   6744   6738    548   1068   -170       C  
ATOM   3571  CG2 ILE A 320      37.919  42.651 -48.984  1.00 60.28           C  
ANISOU 3571  CG2 ILE A 320     9532   6678   6696    537   1041   -167       C  
ATOM   3572  CD1 ILE A 320      39.947  42.795 -51.310  1.00 58.28           C  
ANISOU 3572  CD1 ILE A 320     9383   6250   6512    556   1089   -158       C  
ATOM   3573  N   SER A 321      35.151  41.335 -49.494  1.00 62.03           N  
ANISOU 3573  N   SER A 321     9589   7295   6686    386   1005   -207       N  
ATOM   3574  CA  SER A 321      34.605  39.975 -49.450  1.00 60.54           C  
ANISOU 3574  CA  SER A 321     9393   7173   6435    211   1006   -254       C  
ATOM   3575  C   SER A 321      33.321  39.877 -50.258  1.00 62.90           C  
ANISOU 3575  C   SER A 321     9589   7734   6575    149    989   -259       C  
ATOM   3576  O   SER A 321      33.140  38.950 -51.070  1.00 66.10           O  
ANISOU 3576  O   SER A 321    10022   8184   6911     -4   1005   -300       O  
ATOM   3577  CB  SER A 321      34.340  39.551 -48.007  1.00 60.69           C  
ANISOU 3577  CB  SER A 321     9405   7177   6475    167    995   -264       C  
ATOM   3578  OG  SER A 321      35.525  39.560 -47.245  1.00 58.73           O  
ANISOU 3578  OG  SER A 321     9238   6719   6357    213   1011   -255       O  
ATOM   3579  N   ILE A 322      32.420  40.840 -50.053  1.00 65.28           N  
ANISOU 3579  N   ILE A 322     9777   8224   6802    269    965   -212       N  
ATOM   3580  CA  ILE A 322      31.161  40.842 -50.785  1.00 69.66           C  
ANISOU 3580  CA  ILE A 322    10199   9088   7181    233    947   -198       C  
ATOM   3581  C   ILE A 322      31.405  41.066 -52.269  1.00 70.58           C  
ANISOU 3581  C   ILE A 322    10323   9231   7265    253    961   -193       C  
ATOM   3582  O   ILE A 322      30.776  40.422 -53.114  1.00 73.87           O  
ANISOU 3582  O   ILE A 322    10681   9831   7553    110    957   -217       O  
ATOM   3583  CB  ILE A 322      30.205  41.894 -50.202  1.00 71.83           C  
ANISOU 3583  CB  ILE A 322    10354   9564   7373    407    932   -128       C  
ATOM   3584  CG1 ILE A 322      29.854  41.538 -48.758  1.00 76.85           C  
ANISOU 3584  CG1 ILE A 322    10972  10198   8027    361    915   -139       C  
ATOM   3585  CG2 ILE A 322      28.951  42.000 -51.049  1.00 69.96           C  
ANISOU 3585  CG2 ILE A 322     9954   9692   6934    404    918    -93       C  
ATOM   3586  CD1 ILE A 322      29.178  40.190 -48.596  1.00 79.39           C  
ANISOU 3586  CD1 ILE A 322    11250  10659   8256    110    899   -195       C  
ATOM   3587  N   LEU A 323      32.322  41.975 -52.616  1.00 67.78           N  
ANISOU 3587  N   LEU A 323    10042   8700   7012    413    981   -163       N  
ATOM   3588  CA  LEU A 323      32.574  42.240 -54.027  1.00 66.05           C  
ANISOU 3588  CA  LEU A 323     9831   8500   6764    443    995   -156       C  
ATOM   3589  C   LEU A 323      33.197  41.025 -54.706  1.00 67.38           C  
ANISOU 3589  C   LEU A 323    10087   8551   6964    252   1010   -221       C  
ATOM   3590  O   LEU A 323      32.883  40.730 -55.864  1.00 69.54           O  
ANISOU 3590  O   LEU A 323    10332   8945   7145    177   1014   -234       O  
ATOM   3591  CB  LEU A 323      33.466  43.471 -54.188  1.00 64.79           C  
ANISOU 3591  CB  LEU A 323     9754   8162   6702    639   1019   -114       C  
ATOM   3592  CG  LEU A 323      32.817  44.845 -54.004  1.00 67.70           C  
ANISOU 3592  CG  LEU A 323    10078   8647   6997    860   1032    -40       C  
ATOM   3593  CD1 LEU A 323      33.877  45.932 -53.988  1.00 67.49           C  
ANISOU 3593  CD1 LEU A 323    10190   8381   7072   1001   1070    -16       C  
ATOM   3594  CD2 LEU A 323      31.786  45.131 -55.098  1.00 66.06           C  
ANISOU 3594  CD2 LEU A 323     9748   8730   6621    925   1032      3       C  
ATOM   3595  N   ASN A 324      34.067  40.296 -53.999  1.00 65.57           N  
ANISOU 3595  N   ASN A 324     9971   8095   6849    178   1027   -257       N  
ATOM   3596  CA  ASN A 324      34.643  39.092 -54.577  1.00 66.08           C  
ANISOU 3596  CA  ASN A 324    10148   8035   6924     19   1062   -310       C  
ATOM   3597  C   ASN A 324      33.572  38.046 -54.818  1.00 68.57           C  
ANISOU 3597  C   ASN A 324    10437   8536   7083   -196   1064   -357       C  
ATOM   3598  O   ASN A 324      33.592  37.362 -55.843  1.00 69.09           O  
ANISOU 3598  O   ASN A 324    10563   8610   7079   -327   1092   -394       O  
ATOM   3599  CB  ASN A 324      35.744  38.529 -53.685  1.00 57.05           C  
ANISOU 3599  CB  ASN A 324     9128   6637   5912     16   1091   -322       C  
ATOM   3600  CG  ASN A 324      36.339  37.255 -54.250  1.00 61.68           C  
ANISOU 3600  CG  ASN A 324     9860   7084   6492   -116   1149   -364       C  
ATOM   3601  OD1 ASN A 324      36.887  37.255 -55.351  1.00 64.46           O  
ANISOU 3601  OD1 ASN A 324    10263   7378   6852   -102   1173   -365       O  
ATOM   3602  ND2 ASN A 324      36.242  36.167 -53.500  1.00 60.75           N  
ANISOU 3602  ND2 ASN A 324     9827   6901   6353   -236   1180   -398       N  
ATOM   3603  N   VAL A 325      32.620  37.912 -53.892  1.00 73.32           N  
ANISOU 3603  N   VAL A 325    10953   9294   7612   -252   1037   -358       N  
ATOM   3604  CA  VAL A 325      31.536  36.955 -54.114  1.00 74.84           C  
ANISOU 3604  CA  VAL A 325    11110   9700   7626   -489   1037   -405       C  
ATOM   3605  C   VAL A 325      30.666  37.392 -55.288  1.00 75.31           C  
ANISOU 3605  C   VAL A 325    11028  10058   7528   -506   1014   -384       C  
ATOM   3606  O   VAL A 325      30.373  36.602 -56.196  1.00 73.43           O  
ANISOU 3606  O   VAL A 325    10825   9906   7167   -708   1035   -431       O  
ATOM   3607  CB  VAL A 325      30.709  36.766 -52.832  1.00 73.77           C  
ANISOU 3607  CB  VAL A 325    10900   9688   7442   -541   1012   -405       C  
ATOM   3608  CG1 VAL A 325      29.450  35.978 -53.138  1.00 76.08           C  
ANISOU 3608  CG1 VAL A 325    11117  10274   7514   -793   1005   -444       C  
ATOM   3609  CG2 VAL A 325      31.539  36.051 -51.793  1.00 73.28           C  
ANISOU 3609  CG2 VAL A 325    10995   9340   7507   -571   1046   -435       C  
ATOM   3610  N   LEU A 326      30.265  38.666 -55.306  1.00 77.34           N  
ANISOU 3610  N   LEU A 326    11137  10474   7774   -289    979   -311       N  
ATOM   3611  CA  LEU A 326      29.390  39.153 -56.367  1.00 81.22           C  
ANISOU 3611  CA  LEU A 326    11475  11286   8099   -267    960   -273       C  
ATOM   3612  C   LEU A 326      30.044  39.027 -57.735  1.00 81.58           C  
ANISOU 3612  C   LEU A 326    11601  11233   8161   -298    985   -295       C  
ATOM   3613  O   LEU A 326      29.356  38.773 -58.729  1.00 85.90           O  
ANISOU 3613  O   LEU A 326    12065  12030   8543   -419    980   -302       O  
ATOM   3614  CB  LEU A 326      28.987  40.603 -56.108  1.00 80.22           C  
ANISOU 3614  CB  LEU A 326    11219  11296   7963     24    941   -177       C  
ATOM   3615  CG  LEU A 326      28.073  40.844 -54.908  1.00 82.02           C  
ANISOU 3615  CG  LEU A 326    11330  11708   8125     76    916   -139       C  
ATOM   3616  CD1 LEU A 326      27.788  42.322 -54.801  1.00 85.58           C  
ANISOU 3616  CD1 LEU A 326    11704  12254   8559    394    922    -38       C  
ATOM   3617  CD2 LEU A 326      26.776  40.054 -55.022  1.00 82.22           C  
ANISOU 3617  CD2 LEU A 326    11200  12115   7925   -145    891   -155       C  
ATOM   3618  N   LYS A 327      31.362  39.191 -57.812  1.00 77.93           N  
ANISOU 3618  N   LYS A 327    11293  10433   7884   -198   1013   -303       N  
ATOM   3619  CA  LYS A 327      32.020  39.048 -59.102  1.00 76.99           C  
ANISOU 3619  CA  LYS A 327    11255  10215   7783   -224   1040   -322       C  
ATOM   3620  C   LYS A 327      32.224  37.579 -59.467  1.00 77.66           C  
ANISOU 3620  C   LYS A 327    11484  10202   7822   -492   1081   -403       C  
ATOM   3621  O   LYS A 327      31.848  37.147 -60.558  1.00 76.08           O  
ANISOU 3621  O   LYS A 327    11279  10135   7494   -637   1093   -432       O  
ATOM   3622  CB  LYS A 327      33.353  39.797 -59.096  1.00 74.28           C  
ANISOU 3622  CB  LYS A 327    11014   9578   7633    -23   1058   -293       C  
ATOM   3623  CG  LYS A 327      34.175  39.591 -60.357  1.00 73.73           C  
ANISOU 3623  CG  LYS A 327    11041   9376   7598    -44   1089   -313       C  
ATOM   3624  CD  LYS A 327      35.568  40.168 -60.206  1.00 76.00           C  
ANISOU 3624  CD  LYS A 327    11430   9378   8068    116   1109   -289       C  
ATOM   3625  CE  LYS A 327      36.439  39.821 -61.395  1.00 78.36           C  
ANISOU 3625  CE  LYS A 327    11831   9540   8401     85   1144   -309       C  
ATOM   3626  NZ  LYS A 327      37.793  40.434 -61.275  1.00 81.80           N  
ANISOU 3626  NZ  LYS A 327    12344   9742   8994    234   1161   -279       N  
ATOM   3627  N   ARG A 328      32.796  36.791 -58.560  1.00 78.96           N  
ANISOU 3627  N   ARG A 328    11789  10136   8074   -561   1113   -440       N  
ATOM   3628  CA  ARG A 328      33.198  35.426 -58.882  1.00 78.17           C  
ANISOU 3628  CA  ARG A 328    11889   9871   7942   -772   1179   -509       C  
ATOM   3629  C   ARG A 328      32.044  34.433 -58.801  1.00 79.13           C  
ANISOU 3629  C   ARG A 328    12010  10196   7861  -1062   1189   -567       C  
ATOM   3630  O   ARG A 328      31.881  33.591 -59.689  1.00 80.70           O  
ANISOU 3630  O   ARG A 328    12315  10413   7933  -1275   1235   -622       O  
ATOM   3631  CB  ARG A 328      34.320  34.977 -57.944  1.00 75.11           C  
ANISOU 3631  CB  ARG A 328    11664   9159   7714   -702   1223   -511       C  
ATOM   3632  CG  ARG A 328      35.590  35.768 -58.068  1.00 68.91           C  
ANISOU 3632  CG  ARG A 328    10902   8174   7106   -468   1225   -461       C  
ATOM   3633  CD  ARG A 328      36.138  35.673 -59.474  1.00 66.02           C  
ANISOU 3633  CD  ARG A 328    10611   7746   6730   -474   1259   -469       C  
ATOM   3634  NE  ARG A 328      37.375  36.433 -59.612  1.00 67.13           N  
ANISOU 3634  NE  ARG A 328    10767   7713   7027   -266   1261   -420       N  
ATOM   3635  CZ  ARG A 328      38.147  36.393 -60.692  1.00 66.45           C  
ANISOU 3635  CZ  ARG A 328    10757   7523   6967   -232   1295   -417       C  
ATOM   3636  NH1 ARG A 328      37.799  35.629 -61.718  1.00 66.62           N  
ANISOU 3636  NH1 ARG A 328    10857   7583   6872   -389   1333   -461       N  
ATOM   3637  NH2 ARG A 328      39.263  37.108 -60.750  1.00 63.99           N  
ANISOU 3637  NH2 ARG A 328    10449   7079   6786    -58   1294   -371       N  
ATOM   3638  N   VAL A 329      31.256  34.493 -57.731  1.00 79.69           N  
ANISOU 3638  N   VAL A 329    11974  10416   7888  -1089   1153   -559       N  
ATOM   3639  CA  VAL A 329      30.197  33.507 -57.558  1.00 81.79           C  
ANISOU 3639  CA  VAL A 329    12248  10876   7953  -1390   1165   -618       C  
ATOM   3640  C   VAL A 329      28.985  33.862 -58.407  1.00 85.93           C  
ANISOU 3640  C   VAL A 329    12560  11824   8265  -1494   1117   -605       C  
ATOM   3641  O   VAL A 329      28.478  33.029 -59.166  1.00 88.44           O  
ANISOU 3641  O   VAL A 329    12933  12273   8397  -1776   1148   -664       O  
ATOM   3642  CB  VAL A 329      29.828  33.367 -56.074  1.00 79.18           C  
ANISOU 3642  CB  VAL A 329    11885  10551   7648  -1392   1147   -615       C  
ATOM   3643  CG1 VAL A 329      28.748  32.322 -55.913  1.00 84.49           C  
ANISOU 3643  CG1 VAL A 329    12577  11427   8098  -1728   1166   -680       C  
ATOM   3644  CG2 VAL A 329      31.056  33.010 -55.263  1.00 77.00           C  
ANISOU 3644  CG2 VAL A 329    11807   9881   7568  -1281   1197   -619       C  
ATOM   3645  N   PHE A 330      28.516  35.103 -58.315  1.00 86.32           N  
ANISOU 3645  N   PHE A 330    12375  12101   8322  -1267   1050   -523       N  
ATOM   3646  CA  PHE A 330      27.307  35.506 -59.019  1.00 87.55           C  
ANISOU 3646  CA  PHE A 330    12298  12711   8258  -1324   1006   -488       C  
ATOM   3647  C   PHE A 330      27.576  36.136 -60.373  1.00 89.28           C  
ANISOU 3647  C   PHE A 330    12471  12983   8469  -1210   1004   -455       C  
ATOM   3648  O   PHE A 330      26.621  36.478 -61.078  1.00 95.26           O  
ANISOU 3648  O   PHE A 330    13029  14133   9031  -1243    973   -417       O  
ATOM   3649  CB  PHE A 330      26.492  36.465 -58.159  1.00 84.80           C  
ANISOU 3649  CB  PHE A 330    11719  12623   7878  -1127    950   -404       C  
ATOM   3650  CG  PHE A 330      25.989  35.838 -56.907  1.00 82.98           C  
ANISOU 3650  CG  PHE A 330    11493  12425   7611  -1268    944   -434       C  
ATOM   3651  CD1 PHE A 330      24.846  35.062 -56.924  1.00 84.90           C  
ANISOU 3651  CD1 PHE A 330    11642  13009   7607  -1570    934   -470       C  
ATOM   3652  CD2 PHE A 330      26.671  36.002 -55.716  1.00 80.83           C  
ANISOU 3652  CD2 PHE A 330    11320  11853   7540  -1118    949   -428       C  
ATOM   3653  CE1 PHE A 330      24.385  34.464 -55.767  1.00 85.89           C  
ANISOU 3653  CE1 PHE A 330    11779  13161   7694  -1712    932   -501       C  
ATOM   3654  CE2 PHE A 330      26.217  35.406 -54.563  1.00 81.80           C  
ANISOU 3654  CE2 PHE A 330    11451  12000   7631  -1246    946   -456       C  
ATOM   3655  CZ  PHE A 330      25.073  34.638 -54.588  1.00 84.19           C  
ANISOU 3655  CZ  PHE A 330    11666  12628   7693  -1540    938   -493       C  
ATOM   3656  N   GLY A 331      28.837  36.280 -60.765  1.00 86.88           N  
ANISOU 3656  N   GLY A 331    12337  12319   8356  -1080   1039   -463       N  
ATOM   3657  CA  GLY A 331      29.136  36.739 -62.107  1.00 88.91           C  
ANISOU 3657  CA  GLY A 331    12576  12606   8600  -1006   1043   -443       C  
ATOM   3658  C   GLY A 331      28.716  38.153 -62.429  1.00 89.48           C  
ANISOU 3658  C   GLY A 331    12438  12910   8650   -726   1000   -343       C  
ATOM   3659  O   GLY A 331      28.612  38.504 -63.604  1.00 91.00           O  
ANISOU 3659  O   GLY A 331    12569  13241   8767   -695    999   -321       O  
ATOM   3660  N   MET A 332      28.467  38.982 -61.425  1.00 92.72           N  
ANISOU 3660  N   MET A 332    12752  13362   9115   -513    974   -279       N  
ATOM   3661  CA  MET A 332      28.105  40.357 -61.707  1.00 99.41           C  
ANISOU 3661  CA  MET A 332    13446  14396   9930   -218    956   -176       C  
ATOM   3662  C   MET A 332      29.291  41.100 -62.313  1.00104.42           C  
ANISOU 3662  C   MET A 332    14208  14726  10741    -15    983   -158       C  
ATOM   3663  O   MET A 332      30.414  40.589 -62.382  1.00107.46           O  
ANISOU 3663  O   MET A 332    14779  14767  11283    -83   1009   -217       O  
ATOM   3664  CB  MET A 332      27.632  41.054 -60.438  1.00101.70           C  
ANISOU 3664  CB  MET A 332    13649  14757  10236    -34    939   -114       C  
ATOM   3665  CG  MET A 332      26.316  40.545 -59.916  1.00105.06           C  
ANISOU 3665  CG  MET A 332    13900  15562  10456   -192    908   -108       C  
ATOM   3666  SD  MET A 332      25.747  41.592 -58.573  1.00110.16           S  
ANISOU 3666  SD  MET A 332    14436  16309  11110     94    896    -11       S  
ATOM   3667  CE  MET A 332      25.581  43.153 -59.421  1.00110.97           C  
ANISOU 3667  CE  MET A 332    14449  16560  11154    469    920    114       C  
ATOM   3668  N   PHE A 333      29.019  42.321 -62.773  1.00104.77           N  
ANISOU 3668  N   PHE A 333    14153  14914  10741    244    985    -69       N  
ATOM   3669  CA  PHE A 333      30.013  43.185 -63.407  1.00104.90           C  
ANISOU 3669  CA  PHE A 333    14279  14686  10891    446   1014    -42       C  
ATOM   3670  C   PHE A 333      30.572  42.584 -64.690  1.00110.57           C  
ANISOU 3670  C   PHE A 333    15070  15326  11617    299   1026    -96       C  
ATOM   3671  O   PHE A 333      31.657  42.970 -65.133  1.00110.49           O  
ANISOU 3671  O   PHE A 333    15191  15039  11752    397   1051   -100       O  
ATOM   3672  CB  PHE A 333      31.167  43.512 -62.450  1.00 98.19           C  
ANISOU 3672  CB  PHE A 333    13602  13439  10269    549   1032    -56       C  
ATOM   3673  CG  PHE A 333      30.734  43.744 -61.038  1.00 92.59           C  
ANISOU 3673  CG  PHE A 333    12858  12753   9570    614   1021    -32       C  
ATOM   3674  CD1 PHE A 333      29.670  44.582 -60.753  1.00 91.57           C  
ANISOU 3674  CD1 PHE A 333    12586  12905   9301    795   1019     54       C  
ATOM   3675  CD2 PHE A 333      31.388  43.117 -59.991  1.00 88.59           C  
ANISOU 3675  CD2 PHE A 333    12461  11995   9203    510   1018    -87       C  
ATOM   3676  CE1 PHE A 333      29.268  44.790 -59.453  1.00 88.85           C  
ANISOU 3676  CE1 PHE A 333    12217  12580   8963    859   1012     78       C  
ATOM   3677  CE2 PHE A 333      30.992  43.325 -58.688  1.00 85.29           C  
ANISOU 3677  CE2 PHE A 333    12012  11598   8796    565   1007    -66       C  
ATOM   3678  CZ  PHE A 333      29.930  44.162 -58.418  1.00 86.56           C  
ANISOU 3678  CZ  PHE A 333    12037  12029   8823    735   1003     13       C  
ATOM   3679  N   ALA A 334      29.863  41.627 -65.291  1.00117.68           N  
ANISOU 3679  N   ALA A 334    15896  16466  12352     47   1012   -139       N  
ATOM   3680  CA  ALA A 334      30.321  41.050 -66.551  1.00123.26           C  
ANISOU 3680  CA  ALA A 334    16681  17110  13043   -101   1031   -191       C  
ATOM   3681  C   ALA A 334      30.150  42.042 -67.693  1.00129.69           C  
ANISOU 3681  C   ALA A 334    17397  18092  13788     91   1033   -120       C  
ATOM   3682  O   ALA A 334      31.124  42.437 -68.343  1.00132.20           O  
ANISOU 3682  O   ALA A 334    17831  18166  14234    198   1057   -120       O  
ATOM   3683  CB  ALA A 334      29.569  39.752 -66.843  1.00124.98           C  
ANISOU 3683  CB  ALA A 334    16871  17540  13077   -452   1026   -262       C  
ATOM   3684  N   HIS A 335      28.915  42.460 -67.950  1.00134.36           N  
ANISOU 3684  N   HIS A 335    17769  19115  14165    143   1011    -51       N  
ATOM   3685  CA  HIS A 335      28.614  43.505 -68.924  1.00139.84           C  
ANISOU 3685  CA  HIS A 335    18353  20013  14766    373   1020     38       C  
ATOM   3686  C   HIS A 335      27.955  44.640 -68.148  1.00142.29           C  
ANISOU 3686  C   HIS A 335    18549  20491  15023    674   1026    149       C  
ATOM   3687  O   HIS A 335      26.729  44.706 -68.039  1.00144.47           O  
ANISOU 3687  O   HIS A 335    18612  21197  15082    686   1007    211       O  
ATOM   3688  CB  HIS A 335      27.720  42.987 -70.051  1.00144.81           C  
ANISOU 3688  CB  HIS A 335    18818  21052  15152    183   1002     36       C  
ATOM   3689  CG  HIS A 335      27.369  44.026 -71.071  1.00147.91           C  
ANISOU 3689  CG  HIS A 335    19084  21684  15431    429   1015    137       C  
ATOM   3690  ND1 HIS A 335      26.386  44.970 -70.865  1.00149.50           N  
ANISOU 3690  ND1 HIS A 335    19090  22243  15470    687   1018    262       N  
ATOM   3691  CD2 HIS A 335      27.867  44.266 -72.308  1.00148.30           C  
ANISOU 3691  CD2 HIS A 335    19180  21669  15497    471   1034    138       C  
ATOM   3692  CE1 HIS A 335      26.295  45.748 -71.929  1.00150.53           C  
ANISOU 3692  CE1 HIS A 335    19158  22518  15518    885   1043    338       C  
ATOM   3693  NE2 HIS A 335      27.182  45.342 -72.819  1.00149.59           N  
ANISOU 3693  NE2 HIS A 335    19180  22147  15510    751   1048    261       N  
ATOM   3694  N   THR A 336      28.777  45.525 -67.597  1.00142.85           N  
ANISOU 3694  N   THR A 336    18769  20230  15277    912   1058    177       N  
ATOM   3695  CA  THR A 336      28.304  46.641 -66.794  1.00145.30           C  
ANISOU 3695  CA  THR A 336    19037  20617  15551   1210   1084    277       C  
ATOM   3696  C   THR A 336      28.443  47.937 -67.582  1.00147.53           C  
ANISOU 3696  C   THR A 336    19353  20899  15803   1524   1139    371       C  
ATOM   3697  O   THR A 336      29.462  48.171 -68.240  1.00146.16           O  
ANISOU 3697  O   THR A 336    19333  20439  15763   1545   1162    339       O  
ATOM   3698  CB  THR A 336      29.072  46.732 -65.467  1.00143.29           C  
ANISOU 3698  CB  THR A 336    18951  19993  15501   1234   1092    240       C  
ATOM   3699  OG1 THR A 336      28.731  47.949 -64.790  1.00143.15           O  
ANISOU 3699  OG1 THR A 336    18942  19998  15450   1542   1135    338       O  
ATOM   3700  CG2 THR A 336      30.580  46.678 -65.702  1.00140.58           C  
ANISOU 3700  CG2 THR A 336    18827  19201  15384   1189   1110    171       C  
ATOM   3701  N   GLU A 337      27.398  48.765 -67.531  1.00151.51           N  
ANISOU 3701  N   GLU A 337    19716  21738  16114   1776   1168    492       N  
ATOM   3702  CA  GLU A 337      27.450  50.054 -68.212  1.00154.22           C  
ANISOU 3702  CA  GLU A 337    20113  22081  16402   2111   1240    595       C  
ATOM   3703  C   GLU A 337      28.424  50.999 -67.522  1.00150.44           C  
ANISOU 3703  C   GLU A 337    19900  21154  16107   2300   1303    598       C  
ATOM   3704  O   GLU A 337      29.140  51.757 -68.187  1.00150.55           O  
ANISOU 3704  O   GLU A 337    20070  20952  16183   2442   1358    615       O  
ATOM   3705  CB  GLU A 337      26.054  50.671 -68.276  1.00160.39           C  
ANISOU 3705  CB  GLU A 337    20680  23354  16907   2359   1269    739       C  
ATOM   3706  CG  GLU A 337      25.042  49.838 -69.044  1.00165.79           C  
ANISOU 3706  CG  GLU A 337    21078  24547  17366   2168   1210    749       C  
ATOM   3707  CD  GLU A 337      23.665  50.473 -69.071  1.00171.56           C  
ANISOU 3707  CD  GLU A 337    21571  25814  17801   2434   1241    909       C  
ATOM   3708  OE1 GLU A 337      23.490  51.543 -68.450  1.00173.18           O  
ANISOU 3708  OE1 GLU A 337    21853  25965  17981   2784   1316   1013       O  
ATOM   3709  OE2 GLU A 337      22.758  49.904 -69.713  1.00174.42           O  
ANISOU 3709  OE2 GLU A 337    21671  26662  17939   2293   1196    935       O  
ATOM   3710  N   ASP A 338      28.473  50.962 -66.194  1.00146.42           N  
ANISOU 3710  N   ASP A 338    19451  20505  15677   2287   1299    580       N  
ATOM   3711  CA  ASP A 338      29.359  51.811 -65.404  1.00141.96           C  
ANISOU 3711  CA  ASP A 338    19137  19535  15267   2425   1358    577       C  
ATOM   3712  C   ASP A 338      30.455  50.924 -64.824  1.00132.45           C  
ANISOU 3712  C   ASP A 338    18039  17994  14291   2139   1304    447       C  
ATOM   3713  O   ASP A 338      30.341  50.421 -63.705  1.00131.86           O  
ANISOU 3713  O   ASP A 338    17947  17886  14269   2030   1271    412       O  
ATOM   3714  CB  ASP A 338      28.591  52.539 -64.302  1.00146.45           C  
ANISOU 3714  CB  ASP A 338    19707  20202  15735   2655   1406    665       C  
ATOM   3715  CG  ASP A 338      27.403  53.318 -64.833  1.00151.63           C  
ANISOU 3715  CG  ASP A 338    20231  21249  16132   2961   1466    811       C  
ATOM   3716  OD1 ASP A 338      27.424  53.703 -66.022  1.00153.64           O  
ANISOU 3716  OD1 ASP A 338    20478  21587  16312   3068   1498    854       O  
ATOM   3717  OD2 ASP A 338      26.447  53.547 -64.060  1.00153.82           O  
ANISOU 3717  OD2 ASP A 338    20411  21763  16272   3108   1484    891       O  
ATOM   3718  N   ARG A 339      31.523  50.732 -65.596  1.00123.88           N  
ANISOU 3718  N   ARG A 339    17063  16670  13335   2030   1300    384       N  
ATOM   3719  CA  ARG A 339      32.676  50.006 -65.084  1.00117.28           C  
ANISOU 3719  CA  ARG A 339    16342  15512  12706   1807   1266    281       C  
ATOM   3720  C   ARG A 339      33.582  50.887 -64.235  1.00112.99           C  
ANISOU 3720  C   ARG A 339    16008  14635  12288   1910   1315    284       C  
ATOM   3721  O   ARG A 339      34.323  50.363 -63.397  1.00113.68           O  
ANISOU 3721  O   ARG A 339    16160  14514  12517   1758   1288    219       O  
ATOM   3722  CB  ARG A 339      33.479  49.402 -66.233  1.00116.63           C  
ANISOU 3722  CB  ARG A 339    16289  15325  12699   1652   1247    220       C  
ATOM   3723  CG  ARG A 339      34.077  50.427 -67.161  1.00120.69           C  
ANISOU 3723  CG  ARG A 339    16922  15711  13225   1821   1304    258       C  
ATOM   3724  CD  ARG A 339      35.050  49.783 -68.122  1.00125.34           C  
ANISOU 3724  CD  ARG A 339    17558  16148  13917   1655   1284    190       C  
ATOM   3725  NE  ARG A 339      36.135  49.105 -67.413  1.00126.59           N  
ANISOU 3725  NE  ARG A 339    17814  16033  14252   1482   1261    114       N  
ATOM   3726  CZ  ARG A 339      37.296  49.673 -67.101  1.00125.25           C  
ANISOU 3726  CZ  ARG A 339    17804  15576  14209   1514   1292    104       C  
ATOM   3727  NH1 ARG A 339      37.528  50.937 -67.437  1.00126.06           N  
ANISOU 3727  NH1 ARG A 339    18015  15596  14285   1696   1351    154       N  
ATOM   3728  NH2 ARG A 339      38.223  48.978 -66.453  1.00121.84           N  
ANISOU 3728  NH2 ARG A 339    17428  14951  13913   1362   1270     47       N  
ATOM   3729  N   GLU A 340      33.539  52.206 -64.433  1.00108.81           N  
ANISOU 3729  N   GLU A 340    15595  14056  11692   2160   1395    359       N  
ATOM   3730  CA  GLU A 340      34.354  53.105 -63.623  1.00104.23           C  
ANISOU 3730  CA  GLU A 340    15239  13164  11198   2234   1455    358       C  
ATOM   3731  C   GLU A 340      33.920  53.070 -62.167  1.00 97.13           C  
ANISOU 3731  C   GLU A 340    14334  12270  10299   2240   1448    364       C  
ATOM   3732  O   GLU A 340      34.760  53.084 -61.260  1.00 97.90           O  
ANISOU 3732  O   GLU A 340    14555  12120  10523   2140   1447    316       O  
ATOM   3733  CB  GLU A 340      34.268  54.528 -64.172  1.00109.86           C  
ANISOU 3733  CB  GLU A 340    16110  13828  11805   2503   1561    441       C  
ATOM   3734  CG  GLU A 340      34.761  54.675 -65.601  1.00114.76           C  
ANISOU 3734  CG  GLU A 340    16757  14420  12428   2510   1575    437       C  
ATOM   3735  CD  GLU A 340      36.242  54.376 -65.748  1.00116.61           C  
ANISOU 3735  CD  GLU A 340    17108  14354  12844   2303   1551    349       C  
ATOM   3736  OE1 GLU A 340      37.045  54.911 -64.951  1.00117.26           O  
ANISOU 3736  OE1 GLU A 340    17371  14180  13003   2275   1588    327       O  
ATOM   3737  OE2 GLU A 340      36.600  53.598 -66.657  1.00117.76           O  
ANISOU 3737  OE2 GLU A 340    17162  14537  13043   2166   1499    305       O  
ATOM   3738  N   THR A 341      32.607  53.023 -61.928  1.00 92.10           N  
ANISOU 3738  N   THR A 341    13543  11938   9512   2355   1444    427       N  
ATOM   3739  CA  THR A 341      32.090  52.928 -60.568  1.00 91.29           C  
ANISOU 3739  CA  THR A 341    13414  11875   9398   2363   1434    437       C  
ATOM   3740  C   THR A 341      32.515  51.625 -59.903  1.00 88.59           C  
ANISOU 3740  C   THR A 341    12995  11467   9198   2071   1343    338       C  
ATOM   3741  O   THR A 341      32.912  51.616 -58.731  1.00 88.97           O  
ANISOU 3741  O   THR A 341    13126  11342   9337   2017   1340    308       O  
ATOM   3742  CB  THR A 341      30.568  53.041 -60.593  1.00 95.18           C  
ANISOU 3742  CB  THR A 341    13721  12763   9680   2536   1442    531       C  
ATOM   3743  OG1 THR A 341      30.198  54.288 -61.187  1.00 99.54           O  
ANISOU 3743  OG1 THR A 341    14364  13369  10086   2847   1543    638       O  
ATOM   3744  CG2 THR A 341      29.994  52.951 -59.187  1.00 94.60           C  
ANISOU 3744  CG2 THR A 341    13614  12742   9587   2553   1433    545       C  
ATOM   3745  N   VAL A 342      32.439  50.512 -60.638  1.00 87.97           N  
ANISOU 3745  N   VAL A 342    12775  11523   9128   1882   1278    288       N  
ATOM   3746  CA  VAL A 342      32.835  49.224 -60.081  1.00 86.66           C  
ANISOU 3746  CA  VAL A 342    12567  11284   9077   1617   1211    199       C  
ATOM   3747  C   VAL A 342      34.329  49.204 -59.794  1.00 82.43           C  
ANISOU 3747  C   VAL A 342    12202  10388   8729   1525   1218    140       C  
ATOM   3748  O   VAL A 342      34.770  48.674 -58.765  1.00 81.53           O  
ANISOU 3748  O   VAL A 342    12118  10144   8716   1406   1194     96       O  
ATOM   3749  CB  VAL A 342      32.425  48.082 -61.026  1.00 90.55           C  
ANISOU 3749  CB  VAL A 342    12915  11982   9509   1434   1161    159       C  
ATOM   3750  CG1 VAL A 342      32.748  46.741 -60.395  1.00 89.01           C  
ANISOU 3750  CG1 VAL A 342    12712  11703   9407   1175   1113     73       C  
ATOM   3751  CG2 VAL A 342      30.949  48.183 -61.375  1.00 93.69           C  
ANISOU 3751  CG2 VAL A 342    13120  12789   9690   1518   1154    227       C  
ATOM   3752  N   TYR A 343      35.137  49.786 -60.687  1.00 79.24           N  
ANISOU 3752  N   TYR A 343    11906   9837   8365   1578   1254    144       N  
ATOM   3753  CA  TYR A 343      36.571  49.810 -60.427  1.00 77.48           C  
ANISOU 3753  CA  TYR A 343    11826   9315   8298   1487   1262     98       C  
ATOM   3754  C   TYR A 343      36.896  50.698 -59.230  1.00 76.73           C  
ANISOU 3754  C   TYR A 343    11862   9058   8234   1562   1301    116       C  
ATOM   3755  O   TYR A 343      37.807  50.388 -58.450  1.00 77.89           O  
ANISOU 3755  O   TYR A 343    12066   9032   8495   1440   1285     74       O  
ATOM   3756  CB  TYR A 343      37.336  50.258 -61.668  1.00 78.76           C  
ANISOU 3756  CB  TYR A 343    12068   9376   8480   1518   1292     99       C  
ATOM   3757  CG  TYR A 343      38.793  49.848 -61.628  1.00 83.19           C  
ANISOU 3757  CG  TYR A 343    12713   9707   9189   1373   1282     46       C  
ATOM   3758  CD1 TYR A 343      39.188  48.559 -61.988  1.00 84.02           C  
ANISOU 3758  CD1 TYR A 343    12752   9815   9358   1209   1239     -4       C  
ATOM   3759  CD2 TYR A 343      39.773  50.744 -61.214  1.00 84.89           C  
ANISOU 3759  CD2 TYR A 343    13081   9714   9458   1397   1323     51       C  
ATOM   3760  CE1 TYR A 343      40.521  48.181 -61.941  1.00 85.89           C  
ANISOU 3760  CE1 TYR A 343    13056   9867   9711   1108   1239    -35       C  
ATOM   3761  CE2 TYR A 343      41.105  50.378 -61.168  1.00 85.44           C  
ANISOU 3761  CE2 TYR A 343    13199   9624   9640   1266   1313     15       C  
ATOM   3762  CZ  TYR A 343      41.474  49.098 -61.528  1.00 87.78           C  
ANISOU 3762  CZ  TYR A 343    13411   9943  10000   1139   1271    -22       C  
ATOM   3763  OH  TYR A 343      42.802  48.739 -61.475  1.00 90.61           O  
ANISOU 3763  OH  TYR A 343    13809  10167  10452   1041   1270    -42       O  
ATOM   3764  N   ALA A 344      36.149  51.794 -59.056  1.00 71.92           N  
ANISOU 3764  N   ALA A 344    11306   8510   7508   1767   1358    183       N  
ATOM   3765  CA  ALA A 344      36.337  52.632 -57.879  1.00 73.58           C  
ANISOU 3765  CA  ALA A 344    11664   8569   7725   1834   1407    199       C  
ATOM   3766  C   ALA A 344      35.979  51.880 -56.604  1.00 73.41           C  
ANISOU 3766  C   ALA A 344    11551   8599   7744   1737   1355    174       C  
ATOM   3767  O   ALA A 344      36.687  51.989 -55.595  1.00 73.05           O  
ANISOU 3767  O   ALA A 344    11600   8376   7781   1657   1358    145       O  
ATOM   3768  CB  ALA A 344      35.502  53.904 -57.997  1.00 76.54           C  
ANISOU 3768  CB  ALA A 344    12134   9006   7941   2101   1497    286       C  
ATOM   3769  N   TRP A 345      34.871  51.125 -56.628  1.00 74.64           N  
ANISOU 3769  N   TRP A 345    11520   9011   7828   1732   1308    186       N  
ATOM   3770  CA  TRP A 345      34.495  50.300 -55.480  1.00 74.55           C  
ANISOU 3770  CA  TRP A 345    11416   9060   7851   1621   1256    157       C  
ATOM   3771  C   TRP A 345      35.573  49.285 -55.151  1.00 69.94           C  
ANISOU 3771  C   TRP A 345    10842   8309   7422   1397   1209     79       C  
ATOM   3772  O   TRP A 345      35.880  49.055 -53.978  1.00 69.96           O  
ANISOU 3772  O   TRP A 345    10871   8215   7494   1328   1195     56       O  
ATOM   3773  CB  TRP A 345      33.181  49.577 -55.743  1.00 77.14           C  
ANISOU 3773  CB  TRP A 345    11540   9712   8059   1610   1214    176       C  
ATOM   3774  CG  TRP A 345      31.994  50.362 -55.344  1.00 82.65           C  
ANISOU 3774  CG  TRP A 345    12193  10610   8602   1824   1252    260       C  
ATOM   3775  CD1 TRP A 345      31.146  51.044 -56.173  1.00 87.52           C  
ANISOU 3775  CD1 TRP A 345    12754  11445   9055   2026   1293    342       C  
ATOM   3776  CD2 TRP A 345      31.501  50.557 -54.013  1.00 82.95           C  
ANISOU 3776  CD2 TRP A 345    12233  10664   8619   1878   1258    282       C  
ATOM   3777  NE1 TRP A 345      30.152  51.646 -55.436  1.00 90.02           N  
ANISOU 3777  NE1 TRP A 345    13039  11921   9242   2218   1331    421       N  
ATOM   3778  CE2 TRP A 345      30.351  51.365 -54.110  1.00 85.93           C  
ANISOU 3778  CE2 TRP A 345    12561  11275   8814   2126   1309    382       C  
ATOM   3779  CE3 TRP A 345      31.924  50.133 -52.748  1.00 80.79           C  
ANISOU 3779  CE3 TRP A 345    12001  10239   8458   1753   1230    232       C  
ATOM   3780  CZ2 TRP A 345      29.621  51.754 -52.994  1.00 87.36           C  
ANISOU 3780  CZ2 TRP A 345    12737  11533   8922   2251   1334    433       C  
ATOM   3781  CZ3 TRP A 345      31.200  50.523 -51.644  1.00 81.15           C  
ANISOU 3781  CZ3 TRP A 345    12040  10354   8440   1861   1249    275       C  
ATOM   3782  CH2 TRP A 345      30.061  51.326 -51.772  1.00 84.16           C  
ANISOU 3782  CH2 TRP A 345    12377  10959   8639   2108   1301    374       C  
ATOM   3783  N   PHE A 346      36.161  48.665 -56.172  1.00 69.53           N  
ANISOU 3783  N   PHE A 346    10772   8230   7418   1296   1190     44       N  
ATOM   3784  CA  PHE A 346      37.205  47.679 -55.915  1.00 68.40           C  
ANISOU 3784  CA  PHE A 346    10647   7939   7404   1117   1161    -14       C  
ATOM   3785  C   PHE A 346      38.463  48.329 -55.347  1.00 69.87           C  
ANISOU 3785  C   PHE A 346    10969   7894   7685   1114   1188    -18       C  
ATOM   3786  O   PHE A 346      39.054  47.811 -54.389  1.00 71.60           O  
ANISOU 3786  O   PHE A 346    11195   8025   7984   1016   1170    -43       O  
ATOM   3787  CB  PHE A 346      37.515  46.891 -57.189  1.00 68.64           C  
ANISOU 3787  CB  PHE A 346    10643   7992   7444   1027   1148    -43       C  
ATOM   3788  CG  PHE A 346      36.640  45.680 -57.372  1.00 69.05           C  
ANISOU 3788  CG  PHE A 346    10581   8223   7434    906   1113    -73       C  
ATOM   3789  CD1 PHE A 346      35.397  45.792 -57.970  1.00 72.15           C  
ANISOU 3789  CD1 PHE A 346    10862   8868   7682    951   1105    -46       C  
ATOM   3790  CD2 PHE A 346      37.048  44.435 -56.924  1.00 65.47           C  
ANISOU 3790  CD2 PHE A 346    10136   7695   7044    744   1097   -122       C  
ATOM   3791  CE1 PHE A 346      34.589  44.678 -58.142  1.00 71.47           C  
ANISOU 3791  CE1 PHE A 346    10675   8966   7514    799   1075    -79       C  
ATOM   3792  CE2 PHE A 346      36.244  43.325 -57.089  1.00 64.13           C  
ANISOU 3792  CE2 PHE A 346     9898   7672   6797    606   1078   -156       C  
ATOM   3793  CZ  PHE A 346      35.014  43.446 -57.698  1.00 67.36           C  
ANISOU 3793  CZ  PHE A 346    10195   8341   7059    616   1064   -139       C  
ATOM   3794  N   THR A 347      38.893  49.462 -55.915  1.00 68.06           N  
ANISOU 3794  N   THR A 347    10850   7578   7433   1210   1236      9       N  
ATOM   3795  CA  THR A 347      40.087  50.118 -55.388  1.00 65.55           C  
ANISOU 3795  CA  THR A 347    10665   7063   7177   1171   1266      2       C  
ATOM   3796  C   THR A 347      39.855  50.592 -53.958  1.00 61.11           C  
ANISOU 3796  C   THR A 347    10156   6458   6603   1188   1279     11       C  
ATOM   3797  O   THR A 347      40.757  50.505 -53.111  1.00 64.95           O  
ANISOU 3797  O   THR A 347    10683   6837   7158   1081   1273    -10       O  
ATOM   3798  CB  THR A 347      40.514  51.279 -56.291  1.00 66.60           C  
ANISOU 3798  CB  THR A 347    10931   7109   7265   1255   1326     25       C  
ATOM   3799  OG1 THR A 347      39.457  52.237 -56.370  1.00 72.83           O  
ANISOU 3799  OG1 THR A 347    11776   7961   7933   1438   1377     74       O  
ATOM   3800  CG2 THR A 347      40.846  50.770 -57.688  1.00 61.43           C  
ANISOU 3800  CG2 THR A 347    10221   6487   6631   1227   1310     14       C  
ATOM   3801  N   PHE A 348      38.640  51.067 -53.664  1.00 59.90           N  
ANISOU 3801  N   PHE A 348     9995   6411   6355   1325   1299     47       N  
ATOM   3802  CA  PHE A 348      38.306  51.459 -52.299  1.00 62.69           C  
ANISOU 3802  CA  PHE A 348    10398   6733   6689   1351   1314     58       C  
ATOM   3803  C   PHE A 348      38.347  50.267 -51.354  1.00 62.53           C  
ANISOU 3803  C   PHE A 348    10256   6752   6750   1214   1247     21       C  
ATOM   3804  O   PHE A 348      38.838  50.382 -50.228  1.00 66.88           O  
ANISOU 3804  O   PHE A 348    10861   7205   7346   1149   1248      8       O  
ATOM   3805  CB  PHE A 348      36.928  52.121 -52.246  1.00 64.65           C  
ANISOU 3805  CB  PHE A 348    10645   7119   6802   1553   1354    117       C  
ATOM   3806  CG  PHE A 348      36.411  52.326 -50.837  1.00 68.43           C  
ANISOU 3806  CG  PHE A 348    11147   7598   7256   1586   1363    130       C  
ATOM   3807  CD1 PHE A 348      36.966  53.295 -50.012  1.00 71.53           C  
ANISOU 3807  CD1 PHE A 348    11737   7799   7641   1596   1425    132       C  
ATOM   3808  CD2 PHE A 348      35.373  51.552 -50.338  1.00 68.25           C  
ANISOU 3808  CD2 PHE A 348    10956   7770   7207   1592   1312    137       C  
ATOM   3809  CE1 PHE A 348      36.494  53.486 -48.718  1.00 73.80           C  
ANISOU 3809  CE1 PHE A 348    12056   8081   7904   1625   1437    144       C  
ATOM   3810  CE2 PHE A 348      34.900  51.741 -49.036  1.00 72.28           C  
ANISOU 3810  CE2 PHE A 348    11485   8282   7695   1627   1320    151       C  
ATOM   3811  CZ  PHE A 348      35.463  52.706 -48.231  1.00 72.14           C  
ANISOU 3811  CZ  PHE A 348    11666   8064   7679   1651   1382    155       C  
ATOM   3812  N   SER A 349      37.825  49.114 -51.784  1.00 60.71           N  
ANISOU 3812  N   SER A 349     9875   6664   6529   1159   1195      3       N  
ATOM   3813  CA  SER A 349      37.832  47.953 -50.899  1.00 62.57           C  
ANISOU 3813  CA  SER A 349    10024   6923   6829   1031   1146    -31       C  
ATOM   3814  C   SER A 349      39.260  47.474 -50.639  1.00 63.55           C  
ANISOU 3814  C   SER A 349    10189   6892   7065    906   1138    -61       C  
ATOM   3815  O   SER A 349      39.588  47.062 -49.516  1.00 67.74           O  
ANISOU 3815  O   SER A 349    10711   7380   7648    836   1122    -74       O  
ATOM   3816  CB  SER A 349      36.964  46.842 -51.487  1.00 61.25           C  
ANISOU 3816  CB  SER A 349     9722   6932   6618    977   1108    -48       C  
ATOM   3817  OG  SER A 349      37.637  46.171 -52.537  1.00 65.78           O  
ANISOU 3817  OG  SER A 349    10294   7464   7233    894   1103    -75       O  
ATOM   3818  N   HIS A 350      40.132  47.564 -51.651  1.00 57.15           N  
ANISOU 3818  N   HIS A 350     9418   6015   6283    886   1153    -64       N  
ATOM   3819  CA  HIS A 350      41.549  47.236 -51.452  1.00 59.57           C  
ANISOU 3819  CA  HIS A 350     9754   6208   6674    790   1153    -76       C  
ATOM   3820  C   HIS A 350      42.180  48.148 -50.404  1.00 62.30           C  
ANISOU 3820  C   HIS A 350    10184   6463   7026    771   1173    -66       C  
ATOM   3821  O   HIS A 350      42.821  47.681 -49.436  1.00 60.95           O  
ANISOU 3821  O   HIS A 350     9988   6267   6904    689   1157    -71       O  
ATOM   3822  CB  HIS A 350      42.310  47.355 -52.777  1.00 55.83           C  
ANISOU 3822  CB  HIS A 350     9310   5695   6210    788   1170    -73       C  
ATOM   3823  CG  HIS A 350      41.779  46.473 -53.860  1.00 60.67           C  
ANISOU 3823  CG  HIS A 350     9857   6388   6806    787   1157    -87       C  
ATOM   3824  ND1 HIS A 350      42.064  46.669 -55.193  1.00 62.50           N  
ANISOU 3824  ND1 HIS A 350    10110   6613   7025    813   1172    -84       N  
ATOM   3825  CD2 HIS A 350      40.992  45.373 -53.800  1.00 61.86           C  
ANISOU 3825  CD2 HIS A 350     9933   6629   6941    742   1133   -108       C  
ATOM   3826  CE1 HIS A 350      41.470  45.729 -55.910  1.00 61.87           C  
ANISOU 3826  CE1 HIS A 350     9969   6617   6920    783   1158   -102       C  
ATOM   3827  NE2 HIS A 350      40.812  44.933 -55.087  1.00 64.26           N  
ANISOU 3827  NE2 HIS A 350    10220   6981   7216    731   1136   -119       N  
ATOM   3828  N   TRP A 351      42.001  49.466 -50.589  1.00 59.87           N  
ANISOU 3828  N   TRP A 351     9991   6106   6652    846   1218    -49       N  
ATOM   3829  CA  TRP A 351      42.539  50.419 -49.627  1.00 61.99           C  
ANISOU 3829  CA  TRP A 351    10378   6277   6899    807   1252    -45       C  
ATOM   3830  C   TRP A 351      41.977  50.191 -48.226  1.00 61.95           C  
ANISOU 3830  C   TRP A 351    10342   6297   6899    798   1233    -48       C  
ATOM   3831  O   TRP A 351      42.727  50.263 -47.251  1.00 61.10           O  
ANISOU 3831  O   TRP A 351    10259   6140   6814    697   1231    -55       O  
ATOM   3832  CB  TRP A 351      42.260  51.850 -50.076  1.00 60.94           C  
ANISOU 3832  CB  TRP A 351    10416   6069   6670    904   1324    -25       C  
ATOM   3833  CG  TRP A 351      42.746  52.884 -49.101  1.00 59.89           C  
ANISOU 3833  CG  TRP A 351    10449   5817   6488    845   1376    -27       C  
ATOM   3834  CD1 TRP A 351      44.004  53.391 -49.012  1.00 59.93           C  
ANISOU 3834  CD1 TRP A 351    10551   5735   6486    702   1402    -41       C  
ATOM   3835  CD2 TRP A 351      41.990  53.499 -48.047  1.00 60.71           C  
ANISOU 3835  CD2 TRP A 351    10648   5889   6529    910   1412    -16       C  
ATOM   3836  NE1 TRP A 351      44.075  54.306 -47.994  1.00 64.09           N  
ANISOU 3836  NE1 TRP A 351    11240   6169   6942    655   1455    -45       N  
ATOM   3837  CE2 TRP A 351      42.855  54.389 -47.379  1.00 63.44           C  
ANISOU 3837  CE2 TRP A 351    11169   6107   6830    790   1465    -29       C  
ATOM   3838  CE3 TRP A 351      40.667  53.394 -47.615  1.00 59.68           C  
ANISOU 3838  CE3 TRP A 351    10472   5840   6363   1052   1409      8       C  
ATOM   3839  CZ2 TRP A 351      42.438  55.180 -46.308  1.00 62.50           C  
ANISOU 3839  CZ2 TRP A 351    11204   5909   6635    812   1521    -24       C  
ATOM   3840  CZ3 TRP A 351      40.255  54.169 -46.535  1.00 60.01           C  
ANISOU 3840  CZ3 TRP A 351    10650   5815   6336   1095   1461     20       C  
ATOM   3841  CH2 TRP A 351      41.139  55.052 -45.898  1.00 61.31           C  
ANISOU 3841  CH2 TRP A 351    11012   5824   6461    978   1519      3       C  
ATOM   3842  N   LEU A 352      40.680  49.888 -48.109  1.00 63.13           N  
ANISOU 3842  N   LEU A 352    10425   6545   7018    893   1217    -39       N  
ATOM   3843  CA  LEU A 352      40.074  49.673 -46.798  1.00 64.60           C  
ANISOU 3843  CA  LEU A 352    10578   6764   7203    891   1199    -40       C  
ATOM   3844  C   LEU A 352      40.697  48.471 -46.103  1.00 59.34           C  
ANISOU 3844  C   LEU A 352     9809   6108   6628    762   1149    -64       C  
ATOM   3845  O   LEU A 352      40.961  48.506 -44.889  1.00 57.61           O  
ANISOU 3845  O   LEU A 352     9603   5856   6428    707   1143    -68       O  
ATOM   3846  CB  LEU A 352      38.566  49.488 -46.942  1.00 67.29           C  
ANISOU 3846  CB  LEU A 352    10840   7249   7478   1010   1189    -21       C  
ATOM   3847  CG  LEU A 352      37.776  49.683 -45.651  1.00 69.19           C  
ANISOU 3847  CG  LEU A 352    11082   7524   7684   1054   1190     -9       C  
ATOM   3848  CD1 LEU A 352      37.984  51.105 -45.117  1.00 67.15           C  
ANISOU 3848  CD1 LEU A 352    11016   7135   7364   1122   1262     14       C  
ATOM   3849  CD2 LEU A 352      36.294  49.390 -45.850  1.00 70.32           C  
ANISOU 3849  CD2 LEU A 352    11110   7862   7745   1161   1174     17       C  
ATOM   3850  N   VAL A 353      40.986  47.415 -46.869  1.00 59.33           N  
ANISOU 3850  N   VAL A 353     9723   6147   6673    718   1122    -77       N  
ATOM   3851  CA  VAL A 353      41.716  46.277 -46.307  1.00 59.16           C  
ANISOU 3851  CA  VAL A 353     9635   6119   6724    621   1096    -88       C  
ATOM   3852  C   VAL A 353      43.054  46.730 -45.737  1.00 62.23           C  
ANISOU 3852  C   VAL A 353    10068   6440   7138    550   1110    -76       C  
ATOM   3853  O   VAL A 353      43.426  46.365 -44.617  1.00 67.85           O  
ANISOU 3853  O   VAL A 353    10746   7156   7876    495   1097    -73       O  
ATOM   3854  CB  VAL A 353      41.901  45.175 -47.362  1.00 56.44           C  
ANISOU 3854  CB  VAL A 353     9239   5802   6405    599   1089    -98       C  
ATOM   3855  CG1 VAL A 353      42.884  44.124 -46.865  1.00 52.72           C  
ANISOU 3855  CG1 VAL A 353     8736   5304   5991    532   1088    -93       C  
ATOM   3856  CG2 VAL A 353      40.573  44.544 -47.694  1.00 57.35           C  
ANISOU 3856  CG2 VAL A 353     9299   6014   6476    617   1072   -115       C  
ATOM   3857  N   TYR A 354      43.799  47.534 -46.492  1.00 59.26           N  
ANISOU 3857  N   TYR A 354     9760   6015   6740    541   1137    -68       N  
ATOM   3858  CA  TYR A 354      45.110  47.942 -45.977  1.00 57.18           C  
ANISOU 3858  CA  TYR A 354     9523   5725   6476    441   1150    -56       C  
ATOM   3859  C   TYR A 354      44.993  48.922 -44.814  1.00 61.06           C  
ANISOU 3859  C   TYR A 354    10103   6175   6921    399   1168    -60       C  
ATOM   3860  O   TYR A 354      45.857  48.941 -43.930  1.00 59.98           O  
ANISOU 3860  O   TYR A 354     9950   6058   6782    293   1164    -53       O  
ATOM   3861  CB  TYR A 354      45.965  48.545 -47.092  1.00 59.45           C  
ANISOU 3861  CB  TYR A 354     9865   5983   6740    417   1177    -48       C  
ATOM   3862  CG  TYR A 354      46.413  47.498 -48.075  1.00 60.38           C  
ANISOU 3862  CG  TYR A 354     9895   6143   6905    436   1164    -38       C  
ATOM   3863  CD1 TYR A 354      47.056  46.340 -47.648  1.00 59.98           C  
ANISOU 3863  CD1 TYR A 354     9745   6147   6896    410   1148    -18       C  
ATOM   3864  CD2 TYR A 354      46.167  47.645 -49.427  1.00 56.96           C  
ANISOU 3864  CD2 TYR A 354     9490   5691   6463    495   1176    -43       C  
ATOM   3865  CE1 TYR A 354      47.458  45.371 -48.555  1.00 59.34           C  
ANISOU 3865  CE1 TYR A 354     9617   6086   6843    443   1153     -4       C  
ATOM   3866  CE2 TYR A 354      46.557  46.685 -50.328  1.00 59.15           C  
ANISOU 3866  CE2 TYR A 354     9706   5993   6774    510   1171    -36       C  
ATOM   3867  CZ  TYR A 354      47.196  45.552 -49.895  1.00 58.10           C  
ANISOU 3867  CZ  TYR A 354     9497   5900   6679    486   1164    -17       C  
ATOM   3868  OH  TYR A 354      47.569  44.608 -50.812  1.00 63.18           O  
ANISOU 3868  OH  TYR A 354    10113   6551   7342    516   1177     -5       O  
ATOM   3869  N   ALA A 355      43.947  49.746 -44.799  1.00 61.92           N  
ANISOU 3869  N   ALA A 355    10311   6238   6977    484   1195    -66       N  
ATOM   3870  CA  ALA A 355      43.760  50.680 -43.697  1.00 61.13           C  
ANISOU 3870  CA  ALA A 355    10329   6080   6820    458   1227    -69       C  
ATOM   3871  C   ALA A 355      43.423  49.957 -42.407  1.00 60.69           C  
ANISOU 3871  C   ALA A 355    10180   6074   6804    435   1187    -72       C  
ATOM   3872  O   ALA A 355      43.642  50.510 -41.328  1.00 60.25           O  
ANISOU 3872  O   ALA A 355    10196   5982   6714    366   1204    -76       O  
ATOM   3873  CB  ALA A 355      42.663  51.699 -44.019  1.00 57.50           C  
ANISOU 3873  CB  ALA A 355    10008   5562   6277    599   1282    -60       C  
ATOM   3874  N   ASN A 356      42.875  48.745 -42.493  1.00 64.94           N  
ANISOU 3874  N   ASN A 356    10579   6692   7404    482   1141    -73       N  
ATOM   3875  CA  ASN A 356      42.706  47.957 -41.274  1.00 62.65           C  
ANISOU 3875  CA  ASN A 356    10203   6446   7154    446   1106    -76       C  
ATOM   3876  C   ASN A 356      44.034  47.775 -40.533  1.00 64.68           C  
ANISOU 3876  C   ASN A 356    10430   6715   7431    321   1099    -67       C  
ATOM   3877  O   ASN A 356      44.090  47.867 -39.290  1.00 71.29           O  
ANISOU 3877  O   ASN A 356    11267   7559   8262    268   1093    -67       O  
ATOM   3878  CB  ASN A 356      42.089  46.601 -41.603  1.00 59.89           C  
ANISOU 3878  CB  ASN A 356     9734   6169   6853    484   1070    -82       C  
ATOM   3879  CG  ASN A 356      41.836  45.776 -40.353  1.00 60.40           C  
ANISOU 3879  CG  ASN A 356     9729   6269   6951    452   1043    -86       C  
ATOM   3880  OD1 ASN A 356      40.842  45.988 -39.662  1.00 64.24           O  
ANISOU 3880  OD1 ASN A 356    10221   6775   7413    490   1036    -92       O  
ATOM   3881  ND2 ASN A 356      42.753  44.874 -40.030  1.00 54.25           N  
ANISOU 3881  ND2 ASN A 356     8890   5506   6218    394   1034    -75       N  
ATOM   3882  N   SER A 357      45.112  47.508 -41.282  1.00 64.59           N  
ANISOU 3882  N   SER A 357    10382   6727   7433    276   1102    -52       N  
ATOM   3883  CA  SER A 357      46.428  47.342 -40.670  1.00 65.10           C  
ANISOU 3883  CA  SER A 357    10391   6854   7492    166   1098    -28       C  
ATOM   3884  C   SER A 357      46.902  48.614 -39.977  1.00 64.31           C  
ANISOU 3884  C   SER A 357    10397   6727   7312     47   1125    -36       C  
ATOM   3885  O   SER A 357      47.641  48.543 -38.988  1.00 67.10           O  
ANISOU 3885  O   SER A 357    10700   7153   7642    -58   1116    -21       O  
ATOM   3886  CB  SER A 357      47.455  46.916 -41.718  1.00 62.13           C  
ANISOU 3886  CB  SER A 357     9957   6526   7124    158   1104     -2       C  
ATOM   3887  OG  SER A 357      47.119  45.668 -42.302  1.00 70.83           O  
ANISOU 3887  OG  SER A 357    10988   7641   8284    252   1093      5       O  
ATOM   3888  N   ALA A 358      46.522  49.782 -40.497  1.00 58.87           N  
ANISOU 3888  N   ALA A 358     9866   5937   6565     55   1166    -57       N  
ATOM   3889  CA  ALA A 358      46.901  51.031 -39.847  1.00 62.29           C  
ANISOU 3889  CA  ALA A 358    10453   6313   6900    -71   1212    -71       C  
ATOM   3890  C   ALA A 358      46.010  51.325 -38.649  1.00 66.88           C  
ANISOU 3890  C   ALA A 358    11103   6844   7465    -46   1220    -85       C  
ATOM   3891  O   ALA A 358      46.456  51.959 -37.684  1.00 69.87           O  
ANISOU 3891  O   ALA A 358    11564   7209   7773   -182   1243    -94       O  
ATOM   3892  CB  ALA A 358      46.841  52.186 -40.852  1.00 58.94           C  
ANISOU 3892  CB  ALA A 358    10214   5776   6403    -60   1274    -85       C  
ATOM   3893  N   ALA A 359      44.762  50.853 -38.696  1.00 67.91           N  
ANISOU 3893  N   ALA A 359    11196   6961   7646    115   1201    -85       N  
ATOM   3894  CA  ALA A 359      43.787  51.127 -37.650  1.00 68.27           C  
ANISOU 3894  CA  ALA A 359    11299   6969   7671    168   1211    -91       C  
ATOM   3895  C   ALA A 359      44.067  50.345 -36.375  1.00 67.75           C  
ANISOU 3895  C   ALA A 359    11111   6982   7651     90   1164    -89       C  
ATOM   3896  O   ALA A 359      43.871  50.882 -35.278  1.00 66.06           O  
ANISOU 3896  O   ALA A 359    10979   6730   7390     43   1183    -98       O  
ATOM   3897  CB  ALA A 359      42.380  50.803 -38.154  1.00 68.05           C  
ANISOU 3897  CB  ALA A 359    11237   6953   7666    356   1202    -84       C  
ATOM   3898  N   ASN A 360      44.519  49.090 -36.487  1.00 68.10           N  
ANISOU 3898  N   ASN A 360    10975   7127   7774     84   1112    -75       N  
ATOM   3899  CA  ASN A 360      44.690  48.288 -35.269  1.00 63.22           C  
ANISOU 3899  CA  ASN A 360    10245   6583   7193     41   1076    -65       C  
ATOM   3900  C   ASN A 360      45.592  48.935 -34.214  1.00 61.53           C  
ANISOU 3900  C   ASN A 360    10071   6396   6913   -120   1090    -63       C  
ATOM   3901  O   ASN A 360      45.179  48.998 -33.042  1.00 63.94           O  
ANISOU 3901  O   ASN A 360    10389   6695   7210   -140   1083    -70       O  
ATOM   3902  CB  ASN A 360      45.197  46.887 -35.615  1.00 60.30           C  
ANISOU 3902  CB  ASN A 360     9713   6305   6894     69   1042    -40       C  
ATOM   3903  CG  ASN A 360      44.127  46.005 -36.221  1.00 66.05           C  
ANISOU 3903  CG  ASN A 360    10399   7018   7677    193   1026    -50       C  
ATOM   3904  OD1 ASN A 360      42.926  46.252 -36.066  1.00 63.33           O  
ANISOU 3904  OD1 ASN A 360    10098   6640   7326    258   1024    -70       O  
ATOM   3905  ND2 ASN A 360      44.565  44.945 -36.909  1.00 69.05           N  
ANISOU 3905  ND2 ASN A 360    10700   7438   8098    222   1021    -33       N  
ATOM   3906  N   PRO A 361      46.809  49.401 -34.521  1.00 62.87           N  
ANISOU 3906  N   PRO A 361    10253   6612   7022   -253   1107    -52       N  
ATOM   3907  CA  PRO A 361      47.625  50.026 -33.459  1.00 61.83           C  
ANISOU 3907  CA  PRO A 361    10157   6536   6801   -440   1120    -53       C  
ATOM   3908  C   PRO A 361      46.987  51.270 -32.843  1.00 63.78           C  
ANISOU 3908  C   PRO A 361    10627   6641   6966   -491   1173    -91       C  
ATOM   3909  O   PRO A 361      47.174  51.526 -31.643  1.00 63.23           O  
ANISOU 3909  O   PRO A 361    10581   6598   6845   -607   1176    -98       O  
ATOM   3910  CB  PRO A 361      48.942  50.370 -34.170  1.00 62.69           C  
ANISOU 3910  CB  PRO A 361    10248   6733   6840   -575   1135    -36       C  
ATOM   3911  CG  PRO A 361      48.978  49.497 -35.376  1.00 66.27           C  
ANISOU 3911  CG  PRO A 361    10591   7213   7377   -435   1114    -12       C  
ATOM   3912  CD  PRO A 361      47.556  49.276 -35.789  1.00 64.96           C  
ANISOU 3912  CD  PRO A 361    10480   6913   7288   -254   1112    -36       C  
ATOM   3913  N   ILE A 362      46.233  52.047 -33.625  1.00 63.86           N  
ANISOU 3913  N   ILE A 362    10810   6502   6951   -396   1222   -111       N  
ATOM   3914  CA  ILE A 362      45.495  53.175 -33.061  1.00 67.25           C  
ANISOU 3914  CA  ILE A 362    11478   6781   7294   -391   1291   -136       C  
ATOM   3915  C   ILE A 362      44.478  52.684 -32.040  1.00 70.69           C  
ANISOU 3915  C   ILE A 362    11856   7219   7783   -283   1262   -133       C  
ATOM   3916  O   ILE A 362      44.292  53.293 -30.973  1.00 70.10           O  
ANISOU 3916  O   ILE A 362    11907   7087   7640   -349   1297   -147       O  
ATOM   3917  CB  ILE A 362      44.823  53.977 -34.186  1.00 66.54           C  
ANISOU 3917  CB  ILE A 362    11568   6552   7163   -256   1356   -140       C  
ATOM   3918  CG1 ILE A 362      45.868  54.379 -35.229  1.00 68.77           C  
ANISOU 3918  CG1 ILE A 362    11893   6837   7399   -369   1380   -144       C  
ATOM   3919  CG2 ILE A 362      44.103  55.191 -33.614  1.00 66.82           C  
ANISOU 3919  CG2 ILE A 362    11883   6421   7083   -223   1451   -153       C  
ATOM   3920  CD1 ILE A 362      45.288  54.984 -36.467  1.00 71.37           C  
ANISOU 3920  CD1 ILE A 362    12363   7051   7702   -221   1436   -141       C  
ATOM   3921  N   ILE A 363      43.805  51.572 -32.353  1.00 67.43           N  
ANISOU 3921  N   ILE A 363    11265   6874   7482   -127   1203   -116       N  
ATOM   3922  CA  ILE A 363      42.878  50.979 -31.400  1.00 65.92           C  
ANISOU 3922  CA  ILE A 363    10998   6709   7340    -42   1169   -113       C  
ATOM   3923  C   ILE A 363      43.605  50.588 -30.128  1.00 67.76           C  
ANISOU 3923  C   ILE A 363    11146   7022   7579   -186   1137   -112       C  
ATOM   3924  O   ILE A 363      43.163  50.915 -29.018  1.00 71.52           O  
ANISOU 3924  O   ILE A 363    11687   7463   8024   -205   1150   -121       O  
ATOM   3925  CB  ILE A 363      42.170  49.779 -32.036  1.00 68.25           C  
ANISOU 3925  CB  ILE A 363    11121   7076   7735    102   1115   -101       C  
ATOM   3926  CG1 ILE A 363      41.351  50.261 -33.232  1.00 67.83           C  
ANISOU 3926  CG1 ILE A 363    11148   6970   7654    245   1149    -98       C  
ATOM   3927  CG2 ILE A 363      41.327  49.051 -30.989  1.00 65.92           C  
ANISOU 3927  CG2 ILE A 363    10734   6826   7485    156   1078   -100       C  
ATOM   3928  CD1 ILE A 363      40.673  49.139 -33.991  1.00 69.78           C  
ANISOU 3928  CD1 ILE A 363    11238   7302   7973    352   1101    -91       C  
ATOM   3929  N   TYR A 364      44.753  49.918 -30.265  1.00 67.41           N  
ANISOU 3929  N   TYR A 364    10955   7096   7561   -284   1102    -94       N  
ATOM   3930  CA  TYR A 364      45.486  49.505 -29.073  1.00 67.83           C  
ANISOU 3930  CA  TYR A 364    10904   7264   7605   -407   1073    -80       C  
ATOM   3931  C   TYR A 364      45.880  50.710 -28.227  1.00 70.98           C  
ANISOU 3931  C   TYR A 364    11466   7621   7880   -587   1119   -103       C  
ATOM   3932  O   TYR A 364      45.854  50.651 -26.993  1.00 71.60           O  
ANISOU 3932  O   TYR A 364    11526   7736   7941   -653   1108   -105       O  
ATOM   3933  CB  TYR A 364      46.724  48.698 -29.460  1.00 64.08           C  
ANISOU 3933  CB  TYR A 364    10252   6948   7146   -461   1043    -41       C  
ATOM   3934  CG  TYR A 364      46.447  47.497 -30.341  1.00 62.98           C  
ANISOU 3934  CG  TYR A 364     9988   6832   7109   -299   1015    -19       C  
ATOM   3935  CD1 TYR A 364      45.255  46.799 -30.264  1.00 65.88           C  
ANISOU 3935  CD1 TYR A 364    10335   7142   7555   -157    996    -31       C  
ATOM   3936  CD2 TYR A 364      47.380  47.080 -31.271  1.00 64.93           C  
ANISOU 3936  CD2 TYR A 364    10151   7161   7357   -302   1014     13       C  
ATOM   3937  CE1 TYR A 364      45.012  45.705 -31.090  1.00 67.29           C  
ANISOU 3937  CE1 TYR A 364    10428   7334   7803    -43    982    -18       C  
ATOM   3938  CE2 TYR A 364      47.146  46.004 -32.093  1.00 67.95           C  
ANISOU 3938  CE2 TYR A 364    10453   7545   7818   -164   1003     30       C  
ATOM   3939  CZ  TYR A 364      45.967  45.317 -32.000  1.00 67.53           C  
ANISOU 3939  CZ  TYR A 364    10399   7423   7835    -45    988     11       C  
ATOM   3940  OH  TYR A 364      45.745  44.240 -32.830  1.00 69.48           O  
ANISOU 3940  OH  TYR A 364    10593   7667   8139     61    986     22       O  
ATOM   3941  N   ASN A 365      46.250  51.808 -28.877  1.00 71.06           N  
ANISOU 3941  N   ASN A 365    11654   7550   7796   -677   1178   -123       N  
ATOM   3942  CA  ASN A 365      46.666  53.002 -28.157  1.00 71.02           C  
ANISOU 3942  CA  ASN A 365    11851   7486   7646   -879   1240   -151       C  
ATOM   3943  C   ASN A 365      45.493  53.620 -27.409  1.00 71.95           C  
ANISOU 3943  C   ASN A 365    12159   7440   7737   -794   1288   -174       C  
ATOM   3944  O   ASN A 365      45.658  54.113 -26.287  1.00 69.77           O  
ANISOU 3944  O   ASN A 365    11981   7150   7378   -937   1314   -192       O  
ATOM   3945  CB  ASN A 365      47.284  54.003 -29.137  1.00 75.89           C  
ANISOU 3945  CB  ASN A 365    12644   8034   8158   -992   1305   -169       C  
ATOM   3946  CG  ASN A 365      47.697  55.301 -28.472  1.00 86.62           C  
ANISOU 3946  CG  ASN A 365    14265   9306   9340  -1229   1389   -207       C  
ATOM   3947  OD1 ASN A 365      48.823  55.441 -28.002  1.00 93.71           O  
ANISOU 3947  OD1 ASN A 365    15115  10347  10142  -1482   1382   -210       O  
ATOM   3948  ND2 ASN A 365      46.791  56.270 -28.452  1.00 89.85           N  
ANISOU 3948  ND2 ASN A 365    14964   9490   9685  -1148   1478   -233       N  
ATOM   3949  N   PHE A 366      44.292  53.579 -27.999  1.00 70.81           N  
ANISOU 3949  N   PHE A 366    12061   7191   7651   -557   1301   -168       N  
ATOM   3950  CA  PHE A 366      43.139  54.178 -27.328  1.00 70.81           C  
ANISOU 3950  CA  PHE A 366    12236   7059   7610   -443   1354   -175       C  
ATOM   3951  C   PHE A 366      42.544  53.294 -26.233  1.00 70.55           C  
ANISOU 3951  C   PHE A 366    12038   7107   7660   -379   1289   -165       C  
ATOM   3952  O   PHE A 366      42.004  53.820 -25.254  1.00 66.65           O  
ANISOU 3952  O   PHE A 366    11678   6536   7109   -376   1330   -174       O  
ATOM   3953  CB  PHE A 366      42.057  54.538 -28.346  1.00 74.11           C  
ANISOU 3953  CB  PHE A 366    12756   7376   8028   -206   1399   -160       C  
ATOM   3954  CG  PHE A 366      42.269  55.876 -28.992  1.00 77.60           C  
ANISOU 3954  CG  PHE A 366    13496   7657   8333   -239   1511   -172       C  
ATOM   3955  CD1 PHE A 366      42.188  57.036 -28.239  1.00 81.43           C  
ANISOU 3955  CD1 PHE A 366    14282   7986   8674   -314   1617   -189       C  
ATOM   3956  CD2 PHE A 366      42.570  55.976 -30.340  1.00 77.15           C  
ANISOU 3956  CD2 PHE A 366    13439   7591   8281   -203   1521   -166       C  
ATOM   3957  CE1 PHE A 366      42.391  58.275 -28.823  1.00 84.75           C  
ANISOU 3957  CE1 PHE A 366    15017   8233   8949   -350   1739   -201       C  
ATOM   3958  CE2 PHE A 366      42.770  57.203 -30.927  1.00 81.06           C  
ANISOU 3958  CE2 PHE A 366    14226   7929   8644   -234   1633   -176       C  
ATOM   3959  CZ  PHE A 366      42.680  58.357 -30.168  1.00 83.73           C  
ANISOU 3959  CZ  PHE A 366    14882   8101   8830   -308   1747   -194       C  
ATOM   3960  N   LEU A 367      42.620  51.970 -26.361  1.00 71.33           N  
ANISOU 3960  N   LEU A 367    11870   7348   7884   -327   1200   -147       N  
ATOM   3961  CA  LEU A 367      41.872  51.084 -25.479  1.00 68.79           C  
ANISOU 3961  CA  LEU A 367    11409   7087   7643   -238   1147   -137       C  
ATOM   3962  C   LEU A 367      42.758  50.259 -24.562  1.00 67.27           C  
ANISOU 3962  C   LEU A 367    11042   7030   7487   -371   1090   -128       C  
ATOM   3963  O   LEU A 367      42.250  49.392 -23.851  1.00 67.46           O  
ANISOU 3963  O   LEU A 367    10940   7109   7582   -305   1045   -119       O  
ATOM   3964  CB  LEU A 367      40.976  50.162 -26.301  1.00 70.87           C  
ANISOU 3964  CB  LEU A 367    11535   7391   8001    -49   1105   -122       C  
ATOM   3965  CG  LEU A 367      39.921  50.910 -27.106  1.00 72.71           C  
ANISOU 3965  CG  LEU A 367    11907   7535   8186    115   1158   -117       C  
ATOM   3966  CD1 LEU A 367      39.120  49.957 -27.959  1.00 73.69           C  
ANISOU 3966  CD1 LEU A 367    11875   7741   8385    261   1112   -104       C  
ATOM   3967  CD2 LEU A 367      39.023  51.684 -26.153  1.00 74.99           C  
ANISOU 3967  CD2 LEU A 367    12346   7745   8401    183   1209   -115       C  
ATOM   3968  N   SER A 368      44.060  50.512 -24.551  1.00 67.79           N  
ANISOU 3968  N   SER A 368    11096   7168   7493   -556   1095   -125       N  
ATOM   3969  CA  SER A 368      44.991  49.747 -23.732  1.00 67.79           C  
ANISOU 3969  CA  SER A 368    10912   7340   7505   -668   1047   -101       C  
ATOM   3970  C   SER A 368      46.018  50.705 -23.157  1.00 70.30           C  
ANISOU 3970  C   SER A 368    11327   7702   7681   -918   1083   -113       C  
ATOM   3971  O   SER A 368      46.808  51.286 -23.909  1.00 72.50           O  
ANISOU 3971  O   SER A 368    11666   7996   7884  -1034   1112   -117       O  
ATOM   3972  CB  SER A 368      45.666  48.643 -24.557  1.00 70.39           C  
ANISOU 3972  CB  SER A 368    11040   7800   7905   -612   1005    -61       C  
ATOM   3973  OG  SER A 368      46.861  48.189 -23.951  1.00 73.12           O  
ANISOU 3973  OG  SER A 368    11232   8337   8212   -734    982    -22       O  
ATOM   3974  N   GLY A 369      45.989  50.883 -21.830  1.00 69.61           N  
ANISOU 3974  N   GLY A 369    11261   7639   7547  -1017   1083   -122       N  
ATOM   3975  CA  GLY A 369      46.904  51.812 -21.190  1.00 66.89           C  
ANISOU 3975  CA  GLY A 369    11024   7346   7046  -1289   1122   -140       C  
ATOM   3976  C   GLY A 369      48.349  51.373 -21.279  1.00 70.74           C  
ANISOU 3976  C   GLY A 369    11307   8090   7480  -1447   1085   -100       C  
ATOM   3977  O   GLY A 369      49.256  52.213 -21.343  1.00 71.43           O  
ANISOU 3977  O   GLY A 369    11481   8240   7418  -1688   1122   -114       O  
ATOM   3978  N   LYS A 370      48.588  50.058 -21.297  1.00 72.49           N  
ANISOU 3978  N   LYS A 370    11265   8473   7805  -1315   1022    -44       N  
ATOM   3979  CA  LYS A 370      49.951  49.556 -21.439  1.00 75.81           C  
ANISOU 3979  CA  LYS A 370    11473   9165   8166  -1413    995     15       C  
ATOM   3980  C   LYS A 370      50.498  49.833 -22.834  1.00 72.88           C  
ANISOU 3980  C   LYS A 370    11124   8796   7771  -1426   1014     20       C  
ATOM   3981  O   LYS A 370      51.640  50.290 -22.987  1.00 77.85           O  
ANISOU 3981  O   LYS A 370    11715   9597   8266  -1631   1026     37       O  
ATOM   3982  CB  LYS A 370      49.993  48.064 -21.122  1.00 81.32           C  
ANISOU 3982  CB  LYS A 370    11924  10004   8970  -1227    944     82       C  
ATOM   3983  CG  LYS A 370      49.726  47.737 -19.663  1.00 86.88           C  
ANISOU 3983  CG  LYS A 370    12572  10765   9676  -1244    923     89       C  
ATOM   3984  CD  LYS A 370      50.198  46.338 -19.325  1.00 91.31           C  
ANISOU 3984  CD  LYS A 370    12882  11526  10284  -1105    890    172       C  
ATOM   3985  CE  LYS A 370      49.966  46.032 -17.856  1.00 97.42           C  
ANISOU 3985  CE  LYS A 370    13600  12363  11053  -1125    870    182       C  
ATOM   3986  NZ  LYS A 370      50.583  44.733 -17.461  1.00 99.63           N  
ANISOU 3986  NZ  LYS A 370    13646  12863  11346   -996    853    275       N  
ATOM   3987  N   PHE A 371      49.703  49.563 -23.871  1.00 71.73           N  
ANISOU 3987  N   PHE A 371    11032   8478   7744  -1220   1017      7       N  
ATOM   3988  CA  PHE A 371      50.150  49.903 -25.219  1.00 70.94           C  
ANISOU 3988  CA  PHE A 371    10973   8358   7622  -1230   1039      6       C  
ATOM   3989  C   PHE A 371      50.324  51.406 -25.365  1.00 73.28           C  
ANISOU 3989  C   PHE A 371    11520   8545   7779  -1441   1102    -49       C  
ATOM   3990  O   PHE A 371      51.286  51.865 -25.989  1.00 72.71           O  
ANISOU 3990  O   PHE A 371    11452   8568   7607  -1595   1122    -43       O  
ATOM   3991  CB  PHE A 371      49.177  49.371 -26.273  1.00 69.06           C  
ANISOU 3991  CB  PHE A 371    10756   7958   7526   -980   1033     -2       C  
ATOM   3992  CG  PHE A 371      49.452  47.955 -26.688  1.00 71.53           C  
ANISOU 3992  CG  PHE A 371    10851   8393   7934   -818    994     57       C  
ATOM   3993  CD1 PHE A 371      50.561  47.645 -27.468  1.00 73.04           C  
ANISOU 3993  CD1 PHE A 371    10922   8740   8088   -842    993    106       C  
ATOM   3994  CD2 PHE A 371      48.608  46.932 -26.302  1.00 72.25           C  
ANISOU 3994  CD2 PHE A 371    10874   8441   8137   -644    968     65       C  
ATOM   3995  CE1 PHE A 371      50.815  46.338 -27.852  1.00 73.96           C  
ANISOU 3995  CE1 PHE A 371    10872   8952   8278   -674    975    166       C  
ATOM   3996  CE2 PHE A 371      48.855  45.627 -26.678  1.00 75.66           C  
ANISOU 3996  CE2 PHE A 371    11152   8958   8638   -500    952    117       C  
ATOM   3997  CZ  PHE A 371      49.960  45.328 -27.459  1.00 75.22           C  
ANISOU 3997  CZ  PHE A 371    10995   9041   8543   -504    960    170       C  
ATOM   3998  N   ARG A 372      49.406  52.188 -24.786  1.00 76.21           N  
ANISOU 3998  N   ARG A 372    12115   8713   8127  -1450   1145   -102       N  
ATOM   3999  CA  ARG A 372      49.496  53.642 -24.890  1.00 79.01           C  
ANISOU 3999  CA  ARG A 372    12766   8922   8331  -1638   1230   -155       C  
ATOM   4000  C   ARG A 372      50.774  54.157 -24.249  1.00 80.05           C  
ANISOU 4000  C   ARG A 372    12886   9244   8283  -1974   1243   -157       C  
ATOM   4001  O   ARG A 372      51.477  54.992 -24.831  1.00 82.00           O  
ANISOU 4001  O   ARG A 372    13265   9493   8397  -2171   1293   -179       O  
ATOM   4002  CB  ARG A 372      48.273  54.290 -24.241  1.00 80.55           C  
ANISOU 4002  CB  ARG A 372    13204   8880   8523  -1557   1283   -196       C  
ATOM   4003  CG  ARG A 372      48.305  55.803 -24.240  1.00 82.07           C  
ANISOU 4003  CG  ARG A 372    13757   8886   8540  -1735   1395   -249       C  
ATOM   4004  CD  ARG A 372      46.940  56.374 -23.923  1.00 80.69           C  
ANISOU 4004  CD  ARG A 372    13829   8456   8372  -1556   1462   -271       C  
ATOM   4005  NE  ARG A 372      46.481  55.968 -22.601  1.00 82.93           N  
ANISOU 4005  NE  ARG A 372    14041   8776   8692  -1535   1429   -268       N  
ATOM   4006  CZ  ARG A 372      45.476  55.127 -22.378  1.00 86.79           C  
ANISOU 4006  CZ  ARG A 372    14386   9262   9330  -1282   1373   -243       C  
ATOM   4007  NH1 ARG A 372      44.819  54.595 -23.398  1.00 88.70           N  
ANISOU 4007  NH1 ARG A 372    14536   9475   9690  -1040   1346   -221       N  
ATOM   4008  NH2 ARG A 372      45.133  54.811 -21.134  1.00 87.49           N  
ANISOU 4008  NH2 ARG A 372    14419   9385   9437  -1288   1347   -242       N  
ATOM   4009  N   GLU A 373      51.100  53.654 -23.059  1.00 78.00           N  
ANISOU 4009  N   GLU A 373    12465   9165   8006  -2055   1199   -133       N  
ATOM   4010  CA  GLU A 373      52.335  54.054 -22.401  1.00 84.00           C  
ANISOU 4010  CA  GLU A 373    13171  10168   8579  -2386   1203   -126       C  
ATOM   4011  C   GLU A 373      53.553  53.656 -23.220  1.00 87.72           C  
ANISOU 4011  C   GLU A 373    13421  10905   9003  -2457   1171    -71       C  
ATOM   4012  O   GLU A 373      54.496  54.447 -23.359  1.00 89.28           O  
ANISOU 4012  O   GLU A 373    13684  11224   9014  -2752   1207    -86       O  
ATOM   4013  CB  GLU A 373      52.399  53.445 -21.001  1.00 88.34           C  
ANISOU 4013  CB  GLU A 373    13549  10885   9130  -2415   1155    -98       C  
ATOM   4014  CG  GLU A 373      51.570  54.186 -19.985  1.00 93.85           C  
ANISOU 4014  CG  GLU A 373    14500  11375   9786  -2482   1204   -159       C  
ATOM   4015  CD  GLU A 373      52.097  55.588 -19.737  1.00104.22           C  
ANISOU 4015  CD  GLU A 373    16097  12638  10867  -2838   1292   -220       C  
ATOM   4016  OE1 GLU A 373      53.315  55.811 -19.921  1.00108.41           O  
ANISOU 4016  OE1 GLU A 373    16537  13409  11244  -3102   1290   -206       O  
ATOM   4017  OE2 GLU A 373      51.295  56.468 -19.366  1.00108.14           O  
ANISOU 4017  OE2 GLU A 373    16915  12857  11315  -2859   1371   -280       O  
ATOM   4018  N   GLU A 374      53.553  52.445 -23.785  1.00 87.69           N  
ANISOU 4018  N   GLU A 374    13169  10999   9151  -2198   1111     -6       N  
ATOM   4019  CA  GLU A 374      54.708  52.038 -24.582  1.00 87.28           C  
ANISOU 4019  CA  GLU A 374    12909  11204   9048  -2235   1089     57       C  
ATOM   4020  C   GLU A 374      54.857  52.904 -25.827  1.00 83.50           C  
ANISOU 4020  C   GLU A 374    12617  10588   8519  -2313   1139     16       C  
ATOM   4021  O   GLU A 374      55.978  53.263 -26.210  1.00 83.95           O  
ANISOU 4021  O   GLU A 374    12612  10856   8429  -2525   1148     37       O  
ATOM   4022  CB  GLU A 374      54.604  50.561 -24.957  1.00 88.65           C  
ANISOU 4022  CB  GLU A 374    12830  11465   9388  -1920   1035    135       C  
ATOM   4023  CG  GLU A 374      54.704  49.614 -23.773  1.00 87.22           C  
ANISOU 4023  CG  GLU A 374    12439  11469   9230  -1847    994    194       C  
ATOM   4024  CD  GLU A 374      55.950  49.860 -22.930  1.00 90.49           C  
ANISOU 4024  CD  GLU A 374    12697  12244   9442  -2114    985    241       C  
ATOM   4025  OE1 GLU A 374      57.023  50.174 -23.503  1.00 87.41           O  
ANISOU 4025  OE1 GLU A 374    12224  12073   8915  -2272    994    275       O  
ATOM   4026  OE2 GLU A 374      55.844  49.750 -21.682  1.00 96.78           O  
ANISOU 4026  OE2 GLU A 374    13448  13119  10205  -2176    970    246       O  
ATOM   4027  N   PHE A 375      53.740  53.261 -26.464  1.00 82.95           N  
ANISOU 4027  N   PHE A 375    12773  10188   8558  -2146   1173    -38       N  
ATOM   4028  CA  PHE A 375      53.791  54.137 -27.632  1.00 82.92           C  
ANISOU 4028  CA  PHE A 375    12974  10028   8503  -2202   1231    -78       C  
ATOM   4029  C   PHE A 375      54.291  55.527 -27.255  1.00 83.96           C  
ANISOU 4029  C   PHE A 375    13364  10127   8413  -2555   1308   -137       C  
ATOM   4030  O   PHE A 375      55.068  56.135 -28.001  1.00 85.71           O  
ANISOU 4030  O   PHE A 375    13652  10402   8512  -2737   1344   -147       O  
ATOM   4031  CB  PHE A 375      52.412  54.228 -28.292  1.00 84.65           C  
ANISOU 4031  CB  PHE A 375    13373   9922   8866  -1930   1257   -113       C  
ATOM   4032  CG  PHE A 375      51.958  52.952 -28.945  1.00 89.14           C  
ANISOU 4032  CG  PHE A 375    13729  10512   9628  -1624   1194    -67       C  
ATOM   4033  CD1 PHE A 375      52.876  51.991 -29.337  1.00 93.04           C  
ANISOU 4033  CD1 PHE A 375    13952  11251  10149  -1590   1143      0       C  
ATOM   4034  CD2 PHE A 375      50.610  52.716 -29.175  1.00 90.18           C  
ANISOU 4034  CD2 PHE A 375    13943  10428   9895  -1373   1195    -87       C  
ATOM   4035  CE1 PHE A 375      52.461  50.819 -29.945  1.00 91.92           C  
ANISOU 4035  CE1 PHE A 375    13658  11102  10166  -1321   1103     39       C  
ATOM   4036  CE2 PHE A 375      50.188  51.540 -29.781  1.00 88.38           C  
ANISOU 4036  CE2 PHE A 375    13538  10220   9821  -1130   1144    -51       C  
ATOM   4037  CZ  PHE A 375      51.117  50.592 -30.163  1.00 89.56           C  
ANISOU 4037  CZ  PHE A 375    13453  10580   9997  -1108   1102      7       C  
ATOM   4038  N   LYS A 376      53.854  56.044 -26.102  1.00 85.56           N  
ANISOU 4038  N   LYS A 376    13728  10233   8548  -2667   1342   -178       N  
ATOM   4039  CA  LYS A 376      54.353  57.333 -25.629  1.00 91.36           C  
ANISOU 4039  CA  LYS A 376    14733  10934   9046  -3035   1427   -238       C  
ATOM   4040  C   LYS A 376      55.852  57.274 -25.370  1.00 94.78           C  
ANISOU 4040  C   LYS A 376    14955  11756   9303  -3359   1395   -204       C  
ATOM   4041  O   LYS A 376      56.586  58.210 -25.708  1.00 96.94           O  
ANISOU 4041  O   LYS A 376    15392  12062   9377  -3665   1458   -240       O  
ATOM   4042  CB  LYS A 376      53.614  57.762 -24.357  1.00 94.07           C  
ANISOU 4042  CB  LYS A 376    15271  11120   9352  -3080   1467   -281       C  
ATOM   4043  CG  LYS A 376      52.198  58.272 -24.587  1.00 96.52           C  
ANISOU 4043  CG  LYS A 376    15888  11037   9748  -2835   1539   -322       C  
ATOM   4044  CD  LYS A 376      51.543  58.729 -23.293  1.00 99.63           C  
ANISOU 4044  CD  LYS A 376    16479  11292  10084  -2888   1587   -358       C  
ATOM   4045  CE  LYS A 376      50.110  59.187 -23.539  1.00101.95           C  
ANISOU 4045  CE  LYS A 376    17053  11231  10452  -2602   1662   -380       C  
ATOM   4046  NZ  LYS A 376      49.418  59.594 -22.276  1.00104.53           N  
ANISOU 4046  NZ  LYS A 376    17570  11421  10727  -2620   1712   -407       N  
ATOM   4047  N   ALA A 377      56.322  56.179 -24.770  1.00 95.90           N  
ANISOU 4047  N   ALA A 377    14731  12210   9496  -3295   1304   -128       N  
ATOM   4048  CA  ALA A 377      57.750  56.031 -24.507  1.00 97.12           C  
ANISOU 4048  CA  ALA A 377    14634  12798   9471  -3568   1269    -74       C  
ATOM   4049  C   ALA A 377      58.539  55.965 -25.806  1.00 97.61           C  
ANISOU 4049  C   ALA A 377    14589  12994   9503  -3575   1264    -37       C  
ATOM   4050  O   ALA A 377      59.611  56.573 -25.925  1.00102.77           O  
ANISOU 4050  O   ALA A 377    15232  13881   9936  -3910   1287    -38       O  
ATOM   4051  CB  ALA A 377      57.995  54.787 -23.652  1.00 96.15           C  
ANISOU 4051  CB  ALA A 377    14143  12971   9420  -3422   1182     16       C  
ATOM   4052  N   ALA A 378      58.009  55.255 -26.801  1.00 94.95           N  
ANISOU 4052  N   ALA A 378    14182  12517   9376  -3223   1237     -8       N  
ATOM   4053  CA  ALA A 378      58.663  55.197 -28.105  1.00 93.74           C  
ANISOU 4053  CA  ALA A 378    13951  12455   9212  -3203   1236     23       C  
ATOM   4054  C   ALA A 378      58.724  56.577 -28.755  1.00100.79           C  
ANISOU 4054  C   ALA A 378    15189  13142   9964  -3449   1325    -63       C  
ATOM   4055  O   ALA A 378      59.782  57.005 -29.230  1.00105.24           O  
ANISOU 4055  O   ALA A 378    15713  13919  10356  -3702   1341    -52       O  
ATOM   4056  CB  ALA A 378      57.932  54.207 -29.012  1.00 86.70           C  
ANISOU 4056  CB  ALA A 378    12965  11407   8572  -2783   1200     58       C  
ATOM   4057  N   PHE A 379      57.595  57.291 -28.792  1.00102.21           N  
ANISOU 4057  N   PHE A 379    15719  12914  10201  -3373   1393   -143       N  
ATOM   4058  CA  PHE A 379      57.574  58.586 -29.468  1.00104.06           C  
ANISOU 4058  CA  PHE A 379    16322  12913  10303  -3561   1497   -218       C  
ATOM   4059  C   PHE A 379      58.305  59.663 -28.680  1.00109.59           C  
ANISOU 4059  C   PHE A 379    17220  13703  10717  -4029   1567   -272       C  
ATOM   4060  O   PHE A 379      58.627  60.711 -29.248  1.00112.10           O  
ANISOU 4060  O   PHE A 379    17820  13903  10871  -4263   1658   -328       O  
ATOM   4061  CB  PHE A 379      56.136  59.025 -29.746  1.00102.36           C  
ANISOU 4061  CB  PHE A 379    16426  12252  10212  -3305   1562   -272       C  
ATOM   4062  CG  PHE A 379      55.477  58.270 -30.868  1.00101.27           C  
ANISOU 4062  CG  PHE A 379    16171  12006  10302  -2917   1518   -236       C  
ATOM   4063  CD1 PHE A 379      56.173  57.976 -32.029  1.00102.89           C  
ANISOU 4063  CD1 PHE A 379    16226  12343  10523  -2895   1491   -200       C  
ATOM   4064  CD2 PHE A 379      54.164  57.844 -30.754  1.00 99.43           C  
ANISOU 4064  CD2 PHE A 379    15971  11555  10251  -2587   1505   -236       C  
ATOM   4065  CE1 PHE A 379      55.567  57.276 -33.064  1.00102.83           C  
ANISOU 4065  CE1 PHE A 379    16123  12235  10714  -2556   1455   -171       C  
ATOM   4066  CE2 PHE A 379      53.552  57.151 -31.780  1.00 97.64           C  
ANISOU 4066  CE2 PHE A 379    15639  11249  10210  -2264   1467   -207       C  
ATOM   4067  CZ  PHE A 379      54.252  56.862 -32.935  1.00 99.93           C  
ANISOU 4067  CZ  PHE A 379    15795  11656  10518  -2250   1443   -176       C  
ATOM   4068  N   SER A 380      58.577  59.435 -27.395  1.00112.61           N  
ANISOU 4068  N   SER A 380    17473  14290  11023  -4183   1533   -259       N  
ATOM   4069  CA  SER A 380      59.372  60.377 -26.622  1.00118.72           C  
ANISOU 4069  CA  SER A 380    18400  15206  11502  -4667   1593   -307       C  
ATOM   4070  C   SER A 380      60.863  60.084 -26.691  1.00127.52           C  
ANISOU 4070  C   SER A 380    19180  16830  12442  -4943   1535   -244       C  
ATOM   4071  O   SER A 380      61.671  61.015 -26.596  1.00130.34           O  
ANISOU 4071  O   SER A 380    19692  17309  12524  -5384   1599   -290       O  
ATOM   4072  CB  SER A 380      58.920  60.374 -25.161  1.00117.53           C  
ANISOU 4072  CB  SER A 380    18296  15032  11328  -4727   1593   -328       C  
ATOM   4073  OG  SER A 380      57.543  60.685 -25.059  1.00116.81           O  
ANISOU 4073  OG  SER A 380    18514  14494  11376  -4473   1653   -379       O  
ATOM   4074  N   CYS A 381      61.255  58.816 -26.867  1.00133.71           N  
ANISOU 4074  N   CYS A 381    19520  17925  13361  -4697   1425   -136       N  
ATOM   4075  CA  CYS A 381      62.679  58.505 -26.942  1.00140.42           C  
ANISOU 4075  CA  CYS A 381    20028  19297  14030  -4921   1376    -55       C  
ATOM   4076  C   CYS A 381      63.338  59.092 -28.185  1.00144.23           C  
ANISOU 4076  C   CYS A 381    20592  19807  14400  -5079   1417    -70       C  
ATOM   4077  O   CYS A 381      64.568  59.203 -28.220  1.00147.41           O  
ANISOU 4077  O   CYS A 381    20795  20636  14577  -5380   1401    -25       O  
ATOM   4078  CB  CYS A 381      62.903  56.992 -26.898  1.00140.30           C  
ANISOU 4078  CB  CYS A 381    19550  19578  14180  -4567   1270     75       C  
ATOM   4079  SG  CYS A 381      62.832  56.161 -28.496  1.00139.65           S  
ANISOU 4079  SG  CYS A 381    19318  19427  14316  -4160   1237    140       S  
ATOM   4080  N   CYS A 382      62.557  59.469 -29.198  1.00145.72           N  
ANISOU 4080  N   CYS A 382    21061  19576  14730  -4887   1470   -127       N  
ATOM   4081  CA  CYS A 382      63.105  60.098 -30.393  1.00149.59           C  
ANISOU 4081  CA  CYS A 382    21672  20048  15118  -5034   1518   -149       C  
ATOM   4082  C   CYS A 382      62.920  61.609 -30.418  1.00152.61           C  
ANISOU 4082  C   CYS A 382    22561  20119  15304  -5379   1652   -271       C  
ATOM   4083  O   CYS A 382      63.672  62.295 -31.119  1.00155.75           O  
ANISOU 4083  O   CYS A 382    23065  20596  15517  -5659   1703   -296       O  
ATOM   4084  CB  CYS A 382      62.473  59.494 -31.654  1.00149.69           C  
ANISOU 4084  CB  CYS A 382    21646  19832  15398  -4593   1494   -120       C  
ATOM   4085  SG  CYS A 382      60.683  59.674 -31.745  1.00150.51           S  
ANISOU 4085  SG  CYS A 382    22098  19342  15748  -4228   1543   -192       S  
ATOM   4086  N   CYS A 383      61.946  62.138 -29.683  1.00152.63           N  
ANISOU 4086  N   CYS A 383    22893  19769  15329  -5359   1719   -345       N  
ATOM   4087  CA  CYS A 383      61.745  63.581 -29.592  1.00154.42           C  
ANISOU 4087  CA  CYS A 383    23649  19677  15345  -5676   1870   -457       C  
ATOM   4088  C   CYS A 383      62.651  64.187 -28.527  1.00156.38           C  
ANISOU 4088  C   CYS A 383    23943  20202  15271  -6217   1904   -493       C  
ATOM   4089  O   CYS A 383      63.850  64.356 -28.743  1.00158.18           O  
ANISOU 4089  O   CYS A 383    24018  20801  15282  -6569   1890   -475       O  
ATOM   4090  CB  CYS A 383      60.283  63.909 -29.281  1.00154.24           C  
ANISOU 4090  CB  CYS A 383    23979  19156  15468  -5396   1943   -510       C  
ATOM   4091  SG  CYS A 383      59.119  63.531 -30.612  1.00152.65           S  
ANISOU 4091  SG  CYS A 383    23833  18589  15577  -4831   1940   -488       S  
TER    4092      CYS A 383                                                      
HETATM 4093  C10 7MA A2001      38.452  38.649 -50.444  1.00 57.42           C  
HETATM 4094  C13 7MA A2001      42.156  39.359 -55.101  1.00 47.74           C  
HETATM 4095  C15 7MA A2001      43.350  40.823 -53.668  1.00 58.54           C  
HETATM 4096  C20 7MA A2001      43.311  41.968 -54.476  1.00 56.56           C  
HETATM 4097  C22 7MA A2001      44.008  44.368 -50.474  1.00 58.82           C  
HETATM 4098  C26 7MA A2001      45.441  39.864 -55.880  1.00 60.07           C  
HETATM 4099  C28 7MA A2001      45.766  40.221 -58.238  1.00 62.64           C  
HETATM 4100  C32 7MA A2001      46.741  41.289 -54.314  1.00 62.97           C  
HETATM 4101  C31 7MA A2001      46.370  40.885 -55.600  1.00 64.97           C  
HETATM 4102  C30 7MA A2001      46.978  41.558 -56.655  1.00 65.84           C  
HETATM 4103  C29 7MA A2001      46.679  41.224 -57.962  1.00 64.04           C  
HETATM 4104  C27 7MA A2001      45.157  39.539 -57.200  1.00 59.50           C  
HETATM 4105  S23 7MA A2001      44.614  38.912 -54.618  1.00 57.84           S  
HETATM 4106  O24 7MA A2001      44.252  37.539 -55.187  1.00 62.91           O  
HETATM 4107  O25 7MA A2001      45.572  38.728 -53.461  1.00 57.16           O  
HETATM 4108  N14 7MA A2001      43.223  39.557 -54.121  1.00 56.76           N  
HETATM 4109  C16 7MA A2001      43.546  40.944 -52.294  1.00 56.13           C  
HETATM 4110  N17 7MA A2001      43.700  42.194 -51.703  1.00 54.73           N  
HETATM 4111  C19 7MA A2001      43.459  43.212 -53.861  1.00 58.83           C  
HETATM 4112  C18 7MA A2001      43.650  43.303 -52.468  1.00 60.35           C  
HETATM 4113  O21 7MA A2001      43.798  44.513 -51.882  1.00 59.92           O  
HETATM 4114  C11 7MA A2001      40.840  39.462 -54.319  1.00 56.06           C  
HETATM 4115  O12 7MA A2001      40.122  40.444 -54.436  1.00 60.41           O  
HETATM 4116  N03 7MA A2001      40.519  38.450 -53.467  1.00 58.29           N  
HETATM 4117  C02 7MA A2001      41.328  37.214 -53.307  1.00 52.50           C  
HETATM 4118  C01 7MA A2001      40.658  36.128 -54.139  1.00 53.95           C  
HETATM 4119  C04 7MA A2001      39.254  38.532 -52.721  1.00 57.47           C  
HETATM 4120  C05 7MA A2001      39.481  38.828 -51.363  1.00 59.46           C  
HETATM 4121  C09 7MA A2001      38.641  38.923 -49.102  1.00 59.75           C  
HETATM 4122  C08 7MA A2001      39.864  39.400 -48.649  1.00 58.64           C  
HETATM 4123  N07 7MA A2001      40.905  39.580 -49.549  1.00 60.86           N  
HETATM 4124  C06 7MA A2001      40.709  39.296 -50.902  1.00 60.35           C  
HETATM 4125  C1  OLA A2002      37.381  54.197 -29.155  1.00104.47           C  
HETATM 4126  O1  OLA A2002      36.330  53.514 -29.110  1.00106.65           O  
HETATM 4127  O2  OLA A2002      37.466  55.231 -28.451  1.00105.50           O  
HETATM 4128  C2  OLA A2002      38.536  53.779 -30.037  1.00 98.39           C  
HETATM 4129  C3  OLA A2002      38.122  53.725 -31.505  1.00 93.05           C  
HETATM 4130  C4  OLA A2002      39.233  54.294 -32.381  1.00 88.58           C  
HETATM 4131  C5  OLA A2002      38.974  54.030 -33.864  1.00 85.86           C  
HETATM 4132  C6  OLA A2002      40.276  54.007 -34.663  1.00 84.88           C  
HETATM 4133  C7  OLA A2002      40.111  54.671 -36.030  1.00 85.98           C  
HETATM 4134  C8  OLA A2002      41.458  54.885 -36.722  1.00 87.88           C  
HETATM 4135  C9  OLA A2002      41.289  54.854 -38.226  1.00 89.00           C  
HETATM 4136  C10 OLA A2002      42.448  54.859 -39.142  1.00 89.37           C  
HETATM 4137  C11 OLA A2002      42.763  56.056 -40.010  1.00 88.60           C  
HETATM 4138  C12 OLA A2002      43.945  55.751 -40.930  1.00 89.39           C  
HETATM 4139  C13 OLA A2002      45.261  55.880 -40.175  1.00 89.82           C  
HETATM 4140  C1  OLA A2003      49.186  62.812 -59.193  1.00101.29           C  
HETATM 4141  O1  OLA A2003      48.531  62.109 -59.988  1.00104.91           O  
HETATM 4142  O2  OLA A2003      50.338  63.178 -59.513  1.00103.99           O  
HETATM 4143  C2  OLA A2003      48.595  63.211 -57.871  1.00 94.26           C  
HETATM 4144  C3  OLA A2003      49.737  63.472 -56.905  1.00 88.20           C  
HETATM 4145  C4  OLA A2003      49.516  62.689 -55.623  1.00 83.37           C  
HETATM 4146  C5  OLA A2003      50.721  62.859 -54.717  1.00 83.63           C  
HETATM 4147  C6  OLA A2003      50.298  63.619 -53.473  1.00 86.28           C  
HETATM 4148  C7  OLA A2003      49.621  62.672 -52.495  1.00 87.13           C  
HETATM 4149  C8  OLA A2003      50.621  62.146 -51.472  1.00 87.97           C  
HETATM 4150  C9  OLA A2003      51.345  63.312 -50.845  1.00 88.58           C  
HETATM 4151  C10 OLA A2003      51.770  63.218 -49.441  1.00 89.17           C  
HETATM 4152  C11 OLA A2003      50.790  62.704 -48.415  1.00 87.98           C  
HETATM 4153  C12 OLA A2003      51.426  62.755 -47.031  1.00 87.94           C  
HETATM 4154  C13 OLA A2003      51.442  64.174 -46.476  1.00 89.00           C  
HETATM 4155  C14 OLA A2003      51.613  64.152 -44.961  1.00 89.95           C  
HETATM 4156  C1  OLA A2004      33.148  52.472 -30.027  1.00115.63           C  
HETATM 4157  O1  OLA A2004      32.534  51.411 -29.770  1.00117.55           O  
HETATM 4158  O2  OLA A2004      33.138  53.394 -29.177  1.00116.70           O  
HETATM 4159  C2  OLA A2004      33.887  52.632 -31.339  1.00110.96           C  
HETATM 4160  C3  OLA A2004      33.046  52.074 -32.485  1.00107.20           C  
HETATM 4161  C4  OLA A2004      33.328  52.812 -33.790  1.00104.40           C  
HETATM 4162  C5  OLA A2004      32.845  52.000 -34.988  1.00102.17           C  
HETATM 4163  C6  OLA A2004      33.978  51.761 -35.983  1.00 99.32           C  
HETATM 4164  C7  OLA A2004      33.587  52.211 -37.389  1.00 97.30           C  
HETATM 4165  C8  OLA A2004      34.736  52.867 -38.157  1.00 94.01           C  
HETATM 4166  C9  OLA A2004      35.685  51.813 -38.683  1.00 89.81           C  
HETATM 4167  C10 OLA A2004      37.051  52.152 -39.126  1.00 83.78           C  
HETATM 4168  C11 OLA A2004      37.457  51.922 -40.565  1.00 79.29           C  
HETATM 4169  C12 OLA A2004      38.938  52.234 -40.757  1.00 74.98           C  
HETATM 4170  C13 OLA A2004      39.117  53.128 -41.978  1.00 75.01           C  
HETATM 4171  C1  OLA A2005      35.125  57.553 -56.970  1.00111.65           C  
HETATM 4172  O1  OLA A2005      36.030  58.184 -57.560  1.00113.44           O  
HETATM 4173  O2  OLA A2005      33.961  57.627 -57.427  1.00113.25           O  
HETATM 4174  C2  OLA A2005      35.422  56.709 -55.746  1.00106.92           C  
HETATM 4175  C3  OLA A2005      36.712  57.151 -55.056  1.00102.16           C  
HETATM 4176  C4  OLA A2005      37.700  55.994 -54.903  1.00 97.95           C  
HETATM 4177  C5  OLA A2005      38.827  56.327 -53.929  1.00 95.22           C  
HETATM 4178  C6  OLA A2005      38.846  55.344 -52.761  1.00 93.60           C  
HETATM 4179  C7  OLA A2005      40.158  55.391 -51.983  1.00 90.35           C  
HETATM 4180  C8  OLA A2005      40.193  56.593 -51.043  1.00 87.23           C  
HETATM 4181  C9  OLA A2005      40.988  56.255 -49.810  1.00 85.37           C  
HETATM 4182  C10 OLA A2005      41.052  57.199 -48.684  1.00 84.49           C  
HETATM 4183  C11 OLA A2005      41.654  58.556 -48.920  1.00 83.68           C  
HETATM 4184  C12 OLA A2005      41.920  59.292 -47.613  1.00 84.00           C  
HETATM 4185  C13 OLA A2005      42.711  60.556 -47.938  1.00 86.32           C  
HETATM 4186  C14 OLA A2005      43.194  61.268 -46.682  1.00 90.06           C  
HETATM 4187  C15 OLA A2005      43.698  62.675 -46.999  1.00 93.09           C  
HETATM 4188  OH2 1PE A2006      21.443  47.742  11.527  1.00107.38           O  
HETATM 4189  C12 1PE A2006      20.354  46.824  11.368  1.00108.19           C  
HETATM 4190  C22 1PE A2006      18.995  47.557  11.389  1.00110.42           C  
HETATM 4191  OH3 1PE A2006      18.799  48.246  12.637  1.00111.77           O  
HETATM 4192  C13 1PE A2006      17.333  49.502  14.105  1.00114.84           C  
HETATM 4193  C23 1PE A2006      17.465  48.759  12.770  1.00112.27           C  
HETATM 4194  OH4 1PE A2006      18.256  50.599  14.147  1.00118.19           O  
HETATM 4195  C14 1PE A2006      19.268  52.366  15.483  1.00119.95           C  
HETATM 4196  C24 1PE A2006      18.514  51.028  15.495  1.00119.10           C  
HETATM 4197  OH5 1PE A2006      20.511  52.234  14.776  1.00121.22           O  
HETATM 4198  C15 1PE A2006      22.638  51.128  14.531  1.00122.72           C  
HETATM 4199  C25 1PE A2006      21.425  51.356  15.438  1.00121.77           C  
HETATM 4200  OH6 1PE A2006      23.563  50.242  15.172  1.00123.24           O  
HETATM 4201  OH2 1PE A2007      35.170  40.354 -64.689  1.00110.17           O  
HETATM 4202  C12 1PE A2007      34.656  41.621 -64.258  1.00110.04           C  
HETATM 4203  C22 1PE A2007      35.811  42.619 -64.153  1.00109.21           C  
HETATM 4204  OH3 1PE A2007      35.324  43.900 -63.733  1.00108.77           O  
HETATM 4205  C13 1PE A2007      36.007  44.504 -61.459  1.00104.17           C  
HETATM 4206  C23 1PE A2007      34.894  43.953 -62.364  1.00106.90           C  
HETATM 4207  OH4 1PE A2007      37.137  43.646 -61.533  1.00101.94           O  
HETATM 4208  C14 1PE A2007      39.429  43.209 -61.410  1.00104.31           C  
HETATM 4209  C24 1PE A2007      38.347  44.223 -61.059  1.00100.17           C  
HETATM 4210  OH5 1PE A2007      40.717  43.655 -61.006  1.00108.77           O  
HETATM 4211  C15 1PE A2007      43.068  43.124 -61.086  1.00108.32           C  
HETATM 4212  C25 1PE A2007      41.652  42.646 -61.412  1.00108.41           C  
HETATM 4213  OH6 1PE A2007      44.014  42.133 -61.481  1.00107.24           O  
HETATM 4214  O   HOH A2101      37.317  45.878 -47.966  1.00 65.73           O  
HETATM 4215  O   HOH A2102      36.282  36.774 -47.763  1.00 63.09           O  
HETATM 4216  O   HOH A2103      39.697  48.522 -23.481  1.00 70.98           O  
HETATM 4217  O   HOH A2104      57.909  38.053 -61.324  1.00 56.49           O  
HETATM 4218  O   HOH A2105      47.879  43.838 -34.230  1.00 66.48           O  
HETATM 4219  O   HOH A2106      18.226  41.876  22.857  1.00 56.85           O  
HETATM 4220  O   HOH A2107      32.622  40.708  13.803  1.00 66.84           O  
HETATM 4221  O   HOH A2108      39.081  37.053 -56.969  1.00 63.36           O  
HETATM 4222  O   HOH A2109      20.781  31.947  -3.127  1.00 72.45           O  
HETATM 4223  O   HOH A2110      24.659  49.330   5.344  1.00 61.85           O  
HETATM 4224  O   HOH A2111      27.274  33.772  -4.375  1.00 79.37           O  
HETATM 4225  O   HOH A2112      24.621  15.378  -0.651  1.00 72.55           O  
CONECT  767 1431                                                                
CONECT 1431  767                                                                
CONECT 4093 4120 4121                                                           
CONECT 4094 4108 4114                                                           
CONECT 4095 4096 4108 4109                                                      
CONECT 4096 4095 4111                                                           
CONECT 4097 4113                                                                
CONECT 4098 4101 4104 4105                                                      
CONECT 4099 4103 4104                                                           
CONECT 4100 4101                                                                
CONECT 4101 4098 4100 4102                                                      
CONECT 4102 4101 4103                                                           
CONECT 4103 4099 4102                                                           
CONECT 4104 4098 4099                                                           
CONECT 4105 4098 4106 4107 4108                                                 
CONECT 4106 4105                                                                
CONECT 4107 4105                                                                
CONECT 4108 4094 4095 4105                                                      
CONECT 4109 4095 4110                                                           
CONECT 4110 4109 4112                                                           
CONECT 4111 4096 4112                                                           
CONECT 4112 4110 4111 4113                                                      
CONECT 4113 4097 4112                                                           
CONECT 4114 4094 4115 4116                                                      
CONECT 4115 4114                                                                
CONECT 4116 4114 4117 4119                                                      
CONECT 4117 4116 4118                                                           
CONECT 4118 4117                                                                
CONECT 4119 4116 4120                                                           
CONECT 4120 4093 4119 4124                                                      
CONECT 4121 4093 4122                                                           
CONECT 4122 4121 4123                                                           
CONECT 4123 4122 4124                                                           
CONECT 4124 4120 4123                                                           
CONECT 4125 4126 4127 4128                                                      
CONECT 4126 4125                                                                
CONECT 4127 4125                                                                
CONECT 4128 4125 4129                                                           
CONECT 4129 4128 4130                                                           
CONECT 4130 4129 4131                                                           
CONECT 4131 4130 4132                                                           
CONECT 4132 4131 4133                                                           
CONECT 4133 4132 4134                                                           
CONECT 4134 4133 4135                                                           
CONECT 4135 4134 4136                                                           
CONECT 4136 4135 4137                                                           
CONECT 4137 4136 4138                                                           
CONECT 4138 4137 4139                                                           
CONECT 4139 4138                                                                
CONECT 4140 4141 4142 4143                                                      
CONECT 4141 4140                                                                
CONECT 4142 4140                                                                
CONECT 4143 4140 4144                                                           
CONECT 4144 4143 4145                                                           
CONECT 4145 4144 4146                                                           
CONECT 4146 4145 4147                                                           
CONECT 4147 4146 4148                                                           
CONECT 4148 4147 4149                                                           
CONECT 4149 4148 4150                                                           
CONECT 4150 4149 4151                                                           
CONECT 4151 4150 4152                                                           
CONECT 4152 4151 4153                                                           
CONECT 4153 4152 4154                                                           
CONECT 4154 4153 4155                                                           
CONECT 4155 4154                                                                
CONECT 4156 4157 4158 4159                                                      
CONECT 4157 4156                                                                
CONECT 4158 4156                                                                
CONECT 4159 4156 4160                                                           
CONECT 4160 4159 4161                                                           
CONECT 4161 4160 4162                                                           
CONECT 4162 4161 4163                                                           
CONECT 4163 4162 4164                                                           
CONECT 4164 4163 4165                                                           
CONECT 4165 4164 4166                                                           
CONECT 4166 4165 4167                                                           
CONECT 4167 4166 4168                                                           
CONECT 4168 4167 4169                                                           
CONECT 4169 4168 4170                                                           
CONECT 4170 4169                                                                
CONECT 4171 4172 4173 4174                                                      
CONECT 4172 4171                                                                
CONECT 4173 4171                                                                
CONECT 4174 4171 4175                                                           
CONECT 4175 4174 4176                                                           
CONECT 4176 4175 4177                                                           
CONECT 4177 4176 4178                                                           
CONECT 4178 4177 4179                                                           
CONECT 4179 4178 4180                                                           
CONECT 4180 4179 4181                                                           
CONECT 4181 4180 4182                                                           
CONECT 4182 4181 4183                                                           
CONECT 4183 4182 4184                                                           
CONECT 4184 4183 4185                                                           
CONECT 4185 4184 4186                                                           
CONECT 4186 4185 4187                                                           
CONECT 4187 4186                                                                
CONECT 4188 4189                                                                
CONECT 4189 4188 4190                                                           
CONECT 4190 4189 4191                                                           
CONECT 4191 4190 4193                                                           
CONECT 4192 4193 4194                                                           
CONECT 4193 4191 4192                                                           
CONECT 4194 4192 4196                                                           
CONECT 4195 4196 4197                                                           
CONECT 4196 4194 4195                                                           
CONECT 4197 4195 4199                                                           
CONECT 4198 4199 4200                                                           
CONECT 4199 4197 4198                                                           
CONECT 4200 4198                                                                
CONECT 4201 4202                                                                
CONECT 4202 4201 4203                                                           
CONECT 4203 4202 4204                                                           
CONECT 4204 4203 4206                                                           
CONECT 4205 4206 4207                                                           
CONECT 4206 4204 4205                                                           
CONECT 4207 4205 4209                                                           
CONECT 4208 4209 4210                                                           
CONECT 4209 4207 4208                                                           
CONECT 4210 4208 4212                                                           
CONECT 4211 4212 4213                                                           
CONECT 4212 4210 4211                                                           
CONECT 4213 4211                                                                
MASTER      353    0    7   22    8    0   12    6 4196    1  123   44          
END